data_8Z3G
# 
_entry.id   8Z3G 
# 
_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   8Z3G         pdb_00008z3g 10.2210/pdb8z3g/pdb 
WWPDB D_1300046949 ?            ?                   
# 
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                        8Z3G 
_pdbx_database_status.recvd_initial_deposition_date   2024-04-15 
_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 
PDB 'The same protein 100 ns after illumination of the dark-adapted form' 8Z2D unspecified 
PDB 'The same protein 1 us after illumination of the dark-adapted form'   8Z3D 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    280 ? ? ? ? 
# 
_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 ?   ?   ?   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 51  HOH HOH A . 
D 4 HOH 2   702 189 HOH HOH A . 
D 4 HOH 3   703 227 HOH HOH A . 
D 4 HOH 4   704 120 HOH HOH A . 
D 4 HOH 5   705 240 HOH HOH A . 
D 4 HOH 6   706 115 HOH HOH A . 
D 4 HOH 7   707 171 HOH HOH A . 
D 4 HOH 8   708 126 HOH HOH A . 
D 4 HOH 9   709 122 HOH HOH A . 
D 4 HOH 10  710 264 HOH HOH A . 
D 4 HOH 11  711 79  HOH HOH A . 
D 4 HOH 12  712 223 HOH HOH A . 
D 4 HOH 13  713 30  HOH HOH A . 
D 4 HOH 14  714 75  HOH HOH A . 
D 4 HOH 15  715 236 HOH HOH A . 
D 4 HOH 16  716 266 HOH HOH A . 
D 4 HOH 17  717 210 HOH HOH A . 
D 4 HOH 18  718 254 HOH HOH A . 
D 4 HOH 19  719 149 HOH HOH A . 
D 4 HOH 20  720 142 HOH HOH A . 
D 4 HOH 21  721 143 HOH HOH A . 
D 4 HOH 22  722 169 HOH HOH A . 
D 4 HOH 23  723 265 HOH HOH A . 
D 4 HOH 24  724 205 HOH HOH A . 
D 4 HOH 25  725 248 HOH HOH A . 
D 4 HOH 26  726 127 HOH HOH A . 
D 4 HOH 27  727 167 HOH HOH A . 
D 4 HOH 28  728 173 HOH HOH A . 
D 4 HOH 29  729 140 HOH HOH A . 
D 4 HOH 30  730 179 HOH HOH A . 
D 4 HOH 31  731 95  HOH HOH A . 
D 4 HOH 32  732 43  HOH HOH A . 
D 4 HOH 33  733 74  HOH HOH A . 
D 4 HOH 34  734 3   HOH HOH A . 
D 4 HOH 35  735 110 HOH HOH A . 
D 4 HOH 36  736 92  HOH HOH A . 
D 4 HOH 37  737 261 HOH HOH A . 
D 4 HOH 38  738 60  HOH HOH A . 
D 4 HOH 39  739 273 HOH HOH A . 
D 4 HOH 40  740 5   HOH HOH A . 
D 4 HOH 41  741 181 HOH HOH A . 
D 4 HOH 42  742 165 HOH HOH A . 
D 4 HOH 43  743 182 HOH HOH A . 
D 4 HOH 44  744 88  HOH HOH A . 
D 4 HOH 45  745 11  HOH HOH A . 
D 4 HOH 46  746 151 HOH HOH A . 
D 4 HOH 47  747 86  HOH HOH A . 
D 4 HOH 48  748 138 HOH HOH A . 
D 4 HOH 49  749 262 HOH HOH A . 
D 4 HOH 50  750 47  HOH HOH A . 
D 4 HOH 51  751 21  HOH HOH A . 
D 4 HOH 52  752 209 HOH HOH A . 
D 4 HOH 53  753 176 HOH HOH A . 
D 4 HOH 54  754 277 HOH HOH A . 
D 4 HOH 55  755 25  HOH HOH A . 
D 4 HOH 56  756 199 HOH HOH A . 
D 4 HOH 57  757 278 HOH HOH A . 
D 4 HOH 58  758 225 HOH HOH A . 
D 4 HOH 59  759 123 HOH HOH A . 
D 4 HOH 60  760 195 HOH HOH A . 
D 4 HOH 61  761 219 HOH HOH A . 
D 4 HOH 62  762 250 HOH HOH A . 
D 4 HOH 63  763 31  HOH HOH A . 
D 4 HOH 64  764 157 HOH HOH A . 
D 4 HOH 65  765 73  HOH HOH A . 
D 4 HOH 66  766 274 HOH HOH A . 
D 4 HOH 67  767 135 HOH HOH A . 
D 4 HOH 68  768 69  HOH HOH A . 
D 4 HOH 69  769 12  HOH HOH A . 
D 4 HOH 70  770 112 HOH HOH A . 
D 4 HOH 71  771 49  HOH HOH A . 
D 4 HOH 72  772 170 HOH HOH A . 
D 4 HOH 73  773 56  HOH HOH A . 
D 4 HOH 74  774 28  HOH HOH A . 
D 4 HOH 75  775 201 HOH HOH A . 
D 4 HOH 76  776 154 HOH HOH A . 
D 4 HOH 77  777 20  HOH HOH A . 
D 4 HOH 78  778 141 HOH HOH A . 
D 4 HOH 79  779 27  HOH HOH A . 
D 4 HOH 80  780 217 HOH HOH A . 
D 4 HOH 81  781 64  HOH HOH A . 
D 4 HOH 82  782 107 HOH HOH A . 
D 4 HOH 83  783 29  HOH HOH A . 
D 4 HOH 84  784 231 HOH HOH A . 
D 4 HOH 85  785 172 HOH HOH A . 
D 4 HOH 86  786 17  HOH HOH A . 
D 4 HOH 87  787 280 HOH HOH A . 
D 4 HOH 88  788 83  HOH HOH A . 
D 4 HOH 89  789 2   HOH HOH A . 
D 4 HOH 90  790 13  HOH HOH A . 
D 4 HOH 91  791 279 HOH HOH A . 
D 4 HOH 92  792 276 HOH HOH A . 
D 4 HOH 93  793 131 HOH HOH A . 
D 4 HOH 94  794 38  HOH HOH A . 
D 4 HOH 95  795 180 HOH HOH A . 
D 4 HOH 96  796 59  HOH HOH A . 
D 4 HOH 97  797 63  HOH HOH A . 
D 4 HOH 98  798 101 HOH HOH A . 
D 4 HOH 99  799 202 HOH HOH A . 
D 4 HOH 100 800 241 HOH HOH A . 
D 4 HOH 101 801 139 HOH HOH A . 
D 4 HOH 102 802 4   HOH HOH A . 
D 4 HOH 103 803 168 HOH HOH A . 
D 4 HOH 104 804 228 HOH HOH A . 
D 4 HOH 105 805 103 HOH HOH A . 
D 4 HOH 106 806 119 HOH HOH A . 
D 4 HOH 107 807 46  HOH HOH A . 
D 4 HOH 108 808 58  HOH HOH A . 
D 4 HOH 109 809 66  HOH HOH A . 
D 4 HOH 110 810 156 HOH HOH A . 
D 4 HOH 111 811 272 HOH HOH A . 
D 4 HOH 112 812 238 HOH HOH A . 
D 4 HOH 113 813 163 HOH HOH A . 
D 4 HOH 114 814 1   HOH HOH A . 
D 4 HOH 115 815 111 HOH HOH A . 
D 4 HOH 116 816 15  HOH HOH A . 
D 4 HOH 117 817 230 HOH HOH A . 
D 4 HOH 118 818 194 HOH HOH A . 
D 4 HOH 119 819 39  HOH HOH A . 
D 4 HOH 120 820 32  HOH HOH A . 
D 4 HOH 121 821 7   HOH HOH A . 
D 4 HOH 122 822 239 HOH HOH A . 
D 4 HOH 123 823 160 HOH HOH A . 
D 4 HOH 124 824 77  HOH HOH A . 
D 4 HOH 125 825 33  HOH HOH A . 
D 4 HOH 126 826 37  HOH HOH A . 
D 4 HOH 127 827 84  HOH HOH A . 
D 4 HOH 128 828 52  HOH HOH A . 
D 4 HOH 129 829 196 HOH HOH A . 
D 4 HOH 130 830 45  HOH HOH A . 
D 4 HOH 131 831 10  HOH HOH A . 
D 4 HOH 132 832 18  HOH HOH A . 
D 4 HOH 133 833 62  HOH HOH A . 
D 4 HOH 134 834 48  HOH HOH A . 
D 4 HOH 135 835 251 HOH HOH A . 
D 4 HOH 136 836 96  HOH HOH A . 
D 4 HOH 137 837 237 HOH HOH A . 
D 4 HOH 138 838 177 HOH HOH A . 
D 4 HOH 139 839 93  HOH HOH A . 
D 4 HOH 140 840 243 HOH HOH A . 
D 4 HOH 141 841 267 HOH HOH A . 
D 4 HOH 142 842 70  HOH HOH A . 
D 4 HOH 143 843 109 HOH HOH A . 
D 4 HOH 144 844 106 HOH HOH A . 
D 4 HOH 145 845 222 HOH HOH A . 
D 4 HOH 146 846 102 HOH HOH A . 
D 4 HOH 147 847 44  HOH HOH A . 
D 4 HOH 148 848 164 HOH HOH A . 
D 4 HOH 149 849 186 HOH HOH A . 
D 4 HOH 150 850 197 HOH HOH A . 
D 4 HOH 151 851 8   HOH HOH A . 
D 4 HOH 152 852 108 HOH HOH A . 
D 4 HOH 153 853 19  HOH HOH A . 
D 4 HOH 154 854 14  HOH HOH A . 
D 4 HOH 155 855 24  HOH HOH A . 
D 4 HOH 156 856 16  HOH HOH A . 
D 4 HOH 157 857 244 HOH HOH A . 
D 4 HOH 158 858 100 HOH HOH A . 
D 4 HOH 159 859 78  HOH HOH A . 
D 4 HOH 160 860 221 HOH HOH A . 
D 4 HOH 161 861 97  HOH HOH A . 
D 4 HOH 162 862 208 HOH HOH A . 
D 4 HOH 163 863 54  HOH HOH A . 
D 4 HOH 164 864 134 HOH HOH A . 
D 4 HOH 165 865 72  HOH HOH A . 
D 4 HOH 166 866 35  HOH HOH A . 
D 4 HOH 167 867 187 HOH HOH A . 
D 4 HOH 168 868 121 HOH HOH A . 
D 4 HOH 169 869 99  HOH HOH A . 
D 4 HOH 170 870 9   HOH HOH A . 
D 4 HOH 171 871 128 HOH HOH A . 
D 4 HOH 172 872 22  HOH HOH A . 
D 4 HOH 173 873 26  HOH HOH A . 
D 4 HOH 174 874 67  HOH HOH A . 
D 4 HOH 175 875 36  HOH HOH A . 
D 4 HOH 176 876 188 HOH HOH A . 
D 4 HOH 177 877 215 HOH HOH A . 
D 4 HOH 178 878 242 HOH HOH A . 
D 4 HOH 179 879 23  HOH HOH A . 
D 4 HOH 180 880 144 HOH HOH A . 
D 4 HOH 181 881 129 HOH HOH A . 
D 4 HOH 182 882 105 HOH HOH A . 
D 4 HOH 183 883 80  HOH HOH A . 
D 4 HOH 184 884 174 HOH HOH A . 
D 4 HOH 185 885 40  HOH HOH A . 
D 4 HOH 186 886 258 HOH HOH A . 
D 4 HOH 187 887 42  HOH HOH A . 
D 4 HOH 188 888 87  HOH HOH A . 
D 4 HOH 189 889 118 HOH HOH A . 
D 4 HOH 190 890 212 HOH HOH A . 
D 4 HOH 191 891 68  HOH HOH A . 
D 4 HOH 192 892 247 HOH HOH A . 
D 4 HOH 193 893 136 HOH HOH A . 
D 4 HOH 194 894 94  HOH HOH A . 
D 4 HOH 195 895 234 HOH HOH A . 
D 4 HOH 196 896 200 HOH HOH A . 
D 4 HOH 197 897 147 HOH HOH A . 
D 4 HOH 198 898 90  HOH HOH A . 
D 4 HOH 199 899 81  HOH HOH A . 
D 4 HOH 200 900 275 HOH HOH A . 
D 4 HOH 201 901 249 HOH HOH A . 
D 4 HOH 202 902 218 HOH HOH A . 
D 4 HOH 203 903 158 HOH HOH A . 
D 4 HOH 204 904 145 HOH HOH A . 
D 4 HOH 205 905 91  HOH HOH A . 
D 4 HOH 206 906 98  HOH HOH A . 
D 4 HOH 207 907 104 HOH HOH A . 
D 4 HOH 208 908 235 HOH HOH A . 
D 4 HOH 209 909 270 HOH HOH A . 
D 4 HOH 210 910 252 HOH HOH A . 
D 4 HOH 211 911 124 HOH HOH A . 
D 4 HOH 212 912 229 HOH HOH A . 
D 4 HOH 213 913 41  HOH HOH A . 
D 4 HOH 214 914 263 HOH HOH A . 
D 4 HOH 215 915 203 HOH HOH A . 
D 4 HOH 216 916 178 HOH HOH A . 
D 4 HOH 217 917 6   HOH HOH A . 
D 4 HOH 218 918 253 HOH HOH A . 
D 4 HOH 219 919 175 HOH HOH A . 
D 4 HOH 220 920 50  HOH HOH A . 
D 4 HOH 221 921 65  HOH HOH A . 
D 4 HOH 222 922 53  HOH HOH A . 
D 4 HOH 223 923 85  HOH HOH A . 
D 4 HOH 224 924 114 HOH HOH A . 
D 4 HOH 225 925 113 HOH HOH A . 
D 4 HOH 226 926 76  HOH HOH A . 
D 4 HOH 227 927 166 HOH HOH A . 
D 4 HOH 228 928 117 HOH HOH A . 
D 4 HOH 229 929 246 HOH HOH A . 
D 4 HOH 230 930 55  HOH HOH A . 
D 4 HOH 231 931 137 HOH HOH A . 
D 4 HOH 232 932 89  HOH HOH A . 
D 4 HOH 233 933 268 HOH HOH A . 
D 4 HOH 234 934 153 HOH HOH A . 
D 4 HOH 235 935 271 HOH HOH A . 
D 4 HOH 236 936 198 HOH HOH A . 
D 4 HOH 237 937 183 HOH HOH A . 
D 4 HOH 238 938 191 HOH HOH A . 
D 4 HOH 239 939 216 HOH HOH A . 
D 4 HOH 240 940 185 HOH HOH A . 
D 4 HOH 241 941 161 HOH HOH A . 
D 4 HOH 242 942 232 HOH HOH A . 
D 4 HOH 243 943 184 HOH HOH A . 
D 4 HOH 244 944 214 HOH HOH A . 
D 4 HOH 245 945 190 HOH HOH A . 
D 4 HOH 246 946 162 HOH HOH A . 
D 4 HOH 247 947 155 HOH HOH A . 
D 4 HOH 248 948 233 HOH HOH A . 
D 4 HOH 249 949 256 HOH HOH A . 
D 4 HOH 250 950 260 HOH HOH A . 
D 4 HOH 251 951 226 HOH HOH A . 
D 4 HOH 252 952 148 HOH HOH A . 
D 4 HOH 253 953 204 HOH HOH A . 
D 4 HOH 254 954 34  HOH HOH A . 
D 4 HOH 255 955 193 HOH HOH A . 
D 4 HOH 256 956 61  HOH HOH A . 
D 4 HOH 257 957 255 HOH HOH A . 
D 4 HOH 258 958 133 HOH HOH A . 
D 4 HOH 259 959 220 HOH HOH A . 
D 4 HOH 260 960 224 HOH HOH A . 
D 4 HOH 261 961 257 HOH HOH A . 
D 4 HOH 262 962 259 HOH HOH A . 
D 4 HOH 263 963 130 HOH HOH A . 
D 4 HOH 264 964 150 HOH HOH A . 
D 4 HOH 265 965 116 HOH HOH A . 
D 4 HOH 266 966 207 HOH HOH A . 
D 4 HOH 267 967 82  HOH HOH A . 
D 4 HOH 268 968 132 HOH HOH A . 
D 4 HOH 269 969 206 HOH HOH A . 
D 4 HOH 270 970 211 HOH HOH A . 
D 4 HOH 271 971 269 HOH HOH A . 
D 4 HOH 272 972 146 HOH HOH A . 
D 4 HOH 273 973 71  HOH HOH A . 
D 4 HOH 274 974 245 HOH HOH A . 
D 4 HOH 275 975 57  HOH HOH A . 
D 4 HOH 276 976 213 HOH HOH A . 
D 4 HOH 277 977 152 HOH HOH A . 
D 4 HOH 278 978 125 HOH HOH A . 
D 4 HOH 279 979 192 HOH HOH A . 
D 4 HOH 280 980 159 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 LEU 44  ? CG  ? A LEU 44  CG  
7  1 Y 0 A LEU 44  ? CD1 ? A LEU 44  CD1 
8  1 Y 0 A LEU 44  ? CD2 ? A LEU 44  CD2 
9  1 Y 0 A GLN 45  ? CG  ? A GLN 45  CG  
10 1 Y 0 A GLN 45  ? CD  ? A GLN 45  CD  
11 1 Y 0 A GLN 45  ? OE1 ? A GLN 45  OE1 
12 1 Y 0 A GLN 45  ? NE2 ? A GLN 45  NE2 
13 1 Y 0 A GLN 46  ? CG  ? A GLN 46  CG  
14 1 Y 0 A GLN 46  ? CD  ? A GLN 46  CD  
15 1 Y 0 A GLN 46  ? OE1 ? A GLN 46  OE1 
16 1 Y 0 A GLN 46  ? NE2 ? A GLN 46  NE2 
17 1 Y 1 A LYS 50  ? CG  ? A LYS 50  CG  
18 1 Y 1 A LYS 50  ? CD  ? A LYS 50  CD  
19 1 Y 1 A LYS 50  ? CE  ? A LYS 50  CE  
20 1 Y 1 A LYS 50  ? NZ  ? A LYS 50  NZ  
21 1 Y 0 A LYS 83  ? CD  ? A LYS 83  CD  
22 1 Y 0 A LYS 83  ? CE  ? A LYS 83  CE  
23 1 Y 0 A LYS 83  ? NZ  ? A LYS 83  NZ  
24 1 Y 0 A ARG 119 ? CG  ? A ARG 119 CG  
25 1 Y 0 A ARG 119 ? CD  ? A ARG 119 CD  
26 1 Y 0 A ARG 119 ? NE  ? A ARG 119 NE  
27 1 Y 0 A ARG 119 ? CZ  ? A ARG 119 CZ  
28 1 Y 0 A ARG 119 ? NH1 ? A ARG 119 NH1 
29 1 Y 0 A ARG 119 ? NH2 ? A ARG 119 NH2 
30 1 Y 0 A GLN 155 ? CD  ? A GLN 155 CD  
31 1 Y 0 A GLN 155 ? OE1 ? A GLN 155 OE1 
32 1 Y 0 A GLN 155 ? NE2 ? A GLN 155 NE2 
33 1 Y 0 A LYS 159 ? CD  ? A LYS 159 CD  
34 1 Y 0 A GLU 183 ? CD  ? A GLU 183 CD  
35 1 Y 0 A GLU 183 ? OE1 ? A GLU 183 OE1 
36 1 Y 0 A GLU 183 ? OE2 ? A GLU 183 OE2 
37 1 Y 0 A LYS 204 ? CE  ? A LYS 204 CE  
38 1 Y 0 A LYS 204 ? NZ  ? A LYS 204 NZ  
39 1 Y 0 A LYS 212 ? CE  ? A LYS 212 CE  
40 1 Y 0 A LYS 212 ? NZ  ? A LYS 212 NZ  
41 1 Y 0 A LYS 247 ? CD  ? A LYS 247 CD  
42 1 Y 0 A LYS 247 ? CE  ? A LYS 247 CE  
43 1 Y 0 A LYS 247 ? NZ  ? A LYS 247 NZ  
44 1 Y 0 A ARG 276 ? CD  ? A ARG 276 CD  
45 1 Y 0 A ARG 276 ? NE  ? A ARG 276 NE  
46 1 Y 0 A ARG 276 ? CZ  ? A ARG 276 CZ  
47 1 Y 0 A ARG 276 ? NH1 ? A ARG 276 NH1 
48 1 Y 0 A ARG 276 ? NH2 ? A ARG 276 NH2 
49 1 Y 0 A ARG 277 ? NE  ? A ARG 277 NE  
50 1 Y 0 A ARG 277 ? CZ  ? A ARG 277 CZ  
51 1 Y 0 A ARG 277 ? NH1 ? A ARG 277 NH1 
52 1 Y 0 A ARG 277 ? NH2 ? A ARG 277 NH2 
53 1 Y 0 A ARG 310 ? CD  ? A ARG 310 CD  
54 1 Y 0 A ARG 310 ? NE  ? A ARG 310 NE  
55 1 Y 0 A ARG 310 ? CZ  ? A ARG 310 CZ  
56 1 Y 0 A ARG 310 ? NH1 ? A ARG 310 NH1 
57 1 Y 0 A ARG 310 ? NH2 ? A ARG 310 NH2 
58 1 Y 0 A ASP 321 ? OD1 ? A ASP 321 OD1 
59 1 Y 0 A ASP 321 ? OD2 ? A ASP 321 OD2 
60 1 Y 0 A LYS 423 ? CD  ? A LYS 423 CD  
61 1 Y 0 A LYS 423 ? CE  ? A LYS 423 CE  
62 1 Y 0 A LYS 423 ? NZ  ? A LYS 423 NZ  
63 1 Y 0 A ARG 429 ? CD  ? A ARG 429 CD  
64 1 Y 0 A ARG 429 ? NE  ? A ARG 429 NE  
65 1 Y 0 A ARG 429 ? CZ  ? A ARG 429 CZ  
66 1 Y 0 A ARG 429 ? NH1 ? A ARG 429 NH1 
67 1 Y 0 A ARG 429 ? NH2 ? A ARG 429 NH2 
68 1 Y 0 A LYS 439 ? CD  ? A LYS 439 CD  
69 1 Y 0 A LYS 439 ? CE  ? A LYS 439 CE  
70 1 Y 0 A LYS 439 ? NZ  ? A LYS 439 NZ  
71 1 Y 0 A LYS 444 ? CE  ? A LYS 444 CE  
72 1 Y 0 A LYS 444 ? NZ  ? A LYS 444 NZ  
73 1 Y 0 A GLU 455 ? CD  ? A GLU 455 CD  
74 1 Y 0 A GLU 455 ? OE1 ? A GLU 455 OE1 
75 1 Y 0 A GLU 455 ? OE2 ? A GLU 455 OE2 
76 1 Y 0 A ARG 458 ? CD  ? A ARG 458 CD  
77 1 Y 0 A ARG 458 ? NE  ? A ARG 458 NE  
78 1 Y 0 A ARG 458 ? CZ  ? A ARG 458 CZ  
79 1 Y 0 A ARG 458 ? NH1 ? A ARG 458 NH1 
80 1 Y 0 A ARG 458 ? NH2 ? A ARG 458 NH2 
81 1 Y 0 A LYS 480 ? CD  ? A LYS 480 CD  
82 1 Y 0 A LYS 480 ? CE  ? A LYS 480 CE  
83 1 Y 0 A LYS 480 ? NZ  ? A LYS 480 NZ  
84 1 Y 1 A ARG 492 ? CZ  ? A ARG 492 CZ  
85 1 Y 1 A ARG 492 ? NH1 ? A ARG 492 NH1 
86 1 Y 1 A ARG 492 ? NH2 ? A ARG 492 NH2 
# 
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                     8Z3G 
_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                         8Z3G 
_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                   8Z3G 
_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          46.60 
_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                          13.31 
_reflns.entry_id                                       8Z3G 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.77 
_reflns.d_resolution_low                               32.8 
_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                                     50888 
_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                           99.95 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                328 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          6.42 
_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                                   0.990 
_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                                    1.77 
_reflns_shell.d_res_low                                     1.81 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.41 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2489 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.522 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_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                               15.67 
_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                                 8Z3G 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.95 
_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                     38209 
_refine.ls_number_reflns_R_free                  1197 
_refine.ls_number_reflns_R_work                  37012 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.99 
_refine.ls_percent_reflns_R_free                 3.13 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1813 
_refine.ls_R_factor_R_free                       0.2153 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1802 
_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                 22.5512 
_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                            0.2027 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.95 
_refine_hist.d_res_low                        30.58 
_refine_hist.number_atoms_solvent             280 
_refine_hist.number_atoms_total               4240 
_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        3906 
_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' ? 0.0040  ? 4128 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.6261  ? 5643 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0434  ? 588  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0054  ? 725  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 13.1371 ? 1490 ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.95 2.03  . . 126 4055 100.00 . . . . 0.3043 . . . . . . . . . . . 0.3362 
'X-RAY DIFFRACTION' 2.03 2.12  . . 134 4078 100.00 . . . . 0.2849 . . . . . . . . . . . 0.3265 
'X-RAY DIFFRACTION' 2.12 2.23  . . 135 4028 100.00 . . . . 0.2573 . . . . . . . . . . . 0.2744 
'X-RAY DIFFRACTION' 2.23 2.37  . . 134 4055 100.00 . . . . 0.2418 . . . . . . . . . . . 0.2840 
'X-RAY DIFFRACTION' 2.37 2.55  . . 130 4081 100.00 . . . . 0.2218 . . . . . . . . . . . 0.2519 
'X-RAY DIFFRACTION' 2.55 2.81  . . 136 4079 100.00 . . . . 0.2033 . . . . . . . . . . . 0.2374 
'X-RAY DIFFRACTION' 2.81 3.22  . . 139 4110 100.00 . . . . 0.1733 . . . . . . . . . . . 0.2014 
'X-RAY DIFFRACTION' 3.22 4.05  . . 139 4166 100.00 . . . . 0.1228 . . . . . . . . . . . 0.1466 
'X-RAY DIFFRACTION' 4.05 30.58 . . 124 4360 99.91  . . . . 0.0921 . . . . . . . . . . . 0.1223 
# 
_struct.entry_id                     8Z3G 
_struct.title                        'SFX structure of CraCRY 3 us 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        8Z3G 
_struct_keywords.text            'photoreceptor, FLAVOPROTEIN, time-resolved crystallography, 3 us 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              8Z3G 
_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 8Z3G LYS A 497 ? UNP A8J8W0 ? ? 'expression tag' 497 1  
1 8Z3G LEU A 498 ? UNP A8J8W0 ? ? 'expression tag' 498 2  
1 8Z3G ALA A 499 ? UNP A8J8W0 ? ? 'expression tag' 499 3  
1 8Z3G ALA A 500 ? UNP A8J8W0 ? ? 'expression tag' 500 4  
1 8Z3G ALA A 501 ? UNP A8J8W0 ? ? 'expression tag' 501 5  
1 8Z3G LEU A 502 ? UNP A8J8W0 ? ? 'expression tag' 502 6  
1 8Z3G GLU A 503 ? UNP A8J8W0 ? ? 'expression tag' 503 7  
1 8Z3G HIS A 504 ? UNP A8J8W0 ? ? 'expression tag' 504 8  
1 8Z3G HIS A 505 ? UNP A8J8W0 ? ? 'expression tag' 505 9  
1 8Z3G HIS A 506 ? UNP A8J8W0 ? ? 'expression tag' 506 10 
1 8Z3G HIS A 507 ? UNP A8J8W0 ? ? 'expression tag' 507 11 
1 8Z3G HIS A 508 ? UNP A8J8W0 ? ? 'expression tag' 508 12 
1 8Z3G HIS A 509 ? UNP A8J8W0 ? ? 'expression tag' 509 13 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_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  ? GLY A 96  ? LYS A 83  GLY A 96  1 ? 14 
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 THR A 197 ? GLY A 202 ? THR A 197 GLY A 202 1 ? 6  
HELX_P HELX_P10 AB1 GLY A 214 ? PHE A 226 ? GLY A 214 PHE A 226 1 ? 13 
HELX_P HELX_P11 AB2 ASP A 228 ? GLY A 234 ? ASP A 228 GLY A 234 1 ? 7  
HELX_P HELX_P12 AB3 GLN A 236 ? THR A 240 ? GLN A 236 THR A 240 5 ? 5  
HELX_P HELX_P13 AB4 LEU A 253 ? PHE A 259 ? LEU A 253 PHE A 259 1 ? 7  
HELX_P HELX_P14 AB5 SER A 263 ? HIS A 278 ? SER A 263 HIS A 278 1 ? 16 
HELX_P HELX_P15 AB6 SER A 287 ? THR A 304 ? SER A 287 THR A 304 1 ? 18 
HELX_P HELX_P16 AB7 ASN A 325 ? GLU A 334 ? ASN A 325 GLU A 334 1 ? 10 
HELX_P HELX_P17 AB8 PHE A 339 ? TRP A 352 ? PHE A 339 TRP A 352 1 ? 14 
HELX_P HELX_P18 AB9 HIS A 356 ? THR A 368 ? HIS A 356 THR A 368 1 ? 13 
HELX_P HELX_P19 AC1 SER A 375 ? LEU A 387 ? SER A 375 LEU A 387 1 ? 13 
HELX_P HELX_P20 AC2 ASP A 391 ? SER A 403 ? ASP A 391 SER A 403 1 ? 13 
HELX_P HELX_P21 AC3 VAL A 418 ? LYS A 423 ? VAL A 418 LYS A 423 1 ? 6  
HELX_P HELX_P22 AC4 GLY A 428 ? LEU A 435 ? GLY A 428 LEU A 435 1 ? 8  
HELX_P HELX_P23 AC5 PRO A 436 ? LYS A 439 ? PRO A 436 LYS A 439 5 ? 4  
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 ? ALA A 460 ? PRO A 453 ALA A 460 1 ? 8  
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       4.64 
# 
_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                   8Z3G 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ARG A 12  ? ? -130.14 -70.52  
2  1 LYS A 13  ? ? -94.50  -159.20 
3  1 SER A 75  ? ? -120.41 -161.37 
4  1 SER A 133 ? ? -152.30 -7.09   
5  1 ASP A 324 ? ? -104.68 79.51   
6  1 THR A 368 ? ? -94.45  -107.35 
7  1 ASP A 371 ? ? -134.68 -60.06  
8  1 GLN A 390 ? ? -45.10  109.64  
9  1 PHE A 407 ? ? 64.89   -45.41  
10 1 ARG A 466 ? ? -122.90 -52.26  
11 1 ARG A 492 ? ? -90.12  42.85   
# 
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 19.7006909228 7.27987918077  -14.9651392585 0.0995173499794 ? -0.00177066961299 ? 
-0.00399280103804 ? 0.101574424927  ? 0.00444745138083  ? 0.0891630827419 ? 0.258758763454 ? -0.0350883666744 ? -0.02397286844  ? 
0.622626609497 ? 0.161524545059  ? 0.251418179033 ? 0.0182391132356   ? 0.021897973833  ? 0.0229836623417  ? -0.0145755137698 ? 
-0.0156771914366 ? 0.00568285218959 ? -0.0208248017595 ? -0.0268279105109 ? -0.00552155344143 ? 
2 'X-RAY DIFFRACTION' ? refined 11.4119198503 -18.5029847486 -25.8820270993 0.0943694039714 ? 0.00403058697873  ? 
-0.00096523165646 ? 0.0805098308051 ? -0.00386919457804 ? 0.0718013541684 ? 0.611052752073 ? 0.119327317068   ? 0.0391845814067 ? 
0.45832655734  ? 0.0396987954964 ? 0.277213785274 ? -0.00943286230967 ? 0.0279587538809 ? -0.0416989433832 ? -0.0502459629684 ? 
0.00136825944017 ? 0.0455637068882  ? 0.0196155898152  ? -0.0376281404458 ? 0.00680686106703  ? 
# 
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 488 A 493 ? ? 
;chain 'A' and (resid 228 through 493 )
;
# 
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 LYS 494 ? A LYS 494 
7  1 Y 1 A GLY 495 ? A GLY 495 
8  1 Y 1 A GLU 496 ? A GLU 496 
9  1 Y 1 A LYS 497 ? A LYS 497 
10 1 Y 1 A LEU 498 ? A LEU 498 
11 1 Y 1 A ALA 499 ? A ALA 499 
12 1 Y 1 A ALA 500 ? A ALA 500 
13 1 Y 1 A ALA 501 ? A ALA 501 
14 1 Y 1 A LEU 502 ? A LEU 502 
15 1 Y 1 A GLU 503 ? A GLU 503 
16 1 Y 1 A HIS 504 ? A HIS 504 
17 1 Y 1 A HIS 505 ? A HIS 505 
18 1 Y 1 A HIS 506 ? A HIS 506 
19 1 Y 1 A HIS 507 ? A HIS 507 
20 1 Y 1 A HIS 508 ? A HIS 508 
21 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                    8Z3G 
_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   ? 30.46691  29.98064  -8.66321  1.000 30.98317 ? 3   GLY A C     1 
ATOM   2    O  O     . GLY A 1 3   ? 30.69089  30.08164  -9.87121  1.000 36.60855 ? 3   GLY A O     1 
ATOM   3    N  N     . VAL A 1 4   ? 29.48692  29.23364  -8.17019  1.000 21.20365 ? 4   VAL A N     1 
ATOM   4    C  CA    . VAL A 1 4   ? 29.70893  27.88964  -7.68219  1.000 21.86436 ? 4   VAL A CA    1 
ATOM   5    C  C     . VAL A 1 4   ? 29.17492  26.89464  -8.70619  1.000 24.98135 ? 4   VAL A C     1 
ATOM   6    O  O     . VAL A 1 4   ? 28.47890  27.25464  -9.65417  1.000 20.39081 ? 4   VAL A O     1 
ATOM   7    C  CB    . VAL A 1 4   ? 29.06396  27.67664  -6.28918  1.000 21.33439 ? 4   VAL A CB    1 
ATOM   8    C  CG1   . VAL A 1 4   ? 29.57397  28.72364  -5.30819  1.000 21.70504 ? 4   VAL A CG1   1 
ATOM   9    C  CG2   . VAL A 1 4   ? 27.54195  27.73763  -6.38516  1.000 22.79032 ? 4   VAL A CG2   1 
ATOM   10   N  N     . LYS A 1 5   ? 29.51093  25.61864  -8.52519  1.000 22.99225 ? 5   LYS A N     1 
ATOM   11   C  CA    . LYS A 1 5   ? 29.01292  24.55164  -9.38518  1.000 16.34395 ? 5   LYS A CA    1 
ATOM   12   C  C     . LYS A 1 5   ? 27.85593  23.84163  -8.69516  1.000 13.64005 ? 5   LYS A C     1 
ATOM   13   O  O     . LYS A 1 5   ? 28.02195  23.29663  -7.59817  1.000 13.43610 ? 5   LYS A O     1 
ATOM   14   C  CB    . LYS A 1 5   ? 30.11291  23.54664  -9.72720  1.000 16.09406 ? 5   LYS A CB    1 
ATOM   15   C  CG    . LYS A 1 5   ? 29.57791  22.27164  -10.38019 1.000 15.57585 ? 5   LYS A CG    1 
ATOM   16   C  CD    . LYS A 1 5   ? 30.68890  21.28664  -10.72621 1.000 9.48525  ? 5   LYS A CD    1 
ATOM   17   C  CE    . LYS A 1 5   ? 30.13590  20.04864  -11.40120 1.000 13.82657 ? 5   LYS A CE    1 
ATOM   18   N  NZ    . LYS A 1 5   ? 31.20190  19.04465  -11.71522 1.000 9.36319  ? 5   LYS A NZ    1 
ATOM   19   N  N     . ASN A 1 6   ? 26.69092  23.84563  -9.34215  1.000 14.56378 ? 6   ASN A N     1 
ATOM   20   C  CA    . ASN A 1 6   ? 25.53793  23.05463  -8.93213  1.000 10.09357 ? 6   ASN A CA    1 
ATOM   21   C  C     . ASN A 1 6   ? 25.16291  22.14962  -10.09512 1.000 14.11354 ? 6   ASN A C     1 
ATOM   22   O  O     . ASN A 1 6   ? 24.88789  22.63662  -11.19712 1.000 10.71569 ? 6   ASN A O     1 
ATOM   23   C  CB    . ASN A 1 6   ? 24.36393  23.94862  -8.53511  1.000 15.47634 ? 6   ASN A CB    1 
ATOM   24   C  CG    . ASN A 1 6   ? 24.70295  24.86162  -7.38111  1.000 16.96830 ? 6   ASN A CG    1 
ATOM   25   O  OD1   . ASN A 1 6   ? 25.42596  24.46862  -6.46912  1.000 18.90068 ? 6   ASN A OD1   1 
ATOM   26   N  ND2   . ASN A 1 6   ? 24.18894  26.09062  -7.41510  1.000 15.53062 ? 6   ASN A ND2   1 
ATOM   27   N  N     . SER A 1 7   ? 25.16592  20.83662  -9.85512  1.000 10.89394 ? 7   SER A N     1 
ATOM   28   C  CA    . SER A 1 7   ? 25.00691  19.85562  -10.91712 1.000 10.51530 ? 7   SER A CA    1 
ATOM   29   C  C     . SER A 1 7   ? 23.76191  19.00962  -10.70210 1.000 9.52068  ? 7   SER A C     1 
ATOM   30   O  O     . SER A 1 7   ? 23.29593  18.82562  -9.57209  1.000 10.43352 ? 7   SER A O     1 
ATOM   31   C  CB    . SER A 1 7   ? 26.22791  18.92963  -11.01614 1.000 11.78135 ? 7   SER A CB    1 
ATOM   32   O  OG    . SER A 1 7   ? 26.39493  18.17863  -9.83114  1.000 10.91401 ? 7   SER A OG    1 
ATOM   33   N  N     . ILE A 1 8   ? 23.22790  18.50062  -11.80609 1.000 8.48710  ? 8   ILE A N     1 
ATOM   34   C  CA    . ILE A 1 8   ? 22.16890  17.50161  -11.79407 1.000 8.34506  ? 8   ILE A CA    1 
ATOM   35   C  C     . ILE A 1 8   ? 22.73389  16.21862  -12.38408 1.000 8.22350  ? 8   ILE A C     1 
ATOM   36   O  O     . ILE A 1 8   ? 23.37988  16.24562  -13.43809 1.000 8.26445  ? 8   ILE A O     1 
ATOM   37   C  CB    . ILE A 1 8   ? 20.93389  17.96861  -12.58705 1.000 10.55864 ? 8   ILE A CB    1 
ATOM   38   C  CG1   . ILE A 1 8   ? 20.31689  19.21761  -11.95304 1.000 12.34589 ? 8   ILE A CG1   1 
ATOM   39   C  CG2   . ILE A 1 8   ? 19.90889  16.85761  -12.67904 1.000 13.92807 ? 8   ILE A CG2   1 
ATOM   40   C  CD1   . ILE A 1 8   ? 19.09388  19.73360  -12.69102 1.000 15.73697 ? 8   ILE A CD1   1 
ATOM   41   N  N     . ILE A 1 9   ? 22.50691  15.09962  -11.70308 1.000 8.28236  ? 9   ILE A N     1 
ATOM   42   C  CA    . ILE A 1 9   ? 22.71790  13.77762  -12.28108 1.000 7.97710  ? 9   ILE A CA    1 
ATOM   43   C  C     . ILE A 1 9   ? 21.33790  13.21761  -12.59506 1.000 7.92314  ? 9   ILE A C     1 
ATOM   44   O  O     . ILE A 1 9   ? 20.54092  12.95661  -11.68805 1.000 7.90105  ? 9   ILE A O     1 
ATOM   45   C  CB    . ILE A 1 9   ? 23.52692  12.84962  -11.36010 1.000 8.30422  ? 9   ILE A CB    1 
ATOM   46   C  CG1   . ILE A 1 9   ? 23.40692  11.38862  -11.81009 1.000 7.80336  ? 9   ILE A CG1   1 
ATOM   47   C  CG2   . ILE A 1 9   ? 23.11795  13.01562  -9.89909  1.000 12.41774 ? 9   ILE A CG2   1 
ATOM   48   C  CD1   . ILE A 1 9   ? 24.14990  11.07762  -13.09111 1.000 9.73812  ? 9   ILE A CD1   1 
ATOM   49   N  N     . TRP A 1 10  ? 21.04388  13.06061  -13.88306 1.000 7.94189  ? 10  TRP A N     1 
ATOM   50   C  CA    . TRP A 1 10  ? 19.73287  12.63661  -14.35803 1.000 8.74264  ? 10  TRP A CA    1 
ATOM   51   C  C     . TRP A 1 10  ? 19.74488  11.13261  -14.59703 1.000 8.79517  ? 10  TRP A C     1 
ATOM   52   O  O     . TRP A 1 10  ? 20.46486  10.64261  -15.47605 1.000 7.82685  ? 10  TRP A O     1 
ATOM   53   C  CB    . TRP A 1 10  ? 19.36085  13.38661  -15.63703 1.000 8.08380  ? 10  TRP A CB    1 
ATOM   54   C  CG    . TRP A 1 10  ? 17.99684  13.05460  -16.19700 1.000 9.31439  ? 10  TRP A CG    1 
ATOM   55   C  CD1   . TRP A 1 10  ? 16.96985  12.41360  -15.55499 1.000 8.11031  ? 10  TRP A CD1   1 
ATOM   56   C  CD2   . TRP A 1 10  ? 17.52382  13.34660  -17.51600 1.000 8.29845  ? 10  TRP A CD2   1 
ATOM   57   N  NE1   . TRP A 1 10  ? 15.89184  12.29459  -16.39497 1.000 8.23166  ? 10  TRP A NE1   1 
ATOM   58   C  CE2   . TRP A 1 10  ? 16.20482  12.85360  -17.60497 1.000 8.34912  ? 10  TRP A CE2   1 
ATOM   59   C  CE3   . TRP A 1 10  ? 18.08780  13.97760  -18.62901 1.000 8.43611  ? 10  TRP A CE3   1 
ATOM   60   C  CZ2   . TRP A 1 10  ? 15.43880  12.97659  -18.76496 1.000 8.53385  ? 10  TRP A CZ2   1 
ATOM   61   C  CZ3   . TRP A 1 10  ? 17.32778  14.09860  -19.77899 1.000 9.29684  ? 10  TRP A CZ3   1 
ATOM   62   C  CH2   . TRP A 1 10  ? 16.01478  13.59660  -19.83797 1.000 9.23798  ? 10  TRP A CH2   1 
ATOM   63   N  N     . PHE A 1 11  ? 18.95889  10.40960  -13.81102 1.000 9.32380  ? 11  PHE A N     1 
ATOM   64   C  CA    . PHE A 1 11  ? 18.82289  8.97060   -13.96302 1.000 7.71859  ? 11  PHE A CA    1 
ATOM   65   C  C     . PHE A 1 11  ? 17.68788  8.65360   -14.92600 1.000 7.78777  ? 11  PHE A C     1 
ATOM   66   O  O     . PHE A 1 11  ? 16.58288  9.18660   -14.79398 1.000 9.56988  ? 11  PHE A O     1 
ATOM   67   C  CB    . PHE A 1 11  ? 18.55492  8.30660   -12.61102 1.000 7.68065  ? 11  PHE A CB    1 
ATOM   68   C  CG    . PHE A 1 11  ? 19.75093  8.26761   -11.71004 1.000 7.63910  ? 11  PHE A CG    1 
ATOM   69   C  CD1   . PHE A 1 11  ? 20.72893  7.29961   -11.88105 1.000 10.35215 ? 11  PHE A CD1   1 
ATOM   70   C  CD2   . PHE A 1 11  ? 19.90095  9.19461   -10.69404 1.000 7.69079  ? 11  PHE A CD2   1 
ATOM   71   C  CE1   . PHE A 1 11  ? 21.83395  7.25561   -11.05407 1.000 10.05451 ? 11  PHE A CE1   1 
ATOM   72   C  CE2   . PHE A 1 11  ? 21.00296  9.16161   -9.86406  1.000 9.13733  ? 11  PHE A CE2   1 
ATOM   73   C  CZ    . PHE A 1 11  ? 21.97196  8.18661   -10.04507 1.000 13.94720 ? 11  PHE A CZ    1 
ATOM   74   N  N     . ARG A 1 12  ? 17.96889  7.78996   -15.89846 1.000 8.00226  ? 12  ARG A N     1 
ATOM   75   C  CA    . ARG A 1 12  ? 16.93861  7.21489   -16.75432 1.000 9.82582  ? 12  ARG A CA    1 
ATOM   76   C  C     . ARG A 1 12  ? 17.14845  5.70919   -16.77051 1.000 8.56802  ? 12  ARG A C     1 
ATOM   77   O  O     . ARG A 1 12  ? 16.35208  4.94991   -16.20908 1.000 11.77320 ? 12  ARG A O     1 
ATOM   78   C  CB    . ARG A 1 12  ? 16.99832  7.79686   -18.16886 1.000 12.06172 ? 12  ARG A CB    1 
ATOM   79   C  CG    . ARG A 1 12  ? 16.95248  9.31421   -18.22500 1.000 10.96686 ? 12  ARG A CG    1 
ATOM   80   C  CD    . ARG A 1 12  ? 18.34692  9.92175   -18.26079 1.000 8.62035  ? 12  ARG A CD    1 
ATOM   81   N  NE    . ARG A 1 12  ? 19.06392  9.57322   -19.48167 1.000 9.41912  ? 12  ARG A NE    1 
ATOM   82   C  CZ    . ARG A 1 12  ? 18.90932  10.19458  -20.64278 1.000 10.38512 ? 12  ARG A CZ    1 
ATOM   83   N  NH1   . ARG A 1 12  ? 18.05638  11.19595  -20.78216 1.000 15.17073 ? 12  ARG A NH1   1 
ATOM   84   N  NH2   . ARG A 1 12  ? 19.62979  9.80261   -21.69000 1.000 13.27401 ? 12  ARG A NH2   1 
ATOM   85   N  N     . LYS A 1 13  ? 18.21885  5.27760   -17.42101 1.000 11.76498 ? 13  LYS A N     1 
ATOM   86   C  CA    . LYS A 1 13  ? 18.83186  3.99660   -17.14102 1.000 7.67266  ? 13  LYS A CA    1 
ATOM   87   C  C     . LYS A 1 13  ? 19.95687  4.24961   -16.14104 1.000 8.53772  ? 13  LYS A C     1 
ATOM   88   O  O     . LYS A 1 13  ? 19.97188  5.28261   -15.45904 1.000 7.58299  ? 13  LYS A O     1 
ATOM   89   C  CB    . LYS A 1 13  ? 19.31484  3.34361   -18.44403 1.000 12.10169 ? 13  LYS A CB    1 
ATOM   90   C  CG    . LYS A 1 13  ? 18.19882  2.91160   -19.37901 1.000 10.59016 ? 13  LYS A CG    1 
ATOM   91   C  CD    . LYS A 1 13  ? 18.74980  2.41061   -20.70902 1.000 11.81431 ? 13  LYS A CD    1 
ATOM   92   C  CE    . LYS A 1 13  ? 17.65379  2.34860   -21.76300 1.000 10.64400 ? 13  LYS A CE    1 
ATOM   93   N  NZ    . LYS A 1 13  ? 18.09177  1.61660   -22.99201 1.000 18.63398 ? 13  LYS A NZ    1 
ATOM   94   N  N     . GLY A 1 14  ? 20.91188  3.32661   -16.06206 1.000 7.54902  ? 14  GLY A N     1 
ATOM   95   C  CA    . GLY A 1 14  ? 22.03889  3.46862   -15.15707 1.000 7.51339  ? 14  GLY A CA    1 
ATOM   96   C  C     . GLY A 1 14  ? 21.61991  3.77361   -13.73607 1.000 7.49471  ? 14  GLY A C     1 
ATOM   97   O  O     . GLY A 1 14  ? 22.10192  4.73161   -13.12908 1.000 7.50463  ? 14  GLY A O     1 
ATOM   98   N  N     . LEU A 1 15  ? 20.69293  2.97761   -13.20605 1.000 7.49989  ? 15  LEU A N     1 
ATOM   99   C  CA    . LEU A 1 15  ? 20.16695  3.18561   -11.86104 1.000 7.52713  ? 15  LEU A CA    1 
ATOM   100  C  C     . LEU A 1 15  ? 21.09997  2.47761   -10.88006 1.000 7.54252  ? 15  LEU A C     1 
ATOM   101  O  O     . LEU A 1 15  ? 20.82098  1.39261   -10.35906 1.000 7.58352  ? 15  LEU A O     1 
ATOM   102  C  CB    . LEU A 1 15  ? 18.72995  2.68960   -11.76802 1.000 7.58074  ? 15  LEU A CB    1 
ATOM   103  C  CG    . LEU A 1 15  ? 17.74993  3.14760   -12.86000 1.000 7.61400  ? 15  LEU A CG    1 
ATOM   104  C  CD1   . LEU A 1 15  ? 16.43294  2.40660   -12.73598 1.000 7.70742  ? 15  LEU A CD1   1 
ATOM   105  C  CD2   . LEU A 1 15  ? 17.51393  4.63860   -12.79100 1.000 7.63718  ? 15  LEU A CD2   1 
ATOM   106  N  N     . ARG A 1 16  ? 22.24867  3.10809   -10.64681 1.000 7.54393  ? 16  ARG A N     1 
ATOM   107  C  CA    . ARG A 1 16  ? 23.31538  2.50410   -9.86115  1.000 7.59752  ? 16  ARG A CA    1 
ATOM   108  C  C     . ARG A 1 16  ? 24.32576  3.57912   -9.49265  1.000 7.83842  ? 16  ARG A C     1 
ATOM   109  O  O     . ARG A 1 16  ? 24.43215  4.61295   -10.15904 1.000 7.61360  ? 16  ARG A O     1 
ATOM   110  C  CB    . ARG A 1 16  ? 24.01036  1.37566   -10.63223 1.000 7.59226  ? 16  ARG A CB    1 
ATOM   111  C  CG    . ARG A 1 16  ? 24.78016  1.87075   -11.84703 1.000 7.56887  ? 16  ARG A CG    1 
ATOM   112  C  CD    . ARG A 1 16  ? 25.52872  0.75408   -12.55223 1.000 7.59984  ? 16  ARG A CD    1 
ATOM   113  N  NE    . ARG A 1 16  ? 26.34174  1.27771   -13.64275 1.000 8.77758  ? 16  ARG A NE    1 
ATOM   114  C  CZ    . ARG A 1 16  ? 25.92117  1.39199   -14.89420 1.000 7.60776  ? 16  ARG A CZ    1 
ATOM   115  N  NH1   . ARG A 1 16  ? 24.71402  0.99180   -15.25432 1.000 7.56159  ? 16  ARG A NH1   1 
ATOM   116  N  NH2   . ARG A 1 16  ? 26.73225  1.91825   -15.80691 1.000 7.70585  ? 16  ARG A NH2   1 
ATOM   117  N  N     . LEU A 1 17  ? 25.07700  3.31162   -8.42613  1.000 7.73769  ? 17  LEU A N     1 
ATOM   118  C  CA    . LEU A 1 17  ? 26.18701  4.16363   -8.02314  1.000 8.89955  ? 17  LEU A CA    1 
ATOM   119  C  C     . LEU A 1 17  ? 27.53400  3.65963   -8.51117  1.000 7.88527  ? 17  LEU A C     1 
ATOM   120  O  O     . LEU A 1 17  ? 28.42999  4.46763   -8.76818  1.000 9.87247  ? 17  LEU A O     1 
ATOM   121  C  CB    . LEU A 1 17  ? 26.22603  4.30063   -6.50014  1.000 9.35821  ? 17  LEU A CB    1 
ATOM   122  C  CG    . LEU A 1 17  ? 25.57904  5.55962   -5.91713  1.000 15.32410 ? 17  LEU A CG    1 
ATOM   123  C  CD1   . LEU A 1 17  ? 24.07603  5.58762   -6.16411  1.000 10.88968 ? 17  LEU A CD1   1 
ATOM   124  C  CD2   . LEU A 1 17  ? 25.88906  5.67162   -4.43514  1.000 11.22217 ? 17  LEU A CD2   1 
ATOM   125  N  N     . HIS A 1 18  ? 27.70700  2.34963   -8.64017  1.000 10.91049 ? 18  HIS A N     1 
ATOM   126  C  CA    . HIS A 1 18  ? 28.95200  1.82764   -9.18119  1.000 10.95016 ? 18  HIS A CA    1 
ATOM   127  C  C     . HIS A 1 18  ? 29.00797  2.07564   -10.68219 1.000 9.37560  ? 18  HIS A C     1 
ATOM   128  O  O     . HIS A 1 18  ? 27.98296  2.09963   -11.36117 1.000 7.90335  ? 18  HIS A O     1 
ATOM   129  C  CB    . HIS A 1 18  ? 29.08201  0.33164   -8.88619  1.000 10.13694 ? 18  HIS A CB    1 
ATOM   130  C  CG    . HIS A 1 18  ? 28.15900  -0.52937  -9.69318  1.000 8.78684  ? 18  HIS A CG    1 
ATOM   131  N  ND1   . HIS A 1 18  ? 26.88000  -0.83937  -9.28216  1.000 9.16448  ? 18  HIS A ND1   1 
ATOM   132  C  CD2   . HIS A 1 18  ? 28.33298  -1.15436  -10.88018 1.000 7.89799  ? 18  HIS A CD2   1 
ATOM   133  C  CE1   . HIS A 1 18  ? 26.30599  -1.61737  -10.18315 1.000 9.14632  ? 18  HIS A CE1   1 
ATOM   134  N  NE2   . HIS A 1 18  ? 27.16498  -1.82137  -11.16416 1.000 9.26696  ? 18  HIS A NE2   1 
ATOM   135  N  N     . ASP A 1 19  ? 30.22396  2.27864   -11.19221 1.000 8.55551  ? 19  ASP A N     1 
ATOM   136  C  CA    . ASP A 1 19  ? 30.47994  2.49864   -12.61622 1.000 10.33046 ? 19  ASP A CA    1 
ATOM   137  C  C     . ASP A 1 19  ? 29.48992  3.50164   -13.21020 1.000 7.89066  ? 19  ASP A C     1 
ATOM   138  O  O     . ASP A 1 19  ? 28.72891  3.20364   -14.13319 1.000 10.91553 ? 19  ASP A O     1 
ATOM   139  C  CB    . ASP A 1 19  ? 30.44893  1.17564   -13.38722 1.000 9.05344  ? 19  ASP A CB    1 
ATOM   140  C  CG    . ASP A 1 19  ? 30.93790  1.32765   -14.82022 1.000 11.04643 ? 19  ASP A CG    1 
ATOM   141  O  OD1   . ASP A 1 19  ? 31.71390  2.26565   -15.07524 1.000 9.48619  ? 19  ASP A OD1   1 
ATOM   142  O  OD2   . ASP A 1 19  ? 30.54189  0.52464   -15.69322 1.000 10.64989 ? 19  ASP A OD2   1 
ATOM   143  N  N     . ASN A 1 20  ? 29.49193  4.70664   -12.64520 1.000 9.17520  ? 20  ASN A N     1 
ATOM   144  C  CA    . ASN A 1 20  ? 28.59292  5.77964   -13.07318 1.000 8.86554  ? 20  ASN A CA    1 
ATOM   145  C  C     . ASN A 1 20  ? 29.41591  7.02864   -13.34720 1.000 7.97066  ? 20  ASN A C     1 
ATOM   146  O  O     . ASN A 1 20  ? 29.42892  7.96764   -12.53820 1.000 8.01032  ? 20  ASN A O     1 
ATOM   147  C  CB    . ASN A 1 20  ? 27.51494  6.05563   -12.02416 1.000 9.80471  ? 20  ASN A CB    1 
ATOM   148  C  CG    . ASN A 1 20  ? 26.30892  6.78463   -12.59714 1.000 9.24104  ? 20  ASN A CG    1 
ATOM   149  O  OD1   . ASN A 1 20  ? 25.17593  6.55562   -12.17013 1.000 9.86549  ? 20  ASN A OD1   1 
ATOM   150  N  ND2   . ASN A 1 20  ? 26.54290  7.66163   -13.56415 1.000 7.74963  ? 20  ASN A ND2   1 
ATOM   151  N  N     . PRO A 1 21  ? 30.10389  7.07964   -14.49421 1.000 8.11730  ? 21  PRO A N     1 
ATOM   152  C  CA    . PRO A 1 21  ? 30.89888  8.27565   -14.82622 1.000 10.28554 ? 21  PRO A CA    1 
ATOM   153  C  C     . PRO A 1 21  ? 30.09088  9.56064   -14.85221 1.000 8.20793  ? 21  PRO A C     1 
ATOM   154  O  O     . PRO A 1 21  ? 30.64488  10.63264  -14.58022 1.000 8.33970  ? 21  PRO A O     1 
ATOM   155  C  CB    . PRO A 1 21  ? 31.46886  7.94165   -16.21323 1.000 10.09487 ? 21  PRO A CB    1 
ATOM   156  C  CG    . PRO A 1 21  ? 30.56285  6.85964   -16.75722 1.000 8.19618  ? 21  PRO A CG    1 
ATOM   157  C  CD    . PRO A 1 21  ? 30.18388  6.05564   -15.54921 1.000 10.24093 ? 21  PRO A CD    1 
ATOM   158  N  N     . ALA A 1 22  ? 28.79687  9.48964   -15.16719 1.000 8.07512  ? 22  ALA A N     1 
ATOM   159  C  CA    . ALA A 1 22  ? 27.97187  10.69364  -15.13717 1.000 8.07953  ? 22  ALA A CA    1 
ATOM   160  C  C     . ALA A 1 22  ? 27.82689  11.22063  -13.71617 1.000 8.05977  ? 22  ALA A C     1 
ATOM   161  O  O     . ALA A 1 22  ? 27.86789  12.43463  -13.49117 1.000 8.73672  ? 22  ALA A O     1 
ATOM   162  C  CB    . ALA A 1 22  ? 26.60086  10.41263  -15.75115 1.000 8.75963  ? 22  ALA A CB    1 
ATOM   163  N  N     . LEU A 1 23  ? 27.67091  10.31763  -12.74417 1.000 9.03243  ? 23  LEU A N     1 
ATOM   164  C  CA    . LEU A 1 23  ? 27.54593  10.73163  -11.35216 1.000 10.18498 ? 23  LEU A CA    1 
ATOM   165  C  C     . LEU A 1 23  ? 28.85894  11.29964  -10.82319 1.000 8.33486  ? 23  LEU A C     1 
ATOM   166  O  O     . LEU A 1 23  ? 28.86295  12.30464  -10.10119 1.000 8.24330  ? 23  LEU A O     1 
ATOM   167  C  CB    . LEU A 1 23  ? 27.08395  9.54463   -10.50716 1.000 7.89984  ? 23  LEU A CB    1 
ATOM   168  C  CG    . LEU A 1 23  ? 26.97397  9.73763   -8.99515  1.000 8.74110  ? 23  LEU A CG    1 
ATOM   169  C  CD1   . LEU A 1 23  ? 25.89998  10.75863  -8.65514  1.000 11.46170 ? 23  LEU A CD1   1 
ATOM   170  C  CD2   . LEU A 1 23  ? 26.69599  8.40463   -8.31315  1.000 11.05103 ? 23  LEU A CD2   1 
ATOM   171  N  N     . LEU A 1 24  ? 29.98493  10.67364  -11.17720 1.000 8.81959  ? 24  LEU A N     1 
ATOM   172  C  CA    . LEU A 1 24  ? 31.28594  11.15165  -10.71623 1.000 9.21764  ? 24  LEU A CA    1 
ATOM   173  C  C     . LEU A 1 24  ? 31.55793  12.57465  -11.19423 1.000 11.52362 ? 24  LEU A C     1 
ATOM   174  O  O     . LEU A 1 24  ? 32.01594  13.42565  -10.42224 1.000 12.98374 ? 24  LEU A O     1 
ATOM   175  C  CB    . LEU A 1 24  ? 32.38993  10.20865  -11.19624 1.000 12.29272 ? 24  LEU A CB    1 
ATOM   176  C  CG    . LEU A 1 24  ? 32.33095  8.76065   -10.69924 1.000 14.59356 ? 24  LEU A CG    1 
ATOM   177  C  CD1   . LEU A 1 24  ? 33.49594  7.94465   -11.26726 1.000 14.23784 ? 24  LEU A CD1   1 
ATOM   178  C  CD2   . LEU A 1 24  ? 32.32897  8.72265   -9.18124  1.000 11.94910 ? 24  LEU A CD2   1 
ATOM   179  N  N     . GLU A 1 25  ? 31.29890  12.84165  -12.47623 1.000 8.55777  ? 25  GLU A N     1 
ATOM   180  C  CA    . GLU A 1 25  ? 31.50289  14.18365  -13.00923 1.000 11.06958 ? 25  GLU A CA    1 
ATOM   181  C  C     . GLU A 1 25  ? 30.58790  15.19064  -12.32321 1.000 13.80627 ? 25  GLU A C     1 
ATOM   182  O  O     . GLU A 1 25  ? 31.01690  16.30164  -11.98522 1.000 10.99402 ? 25  GLU A O     1 
ATOM   183  C  CB    . GLU A 1 25  ? 31.27287  14.18765  -14.52022 1.000 9.88453  ? 25  GLU A CB    1 
ATOM   184  C  CG    . GLU A 1 25  ? 31.41585  15.55465  -15.18323 1.000 14.05146 ? 25  GLU A CG    1 
ATOM   185  C  CD    . GLU A 1 25  ? 32.83785  16.08965  -15.14725 1.000 16.66786 ? 25  GLU A CD    1 
ATOM   186  O  OE1   . GLU A 1 25  ? 33.77985  15.26866  -15.13927 1.000 18.45723 ? 25  GLU A OE1   1 
ATOM   187  O  OE2   . GLU A 1 25  ? 33.01085  17.33365  -15.13225 1.000 13.55163 ? 25  GLU A OE2   1 
ATOM   188  N  N     . ALA A 1 26  ? 29.32390  14.81664  -12.10119 1.000 12.51823 ? 26  ALA A N     1 
ATOM   189  C  CA    . ALA A 1 26  ? 28.39091  15.71764  -11.43218 1.000 9.98940  ? 26  ALA A CA    1 
ATOM   190  C  C     . ALA A 1 26  ? 28.85493  16.06564  -10.02518 1.000 13.28822 ? 26  ALA A C     1 
ATOM   191  O  O     . ALA A 1 26  ? 28.57294  17.16464  -9.53518  1.000 12.82299 ? 26  ALA A O     1 
ATOM   192  C  CB    . ALA A 1 26  ? 26.99391  15.09363  -11.39315 1.000 8.29864  ? 26  ALA A CB    1 
ATOM   193  N  N     . CYS A 1 27  ? 29.57095  15.15464  -9.36420  1.000 13.68955 ? 27  CYS A N     1 
ATOM   194  C  CA    . CYS A 1 27  ? 30.03497  15.38464  -8.00320  1.000 16.12852 ? 27  CYS A CA    1 
ATOM   195  C  C     . CYS A 1 27  ? 31.35997  16.12964  -7.92923  1.000 15.27185 ? 27  CYS A C     1 
ATOM   196  O  O     . CYS A 1 27  ? 31.68498  16.67365  -6.86823  1.000 14.13957 ? 27  CYS A O     1 
ATOM   197  C  CB    . CYS A 1 27  ? 30.17099  14.05364  -7.25421  1.000 14.31397 ? 27  CYS A CB    1 
ATOM   198  S  SG    . CYS A 1 27  ? 28.61200  13.25263  -6.84518  1.000 18.08872 ? 27  CYS A SG    1 
ATOM   199  N  N     . LYS A 1 28  ? 32.13195  16.16665  -9.01324  1.000 11.92637 ? 28  LYS A N     1 
ATOM   200  C  CA    . LYS A 1 28  ? 33.45895  16.76865  -8.97026  1.000 18.37043 ? 28  LYS A CA    1 
ATOM   201  C  C     . LYS A 1 28  ? 33.34895  18.28065  -8.79926  1.000 17.64423 ? 28  LYS A C     1 
ATOM   202  O  O     . LYS A 1 28  ? 32.70493  18.95765  -9.60725  1.000 15.33507 ? 28  LYS A O     1 
ATOM   203  C  CB    . LYS A 1 28  ? 34.23493  16.41766  -10.23727 1.000 18.50483 ? 28  LYS A CB    1 
ATOM   204  C  CG    . LYS A 1 28  ? 35.66693  16.92766  -10.25630 1.000 24.13736 ? 28  LYS A CG    1 
ATOM   205  C  CD    . LYS A 1 28  ? 36.41695  16.53466  -8.99631  0.000 22.02985 ? 28  LYS A CD    1 
ATOM   206  C  CE    . LYS A 1 28  ? 37.88895  16.29667  -9.29133  0.000 23.47847 ? 28  LYS A CE    1 
ATOM   207  N  NZ    . LYS A 1 28  ? 38.46193  17.36167  -10.15934 0.000 24.91292 ? 28  LYS A NZ    1 
ATOM   208  N  N     . ASP A 1 29  ? 33.97496  18.80265  -7.73927  1.000 15.21088 ? 29  ASP A N     1 
ATOM   209  C  CA    . ASP A 1 29  ? 33.99096  20.23565  -7.43027  1.000 17.77675 ? 29  ASP A CA    1 
ATOM   210  C  C     . ASP A 1 29  ? 32.58396  20.81565  -7.30424  1.000 16.24291 ? 29  ASP A C     1 
ATOM   211  O  O     . ASP A 1 29  ? 32.36896  22.00665  -7.54124  1.000 14.85975 ? 29  ASP A O     1 
ATOM   212  C  CB    . ASP A 1 29  ? 34.79394  21.02266  -8.47028  1.000 17.36563 ? 29  ASP A CB    1 
ATOM   213  C  CG    . ASP A 1 29  ? 36.20794  20.52166  -8.60930  1.000 27.90157 ? 29  ASP A CG    1 
ATOM   214  O  OD1   . ASP A 1 29  ? 36.75896  20.00966  -7.61131  1.000 24.37654 ? 29  ASP A OD1   1 
ATOM   215  O  OD2   . ASP A 1 29  ? 36.77092  20.63366  -9.71731  1.000 38.07032 ? 29  ASP A OD2   1 
ATOM   216  N  N     . ALA A 1 30  ? 31.62097  19.98565  -6.92323  1.000 12.23257 ? 30  ALA A N     1 
ATOM   217  C  CA    . ALA A 1 30  ? 30.23197  20.40964  -6.83721  1.000 13.03931 ? 30  ALA A CA    1 
ATOM   218  C  C     . ALA A 1 30  ? 29.90299  20.92864  -5.44220  1.000 12.74809 ? 30  ALA A C     1 
ATOM   219  O  O     . ALA A 1 30  ? 30.32201  20.35264  -4.43821  1.000 11.76726 ? 30  ALA A O     1 
ATOM   220  C  CB    . ALA A 1 30  ? 29.30697  19.24764  -7.19319  1.000 10.45541 ? 30  ALA A CB    1 
ATOM   221  N  N     . LYS A 1 31  ? 29.15399  22.03364  -5.39119  1.000 13.52521 ? 31  LYS A N     1 
ATOM   222  C  CA    . LYS A 1 31  ? 28.63501  22.52663  -4.11818  1.000 11.09469 ? 31  LYS A CA    1 
ATOM   223  C  C     . LYS A 1 31  ? 27.33002  21.83263  -3.74716  1.000 12.02440 ? 31  LYS A C     1 
ATOM   224  O  O     . LYS A 1 31  ? 27.12304  21.47163  -2.58415  1.000 14.06439 ? 31  LYS A O     1 
ATOM   225  C  CB    . LYS A 1 31  ? 28.43800  24.04063  -4.18517  1.000 18.03866 ? 31  LYS A CB    1 
ATOM   226  C  CG    . LYS A 1 31  ? 27.93702  24.67963  -2.90017  1.000 17.22392 ? 31  LYS A CG    1 
ATOM   227  C  CD    . LYS A 1 31  ? 28.98704  24.65763  -1.80318  1.000 21.01197 ? 31  LYS A CD    1 
ATOM   228  C  CE    . LYS A 1 31  ? 28.61406  25.62363  -0.68518  1.000 28.29245 ? 31  LYS A CE    1 
ATOM   229  N  NZ    . LYS A 1 31  ? 29.53208  25.53864  0.48881   1.000 28.18669 ? 31  LYS A NZ    1 
ATOM   230  N  N     . HIS A 1 32  ? 26.44000  21.64163  -4.71714  1.000 12.74962 ? 32  HIS A N     1 
ATOM   231  C  CA    . HIS A 1 32  ? 25.20501  20.89762  -4.52512  1.000 16.23492 ? 32  HIS A CA    1 
ATOM   232  C  C     . HIS A 1 32  ? 25.01299  19.96662  -5.71012  1.000 14.30519 ? 32  HIS A C     1 
ATOM   233  O  O     . HIS A 1 32  ? 25.24797  20.36062  -6.85612  1.000 16.19621 ? 32  HIS A O     1 
ATOM   234  C  CB    . HIS A 1 32  ? 23.97901  21.82062  -4.40810  1.000 21.60107 ? 32  HIS A CB    1 
ATOM   235  C  CG    . HIS A 1 32  ? 24.10902  22.89162  -3.36810  1.000 18.24671 ? 32  HIS A CG    1 
ATOM   236  N  ND1   . HIS A 1 32  ? 23.85404  22.66862  -2.03310  1.000 17.99688 ? 32  HIS A ND1   1 
ATOM   237  C  CD2   . HIS A 1 32  ? 24.43802  24.20162  -3.47311  1.000 21.15817 ? 32  HIS A CD2   1 
ATOM   238  C  CE1   . HIS A 1 32  ? 24.03305  23.78862  -1.35710  1.000 19.53652 ? 32  HIS A CE1   1 
ATOM   239  N  NE2   . HIS A 1 32  ? 24.38603  24.73562  -2.20811  1.000 24.18015 ? 32  HIS A NE2   1 
ATOM   240  N  N     . VAL A 1 33  ? 24.56400  18.74462  -5.44011  1.000 16.26159 ? 33  VAL A N     1 
ATOM   241  C  CA    . VAL A 1 33  ? 24.24899  17.77062  -6.48111  1.000 14.98333 ? 33  VAL A CA    1 
ATOM   242  C  C     . VAL A 1 33  ? 22.78899  17.35861  -6.33408  1.000 11.31476 ? 33  VAL A C     1 
ATOM   243  O  O     . VAL A 1 33  ? 22.33101  17.06461  -5.22408  1.000 13.01762 ? 33  VAL A O     1 
ATOM   244  C  CB    . VAL A 1 33  ? 25.17699  16.54362  -6.41712  1.000 13.62731 ? 33  VAL A CB    1 
ATOM   245  C  CG1   . VAL A 1 33  ? 24.77798  15.52462  -7.46812  1.000 8.30218  ? 33  VAL A CG1   1 
ATOM   246  C  CG2   . VAL A 1 33  ? 26.62799  16.96663  -6.59915  1.000 11.50777 ? 33  VAL A CG2   1 
ATOM   247  N  N     . TYR A 1 34  ? 22.06497  17.33961  -7.45207  1.000 12.96783 ? 34  TYR A N     1 
ATOM   248  C  CA    . TYR A 1 34  ? 20.64497  17.00061  -7.45505  1.000 9.39382  ? 34  TYR A CA    1 
ATOM   249  C  C     . TYR A 1 34  ? 20.43097  15.69361  -8.21304  1.000 10.32396 ? 34  TYR A C     1 
ATOM   250  O  O     . TYR A 1 34  ? 20.38295  15.69761  -9.45304  1.000 10.95114 ? 34  TYR A O     1 
ATOM   251  C  CB    . TYR A 1 34  ? 19.82196  18.12761  -8.08503  1.000 10.28333 ? 34  TYR A CB    1 
ATOM   252  C  CG    . TYR A 1 34  ? 19.82097  19.42761  -7.30403  1.000 15.56426 ? 34  TYR A CG    1 
ATOM   253  C  CD1   . TYR A 1 34  ? 20.83996  20.35761  -7.46305  1.000 12.38370 ? 34  TYR A CD1   1 
ATOM   254  C  CD2   . TYR A 1 34  ? 18.78998  19.73260  -6.41902  1.000 11.63115 ? 34  TYR A CD2   1 
ATOM   255  C  CE1   . TYR A 1 34  ? 20.84197  21.54661  -6.76105  1.000 11.08597 ? 34  TYR A CE1   1 
ATOM   256  C  CE2   . TYR A 1 34  ? 18.78499  20.91960  -5.71002  1.000 10.14125 ? 34  TYR A CE2   1 
ATOM   257  C  CZ    . TYR A 1 34  ? 19.81298  21.82260  -5.88703  1.000 16.57675 ? 34  TYR A CZ    1 
ATOM   258  O  OH    . TYR A 1 34  ? 19.81299  23.00760  -5.18703  1.000 15.44193 ? 34  TYR A OH    1 
ATOM   259  N  N     . PRO A 1 35  ? 20.31998  14.55261  -7.52904  1.000 11.44347 ? 35  PRO A N     1 
ATOM   260  C  CA    . PRO A 1 35  ? 20.01797  13.28661  -8.21404  1.000 12.93893 ? 35  PRO A CA    1 
ATOM   261  C  C     . PRO A 1 35  ? 18.53697  13.22460  -8.55501  1.000 8.04922  ? 35  PRO A C     1 
ATOM   262  O  O     . PRO A 1 35  ? 17.68098  13.29260  -7.67100  1.000 8.78536  ? 35  PRO A O     1 
ATOM   263  C  CB    . PRO A 1 35  ? 20.40399  12.21961  -7.18004  1.000 8.31460  ? 35  PRO A CB    1 
ATOM   264  C  CG    . PRO A 1 35  ? 21.12301  12.95261  -6.07906  1.000 8.96247  ? 35  PRO A CG    1 
ATOM   265  C  CD    . PRO A 1 35  ? 20.59601  14.34561  -6.10105  1.000 11.90991 ? 35  PRO A CD    1 
ATOM   266  N  N     . VAL A 1 36  ? 18.23695  13.08860  -9.84201  1.000 7.99886  ? 36  VAL A N     1 
ATOM   267  C  CA    . VAL A 1 36  ? 16.89294  13.30560  -10.35199 1.000 10.48779 ? 36  VAL A CA    1 
ATOM   268  C  C     . VAL A 1 36  ? 16.46693  12.12859  -11.21698 1.000 8.77832  ? 36  VAL A C     1 
ATOM   269  O  O     . VAL A 1 36  ? 17.24292  11.63060  -12.03999 1.000 7.92825  ? 36  VAL A O     1 
ATOM   270  C  CB    . VAL A 1 36  ? 16.81292  14.62560  -11.14498 1.000 9.84779  ? 36  VAL A CB    1 
ATOM   271  C  CG1   . VAL A 1 36  ? 15.55291  14.68059  -11.98896 1.000 13.90407 ? 36  VAL A CG1   1 
ATOM   272  C  CG2   . VAL A 1 36  ? 16.86893  15.80160  -10.18598 1.000 13.73841 ? 36  VAL A CG2   1 
ATOM   273  N  N     . PHE A 1 37  ? 15.23593  11.67459  -11.00396 1.000 8.24154  ? 37  PHE A N     1 
ATOM   274  C  CA    . PHE A 1 37  ? 14.51992  10.80459  -11.92495 1.000 9.39318  ? 37  PHE A CA    1 
ATOM   275  C  C     . PHE A 1 37  ? 13.21391  11.49958  -12.27393 1.000 10.15433 ? 37  PHE A C     1 
ATOM   276  O  O     . PHE A 1 37  ? 12.51393  11.98558  -11.38091 1.000 10.03692 ? 37  PHE A O     1 
ATOM   277  C  CB    . PHE A 1 37  ? 14.25394  9.42659   -11.30794 1.000 8.05250  ? 37  PHE A CB    1 
ATOM   278  C  CG    . PHE A 1 37  ? 13.71092  8.41459   -12.27893 1.000 8.44571  ? 37  PHE A CG    1 
ATOM   279  C  CD1   . PHE A 1 37  ? 12.34792  8.31258   -12.51091 1.000 12.11689 ? 37  PHE A CD1   1 
ATOM   280  C  CD2   . PHE A 1 37  ? 14.56591  7.55359   -12.95195 1.000 7.94371  ? 37  PHE A CD2   1 
ATOM   281  C  CE1   . PHE A 1 37  ? 11.85191  7.37458   -13.39990 1.000 11.11092 ? 37  PHE A CE1   1 
ATOM   282  C  CE2   . PHE A 1 37  ? 14.07690  6.62359   -13.83794 1.000 7.97699  ? 37  PHE A CE2   1 
ATOM   283  C  CZ    . PHE A 1 37  ? 12.72190  6.53558   -14.06692 1.000 9.47797  ? 37  PHE A CZ    1 
ATOM   284  N  N     . VAL A 1 38  ? 12.90489  11.57358  -13.56492 1.000 10.24220 ? 38  VAL A N     1 
ATOM   285  C  CA    . VAL A 1 38  ? 11.70788  12.24858  -14.05190 1.000 8.56502  ? 38  VAL A CA    1 
ATOM   286  C  C     . VAL A 1 38  ? 10.64688  11.19058  -14.31788 1.000 10.89841 ? 38  VAL A C     1 
ATOM   287  O  O     . VAL A 1 38  ? 10.82187  10.32658  -15.18489 1.000 14.18867 ? 38  VAL A O     1 
ATOM   288  C  CB    . VAL A 1 38  ? 12.00286  13.08258  -15.30890 1.000 11.58000 ? 38  VAL A CB    1 
ATOM   289  C  CG1   . VAL A 1 38  ? 10.72985  13.70458  -15.84688 1.000 13.05483 ? 38  VAL A CG1   1 
ATOM   290  C  CG2   . VAL A 1 38  ? 13.02686  14.16558  -14.98492 1.000 11.45853 ? 38  VAL A CG2   1 
ATOM   291  N  N     . LEU A 1 39  ? 9.56389   11.24757  -13.55386 1.000 11.11224 ? 39  LEU A N     1 
ATOM   292  C  CA    . LEU A 1 39  ? 8.47489   10.28557  -13.62385 1.000 13.44418 ? 39  LEU A CA    1 
ATOM   293  C  C     . LEU A 1 39  ? 7.28288   10.92456  -14.32283 1.000 15.57114 ? 39  LEU A C     1 
ATOM   294  O  O     . LEU A 1 39  ? 6.90688   12.05756  -14.00682 1.000 24.05241 ? 39  LEU A O     1 
ATOM   295  C  CB    . LEU A 1 39  ? 8.06992   9.82557   -12.22084 1.000 18.82716 ? 39  LEU A CB    1 
ATOM   296  C  CG    . LEU A 1 39  ? 7.10893   8.64056   -12.09082 1.000 22.34003 ? 39  LEU A CG    1 
ATOM   297  C  CD1   . LEU A 1 39  ? 7.88693   7.35057   -11.92584 1.000 27.83636 ? 39  LEU A CD1   1 
ATOM   298  C  CD2   . LEU A 1 39  ? 6.15594   8.84556   -10.92781 1.000 26.72444 ? 39  LEU A CD2   1 
ATOM   299  N  N     . ASP A 1 40  ? 6.69287   10.20056  -15.26182 1.000 23.45376 ? 40  ASP A N     1 
ATOM   300  C  CA    . ASP A 1 40  ? 5.48285   10.65556  -15.93280 1.000 32.01386 ? 40  ASP A CA    1 
ATOM   301  C  C     . ASP A 1 40  ? 4.25387   10.10255  -15.21778 1.000 28.15586 ? 40  ASP A C     1 
ATOM   302  O  O     . ASP A 1 40  ? 3.92087   8.92155   -15.37977 1.000 33.58487 ? 40  ASP A O     1 
ATOM   303  C  CB    . ASP A 1 40  ? 5.49483   10.22656  -17.40080 1.000 32.78603 ? 40  ASP A CB    1 
ATOM   304  C  CG    . ASP A 1 40  ? 4.24282   10.64156  -18.13878 1.000 36.81740 ? 40  ASP A CG    1 
ATOM   305  O  OD1   . ASP A 1 40  ? 3.91881   11.84855  -18.12577 1.000 37.68102 ? 40  ASP A OD1   1 
ATOM   306  O  OD2   . ASP A 1 40  ? 3.59081   9.76255   -18.73977 1.000 37.24870 ? 40  ASP A OD2   1 
ATOM   307  N  N     . PRO A 1 41  ? 3.54788   10.92355  -14.43276 1.000 33.36386 ? 41  PRO A N     1 
ATOM   308  C  CA    . PRO A 1 41  ? 2.41989   10.41155  -13.63975 1.000 35.85690 ? 41  PRO A CA    1 
ATOM   309  C  C     . PRO A 1 41  ? 1.22088   9.97254   -14.46273 1.000 40.64215 ? 41  PRO A C     1 
ATOM   310  O  O     . PRO A 1 41  ? 0.26689   9.43654   -13.88571 1.000 44.16172 ? 41  PRO A O     1 
ATOM   311  C  CB    . PRO A 1 41  ? 2.05690   11.60555  -12.74474 1.000 32.24941 ? 41  PRO A CB    1 
ATOM   312  C  CG    . PRO A 1 41  ? 2.47489   12.79255  -13.53175 1.000 32.45148 ? 41  PRO A CG    1 
ATOM   313  C  CD    . PRO A 1 41  ? 3.72988   12.37455  -14.25877 1.000 33.07454 ? 41  PRO A CD    1 
ATOM   314  N  N     . HIS A 1 42  ? 1.22786   10.17954  -15.78073 1.000 40.27227 ? 42  HIS A N     1 
ATOM   315  C  CA    . HIS A 1 42  ? 0.12785   9.76654   -16.64271 1.000 41.25394 ? 42  HIS A CA    1 
ATOM   316  C  C     . HIS A 1 42  ? 0.52583   8.63654   -17.58472 1.000 41.62086 ? 42  HIS A C     1 
ATOM   317  O  O     . HIS A 1 42  ? -0.12518  8.43654   -18.61570 1.000 46.95746 ? 42  HIS A O     1 
ATOM   318  C  CB    . HIS A 1 42  ? -0.39517  10.96054  -17.44170 1.000 43.46708 ? 42  HIS A CB    1 
ATOM   319  C  CG    . HIS A 1 42  ? -0.84816  12.10554  -16.59069 1.000 47.19055 ? 42  HIS A CG    1 
ATOM   320  N  ND1   . HIS A 1 42  ? -2.15816  12.26353  -16.19167 1.000 43.12120 ? 42  HIS A ND1   1 
ATOM   321  C  CD2   . HIS A 1 42  ? -0.16416  13.14654  -16.05870 1.000 38.28389 ? 42  HIS A CD2   1 
ATOM   322  C  CE1   . HIS A 1 42  ? -2.26215  13.35453  -15.45367 1.000 49.55519 ? 42  HIS A CE1   1 
ATOM   323  N  NE2   . HIS A 1 42  ? -1.06715  13.90754  -15.35669 1.000 44.25909 ? 42  HIS A NE2   1 
ATOM   324  N  N     . PHE A 1 43  ? 1.57784   7.88755   -17.24773 1.000 32.97811 ? 43  PHE A N     1 
ATOM   325  C  CA    . PHE A 1 43  ? 2.08283   6.87755   -18.16974 1.000 41.51754 ? 43  PHE A CA    1 
ATOM   326  C  C     . PHE A 1 43  ? 1.07883   5.74754   -18.36373 1.000 51.89222 ? 43  PHE A C     1 
ATOM   327  O  O     . PHE A 1 43  ? 0.89281   5.26254   -19.48672 1.000 49.75574 ? 43  PHE A O     1 
ATOM   328  C  CB    . PHE A 1 43  ? 3.42084   6.33455   -17.67076 1.000 45.15404 ? 43  PHE A CB    1 
ATOM   329  C  CG    . PHE A 1 43  ? 4.26682   5.72256   -18.75378 1.000 50.52343 ? 43  PHE A CG    1 
ATOM   330  C  CD1   . PHE A 1 43  ? 5.04381   6.52356   -19.57779 1.000 46.08510 ? 43  PHE A CD1   1 
ATOM   331  C  CD2   . PHE A 1 43  ? 4.28683   4.34956   -18.95078 1.000 46.06766 ? 43  PHE A CD2   1 
ATOM   332  C  CE1   . PHE A 1 43  ? 5.82279   5.96756   -20.57780 1.000 45.12467 ? 43  PHE A CE1   1 
ATOM   333  C  CE2   . PHE A 1 43  ? 5.06581   3.78756   -19.94879 1.000 44.66994 ? 43  PHE A CE2   1 
ATOM   334  C  CZ    . PHE A 1 43  ? 5.83479   4.59756   -20.76381 1.000 48.89199 ? 43  PHE A CZ    1 
ATOM   335  N  N     . LEU A 1 44  ? 0.41885   5.31354   -17.28671 1.000 47.94304 ? 44  LEU A N     1 
ATOM   336  C  CA    . LEU A 1 44  ? -0.57915  4.26054   -17.42870 1.000 45.34739 ? 44  LEU A CA    1 
ATOM   337  C  C     . LEU A 1 44  ? -1.79016  4.74053   -18.21368 1.000 51.12216 ? 44  LEU A C     1 
ATOM   338  O  O     . LEU A 1 44  ? -2.45317  3.93953   -18.88067 1.000 52.70096 ? 44  LEU A O     1 
ATOM   339  C  CB    . LEU A 1 44  ? -1.00912  3.74454   -16.05669 1.000 42.56447 ? 44  LEU A CB    1 
ATOM   340  C  CG    . LEU A 1 44  ? -0.13811  2.65454   -15.43671 0.000 36.26677 ? 44  LEU A CG    1 
ATOM   341  C  CD1   . LEU A 1 44  ? -0.74909  2.16954   -14.13170 0.000 29.64838 ? 44  LEU A CD1   1 
ATOM   342  C  CD2   . LEU A 1 44  ? 0.03888   1.50354   -16.41471 0.000 35.64964 ? 44  LEU A CD2   1 
ATOM   343  N  N     . GLN A 1 45  ? -2.08817  6.03653   -18.15167 1.000 52.96954 ? 45  GLN A N     1 
ATOM   344  C  CA    . GLN A 1 45  ? -3.20918  6.61053   -18.89365 1.000 53.38573 ? 45  GLN A CA    1 
ATOM   345  C  C     . GLN A 1 45  ? -2.74221  6.98353   -20.30166 1.000 54.43587 ? 45  GLN A C     1 
ATOM   346  O  O     . GLN A 1 45  ? -2.66622  8.15153   -20.68966 1.000 52.41188 ? 45  GLN A O     1 
ATOM   347  C  CB    . GLN A 1 45  ? -3.77817  7.81053   -18.14964 1.000 55.18345 ? 45  GLN A CB    1 
ATOM   348  C  CG    . GLN A 1 45  ? -3.70015  7.68953   -16.63865 0.000 51.45773 ? 45  GLN A CG    1 
ATOM   349  C  CD    . GLN A 1 45  ? -4.27414  8.89853   -15.92664 0.000 50.46383 ? 45  GLN A CD    1 
ATOM   350  O  OE1   . GLN A 1 45  ? -3.54714  9.82053   -15.55765 0.000 48.78581 ? 45  GLN A OE1   1 
ATOM   351  N  NE2   . GLN A 1 45  ? -5.58714  8.90052   -15.73061 0.000 50.70641 ? 45  GLN A NE2   1 
ATOM   352  N  N     . GLN A 1 46  ? -2.42021  5.94853   -21.07067 1.000 54.39344 ? 46  GLN A N     1 
ATOM   353  C  CA    . GLN A 1 46  ? -1.96524  6.12054   -22.44467 1.000 56.45921 ? 46  GLN A CA    1 
ATOM   354  C  C     . GLN A 1 46  ? -2.76425  5.23753   -23.39966 1.000 44.40482 ? 46  GLN A C     1 
ATOM   355  O  O     . GLN A 1 46  ? -2.50025  4.04153   -23.52167 1.000 43.12362 ? 46  GLN A O     1 
ATOM   356  C  CB    . GLN A 1 46  ? -0.46924  5.80954   -22.55770 1.000 51.49547 ? 46  GLN A CB    1 
ATOM   357  C  CG    . GLN A 1 46  ? 0.43976   6.94254   -22.10571 0.000 49.50169 ? 46  GLN A CG    1 
ATOM   358  C  CD    . GLN A 1 46  ? 1.89777   6.52755   -22.03174 0.000 47.75732 ? 46  GLN A CD    1 
ATOM   359  O  OE1   . GLN A 1 46  ? 2.22777   5.34855   -22.16974 0.000 48.02800 ? 46  GLN A OE1   1 
ATOM   360  N  NE2   . GLN A 1 46  ? 2.77877   7.49555   -21.80675 0.000 46.72499 ? 46  GLN A NE2   1 
ATOM   361  N  N     . LYS A 1 50  ? -0.13720  -1.86246  -21.54171 1.000 25.15418 ? 50  LYS A N     1 
ATOM   362  C  CA    . LYS A 1 50  ? 1.12179   -1.31045  -22.02473 1.000 26.13351 ? 50  LYS A CA    1 
ATOM   363  C  C     . LYS A 1 50  ? 2.28581   -1.74145  -21.13975 1.000 28.36273 ? 50  LYS A C     1 
ATOM   364  O  O     . LYS A 1 50  ? 3.26880   -2.30445  -21.62576 1.000 29.90679 ? 50  LYS A O     1 
ATOM   365  C  CB    . LYS A 1 50  ? 1.04879   0.21855   -22.09173 1.000 19.67546 ? 50  LYS A CB    1 
ATOM   366  N  N     . VAL A 1 51  ? 2.17183   -1.47245  -19.83975 1.000 27.09722 ? 51  VAL A N     1 
ATOM   367  C  CA    . VAL A 1 51  ? 3.20985   -1.79845  -18.86576 1.000 24.03782 ? 51  VAL A CA    1 
ATOM   368  C  C     . VAL A 1 51  ? 2.57387   -2.59745  -17.74075 1.000 19.32319 ? 51  VAL A C     1 
ATOM   369  O  O     . VAL A 1 51  ? 1.53888   -2.19745  -17.19674 1.000 24.60016 ? 51  VAL A O     1 
ATOM   370  C  CB    . VAL A 1 51  ? 3.89285   -0.53445  -18.30677 1.000 31.47801 ? 51  VAL A CB    1 
ATOM   371  C  CG1   . VAL A 1 51  ? 5.02487   -0.91144  -17.36179 1.000 23.68167 ? 51  VAL A CG1   1 
ATOM   372  C  CG2   . VAL A 1 51  ? 4.40483   0.34556   -19.43978 1.000 38.14908 ? 51  VAL A CG2   1 
ATOM   373  N  N     . SER A 1 52  ? 3.17588   -3.73345  -17.40676 1.000 19.01722 ? 52  SER A N     1 
ATOM   374  C  CA    A SER A 1 52  ? 2.67590   -4.54745  -16.31176 0.434 13.51777 ? 52  SER A CA    1 
ATOM   375  C  CA    B SER A 1 52  ? 2.66490   -4.53845  -16.31276 0.566 13.46598 ? 52  SER A CA    1 
ATOM   376  C  C     . SER A 1 52  ? 3.15592   -3.99745  -14.97476 1.000 12.83418 ? 52  SER A C     1 
ATOM   377  O  O     . SER A 1 52  ? 4.16692   -3.29545  -14.88578 1.000 14.49845 ? 52  SER A O     1 
ATOM   378  C  CB    A SER A 1 52  ? 3.12190   -6.00245  -16.46876 0.434 10.57694 ? 52  SER A CB    1 
ATOM   379  C  CB    B SER A 1 52  ? 3.08190   -6.00145  -16.46876 0.566 10.59218 ? 52  SER A CB    1 
ATOM   380  O  OG    A SER A 1 52  ? 2.79092   -6.76345  -15.31876 0.434 12.09312 ? 52  SER A OG    1 
ATOM   381  O  OG    B SER A 1 52  ? 4.46091   -6.16144  -16.20279 0.566 10.05164 ? 52  SER A OG    1 
ATOM   382  N  N     . VAL A 1 53  ? 2.41694   -4.33445  -13.91875 1.000 10.44325 ? 53  VAL A N     1 
ATOM   383  C  CA    . VAL A 1 53  ? 2.83996   -3.90945  -12.59076 1.000 12.87550 ? 53  VAL A CA    1 
ATOM   384  C  C     . VAL A 1 53  ? 4.18197   -4.53745  -12.24578 1.000 11.39474 ? 53  VAL A C     1 
ATOM   385  O  O     . VAL A 1 53  ? 4.95098   -3.98244  -11.45579 1.000 11.53611 ? 53  VAL A O     1 
ATOM   386  C  CB    . VAL A 1 53  ? 1.76398   -4.25246  -11.54374 1.000 15.28750 ? 53  VAL A CB    1 
ATOM   387  C  CG1   . VAL A 1 53  ? 1.62199   -5.75846  -11.40574 1.000 15.87558 ? 53  VAL A CG1   1 
ATOM   388  C  CG2   . VAL A 1 53  ? 2.10400   -3.59945  -10.20575 1.000 17.89023 ? 53  VAL A CG2   1 
ATOM   389  N  N     . ASN A 1 54  ? 4.49696   -5.68445  -12.85579 1.000 10.00900 ? 54  ASN A N     1 
ATOM   390  C  CA    . ASN A 1 54  ? 5.73997   -6.39244  -12.55781 1.000 10.29067 ? 54  ASN A CA    1 
ATOM   391  C  C     . ASN A 1 54  ? 6.96096   -5.56244  -12.94183 1.000 9.42537  ? 54  ASN A C     1 
ATOM   392  O  O     . ASN A 1 54  ? 7.86797   -5.36543  -12.12784 1.000 11.39644 ? 54  ASN A O     1 
ATOM   393  C  CB    . ASN A 1 54  ? 5.75296   -7.75144  -13.27381 1.000 10.11402 ? 54  ASN A CB    1 
ATOM   394  C  CG    . ASN A 1 54  ? 5.03498   -8.84144  -12.48680 1.000 11.54682 ? 54  ASN A CG    1 
ATOM   395  O  OD1   . ASN A 1 54  ? 4.91200   -8.76444  -11.26279 1.000 10.80620 ? 54  ASN A OD1   1 
ATOM   396  N  ND2   . ASN A 1 54  ? 4.56597   -9.86945  -13.18879 1.000 10.38652 ? 54  ASN A ND2   1 
ATOM   397  N  N     . ARG A 1 55  ? 7.00902   -5.06060  -14.17925 1.000 9.36074  ? 55  ARG A N     1 
ATOM   398  C  CA    . ARG A 1 55  ? 8.18497   -4.29160  -14.57824 1.000 10.30298 ? 55  ARG A CA    1 
ATOM   399  C  C     . ARG A 1 55  ? 8.18920   -2.90788  -13.93764 1.000 11.66014 ? 55  ARG A C     1 
ATOM   400  O  O     . ARG A 1 55  ? 9.25188   -2.39792  -13.56362 1.000 10.48759 ? 55  ARG A O     1 
ATOM   401  C  CB    . ARG A 1 55  ? 8.27978   -4.17452  -16.10171 1.000 12.79448 ? 55  ARG A CB    1 
ATOM   402  C  CG    . ARG A 1 55  ? 9.55173   -3.44762  -16.54772 1.000 11.95825 ? 55  ARG A CG    1 
ATOM   403  C  CD    . ARG A 1 55  ? 9.81856   -3.53672  -18.04439 1.000 12.66568 ? 55  ARG A CD    1 
ATOM   404  N  NE    . ARG A 1 55  ? 8.86350   -2.76567  -18.82988 1.000 17.01355 ? 55  ARG A NE    1 
ATOM   405  C  CZ    . ARG A 1 55  ? 7.84780   -3.29535  -19.49631 1.000 16.38826 ? 55  ARG A CZ    1 
ATOM   406  N  NH1   . ARG A 1 55  ? 7.64153   -4.60210  -19.51602 1.000 15.93226 ? 55  ARG A NH1   1 
ATOM   407  N  NH2   . ARG A 1 55  ? 7.01865   -2.49467  -20.15940 1.000 14.81414 ? 55  ARG A NH2   1 
ATOM   408  N  N     . TYR A 1 56  ? 7.01693   -2.28344  -13.79383 1.000 10.25851 ? 56  TYR A N     1 
ATOM   409  C  CA    . TYR A 1 56  ? 6.98694   -0.94844  -13.20183 1.000 13.43403 ? 56  TYR A CA    1 
ATOM   410  C  C     . TYR A 1 56  ? 7.36596   -0.98944  -11.72583 1.000 9.09772  ? 56  TYR A C     1 
ATOM   411  O  O     . TYR A 1 56  ? 8.08297   -0.10843  -11.24184 1.000 9.04626  ? 56  TYR A O     1 
ATOM   412  C  CB    . TYR A 1 56  ? 5.61393   -0.30044  -13.38580 1.000 10.70094 ? 56  TYR A CB    1 
ATOM   413  C  CG    . TYR A 1 56  ? 5.68193   1.20756   -13.33580 1.000 12.30990 ? 56  TYR A CG    1 
ATOM   414  C  CD1   . TYR A 1 56  ? 5.91191   1.94756   -14.48881 1.000 17.98496 ? 56  TYR A CD1   1 
ATOM   415  C  CD2   . TYR A 1 56  ? 5.54995   1.89056   -12.13780 1.000 12.74050 ? 56  TYR A CD2   1 
ATOM   416  C  CE1   . TYR A 1 56  ? 5.98890   3.32356   -14.45381 1.000 24.80765 ? 56  TYR A CE1   1 
ATOM   417  C  CE2   . TYR A 1 56  ? 5.62294   3.27456   -12.09180 1.000 24.32136 ? 56  TYR A CE2   1 
ATOM   418  C  CZ    . TYR A 1 56  ? 5.84592   3.98356   -13.25381 1.000 30.83005 ? 56  TYR A CZ    1 
ATOM   419  O  OH    . TYR A 1 56  ? 5.92292   5.35556   -13.22381 1.000 34.04845 ? 56  TYR A OH    1 
ATOM   420  N  N     . ASN A 1 57  ? 6.90098   -2.00544  -10.99282 1.000 10.12504 ? 57  ASN A N     1 
ATOM   421  C  CA    . ASN A 1 57  ? 7.32700   -2.14644  -9.60283  1.000 10.68363 ? 57  ASN A CA    1 
ATOM   422  C  C     . ASN A 1 57  ? 8.81301   -2.46443  -9.50586  1.000 11.85197 ? 57  ASN A C     1 
ATOM   423  O  O     . ASN A 1 57  ? 9.47802   -2.01243  -8.56987  1.000 11.33901 ? 57  ASN A O     1 
ATOM   424  C  CB    . ASN A 1 57  ? 6.50202   -3.22044  -8.89282  1.000 19.57390 ? 57  ASN A CB    1 
ATOM   425  C  CG    . ASN A 1 57  ? 6.78404   -3.28444  -7.40382  1.000 17.85371 ? 57  ASN A CG    1 
ATOM   426  O  OD1   . ASN A 1 57  ? 6.32305   -2.43844  -6.63382  1.000 16.43455 ? 57  ASN A OD1   1 
ATOM   427  N  ND2   . ASN A 1 57  ? 7.54105   -4.29144  -6.98884  1.000 17.07422 ? 57  ASN A ND2   1 
ATOM   428  N  N     . PHE A 1 58  ? 9.35299   -3.22943  -10.45987 1.000 9.93973  ? 58  PHE A N     1 
ATOM   429  C  CA    . PHE A 1 58  ? 10.79999  -3.42942  -10.50889 1.000 10.84970 ? 58  PHE A CA    1 
ATOM   430  C  C     . PHE A 1 58  ? 11.53699  -2.09542  -10.60090 1.000 9.23782  ? 58  PHE A C     1 
ATOM   431  O  O     . PHE A 1 58  ? 12.55700  -1.89442  -9.93192  1.000 11.03428 ? 58  PHE A O     1 
ATOM   432  C  CB    . PHE A 1 58  ? 11.16998  -4.33242  -11.68590 1.000 8.59792  ? 58  PHE A CB    1 
ATOM   433  C  CG    . PHE A 1 58  ? 12.59698  -4.79942  -11.66992 1.000 8.42439  ? 58  PHE A CG    1 
ATOM   434  C  CD1   . PHE A 1 58  ? 13.60197  -4.02141  -12.21794 1.000 11.19978 ? 58  PHE A CD1   1 
ATOM   435  C  CD2   . PHE A 1 58  ? 12.93499  -6.02642  -11.11993 1.000 10.37012 ? 58  PHE A CD2   1 
ATOM   436  C  CE1   . PHE A 1 58  ? 14.91397  -4.44741  -12.20296 1.000 9.54982  ? 58  PHE A CE1   1 
ATOM   437  C  CE2   . PHE A 1 58  ? 14.24799  -6.45641  -11.10695 1.000 8.67300  ? 58  PHE A CE2   1 
ATOM   438  C  CZ    . PHE A 1 58  ? 15.23698  -5.66241  -11.64696 1.000 8.18110  ? 58  PHE A CZ    1 
ATOM   439  N  N     . LEU A 1 59  ? 11.02597  -1.16742  -11.41389 1.000 9.16542  ? 59  LEU A N     1 
ATOM   440  C  CA    . LEU A 1 59  ? 11.63496  0.15758   -11.51790 1.000 8.31057  ? 59  LEU A CA    1 
ATOM   441  C  C     . LEU A 1 59  ? 11.53198  0.91758   -10.19990 1.000 8.44932  ? 59  LEU A C     1 
ATOM   442  O  O     . LEU A 1 59  ? 12.51299  1.51858   -9.74092  1.000 11.11216 ? 59  LEU A O     1 
ATOM   443  C  CB    . LEU A 1 59  ? 10.97894  0.94858   -12.65089 1.000 8.36352  ? 59  LEU A CB    1 
ATOM   444  C  CG    . LEU A 1 59  ? 11.26994  2.45358   -12.74690 1.000 8.29406  ? 59  LEU A CG    1 
ATOM   445  C  CD1   . LEU A 1 59  ? 12.73893  2.74958   -13.01392 1.000 8.08539  ? 59  LEU A CD1   1 
ATOM   446  C  CD2   . LEU A 1 59  ? 10.39392  3.08858   -13.81788 1.000 9.77593  ? 59  LEU A CD2   1 
ATOM   447  N  N     . LEU A 1 60  ? 10.34799  0.91057   -9.57988  1.000 8.56864  ? 60  LEU A N     1 
ATOM   448  C  CA    . LEU A 1 60  ? 10.16701  1.62757   -8.32088  1.000 9.79202  ? 60  LEU A CA    1 
ATOM   449  C  C     . LEU A 1 60  ? 11.06603  1.06758   -7.22289  1.000 8.62065  ? 60  LEU A C     1 
ATOM   450  O  O     . LEU A 1 60  ? 11.64704  1.82758   -6.43990  1.000 10.14316 ? 60  LEU A O     1 
ATOM   451  C  CB    . LEU A 1 60  ? 8.70102   1.57857   -7.89685  1.000 8.94511  ? 60  LEU A CB    1 
ATOM   452  C  CG    . LEU A 1 60  ? 7.73000   2.32756   -8.81284  1.000 12.41304 ? 60  LEU A CG    1 
ATOM   453  C  CD1   . LEU A 1 60  ? 6.28801   2.13656   -8.35581  1.000 14.50184 ? 60  LEU A CD1   1 
ATOM   454  C  CD2   . LEU A 1 60  ? 8.08799   3.80657   -8.88384  1.000 9.90617  ? 60  LEU A CD2   1 
ATOM   455  N  N     . GLU A 1 61  ? 11.19804  -0.25942  -7.15190  1.000 8.66155  ? 61  GLU A N     1 
ATOM   456  C  CA    . GLU A 1 61  ? 12.12106  -0.84942  -6.18591  1.000 13.03948 ? 61  GLU A CA    1 
ATOM   457  C  C     . GLU A 1 61  ? 13.56205  -0.44642  -6.47094  1.000 8.42172  ? 61  GLU A C     1 
ATOM   458  O  O     . GLU A 1 61  ? 14.36306  -0.30941  -5.54095  1.000 11.09697 ? 61  GLU A O     1 
ATOM   459  C  CB    . GLU A 1 61  ? 11.98906  -2.37042  -6.18491  1.000 9.60677  ? 61  GLU A CB    1 
ATOM   460  C  CG    . GLU A 1 61  ? 10.69907  -2.87243  -5.58089  1.000 14.28658 ? 61  GLU A CG    1 
ATOM   461  C  CD    . GLU A 1 61  ? 10.54008  -4.36743  -5.72789  1.000 10.25283 ? 61  GLU A CD    1 
ATOM   462  O  OE1   . GLU A 1 61  ? 11.45907  -5.00442  -6.27490  1.000 9.88129  ? 61  GLU A OE1   1 
ATOM   463  O  OE2   . GLU A 1 61  ? 9.49708   -4.90343  -5.30287  1.000 10.77514 ? 61  GLU A OE2   1 
ATOM   464  N  N     . SER A 1 62  ? 13.90803  -0.25741  -7.74594  1.000 8.25223  ? 62  SER A N     1 
ATOM   465  C  CA    . SER A 1 62  ? 15.24502  0.20959   -8.08696  1.000 8.06710  ? 62  SER A CA    1 
ATOM   466  C  C     . SER A 1 62  ? 15.45802  1.64859   -7.64197  1.000 8.45877  ? 62  SER A C     1 
ATOM   467  O  O     . SER A 1 62  ? 16.57203  2.01659   -7.25998  1.000 7.96916  ? 62  SER A O     1 
ATOM   468  C  CB    . SER A 1 62  ? 15.48600  0.07459   -9.59097  1.000 7.94467  ? 62  SER A CB    1 
ATOM   469  O  OG    . SER A 1 62  ? 15.41799  -1.28241  -9.99697  1.000 7.98154  ? 62  SER A OG    1 
ATOM   470  N  N     . LEU A 1 63  ? 14.40002  2.46459   -7.67395  1.000 11.87498 ? 63  LEU A N     1 
ATOM   471  C  CA    . LEU A 1 63  ? 14.50302  3.83559   -7.18795  1.000 12.92763 ? 63  LEU A CA    1 
ATOM   472  C  C     . LEU A 1 63  ? 14.59105  3.86859   -5.66495  1.000 14.38837 ? 63  LEU A C     1 
ATOM   473  O  O     . LEU A 1 63  ? 15.39006  4.62859   -5.10096  1.000 12.73559 ? 63  LEU A O     1 
ATOM   474  C  CB    . LEU A 1 63  ? 13.31701  4.66058   -7.69293  1.000 11.25327 ? 63  LEU A CB    1 
ATOM   475  C  CG    . LEU A 1 63  ? 13.20499  4.82258   -9.21793  1.000 8.65862  ? 63  LEU A CG    1 
ATOM   476  C  CD1   . LEU A 1 63  ? 11.93598  5.55758   -9.62191  1.000 8.27460  ? 63  LEU A CD1   1 
ATOM   477  C  CD2   . LEU A 1 63  ? 14.42397  5.52559   -9.78795  1.000 7.96813  ? 63  LEU A CD2   1 
ATOM   478  N  N     . GLU A 1 64  ? 13.79906  3.03458   -4.98294  1.000 10.05076 ? 64  GLU A N     1 
ATOM   479  C  CA    . GLU A 1 64  ? 13.90109  2.94958   -3.52794  1.000 13.00385 ? 64  GLU A CA    1 
ATOM   480  C  C     . GLU A 1 64  ? 15.31010  2.56559   -3.09896  1.000 12.88091 ? 64  GLU A C     1 
ATOM   481  O  O     . GLU A 1 64  ? 15.81211  3.05559   -2.08097  1.000 11.38081 ? 64  GLU A O     1 
ATOM   482  C  CB    . GLU A 1 64  ? 12.88610  1.94558   -2.97992  1.000 16.37251 ? 64  GLU A CB    1 
ATOM   483  C  CG    . GLU A 1 64  ? 11.44910  2.41758   -3.07990  1.000 15.02579 ? 64  GLU A CG    1 
ATOM   484  C  CD    . GLU A 1 64  ? 10.50911  1.61357   -2.21488  1.000 22.59902 ? 64  GLU A CD    1 
ATOM   485  O  OE1   . GLU A 1 64  ? 10.93713  0.57257   -1.67389  1.000 33.88003 ? 64  GLU A OE1   1 
ATOM   486  O  OE2   . GLU A 1 64  ? 9.33911   2.02657   -2.07386  1.000 28.40150 ? 64  GLU A OE2   1 
ATOM   487  N  N     . ASP A 1 65  ? 15.96309  1.68959   -3.86497  1.000 11.98884 ? 65  ASP A N     1 
ATOM   488  C  CA    . ASP A 1 65  ? 17.33709  1.30960   -3.56000  1.000 8.65252  ? 65  ASP A CA    1 
ATOM   489  C  C     . ASP A 1 65  ? 18.28908  2.48460   -3.75301  1.000 11.00310 ? 65  ASP A C     1 
ATOM   490  O  O     . ASP A 1 65  ? 19.16610  2.72760   -2.91503  1.000 15.70560 ? 65  ASP A O     1 
ATOM   491  C  CB    . ASP A 1 65  ? 17.75408  0.12860   -4.43200  1.000 13.56793 ? 65  ASP A CB    1 
ATOM   492  C  CG    . ASP A 1 65  ? 19.09709  -0.42840  -4.04403  1.000 11.60736 ? 65  ASP A CG    1 
ATOM   493  O  OD1   . ASP A 1 65  ? 19.21311  -0.95340  -2.91403  1.000 17.00869 ? 65  ASP A OD1   1 
ATOM   494  O  OD2   . ASP A 1 65  ? 20.03208  -0.34140  -4.86204  1.000 10.73384 ? 65  ASP A OD2   1 
ATOM   495  N  N     . LEU A 1 66  ? 18.14006  3.21860   -4.86101  1.000 10.09475 ? 66  LEU A N     1 
ATOM   496  C  CA    . LEU A 1 66  ? 18.93106  4.43260   -5.06102  1.000 9.45749  ? 66  LEU A CA    1 
ATOM   497  C  C     . LEU A 1 66  ? 18.69807  5.42760   -3.93502  1.000 8.44108  ? 66  LEU A C     1 
ATOM   498  O  O     . LEU A 1 66  ? 19.64208  6.07560   -3.46403  1.000 8.18348  ? 66  LEU A O     1 
ATOM   499  C  CB    . LEU A 1 66  ? 18.59603  5.07860   -6.40602  1.000 8.16421  ? 66  LEU A CB    1 
ATOM   500  C  CG    . LEU A 1 66  ? 19.14901  4.47760   -7.69703  1.000 9.35955  ? 66  LEU A CG    1 
ATOM   501  C  CD1   . LEU A 1 66  ? 18.66899  5.28560   -8.88602  1.000 7.70114  ? 66  LEU A CD1   1 
ATOM   502  C  CD2   . LEU A 1 66  ? 20.66501  4.43761   -7.65905  1.000 8.46008  ? 66  LEU A CD2   1 
ATOM   503  N  N     . GLN A 1 67  ? 17.45108  5.54560   -3.47400  1.000 8.27633  ? 67  GLN A N     1 
ATOM   504  C  CA    . GLN A 1 67  ? 17.14209  6.49159   -2.40699  1.000 10.81130 ? 67  GLN A CA    1 
ATOM   505  C  C     . GLN A 1 67  ? 17.90712  6.15960   -1.13201  1.000 11.24396 ? 67  GLN A C     1 
ATOM   506  O  O     . GLN A 1 67  ? 18.44612  7.05660   -0.47701  1.000 10.06098 ? 67  GLN A O     1 
ATOM   507  C  CB    . GLN A 1 67  ? 15.63510  6.51859   -2.13597  1.000 11.20282 ? 67  GLN A CB    1 
ATOM   508  C  CG    . GLN A 1 67  ? 15.20511  7.49959   -1.04996  1.000 9.65408  ? 67  GLN A CG    1 
ATOM   509  C  CD    . GLN A 1 67  ? 15.28210  8.94759   -1.49096  1.000 15.99751 ? 67  GLN A CD    1 
ATOM   510  O  OE1   . GLN A 1 67  ? 16.34210  9.57559   -1.43298  1.000 14.79325 ? 67  GLN A OE1   1 
ATOM   511  N  NE2   . GLN A 1 67  ? 14.15109  9.48758   -1.93994  1.000 14.86292 ? 67  GLN A NE2   1 
ATOM   512  N  N     . ARG A 1 68  ? 17.96592  4.87546   -0.76297  1.000 10.59175 ? 68  ARG A N     1 
ATOM   513  C  CA    . ARG A 1 68  ? 18.71634  4.48594   0.42757   1.000 13.64090 ? 68  ARG A CA    1 
ATOM   514  C  C     . ARG A 1 68  ? 20.21259  4.71369   0.24863   1.000 13.72890 ? 68  ARG A C     1 
ATOM   515  O  O     . ARG A 1 68  ? 20.91959  4.98960   1.22651   1.000 12.05454 ? 68  ARG A O     1 
ATOM   516  C  CB    . ARG A 1 68  ? 18.44608  3.01958   0.77011   1.000 13.21405 ? 68  ARG A CB    1 
ATOM   517  C  CG    . ARG A 1 68  ? 16.99719  2.70199   1.09741   1.000 16.81628 ? 68  ARG A CG    1 
ATOM   518  C  CD    . ARG A 1 68  ? 16.84873  1.27275   1.60521   1.000 19.11682 ? 68  ARG A CD    1 
ATOM   519  N  NE    . ARG A 1 68  ? 17.23321  0.28506   0.60252   1.000 27.18924 ? 68  ARG A NE    1 
ATOM   520  C  CZ    . ARG A 1 68  ? 16.39238  -0.28115  -0.25278  1.000 21.79600 ? 68  ARG A CZ    1 
ATOM   521  N  NH1   . ARG A 1 68  ? 15.10368  0.01729   -0.25581  1.000 21.47895 ? 68  ARG A NH1   1 
ATOM   522  N  NH2   . ARG A 1 68  ? 16.85593  -1.16931  -1.12727  1.000 30.49038 ? 68  ARG A NH2   1 
ATOM   523  N  N     . SER A 1 69  ? 20.70912  4.60861   -0.98605  1.000 11.33844 ? 69  SER A N     1 
ATOM   524  C  CA    . SER A 1 69  ? 22.13712  4.77861   -1.22808  1.000 11.71441 ? 69  SER A CA    1 
ATOM   525  C  C     . SER A 1 69  ? 22.55912  6.23661   -1.08408  1.000 13.54465 ? 69  SER A C     1 
ATOM   526  O  O     . SER A 1 69  ? 23.59713  6.52662   -0.47410  1.000 15.72432 ? 69  SER A O     1 
ATOM   527  C  CB    . SER A 1 69  ? 22.50210  4.23961   -2.61108  1.000 12.41265 ? 69  SER A CB    1 
ATOM   528  O  OG    . SER A 1 69  ? 22.38310  2.82761   -2.64008  1.000 8.79694  ? 69  SER A OG    1 
ATOM   529  N  N     . PHE A 1 70  ? 21.77610  7.16861   -1.63807  1.000 11.35789 ? 70  PHE A N     1 
ATOM   530  C  CA    . PHE A 1 70  ? 22.10210  8.58361   -1.47707  1.000 13.00061 ? 70  PHE A CA    1 
ATOM   531  C  C     . PHE A 1 70  ? 21.94312  9.02361   -0.02707  1.000 12.77474 ? 70  PHE A C     1 
ATOM   532  O  O     . PHE A 1 70  ? 22.72013  9.85061   0.46092   1.000 15.28157 ? 70  PHE A O     1 
ATOM   533  C  CB    . PHE A 1 70  ? 21.23608  9.44861   -2.39406  1.000 11.24727 ? 70  PHE A CB    1 
ATOM   534  C  CG    . PHE A 1 70  ? 21.56206  9.30661   -3.85006  1.000 12.66911 ? 70  PHE A CG    1 
ATOM   535  C  CD1   . PHE A 1 70  ? 22.77505  9.74561   -4.34608  1.000 15.46454 ? 70  PHE A CD1   1 
ATOM   536  C  CD2   . PHE A 1 70  ? 20.65205  8.74361   -4.72905  1.000 10.69109 ? 70  PHE A CD2   1 
ATOM   537  C  CE1   . PHE A 1 70  ? 23.08103  9.61462   -5.68909  1.000 7.99224  ? 70  PHE A CE1   1 
ATOM   538  C  CE2   . PHE A 1 70  ? 20.95303  8.61461   -6.07106  1.000 10.15594 ? 70  PHE A CE2   1 
ATOM   539  C  CZ    . PHE A 1 70  ? 22.17402  9.05161   -6.54708  1.000 10.91683 ? 70  PHE A CZ    1 
ATOM   540  N  N     . GLN A 1 71  ? 20.94614  8.48361   0.67795   1.000 11.61752 ? 71  GLN A N     1 
ATOM   541  C  CA    . GLN A 1 71  ? 20.74216  8.86761   2.07195   1.000 13.88751 ? 71  GLN A CA    1 
ATOM   542  C  C     . GLN A 1 71  ? 21.92318  8.44661   2.94093   1.000 13.25061 ? 71  GLN A C     1 
ATOM   543  O  O     . GLN A 1 71  ? 22.36519  9.20661   3.81092   1.000 13.11480 ? 71  GLN A O     1 
ATOM   544  C  CB    . GLN A 1 71  ? 19.43517  8.27260   2.59897   1.000 15.04012 ? 71  GLN A CB    1 
ATOM   545  C  CG    . GLN A 1 71  ? 18.17616  8.94060   2.05499   1.000 18.33813 ? 71  GLN A CG    1 
ATOM   546  C  CD    . GLN A 1 71  ? 16.90517  8.38559   2.66901   1.000 22.18597 ? 71  GLN A CD    1 
ATOM   547  O  OE1   . GLN A 1 71  ? 16.95719  7.54559   3.56301   1.000 20.07294 ? 71  GLN A OE1   1 
ATOM   548  N  NE2   . GLN A 1 71  ? 15.75416  8.86059   2.19703   1.000 24.62579 ? 71  GLN A NE2   1 
ATOM   549  N  N     . ALA A 1 72  ? 22.45818  7.24361   2.71092   1.000 15.85377 ? 72  ALA A N     1 
ATOM   550  C  CA    . ALA A 1 72  ? 23.66119  6.81661   3.41490   1.000 12.89105 ? 72  ALA A CA    1 
ATOM   551  C  C     . ALA A 1 72  ? 24.85618  7.71562   3.11488   1.000 15.20236 ? 72  ALA A C     1 
ATOM   552  O  O     . ALA A 1 72  ? 25.80619  7.75662   3.90486   1.000 14.19860 ? 72  ALA A O     1 
ATOM   553  C  CB    . ALA A 1 72  ? 23.99319  5.36562   3.05689   1.000 16.67930 ? 72  ALA A CB    1 
ATOM   554  N  N     . ARG A 1 73  ? 24.82594  8.44850   2.00113   1.000 17.26237 ? 73  ARG A N     1 
ATOM   555  C  CA    . ARG A 1 73  ? 25.90869  9.34448   1.61630   1.000 11.97673 ? 73  ARG A CA    1 
ATOM   556  C  C     . ARG A 1 73  ? 25.55880  10.81455  1.83847   1.000 17.01366 ? 73  ARG A C     1 
ATOM   557  O  O     . ARG A 1 73  ? 26.23868  11.69702  1.30601   1.000 16.61345 ? 73  ARG A O     1 
ATOM   558  C  CB    . ARG A 1 73  ? 26.29619  9.09838   0.15733   1.000 14.75937 ? 73  ARG A CB    1 
ATOM   559  C  CG    . ARG A 1 73  ? 27.11968  7.83513   -0.05179  1.000 17.25361 ? 73  ARG A CG    1 
ATOM   560  C  CD    . ARG A 1 73  ? 27.29017  7.50653   -1.52595  1.000 19.37837 ? 73  ARG A CD    1 
ATOM   561  N  NE    . ARG A 1 73  ? 28.35276  6.53169   -1.74819  1.000 16.29144 ? 73  ARG A NE    1 
ATOM   562  C  CZ    . ARG A 1 73  ? 28.20026  5.21832   -1.64992  1.000 20.65570 ? 73  ARG A CZ    1 
ATOM   563  N  NH1   . ARG A 1 73  ? 27.03753  4.67975   -1.31911  1.000 23.66801 ? 73  ARG A NH1   1 
ATOM   564  N  NH2   . ARG A 1 73  ? 29.24081  4.42509   -1.88862  1.000 21.68128 ? 73  ARG A NH2   1 
ATOM   565  N  N     . GLY A 1 74  ? 24.51416  11.09462  2.61589   1.000 14.27000 ? 74  GLY A N     1 
ATOM   566  C  CA    . GLY A 1 74  ? 24.14916  12.45562  2.95489   1.000 15.84040 ? 74  GLY A CA    1 
ATOM   567  C  C     . GLY A 1 74  ? 23.32314  13.18661  1.92191   1.000 15.90098 ? 74  GLY A C     1 
ATOM   568  O  O     . GLY A 1 74  ? 23.19414  14.41361  2.01091   1.000 16.11895 ? 74  GLY A O     1 
ATOM   569  N  N     . SER A 1 75  ? 22.75913  12.47761  0.94692   1.000 15.17594 ? 75  SER A N     1 
ATOM   570  C  CA    . SER A 1 75  ? 22.01311  13.10961  -0.13607  1.000 16.82386 ? 75  SER A CA    1 
ATOM   571  C  C     . SER A 1 75  ? 20.57711  12.60361  -0.15805  1.000 13.80419 ? 75  SER A C     1 
ATOM   572  O  O     . SER A 1 75  ? 20.09813  12.04060  0.83096   1.000 15.38185 ? 75  SER A O     1 
ATOM   573  C  CB    . SER A 1 75  ? 22.69709  12.84761  -1.48208  1.000 17.79290 ? 75  SER A CB    1 
ATOM   574  O  OG    . SER A 1 75  ? 22.13807  13.64561  -2.50807  1.000 16.44062 ? 75  SER A OG    1 
ATOM   575  N  N     . ARG A 1 76  ? 19.89175  12.78124  -1.28407  1.000 12.26626 ? 76  ARG A N     1 
ATOM   576  C  CA    . ARG A 1 76  ? 18.49122  12.40320  -1.39051  1.000 12.27480 ? 76  ARG A CA    1 
ATOM   577  C  C     . ARG A 1 76  ? 18.12855  12.29105  -2.86365  1.000 11.09261 ? 76  ARG A C     1 
ATOM   578  O  O     . ARG A 1 76  ? 18.53858  13.12840  -3.67149  1.000 13.01427 ? 76  ARG A O     1 
ATOM   579  C  CB    . ARG A 1 76  ? 17.59686  13.43009  -0.67921  1.000 17.39609 ? 76  ARG A CB    1 
ATOM   580  C  CG    . ARG A 1 76  ? 16.11570  13.09681  -0.64866  1.000 19.59831 ? 76  ARG A CG    1 
ATOM   581  C  CD    . ARG A 1 76  ? 15.37995  14.00347  0.33141   1.000 17.39474 ? 76  ARG A CD    1 
ATOM   582  N  NE    . ARG A 1 76  ? 15.58691  15.41575  0.03334   1.000 17.04358 ? 76  ARG A NE    1 
ATOM   583  C  CZ    . ARG A 1 76  ? 14.72525  16.18040  -0.62392  1.000 22.19144 ? 76  ARG A CZ    1 
ATOM   584  N  NH1   . ARG A 1 76  ? 13.56515  15.70796  -1.04858  1.000 16.07305 ? 76  ARG A NH1   1 
ATOM   585  N  NH2   . ARG A 1 76  ? 15.03543  17.45218  -0.86069  1.000 20.09995 ? 76  ARG A NH2   1 
ATOM   586  N  N     . LEU A 1 77  ? 17.37606  11.24760  -3.20899  1.000 9.81143  ? 77  LEU A N     1 
ATOM   587  C  CA    . LEU A 1 77  ? 16.89604  11.08659  -4.57599  1.000 10.83865 ? 77  LEU A CA    1 
ATOM   588  C  C     . LEU A 1 77  ? 15.63604  11.92059  -4.77797  1.000 10.92712 ? 77  LEU A C     1 
ATOM   589  O  O     . LEU A 1 77  ? 14.73805  11.91459  -3.92895  1.000 16.05738 ? 77  LEU A O     1 
ATOM   590  C  CB    . LEU A 1 77  ? 16.61504  9.61459   -4.87598  1.000 12.20190 ? 77  LEU A CB    1 
ATOM   591  C  CG    . LEU A 1 77  ? 16.04802  9.29459   -6.25797  1.000 9.26916  ? 77  LEU A CG    1 
ATOM   592  C  CD1   . LEU A 1 77  ? 17.02200  9.68460   -7.34299  1.000 11.11296 ? 77  LEU A CD1   1 
ATOM   593  C  CD2   . LEU A 1 77  ? 15.69802  7.82059   -6.36497  1.000 15.90167 ? 77  LEU A CD2   1 
ATOM   594  N  N     . LEU A 1 78  ? 15.57901  12.65159  -5.89396  1.000 8.82897  ? 78  LEU A N     1 
ATOM   595  C  CA    . LEU A 1 78  ? 14.46201  13.53859  -6.21095  1.000 9.54902  ? 78  LEU A CA    1 
ATOM   596  C  C     . LEU A 1 78  ? 13.70799  12.95658  -7.40293  1.000 11.63225 ? 78  LEU A C     1 
ATOM   597  O  O     . LEU A 1 78  ? 14.24097  12.90959  -8.51594  1.000 10.24871 ? 78  LEU A O     1 
ATOM   598  C  CB    . LEU A 1 78  ? 14.95200  14.95759  -6.50395  1.000 9.10875  ? 78  LEU A CB    1 
ATOM   599  C  CG    . LEU A 1 78  ? 15.82001  15.60559  -5.41797  1.000 9.09559  ? 78  LEU A CG    1 
ATOM   600  C  CD1   . LEU A 1 78  ? 16.34300  16.95659  -5.86098  1.000 13.96036 ? 78  LEU A CD1   1 
ATOM   601  C  CD2   . LEU A 1 78  ? 15.04503  15.73859  -4.11995  1.000 11.58298 ? 78  LEU A CD2   1 
ATOM   602  N  N     . VAL A 1 79  ? 12.47899  12.50758  -7.16591  1.000 9.76074  ? 79  VAL A N     1 
ATOM   603  C  CA    . VAL A 1 79  ? 11.60998  11.96658  -8.20490  1.000 8.59009  ? 79  VAL A CA    1 
ATOM   604  C  C     . VAL A 1 79  ? 10.68297  13.09557  -8.64088  1.000 9.92505  ? 79  VAL A C     1 
ATOM   605  O  O     . VAL A 1 79  ? 9.65598   13.35157  -8.00987  1.000 10.79580 ? 79  VAL A O     1 
ATOM   606  C  CB    . VAL A 1 79  ? 10.82399  10.74657  -7.70989  1.000 10.78792 ? 79  VAL A CB    1 
ATOM   607  C  CG1   . VAL A 1 79  ? 9.91797   10.21457  -8.80587  1.000 12.69437 ? 79  VAL A CG1   1 
ATOM   608  C  CG2   . VAL A 1 79  ? 11.77200  9.66458   -7.23790  1.000 11.39458 ? 79  VAL A CG2   1 
ATOM   609  N  N     . LEU A 1 80  ? 11.04095  13.77958  -9.72289  1.000 12.20587 ? 80  LEU A N     1 
ATOM   610  C  CA    . LEU A 1 80  ? 10.22194  14.87557  -10.22287 1.000 11.81804 ? 80  LEU A CA    1 
ATOM   611  C  C     . LEU A 1 80  ? 9.07392   14.34157  -11.07286 1.000 14.79769 ? 80  LEU A C     1 
ATOM   612  O  O     . LEU A 1 80  ? 9.22791   13.37157  -11.82286 1.000 18.63499 ? 80  LEU A O     1 
ATOM   613  C  CB    . LEU A 1 80  ? 11.07792  15.85358  -11.02989 1.000 9.93942  ? 80  LEU A CB    1 
ATOM   614  C  CG    . LEU A 1 80  ? 12.28193  16.41558  -10.26191 1.000 9.75259  ? 80  LEU A CG    1 
ATOM   615  C  CD1   . LEU A 1 80  ? 13.15991  17.29558  -11.12992 1.000 17.69908 ? 80  LEU A CD1   1 
ATOM   616  C  CD2   . LEU A 1 80  ? 11.82395  17.17458  -9.02990  1.000 13.28996 ? 80  LEU A CD2   1 
ATOM   617  N  N     . ARG A 1 81  ? 7.91232   14.97136  -10.94411 1.000 13.96982 ? 81  ARG A N     1 
ATOM   618  C  CA    . ARG A 1 81  ? 6.73500   14.59275  -11.71245 1.000 18.11095 ? 81  ARG A CA    1 
ATOM   619  C  C     . ARG A 1 81  ? 6.59807   15.51345  -12.91817 1.000 17.12643 ? 81  ARG A C     1 
ATOM   620  O  O     . ARG A 1 81  ? 6.69981   16.73684  -12.78484 1.000 18.87388 ? 81  ARG A O     1 
ATOM   621  C  CB    . ARG A 1 81  ? 5.47053   14.65518  -10.85279 1.000 12.35254 ? 81  ARG A CB    1 
ATOM   622  C  CG    . ARG A 1 81  ? 5.12614   13.36465  -10.11254 1.000 15.74411 ? 81  ARG A CG    1 
ATOM   623  C  CD    . ARG A 1 81  ? 6.11201   13.05180  -8.99395  1.000 13.98706 ? 81  ARG A CD    1 
ATOM   624  N  NE    . ARG A 1 81  ? 5.62599   11.97459  -8.13910  1.000 21.03092 ? 81  ARG A NE    1 
ATOM   625  C  CZ    . ARG A 1 81  ? 6.26343   11.51477  -7.07100  1.000 12.07996 ? 81  ARG A CZ    1 
ATOM   626  N  NH1   . ARG A 1 81  ? 7.43527   12.00469  -6.70002  1.000 15.65329 ? 81  ARG A NH1   1 
ATOM   627  N  NH2   . ARG A 1 81  ? 5.70997   10.54094  -6.35517  1.000 13.45412 ? 81  ARG A NH2   1 
ATOM   628  N  N     . GLY A 1 82  ? 6.37787   14.92356  -14.09181 1.000 24.39907 ? 82  GLY A N     1 
ATOM   629  C  CA    . GLY A 1 82  ? 6.10685   15.67156  -15.29981 1.000 23.86904 ? 82  GLY A CA    1 
ATOM   630  C  C     . GLY A 1 82  ? 6.95083   15.18656  -16.45282 1.000 20.47086 ? 82  GLY A C     1 
ATOM   631  O  O     . GLY A 1 82  ? 7.56083   14.11257  -16.40883 1.000 22.39744 ? 82  GLY A O     1 
ATOM   632  N  N     . LYS A 1 83  ? 6.98081   15.99256  -17.51482 1.000 20.64663 ? 83  LYS A N     1 
ATOM   633  C  CA    . LYS A 1 83  ? 7.77079   15.71857  -18.70783 1.000 19.44479 ? 83  LYS A CA    1 
ATOM   634  C  C     . LYS A 1 83  ? 9.11479   16.43057  -18.62886 1.000 20.32704 ? 83  LYS A C     1 
ATOM   635  O  O     . LYS A 1 83  ? 9.17679   17.58357  -18.19186 1.000 25.30312 ? 83  LYS A O     1 
ATOM   636  C  CB    . LYS A 1 83  ? 7.03177   16.17457  -19.96582 1.000 18.31533 ? 83  LYS A CB    1 
ATOM   637  C  CG    . LYS A 1 83  ? 5.56877   15.76956  -20.01580 1.000 20.42219 ? 83  LYS A CG    1 
ATOM   638  C  CD    . LYS A 1 83  ? 5.38678   14.26156  -19.97279 0.000 24.68839 ? 83  LYS A CD    1 
ATOM   639  C  CE    . LYS A 1 83  ? 5.89876   13.60556  -21.24280 0.000 26.16996 ? 83  LYS A CE    1 
ATOM   640  N  NZ    . LYS A 1 83  ? 5.39876   12.21056  -21.38180 0.000 29.55165 ? 83  LYS A NZ    1 
ATOM   641  N  N     . PRO A 1 84  ? 10.20479  15.76758  -19.04287 1.000 18.91966 ? 84  PRO A N     1 
ATOM   642  C  CA    . PRO A 1 84  ? 11.53078  16.40358  -18.95390 1.000 16.05134 ? 84  PRO A CA    1 
ATOM   643  C  C     . PRO A 1 84  ? 11.60777  17.76358  -19.62590 1.000 20.20206 ? 84  PRO A C     1 
ATOM   644  O  O     . PRO A 1 84  ? 12.27577  18.66758  -19.10691 1.000 16.98618 ? 84  PRO A O     1 
ATOM   645  C  CB    . PRO A 1 84  ? 12.44878  15.38458  -19.64191 1.000 14.49336 ? 84  PRO A CB    1 
ATOM   646  C  CG    . PRO A 1 84  ? 11.74978  14.08258  -19.47490 1.000 19.15992 ? 84  PRO A CG    1 
ATOM   647  C  CD    . PRO A 1 84  ? 10.28278  14.38758  -19.54888 1.000 22.28922 ? 84  PRO A CD    1 
ATOM   648  N  N     . GLU A 1 85  ? 10.92775  17.93958  -20.76089 1.000 21.38802 ? 85  GLU A N     1 
ATOM   649  C  CA    . GLU A 1 85  ? 10.98973  19.20658  -21.48189 1.000 21.55277 ? 85  GLU A CA    1 
ATOM   650  C  C     . GLU A 1 85  ? 10.31474  20.33858  -20.72587 1.000 17.16936 ? 85  GLU A C     1 
ATOM   651  O  O     . GLU A 1 85  ? 10.58173  21.50658  -21.02488 1.000 18.18247 ? 85  GLU A O     1 
ATOM   652  C  CB    . GLU A 1 85  ? 10.35171  19.06658  -22.86688 1.000 22.18754 ? 85  GLU A CB    1 
ATOM   653  C  CG    . GLU A 1 85  ? 11.02470  18.04758  -23.77289 1.000 27.11945 ? 85  GLU A CG    1 
ATOM   654  C  CD    . GLU A 1 85  ? 10.57671  16.62958  -23.48888 1.000 26.76795 ? 85  GLU A CD    1 
ATOM   655  O  OE1   . GLU A 1 85  ? 9.56072   16.45758  -22.78286 1.000 21.84714 ? 85  GLU A OE1   1 
ATOM   656  O  OE2   . GLU A 1 85  ? 11.24170  15.68758  -23.96889 1.000 37.92017 ? 85  GLU A OE2   1 
ATOM   657  N  N     . GLU A 1 86  ? 9.44876   20.02157  -19.76186 1.000 20.43235 ? 86  GLU A N     1 
ATOM   658  C  CA    . GLU A 1 86  ? 8.75877   21.02857  -18.96685 1.000 17.61745 ? 86  GLU A CA    1 
ATOM   659  C  C     . GLU A 1 86  ? 9.32179   21.18257  -17.56086 1.000 15.56354 ? 86  GLU A C     1 
ATOM   660  O  O     . GLU A 1 86  ? 9.06680   22.20757  -16.91785 1.000 21.54800 ? 86  GLU A O     1 
ATOM   661  C  CB    . GLU A 1 86  ? 7.26977   20.68757  -18.86882 1.000 18.31663 ? 86  GLU A CB    1 
ATOM   662  C  CG    . GLU A 1 86  ? 6.60875   20.38556  -20.20281 1.000 23.84303 ? 86  GLU A CG    1 
ATOM   663  C  CD    . GLU A 1 86  ? 5.18575   19.89656  -20.04079 1.000 24.15520 ? 86  GLU A CD    1 
ATOM   664  O  OE1   . GLU A 1 86  ? 4.73377   19.75956  -18.88078 1.000 22.20802 ? 86  GLU A OE1   1 
ATOM   665  O  OE2   . GLU A 1 86  ? 4.51974   19.65256  -21.06878 1.000 23.57096 ? 86  GLU A OE2   1 
ATOM   666  N  N     . VAL A 1 87  ? 10.07080  20.20157  -17.06687 1.000 16.61725 ? 87  VAL A N     1 
ATOM   667  C  CA    . VAL A 1 87  ? 10.59583  20.26558  -15.70588 1.000 12.89717 ? 87  VAL A CA    1 
ATOM   668  C  C     . VAL A 1 87  ? 11.98182  20.89758  -15.66390 1.000 14.89934 ? 87  VAL A C     1 
ATOM   669  O  O     . VAL A 1 87  ? 12.28184  21.68758  -14.76391 1.000 19.11164 ? 87  VAL A O     1 
ATOM   670  C  CB    . VAL A 1 87  ? 10.60184  18.85958  -15.08088 1.000 16.04026 ? 87  VAL A CB    1 
ATOM   671  C  CG1   . VAL A 1 87  ? 11.31886  18.87658  -13.74889 1.000 15.43279 ? 87  VAL A CG1   1 
ATOM   672  C  CG2   . VAL A 1 87  ? 9.18385   18.35957  -14.90786 1.000 22.21211 ? 87  VAL A CG2   1 
ATOM   673  N  N     . PHE A 1 88  ? 12.84181  20.56958  -16.62092 1.000 13.29329 ? 88  PHE A N     1 
ATOM   674  C  CA    . PHE A 1 88  ? 14.23281  21.00059  -16.56294 1.000 9.42384  ? 88  PHE A CA    1 
ATOM   675  C  C     . PHE A 1 88  ? 14.40880  22.51159  -16.69894 1.000 9.66146  ? 88  PHE A C     1 
ATOM   676  O  O     . PHE A 1 88  ? 15.20581  23.08959  -15.95095 1.000 11.45875 ? 88  PHE A O     1 
ATOM   677  C  CB    . PHE A 1 88  ? 15.05679  20.26359  -17.61795 1.000 16.42617 ? 88  PHE A CB    1 
ATOM   678  C  CG    . PHE A 1 88  ? 15.42881  18.87559  -17.21396 1.000 10.72701 ? 88  PHE A CG    1 
ATOM   679  C  CD1   . PHE A 1 88  ? 16.12783  18.65460  -16.04397 1.000 12.26354 ? 88  PHE A CD1   1 
ATOM   680  C  CD2   . PHE A 1 88  ? 15.07880  17.78959  -17.99895 1.000 12.80194 ? 88  PHE A CD2   1 
ATOM   681  C  CE1   . PHE A 1 88  ? 16.47284  17.37160  -15.65698 1.000 16.97130 ? 88  PHE A CE1   1 
ATOM   682  C  CE2   . PHE A 1 88  ? 15.42281  16.50559  -17.62196 1.000 12.13200 ? 88  PHE A CE2   1 
ATOM   683  C  CZ    . PHE A 1 88  ? 16.11883  16.29360  -16.44897 1.000 9.63351  ? 88  PHE A CZ    1 
ATOM   684  N  N     . PRO A 1 89  ? 13.71978  23.19259  -17.61793 1.000 11.99046 ? 89  PRO A N     1 
ATOM   685  C  CA    . PRO A 1 89  ? 13.83778  24.65959  -17.64893 1.000 14.66236 ? 89  PRO A CA    1 
ATOM   686  C  C     . PRO A 1 89  ? 13.53080  25.33559  -16.31993 1.000 13.55178 ? 89  PRO A C     1 
ATOM   687  O  O     . PRO A 1 89  ? 14.17080  26.33959  -15.98594 1.000 14.52795 ? 89  PRO A O     1 
ATOM   688  C  CB    . PRO A 1 89  ? 12.83276  25.05958  -18.73191 1.000 17.35234 ? 89  PRO A CB    1 
ATOM   689  C  CG    . PRO A 1 89  ? 12.81975  23.89959  -19.65091 1.000 16.21316 ? 89  PRO A CG    1 
ATOM   690  C  CD    . PRO A 1 89  ? 12.92377  22.69759  -18.75492 1.000 14.10340 ? 89  PRO A CD    1 
ATOM   691  N  N     . ARG A 1 90  ? 12.58755  24.80340  -15.54118 1.000 15.33032 ? 90  ARG A N     1 
ATOM   692  C  CA    . ARG A 1 90  ? 12.27845  25.39341  -14.24269 1.000 18.31831 ? 90  ARG A CA    1 
ATOM   693  C  C     . ARG A 1 90  ? 13.39762  25.14144  -13.24020 1.000 15.09664 ? 90  ARG A C     1 
ATOM   694  O  O     . ARG A 1 90  ? 13.87720  26.07159  -12.58082 1.000 11.78652 ? 90  ARG A O     1 
ATOM   695  C  CB    . ARG A 1 90  ? 10.95913  24.83319  -13.71640 1.000 18.60762 ? 90  ARG A CB    1 
ATOM   696  C  CG    . ARG A 1 90  ? 10.61466  25.28505  -12.31140 1.000 22.44874 ? 90  ARG A CG    1 
ATOM   697  C  CD    . ARG A 1 90  ? 10.06323  24.12755  -11.50724 1.000 22.75379 ? 90  ARG A CD    1 
ATOM   698  N  NE    . ARG A 1 90  ? 9.01496   23.42146  -12.23265 1.000 29.70863 ? 90  ARG A NE    1 
ATOM   699  C  CZ    . ARG A 1 90  ? 8.46111   22.28616  -11.83115 1.000 30.17869 ? 90  ARG A CZ    1 
ATOM   700  N  NH1   . ARG A 1 90  ? 8.83840   21.69194  -10.71091 1.000 22.30860 ? 90  ARG A NH1   1 
ATOM   701  N  NH2   . ARG A 1 90  ? 7.50671   21.73209  -12.57336 1.000 27.15673 ? 90  ARG A NH2   1 
ATOM   702  N  N     . VAL A 1 91  ? 13.82686  23.88459  -13.10893 1.000 13.59269 ? 91  VAL A N     1 
ATOM   703  C  CA    . VAL A 1 91  ? 14.81887  23.55159  -12.09695 1.000 15.24216 ? 91  VAL A CA    1 
ATOM   704  C  C     . VAL A 1 91  ? 16.21887  24.01259  -12.48697 1.000 11.29566 ? 91  VAL A C     1 
ATOM   705  O  O     . VAL A 1 91  ? 17.10188  24.06660  -11.62399 1.000 13.77610 ? 91  VAL A O     1 
ATOM   706  C  CB    . VAL A 1 91  ? 14.80488  22.04159  -11.79695 1.000 10.25389 ? 91  VAL A CB    1 
ATOM   707  C  CG1   . VAL A 1 91  ? 13.47090  21.64058  -11.20693 1.000 15.42174 ? 91  VAL A CG1   1 
ATOM   708  C  CG2   . VAL A 1 91  ? 15.11887  21.24859  -13.04595 1.000 13.19050 ? 91  VAL A CG2   1 
ATOM   709  N  N     . PHE A 1 92  ? 16.45984  24.34360  -13.75898 1.000 13.21799 ? 92  PHE A N     1 
ATOM   710  C  CA    . PHE A 1 92  ? 17.72884  24.97660  -14.11900 1.000 11.13332 ? 92  PHE A CA    1 
ATOM   711  C  C     . PHE A 1 92  ? 17.87784  26.32760  -13.42600 1.000 14.94133 ? 92  PHE A C     1 
ATOM   712  O  O     . PHE A 1 92  ? 18.90885  26.61160  -12.80502 1.000 13.10485 ? 92  PHE A O     1 
ATOM   713  C  CB    . PHE A 1 92  ? 17.83781  25.14360  -15.63600 1.000 12.35241 ? 92  PHE A CB    1 
ATOM   714  C  CG    . PHE A 1 92  ? 18.09680  23.86460  -16.37700 1.000 10.71625 ? 92  PHE A CG    1 
ATOM   715  C  CD1   . PHE A 1 92  ? 18.51982  22.72760  -15.70801 1.000 9.49761  ? 92  PHE A CD1   1 
ATOM   716  C  CD2   . PHE A 1 92  ? 17.91278  23.79960  -17.75000 1.000 13.07553 ? 92  PHE A CD2   1 
ATOM   717  C  CE1   . PHE A 1 92  ? 18.74881  21.55160  -16.39501 1.000 12.46190 ? 92  PHE A CE1   1 
ATOM   718  C  CE2   . PHE A 1 92  ? 18.14377  22.62360  -18.44200 1.000 15.02008 ? 92  PHE A CE2   1 
ATOM   719  C  CZ    . PHE A 1 92  ? 18.56379  21.50060  -17.76301 1.000 9.32604  ? 92  PHE A CZ    1 
ATOM   720  N  N     . ARG A 1 93  ? 16.84973  27.17266  -13.51728 1.000 15.38417 ? 93  ARG A N     1 
ATOM   721  C  CA    . ARG A 1 93  ? 16.91358  28.49723  -12.90811 1.000 22.63601 ? 93  ARG A CA    1 
ATOM   722  C  C     . ARG A 1 93  ? 16.73091  28.43450  -11.39638 1.000 18.40442 ? 93  ARG A C     1 
ATOM   723  O  O     . ARG A 1 93  ? 17.39405  29.17215  -10.65785 1.000 17.73485 ? 93  ARG A O     1 
ATOM   724  C  CB    . ARG A 1 93  ? 15.85558  29.41835  -13.52272 1.000 17.98847 ? 93  ARG A CB    1 
ATOM   725  C  CG    . ARG A 1 93  ? 16.21382  29.99398  -14.88625 1.000 18.65386 ? 93  ARG A CG    1 
ATOM   726  C  CD    . ARG A 1 93  ? 15.96825  28.99718  -16.00375 1.000 19.53308 ? 93  ARG A CD    1 
ATOM   727  N  NE    . ARG A 1 93  ? 16.20440  29.57256  -17.32277 1.000 15.21000 ? 93  ARG A NE    1 
ATOM   728  C  CZ    . ARG A 1 93  ? 16.06320  28.90737  -18.46128 1.000 14.49105 ? 93  ARG A CZ    1 
ATOM   729  N  NH1   . ARG A 1 93  ? 15.68743  27.63825  -18.47832 1.000 14.84577 ? 93  ARG A NH1   1 
ATOM   730  N  NH2   . ARG A 1 93  ? 16.30713  29.52942  -19.61086 1.000 23.46101 ? 93  ARG A NH2   1 
ATOM   731  N  N     . GLU A 1 94  ? 15.83188  27.56959  -10.92096 1.000 19.31991 ? 94  GLU A N     1 
ATOM   732  C  CA    . GLU A 1 94  ? 15.55590  27.50159  -9.48996  1.000 18.22484 ? 94  GLU A CA    1 
ATOM   733  C  C     . GLU A 1 94  ? 16.77992  27.03960  -8.70698  1.000 15.82706 ? 94  GLU A C     1 
ATOM   734  O  O     . GLU A 1 94  ? 17.10693  27.60760  -7.65798  1.000 13.27406 ? 94  GLU A O     1 
ATOM   735  C  CB    . GLU A 1 94  ? 14.37491  26.56959  -9.23294  1.000 14.73444 ? 94  GLU A CB    1 
ATOM   736  C  CG    . GLU A 1 94  ? 14.15094  26.28659  -7.76394  1.000 17.61309 ? 94  GLU A CG    1 
ATOM   737  C  CD    . GLU A 1 94  ? 13.02594  25.31058  -7.51492  1.000 14.31041 ? 94  GLU A CD    1 
ATOM   738  O  OE1   . GLU A 1 94  ? 12.03293  25.33458  -8.26990  1.000 16.76836 ? 94  GLU A OE1   1 
ATOM   739  O  OE2   . GLU A 1 94  ? 13.14296  24.51958  -6.55692  1.000 18.17820 ? 94  GLU A OE2   1 
ATOM   740  N  N     . TRP A 1 95  ? 17.47191  26.01860  -9.20699  1.000 12.52619 ? 95  TRP A N     1 
ATOM   741  C  CA    . TRP A 1 95  ? 18.59393  25.41160  -8.50901  1.000 15.89479 ? 95  TRP A CA    1 
ATOM   742  C  C     . TRP A 1 95  ? 19.93792  26.01961  -8.89003  1.000 13.36297 ? 95  TRP A C     1 
ATOM   743  O  O     . TRP A 1 95  ? 20.96193  25.62361  -8.32405  1.000 14.84221 ? 95  TRP A O     1 
ATOM   744  C  CB    . TRP A 1 95  ? 18.61693  23.90160  -8.77901  1.000 12.29447 ? 95  TRP A CB    1 
ATOM   745  C  CG    . TRP A 1 95  ? 17.39594  23.17760  -8.28999  1.000 11.00919 ? 95  TRP A CG    1 
ATOM   746  C  CD1   . TRP A 1 95  ? 16.46195  23.64559  -7.41398  1.000 11.39350 ? 95  TRP A CD1   1 
ATOM   747  C  CD2   . TRP A 1 95  ? 16.97694  21.85560  -8.65498  1.000 10.64883 ? 95  TRP A CD2   1 
ATOM   748  N  NE1   . TRP A 1 95  ? 15.48996  22.69559  -7.20596  1.000 15.23249 ? 95  TRP A NE1   1 
ATOM   749  C  CE2   . TRP A 1 95  ? 15.78095  21.58859  -7.95696  1.000 13.28392 ? 95  TRP A CE2   1 
ATOM   750  C  CE3   . TRP A 1 95  ? 17.50093  20.86960  -9.49599  1.000 10.56942 ? 95  TRP A CE3   1 
ATOM   751  C  CZ2   . TRP A 1 95  ? 15.09695  20.37559  -8.07795  1.000 12.46515 ? 95  TRP A CZ2   1 
ATOM   752  C  CZ3   . TRP A 1 95  ? 16.81993  19.66860  -9.61598  1.000 15.00609 ? 95  TRP A CZ3   1 
ATOM   753  C  CH2   . TRP A 1 95  ? 15.63094  19.43259  -8.90996  1.000 13.08364 ? 95  TRP A CH2   1 
ATOM   754  N  N     . GLY A 1 96  ? 19.96190  26.97261  -9.81603  1.000 19.59779 ? 96  GLY A N     1 
ATOM   755  C  CA    . GLY A 1 96  ? 21.22889  27.53961  -10.26005 1.000 17.35315 ? 96  GLY A CA    1 
ATOM   756  C  C     . GLY A 1 96  ? 22.15288  26.51161  -10.87507 1.000 13.19153 ? 96  GLY A C     1 
ATOM   757  O  O     . GLY A 1 96  ? 23.35989  26.51862  -10.60009 1.000 12.42816 ? 96  GLY A O     1 
ATOM   758  N  N     . VAL A 1 97  ? 21.60587  25.61961  -11.70206 1.000 9.55461  ? 97  VAL A N     1 
ATOM   759  C  CA    . VAL A 1 97  ? 22.38287  24.53162  -12.28007 1.000 11.24450 ? 97  VAL A CA    1 
ATOM   760  C  C     . VAL A 1 97  ? 23.38385  25.08462  -13.28509 1.000 11.61986 ? 97  VAL A C     1 
ATOM   761  O  O     . VAL A 1 97  ? 23.06383  25.97062  -14.08808 1.000 10.97151 ? 97  VAL A O     1 
ATOM   762  C  CB    . VAL A 1 97  ? 21.44686  23.50261  -12.94006 1.000 10.31819 ? 97  VAL A CB    1 
ATOM   763  C  CG1   . VAL A 1 97  ? 22.23886  22.32062  -13.49807 1.000 12.27855 ? 97  VAL A CG1   1 
ATOM   764  C  CG2   . VAL A 1 97  ? 20.39388  23.03361  -11.94704 1.000 14.69352 ? 97  VAL A CG2   1 
ATOM   765  N  N     . THR A 1 98  ? 24.60985  24.56662  -13.23411 1.000 13.62868 ? 98  THR A N     1 
ATOM   766  C  CA    . THR A 1 98  ? 25.62883  24.87563  -14.22313 1.000 11.08077 ? 98  THR A CA    1 
ATOM   767  C  C     . THR A 1 98  ? 26.03382  23.66863  -15.05713 1.000 13.58061 ? 98  THR A C     1 
ATOM   768  O  O     . THR A 1 98  ? 26.66881  23.84563  -16.10515 1.000 10.06096 ? 98  THR A O     1 
ATOM   769  C  CB    . THR A 1 98  ? 26.87884  25.46763  -13.54615 1.000 12.51663 ? 98  THR A CB    1 
ATOM   770  O  OG1   . THR A 1 98  ? 27.40586  24.53563  -12.59516 1.000 17.97474 ? 98  THR A OG1   1 
ATOM   771  C  CG2   . THR A 1 98  ? 26.54185  26.76363  -12.83514 1.000 13.11926 ? 98  THR A CG2   1 
ATOM   772  N  N     . GLN A 1 99  ? 25.68284  22.45663  -14.63313 1.000 11.74075 ? 99  GLN A N     1 
ATOM   773  C  CA    . GLN A 1 99  ? 26.10283  21.25163  -15.33614 1.000 13.39246 ? 99  GLN A CA    1 
ATOM   774  C  C     . GLN A 1 99  ? 25.03183  20.18263  -15.19812 1.000 9.13213  ? 99  GLN A C     1 
ATOM   775  O  O     . GLN A 1 99  ? 24.53685  19.94162  -14.09411 1.000 9.66146  ? 99  GLN A O     1 
ATOM   776  C  CB    . GLN A 1 99  ? 27.43984  20.72663  -14.79616 1.000 9.74046  ? 99  GLN A CB    1 
ATOM   777  C  CG    . GLN A 1 99  ? 27.99783  19.54464  -15.58917 1.000 14.73150 ? 99  GLN A CG    1 
ATOM   778  C  CD    . GLN A 1 99  ? 29.15984  18.85864  -14.89319 1.000 16.90644 ? 99  GLN A CD    1 
ATOM   779  O  OE1   . GLN A 1 99  ? 28.98886  18.22264  -13.84819 1.000 12.38583 ? 99  GLN A OE1   1 
ATOM   780  N  NE2   . GLN A 1 99  ? 30.34883  18.98164  -15.47221 1.000 17.10654 ? 99  GLN A NE2   1 
ATOM   781  N  N     . LEU A 1 100 ? 24.69582  19.54062  -16.31411 1.000 9.78222  ? 100 LEU A N     1 
ATOM   782  C  CA    . LEU A 1 100 ? 23.74482  18.43562  -16.35510 1.000 10.01835 ? 100 LEU A CA    1 
ATOM   783  C  C     . LEU A 1 100 ? 24.44882  17.19062  -16.88311 1.000 8.61854  ? 100 LEU A C     1 
ATOM   784  O  O     . LEU A 1 100 ? 25.07180  17.23363  -17.94712 1.000 8.92120  ? 100 LEU A O     1 
ATOM   785  C  CB    . LEU A 1 100 ? 22.54181  18.78162  -17.24008 1.000 8.81146  ? 100 LEU A CB    1 
ATOM   786  C  CG    . LEU A 1 100 ? 21.55180  17.65461  -17.53406 1.000 8.67652  ? 100 LEU A CG    1 
ATOM   787  C  CD1   . LEU A 1 100 ? 20.84283  17.23461  -16.26805 1.000 8.70697  ? 100 LEU A CD1   1 
ATOM   788  C  CD2   . LEU A 1 100 ? 20.55079  18.07461  -18.57905 1.000 8.84843  ? 100 LEU A CD2   1 
ATOM   789  N  N     . CYS A 1 101 ? 24.33783  16.08562  -16.15411 1.000 8.42082  ? 101 CYS A N     1 
ATOM   790  C  CA    . CYS A 1 101 ? 25.01283  14.84563  -16.51612 1.000 9.24844  ? 101 CYS A CA    1 
ATOM   791  C  C     . CYS A 1 101 ? 24.01783  13.69662  -16.57710 1.000 8.17968  ? 101 CYS A C     1 
ATOM   792  O  O     . CYS A 1 101 ? 23.18585  13.53162  -15.68009 1.000 8.68470  ? 101 CYS A O     1 
ATOM   793  C  CB    . CYS A 1 101 ? 26.12285  14.48863  -15.51414 1.000 11.35890 ? 101 CYS A CB    1 
ATOM   794  S  SG    . CYS A 1 101 ? 27.32885  15.78463  -15.19916 1.000 14.54698 ? 101 CYS A SG    1 
ATOM   795  N  N     . PHE A 1 102 ? 24.11982  12.88962  -17.62811 1.000 9.43185  ? 102 PHE A N     1 
ATOM   796  C  CA    . PHE A 1 102 ? 23.32282  11.67762  -17.71009 1.000 8.06076  ? 102 PHE A CA    1 
ATOM   797  C  C     . PHE A 1 102 ? 24.00181  10.69862  -18.65311 1.000 10.86501 ? 102 PHE A C     1 
ATOM   798  O  O     . PHE A 1 102 ? 24.81179  11.08463  -19.50012 1.000 8.22602  ? 102 PHE A O     1 
ATOM   799  C  CB    . PHE A 1 102 ? 21.88481  11.96462  -18.15407 1.000 8.10627  ? 102 PHE A CB    1 
ATOM   800  C  CG    . PHE A 1 102 ? 21.77179  12.82062  -19.37907 1.000 8.30790  ? 102 PHE A CG    1 
ATOM   801  C  CD1   . PHE A 1 102 ? 21.73679  14.19862  -19.27807 1.000 8.43956  ? 102 PHE A CD1   1 
ATOM   802  C  CD2   . PHE A 1 102 ? 21.64477  12.24462  -20.63007 1.000 8.39985  ? 102 PHE A CD2   1 
ATOM   803  C  CE1   . PHE A 1 102 ? 21.60377  14.98062  -20.39906 1.000 8.66368  ? 102 PHE A CE1   1 
ATOM   804  C  CE2   . PHE A 1 102 ? 21.51075  13.02462  -21.75806 1.000 13.12658 ? 102 PHE A CE2   1 
ATOM   805  C  CZ    . PHE A 1 102 ? 21.49075  14.39762  -21.64206 1.000 11.93013 ? 102 PHE A CZ    1 
ATOM   806  N  N     . GLU A 1 103 ? 23.65882  9.42262   -18.47910 1.000 7.95979  ? 103 GLU A N     1 
ATOM   807  C  CA    . GLU A 1 103 ? 24.23581  8.35162   -19.27911 1.000 7.97903  ? 103 GLU A CA    1 
ATOM   808  C  C     . GLU A 1 103 ? 23.68478  8.38062   -20.70110 1.000 9.80331  ? 103 GLU A C     1 
ATOM   809  O  O     . GLU A 1 103 ? 22.48878  8.59662   -20.91608 1.000 8.13620  ? 103 GLU A O     1 
ATOM   810  C  CB    . GLU A 1 103 ? 23.93582  7.00262   -18.62411 1.000 8.16603  ? 103 GLU A CB    1 
ATOM   811  C  CG    . GLU A 1 103 ? 24.70582  5.83063   -19.18512 1.000 9.72394  ? 103 GLU A CG    1 
ATOM   812  C  CD    . GLU A 1 103 ? 24.31483  4.52062   -18.51711 1.000 7.74007  ? 103 GLU A CD    1 
ATOM   813  O  OE1   . GLU A 1 103 ? 23.12883  4.14562   -18.59709 1.000 7.70788  ? 103 GLU A OE1   1 
ATOM   814  O  OE2   . GLU A 1 103 ? 25.18485  3.87763   -17.89113 1.000 9.04015  ? 103 GLU A OE2   1 
ATOM   815  N  N     . HIS A 1 104 ? 24.56677  8.15563   -21.67412 1.000 9.39606  ? 104 HIS A N     1 
ATOM   816  C  CA    . HIS A 1 104 ? 24.15774  8.18062   -23.07211 1.000 11.39857 ? 104 HIS A CA    1 
ATOM   817  C  C     . HIS A 1 104 ? 23.17574  7.05262   -23.36009 1.000 11.84398 ? 104 HIS A C     1 
ATOM   818  O  O     . HIS A 1 104 ? 23.31876  5.93462   -22.85410 1.000 10.76690 ? 104 HIS A O     1 
ATOM   819  C  CB    . HIS A 1 104 ? 25.37973  8.06263   -23.98713 1.000 12.81681 ? 104 HIS A CB    1 
ATOM   820  C  CG    . HIS A 1 104 ? 25.05171  8.11163   -25.44712 1.000 14.06018 ? 104 HIS A CG    1 
ATOM   821  N  ND1   . HIS A 1 104 ? 24.56569  9.24463   -26.06311 1.000 16.49862 ? 104 HIS A ND1   1 
ATOM   822  C  CD2   . HIS A 1 104 ? 25.15069  7.17063   -26.41513 1.000 11.26588 ? 104 HIS A CD2   1 
ATOM   823  C  CE1   . HIS A 1 104 ? 24.36967  8.99563   -27.34611 1.000 18.59650 ? 104 HIS A CE1   1 
ATOM   824  N  NE2   . HIS A 1 104 ? 24.71967  7.74463   -27.58612 1.000 15.12072 ? 104 HIS A NE2   1 
ATOM   825  N  N     . ASP A 1 105 ? 22.16673  7.35662   -24.17208 1.000 12.26758 ? 105 ASP A N     1 
ATOM   826  C  CA    . ASP A 1 105 ? 21.14673  6.38962   -24.54606 1.000 13.53247 ? 105 ASP A CA    1 
ATOM   827  C  C     . ASP A 1 105 ? 20.91370  6.47861   -26.04506 1.000 16.58784 ? 105 ASP A C     1 
ATOM   828  O  O     . ASP A 1 105 ? 20.88369  7.57361   -26.61205 1.000 17.10660 ? 105 ASP A O     1 
ATOM   829  C  CB    . ASP A 1 105 ? 19.84174  6.63161   -23.78304 1.000 14.68260 ? 105 ASP A CB    1 
ATOM   830  C  CG    . ASP A 1 105 ? 18.82574  5.53161   -24.00402 1.000 17.67019 ? 105 ASP A CG    1 
ATOM   831  O  OD1   . ASP A 1 105 ? 19.14373  4.55661   -24.71703 1.000 16.13514 ? 105 ASP A OD1   1 
ATOM   832  O  OD2   . ASP A 1 105 ? 17.70675  5.64160   -23.46000 1.000 17.19040 ? 105 ASP A OD2   1 
ATOM   833  N  N     . THR A 1 106 ? 20.75569  5.32161   -26.68105 1.000 12.29511 ? 106 THR A N     1 
ATOM   834  C  CA    . THR A 1 106 ? 20.65367  5.24161   -28.13105 1.000 15.88323 ? 106 THR A CA    1 
ATOM   835  C  C     . THR A 1 106 ? 19.28266  4.78661   -28.61003 1.000 16.40786 ? 106 THR A C     1 
ATOM   836  O  O     . THR A 1 106 ? 19.12364  4.50061   -29.80203 1.000 18.22859 ? 106 THR A O     1 
ATOM   837  C  CB    . THR A 1 106 ? 21.72466  4.29962   -28.68607 1.000 20.14093 ? 106 THR A CB    1 
ATOM   838  O  OG1   . THR A 1 106 ? 21.52868  2.98862   -28.14107 1.000 9.26750  ? 106 THR A OG1   1 
ATOM   839  C  CG2   . THR A 1 106 ? 23.12267  4.79962   -28.33709 1.000 11.01346 ? 106 THR A CG2   1 
ATOM   840  N  N     . GLU A 1 107 ? 18.29268  4.70261   -27.72301 1.000 16.97118 ? 107 GLU A N     1 
ATOM   841  C  CA    . GLU A 1 107 ? 16.94567  4.35760   -28.15799 1.000 16.95795 ? 107 GLU A CA    1 
ATOM   842  C  C     . GLU A 1 107 ? 16.34466  5.49960   -28.97498 1.000 17.64113 ? 107 GLU A C     1 
ATOM   843  O  O     . GLU A 1 107 ? 16.74765  6.65560   -28.83099 1.000 19.04777 ? 107 GLU A O     1 
ATOM   844  C  CB    . GLU A 1 107 ? 16.05969  4.03560   -26.95698 1.000 16.95210 ? 107 GLU A CB    1 
ATOM   845  C  CG    . GLU A 1 107 ? 16.40071  2.71960   -26.27998 1.000 16.55529 ? 107 GLU A CG    1 
ATOM   846  C  CD    . GLU A 1 107 ? 15.34073  2.27660   -25.29296 1.000 19.14448 ? 107 GLU A CD    1 
ATOM   847  O  OE1   . GLU A 1 107 ? 14.18572  2.73859   -25.41194 1.000 17.03691 ? 107 GLU A OE1   1 
ATOM   848  O  OE2   . GLU A 1 107 ? 15.66375  1.46260   -24.39897 1.000 25.08371 ? 107 GLU A OE2   1 
ATOM   849  N  N     . PRO A 1 108 ? 15.37964  5.19560   -29.85296 1.000 25.07880 ? 108 PRO A N     1 
ATOM   850  C  CA    . PRO A 1 108 ? 14.82562  6.25560   -30.71795 1.000 13.96218 ? 108 PRO A CA    1 
ATOM   851  C  C     . PRO A 1 108 ? 14.12763  7.36759   -29.95294 1.000 25.28697 ? 108 PRO A C     1 
ATOM   852  O  O     . PRO A 1 108 ? 14.29562  8.54759   -30.29094 1.000 24.96567 ? 108 PRO A O     1 
ATOM   853  C  CB    . PRO A 1 108 ? 13.84861  5.49259   -31.62394 1.000 19.70774 ? 108 PRO A CB    1 
ATOM   854  C  CG    . PRO A 1 108 ? 14.29462  4.08359   -31.57495 1.000 22.19216 ? 108 PRO A CG    1 
ATOM   855  C  CD    . PRO A 1 108 ? 14.85364  3.86760   -30.20496 1.000 18.90992 ? 108 PRO A CD    1 
ATOM   856  N  N     . TYR A 1 109 ? 13.32965  7.03159   -28.93793 1.000 21.92515 ? 109 TYR A N     1 
ATOM   857  C  CA    . TYR A 1 109 ? 12.69066  8.07959   -28.14792 1.000 24.13352 ? 109 TYR A CA    1 
ATOM   858  C  C     . TYR A 1 109 ? 13.70967  8.86759   -27.33993 1.000 20.61109 ? 109 TYR A C     1 
ATOM   859  O  O     . TYR A 1 109 ? 13.52967  10.07159  -27.12593 1.000 23.41707 ? 109 TYR A O     1 
ATOM   860  C  CB    . TYR A 1 109 ? 11.63468  7.47858   -27.22290 1.000 26.57147 ? 109 TYR A CB    1 
ATOM   861  C  CG    . TYR A 1 109 ? 11.12469  8.43258   -26.16189 1.000 25.10645 ? 109 TYR A CG    1 
ATOM   862  C  CD1   . TYR A 1 109 ? 10.18268  9.40458   -26.46588 1.000 37.04548 ? 109 TYR A CD1   1 
ATOM   863  C  CD2   . TYR A 1 109 ? 11.57671  8.34758   -24.85390 1.000 23.91655 ? 109 TYR A CD2   1 
ATOM   864  C  CE1   . TYR A 1 109 ? 9.71370   10.27058  -25.49587 1.000 34.06979 ? 109 TYR A CE1   1 
ATOM   865  C  CE2   . TYR A 1 109 ? 11.11673  9.20458   -23.88389 1.000 26.41432 ? 109 TYR A CE2   1 
ATOM   866  C  CZ    . TYR A 1 109 ? 10.18672  10.16258  -24.20688 1.000 32.55857 ? 109 TYR A CZ    1 
ATOM   867  O  OH    . TYR A 1 109 ? 9.73173   11.01458  -23.22787 1.000 40.22932 ? 109 TYR A OH    1 
ATOM   868  N  N     . ALA A 1 110 ? 14.77768  8.20659   -26.88695 1.000 20.99085 ? 110 ALA A N     1 
ATOM   869  C  CA    . ALA A 1 110 ? 15.79269  8.88460   -26.08797 1.000 20.41075 ? 110 ALA A CA    1 
ATOM   870  C  C     . ALA A 1 110 ? 16.53967  9.93360   -26.90298 1.000 16.69450 ? 110 ALA A C     1 
ATOM   871  O  O     . ALA A 1 110 ? 16.86768  11.00660  -26.38799 1.000 16.11980 ? 110 ALA A O     1 
ATOM   872  C  CB    . ALA A 1 110 ? 16.77070  7.86660   -25.50999 1.000 17.54087 ? 110 ALA A CB    1 
ATOM   873  N  N     . LYS A 1 111 ? 16.81765  9.63960   -28.17399 1.000 15.89496 ? 111 LYS A N     1 
ATOM   874  C  CA    . LYS A 1 111 ? 17.50964  10.60660  -29.01900 1.000 24.45562 ? 111 LYS A CA    1 
ATOM   875  C  C     . LYS A 1 111 ? 16.67063  11.86060  -29.22598 1.000 20.60975 ? 111 LYS A C     1 
ATOM   876  O  O     . LYS A 1 111 ? 17.20563  12.97260  -29.25899 1.000 20.94318 ? 111 LYS A O     1 
ATOM   877  C  CB    . LYS A 1 111 ? 17.86562  9.97061   -30.36100 1.000 16.62615 ? 111 LYS A CB    1 
ATOM   878  C  CG    . LYS A 1 111 ? 18.81562  8.79061   -30.24202 1.000 25.81528 ? 111 LYS A CG    1 
ATOM   879  C  CD    . LYS A 1 111 ? 19.14660  8.19561   -31.59903 1.000 23.60853 ? 111 LYS A CD    1 
ATOM   880  C  CE    . LYS A 1 111 ? 20.07061  6.99761   -31.45504 1.000 21.74721 ? 111 LYS A CE    1 
ATOM   881  N  NZ    . LYS A 1 111 ? 20.30059  6.31161   -32.75804 1.000 26.17901 ? 111 LYS A NZ    1 
ATOM   882  N  N     . VAL A 1 112 ? 15.35263  11.70060  -29.36896 1.000 18.20433 ? 112 VAL A N     1 
ATOM   883  C  CA    . VAL A 1 112 ? 14.47462  12.85559  -29.53295 1.000 21.55463 ? 112 VAL A CA    1 
ATOM   884  C  C     . VAL A 1 112 ? 14.33464  13.60659  -28.21794 1.000 12.96150 ? 112 VAL A C     1 
ATOM   885  O  O     . VAL A 1 112 ? 14.34464  14.84059  -28.18594 1.000 20.14169 ? 112 VAL A O     1 
ATOM   886  C  CB    . VAL A 1 112 ? 13.10261  12.41559  -30.07992 1.000 17.46949 ? 112 VAL A CB    1 
ATOM   887  C  CG1   . VAL A 1 112 ? 12.11161  13.56859  -30.01891 1.000 28.43066 ? 112 VAL A CG1   1 
ATOM   888  C  CG2   . VAL A 1 112 ? 13.23059  11.90259  -31.50393 1.000 20.77739 ? 112 VAL A CG2   1 
ATOM   889  N  N     . ARG A 1 113 ? 14.20234  12.87354  -27.11296 1.000 19.10778 ? 113 ARG A N     1 
ATOM   890  C  CA    . ARG A 1 113 ? 14.08501  13.50795  -25.80513 1.000 17.81251 ? 113 ARG A CA    1 
ATOM   891  C  C     . ARG A 1 113 ? 15.38221  14.20258  -25.41083 1.000 17.32186 ? 113 ARG A C     1 
ATOM   892  O  O     . ARG A 1 113 ? 15.37024  15.36288  -24.98379 1.000 17.01699 ? 113 ARG A O     1 
ATOM   893  C  CB    . ARG A 1 113 ? 13.69231  12.46614  -24.75790 1.000 18.37538 ? 113 ARG A CB    1 
ATOM   894  C  CG    . ARG A 1 113 ? 13.74883  12.95408  -23.32138 1.000 18.01198 ? 113 ARG A CG    1 
ATOM   895  C  CD    . ARG A 1 113 ? 13.87537  11.77397  -22.36913 1.000 17.13382 ? 113 ARG A CD    1 
ATOM   896  N  NE    . ARG A 1 113 ? 15.09251  11.01330  -22.62826 1.000 15.17757 ? 113 ARG A NE    1 
ATOM   897  C  CZ    . ARG A 1 113 ? 15.35699  9.81385   -22.12742 1.000 15.05178 ? 113 ARG A CZ    1 
ATOM   898  N  NH1   . ARG A 1 113 ? 14.50049  9.18985   -21.33533 1.000 20.07104 ? 113 ARG A NH1   1 
ATOM   899  N  NH2   . ARG A 1 113 ? 16.50984  9.22425   -22.43217 1.000 12.03055 ? 113 ARG A NH2   1 
ATOM   900  N  N     . ASP A 1 114 ? 16.51668  13.50960  -25.55298 1.000 15.75306 ? 114 ASP A N     1 
ATOM   901  C  CA    . ASP A 1 114 ? 17.78169  14.07260  -25.08600 1.000 17.20437 ? 114 ASP A CA    1 
ATOM   902  C  C     . ASP A 1 114 ? 18.22567  15.25561  -25.93901 1.000 20.68268 ? 114 ASP A C     1 
ATOM   903  O  O     . ASP A 1 114 ? 18.83468  16.19861  -25.41502 1.000 17.83896 ? 114 ASP A O     1 
ATOM   904  C  CB    . ASP A 1 114 ? 18.86170  12.99061  -25.04802 1.000 16.08506 ? 114 ASP A CB    1 
ATOM   905  C  CG    . ASP A 1 114 ? 18.55272  11.90561  -24.04301 1.000 12.51347 ? 114 ASP A CG    1 
ATOM   906  O  OD1   . ASP A 1 114 ? 17.58873  12.08760  -23.27100 1.000 14.26326 ? 114 ASP A OD1   1 
ATOM   907  O  OD2   . ASP A 1 114 ? 19.25972  10.87461  -24.02303 1.000 11.70242 ? 114 ASP A OD2   1 
ATOM   908  N  N     . ALA A 1 115 ? 17.92165  15.23760  -27.24100 1.000 17.23118 ? 115 ALA A N     1 
ATOM   909  C  CA    . ALA A 1 115 ? 18.20363  16.40361  -28.07301 1.000 17.37472 ? 115 ALA A CA    1 
ATOM   910  C  C     . ALA A 1 115 ? 17.41564  17.61760  -27.60099 1.000 19.54310 ? 115 ALA A C     1 
ATOM   911  O  O     . ALA A 1 115 ? 17.94763  18.73061  -27.54600 1.000 32.19087 ? 115 ALA A O     1 
ATOM   912  C  CB    . ALA A 1 115 ? 17.89461  16.10261  -29.53900 1.000 20.18105 ? 115 ALA A CB    1 
ATOM   913  N  N     . ALA A 1 116 ? 16.14264  17.42260  -27.25197 1.000 19.29256 ? 116 ALA A N     1 
ATOM   914  C  CA    . ALA A 1 116 ? 15.32965  18.53560  -26.77796 1.000 19.12193 ? 116 ALA A CA    1 
ATOM   915  C  C     . ALA A 1 116 ? 15.85167  19.09160  -25.46097 1.000 18.82201 ? 116 ALA A C     1 
ATOM   916  O  O     . ALA A 1 116 ? 15.69367  20.28660  -25.18496 1.000 16.79841 ? 116 ALA A O     1 
ATOM   917  C  CB    . ALA A 1 116 ? 13.87365  18.09359  -26.62993 1.000 25.06762 ? 116 ALA A CB    1 
ATOM   918  N  N     . VAL A 1 117 ? 16.48268  18.24960  -24.64398 1.000 12.75980 ? 117 VAL A N     1 
ATOM   919  C  CA    . VAL A 1 117 ? 16.99570  18.70760  -23.35899 1.000 20.96199 ? 117 VAL A CA    1 
ATOM   920  C  C     . VAL A 1 117 ? 18.31670  19.45261  -23.52701 1.000 19.23898 ? 117 VAL A C     1 
ATOM   921  O  O     . VAL A 1 117 ? 18.58571  20.41161  -22.79201 1.000 19.74927 ? 117 VAL A O     1 
ATOM   922  C  CB    . VAL A 1 117 ? 17.13572  17.51760  -22.39499 1.000 16.84686 ? 117 VAL A CB    1 
ATOM   923  C  CG1   . VAL A 1 117 ? 17.71474  17.96860  -21.06300 1.000 18.46325 ? 117 VAL A CG1   1 
ATOM   924  C  CG2   . VAL A 1 117 ? 15.78973  16.84860  -22.18897 1.000 19.89103 ? 117 VAL A CG2   1 
ATOM   925  N  N     A ARG A 1 118 ? 19.14957  19.04156  -24.48833 0.614 17.47504 ? 118 ARG A N     1 
ATOM   926  N  N     B ARG A 1 118 ? 19.15342  19.02988  -24.48015 0.386 17.54209 ? 118 ARG A N     1 
ATOM   927  C  CA    A ARG A 1 118 ? 20.42363  19.72156  -24.70516 0.614 21.45690 ? 118 ARG A CA    1 
ATOM   928  C  CA    B ARG A 1 118 ? 20.42152  19.71361  -24.71919 0.386 21.40790 ? 118 ARG A CA    1 
ATOM   929  C  C     A ARG A 1 118 ? 20.21572  21.16990  -25.12842 0.614 19.38856 ? 118 ARG A C     1 
ATOM   930  C  C     B ARG A 1 118 ? 20.20272  21.16726  -25.11636 0.386 19.40588 ? 118 ARG A C     1 
ATOM   931  O  O     A ARG A 1 118 ? 20.93682  22.06588  -24.67363 0.614 19.68624 ? 118 ARG A O     1 
ATOM   932  O  O     B ARG A 1 118 ? 20.90340  22.06372  -24.63147 0.386 19.67545 ? 118 ARG A O     1 
ATOM   933  C  CB    A ARG A 1 118 ? 21.24924  18.97959  -25.75518 0.614 21.59078 ? 118 ARG A CB    1 
ATOM   934  C  CB    B ARG A 1 118 ? 21.21483  18.98725  -25.80477 0.386 21.56910 ? 118 ARG A CB    1 
ATOM   935  C  CG    A ARG A 1 118 ? 21.71091  17.59572  -25.34157 0.614 21.82487 ? 118 ARG A CG    1 
ATOM   936  C  CG    B ARG A 1 118 ? 22.00295  17.77919  -25.33213 0.386 21.87706 ? 118 ARG A CG    1 
ATOM   937  C  CD    A ARG A 1 118 ? 22.55207  16.96943  -26.44094 0.614 23.24104 ? 118 ARG A CD    1 
ATOM   938  C  CD    B ARG A 1 118 ? 22.61641  17.06432  -26.52512 0.386 23.14331 ? 118 ARG A CD    1 
ATOM   939  N  NE    A ARG A 1 118 ? 22.76483  15.54221  -26.23103 0.614 21.74002 ? 118 ARG A NE    1 
ATOM   940  N  NE    B ARG A 1 118 ? 23.59594  16.05328  -26.14568 0.386 23.28792 ? 118 ARG A NE    1 
ATOM   941  C  CZ    A ARG A 1 118 ? 23.86092  15.01626  -25.70240 0.614 19.31294 ? 118 ARG A CZ    1 
ATOM   942  C  CZ    B ARG A 1 118 ? 23.29290  14.82970  -25.73504 0.386 19.63375 ? 118 ARG A CZ    1 
ATOM   943  N  NH1   A ARG A 1 118 ? 24.87360  15.77421  -25.31404 0.614 24.65886 ? 118 ARG A NH1   1 
ATOM   944  N  NH1   B ARG A 1 118 ? 22.03757  14.44430  -25.57676 0.386 21.34125 ? 118 ARG A NH1   1 
ATOM   945  N  NH2   A ARG A 1 118 ? 23.94479  13.69632  -25.56347 0.614 21.72810 ? 118 ARG A NH2   1 
ATOM   946  N  NH2   B ARG A 1 118 ? 24.27424  13.97045  -25.47844 0.386 21.44766 ? 118 ARG A NH2   1 
ATOM   947  N  N     . ARG A 1 119 ? 19.23658  21.41988  -26.00278 1.000 20.23767 ? 119 ARG A N     1 
ATOM   948  C  CA    . ARG A 1 119 ? 18.98076  22.78408  -26.45249 1.000 19.32825 ? 119 ARG A CA    1 
ATOM   949  C  C     . ARG A 1 119 ? 18.39284  23.63948  -25.34029 1.000 19.86346 ? 119 ARG A C     1 
ATOM   950  O  O     . ARG A 1 119 ? 18.67599  24.84068  -25.27025 1.000 14.25873 ? 119 ARG A O     1 
ATOM   951  C  CB    . ARG A 1 119 ? 18.05180  22.77307  -27.66557 1.000 20.50358 ? 119 ARG A CB    1 
ATOM   952  C  CG    . ARG A 1 119 ? 18.64463  22.09301  -28.88971 0.000 20.41449 ? 119 ARG A CG    1 
ATOM   953  C  CD    . ARG A 1 119 ? 17.63668  22.00709  -30.02460 0.000 20.56991 ? 119 ARG A CD    1 
ATOM   954  N  NE    . ARG A 1 119 ? 16.50205  21.15691  -29.68454 0.000 20.72008 ? 119 ARG A NE    1 
ATOM   955  C  CZ    . ARG A 1 119 ? 15.50902  20.86570  -30.51365 0.000 20.84694 ? 119 ARG A CZ    1 
ATOM   956  N  NH1   . ARG A 1 119 ? 15.47662  21.34175  -31.74762 0.000 20.40139 ? 119 ARG A NH1   1 
ATOM   957  N  NH2   . ARG A 1 119 ? 14.52429  20.07599  -30.09460 0.000 21.23604 ? 119 ARG A NH2   1 
ATOM   958  N  N     . LEU A 1 120 ? 17.57367  23.04360  -24.46999 1.000 22.24013 ? 120 LEU A N     1 
ATOM   959  C  CA    . LEU A 1 120 ? 17.07269  23.76660  -23.30899 1.000 16.60327 ? 120 LEU A CA    1 
ATOM   960  C  C     . LEU A 1 120 ? 18.18870  24.06860  -22.32300 1.000 14.12023 ? 120 LEU A C     1 
ATOM   961  O  O     . LEU A 1 120 ? 18.15471  25.10260  -21.64900 1.000 19.84906 ? 120 LEU A O     1 
ATOM   962  C  CB    . LEU A 1 120 ? 15.96670  22.96360  -22.62497 1.000 16.85455 ? 120 LEU A CB    1 
ATOM   963  C  CG    . LEU A 1 120 ? 14.62769  22.83959  -23.35195 1.000 15.43508 ? 120 LEU A CG    1 
ATOM   964  C  CD1   . LEU A 1 120 ? 13.72770  21.84659  -22.63993 1.000 16.25979 ? 120 LEU A CD1   1 
ATOM   965  C  CD2   . LEU A 1 120 ? 13.94668  24.19459  -23.45793 1.000 22.97207 ? 120 LEU A CD2   1 
ATOM   966  N  N     . ALA A 1 121 ? 19.17671  23.18061  -22.21802 1.000 16.89299 ? 121 ALA A N     1 
ATOM   967  C  CA    . ALA A 1 121 ? 20.30572  23.43461  -21.33104 1.000 18.43259 ? 121 ALA A CA    1 
ATOM   968  C  C     . ALA A 1 121 ? 21.23371  24.49761  -21.90805 1.000 17.52782 ? 121 ALA A C     1 
ATOM   969  O  O     . ALA A 1 121 ? 21.80572  25.30162  -21.16506 1.000 17.68630 ? 121 ALA A O     1 
ATOM   970  C  CB    . ALA A 1 121 ? 21.07073  22.13761  -21.07205 1.000 15.42738 ? 121 ALA A CB    1 
ATOM   971  N  N     . ALA A 1 122 ? 21.39469  24.51362  -23.23306 1.000 16.75185 ? 122 ALA A N     1 
ATOM   972  C  CA    . ALA A 1 122 ? 22.20967  25.54162  -23.86907 1.000 20.62557 ? 122 ALA A CA    1 
ATOM   973  C  C     . ALA A 1 122 ? 21.60767  26.92562  -23.66206 1.000 15.05534 ? 122 ALA A C     1 
ATOM   974  O  O     . ALA A 1 122 ? 22.32967  27.89062  -23.39807 1.000 19.59425 ? 122 ALA A O     1 
ATOM   975  C  CB    . ALA A 1 122 ? 22.36865  25.23562  -25.35807 1.000 19.61924 ? 122 ALA A CB    1 
ATOM   976  N  N     . GLU A 1 123 ? 20.30167  27.03861  -23.74304 1.000 15.09086 ? 123 GLU A N     1 
ATOM   977  C  CA    . GLU A 1 123 ? 19.73967  28.38161  -23.54103 1.000 20.72713 ? 123 GLU A CA    1 
ATOM   978  C  C     . GLU A 1 123 ? 19.89969  28.79961  -22.07403 1.000 14.65312 ? 123 GLU A C     1 
ATOM   979  O  O     . GLU A 1 123 ? 20.01869  29.98361  -21.82803 1.000 17.35278 ? 123 GLU A O     1 
ATOM   980  C  CB    . GLU A 1 123 ? 18.28866  28.39461  -24.00200 1.000 19.39263 ? 123 GLU A CB    1 
ATOM   981  C  CG    . GLU A 1 123 ? 18.11064  28.03961  -25.46000 1.000 26.73589 ? 123 GLU A CG    1 
ATOM   982  C  CD    . GLU A 1 123 ? 16.68663  27.67060  -25.82398 1.000 28.12400 ? 123 GLU A CD    1 
ATOM   983  O  OE1   . GLU A 1 123 ? 15.88665  27.47260  -24.90496 1.000 30.65059 ? 123 GLU A OE1   1 
ATOM   984  O  OE2   . GLU A 1 123 ? 16.38761  27.59160  -27.02697 1.000 37.89331 ? 123 GLU A OE2   1 
ATOM   985  N  N     . ALA A 1 124 ? 19.84771  27.84061  -21.15203 1.000 17.39340 ? 124 ALA A N     1 
ATOM   986  C  CA    . ALA A 1 124 ? 20.05973  28.15661  -19.74703 1.000 18.14235 ? 124 ALA A CA    1 
ATOM   987  C  C     . ALA A 1 124 ? 21.53274  28.27161  -19.38106 1.000 20.35678 ? 124 ALA A C     1 
ATOM   988  O  O     . ALA A 1 124 ? 21.84276  28.51162  -18.20806 1.000 22.38108 ? 124 ALA A O     1 
ATOM   989  C  CB    . ALA A 1 124 ? 19.39375  27.09861  -18.86702 1.000 15.04552 ? 124 ALA A CB    1 
ATOM   990  N  N     . GLY A 1 125 ? 22.43772  28.10662  -20.34407 1.000 21.11529 ? 125 GLY A N     1 
ATOM   991  C  CA    . GLY A 1 125 ? 23.85873  28.13062  -20.05410 1.000 19.77686 ? 125 GLY A CA    1 
ATOM   992  C  C     . GLY A 1 125 ? 24.36074  26.93762  -19.27011 1.000 16.64782 ? 125 GLY A C     1 
ATOM   993  O  O     . GLY A 1 125 ? 25.33276  27.06263  -18.52012 1.000 13.66346 ? 125 GLY A O     1 
ATOM   994  N  N     . VAL A 1 126 ? 23.73174  25.77662  -19.43410 1.000 13.42559 ? 126 VAL A N     1 
ATOM   995  C  CA    . VAL A 1 126 ? 24.06576  24.57662  -18.67710 1.000 16.70247 ? 126 VAL A CA    1 
ATOM   996  C  C     . VAL A 1 126 ? 24.95875  23.68363  -19.52912 1.000 12.23006 ? 126 VAL A C     1 
ATOM   997  O  O     . VAL A 1 126 ? 24.64173  23.40663  -20.69211 1.000 16.84406 ? 126 VAL A O     1 
ATOM   998  C  CB    . VAL A 1 126 ? 22.79077  23.83162  -18.24108 1.000 11.70772 ? 126 VAL A CB    1 
ATOM   999  C  CG1   . VAL A 1 126 ? 23.13979  22.50662  -17.59509 1.000 13.32624 ? 126 VAL A CG1   1 
ATOM   1000 C  CG2   . VAL A 1 126 ? 21.97578  24.69262  -17.29407 1.000 15.15057 ? 126 VAL A CG2   1 
ATOM   1001 N  N     . GLU A 1 127 ? 26.07476  23.23563  -18.95214 1.000 15.18335 ? 127 GLU A N     1 
ATOM   1002 C  CA    . GLU A 1 127 ? 26.96675  22.30163  -19.63015 1.000 15.78974 ? 127 GLU A CA    1 
ATOM   1003 C  C     . GLU A 1 127 ? 26.40176  20.89163  -19.54914 1.000 12.65223 ? 127 GLU A C     1 
ATOM   1004 O  O     . GLU A 1 127 ? 25.89378  20.47363  -18.50713 1.000 10.01036 ? 127 GLU A O     1 
ATOM   1005 C  CB    . GLU A 1 127 ? 28.36376  22.33364  -19.00917 1.000 16.75405 ? 127 GLU A CB    1 
ATOM   1006 C  CG    . GLU A 1 127 ? 29.31576  21.28764  -19.58719 1.000 17.87174 ? 127 GLU A CG    1 
ATOM   1007 C  CD    . GLU A 1 127 ? 30.63577  21.19965  -18.84321 1.000 19.21324 ? 127 GLU A CD    1 
ATOM   1008 O  OE1   . GLU A 1 127 ? 30.80178  21.89565  -17.81721 1.000 18.59708 ? 127 GLU A OE1   1 
ATOM   1009 O  OE2   . GLU A 1 127 ? 31.50977  20.42865  -19.28923 1.000 26.86293 ? 127 GLU A OE2   1 
ATOM   1010 N  N     . VAL A 1 128 ? 26.50074  20.15463  -20.65314 1.000 18.54698 ? 128 VAL A N     1 
ATOM   1011 C  CA    . VAL A 1 128 ? 25.92975  18.81563  -20.76813 1.000 11.22960 ? 128 VAL A CA    1 
ATOM   1012 C  C     . VAL A 1 128 ? 27.06475  17.81663  -20.95615 1.000 10.17254 ? 128 VAL A C     1 
ATOM   1013 O  O     . VAL A 1 128 ? 27.84573  17.93264  -21.90517 1.000 9.54524  ? 128 VAL A O     1 
ATOM   1014 C  CB    . VAL A 1 128 ? 24.92773  18.72663  -21.92812 1.000 12.20143 ? 128 VAL A CB    1 
ATOM   1015 C  CG1   . VAL A 1 128 ? 24.24773  17.36162  -21.94911 1.000 18.17966 ? 128 VAL A CG1   1 
ATOM   1016 C  CG2   . VAL A 1 128 ? 23.90873  19.85062  -21.82510 1.000 15.88685 ? 128 VAL A CG2   1 
ATOM   1017 N  N     . VAL A 1 129 ? 27.14576  16.83763  -20.05716 1.000 12.43240 ? 129 VAL A N     1 
ATOM   1018 C  CA    . VAL A 1 129 ? 28.11977  15.75364  -20.11517 1.000 12.41522 ? 129 VAL A CA    1 
ATOM   1019 C  C     . VAL A 1 129 ? 27.36077  14.43863  -20.18616 1.000 11.42393 ? 129 VAL A C     1 
ATOM   1020 O  O     . VAL A 1 129 ? 26.53079  14.15463  -19.31715 1.000 8.60432  ? 129 VAL A O     1 
ATOM   1021 C  CB    . VAL A 1 129 ? 29.06079  15.77064  -18.89619 1.000 12.35233 ? 129 VAL A CB    1 
ATOM   1022 C  CG1   . VAL A 1 129 ? 30.14179  14.69864  -19.03621 1.000 16.18901 ? 129 VAL A CG1   1 
ATOM   1023 C  CG2   . VAL A 1 129 ? 29.65779  17.15764  -18.69720 1.000 15.62825 ? 129 VAL A CG2   1 
ATOM   1024 N  N     . THR A 1 130 ? 27.64876  13.63664  -21.21116 1.000 9.51092  ? 130 THR A N     1 
ATOM   1025 C  CA    . THR A 1 130 ? 26.91076  12.40263  -21.48815 1.000 9.95824  ? 130 THR A CA    1 
ATOM   1026 C  C     . THR A 1 130 ? 27.86476  11.24864  -21.77117 1.000 8.72541  ? 130 THR A C     1 
ATOM   1027 O  O     . THR A 1 130 ? 28.09174  10.89164  -22.93517 1.000 11.16663 ? 130 THR A O     1 
ATOM   1028 C  CB    . THR A 1 130 ? 25.95474  12.59563  -22.66914 1.000 10.87736 ? 130 THR A CB    1 
ATOM   1029 O  OG1   . THR A 1 130 ? 26.69172  13.08163  -23.79715 1.000 11.91522 ? 130 THR A OG1   1 
ATOM   1030 C  CG2   . THR A 1 130 ? 24.88174  13.60063  -22.31912 1.000 13.50377 ? 130 THR A CG2   1 
ATOM   1031 N  N     . PRO A 1 131 ? 28.41177  10.61764  -20.73618 1.000 8.71081  ? 131 PRO A N     1 
ATOM   1032 C  CA    . PRO A 1 131 ? 29.33577  9.50364   -20.95819 1.000 8.62307  ? 131 PRO A CA    1 
ATOM   1033 C  C     . PRO A 1 131 ? 28.59277  8.24664   -21.38018 1.000 8.47522  ? 131 PRO A C     1 
ATOM   1034 O  O     . PRO A 1 131 ? 27.38278  8.11264   -21.19616 1.000 9.32941  ? 131 PRO A O     1 
ATOM   1035 C  CB    . PRO A 1 131 ? 29.99780  9.32064   -19.59021 1.000 12.44457 ? 131 PRO A CB    1 
ATOM   1036 C  CG    . PRO A 1 131 ? 28.93281  9.71264   -18.63219 1.000 11.15204 ? 131 PRO A CG    1 
ATOM   1037 C  CD    . PRO A 1 131 ? 28.15380  10.83364  -19.30117 1.000 9.36905  ? 131 PRO A CD    1 
ATOM   1038 N  N     . ILE A 1 132 ? 29.34277  7.32264   -21.97119 1.000 9.79315  ? 132 ILE A N     1 
ATOM   1039 C  CA    . ILE A 1 132 ? 28.80976  6.02964   -22.38819 1.000 8.48639  ? 132 ILE A CA    1 
ATOM   1040 C  C     . ILE A 1 132 ? 29.16478  5.00664   -21.32019 1.000 8.33959  ? 132 ILE A C     1 
ATOM   1041 O  O     . ILE A 1 132 ? 30.34679  4.81865   -21.00521 1.000 8.42346  ? 132 ILE A O     1 
ATOM   1042 C  CB    . ILE A 1 132 ? 29.35874  5.60864   -23.75720 1.000 8.70967  ? 132 ILE A CB    1 
ATOM   1043 C  CG1   . ILE A 1 132 ? 28.88572  6.58264   -24.83619 1.000 10.37702 ? 132 ILE A CG1   1 
ATOM   1044 C  CG2   . ILE A 1 132 ? 28.93374  4.18464   -24.07119 1.000 10.22706 ? 132 ILE A CG2   1 
ATOM   1045 C  CD1   . ILE A 1 132 ? 29.98370  7.02765   -25.76221 1.000 13.65547 ? 132 ILE A CD1   1 
ATOM   1046 N  N     . SER A 1 133 ? 28.14380  4.34864   -20.76118 1.000 8.15867  ? 133 SER A N     1 
ATOM   1047 C  CA    . SER A 1 133 ? 28.35382  3.35764   -19.71018 1.000 8.04560  ? 133 SER A CA    1 
ATOM   1048 C  C     . SER A 1 133 ? 27.26482  2.28863   -19.67816 1.000 7.93432  ? 133 SER A C     1 
ATOM   1049 O  O     . SER A 1 133 ? 27.39184  1.31063   -18.93916 1.000 7.87532  ? 133 SER A O     1 
ATOM   1050 C  CB    . SER A 1 133 ? 28.45184  4.03664   -18.34118 1.000 9.97380  ? 133 SER A CB    1 
ATOM   1051 O  OG    . SER A 1 133 ? 27.68983  5.23164   -18.30417 1.000 15.01754 ? 133 SER A OG    1 
ATOM   1052 N  N     . HIS A 1 134 ? 26.20281  2.44463   -20.47614 1.000 7.94115  ? 134 HIS A N     1 
ATOM   1053 C  CA    . HIS A 1 134 ? 25.16381  1.41563   -20.53113 1.000 8.94136  ? 134 HIS A CA    1 
ATOM   1054 C  C     . HIS A 1 134 ? 25.58080  0.23763   -21.40113 1.000 7.97848  ? 134 HIS A C     1 
ATOM   1055 O  O     . HIS A 1 134 ? 25.09681  -0.87937  -21.20013 1.000 7.94023  ? 134 HIS A O     1 
ATOM   1056 C  CB    . HIS A 1 134 ? 23.85180  2.01362   -21.04211 1.000 8.47630  ? 134 HIS A CB    1 
ATOM   1057 C  CG    . HIS A 1 134 ? 22.70780  1.04562   -21.08009 1.000 9.30062  ? 134 HIS A CG    1 
ATOM   1058 N  ND1   . HIS A 1 134 ? 22.14382  0.51162   -19.94208 1.000 8.67236  ? 134 HIS A ND1   1 
ATOM   1059 C  CD2   . HIS A 1 134 ? 22.00579  0.53462   -22.12108 1.000 8.97037  ? 134 HIS A CD2   1 
ATOM   1060 C  CE1   . HIS A 1 134 ? 21.15282  -0.29439  -20.27906 1.000 11.48931 ? 134 HIS A CE1   1 
ATOM   1061 N  NE2   . HIS A 1 134 ? 21.04480  -0.29539  -21.59506 1.000 8.33980  ? 134 HIS A NE2   1 
ATOM   1062 N  N     . THR A 1 135 ? 26.46578  0.46963   -22.36015 1.000 8.13217  ? 135 THR A N     1 
ATOM   1063 C  CA    . THR A 1 135 ? 27.03077  -0.56637  -23.20916 1.000 9.19296  ? 135 THR A CA    1 
ATOM   1064 C  C     . THR A 1 135 ? 28.49478  -0.77336  -22.85418 1.000 8.33277  ? 135 THR A C     1 
ATOM   1065 O  O     . THR A 1 135 ? 29.11779  0.06064   -22.19219 1.000 8.65601  ? 135 THR A O     1 
ATOM   1066 C  CB    . THR A 1 135 ? 26.90475  -0.19237  -24.69016 1.000 8.78876  ? 135 THR A CB    1 
ATOM   1067 O  OG1   . THR A 1 135 ? 27.39474  1.14064   -24.88816 1.000 9.09346  ? 135 THR A OG1   1 
ATOM   1068 C  CG2   . THR A 1 135 ? 25.44974  -0.26937  -25.13913 1.000 10.94240 ? 135 THR A CG2   1 
ATOM   1069 N  N     . LEU A 1 136 ? 29.04577  -1.89936  -23.30919 1.000 8.44229  ? 136 LEU A N     1 
ATOM   1070 C  CA    . LEU A 1 136 ? 30.46478  -2.15235  -23.09322 1.000 8.56385  ? 136 LEU A CA    1 
ATOM   1071 C  C     . LEU A 1 136 ? 31.31776  -1.11735  -23.81923 1.000 9.11547  ? 136 LEU A C     1 
ATOM   1072 O  O     . LEU A 1 136 ? 32.25277  -0.55135  -23.24125 1.000 10.31917 ? 136 LEU A O     1 
ATOM   1073 C  CB    . LEU A 1 136 ? 30.82278  -3.56335  -23.55022 1.000 11.28343 ? 136 LEU A CB    1 
ATOM   1074 C  CG    . LEU A 1 136 ? 30.15579  -4.72335  -22.80921 1.000 8.55083  ? 136 LEU A CG    1 
ATOM   1075 C  CD1   . LEU A 1 136 ? 30.47379  -6.02935  -23.50822 1.000 9.18895  ? 136 LEU A CD1   1 
ATOM   1076 C  CD2   . LEU A 1 136 ? 30.61282  -4.76135  -21.35822 1.000 8.45909  ? 136 LEU A CD2   1 
ATOM   1077 N  N     . TYR A 1 137 ? 30.99574  -0.84135  -25.08222 1.000 8.89277  ? 137 TYR A N     1 
ATOM   1078 C  CA    . TYR A 1 137 ? 31.77972  0.05065   -25.92624 1.000 9.13473  ? 137 TYR A CA    1 
ATOM   1079 C  C     . TYR A 1 137 ? 30.95071  1.24465   -26.38122 1.000 9.13367  ? 137 TYR A C     1 
ATOM   1080 O  O     . TYR A 1 137 ? 29.72171  1.26464   -26.27820 1.000 8.97928  ? 137 TYR A O     1 
ATOM   1081 C  CB    . TYR A 1 137 ? 32.31771  -0.68235  -27.16025 1.000 9.40918  ? 137 TYR A CB    1 
ATOM   1082 C  CG    . TYR A 1 137 ? 33.17872  -1.88934  -26.86126 1.000 15.32311 ? 137 TYR A CG    1 
ATOM   1083 C  CD1   . TYR A 1 137 ? 34.54872  -1.75534  -26.64528 1.000 10.55877 ? 137 TYR A CD1   1 
ATOM   1084 C  CD2   . TYR A 1 137 ? 32.63072  -3.16735  -26.82125 1.000 13.02255 ? 137 TYR A CD2   1 
ATOM   1085 C  CE1   . TYR A 1 137 ? 35.34273  -2.85734  -26.38330 1.000 12.23134 ? 137 TYR A CE1   1 
ATOM   1086 C  CE2   . TYR A 1 137 ? 33.41873  -4.27834  -26.56027 1.000 9.48977  ? 137 TYR A CE2   1 
ATOM   1087 C  CZ    . TYR A 1 137 ? 34.77373  -4.11234  -26.34229 1.000 12.86341 ? 137 TYR A CZ    1 
ATOM   1088 O  OH    . TYR A 1 137 ? 35.56274  -5.20734  -26.08530 1.000 17.02860 ? 137 TYR A OH    1 
ATOM   1089 N  N     . ASP A 1 138 ? 31.65470  2.25065   -26.89423 1.000 9.40385  ? 138 ASP A N     1 
ATOM   1090 C  CA    . ASP A 1 138 ? 31.02668  3.28365   -27.71122 1.000 14.28727 ? 138 ASP A CA    1 
ATOM   1091 C  C     . ASP A 1 138 ? 30.54366  2.62665   -28.99722 1.000 10.51639 ? 138 ASP A C     1 
ATOM   1092 O  O     . ASP A 1 138 ? 31.35365  2.24365   -29.84723 1.000 9.91371  ? 138 ASP A O     1 
ATOM   1093 C  CB    . ASP A 1 138 ? 32.01768  4.40965   -28.00124 1.000 14.20703 ? 138 ASP A CB    1 
ATOM   1094 C  CG    . ASP A 1 138 ? 31.37066  5.62165   -28.65923 1.000 13.94649 ? 138 ASP A CG    1 
ATOM   1095 O  OD1   . ASP A 1 138 ? 30.26765  5.49565   -29.22721 1.000 16.63682 ? 138 ASP A OD1   1 
ATOM   1096 O  OD2   . ASP A 1 138 ? 31.98166  6.71065   -28.61824 1.000 16.82419 ? 138 ASP A OD2   1 
ATOM   1097 N  N     . THR A 1 139 ? 29.22566  2.47064   -29.13119 1.000 10.11252 ? 139 THR A N     1 
ATOM   1098 C  CA    . THR A 1 139 ? 28.68765  1.74564   -30.27719 1.000 10.64863 ? 139 THR A CA    1 
ATOM   1099 C  C     . THR A 1 139 ? 28.97562  2.46664   -31.58819 1.000 13.82641 ? 139 THR A C     1 
ATOM   1100 O  O     . THR A 1 139 ? 29.15461  1.81864   -32.62619 1.000 13.23957 ? 139 THR A O     1 
ATOM   1101 C  CB    . THR A 1 139 ? 27.18465  1.52864   -30.10016 1.000 15.21666 ? 139 THR A CB    1 
ATOM   1102 O  OG1   . THR A 1 139 ? 26.54465  2.78364   -29.84315 1.000 26.28596 ? 139 THR A OG1   1 
ATOM   1103 C  CG2   . THR A 1 139 ? 26.91267  0.58464   -28.93616 1.000 14.36908 ? 139 THR A CG2   1 
ATOM   1104 N  N     . ASP A 1 140 ? 29.02662  3.80264   -31.56419 1.000 15.74746 ? 140 ASP A N     1 
ATOM   1105 C  CA    . ASP A 1 140 ? 29.38160  4.55565   -32.76320 1.000 14.00816 ? 140 ASP A CA    1 
ATOM   1106 C  C     . ASP A 1 140 ? 30.85059  4.37265   -33.12022 1.000 16.05039 ? 140 ASP A C     1 
ATOM   1107 O  O     . ASP A 1 140 ? 31.21757  4.44165   -34.29823 1.000 12.87918 ? 140 ASP A O     1 
ATOM   1108 C  CB    . ASP A 1 140 ? 29.06459  6.04164   -32.57119 1.000 15.47184 ? 140 ASP A CB    1 
ATOM   1109 C  CG    . ASP A 1 140 ? 27.57559  6.32164   -32.51917 1.000 16.58592 ? 140 ASP A CG    1 
ATOM   1110 O  OD1   . ASP A 1 140 ? 26.82258  5.65064   -33.25515 1.000 25.86536 ? 140 ASP A OD1   1 
ATOM   1111 O  OD2   . ASP A 1 140 ? 27.15560  7.21164   -31.74716 1.000 20.72088 ? 140 ASP A OD2   1 
ATOM   1112 N  N     . MET A 1 141 ? 31.69961  4.14465   -32.11824 1.000 16.86699 ? 141 MET A N     1 
ATOM   1113 C  CA    . MET A 1 141 ? 33.10060  3.84766   -32.38726 1.000 15.97247 ? 141 MET A CA    1 
ATOM   1114 C  C     . MET A 1 141 ? 33.25360  2.50366   -33.09126 1.000 15.68761 ? 141 MET A C     1 
ATOM   1115 O  O     . MET A 1 141 ? 34.01858  2.39166   -34.05527 1.000 14.85922 ? 141 MET A O     1 
ATOM   1116 C  CB    . MET A 1 141 ? 33.89563  3.87866   -31.07827 1.000 15.58208 ? 141 MET A CB    1 
ATOM   1117 C  CG    . MET A 1 141 ? 35.35463  3.49367   -31.20630 1.000 10.91290 ? 141 MET A CG    1 
ATOM   1118 S  SD    . MET A 1 141 ? 35.63764  1.74167   -30.90330 1.000 23.87288 ? 141 MET A SD    1 
ATOM   1119 C  CE    . MET A 1 141 ? 35.11366  1.59666   -29.19729 1.000 10.31209 ? 141 MET A CE    1 
ATOM   1120 N  N     . LEU A 1 142 ? 32.52761  1.47666   -32.62825 1.000 13.03780 ? 142 LEU A N     1 
ATOM   1121 C  CA    . LEU A 1 142 ? 32.60260  0.16166   -33.26325 1.000 14.87424 ? 142 LEU A CA    1 
ATOM   1122 C  C     . LEU A 1 142 ? 32.19058  0.22966   -34.72924 1.000 12.80002 ? 142 LEU A C     1 
ATOM   1123 O  O     . LEU A 1 142 ? 32.80657  -0.41434  -35.58625 1.000 14.48214 ? 142 LEU A O     1 
ATOM   1124 C  CB    . LEU A 1 142 ? 31.72262  -0.84035  -32.51824 1.000 10.49602 ? 142 LEU A CB    1 
ATOM   1125 C  CG    . LEU A 1 142 ? 32.06664  -1.22535  -31.07824 1.000 10.17890 ? 142 LEU A CG    1 
ATOM   1126 C  CD1   . LEU A 1 142 ? 31.10166  -2.28835  -30.57623 1.000 13.27967 ? 142 LEU A CD1   1 
ATOM   1127 C  CD2   . LEU A 1 142 ? 33.49165  -1.72134  -30.98927 1.000 15.91687 ? 142 LEU A CD2   1 
ATOM   1128 N  N     . VAL A 1 143 ? 31.14957  1.00565   -35.03423 1.000 11.18802 ? 143 VAL A N     1 
ATOM   1129 C  CA    . VAL A 1 143 ? 30.70355  1.14965   -36.41622 1.000 13.44404 ? 143 VAL A CA    1 
ATOM   1130 C  C     . VAL A 1 143 ? 31.76653  1.85366   -37.25024 1.000 13.66329 ? 143 VAL A C     1 
ATOM   1131 O  O     . VAL A 1 143 ? 32.04451  1.45966   -38.38824 1.000 16.97654 ? 143 VAL A O     1 
ATOM   1132 C  CB    . VAL A 1 143 ? 29.35754  1.89565   -36.47020 1.000 15.50071 ? 143 VAL A CB    1 
ATOM   1133 C  CG1   . VAL A 1 143 ? 29.02652  2.30265   -37.90319 1.000 18.17740 ? 143 VAL A CG1   1 
ATOM   1134 C  CG2   . VAL A 1 143 ? 28.25756  1.03164   -35.90418 1.000 14.91889 ? 143 VAL A CG2   1 
ATOM   1135 N  N     . ALA A 1 144 ? 32.38054  2.90066   -36.69825 1.000 17.98135 ? 144 ALA A N     1 
ATOM   1136 C  CA    . ALA A 1 144 ? 33.40352  3.63166   -37.43626 1.000 13.04753 ? 144 ALA A CA    1 
ATOM   1137 C  C     . ALA A 1 144 ? 34.65852  2.79567   -37.64328 1.000 16.14986 ? 144 ALA A C     1 
ATOM   1138 O  O     . ALA A 1 144 ? 35.32950  2.93167   -38.67230 1.000 17.37434 ? 144 ALA A O     1 
ATOM   1139 C  CB    . ALA A 1 144 ? 33.74153  4.93166   -36.70927 1.000 18.29935 ? 144 ALA A CB    1 
ATOM   1140 N  N     . ARG A 1 145 ? 34.99994  1.93818   -36.67792 1.000 14.87979 ? 145 ARG A N     1 
ATOM   1141 C  CA    . ARG A 1 145 ? 36.17053  1.08081   -36.82492 1.000 17.89608 ? 145 ARG A CA    1 
ATOM   1142 C  C     . ARG A 1 145 ? 35.93282  -0.04314  -37.82210 1.000 16.37625 ? 145 ARG A C     1 
ATOM   1143 O  O     . ARG A 1 145 ? 36.89820  -0.57997  -38.37484 1.000 19.18792 ? 145 ARG A O     1 
ATOM   1144 C  CB    . ARG A 1 145 ? 36.57515  0.50103   -35.46807 1.000 21.14296 ? 145 ARG A CB    1 
ATOM   1145 C  CG    . ARG A 1 145 ? 37.00245  1.54903   -34.45009 1.000 21.69130 ? 145 ARG A CG    1 
ATOM   1146 C  CD    . ARG A 1 145 ? 38.48205  1.87557   -34.56423 1.000 34.14765 ? 145 ARG A CD    1 
ATOM   1147 N  NE    . ARG A 1 145 ? 39.30014  0.85409   -33.92259 1.000 36.46888 ? 145 ARG A NE    1 
ATOM   1148 C  CZ    . ARG A 1 145 ? 39.64436  0.86805   -32.64187 1.000 32.20453 ? 145 ARG A CZ    1 
ATOM   1149 N  NH1   . ARG A 1 145 ? 39.28373  1.85638   -31.83963 0.327 29.02084 ? 145 ARG A NH1   1 
ATOM   1150 N  NH2   . ARG A 1 145 ? 40.36620  -0.13616  -32.15299 1.000 38.74593 ? 145 ARG A NH2   1 
ATOM   1151 N  N     . ASN A 1 146 ? 34.67352  -0.40633  -38.06429 1.000 17.31639 ? 146 ASN A N     1 
ATOM   1152 C  CA    . ASN A 1 146 ? 34.31851  -1.40434  -39.05928 1.000 16.07044 ? 146 ASN A CA    1 
ATOM   1153 C  C     . ASN A 1 146 ? 34.12949  -0.80134  -40.44828 1.000 14.17345 ? 146 ASN A C     1 
ATOM   1154 O  O     . ASN A 1 146 ? 33.53947  -1.44634  -41.32027 1.000 16.41525 ? 146 ASN A O     1 
ATOM   1155 C  CB    . ASN A 1 146 ? 33.05452  -2.15434  -38.62426 1.000 16.91028 ? 146 ASN A CB    1 
ATOM   1156 C  CG    . ASN A 1 146 ? 32.91851  -3.51334  -39.29326 1.000 19.77548 ? 146 ASN A CG    1 
ATOM   1157 O  OD1   . ASN A 1 146 ? 33.91251  -4.19134  -39.56427 1.000 18.30656 ? 146 ASN A OD1   1 
ATOM   1158 N  ND2   . ASN A 1 146 ? 31.68051  -3.91534  -39.57024 1.000 15.51422 ? 146 ASN A ND2   1 
ATOM   1159 N  N     . GLY A 1 147 ? 34.62148  0.41367   -40.67428 1.000 18.74497 ? 147 GLY A N     1 
ATOM   1160 C  CA    . GLY A 1 147 ? 34.50945  1.05267   -41.96828 1.000 18.56879 ? 147 GLY A CA    1 
ATOM   1161 C  C     . GLY A 1 147 ? 33.25745  1.87066   -42.18826 1.000 14.00869 ? 147 GLY A C     1 
ATOM   1162 O  O     . GLY A 1 147 ? 33.02743  2.32466   -43.31426 1.000 16.34076 ? 147 GLY A O     1 
ATOM   1163 N  N     . GLY A 1 148 ? 32.43846  2.06966   -41.16025 1.000 16.79912 ? 148 GLY A N     1 
ATOM   1164 C  CA    . GLY A 1 148 ? 31.25746  2.90265   -41.26323 1.000 18.50917 ? 148 GLY A CA    1 
ATOM   1165 C  C     . GLY A 1 148 ? 29.93346  2.16965   -41.31921 1.000 18.88051 ? 148 GLY A C     1 
ATOM   1166 O  O     . GLY A 1 148 ? 28.90545  2.80765   -41.57819 1.000 24.34792 ? 148 GLY A O     1 
ATOM   1167 N  N     . ALA A 1 149 ? 29.91847  0.85865   -41.09221 1.000 22.77227 ? 149 ALA A N     1 
ATOM   1168 C  CA    . ALA A 1 149 ? 28.69047  0.07665   -41.09319 1.000 22.03126 ? 149 ALA A CA    1 
ATOM   1169 C  C     . ALA A 1 149 ? 28.78649  -1.01235  -40.03519 1.000 22.86789 ? 149 ALA A C     1 
ATOM   1170 O  O     . ALA A 1 149 ? 29.84150  -1.62635  -39.86421 1.000 19.92997 ? 149 ALA A O     1 
ATOM   1171 C  CB    . ALA A 1 149 ? 28.42745  -0.54435  -42.47218 1.000 18.24480 ? 149 ALA A CB    1 
ATOM   1172 N  N     . ALA A 1 150 ? 27.68351  -1.24736  -39.33017 1.000 20.57955 ? 150 ALA A N     1 
ATOM   1173 C  CA    . ALA A 1 150 ? 27.68953  -2.24236  -38.26817 1.000 19.54058 ? 150 ALA A CA    1 
ATOM   1174 C  C     . ALA A 1 150 ? 27.79452  -3.64836  -38.85717 1.000 21.87856 ? 150 ALA A C     1 
ATOM   1175 O  O     . ALA A 1 150 ? 27.22451  -3.92436  -39.91916 1.000 19.67204 ? 150 ALA A O     1 
ATOM   1176 C  CB    . ALA A 1 150 ? 26.42654  -2.13136  -37.41115 1.000 14.69206 ? 150 ALA A CB    1 
ATOM   1177 N  N     . PRO A 1 151 ? 28.52654  -4.55136  -38.20419 1.000 20.89877 ? 151 PRO A N     1 
ATOM   1178 C  CA    . PRO A 1 151 ? 28.52853  -5.95136  -38.64719 1.000 21.48308 ? 151 PRO A CA    1 
ATOM   1179 C  C     . PRO A 1 151 ? 27.13554  -6.54336  -38.50616 1.000 18.90539 ? 151 PRO A C     1 
ATOM   1180 O  O     . PRO A 1 151 ? 26.39155  -6.20536  -37.58515 1.000 15.61727 ? 151 PRO A O     1 
ATOM   1181 C  CB    . PRO A 1 151 ? 29.52655  -6.62935  -37.70020 1.000 17.07777 ? 151 PRO A CB    1 
ATOM   1182 C  CG    . PRO A 1 151 ? 30.28556  -5.51735  -37.04321 1.000 15.16988 ? 151 PRO A CG    1 
ATOM   1183 C  CD    . PRO A 1 151 ? 29.35556  -4.34535  -37.00720 1.000 21.36107 ? 151 PRO A CD    1 
ATOM   1184 N  N     . LEU A 1 152 ? 26.77553  -7.42236  -39.43716 1.000 15.56178 ? 152 LEU A N     1 
ATOM   1185 C  CA    . LEU A 1 152 ? 25.46453  -8.05337  -39.41514 1.000 23.45707 ? 152 LEU A CA    1 
ATOM   1186 C  C     . LEU A 1 152 ? 25.50454  -9.50737  -38.95714 1.000 13.78801 ? 152 LEU A C     1 
ATOM   1187 O  O     . LEU A 1 152 ? 24.45254  -10.15037 -38.90312 1.000 17.03244 ? 152 LEU A O     1 
ATOM   1188 C  CB    . LEU A 1 152 ? 24.80650  -7.94337  -40.79812 1.000 21.17596 ? 152 LEU A CB    1 
ATOM   1189 C  CG    . LEU A 1 152 ? 24.49649  -6.50437  -41.22012 1.000 28.65035 ? 152 LEU A CG    1 
ATOM   1190 C  CD1   . LEU A 1 152 ? 23.80047  -6.45237  -42.57411 1.000 29.89465 ? 152 LEU A CD1   1 
ATOM   1191 C  CD2   . LEU A 1 152 ? 23.66051  -5.80137  -40.15910 1.000 27.67767 ? 152 LEU A CD2   1 
ATOM   1192 N  N     . THR A 1 153 ? 26.67655  -10.03736 -38.61516 1.000 16.24552 ? 153 THR A N     1 
ATOM   1193 C  CA    . THR A 1 153 ? 26.80756  -11.38636 -38.08316 1.000 19.44162 ? 153 THR A CA    1 
ATOM   1194 C  C     . THR A 1 153 ? 27.62758  -11.35936 -36.80117 1.000 16.16000 ? 153 THR A C     1 
ATOM   1195 O  O     . THR A 1 153 ? 28.50958  -10.51636 -36.62419 1.000 13.70183 ? 153 THR A O     1 
ATOM   1196 C  CB    . THR A 1 153 ? 27.46955  -12.35436 -39.08017 1.000 17.58171 ? 153 THR A CB    1 
ATOM   1197 O  OG1   . THR A 1 153 ? 28.84654  -11.99135 -39.27119 1.000 21.55649 ? 153 THR A OG1   1 
ATOM   1198 C  CG2   . THR A 1 153 ? 26.74153  -12.33836 -40.41816 1.000 12.79363 ? 153 THR A CG2   1 
ATOM   1199 N  N     . MET A 1 154 ? 27.32560  -12.30636 -35.90917 1.000 13.60268 ? 154 MET A N     1 
ATOM   1200 C  CA    . MET A 1 154 ? 28.03562  -12.38236 -34.63918 1.000 14.67525 ? 154 MET A CA    1 
ATOM   1201 C  C     . MET A 1 154 ? 29.51062  -12.70935 -34.83920 1.000 17.17634 ? 154 MET A C     1 
ATOM   1202 O  O     . MET A 1 154 ? 30.35863  -12.22135 -34.08422 1.000 18.91170 ? 154 MET A O     1 
ATOM   1203 C  CB    . MET A 1 154 ? 27.36564  -13.41736 -33.72917 1.000 16.17492 ? 154 MET A CB    1 
ATOM   1204 C  CG    . MET A 1 154 ? 28.14766  -13.74436 -32.46518 1.000 16.15767 ? 154 MET A CG    1 
ATOM   1205 S  SD    . MET A 1 154 ? 28.56167  -12.29536 -31.47319 1.000 21.59801 ? 154 MET A SD    1 
ATOM   1206 C  CE    . MET A 1 154 ? 26.94568  -11.79336 -30.92416 1.000 11.77670 ? 154 MET A CE    1 
ATOM   1207 N  N     . GLN A 1 155 ? 29.83761  -13.51635 -35.85121 1.000 14.26351 ? 155 GLN A N     1 
ATOM   1208 C  CA    . GLN A 1 155 ? 31.23260  -13.85935 -36.11223 1.000 17.60370 ? 155 GLN A CA    1 
ATOM   1209 C  C     . GLN A 1 155 ? 32.04959  -12.61934 -36.46325 1.000 17.47212 ? 155 GLN A C     1 
ATOM   1210 O  O     . GLN A 1 155 ? 33.09460  -12.36034 -35.85726 1.000 16.38840 ? 155 GLN A O     1 
ATOM   1211 C  CB    . GLN A 1 155 ? 31.31459  -14.90035 -37.23223 1.000 15.53974 ? 155 GLN A CB    1 
ATOM   1212 C  CG    . GLN A 1 155 ? 32.72358  -15.35534 -37.57026 1.000 18.95295 ? 155 GLN A CG    1 
ATOM   1213 C  CD    . GLN A 1 155 ? 33.24060  -16.42034 -36.62527 0.000 17.59582 ? 155 GLN A CD    1 
ATOM   1214 O  OE1   . GLN A 1 155 ? 34.39361  -16.38134 -36.19829 0.000 17.72105 ? 155 GLN A OE1   1 
ATOM   1215 N  NE2   . GLN A 1 155 ? 32.39061  -17.39034 -36.30325 0.000 17.79276 ? 155 GLN A NE2   1 
ATOM   1216 N  N     . SER A 1 156 ? 31.58757  -11.83735 -37.44424 1.000 17.26740 ? 156 SER A N     1 
ATOM   1217 C  CA    . SER A 1 156 ? 32.32056  -10.63434 -37.82525 1.000 18.15377 ? 156 SER A CA    1 
ATOM   1218 C  C     . SER A 1 156 ? 32.29558  -9.58734  -36.72225 1.000 13.33242 ? 156 SER A C     1 
ATOM   1219 O  O     . SER A 1 156 ? 33.23758  -8.79934  -36.60326 1.000 12.64109 ? 156 SER A O     1 
ATOM   1220 C  CB    . SER A 1 156 ? 31.76054  -10.05034 -39.12524 1.000 14.66843 ? 156 SER A CB    1 
ATOM   1221 O  OG    . SER A 1 156 ? 30.38154  -9.75335  -39.00922 1.000 21.15885 ? 156 SER A OG    1 
ATOM   1222 N  N     . PHE A 1 157 ? 31.23659  -9.55935  -35.90823 1.000 14.49575 ? 157 PHE A N     1 
ATOM   1223 C  CA    . PHE A 1 157 ? 31.20961  -8.64635  -34.76823 1.000 13.87546 ? 157 PHE A CA    1 
ATOM   1224 C  C     . PHE A 1 157 ? 32.23963  -9.04434  -33.71825 1.000 15.11760 ? 157 PHE A C     1 
ATOM   1225 O  O     . PHE A 1 157 ? 32.90363  -8.18234  -33.13226 1.000 14.71055 ? 157 PHE A O     1 
ATOM   1226 C  CB    . PHE A 1 157 ? 29.81362  -8.61435  -34.15221 1.000 14.53139 ? 157 PHE A CB    1 
ATOM   1227 C  CG    . PHE A 1 157 ? 29.67263  -7.64335  -33.01321 1.000 11.34668 ? 157 PHE A CG    1 
ATOM   1228 C  CD1   . PHE A 1 157 ? 29.40862  -6.30635  -33.25620 1.000 13.34606 ? 157 PHE A CD1   1 
ATOM   1229 C  CD2   . PHE A 1 157 ? 29.79166  -8.07035  -31.69721 1.000 13.94382 ? 157 PHE A CD2   1 
ATOM   1230 C  CE1   . PHE A 1 157 ? 29.26664  -5.41135  -32.21120 1.000 10.12379 ? 157 PHE A CE1   1 
ATOM   1231 C  CE2   . PHE A 1 157 ? 29.65567  -7.17735  -30.64620 1.000 9.84430  ? 157 PHE A CE2   1 
ATOM   1232 C  CZ    . PHE A 1 157 ? 29.39366  -5.84735  -30.90920 1.000 11.24205 ? 157 PHE A CZ    1 
ATOM   1233 N  N     . THR A 1 158 ? 32.37863  -10.34734 -33.46025 1.000 17.57553 ? 158 THR A N     1 
ATOM   1234 C  CA    . THR A 1 158 ? 33.32065  -10.80134 -32.44327 1.000 18.28279 ? 158 THR A CA    1 
ATOM   1235 C  C     . THR A 1 158 ? 34.76265  -10.53934 -32.86029 1.000 16.07994 ? 158 THR A C     1 
ATOM   1236 O  O     . THR A 1 158 ? 35.60866  -10.24533 -32.00930 1.000 21.93379 ? 158 THR A O     1 
ATOM   1237 C  CB    . THR A 1 158 ? 33.10166  -12.28734 -32.14926 1.000 19.62606 ? 158 THR A CB    1 
ATOM   1238 O  OG1   . THR A 1 158 ? 31.72467  -12.50635 -31.81224 1.000 14.81348 ? 158 THR A OG1   1 
ATOM   1239 C  CG2   . THR A 1 158 ? 33.97068  -12.73934 -30.98828 1.000 18.29170 ? 158 THR A CG2   1 
ATOM   1240 N  N     . LYS A 1 159 ? 35.06062  -10.62433 -34.15830 1.000 17.31624 ? 159 LYS A N     1 
ATOM   1241 C  CA    . LYS A 1 159 ? 36.39762  -10.27533 -34.62032 1.000 12.48674 ? 159 LYS A CA    1 
ATOM   1242 C  C     . LYS A 1 159 ? 36.65761  -8.78033  -34.48232 1.000 21.45287 ? 159 LYS A C     1 
ATOM   1243 O  O     . LYS A 1 159 ? 37.79262  -8.36833  -34.21234 1.000 25.38020 ? 159 LYS A O     1 
ATOM   1244 C  CB    . LYS A 1 159 ? 36.59059  -10.71533 -36.07332 1.000 16.17040 ? 159 LYS A CB    1 
ATOM   1245 C  CG    . LYS A 1 159 ? 36.17359  -12.15533 -36.36831 1.000 19.72139 ? 159 LYS A CG    1 
ATOM   1246 C  CD    . LYS A 1 159 ? 36.74061  -13.14633 -35.36232 0.000 19.34952 ? 159 LYS A CD    1 
ATOM   1247 C  CE    . LYS A 1 159 ? 35.62363  -13.84233 -34.59631 0.403 18.25683 ? 159 LYS A CE    1 
ATOM   1248 N  NZ    . LYS A 1 159 ? 36.10865  -14.99733 -33.79331 0.054 19.73694 ? 159 LYS A NZ    1 
ATOM   1249 N  N     . LEU A 1 160 ? 35.62061  -7.95633  -34.65630 1.000 19.37026 ? 160 LEU A N     1 
ATOM   1250 C  CA    . LEU A 1 160 ? 35.78660  -6.51433  -34.50931 1.000 19.16929 ? 160 LEU A CA    1 
ATOM   1251 C  C     . LEU A 1 160 ? 36.17463  -6.15133  -33.08131 1.000 18.74298 ? 160 LEU A C     1 
ATOM   1252 O  O     . LEU A 1 160 ? 37.14963  -5.42533  -32.85333 1.000 20.71768 ? 160 LEU A O     1 
ATOM   1253 C  CB    . LEU A 1 160 ? 34.49759  -5.79934  -34.91928 1.000 19.16704 ? 160 LEU A CB    1 
ATOM   1254 C  CG    . LEU A 1 160 ? 34.45459  -4.28234  -34.72428 1.000 17.91647 ? 160 LEU A CG    1 
ATOM   1255 C  CD1   . LEU A 1 160 ? 35.49658  -3.59733  -35.59530 1.000 14.01945 ? 160 LEU A CD1   1 
ATOM   1256 C  CD2   . LEU A 1 160 ? 33.05659  -3.74034  -35.01626 1.000 16.57144 ? 160 LEU A CD2   1 
ATOM   1257 N  N     . VAL A 1 161 ? 35.42464  -6.65533  -32.10030 1.000 20.42491 ? 161 VAL A N     1 
ATOM   1258 C  CA    . VAL A 1 161 ? 35.70667  -6.29933  -30.71331 1.000 19.09829 ? 161 VAL A CA    1 
ATOM   1259 C  C     . VAL A 1 161 ? 37.04768  -6.86933  -30.27133 1.000 18.70594 ? 161 VAL A C     1 
ATOM   1260 O  O     . VAL A 1 161 ? 37.72069  -6.29133  -29.41134 1.000 19.41261 ? 161 VAL A O     1 
ATOM   1261 C  CB    . VAL A 1 161 ? 34.55268  -6.75934  -29.80329 1.000 16.49438 ? 161 VAL A CB    1 
ATOM   1262 C  CG1   . VAL A 1 161 ? 33.24667  -6.12334  -30.25726 1.000 13.20162 ? 161 VAL A CG1   1 
ATOM   1263 C  CG2   . VAL A 1 161 ? 34.43369  -8.27134  -29.80428 1.000 18.81197 ? 161 VAL A CG2   1 
ATOM   1264 N  N     . ASP A 1 162 ? 37.46867  -7.99433  -30.85533 1.000 20.77743 ? 162 ASP A N     1 
ATOM   1265 C  CA    . ASP A 1 162 ? 38.79968  -8.52132  -30.57536 1.000 21.31096 ? 162 ASP A CA    1 
ATOM   1266 C  C     . ASP A 1 162 ? 39.88066  -7.58832  -31.10237 1.000 22.89573 ? 162 ASP A C     1 
ATOM   1267 O  O     . ASP A 1 162 ? 40.94767  -7.45732  -30.49139 1.000 21.45627 ? 162 ASP A O     1 
ATOM   1268 C  CB    . ASP A 1 162 ? 38.95367  -9.91232  -31.18736 1.000 20.89503 ? 162 ASP A CB    1 
ATOM   1269 C  CG    . ASP A 1 162 ? 38.14569  -10.96233 -30.45935 1.000 21.08143 ? 162 ASP A CG    1 
ATOM   1270 O  OD1   . ASP A 1 162 ? 37.60570  -10.65233 -29.38134 1.000 25.43998 ? 162 ASP A OD1   1 
ATOM   1271 O  OD2   . ASP A 1 162 ? 38.04768  -12.09933 -30.96735 1.000 26.11187 ? 162 ASP A OD2   1 
ATOM   1272 N  N     . ARG A 1 163 ? 39.63294  -6.94331  -32.24430 1.000 21.92421 ? 163 ARG A N     1 
ATOM   1273 C  CA    . ARG A 1 163 ? 40.58206  -5.96374  -32.75732 1.000 19.27221 ? 163 ARG A CA    1 
ATOM   1274 C  C     . ARG A 1 163 ? 40.53063  -4.66070  -31.97381 1.000 22.43569 ? 163 ARG A C     1 
ATOM   1275 O  O     . ARG A 1 163 ? 41.55251  -3.97647  -31.85007 1.000 21.84029 ? 163 ARG A O     1 
ATOM   1276 C  CB    . ARG A 1 163 ? 40.32152  -5.69415  -34.24051 1.000 21.87572 ? 163 ARG A CB    1 
ATOM   1277 C  CG    . ARG A 1 163 ? 40.98518  -6.69105  -35.17317 1.000 25.54832 ? 163 ARG A CG    1 
ATOM   1278 C  CD    . ARG A 1 163 ? 40.98125  -6.20629  -36.61503 1.000 21.18127 ? 163 ARG A CD    1 
ATOM   1279 N  NE    . ARG A 1 163 ? 39.71398  -6.46438  -37.28923 1.000 31.58825 ? 163 ARG A NE    1 
ATOM   1280 C  CZ    . ARG A 1 163 ? 38.74146  -5.57419  -37.42788 1.000 23.84018 ? 163 ARG A CZ    1 
ATOM   1281 N  NH1   . ARG A 1 163 ? 38.85107  -4.34900  -36.94169 1.000 25.88871 ? 163 ARG A NH1   1 
ATOM   1282 N  NH2   . ARG A 1 163 ? 37.63102  -5.92205  -38.07166 1.000 31.89233 ? 163 ARG A NH2   1 
ATOM   1283 N  N     . VAL A 1 164 ? 39.36165  -4.30532  -31.43837 1.000 20.95581 ? 164 VAL A N     1 
ATOM   1284 C  CA    . VAL A 1 164 ? 39.24566  -3.07432  -30.66136 1.000 23.43907 ? 164 VAL A CA    1 
ATOM   1285 C  C     . VAL A 1 164 ? 39.90768  -3.23632  -29.29837 1.000 22.32101 ? 164 VAL A C     1 
ATOM   1286 O  O     . VAL A 1 164 ? 40.58068  -2.32232  -28.80538 1.000 20.41708 ? 164 VAL A O     1 
ATOM   1287 C  CB    . VAL A 1 164 ? 37.76566  -2.66433  -30.53734 1.000 19.67233 ? 164 VAL A CB    1 
ATOM   1288 C  CG1   . VAL A 1 164 ? 37.59267  -1.58233  -29.48533 1.000 20.17871 ? 164 VAL A CG1   1 
ATOM   1289 C  CG2   . VAL A 1 164 ? 37.23263  -2.19533  -31.88533 1.000 16.83410 ? 164 VAL A CG2   1 
ATOM   1290 N  N     . GLY A 1 165 ? 39.74369  -4.39532  -28.68037 1.000 21.24861 ? 165 GLY A N     1 
ATOM   1291 C  CA    . GLY A 1 165 ? 40.32472  -4.67932  -27.38638 1.000 26.78959 ? 165 GLY A CA    1 
ATOM   1292 C  C     . GLY A 1 165 ? 39.26873  -4.74732  -26.29736 1.000 19.55475 ? 165 GLY A C     1 
ATOM   1293 O  O     . GLY A 1 165 ? 38.06273  -4.82733  -26.55134 1.000 18.66838 ? 165 GLY A O     1 
ATOM   1294 N  N     . ASP A 1 166 ? 39.75476  -4.71632  -25.06037 1.000 18.25539 ? 166 ASP A N     1 
ATOM   1295 C  CA    . ASP A 1 166 ? 38.88177  -4.76832  -23.90336 1.000 13.93743 ? 166 ASP A CA    1 
ATOM   1296 C  C     . ASP A 1 166 ? 37.99277  -3.53033  -23.85734 1.000 16.90176 ? 166 ASP A C     1 
ATOM   1297 O  O     . ASP A 1 166 ? 38.37176  -2.46833  -24.35835 1.000 12.51856 ? 166 ASP A O     1 
ATOM   1298 C  CB    . ASP A 1 166 ? 39.70680  -4.85432  -22.62237 1.000 16.98051 ? 166 ASP A CB    1 
ATOM   1299 C  CG    . ASP A 1 166 ? 40.48280  -6.14432  -22.51838 1.000 17.77103 ? 166 ASP A CG    1 
ATOM   1300 O  OD1   . ASP A 1 166 ? 39.95580  -7.18532  -22.95938 1.000 21.25588 ? 166 ASP A OD1   1 
ATOM   1301 O  OD2   . ASP A 1 166 ? 41.61981  -6.12632  -22.00040 1.000 20.63468 ? 166 ASP A OD2   1 
ATOM   1302 N  N     . PRO A 1 167 ? 36.80078  -3.64333  -23.27332 1.000 15.33408 ? 167 PRO A N     1 
ATOM   1303 C  CA    . PRO A 1 167 ? 35.99678  -2.45433  -22.98631 1.000 12.03615 ? 167 PRO A CA    1 
ATOM   1304 C  C     . PRO A 1 167 ? 36.63980  -1.63733  -21.88432 1.000 11.99689 ? 167 PRO A C     1 
ATOM   1305 O  O     . PRO A 1 167 ? 37.53581  -2.13133  -21.18133 1.000 11.70670 ? 167 PRO A O     1 
ATOM   1306 C  CB    . PRO A 1 167 ? 34.64679  -3.03834  -22.53429 1.000 13.50913 ? 167 PRO A CB    1 
ATOM   1307 C  CG    . PRO A 1 167 ? 34.97780  -4.40934  -22.04429 1.000 9.84297  ? 167 PRO A CG    1 
ATOM   1308 C  CD    . PRO A 1 167 ? 36.09279  -4.88633  -22.92431 1.000 10.96198 ? 167 PRO A CD    1 
ATOM   1309 N  N     . PRO A 1 168 ? 36.22380  -0.38433  -21.70731 1.000 11.95193 ? 168 PRO A N     1 
ATOM   1310 C  CA    . PRO A 1 168 ? 36.80381  0.42867   -20.63532 1.000 13.47538 ? 168 PRO A CA    1 
ATOM   1311 C  C     . PRO A 1 168 ? 36.54384  -0.19033  -19.27132 1.000 12.87477 ? 168 PRO A C     1 
ATOM   1312 O  O     . PRO A 1 168 ? 35.53684  -0.86434  -19.05230 1.000 12.71285 ? 168 PRO A O     1 
ATOM   1313 C  CB    . PRO A 1 168 ? 36.09180  1.77866   -20.79031 1.000 12.78183 ? 168 PRO A CB    1 
ATOM   1314 C  CG    . PRO A 1 168 ? 35.68778  1.82066   -22.22030 1.000 9.27375  ? 168 PRO A CG    1 
ATOM   1315 C  CD    . PRO A 1 168 ? 35.31978  0.40666   -22.56130 1.000 14.72837 ? 168 PRO A CD    1 
ATOM   1316 N  N     . ALA A 1 169 ? 37.48685  0.02267   -18.35833 1.000 19.05645 ? 169 ALA A N     1 
ATOM   1317 C  CA    . ALA A 1 169 ? 37.34487  -0.49133  -17.00633 1.000 14.93769 ? 169 ALA A CA    1 
ATOM   1318 C  C     . ALA A 1 169 ? 36.18788  0.20966   -16.29731 1.000 13.90899 ? 169 ALA A C     1 
ATOM   1319 O  O     . ALA A 1 169 ? 35.87088  1.36066   -16.60331 1.000 14.28489 ? 169 ALA A O     1 
ATOM   1320 C  CB    . ALA A 1 169 ? 38.63689  -0.29433  -16.21835 1.000 15.62123 ? 169 ALA A CB    1 
ATOM   1321 N  N     . PRO A 1 170 ? 35.52890  -0.46834  -15.35730 1.000 15.23316 ? 170 PRO A N     1 
ATOM   1322 C  CA    . PRO A 1 170 ? 34.43291  0.17466   -14.62528 1.000 13.10265 ? 170 PRO A CA    1 
ATOM   1323 C  C     . PRO A 1 170 ? 34.92792  1.37566   -13.83329 1.000 13.82080 ? 170 PRO A C     1 
ATOM   1324 O  O     . PRO A 1 170 ? 36.03693  1.37666   -13.29831 1.000 13.28981 ? 170 PRO A O     1 
ATOM   1325 C  CB    . PRO A 1 170 ? 33.91493  -0.93734  -13.70627 1.000 11.24753 ? 170 PRO A CB    1 
ATOM   1326 C  CG    . PRO A 1 170 ? 35.04294  -1.93534  -13.63329 1.000 11.10219 ? 170 PRO A CG    1 
ATOM   1327 C  CD    . PRO A 1 170 ? 35.69991  -1.87834  -14.96830 1.000 13.52722 ? 170 PRO A CD    1 
ATOM   1328 N  N     . ALA A 1 171 ? 34.09392  2.41266   -13.78328 1.000 12.08072 ? 171 ALA A N     1 
ATOM   1329 C  CA    . ALA A 1 171 ? 34.46093  3.63766   -13.10028 1.000 10.07938 ? 171 ALA A CA    1 
ATOM   1330 C  C     . ALA A 1 171 ? 34.53895  3.40266   -11.59128 1.000 13.74491 ? 171 ALA A C     1 
ATOM   1331 O  O     . ALA A 1 171 ? 33.83496  2.54465   -11.05327 1.000 16.07885 ? 171 ALA A O     1 
ATOM   1332 C  CB    . ALA A 1 171 ? 33.44792  4.73765   -13.40326 1.000 11.35462 ? 171 ALA A CB    1 
ATOM   1333 N  N     . PRO A 1 172 ? 35.38696  4.15166   -10.88430 1.000 10.17228 ? 172 PRO A N     1 
ATOM   1334 C  CA    . PRO A 1 172 ? 35.48599  3.97666   -9.43130  1.000 10.68538 ? 172 PRO A CA    1 
ATOM   1335 C  C     . PRO A 1 172 ? 34.17800  4.32565   -8.73728  1.000 12.88329 ? 172 PRO A C     1 
ATOM   1336 O  O     . PRO A 1 172 ? 33.26298  4.91665   -9.31326  1.000 11.49710 ? 172 PRO A O     1 
ATOM   1337 C  CB    . PRO A 1 172 ? 36.61099  4.93466   -9.02732  1.000 14.96606 ? 172 PRO A CB    1 
ATOM   1338 C  CG    . PRO A 1 172 ? 36.66697  5.94066   -10.13732 1.000 19.04720 ? 172 PRO A CG    1 
ATOM   1339 C  CD    . PRO A 1 172 ? 36.30895  5.18666   -11.38231 1.000 9.00317  ? 172 PRO A CD    1 
ATOM   1340 N  N     . ASP A 1 173 ? 34.09702  3.94165   -7.46828  1.000 16.25632 ? 173 ASP A N     1 
ATOM   1341 C  CA    . ASP A 1 173 ? 32.89203  4.18465   -6.69425  1.000 19.23693 ? 173 ASP A CA    1 
ATOM   1342 C  C     . ASP A 1 173 ? 32.79903  5.66065   -6.30525  1.000 16.40855 ? 173 ASP A C     1 
ATOM   1343 O  O     . ASP A 1 173 ? 33.81903  6.33665   -6.15227  1.000 19.79875 ? 173 ASP A O     1 
ATOM   1344 C  CB    . ASP A 1 173 ? 32.87805  3.30365   -5.44625  1.000 20.98737 ? 173 ASP A CB    1 
ATOM   1345 C  CG    . ASP A 1 173 ? 32.83205  1.82165   -5.78325  1.000 23.34596 ? 173 ASP A CG    1 
ATOM   1346 O  OD1   . ASP A 1 173 ? 33.85405  1.28965   -6.25427  1.000 34.80573 ? 173 ASP A OD1   1 
ATOM   1347 O  OD2   . ASP A 1 173 ? 31.77406  1.18965   -5.58924  1.000 24.04867 ? 173 ASP A OD2   1 
ATOM   1348 N  N     . PRO A 1 174 ? 31.58803  6.19064   -6.16723  1.000 17.34242 ? 174 PRO A N     1 
ATOM   1349 C  CA    . PRO A 1 174 ? 31.43103  7.59364   -5.77923  1.000 18.96770 ? 174 PRO A CA    1 
ATOM   1350 C  C     . PRO A 1 174 ? 31.93106  7.81765   -4.36424  1.000 10.63948 ? 174 PRO A C     1 
ATOM   1351 O  O     . PRO A 1 174 ? 32.10407  6.85465   -3.60224  1.000 14.07800 ? 174 PRO A O     1 
ATOM   1352 C  CB    . PRO A 1 174 ? 29.91403  7.81964   -5.88420  1.000 17.89738 ? 174 PRO A CB    1 
ATOM   1353 C  CG    . PRO A 1 174 ? 29.32904  6.47364   -5.72019  1.000 18.39689 ? 174 PRO A CG    1 
ATOM   1354 C  CD    . PRO A 1 174 ? 30.29103  5.53664   -6.38421  1.000 14.94517 ? 174 PRO A CD    1 
ATOM   1355 N  N     . PRO A 1 175 ? 32.18206  9.06565   -3.97424  1.000 15.19510 ? 175 PRO A N     1 
ATOM   1356 C  CA    . PRO A 1 175 ? 32.73008  9.31965   -2.63625  1.000 17.93661 ? 175 PRO A CA    1 
ATOM   1357 C  C     . PRO A 1 175 ? 31.75010  8.91764   -1.54223  1.000 16.80352 ? 175 PRO A C     1 
ATOM   1358 O  O     . PRO A 1 175 ? 30.55410  8.72664   -1.77621  1.000 14.35340 ? 175 PRO A O     1 
ATOM   1359 C  CB    . PRO A 1 175 ? 32.97807  10.83365  -2.63825  1.000 22.11974 ? 175 PRO A CB    1 
ATOM   1360 C  CG    . PRO A 1 175 ? 32.02106  11.37065  -3.66224  1.000 16.56782 ? 175 PRO A CG    1 
ATOM   1361 C  CD    . PRO A 1 175 ? 31.94604  10.31365  -4.72424  1.000 18.06751 ? 175 PRO A CD    1 
ATOM   1362 N  N     . ALA A 1 176 ? 32.28312  8.77865   -0.32324  1.000 9.76294  ? 176 ALA A N     1 
ATOM   1363 C  CA    . ALA A 1 176 ? 31.45414  8.35964   0.80377   1.000 12.09428 ? 176 ALA A CA    1 
ATOM   1364 C  C     . ALA A 1 176 ? 30.44914  9.42664   1.21679   1.000 18.06674 ? 176 ALA A C     1 
ATOM   1365 O  O     . ALA A 1 176 ? 29.44116  9.09863   1.85380   1.000 20.40373 ? 176 ALA A O     1 
ATOM   1366 C  CB    . ALA A 1 176 ? 32.33116  7.99064   1.99976   1.000 11.28988 ? 176 ALA A CB    1 
ATOM   1367 N  N     . ALA A 1 177 ? 30.70213  10.68764  0.87278   1.000 12.82794 ? 177 ALA A N     1 
ATOM   1368 C  CA    . ALA A 1 177 ? 29.79913  11.79164  1.16980   1.000 17.71823 ? 177 ALA A CA    1 
ATOM   1369 C  C     . ALA A 1 177 ? 29.58511  12.59964  -0.10020  1.000 11.03632 ? 177 ALA A C     1 
ATOM   1370 O  O     . ALA A 1 177 ? 30.54710  12.91364  -0.80921  1.000 17.97530 ? 177 ALA A O     1 
ATOM   1371 C  CB    . ALA A 1 177 ? 30.35515  12.68364  2.28579   1.000 14.21523 ? 177 ALA A CB    1 
ATOM   1372 N  N     . MET A 1 178 ? 28.32911  12.92863  -0.38218  1.000 13.95201 ? 178 MET A N     1 
ATOM   1373 C  CA    . MET A 1 178 ? 27.94008  13.62363  -1.59417  1.000 15.20215 ? 178 MET A CA    1 
ATOM   1374 C  C     . MET A 1 178 ? 27.46208  15.03163  -1.27316  1.000 16.06367 ? 178 MET A C     1 
ATOM   1375 O  O     . MET A 1 178 ? 26.94110  15.28163  -0.18415  1.000 17.80523 ? 178 MET A O     1 
ATOM   1376 C  CB    . MET A 1 178 ? 26.82007  12.87663  -2.32915  1.000 15.97220 ? 178 MET A CB    1 
ATOM   1377 C  CG    . MET A 1 178 ? 27.12207  11.41363  -2.61116  1.000 22.57052 ? 178 MET A CG    1 
ATOM   1378 S  SD    . MET A 1 178 ? 26.84805  10.96963  -4.33315  1.000 33.12847 ? 178 MET A SD    1 
ATOM   1379 C  CE    . MET A 1 178 ? 25.48104  12.04462  -4.74613  1.000 27.05636 ? 178 MET A CE    1 
ATOM   1380 N  N     . PRO A 1 179 ? 27.64706  15.97863  -2.18716  1.000 13.06478 ? 179 PRO A N     1 
ATOM   1381 C  CA    . PRO A 1 179 ? 27.05406  17.30063  -2.01015  1.000 11.49140 ? 179 PRO A CA    1 
ATOM   1382 C  C     . PRO A 1 179 ? 25.54106  17.20462  -2.04613  1.000 19.65281 ? 179 PRO A C     1 
ATOM   1383 O  O     . PRO A 1 179 ? 24.96105  16.74462  -3.04112  1.000 17.71679 ? 179 PRO A O     1 
ATOM   1384 C  CB    . PRO A 1 179 ? 27.59604  18.09763  -3.20616  1.000 17.18671 ? 179 PRO A CB    1 
ATOM   1385 C  CG    . PRO A 1 179 ? 28.85304  17.38863  -3.58518  1.000 16.75451 ? 179 PRO A CG    1 
ATOM   1386 C  CD    . PRO A 1 179 ? 28.56705  15.93763  -3.33518  1.000 14.43673 ? 179 PRO A CD    1 
ATOM   1387 N  N     . PRO A 1 180 ? 24.86708  17.60762  -0.97412  1.000 13.15483 ? 180 PRO A N     1 
ATOM   1388 C  CA    . PRO A 1 180 ? 23.41808  17.43662  -0.90209  1.000 19.16531 ? 180 PRO A CA    1 
ATOM   1389 C  C     . PRO A 1 180 ? 22.70506  18.50661  -1.70708  1.000 17.77803 ? 180 PRO A C     1 
ATOM   1390 O  O     . PRO A 1 180 ? 23.30305  19.53562  -2.05409  1.000 17.39027 ? 180 PRO A O     1 
ATOM   1391 C  CB    . PRO A 1 180 ? 23.13011  17.58061  0.59791   1.000 15.41362 ? 180 PRO A CB    1 
ATOM   1392 C  CG    . PRO A 1 180 ? 24.17111  18.53962  1.05989   1.000 16.51217 ? 180 PRO A CG    1 
ATOM   1393 C  CD    . PRO A 1 180 ? 25.40610  18.25462  0.23387   1.000 19.70829 ? 180 PRO A CD    1 
ATOM   1394 N  N     . PRO A 1 181 ? 21.43206  18.29661  -2.04106  1.000 15.57469 ? 181 PRO A N     1 
ATOM   1395 C  CA    . PRO A 1 181 ? 20.65105  19.37261  -2.65405  1.000 14.21645 ? 181 PRO A CA    1 
ATOM   1396 C  C     . PRO A 1 181 ? 20.51206  20.54361  -1.69604  1.000 15.23719 ? 181 PRO A C     1 
ATOM   1397 O  O     . PRO A 1 181 ? 20.61708  20.39761  -0.47505  1.000 17.05682 ? 181 PRO A O     1 
ATOM   1398 C  CB    . PRO A 1 181 ? 19.29104  18.71660  -2.93102  1.000 18.40229 ? 181 PRO A CB    1 
ATOM   1399 C  CG    . PRO A 1 181 ? 19.54805  17.25260  -2.89703  1.000 17.14705 ? 181 PRO A CG    1 
ATOM   1400 C  CD    . PRO A 1 181 ? 20.65507  17.05661  -1.90705  1.000 9.95153  ? 181 PRO A CD    1 
ATOM   1401 N  N     . ALA A 1 182 ? 20.28604  21.72361  -2.26504  1.000 18.32383 ? 182 ALA A N     1 
ATOM   1402 C  CA    . ALA A 1 182 ? 20.12805  22.90960  -1.43704  1.000 16.98566 ? 182 ALA A CA    1 
ATOM   1403 C  C     . ALA A 1 182 ? 18.83107  22.82460  -0.64402  1.000 16.59659 ? 182 ALA A C     1 
ATOM   1404 O  O     . ALA A 1 182 ? 17.85106  22.21360  -1.07400  1.000 16.24906 ? 182 ALA A O     1 
ATOM   1405 C  CB    . ALA A 1 182 ? 20.14304  24.17660  -2.28904  1.000 16.55776 ? 182 ALA A CB    1 
ATOM   1406 N  N     . GLU A 1 183 ? 18.83508  23.44360  0.52898   1.000 16.47208 ? 183 GLU A N     1 
ATOM   1407 C  CA    . GLU A 1 183 ? 17.68210  23.38659  1.40600   1.000 25.47726 ? 183 GLU A CA    1 
ATOM   1408 C  C     . GLU A 1 183 ? 16.63009  24.40559  0.99002   1.000 21.90303 ? 183 GLU A C     1 
ATOM   1409 O  O     . GLU A 1 183 ? 16.94108  25.48359  0.47502   1.000 27.46791 ? 183 GLU A O     1 
ATOM   1410 C  CB    . GLU A 1 183 ? 18.10012  23.61760  2.85900   1.000 28.47219 ? 183 GLU A CB    1 
ATOM   1411 C  CG    . GLU A 1 183 ? 19.06814  22.56260  3.39498   1.000 24.79872 ? 183 GLU A CG    1 
ATOM   1412 C  CD    . GLU A 1 183 ? 19.39916  22.75260  4.86298   0.000 25.26022 ? 183 GLU A CD    1 
ATOM   1413 O  OE1   . GLU A 1 183 ? 19.14416  23.85260  5.39598   0.000 25.28064 ? 183 GLU A OE1   1 
ATOM   1414 O  OE2   . GLU A 1 183 ? 19.91317  21.79960  5.48397   0.000 25.49060 ? 183 GLU A OE2   1 
ATOM   1415 N  N     . ASP A 1 184 ? 15.36809  24.02959  1.19004   1.000 25.38966 ? 184 ASP A N     1 
ATOM   1416 C  CA    . ASP A 1 184 ? 14.20509  24.89758  0.98906   1.000 30.33077 ? 184 ASP A CA    1 
ATOM   1417 C  C     . ASP A 1 184 ? 14.01506  25.30758  -0.47393  1.000 19.38800 ? 184 ASP A C     1 
ATOM   1418 O  O     . ASP A 1 184 ? 13.38505  26.32458  -0.76292  1.000 18.47256 ? 184 ASP A O     1 
ATOM   1419 C  CB    . ASP A 1 184 ? 14.28410  26.12958  1.89706   1.000 28.29359 ? 184 ASP A CB    1 
ATOM   1420 C  CG    . ASP A 1 184 ? 14.34212  25.75758  3.37006   1.000 34.33351 ? 184 ASP A CG    1 
ATOM   1421 O  OD1   . ASP A 1 184 ? 13.70313  24.75158  3.74807   1.000 30.47081 ? 184 ASP A OD1   1 
ATOM   1422 O  OD2   . ASP A 1 184 ? 15.03113  26.45959  4.14605   1.000 35.33417 ? 184 ASP A OD2   1 
ATOM   1423 N  N     . MET A 1 185 ? 14.53205  24.52059  -1.40694  1.000 21.61692 ? 185 MET A N     1 
ATOM   1424 C  CA    . MET A 1 185 ? 14.18402  24.71058  -2.81094  1.000 21.24387 ? 185 MET A CA    1 
ATOM   1425 C  C     . MET A 1 185 ? 12.79102  24.14158  -3.06691  1.000 19.63440 ? 185 MET A C     1 
ATOM   1426 O  O     . MET A 1 185 ? 12.54303  22.97158  -2.75891  1.000 17.20589 ? 185 MET A O     1 
ATOM   1427 C  CB    . MET A 1 185 ? 15.21201  24.03659  -3.71595  1.000 20.48258 ? 185 MET A CB    1 
ATOM   1428 C  CG    . MET A 1 185 ? 16.59501  24.67159  -3.65898  1.000 16.81513 ? 185 MET A CG    1 
ATOM   1429 S  SD    . MET A 1 185 ? 16.59199  26.32759  -4.36198  1.000 23.70894 ? 185 MET A SD    1 
ATOM   1430 C  CE    . MET A 1 185 ? 18.32299  26.76460  -4.23101  1.000 19.25004 ? 185 MET A CE    1 
ATOM   1431 N  N     . PRO A 1 186 ? 11.86301  24.93158  -3.62190  1.000 19.06974 ? 186 PRO A N     1 
ATOM   1432 C  CA    . PRO A 1 186 ? 10.46501  24.46657  -3.70988  1.000 16.56903 ? 186 PRO A CA    1 
ATOM   1433 C  C     . PRO A 1 186 ? 10.27900  23.20857  -4.53587  1.000 12.20185 ? 186 PRO A C     1 
ATOM   1434 O  O     . PRO A 1 186 ? 9.49201   22.33857  -4.14586  1.000 18.36253 ? 186 PRO A O     1 
ATOM   1435 C  CB    . PRO A 1 186 ? 9.74100   25.66657  -4.33786  1.000 15.98676 ? 186 PRO A CB    1 
ATOM   1436 C  CG    . PRO A 1 186 ? 10.81698  26.44057  -5.03988  1.000 18.49895 ? 186 PRO A CG    1 
ATOM   1437 C  CD    . PRO A 1 186 ? 12.03700  26.27858  -4.18690  1.000 17.84589 ? 186 PRO A CD    1 
ATOM   1438 N  N     . SER A 1 187 ? 10.96898  23.08257  -5.67288  1.000 13.42373 ? 187 SER A N     1 
ATOM   1439 C  CA    . SER A 1 187 ? 10.81097  21.89557  -6.50688  1.000 18.34874 ? 187 SER A CA    1 
ATOM   1440 C  C     . SER A 1 187 ? 11.47299  20.66258  -5.91389  1.000 15.44843 ? 187 SER A C     1 
ATOM   1441 O  O     . SER A 1 187 ? 11.32198  19.57058  -6.47289  1.000 16.18212 ? 187 SER A O     1 
ATOM   1442 C  CB    . SER A 1 187 ? 11.36495  22.15358  -7.90689  1.000 14.82650 ? 187 SER A CB    1 
ATOM   1443 O  OG    . SER A 1 187 ? 10.69194  23.24557  -8.49288  1.000 14.84497 ? 187 SER A OG    1 
ATOM   1444 N  N     . ALA A 1 188 ? 12.20500  20.81258  -4.81491  1.000 19.39867 ? 188 ALA A N     1 
ATOM   1445 C  CA    . ALA A 1 188 ? 12.82502  19.70058  -4.11192  1.000 15.41072 ? 188 ALA A CA    1 
ATOM   1446 C  C     . ALA A 1 188 ? 12.06404  19.32058  -2.84890  1.000 16.94696 ? 188 ALA A C     1 
ATOM   1447 O  O     . ALA A 1 188 ? 12.60606  18.59458  -2.00891  1.000 13.76230 ? 188 ALA A O     1 
ATOM   1448 C  CB    . ALA A 1 188 ? 14.28002  20.04259  -3.77194  1.000 14.79344 ? 188 ALA A CB    1 
ATOM   1449 N  N     . ALA A 1 189 ? 10.82604  19.78957  -2.70388  1.000 14.17870 ? 189 ALA A N     1 
ATOM   1450 C  CA    . ALA A 1 189 ? 10.05206  19.50057  -1.50787  1.000 15.66353 ? 189 ALA A CA    1 
ATOM   1451 C  C     . ALA A 1 189 ? 9.88707   17.99457  -1.35387  1.000 15.32468 ? 189 ALA A C     1 
ATOM   1452 O  O     . ALA A 1 189 ? 9.52506   17.31457  -2.32386  1.000 19.52799 ? 189 ALA A O     1 
ATOM   1453 C  CB    . ALA A 1 189 ? 8.68506   20.17457  -1.57185  1.000 14.89077 ? 189 ALA A CB    1 
ATOM   1454 N  N     . PRO A 1 190 ? 10.16409  17.43457  -0.17287  1.000 20.47953 ? 190 PRO A N     1 
ATOM   1455 C  CA    . PRO A 1 190 ? 10.11510  15.96757  -0.02487  1.000 16.40341 ? 190 PRO A CA    1 
ATOM   1456 C  C     . PRO A 1 190 ? 8.77510   15.35257  -0.39785  1.000 18.19311 ? 190 PRO A C     1 
ATOM   1457 O  O     . PRO A 1 190 ? 8.74909   14.23957  -0.93685  1.000 12.46453 ? 190 PRO A O     1 
ATOM   1458 C  CB    . PRO A 1 190 ? 10.43713  15.76257  1.46112   1.000 16.53163 ? 190 PRO A CB    1 
ATOM   1459 C  CG    . PRO A 1 190 ? 11.25913  16.97157  1.83411   1.000 10.07407 ? 190 PRO A CG    1 
ATOM   1460 C  CD    . PRO A 1 190 ? 10.67811  18.10357  1.03712   1.000 15.55524 ? 190 PRO A CD    1 
ATOM   1461 N  N     . ALA A 1 191 ? 7.66410   16.05156  -0.14183  1.000 16.01804 ? 191 ALA A N     1 
ATOM   1462 C  CA    . ALA A 1 191 ? 6.34210   15.51056  -0.43181  1.000 12.73584 ? 191 ALA A CA    1 
ATOM   1463 C  C     . ALA A 1 191 ? 6.06107   15.41456  -1.92281  1.000 15.98689 ? 191 ALA A C     1 
ATOM   1464 O  O     . ALA A 1 191 ? 5.20507   14.62255  -2.32879  1.000 16.20931 ? 191 ALA A O     1 
ATOM   1465 C  CB    . ALA A 1 191 ? 5.26610   16.36455  0.24121   1.000 19.01630 ? 191 ALA A CB    1 
ATOM   1466 N  N     . ALA A 1 192 ? 6.74905   16.19356  -2.74782  1.000 11.40570 ? 192 ALA A N     1 
ATOM   1467 C  CA    . ALA A 1 192 ? 6.54303   16.14956  -4.18681  1.000 15.30063 ? 192 ALA A CA    1 
ATOM   1468 C  C     . ALA A 1 192 ? 7.64102   15.39956  -4.92683  1.000 12.38631 ? 192 ALA A C     1 
ATOM   1469 O  O     . ALA A 1 192 ? 7.56200   15.26656  -6.14883  1.000 14.89679 ? 192 ALA A O     1 
ATOM   1470 C  CB    . ALA A 1 192 ? 6.42202   17.57056  -4.75181  1.000 17.48419 ? 192 ALA A CB    1 
ATOM   1471 N  N     . THR A 1 193 ? 8.66503   14.91357  -4.22685  1.000 13.15053 ? 193 THR A N     1 
ATOM   1472 C  CA    . THR A 1 193 ? 9.79003   14.25157  -4.87587  1.000 15.28220 ? 193 THR A CA    1 
ATOM   1473 C  C     . THR A 1 193 ? 10.03004  12.83257  -4.37187  1.000 16.03353 ? 193 THR A C     1 
ATOM   1474 O  O     . THR A 1 193 ? 11.06004  12.23757  -4.71289  1.000 11.26348 ? 193 THR A O     1 
ATOM   1475 C  CB    . THR A 1 193 ? 11.06703  15.07857  -4.70789  1.000 9.79725  ? 193 THR A CB    1 
ATOM   1476 O  OG1   . THR A 1 193 ? 11.29405  15.33457  -3.31589  1.000 12.51211 ? 193 THR A OG1   1 
ATOM   1477 C  CG2   . THR A 1 193 ? 10.94101  16.39957  -5.44689  1.000 16.53639 ? 193 THR A CG2   1 
ATOM   1478 N  N     . GLY A 1 194 ? 9.11305   12.26557  -3.59186  1.000 11.03707 ? 194 GLY A N     1 
ATOM   1479 C  CA    . GLY A 1 194 ? 9.31207   10.93157  -3.06686  1.000 9.56751  ? 194 GLY A CA    1 
ATOM   1480 C  C     . GLY A 1 194 ? 9.14705   9.85557   -4.12586  1.000 15.11407 ? 194 GLY A C     1 
ATOM   1481 O  O     . GLY A 1 194 ? 8.66703   10.08957  -5.23285  1.000 10.03315 ? 194 GLY A O     1 
ATOM   1482 N  N     . VAL A 1 195 ? 9.56606   8.64357   -3.76687  1.000 14.74686 ? 195 VAL A N     1 
ATOM   1483 C  CA    . VAL A 1 195 ? 9.38905   7.47557   -4.62786  1.000 14.66287 ? 195 VAL A CA    1 
ATOM   1484 C  C     . VAL A 1 195 ? 7.98306   6.92056   -4.42584  1.000 10.46290 ? 195 VAL A C     1 
ATOM   1485 O  O     . VAL A 1 195 ? 7.64808   6.49256   -3.31483  1.000 14.22333 ? 195 VAL A O     1 
ATOM   1486 C  CB    . VAL A 1 195 ? 10.44806  6.39757   -4.34288  1.000 13.86049 ? 195 VAL A CB    1 
ATOM   1487 C  CG1   . VAL A 1 195 ? 10.16105  5.15657   -5.16388  1.000 14.48964 ? 195 VAL A CG1   1 
ATOM   1488 C  CG2   . VAL A 1 195 ? 11.84706  6.91758   -4.63590  1.000 12.66564 ? 195 VAL A CG2   1 
ATOM   1489 N  N     . PRO A 1 196 ? 7.13304   6.90856   -5.44983  1.000 14.89993 ? 196 PRO A N     1 
ATOM   1490 C  CA    . PRO A 1 196 ? 5.77305   6.39256   -5.26980  1.000 15.16824 ? 196 PRO A CA    1 
ATOM   1491 C  C     . PRO A 1 196 ? 5.75105   4.87456   -5.18080  1.000 15.78912 ? 196 PRO A C     1 
ATOM   1492 O  O     . PRO A 1 196 ? 6.67205   4.17956   -5.61582  1.000 16.38138 ? 196 PRO A O     1 
ATOM   1493 C  CB    . PRO A 1 196 ? 5.04502   6.88055   -6.52479  1.000 15.18696 ? 196 PRO A CB    1 
ATOM   1494 C  CG    . PRO A 1 196 ? 6.10901   6.95456   -7.54681  1.000 9.43735  ? 196 PRO A CG    1 
ATOM   1495 C  CD    . PRO A 1 196 ? 7.33902   7.43156   -6.81183  1.000 16.38342 ? 196 PRO A CD    1 
ATOM   1496 N  N     . THR A 1 197 ? 4.67406   4.36555   -4.59179  1.000 15.52192 ? 197 THR A N     1 
ATOM   1497 C  CA    . THR A 1 197 ? 4.40607   2.93655   -4.55978  1.000 20.18554 ? 197 THR A CA    1 
ATOM   1498 C  C     . THR A 1 197 ? 3.61405   2.52755   -5.80177  1.000 20.72562 ? 197 THR A C     1 
ATOM   1499 O  O     . THR A 1 197 ? 3.14903   3.36455   -6.57976  1.000 16.96165 ? 197 THR A O     1 
ATOM   1500 C  CB    . THR A 1 197 ? 3.64209   2.55655   -3.28977  1.000 23.39908 ? 197 THR A CB    1 
ATOM   1501 O  OG1   . THR A 1 197 ? 2.42709   3.31154   -3.21575  1.000 24.16944 ? 197 THR A OG1   1 
ATOM   1502 C  CG2   . THR A 1 197 ? 4.48111   2.84055   -2.04878  1.000 22.57594 ? 197 THR A CG2   1 
ATOM   1503 N  N     . TRP A 1 198 ? 3.45905   1.21455   -5.98577  1.000 24.08772 ? 198 TRP A N     1 
ATOM   1504 C  CA    . TRP A 1 198 ? 2.74603   0.74255   -7.16775  1.000 24.67320 ? 198 TRP A CA    1 
ATOM   1505 C  C     . TRP A 1 198 ? 1.24903   1.02054   -7.07173  1.000 23.34032 ? 198 TRP A C     1 
ATOM   1506 O  O     . TRP A 1 198 ? 0.58902   1.18354   -8.10272  1.000 22.52985 ? 198 TRP A O     1 
ATOM   1507 C  CB    . TRP A 1 198 ? 3.01504   -0.74745  -7.39376  1.000 24.49910 ? 198 TRP A CB    1 
ATOM   1508 C  CG    . TRP A 1 198 ? 2.49606   -1.64845  -6.31975  1.000 27.23329 ? 198 TRP A CG    1 
ATOM   1509 C  CD1   . TRP A 1 198 ? 3.19608   -2.15145  -5.26076  1.000 23.42820 ? 198 TRP A CD1   1 
ATOM   1510 C  CD2   . TRP A 1 198 ? 1.16606   -2.17246  -6.20973  1.000 23.53257 ? 198 TRP A CD2   1 
ATOM   1511 N  NE1   . TRP A 1 198 ? 2.38009   -2.94946  -4.49275  1.000 23.63029 ? 198 TRP A NE1   1 
ATOM   1512 C  CE2   . TRP A 1 198 ? 1.13008   -2.97746  -5.05273  1.000 21.62312 ? 198 TRP A CE2   1 
ATOM   1513 C  CE3   . TRP A 1 198 ? 0.00205   -2.03446  -6.97371  1.000 21.44746 ? 198 TRP A CE3   1 
ATOM   1514 C  CZ2   . TRP A 1 198 ? -0.02291  -3.63946  -4.64171  1.000 18.92623 ? 198 TRP A CZ2   1 
ATOM   1515 C  CZ3   . TRP A 1 198 ? -1.14294  -2.69447  -6.56369  1.000 26.52875 ? 198 TRP A CZ3   1 
ATOM   1516 C  CH2   . TRP A 1 198 ? -1.14692  -3.48647  -5.40769  1.000 26.09063 ? 198 TRP A CH2   1 
ATOM   1517 N  N     . GLN A 1 199 ? 0.69605   1.08854   -5.85472  1.000 19.53116 ? 199 GLN A N     1 
ATOM   1518 C  CA    . GLN A 1 199 ? -0.71994  1.41853   -5.71370  1.000 24.51420 ? 199 GLN A CA    1 
ATOM   1519 C  C     . GLN A 1 199 ? -0.99396  2.86253   -6.11269  1.000 25.49980 ? 199 GLN A C     1 
ATOM   1520 O  O     . GLN A 1 199 ? -2.04697  3.16653   -6.68567  1.000 29.81980 ? 199 GLN A O     1 
ATOM   1521 C  CB    . GLN A 1 199 ? -1.19092  1.18553   -4.27769  1.000 23.95427 ? 199 GLN A CB    1 
ATOM   1522 C  CG    . GLN A 1 199 ? -1.07391  -0.23847  -3.78169  1.000 27.09524 ? 199 GLN A CG    1 
ATOM   1523 C  CD    . GLN A 1 199 ? 0.17011   -0.44846  -2.94271  1.000 31.61041 ? 199 GLN A CD    1 
ATOM   1524 O  OE1   . GLN A 1 199 ? 1.14010   0.30254   -3.05473  1.000 22.68748 ? 199 GLN A OE1   1 
ATOM   1525 N  NE2   . GLN A 1 199 ? 0.14313   -1.46646  -2.08771  1.000 31.14646 ? 199 GLN A NE2   1 
ATOM   1526 N  N     . GLU A 1 200 ? -0.05695  3.76654   -5.81371  1.000 23.52963 ? 200 GLU A N     1 
ATOM   1527 C  CA    . GLU A 1 200 ? -0.29496  5.18554   -6.04070  1.000 22.56773 ? 200 GLU A CA    1 
ATOM   1528 C  C     . GLU A 1 200 ? -0.22399  5.55154   -7.51570  1.000 24.57518 ? 200 GLU A C     1 
ATOM   1529 O  O     . GLU A 1 200 ? -0.87200  6.51653   -7.93969  1.000 33.51221 ? 200 GLU A O     1 
ATOM   1530 C  CB    . GLU A 1 200 ? 0.71105   6.01454   -5.24272  1.000 18.93807 ? 200 GLU A CB    1 
ATOM   1531 C  CG    . GLU A 1 200 ? 0.56607   5.86854   -3.74272  1.000 21.66363 ? 200 GLU A CG    1 
ATOM   1532 C  CD    . GLU A 1 200 ? 1.70408   6.51854   -2.98774  1.000 24.33615 ? 200 GLU A CD    1 
ATOM   1533 O  OE1   . GLU A 1 200 ? 2.86308   6.40955   -3.44276  1.000 19.76831 ? 200 GLU A OE1   1 
ATOM   1534 O  OE2   . GLU A 1 200 ? 1.43610   7.14554   -1.94273  1.000 25.91724 ? 200 GLU A OE2   1 
ATOM   1535 N  N     . VAL A 1 201 ? 0.54900   4.80954   -8.31572  1.000 25.80283 ? 201 VAL A N     1 
ATOM   1536 C  CA    . VAL A 1 201 ? 0.71198   5.17054   -9.72372  1.000 19.71494 ? 201 VAL A CA    1 
ATOM   1537 C  C     . VAL A 1 201 ? -0.43804  4.69754   -10.59570 1.000 26.32687 ? 201 VAL A C     1 
ATOM   1538 O  O     . VAL A 1 201 ? -0.55506  5.15154   -11.74070 1.000 23.37642 ? 201 VAL A O     1 
ATOM   1539 C  CB    . VAL A 1 201 ? 2.03097   4.62955   -10.30374 1.000 27.43886 ? 201 VAL A CB    1 
ATOM   1540 C  CG1   . VAL A 1 201 ? 3.22298   5.31755   -9.64276  1.000 21.89516 ? 201 VAL A CG1   1 
ATOM   1541 C  CG2   . VAL A 1 201 ? 2.10998   3.12655   -10.13474 1.000 22.45334 ? 201 VAL A CG2   1 
ATOM   1542 N  N     . GLY A 1 202 ? -1.28803  3.80453   -10.09669 1.000 25.44086 ? 202 GLY A N     1 
ATOM   1543 C  CA    . GLY A 1 202 ? -2.48904  3.45753   -10.82667 1.000 28.68217 ? 202 GLY A CA    1 
ATOM   1544 C  C     . GLY A 1 202 ? -2.81303  1.98053   -10.88666 1.000 24.55591 ? 202 GLY A C     1 
ATOM   1545 O  O     . GLY A 1 202 ? -3.93604  1.60953   -11.23664 1.000 26.61622 ? 202 GLY A O     1 
ATOM   1546 N  N     . PHE A 1 203 ? -1.84902  1.12553   -10.55468 1.000 27.59120 ? 203 PHE A N     1 
ATOM   1547 C  CA    . PHE A 1 203 ? -2.07202  -0.31147  -10.64268 1.000 25.38922 ? 203 PHE A CA    1 
ATOM   1548 C  C     . PHE A 1 203 ? -3.01500  -0.78547  -9.54266  1.000 24.29594 ? 203 PHE A C     1 
ATOM   1549 O  O     . PHE A 1 203 ? -2.97198  -0.29847  -8.40966  1.000 25.44758 ? 203 PHE A O     1 
ATOM   1550 C  CB    . PHE A 1 203 ? -0.74402  -1.06446  -10.55770 1.000 19.76171 ? 203 PHE A CB    1 
ATOM   1551 C  CG    . PHE A 1 203 ? 0.19996   -0.75646  -11.68271 1.000 19.31603 ? 203 PHE A CG    1 
ATOM   1552 C  CD1   . PHE A 1 203 ? -0.03906  -1.24446  -12.95571 1.000 19.98870 ? 203 PHE A CD1   1 
ATOM   1553 C  CD2   . PHE A 1 203 ? 1.33096   0.01354   -11.46673 1.000 19.71228 ? 203 PHE A CD2   1 
ATOM   1554 C  CE1   . PHE A 1 203 ? 0.83393   -0.97046  -13.99372 1.000 17.24457 ? 203 PHE A CE1   1 
ATOM   1555 C  CE2   . PHE A 1 203 ? 2.20495   0.29555   -12.49975 1.000 19.29225 ? 203 PHE A CE2   1 
ATOM   1556 C  CZ    . PHE A 1 203 ? 1.95493   -0.19545  -13.76674 1.000 19.48580 ? 203 PHE A CZ    1 
ATOM   1557 N  N     . LYS A 1 204 ? -3.86700  -1.75347  -9.88365  1.000 26.26039 ? 204 LYS A N     1 
ATOM   1558 C  CA    . LYS A 1 204 ? -4.84199  -2.30548  -8.95263  1.000 28.30690 ? 204 LYS A CA    1 
ATOM   1559 C  C     . LYS A 1 204 ? -4.48897  -3.69648  -8.44664  1.000 30.31829 ? 204 LYS A C     1 
ATOM   1560 O  O     . LYS A 1 204 ? -4.86795  -4.04248  -7.32663  1.000 32.00365 ? 204 LYS A O     1 
ATOM   1561 C  CB    . LYS A 1 204 ? -6.23500  -2.36048  -9.59661  1.000 31.75592 ? 204 LYS A CB    1 
ATOM   1562 C  CG    . LYS A 1 204 ? -6.31202  -1.84948  -11.03661 1.000 35.52158 ? 204 LYS A CG    1 
ATOM   1563 C  CD    . LYS A 1 204 ? -6.44503  -0.33248  -11.10460 1.000 26.87845 ? 204 LYS A CD    1 
ATOM   1564 C  CE    . LYS A 1 204 ? -7.40801  0.18951   -10.05059 0.000 30.05975 ? 204 LYS A CE    1 
ATOM   1565 N  NZ    . LYS A 1 204 ? -8.01102  1.49051   -10.44358 0.000 30.98276 ? 204 LYS A NZ    1 
ATOM   1566 N  N     . GLU A 1 205 ? -3.78798  -4.50547  -9.24065  1.000 30.92762 ? 205 GLU A N     1 
ATOM   1567 C  CA    . GLU A 1 205 ? -3.39797  -5.82647  -8.76065  1.000 25.15445 ? 205 GLU A CA    1 
ATOM   1568 C  C     . GLU A 1 205 ? -1.91696  -5.85047  -8.40268  1.000 20.79594 ? 205 GLU A C     1 
ATOM   1569 O  O     . GLU A 1 205 ? -1.10498  -5.19647  -9.06469  1.000 23.78916 ? 205 GLU A O     1 
ATOM   1570 C  CB    . GLU A 1 205 ? -3.68698  -6.90447  -9.80965  1.000 35.16876 ? 205 GLU A CB    1 
ATOM   1571 C  CG    . GLU A 1 205 ? -5.16999  -7.14948  -10.06363 1.000 35.22237 ? 205 GLU A CG    1 
ATOM   1572 C  CD    . GLU A 1 205 ? -5.43899  -8.45748  -10.78562 1.000 43.03127 ? 205 GLU A CD    1 
ATOM   1573 O  OE1   . GLU A 1 205 ? -4.74399  -9.45648  -10.50063 1.000 40.58555 ? 205 GLU A OE1   1 
ATOM   1574 O  OE2   . GLU A 1 205 ? -6.34701  -8.48548  -11.64361 1.000 49.24704 ? 205 GLU A OE2   1 
ATOM   1575 N  N     . PRO A 1 206 ? -1.53794  -6.57747  -7.35669  1.000 22.32723 ? 206 PRO A N     1 
ATOM   1576 C  CA    . PRO A 1 206 ? -0.14494  -6.55046  -6.89371  1.000 23.57372 ? 206 PRO A CA    1 
ATOM   1577 C  C     . PRO A 1 206 ? 0.76705   -7.32346  -7.82872  1.000 22.43837 ? 206 PRO A C     1 
ATOM   1578 O  O     . PRO A 1 206 ? 0.30704   -8.19046  -8.58672  1.000 23.92102 ? 206 PRO A O     1 
ATOM   1579 C  CB    . PRO A 1 206 ? -0.22191  -7.21846  -5.51271  1.000 22.77429 ? 206 PRO A CB    1 
ATOM   1580 C  CG    . PRO A 1 206 ? -1.39091  -8.13847  -5.62069  1.000 27.34161 ? 206 PRO A CG    1 
ATOM   1581 C  CD    . PRO A 1 206 ? -2.38493  -7.44047  -6.51467  1.000 27.64280 ? 206 PRO A CD    1 
ATOM   1582 N  N     . PRO A 1 207 ? 2.06705   -7.03746  -7.80575  1.000 23.76736 ? 207 PRO A N     1 
ATOM   1583 C  CA    . PRO A 1 207 ? 3.01504   -7.80545  -8.61976  1.000 23.79612 ? 207 PRO A CA    1 
ATOM   1584 C  C     . PRO A 1 207 ? 3.28605   -9.18045  -8.02877  1.000 20.22865 ? 207 PRO A C     1 
ATOM   1585 O  O     . PRO A 1 207 ? 3.24307   -9.38645  -6.81477  1.000 18.72168 ? 207 PRO A O     1 
ATOM   1586 C  CB    . PRO A 1 207 ? 4.27904   -6.93845  -8.59178  1.000 18.12981 ? 207 PRO A CB    1 
ATOM   1587 C  CG    . PRO A 1 207 ? 4.18706   -6.20245  -7.30178  1.000 17.82239 ? 207 PRO A CG    1 
ATOM   1588 C  CD    . PRO A 1 207 ? 2.72506   -5.93545  -7.08076  1.000 19.69674 ? 207 PRO A CD    1 
ATOM   1589 N  N     . LEU A 1 208 ? 3.57504   -10.13245 -8.91477  1.000 17.10352 ? 208 LEU A N     1 
ATOM   1590 C  CA    . LEU A 1 208 ? 3.82205   -11.50645 -8.51178  1.000 15.25686 ? 208 LEU A CA    1 
ATOM   1591 C  C     . LEU A 1 208 ? 5.25605   -11.95944 -8.73980  1.000 12.59674 ? 208 LEU A C     1 
ATOM   1592 O  O     . LEU A 1 208 ? 5.60406   -13.07944 -8.34381  1.000 10.89144 ? 208 LEU A O     1 
ATOM   1593 C  CB    . LEU A 1 208 ? 2.87204   -12.46045 -9.25676  1.000 15.68658 ? 208 LEU A CB    1 
ATOM   1594 C  CG    . LEU A 1 208 ? 1.37205   -12.23346 -9.06374  1.000 20.90491 ? 208 LEU A CG    1 
ATOM   1595 C  CD1   . LEU A 1 208 ? 0.56704   -13.29546 -9.80872  1.000 22.14976 ? 208 LEU A CD1   1 
ATOM   1596 C  CD2   . LEU A 1 208 ? 1.02407   -12.23246 -7.58873  1.000 20.55438 ? 208 LEU A CD2   1 
ATOM   1597 N  N     . THR A 1 209 ? 6.09604   -11.13144 -9.35181  1.000 13.03852 ? 209 THR A N     1 
ATOM   1598 C  CA    . THR A 1 209 ? 7.44203   -11.56944 -9.67884  1.000 10.13655 ? 209 THR A CA    1 
ATOM   1599 C  C     . THR A 1 209 ? 8.25206   -11.81743 -8.41385  1.000 11.31372 ? 209 THR A C     1 
ATOM   1600 O  O     . THR A 1 209 ? 7.98307   -11.24644 -7.35385  1.000 17.28916 ? 209 THR A O     1 
ATOM   1601 C  CB    . THR A 1 209 ? 8.14902   -10.54343 -10.56385 1.000 12.44068 ? 209 THR A CB    1 
ATOM   1602 O  OG1   . THR A 1 209 ? 9.37801   -11.10743 -11.03787 1.000 9.59274  ? 209 THR A OG1   1 
ATOM   1603 C  CG2   . THR A 1 209 ? 8.45002   -9.26443  -9.78985  1.000 9.77968  ? 209 THR A CG2   1 
ATOM   1604 N  N     . VAL A 1 210 ? 9.25106   -12.69743 -8.53187  1.000 10.58716 ? 210 VAL A N     1 
ATOM   1605 C  CA    . VAL A 1 210 ? 10.09808  -13.07843 -7.40488  1.000 10.07938 ? 210 VAL A CA    1 
ATOM   1606 C  C     . VAL A 1 210 ? 11.45207  -12.39142 -7.43490  1.000 14.23442 ? 210 VAL A C     1 
ATOM   1607 O  O     . VAL A 1 210 ? 12.29709  -12.66342 -6.56592  1.000 12.82021 ? 210 VAL A O     1 
ATOM   1608 C  CB    . VAL A 1 210 ? 10.29408  -14.60843 -7.34589  1.000 15.14407 ? 210 VAL A CB    1 
ATOM   1609 C  CG1   . VAL A 1 210 ? 8.96509   -15.31643 -7.17186  1.000 10.67499 ? 210 VAL A CG1   1 
ATOM   1610 C  CG2   . VAL A 1 210 ? 11.00906  -15.10442 -8.59690  1.000 11.17553 ? 210 VAL A CG2   1 
ATOM   1611 N  N     . PHE A 1 211 ? 11.69306  -11.52042 -8.40891  1.000 10.09792 ? 211 PHE A N     1 
ATOM   1612 C  CA    . PHE A 1 211 ? 12.97305  -10.84642 -8.55893  1.000 9.81806  ? 211 PHE A CA    1 
ATOM   1613 C  C     . PHE A 1 211 ? 12.82305  -9.39242  -8.13593  1.000 10.63231 ? 211 PHE A C     1 
ATOM   1614 O  O     . PHE A 1 211 ? 11.96204  -8.67442  -8.65791  1.000 14.50870 ? 211 PHE A O     1 
ATOM   1615 C  CB    . PHE A 1 211 ? 13.48103  -10.94242 -9.99794  1.000 10.13734 ? 211 PHE A CB    1 
ATOM   1616 C  CG    . PHE A 1 211 ? 13.56602  -12.34642 -10.51094 1.000 10.89405 ? 211 PHE A CG    1 
ATOM   1617 C  CD1   . PHE A 1 211 ? 14.48503  -13.23641 -9.98195  1.000 10.70798 ? 211 PHE A CD1   1 
ATOM   1618 C  CD2   . PHE A 1 211 ? 12.72301  -12.78042 -11.52193 1.000 13.77974 ? 211 PHE A CD2   1 
ATOM   1619 C  CE1   . PHE A 1 211 ? 14.56503  -14.53541 -10.45296 1.000 12.63458 ? 211 PHE A CE1   1 
ATOM   1620 C  CE2   . PHE A 1 211 ? 12.79600  -14.07642 -11.99793 1.000 9.72397  ? 211 PHE A CE2   1 
ATOM   1621 C  CZ    . PHE A 1 211 ? 13.72202  -14.95441 -11.46494 1.000 13.29350 ? 211 PHE A CZ    1 
ATOM   1622 N  N     . LYS A 1 212 ? 13.66307  -8.96942  -7.19694  1.000 10.45097 ? 212 LYS A N     1 
ATOM   1623 C  CA    . LYS A 1 212 ? 13.57707  -7.64442  -6.60494  1.000 17.63576 ? 212 LYS A CA    1 
ATOM   1624 C  C     . LYS A 1 212 ? 14.48106  -6.66441  -7.33895  1.000 8.67668  ? 212 LYS A C     1 
ATOM   1625 O  O     . LYS A 1 212 ? 15.61705  -6.99241  -7.68597  1.000 12.81483 ? 212 LYS A O     1 
ATOM   1626 C  CB    . LYS A 1 212 ? 13.96410  -7.70242  -5.12794  1.000 16.45959 ? 212 LYS A CB    1 
ATOM   1627 C  CG    . LYS A 1 212 ? 13.10711  -8.65042  -4.30293  1.000 20.51549 ? 212 LYS A CG    1 
ATOM   1628 C  CD    . LYS A 1 212 ? 11.66911  -8.16142  -4.20491  1.000 21.21828 ? 212 LYS A CD    1 
ATOM   1629 C  CE    . LYS A 1 212 ? 11.58412  -6.85142  -3.43990  0.000 16.51242 ? 212 LYS A CE    1 
ATOM   1630 N  NZ    . LYS A 1 212 ? 10.68914  -6.95943  -2.25589  0.000 17.11113 ? 212 LYS A NZ    1 
ATOM   1631 N  N     . GLY A 1 213 ? 13.97605  -5.45341  -7.55994  1.000 8.59888  ? 213 GLY A N     1 
ATOM   1632 C  CA    . GLY A 1 213 ? 14.75103  -4.44241  -8.24696  1.000 10.00892 ? 213 GLY A CA    1 
ATOM   1633 C  C     . GLY A 1 213 ? 15.81605  -3.82341  -7.36397  1.000 11.59866 ? 213 GLY A C     1 
ATOM   1634 O  O     . GLY A 1 213 ? 15.80807  -3.96541  -6.14097  1.000 14.21214 ? 213 GLY A O     1 
ATOM   1635 N  N     . GLY A 1 214 ? 16.75103  -3.12441  -8.00799  1.000 8.11811  ? 214 GLY A N     1 
ATOM   1636 C  CA    . GLY A 1 214 ? 17.76904  -2.37840  -7.29001  1.000 8.77530  ? 214 GLY A CA    1 
ATOM   1637 C  C     . GLY A 1 214 ? 19.20304  -2.77940  -7.58203  1.000 10.16422 ? 214 GLY A C     1 
ATOM   1638 O  O     . GLY A 1 214 ? 19.47804  -3.92440  -7.94803  1.000 10.09747 ? 214 GLY A O     1 
ATOM   1639 N  N     . GLU A 1 215 ? 20.12604  -1.82939  -7.42004  1.000 10.97994 ? 215 GLU A N     1 
ATOM   1640 C  CA    . GLU A 1 215 ? 21.54804  -2.11439  -7.59407  1.000 9.21723  ? 215 GLU A CA    1 
ATOM   1641 C  C     . GLU A 1 215 ? 22.05506  -3.10639  -6.55508  1.000 9.64080  ? 215 GLU A C     1 
ATOM   1642 O  O     . GLU A 1 215 ? 22.94906  -3.91338  -6.84509  1.000 8.09707  ? 215 GLU A O     1 
ATOM   1643 C  CB    . GLU A 1 215 ? 22.33903  -0.80339  -7.52008  1.000 9.93950  ? 215 GLU A CB    1 
ATOM   1644 C  CG    . GLU A 1 215 ? 23.85104  -0.95638  -7.42111  1.000 9.17343  ? 215 GLU A CG    1 
ATOM   1645 C  CD    . GLU A 1 215 ? 24.54004  0.35262   -7.08012  1.000 9.80244  ? 215 GLU A CD    1 
ATOM   1646 O  OE1   . GLU A 1 215 ? 23.85904  1.26462   -6.55611  1.000 7.89042  ? 215 GLU A OE1   1 
ATOM   1647 O  OE2   . GLU A 1 215 ? 25.75403  0.46763   -7.34014  1.000 9.13464  ? 215 GLU A OE2   1 
ATOM   1648 N  N     . THR A 1 216 ? 21.49508  -3.06139  -5.34407  1.000 8.21504  ? 216 THR A N     1 
ATOM   1649 C  CA    . THR A 1 216 ? 21.90410  -3.97239  -4.28007  1.000 12.34026 ? 216 THR A CA    1 
ATOM   1650 C  C     . THR A 1 216 ? 21.59410  -5.41839  -4.64407  1.000 9.84028  ? 216 THR A C     1 
ATOM   1651 O  O     . THR A 1 216 ? 22.43910  -6.30539  -4.49108  1.000 12.25622 ? 216 THR A O     1 
ATOM   1652 C  CB    . THR A 1 216 ? 21.20912  -3.58339  -2.97406  1.000 10.38807 ? 216 THR A CB    1 
ATOM   1653 O  OG1   . THR A 1 216 ? 21.61312  -2.26139  -2.59807  1.000 11.80067 ? 216 THR A OG1   1 
ATOM   1654 C  CG2   . THR A 1 216 ? 21.55014  -4.56139  -1.86607  1.000 11.95715 ? 216 THR A CG2   1 
ATOM   1655 N  N     . GLU A 1 217 ? 20.37909  -5.67039  -5.12705  1.000 12.68028 ? 217 GLU A N     1 
ATOM   1656 C  CA    . GLU A 1 217 ? 20.00509  -7.01039  -5.56304  1.000 12.45737 ? 217 GLU A CA    1 
ATOM   1657 C  C     . GLU A 1 217 ? 20.80107  -7.44939  -6.78206  1.000 12.17351 ? 217 GLU A C     1 
ATOM   1658 O  O     . GLU A 1 217 ? 21.08507  -8.64339  -6.93606  1.000 12.00174 ? 217 GLU A O     1 
ATOM   1659 C  CB    . GLU A 1 217 ? 18.51008  -7.06140  -5.86702  1.000 10.96160 ? 217 GLU A CB    1 
ATOM   1660 C  CG    . GLU A 1 217 ? 17.63010  -6.91440  -4.64800  1.000 20.58279 ? 217 GLU A CG    1 
ATOM   1661 C  CD    . GLU A 1 217 ? 17.68912  -8.12240  -3.74001  1.000 19.59831 ? 217 GLU A CD    1 
ATOM   1662 O  OE1   . GLU A 1 217 ? 18.06312  -9.21340  -4.22101  1.000 19.19694 ? 217 GLU A OE1   1 
ATOM   1663 O  OE2   . GLU A 1 217 ? 17.36414  -7.97840  -2.54300  1.000 22.93876 ? 217 GLU A OE2   1 
ATOM   1664 N  N     . ALA A 1 218 ? 21.15405  -6.50639  -7.66006  1.000 10.09506 ? 218 ALA A N     1 
ATOM   1665 C  CA    . ALA A 1 218 ? 21.96703  -6.83339  -8.82408  1.000 8.12680  ? 218 ALA A CA    1 
ATOM   1666 C  C     . ALA A 1 218 ? 23.34204  -7.32538  -8.39910  1.000 9.97411  ? 218 ALA A C     1 
ATOM   1667 O  O     . ALA A 1 218 ? 23.82404  -8.35638  -8.88011  1.000 9.52311  ? 218 ALA A O     1 
ATOM   1668 C  CB    . ALA A 1 218 ? 22.09001  -5.60939  -9.73408  1.000 9.39490  ? 218 ALA A CB    1 
ATOM   1669 N  N     . LEU A 1 219 ? 23.98205  -6.60138  -7.48111  1.000 8.26226  ? 219 LEU A N     1 
ATOM   1670 C  CA    . LEU A 1 219 ? 25.31006  -6.99438  -7.02413  1.000 10.20788 ? 219 LEU A CA    1 
ATOM   1671 C  C     . LEU A 1 219 ? 25.26108  -8.29338  -6.22613  1.000 9.63593  ? 219 LEU A C     1 
ATOM   1672 O  O     . LEU A 1 219 ? 26.18708  -9.10737  -6.30415  1.000 9.33030  ? 219 LEU A O     1 
ATOM   1673 C  CB    . LEU A 1 219 ? 25.92507  -5.87237  -6.19514  1.000 8.46188  ? 219 LEU A CB    1 
ATOM   1674 C  CG    . LEU A 1 219 ? 26.11106  -4.56337  -6.97314  1.000 11.24374 ? 219 LEU A CG    1 
ATOM   1675 C  CD1   . LEU A 1 219 ? 26.59607  -3.46037  -6.06215  1.000 8.29741  ? 219 LEU A CD1   1 
ATOM   1676 C  CD2   . LEU A 1 219 ? 27.06504  -4.75737  -8.14416  1.000 14.29613 ? 219 LEU A CD2   1 
ATOM   1677 N  N     . ALA A 1 220 ? 24.19309  -8.50438  -5.44711  1.000 9.13651  ? 220 ALA A N     1 
ATOM   1678 C  CA    . ALA A 1 220 ? 24.05311  -9.75538  -4.70511  1.000 11.41651 ? 220 ALA A CA    1 
ATOM   1679 C  C     . ALA A 1 220 ? 23.85210  -10.94238 -5.64111  1.000 11.57876 ? 220 ALA A C     1 
ATOM   1680 O  O     . ALA A 1 220 ? 24.36811  -12.03438 -5.38812  1.000 9.29901  ? 220 ALA A O     1 
ATOM   1681 C  CB    . ALA A 1 220 ? 22.89513  -9.64739  -3.71509  1.000 13.75697 ? 220 ALA A CB    1 
ATOM   1682 N  N     . ARG A 1 221 ? 23.08703  -10.75536 -6.71710  1.000 11.37718 ? 221 ARG A N     1 
ATOM   1683 C  CA    . ARG A 1 221 ? 22.92417  -11.83234 -7.68626  1.000 13.74371 ? 221 ARG A CA    1 
ATOM   1684 C  C     . ARG A 1 221 ? 24.20850  -12.07094 -8.46806  1.000 11.84132 ? 221 ARG A C     1 
ATOM   1685 O  O     . ARG A 1 221 ? 24.49296  -13.20806 -8.86023  1.000 11.62895 ? 221 ARG A O     1 
ATOM   1686 C  CB    . ARG A 1 221 ? 21.76780  -11.51946 -8.63787  1.000 10.62760 ? 221 ARG A CB    1 
ATOM   1687 C  CG    . ARG A 1 221 ? 21.33171  -12.71140 -9.47133  1.000 15.50783 ? 221 ARG A CG    1 
ATOM   1688 C  CD    . ARG A 1 221 ? 19.88346  -12.58795 -9.91750  1.000 15.05351 ? 221 ARG A CD    1 
ATOM   1689 N  NE    . ARG A 1 221 ? 19.34504  -13.87827 -10.33177 1.000 18.06966 ? 221 ARG A NE    1 
ATOM   1690 C  CZ    . ARG A 1 221 ? 18.68468  -14.70754 -9.53438  1.000 14.88428 ? 221 ARG A CZ    1 
ATOM   1691 N  NH1   . ARG A 1 221 ? 18.43214  -14.40019 -8.27312  1.000 16.92243 ? 221 ARG A NH1   1 
ATOM   1692 N  NH2   . ARG A 1 221 ? 18.26684  -15.87491 -10.01492 1.000 19.00019 ? 221 ARG A NH2   1 
ATOM   1693 N  N     . LEU A 1 222 ? 24.99705  -11.01738 -8.68913  1.000 10.35901 ? 222 LEU A N     1 
ATOM   1694 C  CA    . LEU A 1 222 ? 26.26404  -11.16537 -9.39815  1.000 12.39244 ? 222 LEU A CA    1 
ATOM   1695 C  C     . LEU A 1 222 ? 27.23605  -12.03437 -8.60917  1.000 10.62904 ? 222 LEU A C     1 
ATOM   1696 O  O     . LEU A 1 222 ? 27.77705  -13.01437 -9.13618  1.000 8.99995  ? 222 LEU A O     1 
ATOM   1697 C  CB    . LEU A 1 222 ? 26.86603  -9.78737  -9.67416  1.000 8.58865  ? 222 LEU A CB    1 
ATOM   1698 C  CG    . LEU A 1 222 ? 28.20502  -9.74837  -10.41218 1.000 10.75654 ? 222 LEU A CG    1 
ATOM   1699 C  CD1   . LEU A 1 222 ? 28.05199  -10.26637 -11.83318 1.000 8.46595  ? 222 LEU A CD1   1 
ATOM   1700 C  CD2   . LEU A 1 222 ? 28.77001  -8.33336  -10.40419 1.000 13.36017 ? 222 LEU A CD2   1 
ATOM   1701 N  N     . GLU A 1 223 ? 27.46207  -11.69737 -7.33217  1.000 9.00983  ? 223 GLU A N     1 
ATOM   1702 C  CA    . GLU A 1 223 ? 28.36709  -12.48537 -6.50119  1.000 9.29684  ? 223 GLU A CA    1 
ATOM   1703 C  C     . GLU A 1 223 ? 27.88110  -13.91737 -6.34418  1.000 14.37887 ? 223 GLU A C     1 
ATOM   1704 O  O     . GLU A 1 223 ? 28.69610  -14.84037 -6.22319  1.000 13.33191 ? 223 GLU A O     1 
ATOM   1705 C  CB    . GLU A 1 223 ? 28.52611  -11.83737 -5.12419  1.000 15.27596 ? 223 GLU A CB    1 
ATOM   1706 C  CG    . GLU A 1 223 ? 29.12911  -10.44036 -5.13820  1.000 12.99187 ? 223 GLU A CG    1 
ATOM   1707 C  CD    . GLU A 1 223 ? 30.60310  -10.44136 -5.48122  1.000 15.69825 ? 223 GLU A CD    1 
ATOM   1708 O  OE1   . GLU A 1 223 ? 31.23111  -11.51336 -5.40323  1.000 24.56395 ? 223 GLU A OE1   1 
ATOM   1709 O  OE2   . GLU A 1 223 ? 31.13609  -9.37236  -5.83223  1.000 18.48331 ? 223 GLU A OE2   1 
ATOM   1710 N  N     . ALA A 1 224 ? 26.56010  -14.12337 -6.33116  1.000 13.19377 ? 224 ALA A N     1 
ATOM   1711 C  CA    . ALA A 1 224 ? 26.02810  -15.47637 -6.22415  1.000 15.08443 ? 224 ALA A CA    1 
ATOM   1712 C  C     . ALA A 1 224 ? 26.39309  -16.30137 -7.44915  1.000 14.14989 ? 224 ALA A C     1 
ATOM   1713 O  O     . ALA A 1 224 ? 26.70609  -17.49137 -7.33316  1.000 13.48944 ? 224 ALA A O     1 
ATOM   1714 C  CB    . ALA A 1 224 ? 24.50911  -15.43038 -6.02712  1.000 12.39294 ? 224 ALA A CB    1 
ATOM   1715 N  N     . ALA A 1 225 ? 26.38007  -15.67837 -8.62915  1.000 12.85689 ? 225 ALA A N     1 
ATOM   1716 C  CA    . ALA A 1 225 ? 26.73805  -16.38837 -9.84916  1.000 14.57788 ? 225 ALA A CA    1 
ATOM   1717 C  C     . ALA A 1 225 ? 28.22205  -16.71637 -9.88918  1.000 17.45674 ? 225 ALA A C     1 
ATOM   1718 O  O     . ALA A 1 225 ? 28.61104  -17.75936 -10.43019 1.000 14.55540 ? 225 ALA A O     1 
ATOM   1719 C  CB    . ALA A 1 225 ? 26.35102  -15.55837 -11.07115 1.000 11.51459 ? 225 ALA A CB    1 
ATOM   1720 N  N     . PHE A 1 226 ? 29.05705  -15.85236 -9.31820  1.000 11.61911 ? 226 PHE A N     1 
ATOM   1721 C  CA    . PHE A 1 226 ? 30.50006  -16.05036 -9.31322  1.000 13.53536 ? 226 PHE A CA    1 
ATOM   1722 C  C     . PHE A 1 226 ? 30.98908  -16.82836 -8.09723  1.000 13.35861 ? 226 PHE A C     1 
ATOM   1723 O  O     . PHE A 1 226 ? 32.20108  -16.95635 -7.90825  1.000 14.86872 ? 226 PHE A O     1 
ATOM   1724 C  CB    . PHE A 1 226 ? 31.21705  -14.69936 -9.39923  1.000 15.76556 ? 226 PHE A CB    1 
ATOM   1725 C  CG    . PHE A 1 226 ? 31.25102  -14.12035 -10.78623 1.000 12.43471 ? 226 PHE A CG    1 
ATOM   1726 C  CD1   . PHE A 1 226 ? 30.11601  -13.55336 -11.34321 1.000 15.84735 ? 226 PHE A CD1   1 
ATOM   1727 C  CD2   . PHE A 1 226 ? 32.42001  -14.13935 -11.53025 1.000 14.10574 ? 226 PHE A CD2   1 
ATOM   1728 C  CE1   . PHE A 1 226 ? 30.14899  -13.02236 -12.62021 1.000 12.43579 ? 226 PHE A CE1   1 
ATOM   1729 C  CE2   . PHE A 1 226 ? 32.46099  -13.60635 -12.80225 1.000 9.28106  ? 226 PHE A CE2   1 
ATOM   1730 C  CZ    . PHE A 1 226 ? 31.32698  -13.05035 -13.35123 1.000 11.98346 ? 226 PHE A CZ    1 
ATOM   1731 N  N     . GLN A 1 227 ? 30.07609  -17.36236 -7.28222  1.000 19.56211 ? 227 GLN A N     1 
ATOM   1732 C  CA    . GLN A 1 227 ? 30.49012  -18.20836 -6.16722  1.000 21.20901 ? 227 GLN A CA    1 
ATOM   1733 C  C     . GLN A 1 227 ? 31.20211  -19.46536 -6.64423  1.000 13.85638 ? 227 GLN A C     1 
ATOM   1734 O  O     . GLN A 1 227 ? 32.09412  -19.97135 -5.95225  1.000 19.84768 ? 227 GLN A O     1 
ATOM   1735 C  CB    . GLN A 1 227 ? 29.28113  -18.58136 -5.31120  1.000 20.60909 ? 227 GLN A CB    1 
ATOM   1736 C  CG    . GLN A 1 227 ? 28.80214  -17.46537 -4.39919  1.000 17.44212 ? 227 GLN A CG    1 
ATOM   1737 C  CD    . GLN A 1 227 ? 29.79416  -17.15236 -3.29421  1.000 29.02565 ? 227 GLN A CD    1 
ATOM   1738 O  OE1   . GLN A 1 227 ? 30.70717  -17.93336 -3.02223  1.000 35.48711 ? 227 GLN A OE1   1 
ATOM   1739 N  NE2   . GLN A 1 227 ? 29.61917  -16.00436 -2.65021  1.000 34.57856 ? 227 GLN A NE2   1 
ATOM   1740 N  N     . ASP A 1 228 ? 30.81909  -19.99436 -7.80823  1.000 18.35236 ? 228 ASP A N     1 
ATOM   1741 C  CA    . ASP A 1 228 ? 31.44509  -21.18035 -8.39024  1.000 19.64222 ? 228 ASP A CA    1 
ATOM   1742 C  C     . ASP A 1 228 ? 32.15107  -20.76935 -9.67425  1.000 16.30036 ? 228 ASP A C     1 
ATOM   1743 O  O     . ASP A 1 228 ? 31.52205  -20.70335 -10.74224 1.000 15.25747 ? 228 ASP A O     1 
ATOM   1744 C  CB    . ASP A 1 228 ? 30.41009  -22.27536 -8.66422  1.000 17.64521 ? 228 ASP A CB    1 
ATOM   1745 C  CG    . ASP A 1 228 ? 31.03508  -23.56336 -9.17223  1.000 14.39696 ? 228 ASP A CG    1 
ATOM   1746 O  OD1   . ASP A 1 228 ? 32.27508  -23.69135 -9.12025  1.000 19.84659 ? 228 ASP A OD1   1 
ATOM   1747 O  OD2   . ASP A 1 228 ? 30.28408  -24.44736 -9.63322  1.000 17.51661 ? 228 ASP A OD2   1 
ATOM   1748 N  N     . PRO A 1 229 ? 33.45307  -20.47735 -9.62527  1.000 17.54206 ? 229 PRO A N     1 
ATOM   1749 C  CA    . PRO A 1 229 ? 34.14604  -20.02935 -10.84328 1.000 12.01263 ? 229 PRO A CA    1 
ATOM   1750 C  C     . PRO A 1 229 ? 34.17503  -21.06934 -11.95028 1.000 12.56694 ? 229 PRO A C     1 
ATOM   1751 O  O     . PRO A 1 229 ? 34.26601  -20.69734 -13.12629 1.000 14.22133 ? 229 PRO A O     1 
ATOM   1752 C  CB    . PRO A 1 229 ? 35.55805  -19.68934 -10.33831 1.000 11.56263 ? 229 PRO A CB    1 
ATOM   1753 C  CG    . PRO A 1 229 ? 35.69308  -20.41434 -9.03231  1.000 13.41163 ? 229 PRO A CG    1 
ATOM   1754 C  CD    . PRO A 1 229 ? 34.32308  -20.43435 -8.43929  1.000 15.83621 ? 229 PRO A CD    1 
ATOM   1755 N  N     . LYS A 1 230 ? 34.09204  -22.36034 -11.62028 1.000 15.27191 ? 230 LYS A N     1 
ATOM   1756 C  CA    . LYS A 1 230 ? 34.03002  -23.37734 -12.66528 1.000 17.37651 ? 230 LYS A CA    1 
ATOM   1757 C  C     . LYS A 1 230 ? 32.75301  -23.25135 -13.48826 1.000 13.62626 ? 230 LYS A C     1 
ATOM   1758 O  O     . LYS A 1 230 ? 32.77699  -23.42635 -14.71226 1.000 15.57340 ? 230 LYS A O     1 
ATOM   1759 C  CB    . LYS A 1 230 ? 34.13204  -24.77434 -12.05328 1.000 15.34046 ? 230 LYS A CB    1 
ATOM   1760 C  CG    . LYS A 1 230 ? 35.43605  -25.03734 -11.33231 1.000 19.25017 ? 230 LYS A CG    1 
ATOM   1761 C  CD    . LYS A 1 230 ? 35.59806  -26.51434 -11.02231 1.000 19.67099 ? 230 LYS A CD    1 
ATOM   1762 C  CE    . LYS A 1 230 ? 36.93907  -26.79234 -10.35933 1.000 23.62479 ? 230 LYS A CE    1 
ATOM   1763 N  NZ    . LYS A 1 230 ? 38.06306  -26.14833 -11.10035 0.270 16.26704 ? 230 LYS A NZ    1 
ATOM   1764 N  N     . TRP A 1 231 ? 31.62602  -22.95635 -12.83324 1.000 10.08630 ? 231 TRP A N     1 
ATOM   1765 C  CA    . TRP A 1 231 ? 30.36601  -22.78736 -13.55422 1.000 16.28191 ? 231 TRP A CA    1 
ATOM   1766 C  C     . TRP A 1 231 ? 30.41799  -21.58636 -14.48922 1.000 14.50208 ? 231 TRP A C     1 
ATOM   1767 O  O     . TRP A 1 231 ? 29.84397  -21.61636 -15.58521 1.000 16.42104 ? 231 TRP A O     1 
ATOM   1768 C  CB    . TRP A 1 231 ? 29.20402  -22.63436 -12.57120 1.000 15.52110 ? 231 TRP A CB    1 
ATOM   1769 C  CG    . TRP A 1 231 ? 27.86901  -22.37437 -13.23718 1.000 13.75907 ? 231 TRP A CG    1 
ATOM   1770 C  CD1   . TRP A 1 231 ? 26.96001  -23.31137 -13.64317 1.000 19.05501 ? 231 TRP A CD1   1 
ATOM   1771 C  CD2   . TRP A 1 231 ? 27.30000  -21.09937 -13.56417 1.000 11.22735 ? 231 TRP A CD2   1 
ATOM   1772 N  NE1   . TRP A 1 231 ? 25.86500  -22.70037 -14.20215 1.000 15.78147 ? 231 TRP A NE1   1 
ATOM   1773 C  CE2   . TRP A 1 231 ? 26.04999  -21.34237 -14.16715 1.000 16.17658 ? 231 TRP A CE2   1 
ATOM   1774 C  CE3   . TRP A 1 231 ? 27.72600  -19.78037 -13.40718 1.000 12.07144 ? 231 TRP A CE3   1 
ATOM   1775 C  CZ2   . TRP A 1 231 ? 25.22298  -20.31137 -14.61114 1.000 10.23813 ? 231 TRP A CZ2   1 
ATOM   1776 C  CZ3   . TRP A 1 231 ? 26.90799  -18.76037 -13.85316 1.000 11.38265 ? 231 TRP A CZ3   1 
ATOM   1777 C  CH2   . TRP A 1 231 ? 25.66798  -19.03137 -14.44314 1.000 13.44768 ? 231 TRP A CH2   1 
ATOM   1778 N  N     . VAL A 1 232 ? 31.08299  -20.51135 -14.06723 1.000 11.34514 ? 232 VAL A N     1 
ATOM   1779 C  CA    . VAL A 1 232 ? 31.20197  -19.33935 -14.92523 1.000 11.94356 ? 232 VAL A CA    1 
ATOM   1780 C  C     . VAL A 1 232 ? 32.05795  -19.66135 -16.13925 1.000 8.85227  ? 232 VAL A C     1 
ATOM   1781 O  O     . VAL A 1 232 ? 31.67893  -19.37535 -17.28024 1.000 9.05414  ? 232 VAL A O     1 
ATOM   1782 C  CB    . VAL A 1 232 ? 31.77098  -18.15135 -14.13324 1.000 11.64163 ? 232 VAL A CB    1 
ATOM   1783 C  CG1   . VAL A 1 232 ? 31.98096  -16.95735 -15.05125 1.000 11.74772 ? 232 VAL A CG1   1 
ATOM   1784 C  CG2   . VAL A 1 232 ? 30.83900  -17.79536 -12.99323 1.000 12.27885 ? 232 VAL A CG2   1 
ATOM   1785 N  N     . ALA A 1 233 ? 33.21596  -20.28435 -15.91227 1.000 14.89458 ? 233 ALA A N     1 
ATOM   1786 C  CA    . ALA A 1 233 ? 34.17694  -20.48634 -16.99228 1.000 14.29783 ? 233 ALA A CA    1 
ATOM   1787 C  C     . ALA A 1 233 ? 33.65893  -21.47734 -18.02628 1.000 15.86768 ? 233 ALA A C     1 
ATOM   1788 O  O     . ALA A 1 233 ? 33.93091  -21.33234 -19.22328 1.000 12.63220 ? 233 ALA A O     1 
ATOM   1789 C  CB    . ALA A 1 233 ? 35.51295  -20.95834 -16.42631 1.000 16.15899 ? 233 ALA A CB    1 
ATOM   1790 N  N     . GLY A 1 234 ? 32.93894  -22.50735 -17.58426 1.000 10.62815 ? 234 GLY A N     1 
ATOM   1791 C  CA    . GLY A 1 234 ? 32.41793  -23.51835 -18.48226 1.000 11.75767 ? 234 GLY A CA    1 
ATOM   1792 C  C     . GLY A 1 234 ? 31.03192  -23.24735 -19.01823 1.000 9.73723  ? 234 GLY A C     1 
ATOM   1793 O  O     . GLY A 1 234 ? 30.43491  -24.13135 -19.64122 1.000 10.17108 ? 234 GLY A O     1 
ATOM   1794 N  N     . PHE A 1 235 ? 30.50592  -22.04535 -18.80722 1.000 7.45327  ? 235 PHE A N     1 
ATOM   1795 C  CA    . PHE A 1 235 ? 29.13091  -21.74436 -19.17520 1.000 9.19212  ? 235 PHE A CA    1 
ATOM   1796 C  C     . PHE A 1 235 ? 28.94389  -21.88336 -20.68020 1.000 8.91531  ? 235 PHE A C     1 
ATOM   1797 O  O     . PHE A 1 235 ? 29.69687  -21.30936 -21.47221 1.000 8.57707  ? 235 PHE A O     1 
ATOM   1798 C  CB    . PHE A 1 235 ? 28.77291  -20.33436 -18.70219 1.000 10.07205 ? 235 PHE A CB    1 
ATOM   1799 C  CG    . PHE A 1 235 ? 27.36991  -19.90737 -19.02817 1.000 9.04401  ? 235 PHE A CG    1 
ATOM   1800 C  CD1   . PHE A 1 235 ? 27.08689  -19.26637 -20.22617 1.000 11.53610 ? 235 PHE A CD1   1 
ATOM   1801 C  CD2   . PHE A 1 235 ? 26.34492  -20.10937 -18.12715 1.000 7.83095  ? 235 PHE A CD2   1 
ATOM   1802 C  CE1   . PHE A 1 235 ? 25.80388  -18.85837 -20.52914 1.000 6.45851  ? 235 PHE A CE1   1 
ATOM   1803 C  CE2   . PHE A 1 235 ? 25.06092  -19.70137 -18.42213 1.000 9.70839  ? 235 PHE A CE2   1 
ATOM   1804 C  CZ    . PHE A 1 235 ? 24.78889  -19.07637 -19.62713 1.000 8.18559  ? 235 PHE A CZ    1 
ATOM   1805 N  N     . GLN A 1 236 ? 27.95488  -22.68236 -21.07218 1.000 8.35332  ? 236 GLN A N     1 
ATOM   1806 C  CA    . GLN A 1 236 ? 27.58386  -22.85636 -22.47518 1.000 10.56387 ? 236 GLN A CA    1 
ATOM   1807 C  C     . GLN A 1 236 ? 26.07886  -22.64437 -22.58615 1.000 12.85731 ? 236 GLN A C     1 
ATOM   1808 O  O     . GLN A 1 236 ? 25.29587  -23.50537 -22.16914 1.000 12.89764 ? 236 GLN A O     1 
ATOM   1809 C  CB    . GLN A 1 236 ? 27.99786  -24.23336 -23.00518 1.000 7.88785  ? 236 GLN A CB    1 
ATOM   1810 C  CG    . GLN A 1 236 ? 29.49986  -24.45336 -23.02021 1.000 12.44324 ? 236 GLN A CG    1 
ATOM   1811 C  CD    . GLN A 1 236 ? 29.93884  -25.54036 -23.99222 1.000 16.22423 ? 236 GLN A CD    1 
ATOM   1812 O  OE1   . GLN A 1 236 ? 30.77485  -26.38335 -23.66323 1.000 20.33754 ? 236 GLN A OE1   1 
ATOM   1813 N  NE2   . GLN A 1 236 ? 29.38682  -25.51336 -25.20321 1.000 19.67304 ? 236 GLN A NE2   1 
ATOM   1814 N  N     . LYS A 1 237 ? 25.69384  -21.49937 -23.15214 1.000 6.76680  ? 237 LYS A N     1 
ATOM   1815 C  CA    . LYS A 1 237 ? 24.29484  -21.08337 -23.14112 1.000 7.06507  ? 237 LYS A CA    1 
ATOM   1816 C  C     . LYS A 1 237 ? 23.33184  -22.08438 -23.77010 1.000 6.88790  ? 237 LYS A C     1 
ATOM   1817 O  O     . LYS A 1 237 ? 22.25985  -22.30838 -23.18009 1.000 6.61036  ? 237 LYS A O     1 
ATOM   1818 C  CB    . LYS A 1 237 ? 24.16583  -19.71537 -23.82512 1.000 6.45884  ? 237 LYS A CB    1 
ATOM   1819 C  CG    . LYS A 1 237 ? 22.76382  -19.15738 -23.84909 1.000 6.31460  ? 237 LYS A CG    1 
ATOM   1820 C  CD    . LYS A 1 237 ? 22.23785  -18.95238 -22.43909 1.000 6.22406  ? 237 LYS A CD    1 
ATOM   1821 C  CE    . LYS A 1 237 ? 21.00584  -18.06539 -22.43306 1.000 6.10310  ? 237 LYS A CE    1 
ATOM   1822 N  NZ    . LYS A 1 237 ? 21.30883  -16.72538 -22.97707 1.000 6.55364  ? 237 LYS A NZ    1 
ATOM   1823 N  N     . PRO A 1 238 ? 23.61282  -22.70038 -24.92811 1.000 12.54534 ? 238 PRO A N     1 
ATOM   1824 C  CA    . PRO A 1 238 ? 22.63681  -23.64538 -25.49609 1.000 10.20455 ? 238 PRO A CA    1 
ATOM   1825 C  C     . PRO A 1 238 ? 22.40483  -24.88038 -24.64909 1.000 7.06884  ? 238 PRO A C     1 
ATOM   1826 O  O     . PRO A 1 238 ? 21.40383  -25.57138 -24.86007 1.000 9.76511  ? 238 PRO A O     1 
ATOM   1827 C  CB    . PRO A 1 238 ? 23.25179  -24.01338 -26.85310 1.000 12.86642 ? 238 PRO A CB    1 
ATOM   1828 C  CG    . PRO A 1 238 ? 24.14478  -22.90337 -27.18312 1.000 11.40547 ? 238 PRO A CG    1 
ATOM   1829 C  CD    . PRO A 1 238 ? 24.70580  -22.42737 -25.87813 1.000 10.34417 ? 238 PRO A CD    1 
ATOM   1830 N  N     . ASP A 1 239 ? 23.28385  -25.18138 -23.70010 1.000 10.79614 ? 239 ASP A N     1 
ATOM   1831 C  CA    . ASP A 1 239 ? 23.17487  -26.38338 -22.88110 1.000 9.23733  ? 239 ASP A CA    1 
ATOM   1832 C  C     . ASP A 1 239 ? 22.43389  -26.15638 -21.56909 1.000 13.07093 ? 239 ASP A C     1 
ATOM   1833 O  O     . ASP A 1 239 ? 22.34790  -27.08638 -20.75709 1.000 14.85060 ? 239 ASP A O     1 
ATOM   1834 C  CB    . ASP A 1 239 ? 24.56787  -26.94337 -22.57513 1.000 8.31447  ? 239 ASP A CB    1 
ATOM   1835 C  CG    . ASP A 1 239 ? 25.32985  -27.34037 -23.82714 1.000 15.07985 ? 239 ASP A CG    1 
ATOM   1836 O  OD1   . ASP A 1 239 ? 24.68784  -27.59337 -24.86413 1.000 15.13534 ? 239 ASP A OD1   1 
ATOM   1837 O  OD2   . ASP A 1 239 ? 26.57685  -27.40437 -23.77016 1.000 20.28320 ? 239 ASP A OD2   1 
ATOM   1838 N  N     . THR A 1 240 ? 21.90289  -24.96038 -21.33508 1.000 7.37308  ? 240 THR A N     1 
ATOM   1839 C  CA    . THR A 1 240 ? 21.25091  -24.67439 -20.06807 1.000 8.01799  ? 240 THR A CA    1 
ATOM   1840 C  C     . THR A 1 240 ? 19.78691  -25.11939 -20.09505 1.000 8.86909  ? 240 THR A C     1 
ATOM   1841 O  O     . THR A 1 240 ? 19.17889  -25.28939 -21.15404 1.000 8.40938  ? 240 THR A O     1 
ATOM   1842 C  CB    . THR A 1 240 ? 21.35391  -23.18839 -19.73107 1.000 7.37129  ? 240 THR A CB    1 
ATOM   1843 O  OG1   . THR A 1 240 ? 20.92689  -22.39739 -20.84806 1.000 8.85802  ? 240 THR A OG1   1 
ATOM   1844 C  CG2   . THR A 1 240 ? 22.78991  -22.83138 -19.38410 1.000 12.44427 ? 240 THR A CG2   1 
ATOM   1845 N  N     . ASP A 1 241 ? 19.22693  -25.30939 -18.89804 1.000 11.09557 ? 241 ASP A N     1 
ATOM   1846 C  CA    . ASP A 1 241 ? 17.94193  -25.98340 -18.73702 1.000 12.31021 ? 241 ASP A CA    1 
ATOM   1847 C  C     . ASP A 1 241 ? 16.81593  -24.96040 -18.70200 1.000 7.73378  ? 241 ASP A C     1 
ATOM   1848 O  O     . ASP A 1 241 ? 16.75194  -24.16240 -17.75900 1.000 9.76936  ? 241 ASP A O     1 
ATOM   1849 C  CB    . ASP A 1 241 ? 17.93096  -26.80840 -17.45602 1.000 11.42596 ? 241 ASP A CB    1 
ATOM   1850 C  CG    . ASP A 1 241 ? 16.73696  -27.75040 -17.36100 1.000 8.83749  ? 241 ASP A CG    1 
ATOM   1851 O  OD1   . ASP A 1 241 ? 15.72095  -27.52741 -18.04898 1.000 9.23647  ? 241 ASP A OD1   1 
ATOM   1852 O  OD2   . ASP A 1 241 ? 16.81998  -28.72740 -16.58900 1.000 15.31069 ? 241 ASP A OD2   1 
ATOM   1853 N  N     . PRO A 1 242 ? 15.90491  -24.96040 -19.67698 1.000 6.92542  ? 242 PRO A N     1 
ATOM   1854 C  CA    . PRO A 1 242 ? 14.79091  -24.00541 -19.63596 1.000 7.63463  ? 242 PRO A CA    1 
ATOM   1855 C  C     . PRO A 1 242 ? 13.73293  -24.35241 -18.60395 1.000 8.66151  ? 242 PRO A C     1 
ATOM   1856 O  O     . PRO A 1 242 ? 12.97093  -23.46341 -18.20193 1.000 7.97303  ? 242 PRO A O     1 
ATOM   1857 C  CB    . PRO A 1 242 ? 14.22389  -24.07741 -21.05695 1.000 7.89640  ? 242 PRO A CB    1 
ATOM   1858 C  CG    . PRO A 1 242 ? 14.52789  -25.45241 -21.49096 1.000 7.35228  ? 242 PRO A CG    1 
ATOM   1859 C  CD    . PRO A 1 242 ? 15.85990  -25.79740 -20.88598 1.000 9.01724  ? 242 PRO A CD    1 
ATOM   1860 N  N     . SER A 1 243 ? 13.65394  -25.60541 -18.16994 1.000 9.28375  ? 243 SER A N     1 
ATOM   1861 C  CA    . SER A 1 243 ? 12.64596  -26.01042 -17.19993 1.000 10.34621 ? 243 SER A CA    1 
ATOM   1862 C  C     . SER A 1 243 ? 13.06198  -25.74242 -15.75793 1.000 10.33402 ? 243 SER A C     1 
ATOM   1863 O  O     . SER A 1 243 ? 12.24800  -25.96642 -14.85692 1.000 14.48690 ? 243 SER A O     1 
ATOM   1864 C  CB    . SER A 1 243 ? 12.31596  -27.49542 -17.37792 1.000 9.05325  ? 243 SER A CB    1 
ATOM   1865 O  OG    . SER A 1 243 ? 13.39397  -28.31641 -16.96594 1.000 13.16960 ? 243 SER A OG    1 
ATOM   1866 N  N     . ALA A 1 244 ? 14.29098  -25.27741 -15.51796 1.000 7.26926  ? 244 ALA A N     1 
ATOM   1867 C  CA    . ALA A 1 244 ? 14.76601  -24.99341 -14.16496 1.000 14.52682 ? 244 ALA A CA    1 
ATOM   1868 C  C     . ALA A 1 244 ? 14.16701  -23.68541 -13.65395 1.000 9.74513  ? 244 ALA A C     1 
ATOM   1869 O  O     . ALA A 1 244 ? 14.39000  -22.61841 -14.24296 1.000 11.21838 ? 244 ALA A O     1 
ATOM   1870 C  CB    . ALA A 1 244 ? 16.29401  -24.92640 -14.13399 1.000 9.75850  ? 244 ALA A CB    1 
ATOM   1871 N  N     . TRP A 1 245 ? 13.42403  -23.76442 -12.55094 1.000 9.47670  ? 245 TRP A N     1 
ATOM   1872 C  CA    . TRP A 1 245 ? 12.74703  -22.59342 -12.01093 1.000 13.64693 ? 245 TRP A CA    1 
ATOM   1873 C  C     . TRP A 1 245 ? 13.08406  -22.37842 -10.53893 1.000 16.45138 ? 245 TRP A C     1 
ATOM   1874 O  O     . TRP A 1 245 ? 13.12606  -21.23442 -10.08493 1.000 12.43188 ? 245 TRP A O     1 
ATOM   1875 C  CB    . TRP A 1 245 ? 11.22503  -22.71842 -12.19290 1.000 10.69295 ? 245 TRP A CB    1 
ATOM   1876 C  CG    . TRP A 1 245 ? 10.61505  -23.88842 -11.49189 1.000 18.30895 ? 245 TRP A CG    1 
ATOM   1877 C  CD1   . TRP A 1 245 ? 10.39804  -25.12943 -12.01089 1.000 15.20498 ? 245 TRP A CD1   1 
ATOM   1878 C  CD2   . TRP A 1 245 ? 10.13307  -23.92843 -10.14389 1.000 17.26677 ? 245 TRP A CD2   1 
ATOM   1879 N  NE1   . TRP A 1 245 ? 9.81906   -25.94043 -11.07088 1.000 11.16621 ? 245 TRP A NE1   1 
ATOM   1880 C  CE2   . TRP A 1 245 ? 9.64508   -25.22743 -9.91388  1.000 17.24385 ? 245 TRP A CE2   1 
ATOM   1881 C  CE3   . TRP A 1 245 ? 10.07308  -22.99243 -9.10688  1.000 22.70387 ? 245 TRP A CE3   1 
ATOM   1882 C  CZ2   . TRP A 1 245 ? 9.09910   -25.61743 -8.68887  1.000 22.44318 ? 245 TRP A CZ2   1 
ATOM   1883 C  CZ3   . TRP A 1 245 ? 9.53110   -23.37543 -7.89488  1.000 21.66456 ? 245 TRP A CZ3   1 
ATOM   1884 C  CH2   . TRP A 1 245 ? 9.05211   -24.68043 -7.69487  1.000 25.00562 ? 245 TRP A CH2   1 
ATOM   1885 N  N     . GLU A 1 246 ? 13.31807  -23.45942 -9.78294  1.000 14.90211 ? 246 GLU A N     1 
ATOM   1886 C  CA    . GLU A 1 246 ? 13.80310  -23.30542 -8.41395  1.000 13.65798 ? 246 GLU A CA    1 
ATOM   1887 C  C     . GLU A 1 246 ? 15.13909  -22.57341 -8.39897  1.000 15.03814 ? 246 GLU A C     1 
ATOM   1888 O  O     . GLU A 1 246 ? 15.30310  -21.55541 -7.71697  1.000 16.63248 ? 246 GLU A O     1 
ATOM   1889 C  CB    . GLU A 1 246 ? 13.93711  -24.67241 -7.74295  1.000 17.47692 ? 246 GLU A CB    1 
ATOM   1890 C  CG    . GLU A 1 246 ? 12.62312  -25.32242 -7.36393  1.000 23.65430 ? 246 GLU A CG    1 
ATOM   1891 C  CD    . GLU A 1 246 ? 12.81513  -26.68442 -6.72793  1.000 27.41862 ? 246 GLU A CD    1 
ATOM   1892 O  OE1   . GLU A 1 246 ? 13.16313  -27.64242 -7.45094  1.000 39.57589 ? 246 GLU A OE1   1 
ATOM   1893 O  OE2   . GLU A 1 246 ? 12.63116  -26.79942 -5.49993  1.000 28.84459 ? 246 GLU A OE2   1 
ATOM   1894 N  N     . LYS A 1 247 ? 16.11008  -23.08741 -9.14298  1.000 17.55900 ? 247 LYS A N     1 
ATOM   1895 C  CA    . LYS A 1 247 ? 17.38008  -22.40540 -9.37701  1.000 16.15933 ? 247 LYS A CA    1 
ATOM   1896 C  C     . LYS A 1 247 ? 17.52205  -22.21240 -10.87801 1.000 8.27828  ? 247 LYS A C     1 
ATOM   1897 O  O     . LYS A 1 247 ? 17.89904  -23.15940 -11.59101 1.000 12.12405 ? 247 LYS A O     1 
ATOM   1898 C  CB    . LYS A 1 247 ? 18.54909  -23.21340 -8.82003  1.000 19.78412 ? 247 LYS A CB    1 
ATOM   1899 C  CG    . LYS A 1 247 ? 19.88209  -22.47439 -8.80405  1.000 16.23663 ? 247 LYS A CG    1 
ATOM   1900 C  CD    . LYS A 1 247 ? 19.95510  -21.47939 -7.65305  0.000 15.76028 ? 247 LYS A CD    1 
ATOM   1901 C  CE    . LYS A 1 247 ? 19.43513  -22.08540 -6.35104  0.000 16.58119 ? 247 LYS A CE    1 
ATOM   1902 N  NZ    . LYS A 1 247 ? 20.11914  -23.35839 -5.98105  0.000 17.16394 ? 247 LYS A NZ    1 
ATOM   1903 N  N     . PRO A 1 248 ? 17.21404  -21.02840 -11.40600 1.000 7.81386  ? 248 PRO A N     1 
ATOM   1904 C  CA    . PRO A 1 248 ? 17.30801  -20.82440 -12.85600 1.000 6.98098  ? 248 PRO A CA    1 
ATOM   1905 C  C     . PRO A 1 248 ? 18.71001  -21.11040 -13.36803 1.000 11.61216 ? 248 PRO A C     1 
ATOM   1906 O  O     . PRO A 1 248 ? 19.70902  -20.81739 -12.70504 1.000 9.88944  ? 248 PRO A O     1 
ATOM   1907 C  CB    . PRO A 1 248 ? 16.93000  -19.34940 -13.03500 1.000 8.71432  ? 248 PRO A CB    1 
ATOM   1908 C  CG    . PRO A 1 248 ? 16.09902  -19.03041 -11.84998 1.000 10.91109 ? 248 PRO A CG    1 
ATOM   1909 C  CD    . PRO A 1 248 ? 16.68605  -19.84040 -10.71799 1.000 9.83330  ? 248 PRO A CD    1 
ATOM   1910 N  N     . ALA A 1 249 ? 18.76499  -21.70240 -14.56703 1.000 8.11728  ? 249 ALA A N     1 
ATOM   1911 C  CA    . ALA A 1 249 ? 20.00398  -22.23139 -15.11805 1.000 8.11597  ? 249 ALA A CA    1 
ATOM   1912 C  C     . ALA A 1 249 ? 20.95997  -21.13839 -15.56806 1.000 7.09848  ? 249 ALA A C     1 
ATOM   1913 O  O     . ALA A 1 249 ? 22.13797  -21.42238 -15.79808 1.000 8.01020  ? 249 ALA A O     1 
ATOM   1914 C  CB    . ALA A 1 249 ? 19.69296  -23.16039 -16.29104 1.000 9.29963  ? 249 ALA A CB    1 
ATOM   1915 N  N     . THR A 1 250 ? 20.48496  -19.91139 -15.71706 1.000 6.50907  ? 250 THR A N     1 
ATOM   1916 C  CA    . THR A 1 250 ? 21.32795  -18.79839 -16.11107 1.000 6.39475  ? 250 THR A CA    1 
ATOM   1917 C  C     . THR A 1 250 ? 21.36397  -17.77439 -14.97007 1.000 7.44543  ? 250 THR A C     1 
ATOM   1918 O  O     . THR A 1 250 ? 20.86399  -18.02439 -13.87106 1.000 7.28105  ? 250 THR A O     1 
ATOM   1919 C  CB    . THR A 1 250 ? 20.84293  -18.22139 -17.44406 1.000 6.22844  ? 250 THR A CB    1 
ATOM   1920 O  OG1   . THR A 1 250 ? 19.46193  -17.85839 -17.35004 1.000 6.18051  ? 250 THR A OG1   1 
ATOM   1921 C  CG2   . THR A 1 250 ? 21.00191  -19.26039 -18.55606 1.000 6.51796  ? 250 THR A CG2   1 
ATOM   1922 N  N     . THR A 1 251 ? 21.97896  -16.61839 -15.23408 1.000 6.34788  ? 251 THR A N     1 
ATOM   1923 C  CA    . THR A 1 251 ? 22.26297  -15.65538 -14.17208 1.000 6.42891  ? 251 THR A CA    1 
ATOM   1924 C  C     . THR A 1 251 ? 21.03498  -14.85339 -13.74306 1.000 7.24221  ? 251 THR A C     1 
ATOM   1925 O  O     . THR A 1 251 ? 20.98300  -14.37739 -12.60206 1.000 6.55754  ? 251 THR A O     1 
ATOM   1926 C  CB    . THR A 1 251 ? 23.35396  -14.68638 -14.61910 1.000 6.38875  ? 251 THR A CB    1 
ATOM   1927 O  OG1   . THR A 1 251 ? 22.88394  -13.93638 -15.74309 1.000 6.23311  ? 251 THR A OG1   1 
ATOM   1928 C  CG2   . THR A 1 251 ? 24.61796  -15.43738 -15.00412 1.000 6.44980  ? 251 THR A CG2   1 
ATOM   1929 N  N     . VAL A 1 252 ? 20.05796  -14.68739 -14.63405 1.000 6.28623  ? 252 VAL A N     1 
ATOM   1930 C  CA    . VAL A 1 252 ? 18.88796  -13.83740 -14.42103 1.000 6.34769  ? 252 VAL A CA    1 
ATOM   1931 C  C     . VAL A 1 252 ? 19.35296  -12.42739 -14.07504 1.000 6.32803  ? 252 VAL A C     1 
ATOM   1932 O  O     . VAL A 1 252 ? 18.77798  -11.75340 -13.21003 1.000 6.45172  ? 252 VAL A O     1 
ATOM   1933 C  CB    . VAL A 1 252 ? 17.94998  -14.40740 -13.33901 1.000 7.82884  ? 252 VAL A CB    1 
ATOM   1934 C  CG1   . VAL A 1 252 ? 16.55598  -13.81140 -13.47299 1.000 7.32167  ? 252 VAL A CG1   1 
ATOM   1935 C  CG2   . VAL A 1 252 ? 17.86899  -15.91340 -13.45501 1.000 6.47496  ? 252 VAL A CG2   1 
ATOM   1936 N  N     . LEU A 1 253 ? 20.39595  -11.96839 -14.75205 1.000 6.25872  ? 253 LEU A N     1 
ATOM   1937 C  CA    . LEU A 1 253 ? 20.85695  -10.59839 -14.59806 1.000 6.31067  ? 253 LEU A CA    1 
ATOM   1938 C  C     . LEU A 1 253 ? 20.23993  -9.65939  -15.61905 1.000 6.23770  ? 253 LEU A C     1 
ATOM   1939 O  O     . LEU A 1 253 ? 20.51793  -8.45639  -15.57805 1.000 7.70219  ? 253 LEU A O     1 
ATOM   1940 C  CB    . LEU A 1 253 ? 22.38795  -10.54438 -14.68909 1.000 6.33564  ? 253 LEU A CB    1 
ATOM   1941 C  CG    . LEU A 1 253 ? 23.13597  -11.08838 -13.47210 1.000 6.49324  ? 253 LEU A CG    1 
ATOM   1942 C  CD1   . LEU A 1 253 ? 24.64197  -11.11838 -13.71212 1.000 6.53595  ? 253 LEU A CD1   1 
ATOM   1943 C  CD2   . LEU A 1 253 ? 22.80599  -10.25838 -12.25209 1.000 8.55268  ? 253 LEU A CD2   1 
ATOM   1944 N  N     . SER A 1 254 ? 19.39292  -10.17339 -16.51604 1.000 6.73585  ? 254 SER A N     1 
ATOM   1945 C  CA    . SER A 1 254 ? 18.84590  -9.34439  -17.58803 1.000 6.82410  ? 254 SER A CA    1 
ATOM   1946 C  C     . SER A 1 254 ? 18.00390  -8.16440  -17.11001 1.000 6.22870  ? 254 SER A C     1 
ATOM   1947 O  O     . SER A 1 254 ? 18.14589  -7.07840  -17.69901 1.000 6.27598  ? 254 SER A O     1 
ATOM   1948 C  CB    . SER A 1 254 ? 18.05088  -10.21240 -18.57701 1.000 6.02576  ? 254 SER A CB    1 
ATOM   1949 O  OG    . SER A 1 254 ? 16.99289  -10.92140 -17.95700 1.000 6.05393  ? 254 SER A OG    1 
ATOM   1950 N  N     . PRO A 1 255 ? 17.13292  -8.27540  -16.09800 1.000 7.24795  ? 255 PRO A N     1 
ATOM   1951 C  CA    . PRO A 1 255 ? 16.38492  -7.07540  -15.68798 1.000 8.85475  ? 255 PRO A CA    1 
ATOM   1952 C  C     . PRO A 1 255 ? 17.27793  -6.01340  -15.07700 1.000 7.14360  ? 255 PRO A C     1 
ATOM   1953 O  O     . PRO A 1 255 ? 16.99192  -4.81640  -15.21799 1.000 6.74502  ? 255 PRO A O     1 
ATOM   1954 C  CB    . PRO A 1 255 ? 15.36194  -7.60941  -14.67297 1.000 6.59801  ? 255 PRO A CB    1 
ATOM   1955 C  CG    . PRO A 1 255 ? 15.39994  -9.10541  -14.81197 1.000 7.64812  ? 255 PRO A CG    1 
ATOM   1956 C  CD    . PRO A 1 255 ? 16.78793  -9.42740  -15.24899 1.000 6.39603  ? 255 PRO A CD    1 
ATOM   1957 N  N     . TYR A 1 256 ? 18.36294  -6.42240  -14.41702 1.000 6.60924  ? 256 TYR A N     1 
ATOM   1958 C  CA    . TYR A 1 256 ? 19.30094  -5.48039  -13.82203 1.000 6.75482  ? 256 TYR A CA    1 
ATOM   1959 C  C     . TYR A 1 256 ? 20.19292  -4.82939  -14.86905 1.000 6.69950  ? 256 TYR A C     1 
ATOM   1960 O  O     . TYR A 1 256 ? 20.56992  -3.66239  -14.71505 1.000 6.85658  ? 256 TYR A O     1 
ATOM   1961 C  CB    . TYR A 1 256 ? 20.14496  -6.19139  -12.76505 1.000 6.81286  ? 256 TYR A CB    1 
ATOM   1962 C  CG    . TYR A 1 256 ? 19.30598  -6.95540  -11.77603 1.000 7.98077  ? 256 TYR A CG    1 
ATOM   1963 C  CD1   . TYR A 1 256 ? 18.70000  -6.30640  -10.71302 1.000 7.85634  ? 256 TYR A CD1   1 
ATOM   1964 C  CD2   . TYR A 1 256 ? 19.09899  -8.31940  -11.91803 1.000 8.28307  ? 256 TYR A CD2   1 
ATOM   1965 C  CE1   . TYR A 1 256 ? 17.92202  -6.99040  -9.81201  1.000 10.67124 ? 256 TYR A CE1   1 
ATOM   1966 C  CE2   . TYR A 1 256 ? 18.31700  -9.01540  -11.01402 1.000 9.59092  ? 256 TYR A CE2   1 
ATOM   1967 C  CZ    . TYR A 1 256 ? 17.73102  -8.34140  -9.96501  1.000 7.14740  ? 256 TYR A CZ    1 
ATOM   1968 O  OH    . TYR A 1 256 ? 16.95604  -9.01340  -9.05599  1.000 10.36306 ? 256 TYR A OH    1 
ATOM   1969 N  N     . LEU A 1 257 ? 20.52791  -5.55639  -15.93605 1.000 6.51891  ? 257 LEU A N     1 
ATOM   1970 C  CA    . LEU A 1 257 ? 21.27589  -4.95239  -17.03006 1.000 6.96904  ? 257 LEU A CA    1 
ATOM   1971 C  C     . LEU A 1 257 ? 20.39287  -4.03739  -17.87605 1.000 6.56387  ? 257 LEU A C     1 
ATOM   1972 O  O     . LEU A 1 257 ? 20.87986  -3.03939  -18.41006 1.000 11.52084 ? 257 LEU A O     1 
ATOM   1973 C  CB    . LEU A 1 257 ? 21.91388  -6.04538  -17.88808 1.000 6.35070  ? 257 LEU A CB    1 
ATOM   1974 C  CG    . LEU A 1 257 ? 23.09089  -6.77938  -17.24410 1.000 6.35185  ? 257 LEU A CG    1 
ATOM   1975 C  CD1   . LEU A 1 257 ? 23.46188  -8.00138  -18.06710 1.000 11.81796 ? 257 LEU A CD1   1 
ATOM   1976 C  CD2   . LEU A 1 257 ? 24.29189  -5.85638  -17.09912 1.000 6.57436  ? 257 LEU A CD2   1 
ATOM   1977 N  N     . LYS A 1 258 ? 19.09587  -4.34139  -17.97903 1.000 7.48935  ? 258 LYS A N     1 
ATOM   1978 C  CA    . LYS A 1 258 ? 18.17286  -3.49940  -18.74101 1.000 6.63472  ? 258 LYS A CA    1 
ATOM   1979 C  C     . LYS A 1 258 ? 17.99986  -2.13040  -18.08901 1.000 8.98286  ? 258 LYS A C     1 
ATOM   1980 O  O     . LYS A 1 258 ? 18.08985  -1.09540  -18.76101 1.000 7.01436  ? 258 LYS A O     1 
ATOM   1981 C  CB    . LYS A 1 258 ? 16.82486  -4.21340  -18.88599 1.000 6.58229  ? 258 LYS A CB    1 
ATOM   1982 C  CG    . LYS A 1 258 ? 15.68784  -3.38541  -19.51397 1.000 9.68914  ? 258 LYS A CG    1 
ATOM   1983 C  CD    . LYS A 1 258 ? 14.80386  -2.75241  -18.43896 1.000 7.19443  ? 258 LYS A CD    1 
ATOM   1984 C  CE    . LYS A 1 258 ? 13.60085  -2.03341  -19.01994 1.000 8.30908  ? 258 LYS A CE    1 
ATOM   1985 N  NZ    . LYS A 1 258 ? 13.95582  -1.30341  -20.26794 1.000 15.43799 ? 258 LYS A NZ    1 
ATOM   1986 N  N     . PHE A 1 259 ? 17.72988  -2.10440  -16.78100 1.000 7.70687  ? 259 PHE A N     1 
ATOM   1987 C  CA    . PHE A 1 259 ? 17.57289  -0.84740  -16.05700 1.000 7.38793  ? 259 PHE A CA    1 
ATOM   1988 C  C     . PHE A 1 259 ? 18.90290  -0.22540  -15.64302 1.000 7.81630  ? 259 PHE A C     1 
ATOM   1989 O  O     . PHE A 1 259 ? 18.90690  0.88460   -15.09802 1.000 8.51296  ? 259 PHE A O     1 
ATOM   1990 C  CB    . PHE A 1 259 ? 16.69591  -1.05440  -14.81899 1.000 10.75227 ? 259 PHE A CB    1 
ATOM   1991 C  CG    . PHE A 1 259 ? 15.22391  -1.16441  -15.12096 1.000 7.39966  ? 259 PHE A CG    1 
ATOM   1992 C  CD1   . PHE A 1 259 ? 14.47790  -0.03341  -15.41195 1.000 12.39614 ? 259 PHE A CD1   1 
ATOM   1993 C  CD2   . PHE A 1 259 ? 14.58491  -2.38741  -15.09495 1.000 9.59112  ? 259 PHE A CD2   1 
ATOM   1994 C  CE1   . PHE A 1 259 ? 13.12990  -0.12342  -15.67993 1.000 9.83352  ? 259 PHE A CE1   1 
ATOM   1995 C  CE2   . PHE A 1 259 ? 13.22391  -2.48141  -15.35993 1.000 9.73285  ? 259 PHE A CE2   1 
ATOM   1996 C  CZ    . PHE A 1 259 ? 12.50290  -1.35142  -15.65892 1.000 11.01818 ? 259 PHE A CZ    1 
ATOM   1997 N  N     . GLY A 1 260 ? 20.02389  -0.90339  -15.88404 1.000 7.32546  ? 260 GLY A N     1 
ATOM   1998 C  CA    . GLY A 1 260 ? 21.30590  -0.39139  -15.45406 1.000 8.84128  ? 260 GLY A CA    1 
ATOM   1999 C  C     . GLY A 1 260 ? 21.58093  -0.49539  -13.97307 1.000 7.41729  ? 260 GLY A C     1 
ATOM   2000 O  O     . GLY A 1 260 ? 22.46793  0.20662   -13.47408 1.000 7.60593  ? 260 GLY A O     1 
ATOM   2001 N  N     . CYS A 1 261 ? 20.84894  -1.34839  -13.24806 1.000 7.36387  ? 261 CYS A N     1 
ATOM   2002 C  CA    . CYS A 1 261 ? 21.20796  -1.62139  -11.85906 1.000 7.96697  ? 261 CYS A CA    1 
ATOM   2003 C  C     . CYS A 1 261 ? 22.55997  -2.31738  -11.76009 1.000 7.43270  ? 261 CYS A C     1 
ATOM   2004 O  O     . CYS A 1 261 ? 23.23398  -2.21338  -10.72910 1.000 9.97528  ? 261 CYS A O     1 
ATOM   2005 C  CB    . CYS A 1 261 ? 20.12998  -2.47739  -11.18304 1.000 7.73740  ? 261 CYS A CB    1 
ATOM   2006 S  SG    . CYS A 1 261 ? 18.45997  -1.80440  -11.28802 1.000 8.60243  ? 261 CYS A SG    1 
ATOM   2007 N  N     . LEU A 1 262 ? 22.96395  -3.04038  -12.80509 1.000 9.07373  ? 262 LEU A N     1 
ATOM   2008 C  CA    . LEU A 1 262 ? 24.27595  -3.67038  -12.86811 1.000 7.14022  ? 262 LEU A CA    1 
ATOM   2009 C  C     . LEU A 1 262 ? 25.03093  -3.13038  -14.07513 1.000 7.09203  ? 262 LEU A C     1 
ATOM   2010 O  O     . LEU A 1 262 ? 24.46891  -3.01238  -15.16712 1.000 6.97006  ? 262 LEU A O     1 
ATOM   2011 C  CB    . LEU A 1 262 ? 24.16196  -5.19938  -12.94511 1.000 6.95529  ? 262 LEU A CB    1 
ATOM   2012 C  CG    . LEU A 1 262 ? 25.48396  -5.96237  -13.05814 1.000 6.93339  ? 262 LEU A CG    1 
ATOM   2013 C  CD1   . LEU A 1 262 ? 26.35598  -5.78437  -11.80615 1.000 7.88951  ? 262 LEU A CD1   1 
ATOM   2014 C  CD2   . LEU A 1 262 ? 25.24796  -7.43437  -13.35513 1.000 11.49435 ? 262 LEU A CD2   1 
ATOM   2015 N  N     . SER A 1 263 ? 26.29793  -2.79537  -13.87115 1.000 8.98906  ? 263 SER A N     1 
ATOM   2016 C  CA    . SER A 1 263 ? 27.15392  -2.34337  -14.95616 1.000 7.23668  ? 263 SER A CA    1 
ATOM   2017 C  C     . SER A 1 263 ? 27.58190  -3.51937  -15.82517 1.000 7.05018  ? 263 SER A C     1 
ATOM   2018 O  O     . SER A 1 263 ? 28.08392  -4.52736  -15.31618 1.000 7.00853  ? 263 SER A O     1 
ATOM   2019 C  CB    . SER A 1 263 ? 28.39092  -1.63936  -14.39618 1.000 8.53707  ? 263 SER A CB    1 
ATOM   2020 O  OG    . SER A 1 263 ? 29.35390  -1.43236  -15.41120 1.000 7.50297  ? 263 SER A OG    1 
ATOM   2021 N  N     . ALA A 1 264 ? 27.39888  -3.37437  -17.14217 1.000 6.94771  ? 264 ALA A N     1 
ATOM   2022 C  CA    . ALA A 1 264 ? 27.91287  -4.36836  -18.07917 1.000 7.85560  ? 264 ALA A CA    1 
ATOM   2023 C  C     . ALA A 1 264 ? 29.43187  -4.44636  -18.02320 1.000 8.81495  ? 264 ALA A C     1 
ATOM   2024 O  O     . ALA A 1 264 ? 30.01187  -5.53136  -18.16521 1.000 6.91915  ? 264 ALA A O     1 
ATOM   2025 C  CB    . ALA A 1 264 ? 27.44785  -4.04637  -19.50017 1.000 10.82006 ? 264 ALA A CB    1 
ATOM   2026 N  N     . ARG A 1 265 ? 30.09481  -3.30634  -17.81425 1.000 8.14604  ? 265 ARG A N     1 
ATOM   2027 C  CA    . ARG A 1 265 ? 31.55182  -3.30137  -17.74421 1.000 11.07846 ? 265 ARG A CA    1 
ATOM   2028 C  C     . ARG A 1 265 ? 32.04634  -4.00609  -16.48887 1.000 8.95410  ? 265 ARG A C     1 
ATOM   2029 O  O     . ARG A 1 265 ? 33.05829  -4.71345  -16.52884 1.000 7.66531  ? 265 ARG A O     1 
ATOM   2030 C  CB    . ARG A 1 265 ? 32.07396  -1.86691  -17.80799 1.000 9.05668  ? 265 ARG A CB    1 
ATOM   2031 C  CG    . ARG A 1 265 ? 31.96376  -1.25610  -19.19230 1.000 9.50741  ? 265 ARG A CG    1 
ATOM   2032 C  CD    . ARG A 1 265 ? 32.25656  0.23164   -19.19161 1.000 10.05348 ? 265 ARG A CD    1 
ATOM   2033 N  NE    . ARG A 1 265 ? 32.07040  0.79212   -20.52400 1.000 9.64618  ? 265 ARG A NE    1 
ATOM   2034 C  CZ    . ARG A 1 265 ? 32.07136  2.08693   -20.80327 1.000 10.92980 ? 265 ARG A CZ    1 
ATOM   2035 N  NH1   . ARG A 1 265 ? 32.24054  2.99595   -19.85937 1.000 8.39961  ? 265 ARG A NH1   1 
ATOM   2036 N  NH2   . ARG A 1 265 ? 31.89846  2.47854   -22.06287 1.000 14.00963 ? 265 ARG A NH2   1 
ATOM   2037 N  N     . LEU A 1 266 ? 31.34791  -3.82435  -15.36623 1.000 7.73321  ? 266 LEU A N     1 
ATOM   2038 C  CA    . LEU A 1 266 ? 31.68294  -4.57235  -14.15824 1.000 8.38014  ? 266 LEU A CA    1 
ATOM   2039 C  C     . LEU A 1 266 ? 31.50994  -6.06935  -14.38724 1.000 8.38181  ? 266 LEU A C     1 
ATOM   2040 O  O     . LEU A 1 266 ? 32.37795  -6.87035  -14.02325 1.000 11.03145 ? 266 LEU A O     1 
ATOM   2041 C  CB    . LEU A 1 266 ? 30.81495  -4.09936  -12.98922 1.000 7.58436  ? 266 LEU A CB    1 
ATOM   2042 C  CG    . LEU A 1 266 ? 31.10198  -4.78736  -11.64523 1.000 16.22154 ? 266 LEU A CG    1 
ATOM   2043 C  CD1   . LEU A 1 266 ? 32.54598  -4.54935  -11.21325 1.000 12.37103 ? 266 LEU A CD1   1 
ATOM   2044 C  CD2   . LEU A 1 266 ? 30.13599  -4.33436  -10.56121 1.000 12.82907 ? 266 LEU A CD2   1 
ATOM   2045 N  N     . PHE A 1 267 ? 30.37993  -6.46036  -14.98122 1.000 9.69547  ? 267 PHE A N     1 
ATOM   2046 C  CA    . PHE A 1 267 ? 30.15893  -7.85436  -15.35821 1.000 10.21323 ? 267 PHE A CA    1 
ATOM   2047 C  C     . PHE A 1 267 ? 31.30391  -8.36235  -16.22523 1.000 9.19887  ? 267 PHE A C     1 
ATOM   2048 O  O     . PHE A 1 267 ? 31.88992  -9.41435  -15.94824 1.000 11.13223 ? 267 PHE A O     1 
ATOM   2049 C  CB    . PHE A 1 267 ? 28.81392  -7.97536  -16.08519 1.000 8.83503  ? 267 PHE A CB    1 
ATOM   2050 C  CG    . PHE A 1 267 ? 28.27392  -9.38536  -16.19018 1.000 9.96026  ? 267 PHE A CG    1 
ATOM   2051 C  CD1   . PHE A 1 267 ? 29.00793  -10.48136 -15.77420 1.000 9.70868  ? 267 PHE A CD1   1 
ATOM   2052 C  CD2   . PHE A 1 267 ? 27.01591  -9.60437  -16.72916 1.000 13.26948 ? 267 PHE A CD2   1 
ATOM   2053 C  CE1   . PHE A 1 267 ? 28.49693  -11.76736 -15.88719 1.000 13.06215 ? 267 PHE A CE1   1 
ATOM   2054 C  CE2   . PHE A 1 267 ? 26.49891  -10.89237 -16.84415 1.000 9.82242  ? 267 PHE A CE2   1 
ATOM   2055 C  CZ    . PHE A 1 267 ? 27.23992  -11.96937 -16.41917 1.000 9.26313  ? 267 PHE A CZ    1 
ATOM   2056 N  N     . HIS A 1 268 ? 31.66189  -7.59935  -17.26324 1.000 8.10357  ? 268 HIS A N     1 
ATOM   2057 C  CA    . HIS A 1 268 ? 32.73088  -8.02335  -18.16126 1.000 7.10897  ? 268 HIS A CA    1 
ATOM   2058 C  C     . HIS A 1 268 ? 34.06789  -8.11434  -17.43128 1.000 10.30271 ? 268 HIS A C     1 
ATOM   2059 O  O     . HIS A 1 268 ? 34.84689  -9.04434  -17.66829 1.000 8.46894  ? 268 HIS A O     1 
ATOM   2060 C  CB    . HIS A 1 268 ? 32.82086  -7.06735  -19.35826 1.000 7.47669  ? 268 HIS A CB    1 
ATOM   2061 C  CG    . HIS A 1 268 ? 33.64984  -7.58834  -20.49427 1.000 13.36250 ? 268 HIS A CG    1 
ATOM   2062 N  ND1   . HIS A 1 268 ? 35.02584  -7.53234  -20.49829 1.000 7.46360  ? 268 HIS A ND1   1 
ATOM   2063 C  CD2   . HIS A 1 268 ? 33.29482  -8.17234  -21.66427 1.000 10.03696 ? 268 HIS A CD2   1 
ATOM   2064 C  CE1   . HIS A 1 268 ? 35.48382  -8.06034  -21.61930 1.000 8.29340  ? 268 HIS A CE1   1 
ATOM   2065 N  NE2   . HIS A 1 268 ? 34.45381  -8.45634  -22.34428 1.000 10.25756 ? 268 HIS A NE2   1 
ATOM   2066 N  N     . ALA A 1 269 ? 34.34891  -7.17034  -16.52828 1.000 8.09860  ? 269 ALA A N     1 
ATOM   2067 C  CA    . ALA A 1 269 ? 35.63592  -7.18034  -15.83430 1.000 13.31470 ? 269 ALA A CA    1 
ATOM   2068 C  C     . ALA A 1 269 ? 35.75794  -8.37134  -14.88431 1.000 12.12877 ? 269 ALA A C     1 
ATOM   2069 O  O     . ALA A 1 269 ? 36.83794  -8.96233  -14.75632 1.000 8.16021  ? 269 ALA A O     1 
ATOM   2070 C  CB    . ALA A 1 269 ? 35.83692  -5.86634  -15.08531 1.000 10.56760 ? 269 ALA A CB    1 
ATOM   2071 N  N     . ARG A 1 270 ? 34.66487  -8.73466  -14.20778 1.000 10.30641 ? 270 ARG A N     1 
ATOM   2072 C  CA    . ARG A 1 270 ? 34.68374  -9.91567  -13.34908 1.000 11.83965 ? 270 ARG A CA    1 
ATOM   2073 C  C     . ARG A 1 270 ? 34.86117  -11.18878 -14.16632 1.000 11.67985 ? 270 ARG A C     1 
ATOM   2074 O  O     . ARG A 1 270 ? 35.51931  -12.13543 -13.71762 1.000 16.02586 ? 270 ARG A O     1 
ATOM   2075 C  CB    . ARG A 1 270 ? 33.39871  -9.98581  -12.52515 1.000 10.94024 ? 270 ARG A CB    1 
ATOM   2076 C  CG    . ARG A 1 270 ? 33.22131  -8.84229  -11.54543 1.000 13.57172 ? 270 ARG A CG    1 
ATOM   2077 C  CD    . ARG A 1 270 ? 34.15698  -8.97778  -10.35689 1.000 18.63296 ? 270 ARG A CD    1 
ATOM   2078 N  NE    . ARG A 1 270 ? 33.91224  -10.20502 -9.60842  1.000 23.03289 ? 270 ARG A NE    1 
ATOM   2079 C  CZ    . ARG A 1 270 ? 32.96114  -10.34928 -8.69568  1.000 22.19997 ? 270 ARG A CZ    1 
ATOM   2080 N  NH1   . ARG A 1 270 ? 32.12885  -9.36353  -8.40252  1.000 16.42566 ? 270 ARG A NH1   1 
ATOM   2081 N  NH2   . ARG A 1 270 ? 32.84152  -11.51262 -8.06144  1.000 25.86053 ? 270 ARG A NH2   1 
ATOM   2082 N  N     . LEU A 1 271 ? 34.27194  -11.23134 -15.36428 1.000 8.75287  ? 271 LEU A N     1 
ATOM   2083 C  CA    . LEU A 1 271 ? 34.44693  -12.37834 -16.24929 1.000 7.51952  ? 271 LEU A CA    1 
ATOM   2084 C  C     . LEU A 1 271 ? 35.91392  -12.59034 -16.60331 1.000 12.06493 ? 271 LEU A C     1 
ATOM   2085 O  O     . LEU A 1 271 ? 36.42193  -13.71434 -16.52132 1.000 15.92130 ? 271 LEU A O     1 
ATOM   2086 C  CB    . LEU A 1 271 ? 33.61491  -12.19034 -17.51527 1.000 7.21127  ? 271 LEU A CB    1 
ATOM   2087 C  CG    . LEU A 1 271 ? 32.10691  -12.38235 -17.36425 1.000 7.02593  ? 271 LEU A CG    1 
ATOM   2088 C  CD1   . LEU A 1 271 ? 31.43489  -11.92235 -18.62024 1.000 8.83359  ? 271 LEU A CD1   1 
ATOM   2089 C  CD2   . LEU A 1 271 ? 31.76292  -13.83335 -17.07724 1.000 8.58413  ? 271 LEU A CD2   1 
ATOM   2090 N  N     . LEU A 1 272 ? 36.61291  -11.52233 -17.00432 1.000 8.38258  ? 272 LEU A N     1 
ATOM   2091 C  CA    . LEU A 1 272 ? 38.01591  -11.65933 -17.39035 1.000 11.99477 ? 272 LEU A CA    1 
ATOM   2092 C  C     . LEU A 1 272 ? 38.87093  -12.15833 -16.23136 1.000 11.02833 ? 272 LEU A C     1 
ATOM   2093 O  O     . LEU A 1 272 ? 39.81793  -12.92532 -16.43938 1.000 11.73164 ? 272 LEU A O     1 
ATOM   2094 C  CB    . LEU A 1 272 ? 38.55489  -10.33233 -17.92135 1.000 11.24595 ? 272 LEU A CB    1 
ATOM   2095 C  CG    . LEU A 1 272 ? 37.95387  -9.85533  -19.24534 1.000 14.89109 ? 272 LEU A CG    1 
ATOM   2096 C  CD1   . LEU A 1 272 ? 38.62286  -8.56433  -19.71735 1.000 15.27970 ? 272 LEU A CD1   1 
ATOM   2097 C  CD2   . LEU A 1 272 ? 38.05386  -10.94233 -20.30735 1.000 17.32280 ? 272 LEU A CD2   1 
ATOM   2098 N  N     . GLU A 1 273 ? 38.54995  -11.74033 -15.00135 1.000 13.47088 ? 273 GLU A N     1 
ATOM   2099 C  CA    . GLU A 1 273 ? 39.30097  -12.21533 -13.84237 1.000 16.81769 ? 273 GLU A CA    1 
ATOM   2100 C  C     . GLU A 1 273 ? 39.18897  -13.72633 -13.69137 1.000 11.42517 ? 273 GLU A C     1 
ATOM   2101 O  O     . GLU A 1 273 ? 40.15798  -14.39132 -13.30338 1.000 18.37014 ? 273 GLU A O     1 
ATOM   2102 C  CB    . GLU A 1 273 ? 38.81299  -11.52133 -12.56936 1.000 22.17652 ? 273 GLU A CB    1 
ATOM   2103 C  CG    . GLU A 1 273 ? 39.20098  -10.06133 -12.44636 1.000 21.57964 ? 273 GLU A CG    1 
ATOM   2104 C  CD    . GLU A 1 273 ? 38.50900  -9.38933  -11.27835 1.000 27.96174 ? 273 GLU A CD    1 
ATOM   2105 O  OE1   . GLU A 1 273 ? 37.96302  -10.11133 -10.41434 1.000 27.18921 ? 273 GLU A OE1   1 
ATOM   2106 O  OE2   . GLU A 1 273 ? 38.50100  -8.14033  -11.22735 1.000 35.52969 ? 273 GLU A OE2   1 
ATOM   2107 N  N     . VAL A 1 274 ? 38.01297  -14.28633 -13.98535 1.000 13.93426 ? 274 VAL A N     1 
ATOM   2108 C  CA    . VAL A 1 274 ? 37.82898  -15.73133 -13.88734 1.000 14.83071 ? 274 VAL A CA    1 
ATOM   2109 C  C     . VAL A 1 274 ? 38.45796  -16.43633 -15.08335 1.000 13.22814 ? 274 VAL A C     1 
ATOM   2110 O  O     . VAL A 1 274 ? 39.08897  -17.48833 -14.93436 1.000 12.81568 ? 274 VAL A O     1 
ATOM   2111 C  CB    . VAL A 1 274 ? 36.33498  -16.07834 -13.74532 1.000 15.87041 ? 274 VAL A CB    1 
ATOM   2112 C  CG1   . VAL A 1 274 ? 36.12999  -17.58134 -13.82632 1.000 14.31533 ? 274 VAL A CG1   1 
ATOM   2113 C  CG2   . VAL A 1 274 ? 35.78900  -15.54334 -12.43131 1.000 15.58922 ? 274 VAL A CG2   1 
ATOM   2114 N  N     . TYR A 1 275 ? 38.31894  -15.86133 -16.28035 1.000 11.35426 ? 275 TYR A N     1 
ATOM   2115 C  CA    . TYR A 1 275 ? 38.89792  -16.47833 -17.47236 1.000 12.66528 ? 275 TYR A CA    1 
ATOM   2116 C  C     . TYR A 1 275 ? 40.41592  -16.57732 -17.38339 1.000 8.89085  ? 275 TYR A C     1 
ATOM   2117 O  O     . TYR A 1 275 ? 41.00592  -17.52432 -17.91140 1.000 10.37474 ? 275 TYR A O     1 
ATOM   2118 C  CB    . TYR A 1 275 ? 38.49690  -15.69033 -18.72135 1.000 11.35254 ? 275 TYR A CB    1 
ATOM   2119 C  CG    . TYR A 1 275 ? 37.04389  -15.83233 -19.12833 1.000 7.96269  ? 275 TYR A CG    1 
ATOM   2120 C  CD1   . TYR A 1 275 ? 36.22690  -16.79734 -18.55232 1.000 11.63355 ? 275 TYR A CD1   1 
ATOM   2121 C  CD2   . TYR A 1 275 ? 36.49187  -15.00133 -20.09832 1.000 8.22907  ? 275 TYR A CD2   1 
ATOM   2122 C  CE1   . TYR A 1 275 ? 34.89990  -16.92834 -18.92830 1.000 12.46445 ? 275 TYR A CE1   1 
ATOM   2123 C  CE2   . TYR A 1 275 ? 35.17087  -15.12734 -20.48330 1.000 7.51271  ? 275 TYR A CE2   1 
ATOM   2124 C  CZ    . TYR A 1 275 ? 34.37788  -16.09434 -19.90029 1.000 7.58107  ? 275 TYR A CZ    1 
ATOM   2125 O  OH    . TYR A 1 275 ? 33.05287  -16.21435 -20.27926 1.000 9.15265  ? 275 TYR A OH    1 
ATOM   2126 N  N     . ARG A 1 276 ? 41.06536  -15.61836 -16.71661 1.000 10.64914 ? 276 ARG A N     1 
ATOM   2127 C  CA    . ARG A 1 276 ? 42.52532  -15.60849 -16.65345 1.000 14.75951 ? 276 ARG A CA    1 
ATOM   2128 C  C     . ARG A 1 276 ? 43.07419  -16.77615 -15.84517 1.000 12.90025 ? 276 ARG A C     1 
ATOM   2129 O  O     . ARG A 1 276 ? 44.20424  -17.21452 -16.08704 1.000 13.45034 ? 276 ARG A O     1 
ATOM   2130 C  CB    . ARG A 1 276 ? 43.02000  -14.28645 -16.06437 1.000 11.47725 ? 276 ARG A CB    1 
ATOM   2131 C  CG    . ARG A 1 276 ? 43.00106  -13.12785 -17.04385 1.000 17.17909 ? 276 ARG A CG    1 
ATOM   2132 C  CD    . ARG A 1 276 ? 44.15980  -13.21240 -18.02264 0.000 15.17536 ? 276 ARG A CD    1 
ATOM   2133 N  NE    . ARG A 1 276 ? 45.08517  -12.09673 -17.86370 0.000 15.37247 ? 276 ARG A NE    1 
ATOM   2134 C  CZ    . ARG A 1 276 ? 46.08984  -12.07279 -16.99853 0.000 15.36296 ? 276 ARG A CZ    1 
ATOM   2135 N  NH1   . ARG A 1 276 ? 46.33021  -13.09177 -16.18968 0.000 15.79550 ? 276 ARG A NH1   1 
ATOM   2136 N  NH2   . ARG A 1 276 ? 46.87265  -10.99895 -16.94285 0.000 15.06589 ? 276 ARG A NH2   1 
ATOM   2137 N  N     . ARG A 1 277 ? 42.30377  -17.28664 -14.88718 1.000 16.66932 ? 277 ARG A N     1 
ATOM   2138 C  CA    . ARG A 1 277 ? 42.71644  -18.41959 -14.07220 1.000 16.35291 ? 277 ARG A CA    1 
ATOM   2139 C  C     . ARG A 1 277 ? 42.12980  -19.74143 -14.54890 1.000 15.80323 ? 277 ARG A C     1 
ATOM   2140 O  O     . ARG A 1 277 ? 42.39468  -20.77758 -13.93149 1.000 13.87286 ? 277 ARG A O     1 
ATOM   2141 C  CB    . ARG A 1 277 ? 42.32855  -18.18520 -12.60800 1.000 20.21481 ? 277 ARG A CB    1 
ATOM   2142 C  CG    . ARG A 1 277 ? 42.95453  -16.94718 -11.99133 1.000 22.88128 ? 277 ARG A CG    1 
ATOM   2143 C  CD    . ARG A 1 277 ? 42.50576  -16.76768 -10.54994 1.000 24.35286 ? 277 ARG A CD    1 
ATOM   2144 N  NE    . ARG A 1 277 ? 43.12001  -15.60135 -9.92678  0.000 25.68556 ? 277 ARG A NE    1 
ATOM   2145 C  CZ    . ARG A 1 277 ? 42.90613  -15.22153 -8.67445  0.000 26.46224 ? 277 ARG A CZ    1 
ATOM   2146 N  NH1   . ARG A 1 277 ? 42.09365  -15.89547 -7.87692  0.000 26.79758 ? 277 ARG A NH1   1 
ATOM   2147 N  NH2   . ARG A 1 277 ? 43.52301  -14.13839 -8.21048  0.000 26.88105 ? 277 ARG A NH2   1 
ATOM   2148 N  N     . HIS A 1 278 ? 41.34296  -19.73432 -15.62440 1.000 13.54409 ? 278 HIS A N     1 
ATOM   2149 C  CA    . HIS A 1 278 ? 40.71696  -20.94432 -16.15839 1.000 15.54052 ? 278 HIS A CA    1 
ATOM   2150 C  C     . HIS A 1 278 ? 40.95393  -20.99632 -17.66140 1.000 12.78321 ? 278 HIS A C     1 
ATOM   2151 O  O     . HIS A 1 278 ? 40.12792  -20.51632 -18.44738 1.000 9.22844  ? 278 HIS A O     1 
ATOM   2152 C  CB    . HIS A 1 278 ? 39.22596  -20.98433 -15.82637 1.000 13.10841 ? 278 HIS A CB    1 
ATOM   2153 C  CG    . HIS A 1 278 ? 38.94299  -21.09333 -14.36136 1.000 11.88889 ? 278 HIS A CG    1 
ATOM   2154 N  ND1   . HIS A 1 278 ? 38.84900  -22.30333 -13.70936 1.000 16.07657 ? 278 HIS A ND1   1 
ATOM   2155 C  CD2   . HIS A 1 278 ? 38.75200  -20.14233 -13.41536 1.000 15.90885 ? 278 HIS A CD2   1 
ATOM   2156 C  CE1   . HIS A 1 278 ? 38.61002  -22.09433 -12.42736 1.000 21.32493 ? 278 HIS A CE1   1 
ATOM   2157 N  NE2   . HIS A 1 278 ? 38.54302  -20.79133 -12.22136 1.000 16.24996 ? 278 HIS A NE2   1 
ATOM   2158 N  N     . PRO A 1 279 ? 42.06093  -21.60232 -18.09942 1.000 11.55149 ? 279 PRO A N     1 
ATOM   2159 C  CA    . PRO A 1 279 ? 42.44490  -21.49231 -19.51742 1.000 14.80116 ? 279 PRO A CA    1 
ATOM   2160 C  C     . PRO A 1 279 ? 41.50689  -22.20132 -20.47241 1.000 13.08039 ? 279 PRO A C     1 
ATOM   2161 O  O     . PRO A 1 279 ? 41.50787  -21.87632 -21.66741 1.000 9.77769  ? 279 PRO A O     1 
ATOM   2162 C  CB    . PRO A 1 279 ? 43.84791  -22.11131 -19.54945 1.000 17.70556 ? 279 PRO A CB    1 
ATOM   2163 C  CG    . PRO A 1 279 ? 43.88693  -23.01831 -18.36345 1.000 22.56540 ? 279 PRO A CG    1 
ATOM   2164 C  CD    . PRO A 1 279 ? 43.05094  -22.35231 -17.31043 1.000 17.61821 ? 279 PRO A CD    1 
ATOM   2165 N  N     . ALA A 1 280 ? 40.70290  -23.14932 -19.99439 1.000 13.02116 ? 280 ALA A N     1 
ATOM   2166 C  CA    . ALA A 1 280 ? 39.76289  -23.88032 -20.83138 1.000 14.67817 ? 280 ALA A CA    1 
ATOM   2167 C  C     . ALA A 1 280 ? 38.35889  -23.29333 -20.77335 1.000 11.14945 ? 280 ALA A C     1 
ATOM   2168 O  O     . ALA A 1 280 ? 37.38589  -24.00433 -21.04434 1.000 10.12070 ? 280 ALA A O     1 
ATOM   2169 C  CB    . ALA A 1 280 ? 39.73490  -25.35532 -20.43238 1.000 11.48574 ? 280 ALA A CB    1 
ATOM   2170 N  N     . HIS A 1 281 ? 38.23989  -22.01633 -20.41435 1.000 8.93601  ? 281 HIS A N     1 
ATOM   2171 C  CA    . HIS A 1 281 ? 36.93689  -21.37433 -20.33133 1.000 11.80370 ? 281 HIS A CA    1 
ATOM   2172 C  C     . HIS A 1 281 ? 36.27387  -21.32533 -21.70432 1.000 9.41571  ? 281 HIS A C     1 
ATOM   2173 O  O     . HIS A 1 281 ? 36.93985  -21.27833 -22.73933 1.000 8.99796  ? 281 HIS A O     1 
ATOM   2174 C  CB    . HIS A 1 281 ? 37.07490  -19.96333 -19.75633 1.000 9.65327  ? 281 HIS A CB    1 
ATOM   2175 C  CG    . HIS A 1 281 ? 37.85188  -19.02333 -20.62734 1.000 8.42529  ? 281 HIS A CG    1 
ATOM   2176 N  ND1   . HIS A 1 281 ? 37.26686  -18.28233 -21.63033 1.000 12.27047 ? 281 HIS A ND1   1 
ATOM   2177 C  CD2   . HIS A 1 281 ? 39.16488  -18.69332 -20.63737 1.000 10.78935 ? 281 HIS A CD2   1 
ATOM   2178 C  CE1   . HIS A 1 281 ? 38.18485  -17.54533 -22.22935 1.000 11.75769 ? 281 HIS A CE1   1 
ATOM   2179 N  NE2   . HIS A 1 281 ? 39.34686  -17.77632 -21.64537 1.000 13.15350 ? 281 HIS A NE2   1 
ATOM   2180 N  N     . SER A 1 282 ? 34.94287  -21.34934 -21.70430 1.000 11.43638 ? 282 SER A N     1 
ATOM   2181 C  CA    . SER A 1 282 ? 34.20285  -21.29034 -22.95528 1.000 12.64320 ? 282 SER A CA    1 
ATOM   2182 C  C     . SER A 1 282 ? 34.46283  -19.96634 -23.67229 1.000 11.90046 ? 282 SER A C     1 
ATOM   2183 O  O     . SER A 1 282 ? 34.81184  -18.95434 -23.05829 1.000 11.81571 ? 282 SER A O     1 
ATOM   2184 C  CB    . SER A 1 282 ? 32.69985  -21.48335 -22.70326 1.000 10.80513 ? 282 SER A CB    1 
ATOM   2185 O  OG    . SER A 1 282 ? 32.23087  -20.64735 -21.66025 1.000 9.33673  ? 282 SER A OG    1 
ATOM   2186 N  N     . GLN A 1 283 ? 34.29381  -19.98734 -24.99029 1.000 11.52234 ? 283 GLN A N     1 
ATOM   2187 C  CA    . GLN A 1 283 ? 34.52179  -18.84934 -25.86629 1.000 13.38387 ? 283 GLN A CA    1 
ATOM   2188 C  C     . GLN A 1 283 ? 33.21678  -18.38534 -26.50227 1.000 12.08060 ? 283 GLN A C     1 
ATOM   2189 O  O     . GLN A 1 283 ? 32.22778  -19.12235 -26.52525 1.000 13.57006 ? 283 GLN A O     1 
ATOM   2190 C  CB    . GLN A 1 283 ? 35.52677  -19.22034 -26.96731 1.000 17.53044 ? 283 GLN A CB    1 
ATOM   2191 C  CG    . GLN A 1 283 ? 36.89678  -19.64833 -26.45433 1.000 13.23762 ? 283 GLN A CG    1 
ATOM   2192 C  CD    . GLN A 1 283 ? 37.71479  -18.49333 -25.90734 1.000 11.96383 ? 283 GLN A CD    1 
ATOM   2193 O  OE1   . GLN A 1 283 ? 38.73880  -18.70132 -25.26236 1.000 18.52144 ? 283 GLN A OE1   1 
ATOM   2194 N  NE2   . GLN A 1 283 ? 37.27278  -17.27233 -26.16933 1.000 17.63635 ? 283 GLN A NE2   1 
ATOM   2195 N  N     . PRO A 1 284 ? 33.17577  -17.15334 -27.01527 1.000 11.60587 ? 284 PRO A N     1 
ATOM   2196 C  CA    . PRO A 1 284 ? 31.97475  -16.70835 -27.71925 1.000 13.66668 ? 284 PRO A CA    1 
ATOM   2197 C  C     . PRO A 1 284 ? 31.65974  -17.63135 -28.87924 1.000 14.23197 ? 284 PRO A C     1 
ATOM   2198 O  O     . PRO A 1 284 ? 32.56473  -18.24334 -29.47126 1.000 16.51812 ? 284 PRO A O     1 
ATOM   2199 C  CB    . PRO A 1 284 ? 32.35974  -15.30235 -28.20625 1.000 14.48372 ? 284 PRO A CB    1 
ATOM   2200 C  CG    . PRO A 1 284 ? 33.41275  -14.85134 -27.25327 1.000 16.64906 ? 284 PRO A CG    1 
ATOM   2201 C  CD    . PRO A 1 284 ? 34.17176  -16.08134 -26.87328 1.000 12.07107 ? 284 PRO A CD    1 
ATOM   2202 N  N     . PRO A 1 285 ? 30.38073  -17.74935 -29.24722 1.000 15.21065 ? 285 PRO A N     1 
ATOM   2203 C  CA    . PRO A 1 285 ? 29.22674  -17.01336 -28.71920 1.000 13.44520 ? 285 PRO A CA    1 
ATOM   2204 C  C     . PRO A 1 285 ? 28.52176  -17.69636 -27.54219 1.000 13.08394 ? 285 PRO A C     1 
ATOM   2205 O  O     . PRO A 1 285 ? 27.56677  -17.13836 -27.00117 1.000 12.53195 ? 285 PRO A O     1 
ATOM   2206 C  CB    . PRO A 1 285 ? 28.31472  -16.91936 -29.94719 1.000 7.84272  ? 285 PRO A CB    1 
ATOM   2207 C  CG    . PRO A 1 285 ? 28.55171  -18.22936 -30.65819 1.000 14.59723 ? 285 PRO A CG    1 
ATOM   2208 C  CD    . PRO A 1 285 ? 30.01171  -18.57135 -30.41621 1.000 13.89119 ? 285 PRO A CD    1 
ATOM   2209 N  N     . VAL A 1 286 ? 28.96077  -18.88736 -27.12120 1.000 11.83133 ? 286 VAL A N     1 
ATOM   2210 C  CA    . VAL A 1 286 ? 28.23879  -19.63336 -26.09119 1.000 8.42582  ? 286 VAL A CA    1 
ATOM   2211 C  C     . VAL A 1 286 ? 28.61481  -19.21336 -24.67319 1.000 8.61982  ? 286 VAL A C     1 
ATOM   2212 O  O     . VAL A 1 286 ? 27.82683  -19.43436 -23.74418 1.000 9.50050  ? 286 VAL A O     1 
ATOM   2213 C  CB    . VAL A 1 286 ? 28.46679  -21.14836 -26.24919 1.000 9.79813  ? 286 VAL A CB    1 
ATOM   2214 C  CG1   . VAL A 1 286 ? 27.89677  -21.64636 -27.56918 1.000 7.49082  ? 286 VAL A CG1   1 
ATOM   2215 C  CG2   . VAL A 1 286 ? 29.93779  -21.48335 -26.14121 1.000 7.45894  ? 286 VAL A CG2   1 
ATOM   2216 N  N     . SER A 1 287 ? 29.78681  -18.61036 -24.47821 1.000 7.83124  ? 287 SER A N     1 
ATOM   2217 C  CA    . SER A 1 287 ? 30.26783  -18.29835 -23.14322 1.000 7.26615  ? 287 SER A CA    1 
ATOM   2218 C  C     . SER A 1 287 ? 29.40984  -17.21136 -22.50820 1.000 7.78671  ? 287 SER A C     1 
ATOM   2219 O  O     . SER A 1 287 ? 28.55583  -16.59636 -23.15219 1.000 10.46188 ? 287 SER A O     1 
ATOM   2220 C  CB    . SER A 1 287 ? 31.73083  -17.86035 -23.19224 1.000 7.77933  ? 287 SER A CB    1 
ATOM   2221 O  OG    . SER A 1 287 ? 31.84682  -16.59035 -23.80124 1.000 7.09503  ? 287 SER A OG    1 
ATOM   2222 N  N     . LEU A 1 288 ? 29.62686  -16.99436 -21.20721 1.000 6.95612  ? 288 LEU A N     1 
ATOM   2223 C  CA    . LEU A 1 288 ? 28.93187  -15.90836 -20.52120 1.000 7.12146  ? 288 LEU A CA    1 
ATOM   2224 C  C     . LEU A 1 288 ? 29.35786  -14.55136 -21.06920 1.000 6.55938  ? 288 LEU A C     1 
ATOM   2225 O  O     . LEU A 1 288 ? 28.52485  -13.65236 -21.22819 1.000 8.18168  ? 288 LEU A O     1 
ATOM   2226 C  CB    . LEU A 1 288 ? 29.18389  -15.98336 -19.01920 1.000 11.50388 ? 288 LEU A CB    1 
ATOM   2227 C  CG    . LEU A 1 288 ? 27.94991  -16.20536 -18.15118 1.000 10.34383 ? 288 LEU A CG    1 
ATOM   2228 C  CD1   . LEU A 1 288 ? 28.30193  -16.01236 -16.68119 1.000 13.08468 ? 288 LEU A CD1   1 
ATOM   2229 C  CD2   . LEU A 1 288 ? 26.82090  -15.28737 -18.58216 1.000 10.01225 ? 288 LEU A CD2   1 
ATOM   2230 N  N     . ARG A 1 289 ? 30.64928  -14.37741 -21.36164 1.000 6.72536  ? 289 ARG A N     1 
ATOM   2231 C  CA    . ARG A 1 289 ? 31.07607  -13.16113 -22.04577 1.000 6.76121  ? 289 ARG A CA    1 
ATOM   2232 C  C     . ARG A 1 289 ? 30.38585  -13.02618 -23.39830 1.000 6.70772  ? 289 ARG A C     1 
ATOM   2233 O  O     . ARG A 1 289 ? 29.98667  -11.92499 -23.79463 1.000 6.66550  ? 289 ARG A O     1 
ATOM   2234 C  CB    . ARG A 1 289 ? 32.59517  -13.14805 -22.21280 1.000 9.48491  ? 289 ARG A CB    1 
ATOM   2235 C  CG    . ARG A 1 289 ? 33.08966  -12.04336 -23.12685 1.000 9.74589  ? 289 ARG A CG    1 
ATOM   2236 C  CD    . ARG A 1 289 ? 34.60362  -11.99712 -23.20950 1.000 8.88632  ? 289 ARG A CD    1 
ATOM   2237 N  NE    . ARG A 1 289 ? 35.04458  -10.94000 -24.11076 1.000 8.32370  ? 289 ARG A NE    1 
ATOM   2238 C  CZ    . ARG A 1 289 ? 35.42137  -11.13163 -25.36796 1.000 9.89755  ? 289 ARG A CZ    1 
ATOM   2239 N  NH1   . ARG A 1 289 ? 35.46737  -12.34279 -25.90003 1.000 13.74032 ? 289 ARG A NH1   1 
ATOM   2240 N  NH2   . ARG A 1 289 ? 35.76738  -10.08269 -26.10745 1.000 7.78852  ? 289 ARG A NH2   1 
ATOM   2241 N  N     . GLY A 1 290 ? 30.22780  -14.14135 -24.11522 1.000 6.74892  ? 290 GLY A N     1 
ATOM   2242 C  CA    . GLY A 1 290 ? 29.52878  -14.10536 -25.38720 1.000 6.74041  ? 290 GLY A CA    1 
ATOM   2243 C  C     . GLY A 1 290 ? 28.09078  -13.64136 -25.26218 1.000 6.54782  ? 290 GLY A C     1 
ATOM   2244 O  O     . GLY A 1 290 ? 27.55176  -13.03536 -26.18817 1.000 6.55806  ? 290 GLY A O     1 
ATOM   2245 N  N     . GLN A 1 291 ? 27.45280  -13.90636 -24.11517 1.000 6.41113  ? 291 GLN A N     1 
ATOM   2246 C  CA    . GLN A 1 291 ? 26.08780  -13.43437 -23.90815 1.000 6.26302  ? 291 GLN A CA    1 
ATOM   2247 C  C     . GLN A 1 291 ? 26.03180  -11.91837 -23.78015 1.000 6.24791  ? 291 GLN A C     1 
ATOM   2248 O  O     . GLN A 1 291 ? 25.05979  -11.29837 -24.22413 1.000 6.20607  ? 291 GLN A O     1 
ATOM   2249 C  CB    . GLN A 1 291 ? 25.47783  -14.09737 -22.67514 1.000 6.17605  ? 291 GLN A CB    1 
ATOM   2250 C  CG    . GLN A 1 291 ? 25.44283  -15.60837 -22.73814 1.000 6.22526  ? 291 GLN A CG    1 
ATOM   2251 C  CD    . GLN A 1 291 ? 24.83681  -16.13137 -24.02713 1.000 6.25253  ? 291 GLN A CD    1 
ATOM   2252 O  OE1   . GLN A 1 291 ? 23.65181  -15.93538 -24.30111 1.000 7.21008  ? 291 GLN A OE1   1 
ATOM   2253 N  NE2   . GLN A 1 291 ? 25.64480  -16.81137 -24.81614 1.000 7.22587  ? 291 GLN A NE2   1 
ATOM   2254 N  N     . LEU A 1 292 ? 27.05681  -11.30537 -23.17916 1.000 6.31762  ? 292 LEU A N     1 
ATOM   2255 C  CA    . LEU A 1 292 ? 27.13980  -9.84736  -23.18316 1.000 6.36160  ? 292 LEU A CA    1 
ATOM   2256 C  C     . LEU A 1 292 ? 27.44978  -9.31336  -24.57117 1.000 6.48491  ? 292 LEU A C     1 
ATOM   2257 O  O     . LEU A 1 292 ? 27.11177  -8.16436  -24.88316 1.000 6.53466  ? 292 LEU A O     1 
ATOM   2258 C  CB    . LEU A 1 292 ? 28.19982  -9.36136  -22.19418 1.000 6.44917  ? 292 LEU A CB    1 
ATOM   2259 C  CG    . LEU A 1 292 ? 27.90284  -9.53136  -20.70418 1.000 9.06978  ? 292 LEU A CG    1 
ATOM   2260 C  CD1   . LEU A 1 292 ? 29.11286  -9.10436  -19.87720 1.000 12.65569 ? 292 LEU A CD1   1 
ATOM   2261 C  CD2   . LEU A 1 292 ? 26.67285  -8.72837  -20.30716 1.000 10.18253 ? 292 LEU A CD2   1 
ATOM   2262 N  N     . LEU A 1 293 ? 28.09577  -10.11736 -25.41518 1.000 7.23647  ? 293 LEU A N     1 
ATOM   2263 C  CA    . LEU A 1 293 ? 28.38474  -9.66536  -26.77118 1.000 7.86092  ? 293 LEU A CA    1 
ATOM   2264 C  C     . LEU A 1 293 ? 27.15373  -9.73836  -27.66616 1.000 8.15736  ? 293 LEU A C     1 
ATOM   2265 O  O     . LEU A 1 293 ? 27.01671  -8.92036  -28.57916 1.000 8.93318  ? 293 LEU A O     1 
ATOM   2266 C  CB    . LEU A 1 293 ? 29.54174  -10.47136 -27.36720 1.000 9.78350  ? 293 LEU A CB    1 
ATOM   2267 C  CG    . LEU A 1 293 ? 30.89875  -10.21535 -26.70523 1.000 7.81736  ? 293 LEU A CG    1 
ATOM   2268 C  CD1   . LEU A 1 293 ? 31.99774  -11.04135 -27.33424 1.000 9.34799  ? 293 LEU A CD1   1 
ATOM   2269 C  CD2   . LEU A 1 293 ? 31.24874  -8.73535  -26.77223 1.000 10.60584 ? 293 LEU A CD2   1 
ATOM   2270 N  N     . TRP A 1 294 ? 26.26074  -10.70437 -27.43615 1.000 6.59279  ? 294 TRP A N     1 
ATOM   2271 C  CA    . TRP A 1 294 ? 24.97172  -10.68937 -28.12113 1.000 6.56635  ? 294 TRP A CA    1 
ATOM   2272 C  C     . TRP A 1 294 ? 24.23073  -9.38937  -27.83012 1.000 6.53581  ? 294 TRP A C     1 
ATOM   2273 O  O     . TRP A 1 294 ? 23.67371  -8.75937  -28.73711 1.000 8.64917  ? 294 TRP A O     1 
ATOM   2274 C  CB    . TRP A 1 294 ? 24.12274  -11.89637 -27.69711 1.000 8.00234  ? 294 TRP A CB    1 
ATOM   2275 C  CG    . TRP A 1 294 ? 24.51973  -13.21537 -28.30712 1.000 7.26878  ? 294 TRP A CG    1 
ATOM   2276 C  CD1   . TRP A 1 294 ? 25.11874  -14.26037 -27.67013 1.000 8.89531  ? 294 TRP A CD1   1 
ATOM   2277 C  CD2   . TRP A 1 294 ? 24.33871  -13.62937 -29.66912 1.000 8.55744  ? 294 TRP A CD2   1 
ATOM   2278 N  NE1   . TRP A 1 294 ? 25.32473  -15.29537 -28.54614 1.000 6.65876  ? 294 TRP A NE1   1 
ATOM   2279 C  CE2   . TRP A 1 294 ? 24.85871  -14.93237 -29.78113 1.000 10.43694 ? 294 TRP A CE2   1 
ATOM   2280 C  CE3   . TRP A 1 294 ? 23.79669  -13.02137 -30.80511 1.000 13.59335 ? 294 TRP A CE3   1 
ATOM   2281 C  CZ2   . TRP A 1 294 ? 24.85069  -15.64137 -30.98313 1.000 15.12726 ? 294 TRP A CZ2   1 
ATOM   2282 C  CZ3   . TRP A 1 294 ? 23.79567  -13.72537 -32.00311 1.000 13.14809 ? 294 TRP A CZ3   1 
ATOM   2283 C  CH2   . TRP A 1 294 ? 24.31967  -15.02137 -32.08012 1.000 15.73737 ? 294 TRP A CH2   1 
ATOM   2284 N  N     . ARG A 1 295 ? 24.21611  -8.97730  -26.55979 1.000 6.41907  ? 295 ARG A N     1 
ATOM   2285 C  CA    . ARG A 1 295 ? 23.61688  -7.70214  -26.17967 1.000 7.50286  ? 295 ARG A CA    1 
ATOM   2286 C  C     . ARG A 1 295 ? 24.28884  -6.54125  -26.90432 1.000 6.63500  ? 295 ARG A C     1 
ATOM   2287 O  O     . ARG A 1 295 ? 23.61474  -5.68767  -27.49120 1.000 6.74966  ? 295 ARG A O     1 
ATOM   2288 C  CB    . ARG A 1 295 ? 23.70916  -7.52697  -24.66152 1.000 6.33287  ? 295 ARG A CB    1 
ATOM   2289 C  CG    . ARG A 1 295 ? 23.16306  -6.21660  -24.11494 1.000 6.38826  ? 295 ARG A CG    1 
ATOM   2290 C  CD    . ARG A 1 295 ? 23.24974  -6.20002  -22.58870 1.000 6.32639  ? 295 ARG A CD    1 
ATOM   2291 N  NE    . ARG A 1 295 ? 22.69918  -4.98643  -21.99583 1.000 6.41811  ? 295 ARG A NE    1 
ATOM   2292 C  CZ    . ARG A 1 295 ? 23.41632  -3.92098  -21.66366 1.000 6.56120  ? 295 ARG A CZ    1 
ATOM   2293 N  NH1   . ARG A 1 295 ? 24.72549  -3.88206  -21.85059 1.000 7.72825  ? 295 ARG A NH1   1 
ATOM   2294 N  NH2   . ARG A 1 295 ? 22.80420  -2.86714  -21.13113 1.000 6.67743  ? 295 ARG A NH2   1 
ATOM   2295 N  N     . GLU A 1 296 ? 25.62473  -6.50037  -26.87714 1.000 6.71730  ? 296 GLU A N     1 
ATOM   2296 C  CA    . GLU A 1 296 ? 26.35372  -5.44137  -27.56615 1.000 7.11508  ? 296 GLU A CA    1 
ATOM   2297 C  C     . GLU A 1 296 ? 26.11469  -5.50837  -29.06715 1.000 7.12007  ? 296 GLU A C     1 
ATOM   2298 O  O     . GLU A 1 296 ? 26.00168  -4.47337  -29.73514 1.000 9.18034  ? 296 GLU A O     1 
ATOM   2299 C  CB    . GLU A 1 296 ? 27.84972  -5.54636  -27.25317 1.000 7.02776  ? 296 GLU A CB    1 
ATOM   2300 C  CG    . GLU A 1 296 ? 28.64771  -4.25836  -27.47219 1.000 7.26738  ? 296 GLU A CG    1 
ATOM   2301 C  CD    . GLU A 1 296 ? 28.43473  -3.21836  -26.37918 1.000 9.36640  ? 296 GLU A CD    1 
ATOM   2302 O  OE1   . GLU A 1 296 ? 27.78275  -3.53136  -25.35717 1.000 7.05987  ? 296 GLU A OE1   1 
ATOM   2303 O  OE2   . GLU A 1 296 ? 28.93572  -2.08036  -26.54119 1.000 9.52795  ? 296 GLU A OE2   1 
ATOM   2304 N  N     . PHE A 1 297 ? 26.02869  -6.72437  -29.61214 1.000 8.13950  ? 297 PHE A N     1 
ATOM   2305 C  CA    . PHE A 1 297 ? 25.79566  -6.89137  -31.04114 1.000 8.12073  ? 297 PHE A CA    1 
ATOM   2306 C  C     . PHE A 1 297 ? 24.45365  -6.30237  -31.45212 1.000 7.32213  ? 297 PHE A C     1 
ATOM   2307 O  O     . PHE A 1 297 ? 24.36764  -5.53637  -32.41812 1.000 7.58060  ? 297 PHE A O     1 
ATOM   2308 C  CB    . PHE A 1 297 ? 25.86966  -8.37237  -31.40014 1.000 10.51057 ? 297 PHE A CB    1 
ATOM   2309 C  CG    . PHE A 1 297 ? 25.53864  -8.66837  -32.82914 1.000 11.49303 ? 297 PHE A CG    1 
ATOM   2310 C  CD1   . PHE A 1 297 ? 26.32462  -8.17236  -33.84915 1.000 11.32904 ? 297 PHE A CD1   1 
ATOM   2311 C  CD2   . PHE A 1 297 ? 24.44664  -9.45537  -33.14812 1.000 10.96319 ? 297 PHE A CD2   1 
ATOM   2312 C  CE1   . PHE A 1 297 ? 26.01860  -8.44936  -35.17414 1.000 19.30443 ? 297 PHE A CE1   1 
ATOM   2313 C  CE2   . PHE A 1 297 ? 24.13862  -9.74237  -34.46511 1.000 14.71917 ? 297 PHE A CE2   1 
ATOM   2314 C  CZ    . PHE A 1 297 ? 24.92260  -9.23637  -35.48013 1.000 14.02841 ? 297 PHE A CZ    1 
ATOM   2315 N  N     . PHE A 1 298 ? 23.39267  -6.64138  -30.71810 1.000 7.10601  ? 298 PHE A N     1 
ATOM   2316 C  CA    . PHE A 1 298 ? 22.06366  -6.16138  -31.08108 1.000 7.16631  ? 298 PHE A CA    1 
ATOM   2317 C  C     . PHE A 1 298 ? 21.91166  -4.66538  -30.82008 1.000 7.28613  ? 298 PHE A C     1 
ATOM   2318 O  O     . PHE A 1 298 ? 21.21664  -3.97638  -31.57406 1.000 7.49639  ? 298 PHE A O     1 
ATOM   2319 C  CB    . PHE A 1 298 ? 21.00168  -6.96138  -30.32706 1.000 6.93675  ? 298 PHE A CB    1 
ATOM   2320 C  CG    . PHE A 1 298 ? 20.89167  -8.39138  -30.77406 1.000 6.89028  ? 298 PHE A CG    1 
ATOM   2321 C  CD1   . PHE A 1 298 ? 21.10965  -8.73538  -32.10006 1.000 9.37950  ? 298 PHE A CD1   1 
ATOM   2322 C  CD2   . PHE A 1 298 ? 20.58169  -9.39639  -29.86805 1.000 6.81114  ? 298 PHE A CD2   1 
ATOM   2323 C  CE1   . PHE A 1 298 ? 21.00065  -10.04638 -32.51706 1.000 7.10939  ? 298 PHE A CE1   1 
ATOM   2324 C  CE2   . PHE A 1 298 ? 20.48369  -10.70639 -30.27505 1.000 6.67071  ? 298 PHE A CE2   1 
ATOM   2325 C  CZ    . PHE A 1 298 ? 20.68867  -11.03338 -31.60206 1.000 9.12085  ? 298 PHE A CZ    1 
ATOM   2326 N  N     . TYR A 1 299 ? 22.55367  -4.14238  -29.76809 1.000 9.64845  ? 299 TYR A N     1 
ATOM   2327 C  CA    . TYR A 1 299 ? 22.55567  -2.69638  -29.55609 1.000 8.92918  ? 299 TYR A CA    1 
ATOM   2328 C  C     . TYR A 1 299 ? 23.25065  -1.97738  -30.70110 1.000 7.68562  ? 299 TYR A C     1 
ATOM   2329 O  O     . TYR A 1 299 ? 22.80864  -0.90438  -31.13109 1.000 9.74404  ? 299 TYR A O     1 
ATOM   2330 C  CB    . TYR A 1 299 ? 23.22869  -2.35138  -28.22810 1.000 7.25282  ? 299 TYR A CB    1 
ATOM   2331 C  CG    . TYR A 1 299 ? 22.26271  -2.14338  -27.09108 1.000 10.09126 ? 299 TYR A CG    1 
ATOM   2332 C  CD1   . TYR A 1 299 ? 21.70573  -3.22738  -26.41507 1.000 10.48756 ? 299 TYR A CD1   1 
ATOM   2333 C  CD2   . TYR A 1 299 ? 21.90272  -0.86738  -26.68707 1.000 9.04139  ? 299 TYR A CD2   1 
ATOM   2334 C  CE1   . TYR A 1 299 ? 20.81774  -3.03939  -25.37006 1.000 6.80622  ? 299 TYR A CE1   1 
ATOM   2335 C  CE2   . TYR A 1 299 ? 21.01473  -0.67538  -25.64106 1.000 8.12079  ? 299 TYR A CE2   1 
ATOM   2336 C  CZ    . TYR A 1 299 ? 20.47675  -1.76539  -24.99105 1.000 6.97434  ? 299 TYR A CZ    1 
ATOM   2337 O  OH    . TYR A 1 299 ? 19.59776  -1.57839  -23.94804 1.000 7.71187  ? 299 TYR A OH    1 
ATOM   2338 N  N     . THR A 1 300 ? 24.32765  -2.57037  -31.22111 1.000 8.58631  ? 300 THR A N     1 
ATOM   2339 C  CA    . THR A 1 300 ? 25.08663  -1.94937  -32.30113 1.000 8.57634  ? 300 THR A CA    1 
ATOM   2340 C  C     . THR A 1 300 ? 24.28060  -1.91937  -33.59211 1.000 8.96590  ? 300 THR A C     1 
ATOM   2341 O  O     . THR A 1 300 ? 24.21759  -0.89037  -34.27011 1.000 10.23134 ? 300 THR A O     1 
ATOM   2342 C  CB    . THR A 1 300 ? 26.40862  -2.69836  -32.50815 1.000 11.50113 ? 300 THR A CB    1 
ATOM   2343 O  OG1   . THR A 1 300 ? 27.18264  -2.65436  -31.30216 1.000 12.40248 ? 300 THR A OG1   1 
ATOM   2344 C  CG2   . THR A 1 300 ? 27.21260  -2.07136  -33.62416 1.000 10.49164 ? 300 THR A CG2   1 
ATOM   2345 N  N     . VAL A 1 301 ? 23.64260  -3.03737  -33.94210 1.000 11.46925 ? 301 VAL A N     1 
ATOM   2346 C  CA    . VAL A 1 301 ? 22.90158  -3.10038  -35.19909 1.000 10.92672 ? 301 VAL A CA    1 
ATOM   2347 C  C     . VAL A 1 301 ? 21.62858  -2.26738  -35.11307 1.000 8.52082  ? 301 VAL A C     1 
ATOM   2348 O  O     . VAL A 1 301 ? 21.32556  -1.47438  -36.01006 1.000 8.87710  ? 301 VAL A O     1 
ATOM   2349 C  CB    . VAL A 1 301 ? 22.59358  -4.56138  -35.57209 1.000 8.33102  ? 301 VAL A CB    1 
ATOM   2350 C  CG1   . VAL A 1 301 ? 21.87056  -4.62238  -36.91207 1.000 10.56501 ? 301 VAL A CG1   1 
ATOM   2351 C  CG2   . VAL A 1 301 ? 23.87158  -5.37637  -35.61811 1.000 11.79681 ? 301 VAL A CG2   1 
ATOM   2352 N  N     . GLY A 1 302 ? 20.87360  -2.42738  -34.02706 1.000 10.27653 ? 302 GLY A N     1 
ATOM   2353 C  CA    . GLY A 1 302 ? 19.58360  -1.76739  -33.92704 1.000 8.31178  ? 302 GLY A CA    1 
ATOM   2354 C  C     . GLY A 1 302 ? 19.68359  -0.25639  -33.87904 1.000 11.24902 ? 302 GLY A C     1 
ATOM   2355 O  O     . GLY A 1 302 ? 18.84058  0.44661   -34.44402 1.000 12.41901 ? 302 GLY A O     1 
ATOM   2356 N  N     . SER A 1 303 ? 20.71360  0.26762   -33.20805 1.000 12.84269 ? 303 SER A N     1 
ATOM   2357 C  CA    . SER A 1 303 ? 20.84860  1.71362   -33.08106 1.000 14.49775 ? 303 SER A CA    1 
ATOM   2358 C  C     . SER A 1 303 ? 21.23258  2.37562   -34.39506 1.000 16.23574 ? 303 SER A C     1 
ATOM   2359 O  O     . SER A 1 303 ? 21.05157  3.59062   -34.53806 1.000 20.76063 ? 303 SER A O     1 
ATOM   2360 C  CB    . SER A 1 303 ? 21.87462  2.06062   -31.99907 1.000 16.95206 ? 303 SER A CB    1 
ATOM   2361 O  OG    . SER A 1 303 ? 23.19061  1.71362   -32.39409 1.000 16.13569 ? 303 SER A OG    1 
ATOM   2362 N  N     . THR A 1 304 ? 21.75256  1.61162   -35.35707 1.000 13.71240 ? 304 THR A N     1 
ATOM   2363 C  CA    . THR A 1 304 ? 22.11654  2.14562   -36.66408 1.000 16.98898 ? 304 THR A CA    1 
ATOM   2364 C  C     . THR A 1 304 ? 21.16052  1.69462   -37.75906 1.000 13.27799 ? 304 THR A C     1 
ATOM   2365 O  O     . THR A 1 304 ? 21.41350  1.96362   -38.93606 1.000 19.00007 ? 304 THR A O     1 
ATOM   2366 C  CB    . THR A 1 304 ? 23.54853  1.74663   -37.04110 1.000 14.95948 ? 304 THR A CB    1 
ATOM   2367 O  OG1   . THR A 1 304 ? 23.65454  0.31963   -37.10610 1.000 14.91528 ? 304 THR A OG1   1 
ATOM   2368 C  CG2   . THR A 1 304 ? 24.54455  2.28463   -36.02612 1.000 14.66342 ? 304 THR A CG2   1 
ATOM   2369 N  N     . THR A 1 305 ? 20.07253  1.01962   -37.40304 1.000 13.50565 ? 305 THR A N     1 
ATOM   2370 C  CA    . THR A 1 305 ? 19.11352  0.52061   -38.37803 1.000 17.68921 ? 305 THR A CA    1 
ATOM   2371 C  C     . THR A 1 305 ? 17.77552  1.21961   -38.18500 1.000 20.15921 ? 305 THR A C     1 
ATOM   2372 O  O     . THR A 1 305 ? 17.17854  1.11661   -37.09799 1.000 14.80613 ? 305 THR A O     1 
ATOM   2373 C  CB    . THR A 1 305 ? 18.94652  -0.99339  -38.25002 1.000 16.53535 ? 305 THR A CB    1 
ATOM   2374 O  OG1   . THR A 1 305 ? 20.22952  -1.62338  -38.34905 1.000 13.64387 ? 305 THR A OG1   1 
ATOM   2375 C  CG2   . THR A 1 305 ? 18.04251  -1.52139  -39.34501 1.000 11.31171 ? 305 THR A CG2   1 
ATOM   2376 N  N     . PRO A 1 306 ? 17.26550  1.93161   -39.19000 1.000 20.56085 ? 306 PRO A N     1 
ATOM   2377 C  CA    . PRO A 1 306 ? 15.96450  2.59060   -39.03597 1.000 19.55278 ? 306 PRO A CA    1 
ATOM   2378 C  C     . PRO A 1 306 ? 14.83250  1.57760   -38.98896 1.000 17.89105 ? 306 PRO A C     1 
ATOM   2379 O  O     . PRO A 1 306 ? 14.87049  0.54460   -39.66096 1.000 20.31246 ? 306 PRO A O     1 
ATOM   2380 C  CB    . PRO A 1 306 ? 15.87047  3.48360   -40.27997 1.000 21.26021 ? 306 PRO A CB    1 
ATOM   2381 C  CG    . PRO A 1 306 ? 16.75646  2.82661   -41.28399 1.000 22.82775 ? 306 PRO A CG    1 
ATOM   2382 C  CD    . PRO A 1 306 ? 17.88347  2.21361   -40.49701 1.000 17.56141 ? 306 PRO A CD    1 
ATOM   2383 N  N     . ASN A 1 307 ? 13.82151  1.88659   -38.17494 1.000 13.28042 ? 307 ASN A N     1 
ATOM   2384 C  CA    . ASN A 1 307 ? 12.62552  1.05859   -38.03992 1.000 15.70175 ? 307 ASN A CA    1 
ATOM   2385 C  C     . ASN A 1 307 ? 12.97753  -0.35541  -37.58493 1.000 18.63941 ? 307 ASN A C     1 
ATOM   2386 O  O     . ASN A 1 307 ? 12.38553  -1.34041  -38.02892 1.000 15.29521 ? 307 ASN A O     1 
ATOM   2387 C  CB    . ASN A 1 307 ? 11.82550  1.03859   -39.34391 1.000 24.38439 ? 307 ASN A CB    1 
ATOM   2388 C  CG    . ASN A 1 307 ? 11.37249  2.42359   -39.76490 1.000 15.73194 ? 307 ASN A CG    1 
ATOM   2389 O  OD1   . ASN A 1 307 ? 11.62947  2.86559   -40.88590 1.000 22.30132 ? 307 ASN A OD1   1 
ATOM   2390 N  ND2   . ASN A 1 307 ? 10.70650  3.12258   -38.85489 1.000 21.26732 ? 307 ASN A ND2   1 
ATOM   2391 N  N     . PHE A 1 308 ? 13.94055  -0.44741  -36.66494 1.000 18.45312 ? 308 PHE A N     1 
ATOM   2392 C  CA    . PHE A 1 308 ? 14.46156  -1.74540  -36.24995 1.000 17.49392 ? 308 PHE A CA    1 
ATOM   2393 C  C     . PHE A 1 308 ? 13.42257  -2.58341  -35.50793 1.000 15.28762 ? 308 PHE A C     1 
ATOM   2394 O  O     . PHE A 1 308 ? 13.47858  -3.81541  -35.55993 1.000 14.13433 ? 308 PHE A O     1 
ATOM   2395 C  CB    . PHE A 1 308 ? 15.70357  -1.54540  -35.38097 1.000 14.91619 ? 308 PHE A CB    1 
ATOM   2396 C  CG    . PHE A 1 308 ? 16.42958  -2.81740  -35.06298 1.000 9.45809  ? 308 PHE A CG    1 
ATOM   2397 C  CD1   . PHE A 1 308 ? 17.16957  -3.46939  -36.03700 1.000 9.81068  ? 308 PHE A CD1   1 
ATOM   2398 C  CD2   . PHE A 1 308 ? 16.37961  -3.35940  -33.79498 1.000 9.16984  ? 308 PHE A CD2   1 
ATOM   2399 C  CE1   . PHE A 1 308 ? 17.84358  -4.63439  -35.75201 1.000 11.80058 ? 308 PHE A CE1   1 
ATOM   2400 C  CE2   . PHE A 1 308 ? 17.05461  -4.52640  -33.49999 1.000 11.57788 ? 308 PHE A CE2   1 
ATOM   2401 C  CZ    . PHE A 1 308 ? 17.78760  -5.16639  -34.48101 1.000 13.61822 ? 308 PHE A CZ    1 
ATOM   2402 N  N     A HIS A 1 309 ? 12.47958  -1.94641  -34.81492 0.735 18.12627 ? 309 HIS A N     1 
ATOM   2403 N  N     B HIS A 1 309 ? 12.47758  -1.94341  -34.81992 0.265 18.09848 ? 309 HIS A N     1 
ATOM   2404 C  CA    A HIS A 1 309 ? 11.45660  -2.65441  -34.05390 0.735 19.19242 ? 309 HIS A CA    1 
ATOM   2405 C  CA    B HIS A 1 309 ? 11.46160  -2.65641  -34.05490 0.265 19.11904 ? 309 HIS A CA    1 
ATOM   2406 C  C     A HIS A 1 309 ? 10.22959  -3.00942  -34.87888 0.735 18.29314 ? 309 HIS A C     1 
ATOM   2407 C  C     B HIS A 1 309 ? 10.24059  -3.02842  -34.88288 0.265 18.28530 ? 309 HIS A C     1 
ATOM   2408 O  O     A HIS A 1 309 ? 9.28260   -3.58342  -34.33086 0.735 18.07507 ? 309 HIS A O     1 
ATOM   2409 O  O     B HIS A 1 309 ? 9.31460   -3.64642  -34.34687 0.265 18.06382 ? 309 HIS A O     1 
ATOM   2410 C  CB    A HIS A 1 309 ? 11.01300  -1.82300  -32.85200 0.735 19.73963 ? 309 HIS A CB    1 
ATOM   2411 C  CB    B HIS A 1 309 ? 11.01800  -1.82600  -32.84700 0.265 19.67529 ? 309 HIS A CB    1 
ATOM   2412 C  CG    A HIS A 1 309 ? 10.44700  -0.50200  -33.22600 0.735 17.88653 ? 309 HIS A CG    1 
ATOM   2413 C  CG    B HIS A 1 309 ? 10.86100  -2.62100  -31.60000 0.265 18.08052 ? 309 HIS A CG    1 
ATOM   2414 N  ND1   A HIS A 1 309 ? 11.22200  0.49500   -33.80200 0.735 18.73149 ? 309 HIS A ND1   1 
ATOM   2415 N  ND1   B HIS A 1 309 ? 11.40100  -3.89200  -31.46200 0.265 17.76646 ? 309 HIS A ND1   1 
ATOM   2416 C  CD2   A HIS A 1 309 ? 9.20000   -0.00700  -33.11000 0.735 21.10843 ? 309 HIS A CD2   1 
ATOM   2417 C  CD2   B HIS A 1 309 ? 10.23300  -2.34100  -30.44400 0.265 18.48585 ? 309 HIS A CD2   1 
ATOM   2418 C  CE1   A HIS A 1 309 ? 10.47300  1.54900   -34.02800 0.735 22.07046 ? 309 HIS A CE1   1 
ATOM   2419 C  CE1   B HIS A 1 309 ? 11.11300  -4.36100  -30.27300 0.265 18.24418 ? 309 HIS A CE1   1 
ATOM   2420 N  NE2   A HIS A 1 309 ? 9.22500   1.26500   -33.61500 0.735 21.73811 ? 309 HIS A NE2   1 
ATOM   2421 N  NE2   B HIS A 1 309 ? 10.39700  -3.42600  -29.62400 0.265 17.33114 ? 309 HIS A NE2   1 
ATOM   2422 N  N     . ARG A 1 310 ? 10.21213  -2.67405  -36.16264 1.000 18.37087 ? 310 ARG A N     1 
ATOM   2423 C  CA    . ARG A 1 310 ? 9.08009   -2.95190  -37.03037 1.000 17.88032 ? 310 ARG A CA    1 
ATOM   2424 C  C     . ARG A 1 310 ? 9.53666   -3.79276  -38.21465 1.000 21.31034 ? 310 ARG A C     1 
ATOM   2425 O  O     . ARG A 1 310 ? 10.73036  -4.02883  -38.41905 1.000 19.84431 ? 310 ARG A O     1 
ATOM   2426 C  CB    . ARG A 1 310 ? 8.42254   -1.64966  -37.50873 1.000 20.27910 ? 310 ARG A CB    1 
ATOM   2427 C  CG    . ARG A 1 310 ? 7.87921   -0.78859  -36.37647 1.000 24.55082 ? 310 ARG A CG    1 
ATOM   2428 C  CD    . ARG A 1 310 ? 7.13354   0.43231   -36.89118 0.000 23.98504 ? 310 ARG A CD    1 
ATOM   2429 N  NE    . ARG A 1 310 ? 7.96990   1.62644   -36.90107 0.000 23.46567 ? 310 ARG A NE    1 
ATOM   2430 C  CZ    . ARG A 1 310 ? 7.52761   2.84646   -37.17379 0.000 23.83682 ? 310 ARG A CZ    1 
ATOM   2431 N  NH1   . ARG A 1 310 ? 6.25843   3.07079   -37.47236 0.000 24.21785 ? 310 ARG A NH1   1 
ATOM   2432 N  NH2   . ARG A 1 310 ? 8.37898   3.86766   -37.14252 0.000 23.82488 ? 310 ARG A NH2   1 
ATOM   2433 N  N     . MET A 1 311 ? 8.56152   -4.25742  -38.99385 1.000 19.31230 ? 311 MET A N     1 
ATOM   2434 C  CA    . MET A 1 311 ? 8.85450   -5.01842  -40.19886 1.000 19.35578 ? 311 MET A CA    1 
ATOM   2435 C  C     . MET A 1 311 ? 8.97748   -4.10742  -41.41586 1.000 20.73566 ? 311 MET A C     1 
ATOM   2436 O  O     . MET A 1 311 ? 9.96947   -4.17142  -42.14988 1.000 19.34444 ? 311 MET A O     1 
ATOM   2437 C  CB    . MET A 1 311 ? 7.76850   -6.07343  -40.42984 1.000 19.63469 ? 311 MET A CB    1 
ATOM   2438 C  CG    . MET A 1 311 ? 8.13449   -7.10842  -41.47585 1.000 20.76506 ? 311 MET A CG    1 
ATOM   2439 S  SD    . MET A 1 311 ? 6.70148   -7.99843  -42.08882 1.000 20.11705 ? 311 MET A SD    1 
ATOM   2440 C  CE    . MET A 1 311 ? 5.82346   -6.68143  -42.92181 1.000 29.49125 ? 311 MET A CE    1 
ATOM   2441 N  N     . ALA A 1 312 ? 7.98247   -3.24942  -41.62884 1.000 21.47017 ? 312 ALA A N     1 
ATOM   2442 C  CA    . ALA A 1 312 ? 7.99745   -2.32942  -42.75584 1.000 17.54768 ? 312 ALA A CA    1 
ATOM   2443 C  C     . ALA A 1 312 ? 9.05245   -1.25242  -42.55186 1.000 23.86063 ? 312 ALA A C     1 
ATOM   2444 O  O     . ALA A 1 312 ? 9.27947   -0.78542  -41.43286 1.000 23.34436 ? 312 ALA A O     1 
ATOM   2445 C  CB    . ALA A 1 312 ? 6.62245   -1.69043  -42.93582 1.000 24.95618 ? 312 ALA A CB    1 
ATOM   2446 N  N     . GLY A 1 313 ? 9.70143   -0.85742  -43.64587 1.000 28.19970 ? 313 GLY A N     1 
ATOM   2447 C  CA    . GLY A 1 313 ? 10.77543  0.11059   -43.56989 1.000 25.48272 ? 313 GLY A CA    1 
ATOM   2448 C  C     . GLY A 1 313 ? 12.03544  -0.38041  -42.89591 1.000 24.83920 ? 313 GLY A C     1 
ATOM   2449 O  O     . GLY A 1 313 ? 12.98744  0.39659   -42.76293 1.000 23.37469 ? 313 GLY A O     1 
ATOM   2450 N  N     . ASN A 1 314 ? 12.07446  -1.64041  -42.46491 1.000 23.91932 ? 314 ASN A N     1 
ATOM   2451 C  CA    . ASN A 1 314 ? 13.26447  -2.21341  -41.84793 1.000 20.07743 ? 314 ASN A CA    1 
ATOM   2452 C  C     . ASN A 1 314 ? 14.12645  -2.86540  -42.92195 1.000 19.86379 ? 314 ASN A C     1 
ATOM   2453 O  O     . ASN A 1 314 ? 13.68144  -3.83640  -43.54894 1.000 17.49611 ? 314 ASN A O     1 
ATOM   2454 C  CB    . ASN A 1 314 ? 12.87349  -3.23641  -40.79492 1.000 15.79012 ? 314 ASN A CB    1 
ATOM   2455 C  CG    . ASN A 1 314 ? 14.03950  -3.65840  -39.92194 1.000 15.36307 ? 314 ASN A CG    1 
ATOM   2456 O  OD1   . ASN A 1 314 ? 15.19850  -3.44440  -40.26596 1.000 16.35734 ? 314 ASN A OD1   1 
ATOM   2457 N  ND2   . ASN A 1 314 ? 13.73353  -4.27141  -38.78494 1.000 13.94265 ? 314 ASN A ND2   1 
ATOM   2458 N  N     . PRO A 1 315 ? 15.34745  -2.37640  -43.16897 1.000 14.21128 ? 315 PRO A N     1 
ATOM   2459 C  CA    . PRO A 1 315 ? 16.17143  -2.97140  -44.23498 1.000 20.84247 ? 315 PRO A CA    1 
ATOM   2460 C  C     . PRO A 1 315 ? 16.74044  -4.34039  -43.89999 1.000 17.45311 ? 315 PRO A C     1 
ATOM   2461 O  O     . PRO A 1 315 ? 17.06843  -5.09039  -44.82599 1.000 24.63945 ? 315 PRO A O     1 
ATOM   2462 C  CB    . PRO A 1 315 ? 17.29142  -1.94039  -44.43100 1.000 14.29793 ? 315 PRO A CB    1 
ATOM   2463 C  CG    . PRO A 1 315 ? 17.37144  -1.22039  -43.12800 1.000 17.92921 ? 315 PRO A CG    1 
ATOM   2464 C  CD    . PRO A 1 315 ? 15.96545  -1.16640  -42.59998 1.000 23.04198 ? 315 PRO A CD    1 
ATOM   2465 N  N     . VAL A 1 316 ? 16.87846  -4.70139  -42.61999 1.000 16.42983 ? 316 VAL A N     1 
ATOM   2466 C  CA    . VAL A 1 316 ? 17.40847  -6.02339  -42.29400 1.000 16.78330 ? 316 VAL A CA    1 
ATOM   2467 C  C     . VAL A 1 316 ? 16.32148  -7.06440  -42.07798 1.000 14.86000 ? 316 VAL A C     1 
ATOM   2468 O  O     . VAL A 1 316 ? 16.63249  -8.26339  -42.02099 1.000 17.02182 ? 316 VAL A O     1 
ATOM   2469 C  CB    . VAL A 1 316 ? 18.30849  -5.99239  -41.04302 1.000 16.93650 ? 316 VAL A CB    1 
ATOM   2470 C  CG1   . VAL A 1 316 ? 19.40349  -4.94739  -41.19903 1.000 21.64861 ? 316 VAL A CG1   1 
ATOM   2471 C  CG2   . VAL A 1 316 ? 17.48551  -5.75039  -39.78600 1.000 19.27771 ? 316 VAL A CG2   1 
ATOM   2472 N  N     . CYS A 1 317 ? 15.06148  -6.65940  -41.96896 1.000 15.82706 ? 317 CYS A N     1 
ATOM   2473 C  CA    . CYS A 1 317 ? 13.98549  -7.59440  -41.67394 1.000 15.73308 ? 317 CYS A CA    1 
ATOM   2474 C  C     . CYS A 1 317 ? 13.31447  -8.05341  -42.96193 1.000 13.97166 ? 317 CYS A C     1 
ATOM   2475 O  O     . CYS A 1 317 ? 12.95945  -7.23241  -43.81393 1.000 18.07022 ? 317 CYS A O     1 
ATOM   2476 C  CB    . CYS A 1 317 ? 12.95450  -6.96041  -40.74293 1.000 15.71409 ? 317 CYS A CB    1 
ATOM   2477 S  SG    . CYS A 1 317 ? 11.55951  -8.03841  -40.38090 1.000 13.96573 ? 317 CYS A SG    1 
ATOM   2478 N  N     . LYS A 1 318 ? 13.14147  -9.36641  -43.09593 1.000 15.55882 ? 318 LYS A N     1 
ATOM   2479 C  CA    . LYS A 1 318 ? 12.47745  -9.92441  -44.26392 1.000 19.51842 ? 318 LYS A CA    1 
ATOM   2480 C  C     . LYS A 1 318 ? 10.97545  -9.66641  -44.21090 1.000 19.37300 ? 318 LYS A C     1 
ATOM   2481 O  O     . LYS A 1 318 ? 10.35047  -9.76142  -43.15088 1.000 19.52085 ? 318 LYS A O     1 
ATOM   2482 C  CB    . LYS A 1 318 ? 12.73846  -11.42341 -44.35692 1.000 23.06506 ? 318 LYS A CB    1 
ATOM   2483 C  CG    . LYS A 1 318 ? 12.21644  -12.03141 -45.64092 1.000 28.66258 ? 318 LYS A CG    1 
ATOM   2484 C  CD    . LYS A 1 318 ? 12.25944  -13.53341 -45.60592 1.000 23.05562 ? 318 LYS A CD    1 
ATOM   2485 C  CE    . LYS A 1 318 ? 12.11242  -14.06241 -47.00292 1.000 31.20681 ? 318 LYS A CE    1 
ATOM   2486 N  NZ    . LYS A 1 318 ? 13.07540  -13.39440 -47.92493 1.000 33.93864 ? 318 LYS A NZ    1 
ATOM   2487 N  N     . GLN A 1 319 ? 10.39543  -9.35341  -45.37189 1.000 18.01314 ? 319 GLN A N     1 
ATOM   2488 C  CA    . GLN A 1 319 ? 8.97543   -9.01642  -45.48786 1.000 19.17453 ? 319 GLN A CA    1 
ATOM   2489 C  C     . GLN A 1 319 ? 8.17543   -10.28742 -45.76285 1.000 18.25846 ? 319 GLN A C     1 
ATOM   2490 O  O     . GLN A 1 319 ? 8.12441   -10.77042 -46.89685 1.000 19.77070 ? 319 GLN A O     1 
ATOM   2491 C  CB    . GLN A 1 319 ? 8.77041   -7.98542  -46.59386 1.000 25.94331 ? 319 GLN A CB    1 
ATOM   2492 C  CG    . GLN A 1 319 ? 9.77640   -6.84042  -46.56587 1.000 22.95861 ? 319 GLN A CG    1 
ATOM   2493 C  CD    . GLN A 1 319 ? 9.61542   -5.96042  -45.34687 1.000 23.44269 ? 319 GLN A CD    1 
ATOM   2494 O  OE1   . GLN A 1 319 ? 8.50743   -5.55442  -45.00385 1.000 22.97691 ? 319 GLN A OE1   1 
ATOM   2495 N  NE2   . GLN A 1 319 ? 10.72443  -5.66241  -44.68089 1.000 24.82783 ? 319 GLN A NE2   1 
ATOM   2496 N  N     . ILE A 1 320 ? 7.52545   -10.81442 -44.72384 1.000 22.14142 ? 320 ILE A N     1 
ATOM   2497 C  CA    . ILE A 1 320 ? 6.70645   -12.02543 -44.79382 1.000 15.38650 ? 320 ILE A CA    1 
ATOM   2498 C  C     . ILE A 1 320 ? 5.25846   -11.63943 -44.52480 1.000 21.36416 ? 320 ILE A C     1 
ATOM   2499 O  O     . ILE A 1 320 ? 4.99747   -10.77243 -43.68280 1.000 18.87403 ? 320 ILE A O     1 
ATOM   2500 C  CB    . ILE A 1 320 ? 7.20947   -13.06543 -43.77283 1.000 18.14712 ? 320 ILE A CB    1 
ATOM   2501 C  CG1   . ILE A 1 320 ? 8.58147   -13.59342 -44.19286 1.000 21.17046 ? 320 ILE A CG1   1 
ATOM   2502 C  CG2   . ILE A 1 320 ? 6.21148   -14.19543 -43.59282 1.000 21.06721 ? 320 ILE A CG2   1 
ATOM   2503 C  CD1   . ILE A 1 320 ? 9.27849   -14.39042 -43.13287 1.000 19.22943 ? 320 ILE A CD1   1 
ATOM   2504 N  N     . ASP A 1 321 ? 4.31300   -12.27000 -45.22900 1.000 24.29854 ? 321 ASP A N     1 
ATOM   2505 C  CA    . ASP A 1 321 ? 2.90900   -11.80600 -45.10000 1.000 30.26601 ? 321 ASP A CA    1 
ATOM   2506 C  C     . ASP A 1 321 ? 2.21500   -12.51500 -43.93000 1.000 24.10849 ? 321 ASP A C     1 
ATOM   2507 O  O     . ASP A 1 321 ? 1.13800   -13.05200 -44.15000 1.000 31.30755 ? 321 ASP A O     1 
ATOM   2508 C  CB    . ASP A 1 321 ? 2.15200   -12.06300 -46.41700 1.000 35.54612 ? 321 ASP A CB    1 
ATOM   2509 C  CG    . ASP A 1 321 ? 2.81500   -11.51800 -47.69200 1.000 42.19371 ? 321 ASP A CG    1 
ATOM   2510 O  OD1   . ASP A 1 321 ? 3.30400   -10.36700 -47.65000 0.000 36.63207 ? 321 ASP A OD1   1 
ATOM   2511 O  OD2   . ASP A 1 321 ? 2.84900   -12.24000 -48.72400 0.000 38.76365 ? 321 ASP A OD2   1 
ATOM   2512 N  N     . TRP A 1 322 ? 2.71700   -12.34900 -42.72800 1.000 16.47021 ? 322 TRP A N     1 
ATOM   2513 C  CA    . TRP A 1 322 ? 2.12751   -13.00444 -41.53975 1.000 21.15462 ? 322 TRP A CA    1 
ATOM   2514 C  C     . TRP A 1 322 ? 0.59751   -12.94045 -41.52072 1.000 18.44548 ? 322 TRP A C     1 
ATOM   2515 O  O     . TRP A 1 322 ? 0.00950   -11.95945 -41.98371 1.000 22.16563 ? 322 TRP A O     1 
ATOM   2516 C  CB    . TRP A 1 322 ? 2.74853   -12.40044 -40.27276 1.000 18.56814 ? 322 TRP A CB    1 
ATOM   2517 C  CG    . TRP A 1 322 ? 4.24653   -12.50644 -40.20478 1.000 14.31421 ? 322 TRP A CG    1 
ATOM   2518 C  CD1   . TRP A 1 322 ? 5.15052   -11.50443 -40.38980 1.000 15.60983 ? 322 TRP A CD1   1 
ATOM   2519 C  CD2   . TRP A 1 322 ? 5.01354   -13.68643 -39.88980 1.000 15.15283 ? 322 TRP A CD2   1 
ATOM   2520 N  NE1   . TRP A 1 322 ? 6.42253   -11.97843 -40.22382 1.000 14.87484 ? 322 TRP A NE1   1 
ATOM   2521 C  CE2   . TRP A 1 322 ? 6.37154   -13.30843 -39.91582 1.000 11.91934 ? 322 TRP A CE2   1 
ATOM   2522 C  CE3   . TRP A 1 322 ? 4.68855   -15.01244 -39.59279 1.000 14.80492 ? 322 TRP A CE3   1 
ATOM   2523 C  CZ2   . TRP A 1 322 ? 7.39654   -14.21243 -39.65584 1.000 13.40331 ? 322 TRP A CZ2   1 
ATOM   2524 C  CZ3   . TRP A 1 322 ? 5.70556   -15.90343 -39.33781 1.000 15.13130 ? 322 TRP A CZ3   1 
ATOM   2525 C  CH2   . TRP A 1 322 ? 7.03955   -15.50643 -39.36683 1.000 12.07450 ? 322 TRP A CH2   1 
ATOM   2526 N  N     . ASP A 1 323 ? -0.01548  -13.96245 -40.94171 1.000 18.19691 ? 323 ASP A N     1 
ATOM   2527 C  CA    . ASP A 1 323 ? -1.46548  -13.99946 -40.81569 1.000 19.35757 ? 323 ASP A CA    1 
ATOM   2528 C  C     . ASP A 1 323 ? -1.94546  -13.05946 -39.71468 1.000 21.01364 ? 323 ASP A C     1 
ATOM   2529 O  O     . ASP A 1 323 ? -1.26244  -12.83146 -38.71169 1.000 25.22254 ? 323 ASP A O     1 
ATOM   2530 C  CB    . ASP A 1 323 ? -1.94747  -15.41946 -40.51968 1.000 22.05642 ? 323 ASP A CB    1 
ATOM   2531 C  CG    . ASP A 1 323 ? -1.76748  -16.35546 -41.69869 1.000 22.98227 ? 323 ASP A CG    1 
ATOM   2532 O  OD1   . ASP A 1 323 ? -1.37750  -15.87446 -42.78369 1.000 27.11726 ? 323 ASP A OD1   1 
ATOM   2533 O  OD2   . ASP A 1 323 ? -2.01147  -17.56846 -41.53668 1.000 17.99086 ? 323 ASP A OD2   1 
ATOM   2534 N  N     . ASP A 1 324 ? -3.14247  -12.51946 -39.91866 1.000 24.28355 ? 324 ASP A N     1 
ATOM   2535 C  CA    . ASP A 1 324 ? -3.82645  -11.65747 -38.96765 1.000 26.21589 ? 324 ASP A CA    1 
ATOM   2536 C  C     . ASP A 1 324 ? -4.93444  -12.48647 -38.31863 1.000 24.13795 ? 324 ASP A C     1 
ATOM   2537 O  O     . ASP A 1 324 ? -6.11045  -12.39747 -38.68461 1.000 28.39994 ? 324 ASP A O     1 
ATOM   2538 C  CB    . ASP A 1 324 ? -4.37247  -10.38947 -39.68864 1.000 27.33729 ? 324 ASP A CB    1 
ATOM   2539 C  CG    . ASP A 1 324 ? -5.00846  -9.39847  -38.72863 1.000 30.88946 ? 324 ASP A CG    1 
ATOM   2540 O  OD1   . ASP A 1 324 ? -4.77144  -9.49747  -37.51463 1.000 37.17657 ? 324 ASP A OD1   1 
ATOM   2541 O  OD2   . ASP A 1 324 ? -5.76047  -8.51447  -39.20462 1.000 40.73353 ? 324 ASP A OD2   1 
ATOM   2542 N  N     . ASN A 1 325 ? -4.54542  -13.31247 -37.34664 1.000 27.89929 ? 325 ASN A N     1 
ATOM   2543 C  CA    . ASN A 1 325 ? -5.45641  -14.22147 -36.65862 1.000 24.22610 ? 325 ASN A CA    1 
ATOM   2544 C  C     . ASN A 1 325 ? -5.59138  -13.78647 -35.20462 1.000 17.58037 ? 325 ASN A C     1 
ATOM   2545 O  O     . ASN A 1 325 ? -4.78937  -14.19447 -34.35063 1.000 17.58935 ? 325 ASN A O     1 
ATOM   2546 C  CB    . ASN A 1 325 ? -4.94940  -15.66347 -36.74763 1.000 23.38146 ? 325 ASN A CB    1 
ATOM   2547 C  CG    . ASN A 1 325 ? -6.04939  -16.69047 -36.53661 1.000 20.81792 ? 325 ASN A CG    1 
ATOM   2548 O  OD1   . ASN A 1 325 ? -6.11940  -17.68547 -37.25261 1.000 28.28547 ? 325 ASN A OD1   1 
ATOM   2549 N  ND2   . ASN A 1 325 ? -6.91238  -16.45448 -35.55460 1.000 23.01831 ? 325 ASN A ND2   1 
ATOM   2550 N  N     . PRO A 1 326 ? -6.59138  -12.97048 -34.86560 1.000 17.17132 ? 326 PRO A N     1 
ATOM   2551 C  CA    . PRO A 1 326 ? -6.73736  -12.54548 -33.46560 1.000 20.67132 ? 326 PRO A CA    1 
ATOM   2552 C  C     . PRO A 1 326 ? -7.05134  -13.69148 -32.52860 1.000 22.20114 ? 326 PRO A C     1 
ATOM   2553 O  O     . PRO A 1 326 ? -6.71532  -13.61948 -31.33960 1.000 18.41590 ? 326 PRO A O     1 
ATOM   2554 C  CB    . PRO A 1 326 ? -7.89336  -11.53548 -33.52058 1.000 25.45366 ? 326 PRO A CB    1 
ATOM   2555 C  CG    . PRO A 1 326 ? -8.03039  -11.16648 -34.96258 1.000 26.69103 ? 326 PRO A CG    1 
ATOM   2556 C  CD    . PRO A 1 326 ? -7.62340  -12.38248 -35.73059 1.000 19.04411 ? 326 PRO A CD    1 
ATOM   2557 N  N     . GLU A 1 327 ? -7.69034  -14.75048 -33.03159 1.000 17.64837 ? 327 GLU A N     1 
ATOM   2558 C  CA    . GLU A 1 327 ? -8.03333  -15.88148 -32.17758 1.000 19.78127 ? 327 GLU A CA    1 
ATOM   2559 C  C     . GLU A 1 327 ? -6.78732  -16.65748 -31.77260 1.000 18.49525 ? 327 GLU A C     1 
ATOM   2560 O  O     . GLU A 1 327 ? -6.61230  -16.99548 -30.59661 1.000 19.12111 ? 327 GLU A O     1 
ATOM   2561 C  CB    . GLU A 1 327 ? -9.03833  -16.79349 -32.88256 1.000 22.66570 ? 327 GLU A CB    1 
ATOM   2562 C  CG    . GLU A 1 327 ? -10.37834 -16.13949 -33.18654 1.000 25.16206 ? 327 GLU A CG    1 
ATOM   2563 C  CD    . GLU A 1 327 ? -10.34336 -15.26149 -34.43054 1.000 33.73916 ? 327 GLU A CD    1 
ATOM   2564 O  OE1   . GLU A 1 327 ? -9.42438  -15.42649 -35.26556 1.000 29.59386 ? 327 GLU A OE1   1 
ATOM   2565 O  OE2   . GLU A 1 327 ? -11.23837 -14.40349 -34.57353 1.000 34.25013 ? 327 GLU A OE2   1 
ATOM   2566 N  N     . PHE A 1 328 ? -5.90133  -16.93847 -32.73362 1.000 20.64551 ? 328 PHE A N     1 
ATOM   2567 C  CA    . PHE A 1 328 ? -4.65332  -17.62147 -32.40764 1.000 14.80327 ? 328 PHE A CA    1 
ATOM   2568 C  C     . PHE A 1 328 ? -3.79331  -16.78047 -31.47465 1.000 14.54612 ? 328 PHE A C     1 
ATOM   2569 O  O     . PHE A 1 328 ? -3.11829  -17.31347 -30.58666 1.000 19.19496 ? 328 PHE A O     1 
ATOM   2570 C  CB    . PHE A 1 328 ? -3.88034  -17.95747 -33.68465 1.000 18.97415 ? 328 PHE A CB    1 
ATOM   2571 C  CG    . PHE A 1 328 ? -4.38635  -19.17947 -34.40264 1.000 20.98584 ? 328 PHE A CG    1 
ATOM   2572 C  CD1   . PHE A 1 328 ? -5.32234  -20.01147 -33.81263 1.000 17.97423 ? 328 PHE A CD1   1 
ATOM   2573 C  CD2   . PHE A 1 328 ? -3.91637  -19.50047 -35.66265 1.000 19.33934 ? 328 PHE A CD2   1 
ATOM   2574 C  CE1   . PHE A 1 328 ? -5.78335  -21.12947 -34.46862 1.000 16.48794 ? 328 PHE A CE1   1 
ATOM   2575 C  CE2   . PHE A 1 328 ? -4.37638  -20.61647 -36.32364 1.000 16.88221 ? 328 PHE A CE2   1 
ATOM   2576 C  CZ    . PHE A 1 328 ? -5.31137  -21.43247 -35.72663 1.000 18.37423 ? 328 PHE A CZ    1 
ATOM   2577 N  N     . LEU A 1 329 ? -3.80232  -15.46047 -31.65865 1.000 17.86259 ? 329 LEU A N     1 
ATOM   2578 C  CA    . LEU A 1 329 ? -2.99931  -14.59447 -30.80366 1.000 16.27597 ? 329 LEU A CA    1 
ATOM   2579 C  C     . LEU A 1 329 ? -3.56228  -14.53947 -29.38865 1.000 16.26745 ? 329 LEU A C     1 
ATOM   2580 O  O     . LEU A 1 329 ? -2.80327  -14.55747 -28.41067 1.000 11.90799 ? 329 LEU A O     1 
ATOM   2581 C  CB    . LEU A 1 329 ? -2.91932  -13.19346 -31.41067 1.000 18.07603 ? 329 LEU A CB    1 
ATOM   2582 C  CG    . LEU A 1 329 ? -2.08731  -12.15046 -30.66168 1.000 18.04819 ? 329 LEU A CG    1 
ATOM   2583 C  CD1   . LEU A 1 329 ? -0.67231  -12.64346 -30.48370 1.000 17.10748 ? 329 LEU A CD1   1 
ATOM   2584 C  CD2   . LEU A 1 329 ? -2.10633  -10.82246 -31.40968 1.000 19.72194 ? 329 LEU A CD2   1 
ATOM   2585 N  N     . ALA A 1 330 ? -4.89228  -14.48047 -29.25963 1.000 13.74956 ? 330 ALA A N     1 
ATOM   2586 C  CA    . ALA A 1 330 ? -5.51026  -14.42047 -27.93862 1.000 13.14980 ? 330 ALA A CA    1 
ATOM   2587 C  C     . ALA A 1 330 ? -5.26324  -15.70047 -27.15363 1.000 11.85893 ? 330 ALA A C     1 
ATOM   2588 O  O     . ALA A 1 330 ? -4.96622  -15.64947 -25.95563 1.000 12.13448 ? 330 ALA A O     1 
ATOM   2589 C  CB    . ALA A 1 330 ? -7.00926  -14.15148 -28.06460 1.000 15.21092 ? 330 ALA A CB    1 
ATOM   2590 N  N     . ALA A 1 331 ? -5.37225  -16.85647 -27.81163 1.000 12.51279 ? 331 ALA A N     1 
ATOM   2591 C  CA    . ALA A 1 331 ? -5.13823  -18.12147 -27.12163 1.000 9.99774  ? 331 ALA A CA    1 
ATOM   2592 C  C     . ALA A 1 331 ? -3.68923  -18.24347 -26.67165 1.000 10.58704 ? 331 ALA A C     1 
ATOM   2593 O  O     . ALA A 1 331 ? -3.41421  -18.75147 -25.57966 1.000 8.91114  ? 331 ALA A O     1 
ATOM   2594 C  CB    . ALA A 1 331 ? -5.52424  -19.29347 -28.02562 1.000 9.67119  ? 331 ALA A CB    1 
ATOM   2595 N  N     . TRP A 1 332 ? -2.75424  -17.77747 -27.50267 1.000 8.86639  ? 332 TRP A N     1 
ATOM   2596 C  CA    . TRP A 1 332 ? -1.34323  -17.78046 -27.13269 1.000 9.61893  ? 332 TRP A CA    1 
ATOM   2597 C  C     . TRP A 1 332 ? -1.06622  -16.79146 -26.00670 1.000 11.23579 ? 332 TRP A C     1 
ATOM   2598 O  O     . TRP A 1 332 ? -0.33920  -17.10846 -25.05671 1.000 16.10860 ? 332 TRP A O     1 
ATOM   2599 C  CB    . TRP A 1 332 ? -0.50026  -17.46246 -28.36471 1.000 8.42676  ? 332 TRP A CB    1 
ATOM   2600 C  CG    . TRP A 1 332 ? 0.98475   -17.38345 -28.12673 1.000 10.14465 ? 332 TRP A CG    1 
ATOM   2601 C  CD1   . TRP A 1 332 ? 1.86575   -18.42345 -28.09375 1.000 11.72149 ? 332 TRP A CD1   1 
ATOM   2602 C  CD2   . TRP A 1 332 ? 1.76075   -16.19645 -27.93174 1.000 7.90377  ? 332 TRP A CD2   1 
ATOM   2603 N  NE1   . TRP A 1 332 ? 3.13975   -17.96145 -27.86877 1.000 12.73117 ? 332 TRP A NE1   1 
ATOM   2604 C  CE2   . TRP A 1 332 ? 3.10075   -16.59545 -27.76677 1.000 9.35297  ? 332 TRP A CE2   1 
ATOM   2605 C  CE3   . TRP A 1 332 ? 1.44974   -14.83545 -27.86274 1.000 11.06009 ? 332 TRP A CE3   1 
ATOM   2606 C  CZ2   . TRP A 1 332 ? 4.13075   -15.68244 -27.54578 1.000 7.76350  ? 332 TRP A CZ2   1 
ATOM   2607 C  CZ3   . TRP A 1 332 ? 2.47074   -13.93045 -27.64776 1.000 8.03571  ? 332 TRP A CZ3   1 
ATOM   2608 C  CH2   . TRP A 1 332 ? 3.79575   -14.35844 -27.48978 1.000 10.43500 ? 332 TRP A CH2   1 
ATOM   2609 N  N     . ARG A 1 333 ? -1.65537  -15.59607 -26.09165 1.000 11.09988 ? 333 ARG A N     1 
ATOM   2610 C  CA    . ARG A 1 333 ? -1.44129  -14.56465 -25.08170 1.000 9.71399  ? 333 ARG A CA    1 
ATOM   2611 C  C     . ARG A 1 333 ? -2.02161  -14.97237 -23.73129 1.000 11.75171 ? 333 ARG A C     1 
ATOM   2612 O  O     . ARG A 1 333 ? -1.42075  -14.70487 -22.68417 1.000 8.30235  ? 333 ARG A O     1 
ATOM   2613 C  CB    . ARG A 1 333 ? -2.05990  -13.24831 -25.55864 1.000 11.05365 ? 333 ARG A CB    1 
ATOM   2614 C  CG    . ARG A 1 333 ? -1.95558  -12.09588 -24.57140 1.000 14.75596 ? 333 ARG A CG    1 
ATOM   2615 C  CD    . ARG A 1 333 ? -2.61954  -10.82470 -25.10413 1.000 18.25081 ? 333 ARG A CD    1 
ATOM   2616 N  NE    . ARG A 1 333 ? -4.07564  -10.92142 -25.13449 1.000 21.62996 ? 333 ARG A NE    1 
ATOM   2617 C  CZ    . ARG A 1 333 ? -4.80537  -10.99150 -26.24008 1.000 15.68162 ? 333 ARG A CZ    1 
ATOM   2618 N  NH1   . ARG A 1 333 ? -4.24925  -10.96120 -27.43982 1.000 18.71184 ? 333 ARG A NH1   1 
ATOM   2619 N  NH2   . ARG A 1 333 ? -6.12843  -11.08575 -26.13939 1.000 22.78610 ? 333 ARG A NH2   1 
ATOM   2620 N  N     . GLU A 1 334 ? -3.18519  -15.61847 -23.73466 1.000 16.38885 ? 334 GLU A N     1 
ATOM   2621 C  CA    . GLU A 1 334 ? -3.88616  -15.99647 -22.51465 1.000 11.51900 ? 334 GLU A CA    1 
ATOM   2622 C  C     . GLU A 1 334 ? -3.48615  -17.37647 -22.00666 1.000 13.92721 ? 334 GLU A C     1 
ATOM   2623 O  O     . GLU A 1 334 ? -4.12813  -17.89347 -21.08465 1.000 12.10841 ? 334 GLU A O     1 
ATOM   2624 C  CB    . GLU A 1 334 ? -5.39517  -15.93848 -22.74462 1.000 12.63354 ? 334 GLU A CB    1 
ATOM   2625 C  CG    . GLU A 1 334 ? -5.88918  -14.53948 -23.09162 1.000 18.18451 ? 334 GLU A CG    1 
ATOM   2626 C  CD    . GLU A 1 334 ? -7.35519  -14.50148 -23.47459 1.000 18.22239 ? 334 GLU A CD    1 
ATOM   2627 O  OE1   . GLU A 1 334 ? -8.05218  -15.51948 -23.29958 1.000 14.68003 ? 334 GLU A OE1   1 
ATOM   2628 O  OE2   . GLU A 1 334 ? -7.81220  -13.44348 -23.95758 1.000 23.92287 ? 334 GLU A OE2   1 
ATOM   2629 N  N     . ALA A 1 335 ? -2.44916  -17.97747 -22.59367 1.000 14.14469 ? 335 ALA A N     1 
ATOM   2630 C  CA    . ALA A 1 335 ? -1.91715  -19.27246 -22.15968 1.000 12.48137 ? 335 ALA A CA    1 
ATOM   2631 C  C     . ALA A 1 335 ? -2.99114  -20.35747 -22.17267 1.000 11.28106 ? 335 ALA A C     1 
ATOM   2632 O  O     . ALA A 1 335 ? -3.11013  -21.14847 -21.23566 1.000 14.05416 ? 335 ALA A O     1 
ATOM   2633 C  CB    . ALA A 1 335 ? -1.26412  -19.16846 -20.77969 1.000 17.43805 ? 335 ALA A CB    1 
ATOM   2634 N  N     . ARG A 1 336 ? -3.77895  -20.39901 -23.24249 1.000 11.32264 ? 336 ARG A N     1 
ATOM   2635 C  CA    . ARG A 1 336 ? -4.77778  -21.44504 -23.43901 1.000 9.31675  ? 336 ARG A CA    1 
ATOM   2636 C  C     . ARG A 1 336 ? -4.61728  -22.07400 -24.81744 1.000 12.07665 ? 336 ARG A C     1 
ATOM   2637 O  O     . ARG A 1 336 ? -5.58322  -22.28099 -25.55531 1.000 12.52018 ? 336 ARG A O     1 
ATOM   2638 C  CB    . ARG A 1 336 ? -6.19375  -20.90710 -23.23580 1.000 10.65038 ? 336 ARG A CB    1 
ATOM   2639 C  CG    . ARG A 1 336 ? -6.50512  -19.61552 -23.97367 1.000 12.79419 ? 336 ARG A CG    1 
ATOM   2640 C  CD    . ARG A 1 336 ? -7.95876  -19.21178 -23.77787 1.000 10.11619 ? 336 ARG A CD    1 
ATOM   2641 N  NE    . ARG A 1 336 ? -8.26885  -17.94568 -24.43087 1.000 15.82689 ? 336 ARG A NE    1 
ATOM   2642 C  CZ    . ARG A 1 336 ? -8.71141  -17.82988 -25.67552 1.000 11.33967 ? 336 ARG A CZ    1 
ATOM   2643 N  NH1   . ARG A 1 336 ? -8.90770  -18.89039 -26.44123 1.000 16.52578 ? 336 ARG A NH1   1 
ATOM   2644 N  NH2   . ARG A 1 336 ? -8.96391  -16.61875 -26.16411 1.000 15.85117 ? 336 ARG A NH2   1 
ATOM   2645 N  N     . THR A 1 337 ? -3.37319  -22.39247 -25.18266 1.000 9.09051  ? 337 THR A N     1 
ATOM   2646 C  CA    . THR A 1 337 ? -3.12421  -23.08947 -26.43767 1.000 9.87333  ? 337 THR A CA    1 
ATOM   2647 C  C     . THR A 1 337 ? -3.43720  -24.57547 -26.35966 1.000 9.38972  ? 337 THR A C     1 
ATOM   2648 O  O     . THR A 1 337 ? -3.53921  -25.22647 -27.40466 1.000 10.28936 ? 337 THR A O     1 
ATOM   2649 C  CB    . THR A 1 337 ? -1.66621  -22.91946 -26.88069 1.000 8.84706  ? 337 THR A CB    1 
ATOM   2650 O  OG1   . THR A 1 337 ? -0.79420  -23.54746 -25.93470 1.000 9.95227  ? 337 THR A OG1   1 
ATOM   2651 C  CG2   . THR A 1 337 ? -1.30322  -21.45146 -27.00569 1.000 8.65438  ? 337 THR A CG2   1 
ATOM   2652 N  N     . GLY A 1 338 ? -3.59618  -25.12347 -25.16266 1.000 9.74239  ? 338 GLY A N     1 
ATOM   2653 C  CA    . GLY A 1 338 ? -3.77217  -26.54747 -25.00766 1.000 11.22855 ? 338 GLY A CA    1 
ATOM   2654 C  C     . GLY A 1 338 ? -2.48917  -27.34447 -25.01768 1.000 9.91151  ? 338 GLY A C     1 
ATOM   2655 O  O     . GLY A 1 338 ? -2.54216  -28.57047 -24.85268 1.000 14.11088 ? 338 GLY A O     1 
ATOM   2656 N  N     . PHE A 1 339 ? -1.34017  -26.69446 -25.22670 1.000 9.86394  ? 339 PHE A N     1 
ATOM   2657 C  CA    . PHE A 1 339 ? -0.04317  -27.34346 -25.10972 1.000 9.91848  ? 339 PHE A CA    1 
ATOM   2658 C  C     . PHE A 1 339 ? 0.55985   -26.95046 -23.77173 1.000 8.73726  ? 339 PHE A C     1 
ATOM   2659 O  O     . PHE A 1 339 ? 0.98585   -25.79545 -23.61673 1.000 9.24011  ? 339 PHE A O     1 
ATOM   2660 C  CB    . PHE A 1 339 ? 0.88081   -26.93545 -26.25973 1.000 8.78663  ? 339 PHE A CB    1 
ATOM   2661 C  CG    . PHE A 1 339 ? 0.44079   -27.44945 -27.60473 1.000 11.87583 ? 339 PHE A CG    1 
ATOM   2662 C  CD1   . PHE A 1 339 ? 0.80279   -28.72045 -28.03273 1.000 12.20341 ? 339 PHE A CD1   1 
ATOM   2663 C  CD2   . PHE A 1 339 ? -0.33823  -26.66746 -28.44071 1.000 11.71159 ? 339 PHE A CD2   1 
ATOM   2664 C  CE1   . PHE A 1 339 ? 0.39877   -29.19445 -29.26473 1.000 9.53512  ? 339 PHE A CE1   1 
ATOM   2665 C  CE2   . PHE A 1 339 ? -0.74725  -27.13746 -29.66771 1.000 9.45517  ? 339 PHE A CE2   1 
ATOM   2666 C  CZ    . PHE A 1 339 ? -0.37825  -28.40346 -30.08071 1.000 11.07084 ? 339 PHE A CZ    1 
ATOM   2667 N  N     . PRO A 1 340 ? 0.60587   -27.85146 -22.78273 1.000 8.86178  ? 340 PRO A N     1 
ATOM   2668 C  CA    . PRO A 1 340 ? 1.06289   -27.44845 -21.43874 1.000 10.97972 ? 340 PRO A CA    1 
ATOM   2669 C  C     . PRO A 1 340 ? 2.43689   -26.80545 -21.40876 1.000 10.53288 ? 340 PRO A C     1 
ATOM   2670 O  O     . PRO A 1 340 ? 2.66290   -25.89145 -20.60476 1.000 9.65758  ? 340 PRO A O     1 
ATOM   2671 C  CB    . PRO A 1 340 ? 1.04591   -28.77145 -20.66074 1.000 13.05858 ? 340 PRO A CB    1 
ATOM   2672 C  CG    . PRO A 1 340 ? 0.00790   -29.58746 -21.34672 1.000 9.54288  ? 340 PRO A CG    1 
ATOM   2673 C  CD    . PRO A 1 340 ? 0.10388   -29.23746 -22.80372 1.000 10.23733 ? 340 PRO A CD    1 
ATOM   2674 N  N     . TRP A 1 341 ? 3.36788   -27.26345 -22.24477 1.000 8.28477  ? 341 TRP A N     1 
ATOM   2675 C  CA    . TRP A 1 341 ? 4.68888   -26.64744 -22.26780 1.000 9.19674  ? 341 TRP A CA    1 
ATOM   2676 C  C     . TRP A 1 341 ? 4.59986   -25.17844 -22.65279 1.000 7.77803  ? 341 TRP A C     1 
ATOM   2677 O  O     . TRP A 1 341 ? 5.23287   -24.32644 -22.02280 1.000 7.87147  ? 341 TRP A O     1 
ATOM   2678 C  CB    . TRP A 1 341 ? 5.60286   -27.40044 -23.22981 1.000 11.06385 ? 341 TRP A CB    1 
ATOM   2679 C  CG    . TRP A 1 341 ? 6.98586   -26.82143 -23.32483 1.000 7.73015  ? 341 TRP A CG    1 
ATOM   2680 C  CD1   . TRP A 1 341 ? 7.53584   -26.19043 -24.40284 1.000 9.49747  ? 341 TRP A CD1   1 
ATOM   2681 C  CD2   . TRP A 1 341 ? 7.98988   -26.81543 -22.30185 1.000 8.15884  ? 341 TRP A CD2   1 
ATOM   2682 N  NE1   . TRP A 1 341 ? 8.81984   -25.79943 -24.11786 1.000 7.59536  ? 341 TRP A NE1   1 
ATOM   2683 C  CE2   . TRP A 1 341 ? 9.12387   -26.16743 -22.83287 1.000 7.39462  ? 341 TRP A CE2   1 
ATOM   2684 C  CE3   . TRP A 1 341 ? 8.04090   -27.29343 -20.98985 1.000 7.69730  ? 341 TRP A CE3   1 
ATOM   2685 C  CZ2   . TRP A 1 341 ? 10.29788  -25.98742 -22.09689 1.000 7.26104  ? 341 TRP A CZ2   1 
ATOM   2686 C  CZ3   . TRP A 1 341 ? 9.20291   -27.10943 -20.26187 1.000 7.57157  ? 341 TRP A CZ3   1 
ATOM   2687 C  CH2   . TRP A 1 341 ? 10.31690  -26.46442 -20.81789 1.000 10.26365 ? 341 TRP A CH2   1 
ATOM   2688 N  N     . ILE A 1 342 ? 3.79785   -24.86644 -23.66978 1.000 7.87294  ? 342 ILE A N     1 
ATOM   2689 C  CA    . ILE A 1 342 ? 3.64383   -23.48644 -24.11878 1.000 7.98678  ? 342 ILE A CA    1 
ATOM   2690 C  C     . ILE A 1 342 ? 2.88585   -22.66745 -23.07976 1.000 8.23904  ? 342 ILE A C     1 
ATOM   2691 O  O     . ILE A 1 342 ? 3.27985   -21.54445 -22.73777 1.000 8.33539  ? 342 ILE A O     1 
ATOM   2692 C  CB    . ILE A 1 342 ? 2.93881   -23.45445 -25.48877 1.000 9.08808  ? 342 ILE A CB    1 
ATOM   2693 C  CG1   . ILE A 1 342 ? 3.73280   -24.25244 -26.52478 1.000 8.71325  ? 342 ILE A CG1   1 
ATOM   2694 C  CG2   . ILE A 1 342 ? 2.71680   -22.01645 -25.94776 1.000 11.78373 ? 342 ILE A CG2   1 
ATOM   2695 C  CD1   . ILE A 1 342 ? 5.12279   -23.72444 -26.76180 1.000 7.69526  ? 342 ILE A CD1   1 
ATOM   2696 N  N     . ASP A 1 343 ? 1.78386   -23.21445 -22.56575 1.000 7.99767  ? 343 ASP A N     1 
ATOM   2697 C  CA    . ASP A 1 343 ? 0.96287   -22.48245 -21.60473 1.000 10.07085 ? 343 ASP A CA    1 
ATOM   2698 C  C     . ASP A 1 343 ? 1.70189   -22.22645 -20.29674 1.000 7.96486  ? 343 ASP A C     1 
ATOM   2699 O  O     . ASP A 1 343 ? 1.47290   -21.19845 -19.64874 1.000 10.37779 ? 343 ASP A O     1 
ATOM   2700 C  CB    . ASP A 1 343 ? -0.34012  -23.24146 -21.35171 1.000 8.42293  ? 343 ASP A CB    1 
ATOM   2701 C  CG    . ASP A 1 343 ? -1.22714  -23.29146 -22.58070 1.000 9.19175  ? 343 ASP A CG    1 
ATOM   2702 O  OD1   . ASP A 1 343 ? -1.04016  -22.43946 -23.47670 1.000 8.49844  ? 343 ASP A OD1   1 
ATOM   2703 O  OD2   . ASP A 1 343 ? -2.11514  -24.17546 -22.64568 1.000 8.90367  ? 343 ASP A OD2   1 
ATOM   2704 N  N     . ALA A 1 344 ? 2.59490   -23.13245 -19.89776 1.000 7.88792  ? 344 ALA A N     1 
ATOM   2705 C  CA    . ALA A 1 344 ? 3.34892   -22.92545 -18.66577 1.000 8.21286  ? 344 ALA A CA    1 
ATOM   2706 C  C     . ALA A 1 344 ? 4.37492   -21.80644 -18.81179 1.000 7.50834  ? 344 ALA A C     1 
ATOM   2707 O  O     . ALA A 1 344 ? 4.62793   -21.07044 -17.84979 1.000 8.75086  ? 344 ALA A O     1 
ATOM   2708 C  CB    . ALA A 1 344 ? 4.03093   -24.22445 -18.23978 1.000 7.86736  ? 344 ALA A CB    1 
ATOM   2709 N  N     . ILE A 1 345 ? 4.97190   -21.66044 -19.99480 1.000 7.34900  ? 345 ILE A N     1 
ATOM   2710 C  CA    . ILE A 1 345 ? 5.92689   -20.57844 -20.21181 1.000 7.11018  ? 345 ILE A CA    1 
ATOM   2711 C  C     . ILE A 1 345 ? 5.21088   -19.23444 -20.26380 1.000 8.27873  ? 345 ILE A C     1 
ATOM   2712 O  O     . ILE A 1 345 ? 5.67289   -18.24844 -19.67881 1.000 8.14568  ? 345 ILE A O     1 
ATOM   2713 C  CB    . ILE A 1 345 ? 6.73687   -20.83243 -21.49383 1.000 6.99688  ? 345 ILE A CB    1 
ATOM   2714 C  CG1   . ILE A 1 345 ? 7.42888   -22.19643 -21.42784 1.000 10.02902 ? 345 ILE A CG1   1 
ATOM   2715 C  CG2   . ILE A 1 345 ? 7.75386   -19.73243 -21.70084 1.000 9.56730  ? 345 ILE A CG2   1 
ATOM   2716 C  CD1   . ILE A 1 345 ? 8.15086   -22.56143 -22.69685 1.000 6.99788  ? 345 ILE A CD1   1 
ATOM   2717 N  N     . MET A 1 346 ? 4.06787   -19.17844 -20.95978 1.000 8.69611  ? 346 MET A N     1 
ATOM   2718 C  CA    . MET A 1 346 ? 3.30087   -17.93945 -21.05077 1.000 11.75266 ? 346 MET A CA    1 
ATOM   2719 C  C     . MET A 1 346 ? 2.73489   -17.52245 -19.69876 1.000 12.39509 ? 346 MET A C     1 
ATOM   2720 O  O     . MET A 1 346 ? 2.50789   -16.32845 -19.46476 1.000 10.92789 ? 346 MET A O     1 
ATOM   2721 C  CB    . MET A 1 346 ? 2.17485   -18.09245 -22.07175 1.000 11.32456 ? 346 MET A CB    1 
ATOM   2722 C  CG    . MET A 1 346 ? 2.66883   -18.33345 -23.48676 1.000 9.84610  ? 346 MET A CG    1 
ATOM   2723 S  SD    . MET A 1 346 ? 3.75381   -17.00444 -24.01578 1.000 10.96811 ? 346 MET A SD    1 
ATOM   2724 C  CE    . MET A 1 346 ? 2.66181   -15.59845 -23.82176 1.000 9.26787  ? 346 MET A CE    1 
ATOM   2725 N  N     . THR A 1 347 ? 2.57091   -18.48945 -18.81476 1.000 9.81102  ? 347 THR A N     1 
ATOM   2726 C  CA    . THR A 1 347 ? 2.09193   -18.16145 -17.45575 1.000 8.67359  ? 347 THR A CA    1 
ATOM   2727 C  C     . THR A 1 347 ? 3.28094   -17.64045 -16.63177 1.000 7.58507  ? 347 THR A C     1 
ATOM   2728 O  O     . THR A 1 347 ? 3.09295   -16.74945 -15.82477 1.000 9.37728  ? 347 THR A O     1 
ATOM   2729 C  CB    . THR A 1 347 ? 1.27194   -19.32946 -16.89374 1.000 13.74402 ? 347 THR A CB    1 
ATOM   2730 O  OG1   . THR A 1 347 ? 0.05193   -19.46546 -17.61772 1.000 12.83846 ? 347 THR A OG1   1 
ATOM   2731 C  CG2   . THR A 1 347 ? 0.98896   -19.17946 -15.41273 1.000 11.64614 ? 347 THR A CG2   1 
ATOM   2732 N  N     . GLN A 1 348 ? 4.46194   -18.19944 -16.84779 1.000 11.05412 ? 348 GLN A N     1 
ATOM   2733 C  CA    . GLN A 1 348 ? 5.65695   -17.68044 -16.18781 1.000 8.16663  ? 348 GLN A CA    1 
ATOM   2734 C  C     . GLN A 1 348 ? 5.93793   -16.24444 -16.61881 1.000 9.54891  ? 348 GLN A C     1 
ATOM   2735 O  O     . GLN A 1 348 ? 6.35695   -15.40944 -15.80482 1.000 7.11207  ? 348 GLN A O     1 
ATOM   2736 C  CB    . GLN A 1 348 ? 6.85794   -18.58144 -16.49283 1.000 8.22102  ? 348 GLN A CB    1 
ATOM   2737 C  CG    . GLN A 1 348 ? 8.11296   -18.24443 -15.70385 1.000 7.70861  ? 348 GLN A CG    1 
ATOM   2738 C  CD    . GLN A 1 348 ? 9.32295   -19.04643 -16.14487 1.000 7.34348  ? 348 GLN A CD    1 
ATOM   2739 O  OE1   . GLN A 1 348 ? 9.40393   -19.50343 -17.28487 1.000 11.36991 ? 348 GLN A OE1   1 
ATOM   2740 N  NE2   . GLN A 1 348 ? 10.26397  -19.23342 -15.23689 1.000 11.08778 ? 348 GLN A NE2   1 
ATOM   2741 N  N     . LEU A 1 349 ? 5.69591   -15.93744 -17.89681 1.000 7.47679  ? 349 LEU A N     1 
ATOM   2742 C  CA    . LEU A 1 349 ? 5.83890   -14.56944 -18.38681 1.000 8.60741  ? 349 LEU A CA    1 
ATOM   2743 C  C     . LEU A 1 349 ? 4.96091   -13.59844 -17.60480 1.000 10.67123 ? 349 LEU A C     1 
ATOM   2744 O  O     . LEU A 1 349 ? 5.42991   -12.54244 -17.16880 1.000 7.17071  ? 349 LEU A O     1 
ATOM   2745 C  CB    . LEU A 1 349 ? 5.50287   -14.50744 -19.87981 1.000 7.97467  ? 349 LEU A CB    1 
ATOM   2746 C  CG    . LEU A 1 349 ? 5.35686   -13.11744 -20.50780 1.000 7.40510  ? 349 LEU A CG    1 
ATOM   2747 C  CD1   . LEU A 1 349 ? 6.70685   -12.42544 -20.66882 1.000 8.63766  ? 349 LEU A CD1   1 
ATOM   2748 C  CD2   . LEU A 1 349 ? 4.64584   -13.19944 -21.84879 1.000 9.69901  ? 349 LEU A CD2   1 
ATOM   2749 N  N     . VAL A 1 350 ? 3.67891   -13.93045 -17.42478 1.000 8.12871  ? 350 VAL A N     1 
ATOM   2750 C  CA    . VAL A 1 350 ? 2.76792   -12.98245 -16.78176 1.000 12.18992 ? 350 VAL A CA    1 
ATOM   2751 C  C     . VAL A 1 350 ? 2.91895   -12.98445 -15.25876 1.000 11.67769 ? 350 VAL A C     1 
ATOM   2752 O  O     . VAL A 1 350 ? 2.60395   -11.98045 -14.60476 1.000 12.91293 ? 350 VAL A O     1 
ATOM   2753 C  CB    . VAL A 1 350 ? 1.30892   -13.25645 -17.19274 1.000 11.26541 ? 350 VAL A CB    1 
ATOM   2754 C  CG1   . VAL A 1 350 ? 1.14489   -13.12545 -18.68973 1.000 13.16060 ? 350 VAL A CG1   1 
ATOM   2755 C  CG2   . VAL A 1 350 ? 0.85893   -14.63146 -16.72273 1.000 14.47375 ? 350 VAL A CG2   1 
ATOM   2756 N  N     . THR A 1 351 ? 3.38696   -14.08445 -14.66277 1.000 8.30141  ? 351 THR A N     1 
ATOM   2757 C  CA    . THR A 1 351 ? 3.58698   -14.11945 -13.21577 1.000 9.56687  ? 351 THR A CA    1 
ATOM   2758 C  C     . THR A 1 351 ? 4.97399   -13.61744 -12.82280 1.000 9.83007  ? 351 THR A C     1 
ATOM   2759 O  O     . THR A 1 351 ? 5.09500   -12.75044 -11.95180 1.000 10.64516 ? 351 THR A O     1 
ATOM   2760 C  CB    . THR A 1 351 ? 3.36600   -15.53845 -12.66377 1.000 9.69460  ? 351 THR A CB    1 
ATOM   2761 O  OG1   . THR A 1 351 ? 4.26399   -16.45645 -13.29779 1.000 15.68650 ? 351 THR A OG1   1 
ATOM   2762 C  CG2   . THR A 1 351 ? 1.93300   -16.00245 -12.89175 1.000 9.43195  ? 351 THR A CG2   1 
ATOM   2763 N  N     . TRP A 1 352 ? 6.02698   -14.14044 -13.45181 1.000 8.84004  ? 352 TRP A N     1 
ATOM   2764 C  CA    . TRP A 1 352 ? 7.38698   -13.74144 -13.09684 1.000 12.11488 ? 352 TRP A CA    1 
ATOM   2765 C  C     . TRP A 1 352 ? 7.92097   -12.59043 -13.93885 1.000 8.85790  ? 352 TRP A C     1 
ATOM   2766 O  O     . TRP A 1 352 ? 8.70297   -11.77643 -13.43486 1.000 12.91933 ? 352 TRP A O     1 
ATOM   2767 C  CB    . TRP A 1 352 ? 8.35399   -14.91843 -13.23385 1.000 9.85623  ? 352 TRP A CB    1 
ATOM   2768 C  CG    . TRP A 1 352 ? 8.23701   -15.95043 -12.17785 1.000 9.97416  ? 352 TRP A CG    1 
ATOM   2769 C  CD1   . TRP A 1 352 ? 7.22402   -16.10044 -11.29183 1.000 11.91699 ? 352 TRP A CD1   1 
ATOM   2770 C  CD2   . TRP A 1 352 ? 9.18602   -16.98143 -11.88687 1.000 9.92212  ? 352 TRP A CD2   1 
ATOM   2771 N  NE1   . TRP A 1 352 ? 7.47204   -17.17044 -10.46684 1.000 16.19580 ? 352 TRP A NE1   1 
ATOM   2772 C  CE2   . TRP A 1 352 ? 8.67504   -17.72543 -10.80886 1.000 12.81520 ? 352 TRP A CE2   1 
ATOM   2773 C  CE3   . TRP A 1 352 ? 10.42201  -17.34343 -12.42889 1.000 15.45811 ? 352 TRP A CE3   1 
ATOM   2774 C  CZ2   . TRP A 1 352 ? 9.34805   -18.81943 -10.26887 1.000 12.69951 ? 352 TRP A CZ2   1 
ATOM   2775 C  CZ3   . TRP A 1 352 ? 11.09102  -18.43342 -11.88990 1.000 13.10029 ? 352 TRP A CZ3   1 
ATOM   2776 C  CH2   . TRP A 1 352 ? 10.55104  -19.15543 -10.82289 1.000 9.55619  ? 352 TRP A CH2   1 
ATOM   2777 N  N     . GLY A 1 353 ? 7.54895   -12.51443 -15.21284 1.000 9.72255  ? 353 GLY A N     1 
ATOM   2778 C  CA    . GLY A 1 353 ? 8.14693   -11.52943 -16.08885 1.000 7.69083  ? 353 GLY A CA    1 
ATOM   2779 C  C     . GLY A 1 353 ? 9.50292   -11.91143 -16.63387 1.000 8.30555  ? 353 GLY A C     1 
ATOM   2780 O  O     . GLY A 1 353 ? 10.16891  -11.06442 -17.23688 1.000 10.70679 ? 353 GLY A O     1 
ATOM   2781 N  N     . TRP A 1 354 ? 9.92993   -13.15843 -16.43888 1.000 6.59891  ? 354 TRP A N     1 
ATOM   2782 C  CA    . TRP A 1 354 ? 11.21992  -13.63442 -16.92090 1.000 8.72411  ? 354 TRP A CA    1 
ATOM   2783 C  C     . TRP A 1 354 ? 11.12392  -15.12642 -17.19790 1.000 8.43035  ? 354 TRP A C     1 
ATOM   2784 O  O     . TRP A 1 354 ? 10.65794  -15.88742 -16.34689 1.000 6.54165  ? 354 TRP A O     1 
ATOM   2785 C  CB    . TRP A 1 354 ? 12.33494  -13.36742 -15.90392 1.000 6.41469  ? 354 TRP A CB    1 
ATOM   2786 C  CG    . TRP A 1 354 ? 13.68593  -13.85041 -16.36394 1.000 6.27204  ? 354 TRP A CG    1 
ATOM   2787 C  CD1   . TRP A 1 354 ? 14.64692  -13.11241 -16.98496 1.000 6.16765  ? 354 TRP A CD1   1 
ATOM   2788 C  CD2   . TRP A 1 354 ? 14.21994  -15.17841 -16.23895 1.000 6.94950  ? 354 TRP A CD2   1 
ATOM   2789 N  NE1   . TRP A 1 354 ? 15.74892  -13.89341 -17.24998 1.000 6.09510  ? 354 TRP A NE1   1 
ATOM   2790 C  CE2   . TRP A 1 354 ? 15.51193  -15.16441 -16.80097 1.000 6.15522  ? 354 TRP A CE2   1 
ATOM   2791 C  CE3   . TRP A 1 354 ? 13.73495  -16.37441 -15.69494 1.000 8.70395  ? 354 TRP A CE3   1 
ATOM   2792 C  CZ2   . TRP A 1 354 ? 16.31593  -16.29940 -16.85299 1.000 6.15898  ? 354 TRP A CZ2   1 
ATOM   2793 C  CZ3   . TRP A 1 354 ? 14.53495  -17.49941 -15.74396 1.000 6.41181  ? 354 TRP A CZ3   1 
ATOM   2794 C  CH2   . TRP A 1 354 ? 15.81194  -17.45541 -16.32198 1.000 6.41315  ? 354 TRP A CH2   1 
ATOM   2795 N  N     . MET A 1 355 ? 11.56690  -15.53942 -18.38091 1.000 6.30406  ? 355 MET A N     1 
ATOM   2796 C  CA    . MET A 1 355 ? 11.69190  -16.94842 -18.71391 1.000 6.45844  ? 355 MET A CA    1 
ATOM   2797 C  C     . MET A 1 355 ? 13.09989  -17.20141 -19.23093 1.000 7.88117  ? 355 MET A C     1 
ATOM   2798 O  O     . MET A 1 355 ? 13.80688  -16.27341 -19.63094 1.000 6.11044  ? 355 MET A O     1 
ATOM   2799 C  CB    . MET A 1 355 ? 10.66389  -17.39442 -19.76689 1.000 7.29543  ? 355 MET A CB    1 
ATOM   2800 C  CG    . MET A 1 355 ? 9.25289   -16.86943 -19.55087 1.000 10.04868 ? 355 MET A CG    1 
ATOM   2801 S  SD    . MET A 1 355 ? 8.93387   -15.38243 -20.50886 1.000 11.41785 ? 355 MET A SD    1 
ATOM   2802 C  CE    . MET A 1 355 ? 8.86784   -16.05243 -22.16586 1.000 13.67890 ? 355 MET A CE    1 
ATOM   2803 N  N     . HIS A 1 356 ? 13.50290  -18.47041 -19.20994 1.000 7.78778  ? 356 HIS A N     1 
ATOM   2804 C  CA    . HIS A 1 356 ? 14.79389  -18.85041 -19.76396 1.000 6.19380  ? 356 HIS A CA    1 
ATOM   2805 C  C     . HIS A 1 356 ? 14.81187  -18.60441 -21.26896 1.000 6.14867  ? 356 HIS A C     1 
ATOM   2806 O  O     . HIS A 1 356 ? 13.77385  -18.61241 -21.93794 1.000 6.52386  ? 356 HIS A O     1 
ATOM   2807 C  CB    . HIS A 1 356 ? 15.09590  -20.32041 -19.46697 1.000 6.31412  ? 356 HIS A CB    1 
ATOM   2808 C  CG    . HIS A 1 356 ? 16.45590  -20.76640 -19.91399 1.000 6.80239  ? 356 HIS A CG    1 
ATOM   2809 N  ND1   . HIS A 1 356 ? 16.68888  -21.31340 -21.15599 1.000 7.54146  ? 356 HIS A ND1   1 
ATOM   2810 C  CD2   . HIS A 1 356 ? 17.65491  -20.75040 -19.28101 1.000 8.31431  ? 356 HIS A CD2   1 
ATOM   2811 C  CE1   . HIS A 1 356 ? 17.97088  -21.61040 -21.27402 1.000 8.88277  ? 356 HIS A CE1   1 
ATOM   2812 N  NE2   . HIS A 1 356 ? 18.58089  -21.27840 -20.15003 1.000 7.21065  ? 356 HIS A NE2   1 
ATOM   2813 N  N     . HIS A 1 357 ? 16.01586  -18.38340 -21.79598 1.000 6.57546  ? 357 HIS A N     1 
ATOM   2814 C  CA    . HIS A 1 357 ? 16.18183  -18.07440 -23.21198 1.000 6.09587  ? 357 HIS A CA    1 
ATOM   2815 C  C     . HIS A 1 357 ? 15.51682  -19.11140 -24.10797 1.000 6.21541  ? 357 HIS A C     1 
ATOM   2816 O  O     . HIS A 1 357 ? 14.83780  -18.75941 -25.07996 1.000 6.26271  ? 357 HIS A O     1 
ATOM   2817 C  CB    . HIS A 1 357 ? 17.66683  -17.96740 -23.53301 1.000 6.07908  ? 357 HIS A CB    1 
ATOM   2818 C  CG    . HIS A 1 357 ? 17.94780  -17.63940 -24.95701 1.000 6.12726  ? 357 HIS A CG    1 
ATOM   2819 N  ND1   . HIS A 1 357 ? 17.42179  -16.52840 -25.58000 1.000 6.43056  ? 357 HIS A ND1   1 
ATOM   2820 C  CD2   . HIS A 1 357 ? 18.69579  -18.27639 -25.88803 1.000 7.00176  ? 357 HIS A CD2   1 
ATOM   2821 C  CE1   . HIS A 1 357 ? 17.83577  -16.49440 -26.83301 1.000 7.20400  ? 357 HIS A CE1   1 
ATOM   2822 N  NE2   . HIS A 1 357 ? 18.61277  -17.54339 -27.04402 1.000 6.28818  ? 357 HIS A NE2   1 
ATOM   2823 N  N     . LEU A 1 358 ? 15.70383  -20.39640 -23.80398 1.000 6.30541  ? 358 LEU A N     1 
ATOM   2824 C  CA    . LEU A 1 358 ? 15.11382  -21.44441 -24.62497 1.000 7.25202  ? 358 LEU A CA    1 
ATOM   2825 C  C     . LEU A 1 358 ? 13.61582  -21.59241 -24.39494 1.000 6.52066  ? 358 LEU A C     1 
ATOM   2826 O  O     . LEU A 1 358 ? 12.91781  -22.10441 -25.27193 1.000 7.28865  ? 358 LEU A O     1 
ATOM   2827 C  CB    . LEU A 1 358 ? 15.82683  -22.77840 -24.37098 1.000 6.58802  ? 358 LEU A CB    1 
ATOM   2828 C  CG    . LEU A 1 358 ? 17.23682  -22.87940 -24.95800 1.000 7.73635  ? 358 LEU A CG    1 
ATOM   2829 C  CD1   . LEU A 1 358 ? 17.84683  -24.24940 -24.71201 1.000 8.17854  ? 358 LEU A CD1   1 
ATOM   2830 C  CD2   . LEU A 1 358 ? 17.19979  -22.56940 -26.44700 1.000 10.31453 ? 358 LEU A CD2   1 
ATOM   2831 N  N     . ALA A 1 359 ? 13.10784  -21.15641 -23.24493 1.000 6.45981  ? 359 ALA A N     1 
ATOM   2832 C  CA    . ALA A 1 359 ? 11.66284  -21.06642 -23.07991 1.000 6.53619  ? 359 ALA A CA    1 
ATOM   2833 C  C     . ALA A 1 359 ? 11.07782  -20.00942 -24.00690 1.000 6.51631  ? 359 ALA A C     1 
ATOM   2834 O  O     . ALA A 1 359 ? 10.02682  -20.22342 -24.62388 1.000 6.64871  ? 359 ALA A O     1 
ATOM   2835 C  CB    . ALA A 1 359 ? 11.32087  -20.76142 -21.62390 1.000 6.51849  ? 359 ALA A CB    1 
ATOM   2836 N  N     . ARG A 1 360 ? 11.75983  -18.87036 -24.14108 1.000 6.38941  ? 360 ARG A N     1 
ATOM   2837 C  CA    . ARG A 1 360 ? 11.30562  -17.84506 -25.07381 1.000 6.41405  ? 360 ARG A CA    1 
ATOM   2838 C  C     . ARG A 1 360 ? 11.36014  -18.33426 -26.51694 1.000 6.53626  ? 360 ARG A C     1 
ATOM   2839 O  O     . ARG A 1 360 ? 10.51363  -17.95160 -27.33067 1.000 6.65968  ? 360 ARG A O     1 
ATOM   2840 C  CB    . ARG A 1 360 ? 12.14050  -16.57596 -24.90234 1.000 6.29130  ? 360 ARG A CB    1 
ATOM   2841 C  CG    . ARG A 1 360 ? 12.28011  -16.12425 -23.45249 1.000 6.20394  ? 360 ARG A CG    1 
ATOM   2842 C  CD    . ARG A 1 360 ? 12.83154  -14.70738 -23.34370 1.000 7.43985  ? 360 ARG A CD    1 
ATOM   2843 N  NE    . ARG A 1 360 ? 13.18645  -14.38949 -21.96663 1.000 6.36872  ? 360 ARG A NE    1 
ATOM   2844 C  CZ    . ARG A 1 360 ? 13.54903  -13.19125 -21.53021 1.000 6.06519  ? 360 ARG A CZ    1 
ATOM   2845 N  NH1   . ARG A 1 360 ? 13.59577  -12.14446 -22.33698 1.000 6.09068  ? 360 ARG A NH1   1 
ATOM   2846 N  NH2   . ARG A 1 360 ? 13.87348  -13.04078 -20.24967 1.000 6.30916  ? 360 ARG A NH2   1 
ATOM   2847 N  N     . HIS A 1 361 ? 12.34877  -19.16941 -26.85092 1.000 6.54574  ? 361 HIS A N     1 
ATOM   2848 C  CA    . HIS A 1 361 ? 12.39675  -19.79841 -28.16892 1.000 6.71894  ? 361 HIS A CA    1 
ATOM   2849 C  C     . HIS A 1 361 ? 11.13875  -20.61242 -28.44190 1.000 7.83776  ? 361 HIS A C     1 
ATOM   2850 O  O     . HIS A 1 361 ? 10.61473  -20.60042 -29.56189 1.000 8.41313  ? 361 HIS A O     1 
ATOM   2851 C  CB    . HIS A 1 361 ? 13.61776  -20.71341 -28.27894 1.000 8.25904  ? 361 HIS A CB    1 
ATOM   2852 C  CG    . HIS A 1 361 ? 14.86475  -20.03140 -28.74396 1.000 8.04951  ? 361 HIS A CG    1 
ATOM   2853 N  ND1   . HIS A 1 361 ? 15.55173  -20.43240 -29.86997 1.000 9.73820  ? 361 HIS A ND1   1 
ATOM   2854 C  CD2   . HIS A 1 361 ? 15.56175  -18.99140 -28.22797 1.000 9.20644  ? 361 HIS A CD2   1 
ATOM   2855 C  CE1   . HIS A 1 361 ? 16.61272  -19.66240 -30.03199 1.000 12.50503 ? 361 HIS A CE1   1 
ATOM   2856 N  NE2   . HIS A 1 361 ? 16.64174  -18.77840 -29.04999 1.000 10.89231 ? 361 HIS A NE2   1 
ATOM   2857 N  N     . SER A 1 362 ? 10.66577  -21.36142 -27.44289 1.000 6.89734  ? 362 SER A N     1 
ATOM   2858 C  CA    . SER A 1 362 ? 9.53477   -22.25942 -27.66088 1.000 8.89629  ? 362 SER A CA    1 
ATOM   2859 C  C     . SER A 1 362 ? 8.25676   -21.48043 -27.95885 1.000 7.18332  ? 362 SER A C     1 
ATOM   2860 O  O     . SER A 1 362 ? 7.52475   -21.80643 -28.89884 1.000 7.39894  ? 362 SER A O     1 
ATOM   2861 C  CB    . SER A 1 362 ? 9.34179   -23.17142 -26.44687 1.000 9.17364  ? 362 SER A CB    1 
ATOM   2862 O  OG    . SER A 1 362 ? 10.34180  -24.17542 -26.39389 1.000 9.64896  ? 362 SER A OG    1 
ATOM   2863 N  N     . VAL A 1 363 ? 7.97177   -20.44543 -27.16685 1.000 7.05077  ? 363 VAL A N     1 
ATOM   2864 C  CA    . VAL A 1 363 ? 6.73277   -19.70243 -27.36683 1.000 8.83373  ? 363 VAL A CA    1 
ATOM   2865 C  C     . VAL A 1 363 ? 6.83574   -18.77643 -28.57383 1.000 8.30894  ? 363 VAL A C     1 
ATOM   2866 O  O     . VAL A 1 363 ? 5.83773   -18.54244 -29.26381 1.000 9.25284  ? 363 VAL A O     1 
ATOM   2867 C  CB    . VAL A 1 363 ? 6.35179   -18.92943 -26.08882 1.000 7.06588  ? 363 VAL A CB    1 
ATOM   2868 C  CG1   . VAL A 1 363 ? 5.96681   -19.89644 -24.98882 1.000 8.33893  ? 363 VAL A CG1   1 
ATOM   2869 C  CG2   . VAL A 1 363 ? 7.49579   -18.05043 -25.62984 1.000 6.84452  ? 363 VAL A CG2   1 
ATOM   2870 N  N     . ALA A 1 364 ? 8.02674   -18.24143 -28.85885 1.000 7.09021  ? 364 ALA A N     1 
ATOM   2871 C  CA    . ALA A 1 364 ? 8.17672   -17.36743 -30.01685 1.000 8.78045  ? 364 ALA A CA    1 
ATOM   2872 C  C     . ALA A 1 364 ? 8.09470   -18.15743 -31.31385 1.000 8.42795  ? 364 ALA A C     1 
ATOM   2873 O  O     . ALA A 1 364 ? 7.49168   -17.69643 -32.28684 1.000 8.62396  ? 364 ALA A O     1 
ATOM   2874 C  CB    . ALA A 1 364 ? 9.49571   -16.60542 -29.94487 1.000 7.01971  ? 364 ALA A CB    1 
ATOM   2875 N  N     . CYS A 1 365 ? 8.70170   -19.34543 -31.34986 1.000 7.42797  ? 365 CYS A N     1 
ATOM   2876 C  CA    . CYS A 1 365 ? 8.59068   -20.17843 -32.54186 1.000 10.09363 ? 365 CYS A CA    1 
ATOM   2877 C  C     . CYS A 1 365 ? 7.15368   -20.63043 -32.75584 1.000 11.30248 ? 365 CYS A C     1 
ATOM   2878 O  O     . CYS A 1 365 ? 6.64666   -20.60043 -33.88483 1.000 18.16675 ? 365 CYS A O     1 
ATOM   2879 C  CB    . CYS A 1 365 ? 9.52469   -21.38542 -32.43287 1.000 12.53765 ? 365 CYS A CB    1 
ATOM   2880 S  SG    . CYS A 1 365 ? 9.51667   -22.46542 -33.87987 1.000 8.07246  ? 365 CYS A SG    1 
ATOM   2881 N  N     . PHE A 1 366 ? 6.48470   -21.04343 -31.67782 1.000 7.85440  ? 366 PHE A N     1 
ATOM   2882 C  CA    . PHE A 1 366 ? 5.11370   -21.53044 -31.78280 1.000 8.95459  ? 366 PHE A CA    1 
ATOM   2883 C  C     . PHE A 1 366 ? 4.19069   -20.46644 -32.36279 1.000 9.15500  ? 366 PHE A C     1 
ATOM   2884 O  O     . PHE A 1 366 ? 3.34267   -20.76344 -33.20677 1.000 9.36254  ? 366 PHE A O     1 
ATOM   2885 C  CB    . PHE A 1 366 ? 4.62373   -21.97744 -30.40579 1.000 8.68953  ? 366 PHE A CB    1 
ATOM   2886 C  CG    . PHE A 1 366 ? 3.23773   -22.54944 -30.40577 1.000 12.38390 ? 366 PHE A CG    1 
ATOM   2887 C  CD1   . PHE A 1 366 ? 3.03373   -23.89544 -30.65077 1.000 11.76242 ? 366 PHE A CD1   1 
ATOM   2888 C  CD2   . PHE A 1 366 ? 2.13973   -21.74445 -30.14475 1.000 12.70668 ? 366 PHE A CD2   1 
ATOM   2889 C  CE1   . PHE A 1 366 ? 1.75273   -24.42545 -30.64675 1.000 18.49320 ? 366 PHE A CE1   1 
ATOM   2890 C  CE2   . PHE A 1 366 ? 0.85773   -22.26845 -30.14773 1.000 9.41205  ? 366 PHE A CE2   1 
ATOM   2891 C  CZ    . PHE A 1 366 ? 0.66473   -23.60845 -30.39973 1.000 10.45669 ? 366 PHE A CZ    1 
ATOM   2892 N  N     . LEU A 1 367 ? 4.35569   -19.21444 -31.93379 1.000 9.49483  ? 367 LEU A N     1 
ATOM   2893 C  CA    . LEU A 1 367 ? 3.48068   -18.15344 -32.41177 1.000 8.73718  ? 367 LEU A CA    1 
ATOM   2894 C  C     . LEU A 1 367 ? 3.78065   -17.78644 -33.85878 1.000 11.07177 ? 367 LEU A C     1 
ATOM   2895 O  O     . LEU A 1 367 ? 2.85864   -17.55444 -34.64576 1.000 13.77992 ? 367 LEU A O     1 
ATOM   2896 C  CB    . LEU A 1 367 ? 3.61569   -16.92744 -31.51678 1.000 8.05426  ? 367 LEU A CB    1 
ATOM   2897 C  CG    . LEU A 1 367 ? 2.81568   -15.71844 -31.98876 1.000 8.26569  ? 367 LEU A CG    1 
ATOM   2898 C  CD1   . LEU A 1 367 ? 1.34468   -15.87845 -31.64974 1.000 9.00373  ? 367 LEU A CD1   1 
ATOM   2899 C  CD2   . LEU A 1 367 ? 3.37468   -14.47944 -31.37177 1.000 8.07731  ? 367 LEU A CD2   1 
ATOM   2900 N  N     . THR A 1 368 ? 5.05865   -17.72544 -34.22880 1.000 11.59099 ? 368 THR A N     1 
ATOM   2901 C  CA    . THR A 1 368 ? 5.42962   -17.21343 -35.54181 1.000 9.69949  ? 368 THR A CA    1 
ATOM   2902 C  C     . THR A 1 368 ? 5.59061   -18.32443 -36.57281 1.000 11.72435 ? 368 THR A C     1 
ATOM   2903 O  O     . THR A 1 368 ? 4.60260   -18.90544 -37.02679 1.000 11.66485 ? 368 THR A O     1 
ATOM   2904 C  CB    . THR A 1 368 ? 6.72162   -16.39843 -35.45383 1.000 10.73631 ? 368 THR A CB    1 
ATOM   2905 O  OG1   . THR A 1 368 ? 7.77263   -17.23143 -34.95684 1.000 10.48370 ? 368 THR A OG1   1 
ATOM   2906 C  CG2   . THR A 1 368 ? 6.53863   -15.20443 -34.51982 1.000 11.66427 ? 368 THR A CG2   1 
ATOM   2907 N  N     . ARG A 1 369 ? 6.83617   -18.61407 -36.95126 1.000 8.78418  ? 369 ARG A N     1 
ATOM   2908 C  CA    . ARG A 1 369 ? 7.14337   -19.48664 -38.07902 1.000 11.84514 ? 369 ARG A CA    1 
ATOM   2909 C  C     . ARG A 1 369 ? 6.89633   -20.96459 -37.79541 1.000 11.78544 ? 369 ARG A C     1 
ATOM   2910 O  O     . ARG A 1 369 ? 7.06087   -21.78363 -38.70719 1.000 9.44058  ? 369 ARG A O     1 
ATOM   2911 C  CB    . ARG A 1 369 ? 8.60149   -19.28694 -38.49847 1.000 10.37255 ? 369 ARG A CB    1 
ATOM   2912 C  CG    . ARG A 1 369 ? 9.60591   -19.66305 -37.41744 1.000 10.00376 ? 369 ARG A CG    1 
ATOM   2913 C  CD    . ARG A 1 369 ? 11.02512  -19.73234 -37.96278 1.000 8.70882  ? 369 ARG A CD    1 
ATOM   2914 N  NE    . ARG A 1 369 ? 11.97706  -20.13606 -36.93462 1.000 13.99100 ? 369 ARG A NE    1 
ATOM   2915 C  CZ    . ARG A 1 369 ? 12.31738  -21.39219 -36.67977 1.000 12.91589 ? 369 ARG A CZ    1 
ATOM   2916 N  NH1   . ARG A 1 369 ? 11.81336  -22.39973 -37.37395 1.000 8.93944  ? 369 ARG A NH1   1 
ATOM   2917 N  NH2   . ARG A 1 369 ? 13.18494  -21.64373 -35.70426 1.000 14.50409 ? 369 ARG A NH2   1 
ATOM   2918 N  N     . GLY A 1 370 ? 6.50662   -21.33443 -36.58082 1.000 11.85668 ? 370 GLY A N     1 
ATOM   2919 C  CA    . GLY A 1 370 ? 6.38463   -22.74043 -36.25382 1.000 11.55795 ? 370 GLY A CA    1 
ATOM   2920 C  C     . GLY A 1 370 ? 4.98363   -23.30044 -36.37180 1.000 11.59540 ? 370 GLY A C     1 
ATOM   2921 O  O     . GLY A 1 370 ? 4.78362   -24.37644 -36.94780 1.000 14.13806 ? 370 GLY A O     1 
ATOM   2922 N  N     . ASP A 1 371 ? 4.00264   -22.58544 -35.82678 1.000 10.66561 ? 371 ASP A N     1 
ATOM   2923 C  CA    . ASP A 1 371 ? 2.65264   -23.12944 -35.75376 1.000 9.41120  ? 371 ASP A CA    1 
ATOM   2924 C  C     . ASP A 1 371 ? 1.58063   -22.13145 -36.17674 1.000 11.42226 ? 371 ASP A C     1 
ATOM   2925 O  O     . ASP A 1 371 ? 0.83161   -22.38745 -37.12673 1.000 16.65401 ? 371 ASP A O     1 
ATOM   2926 C  CB    . ASP A 1 371 ? 2.36967   -23.63445 -34.33376 1.000 9.37828  ? 371 ASP A CB    1 
ATOM   2927 C  CG    . ASP A 1 371 ? 3.24868   -24.81144 -33.94577 1.000 9.50056  ? 371 ASP A CG    1 
ATOM   2928 O  OD1   . ASP A 1 371 ? 4.38368   -24.58944 -33.47879 1.000 10.77019 ? 371 ASP A OD1   1 
ATOM   2929 O  OD2   . ASP A 1 371 ? 2.80768   -25.96644 -34.11176 1.000 16.39373 ? 371 ASP A OD2   1 
ATOM   2930 N  N     . LEU A 1 372 ? 1.48564   -20.99645 -35.48074 1.000 14.78453 ? 372 LEU A N     1 
ATOM   2931 C  CA    . LEU A 1 372 ? 0.33763   -20.11045 -35.63972 1.000 10.66698 ? 372 LEU A CA    1 
ATOM   2932 C  C     . LEU A 1 372 ? 0.49461   -19.10245 -36.77172 1.000 14.54192 ? 372 LEU A C     1 
ATOM   2933 O  O     . LEU A 1 372 ? -0.51340  -18.54945 -37.22971 1.000 14.17017 ? 372 LEU A O     1 
ATOM   2934 C  CB    . LEU A 1 372 ? 0.06265   -19.37345 -34.32572 1.000 12.55624 ? 372 LEU A CB    1 
ATOM   2935 C  CG    . LEU A 1 372 ? -0.20933  -20.27745 -33.12071 1.000 12.08397 ? 372 LEU A CG    1 
ATOM   2936 C  CD1   . LEU A 1 372 ? -0.43231  -19.46346 -31.85871 1.000 10.19929 ? 372 LEU A CD1   1 
ATOM   2937 C  CD2   . LEU A 1 372 ? -1.39533  -21.19246 -33.39869 1.000 15.12875 ? 372 LEU A CD2   1 
ATOM   2938 N  N     . TYR A 1 373 ? 1.72360   -18.85745 -37.23574 1.000 15.80289 ? 373 TYR A N     1 
ATOM   2939 C  CA    . TYR A 1 373 ? 1.99958   -17.93045 -38.33975 1.000 15.19994 ? 373 TYR A CA    1 
ATOM   2940 C  C     . TYR A 1 373 ? 1.44758   -16.53345 -38.06374 1.000 15.75010 ? 373 TYR A C     1 
ATOM   2941 O  O     . TYR A 1 373 ? 0.88756   -15.87445 -38.94473 1.000 15.70181 ? 373 TYR A O     1 
ATOM   2942 C  CB    . TYR A 1 373 ? 1.47256   -18.46545 -39.67274 1.000 19.19382 ? 373 TYR A CB    1 
ATOM   2943 C  CG    . TYR A 1 373 ? 2.43254   -18.22344 -40.81476 1.000 18.48099 ? 373 TYR A CG    1 
ATOM   2944 C  CD1   . TYR A 1 373 ? 3.59254   -18.97744 -40.93878 1.000 17.03340 ? 373 TYR A CD1   1 
ATOM   2945 C  CD2   . TYR A 1 373 ? 2.19052   -17.23644 -41.75975 1.000 17.86015 ? 373 TYR A CD2   1 
ATOM   2946 C  CE1   . TYR A 1 373 ? 4.47552   -18.76544 -41.96979 1.000 20.41535 ? 373 TYR A CE1   1 
ATOM   2947 C  CE2   . TYR A 1 373 ? 3.07450   -17.01644 -42.79577 1.000 21.19968 ? 373 TYR A CE2   1 
ATOM   2948 C  CZ    . TYR A 1 373 ? 4.21650   -17.78444 -42.89479 1.000 19.79574 ? 373 TYR A CZ    1 
ATOM   2949 O  OH    . TYR A 1 373 ? 5.10349   -17.57643 -43.92280 1.000 17.93208 ? 373 TYR A OH    1 
ATOM   2950 N  N     . VAL A 1 374 ? 1.61660   -16.07445 -36.83874 1.000 18.46769 ? 374 VAL A N     1 
ATOM   2951 C  CA    . VAL A 1 374 ? 1.25760   -14.71645 -36.45674 1.000 16.95817 ? 374 VAL A CA    1 
ATOM   2952 C  C     . VAL A 1 374 ? 2.52860   -13.88644 -36.44776 1.000 11.81052 ? 374 VAL A C     1 
ATOM   2953 O  O     . VAL A 1 374 ? 3.61360   -14.38744 -36.13777 1.000 11.88047 ? 374 VAL A O     1 
ATOM   2954 C  CB    . VAL A 1 374 ? 0.54262   -14.69045 -35.08972 1.000 17.08002 ? 374 VAL A CB    1 
ATOM   2955 C  CG1   . VAL A 1 374 ? 0.22162   -13.26645 -34.67172 1.000 23.74476 ? 374 VAL A CG1   1 
ATOM   2956 C  CG2   . VAL A 1 374 ? -0.72938  -15.52346 -35.15070 1.000 17.55359 ? 374 VAL A CG2   1 
ATOM   2957 N  N     . SER A 1 375 ? 2.39759   -12.61144 -36.81275 1.000 13.22801 ? 375 SER A N     1 
ATOM   2958 C  CA    . SER A 1 375 ? 3.54858   -11.72644 -36.91877 1.000 12.50378 ? 375 SER A CA    1 
ATOM   2959 C  C     . SER A 1 375 ? 4.31560   -11.63644 -35.60878 1.000 11.74659 ? 375 SER A C     1 
ATOM   2960 O  O     . SER A 1 375 ? 3.73062   -11.62844 -34.52178 1.000 10.74454 ? 375 SER A O     1 
ATOM   2961 C  CB    . SER A 1 375 ? 3.10157   -10.32744 -37.34076 1.000 13.61995 ? 375 SER A CB    1 
ATOM   2962 O  OG    . SER A 1 375 ? 4.14757   -9.39544  -37.12878 1.000 13.92482 ? 375 SER A OG    1 
ATOM   2963 N  N     . TRP A 1 376 ? 5.64360   -11.55043 -35.72181 1.000 11.64205 ? 376 TRP A N     1 
ATOM   2964 C  CA    . TRP A 1 376 ? 6.48962   -11.37343 -34.54882 1.000 10.25626 ? 376 TRP A CA    1 
ATOM   2965 C  C     . TRP A 1 376 ? 6.27263   -10.02543 -33.87582 1.000 12.86199 ? 376 TRP A C     1 
ATOM   2966 O  O     . TRP A 1 376 ? 6.59265   -9.88543  -32.68982 1.000 9.53051  ? 376 TRP A O     1 
ATOM   2967 C  CB    . TRP A 1 376 ? 7.96361   -11.52943 -34.92585 1.000 8.25541  ? 376 TRP A CB    1 
ATOM   2968 C  CG    . TRP A 1 376 ? 8.42659   -10.55042 -35.96485 1.000 11.73710 ? 376 TRP A CG    1 
ATOM   2969 C  CD1   . TRP A 1 376 ? 8.38857   -10.71342 -37.31685 1.000 11.24278 ? 376 TRP A CD1   1 
ATOM   2970 C  CD2   . TRP A 1 376 ? 8.99759   -9.25842  -35.73186 1.000 9.88628  ? 376 TRP A CD2   1 
ATOM   2971 N  NE1   . TRP A 1 376 ? 8.89756   -9.60142  -37.94186 1.000 12.84475 ? 376 TRP A NE1   1 
ATOM   2972 C  CE2   . TRP A 1 376 ? 9.28257   -8.69542  -36.98987 1.000 13.19936 ? 376 TRP A CE2   1 
ATOM   2973 C  CE3   . TRP A 1 376 ? 9.29761   -8.52342  -34.58287 1.000 8.99587  ? 376 TRP A CE3   1 
ATOM   2974 C  CZ2   . TRP A 1 376 ? 9.84956   -7.43042  -37.12988 1.000 10.84462 ? 376 TRP A CZ2   1 
ATOM   2975 C  CZ3   . TRP A 1 376 ? 9.85860   -7.27142  -34.72488 1.000 10.23744 ? 376 TRP A CZ3   1 
ATOM   2976 C  CH2   . TRP A 1 376 ? 10.12558  -6.73542  -35.98888 1.000 9.95491  ? 376 TRP A CH2   1 
ATOM   2977 N  N     . GLU A 1 377 ? 5.74961   -9.03043  -34.59581 1.000 8.62090  ? 377 GLU A N     1 
ATOM   2978 C  CA    . GLU A 1 377 ? 5.44462   -7.76044  -33.94680 1.000 10.07554 ? 377 GLU A CA    1 
ATOM   2979 C  C     . GLU A 1 377 ? 4.34064   -7.91744  -32.90678 1.000 14.74186 ? 377 GLU A C     1 
ATOM   2980 O  O     . GLU A 1 377 ? 4.37365   -7.24844  -31.86878 1.000 13.08759 ? 377 GLU A O     1 
ATOM   2981 C  CB    . GLU A 1 377 ? 5.04160   -6.71444  -34.98280 1.000 13.50974 ? 377 GLU A CB    1 
ATOM   2982 C  CG    . GLU A 1 377 ? 5.98958   -6.60043  -36.15381 1.000 10.09277 ? 377 GLU A CG    1 
ATOM   2983 C  CD    . GLU A 1 377 ? 5.68956   -5.39743  -37.01381 1.000 14.05700 ? 377 GLU A CD    1 
ATOM   2984 O  OE1   . GLU A 1 377 ? 5.68456   -4.27743  -36.46981 1.000 17.34250 ? 377 GLU A OE1   1 
ATOM   2985 O  OE2   . GLU A 1 377 ? 5.44054   -5.56943  -38.22480 1.000 14.05440 ? 377 GLU A OE2   1 
ATOM   2986 N  N     . ARG A 1 378 ? 3.36776   -8.79776  -33.16489 1.000 15.00601 ? 378 ARG A N     1 
ATOM   2987 C  CA    . ARG A 1 378 ? 2.28222   -9.02005  -32.21351 1.000 14.89837 ? 378 ARG A CA    1 
ATOM   2988 C  C     . ARG A 1 378 ? 2.78400   -9.72868  -30.96272 1.000 11.01272 ? 378 ARG A C     1 
ATOM   2989 O  O     . ARG A 1 378 ? 2.42272   -9.35979  -29.83873 1.000 9.95147  ? 378 ARG A O     1 
ATOM   2990 C  CB    . ARG A 1 378 ? 1.16462   -9.83433  -32.86740 1.000 15.33174 ? 378 ARG A CB    1 
ATOM   2991 C  CG    . ARG A 1 378 ? 0.50500   -9.19239  -34.07808 1.000 15.09976 ? 378 ARG A CG    1 
ATOM   2992 C  CD    . ARG A 1 378 ? -0.34345  -7.99059  -33.69078 1.000 21.41692 ? 378 ARG A CD    1 
ATOM   2993 N  NE    . ARG A 1 378 ? 0.45069   -6.77275  -33.59240 1.000 19.94401 ? 378 ARG A NE    1 
ATOM   2994 C  CZ    . ARG A 1 378 ? 0.65214   -5.93048  -34.59535 1.000 21.67822 ? 378 ARG A CZ    1 
ATOM   2995 N  NH1   . ARG A 1 378 ? 0.10726   -6.13014  -35.78406 1.000 18.72595 ? 378 ARG A NH1   1 
ATOM   2996 N  NH2   . ARG A 1 378 ? 1.41954   -4.86184  -34.40058 1.000 19.87522 ? 378 ARG A NH2   1 
ATOM   2997 N  N     . GLY A 1 379 ? 3.59867   -10.76944 -31.14077 1.000 8.17049  ? 379 GLY A N     1 
ATOM   2998 C  CA    . GLY A 1 379 ? 4.17770   -11.44244 -29.99578 1.000 11.87042 ? 379 GLY A CA    1 
ATOM   2999 C  C     . GLY A 1 379 ? 5.11971   -10.54944 -29.22680 1.000 8.93699  ? 379 GLY A C     1 
ATOM   3000 O  O     . GLY A 1 379 ? 5.21173   -10.64244 -27.99980 1.000 12.57719 ? 379 GLY A O     1 
ATOM   3001 N  N     . MET A 1 380 ? 5.82269   -9.66844  -29.92981 1.000 9.08539  ? 380 MET A N     1 
ATOM   3002 C  CA    . MET A 1 380 ? 6.66170   -8.69543  -29.24582 1.000 11.96725 ? 380 MET A CA    1 
ATOM   3003 C  C     . MET A 1 380 ? 5.83671   -7.82544  -28.30381 1.000 12.57309 ? 380 MET A C     1 
ATOM   3004 O  O     . MET A 1 380 ? 6.17373   -7.68444  -27.12481 1.000 12.27761 ? 380 MET A O     1 
ATOM   3005 C  CB    . MET A 1 380 ? 7.38268   -7.83743  -30.26783 1.000 9.95326  ? 380 MET A CB    1 
ATOM   3006 C  CG    . MET A 1 380 ? 8.50969   -7.03843  -29.70585 1.000 11.76977 ? 380 MET A CG    1 
ATOM   3007 S  SD    . MET A 1 380 ? 9.30666   -6.32542  -31.12687 1.000 19.37831 ? 380 MET A SD    1 
ATOM   3008 C  CE    . MET A 1 380 ? 8.01165   -5.24243  -31.73384 1.000 18.07010 ? 380 MET A CE    1 
ATOM   3009 N  N     . GLU A 1 381 ? 4.73970   -7.24944  -28.80779 1.000 12.03589 ? 381 GLU A N     1 
ATOM   3010 C  CA    . GLU A 1 381 ? 3.88671   -6.39244  -27.98878 1.000 9.05179  ? 381 GLU A CA    1 
ATOM   3011 C  C     . GLU A 1 381 ? 3.41774   -7.09544  -26.72177 1.000 10.85068 ? 381 GLU A C     1 
ATOM   3012 O  O     . GLU A 1 381 ? 3.21275   -6.44645  -25.68876 1.000 11.17965 ? 381 GLU A O     1 
ATOM   3013 C  CB    . GLU A 1 381 ? 2.68670   -5.92045  -28.81076 1.000 11.18962 ? 381 GLU A CB    1 
ATOM   3014 C  CG    . GLU A 1 381 ? 3.06667   -5.02844  -29.98276 1.000 16.56141 ? 381 GLU A CG    1 
ATOM   3015 C  CD    . GLU A 1 381 ? 1.96666   -4.92345  -31.01674 1.000 20.23709 ? 381 GLU A CD    1 
ATOM   3016 O  OE1   . GLU A 1 381 ? 0.94366   -5.61645  -30.85873 1.000 19.88995 ? 381 GLU A OE1   1 
ATOM   3017 O  OE2   . GLU A 1 381 ? 2.12364   -4.15345  -31.98975 1.000 28.40420 ? 381 GLU A OE2   1 
ATOM   3018 N  N     . VAL A 1 382 ? 3.24274   -8.41545  -26.77577 1.000 10.78215 ? 382 VAL A N     1 
ATOM   3019 C  CA    . VAL A 1 382 ? 2.89276   -9.15245  -25.56876 1.000 8.22436  ? 382 VAL A CA    1 
ATOM   3020 C  C     . VAL A 1 382 ? 4.09278   -9.23244  -24.63378 1.000 9.13985  ? 382 VAL A C     1 
ATOM   3021 O  O     . VAL A 1 382 ? 3.96780   -9.01444  -23.42278 1.000 7.50180  ? 382 VAL A O     1 
ATOM   3022 C  CB    . VAL A 1 382 ? 2.34976   -10.54445 -25.93075 1.000 8.62241  ? 382 VAL A CB    1 
ATOM   3023 C  CG1   . VAL A 1 382 ? 2.06578   -11.34545 -24.68175 1.000 10.29753 ? 382 VAL A CG1   1 
ATOM   3024 C  CG2   . VAL A 1 382 ? 1.08675   -10.41445 -26.76273 1.000 11.32855 ? 382 VAL A CG2   1 
ATOM   3025 N  N     . PHE A 1 383 ? 5.27777   -9.51344  -25.18880 1.000 7.36364  ? 383 PHE A N     1 
ATOM   3026 C  CA    . PHE A 1 383 ? 6.49878   -9.54643  -24.38782 1.000 7.91753  ? 383 PHE A CA    1 
ATOM   3027 C  C     . PHE A 1 383 ? 6.81279   -8.18743  -23.77783 1.000 10.12941 ? 383 PHE A C     1 
ATOM   3028 O  O     . PHE A 1 383 ? 7.21481   -8.10743  -22.61183 1.000 9.55510  ? 383 PHE A O     1 
ATOM   3029 C  CB    . PHE A 1 383 ? 7.67977   -10.01743 -25.23484 1.000 10.19366 ? 383 PHE A CB    1 
ATOM   3030 C  CG    . PHE A 1 383 ? 7.84977   -11.51443 -25.27284 1.000 6.79937  ? 383 PHE A CG    1 
ATOM   3031 C  CD1   . PHE A 1 383 ? 6.77878   -12.35843 -25.03983 1.000 6.89509  ? 383 PHE A CD1   1 
ATOM   3032 C  CD2   . PHE A 1 383 ? 9.08777   -12.07143 -25.53186 1.000 6.63780  ? 383 PHE A CD2   1 
ATOM   3033 C  CE1   . PHE A 1 383 ? 6.93879   -13.72943 -25.07483 1.000 6.83396  ? 383 PHE A CE1   1 
ATOM   3034 C  CE2   . PHE A 1 383 ? 9.25578   -13.43843 -25.56387 1.000 6.58034  ? 383 PHE A CE2   1 
ATOM   3035 C  CZ    . PHE A 1 383 ? 8.18278   -14.26943 -25.33685 1.000 6.67907  ? 383 PHE A CZ    1 
ATOM   3036 N  N     . GLU A 1 384 ? 6.65877   -7.10543  -24.55282 1.000 10.88924 ? 384 GLU A N     1 
ATOM   3037 C  CA    . GLU A 1 384 ? 6.98478   -5.77743  -24.03283 1.000 12.20753 ? 384 GLU A CA    1 
ATOM   3038 C  C     . GLU A 1 384 ? 6.09179   -5.40044  -22.86281 1.000 11.58086 ? 384 GLU A C     1 
ATOM   3039 O  O     . GLU A 1 384 ? 6.48081   -4.58644  -22.01782 1.000 14.46374 ? 384 GLU A O     1 
ATOM   3040 C  CB    . GLU A 1 384 ? 6.87000   -4.72800  -25.13400 1.000 15.17041 ? 384 GLU A CB    1 
ATOM   3041 C  CG    . GLU A 1 384 ? 7.46400   -5.19200  -26.45100 1.000 20.92445 ? 384 GLU A CG    1 
ATOM   3042 C  CD    . GLU A 1 384 ? 8.62900   -4.37200  -26.99700 1.000 22.51130 ? 384 GLU A CD    1 
ATOM   3043 O  OE1   . GLU A 1 384 ? 8.39800   -3.23600  -27.47000 1.000 31.11900 ? 384 GLU A OE1   1 
ATOM   3044 O  OE2   . GLU A 1 384 ? 9.76400   -4.90200  -26.98900 1.000 22.19940 ? 384 GLU A OE2   1 
ATOM   3045 N  N     . GLU A 1 385 ? 4.89580   -5.98544  -22.79479 1.000 9.13491  ? 385 GLU A N     1 
ATOM   3046 C  CA    . GLU A 1 385 ? 3.97781   -5.66944  -21.70778 1.000 11.67293 ? 385 GLU A CA    1 
ATOM   3047 C  C     . GLU A 1 385 ? 4.42884   -6.30644  -20.39779 1.000 12.75105 ? 385 GLU A C     1 
ATOM   3048 O  O     . GLU A 1 385 ? 4.32885   -5.68244  -19.33478 1.000 13.17199 ? 385 GLU A O     1 
ATOM   3049 C  CB    . GLU A 1 385 ? 2.56581   -6.13345  -22.07475 1.000 13.87980 ? 385 GLU A CB    1 
ATOM   3050 C  CG    . GLU A 1 385 ? 1.46182   -5.64045  -21.15274 1.000 12.03816 ? 385 GLU A CG    1 
ATOM   3051 C  CD    . GLU A 1 385 ? 0.08382   -6.10046  -21.60671 1.000 21.92117 ? 385 GLU A CD    1 
ATOM   3052 O  OE1   . GLU A 1 385 ? -0.06220  -6.46046  -22.79371 1.000 24.96233 ? 385 GLU A OE1   1 
ATOM   3053 O  OE2   . GLU A 1 385 ? -0.85117  -6.11246  -20.77870 1.000 17.67429 ? 385 GLU A OE2   1 
ATOM   3054 N  N     . HIS A 1 386 ? 4.94784   -7.53644  -20.45379 1.000 8.71221  ? 386 HIS A N     1 
ATOM   3055 C  CA    . HIS A 1 386 ? 5.10186   -8.36744  -19.26480 1.000 9.44441  ? 386 HIS A CA    1 
ATOM   3056 C  C     . HIS A 1 386 ? 6.54287   -8.62044  -18.83882 1.000 7.13179  ? 386 HIS A C     1 
ATOM   3057 O  O     . HIS A 1 386 ? 6.77989   -8.83744  -17.65083 1.000 9.18931  ? 386 HIS A O     1 
ATOM   3058 C  CB    . HIS A 1 386 ? 4.40287   -9.72444  -19.46779 1.000 9.39897  ? 386 HIS A CB    1 
ATOM   3059 C  CG    . HIS A 1 386 ? 2.91486   -9.62745  -19.62676 1.000 7.65706  ? 386 HIS A CG    1 
ATOM   3060 N  ND1   . HIS A 1 386 ? 2.05688   -9.50945  -18.55375 1.000 9.71530  ? 386 HIS A ND1   1 
ATOM   3061 C  CD2   . HIS A 1 386 ? 2.13184   -9.63645  -20.73175 1.000 14.25377 ? 386 HIS A CD2   1 
ATOM   3062 C  CE1   . HIS A 1 386 ? 0.81087   -9.43646  -18.99073 1.000 9.25983  ? 386 HIS A CE1   1 
ATOM   3063 N  NE2   . HIS A 1 386 ? 0.82885   -9.51346  -20.30973 1.000 11.79201 ? 386 HIS A NE2   1 
ATOM   3064 N  N     . LEU A 1 387 ? 7.50686   -8.61143  -19.75584 1.000 6.95241  ? 387 LEU A N     1 
ATOM   3065 C  CA    . LEU A 1 387 ? 8.89386   -8.90243  -19.39186 1.000 6.74957  ? 387 LEU A CA    1 
ATOM   3066 C  C     . LEU A 1 387 ? 9.48187   -7.80443  -18.50987 1.000 6.80892  ? 387 LEU A C     1 
ATOM   3067 O  O     . LEU A 1 387 ? 9.43086   -6.62343  -18.85587 1.000 11.11192 ? 387 LEU A O     1 
ATOM   3068 C  CB    . LEU A 1 387 ? 9.75584   -9.05642  -20.64187 1.000 6.60138  ? 387 LEU A CB    1 
ATOM   3069 C  CG    . LEU A 1 387 ? 9.80684   -10.39942 -21.36688 1.000 6.49803  ? 387 LEU A CG    1 
ATOM   3070 C  CD1   . LEU A 1 387 ? 10.74182  -10.28042 -22.54789 1.000 6.41488  ? 387 LEU A CD1   1 
ATOM   3071 C  CD2   . LEU A 1 387 ? 10.27386  -11.50342 -20.43488 1.000 6.39958  ? 387 LEU A CD2   1 
ATOM   3072 N  N     . ILE A 1 388 ? 10.06789  -8.19042  -17.37488 1.000 8.83638  ? 388 ILE A N     1 
ATOM   3073 C  CA    . ILE A 1 388 ? 10.74191  -7.19942  -16.53789 1.000 7.81459  ? 388 ILE A CA    1 
ATOM   3074 C  C     . ILE A 1 388 ? 12.09389  -6.79742  -17.10391 1.000 10.09062 ? 388 ILE A C     1 
ATOM   3075 O  O     . ILE A 1 388 ? 12.66790  -5.79042  -16.66192 1.000 10.43062 ? 388 ILE A O     1 
ATOM   3076 C  CB    . ILE A 1 388 ? 10.90293  -7.69042  -15.08489 1.000 10.90994 ? 388 ILE A CB    1 
ATOM   3077 C  CG1   . ILE A 1 388 ? 11.70794  -8.99242  -15.00791 1.000 10.03687 ? 388 ILE A CG1   1 
ATOM   3078 C  CG2   . ILE A 1 388 ? 9.54294   -7.85443  -14.41887 1.000 9.78032  ? 388 ILE A CG2   1 
ATOM   3079 C  CD1   . ILE A 1 388 ? 11.98296  -9.44442  -13.57591 1.000 9.67054  ? 388 ILE A CD1   1 
ATOM   3080 N  N     . ASP A 1 389 ? 12.60988  -7.53642  -18.08892 1.000 9.02434  ? 389 ASP A N     1 
ATOM   3081 C  CA    . ASP A 1 389 ? 13.85687  -7.18541  -18.75394 1.000 7.16626  ? 389 ASP A CA    1 
ATOM   3082 C  C     . ASP A 1 389 ? 13.63084  -6.62541  -20.15994 1.000 6.45543  ? 389 ASP A C     1 
ATOM   3083 O  O     . ASP A 1 389 ? 14.57383  -6.56041  -20.95195 1.000 6.38736  ? 389 ASP A O     1 
ATOM   3084 C  CB    . ASP A 1 389 ? 14.80187  -8.39241  -18.78396 1.000 6.25518  ? 389 ASP A CB    1 
ATOM   3085 C  CG    . ASP A 1 389 ? 14.21686  -9.60941  -19.50495 1.000 6.18218  ? 389 ASP A CG    1 
ATOM   3086 O  OD1   . ASP A 1 389 ? 13.16385  -9.51141  -20.17593 1.000 6.61064  ? 389 ASP A OD1   1 
ATOM   3087 O  OD2   . ASP A 1 389 ? 14.83287  -10.68741 -19.40396 1.000 6.09180  ? 389 ASP A OD2   1 
ATOM   3088 N  N     . GLN A 1 390 ? 12.39884  -6.21142  -20.47192 1.000 6.59965  ? 390 GLN A N     1 
ATOM   3089 C  CA    . GLN A 1 390 ? 12.03181  -5.63942  -21.76591 1.000 6.70009  ? 390 GLN A CA    1 
ATOM   3090 C  C     . GLN A 1 390 ? 13.04980  -4.61141  -22.24293 1.000 7.51581  ? 390 GLN A C     1 
ATOM   3091 O  O     . GLN A 1 390 ? 13.15981  -3.52141  -21.67693 1.000 7.17293  ? 390 GLN A O     1 
ATOM   3092 C  CB    . GLN A 1 390 ? 10.63381  -5.01242  -21.68689 1.000 7.86186  ? 390 GLN A CB    1 
ATOM   3093 C  CG    . GLN A 1 390 ? 10.18079  -4.29342  -22.94988 1.000 11.72076 ? 390 GLN A CG    1 
ATOM   3094 C  CD    . GLN A 1 390 ? 10.53278  -2.81442  -22.95789 1.000 16.17037 ? 390 GLN A CD    1 
ATOM   3095 O  OE1   . GLN A 1 390 ? 10.75376  -2.22342  -24.01789 1.000 15.37318 ? 390 GLN A OE1   1 
ATOM   3096 N  NE2   . GLN A 1 390 ? 10.58280  -2.20942  -21.77689 1.000 10.72781 ? 390 GLN A NE2   1 
ATOM   3097 N  N     . ASP A 1 391 ? 13.80279  -4.96041  -23.27894 1.000 11.70394 ? 391 ASP A N     1 
ATOM   3098 C  CA    . ASP A 1 391 ? 14.81677  -4.09241  -23.86196 1.000 7.28347  ? 391 ASP A CA    1 
ATOM   3099 C  C     . ASP A 1 391 ? 14.48475  -3.90741  -25.33695 1.000 7.87084  ? 391 ASP A C     1 
ATOM   3100 O  O     . ASP A 1 391 ? 14.35674  -4.89141  -26.07095 1.000 7.29565  ? 391 ASP A O     1 
ATOM   3101 C  CB    . ASP A 1 391 ? 16.21378  -4.68940  -23.66698 1.000 6.86160  ? 391 ASP A CB    1 
ATOM   3102 C  CG    . ASP A 1 391 ? 17.32377  -3.75340  -24.11300 1.000 8.32544  ? 391 ASP A CG    1 
ATOM   3103 O  OD1   . ASP A 1 391 ? 17.42675  -3.50140  -25.32500 1.000 8.04317  ? 391 ASP A OD1   1 
ATOM   3104 O  OD2   . ASP A 1 391 ? 18.09678  -3.28140  -23.24701 1.000 9.51183  ? 391 ASP A OD2   1 
ATOM   3105 N  N     . HIS A 1 392 ? 14.34374  -2.64441  -25.75595 1.000 9.34185  ? 392 HIS A N     1 
ATOM   3106 C  CA    . HIS A 1 392 ? 13.90671  -2.29641  -27.10694 1.000 8.32336  ? 392 HIS A CA    1 
ATOM   3107 C  C     . HIS A 1 392 ? 14.63870  -3.10441  -28.17495 1.000 9.13220  ? 392 HIS A C     1 
ATOM   3108 O  O     . HIS A 1 392 ? 14.01800  -3.79400  -28.99100 1.000 10.96939 ? 392 HIS A O     1 
ATOM   3109 C  CB    . HIS A 1 392 ? 14.11500  -0.79800  -27.32800 1.000 14.38251 ? 392 HIS A CB    1 
ATOM   3110 C  CG    . HIS A 1 392 ? 13.56500  -0.29000  -28.62700 1.000 17.70069 ? 392 HIS A CG    1 
ATOM   3111 N  ND1   . HIS A 1 392 ? 12.24200  0.06200   -28.78900 1.000 21.40032 ? 392 HIS A ND1   1 
ATOM   3112 C  CD2   . HIS A 1 392 ? 14.16200  -0.06800  -29.82200 1.000 20.43761 ? 392 HIS A CD2   1 
ATOM   3113 C  CE1   . HIS A 1 392 ? 12.04700  0.47500   -30.02900 1.000 17.84451 ? 392 HIS A CE1   1 
ATOM   3114 N  NE2   . HIS A 1 392 ? 13.19600  0.40700   -30.67600 1.000 18.78738 ? 392 HIS A NE2   1 
ATOM   3115 N  N     . TYR A 1 393 ? 15.96970  -3.04540  -28.16798 1.000 10.04065 ? 393 TYR A N     1 
ATOM   3116 C  CA    . TYR A 1 393 ? 16.75868  -3.69440  -29.20999 1.000 7.36205  ? 393 TYR A CA    1 
ATOM   3117 C  C     . TYR A 1 393 ? 16.86369  -5.20140  -29.02899 1.000 6.97146  ? 393 TYR A C     1 
ATOM   3118 O  O     . TYR A 1 393 ? 16.91168  -5.93340  -30.02299 1.000 7.02728  ? 393 TYR A O     1 
ATOM   3119 C  CB    . TYR A 1 393 ? 18.15868  -3.08139  -29.25801 1.000 7.25883  ? 393 TYR A CB    1 
ATOM   3120 C  CG    . TYR A 1 393 ? 18.17267  -1.64239  -29.72301 1.000 8.86018  ? 393 TYR A CG    1 
ATOM   3121 C  CD1   . TYR A 1 393 ? 17.52965  -1.26540  -30.89900 1.000 10.42416 ? 393 TYR A CD1   1 
ATOM   3122 C  CD2   . TYR A 1 393 ? 18.82068  -0.66039  -28.98702 1.000 7.80037  ? 393 TYR A CD2   1 
ATOM   3123 C  CE1   . TYR A 1 393 ? 17.53963  0.04760   -31.32800 1.000 9.30240  ? 393 TYR A CE1   1 
ATOM   3124 C  CE2   . TYR A 1 393 ? 18.83666  0.65061   -29.40902 1.000 13.07451 ? 393 TYR A CE2   1 
ATOM   3125 C  CZ    . TYR A 1 393 ? 18.19164  0.99961   -30.58001 1.000 12.15798 ? 393 TYR A CZ    1 
ATOM   3126 O  OH    . TYR A 1 393 ? 18.20963  2.30861   -30.99401 1.000 14.00431 ? 393 TYR A OH    1 
ATOM   3127 N  N     . LEU A 1 394 ? 16.91071  -5.68440  -27.78999 1.000 8.65114  ? 394 LEU A N     1 
ATOM   3128 C  CA    . LEU A 1 394 ? 17.06572  -7.12040  -27.57500 1.000 6.57169  ? 394 LEU A CA    1 
ATOM   3129 C  C     . LEU A 1 394 ? 15.77572  -7.87440  -27.88897 1.000 6.58607  ? 394 LEU A C     1 
ATOM   3130 O  O     . LEU A 1 394 ? 15.80371  -8.92340  -28.53998 1.000 6.57902  ? 394 LEU A O     1 
ATOM   3131 C  CB    . LEU A 1 394 ? 17.51275  -7.38240  -26.13700 1.000 6.39177  ? 394 LEU A CB    1 
ATOM   3132 C  CG    . LEU A 1 394 ? 18.75275  -6.60439  -25.69002 1.000 6.40421  ? 394 LEU A CG    1 
ATOM   3133 C  CD1   . LEU A 1 394 ? 19.19878  -7.02239  -24.29903 1.000 6.26420  ? 394 LEU A CD1   1 
ATOM   3134 C  CD2   . LEU A 1 394 ? 19.87674  -6.78739  -26.69204 1.000 9.58321  ? 394 LEU A CD2   1 
ATOM   3135 N  N     . ASN A 1 395 ? 14.63872  -7.34941  -27.43196 1.000 6.64211  ? 395 ASN A N     1 
ATOM   3136 C  CA    . ASN A 1 395 ? 13.34172  -7.95341  -27.73093 1.000 6.70308  ? 395 ASN A CA    1 
ATOM   3137 C  C     . ASN A 1 395 ? 13.07970  -7.95441  -29.23993 1.000 7.88879  ? 395 ASN A C     1 
ATOM   3138 O  O     . ASN A 1 395 ? 12.58869  -8.94541  -29.79192 1.000 6.97232  ? 395 ASN A O     1 
ATOM   3139 C  CB    . ASN A 1 395 ? 12.27100  -7.17300  -26.96800 1.000 6.78502  ? 395 ASN A CB    1 
ATOM   3140 C  CG    . ASN A 1 395 ? 11.11100  -8.00000  -26.45600 1.000 9.00716  ? 395 ASN A CG    1 
ATOM   3141 O  OD1   . ASN A 1 395 ? 10.12800  -8.19500  -27.16200 1.000 9.90713  ? 395 ASN A OD1   1 
ATOM   3142 N  ND2   . ASN A 1 395 ? 11.24300  -8.48900  -25.22600 1.000 13.50654 ? 395 ASN A ND2   1 
ATOM   3143 N  N     . ALA A 1 396 ? 13.44468  -6.86141  -29.92494 1.000 7.56575  ? 396 ALA A N     1 
ATOM   3144 C  CA    . ALA A 1 396 ? 13.30266  -6.76141  -31.37893 1.000 10.82258 ? 396 ALA A CA    1 
ATOM   3145 C  C     . ALA A 1 396 ? 14.10965  -7.82641  -32.10095 1.000 8.78113  ? 396 ALA A C     1 
ATOM   3146 O  O     . ALA A 1 396 ? 13.58864  -8.55841  -32.94994 1.000 8.07135  ? 396 ALA A O     1 
ATOM   3147 C  CB    . ALA A 1 396 ? 13.77664  -5.39541  -31.86294 1.000 11.16693 ? 396 ALA A CB    1 
ATOM   3148 N  N     . ALA A 1 397 ? 15.41365  -7.86740  -31.81897 1.000 9.71074  ? 397 ALA A N     1 
ATOM   3149 C  CA    . ALA A 1 397 ? 16.32564  -8.71940  -32.56698 1.000 9.99068  ? 397 ALA A CA    1 
ATOM   3150 C  C     . ALA A 1 397 ? 15.97965  -10.18740 -32.39898 1.000 7.71484  ? 397 ALA A C     1 
ATOM   3151 O  O     . ALA A 1 397 ? 15.99264  -10.94840 -33.37398 1.000 7.29604  ? 397 ALA A O     1 
ATOM   3152 C  CB    . ALA A 1 397 ? 17.76165  -8.46439  -32.12001 1.000 12.04292 ? 397 ALA A CB    1 
ATOM   3153 N  N     . ASN A 1 398 ? 15.67067  -10.60740 -31.16897 1.000 6.86898  ? 398 ASN A N     1 
ATOM   3154 C  CA    . ASN A 1 398 ? 15.41468  -12.02340 -30.92897 1.000 7.79244  ? 398 ASN A CA    1 
ATOM   3155 C  C     . ASN A 1 398 ? 14.06067  -12.45441 -31.48795 1.000 6.92367  ? 398 ASN A C     1 
ATOM   3156 O  O     . ASN A 1 398 ? 13.89567  -13.62341 -31.85494 1.000 6.97338  ? 398 ASN A O     1 
ATOM   3157 C  CB    . ASN A 1 398 ? 15.51371  -12.33640 -29.42997 1.000 6.53912  ? 398 ASN A CB    1 
ATOM   3158 C  CG    . ASN A 1 398 ? 16.96572  -12.42040 -28.93100 1.000 6.42729  ? 398 ASN A CG    1 
ATOM   3159 O  OD1   . ASN A 1 398 ? 17.60672  -13.46840 -29.01901 1.000 6.41454  ? 398 ASN A OD1   1 
ATOM   3160 N  ND2   . ASN A 1 398 ? 17.47772  -11.31540 -28.40100 1.000 6.38194  ? 398 ASN A ND2   1 
ATOM   3161 N  N     . TRP A 1 399 ? 13.08467  -11.54141 -31.56593 1.000 7.02832  ? 399 TRP A N     1 
ATOM   3162 C  CA    . TRP A 1 399 ? 11.82066  -11.88341 -32.22091 1.000 7.22445  ? 399 TRP A CA    1 
ATOM   3163 C  C     . TRP A 1 399 ? 12.00764  -12.04941 -33.72491 1.000 9.17145  ? 399 TRP A C     1 
ATOM   3164 O  O     . TRP A 1 399 ? 11.37563  -12.91442 -34.34690 1.000 7.65565  ? 399 TRP A O     1 
ATOM   3165 C  CB    . TRP A 1 399 ? 10.74966  -10.82842 -31.92789 1.000 9.11324  ? 399 TRP A CB    1 
ATOM   3166 C  CG    . TRP A 1 399 ? 9.94368   -11.13142 -30.70188 1.000 7.20169  ? 399 TRP A CG    1 
ATOM   3167 C  CD1   . TRP A 1 399 ? 10.04070  -10.52542 -29.48788 1.000 8.39621  ? 399 TRP A CD1   1 
ATOM   3168 C  CD2   . TRP A 1 399 ? 8.93969   -12.14542 -30.56686 1.000 8.23881  ? 399 TRP A CD2   1 
ATOM   3169 N  NE1   . TRP A 1 399 ? 9.14672   -11.08742 -28.60487 1.000 9.69710  ? 399 TRP A NE1   1 
ATOM   3170 C  CE2   . TRP A 1 399 ? 8.45971   -12.08543 -29.24385 1.000 7.08346  ? 399 TRP A CE2   1 
ATOM   3171 C  CE3   . TRP A 1 399 ? 8.39268   -13.09043 -31.43985 1.000 7.38472  ? 399 TRP A CE3   1 
ATOM   3172 C  CZ2   . TRP A 1 399 ? 7.46172   -12.93143 -28.77384 1.000 7.11825  ? 399 TRP A CZ2   1 
ATOM   3173 C  CZ3   . TRP A 1 399 ? 7.40569   -13.92643 -30.97584 1.000 7.41018  ? 399 TRP A CZ3   1 
ATOM   3174 C  CH2   . TRP A 1 399 ? 6.95071   -13.84743 -29.65083 1.000 8.75214  ? 399 TRP A CH2   1 
ATOM   3175 N  N     . MET A 1 400 ? 12.87062  -11.22841 -34.32893 1.000 7.60575  ? 400 MET A N     1 
ATOM   3176 C  CA    . MET A 1 400 ? 13.18560  -11.40341 -35.74193 1.000 10.46664 ? 400 MET A CA    1 
ATOM   3177 C  C     . MET A 1 400 ? 13.99460  -12.67441 -35.96495 1.000 11.11867 ? 400 MET A C     1 
ATOM   3178 O  O     . MET A 1 400 ? 13.82459  -13.35741 -36.98194 1.000 11.84098 ? 400 MET A O     1 
ATOM   3179 C  CB    . MET A 1 400 ? 13.94459  -10.18341 -36.26294 1.000 9.51304  ? 400 MET A CB    1 
ATOM   3180 C  CG    . MET A 1 400 ? 13.07258  -8.96041  -36.48493 1.000 10.73227 ? 400 MET A CG    1 
ATOM   3181 S  SD    . MET A 1 400 ? 13.96556  -7.59941  -37.24994 1.000 14.94335 ? 400 MET A SD    1 
ATOM   3182 C  CE    . MET A 1 400 ? 14.98558  -7.05240  -35.88196 1.000 8.84467  ? 400 MET A CE    1 
ATOM   3183 N  N     . TRP A 1 401 ? 14.87962  -12.99540 -35.01796 1.000 8.80875  ? 401 TRP A N     1 
ATOM   3184 C  CA    . TRP A 1 401 ? 15.64262  -14.23940 -35.05197 1.000 13.25232 ? 401 TRP A CA    1 
ATOM   3185 C  C     . TRP A 1 401 ? 14.71763  -15.45140 -35.01896 1.000 11.37564 ? 401 TRP A C     1 
ATOM   3186 O  O     . TRP A 1 401 ? 14.80261  -16.33940 -35.87796 1.000 8.90424  ? 401 TRP A O     1 
ATOM   3187 C  CB    . TRP A 1 401 ? 16.61264  -14.26340 -33.86799 1.000 8.59911  ? 401 TRP A CB    1 
ATOM   3188 C  CG    . TRP A 1 401 ? 17.56265  -15.41839 -33.83201 1.000 10.56319 ? 401 TRP A CG    1 
ATOM   3189 C  CD1   . TRP A 1 401 ? 17.25665  -16.73440 -33.64000 1.000 14.97037 ? 401 TRP A CD1   1 
ATOM   3190 C  CD2   . TRP A 1 401 ? 18.98564  -15.35239 -33.95203 1.000 12.86008 ? 401 TRP A CD2   1 
ATOM   3191 N  NE1   . TRP A 1 401 ? 18.40066  -17.49439 -33.65502 1.000 13.63245 ? 401 TRP A NE1   1 
ATOM   3192 C  CE2   . TRP A 1 401 ? 19.47665  -16.66739 -33.84304 1.000 15.69512 ? 401 TRP A CE2   1 
ATOM   3193 C  CE3   . TRP A 1 401 ? 19.89164  -14.30839 -34.15104 1.000 14.77234 ? 401 TRP A CE3   1 
ATOM   3194 C  CZ2   . TRP A 1 401 ? 20.83465  -16.96638 -33.92906 1.000 18.30977 ? 401 TRP A CZ2   1 
ATOM   3195 C  CZ3   . TRP A 1 401 ? 21.24264  -14.60638 -34.23507 1.000 12.35221 ? 401 TRP A CZ3   1 
ATOM   3196 C  CH2   . TRP A 1 401 ? 21.69964  -15.92338 -34.12308 1.000 23.44456 ? 401 TRP A CH2   1 
ATOM   3197 N  N     . LEU A 1 402 ? 13.82264  -15.50041 -34.02694 1.000 9.82011  ? 402 LEU A N     1 
ATOM   3198 C  CA    . LEU A 1 402 ? 12.94765  -16.64841 -33.84393 1.000 10.01764 ? 402 LEU A CA    1 
ATOM   3199 C  C     . LEU A 1 402 ? 11.91163  -16.77741 -34.95191 1.000 9.68647  ? 402 LEU A C     1 
ATOM   3200 O  O     . LEU A 1 402 ? 11.40863  -17.88341 -35.18090 1.000 7.87362  ? 402 LEU A O     1 
ATOM   3201 C  CB    . LEU A 1 402 ? 12.25067  -16.56741 -32.48492 1.000 8.55918  ? 402 LEU A CB    1 
ATOM   3202 C  CG    . LEU A 1 402 ? 12.84369  -17.39041 -31.33793 1.000 6.99417  ? 402 LEU A CG    1 
ATOM   3203 C  CD1   . LEU A 1 402 ? 12.81969  -18.87441 -31.66993 1.000 8.77775  ? 402 LEU A CD1   1 
ATOM   3204 C  CD2   . LEU A 1 402 ? 14.25670  -16.92641 -31.01195 1.000 8.65994  ? 402 LEU A CD2   1 
ATOM   3205 N  N     . SER A 1 403 ? 11.57562  -15.68241 -35.63091 1.000 11.51292 ? 403 SER A N     1 
ATOM   3206 C  CA    . SER A 1 403 ? 10.63360  -15.71842 -36.74089 1.000 8.91387  ? 403 SER A CA    1 
ATOM   3207 C  C     . SER A 1 403 ? 11.31158  -15.93241 -38.08390 1.000 9.68144  ? 403 SER A C     1 
ATOM   3208 O  O     . SER A 1 403 ? 10.62956  -15.89742 -39.11389 1.000 11.64065 ? 403 SER A O     1 
ATOM   3209 C  CB    . SER A 1 403 ? 9.81559   -14.42142 -36.78488 1.000 10.30319 ? 403 SER A CB    1 
ATOM   3210 O  OG    . SER A 1 403 ? 10.65959  -13.30142 -36.95389 1.000 13.40882 ? 403 SER A OG    1 
ATOM   3211 N  N     . ALA A 1 404 ? 12.62658  -16.16541 -38.09192 1.000 10.99785 ? 404 ALA A N     1 
ATOM   3212 C  CA    . ALA A 1 404 ? 13.40456  -16.29341 -39.32494 1.000 12.29382 ? 404 ALA A CA    1 
ATOM   3213 C  C     . ALA A 1 404 ? 13.21854  -15.07241 -40.21993 1.000 14.11719 ? 404 ALA A C     1 
ATOM   3214 O  O     . ALA A 1 404 ? 13.18252  -15.17241 -41.44693 1.000 15.25735 ? 404 ALA A O     1 
ATOM   3215 C  CB    . ALA A 1 404 ? 13.06155  -17.58141 -40.07793 1.000 15.92145 ? 404 ALA A CB    1 
ATOM   3216 N  N     . SER A 1 405 ? 13.08954  -13.90441 -39.59993 1.000 8.91119  ? 405 SER A N     1 
ATOM   3217 C  CA    . SER A 1 405 ? 12.98453  -12.66341 -40.35193 1.000 13.68455 ? 405 SER A CA    1 
ATOM   3218 C  C     . SER A 1 405 ? 14.30352  -11.91540 -40.44995 1.000 15.62296 ? 405 SER A C     1 
ATOM   3219 O  O     . SER A 1 405 ? 14.49251  -11.14640 -41.39495 1.000 17.89643 ? 405 SER A O     1 
ATOM   3220 C  CB    . SER A 1 405 ? 11.92654  -11.74941 -39.72091 1.000 15.05426 ? 405 SER A CB    1 
ATOM   3221 O  OG    . SER A 1 405 ? 10.65254  -12.38242 -39.70689 1.000 10.45233 ? 405 SER A OG    1 
ATOM   3222 N  N     . ALA A 1 406 ? 15.21454  -12.11140 -39.49897 1.000 14.87950 ? 406 ALA A N     1 
ATOM   3223 C  CA    . ALA A 1 406 ? 16.53854  -11.51340 -39.57399 1.000 15.02655 ? 406 ALA A CA    1 
ATOM   3224 C  C     . ALA A 1 406 ? 17.52355  -12.39439 -38.82400 1.000 14.22471 ? 406 ALA A C     1 
ATOM   3225 O  O     . ALA A 1 406 ? 17.14757  -13.11939 -37.90000 1.000 15.18253 ? 406 ALA A O     1 
ATOM   3226 C  CB    . ALA A 1 406 ? 16.55854  -10.09540 -38.99599 1.000 20.56276 ? 406 ALA A CB    1 
ATOM   3227 N  N     . PHE A 1 407 ? 18.78855  -12.33539 -39.24903 1.000 19.97380 ? 407 PHE A N     1 
ATOM   3228 C  CA    . PHE A 1 407 ? 19.90156  -13.04238 -38.61604 1.000 17.88278 ? 407 PHE A CA    1 
ATOM   3229 C  C     . PHE A 1 407 ? 19.77756  -14.56439 -38.70704 1.000 18.14124 ? 407 PHE A C     1 
ATOM   3230 O  O     . PHE A 1 407 ? 20.75956  -15.24438 -39.02206 1.000 32.68992 ? 407 PHE A O     1 
ATOM   3231 C  CB    . PHE A 1 407 ? 20.04958  -12.60938 -37.15205 1.000 17.63711 ? 407 PHE A CB    1 
ATOM   3232 C  CG    . PHE A 1 407 ? 20.01958  -11.11638 -36.95205 1.000 15.51181 ? 407 PHE A CG    1 
ATOM   3233 C  CD1   . PHE A 1 407 ? 21.04257  -10.31638 -37.43006 1.000 15.54906 ? 407 PHE A CD1   1 
ATOM   3234 C  CD2   . PHE A 1 407 ? 18.97659  -10.51839 -36.26903 1.000 15.20218 ? 407 PHE A CD2   1 
ATOM   3235 C  CE1   . PHE A 1 407 ? 21.01557  -8.94438  -37.24706 1.000 19.15518 ? 407 PHE A CE1   1 
ATOM   3236 C  CE2   . PHE A 1 407 ? 18.94559  -9.14539  -36.08103 1.000 18.60900 ? 407 PHE A CE2   1 
ATOM   3237 C  CZ    . PHE A 1 407 ? 19.96758  -8.35939  -36.56904 1.000 17.15132 ? 407 PHE A CZ    1 
ATOM   3238 N  N     . PHE A 1 408 ? 18.59857  -15.11339 -38.42902 1.000 19.69837 ? 408 PHE A N     1 
ATOM   3239 C  CA    . PHE A 1 408 ? 18.35857  -16.54939 -38.49402 1.000 17.70687 ? 408 PHE A CA    1 
ATOM   3240 C  C     . PHE A 1 408 ? 17.54655  -16.88839 -39.74101 1.000 21.60688 ? 408 PHE A C     1 
ATOM   3241 O  O     . PHE A 1 408 ? 16.58754  -16.18840 -40.07699 1.000 18.36544 ? 408 PHE A O     1 
ATOM   3242 C  CB    . PHE A 1 408 ? 17.62559  -17.02239 -37.23601 1.000 21.08417 ? 408 PHE A CB    1 
ATOM   3243 C  CG    . PHE A 1 408 ? 17.45860  -18.51839 -37.14201 1.000 15.60934 ? 408 PHE A CG    1 
ATOM   3244 C  CD1   . PHE A 1 408 ? 18.54161  -19.33739 -36.86502 1.000 11.82554 ? 408 PHE A CD1   1 
ATOM   3245 C  CD2   . PHE A 1 408 ? 16.20960  -19.09840 -37.29899 1.000 14.42467 ? 408 PHE A CD2   1 
ATOM   3246 C  CE1   . PHE A 1 408 ? 18.38561  -20.71039 -36.77302 1.000 18.26404 ? 408 PHE A CE1   1 
ATOM   3247 C  CE2   . PHE A 1 408 ? 16.04761  -20.47040 -37.20298 1.000 18.50999 ? 408 PHE A CE2   1 
ATOM   3248 C  CZ    . PHE A 1 408 ? 17.13661  -21.27639 -36.94000 1.000 14.51922 ? 408 PHE A CZ    1 
ATOM   3249 N  N     . SER A 1 409 ? 17.93454  -17.96739 -40.42901 1.000 20.44252 ? 409 SER A N     1 
ATOM   3250 C  CA    . SER A 1 409 ? 17.28553  -18.33739 -41.68000 1.000 20.65187 ? 409 SER A CA    1 
ATOM   3251 C  C     . SER A 1 409 ? 16.95953  -19.82139 -41.80900 1.000 19.61647 ? 409 SER A C     1 
ATOM   3252 O  O     . SER A 1 409 ? 16.39451  -20.22340 -42.83099 1.000 14.24594 ? 409 SER A O     1 
ATOM   3253 C  CB    . SER A 1 409 ? 18.15050  -17.90939 -42.87502 1.000 21.75584 ? 409 SER A CB    1 
ATOM   3254 O  OG    . SER A 1 409 ? 19.43551  -18.50938 -42.82404 1.000 24.61756 ? 409 SER A OG    1 
ATOM   3255 N  N     . GLN A 1 410 ? 17.29055  -20.64339 -40.81400 1.000 16.52706 ? 410 GLN A N     1 
ATOM   3256 C  CA    . GLN A 1 410 ? 17.02855  -22.07839 -40.89400 1.000 14.15333 ? 410 GLN A CA    1 
ATOM   3257 C  C     . GLN A 1 410 ? 15.61156  -22.34640 -40.39498 1.000 9.47935  ? 410 GLN A C     1 
ATOM   3258 O  O     . GLN A 1 410 ? 15.37758  -22.76840 -39.26197 1.000 11.84506 ? 410 GLN A O     1 
ATOM   3259 C  CB    . GLN A 1 410 ? 18.06957  -22.86039 -40.10702 1.000 15.58308 ? 410 GLN A CB    1 
ATOM   3260 C  CG    . GLN A 1 410 ? 17.94657  -24.34439 -40.30002 1.000 15.88448 ? 410 GLN A CG    1 
ATOM   3261 C  CD    . GLN A 1 410 ? 17.79855  -24.71139 -41.76001 1.000 16.90494 ? 410 GLN A CD    1 
ATOM   3262 O  OE1   . GLN A 1 410 ? 16.77954  -25.26439 -42.16600 1.000 20.61622 ? 410 GLN A OE1   1 
ATOM   3263 N  NE2   . GLN A 1 410 ? 18.81353  -24.39939 -42.56003 1.000 19.66733 ? 410 GLN A NE2   1 
ATOM   3264 N  N     . TYR A 1 411 ? 14.64754  -22.09640 -41.27596 1.000 13.89401 ? 411 TYR A N     1 
ATOM   3265 C  CA    . TYR A 1 411 ? 13.23855  -22.26741 -40.94894 1.000 13.61726 ? 411 TYR A CA    1 
ATOM   3266 C  C     . TYR A 1 411 ? 12.79256  -23.72541 -40.96393 1.000 12.46460 ? 411 TYR A C     1 
ATOM   3267 O  O     . TYR A 1 411 ? 11.61956  -24.00141 -40.68391 1.000 16.54400 ? 411 TYR A O     1 
ATOM   3268 C  CB    . TYR A 1 411 ? 12.38153  -21.44641 -41.91592 1.000 15.96873 ? 411 TYR A CB    1 
ATOM   3269 C  CG    . TYR A 1 411 ? 12.60951  -21.78041 -43.36993 1.000 17.67478 ? 411 TYR A CG    1 
ATOM   3270 C  CD1   . TYR A 1 411 ? 11.91950  -22.81941 -43.97591 1.000 20.00337 ? 411 TYR A CD1   1 
ATOM   3271 C  CD2   . TYR A 1 411 ? 13.51349  -21.05640 -44.13794 1.000 16.70476 ? 411 TYR A CD2   1 
ATOM   3272 C  CE1   . TYR A 1 411 ? 12.12148  -23.13041 -45.30092 1.000 20.32207 ? 411 TYR A CE1   1 
ATOM   3273 C  CE2   . TYR A 1 411 ? 13.72047  -21.36240 -45.46894 1.000 23.36821 ? 411 TYR A CE2   1 
ATOM   3274 C  CZ    . TYR A 1 411 ? 13.02147  -22.40041 -46.04393 1.000 23.36952 ? 411 TYR A CZ    1 
ATOM   3275 O  OH    . TYR A 1 411 ? 13.21945  -22.71340 -47.36994 1.000 29.65689 ? 411 TYR A OH    1 
ATOM   3276 N  N     . PHE A 1 412 ? 13.68155  -24.66440 -41.28994 1.000 13.36383 ? 412 PHE A N     1 
ATOM   3277 C  CA    . PHE A 1 412 ? 13.33756  -26.07241 -41.15494 1.000 12.23680 ? 412 PHE A CA    1 
ATOM   3278 C  C     . PHE A 1 412 ? 13.49159  -26.56941 -39.72394 1.000 14.37465 ? 412 PHE A C     1 
ATOM   3279 O  O     . PHE A 1 412 ? 12.95360  -27.62841 -39.38793 1.000 16.83239 ? 412 PHE A O     1 
ATOM   3280 C  CB    . PHE A 1 412 ? 14.19055  -26.92440 -42.09395 1.000 16.04930 ? 412 PHE A CB    1 
ATOM   3281 C  CG    . PHE A 1 412 ? 13.86752  -26.74440 -43.55295 1.000 17.96306 ? 412 PHE A CG    1 
ATOM   3282 C  CD1   . PHE A 1 412 ? 12.79952  -27.41341 -44.12693 1.000 19.48112 ? 412 PHE A CD1   1 
ATOM   3283 C  CD2   . PHE A 1 412 ? 14.64551  -25.92640 -44.35396 1.000 15.99896 ? 412 PHE A CD2   1 
ATOM   3284 C  CE1   . PHE A 1 412 ? 12.50749  -27.26041 -45.46993 1.000 18.25481 ? 412 PHE A CE1   1 
ATOM   3285 C  CE2   . PHE A 1 412 ? 14.36348  -25.77140 -45.69296 1.000 16.75848 ? 412 PHE A CE2   1 
ATOM   3286 C  CZ    . PHE A 1 412 ? 13.29348  -26.44240 -46.25194 1.000 20.37360 ? 412 PHE A CZ    1 
ATOM   3287 N  N     . ARG A 1 413 ? 14.21153  -25.83323 -38.87950 1.000 14.59903 ? 413 ARG A N     1 
ATOM   3288 C  CA    . ARG A 1 413 ? 14.35709  -26.17763 -37.46687 1.000 14.14670 ? 413 ARG A CA    1 
ATOM   3289 C  C     . ARG A 1 413 ? 13.14580  -25.63773 -36.71964 1.000 14.77066 ? 413 ARG A C     1 
ATOM   3290 O  O     . ARG A 1 413 ? 13.06755  -24.44470 -36.41706 1.000 12.58238 ? 413 ARG A O     1 
ATOM   3291 C  CB    . ARG A 1 413 ? 15.65217  -25.60695 -36.90254 1.000 15.71972 ? 413 ARG A CB    1 
ATOM   3292 C  CG    . ARG A 1 413 ? 15.86123  -25.89221 -35.42150 1.000 12.42042 ? 413 ARG A CG    1 
ATOM   3293 C  CD    . ARG A 1 413 ? 16.17146  -27.36020 -35.16972 1.000 14.88973 ? 413 ARG A CD    1 
ATOM   3294 N  NE    . ARG A 1 413 ? 16.28964  -27.65570 -33.74589 1.000 14.48993 ? 413 ARG A NE    1 
ATOM   3295 C  CZ    . ARG A 1 413 ? 15.32274  -28.18171 -33.00613 1.000 16.52921 ? 413 ARG A CZ    1 
ATOM   3296 N  NH1   . ARG A 1 413 ? 14.14722  -28.49588 -33.52604 1.000 17.09347 ? 413 ARG A NH1   1 
ATOM   3297 N  NH2   . ARG A 1 413 ? 15.54181  -28.40208 -31.71285 1.000 19.17690 ? 413 ARG A NH2   1 
ATOM   3298 N  N     . VAL A 1 414 ? 12.19564  -26.51841 -36.41892 1.000 11.66014 ? 414 VAL A N     1 
ATOM   3299 C  CA    . VAL A 1 414 ? 10.94365  -26.15042 -35.76690 1.000 14.56994 ? 414 VAL A CA    1 
ATOM   3300 C  C     . VAL A 1 414 ? 10.84667  -26.90742 -34.44890 1.000 14.18547 ? 414 VAL A C     1 
ATOM   3301 O  O     . VAL A 1 414 ? 10.74968  -28.14142 -34.44390 1.000 9.52475  ? 414 VAL A O     1 
ATOM   3302 C  CB    . VAL A 1 414 ? 9.72764   -26.45042 -36.65688 1.000 15.61854 ? 414 VAL A CB    1 
ATOM   3303 C  CG1   . VAL A 1 414 ? 8.43965   -26.11142 -35.92686 1.000 17.15203 ? 414 VAL A CG1   1 
ATOM   3304 C  CG2   . VAL A 1 414 ? 9.82961   -25.68742 -37.97588 1.000 17.91511 ? 414 VAL A CG2   1 
ATOM   3305 N  N     . TYR A 1 415 ? 10.86069  -26.17042 -33.33990 1.000 10.90241 ? 415 TYR A N     1 
ATOM   3306 C  CA    . TYR A 1 415 ? 10.72971  -26.78242 -32.02590 1.000 14.94272 ? 415 TYR A CA    1 
ATOM   3307 C  C     . TYR A 1 415 ? 9.35372   -27.42042 -31.86087 1.000 14.83121 ? 415 TYR A C     1 
ATOM   3308 O  O     . TYR A 1 415 ? 8.34071   -26.87043 -32.30086 1.000 10.70512 ? 415 TYR A O     1 
ATOM   3309 C  CB    . TYR A 1 415 ? 10.94873  -25.74042 -30.92790 1.000 15.03710 ? 415 TYR A CB    1 
ATOM   3310 C  CG    . TYR A 1 415 ? 12.28073  -25.01841 -30.99792 1.000 20.44487 ? 415 TYR A CG    1 
ATOM   3311 C  CD1   . TYR A 1 415 ? 13.46173  -25.67241 -30.68494 1.000 14.99637 ? 415 TYR A CD1   1 
ATOM   3312 C  CD2   . TYR A 1 415 ? 12.34972  -23.67841 -31.35592 1.000 13.45363 ? 415 TYR A CD2   1 
ATOM   3313 C  CE1   . TYR A 1 415 ? 14.67573  -25.01640 -30.73896 1.000 16.74548 ? 415 TYR A CE1   1 
ATOM   3314 C  CE2   . TYR A 1 415 ? 13.55471  -23.01541 -31.41494 1.000 14.49871 ? 415 TYR A CE2   1 
ATOM   3315 C  CZ    . TYR A 1 415 ? 14.71672  -23.69040 -31.10596 1.000 19.05452 ? 415 TYR A CZ    1 
ATOM   3316 O  OH    . TYR A 1 415 ? 15.92772  -23.03940 -31.15798 1.000 18.06904 ? 415 TYR A OH    1 
ATOM   3317 N  N     . SER A 1 416 ? 9.32173   -28.59142 -31.20587 1.000 9.74664  ? 416 SER A N     1 
ATOM   3318 C  CA    . SER A 1 416 ? 8.05374   -29.26543 -30.94885 1.000 10.15094 ? 416 SER A CA    1 
ATOM   3319 C  C     . SER A 1 416 ? 7.49076   -28.83543 -29.60184 1.000 11.17824 ? 416 SER A C     1 
ATOM   3320 O  O     . SER A 1 416 ? 8.19178   -28.92543 -28.59085 1.000 12.40912 ? 416 SER A O     1 
ATOM   3321 C  CB    . SER A 1 416 ? 8.22275   -30.77543 -30.95786 1.000 12.48259 ? 416 SER A CB    1 
ATOM   3322 O  OG    . SER A 1 416 ? 7.03676   -31.40243 -30.49684 1.000 13.25309 ? 416 SER A OG    1 
ATOM   3323 N  N     . PRO A 1 417 ? 6.23476   -28.38943 -29.53982 1.000 13.04093 ? 417 PRO A N     1 
ATOM   3324 C  CA    . PRO A 1 417 ? 5.65278   -28.01344 -28.24381 1.000 9.52955  ? 417 PRO A CA    1 
ATOM   3325 C  C     . PRO A 1 417 ? 5.42280   -29.19844 -27.32081 1.000 11.87360 ? 417 PRO A C     1 
ATOM   3326 O  O     . PRO A 1 417 ? 5.07482   -28.98944 -26.15080 1.000 14.23992 ? 417 PRO A O     1 
ATOM   3327 C  CB    . PRO A 1 417 ? 4.33277   -27.33444 -28.63979 1.000 12.02564 ? 417 PRO A CB    1 
ATOM   3328 C  CG    . PRO A 1 417 ? 3.96975   -27.96744 -29.94378 1.000 12.21777 ? 417 PRO A CG    1 
ATOM   3329 C  CD    . PRO A 1 417 ? 5.27074   -28.25044 -30.64581 1.000 17.38383 ? 417 PRO A CD    1 
ATOM   3330 N  N     . VAL A 1 418 ? 5.63780   -30.41944 -27.80281 1.000 15.27666 ? 418 VAL A N     1 
ATOM   3331 C  CA    . VAL A 1 418 ? 5.46481   -31.63644 -27.02081 1.000 12.26413 ? 418 VAL A CA    1 
ATOM   3332 C  C     . VAL A 1 418 ? 6.80682   -32.21143 -26.57683 1.000 12.92830 ? 418 VAL A C     1 
ATOM   3333 O  O     . VAL A 1 418 ? 6.99684   -32.53343 -25.40284 1.000 19.04400 ? 418 VAL A O     1 
ATOM   3334 C  CB    . VAL A 1 418 ? 4.66680   -32.68144 -27.83180 1.000 15.21352 ? 418 VAL A CB    1 
ATOM   3335 C  CG1   . VAL A 1 418 ? 4.83482   -34.06444 -27.22080 1.000 18.59754 ? 418 VAL A CG1   1 
ATOM   3336 C  CG2   . VAL A 1 418 ? 3.19680   -32.29444 -27.90977 1.000 16.13543 ? 418 VAL A CG2   1 
ATOM   3337 N  N     . VAL A 1 419 ? 7.75781   -32.33343 -27.50785 1.000 11.32583 ? 419 VAL A N     1 
ATOM   3338 C  CA    . VAL A 1 419 ? 8.98682   -33.07243 -27.23187 1.000 15.73431 ? 419 VAL A CA    1 
ATOM   3339 C  C     . VAL A 1 419 ? 10.05182  -32.19142 -26.57289 1.000 8.84640  ? 419 VAL A C     1 
ATOM   3340 O  O     . VAL A 1 419 ? 10.89784  -32.69842 -25.82590 1.000 11.19949 ? 419 VAL A O     1 
ATOM   3341 C  CB    . VAL A 1 419 ? 9.51380   -33.69642 -28.53488 1.000 13.42441 ? 419 VAL A CB    1 
ATOM   3342 C  CG1   . VAL A 1 419 ? 10.81280  -34.46942 -28.28390 1.000 11.07079 ? 419 VAL A CG1   1 
ATOM   3343 C  CG2   . VAL A 1 419 ? 8.46179   -34.59743 -29.13586 1.000 15.80711 ? 419 VAL A CG2   1 
ATOM   3344 N  N     . PHE A 1 420 ? 10.03581  -30.87442 -26.82389 1.000 10.57925 ? 420 PHE A N     1 
ATOM   3345 C  CA    . PHE A 1 420 ? 11.18182  -30.03142 -26.47691 1.000 10.44223 ? 420 PHE A CA    1 
ATOM   3346 C  C     . PHE A 1 420 ? 11.45784  -30.04242 -24.97791 1.000 11.37349 ? 420 PHE A C     1 
ATOM   3347 O  O     . PHE A 1 420 ? 12.59185  -30.28541 -24.54193 1.000 11.20125 ? 420 PHE A O     1 
ATOM   3348 C  CB    . PHE A 1 420 ? 10.95380  -28.60242 -26.96690 1.000 12.75671 ? 420 PHE A CB    1 
ATOM   3349 C  CG    . PHE A 1 420 ? 12.13281  -27.69241 -26.74492 1.000 11.63308 ? 420 PHE A CG    1 
ATOM   3350 C  CD1   . PHE A 1 420 ? 13.24579  -27.76541 -27.56794 1.000 13.52068 ? 420 PHE A CD1   1 
ATOM   3351 C  CD2   . PHE A 1 420 ? 12.12582  -26.76142 -25.71892 1.000 12.01301 ? 420 PHE A CD2   1 
ATOM   3352 C  CE1   . PHE A 1 420 ? 14.33579  -26.93941 -27.36696 1.000 12.90989 ? 420 PHE A CE1   1 
ATOM   3353 C  CE2   . PHE A 1 420 ? 13.20182  -25.92941 -25.51194 1.000 9.64811  ? 420 PHE A CE2   1 
ATOM   3354 C  CZ    . PHE A 1 420 ? 14.31381  -26.01541 -26.33996 1.000 13.66270 ? 420 PHE A CZ    1 
ATOM   3355 N  N     . GLY A 1 421 ? 10.43086  -29.77742 -24.16989 1.000 11.30443 ? 421 GLY A N     1 
ATOM   3356 C  CA    . GLY A 1 421 ? 10.60888  -29.73542 -22.73090 1.000 10.32510 ? 421 GLY A CA    1 
ATOM   3357 C  C     . GLY A 1 421 ? 10.71189  -31.09042 -22.07090 1.000 9.55435  ? 421 GLY A C     1 
ATOM   3358 O  O     . GLY A 1 421 ? 11.27491  -31.19142 -20.97891 1.000 11.71168 ? 421 GLY A O     1 
ATOM   3359 N  N     . LYS A 1 422 ? 10.19089  -32.13442 -22.71389 1.000 12.53794 ? 422 LYS A N     1 
ATOM   3360 C  CA    . LYS A 1 422 ? 10.24690  -33.47142 -22.13489 1.000 12.51688 ? 422 LYS A CA    1 
ATOM   3361 C  C     . LYS A 1 422 ? 11.68191  -33.97342 -22.01491 1.000 13.87128 ? 422 LYS A C     1 
ATOM   3362 O  O     . LYS A 1 422 ? 11.98292  -34.79842 -21.14492 1.000 15.43940 ? 422 LYS A O     1 
ATOM   3363 C  CB    . LYS A 1 422 ? 9.40689   -34.43143 -22.98188 1.000 16.23403 ? 422 LYS A CB    1 
ATOM   3364 C  CG    . LYS A 1 422 ? 9.38690   -35.87143 -22.49888 1.000 15.14471 ? 422 LYS A CG    1 
ATOM   3365 C  CD    . LYS A 1 422 ? 8.59289   -36.75643 -23.43986 1.000 22.35042 ? 422 LYS A CD    1 
ATOM   3366 C  CE    . LYS A 1 422 ? 7.14089   -36.31943 -23.51284 1.000 18.34313 ? 422 LYS A CE    1 
ATOM   3367 N  NZ    . LYS A 1 422 ? 6.34488   -37.20744 -24.40583 1.000 13.08293 ? 422 LYS A NZ    1 
ATOM   3368 N  N     . LYS A 1 423 ? 12.58289  -33.48741 -22.86593 1.000 13.85505 ? 423 LYS A N     1 
ATOM   3369 C  CA    . LYS A 1 423 ? 13.96189  -33.95841 -22.79695 1.000 20.36031 ? 423 LYS A CA    1 
ATOM   3370 C  C     . LYS A 1 423 ? 14.67391  -33.43041 -21.55396 1.000 11.73170 ? 423 LYS A C     1 
ATOM   3371 O  O     . LYS A 1 423 ? 15.53392  -34.12141 -20.99698 1.000 14.76896 ? 423 LYS A O     1 
ATOM   3372 C  CB    . LYS A 1 423 ? 14.71787  -33.57241 -24.06996 1.000 17.61424 ? 423 LYS A CB    1 
ATOM   3373 C  CG    . LYS A 1 423 ? 15.17586  -32.12841 -24.11397 1.000 20.72720 ? 423 LYS A CG    1 
ATOM   3374 C  CD    . LYS A 1 423 ? 16.12784  -31.88540 -25.26999 0.000 14.53100 ? 423 LYS A CD    1 
ATOM   3375 C  CE    . LYS A 1 423 ? 15.37882  -31.42040 -26.49998 0.000 13.89125 ? 423 LYS A CE    1 
ATOM   3376 N  NZ    . LYS A 1 423 ? 14.65482  -30.15641 -26.21196 0.000 12.82633 ? 423 LYS A NZ    1 
ATOM   3377 N  N     . TYR A 1 424 ? 14.32291  -32.23241 -21.08896 1.000 11.34015 ? 424 TYR A N     1 
ATOM   3378 C  CA    . TYR A 1 424 ? 14.90493  -31.71641 -19.85697 1.000 9.64448  ? 424 TYR A CA    1 
ATOM   3379 C  C     . TYR A 1 424 ? 14.13296  -32.16241 -18.62495 1.000 13.91067 ? 424 TYR A C     1 
ATOM   3380 O  O     . TYR A 1 424 ? 14.73497  -32.41441 -17.57596 1.000 13.36008 ? 424 TYR A O     1 
ATOM   3381 C  CB    . TYR A 1 424 ? 14.95193  -30.18741 -19.88197 1.000 12.10207 ? 424 TYR A CB    1 
ATOM   3382 C  CG    . TYR A 1 424 ? 15.65891  -29.60540 -21.07498 1.000 8.87488  ? 424 TYR A CG    1 
ATOM   3383 C  CD1   . TYR A 1 424 ? 17.04591  -29.51240 -21.10800 1.000 11.14704 ? 424 TYR A CD1   1 
ATOM   3384 C  CD2   . TYR A 1 424 ? 14.94189  -29.13341 -22.16497 1.000 11.47413 ? 424 TYR A CD2   1 
ATOM   3385 C  CE1   . TYR A 1 424 ? 17.69889  -28.97540 -22.20101 1.000 9.50063  ? 424 TYR A CE1   1 
ATOM   3386 C  CE2   . TYR A 1 424 ? 15.59187  -28.58540 -23.26398 1.000 10.24253 ? 424 TYR A CE2   1 
ATOM   3387 C  CZ    . TYR A 1 424 ? 16.96487  -28.51640 -23.27400 1.000 9.19077  ? 424 TYR A CZ    1 
ATOM   3388 O  OH    . TYR A 1 424 ? 17.61185  -27.97340 -24.35801 1.000 11.98562 ? 424 TYR A OH    1 
ATOM   3389 N  N     . ASP A 1 425 ? 12.80995  -32.27142 -18.73893 1.000 15.30348 ? 425 ASP A N     1 
ATOM   3390 C  CA    . ASP A 1 425 ? 11.91997  -32.42642 -17.58792 1.000 12.07623 ? 425 ASP A CA    1 
ATOM   3391 C  C     . ASP A 1 425 ? 10.82997  -33.43342 -17.93190 1.000 11.91783 ? 425 ASP A C     1 
ATOM   3392 O  O     . ASP A 1 425 ? 9.69097   -33.06343 -18.23688 1.000 14.44889 ? 425 ASP A O     1 
ATOM   3393 C  CB    . ASP A 1 425 ? 11.32598  -31.07042 -17.19491 1.000 15.30464 ? 425 ASP A CB    1 
ATOM   3394 C  CG    . ASP A 1 425 ? 10.46100  -31.13542 -15.95089 1.000 16.66965 ? 425 ASP A CG    1 
ATOM   3395 O  OD1   . ASP A 1 425 ? 10.39601  -32.20042 -15.29989 1.000 14.56779 ? 425 ASP A OD1   1 
ATOM   3396 O  OD2   . ASP A 1 425 ? 9.84200   -30.10143 -15.62788 1.000 12.63237 ? 425 ASP A OD2   1 
ATOM   3397 N  N     . PRO A 1 426 ? 11.14498  -34.73442 -17.88291 1.000 14.07498 ? 426 PRO A N     1 
ATOM   3398 C  CA    . PRO A 1 426 ? 10.14097  -35.74342 -18.26289 1.000 14.99154 ? 426 PRO A CA    1 
ATOM   3399 C  C     . PRO A 1 426 ? 8.97799   -35.85343 -17.29687 1.000 16.33473 ? 426 PRO A C     1 
ATOM   3400 O  O     . PRO A 1 426 ? 7.92799   -36.37643 -17.68785 1.000 20.37338 ? 426 PRO A O     1 
ATOM   3401 C  CB    . PRO A 1 426 ? 10.94998  -37.04842 -18.30690 1.000 12.73719 ? 426 PRO A CB    1 
ATOM   3402 C  CG    . PRO A 1 426 ? 12.11699  -36.79442 -17.41092 1.000 18.56965 ? 426 PRO A CG    1 
ATOM   3403 C  CD    . PRO A 1 426 ? 12.45098  -35.34242 -17.57693 1.000 11.67810 ? 426 PRO A CD    1 
ATOM   3404 N  N     . GLU A 1 427 ? 9.12001   -35.39543 -16.05387 1.000 15.85646 ? 427 GLU A N     1 
ATOM   3405 C  CA    . GLU A 1 427 ? 8.01903   -35.45943 -15.09985 1.000 18.73323 ? 427 GLU A CA    1 
ATOM   3406 C  C     . GLU A 1 427 ? 7.09502   -34.25744 -15.18884 1.000 17.29609 ? 427 GLU A C     1 
ATOM   3407 O  O     . GLU A 1 427 ? 5.99203   -34.29844 -14.63282 1.000 19.77248 ? 427 GLU A O     1 
ATOM   3408 C  CB    . GLU A 1 427 ? 8.55605   -35.58943 -13.67286 1.000 14.96456 ? 427 GLU A CB    1 
ATOM   3409 C  CG    . GLU A 1 427 ? 9.23606   -36.91543 -13.42687 1.000 22.34995 ? 427 GLU A CG    1 
ATOM   3410 C  CD    . GLU A 1 427 ? 8.38605   -38.08143 -13.89286 1.000 32.00817 ? 427 GLU A CD    1 
ATOM   3411 O  OE1   . GLU A 1 427 ? 7.30807   -38.30844 -13.30384 1.000 35.70502 ? 427 GLU A OE1   1 
ATOM   3412 O  OE2   . GLU A 1 427 ? 8.78704   -38.76043 -14.86187 1.000 34.23362 ? 427 GLU A OE2   1 
ATOM   3413 N  N     . GLY A 1 428 ? 7.51500   -33.20443 -15.87885 1.000 11.95056 ? 428 GLY A N     1 
ATOM   3414 C  CA    . GLY A 1 428 ? 6.70600   -32.00844 -15.99783 1.000 14.80132 ? 428 GLY A CA    1 
ATOM   3415 C  C     . GLY A 1 428 ? 6.67802   -31.15944 -14.74683 1.000 14.73979 ? 428 GLY A C     1 
ATOM   3416 O  O     . GLY A 1 428 ? 5.63702   -30.57444 -14.42981 1.000 16.07431 ? 428 GLY A O     1 
ATOM   3417 N  N     . ARG A 1 429 ? 7.79527   -31.07937 -14.01889 1.000 14.22472 ? 429 ARG A N     1 
ATOM   3418 C  CA    . ARG A 1 429 ? 7.81598   -30.28243 -12.79468 1.000 15.35484 ? 429 ARG A CA    1 
ATOM   3419 C  C     . ARG A 1 429 ? 7.54377   -28.81148 -13.08688 1.000 16.01162 ? 429 ARG A C     1 
ATOM   3420 O  O     . ARG A 1 429 ? 6.76679   -28.16425 -12.37616 1.000 12.22821 ? 429 ARG A O     1 
ATOM   3421 C  CB    . ARG A 1 429 ? 9.15527   -30.44947 -12.07374 1.000 17.67418 ? 429 ARG A CB    1 
ATOM   3422 C  CG    . ARG A 1 429 ? 9.23391   -31.67917 -11.17416 1.000 20.35088 ? 429 ARG A CG    1 
ATOM   3423 C  CD    . ARG A 1 429 ? 9.98885   -32.82106 -11.82925 0.000 18.48973 ? 429 ARG A CD    1 
ATOM   3424 N  NE    . ARG A 1 429 ? 10.04380  -33.99231 -10.96226 0.000 19.55220 ? 429 ARG A NE    1 
ATOM   3425 C  CZ    . ARG A 1 429 ? 10.93174  -34.16611 -9.99266  0.000 20.32009 ? 429 ARG A CZ    1 
ATOM   3426 N  NH1   . ARG A 1 429 ? 11.86261  -33.26130 -9.73722  0.000 20.50441 ? 429 ARG A NH1   1 
ATOM   3427 N  NH2   . ARG A 1 429 ? 10.88301  -35.27451 -9.25914  0.000 20.76634 ? 429 ARG A NH2   1 
ATOM   3428 N  N     . PHE A 1 430 ? 8.18002   -28.26843 -14.12885 1.000 15.23832 ? 430 PHE A N     1 
ATOM   3429 C  CA    . PHE A 1 430 ? 7.91301   -26.89743 -14.54785 1.000 11.30798 ? 430 PHE A CA    1 
ATOM   3430 C  C     . PHE A 1 430 ? 6.43900   -26.70344 -14.87083 1.000 8.22142  ? 430 PHE A C     1 
ATOM   3431 O  O     . PHE A 1 430 ? 5.84000   -25.68544 -14.50381 1.000 14.22327 ? 430 PHE A O     1 
ATOM   3432 C  CB    . PHE A 1 430 ? 8.78698   -26.56343 -15.75786 1.000 8.95040  ? 430 PHE A CB    1 
ATOM   3433 C  CG    . PHE A 1 430 ? 8.57297   -25.18343 -16.32586 1.000 10.65206 ? 430 PHE A CG    1 
ATOM   3434 C  CD1   . PHE A 1 430 ? 9.24597   -24.09343 -15.80887 1.000 12.58686 ? 430 PHE A CD1   1 
ATOM   3435 C  CD2   . PHE A 1 430 ? 7.73995   -24.99043 -17.41485 1.000 12.64644 ? 430 PHE A CD2   1 
ATOM   3436 C  CE1   . PHE A 1 430 ? 9.07196   -22.83043 -16.34587 1.000 7.73054  ? 430 PHE A CE1   1 
ATOM   3437 C  CE2   . PHE A 1 430 ? 7.55694   -23.72243 -17.95284 1.000 7.75514  ? 430 PHE A CE2   1 
ATOM   3438 C  CZ    . PHE A 1 430 ? 8.22294   -22.64643 -17.41585 1.000 7.17206  ? 430 PHE A CZ    1 
ATOM   3439 N  N     . ILE A 1 431 ? 5.83299   -27.68344 -15.54182 1.000 12.34499 ? 431 ILE A N     1 
ATOM   3440 C  CA    . ILE A 1 431 ? 4.42998   -27.58244 -15.93179 1.000 14.38815 ? 431 ILE A CA    1 
ATOM   3441 C  C     . ILE A 1 431 ? 3.53201   -27.57345 -14.70178 1.000 12.90228 ? 431 ILE A C     1 
ATOM   3442 O  O     . ILE A 1 431 ? 2.62300   -26.74445 -14.58376 1.000 11.00703 ? 431 ILE A O     1 
ATOM   3443 C  CB    . ILE A 1 431 ? 4.06497   -28.72745 -16.89379 1.000 15.87625 ? 431 ILE A CB    1 
ATOM   3444 C  CG1   . ILE A 1 431 ? 4.81795   -28.56444 -18.21680 1.000 14.90879 ? 431 ILE A CG1   1 
ATOM   3445 C  CG2   . ILE A 1 431 ? 2.56097   -28.79645 -17.11476 1.000 14.37910 ? 431 ILE A CG2   1 
ATOM   3446 C  CD1   . ILE A 1 431 ? 4.48994   -29.62244 -19.23979 1.000 10.63603 ? 431 ILE A CD1   1 
ATOM   3447 N  N     . ARG A 1 432 ? 3.78125   -28.48880 -13.76093 1.000 12.86311 ? 432 ARG A N     1 
ATOM   3448 C  CA    . ARG A 1 432 ? 2.94477   -28.57207 -12.56751 1.000 15.73961 ? 432 ARG A CA    1 
ATOM   3449 C  C     . ARG A 1 432 ? 3.05668   -27.32028 -11.70811 1.000 12.43367 ? 432 ARG A C     1 
ATOM   3450 O  O     . ARG A 1 432 ? 2.09416   -26.94870 -11.02676 1.000 11.50307 ? 432 ARG A O     1 
ATOM   3451 C  CB    . ARG A 1 432 ? 3.31887   -29.80954 -11.75034 1.000 16.36198 ? 432 ARG A CB    1 
ATOM   3452 C  CG    . ARG A 1 432 ? 3.17766   -31.11230 -12.51381 1.000 19.08262 ? 432 ARG A CG    1 
ATOM   3453 C  CD    . ARG A 1 432 ? 3.84215   -32.26672 -11.78615 1.000 16.57240 ? 432 ARG A CD    1 
ATOM   3454 N  NE    . ARG A 1 432 ? 4.02883   -33.41604 -12.66304 1.000 14.34438 ? 432 ARG A NE    1 
ATOM   3455 C  CZ    . ARG A 1 432 ? 3.11606   -34.35305 -12.87810 1.000 18.19039 ? 432 ARG A CZ    1 
ATOM   3456 N  NH1   . ARG A 1 432 ? 1.92848   -34.30798 -12.29685 1.000 20.08464 ? 432 ARG A NH1   1 
ATOM   3457 N  NH2   . ARG A 1 432 ? 3.40220   -35.36129 -13.69709 1.000 27.83785 ? 432 ARG A NH2   1 
ATOM   3458 N  N     . LYS A 1 433 ? 4.21505   -26.65945 -11.72279 1.000 15.00931 ? 433 LYS A N     1 
ATOM   3459 C  CA    . LYS A 1 433 ? 4.38806   -25.45745 -10.91279 1.000 16.73845 ? 433 LYS A CA    1 
ATOM   3460 C  C     . LYS A 1 433 ? 3.51005   -24.32145 -11.41978 1.000 14.77603 ? 433 LYS A C     1 
ATOM   3461 O  O     . LYS A 1 433 ? 2.77206   -23.70245 -10.64576 1.000 17.22240 ? 433 LYS A O     1 
ATOM   3462 C  CB    . LYS A 1 433 ? 5.85906   -25.04044 -10.89981 1.000 15.69420 ? 433 LYS A CB    1 
ATOM   3463 C  CG    . LYS A 1 433 ? 6.12706   -23.62544 -10.37182 1.000 21.34516 ? 433 LYS A CG    1 
ATOM   3464 C  CD    . LYS A 1 433 ? 5.63209   -23.41244 -8.94381  1.000 22.11527 ? 433 LYS A CD    1 
ATOM   3465 C  CE    . LYS A 1 433 ? 5.94409   -21.99244 -8.46682  1.000 26.73697 ? 433 LYS A CE    1 
ATOM   3466 N  NZ    . LYS A 1 433 ? 5.44211   -21.73744 -7.08581  1.000 31.90036 ? 433 LYS A NZ    1 
ATOM   3467 N  N     . PHE A 1 434 ? 3.57303   -24.03445 -12.71778 1.000 12.79643 ? 434 PHE A N     1 
ATOM   3468 C  CA    . PHE A 1 434 ? 2.86901   -22.88945 -13.27576 1.000 10.01539 ? 434 PHE A CA    1 
ATOM   3469 C  C     . PHE A 1 434 ? 1.50100   -23.24346 -13.83874 1.000 11.83740 ? 434 PHE A C     1 
ATOM   3470 O  O     . PHE A 1 434 ? 0.69600   -22.33546 -14.07873 1.000 14.06318 ? 434 PHE A O     1 
ATOM   3471 C  CB    . PHE A 1 434 ? 3.71799   -22.22845 -14.36678 1.000 13.00748 ? 434 PHE A CB    1 
ATOM   3472 C  CG    . PHE A 1 434 ? 5.02500   -21.68544 -13.86680 1.000 12.54674 ? 434 PHE A CG    1 
ATOM   3473 C  CD1   . PHE A 1 434 ? 5.08001   -20.46044 -13.22480 1.000 13.41715 ? 434 PHE A CD1   1 
ATOM   3474 C  CD2   . PHE A 1 434 ? 6.19500   -22.39544 -14.03682 1.000 10.42555 ? 434 PHE A CD2   1 
ATOM   3475 C  CE1   . PHE A 1 434 ? 6.28201   -19.95644 -12.76482 1.000 11.63208 ? 434 PHE A CE1   1 
ATOM   3476 C  CE2   . PHE A 1 434 ? 7.39300   -21.89544 -13.57284 1.000 11.78809 ? 434 PHE A CE2   1 
ATOM   3477 C  CZ    . PHE A 1 434 ? 7.43401   -20.67444 -12.93984 1.000 9.50934  ? 434 PHE A CZ    1 
ATOM   3478 N  N     . LEU A 1 435 ? 1.21901   -24.52846 -14.06274 1.000 13.29404 ? 435 LEU A N     1 
ATOM   3479 C  CA    . LEU A 1 435 ? -0.10400  -25.00446 -14.46872 1.000 14.40439 ? 435 LEU A CA    1 
ATOM   3480 C  C     . LEU A 1 435 ? -0.60298  -25.99946 -13.42571 1.000 13.20323 ? 435 LEU A C     1 
ATOM   3481 O  O     . LEU A 1 435 ? -0.67898  -27.20646 -13.69171 1.000 14.89899 ? 435 LEU A O     1 
ATOM   3482 C  CB    . LEU A 1 435 ? -0.07102  -25.65446 -15.85272 1.000 14.54622 ? 435 LEU A CB    1 
ATOM   3483 C  CG    . LEU A 1 435 ? -0.25704  -24.79246 -17.09971 1.000 14.51525 ? 435 LEU A CG    1 
ATOM   3484 C  CD1   . LEU A 1 435 ? 0.24694   -25.52746 -18.31872 1.000 15.24048 ? 435 LEU A CD1   1 
ATOM   3485 C  CD2   . LEU A 1 435 ? -1.72405  -24.44447 -17.28069 1.000 22.43792 ? 435 LEU A CD2   1 
ATOM   3486 N  N     . PRO A 1 436 ? -0.95596  -25.52746 -12.22670 1.000 16.97694 ? 436 PRO A N     1 
ATOM   3487 C  CA    . PRO A 1 436 ? -1.37394  -26.45847 -11.16970 1.000 14.73858 ? 436 PRO A CA    1 
ATOM   3488 C  C     . PRO A 1 436 ? -2.66294  -27.20247 -11.47767 1.000 14.48241 ? 436 PRO A C     1 
ATOM   3489 O  O     . PRO A 1 436 ? -3.02093  -28.11147 -10.71967 1.000 12.03513 ? 436 PRO A O     1 
ATOM   3490 C  CB    . PRO A 1 436 ? -1.53292  -25.55147 -9.94369  1.000 13.21564 ? 436 PRO A CB    1 
ATOM   3491 C  CG    . PRO A 1 436 ? -1.79794  -24.19847 -10.50869 1.000 16.55736 ? 436 PRO A CG    1 
ATOM   3492 C  CD    . PRO A 1 436 ? -1.03396  -24.12146 -11.78970 1.000 10.04699 ? 436 PRO A CD    1 
ATOM   3493 N  N     . VAL A 1 437 ? -3.36596  -26.86647 -12.56266 1.000 12.75230 ? 437 VAL A N     1 
ATOM   3494 C  CA    . VAL A 1 437 ? -4.53096  -27.66448 -12.92064 1.000 13.43434 ? 437 VAL A CA    1 
ATOM   3495 C  C     . VAL A 1 437 ? -4.09697  -29.06547 -13.33665 1.000 18.64732 ? 437 VAL A C     1 
ATOM   3496 O  O     . VAL A 1 437 ? -4.83396  -30.03848 -13.13164 1.000 17.39757 ? 437 VAL A O     1 
ATOM   3497 C  CB    . VAL A 1 437 ? -5.36199  -26.95448 -14.01063 1.000 15.05640 ? 437 VAL A CB    1 
ATOM   3498 C  CG1   . VAL A 1 437 ? -4.59501  -26.85148 -15.31864 1.000 17.07919 ? 437 VAL A CG1   1 
ATOM   3499 C  CG2   . VAL A 1 437 ? -6.71199  -27.65448 -14.20661 1.000 19.61189 ? 437 VAL A CG2   1 
ATOM   3500 N  N     . LEU A 1 438 ? -2.88298  -29.20247 -13.87267 1.000 16.51283 ? 438 LEU A N     1 
ATOM   3501 C  CA    . LEU A 1 438 ? -2.33798  -30.48347 -14.29968 1.000 12.37079 ? 438 LEU A CA    1 
ATOM   3502 C  C     . LEU A 1 438 ? -1.44896  -31.12447 -13.24070 1.000 14.34766 ? 438 LEU A C     1 
ATOM   3503 O  O     . LEU A 1 438 ? -0.62096  -31.97546 -13.57871 1.000 18.78361 ? 438 LEU A O     1 
ATOM   3504 C  CB    . LEU A 1 438 ? -1.54900  -30.30847 -15.59869 1.000 12.51312 ? 438 LEU A CB    1 
ATOM   3505 C  CG    . LEU A 1 438 ? -2.31802  -29.96347 -16.87568 1.000 15.54400 ? 438 LEU A CG    1 
ATOM   3506 C  CD1   . LEU A 1 438 ? -1.42904  -29.15746 -17.80170 1.000 19.37126 ? 438 LEU A CD1   1 
ATOM   3507 C  CD2   . LEU A 1 438 ? -2.79903  -31.22947 -17.57867 1.000 14.97663 ? 438 LEU A CD2   1 
ATOM   3508 N  N     . LYS A 1 439 ? -1.59794  -30.73447 -11.96869 1.000 15.24491 ? 439 LYS A N     1 
ATOM   3509 C  CA    . LYS A 1 439 ? -0.67992  -31.21946 -10.94171 1.000 20.02980 ? 439 LYS A CA    1 
ATOM   3510 C  C     . LYS A 1 439 ? -0.76691  -32.73146 -10.76171 1.000 14.53599 ? 439 LYS A C     1 
ATOM   3511 O  O     . LYS A 1 439 ? 0.24410   -33.37746 -10.46372 1.000 15.93799 ? 439 LYS A O     1 
ATOM   3512 C  CB    . LYS A 1 439 ? -0.94790  -30.51546 -9.60870  1.000 22.51698 ? 439 LYS A CB    1 
ATOM   3513 C  CG    . LYS A 1 439 ? -2.32789  -30.78447 -9.02468  1.000 20.34496 ? 439 LYS A CG    1 
ATOM   3514 C  CD    . LYS A 1 439 ? -2.32786  -30.68147 -7.50668  0.000 19.96158 ? 439 LYS A CD    1 
ATOM   3515 C  CE    . LYS A 1 439 ? -1.69486  -29.38647 -7.03169  0.000 19.22565 ? 439 LYS A CE    1 
ATOM   3516 N  NZ    . LYS A 1 439 ? -1.82884  -29.21847 -5.55769  0.000 19.25365 ? 439 LYS A NZ    1 
ATOM   3517 N  N     . ASP A 1 440 ? -1.94991  -33.31347 -10.95269 1.000 16.65745 ? 440 ASP A N     1 
ATOM   3518 C  CA    . ASP A 1 440 ? -2.17890  -34.72747 -10.69068 1.000 20.30343 ? 440 ASP A CA    1 
ATOM   3519 C  C     . ASP A 1 440 ? -2.14992  -35.57647 -11.95469 1.000 19.47001 ? 440 ASP A C     1 
ATOM   3520 O  O     . ASP A 1 440 ? -2.45692  -36.77347 -11.88968 1.000 23.22645 ? 440 ASP A O     1 
ATOM   3521 C  CB    . ASP A 1 440 ? -3.51489  -34.91647 -9.96566  1.000 25.62744 ? 440 ASP A CB    1 
ATOM   3522 C  CG    . ASP A 1 440 ? -3.51487  -34.30847 -8.57566  1.000 27.74312 ? 440 ASP A CG    1 
ATOM   3523 O  OD1   . ASP A 1 440 ? -2.44486  -33.85247 -8.12368  1.000 23.69164 ? 440 ASP A OD1   1 
ATOM   3524 O  OD2   . ASP A 1 440 ? -4.59086  -34.28948 -7.93664  1.000 33.48756 ? 440 ASP A OD2   1 
ATOM   3525 N  N     . MET A 1 441 ? -1.79794  -34.98647 -13.09169 1.000 16.00511 ? 441 MET A N     1 
ATOM   3526 C  CA    . MET A 1 441 ? -1.73196  -35.73147 -14.33869 1.000 17.69211 ? 441 MET A CA    1 
ATOM   3527 C  C     . MET A 1 441 ? -0.48596  -36.61046 -14.34371 1.000 20.27914 ? 441 MET A C     1 
ATOM   3528 O  O     . MET A 1 441 ? 0.61904   -36.11246 -14.07473 1.000 19.97964 ? 441 MET A O     1 
ATOM   3529 C  CB    . MET A 1 441 ? -1.70298  -34.76347 -15.52769 1.000 17.95134 ? 441 MET A CB    1 
ATOM   3530 C  CG    . MET A 1 441 ? -1.85000  -35.43747 -16.87869 1.000 17.52722 ? 441 MET A CG    1 
ATOM   3531 S  SD    . MET A 1 441 ? -3.44601  -36.24147 -17.10466 1.000 22.82870 ? 441 MET A SD    1 
ATOM   3532 C  CE    . MET A 1 441 ? -4.55800  -34.95148 -16.55765 1.000 21.18930 ? 441 MET A CE    1 
ATOM   3533 N  N     . PRO A 1 442 ? -0.61396  -37.90946 -14.61271 1.000 13.82616 ? 442 PRO A N     1 
ATOM   3534 C  CA    . PRO A 1 442 ? 0.57204   -38.76646 -14.68673 1.000 21.09239 ? 442 PRO A CA    1 
ATOM   3535 C  C     . PRO A 1 442 ? 1.55302   -38.27945 -15.74375 1.000 17.26126 ? 442 PRO A C     1 
ATOM   3536 O  O     . PRO A 1 442 ? 1.17601   -37.64946 -16.73374 1.000 14.91250 ? 442 PRO A O     1 
ATOM   3537 C  CB    . PRO A 1 442 ? -0.00396  -40.14146 -15.04272 1.000 20.62622 ? 442 PRO A CB    1 
ATOM   3538 C  CG    . PRO A 1 442 ? -1.41395  -40.10146 -14.52570 1.000 17.24234 ? 442 PRO A CG    1 
ATOM   3539 C  CD    . PRO A 1 442 ? -1.86596  -38.67847 -14.72069 1.000 15.31417 ? 442 PRO A CD    1 
ATOM   3540 N  N     . ALA A 1 443 ? 2.83203   -38.59845 -15.51977 1.000 11.62471 ? 443 ALA A N     1 
ATOM   3541 C  CA    . ALA A 1 443 ? 3.90101   -38.05745 -16.35279 1.000 13.20747 ? 443 ALA A CA    1 
ATOM   3542 C  C     . ALA A 1 443 ? 3.77099   -38.48545 -17.80678 1.000 17.58137 ? 443 ALA A C     1 
ATOM   3543 O  O     . ALA A 1 443 ? 4.24197   -37.77544 -18.70279 1.000 21.26167 ? 443 ALA A O     1 
ATOM   3544 C  CB    . ALA A 1 443 ? 5.26102   -38.48344 -15.80381 1.000 15.77275 ? 443 ALA A CB    1 
ATOM   3545 N  N     . LYS A 1 444 ? 3.13399   -39.63345 -18.06077 1.000 17.01683 ? 444 LYS A N     1 
ATOM   3546 C  CA    . LYS A 1 444 ? 3.03297   -40.15345 -19.42177 1.000 18.87659 ? 444 LYS A CA    1 
ATOM   3547 C  C     . LYS A 1 444 ? 2.26695   -39.20145 -20.33076 1.000 14.41664 ? 444 LYS A C     1 
ATOM   3548 O  O     . LYS A 1 444 ? 2.53493   -39.13945 -21.53676 1.000 19.70221 ? 444 LYS A O     1 
ATOM   3549 C  CB    . LYS A 1 444 ? 2.36597   -41.53245 -19.39676 1.000 23.00786 ? 444 LYS A CB    1 
ATOM   3550 C  CG    . LYS A 1 444 ? 2.21795   -42.21145 -20.74776 1.000 23.96734 ? 444 LYS A CG    1 
ATOM   3551 C  CD    . LYS A 1 444 ? 2.18896   -43.72745 -20.57976 1.000 26.89911 ? 444 LYS A CD    1 
ATOM   3552 C  CE    . LYS A 1 444 ? 1.76294   -44.43645 -21.85475 0.000 24.26731 ? 444 LYS A CE    1 
ATOM   3553 N  NZ    . LYS A 1 444 ? 0.28194   -44.51646 -21.97973 0.000 23.91566 ? 444 LYS A NZ    1 
ATOM   3554 N  N     . TYR A 1 445 ? 1.33596   -38.42945 -19.77074 1.000 20.49675 ? 445 TYR A N     1 
ATOM   3555 C  CA    . TYR A 1 445 ? 0.44994   -37.59446 -20.56973 1.000 15.22219 ? 445 TYR A CA    1 
ATOM   3556 C  C     . TYR A 1 445 ? 0.57694   -36.10746 -20.26373 1.000 16.57410 ? 445 TYR A C     1 
ATOM   3557 O  O     . TYR A 1 445 ? -0.18307  -35.31446 -20.82772 1.000 16.56148 ? 445 TYR A O     1 
ATOM   3558 C  CB    . TYR A 1 445 ? -0.99905  -38.02846 -20.35971 1.000 13.81448 ? 445 TYR A CB    1 
ATOM   3559 C  CG    . TYR A 1 445 ? -1.21705  -39.51546 -20.48570 1.000 19.85626 ? 445 TYR A CG    1 
ATOM   3560 C  CD1   . TYR A 1 445 ? -1.30407  -40.11846 -21.73170 1.000 20.25566 ? 445 TYR A CD1   1 
ATOM   3561 C  CD2   . TYR A 1 445 ? -1.34203  -40.32046 -19.36070 1.000 20.84848 ? 445 TYR A CD2   1 
ATOM   3562 C  CE1   . TYR A 1 445 ? -1.50507  -41.47446 -21.85770 1.000 18.69553 ? 445 TYR A CE1   1 
ATOM   3563 C  CE2   . TYR A 1 445 ? -1.54303  -41.68546 -19.47670 1.000 18.16259 ? 445 TYR A CE2   1 
ATOM   3564 C  CZ    . TYR A 1 445 ? -1.62604  -42.25246 -20.73070 1.000 20.93794 ? 445 TYR A CZ    1 
ATOM   3565 O  OH    . TYR A 1 445 ? -1.82604  -43.60546 -20.86269 1.000 30.42251 ? 445 TYR A OH    1 
ATOM   3566 N  N     . ILE A 1 446 ? 1.50895   -35.69445 -19.40075 1.000 13.80958 ? 446 ILE A N     1 
ATOM   3567 C  CA    . ILE A 1 446 ? 1.49596   -34.30045 -18.94775 1.000 15.99479 ? 446 ILE A CA    1 
ATOM   3568 C  C     . ILE A 1 446 ? 1.84994   -33.33745 -20.07675 1.000 17.27308 ? 446 ILE A C     1 
ATOM   3569 O  O     . ILE A 1 446 ? 1.44493   -32.16845 -20.05074 1.000 16.03945 ? 446 ILE A O     1 
ATOM   3570 C  CB    . ILE A 1 446 ? 2.42298   -34.11145 -17.73376 1.000 15.02639 ? 446 ILE A CB    1 
ATOM   3571 C  CG1   . ILE A 1 446 ? 2.12798   -32.76745 -17.06176 1.000 14.53352 ? 446 ILE A CG1   1 
ATOM   3572 C  CG2   . ILE A 1 446 ? 3.88897   -34.20545 -18.14979 1.000 13.24279 ? 446 ILE A CG2   1 
ATOM   3573 C  CD1   . ILE A 1 446 ? 2.90000   -32.52845 -15.80377 1.000 16.81115 ? 446 ILE A CD1   1 
ATOM   3574 N  N     . TYR A 1 447 ? 2.59192   -33.79545 -21.08276 1.000 18.89496 ? 447 TYR A N     1 
ATOM   3575 C  CA    . TYR A 1 447 ? 2.84190   -32.97745 -22.25977 1.000 14.12086 ? 447 TYR A CA    1 
ATOM   3576 C  C     . TYR A 1 447 ? 1.77288   -33.13345 -23.32875 1.000 17.49674 ? 447 TYR A C     1 
ATOM   3577 O  O     . TYR A 1 447 ? 1.66286   -32.26845 -24.20375 1.000 15.34815 ? 447 TYR A O     1 
ATOM   3578 C  CB    . TYR A 1 447 ? 4.20889   -33.31144 -22.85479 1.000 18.67306 ? 447 TYR A CB    1 
ATOM   3579 C  CG    . TYR A 1 447 ? 5.36490   -32.80044 -22.02781 1.000 16.14111 ? 447 TYR A CG    1 
ATOM   3580 C  CD1   . TYR A 1 447 ? 5.84089   -31.50844 -22.19282 1.000 10.84894 ? 447 TYR A CD1   1 
ATOM   3581 C  CD2   . TYR A 1 447 ? 5.97392   -33.60844 -21.08082 1.000 13.80911 ? 447 TYR A CD2   1 
ATOM   3582 C  CE1   . TYR A 1 447 ? 6.89991   -31.03943 -21.43883 1.000 10.62667 ? 447 TYR A CE1   1 
ATOM   3583 C  CE2   . TYR A 1 447 ? 7.02593   -33.14943 -20.32284 1.000 13.63270 ? 447 TYR A CE2   1 
ATOM   3584 C  CZ    . TYR A 1 447 ? 7.48692   -31.86543 -20.50284 1.000 11.69290 ? 447 TYR A CZ    1 
ATOM   3585 O  OH    . TYR A 1 447 ? 8.54293   -31.41843 -19.73986 1.000 14.69562 ? 447 TYR A OH    1 
ATOM   3586 N  N     . GLU A 1 448 ? 0.98589   -34.20345 -23.27074 1.000 18.42683 ? 448 GLU A N     1 
ATOM   3587 C  CA    . GLU A 1 448 ? -0.06613  -34.49146 -24.24372 1.000 16.33061 ? 448 GLU A CA    1 
ATOM   3588 C  C     . GLU A 1 448 ? -1.32512  -34.92346 -23.50470 1.000 21.19967 ? 448 GLU A C     1 
ATOM   3589 O  O     . GLU A 1 448 ? -1.77911  -36.07046 -23.64869 1.000 18.54831 ? 448 GLU A O     1 
ATOM   3590 C  CB    . GLU A 1 448 ? 0.38186   -35.57546 -25.22673 1.000 20.45585 ? 448 GLU A CB    1 
ATOM   3591 C  CG    . GLU A 1 448 ? 1.60284   -35.20745 -26.05475 1.000 25.15889 ? 448 GLU A CG    1 
ATOM   3592 C  CD    . GLU A 1 448 ? 2.14183   -36.38445 -26.83776 1.000 26.71248 ? 448 GLU A CD    1 
ATOM   3593 O  OE1   . GLU A 1 448 ? 2.44185   -37.42745 -26.21776 1.000 32.64951 ? 448 GLU A OE1   1 
ATOM   3594 O  OE2   . GLU A 1 448 ? 2.25381   -36.27045 -28.07676 1.000 29.86732 ? 448 GLU A OE2   1 
ATOM   3595 N  N     . PRO A 1 449 ? -1.92811  -34.02646 -22.71469 1.000 16.32042 ? 449 PRO A N     1 
ATOM   3596 C  CA    . PRO A 1 449 ? -3.05409  -34.44947 -21.86767 1.000 16.57666 ? 449 PRO A CA    1 
ATOM   3597 C  C     . PRO A 1 449 ? -4.25810  -34.92847 -22.65465 1.000 19.13385 ? 449 PRO A C     1 
ATOM   3598 O  O     . PRO A 1 449 ? -5.03709  -35.74147 -22.13964 1.000 22.45322 ? 449 PRO A O     1 
ATOM   3599 C  CB    . PRO A 1 449 ? -3.36708  -33.19047 -21.05066 1.000 18.75657 ? 449 PRO A CB    1 
ATOM   3600 C  CG    . PRO A 1 449 ? -2.85910  -32.06247 -21.88067 1.000 16.72903 ? 449 PRO A CG    1 
ATOM   3601 C  CD    . PRO A 1 449 ? -1.64011  -32.58946 -22.57669 1.000 15.73703 ? 449 PRO A CD    1 
ATOM   3602 N  N     . TRP A 1 450 ? -4.42112  -34.47347 -23.89965 1.000 15.37854 ? 450 TRP A N     1 
ATOM   3603 C  CA    . TRP A 1 450 ? -5.53114  -34.93848 -24.72263 1.000 15.67354 ? 450 TRP A CA    1 
ATOM   3604 C  C     . TRP A 1 450 ? -5.41914  -36.41548 -25.07363 1.000 15.03506 ? 450 TRP A C     1 
ATOM   3605 O  O     . TRP A 1 450 ? -6.43314  -37.03048 -25.41561 1.000 14.50172 ? 450 TRP A O     1 
ATOM   3606 C  CB    . TRP A 1 450 ? -5.63216  -34.10248 -26.00463 1.000 19.67038 ? 450 TRP A CB    1 
ATOM   3607 C  CG    . TRP A 1 450 ? -4.41317  -34.15847 -26.88165 1.000 15.56027 ? 450 TRP A CG    1 
ATOM   3608 C  CD1   . TRP A 1 450 ? -4.19719  -35.00547 -27.93265 1.000 24.02016 ? 450 TRP A CD1   1 
ATOM   3609 C  CD2   . TRP A 1 450 ? -3.24718  -33.33247 -26.79067 1.000 16.21532 ? 450 TRP A CD2   1 
ATOM   3610 N  NE1   . TRP A 1 450 ? -2.96820  -34.75947 -28.49667 1.000 14.79569 ? 450 TRP A NE1   1 
ATOM   3611 C  CE2   . TRP A 1 450 ? -2.36619  -33.73546 -27.81668 1.000 15.66353 ? 450 TRP A CE2   1 
ATOM   3612 C  CE3   . TRP A 1 450 ? -2.86217  -32.28747 -25.94467 1.000 17.60057 ? 450 TRP A CE3   1 
ATOM   3613 C  CZ2   . TRP A 1 450 ? -1.12420  -33.13246 -28.01570 1.000 21.52862 ? 450 TRP A CZ2   1 
ATOM   3614 C  CZ3   . TRP A 1 450 ? -1.62517  -31.68846 -26.14269 1.000 19.26604 ? 450 TRP A CZ3   1 
ATOM   3615 C  CH2   . TRP A 1 450 ? -0.77319  -32.11346 -27.17171 1.000 18.09831 ? 450 TRP A CH2   1 
ATOM   3616 N  N     . THR A 1 451 ? -4.22513  -37.00147 -24.98965 1.000 14.68254 ? 451 THR A N     1 
ATOM   3617 C  CA    . THR A 1 451 ? -4.03213  -38.40947 -25.32265 1.000 22.28478 ? 451 THR A CA    1 
ATOM   3618 C  C     . THR A 1 451 ? -4.29511  -39.34447 -24.14965 1.000 17.51315 ? 451 THR A C     1 
ATOM   3619 O  O     . THR A 1 451 ? -4.23811  -40.56547 -24.32565 1.000 15.22151 ? 451 THR A O     1 
ATOM   3620 C  CB    . THR A 1 451 ? -2.61014  -38.64747 -25.85068 1.000 15.40270 ? 451 THR A CB    1 
ATOM   3621 O  OG1   . THR A 1 451 ? -1.65513  -38.26746 -24.85569 1.000 18.05508 ? 451 THR A OG1   1 
ATOM   3622 C  CG2   . THR A 1 451 ? -2.36617  -37.84446 -27.11068 1.000 14.14487 ? 451 THR A CG2   1 
ATOM   3623 N  N     . ALA A 1 452 ? -4.57809  -38.80947 -22.97065 1.000 18.61126 ? 452 ALA A N     1 
ATOM   3624 C  CA    . ALA A 1 452 ? -4.84207  -39.63247 -21.80064 1.000 17.01847 ? 452 ALA A CA    1 
ATOM   3625 C  C     . ALA A 1 452 ? -6.27007  -40.17248 -21.84562 1.000 15.69504 ? 452 ALA A C     1 
ATOM   3626 O  O     . ALA A 1 452 ? -7.19708  -39.44648 -22.21560 1.000 15.22945 ? 452 ALA A O     1 
ATOM   3627 C  CB    . ALA A 1 452 ? -4.63305  -38.82947 -20.52064 1.000 19.91270 ? 452 ALA A CB    1 
ATOM   3628 N  N     . PRO A 1 453 ? -6.47006  -41.43848 -21.48462 1.000 18.86812 ? 453 PRO A N     1 
ATOM   3629 C  CA    . PRO A 1 453 ? -7.82906  -41.98748 -21.45759 1.000 17.93854 ? 453 PRO A CA    1 
ATOM   3630 C  C     . PRO A 1 453 ? -8.71905  -41.18749 -20.51958 1.000 20.74123 ? 453 PRO A C     1 
ATOM   3631 O  O     . PRO A 1 453 ? -8.25803  -40.60549 -19.53559 1.000 23.64741 ? 453 PRO A O     1 
ATOM   3632 C  CB    . PRO A 1 453 ? -7.62404  -43.42148 -20.95460 1.000 25.96619 ? 453 PRO A CB    1 
ATOM   3633 C  CG    . PRO A 1 453 ? -6.18805  -43.72848 -21.26462 1.000 21.30524 ? 453 PRO A CG    1 
ATOM   3634 C  CD    . PRO A 1 453 ? -5.45905  -42.43248 -21.09563 1.000 19.86389 ? 453 PRO A CD    1 
ATOM   3635 N  N     . LEU A 1 454 ? -10.01505 -41.15449 -20.84456 1.000 22.45010 ? 454 LEU A N     1 
ATOM   3636 C  CA    . LEU A 1 454 ? -10.95104 -40.34650 -20.06854 1.000 22.94773 ? 454 LEU A CA    1 
ATOM   3637 C  C     . LEU A 1 454 ? -10.94401 -40.72850 -18.59054 1.000 28.12727 ? 454 LEU A C     1 
ATOM   3638 O  O     . LEU A 1 454 ? -11.15500 -39.86850 -17.72754 1.000 27.21153 ? 454 LEU A O     1 
ATOM   3639 C  CB    . LEU A 1 454 ? -12.35605 -40.47850 -20.65352 1.000 20.37191 ? 454 LEU A CB    1 
ATOM   3640 C  CG    . LEU A 1 454 ? -13.46804 -39.60950 -20.06150 1.000 21.47004 ? 454 LEU A CG    1 
ATOM   3641 C  CD1   . LEU A 1 454 ? -13.13405 -38.13650 -20.19750 1.000 22.58466 ? 454 LEU A CD1   1 
ATOM   3642 C  CD2   . LEU A 1 454 ? -14.80005 -39.91751 -20.73348 1.000 15.95779 ? 454 LEU A CD2   1 
ATOM   3643 N  N     . GLU A 1 455 ? -10.68101 -42.00150 -18.27955 1.000 25.11634 ? 455 GLU A N     1 
ATOM   3644 C  CA    . GLU A 1 455 ? -10.64898 -42.43650 -16.88655 1.000 26.73653 ? 455 GLU A CA    1 
ATOM   3645 C  C     . GLU A 1 455 ? -9.54997  -41.72649 -16.10656 1.000 24.48998 ? 455 GLU A C     1 
ATOM   3646 O  O     . GLU A 1 455 ? -9.77395  -41.26949 -14.98056 1.000 25.64051 ? 455 GLU A O     1 
ATOM   3647 C  CB    . GLU A 1 455 ? -10.46097 -43.95250 -16.81555 1.000 28.10232 ? 455 GLU A CB    1 
ATOM   3648 C  CG    . GLU A 1 455 ? -10.13995 -44.47349 -15.42156 1.000 20.55366 ? 455 GLU A CG    1 
ATOM   3649 C  CD    . GLU A 1 455 ? -9.68494  -45.91849 -15.42756 0.000 23.50794 ? 455 GLU A CD    1 
ATOM   3650 O  OE1   . GLU A 1 455 ? -10.31795 -46.73949 -16.12555 0.000 23.37824 ? 455 GLU A OE1   1 
ATOM   3651 O  OE2   . GLU A 1 455 ? -8.69293  -46.23449 -14.73758 0.000 23.51234 ? 455 GLU A OE2   1 
ATOM   3652 N  N     . VAL A 1 456 ? -8.35598  -41.61849 -16.69258 1.000 28.47698 ? 456 VAL A N     1 
ATOM   3653 C  CA    . VAL A 1 456 ? -7.24497  -40.98548 -15.98960 1.000 25.35278 ? 456 VAL A CA    1 
ATOM   3654 C  C     . VAL A 1 456 ? -7.46297  -39.48349 -15.88160 1.000 24.14936 ? 456 VAL A C     1 
ATOM   3655 O  O     . VAL A 1 456 ? -7.08096  -38.86648 -14.87960 1.000 27.27961 ? 456 VAL A O     1 
ATOM   3656 C  CB    . VAL A 1 456 ? -5.90998  -41.31148 -16.68562 1.000 25.97404 ? 456 VAL A CB    1 
ATOM   3657 C  CG1   . VAL A 1 456 ? -4.73897  -40.74848 -15.89064 1.000 28.18563 ? 456 VAL A CG1   1 
ATOM   3658 C  CG2   . VAL A 1 456 ? -5.76198  -42.80948 -16.86863 1.000 21.33938 ? 456 VAL A CG2   1 
ATOM   3659 N  N     . GLN A 1 457 ? -8.07499  -38.86949 -16.89959 1.000 20.86580 ? 457 GLN A N     1 
ATOM   3660 C  CA    . GLN A 1 457 ? -8.41000  -37.45249 -16.81458 1.000 23.13079 ? 457 GLN A CA    1 
ATOM   3661 C  C     . GLN A 1 457 ? -9.33198  -37.17249 -15.63557 1.000 21.49417 ? 457 GLN A C     1 
ATOM   3662 O  O     . GLN A 1 457 ? -9.13097  -36.20149 -14.89857 1.000 20.25242 ? 457 GLN A O     1 
ATOM   3663 C  CB    . GLN A 1 457 ? -9.06302  -36.98549 -18.11557 1.000 21.72970 ? 457 GLN A CB    1 
ATOM   3664 C  CG    . GLN A 1 457 ? -8.12704  -36.90949 -19.30159 1.000 22.09080 ? 457 GLN A CG    1 
ATOM   3665 C  CD    . GLN A 1 457 ? -8.81106  -36.34849 -20.52357 1.000 21.12794 ? 457 GLN A CD    1 
ATOM   3666 O  OE1   . GLN A 1 457 ? -9.88706  -35.75749 -20.42956 1.000 22.30496 ? 457 GLN A OE1   1 
ATOM   3667 N  NE2   . GLN A 1 457 ? -8.19808  -36.53749 -21.68259 1.000 26.88892 ? 457 GLN A NE2   1 
ATOM   3668 N  N     . ARG A 1 458 ? -10.35033 -38.01571 -15.44175 1.000 24.71702 ? 458 ARG A N     1 
ATOM   3669 C  CA    . ARG A 1 458 ? -11.26768 -37.82798 -14.32181 1.000 29.25464 ? 458 ARG A CA    1 
ATOM   3670 C  C     . ARG A 1 458 ? -10.57197 -38.06842 -12.98746 1.000 27.14833 ? 458 ARG A C     1 
ATOM   3671 O  O     . ARG A 1 458 ? -10.82985 -37.35503 -12.01072 1.000 30.83126 ? 458 ARG A O     1 
ATOM   3672 C  CB    . ARG A 1 458 ? -12.47515 -38.75429 -14.46775 1.000 25.99204 ? 458 ARG A CB    1 
ATOM   3673 C  CG    . ARG A 1 458 ? -13.35865 -38.45423 -15.66460 1.000 21.59728 ? 458 ARG A CG    1 
ATOM   3674 C  CD    . ARG A 1 458 ? -14.37326 -39.56756 -15.87660 0.000 24.73551 ? 458 ARG A CD    1 
ATOM   3675 N  NE    . ARG A 1 458 ? -15.27841 -39.28948 -16.98503 0.000 24.47834 ? 458 ARG A NE    1 
ATOM   3676 C  CZ    . ARG A 1 458 ? -16.48517 -38.75681 -16.85049 0.000 24.75615 ? 458 ARG A CZ    1 
ATOM   3677 N  NH1   . ARG A 1 458 ? -16.96877 -38.43179 -15.66271 0.000 25.50757 ? 458 ARG A NH1   1 
ATOM   3678 N  NH2   . ARG A 1 458 ? -17.22626 -38.54680 -17.93466 0.000 24.60033 ? 458 ARG A NH2   1 
ATOM   3679 N  N     . LYS A 1 459 ? -9.69193  -39.07149 -12.92156 1.000 29.96193 ? 459 LYS A N     1 
ATOM   3680 C  CA    A LYS A 1 459 ? -8.96190  -39.34949 -11.68857 0.539 26.09545 ? 459 LYS A CA    1 
ATOM   3681 C  CA    B LYS A 1 459 ? -8.97990  -39.33749 -11.67957 0.461 26.10015 ? 459 LYS A CA    1 
ATOM   3682 C  C     . LYS A 1 459 ? -7.96390  -38.25249 -11.35459 1.000 24.87607 ? 459 LYS A C     1 
ATOM   3683 O  O     . LYS A 1 459 ? -7.60388  -38.08949 -10.18560 1.000 25.39124 ? 459 LYS A O     1 
ATOM   3684 C  CB    A LYS A 1 459 ? -8.23590  -40.69449 -11.79259 0.539 29.17181 ? 459 LYS A CB    1 
ATOM   3685 C  CB    B LYS A 1 459 ? -8.29790  -40.70549 -11.74758 0.461 29.16420 ? 459 LYS A CB    1 
ATOM   3686 C  CG    A LYS A 1 459 ? -8.57488  -41.68749 -10.68258 0.539 29.10334 ? 459 LYS A CG    1 
ATOM   3687 C  CG    B LYS A 1 459 ? -8.76588  -41.66849 -10.66858 0.461 29.08567 ? 459 LYS A CG    1 
ATOM   3688 C  CD    A LYS A 1 459 ? -8.06686  -41.21749 -9.32259  0.539 33.00183 ? 459 LYS A CD    1 
ATOM   3689 C  CD    B LYS A 1 459 ? -10.28388 -41.65850 -10.54755 0.461 28.11692 ? 459 LYS A CD    1 
ATOM   3690 C  CE    A LYS A 1 459 ? -6.59385  -41.55348 -9.11461  0.539 29.99856 ? 459 LYS A CE    1 
ATOM   3691 C  CE    B LYS A 1 459 ? -10.91389 -42.80850 -11.30954 0.461 30.65967 ? 459 LYS A CE    1 
ATOM   3692 N  NZ    A LYS A 1 459 ? -6.38684  -42.99348 -8.78362  0.539 21.87299 ? 459 LYS A NZ    1 
ATOM   3693 N  NZ    B LYS A 1 459 ? -10.52587 -44.12050 -10.72155 0.461 30.17157 ? 459 LYS A NZ    1 
ATOM   3694 N  N     . ALA A 1 460 ? -7.50792  -37.50549 -12.35160 1.000 27.44131 ? 460 ALA A N     1 
ATOM   3695 C  CA    . ALA A 1 460 ? -6.58492  -36.40348 -12.14761 1.000 16.69150 ? 460 ALA A CA    1 
ATOM   3696 C  C     . ALA A 1 460 ? -7.29292  -35.06649 -12.00760 1.000 15.66162 ? 460 ALA A C     1 
ATOM   3697 O  O     . ALA A 1 460 ? -6.62792  -34.05048 -11.79261 1.000 20.79027 ? 460 ALA A O     1 
ATOM   3698 C  CB    . ALA A 1 460 ? -5.57994  -36.33648 -13.30063 1.000 16.99624 ? 460 ALA A CB    1 
ATOM   3699 N  N     . GLY A 1 461 ? -8.61693  -35.04049 -12.14058 1.000 19.44399 ? 461 GLY A N     1 
ATOM   3700 C  CA    . GLY A 1 461 ? -9.36093  -33.80449 -11.98756 1.000 16.63780 ? 461 GLY A CA    1 
ATOM   3701 C  C     . GLY A 1 461 ? -9.07595  -32.77249 -13.05257 1.000 22.04197 ? 461 GLY A C     1 
ATOM   3702 O  O     . GLY A 1 461 ? -9.19695  -31.56949 -12.79457 1.000 21.61139 ? 461 GLY A O     1 
ATOM   3703 N  N     . CYS A 1 462 ? -8.69697  -33.21249 -14.25158 1.000 19.05067 ? 462 CYS A N     1 
ATOM   3704 C  CA    . CYS A 1 462 ? -8.36499  -32.32049 -15.36258 1.000 16.85043 ? 462 CYS A CA    1 
ATOM   3705 C  C     . CYS A 1 462 ? -8.91401  -32.96649 -16.63257 1.000 14.55772 ? 462 CYS A C     1 
ATOM   3706 O  O     . CYS A 1 462 ? -8.21202  -33.72149 -17.30958 1.000 21.62518 ? 462 CYS A O     1 
ATOM   3707 C  CB    . CYS A 1 462 ? -6.86399  -32.07748 -15.44961 1.000 17.37956 ? 462 CYS A CB    1 
ATOM   3708 S  SG    . CYS A 1 462 ? -6.35002  -30.94448 -16.76961 1.000 18.15157 ? 462 CYS A SG    1 
ATOM   3709 N  N     . VAL A 1 463 ? -10.17201 -32.67549 -16.94455 1.000 17.27241 ? 463 VAL A N     1 
ATOM   3710 C  CA    . VAL A 1 463 ? -10.80903 -33.16850 -18.16254 1.000 16.91307 ? 463 VAL A CA    1 
ATOM   3711 C  C     . VAL A 1 463 ? -10.48606 -32.20649 -19.29855 1.000 17.49474 ? 463 VAL A C     1 
ATOM   3712 O  O     . VAL A 1 463 ? -10.77706 -31.00850 -19.20554 1.000 21.08471 ? 463 VAL A O     1 
ATOM   3713 C  CB    . VAL A 1 463 ? -12.32603 -33.31450 -17.97552 1.000 16.27949 ? 463 VAL A CB    1 
ATOM   3714 C  CG1   . VAL A 1 463 ? -12.99205 -33.66050 -19.29650 1.000 20.03000 ? 463 VAL A CG1   1 
ATOM   3715 C  CG2   . VAL A 1 463 ? -12.63301 -34.37250 -16.92351 1.000 28.21493 ? 463 VAL A CG2   1 
ATOM   3716 N  N     . VAL A 1 464 ? -9.87507  -32.72249 -20.36756 1.000 16.23898 ? 464 VAL A N     1 
ATOM   3717 C  CA    . VAL A 1 464 ? -9.58309  -31.88349 -21.52356 1.000 17.45521 ? 464 VAL A CA    1 
ATOM   3718 C  C     . VAL A 1 464 ? -10.88711 -31.41249 -22.14654 1.000 15.46172 ? 464 VAL A C     1 
ATOM   3719 O  O     . VAL A 1 464 ? -11.78211 -32.21350 -22.43952 1.000 16.32697 ? 464 VAL A O     1 
ATOM   3720 C  CB    . VAL A 1 464 ? -8.72411  -32.63749 -22.54658 1.000 20.43556 ? 464 VAL A CB    1 
ATOM   3721 C  CG1   . VAL A 1 464 ? -8.45013  -31.74349 -23.75458 1.000 21.37567 ? 464 VAL A CG1   1 
ATOM   3722 C  CG2   . VAL A 1 464 ? -7.42610  -33.09048 -21.91360 1.000 19.85648 ? 464 VAL A CG2   1 
ATOM   3723 N  N     . GLY A 1 465 ? -10.99711 -30.10050 -22.34954 1.000 19.21903 ? 465 GLY A N     1 
ATOM   3724 C  CA    . GLY A 1 465 ? -12.21012 -29.48350 -22.83752 1.000 13.77354 ? 465 GLY A CA    1 
ATOM   3725 C  C     . GLY A 1 465 ? -13.09911 -28.90750 -21.75950 1.000 15.45176 ? 465 GLY A C     1 
ATOM   3726 O  O     . GLY A 1 465 ? -14.04512 -28.17951 -22.08449 1.000 17.72381 ? 465 GLY A O     1 
ATOM   3727 N  N     . ARG A 1 466 ? -12.82870 -29.21152 -20.49272 1.000 17.25498 ? 466 ARG A N     1 
ATOM   3728 C  CA    . ARG A 1 466 ? -13.59352 -28.67594 -19.37411 1.000 19.98506 ? 466 ARG A CA    1 
ATOM   3729 C  C     . ARG A 1 466 ? -12.71578 -27.93238 -18.38203 1.000 21.83365 ? 466 ARG A C     1 
ATOM   3730 O  O     . ARG A 1 466 ? -13.01046 -26.77985 -18.03916 1.000 12.56917 ? 466 ARG A O     1 
ATOM   3731 C  CB    . ARG A 1 466 ? -14.34770 -29.80960 -18.66217 1.000 24.09213 ? 466 ARG A CB    1 
ATOM   3732 C  CG    . ARG A 1 466 ? -15.27788 -29.33776 -17.56070 1.000 23.80160 ? 466 ARG A CG    1 
ATOM   3733 C  CD    . ARG A 1 466 ? -16.04061 -30.49903 -16.95091 1.000 24.37406 ? 466 ARG A CD    1 
ATOM   3734 N  NE    . ARG A 1 466 ? -15.14932 -31.46505 -16.31961 1.000 33.84251 ? 466 ARG A NE    1 
ATOM   3735 C  CZ    . ARG A 1 466 ? -14.70777 -31.37190 -15.07270 1.000 30.10311 ? 466 ARG A CZ    1 
ATOM   3736 N  NH1   . ARG A 1 466 ? -15.04657 -30.35793 -14.29326 1.000 33.46322 ? 466 ARG A NH1   1 
ATOM   3737 N  NH2   . ARG A 1 466 ? -13.90533 -32.31902 -14.59612 1.000 25.10876 ? 466 ARG A NH2   1 
ATOM   3738 N  N     . ASP A 1 467 ? -11.64204 -28.56450 -17.91153 1.000 15.10520 ? 467 ASP A N     1 
ATOM   3739 C  CA    . ASP A 1 467 ? -10.67303 -27.95350 -17.01054 1.000 17.01797 ? 467 ASP A CA    1 
ATOM   3740 C  C     . ASP A 1 467 ? -9.46005  -27.39949 -17.74256 1.000 15.73646 ? 467 ASP A C     1 
ATOM   3741 O  O     . ASP A 1 467 ? -8.93804  -26.34649 -17.36557 1.000 15.11443 ? 467 ASP A O     1 
ATOM   3742 C  CB    . ASP A 1 467 ? -10.20801 -28.97549 -15.96855 1.000 17.13934 ? 467 ASP A CB    1 
ATOM   3743 C  CG    . ASP A 1 467 ? -11.36200 -29.58650 -15.19553 1.000 19.71692 ? 467 ASP A CG    1 
ATOM   3744 O  OD1   . ASP A 1 467 ? -12.21599 -28.82150 -14.70252 1.000 20.41795 ? 467 ASP A OD1   1 
ATOM   3745 O  OD2   . ASP A 1 467 ? -11.41499 -30.82850 -15.08653 1.000 16.98064 ? 467 ASP A OD2   1 
ATOM   3746 N  N     . TYR A 1 468 ? -8.99506  -28.09849 -18.77157 1.000 14.67617 ? 468 TYR A N     1 
ATOM   3747 C  CA    . TYR A 1 468 ? -7.88508  -27.65949 -19.59159 1.000 20.57134 ? 468 TYR A CA    1 
ATOM   3748 C  C     . TYR A 1 468 ? -8.29310  -27.75949 -21.05358 1.000 17.80007 ? 468 TYR A C     1 
ATOM   3749 O  O     . TYR A 1 468 ? -8.95210  -28.72949 -21.44757 1.000 17.05775 ? 468 TYR A O     1 
ATOM   3750 C  CB    . TYR A 1 468 ? -6.62907  -28.50348 -19.32761 1.000 17.28233 ? 468 TYR A CB    1 
ATOM   3751 C  CG    . TYR A 1 468 ? -5.39008  -27.94548 -19.97963 1.000 12.17829 ? 468 TYR A CG    1 
ATOM   3752 C  CD1   . TYR A 1 468 ? -4.76108  -26.81847 -19.47064 1.000 14.88860 ? 468 TYR A CD1   1 
ATOM   3753 C  CD2   . TYR A 1 468 ? -4.85610  -28.53547 -21.11264 1.000 15.03269 ? 468 TYR A CD2   1 
ATOM   3754 C  CE1   . TYR A 1 468 ? -3.63009  -26.29847 -20.07166 1.000 12.85227 ? 468 TYR A CE1   1 
ATOM   3755 C  CE2   . TYR A 1 468 ? -3.72511  -28.02547 -21.71466 1.000 14.85935 ? 468 TYR A CE2   1 
ATOM   3756 C  CZ    . TYR A 1 468 ? -3.11510  -26.90947 -21.18967 1.000 9.50992  ? 468 TYR A CZ    1 
ATOM   3757 O  OH    . TYR A 1 468 ? -1.99512  -26.40046 -21.79668 1.000 9.16807  ? 468 TYR A OH    1 
ATOM   3758 N  N     . PRO A 1 469 ? -7.95012  -26.77048 -21.87259 1.000 14.24713 ? 469 PRO A N     1 
ATOM   3759 C  CA    . PRO A 1 469 ? -8.42114  -26.76949 -23.25858 1.000 18.79457 ? 469 PRO A CA    1 
ATOM   3760 C  C     . PRO A 1 469 ? -7.71315  -27.80848 -24.11059 1.000 16.49148 ? 469 PRO A C     1 
ATOM   3761 O  O     . PRO A 1 469 ? -6.62914  -28.29848 -23.78561 1.000 18.52394 ? 469 PRO A O     1 
ATOM   3762 C  CB    . PRO A 1 469 ? -8.10015  -25.35148 -23.74358 1.000 18.94296 ? 469 PRO A CB    1 
ATOM   3763 C  CG    . PRO A 1 469 ? -6.97314  -24.91248 -22.88760 1.000 15.01106 ? 469 PRO A CG    1 
ATOM   3764 C  CD    . PRO A 1 469 ? -7.24512  -25.52248 -21.53460 1.000 12.71959 ? 469 PRO A CD    1 
ATOM   3765 N  N     . ALA A 1 470 ? -8.36617  -28.14649 -25.21758 1.000 19.12587 ? 470 ALA A N     1 
ATOM   3766 C  CA    . ALA A 1 470 ? -7.78318  -28.97948 -26.25159 1.000 13.82245 ? 470 ALA A CA    1 
ATOM   3767 C  C     . ALA A 1 470 ? -6.80420  -28.15948 -27.08261 1.000 14.89529 ? 470 ALA A C     1 
ATOM   3768 O  O     . ALA A 1 470 ? -6.91620  -26.93448 -27.15060 1.000 18.13826 ? 470 ALA A O     1 
ATOM   3769 C  CB    . ALA A 1 470 ? -8.88319  -29.55249 -27.13657 1.000 16.25246 ? 470 ALA A CB    1 
ATOM   3770 N  N     . PRO A 1 471 ? -5.82421  -28.80648 -27.71262 1.000 15.90428 ? 471 PRO A N     1 
ATOM   3771 C  CA    . PRO A 1 471 ? -4.85122  -28.05547 -28.51864 1.000 11.62802 ? 471 PRO A CA    1 
ATOM   3772 C  C     . PRO A 1 471 ? -5.53124  -27.32547 -29.66863 1.000 14.97872 ? 471 PRO A C     1 
ATOM   3773 O  O     . PRO A 1 471 ? -6.32625  -27.90248 -30.41161 1.000 21.13849 ? 471 PRO A O     1 
ATOM   3774 C  CB    . PRO A 1 471 ? -3.89323  -29.14147 -29.02065 1.000 18.33147 ? 471 PRO A CB    1 
ATOM   3775 C  CG    . PRO A 1 471 ? -4.68022  -30.40947 -28.94464 1.000 16.23211 ? 471 PRO A CG    1 
ATOM   3776 C  CD    . PRO A 1 471 ? -5.55020  -30.25347 -27.73363 1.000 20.39333 ? 471 PRO A CD    1 
ATOM   3777 N  N     . ILE A 1 472 ? -5.21525  -26.03447 -29.80563 1.000 18.41895 ? 472 ILE A N     1 
ATOM   3778 C  CA    . ILE A 1 472 ? -5.83327  -25.22747 -30.84962 1.000 16.16173 ? 472 ILE A CA    1 
ATOM   3779 C  C     . ILE A 1 472 ? -5.38729  -25.64547 -32.24363 1.000 13.75067 ? 472 ILE A C     1 
ATOM   3780 O  O     . ILE A 1 472 ? -6.08531  -25.35447 -33.22062 1.000 20.38037 ? 472 ILE A O     1 
ATOM   3781 C  CB    . ILE A 1 472 ? -5.53627  -23.73647 -30.62263 1.000 19.44115 ? 472 ILE A CB    1 
ATOM   3782 C  CG1   . ILE A 1 472 ? -4.07227  -23.55147 -30.22565 1.000 14.86578 ? 472 ILE A CG1   1 
ATOM   3783 C  CG2   . ILE A 1 472 ? -6.48026  -23.15648 -29.57161 1.000 22.89296 ? 472 ILE A CG2   1 
ATOM   3784 C  CD1   . ILE A 1 472 ? -3.55427  -22.15247 -30.44166 1.000 14.52563 ? 472 ILE A CD1   1 
ATOM   3785 N  N     . VAL A 1 473 ? -4.23429  -26.30347 -32.37165 1.000 15.02232 ? 473 VAL A N     1 
ATOM   3786 C  CA    . VAL A 1 473 ? -3.76831  -26.82047 -33.65166 1.000 18.56459 ? 473 VAL A CA    1 
ATOM   3787 C  C     . VAL A 1 473 ? -3.19930  -28.21746 -33.45167 1.000 21.99135 ? 473 VAL A C     1 
ATOM   3788 O  O     . VAL A 1 473 ? -2.82328  -28.61446 -32.34667 1.000 19.99998 ? 473 VAL A O     1 
ATOM   3789 C  CB    . VAL A 1 473 ? -2.69233  -25.92646 -34.32167 1.000 15.44399 ? 473 VAL A CB    1 
ATOM   3790 C  CG1   . VAL A 1 473 ? -3.24334  -24.54046 -34.65366 1.000 15.59883 ? 473 VAL A CG1   1 
ATOM   3791 C  CG2   . VAL A 1 473 ? -1.45531  -25.83246 -33.44169 1.000 15.26670 ? 473 VAL A CG2   1 
ATOM   3792 N  N     . ASP A 1 474 ? -3.14832  -28.96146 -34.55267 1.000 14.72785 ? 474 ASP A N     1 
ATOM   3793 C  CA    . ASP A 1 474 ? -2.32632  -30.15546 -34.65968 1.000 22.56892 ? 474 ASP A CA    1 
ATOM   3794 C  C     . ASP A 1 474 ? -0.93633  -29.71546 -35.10870 1.000 15.10628 ? 474 ASP A C     1 
ATOM   3795 O  O     . ASP A 1 474 ? -0.79835  -29.05246 -36.14171 1.000 16.98173 ? 474 ASP A O     1 
ATOM   3796 C  CB    . ASP A 1 474 ? -2.95433  -31.13746 -35.64967 1.000 21.90402 ? 474 ASP A CB    1 
ATOM   3797 C  CG    . ASP A 1 474 ? -2.18833  -32.44546 -35.76268 1.000 22.50139 ? 474 ASP A CG    1 
ATOM   3798 O  OD1   . ASP A 1 474 ? -0.94333  -32.43746 -35.69170 1.000 23.86560 ? 474 ASP A OD1   1 
ATOM   3799 O  OD2   . ASP A 1 474 ? -2.84133  -33.49346 -35.94267 1.000 27.19289 ? 474 ASP A OD2   1 
ATOM   3800 N  N     . HIS A 1 475 ? 0.08969   -30.08045 -34.33672 1.000 20.45409 ? 475 HIS A N     1 
ATOM   3801 C  CA    . HIS A 1 475 ? 1.43568   -29.58845 -34.62274 1.000 16.39745 ? 475 HIS A CA    1 
ATOM   3802 C  C     . HIS A 1 475 ? 1.97066   -30.12745 -35.94575 1.000 15.50599 ? 475 HIS A C     1 
ATOM   3803 O  O     . HIS A 1 475 ? 2.60765   -29.39044 -36.70576 1.000 21.04205 ? 475 HIS A O     1 
ATOM   3804 C  CB    . HIS A 1 475 ? 2.38770   -29.94245 -33.48276 1.000 13.37855 ? 475 HIS A CB    1 
ATOM   3805 C  CG    . HIS A 1 475 ? 3.76170   -29.37444 -33.65278 1.000 13.71526 ? 475 HIS A CG    1 
ATOM   3806 N  ND1   . HIS A 1 475 ? 3.98969   -28.03244 -33.86778 1.000 13.89326 ? 475 HIS A ND1   1 
ATOM   3807 C  CD2   . HIS A 1 475 ? 4.97870   -29.96644 -33.65380 1.000 13.76578 ? 475 HIS A CD2   1 
ATOM   3808 C  CE1   . HIS A 1 475 ? 5.28669   -27.82144 -33.99281 1.000 16.54601 ? 475 HIS A CE1   1 
ATOM   3809 N  NE2   . HIS A 1 475 ? 5.90869   -28.97943 -33.86782 1.000 19.43553 ? 475 HIS A NE2   1 
ATOM   3810 N  N     . ALA A 1 476 ? 1.74066   -31.41145 -36.23275 1.000 19.11757 ? 476 ALA A N     1 
ATOM   3811 C  CA    . ALA A 1 476 ? 2.21264   -31.98545 -37.49076 1.000 18.51872 ? 476 ALA A CA    1 
ATOM   3812 C  C     . ALA A 1 476 ? 1.61562   -31.25845 -38.68975 1.000 21.26459 ? 476 ALA A C     1 
ATOM   3813 O  O     . ALA A 1 476 ? 2.31160   -30.99244 -39.67576 1.000 23.54359 ? 476 ALA A O     1 
ATOM   3814 C  CB    . ALA A 1 476 ? 1.87165   -33.47345 -37.54375 1.000 18.68574 ? 476 ALA A CB    1 
ATOM   3815 N  N     . VAL A 1 477 ? 0.32862   -30.91845 -38.61372 1.000 21.26320 ? 477 VAL A N     1 
ATOM   3816 C  CA    . VAL A 1 477 ? -0.34640  -30.24345 -39.71771 1.000 17.12735 ? 477 VAL A CA    1 
ATOM   3817 C  C     . VAL A 1 477 ? 0.08359   -28.78545 -39.79972 1.000 19.68299 ? 477 VAL A C     1 
ATOM   3818 O  O     . VAL A 1 477 ? 0.39057   -28.26945 -40.88073 1.000 25.37420 ? 477 VAL A O     1 
ATOM   3819 C  CB    . VAL A 1 477 ? -1.87240  -30.37446 -39.56169 1.000 23.01852 ? 477 VAL A CB    1 
ATOM   3820 C  CG1   . VAL A 1 477 ? -2.59442  -29.36346 -40.44668 1.000 22.88950 ? 477 VAL A CG1   1 
ATOM   3821 C  CG2   . VAL A 1 477 ? -2.31840  -31.79446 -39.88468 0.810 24.05634 ? 477 VAL A CG2   1 
ATOM   3822 N  N     . ALA A 1 478 ? 0.11561   -28.10245 -38.65572 1.000 22.28199 ? 478 ALA A N     1 
ATOM   3823 C  CA    . ALA A 1 478 ? 0.41860   -26.67445 -38.64773 1.000 20.68635 ? 478 ALA A CA    1 
ATOM   3824 C  C     . ALA A 1 478 ? 1.87760   -26.40445 -39.00075 1.000 22.68294 ? 478 ALA A C     1 
ATOM   3825 O  O     . ALA A 1 478 ? 2.17058   -25.48344 -39.77475 1.000 20.13710 ? 478 ALA A O     1 
ATOM   3826 C  CB    . ALA A 1 478 ? 0.07762   -26.07745 -37.28272 1.000 15.38492 ? 478 ALA A CB    1 
ATOM   3827 N  N     . SER A 1 479 ? 2.80561   -27.18644 -38.44476 1.000 16.56374 ? 479 SER A N     1 
ATOM   3828 C  CA    . SER A 1 479 ? 4.21960   -26.95244 -38.72679 1.000 18.37605 ? 479 SER A CA    1 
ATOM   3829 C  C     . SER A 1 479 ? 4.55458   -27.24744 -40.18379 1.000 20.12533 ? 479 SER A C     1 
ATOM   3830 O  O     . SER A 1 479 ? 5.37257   -26.54743 -40.78781 1.000 14.63726 ? 479 SER A O     1 
ATOM   3831 C  CB    . SER A 1 479 ? 5.09562   -27.78944 -37.79280 1.000 19.01666 ? 479 SER A CB    1 
ATOM   3832 O  OG    . SER A 1 479 ? 4.87162   -29.17444 -37.99080 1.000 23.60029 ? 479 SER A OG    1 
ATOM   3833 N  N     . LYS A 1 480 ? 3.93157   -28.27644 -40.76678 1.000 20.81821 ? 480 LYS A N     1 
ATOM   3834 C  CA    . LYS A 1 480 ? 4.13855   -28.54544 -42.18679 1.000 25.77880 ? 480 LYS A CA    1 
ATOM   3835 C  C     . LYS A 1 480 ? 3.69653   -27.35844 -43.03778 1.000 25.83252 ? 480 LYS A C     1 
ATOM   3836 O  O     . LYS A 1 480 ? 4.39352   -26.96644 -43.98079 1.000 19.74417 ? 480 LYS A O     1 
ATOM   3837 C  CB    . LYS A 1 480 ? 3.38755   -29.81144 -42.59678 1.000 22.18326 ? 480 LYS A CB    1 
ATOM   3838 C  CG    . LYS A 1 480 ? 3.71053   -30.32644 -43.98878 1.000 20.72023 ? 480 LYS A CG    1 
ATOM   3839 C  CD    . LYS A 1 480 ? 5.00653   -31.11543 -44.00180 0.000 22.24536 ? 480 LYS A CD    1 
ATOM   3840 C  CE    . LYS A 1 480 ? 5.12251   -31.94943 -45.26580 0.000 22.43916 ? 480 LYS A CE    1 
ATOM   3841 N  NZ    . LYS A 1 480 ? 6.17852   -32.99143 -45.15082 0.000 23.11928 ? 480 LYS A NZ    1 
ATOM   3842 N  N     . ALA A 1 481 ? 2.54954   -26.75944 -42.70276 1.000 27.74342 ? 481 ALA A N     1 
ATOM   3843 C  CA    . ALA A 1 481 ? 2.04452   -25.63044 -43.47575 1.000 23.10361 ? 481 ALA A CA    1 
ATOM   3844 C  C     . ALA A 1 481 ? 2.93752   -24.40844 -43.32077 1.000 19.80018 ? 481 ALA A C     1 
ATOM   3845 O  O     . ALA A 1 481 ? 3.17550   -23.68044 -44.29077 1.000 23.14386 ? 481 ALA A O     1 
ATOM   3846 C  CB    . ALA A 1 481 ? 0.61153   -25.30345 -43.05673 1.000 20.71954 ? 481 ALA A CB    1 
ATOM   3847 N  N     . CYS A 1 482 ? 3.44554   -24.17044 -42.10977 1.000 22.20871 ? 482 CYS A N     1 
ATOM   3848 C  CA    . CYS A 1 482 ? 4.28454   -22.99944 -41.87779 1.000 18.63754 ? 482 CYS A CA    1 
ATOM   3849 C  C     . CYS A 1 482 ? 5.62453   -23.13243 -42.58481 1.000 18.22564 ? 482 CYS A C     1 
ATOM   3850 O  O     . CYS A 1 482 ? 6.14251   -22.15543 -43.13482 1.000 20.86072 ? 482 CYS A O     1 
ATOM   3851 C  CB    . CYS A 1 482 ? 4.49456   -22.78644 -40.37879 1.000 18.37002 ? 482 CYS A CB    1 
ATOM   3852 S  SG    . CYS A 1 482 ? 2.99558   -22.40344 -39.43777 1.000 17.69857 ? 482 CYS A SG    1 
ATOM   3853 N  N     . ILE A 1 483 ? 6.20553   -24.33243 -42.57082 1.000 19.74430 ? 483 ILE A N     1 
ATOM   3854 C  CA    . ILE A 1 483 ? 7.47452   -24.55243 -43.25584 1.000 19.36154 ? 483 ILE A CA    1 
ATOM   3855 C  C     . ILE A 1 483 ? 7.31749   -24.31243 -44.75184 1.000 21.86001 ? 483 ILE A C     1 
ATOM   3856 O  O     . ILE A 1 483 ? 8.16048   -23.66342 -45.38285 1.000 23.74955 ? 483 ILE A O     1 
ATOM   3857 C  CB    . ILE A 1 483 ? 8.00253   -25.96842 -42.95485 1.000 18.92691 ? 483 ILE A CB    1 
ATOM   3858 C  CG1   . ILE A 1 483 ? 8.39256   -26.08542 -41.48086 1.000 19.83967 ? 483 ILE A CG1   1 
ATOM   3859 C  CG2   . ILE A 1 483 ? 9.18852   -26.30642 -43.84187 1.000 19.80286 ? 483 ILE A CG2   1 
ATOM   3860 C  CD1   . ILE A 1 483 ? 8.79057   -27.48442 -41.06786 1.000 20.75727 ? 483 ILE A CD1   1 
ATOM   3861 N  N     . ALA A 1 484 ? 6.22149   -24.80543 -45.33482 1.000 20.63163 ? 484 ALA A N     1 
ATOM   3862 C  CA    . ALA A 1 484 ? 5.99646   -24.64343 -46.76482 1.000 21.19273 ? 484 ALA A CA    1 
ATOM   3863 C  C     . ALA A 1 484 ? 5.73745   -23.18943 -47.13481 1.000 26.20314 ? 484 ALA A C     1 
ATOM   3864 O  O     . ALA A 1 484 ? 6.06443   -22.76643 -48.25082 1.000 29.36114 ? 484 ALA A O     1 
ATOM   3865 C  CB    . ALA A 1 484 ? 4.82746   -25.51743 -47.20880 1.000 25.92750 ? 484 ALA A CB    1 
ATOM   3866 N  N     . ARG A 1 485 ? 5.14859   -22.41328 -46.22356 1.000 25.49407 ? 485 ARG A N     1 
ATOM   3867 C  CA    . ARG A 1 485 ? 4.92543   -20.99770 -46.49051 1.000 24.53270 ? 485 ARG A CA    1 
ATOM   3868 C  C     . ARG A 1 485 ? 6.17849   -20.16961 -46.24251 1.000 21.64249 ? 485 ARG A C     1 
ATOM   3869 O  O     . ARG A 1 485 ? 6.40247   -19.17212 -46.93684 1.000 21.97718 ? 485 ARG A O     1 
ATOM   3870 C  CB    . ARG A 1 485 ? 3.76765   -20.47866 -45.63836 1.000 21.02303 ? 485 ARG A CB    1 
ATOM   3871 C  CG    . ARG A 1 485 ? 2.42691   -21.10698 -45.98243 1.000 18.94205 ? 485 ARG A CG    1 
ATOM   3872 C  CD    . ARG A 1 485 ? 1.34153   -20.66321 -45.01506 1.000 19.59202 ? 485 ARG A CD    1 
ATOM   3873 N  NE    . ARG A 1 485 ? 1.09321   -19.22818 -45.08602 1.000 22.34331 ? 485 ARG A NE    1 
ATOM   3874 C  CZ    . ARG A 1 485 ? 0.20750   -18.58520 -44.33749 1.000 27.27831 ? 485 ARG A CZ    1 
ATOM   3875 N  NH1   . ARG A 1 485 ? -0.52643  -19.21949 -43.43786 1.000 24.90954 ? 485 ARG A NH1   1 
ATOM   3876 N  NH2   . ARG A 1 485 ? 0.05428   -17.27299 -44.49559 1.000 23.23145 ? 485 ARG A NH2   1 
ATOM   3877 N  N     . MET A 1 486 ? 6.99747   -20.55943 -45.26283 1.000 18.60825 ? 486 MET A N     1 
ATOM   3878 C  CA    . MET A 1 486 ? 8.27847   -19.89142 -45.06185 1.000 20.10932 ? 486 MET A CA    1 
ATOM   3879 C  C     . MET A 1 486 ? 9.20946   -20.12542 -46.24387 1.000 22.69664 ? 486 MET A C     1 
ATOM   3880 O  O     . MET A 1 486 ? 9.93445   -19.21442 -46.66088 1.000 23.77530 ? 486 MET A O     1 
ATOM   3881 C  CB    . MET A 1 486 ? 8.93050   -20.37542 -43.76786 1.000 17.74901 ? 486 MET A CB    1 
ATOM   3882 C  CG    . MET A 1 486 ? 8.23652   -19.90342 -42.49885 1.000 19.94229 ? 486 MET A CG    1 
ATOM   3883 S  SD    . MET A 1 486 ? 8.26951   -18.11542 -42.29985 1.000 23.32816 ? 486 MET A SD    1 
ATOM   3884 C  CE    . MET A 1 486 ? 10.02952  -17.82642 -42.15188 1.000 17.37662 ? 486 MET A CE    1 
ATOM   3885 N  N     . ALA A 1 487 ? 9.20145   -21.34142 -46.79587 1.000 24.75868 ? 487 ALA A N     1 
ATOM   3886 C  CA    . ALA A 1 487 ? 10.05043  -21.64842 -47.94288 1.000 26.94394 ? 487 ALA A CA    1 
ATOM   3887 C  C     . ALA A 1 487 ? 9.65041   -20.82942 -49.15988 1.000 32.63262 ? 487 ALA A C     1 
ATOM   3888 O  O     . ALA A 1 487 ? 10.51040  -20.40141 -49.93889 1.000 34.78683 ? 487 ALA A O     1 
ATOM   3889 C  CB    . ALA A 1 487 ? 9.98743   -23.14142 -48.26088 1.000 19.03184 ? 487 ALA A CB    1 
ATOM   3890 N  N     . ALA A 1 488 ? 8.34941   -20.60542 -49.34585 1.000 32.93345 ? 488 ALA A N     1 
ATOM   3891 C  CA    . ALA A 1 488 ? 7.90938   -19.77742 -50.46085 1.000 35.03536 ? 488 ALA A CA    1 
ATOM   3892 C  C     . ALA A 1 488 ? 8.29438   -18.32142 -50.24085 1.000 33.32169 ? 488 ALA A C     1 
ATOM   3893 O  O     . ALA A 1 488 ? 8.65936   -17.62142 -51.19086 1.000 33.85981 ? 488 ALA A O     1 
ATOM   3894 C  CB    . ALA A 1 488 ? 6.40038   -19.91343 -50.65882 1.000 35.68390 ? 488 ALA A CB    1 
ATOM   3895 N  N     . ALA A 1 489 ? 8.23640   -17.85442 -48.99185 1.000 27.04374 ? 489 ALA A N     1 
ATOM   3896 C  CA    . ALA A 1 489 ? 8.62840   -16.47842 -48.70286 1.000 32.37862 ? 489 ALA A CA    1 
ATOM   3897 C  C     . ALA A 1 489 ? 10.11440  -16.25541 -48.95888 1.000 29.38266 ? 489 ALA A C     1 
ATOM   3898 O  O     . ALA A 1 489 ? 10.50739  -15.20041 -49.46989 1.000 33.66080 ? 489 ALA A O     1 
ATOM   3899 C  CB    . ALA A 1 489 ? 8.27442   -16.11842 -47.26185 1.000 24.82940 ? 489 ALA A CB    1 
ATOM   3900 N  N     . TYR A 1 490 ? 10.95441  -17.23841 -48.62190 1.000 30.86649 ? 490 TYR A N     1 
ATOM   3901 C  CA    . TYR A 1 490 ? 12.39540  -17.08441 -48.80292 1.000 28.17194 ? 490 TYR A CA    1 
ATOM   3902 C  C     . TYR A 1 490 ? 12.81938  -17.11340 -50.26393 1.000 33.03263 ? 490 TYR A C     1 
ATOM   3903 O  O     . TYR A 1 490 ? 13.90037  -16.61040 -50.58595 1.000 36.51426 ? 490 TYR A O     1 
ATOM   3904 C  CB    . TYR A 1 490 ? 13.14942  -18.16340 -48.02593 1.000 24.05205 ? 490 TYR A CB    1 
ATOM   3905 C  CG    . TYR A 1 490 ? 13.65444  -17.67340 -46.69694 1.000 22.54356 ? 490 TYR A CG    1 
ATOM   3906 C  CD1   . TYR A 1 490 ? 12.82246  -17.64241 -45.59293 1.000 20.27128 ? 490 TYR A CD1   1 
ATOM   3907 C  CD2   . TYR A 1 490 ? 14.95944  -17.21740 -46.55096 1.000 23.10494 ? 490 TYR A CD2   1 
ATOM   3908 C  CE1   . TYR A 1 490 ? 13.27248  -17.18541 -44.37794 1.000 21.08827 ? 490 TYR A CE1   1 
ATOM   3909 C  CE2   . TYR A 1 490 ? 15.42146  -16.75940 -45.33997 1.000 18.31201 ? 490 TYR A CE2   1 
ATOM   3910 C  CZ    . TYR A 1 490 ? 14.57048  -16.74540 -44.25496 1.000 23.36800 ? 490 TYR A CZ    1 
ATOM   3911 O  OH    . TYR A 1 490 ? 15.01050  -16.29240 -43.03696 1.000 20.88354 ? 490 TYR A OH    1 
ATOM   3912 N  N     . ARG A 1 491 ? 11.99702  -17.67404 -51.15321 1.000 37.52068 ? 491 ARG A N     1 
ATOM   3913 C  CA    . ARG A 1 491 ? 12.33258  -17.71777 -52.57012 1.000 40.95647 ? 491 ARG A CA    1 
ATOM   3914 C  C     . ARG A 1 491 ? 11.72421  -16.57470 -53.37010 1.000 36.00551 ? 491 ARG A C     1 
ATOM   3915 O  O     . ARG A 1 491 ? 12.21640  -16.28154 -54.46501 1.000 43.24390 ? 491 ARG A O     1 
ATOM   3916 C  CB    . ARG A 1 491 ? 11.89591  -19.05234 -53.19120 1.000 42.62261 ? 491 ARG A CB    1 
ATOM   3917 C  CG    . ARG A 1 491 ? 10.47047  -19.07306 -53.71701 1.000 47.97557 ? 491 ARG A CG    1 
ATOM   3918 C  CD    . ARG A 1 491 ? 10.22436  -20.29305 -54.59477 1.000 44.96400 ? 491 ARG A CD    1 
ATOM   3919 N  NE    . ARG A 1 491 ? 10.28450  -21.53635 -53.83661 1.000 44.48620 ? 491 ARG A NE    1 
ATOM   3920 C  CZ    . ARG A 1 491 ? 9.22645   -22.15783 -53.33440 1.000 50.27401 ? 491 ARG A CZ    1 
ATOM   3921 N  NH1   . ARG A 1 491 ? 8.00219   -21.68534 -53.50406 1.000 40.89900 ? 491 ARG A NH1   1 
ATOM   3922 N  NH2   . ARG A 1 491 ? 9.40086   -23.28208 -52.64540 1.000 55.15640 ? 491 ARG A NH2   1 
ATOM   3923 N  N     . ARG A 1 492 ? 10.67583  -15.92647 -52.86306 1.000 29.69891 ? 492 ARG A N     1 
ATOM   3924 C  CA    . ARG A 1 492 ? 10.11183  -14.75044 -53.52622 1.000 35.79857 ? 492 ARG A CA    1 
ATOM   3925 C  C     . ARG A 1 492 ? 10.76429  -13.46485 -53.04258 1.000 42.96008 ? 492 ARG A C     1 
ATOM   3926 O  O     . ARG A 1 492 ? 10.09554  -12.45491 -52.79988 1.000 36.28135 ? 492 ARG A O     1 
ATOM   3927 C  CB    . ARG A 1 492 ? 8.59628   -14.70722 -53.33735 1.000 34.76116 ? 492 ARG A CB    1 
ATOM   3928 C  CG    . ARG A 1 492 ? 8.10374   -14.66691 -51.89654 1.000 31.36885 ? 492 ARG A CG    1 
ATOM   3929 C  CD    . ARG A 1 492 ? 6.57860   -14.69629 -51.84596 1.000 29.89623 ? 492 ARG A CD    1 
ATOM   3930 N  NE    . ARG A 1 492 ? 6.06146   -14.56267 -50.48901 1.000 27.49871 ? 492 ARG A NE    1 
ATOM   3931 N  N     . SER A 1 493 ? 12.08532  -13.48641 -52.90191 1.000 40.09399 ? 493 SER A N     1 
ATOM   3932 C  CA    . SER A 1 493 ? 12.84633  -12.33340 -52.44393 1.000 39.34888 ? 493 SER A CA    1 
ATOM   3933 C  C     . SER A 1 493 ? 13.74031  -11.80140 -53.55894 1.000 45.67692 ? 493 SER A C     1 
ATOM   3934 O  O     . SER A 1 493 ? 14.51331  -10.86640 -53.35495 1.000 42.43464 ? 493 SER A O     1 
ATOM   3935 C  CB    . SER A 1 493 ? 13.69035  -12.70340 -51.22594 1.000 38.07535 ? 493 SER A CB    1 
ATOM   3936 O  OG    . SER A 1 493 ? 13.02536  -13.67340 -50.43593 1.000 40.04145 ? 493 SER A OG    1 
HETATM 3937 P  PA    . FAD B 2 .   ? 22.37588  -14.98038 -19.43209 1.000 5.18575  ? 601 FAD A PA    1 
HETATM 3938 O  O1A   . FAD B 2 .   ? 22.89291  -14.98438 -18.04809 1.000 4.66547  ? 601 FAD A O1A   1 
HETATM 3939 O  O2A   . FAD B 2 .   ? 22.43488  -16.25238 -20.17509 1.000 7.46373  ? 601 FAD A O2A   1 
HETATM 3940 O  O5B   . FAD B 2 .   ? 23.10287  -13.84538 -20.28110 1.000 5.19659  ? 601 FAD A O5B   1 
HETATM 3941 C  C5B   . FAD B 2 .   ? 23.59587  -12.71738 -19.55811 1.000 7.85632  ? 601 FAD A C5B   1 
HETATM 3942 C  C4B   . FAD B 2 .   ? 23.14086  -11.44738 -20.23010 1.000 2.33916  ? 601 FAD A C4B   1 
HETATM 3943 O  O4B   . FAD B 2 .   ? 23.47184  -11.49638 -21.63310 1.000 3.42101  ? 601 FAD A O4B   1 
HETATM 3944 C  C3B   . FAD B 2 .   ? 21.63586  -11.17638 -20.18807 1.000 7.33196  ? 601 FAD A C3B   1 
HETATM 3945 O  O3B   . FAD B 2 .   ? 21.29488  -10.54239 -18.96807 1.000 4.70338  ? 601 FAD A O3B   1 
HETATM 3946 C  C2B   . FAD B 2 .   ? 21.44783  -10.26738 -21.40907 1.000 3.64679  ? 601 FAD A C2B   1 
HETATM 3947 O  O2B   . FAD B 2 .   ? 21.77783  -8.92438  -21.14407 1.000 4.01320  ? 601 FAD A O2B   1 
HETATM 3948 C  C1B   . FAD B 2 .   ? 22.45882  -10.85638 -22.39809 1.000 4.25648  ? 601 FAD A C1B   1 
HETATM 3949 N  N9A   . FAD B 2 .   ? 21.87181  -11.82038 -23.32508 1.000 7.09768  ? 601 FAD A N9A   1 
HETATM 3950 C  C8A   . FAD B 2 .   ? 21.68982  -13.16338 -23.14107 1.000 6.35455  ? 601 FAD A C8A   1 
HETATM 3951 N  N7A   . FAD B 2 .   ? 21.12080  -13.76039 -24.15807 1.000 7.54309  ? 601 FAD A N7A   1 
HETATM 3952 C  C5A   . FAD B 2 .   ? 20.91878  -12.74239 -25.07506 1.000 5.26763  ? 601 FAD A C5A   1 
HETATM 3953 C  C6A   . FAD B 2 .   ? 20.35476  -12.73439 -26.36305 1.000 7.54942  ? 601 FAD A C6A   1 
HETATM 3954 N  N6A   . FAD B 2 .   ? 19.86375  -13.81539 -26.96304 1.000 11.38736 ? 601 FAD A N6A   1 
HETATM 3955 N  N1A   . FAD B 2 .   ? 20.29575  -11.54739 -27.01005 1.000 6.05220  ? 601 FAD A N1A   1 
HETATM 3956 C  C2A   . FAD B 2 .   ? 20.79475  -10.46639 -26.40206 1.000 3.47921  ? 601 FAD A C2A   1 
HETATM 3957 N  N3A   . FAD B 2 .   ? 21.34377  -10.35638 -25.20207 1.000 5.60245  ? 601 FAD A N3A   1 
HETATM 3958 C  C4A   . FAD B 2 .   ? 21.37879  -11.54238 -24.57507 1.000 5.84458  ? 601 FAD A C4A   1 
HETATM 3959 N  N1    . FAD B 2 .   ? 16.79000  -10.28400 -23.45500 1.000 4.00971  ? 601 FAD A N1    1 
HETATM 3960 C  C2    . FAD B 2 .   ? 16.57900  -9.14600  -22.77500 1.000 6.59505  ? 601 FAD A C2    1 
HETATM 3961 O  O2    . FAD B 2 .   ? 17.37700  -8.75700  -21.93800 1.000 6.03470  ? 601 FAD A O2    1 
HETATM 3962 N  N3    . FAD B 2 .   ? 15.49400  -8.36800  -23.00300 1.000 3.11515  ? 601 FAD A N3    1 
HETATM 3963 C  C4    . FAD B 2 .   ? 14.51300  -8.71100  -23.89200 1.000 5.89097  ? 601 FAD A C4    1 
HETATM 3964 O  O4    . FAD B 2 .   ? 13.56800  -7.93300  -24.07700 1.000 6.44508  ? 601 FAD A O4    1 
HETATM 3965 C  C4X   . FAD B 2 .   ? 14.64100  -9.98200  -24.54400 1.000 4.06114  ? 601 FAD A C4X   1 
HETATM 3966 N  N5    . FAD B 2 .   ? 13.67400  -10.40000 -25.33500 1.000 3.66917  ? 601 FAD A N5    1 
HETATM 3967 C  C5X   . FAD B 2 .   ? 13.82400  -11.62900 -25.92900 1.000 4.94910  ? 601 FAD A C5X   1 
HETATM 3968 C  C6    . FAD B 2 .   ? 12.81200  -12.09500 -26.79500 1.000 5.00932  ? 601 FAD A C6    1 
HETATM 3969 C  C7    . FAD B 2 .   ? 12.88100  -13.34300 -27.38000 1.000 7.28712  ? 601 FAD A C7    1 
HETATM 3970 C  C7M   . FAD B 2 .   ? 11.77700  -13.79400 -28.29700 1.000 6.43161  ? 601 FAD A C7M   1 
HETATM 3971 C  C8    . FAD B 2 .   ? 13.98900  -14.19400 -27.08600 1.000 5.86970  ? 601 FAD A C8    1 
HETATM 3972 C  C8M   . FAD B 2 .   ? 14.11500  -15.55700 -27.71100 1.000 5.40265  ? 601 FAD A C8M   1 
HETATM 3973 C  C9    . FAD B 2 .   ? 15.02000  -13.71300 -26.31000 1.000 3.99104  ? 601 FAD A C9    1 
HETATM 3974 C  C9A   . FAD B 2 .   ? 14.96400  -12.44100 -25.70500 1.000 4.62202  ? 601 FAD A C9A   1 
HETATM 3975 N  N10   . FAD B 2 .   ? 15.98600  -11.93200 -24.90500 1.000 5.99473  ? 601 FAD A N10   1 
HETATM 3976 C  C10   . FAD B 2 .   ? 15.83700  -10.71700 -24.25700 1.000 4.75318  ? 601 FAD A C10   1 
HETATM 3977 C  "C1'" . FAD B 2 .   ? 17.22979  -12.75240 -24.64500 1.000 4.62252  ? 601 FAD A "C1'" 1 
HETATM 3978 C  "C2'" . FAD B 2 .   ? 17.24681  -13.81740 -23.57800 1.000 3.91022  ? 601 FAD A "C2'" 1 
HETATM 3979 O  "O2'" . FAD B 2 .   ? 16.01781  -14.53040 -23.55698 1.000 6.40377  ? 601 FAD A "O2'" 1 
HETATM 3980 C  "C3'" . FAD B 2 .   ? 17.55983  -13.15240 -22.23701 1.000 4.65107  ? 601 FAD A "C3'" 1 
HETATM 3981 O  "O3'" . FAD B 2 .   ? 18.53282  -12.12739 -22.41602 1.000 4.58456  ? 601 FAD A "O3'" 1 
HETATM 3982 C  "C4'" . FAD B 2 .   ? 18.07885  -14.14640 -21.20901 1.000 4.72393  ? 601 FAD A "C4'" 1 
HETATM 3983 O  "O4'" . FAD B 2 .   ? 17.29685  -15.32940 -21.30300 1.000 5.60274  ? 601 FAD A "O4'" 1 
HETATM 3984 C  "C5'" . FAD B 2 .   ? 18.00487  -13.55640 -19.81901 1.000 3.00897  ? 601 FAD A "C5'" 1 
HETATM 3985 O  "O5'" . FAD B 2 .   ? 18.46589  -14.51140 -18.87202 1.000 2.74085  ? 601 FAD A "O5'" 1 
HETATM 3986 P  P     . FAD B 2 .   ? 19.87690  -14.27039 -18.19304 1.000 3.47390  ? 601 FAD A P     1 
HETATM 3987 O  O1P   . FAD B 2 .   ? 19.98390  -12.86139 -17.75305 1.000 4.35374  ? 601 FAD A O1P   1 
HETATM 3988 O  O2P   . FAD B 2 .   ? 20.05992  -15.32039 -17.17405 1.000 3.98362  ? 601 FAD A O2P   1 
HETATM 3989 O  O3P   . FAD B 2 .   ? 20.87688  -14.47439 -19.39506 1.000 4.80995  ? 601 FAD A O3P   1 
HETATM 3990 CL CL    . CL  C 3 .   ? 12.38975  -30.34041 -30.76793 1.000 22.93101 ? 602 CL  A CL    1 
HETATM 3991 O  O     . HOH D 4 .   ? 20.40775  2.81761   -24.11805 1.000 19.01965 ? 701 HOH A O     1 
HETATM 3992 O  O     . HOH D 4 .   ? 5.05255   -2.15944  -36.92479 1.000 35.85158 ? 702 HOH A O     1 
HETATM 3993 O  O     . HOH D 4 .   ? 20.76965  14.53861  -27.47505 1.000 27.33029 ? 703 HOH A O     1 
HETATM 3994 O  O     . HOH D 4 .   ? 16.50152  -14.38540 -41.47799 1.000 26.41327 ? 704 HOH A O     1 
HETATM 3995 O  O     . HOH D 4 .   ? 19.20315  -10.61340 -2.79203  1.000 31.52246 ? 705 HOH A O     1 
HETATM 3996 O  O     . HOH D 4 .   ? 24.27513  -6.25938  -3.08212  1.000 21.40897 ? 706 HOH A O     1 
HETATM 3997 O  O     . HOH D 4 .   ? 20.05669  9.86061   -25.95604 1.000 16.72283 ? 707 HOH A O     1 
HETATM 3998 O  O     . HOH D 4 .   ? -4.52935  -33.54047 -37.54465 1.000 28.92868 ? 708 HOH A O     1 
HETATM 3999 O  O     . HOH D 4 .   ? 28.18606  -19.93837 -9.73018  1.000 23.80331 ? 709 HOH A O     1 
HETATM 4000 O  O     . HOH D 4 .   ? 17.14678  6.61960   -21.39599 1.000 13.94512 ? 710 HOH A O     1 
HETATM 4001 O  O     . HOH D 4 .   ? 28.87885  -0.50236  -18.60719 1.000 18.76215 ? 711 HOH A O     1 
HETATM 4002 O  O     . HOH D 4 .   ? 10.84791  27.27658  -9.01888  1.000 19.64453 ? 712 HOH A O     1 
HETATM 4003 O  O     . HOH D 4 .   ? 32.55000  1.44165   -9.35825  1.000 16.72624 ? 713 HOH A O     1 
HETATM 4004 O  O     . HOH D 4 .   ? 23.39404  15.05562  -3.99909  1.000 19.84349 ? 714 HOH A O     1 
HETATM 4005 O  O     . HOH D 4 .   ? 6.34095   -37.15144 -19.72283 1.000 24.85048 ? 715 HOH A O     1 
HETATM 4006 O  O     . HOH D 4 .   ? 10.42510  12.54257  -0.53888  1.000 26.75517 ? 716 HOH A O     1 
HETATM 4007 O  O     . HOH D 4 .   ? 25.18849  -2.93637  -40.79013 1.000 25.98509 ? 717 HOH A O     1 
HETATM 4008 O  O     . HOH D 4 .   ? 20.80093  -28.39439 -19.41706 1.000 20.55730 ? 718 HOH A O     1 
HETATM 4009 O  O     . HOH D 4 .   ? 19.82303  -24.43239 -12.35905 1.000 15.95524 ? 719 HOH A O     1 
HETATM 4010 O  O     . HOH D 4 .   ? 17.18608  -17.15640 -8.25300  1.000 25.37820 ? 720 HOH A O     1 
HETATM 4011 O  O     . HOH D 4 .   ? 16.64257  1.74460   -34.80799 1.000 23.30758 ? 721 HOH A O     1 
HETATM 4012 O  O     . HOH D 4 .   ? 11.24403  -34.44342 -14.87791 1.000 20.98794 ? 722 HOH A O     1 
HETATM 4013 O  O     . HOH D 4 .   ? 15.18001  -32.29041 -15.17897 1.000 26.88154 ? 723 HOH A O     1 
HETATM 4014 O  O     . HOH D 4 .   ? 8.36511   -3.61344  -3.56485  1.000 22.87288 ? 724 HOH A O     1 
HETATM 4015 O  O     . HOH D 4 .   ? 15.05269  27.77259  -22.60695 1.000 26.82254 ? 725 HOH A O     1 
HETATM 4016 O  O     . HOH D 4 .   ? 27.23414  15.00263  2.25084   1.000 21.18921 ? 726 HOH A O     1 
HETATM 4017 O  O     . HOH D 4 .   ? 7.57084   24.35257  -14.01183 1.000 32.25258 ? 727 HOH A O     1 
HETATM 4018 O  O     . HOH D 4 .   ? 12.59807  22.29558  -0.36091  1.000 23.80434 ? 728 HOH A O     1 
HETATM 4019 O  O     . HOH D 4 .   ? 25.53061  3.77463   -31.89813 1.000 21.43570 ? 729 HOH A O     1 
HETATM 4020 O  O     . HOH D 4 .   ? 31.27311  -13.99636 -5.67723  1.000 22.33287 ? 730 HOH A O     1 
HETATM 4021 O  O     . HOH D 4 .   ? 11.80502  -28.18742 -13.78191 1.000 20.90888 ? 731 HOH A O     1 
HETATM 4022 O  O     . HOH D 4 .   ? 21.77407  1.95261   -4.91007  1.000 14.13988 ? 732 HOH A O     1 
HETATM 4023 O  O     . HOH D 4 .   ? 14.18660  0.89359   -32.94495 1.000 21.80368 ? 733 HOH A O     1 
HETATM 4024 O  O     . HOH D 4 .   ? 31.85289  -18.66935 -19.69924 1.000 12.47286 ? 734 HOH A O     1 
HETATM 4025 O  O     . HOH D 4 .   ? 5.20682   18.63656  -16.66679 1.000 25.66298 ? 735 HOH A O     1 
HETATM 4026 O  O     . HOH D 4 .   ? 19.62510  -10.84640 -5.36304  1.000 24.11297 ? 736 HOH A O     1 
HETATM 4027 O  O     . HOH D 4 .   ? 17.85774  -24.13039 -29.92901 1.000 26.22525 ? 737 HOH A O     1 
HETATM 4028 O  O     . HOH D 4 .   ? 23.27798  -23.68438 -15.67610 1.000 11.50701 ? 738 HOH A O     1 
HETATM 4029 O  O     . HOH D 4 .   ? -0.65705  -21.78246 -16.85971 1.000 28.54805 ? 739 HOH A O     1 
HETATM 4030 O  O     . HOH D 4 .   ? 18.17588  -17.46340 -20.23802 1.000 4.32164  ? 740 HOH A O     1 
HETATM 4031 O  O     . HOH D 4 .   ? 39.92262  -9.74332  -34.44038 1.000 22.04031 ? 741 HOH A O     1 
HETATM 4032 O  O     . HOH D 4 .   ? 33.25297  12.88865  -8.25926  1.000 18.56593 ? 742 HOH A O     1 
HETATM 4033 O  O     . HOH D 4 .   ? 43.03589  -17.62831 -19.45243 1.000 14.15525 ? 743 HOH A O     1 
HETATM 4034 O  O     . HOH D 4 .   ? 10.20504  -6.85143  -8.31688  1.000 17.29437 ? 744 HOH A O     1 
HETATM 4035 O  O     . HOH D 4 .   ? 19.73286  -26.79539 -23.35805 1.000 14.35400 ? 745 HOH A O     1 
HETATM 4036 O  O     . HOH D 4 .   ? 17.47271  -15.76340 -30.14301 1.000 9.78522  ? 746 HOH A O     1 
HETATM 4037 O  O     . HOH D 4 .   ? -0.38343  -10.77945 -37.45271 1.000 17.97952 ? 747 HOH A O     1 
HETATM 4038 O  O     . HOH D 4 .   ? 1.37599   -11.31146 -12.45174 1.000 17.89325 ? 748 HOH A O     1 
HETATM 4039 O  O     . HOH D 4 .   ? 6.06007   12.24256  -2.79781  1.000 22.16587 ? 749 HOH A O     1 
HETATM 4040 O  O     . HOH D 4 .   ? 21.59297  24.82461  -5.95606  1.000 10.35934 ? 750 HOH A O     1 
HETATM 4041 O  O     . HOH D 4 .   ? 9.44157   -22.17642 -39.61587 1.000 19.82880 ? 751 HOH A O     1 
HETATM 4042 O  O     . HOH D 4 .   ? 34.60998  -24.95934 -15.68229 1.000 25.10899 ? 752 HOH A O     1 
HETATM 4043 O  O     . HOH D 4 .   ? 32.08561  7.57065   -31.04924 1.000 15.18381 ? 753 HOH A O     1 
HETATM 4044 O  O     . HOH D 4 .   ? 20.94556  -24.53238 -41.10607 1.000 34.48294 ? 754 HOH A O     1 
HETATM 4045 O  O     . HOH D 4 .   ? 21.46180  5.13261   -20.30906 1.000 5.56761  ? 755 HOH A O     1 
HETATM 4046 O  O     . HOH D 4 .   ? 37.11886  3.50567   -17.33533 1.000 18.23024 ? 756 HOH A O     1 
HETATM 4047 O  O     . HOH D 4 .   ? 4.92642   -13.74543 -47.26780 1.000 29.82594 ? 757 HOH A O     1 
HETATM 4048 O  O     . HOH D 4 .   ? 14.47477  -0.65541  -23.49195 1.000 15.12868 ? 758 HOH A O     1 
HETATM 4049 O  O     . HOH D 4 .   ? -0.13447  -28.84545 -43.36172 1.000 28.40207 ? 759 HOH A O     1 
HETATM 4050 O  O     . HOH D 4 .   ? 15.69394  29.56859  -6.69396  1.000 19.17454 ? 760 HOH A O     1 
HETATM 4051 O  O     . HOH D 4 .   ? 22.24402  -21.17039 -12.22009 1.000 16.60147 ? 761 HOH A O     1 
HETATM 4052 O  O     . HOH D 4 .   ? 18.54401  -28.74240 -14.63403 1.000 28.71826 ? 762 HOH A O     1 
HETATM 4053 O  O     . HOH D 4 .   ? 34.55576  -7.41834  -25.12329 1.000 11.84104 ? 763 HOH A O     1 
HETATM 4054 O  O     . HOH D 4 .   ? 24.99715  -12.63738 -2.92113  1.000 19.60990 ? 764 HOH A O     1 
HETATM 4055 O  O     . HOH D 4 .   ? 37.88678  -8.15733  -24.23434 1.000 17.22584 ? 765 HOH A O     1 
HETATM 4056 O  O     . HOH D 4 .   ? 0.47053   -21.07945 -41.88572 1.000 26.47865 ? 766 HOH A O     1 
HETATM 4057 O  O     . HOH D 4 .   ? 0.00393   -5.21346  -14.44071 1.000 25.95251 ? 767 HOH A O     1 
HETATM 4058 O  O     . HOH D 4 .   ? 5.03853   -7.97644  -39.18580 1.000 17.11789 ? 768 HOH A O     1 
HETATM 4059 O  O     . HOH D 4 .   ? 5.15793   -9.86144  -15.85680 1.000 10.80603 ? 769 HOH A O     1 
HETATM 4060 O  O     . HOH D 4 .   ? -2.40743  -18.51146 -39.05368 1.000 21.47834 ? 770 HOH A O     1 
HETATM 4061 O  O     . HOH D 4 .   ? 13.25507  13.26058  -2.21493  1.000 15.67971 ? 771 HOH A O     1 
HETATM 4062 O  O     . HOH D 4 .   ? 22.99602  -15.10938 -11.06510 1.000 10.23452 ? 772 HOH A O     1 
HETATM 4063 O  O     . HOH D 4 .   ? 7.03470   -24.58843 -32.56183 1.000 8.51797  ? 773 HOH A O     1 
HETATM 4064 O  O     . HOH D 4 .   ? 34.39982  -15.97034 -23.51429 1.000 8.64286  ? 774 HOH A O     1 
HETATM 4065 O  O     . HOH D 4 .   ? 19.80962  13.39261  -29.42503 1.000 31.13292 ? 775 HOH A O     1 
HETATM 4066 O  O     . HOH D 4 .   ? 26.75992  -24.30537 -19.35516 1.000 25.20457 ? 776 HOH A O     1 
HETATM 4067 O  O     . HOH D 4 .   ? 25.69373  3.18463   -24.97714 1.000 9.51322  ? 777 HOH A O     1 
HETATM 4068 O  O     . HOH D 4 .   ? 14.27811  -1.40942  -3.11895  1.000 18.54795 ? 778 HOH A O     1 
HETATM 4069 O  O     . HOH D 4 .   ? 18.79102  0.87360   -8.18402  1.000 14.26109 ? 779 HOH A O     1 
HETATM 4070 O  O     . HOH D 4 .   ? 13.95285  5.33859   -17.29494 1.000 23.24364 ? 780 HOH A O     1 
HETATM 4071 O  O     . HOH D 4 .   ? 7.71008   1.55556   -4.12784  1.000 18.92256 ? 781 HOH A O     1 
HETATM 4072 O  O     . HOH D 4 .   ? 24.76769  23.36563  -23.35311 1.000 23.66079 ? 782 HOH A O     1 
HETATM 4073 O  O     . HOH D 4 .   ? 17.46773  -0.93740  -26.04800 1.000 8.42885  ? 783 HOH A O     1 
HETATM 4074 O  O     . HOH D 4 .   ? -6.23104  -34.15948 -19.04062 1.000 27.46781 ? 784 HOH A O     1 
HETATM 4075 O  O     . HOH D 4 .   ? 33.46776  4.35466   -23.13426 1.000 22.40239 ? 785 HOH A O     1 
HETATM 4076 O  O     . HOH D 4 .   ? 16.29996  -22.05740 -16.17899 1.000 3.48193  ? 786 HOH A O     1 
HETATM 4077 O  O     . HOH D 4 .   ? -6.20730  -11.48248 -29.81061 1.000 27.25915 ? 787 HOH A O     1 
HETATM 4078 O  O     . HOH D 4 .   ? 35.10403  8.63666   -5.67029  1.000 35.98931 ? 788 HOH A O     1 
HETATM 4079 O  O     . HOH D 4 .   ? 30.74797  5.21664   -10.18822 1.000 10.67913 ? 789 HOH A O     1 
HETATM 4080 O  O     . HOH D 4 .   ? 23.00986  1.64962   -17.62909 1.000 5.01612  ? 790 HOH A O     1 
HETATM 4081 O  O     . HOH D 4 .   ? 8.72538   -13.22442 -49.11886 1.000 38.35987 ? 791 HOH A O     1 
HETATM 4082 O  O     . HOH D 4 .   ? 7.43374   -1.71743  -25.47383 1.000 27.42781 ? 792 HOH A O     1 
HETATM 4083 O  O     . HOH D 4 .   ? 33.31480  -22.32234 -25.89427 1.000 17.54088 ? 793 HOH A O     1 
HETATM 4084 O  O     . HOH D 4 .   ? 2.03692   -9.35945  -15.86575 1.000 13.00703 ? 794 HOH A O     1 
HETATM 4085 O  O     . HOH D 4 .   ? 39.40084  1.86868   -18.78836 1.000 19.22422 ? 795 HOH A O     1 
HETATM 4086 O  O     . HOH D 4 .   ? 6.62760   -3.15843  -34.14782 1.000 16.90954 ? 796 HOH A O     1 
HETATM 4087 O  O     . HOH D 4 .   ? 6.30874   -33.50143 -32.02783 1.000 26.65300 ? 797 HOH A O     1 
HETATM 4088 O  O     . HOH D 4 .   ? 15.37109  -10.61941 -5.91297  1.000 17.33461 ? 798 HOH A O     1 
HETATM 4089 O  O     . HOH D 4 .   ? 9.78541   -2.61642  -45.69387 1.000 31.60996 ? 799 HOH A O     1 
HETATM 4090 O  O     . HOH D 4 .   ? 36.35672  -12.91933 -28.60732 1.000 23.35556 ? 800 HOH A O     1 
HETATM 4091 O  O     . HOH D 4 .   ? -1.60340  -22.72346 -38.25769 1.000 12.80471 ? 801 HOH A O     1 
HETATM 4092 O  O     . HOH D 4 .   ? 25.68376  4.63663   -22.58613 1.000 4.83830  ? 802 HOH A O     1 
HETATM 4093 O  O     . HOH D 4 .   ? 5.90306   9.75656   -3.76480  1.000 18.76958 ? 803 HOH A O     1 
HETATM 4094 O  O     . HOH D 4 .   ? 6.22240   -4.82943  -46.27881 1.000 19.81157 ? 804 HOH A O     1 
HETATM 4095 O  O     . HOH D 4 .   ? 29.09696  -24.00536 -16.64320 1.000 17.53721 ? 805 HOH A O     1 
HETATM 4096 O  O     . HOH D 4 .   ? -0.12231  -8.40146  -29.73671 1.000 25.27854 ? 806 HOH A O     1 
HETATM 4097 O  O     . HOH D 4 .   ? 12.71597  -20.70042 -15.20593 1.000 9.34453  ? 807 HOH A O     1 
HETATM 4098 O  O     . HOH D 4 .   ? -4.27994  -32.64048 -12.18865 1.000 14.51057 ? 808 HOH A O     1 
HETATM 4099 O  O     . HOH D 4 .   ? 7.29796   16.50856  -8.55783  1.000 24.75723 ? 809 HOH A O     1 
HETATM 4100 O  O     . HOH D 4 .   ? 14.19210  -4.25242  -3.96695  1.000 21.51534 ? 810 HOH A O     1 
HETATM 4101 O  O     . HOH D 4 .   ? 19.55967  -19.93139 -33.28304 1.000 34.15083 ? 811 HOH A O     1 
HETATM 4102 O  O     . HOH D 4 .   ? 5.45310   -38.36844 -11.30781 1.000 35.92639 ? 812 HOH A O     1 
HETATM 4103 O  O     . HOH D 4 .   ? 7.05700   21.57556  -5.10782  1.000 38.11951 ? 813 HOH A O     1 
HETATM 4104 O  O     . HOH D 4 .   ? 21.94885  8.58862   -16.49407 1.000 7.69985  ? 814 HOH A O     1 
HETATM 4105 O  O     . HOH D 4 .   ? 14.10614  3.96758   -0.14794  1.000 26.87544 ? 815 HOH A O     1 
HETATM 4106 O  O     . HOH D 4 .   ? 14.11386  10.02159  -15.62594 1.000 6.58946  ? 816 HOH A O     1 
HETATM 4107 O  O     . HOH D 4 .   ? 1.66745   -15.58444 -45.92174 1.000 30.33348 ? 817 HOH A O     1 
HETATM 4108 O  O     . HOH D 4 .   ? 19.32285  30.65660  -11.90902 1.000 23.30840 ? 818 HOH A O     1 
HETATM 4109 O  O     . HOH D 4 .   ? 26.74569  3.95164   -27.37615 1.000 17.31693 ? 819 HOH A O     1 
HETATM 4110 O  O     . HOH D 4 .   ? 34.19472  2.52866   -25.89828 1.000 13.24859 ? 820 HOH A O     1 
HETATM 4111 O  O     . HOH D 4 .   ? 33.17386  3.05565   -17.27926 1.000 12.42090 ? 821 HOH A O     1 
HETATM 4112 O  O     . HOH D 4 .   ? 31.88975  8.14865   -22.57924 1.000 10.68264 ? 822 HOH A O     1 
HETATM 4113 O  O     . HOH D 4 .   ? 0.81388   -39.46445 -24.74374 1.000 28.54370 ? 823 HOH A O     1 
HETATM 4114 O  O     . HOH D 4 .   ? 15.65372  26.20060  -20.81896 1.000 23.76479 ? 824 HOH A O     1 
HETATM 4115 O  O     . HOH D 4 .   ? -4.80214  -30.30847 -24.22064 1.000 9.59900  ? 825 HOH A O     1 
HETATM 4116 O  O     . HOH D 4 .   ? 5.14250   -3.47843  -39.99280 1.000 24.58035 ? 826 HOH A O     1 
HETATM 4117 O  O     . HOH D 4 .   ? 39.66784  -20.69432 -23.34238 1.000 19.64385 ? 827 HOH A O     1 
HETATM 4118 O  O     . HOH D 4 .   ? 23.71987  -2.02338  -17.63010 1.000 9.25215  ? 828 HOH A O     1 
HETATM 4119 O  O     . HOH D 4 .   ? 21.01510  24.66961  1.70895   1.000 26.48485 ? 829 HOH A O     1 
HETATM 4120 O  O     . HOH D 4 .   ? 17.86580  -1.09640  -21.52201 1.000 13.68214 ? 830 HOH A O     1 
HETATM 4121 O  O     . HOH D 4 .   ? 3.12785   -29.54445 -24.25777 1.000 7.68038  ? 831 HOH A O     1 
HETATM 4122 O  O     . HOH D 4 .   ? 36.78886  -6.04133  -18.96432 1.000 11.43093 ? 832 HOH A O     1 
HETATM 4123 O  O     . HOH D 4 .   ? 35.02287  -3.74234  -18.22729 1.000 10.91098 ? 833 HOH A O     1 
HETATM 4124 O  O     . HOH D 4 .   ? 32.80508  14.37365  -1.49525  1.000 21.98332 ? 834 HOH A O     1 
HETATM 4125 O  O     . HOH D 4 .   ? 6.26440   -24.47043 -50.43282 1.000 37.58060 ? 835 HOH A O     1 
HETATM 4126 O  O     . HOH D 4 .   ? 33.38787  10.88765  -14.95726 1.000 23.92528 ? 836 HOH A O     1 
HETATM 4127 O  O     . HOH D 4 .   ? 3.49974   -3.68244  -25.57277 1.000 27.50672 ? 837 HOH A O     1 
HETATM 4128 O  O     . HOH D 4 .   ? -0.12313  -15.93146 -20.27571 1.000 20.16553 ? 838 HOH A O     1 
HETATM 4129 O  O     . HOH D 4 .   ? 11.64239  -9.43241  -47.85891 1.000 30.46430 ? 839 HOH A O     1 
HETATM 4130 O  O     . HOH D 4 .   ? 10.25315  -28.13243 -6.06989  1.000 32.18107 ? 840 HOH A O     1 
HETATM 4131 O  O     . HOH D 4 .   ? -0.71010  -3.46146  -16.14470 1.000 28.08690 ? 841 HOH A O     1 
HETATM 4132 O  O     . HOH D 4 .   ? -8.31120  -21.78248 -25.86658 1.000 20.87193 ? 842 HOH A O     1 
HETATM 4133 O  O     . HOH D 4 .   ? 37.76773  -7.80433  -27.06534 1.000 19.48688 ? 843 HOH A O     1 
HETATM 4134 O  O     . HOH D 4 .   ? 27.74906  0.50463   -5.38617  1.000 14.76612 ? 844 HOH A O     1 
HETATM 4135 O  O     . HOH D 4 .   ? -1.60335  -35.26046 -37.71769 1.000 31.48445 ? 845 HOH A O     1 
HETATM 4136 O  O     . HOH D 4 .   ? 29.92553  5.45265   -36.57221 1.000 21.65306 ? 846 HOH A O     1 
HETATM 4137 O  O     . HOH D 4 .   ? 7.94496   -29.47243 -17.59885 1.000 15.07525 ? 847 HOH A O     1 
HETATM 4138 O  O     . HOH D 4 .   ? 19.67250  -11.25638 -41.68804 1.000 26.63613 ? 848 HOH A O     1 
HETATM 4139 O  O     . HOH D 4 .   ? 3.03405   9.10555   -4.22776  1.000 24.57589 ? 849 HOH A O     1 
HETATM 4140 O  O     . HOH D 4 .   ? 17.78975  31.88860  -17.56699 1.000 23.66682 ? 850 HOH A O     1 
HETATM 4141 O  O     . HOH D 4 .   ? 26.58078  -5.53937  -23.78715 1.000 7.74031  ? 851 HOH A O     1 
HETATM 4142 O  O     . HOH D 4 .   ? 35.67203  -12.31134 -10.25531 1.000 20.08409 ? 852 HOH A O     1 
HETATM 4143 O  O     . HOH D 4 .   ? 27.12486  7.18263   -16.29616 1.000 10.17329 ? 853 HOH A O     1 
HETATM 4144 O  O     . HOH D 4 .   ? 8.82051   -10.50442 -40.88186 1.000 17.58164 ? 854 HOH A O     1 
HETATM 4145 O  O     . HOH D 4 .   ? 36.36580  -14.56933 -24.38732 1.000 15.08216 ? 855 HOH A O     1 
HETATM 4146 O  O     . HOH D 4 .   ? 19.45384  -7.41439  -20.53004 1.000 9.33089  ? 856 HOH A O     1 
HETATM 4147 O  O     . HOH D 4 .   ? 36.19083  15.68566  -16.57931 1.000 32.72774 ? 857 HOH A O     1 
HETATM 4148 O  O     . HOH D 4 .   ? 19.82003  -17.92839 -11.23204 1.000 12.04264 ? 858 HOH A O     1 
HETATM 4149 O  O     . HOH D 4 .   ? 20.16679  -25.63639 -27.41705 1.000 21.84245 ? 859 HOH A O     1 
HETATM 4150 O  O     . HOH D 4 .   ? -1.87801  -21.14347 -14.25069 1.000 16.76598 ? 860 HOH A O     1 
HETATM 4151 O  O     . HOH D 4 .   ? 22.64153  -11.84337 -40.29509 1.000 27.50068 ? 861 HOH A O     1 
HETATM 4152 O  O     . HOH D 4 .   ? 16.45147  -10.85539 -43.44499 1.000 19.61489 ? 862 HOH A O     1 
HETATM 4153 O  O     . HOH D 4 .   ? 37.541    3.630     -40.332   1.000 16.69084 ? 863 HOH A O     1 
HETATM 4154 O  O     . HOH D 4 .   ? 8.31682   11.69457  -17.72184 1.000 33.47236 ? 864 HOH A O     1 
HETATM 4155 O  O     . HOH D 4 .   ? 8.42768   -29.99942 -34.73986 1.000 12.23941 ? 865 HOH A O     1 
HETATM 4156 O  O     . HOH D 4 .   ? 7.33075   -24.54043 -29.71984 1.000 12.91923 ? 866 HOH A O     1 
HETATM 4157 O  O     . HOH D 4 .   ? 19.59020  4.75460   3.74997   1.000 29.47382 ? 867 HOH A O     1 
HETATM 4158 O  O     . HOH D 4 .   ? 19.22072  -18.22339 -30.16203 1.000 25.33543 ? 868 HOH A O     1 
HETATM 4159 O  O     . HOH D 4 .   ? 16.37807  -25.73041 -10.21399 1.000 24.48823 ? 869 HOH A O     1 
HETATM 4160 O  O     . HOH D 4 .   ? 12.10293  -20.72942 -18.11292 1.000 7.52265  ? 870 HOH A O     1 
HETATM 4161 O  O     . HOH D 4 .   ? 17.48607  -11.49440 -7.71200  1.000 12.88465 ? 871 HOH A O     1 
HETATM 4162 O  O     . HOH D 4 .   ? 19.89182  -4.88939  -21.37504 1.000 6.52177  ? 872 HOH A O     1 
HETATM 4163 O  O     . HOH D 4 .   ? 8.48778   -26.15443 -27.84786 1.000 8.83544  ? 873 HOH A O     1 
HETATM 4164 O  O     . HOH D 4 .   ? 7.62084   -29.45843 -24.74785 1.000 11.43731 ? 874 HOH A O     1 
HETATM 4165 O  O     . HOH D 4 .   ? 7.99702   -6.01543  -9.31284  1.000 13.65753 ? 875 HOH A O     1 
HETATM 4166 O  O     . HOH D 4 .   ? 25.13150  0.08763   -39.60513 1.000 22.67876 ? 876 HOH A O     1 
HETATM 4167 O  O     . HOH D 4 .   ? 6.80410   8.59756   -1.51782  1.000 27.20079 ? 877 HOH A O     1 
HETATM 4168 O  O     . HOH D 4 .   ? -9.18927  -17.71649 -29.07456 1.000 23.10017 ? 878 HOH A O     1 
HETATM 4169 O  O     . HOH D 4 .   ? 25.90686  -1.01937  -17.93714 1.000 10.40754 ? 879 HOH A O     1 
HETATM 4170 O  O     . HOH D 4 .   ? 14.07760  17.12259  -29.95694 1.000 29.41854 ? 880 HOH A O     1 
HETATM 4171 O  O     . HOH D 4 .   ? 6.32409   -28.78444 -9.57482  1.000 13.29662 ? 881 HOH A O     1 
HETATM 4172 O  O     . HOH D 4 .   ? 26.91170  21.77163  -23.03815 1.000 25.75911 ? 882 HOH A O     1 
HETATM 4173 O  O     . HOH D 4 .   ? -12.25209 -35.07050 -22.13652 1.000 19.15565 ? 883 HOH A O     1 
HETATM 4174 O  O     . HOH D 4 .   ? 23.74666  1.65163   -29.48210 1.000 16.10090 ? 884 HOH A O     1 
HETATM 4175 O  O     . HOH D 4 .   ? 20.30183  7.05361   -18.43604 1.000 7.84900  ? 885 HOH A O     1 
HETATM 4176 O  O     . HOH D 4 .   ? -3.90999  -12.09347 -11.43965 1.000 42.07374 ? 886 HOH A O     1 
HETATM 4177 O  O     . HOH D 4 .   ? 18.13810  -3.75540  -4.37301  1.000 20.28827 ? 887 HOH A O     1 
HETATM 4178 O  O     . HOH D 4 .   ? 27.34065  5.60264   -29.05916 1.000 20.78824 ? 888 HOH A O     1 
HETATM 4179 O  O     . HOH D 4 .   ? 23.66667  21.06762  -25.08310 1.000 24.27846 ? 889 HOH A O     1 
HETATM 4180 O  O     . HOH D 4 .   ? 39.07585  -3.94133  -19.45336 1.000 27.08230 ? 890 HOH A O     1 
HETATM 4181 O  O     . HOH D 4 .   ? 11.43710  8.25357   -1.53490  1.000 13.61654 ? 891 HOH A O     1 
HETATM 4182 O  O     . HOH D 4 .   ? 29.79072  14.39764  -23.07420 1.000 16.06143 ? 892 HOH A O     1 
HETATM 4183 O  O     . HOH D 4 .   ? 10.54972  -0.37442  -26.41788 1.000 24.08143 ? 893 HOH A O     1 
HETATM 4184 O  O     . HOH D 4 .   ? 6.10008   -18.28444 -8.09282  1.000 26.66387 ? 894 HOH A O     1 
HETATM 4185 O  O     . HOH D 4 .   ? -5.96819  -10.61948 -22.87461 1.000 26.53717 ? 895 HOH A O     1 
HETATM 4186 O  O     . HOH D 4 .   ? 24.40411  -1.31938  -2.92412  1.000 24.43649 ? 896 HOH A O     1 
HETATM 4187 O  O     . HOH D 4 .   ? 19.63717  12.88360  3.63697   1.000 23.59141 ? 897 HOH A O     1 
HETATM 4188 O  O     . HOH D 4 .   ? -4.23637  -28.04647 -37.15965 1.000 18.10760 ? 898 HOH A O     1 
HETATM 4189 O  O     . HOH D 4 .   ? 29.06150  -8.71235  -41.45820 1.000 19.62507 ? 899 HOH A O     1 
HETATM 4190 O  O     . HOH D 4 .   ? -15.39006 -25.01451 -18.29146 1.000 30.33555 ? 900 HOH A O     1 
HETATM 4191 O  O     . HOH D 4 .   ? 12.40386  28.62158  -12.16291 1.000 25.93206 ? 901 HOH A O     1 
HETATM 4192 O  O     . HOH D 4 .   ? 17.17047  -20.55339 -45.68500 1.000 23.38552 ? 902 HOH A O     1 
HETATM 4193 O  O     . HOH D 4 .   ? 42.72876  -4.76831  -24.94642 1.000 20.93448 ? 903 HOH A O     1 
HETATM 4194 O  O     . HOH D 4 .   ? -11.07818 -26.95849 -25.55153 1.000 20.75124 ? 904 HOH A O     1 
HETATM 4195 O  O     . HOH D 4 .   ? 39.823    -23.916   -17.244   1.000 14.68975 ? 905 HOH A O     1 
HETATM 4196 O  O     . HOH D 4 .   ? -2.77339  -12.14046 -35.18267 1.000 23.51634 ? 906 HOH A O     1 
HETATM 4197 O  O     . HOH D 4 .   ? 35.24113  8.95666   0.11971   1.000 17.87370 ? 907 HOH A O     1 
HETATM 4198 O  O     . HOH D 4 .   ? 11.92975  0.51058   -24.39491 1.000 30.75606 ? 908 HOH A O     1 
HETATM 4199 O  O     . HOH D 4 .   ? 28.01360  -15.80736 -36.53518 1.000 34.68250 ? 909 HOH A O     1 
HETATM 4200 O  O     . HOH D 4 .   ? 25.29889  5.12963   -15.15113 1.000 10.92657 ? 910 HOH A O     1 
HETATM 4201 O  O     . HOH D 4 .   ? 39.48493  -7.53733  -14.98937 1.000 19.43403 ? 911 HOH A O     1 
HETATM 4202 O  O     . HOH D 4 .   ? 4.63843   -16.72843 -46.83079 1.000 25.08944 ? 912 HOH A O     1 
HETATM 4203 O  O     . HOH D 4 .   ? 21.27896  -26.04939 -16.81007 1.000 7.51722  ? 913 HOH A O     1 
HETATM 4204 O  O     . HOH D 4 .   ? 2.09854   -5.17645  -37.85475 1.000 23.47272 ? 914 HOH A O     1 
HETATM 4205 O  O     . HOH D 4 .   ? 45.66890  -16.16030 -18.52047 1.000 25.08196 ? 915 HOH A O     1 
HETATM 4206 O  O     . HOH D 4 .   ? 26.74980  -25.53637 -26.71816 1.000 18.85285 ? 916 HOH A O     1 
HETATM 4207 O  O     . HOH D 4 .   ? 23.22289  7.17462   -14.57209 1.000 5.43849  ? 917 HOH A O     1 
HETATM 4208 O  O     . HOH D 4 .   ? 15.67767  -21.40340 -33.73498 1.000 21.26333 ? 918 HOH A O     1 
HETATM 4209 O  O     . HOH D 4 .   ? 20.74556  -18.99538 -39.77106 1.000 31.46764 ? 919 HOH A O     1 
HETATM 4210 O  O     . HOH D 4 .   ? 13.63106  -26.31441 -10.85394 1.000 13.33828 ? 920 HOH A O     1 
HETATM 4211 O  O     . HOH D 4 .   ? 21.70177  -16.81738 -26.49808 1.000 16.69819 ? 921 HOH A O     1 
HETATM 4212 O  O     . HOH D 4 .   ? 5.88609   -0.51344  -4.28381  1.000 29.30804 ? 922 HOH A O     1 
HETATM 4213 O  O     . HOH D 4 .   ? 3.96091   -36.38344 -22.01179 1.000 16.90929 ? 923 HOH A O     1 
HETATM 4214 O  O     . HOH D 4 .   ? 31.73996  24.80265  -6.43123  1.000 21.49979 ? 924 HOH A O     1 
HETATM 4215 O  O     . HOH D 4 .   ? 1.42800   -9.03046  -11.33074 1.000 23.24312 ? 925 HOH A O     1 
HETATM 4216 O  O     . HOH D 4 .   ? 8.48796   19.33357  -7.66384  1.000 13.86070 ? 926 HOH A O     1 
HETATM 4217 O  O     . HOH D 4 .   ? 17.57414  -5.01340  -1.69200  1.000 24.16060 ? 927 HOH A O     1 
HETATM 4218 O  O     . HOH D 4 .   ? -4.88592  -39.68348 -12.85464 1.000 17.97149 ? 928 HOH A O     1 
HETATM 4219 O  O     . HOH D 4 .   ? -11.162   -15.690   -24.188   1.000 20.28146 ? 929 HOH A O     1 
HETATM 4220 O  O     . HOH D 4 .   ? -0.15626  -31.76746 -31.73772 1.000 11.60087 ? 930 HOH A O     1 
HETATM 4221 O  O     . HOH D 4 .   ? 32.29203  15.27365  -4.15124  1.000 26.19402 ? 931 HOH A O     1 
HETATM 4222 O  O     . HOH D 4 .   ? 24.84760  -14.18537 -36.13313 1.000 19.27871 ? 932 HOH A O     1 
HETATM 4223 O  O     . HOH D 4 .   ? 13.46057  2.42159   -34.87693 0.736 16.09438 ? 933 HOH A O     1 
HETATM 4224 O  O     . HOH D 4 .   ? 0.31503   -20.41446 -11.60872 1.000 24.24998 ? 934 HOH A O     1 
HETATM 4225 O  O     . HOH D 4 .   ? 4.69868   -32.19944 -35.45880 1.000 25.86930 ? 935 HOH A O     1 
HETATM 4226 O  O     . HOH D 4 .   ? 26.66395  -23.86137 -17.04716 1.000 29.30436 ? 936 HOH A O     1 
HETATM 4227 O  O     . HOH D 4 .   ? 35.46501  17.43766  -5.28429  1.000 27.63888 ? 937 HOH A O     1 
HETATM 4228 O  O     . HOH D 4 .   ? 34.62589  12.78166  -13.34628 1.000 27.91471 ? 938 HOH A O     1 
HETATM 4229 O  O     . HOH D 4 .   ? 34.14401  15.31865  -5.36427  1.000 25.25809 ? 939 HOH A O     1 
HETATM 4230 O  O     . HOH D 4 .   ? 12.53168  4.00159   -27.82892 1.000 24.94722 ? 940 HOH A O     1 
HETATM 4231 O  O     . HOH D 4 .   ? 22.04564  12.58162  -28.17907 1.000 28.84750 ? 941 HOH A O     1 
HETATM 4232 O  O     . HOH D 4 .   ? 15.34744  -13.27740 -45.64497 1.000 29.59594 ? 942 HOH A O     1 
HETATM 4233 O  O     . HOH D 4 .   ? 11.413    -11.368   -55.558   1.000 28.83450 ? 943 HOH A O     1 
HETATM 4234 O  O     . HOH D 4 .   ? 10.72613  23.59257  3.15812   1.000 28.23485 ? 944 HOH A O     1 
HETATM 4235 O  O     . HOH D 4 .   ? 0.98846   -24.05445 -46.67073 1.000 25.56175 ? 945 HOH A O     1 
HETATM 4236 O  O     . HOH D 4 .   ? 9.65286   0.15657   -17.63587 1.000 23.98920 ? 946 HOH A O     1 
HETATM 4237 O  O     . HOH D 4 .   ? 23.44857  -13.14637 -38.12010 1.000 22.81196 ? 947 HOH A O     1 
HETATM 4238 O  O     . HOH D 4 .   ? 10.13713  -12.39043 -4.14188  1.000 33.91190 ? 948 HOH A O     1 
HETATM 4239 O  O     . HOH D 4 .   ? 4.46907   -16.14845 -8.34079  1.000 22.89668 ? 949 HOH A O     1 
HETATM 4240 O  O     . HOH D 4 .   ? 11.98379  10.80158  -19.98291 1.000 25.80031 ? 950 HOH A O     1 
HETATM 4241 O  O     . HOH D 4 .   ? 35.78772  -17.68433 -29.86831 1.000 29.46653 ? 951 HOH A O     1 
HETATM 4242 O  O     . HOH D 4 .   ? 14.04954  4.34459   -35.98394 1.000 26.04514 ? 952 HOH A O     1 
HETATM 4243 O  O     . HOH D 4 .   ? 32.61775  -21.51234 -28.95126 1.000 25.67785 ? 953 HOH A O     1 
HETATM 4244 O  O     . HOH D 4 .   ? 22.83473  2.61862   -25.11409 1.000 12.49751 ? 954 HOH A O     1 
HETATM 4245 O  O     . HOH D 4 .   ? 27.03913  -8.25937  -3.20316  1.000 24.00640 ? 955 HOH A O     1 
HETATM 4246 O  O     . HOH D 4 .   ? -3.50699  -23.76447 -13.75666 1.000 22.31610 ? 956 HOH A O     1 
HETATM 4247 O  O     . HOH D 4 .   ? 33.58681  6.06166   -19.81327 1.000 21.54863 ? 957 HOH A O     1 
HETATM 4248 O  O     . HOH D 4 .   ? 11.96292  -38.12742 -21.71192 1.000 33.80623 ? 958 HOH A O     1 
HETATM 4249 O  O     . HOH D 4 .   ? -8.94232  -23.52948 -33.42657 1.000 21.42965 ? 959 HOH A O     1 
HETATM 4250 O  O     . HOH D 4 .   ? 36.948    5.669     -4.948    1.000 28.27529 ? 960 HOH A O     1 
HETATM 4251 O  O     . HOH D 4 .   ? -5.19320  -8.34348  -23.18563 1.000 32.60556 ? 961 HOH A O     1 
HETATM 4252 O  O     . HOH D 4 .   ? 8.16578   9.97257   -20.25684 1.000 43.00712 ? 962 HOH A O     1 
HETATM 4253 O  O     . HOH D 4 .   ? 11.27113  4.68357   -0.73290  1.000 25.83377 ? 963 HOH A O     1 
HETATM 4254 O  O     . HOH D 4 .   ? 4.40213   -1.24145  -2.09178  1.000 25.03321 ? 964 HOH A O     1 
HETATM 4255 O  O     . HOH D 4 .   ? 8.45963   -29.36442 -37.89886 1.000 34.19891 ? 965 HOH A O     1 
HETATM 4256 O  O     . HOH D 4 .   ? 23.49072  31.53962  -19.96509 1.000 26.78856 ? 966 HOH A O     1 
HETATM 4257 O  O     . HOH D 4 .   ? 38.68080  -10.59033 -23.71536 1.000 25.87277 ? 967 HOH A O     1 
HETATM 4258 O  O     . HOH D 4 .   ? 22.19599  26.99961  -4.38707  1.000 24.21072 ? 968 HOH A O     1 
HETATM 4259 O  O     . HOH D 4 .   ? 34.30599  -1.07734  -10.05828 1.000 28.98145 ? 969 HOH A O     1 
HETATM 4260 O  O     . HOH D 4 .   ? 14.75080  5.53159   -20.18695 1.000 15.18290 ? 970 HOH A O     1 
HETATM 4261 O  O     . HOH D 4 .   ? 20.02279  -21.08839 -26.57705 1.000 24.04474 ? 971 HOH A O     1 
HETATM 4262 O  O     . HOH D 4 .   ? 34.05685  5.33866   -17.34327 1.000 15.46558 ? 972 HOH A O     1 
HETATM 4263 O  O     . HOH D 4 .   ? 37.95882  -13.21133 -22.77334 1.000 14.12955 ? 973 HOH A O     1 
HETATM 4264 O  O     . HOH D 4 .   ? 27.44095  -26.26837 -17.89217 1.000 23.97407 ? 974 HOH A O     1 
HETATM 4265 O  O     . HOH D 4 .   ? 21.86276  -19.84738 -28.10008 1.000 31.40523 ? 975 HOH A O     1 
HETATM 4266 O  O     . HOH D 4 .   ? 4.70212   -26.72945 -7.40480  1.000 22.76872 ? 976 HOH A O     1 
HETATM 4267 O  O     . HOH D 4 .   ? 20.24500  -26.38739 -14.54405 1.000 16.93197 ? 977 HOH A O     1 
HETATM 4268 O  O     . HOH D 4 .   ? 26.17712  -4.02037  -2.81815  1.000 19.42571 ? 978 HOH A O     1 
HETATM 4269 O  O     . HOH D 4 .   ? 38.65488  -5.06733  -17.37135 1.000 26.22622 ? 979 HOH A O     1 
HETATM 4270 O  O     . HOH D 4 .   ? 20.15075  -22.32539 -28.76405 1.000 24.02521 ? 980 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   ? 0.39865 0.35259 0.42598 -0.01478 0.00900  -0.00643 3   GLY A C   
2    O O   . GLY A 3   ? 0.47018 0.42288 0.49790 -0.01511 0.01185  -0.00389 3   GLY A O   
3    N N   . VAL A 4   ? 0.27564 0.23179 0.29821 -0.01285 0.00703  -0.00640 4   VAL A N   
4    C CA  . VAL A 4   ? 0.28261 0.24355 0.30459 -0.01281 0.00458  -0.00735 4   VAL A CA  
5    C C   . VAL A 4   ? 0.32230 0.28564 0.34124 -0.01153 0.00555  -0.00448 4   VAL A C   
6    O O   . VAL A 4   ? 0.26567 0.22697 0.28212 -0.01036 0.00758  -0.00197 4   VAL A O   
7    C CB  . VAL A 4   ? 0.27691 0.23827 0.29543 -0.01188 0.00179  -0.00962 4   VAL A CB  
8    C CG1 . VAL A 4   ? 0.28177 0.24021 0.30272 -0.01307 0.00074  -0.01265 4   VAL A CG1 
9    C CG2 . VAL A 4   ? 0.29740 0.25780 0.31073 -0.00959 0.00259  -0.00813 4   VAL A CG2 
10   N N   . LYS A 5   ? 0.29573 0.26318 0.31469 -0.01165 0.00386  -0.00491 5   LYS A N   
11   C CA  . LYS A 5   ? 0.21166 0.18160 0.22773 -0.01050 0.00441  -0.00265 5   LYS A CA  
12   C C   . LYS A 5   ? 0.17848 0.14995 0.18982 -0.00886 0.00256  -0.00286 5   LYS A C   
13   O O   . LYS A 5   ? 0.17560 0.14849 0.18642 -0.00913 0.00021  -0.00482 5   LYS A O   
14   C CB  . LYS A 5   ? 0.20625 0.17957 0.22568 -0.01166 0.00409  -0.00292 5   LYS A CB  
15   C CG  . LYS A 5   ? 0.19987 0.17597 0.21597 -0.01044 0.00402  -0.00118 5   LYS A CG  
16   C CD  . LYS A 5   ? 0.12047 0.09972 0.14021 -0.01145 0.00384  -0.00163 5   LYS A CD  
17   C CE  . LYS A 5   ? 0.17583 0.15739 0.19212 -0.01027 0.00386  -0.00003 5   LYS A CE  
18   N NZ  . LYS A 5   ? 0.11708 0.10165 0.13703 -0.01106 0.00370  -0.00064 5   LYS A NZ  
19   N N   . ASN A 6   ? 0.19149 0.16248 0.19938 -0.00716 0.00361  -0.00089 6   ASN A N   
20   C CA  . ASN A 6   ? 0.13545 0.10842 0.13964 -0.00570 0.00247  -0.00083 6   ASN A CA  
21   C C   . ASN A 6   ? 0.18615 0.16127 0.18883 -0.00486 0.00307  0.00137  6   ASN A C   
22   O O   . ASN A 6   ? 0.14388 0.11736 0.14591 -0.00411 0.00459  0.00332  6   ASN A O   
23   C CB  . ASN A 6   ? 0.20498 0.17570 0.20734 -0.00429 0.00290  -0.00110 6   ASN A CB  
24   C CG  . ASN A 6   ? 0.22439 0.19258 0.22775 -0.00507 0.00238  -0.00352 6   ASN A CG  
25   O OD1 . ASN A 6   ? 0.24845 0.21744 0.25224 -0.00627 0.00076  -0.00544 6   ASN A OD1 
26   N ND2 . ASN A 6   ? 0.20722 0.17206 0.21081 -0.00429 0.00352  -0.00353 6   ASN A ND2 
27   N N   . SER A 7   ? 0.14463 0.12295 0.14634 -0.00496 0.00178  0.00106  7   SER A N   
28   C CA  . SER A 7   ? 0.13948 0.11995 0.14011 -0.00446 0.00214  0.00273  7   SER A CA  
29   C C   . SER A 7   ? 0.12713 0.10966 0.12495 -0.00325 0.00125  0.00286  7   SER A C   
30   O O   . SER A 7   ? 0.13892 0.12180 0.13571 -0.00323 0.00032  0.00147  7   SER A O   
31   C CB  . SER A 7   ? 0.15410 0.13661 0.15692 -0.00575 0.00164  0.00226  7   SER A CB  
32   O OG  . SER A 7   ? 0.14271 0.12668 0.14529 -0.00616 -0.00048 0.00057  7   SER A OG  
33   N N   . ILE A 8   ? 0.11411 0.09776 0.11060 -0.00230 0.00167  0.00446  8   ILE A N   
34   C CA  . ILE A 8   ? 0.11205 0.09821 0.10681 -0.00144 0.00083  0.00452  8   ILE A CA  
35   C C   . ILE A 8   ? 0.10987 0.09817 0.10442 -0.00200 0.00047  0.00497  8   ILE A C   
36   O O   . ILE A 8   ? 0.11051 0.09827 0.10524 -0.00214 0.00135  0.00606  8   ILE A O   
37   C CB  . ILE A 8   ? 0.14057 0.12638 0.13424 0.00039  0.00109  0.00565  8   ILE A CB  
38   C CG1 . ILE A 8   ? 0.16369 0.14739 0.15801 0.00117  0.00146  0.00502  8   ILE A CG1 
39   C CG2 . ILE A 8   ? 0.18247 0.17135 0.17538 0.00105  0.00021  0.00549  8   ILE A CG2 
40   C CD1 . ILE A 8   ? 0.20689 0.19023 0.20081 0.00329  0.00132  0.00598  8   ILE A CD1 
41   N N   . ILE A 9   ? 0.11016 0.10045 0.10409 -0.00236 -0.00060 0.00411  9   ILE A N   
42   C CA  . ILE A 9   ? 0.10576 0.09808 0.09925 -0.00257 -0.00105 0.00449  9   ILE A CA  
43   C C   . ILE A 9   ? 0.10501 0.09894 0.09710 -0.00158 -0.00134 0.00479  9   ILE A C   
44   O O   . ILE A 9   ? 0.10465 0.09922 0.09633 -0.00161 -0.00164 0.00393  9   ILE A O   
45   C CB  . ILE A 9   ? 0.10953 0.10251 0.10348 -0.00365 -0.00220 0.00340  9   ILE A CB  
46   C CG1 . ILE A 9   ? 0.10281 0.09770 0.09599 -0.00364 -0.00273 0.00367  9   ILE A CG1 
47   C CG2 . ILE A 9   ? 0.16237 0.15440 0.15505 -0.00391 -0.00293 0.00220  9   ILE A CG2 
48   C CD1 . ILE A 9   ? 0.12677 0.12227 0.12096 -0.00362 -0.00202 0.00442  9   ILE A CD1 
49   N N   . TRP A 10  ? 0.10534 0.09974 0.09668 -0.00075 -0.00116 0.00588  10  TRP A N   
50   C CA  . TRP A 10  ? 0.11515 0.11121 0.10582 0.00033  -0.00180 0.00600  10  TRP A CA  
51   C C   . TRP A 10  ? 0.11527 0.11338 0.10553 -0.00022 -0.00245 0.00567  10  TRP A C   
52   O O   . TRP A 10  ? 0.10331 0.10131 0.09277 -0.00037 -0.00233 0.00620  10  TRP A O   
53   C CB  . TRP A 10  ? 0.10764 0.10246 0.09705 0.00181  -0.00176 0.00730  10  TRP A CB  
54   C CG  . TRP A 10  ? 0.12269 0.11930 0.11191 0.00321  -0.00301 0.00723  10  TRP A CG  
55   C CD1 . TRP A 10  ? 0.10593 0.10521 0.09702 0.00315  -0.00365 0.00598  10  TRP A CD1 
56   C CD2 . TRP A 10  ? 0.11080 0.10652 0.09798 0.00484  -0.00387 0.00831  10  TRP A CD2 
57   N NE1 . TRP A 10  ? 0.10691 0.10759 0.09827 0.00461  -0.00500 0.00600  10  TRP A NE1 
58   C CE2 . TRP A 10  ? 0.11006 0.10849 0.09868 0.00580  -0.00545 0.00744  10  TRP A CE2 
59   C CE3 . TRP A 10  ? 0.11465 0.10723 0.09866 0.00556  -0.00340 0.00993  10  TRP A CE3 
60   C CZ2 . TRP A 10  ? 0.11295 0.11124 0.10006 0.00766  -0.00718 0.00799  10  TRP A CZ2 
61   C CZ3 . TRP A 10  ? 0.12669 0.11848 0.10807 0.00742  -0.00487 0.01075  10  TRP A CZ3 
62   C CH2 . TRP A 10  ? 0.12441 0.11916 0.10742 0.00856  -0.00705 0.00971  10  TRP A CH2 
63   N N   . PHE A 11  ? 0.12127 0.12093 0.11206 -0.00060 -0.00285 0.00473  11  PHE A N   
64   C CA  . PHE A 11  ? 0.10048 0.10176 0.09103 -0.00118 -0.00341 0.00434  11  PHE A CA  
65   C C   . PHE A 11  ? 0.10064 0.10374 0.09152 -0.00021 -0.00411 0.00431  11  PHE A C   
66   O O   . PHE A 11  ? 0.12244 0.12648 0.11469 0.00058  -0.00424 0.00394  11  PHE A O   
67   C CB  . PHE A 11  ? 0.09996 0.10135 0.09052 -0.00227 -0.00324 0.00342  11  PHE A CB  
68   C CG  . PHE A 11  ? 0.10035 0.09988 0.09002 -0.00316 -0.00335 0.00328  11  PHE A CG  
69   C CD1 . PHE A 11  ? 0.13485 0.13422 0.12426 -0.00371 -0.00402 0.00336  11  PHE A CD1 
70   C CD2 . PHE A 11  ? 0.10167 0.09958 0.09097 -0.00333 -0.00303 0.00285  11  PHE A CD2 
71   C CE1 . PHE A 11  ? 0.13167 0.12952 0.12084 -0.00429 -0.00465 0.00305  11  PHE A CE1 
72   C CE2 . PHE A 11  ? 0.12083 0.11701 0.10934 -0.00404 -0.00369 0.00249  11  PHE A CE2 
73   C CZ  . PHE A 11  ? 0.18168 0.17794 0.17031 -0.00447 -0.00466 0.00260  11  PHE A CZ  
74   N N   . ARG A 12  ? 0.10351 0.10714 0.09340 -0.00019 -0.00468 0.00450  12  ARG A N   
75   C CA  . ARG A 12  ? 0.12591 0.13137 0.11605 0.00052  -0.00583 0.00407  12  ARG A CA  
76   C C   . ARG A 12  ? 0.10970 0.11604 0.09980 -0.00058 -0.00608 0.00336  12  ARG A C   
77   O O   . ARG A 12  ? 0.14924 0.15706 0.14103 -0.00131 -0.00621 0.00241  12  ARG A O   
78   C CB  . ARG A 12  ? 0.15535 0.15975 0.14319 0.00200  -0.00650 0.00500  12  ARG A CB  
79   C CG  . ARG A 12  ? 0.14227 0.14481 0.12961 0.00314  -0.00615 0.00600  12  ARG A CG  
80   C CD  . ARG A 12  ? 0.11396 0.11381 0.09976 0.00258  -0.00458 0.00704  12  ARG A CD  
81   N NE  . ARG A 12  ? 0.12551 0.12404 0.10833 0.00276  -0.00424 0.00777  12  ARG A NE  
82   C CZ  . ARG A 12  ? 0.13957 0.13596 0.11905 0.00411  -0.00443 0.00890  12  ARG A CZ  
83   N NH1 . ARG A 12  ? 0.20065 0.19607 0.17971 0.00560  -0.00534 0.00951  12  ARG A NH1 
84   N NH2 . ARG A 12  ? 0.17777 0.17262 0.15396 0.00406  -0.00363 0.00943  12  ARG A NH2 
85   N N   . LYS A 13  ? 0.15113 0.15639 0.13950 -0.00074 -0.00591 0.00377  13  LYS A N   
86   C CA  . LYS A 13  ? 0.09926 0.10451 0.08776 -0.00183 -0.00584 0.00323  13  LYS A CA  
87   C C   . LYS A 13  ? 0.11057 0.11438 0.09944 -0.00255 -0.00510 0.00354  13  LYS A C   
88   O O   . LYS A 13  ? 0.09857 0.10172 0.08782 -0.00248 -0.00468 0.00387  13  LYS A O   
89   C CB  . LYS A 13  ? 0.15600 0.16101 0.14280 -0.00144 -0.00608 0.00314  13  LYS A CB  
90   C CG  . LYS A 13  ? 0.13663 0.14294 0.12281 -0.00077 -0.00740 0.00246  13  LYS A CG  
91   C CD  . LYS A 13  ? 0.15338 0.15876 0.13674 -0.00024 -0.00751 0.00233  13  LYS A CD  
92   C CE  . LYS A 13  ? 0.13882 0.14496 0.12064 0.00085  -0.00930 0.00175  13  LYS A CE  
93   N NZ  . LYS A 13  ? 0.24152 0.24651 0.21998 0.00121  -0.00951 0.00122  13  LYS A NZ  
94   N N   . GLY A 14  ? 0.09820 0.10147 0.08716 -0.00313 -0.00514 0.00329  14  GLY A N   
95   C CA  . GLY A 14  ? 0.09789 0.09995 0.08763 -0.00364 -0.00506 0.00335  14  GLY A CA  
96   C C   . GLY A 14  ? 0.09800 0.09927 0.08749 -0.00416 -0.00530 0.00324  14  GLY A C   
97   O O   . GLY A 14  ? 0.09833 0.09869 0.08812 -0.00417 -0.00516 0.00337  14  GLY A O   
98   N N   . LEU A 15  ? 0.09825 0.09965 0.08707 -0.00469 -0.00545 0.00289  15  LEU A N   
99   C CA  . LEU A 15  ? 0.09932 0.09956 0.08711 -0.00528 -0.00516 0.00273  15  LEU A CA  
100  C C   . LEU A 15  ? 0.10081 0.09869 0.08708 -0.00583 -0.00601 0.00273  15  LEU A C   
101  O O   . LEU A 15  ? 0.10224 0.09885 0.08705 -0.00648 -0.00615 0.00267  15  LEU A O   
102  C CB  . LEU A 15  ? 0.09955 0.10087 0.08761 -0.00574 -0.00447 0.00230  15  LEU A CB  
103  C CG  . LEU A 15  ? 0.09845 0.10237 0.08848 -0.00495 -0.00439 0.00206  15  LEU A CG  
104  C CD1 . LEU A 15  ? 0.09867 0.10403 0.09014 -0.00563 -0.00392 0.00124  15  LEU A CD1 
105  C CD2 . LEU A 15  ? 0.09849 0.10263 0.08906 -0.00408 -0.00399 0.00229  15  LEU A CD2 
106  N N   . ARG A 16  ? 0.10093 0.09802 0.08769 -0.00552 -0.00672 0.00276  16  ARG A N   
107  C CA  . ARG A 16  ? 0.10254 0.09761 0.08852 -0.00566 -0.00822 0.00261  16  ARG A CA  
108  C C   . ARG A 16  ? 0.10529 0.09996 0.09258 -0.00540 -0.00894 0.00229  16  ARG A C   
109  O O   . ARG A 16  ? 0.10132 0.09734 0.09062 -0.00516 -0.00803 0.00234  16  ARG A O   
110  C CB  . ARG A 16  ? 0.10177 0.09740 0.08930 -0.00541 -0.00888 0.00253  16  ARG A CB  
111  C CG  . ARG A 16  ? 0.09974 0.09741 0.09043 -0.00488 -0.00832 0.00238  16  ARG A CG  
112  C CD  . ARG A 16  ? 0.09946 0.09754 0.09176 -0.00459 -0.00870 0.00202  16  ARG A CD  
113  N NE  . ARG A 16  ? 0.11295 0.11258 0.10798 -0.00422 -0.00763 0.00180  16  ARG A NE  
114  C CZ  . ARG A 16  ? 0.09790 0.09867 0.09249 -0.00400 -0.00617 0.00198  16  ARG A CZ  
115  N NH1 . ARG A 16  ? 0.09796 0.09901 0.09033 -0.00404 -0.00604 0.00217  16  ARG A NH1 
116  N NH2 . ARG A 16  ? 0.09832 0.09977 0.09469 -0.00377 -0.00480 0.00190  16  ARG A NH2 
117  N N   . LEU A 17  ? 0.10518 0.09764 0.09118 -0.00544 -0.01074 0.00194  17  LEU A N   
118  C CA  . LEU A 17  ? 0.11935 0.11149 0.10731 -0.00526 -0.01202 0.00126  17  LEU A CA  
119  C C   . LEU A 17  ? 0.10481 0.09803 0.09677 -0.00486 -0.01331 0.00076  17  LEU A C   
120  O O   . LEU A 17  ? 0.12831 0.12270 0.12411 -0.00485 -0.01340 0.00011  17  LEU A O   
121  C CB  . LEU A 17  ? 0.12754 0.11645 0.11158 -0.00539 -0.01367 0.00085  17  LEU A CB  
122  C CG  . LEU A 17  ? 0.20398 0.19206 0.18621 -0.00569 -0.01262 0.00054  17  LEU A CG  
123  C CD1 . LEU A 17  ? 0.14820 0.13690 0.12865 -0.00596 -0.01011 0.00115  17  LEU A CD1 
124  C CD2 . LEU A 17  ? 0.15464 0.13911 0.13265 -0.00573 -0.01461 -0.00015 17  LEU A CD2 
125  N N   . HIS A 18  ? 0.14337 0.13618 0.13499 -0.00456 -0.01415 0.00091  18  HIS A N   
126  C CA  . HIS A 18  ? 0.14194 0.13606 0.13805 -0.00403 -0.01512 0.00023  18  HIS A CA  
127  C C   . HIS A 18  ? 0.11997 0.11692 0.11934 -0.00410 -0.01260 0.00029  18  HIS A C   
128  O O   . HIS A 18  ? 0.10183 0.09933 0.09913 -0.00431 -0.01079 0.00101  18  HIS A O   
129  C CB  . HIS A 18  ? 0.13272 0.12512 0.12732 -0.00353 -0.01675 0.00037  18  HIS A CB  
130  C CG  . HIS A 18  ? 0.11601 0.10880 0.10904 -0.00377 -0.01498 0.00101  18  HIS A CG  
131  N ND1 . HIS A 18  ? 0.12285 0.11400 0.11136 -0.00439 -0.01418 0.00180  18  HIS A ND1 
132  C CD2 . HIS A 18  ? 0.10331 0.09791 0.09887 -0.00353 -0.01384 0.00077  18  HIS A CD2 
133  C CE1 . HIS A 18  ? 0.12220 0.11434 0.11097 -0.00456 -0.01292 0.00194  18  HIS A CE1 
134  N NE2 . HIS A 18  ? 0.12183 0.11587 0.11440 -0.00399 -0.01277 0.00133  18  HIS A NE2 
135  N N   . ASP A 19  ? 0.10734 0.10592 0.11181 -0.00390 -0.01249 -0.00057 19  ASP A N   
136  C CA  . ASP A 19  ? 0.12823 0.12887 0.13541 -0.00398 -0.00980 -0.00058 19  ASP A CA  
137  C C   . ASP A 19  ? 0.09821 0.09890 0.10270 -0.00438 -0.00760 0.00043  19  ASP A C   
138  O O   . ASP A 19  ? 0.13717 0.13819 0.13938 -0.00423 -0.00617 0.00107  19  ASP A O   
139  C CB  . ASP A 19  ? 0.11197 0.11302 0.11900 -0.00351 -0.00939 -0.00069 19  ASP A CB  
140  C CG  . ASP A 19  ? 0.13581 0.13853 0.14537 -0.00352 -0.00661 -0.00099 19  ASP A CG  
141  O OD1 . ASP A 19  ? 0.11459 0.11823 0.12761 -0.00388 -0.00530 -0.00137 19  ASP A OD1 
142  O OD2 . ASP A 19  ? 0.13133 0.13415 0.13916 -0.00325 -0.00559 -0.00091 19  ASP A OD2 
143  N N   . ASN A 20  ? 0.11458 0.11472 0.11932 -0.00476 -0.00764 0.00047  20  ASN A N   
144  C CA  . ASN A 20  ? 0.11152 0.11131 0.11401 -0.00492 -0.00589 0.00140  20  ASN A CA  
145  C C   . ASN A 20  ? 0.09905 0.09891 0.10489 -0.00539 -0.00455 0.00116  20  ASN A C   
146  O O   . ASN A 20  ? 0.09977 0.09867 0.10592 -0.00572 -0.00519 0.00087  20  ASN A O   
147  C CB  . ASN A 20  ? 0.12506 0.12352 0.12395 -0.00494 -0.00694 0.00169  20  ASN A CB  
148  C CG  . ASN A 20  ? 0.11871 0.11715 0.11525 -0.00472 -0.00537 0.00262  20  ASN A CG  
149  O OD1 . ASN A 20  ? 0.12761 0.12577 0.12146 -0.00460 -0.00566 0.00285  20  ASN A OD1 
150  N ND2 . ASN A 20  ? 0.09941 0.09798 0.09706 -0.00462 -0.00367 0.00313  20  ASN A ND2 
151  N N   . PRO A 21  ? 0.09984 0.10050 0.10808 -0.00552 -0.00240 0.00121  21  PRO A N   
152  C CA  . PRO A 21  ? 0.12628 0.12665 0.13788 -0.00624 -0.00051 0.00106  21  PRO A CA  
153  C C   . PRO A 21  ? 0.10149 0.10005 0.11032 -0.00630 0.00047  0.00213  21  PRO A C   
154  O O   . PRO A 21  ? 0.10252 0.10028 0.11407 -0.00702 0.00112  0.00177  21  PRO A O   
155  C CB  . PRO A 21  ? 0.12327 0.12424 0.13605 -0.00630 0.00230  0.00125  21  PRO A CB  
156  C CG  . PRO A 21  ? 0.10067 0.10178 0.10897 -0.00543 0.00190  0.00187  21  PRO A CG  
157  C CD  . PRO A 21  ? 0.12661 0.12813 0.13436 -0.00513 -0.00130 0.00131  21  PRO A CD  
158  N N   . ALA A 22  ? 0.10165 0.09952 0.10564 -0.00555 0.00048  0.00329  22  ALA A N   
159  C CA  . ALA A 22  ? 0.10304 0.09918 0.10476 -0.00530 0.00108  0.00420  22  ALA A CA  
160  C C   . ALA A 22  ? 0.10275 0.09834 0.10515 -0.00559 -0.00066 0.00333  22  ALA A C   
161  O O   . ALA A 22  ? 0.11160 0.10564 0.11471 -0.00586 0.00000  0.00338  22  ALA A O   
162  C CB  . ALA A 22  ? 0.11318 0.10920 0.11045 -0.00424 0.00101  0.00529  22  ALA A CB  
163  N N   . LEU A 23  ? 0.11503 0.11139 0.11677 -0.00554 -0.00281 0.00252  23  LEU A N   
164  C CA  . LEU A 23  ? 0.13016 0.12544 0.13138 -0.00578 -0.00448 0.00160  23  LEU A CA  
165  C C   . LEU A 23  ? 0.10545 0.10043 0.11081 -0.00656 -0.00524 0.00031  23  LEU A C   
166  O O   . LEU A 23  ? 0.10471 0.09822 0.11027 -0.00689 -0.00562 -0.00036 23  LEU A O   
167  C CB  . LEU A 23  ? 0.10207 0.09748 0.10062 -0.00556 -0.00634 0.00126  23  LEU A CB  
168  C CG  . LEU A 23  ? 0.11398 0.10763 0.11052 -0.00576 -0.00813 0.00030  23  LEU A CG  
169  C CD1 . LEU A 23  ? 0.14959 0.14204 0.14387 -0.00559 -0.00703 0.00047  23  LEU A CD1 
170  C CD2 . LEU A 23  ? 0.14441 0.13756 0.13793 -0.00562 -0.00965 0.00026  23  LEU A CD2 
171  N N   . LEU A 24  ? 0.10983 0.10628 0.11899 -0.00686 -0.00549 -0.00031 24  LEU A N   
172  C CA  . LEU A 24  ? 0.11300 0.10978 0.12745 -0.00762 -0.00641 -0.00188 24  LEU A CA  
173  C C   . LEU A 24  ? 0.14170 0.13750 0.15865 -0.00844 -0.00408 -0.00176 24  LEU A C   
174  O O   . LEU A 24  ? 0.15972 0.15461 0.17899 -0.00909 -0.00509 -0.00302 24  LEU A O   
175  C CB  . LEU A 24  ? 0.14970 0.14866 0.16871 -0.00766 -0.00662 -0.00262 24  LEU A CB  
176  C CG  . LEU A 24  ? 0.17924 0.17875 0.19650 -0.00683 -0.00917 -0.00287 24  LEU A CG  
177  C CD1 . LEU A 24  ? 0.17216 0.17388 0.19494 -0.00673 -0.00912 -0.00379 24  LEU A CD1 
178  C CD2 . LEU A 24  ? 0.14692 0.14486 0.16223 -0.00661 -0.01271 -0.00385 24  LEU A CD2 
179  N N   . GLU A 25  ? 0.10448 0.10002 0.12066 -0.00841 -0.00100 -0.00026 25  GLU A N   
180  C CA  . GLU A 25  ? 0.13639 0.13013 0.15408 -0.00915 0.00154  0.00024  25  GLU A CA  
181  C C   . GLU A 25  ? 0.17284 0.16427 0.18746 -0.00885 0.00093  0.00049  25  GLU A C   
182  O O   . GLU A 25  ? 0.13688 0.12675 0.15409 -0.00968 0.00139  -0.00024 25  GLU A O   
183  C CB  . GLU A 25  ? 0.12232 0.11536 0.13789 -0.00889 0.00478  0.00209  25  GLU A CB  
184  C CG  . GLU A 25  ? 0.17594 0.16611 0.19184 -0.00956 0.00774  0.00309  25  GLU A CG  
185  C CD  . GLU A 25  ? 0.20667 0.19714 0.22949 -0.01128 0.00926  0.00171  25  GLU A CD  
186  O OE1 . GLU A 25  ? 0.22690 0.22013 0.25427 -0.01177 0.00895  0.00035  25  GLU A OE1 
187  O OE2 . GLU A 25  ? 0.16758 0.15554 0.19178 -0.01215 0.01079  0.00187  25  GLU A OE2 
188  N N   . ALA A 26  ? 0.15829 0.14948 0.16786 -0.00770 0.00000  0.00130  26  ALA A N   
189  C CA  . ALA A 26  ? 0.12779 0.11700 0.13476 -0.00726 -0.00038 0.00132  26  ALA A CA  
190  C C   . ALA A 26  ? 0.16930 0.15786 0.17773 -0.00790 -0.00250 -0.00070 26  ALA A C   
191  O O   . ALA A 26  ? 0.16422 0.15066 0.17233 -0.00800 -0.00229 -0.00118 26  ALA A O   
192  C CB  . ALA A 26  ? 0.10773 0.09748 0.11011 -0.00603 -0.00094 0.00216  26  ALA A CB  
193  N N   . CYS A 27  ? 0.17343 0.16347 0.18323 -0.00821 -0.00475 -0.00196 27  CYS A N   
194  C CA  . CYS A 27  ? 0.20447 0.19356 0.21478 -0.00862 -0.00738 -0.00397 27  CYS A CA  
195  C C   . CYS A 27  ? 0.19154 0.18070 0.20802 -0.00982 -0.00769 -0.00555 27  CYS A C   
196  O O   . CYS A 27  ? 0.17748 0.16529 0.19447 -0.01022 -0.00976 -0.00739 27  CYS A O   
197  C CB  . CYS A 27  ? 0.18187 0.17184 0.19015 -0.00817 -0.01015 -0.00455 27  CYS A CB  
198  S SG  . CYS A 27  ? 0.23237 0.22154 0.23338 -0.00718 -0.01012 -0.00338 27  CYS A SG  
199  N N   . LYS A 28  ? 0.14712 0.13770 0.16833 -0.01048 -0.00560 -0.00507 28  LYS A N   
200  C CA  . LYS A 28  ? 0.22616 0.21732 0.25451 -0.01185 -0.00562 -0.00681 28  LYS A CA  
201  C C   . LYS A 28  ? 0.21761 0.20600 0.24679 -0.01268 -0.00433 -0.00721 28  LYS A C   
202  O O   . LYS A 28  ? 0.18971 0.17623 0.21672 -0.01255 -0.00133 -0.00537 28  LYS A O   
203  C CB  . LYS A 28  ? 0.22566 0.21882 0.25862 -0.01244 -0.00286 -0.00613 28  LYS A CB  
204  C CG  . LYS A 28  ? 0.29367 0.28806 0.33538 -0.01404 -0.00245 -0.00815 28  LYS A CG  
205  C CD  . LYS A 28  ? 0.26529 0.26122 0.31053 -0.01401 -0.00707 -0.01088 28  LYS A CD  
206  C CE  . LYS A 28  ? 0.27934 0.27844 0.33430 -0.01503 -0.00699 -0.01283 28  LYS A CE  
207  N NZ  . LYS A 28  ? 0.29580 0.29443 0.35635 -0.01687 -0.00265 -0.01282 28  LYS A NZ  
208  N N   . ASP A 29  ? 0.18601 0.17382 0.21811 -0.01341 -0.00685 -0.00967 29  ASP A N   
209  C CA  . ASP A 29  ? 0.21897 0.20397 0.25249 -0.01435 -0.00604 -0.01060 29  ASP A CA  
210  C C   . ASP A 29  ? 0.20281 0.18483 0.22951 -0.01328 -0.00495 -0.00917 29  ASP A C   
211  O O   . ASP A 29  ? 0.18602 0.16532 0.21326 -0.01374 -0.00293 -0.00888 29  ASP A O   
212  C CB  . ASP A 29  ? 0.21173 0.19652 0.25156 -0.01593 -0.00248 -0.01026 29  ASP A CB  
213  C CG  . ASP A 29  ? 0.34135 0.32947 0.38932 -0.01709 -0.00312 -0.01202 29  ASP A CG  
214  O OD1 . ASP A 29  ? 0.29540 0.28528 0.34552 -0.01693 -0.00723 -0.01436 29  ASP A OD1 
215  O OD2 . ASP A 29  ? 0.46851 0.45734 0.52065 -0.01810 0.00050  -0.01113 29  ASP A OD2 
216  N N   . ALA A 30  ? 0.15390 0.13631 0.17457 -0.01185 -0.00619 -0.00837 30  ALA A N   
217  C CA  . ALA A 30  ? 0.16670 0.14700 0.18173 -0.01071 -0.00505 -0.00718 30  ALA A CA  
218  C C   . ALA A 30  ? 0.16471 0.14272 0.17693 -0.01059 -0.00710 -0.00924 30  ALA A C   
219  O O   . ALA A 30  ? 0.15253 0.13089 0.16368 -0.01069 -0.01010 -0.01095 30  ALA A O   
220  C CB  . ALA A 30  ? 0.13489 0.11691 0.14546 -0.00942 -0.00489 -0.00541 30  ALA A CB  
221  N N   . LYS A 31  ? 0.17598 0.15125 0.18667 -0.01025 -0.00551 -0.00911 31  LYS A N   
222  C CA  . LYS A 31  ? 0.14723 0.12002 0.15430 -0.00991 -0.00686 -0.01103 31  LYS A CA  
223  C C   . LYS A 31  ? 0.16093 0.13400 0.16195 -0.00851 -0.00662 -0.01020 31  LYS A C   
224  O O   . LYS A 31  ? 0.18847 0.16053 0.18538 -0.00834 -0.00838 -0.01171 31  LYS A O   
225  C CB  . LYS A 31  ? 0.23574 0.20528 0.24437 -0.01014 -0.00515 -0.01155 31  LYS A CB  
226  C CG  . LYS A 31  ? 0.22757 0.19417 0.23269 -0.00982 -0.00621 -0.01385 31  LYS A CG  
227  C CD  . LYS A 31  ? 0.27550 0.24143 0.28144 -0.01096 -0.00950 -0.01682 31  LYS A CD  
228  C CE  . LYS A 31  ? 0.36999 0.33206 0.37293 -0.01087 -0.01009 -0.01934 31  LYS A CE  
229  N NZ  . LYS A 31  ? 0.36921 0.33022 0.37153 -0.01172 -0.01390 -0.02245 31  LYS A NZ  
230  N N   . HIS A 32  ? 0.16996 0.14418 0.17028 -0.00753 -0.00445 -0.00791 32  HIS A N   
231  C CA  . HIS A 32  ? 0.21523 0.19043 0.21120 -0.00636 -0.00399 -0.00713 32  HIS A CA  
232  C C   . HIS A 32  ? 0.18957 0.16768 0.18629 -0.00592 -0.00321 -0.00486 32  HIS A C   
233  O O   . HIS A 32  ? 0.21255 0.19089 0.21194 -0.00588 -0.00187 -0.00342 32  HIS A O   
234  C CB  . HIS A 32  ? 0.28428 0.25768 0.27878 -0.00524 -0.00218 -0.00719 32  HIS A CB  
235  C CG  . HIS A 32  ? 0.24311 0.21321 0.23697 -0.00557 -0.00252 -0.00950 32  HIS A CG  
236  N ND1 . HIS A 32  ? 0.24184 0.21053 0.23143 -0.00565 -0.00351 -0.01148 32  HIS A ND1 
237  C CD2 . HIS A 32  ? 0.27997 0.24744 0.27650 -0.00584 -0.00187 -0.01021 32  HIS A CD2 
238  C CE1 . HIS A 32  ? 0.26238 0.22791 0.25202 -0.00591 -0.00362 -0.01349 32  HIS A CE1 
239  N NE2 . HIS A 32  ? 0.31992 0.28473 0.31408 -0.00606 -0.00267 -0.01279 32  HIS A NE2 
240  N N   . VAL A 33  ? 0.21471 0.19455 0.20861 -0.00563 -0.00390 -0.00455 33  VAL A N   
241  C CA  . VAL A 33  ? 0.19755 0.18005 0.19170 -0.00517 -0.00330 -0.00270 33  VAL A CA  
242  C C   . VAL A 33  ? 0.15177 0.13505 0.14309 -0.00419 -0.00240 -0.00229 33  VAL A C   
243  O O   . VAL A 33  ? 0.17464 0.15706 0.16291 -0.00430 -0.00272 -0.00343 33  VAL A O   
244  C CB  . VAL A 33  ? 0.17972 0.16383 0.17422 -0.00586 -0.00499 -0.00278 33  VAL A CB  
245  C CG1 . VAL A 33  ? 0.11148 0.09805 0.10591 -0.00538 -0.00429 -0.00110 33  VAL A CG1 
246  C CG2 . VAL A 33  ? 0.15153 0.13547 0.15024 -0.00684 -0.00576 -0.00348 33  VAL A CG2 
247  N N   . TYR A 34  ? 0.17190 0.15663 0.16419 -0.00326 -0.00126 -0.00078 34  TYR A N   
248  C CA  . TYR A 34  ? 0.12660 0.11265 0.11767 -0.00229 -0.00046 -0.00057 34  TYR A CA  
249  C C   . TYR A 34  ? 0.13753 0.12629 0.12844 -0.00225 -0.00081 0.00052  34  TYR A C   
250  O O   . TYR A 34  ? 0.14474 0.13449 0.13686 -0.00161 -0.00063 0.00185  34  TYR A O   
251  C CB  . TYR A 34  ? 0.13757 0.12297 0.13017 -0.00091 0.00063  -0.00004 34  TYR A CB  
252  C CG  . TYR A 34  ? 0.20534 0.18786 0.19817 -0.00078 0.00119  -0.00131 34  TYR A CG  
253  C CD1 . TYR A 34  ? 0.16542 0.14553 0.15957 -0.00134 0.00110  -0.00130 34  TYR A CD1 
254  C CD2 . TYR A 34  ? 0.15594 0.13806 0.14793 -0.00018 0.00206  -0.00269 34  TYR A CD2 
255  C CE1 . TYR A 34  ? 0.14984 0.12707 0.14431 -0.00128 0.00155  -0.00264 34  TYR A CE1 
256  C CE2 . TYR A 34  ? 0.13801 0.11726 0.13005 0.00000  0.00265  -0.00407 34  TYR A CE2 
257  C CZ  . TYR A 34  ? 0.21997 0.19670 0.21317 -0.00053 0.00224  -0.00404 34  TYR A CZ  
258  O OH  . TYR A 34  ? 0.20657 0.18020 0.19995 -0.00042 0.00276  -0.00559 34  TYR A OH  
259  N N   . PRO A 35  ? 0.15210 0.14163 0.14107 -0.00291 -0.00130 0.00002  35  PRO A N   
260  C CA  . PRO A 35  ? 0.17026 0.16214 0.15922 -0.00292 -0.00154 0.00087  35  PRO A CA  
261  C C   . PRO A 35  ? 0.10748 0.10115 0.09721 -0.00203 -0.00057 0.00094  35  PRO A C   
262  O O   . PRO A 35  ? 0.11710 0.11056 0.10613 -0.00209 0.00039  -0.00005 35  PRO A O   
263  C CB  . PRO A 35  ? 0.11281 0.10394 0.09916 -0.00395 -0.00235 0.00023  35  PRO A CB  
264  C CG  . PRO A 35  ? 0.12240 0.11081 0.10732 -0.00441 -0.00299 -0.00089 35  PRO A CG  
265  C CD  . PRO A 35  ? 0.15958 0.14720 0.14575 -0.00375 -0.00182 -0.00131 35  PRO A CD  
266  N N   . VAL A 36  ? 0.10577 0.10115 0.09700 -0.00121 -0.00082 0.00197  36  VAL A N   
267  C CA  . VAL A 36  ? 0.13614 0.13328 0.12906 0.00002  -0.00047 0.00194  36  VAL A CA  
268  C C   . VAL A 36  ? 0.11350 0.11316 0.10688 0.00008  -0.00118 0.00235  36  VAL A C   
269  O O   . VAL A 36  ? 0.10301 0.10267 0.09555 -0.00011 -0.00191 0.00323  36  VAL A O   
270  C CB  . VAL A 36  ? 0.12809 0.12403 0.12205 0.00149  -0.00054 0.00271  36  VAL A CB  
271  C CG1 . VAL A 36  ? 0.17820 0.17613 0.17396 0.00312  -0.00107 0.00291  36  VAL A CG1 
272  C CG2 . VAL A 36  ? 0.17808 0.17171 0.17221 0.00155  0.00033  0.00186  36  VAL A CG2 
273  N N   . PHE A 37  ? 0.10544 0.10724 0.10046 0.00024  -0.00080 0.00150  37  PHE A N   
274  C CA  . PHE A 37  ? 0.11864 0.12311 0.11515 0.00061  -0.00166 0.00153  37  PHE A CA  
275  C C   . PHE A 37  ? 0.12657 0.13287 0.12637 0.00220  -0.00187 0.00092  37  PHE A C   
276  O O   . PHE A 37  ? 0.12440 0.13097 0.12599 0.00226  -0.00055 -0.00019 37  PHE A O   
277  C CB  . PHE A 37  ? 0.10134 0.10692 0.09771 -0.00095 -0.00108 0.00077  37  PHE A CB  
278  C CG  . PHE A 37  ? 0.10498 0.11305 0.10286 -0.00087 -0.00214 0.00065  37  PHE A CG  
279  C CD1 . PHE A 37  ? 0.14927 0.16021 0.15090 -0.00033 -0.00222 -0.00044 37  PHE A CD1 
280  C CD2 . PHE A 37  ? 0.09941 0.10703 0.09538 -0.00133 -0.00311 0.00135  37  PHE A CD2 
281  C CE1 . PHE A 37  ? 0.13524 0.14846 0.13846 -0.00032 -0.00351 -0.00085 37  PHE A CE1 
282  C CE2 . PHE A 37  ? 0.09881 0.10841 0.09586 -0.00128 -0.00415 0.00100  37  PHE A CE2 
283  C CZ  . PHE A 37  ? 0.11574 0.12808 0.11630 -0.00081 -0.00449 -0.00011 37  PHE A CZ  
284  N N   . VAL A 38  ? 0.12714 0.13445 0.12757 0.00362  -0.00358 0.00154  38  VAL A N   
285  C CA  . VAL A 38  ? 0.10427 0.11321 0.10795 0.00558  -0.00457 0.00102  38  VAL A CA  
286  C C   . VAL A 38  ? 0.13143 0.14418 0.13849 0.00538  -0.00536 -0.00030 38  VAL A C   
287  O O   . VAL A 38  ? 0.17325 0.18675 0.17910 0.00519  -0.00679 0.00002  38  VAL A O   
288  C CB  . VAL A 38  ? 0.14383 0.15075 0.14540 0.00751  -0.00631 0.00258  38  VAL A CB  
289  C CG1 . VAL A 38  ? 0.16089 0.16937 0.16577 0.00987  -0.00800 0.00203  38  VAL A CG1 
290  C CG2 . VAL A 38  ? 0.14442 0.14750 0.14346 0.00742  -0.00513 0.00371  38  VAL A CG2 
291  N N   . LEU A 39  ? 0.13187 0.14696 0.14338 0.00529  -0.00420 -0.00197 39  LEU A N   
292  C CA  . LEU A 39  ? 0.15860 0.17758 0.17464 0.00476  -0.00441 -0.00362 39  LEU A CA  
293  C C   . LEU A 39  ? 0.18291 0.20464 0.20408 0.00713  -0.00641 -0.00462 39  LEU A C   
294  O O   . LEU A 39  ? 0.28984 0.31111 0.31293 0.00860  -0.00598 -0.00488 39  LEU A O   
295  C CB  . LEU A 39  ? 0.22595 0.24560 0.24379 0.00275  -0.00119 -0.00499 39  LEU A CB  
296  C CG  . LEU A 39  ? 0.26784 0.29091 0.29007 0.00133  -0.00042 -0.00667 39  LEU A CG  
297  C CD1 . LEU A 39  ? 0.33931 0.36077 0.35758 -0.00085 0.00010  -0.00594 39  LEU A CD1 
298  C CD2 . LEU A 39  ? 0.32152 0.34598 0.34791 0.00056  0.00281  -0.00846 39  LEU A CD2 
299  N N   . ASP A 40  ? 0.28106 0.30552 0.30455 0.00761  -0.00880 -0.00532 40  ASP A N   
300  C CA  . ASP A 40  ? 0.38659 0.41414 0.41566 0.00994  -0.01133 -0.00661 40  ASP A CA  
301  C C   . ASP A 40  ? 0.33352 0.36570 0.37057 0.00885  -0.00974 -0.00932 40  ASP A C   
302  O O   . ASP A 40  ? 0.40073 0.43535 0.44000 0.00729  -0.00994 -0.01045 40  ASP A O   
303  C CB  . ASP A 40  ? 0.39698 0.42475 0.42399 0.01124  -0.01526 -0.00613 40  ASP A CB  
304  C CG  . ASP A 40  ? 0.44513 0.47601 0.47775 0.01388  -0.01868 -0.00759 40  ASP A CG  
305  O OD1 . ASP A 40  ? 0.45592 0.48592 0.48986 0.01616  -0.01936 -0.00727 40  ASP A OD1 
306  O OD2 . ASP A 40  ? 0.44844 0.48253 0.48431 0.01376  -0.02092 -0.00917 40  ASP A OD2 
307  N N   . PRO A 41  ? 0.39750 0.43089 0.43929 0.00956  -0.00791 -0.01054 41  PRO A N   
308  C CA  . PRO A 41  ? 0.42507 0.46269 0.47463 0.00820  -0.00541 -0.01322 41  PRO A CA  
309  C C   . PRO A 41  ? 0.48126 0.52411 0.53884 0.00926  -0.00832 -0.01540 41  PRO A C   
310  O O   . PRO A 41  ? 0.52207 0.56884 0.58703 0.00784  -0.00612 -0.01785 41  PRO A O   
311  C CB  . PRO A 41  ? 0.37872 0.41582 0.43079 0.00925  -0.00298 -0.01393 41  PRO A CB  
312  C CG  . PRO A 41  ? 0.38323 0.41763 0.43214 0.01224  -0.00608 -0.01223 41  PRO A CG  
313  C CD  . PRO A 41  ? 0.39512 0.42593 0.43563 0.01166  -0.00785 -0.00966 41  PRO A CD  
314  N N   . HIS A 42  ? 0.47698 0.51985 0.53333 0.01165  -0.01313 -0.01472 42  HIS A N   
315  C CA  . HIS A 42  ? 0.48543 0.53306 0.54898 0.01290  -0.01677 -0.01693 42  HIS A CA  
316  C C   . HIS A 42  ? 0.49144 0.53878 0.55119 0.01195  -0.01939 -0.01653 42  HIS A C   
317  O O   . HIS A 42  ? 0.55712 0.60700 0.62005 0.01363  -0.02378 -0.01780 42  HIS A O   
318  C CB  . HIS A 42  ? 0.51268 0.56056 0.57831 0.01697  -0.02090 -0.01690 42  HIS A CB  
319  C CG  . HIS A 42  ? 0.55828 0.60647 0.62828 0.01824  -0.01859 -0.01755 42  HIS A CG  
320  N ND1 . HIS A 42  ? 0.50123 0.55476 0.58242 0.01896  -0.01806 -0.02068 42  HIS A ND1 
321  C CD2 . HIS A 42  ? 0.44859 0.49240 0.51363 0.01890  -0.01656 -0.01571 42  HIS A CD2 
322  C CE1 . HIS A 42  ? 0.58266 0.63495 0.66526 0.02012  -0.01572 -0.02070 42  HIS A CE1 
323  N NE2 . HIS A 42  ? 0.52087 0.56717 0.59361 0.02007  -0.01487 -0.01772 42  HIS A NE2 
324  N N   . PHE A 43  ? 0.38526 0.42944 0.43832 0.00940  -0.01698 -0.01497 43  PHE A N   
325  C CA  . PHE A 43  ? 0.49519 0.53843 0.54387 0.00868  -0.01931 -0.01448 43  PHE A CA  
326  C C   . PHE A 43  ? 0.62248 0.67050 0.67869 0.00731  -0.02026 -0.01740 43  PHE A C   
327  O O   . PHE A 43  ? 0.59523 0.64418 0.65109 0.00823  -0.02429 -0.01812 43  PHE A O   
328  C CB  . PHE A 43  ? 0.54525 0.58425 0.58614 0.00635  -0.01636 -0.01238 43  PHE A CB  
329  C CG  . PHE A 43  ? 0.61631 0.65282 0.65053 0.00650  -0.01881 -0.01115 43  PHE A CG  
330  C CD1 . PHE A 43  ? 0.56356 0.59646 0.59100 0.00861  -0.02076 -0.00899 43  PHE A CD1 
331  C CD2 . PHE A 43  ? 0.55942 0.59688 0.59406 0.00447  -0.01886 -0.01220 43  PHE A CD2 
332  C CE1 . PHE A 43  ? 0.55433 0.58476 0.57544 0.00870  -0.02250 -0.00800 43  PHE A CE1 
333  C CE2 . PHE A 43  ? 0.54456 0.57963 0.57306 0.00468  -0.02089 -0.01130 43  PHE A CE2 
334  C CZ  . PHE A 43  ? 0.60146 0.63308 0.62313 0.00680  -0.02260 -0.00924 43  PHE A CZ  
335  N N   . LEU A 44  ? 0.56930 0.62012 0.63220 0.00501  -0.01649 -0.01919 44  LEU A N   
336  C CA  . LEU A 44  ? 0.53214 0.58761 0.60324 0.00342  -0.01697 -0.02216 44  LEU A CA  
337  C C   . LEU A 44  ? 0.60079 0.66118 0.68044 0.00608  -0.02130 -0.02466 44  LEU A C   
338  O O   . LEU A 44  ? 0.61790 0.68172 0.70277 0.00570  -0.02410 -0.02698 44  LEU A O   
339  C CB  . LEU A 44  ? 0.49482 0.55159 0.57085 0.00024  -0.01129 -0.02339 44  LEU A CB  
340  C CG  . LEU A 44  ? 0.41840 0.47135 0.48822 -0.00303 -0.00789 -0.02198 44  LEU A CG  
341  C CD1 . LEU A 44  ? 0.33257 0.38656 0.40737 -0.00603 -0.00236 -0.02334 44  LEU A CD1 
342  C CD2 . LEU A 44  ? 0.41093 0.46403 0.47956 -0.00381 -0.01090 -0.02249 44  LEU A CD2 
343  N N   . GLN A 45  ? 0.62352 0.68422 0.70486 0.00887  -0.02217 -0.02435 45  GLN A N   
344  C CA  . GLN A 45  ? 0.62468 0.68971 0.71403 0.01197  -0.02679 -0.02658 45  GLN A CA  
345  C C   . GLN A 45  ? 0.64152 0.70349 0.72331 0.01508  -0.03274 -0.02490 45  GLN A C   
346  O O   . GLN A 45  ? 0.61753 0.67736 0.69652 0.01834  -0.03512 -0.02349 45  GLN A O   
347  C CB  . GLN A 45  ? 0.64511 0.71158 0.74003 0.01365  -0.02486 -0.02715 45  GLN A CB  
348  C CG  . GLN A 45  ? 0.59747 0.66369 0.69399 0.01061  -0.01785 -0.02732 45  GLN A CG  
349  C CD  . GLN A 45  ? 0.58267 0.65015 0.68457 0.01240  -0.01585 -0.02816 45  GLN A CD  
350  O OE1 . GLN A 45  ? 0.56513 0.62818 0.66032 0.01344  -0.01450 -0.02586 45  GLN A OE1 
351  N NE2 . GLN A 45  ? 0.57947 0.65310 0.69405 0.01274  -0.01557 -0.03169 45  GLN A NE2 
352  N N   . GLN A 46  ? 0.64247 0.70376 0.72047 0.01399  -0.03495 -0.02505 46  GLN A N   
353  C CA  . GLN A 46  ? 0.67245 0.73042 0.74232 0.01657  -0.04025 -0.02365 46  GLN A CA  
354  C C   . GLN A 46  ? 0.51699 0.57863 0.59156 0.01687  -0.04512 -0.02664 46  GLN A C   
355  O O   . GLN A 46  ? 0.50115 0.56287 0.57448 0.01427  -0.04438 -0.02743 46  GLN A O   
356  C CB  . GLN A 46  ? 0.61569 0.66758 0.67332 0.01516  -0.03810 -0.02044 46  GLN A CB  
357  C CG  . GLN A 46  ? 0.59427 0.64143 0.64514 0.01610  -0.03551 -0.01719 46  GLN A CG  
358  C CD  . GLN A 46  ? 0.57715 0.61929 0.61813 0.01419  -0.03275 -0.01454 46  GLN A CD  
359  O OE1 . GLN A 46  ? 0.58106 0.62327 0.62052 0.01200  -0.03219 -0.01511 46  GLN A OE1 
360  N NE2 . GLN A 46  ? 0.56760 0.60538 0.60235 0.01502  -0.03102 -0.01178 46  GLN A NE2 
361  N N   . LYS A 50  ? 0.27802 0.33375 0.34398 -0.00240 -0.02886 -0.02777 50  LYS A N   
362  C CA  . LYS A 50  ? 0.29589 0.34653 0.35054 -0.00054 -0.02967 -0.02459 50  LYS A CA  
363  C C   . LYS A 50  ? 0.32758 0.37390 0.37617 -0.00275 -0.02498 -0.02212 50  LYS A C   
364  O O   . LYS A 50  ? 0.35072 0.39344 0.39216 -0.00301 -0.02533 -0.02094 50  LYS A O   
365  C CB  . LYS A 50  ? 0.21453 0.26510 0.26795 0.00255  -0.03091 -0.02313 50  LYS A CB  
366  N N   . VAL A 51  ? 0.31054 0.35710 0.36194 -0.00422 -0.02067 -0.02147 51  VAL A N   
367  C CA  . VAL A 51  ? 0.27506 0.31741 0.32087 -0.00612 -0.01648 -0.01919 51  VAL A CA  
368  C C   . VAL A 51  ? 0.21303 0.25655 0.26462 -0.00926 -0.01248 -0.02047 51  VAL A C   
369  O O   . VAL A 51  ? 0.27623 0.32326 0.33521 -0.00958 -0.01106 -0.02202 51  VAL A O   
370  C CB  . VAL A 51  ? 0.37165 0.41161 0.41276 -0.00464 -0.01496 -0.01664 51  VAL A CB  
371  C CG1 . VAL A 51  ? 0.27638 0.31191 0.31151 -0.00641 -0.01141 -0.01448 51  VAL A CG1 
372  C CG2 . VAL A 51  ? 0.45832 0.49696 0.49421 -0.00158 -0.01859 -0.01537 51  VAL A CG2 
373  N N   . SER A 52  ? 0.21130 0.25166 0.25962 -0.01156 -0.01054 -0.01988 52  SER A N   
374  C CA  A SER A 52  ? 0.14041 0.18054 0.19267 -0.01471 -0.00634 -0.02066 52  SER A CA  
375  C CA  B SER A 52  ? 0.13971 0.17989 0.19204 -0.01470 -0.00635 -0.02068 52  SER A CA  
376  C C   . SER A 52  ? 0.13413 0.17111 0.18240 -0.01531 -0.00222 -0.01849 52  SER A C   
377  O O   . SER A 52  ? 0.15846 0.19254 0.19987 -0.01376 -0.00263 -0.01617 52  SER A O   
378  C CB  A SER A 52  ? 0.10490 0.14214 0.15484 -0.01683 -0.00600 -0.02079 52  SER A CB  
379  C CB  B SER A 52  ? 0.10496 0.14234 0.15516 -0.01686 -0.00600 -0.02087 52  SER A CB  
380  O OG  A SER A 52  ? 0.12399 0.15953 0.17596 -0.01992 -0.00149 -0.02091 52  SER A OG  
381  O OG  B SER A 52  ? 0.10287 0.13498 0.14407 -0.01666 -0.00523 -0.01812 52  SER A OG  
382  N N   . VAL A 53  ? 0.10228 0.13966 0.15486 -0.01771 0.00192  -0.01938 53  VAL A N   
383  C CA  . VAL A 53  ? 0.13586 0.16959 0.18376 -0.01845 0.00597  -0.01748 53  VAL A CA  
384  C C   . VAL A 53  ? 0.12225 0.14989 0.16081 -0.01908 0.00643  -0.01492 53  VAL A C   
385  O O   . VAL A 53  ? 0.12728 0.15138 0.15966 -0.01861 0.00785  -0.01289 53  VAL A O   
386  C CB  . VAL A 53  ? 0.16413 0.19888 0.21785 -0.02112 0.01081  -0.01901 53  VAL A CB  
387  C CG1 . VAL A 53  ? 0.17201 0.20467 0.22651 -0.02416 0.01257  -0.01956 53  VAL A CG1 
388  C CG2 . VAL A 53  ? 0.20009 0.23114 0.24852 -0.02145 0.01477  -0.01730 53  VAL A CG2 
389  N N   . ASN A 54  ? 0.10543 0.13179 0.14308 -0.01999 0.00494  -0.01515 54  ASN A N   
390  C CA  . ASN A 54  ? 0.11352 0.13422 0.14326 -0.02049 0.00521  -0.01297 54  ASN A CA  
391  C C   . ASN A 54  ? 0.10512 0.12434 0.12867 -0.01792 0.00273  -0.01105 54  ASN A C   
392  O O   . ASN A 54  ? 0.13344 0.14860 0.15097 -0.01783 0.00397  -0.00903 54  ASN A O   
393  C CB  . ASN A 54  ? 0.11109 0.13113 0.14207 -0.02174 0.00388  -0.01402 54  ASN A CB  
394  C CG  . ASN A 54  ? 0.12883 0.14713 0.16276 -0.02499 0.00752  -0.01484 54  ASN A CG  
395  O OD1 . ASN A 54  ? 0.12105 0.13655 0.15299 -0.02639 0.01136  -0.01378 54  ASN A OD1 
396  N ND2 . ASN A 54  ? 0.11227 0.13179 0.15058 -0.02630 0.00645  -0.01676 54  ASN A ND2 
397  N N   . ARG A 55  ? 0.10288 0.12510 0.12768 -0.01581 -0.00081 -0.01169 55  ARG A N   
398  C CA  . ARG A 55  ? 0.11728 0.13782 0.13637 -0.01362 -0.00266 -0.00986 55  ARG A CA  
399  C C   . ARG A 55  ? 0.13462 0.15548 0.15294 -0.01244 -0.00163 -0.00892 55  ARG A C   
400  O O   . ARG A 55  ? 0.12249 0.14043 0.13556 -0.01168 -0.00144 -0.00709 55  ARG A O   
401  C CB  . ARG A 55  ? 0.14805 0.17069 0.16739 -0.01177 -0.00638 -0.01063 55  ARG A CB  
402  C CG  . ARG A 55  ? 0.14018 0.16064 0.15354 -0.00981 -0.00766 -0.00871 55  ARG A CG  
403  C CD  . ARG A 55  ? 0.14944 0.17059 0.16121 -0.00825 -0.01075 -0.00925 55  ARG A CD  
404  N NE  . ARG A 55  ? 0.20234 0.22688 0.21722 -0.00665 -0.01305 -0.01040 55  ARG A NE  
405  C CZ  . ARG A 55  ? 0.19199 0.21941 0.21128 -0.00682 -0.01501 -0.01267 55  ARG A CZ  
406  N NH1 . ARG A 55  ? 0.18562 0.21293 0.20680 -0.00870 -0.01473 -0.01408 55  ARG A NH1 
407  N NH2 . ARG A 55  ? 0.17017 0.20050 0.19220 -0.00500 -0.01752 -0.01363 55  ARG A NH2 
408  N N   . TYR A 56  ? 0.11379 0.13822 0.13777 -0.01226 -0.00100 -0.01034 56  TYR A N   
409  C CA  . TYR A 56  ? 0.15412 0.17871 0.17760 -0.01102 0.00001  -0.00965 56  TYR A CA  
410  C C   . TYR A 56  ? 0.10172 0.12255 0.12140 -0.01255 0.00357  -0.00853 56  TYR A C   
411  O O   . TYR A 56  ? 0.10319 0.12183 0.11870 -0.01156 0.00386  -0.00717 56  TYR A O   
412  C CB  . TYR A 56  ? 0.11538 0.14475 0.14645 -0.01029 -0.00015 -0.01167 56  TYR A CB  
413  C CG  . TYR A 56  ? 0.13580 0.16561 0.16630 -0.00803 -0.00071 -0.01100 56  TYR A CG  
414  C CD1 . TYR A 56  ? 0.20766 0.23840 0.23729 -0.00547 -0.00429 -0.01056 56  TYR A CD1 
415  C CD2 . TYR A 56  ? 0.14176 0.17041 0.17191 -0.00844 0.00245  -0.01077 56  TYR A CD2 
416  C CE1 . TYR A 56  ? 0.29438 0.32489 0.32331 -0.00342 -0.00473 -0.00982 56  TYR A CE1 
417  C CE2 . TYR A 56  ? 0.28855 0.31728 0.31828 -0.00637 0.00194  -0.01028 56  TYR A CE2 
418  C CZ  . TYR A 56  ? 0.37082 0.40045 0.40013 -0.00388 -0.00166 -0.00975 56  TYR A CZ  
419  O OH  . TYR A 56  ? 0.41191 0.44107 0.44071 -0.00185 -0.00211 -0.00915 56  TYR A OH  
420  N N   . ASN A 57  ? 0.11480 0.13441 0.13549 -0.01498 0.00629  -0.00910 57  ASN A N   
421  C CA  . ASN A 57  ? 0.12520 0.14011 0.14062 -0.01638 0.00948  -0.00783 57  ASN A CA  
422  C C   . ASN A 57  ? 0.14402 0.15436 0.15194 -0.01595 0.00800  -0.00574 57  ASN A C   
423  O O   . ASN A 57  ? 0.14045 0.14726 0.14312 -0.01581 0.00901  -0.00446 57  ASN A O   
424  C CB  . ASN A 57  ? 0.23744 0.25130 0.25498 -0.01918 0.01295  -0.00872 57  ASN A CB  
425  C CG  . ASN A 57  ? 0.21950 0.22800 0.23086 -0.02056 0.01654  -0.00745 57  ASN A CG  
426  O OD1 . ASN A 57  ? 0.20138 0.21008 0.21298 -0.02050 0.01899  -0.00785 57  ASN A OD1 
427  N ND2 . ASN A 57  ? 0.21332 0.21666 0.21877 -0.02168 0.01679  -0.00595 57  ASN A ND2 
428  N N   . PHE A 58  ? 0.11990 0.13029 0.12747 -0.01566 0.00551  -0.00558 58  PHE A N   
429  C CA  . PHE A 58  ? 0.13456 0.14140 0.13628 -0.01488 0.00386  -0.00388 58  PHE A CA  
430  C C   . PHE A 58  ? 0.11476 0.12187 0.11437 -0.01289 0.00256  -0.00299 58  PHE A C   
431  O O   . PHE A 58  ? 0.14023 0.14394 0.13508 -0.01263 0.00251  -0.00168 58  PHE A O   
432  C CB  . PHE A 58  ? 0.10552 0.11307 0.10809 -0.01462 0.00152  -0.00426 58  PHE A CB  
433  C CG  . PHE A 58  ? 0.10621 0.11009 0.10379 -0.01411 0.00029  -0.00284 58  PHE A CG  
434  C CD1 . PHE A 58  ? 0.14187 0.14608 0.13760 -0.01227 -0.00154 -0.00208 58  PHE A CD1 
435  C CD2 . PHE A 58  ? 0.13298 0.13295 0.12808 -0.01546 0.00104  -0.00233 58  PHE A CD2 
436  C CE1 . PHE A 58  ? 0.12305 0.12441 0.11539 -0.01179 -0.00257 -0.00108 58  PHE A CE1 
437  C CE2 . PHE A 58  ? 0.11381 0.11063 0.10509 -0.01473 -0.00036 -0.00121 58  PHE A CE2 
438  C CZ  . PHE A 58  ? 0.10756 0.10540 0.09788 -0.01289 -0.00216 -0.00071 58  PHE A CZ  
439  N N   . LEU A 59  ? 0.11138 0.12229 0.11457 -0.01145 0.00138  -0.00374 59  LEU A N   
440  C CA  . LEU A 59  ? 0.10114 0.11201 0.10262 -0.00968 0.00044  -0.00289 59  LEU A CA  
441  C C   . LEU A 59  ? 0.10407 0.11312 0.10385 -0.01003 0.00265  -0.00262 59  LEU A C   
442  O O   . LEU A 59  ? 0.13993 0.14645 0.13584 -0.00946 0.00233  -0.00157 59  LEU A O   
443  C CB  . LEU A 59  ? 0.09927 0.11393 0.10458 -0.00799 -0.00129 -0.00367 59  LEU A CB  
444  C CG  . LEU A 59  ? 0.09865 0.11333 0.10315 -0.00619 -0.00184 -0.00297 59  LEU A CG  
445  C CD1 . LEU A 59  ? 0.09840 0.11042 0.09839 -0.00550 -0.00284 -0.00143 59  LEU A CD1 
446  C CD2 . LEU A 59  ? 0.11502 0.13306 0.12336 -0.00449 -0.00364 -0.00380 59  LEU A CD2 
447  N N   . LEU A 60  ? 0.10413 0.11447 0.10697 -0.01102 0.00500  -0.00378 60  LEU A N   
448  C CA  . LEU A 60  ? 0.12092 0.12932 0.12181 -0.01138 0.00749  -0.00379 60  LEU A CA  
449  C C   . LEU A 60  ? 0.11012 0.11320 0.10422 -0.01253 0.00844  -0.00256 60  LEU A C   
450  O O   . LEU A 60  ? 0.13161 0.13205 0.12173 -0.01207 0.00872  -0.00201 60  LEU A O   
451  C CB  . LEU A 60  ? 0.10771 0.11854 0.11362 -0.01243 0.01034  -0.00549 60  LEU A CB  
452  C CG  . LEU A 60  ? 0.14747 0.16359 0.16057 -0.01092 0.00916  -0.00695 60  LEU A CG  
453  C CD1 . LEU A 60  ? 0.17092 0.18986 0.19023 -0.01215 0.01215  -0.00897 60  LEU A CD1 
454  C CD2 . LEU A 60  ? 0.11605 0.13214 0.12820 -0.00879 0.00809  -0.00649 60  LEU A CD2 
455  N N   . GLU A 61  ? 0.11179 0.11294 0.10436 -0.01393 0.00868  -0.00219 61  GLU A N   
456  C CA  . GLU A 61  ? 0.17137 0.16699 0.15709 -0.01467 0.00890  -0.00086 61  GLU A CA  
457  C C   . GLU A 61  ? 0.11429 0.10864 0.09705 -0.01313 0.00584  0.00021  61  GLU A C   
458  O O   . GLU A 61  ? 0.15129 0.14161 0.12873 -0.01307 0.00555  0.00102  61  GLU A O   
459  C CB  . GLU A 61  ? 0.12879 0.12239 0.11383 -0.01627 0.00950  -0.00060 61  GLU A CB  
460  C CG  . GLU A 61  ? 0.18750 0.18091 0.17442 -0.01833 0.01325  -0.00150 61  GLU A CG  
461  C CD  . GLU A 61  ? 0.13702 0.12851 0.12403 -0.02000 0.01380  -0.00133 61  GLU A CD  
462  O OE1 . GLU A 61  ? 0.13330 0.12351 0.11863 -0.01936 0.01112  -0.00052 61  GLU A OE1 
463  O OE2 . GLU A 61  ? 0.14302 0.13425 0.13213 -0.02200 0.01710  -0.00212 61  GLU A OE2 
464  N N   . SER A 62  ? 0.10996 0.10755 0.09604 -0.01191 0.00359  0.00011  62  SER A N   
465  C CA  . SER A 62  ? 0.10847 0.10529 0.09275 -0.01059 0.00124  0.00092  62  SER A CA  
466  C C   . SER A 62  ? 0.11370 0.11044 0.09725 -0.00968 0.00135  0.00091  62  SER A C   
467  O O   . SER A 62  ? 0.10914 0.10369 0.08995 -0.00918 0.00008  0.00148  62  SER A O   
468  C CB  . SER A 62  ? 0.10481 0.10472 0.09233 -0.00964 -0.00056 0.00077  62  SER A CB  
469  O OG  . SER A 62  ? 0.10525 0.10483 0.09319 -0.01044 -0.00087 0.00061  62  SER A OG  
470  N N   . LEU A 63  ? 0.15521 0.15434 0.14165 -0.00945 0.00276  0.00008  63  LEU A N   
471  C CA  . LEU A 63  ? 0.16891 0.16758 0.15471 -0.00862 0.00313  -0.00009 63  LEU A CA  
472  C C   . LEU A 63  ? 0.19036 0.18501 0.17132 -0.00953 0.00469  -0.00016 63  LEU A C   
473  O O   . LEU A 63  ? 0.17114 0.16354 0.14921 -0.00902 0.00388  0.00001  63  LEU A O   
474  C CB  . LEU A 63  ? 0.14490 0.14716 0.13551 -0.00784 0.00403  -0.00106 63  LEU A CB  
475  C CG  . LEU A 63  ? 0.10966 0.11529 0.10404 -0.00657 0.00209  -0.00096 63  LEU A CG  
476  C CD1 . LEU A 63  ? 0.10210 0.11102 0.10128 -0.00561 0.00258  -0.00203 63  LEU A CD1 
477  C CD2 . LEU A 63  ? 0.10182 0.10641 0.09452 -0.00544 0.00030  0.00006  63  LEU A CD2 
478  N N   . GLU A 64  ? 0.13629 0.12962 0.11598 -0.01097 0.00695  -0.00046 64  GLU A N   
479  C CA  . GLU A 64  ? 0.17734 0.16585 0.15090 -0.01189 0.00858  -0.00035 64  GLU A CA  
480  C C   . GLU A 64  ? 0.17894 0.16340 0.14707 -0.01164 0.00602  0.00075  64  GLU A C   
481  O O   . GLU A 64  ? 0.16286 0.14364 0.12593 -0.01151 0.00578  0.00074  64  GLU A O   
482  C CB  . GLU A 64  ? 0.22068 0.20791 0.19349 -0.01369 0.01170  -0.00060 64  GLU A CB  
483  C CG  . GLU A 64  ? 0.20056 0.19147 0.17887 -0.01405 0.01469  -0.00211 64  GLU A CG  
484  C CD  . GLU A 64  ? 0.29772 0.28642 0.27452 -0.01612 0.01867  -0.00253 64  GLU A CD  
485  O OE1 . GLU A 64  ? 0.44396 0.42808 0.41525 -0.01729 0.01893  -0.00139 64  GLU A OE1 
486  O OE2 . GLU A 64  ? 0.36883 0.36019 0.35010 -0.01657 0.02168  -0.00402 64  GLU A OE2 
487  N N   . ASP A 65  ? 0.16704 0.15213 0.13635 -0.01147 0.00392  0.00150  65  ASP A N   
488  C CA  . ASP A 65  ? 0.12711 0.10899 0.09265 -0.01098 0.00116  0.00233  65  ASP A CA  
489  C C   . ASP A 65  ? 0.15614 0.13908 0.12285 -0.00970 -0.00090 0.00205  65  ASP A C   
490  O O   . ASP A 65  ? 0.21812 0.19775 0.18087 -0.00939 -0.00251 0.00211  65  ASP A O   
491  C CB  . ASP A 65  ? 0.18841 0.17116 0.15594 -0.01099 -0.00029 0.00291  65  ASP A CB  
492  C CG  . ASP A 65  ? 0.16586 0.14517 0.13000 -0.01042 -0.00305 0.00364  65  ASP A CG  
493  O OD1 . ASP A 65  ? 0.23791 0.21221 0.19614 -0.01090 -0.00304 0.00420  65  ASP A OD1 
494  O OD2 . ASP A 65  ? 0.15304 0.13446 0.12034 -0.00943 -0.00519 0.00360  65  ASP A OD2 
495  N N   . LEU A 66  ? 0.14143 0.12866 0.11346 -0.00896 -0.00100 0.00172  66  LEU A N   
496  C CA  . LEU A 66  ? 0.13265 0.12063 0.10607 -0.00798 -0.00233 0.00147  66  LEU A CA  
497  C C   . LEU A 66  ? 0.12152 0.10720 0.09199 -0.00804 -0.00139 0.00075  66  LEU A C   
498  O O   . LEU A 66  ? 0.11935 0.10326 0.08833 -0.00764 -0.00301 0.00046  66  LEU A O   
499  C CB  . LEU A 66  ? 0.11316 0.10528 0.09176 -0.00720 -0.00207 0.00143  66  LEU A CB  
500  C CG  . LEU A 66  ? 0.12668 0.12094 0.10801 -0.00679 -0.00332 0.00196  66  LEU A CG  
501  C CD1 . LEU A 66  ? 0.10348 0.10080 0.08833 -0.00591 -0.00293 0.00197  66  LEU A CD1 
502  C CD2 . LEU A 66  ? 0.11586 0.10880 0.09678 -0.00650 -0.00524 0.00219  66  LEU A CD2 
503  N N   . GLN A 67  ? 0.11965 0.10532 0.08950 -0.00858 0.00127  0.00023  67  GLN A N   
504  C CA  . GLN A 67  ? 0.15352 0.13686 0.12040 -0.00862 0.00262  -0.00069 67  GLN A CA  
505  C C   . GLN A 67  ? 0.16312 0.14119 0.12291 -0.00905 0.00150  -0.00063 67  GLN A C   
506  O O   . GLN A 67  ? 0.14963 0.12559 0.10705 -0.00864 0.00054  -0.00137 67  GLN A O   
507  C CB  . GLN A 67  ? 0.15777 0.14217 0.12572 -0.00922 0.00612  -0.00143 67  GLN A CB  
508  C CG  . GLN A 67  ? 0.13992 0.12194 0.10495 -0.00923 0.00811  -0.00264 67  GLN A CG  
509  C CD  . GLN A 67  ? 0.21832 0.20236 0.18715 -0.00795 0.00753  -0.00337 67  GLN A CD  
510  O OE1 . GLN A 67  ? 0.20392 0.18655 0.17160 -0.00740 0.00528  -0.00333 67  GLN A OE1 
511  N NE2 . GLN A 67  ? 0.20122 0.18850 0.17500 -0.00745 0.00952  -0.00412 67  GLN A NE2 
512  N N   . ARG A 68  ? 0.15695 0.13246 0.11304 -0.00980 0.00139  0.00021  68  ARG A N   
513  C CA  . ARG A 68  ? 0.19997 0.16980 0.14852 -0.00994 -0.00021 0.00046  68  ARG A CA  
514  C C   . ARG A 68  ? 0.20085 0.17054 0.15024 -0.00892 -0.00436 0.00047  68  ARG A C   
515  O O   . ARG A 68  ? 0.18265 0.14839 0.12698 -0.00861 -0.00635 0.00002  68  ARG A O   
516  C CB  . ARG A 68  ? 0.19696 0.16367 0.14144 -0.01087 0.00056  0.00160  68  ARG A CB  
517  C CG  . ARG A 68  ? 0.24304 0.20933 0.18657 -0.01223 0.00503  0.00145  68  ARG A CG  
518  C CD  . ARG A 68  ? 0.27542 0.23721 0.21372 -0.01333 0.00588  0.00268  68  ARG A CD  
519  N NE  . ARG A 68  ? 0.37551 0.33956 0.31799 -0.01319 0.00404  0.00353  68  ARG A NE  
520  C CZ  . ARG A 68  ? 0.30416 0.27187 0.25212 -0.01400 0.00595  0.00347  68  ARG A CZ  
521  N NH1 . ARG A 68  ? 0.29845 0.26842 0.24923 -0.01500 0.00965  0.00258  68  ARG A NH1 
522  N NH2 . ARG A 68  ? 0.41277 0.38195 0.36377 -0.01376 0.00401  0.00408  68  ARG A NH2 
523  N N   . SER A 69  ? 0.16705 0.14094 0.12282 -0.00840 -0.00567 0.00081  69  SER A N   
524  C CA  . SER A 69  ? 0.17101 0.14526 0.12882 -0.00758 -0.00915 0.00064  69  SER A CA  
525  C C   . SER A 69  ? 0.19337 0.16830 0.15296 -0.00717 -0.00978 -0.00053 69  SER A C   
526  O O   . SER A 69  ? 0.22217 0.19501 0.18027 -0.00679 -0.01257 -0.00123 69  SER A O   
527  C CB  . SER A 69  ? 0.17651 0.15478 0.14034 -0.00726 -0.00967 0.00124  69  SER A CB  
528  O OG  . SER A 69  ? 0.13178 0.10869 0.09377 -0.00756 -0.00983 0.00212  69  SER A OG  
529  N N   . PHE A 70  ? 0.16362 0.14131 0.12661 -0.00718 -0.00742 -0.00086 70  PHE A N   
530  C CA  . PHE A 70  ? 0.18389 0.16166 0.14841 -0.00685 -0.00774 -0.00195 70  PHE A CA  
531  C C   . PHE A 70  ? 0.18461 0.15795 0.14282 -0.00707 -0.00772 -0.00305 70  PHE A C   
532  O O   . PHE A 70  ? 0.21701 0.18883 0.17478 -0.00684 -0.00959 -0.00420 70  PHE A O   
533  C CB  . PHE A 70  ? 0.15904 0.14013 0.12818 -0.00657 -0.00532 -0.00191 70  PHE A CB  
534  C CG  . PHE A 70  ? 0.17399 0.15877 0.14861 -0.00619 -0.00563 -0.00101 70  PHE A CG  
535  C CD1 . PHE A 70  ? 0.20811 0.19359 0.18589 -0.00598 -0.00732 -0.00110 70  PHE A CD1 
536  C CD2 . PHE A 70  ? 0.14741 0.13481 0.12400 -0.00611 -0.00413 -0.00022 70  PHE A CD2 
537  C CE1 . PHE A 70  ? 0.11110 0.09943 0.09313 -0.00570 -0.00712 -0.00027 70  PHE A CE1 
538  C CE2 . PHE A 70  ? 0.13839 0.12858 0.11891 -0.00569 -0.00445 0.00053  70  PHE A CE2 
539  C CZ  . PHE A 70  ? 0.14716 0.13761 0.13002 -0.00549 -0.00576 0.00058  70  PHE A CZ  
540  N N   . GLN A 71  ? 0.17238 0.14342 0.12560 -0.00760 -0.00550 -0.00286 71  GLN A N   
541  C CA  . GLN A 71  ? 0.20512 0.17133 0.15121 -0.00784 -0.00502 -0.00393 71  GLN A CA  
542  C C   . GLN A 71  ? 0.20030 0.16222 0.14094 -0.00760 -0.00886 -0.00411 71  GLN A C   
543  O O   . GLN A 71  ? 0.20083 0.15967 0.13781 -0.00738 -0.01035 -0.00551 71  GLN A O   
544  C CB  . GLN A 71  ? 0.22168 0.18616 0.16361 -0.00865 -0.00127 -0.00361 71  GLN A CB  
545  C CG  . GLN A 71  ? 0.26054 0.22873 0.20750 -0.00871 0.00243  -0.00414 71  GLN A CG  
546  C CD  . GLN A 71  ? 0.31092 0.27752 0.25453 -0.00968 0.00644  -0.00422 71  GLN A CD  
547  O OE1 . GLN A 71  ? 0.28810 0.25006 0.22452 -0.01043 0.00680  -0.00372 71  GLN A OE1 
548  N NE2 . GLN A 71  ? 0.33883 0.30909 0.28775 -0.00966 0.00955  -0.00487 71  GLN A NE2 
549  N N   . ALA A 72  ? 0.23353 0.19511 0.17373 -0.00750 -0.01079 -0.00287 72  ALA A N   
550  C CA  . ALA A 72  ? 0.19855 0.15650 0.13475 -0.00691 -0.01513 -0.00306 72  ALA A CA  
551  C C   . ALA A 72  ? 0.22523 0.18544 0.16695 -0.00629 -0.01838 -0.00440 72  ALA A C   
552  O O   . ALA A 72  ? 0.21461 0.17171 0.15316 -0.00575 -0.02220 -0.00534 72  ALA A O   
553  C CB  . ALA A 72  ? 0.24663 0.20432 0.18278 -0.00674 -0.01649 -0.00149 72  ALA A CB  
554  N N   . ARG A 73  ? 0.24693 0.21222 0.19674 -0.00638 -0.01698 -0.00457 73  ARG A N   
555  C CA  . ARG A 73  ? 0.17724 0.14476 0.13306 -0.00610 -0.01925 -0.00578 73  ARG A CA  
556  C C   . ARG A 73  ? 0.24084 0.20820 0.19741 -0.00635 -0.01775 -0.00717 73  ARG A C   
557  O O   . ARG A 73  ? 0.23301 0.20263 0.19560 -0.00638 -0.01849 -0.00801 73  ARG A O   
558  C CB  . ARG A 73  ? 0.20806 0.18065 0.17208 -0.00604 -0.01875 -0.00488 73  ARG A CB  
559  C CG  . ARG A 73  ? 0.23924 0.21211 0.20421 -0.00559 -0.02129 -0.00420 73  ARG A CG  
560  C CD  . ARG A 73  ? 0.26225 0.23978 0.23425 -0.00558 -0.01994 -0.00330 73  ARG A CD  
561  N NE  . ARG A 73  ? 0.22210 0.20025 0.19665 -0.00503 -0.02265 -0.00324 73  ARG A NE  
562  C CZ  . ARG A 73  ? 0.27884 0.25554 0.25043 -0.00470 -0.02326 -0.00221 73  ARG A CZ  
563  N NH1 . ARG A 73  ? 0.31960 0.29413 0.28555 -0.00510 -0.02122 -0.00112 73  ARG A NH1 
564  N NH2 . ARG A 73  ? 0.29054 0.26793 0.26532 -0.00399 -0.02585 -0.00238 73  ARG A NH2 
565  N N   . GLY A 74  ? 0.20899 0.17350 0.15970 -0.00657 -0.01540 -0.00751 74  GLY A N   
566  C CA  . GLY A 74  ? 0.22912 0.19283 0.17992 -0.00666 -0.01399 -0.00905 74  GLY A CA  
567  C C   . GLY A 74  ? 0.22665 0.19414 0.18337 -0.00663 -0.01061 -0.00856 74  GLY A C   
568  O O   . GLY A 74  ? 0.22899 0.19613 0.18733 -0.00654 -0.00977 -0.00980 74  GLY A O   
569  N N   . SER A 75  ? 0.21534 0.18612 0.17516 -0.00659 -0.00888 -0.00686 75  SER A N   
570  C CA  . SER A 75  ? 0.23319 0.20750 0.19854 -0.00629 -0.00633 -0.00629 75  SER A CA  
571  C C   . SER A 75  ? 0.19516 0.17028 0.15905 -0.00631 -0.00324 -0.00568 75  SER A C   
572  O O   . SER A 75  ? 0.21799 0.19029 0.17615 -0.00675 -0.00233 -0.00599 75  SER A O   
573  C CB  . SER A 75  ? 0.24226 0.22016 0.21363 -0.00613 -0.00729 -0.00506 75  SER A CB  
574  O OG  . SER A 75  ? 0.22280 0.20316 0.19870 -0.00566 -0.00537 -0.00454 75  SER A OG  
575  N N   . ARG A 76  ? 0.17277 0.15154 0.14176 -0.00586 -0.00162 -0.00486 76  ARG A N   
576  C CA  . ARG A 76  ? 0.17228 0.15255 0.14155 -0.00584 0.00116  -0.00465 76  ARG A CA  
577  C C   . ARG A 76  ? 0.15397 0.13849 0.12901 -0.00523 0.00138  -0.00349 76  ARG A C   
578  O O   . ARG A 76  ? 0.17675 0.16242 0.15531 -0.00454 0.00065  -0.00320 76  ARG A O   
579  C CB  . ARG A 76  ? 0.23789 0.21682 0.20627 -0.00553 0.00352  -0.00614 76  ARG A CB  
580  C CG  . ARG A 76  ? 0.26484 0.24549 0.23431 -0.00556 0.00669  -0.00639 76  ARG A CG  
581  C CD  . ARG A 76  ? 0.23829 0.21678 0.20585 -0.00538 0.00920  -0.00821 76  ARG A CD  
582  N NE  . ARG A 76  ? 0.23278 0.21134 0.20347 -0.00430 0.00864  -0.00895 76  ARG A NE  
583  C CZ  . ARG A 76  ? 0.29532 0.27645 0.27140 -0.00314 0.00996  -0.00924 76  ARG A CZ  
584  N NH1 . ARG A 76  ? 0.21558 0.19997 0.19516 -0.00286 0.01180  -0.00913 76  ARG A NH1 
585  N NH2 . ARG A 76  ? 0.26839 0.24867 0.24664 -0.00219 0.00928  -0.00972 76  ARG A NH2 
586  N N   . LEU A 77  ? 0.13691 0.12334 0.11254 -0.00553 0.00237  -0.00287 77  LEU A N   
587  C CA  . LEU A 77  ? 0.14702 0.13728 0.12752 -0.00487 0.00239  -0.00202 77  LEU A CA  
588  C C   . LEU A 77  ? 0.14647 0.13851 0.13020 -0.00398 0.00425  -0.00275 77  LEU A C   
589  O O   . LEU A 77  ? 0.21195 0.20344 0.19471 -0.00433 0.00639  -0.00383 77  LEU A O   
590  C CB  . LEU A 77  ? 0.16394 0.15550 0.14418 -0.00559 0.00241  -0.00135 77  LEU A CB  
591  C CG  . LEU A 77  ? 0.12405 0.11941 0.10873 -0.00497 0.00219  -0.00076 77  LEU A CG  
592  C CD1 . LEU A 77  ? 0.14665 0.14269 0.13290 -0.00421 0.00036  0.00016  77  LEU A CD1 
593  C CD2 . LEU A 77  ? 0.20791 0.20409 0.19219 -0.00592 0.00241  -0.00048 77  LEU A CD2 
594  N N   . LEU A 78  ? 0.11802 0.11193 0.10551 -0.00275 0.00350  -0.00220 78  LEU A N   
595  C CA  . LEU A 78  ? 0.12542 0.12092 0.11648 -0.00144 0.00460  -0.00281 78  LEU A CA  
596  C C   . LEU A 78  ? 0.14940 0.14852 0.14405 -0.00074 0.00399  -0.00221 78  LEU A C   
597  O O   . LEU A 78  ? 0.13150 0.13123 0.12668 -0.00017 0.00231  -0.00097 78  LEU A O   
598  C CB  . LEU A 78  ? 0.12011 0.11395 0.11203 -0.00035 0.00399  -0.00263 78  LEU A CB  
599  C CG  . LEU A 78  ? 0.12220 0.11243 0.11096 -0.00107 0.00408  -0.00346 78  LEU A CG  
600  C CD1 . LEU A 78  ? 0.18386 0.17243 0.17414 -0.00018 0.00351  -0.00321 78  LEU A CD1 
601  C CD2 . LEU A 78  ? 0.15477 0.14370 0.14164 -0.00142 0.00615  -0.00521 78  LEU A CD2 
602  N N   . VAL A 79  ? 0.12414 0.12552 0.12120 -0.00084 0.00543  -0.00324 79  VAL A N   
603  C CA  . VAL A 79  ? 0.10672 0.11180 0.10787 -0.00017 0.00465  -0.00318 79  VAL A CA  
604  C C   . VAL A 79  ? 0.12165 0.12830 0.12715 0.00186  0.00454  -0.00384 79  VAL A C   
605  O O   . VAL A 79  ? 0.13124 0.13919 0.13977 0.00205  0.00641  -0.00542 79  VAL A O   
606  C CB  . VAL A 79  ? 0.13364 0.14045 0.13580 -0.00165 0.00625  -0.00412 79  VAL A CB  
607  C CG1 . VAL A 79  ? 0.15479 0.16567 0.16187 -0.00098 0.00508  -0.00442 79  VAL A CG1 
608  C CG2 . VAL A 79  ? 0.14371 0.14817 0.14106 -0.00341 0.00616  -0.00331 79  VAL A CG2 
609  N N   . LEU A 80  ? 0.15058 0.15683 0.15636 0.00344  0.00247  -0.00263 80  LEU A N   
610  C CA  . LEU A 80  ? 0.14418 0.15124 0.15361 0.00570  0.00184  -0.00298 80  LEU A CA  
611  C C   . LEU A 80  ? 0.17903 0.19016 0.19305 0.00677  0.00048  -0.00358 80  LEU A C   
612  O O   . LEU A 80  ? 0.22741 0.23991 0.24072 0.00626  -0.00096 -0.00297 80  LEU A O   
613  C CB  . LEU A 80  ? 0.12217 0.12624 0.12924 0.00696  0.00029  -0.00124 80  LEU A CB  
614  C CG  . LEU A 80  ? 0.12230 0.12255 0.12571 0.00582  0.00134  -0.00087 80  LEU A CG  
615  C CD1 . LEU A 80  ? 0.22454 0.22183 0.22611 0.00669  0.00022  0.00085  80  LEU A CD1 
616  C CD2 . LEU A 80  ? 0.16713 0.16630 0.17152 0.00583  0.00330  -0.00257 80  LEU A CD2 
617  N N   . ARG A 81  ? 0.16617 0.17932 0.18531 0.00829  0.00083  -0.00503 81  ARG A N   
618  C CA  . ARG A 81  ? 0.21534 0.23272 0.24007 0.00957  -0.00084 -0.00603 81  ARG A CA  
619  C C   . ARG A 81  ? 0.20299 0.21957 0.22817 0.01250  -0.00404 -0.00493 81  ARG A C   
620  O O   . ARG A 81  ? 0.22611 0.24010 0.25091 0.01401  -0.00389 -0.00453 81  ARG A O   
621  C CB  . ARG A 81  ? 0.13920 0.15977 0.17038 0.00954  0.00148  -0.00860 81  ARG A CB  
622  C CG  . ARG A 81  ? 0.18103 0.20377 0.21341 0.00685  0.00400  -0.00989 81  ARG A CG  
623  C CD  . ARG A 81  ? 0.16223 0.18113 0.18809 0.00448  0.00664  -0.00921 81  ARG A CD  
624  N NE  . ARG A 81  ? 0.25071 0.27086 0.27750 0.00210  0.00960  -0.01048 81  ARG A NE  
625  C CZ  . ARG A 81  ? 0.14032 0.15715 0.16151 -0.00002 0.01200  -0.01015 81  ARG A CZ  
626  N NH1 . ARG A 81  ? 0.18909 0.20169 0.20397 -0.00010 0.01154  -0.00884 81  ARG A NH1 
627  N NH2 . ARG A 81  ? 0.15724 0.17479 0.17916 -0.00210 0.01487  -0.01119 81  ARG A NH2 
628  N N   . GLY A 82  ? 0.29445 0.31272 0.31989 0.01332  -0.00697 -0.00442 82  GLY A N   
629  C CA  . GLY A 82  ? 0.28811 0.30542 0.31338 0.01628  -0.01037 -0.00341 82  GLY A CA  
630  C C   . GLY A 82  ? 0.24779 0.26296 0.26705 0.01621  -0.01249 -0.00139 82  GLY A C   
631  O O   . GLY A 82  ? 0.27289 0.28848 0.28964 0.01400  -0.01170 -0.00120 82  GLY A O   
632  N N   . LYS A 83  ? 0.25182 0.26425 0.26841 0.01876  -0.01513 0.00014  83  LYS A N   
633  C CA  . LYS A 83  ? 0.23978 0.24927 0.24976 0.01902  -0.01690 0.00219  83  LYS A CA  
634  C C   . LYS A 83  ? 0.25468 0.25888 0.25877 0.01825  -0.01488 0.00441  83  LYS A C   
635  O O   . LYS A 83  ? 0.31840 0.32006 0.32294 0.01912  -0.01389 0.00487  83  LYS A O   
636  C CB  . LYS A 83  ? 0.22593 0.23467 0.23530 0.02230  -0.02099 0.00271  83  LYS A CB  
637  C CG  . LYS A 83  ? 0.24828 0.26246 0.26521 0.02362  -0.02346 0.00015  83  LYS A CG  
638  C CD  . LYS A 83  ? 0.30017 0.31862 0.31926 0.02137  -0.02338 -0.00151 83  LYS A CD  
639  C CE  . LYS A 83  ? 0.32173 0.33824 0.33437 0.02158  -0.02584 -0.00031 83  LYS A CE  
640  N NZ  . LYS A 83  ? 0.36195 0.38292 0.37796 0.02012  -0.02684 -0.00240 83  LYS A NZ  
641  N N   . PRO A 84  ? 0.23909 0.24161 0.23816 0.01658  -0.01415 0.00562  84  PRO A N   
642  C CA  . PRO A 84  ? 0.20578 0.20374 0.20036 0.01558  -0.01201 0.00744  84  PRO A CA  
643  C C   . PRO A 84  ? 0.26095 0.25409 0.25255 0.01778  -0.01271 0.00932  84  PRO A C   
644  O O   . PRO A 84  ? 0.22150 0.21149 0.21241 0.01723  -0.01070 0.01006  84  PRO A O   
645  C CB  . PRO A 84  ? 0.18763 0.18512 0.17793 0.01411  -0.01180 0.00823  84  PRO A CB  
646  C CG  . PRO A 84  ? 0.24408 0.24633 0.23758 0.01332  -0.01279 0.00636  84  PRO A CG  
647  C CD  . PRO A 84  ? 0.28132 0.28622 0.27935 0.01541  -0.01503 0.00508  84  PRO A CD  
648  N N   . GLU A 85  ? 0.27696 0.26909 0.26660 0.02031  -0.01568 0.01006  85  GLU A N   
649  C CA  . GLU A 85  ? 0.28219 0.26879 0.26793 0.02261  -0.01653 0.01217  85  GLU A CA  
650  C C   . GLU A 85  ? 0.22527 0.21149 0.21560 0.02412  -0.01645 0.01151  85  GLU A C   
651  O O   . GLU A 85  ? 0.24083 0.22175 0.22827 0.02547  -0.01621 0.01329  85  GLU A O   
652  C CB  . GLU A 85  ? 0.29194 0.27725 0.27383 0.02525  -0.02030 0.01304  85  GLU A CB  
653  C CG  . GLU A 85  ? 0.35652 0.34119 0.33271 0.02407  -0.02039 0.01375  85  GLU A CG  
654  C CD  . GLU A 85  ? 0.34860 0.33950 0.32896 0.02269  -0.02122 0.01133  85  GLU A CD  
655  O OE1 . GLU A 85  ? 0.28235 0.27798 0.26977 0.02304  -0.02225 0.00920  85  GLU A OE1 
656  O OE2 . GLU A 85  ? 0.49104 0.48195 0.46780 0.02118  -0.02060 0.01149  85  GLU A OE2 
657  N N   . GLU A 86  ? 0.26254 0.25393 0.25987 0.02388  -0.01637 0.00897  86  GLU A N   
658  C CA  . GLU A 86  ? 0.22521 0.21668 0.22749 0.02526  -0.01592 0.00788  86  GLU A CA  
659  C C   . GLU A 86  ? 0.19836 0.19024 0.20274 0.02276  -0.01226 0.00674  86  GLU A C   
660  O O   . GLU A 86  ? 0.27387 0.26414 0.28072 0.02367  -0.01128 0.00617  86  GLU A O   
661  C CB  . GLU A 86  ? 0.22994 0.22683 0.23918 0.02703  -0.01821 0.00551  86  GLU A CB  
662  C CG  . GLU A 86  ? 0.30026 0.29757 0.30809 0.02953  -0.02254 0.00606  86  GLU A CG  
663  C CD  . GLU A 86  ? 0.29935 0.30299 0.31545 0.03081  -0.02474 0.00321  86  GLU A CD  
664  O OE1 . GLU A 86  ? 0.27118 0.27876 0.29387 0.02954  -0.02230 0.00093  86  GLU A OE1 
665  O OE2 . GLU A 86  ? 0.29167 0.29623 0.30769 0.03305  -0.02886 0.00314  86  GLU A OE2 
666  N N   . VAL A 87  ? 0.21149 0.20515 0.21474 0.01980  -0.01041 0.00629  87  VAL A N   
667  C CA  . VAL A 87  ? 0.16387 0.15773 0.16844 0.01752  -0.00743 0.00509  87  VAL A CA  
668  C C   . VAL A 87  ? 0.19227 0.18128 0.19256 0.01622  -0.00582 0.00669  87  VAL A C   
669  O O   . VAL A 87  ? 0.24597 0.23302 0.24717 0.01564  -0.00412 0.00603  87  VAL A O   
670  C CB  . VAL A 87  ? 0.20181 0.19995 0.20769 0.01516  -0.00651 0.00363  87  VAL A CB  
671  C CG1 . VAL A 87  ? 0.19453 0.19185 0.19999 0.01284  -0.00381 0.00272  87  VAL A CG1 
672  C CG2 . VAL A 87  ? 0.27653 0.27949 0.28795 0.01610  -0.00737 0.00162  87  VAL A CG2 
673  N N   . PHE A 88  ? 0.17407 0.16109 0.16992 0.01565  -0.00619 0.00858  88  PHE A N   
674  C CA  . PHE A 88  ? 0.12736 0.11054 0.12016 0.01395  -0.00430 0.00979  88  PHE A CA  
675  C C   . PHE A 88  ? 0.13241 0.11037 0.12431 0.01516  -0.00371 0.01095  88  PHE A C   
676  O O   . PHE A 88  ? 0.15572 0.13157 0.14810 0.01363  -0.00184 0.01056  88  PHE A O   
677  C CB  . PHE A 88  ? 0.21769 0.20009 0.20634 0.01312  -0.00443 0.01137  88  PHE A CB  
678  C CG  . PHE A 88  ? 0.14395 0.13027 0.13335 0.01105  -0.00409 0.01022  88  PHE A CG  
679  C CD1 . PHE A 88  ? 0.16256 0.14976 0.15364 0.00890  -0.00253 0.00900  88  PHE A CD1 
680  C CD2 . PHE A 88  ? 0.16983 0.15857 0.15802 0.01137  -0.00556 0.01029  88  PHE A CD2 
681  C CE1 . PHE A 88  ? 0.22107 0.21128 0.21249 0.00720  -0.00243 0.00809  88  PHE A CE1 
682  C CE2 . PHE A 88  ? 0.16006 0.15195 0.14896 0.00951  -0.00521 0.00926  88  PHE A CE2 
683  C CZ  . PHE A 88  ? 0.12768 0.12020 0.11815 0.00749  -0.00364 0.00827  88  PHE A CZ  
684  N N   . PRO A 89  ? 0.16322 0.13863 0.15373 0.01788  -0.00539 0.01232  89  PRO A N   
685  C CA  . PRO A 89  ? 0.19912 0.16906 0.18893 0.01908  -0.00473 0.01339  89  PRO A CA  
686  C C   . PRO A 89  ? 0.18335 0.15386 0.17770 0.01887  -0.00357 0.01126  89  PRO A C   
687  O O   . PRO A 89  ? 0.19729 0.16351 0.19120 0.01827  -0.00198 0.01161  89  PRO A O   
688  C CB  . PRO A 89  ? 0.23432 0.20247 0.22252 0.02255  -0.00755 0.01475  89  PRO A CB  
689  C CG  . PRO A 89  ? 0.22012 0.19058 0.20532 0.02243  -0.00907 0.01540  89  PRO A CG  
690  C CD  . PRO A 89  ? 0.19020 0.16671 0.17896 0.02000  -0.00815 0.01314  89  PRO A CD  
691  N N   . ARG A 90  ? 0.20277 0.17829 0.20142 0.01919  -0.00406 0.00892  90  ARG A N   
692  C CA  . ARG A 90  ? 0.23926 0.21515 0.24160 0.01892  -0.00258 0.00668  90  ARG A CA  
693  C C   . ARG A 90  ? 0.19883 0.17452 0.20026 0.01576  -0.00042 0.00569  90  ARG A C   
694  O O   . ARG A 90  ? 0.15794 0.13031 0.15958 0.01516  0.00093  0.00509  90  ARG A O   
695  C CB  . ARG A 90  ? 0.23955 0.22080 0.24665 0.01996  -0.00318 0.00440  90  ARG A CB  
696  C CG  . ARG A 90  ? 0.28689 0.26876 0.29730 0.01946  -0.00112 0.00181  90  ARG A CG  
697  C CD  . ARG A 90  ? 0.28815 0.27540 0.30099 0.01807  -0.00020 -0.00033 90  ARG A CD  
698  N NE  . ARG A 90  ? 0.37381 0.36532 0.38966 0.01958  -0.00210 -0.00045 90  ARG A NE  
699  C CZ  . ARG A 90  ? 0.37737 0.37369 0.39559 0.01843  -0.00157 -0.00196 90  ARG A CZ  
700  N NH1 . ARG A 90  ? 0.27778 0.27492 0.29492 0.01587  0.00082  -0.00324 90  ARG A NH1 
701  N NH2 . ARG A 90  ? 0.33672 0.33681 0.35831 0.01988  -0.00359 -0.00222 90  ARG A NH2 
702  N N   . VAL A 91  ? 0.17899 0.15802 0.17945 0.01379  -0.00032 0.00541  91  VAL A N   
703  C CA  . VAL A 91  ? 0.20010 0.17919 0.19984 0.01107  0.00114  0.00428  91  VAL A CA  
704  C C   . VAL A 91  ? 0.15215 0.12743 0.14960 0.00966  0.00181  0.00570  91  VAL A C   
705  O O   . VAL A 91  ? 0.18380 0.15832 0.18131 0.00768  0.00273  0.00459  91  VAL A O   
706  C CB  . VAL A 91  ? 0.13552 0.11903 0.13505 0.00958  0.00091  0.00353  91  VAL A CB  
707  C CG1 . VAL A 91  ? 0.19882 0.18589 0.20124 0.01045  0.00098  0.00174  91  VAL A CG1 
708  C CG2 . VAL A 91  ? 0.17305 0.15751 0.17062 0.00961  -0.00024 0.00538  91  VAL A CG2 
709  N N   . PHE A 92  ? 0.17804 0.15074 0.17344 0.01059  0.00142  0.00805  92  PHE A N   
710  C CA  . PHE A 92  ? 0.15356 0.12207 0.14739 0.00922  0.00274  0.00932  92  PHE A CA  
711  C C   . PHE A 92  ? 0.20259 0.16716 0.19795 0.00923  0.00377  0.00850  92  PHE A C   
712  O O   . PHE A 92  ? 0.17951 0.14270 0.17572 0.00712  0.00489  0.00760  92  PHE A O   
713  C CB  . PHE A 92  ? 0.17111 0.13671 0.16152 0.01037  0.00254  0.01212  92  PHE A CB  
714  C CG  . PHE A 92  ? 0.15011 0.11861 0.13845 0.00975  0.00200  0.01287  92  PHE A CG  
715  C CD1 . PHE A 92  ? 0.13275 0.10553 0.12259 0.00786  0.00204  0.01134  92  PHE A CD1 
716  C CD2 . PHE A 92  ? 0.18198 0.14844 0.16639 0.01119  0.00136  0.01510  92  PHE A CD2 
717  C CE1 . PHE A 92  ? 0.17006 0.14525 0.15818 0.00738  0.00158  0.01191  92  PHE A CE1 
718  C CE2 . PHE A 92  ? 0.20651 0.17540 0.18878 0.01065  0.00092  0.01555  92  PHE A CE2 
719  C CZ  . PHE A 92  ? 0.13217 0.10554 0.11664 0.00873  0.00111  0.01390  92  PHE A CZ  
720  N N   . ARG A 93  ? 0.20856 0.17131 0.20466 0.01168  0.00322  0.00861  93  ARG A N   
721  C CA  . ARG A 93  ? 0.30131 0.25989 0.29886 0.01193  0.00420  0.00776  93  ARG A CA  
722  C C   . ARG A 93  ? 0.24616 0.20697 0.24615 0.01098  0.00467  0.00461  93  ARG A C   
723  O O   . ARG A 93  ? 0.23839 0.19637 0.23909 0.00966  0.00569  0.00334  93  ARG A O   
724  C CB  . ARG A 93  ? 0.24341 0.19903 0.24104 0.01517  0.00331  0.00889  93  ARG A CB  
725  C CG  . ARG A 93  ? 0.25478 0.20516 0.24881 0.01612  0.00328  0.01214  93  ARG A CG  
726  C CD  . ARG A 93  ? 0.26615 0.21884 0.25718 0.01694  0.00180  0.01395  93  ARG A CD  
727  N NE  . ARG A 93  ? 0.21487 0.16181 0.20123 0.01815  0.00177  0.01714  93  ARG A NE  
728  C CZ  . ARG A 93  ? 0.20701 0.15423 0.18935 0.01908  0.00053  0.01903  93  ARG A CZ  
729  N NH1 . ARG A 93  ? 0.20927 0.16248 0.19232 0.01891  -0.00087 0.01801  93  ARG A NH1 
730  N NH2 . ARG A 93  ? 0.32449 0.26538 0.30154 0.02017  0.00078  0.02200  93  ARG A NH2 
731  N N   . GLU A 94  ? 0.25582 0.22137 0.25688 0.01156  0.00402  0.00323  94  GLU A N   
732  C CA  . GLU A 94  ? 0.24100 0.20808 0.24337 0.01078  0.00482  0.00031  94  GLU A CA  
733  C C   . GLU A 94  ? 0.21111 0.17825 0.21200 0.00787  0.00522  -0.00073 94  GLU A C   
734  O O   . GLU A 94  ? 0.17942 0.14455 0.18039 0.00696  0.00588  -0.00276 94  GLU A O   
735  C CB  . GLU A 94  ? 0.19469 0.16672 0.19843 0.01171  0.00449  -0.00073 94  GLU A CB  
736  C CG  . GLU A 94  ? 0.23064 0.20407 0.23451 0.01055  0.00577  -0.00355 94  GLU A CG  
737  C CD  . GLU A 94  ? 0.18672 0.16487 0.19214 0.01107  0.00604  -0.00455 94  GLU A CD  
738  O OE1 . GLU A 94  ? 0.21625 0.19637 0.22450 0.01318  0.00529  -0.00395 94  GLU A OE1 
739  O OE2 . GLU A 94  ? 0.23574 0.21542 0.23953 0.00935  0.00695  -0.00596 94  GLU A OE2 
740  N N   . TRP A 95  ? 0.16902 0.13831 0.16861 0.00654  0.00460  0.00048  95  TRP A N   
741  C CA  . TRP A 95  ? 0.21176 0.18174 0.21043 0.00408  0.00447  -0.00053 95  TRP A CA  
742  C C   . TRP A 95  ? 0.18054 0.14745 0.17974 0.00262  0.00477  0.00020  95  TRP A C   
743  O O   . TRP A 95  ? 0.19906 0.16648 0.19839 0.00065  0.00435  -0.00086 95  TRP A O   
744  C CB  . TRP A 95  ? 0.16515 0.13926 0.16272 0.00345  0.00368  0.00011  95  TRP A CB  
745  C CG  . TRP A 95  ? 0.14785 0.12513 0.14532 0.00431  0.00368  -0.00088 95  TRP A CG  
746  C CD1 . TRP A 95  ? 0.15257 0.12960 0.15073 0.00516  0.00454  -0.00268 95  TRP A CD1 
747  C CD2 . TRP A 95  ? 0.14217 0.12325 0.13919 0.00426  0.00311  -0.00028 95  TRP A CD2 
748  N NE1 . TRP A 95  ? 0.19991 0.18050 0.19836 0.00552  0.00476  -0.00321 95  TRP A NE1 
749  C CE2 . TRP A 95  ? 0.17463 0.15768 0.17242 0.00494  0.00377  -0.00175 95  TRP A CE2 
750  C CE3 . TRP A 95  ? 0.14083 0.12372 0.13705 0.00363  0.00229  0.00119  95  TRP A CE3 
751  C CZ2 . TRP A 95  ? 0.16295 0.14968 0.16099 0.00486  0.00361  -0.00174 95  TRP A CZ2 
752  C CZ3 . TRP A 95  ? 0.19588 0.18227 0.19201 0.00371  0.00188  0.00117  95  TRP A CZ3 
753  C CH2 . TRP A 95  ? 0.17057 0.15883 0.16772 0.00424  0.00252  -0.00026 95  TRP A CH2 
754  N N   . GLY A 96  ? 0.26048 0.22403 0.26012 0.00352  0.00548  0.00192  96  GLY A N   
755  C CA  . GLY A 96  ? 0.23280 0.19327 0.23327 0.00190  0.00636  0.00272  96  GLY A CA  
756  C C   . GLY A 96  ? 0.17936 0.14226 0.17959 0.00041  0.00630  0.00377  96  GLY A C   
757  O O   . GLY A 96  ? 0.16917 0.13176 0.17128 -0.00169 0.00660  0.00292  96  GLY A O   
758  N N   . VAL A 97  ? 0.13308 0.09851 0.13145 0.00150  0.00583  0.00537  97  VAL A N   
759  C CA  . VAL A 97  ? 0.15377 0.12171 0.15176 0.00029  0.00581  0.00616  97  VAL A CA  
760  C C   . VAL A 97  ? 0.15953 0.12424 0.15773 -0.00067 0.00762  0.00785  97  VAL A C   
761  O O   . VAL A 97  ? 0.15317 0.11395 0.14974 0.00046  0.00864  0.00967  97  VAL A O   
762  C CB  . VAL A 97  ? 0.14175 0.11277 0.13753 0.00180  0.00484  0.00725  97  VAL A CB  
763  C CG1 . VAL A 97  ? 0.16589 0.13942 0.16122 0.00060  0.00485  0.00781  97  VAL A CG1 
764  C CG2 . VAL A 97  ? 0.19610 0.17002 0.19217 0.00258  0.00365  0.00554  97  VAL A CG2 
765  N N   . THR A 98  ? 0.18380 0.14995 0.18408 -0.00275 0.00813  0.00723  98  THR A N   
766  C CA  . THR A 98  ? 0.15210 0.11589 0.15304 -0.00399 0.01040  0.00866  98  THR A CA  
767  C C   . THR A 98  ? 0.18319 0.14977 0.18304 -0.00431 0.01075  0.00959  98  THR A C   
768  O O   . THR A 98  ? 0.13960 0.10396 0.13871 -0.00495 0.01307  0.01117  98  THR A O   
769  C CB  . THR A 98  ? 0.16899 0.13182 0.17477 -0.00637 0.01121  0.00684  98  THR A CB  
770  O OG1 . THR A 98  ? 0.23583 0.20294 0.24419 -0.00742 0.00928  0.00454  98  THR A OG1 
771  C CG2 . THR A 98  ? 0.17753 0.13678 0.18417 -0.00614 0.01116  0.00590  98  THR A CG2 
772  N N   . GLN A 99  ? 0.15855 0.12950 0.15804 -0.00393 0.00879  0.00864  99  GLN A N   
773  C CA  . GLN A 99  ? 0.17880 0.15243 0.17763 -0.00426 0.00900  0.00917  99  GLN A CA  
774  C C   . GLN A 99  ? 0.12459 0.10144 0.12096 -0.00284 0.00689  0.00904  99  GLN A C   
775  O O   . GLN A 99  ? 0.13043 0.10911 0.12756 -0.00267 0.00519  0.00753  99  GLN A O   
776  C CB  . GLN A 99  ? 0.13024 0.10621 0.13365 -0.00631 0.00904  0.00739  99  GLN A CB  
777  C CG  . GLN A 99  ? 0.19266 0.17107 0.19601 -0.00666 0.00968  0.00781  99  GLN A CG  
778  C CD  . GLN A 99  ? 0.21752 0.19896 0.22589 -0.00819 0.00885  0.00573  99  GLN A CD  
779  O OE1 . GLN A 99  ? 0.15929 0.14306 0.16825 -0.00803 0.00623  0.00425  99  GLN A OE1 
780  N NE2 . GLN A 99  ? 0.21892 0.20013 0.23092 -0.00962 0.01113  0.00560  99  GLN A NE2 
781  N N   . LEU A 100 ? 0.13370 0.11098 0.12700 -0.00193 0.00716  0.01052  100 LEU A N   
782  C CA  . LEU A 100 ? 0.13627 0.11668 0.12770 -0.00079 0.00531  0.01034  100 LEU A CA  
783  C C   . LEU A 100 ? 0.11779 0.10048 0.10920 -0.00159 0.00559  0.01023  100 LEU A C   
784  O O   . LEU A 100 ? 0.12263 0.10366 0.11267 -0.00187 0.00740  0.01138  100 LEU A O   
785  C CB  . LEU A 100 ? 0.12272 0.10159 0.11049 0.00135  0.00476  0.01190  100 LEU A CB  
786  C CG  . LEU A 100 ? 0.12048 0.10252 0.10666 0.00250  0.00291  0.01171  100 LEU A CG  
787  C CD1 . LEU A 100 ? 0.11903 0.10414 0.10765 0.00242  0.00149  0.00993  100 LEU A CD1 
788  C CD2 . LEU A 100 ? 0.12444 0.10458 0.10717 0.00468  0.00209  0.01322  100 LEU A CD2 
789  N N   . CYS A 101 ? 0.11376 0.09982 0.10637 -0.00194 0.00400  0.00888  101 CYS A N   
790  C CA  . CYS A 101 ? 0.12336 0.11158 0.11646 -0.00261 0.00403  0.00851  101 CYS A CA  
791  C C   . CYS A 101 ? 0.10967 0.10030 0.10083 -0.00174 0.00237  0.00831  101 CYS A C   
792  O O   . CYS A 101 ? 0.11559 0.10742 0.10697 -0.00144 0.00097  0.00754  101 CYS A O   
793  C CB  . CYS A 101 ? 0.14827 0.13792 0.14539 -0.00409 0.00357  0.00688  101 CYS A CB  
794  S SG  . CYS A 101 ? 0.18807 0.17555 0.18910 -0.00546 0.00509  0.00638  101 CYS A SG  
795  N N   . PHE A 102 ? 0.12595 0.11713 0.11528 -0.00147 0.00275  0.00883  102 PHE A N   
796  C CA  . PHE A 102 ? 0.10821 0.10174 0.09633 -0.00094 0.00119  0.00835  102 PHE A CA  
797  C C   . PHE A 102 ? 0.14386 0.13789 0.13107 -0.00122 0.00193  0.00836  102 PHE A C   
798  O O   . PHE A 102 ? 0.11130 0.10354 0.09771 -0.00145 0.00388  0.00907  102 PHE A O   
799  C CB  . PHE A 102 ? 0.10963 0.10303 0.09534 0.00061  0.00009  0.00896  102 PHE A CB  
800  C CG  . PHE A 102 ? 0.11424 0.10474 0.09668 0.00174  0.00089  0.01054  102 PHE A CG  
801  C CD1 . PHE A 102 ? 0.11687 0.10462 0.09917 0.00219  0.00164  0.01143  102 PHE A CD1 
802  C CD2 . PHE A 102 ? 0.11676 0.10675 0.09564 0.00247  0.00079  0.01114  102 PHE A CD2 
803  C CE1 . PHE A 102 ? 0.12214 0.10640 0.10064 0.00335  0.00231  0.01313  102 PHE A CE1 
804  C CE2 . PHE A 102 ? 0.17922 0.16573 0.15381 0.00366  0.00138  0.01275  102 PHE A CE2 
805  C CZ  . PHE A 102 ? 0.16517 0.14866 0.13946 0.00412  0.00216  0.01388  102 PHE A CZ  
806  N N   . GLU A 103 ? 0.10630 0.10252 0.09361 -0.00127 0.00061  0.00749  103 GLU A N   
807  C CA  . GLU A 103 ? 0.10656 0.10338 0.09322 -0.00147 0.00113  0.00715  103 GLU A CA  
808  C C   . GLU A 103 ? 0.13157 0.12708 0.11383 -0.00037 0.00148  0.00801  103 GLU A C   
809  O O   . GLU A 103 ? 0.11112 0.10666 0.09136 0.00069  0.00003  0.00836  103 GLU A O   
810  C CB  . GLU A 103 ? 0.10781 0.10679 0.09567 -0.00181 -0.00051 0.00599  103 GLU A CB  
811  C CG  . GLU A 103 ? 0.12722 0.12680 0.11544 -0.00211 -0.00007 0.00530  103 GLU A CG  
812  C CD  . GLU A 103 ? 0.10133 0.10236 0.09040 -0.00241 -0.00174 0.00432  103 GLU A CD  
813  O OE1 . GLU A 103 ? 0.10122 0.10290 0.08874 -0.00207 -0.00284 0.00423  103 GLU A OE1 
814  O OE2 . GLU A 103 ? 0.11688 0.11823 0.10838 -0.00297 -0.00202 0.00362  103 GLU A OE2 
815  N N   . HIS A 104 ? 0.12731 0.12159 0.10811 -0.00057 0.00337  0.00820  104 HIS A N   
816  C CA  . HIS A 104 ? 0.15516 0.14739 0.13054 0.00050  0.00380  0.00902  104 HIS A CA  
817  C C   . HIS A 104 ? 0.16076 0.15474 0.13452 0.00119  0.00145  0.00810  104 HIS A C   
818  O O   . HIS A 104 ? 0.14547 0.14172 0.12190 0.00051  0.00073  0.00679  104 HIS A O   
819  C CB  . HIS A 104 ? 0.17416 0.16459 0.14823 -0.00007 0.00686  0.00915  104 HIS A CB  
820  C CG  . HIS A 104 ? 0.19322 0.18063 0.16037 0.00102  0.00759  0.01004  104 HIS A CG  
821  N ND1 . HIS A 104 ? 0.22688 0.21072 0.18926 0.00204  0.00783  0.01183  104 HIS A ND1 
822  C CD2 . HIS A 104 ? 0.15918 0.14609 0.12279 0.00134  0.00801  0.00936  104 HIS A CD2 
823  C CE1 . HIS A 104 ? 0.25659 0.23771 0.21229 0.00300  0.00820  0.01230  104 HIS A CE1 
824  N NE2 . HIS A 104 ? 0.21174 0.19474 0.16804 0.00254  0.00839  0.01072  104 HIS A NE2 
825  N N   . ASP A 105 ? 0.16797 0.16068 0.13746 0.00260  0.00007  0.00873  105 ASP A N   
826  C CA  . ASP A 105 ? 0.18386 0.17823 0.15208 0.00329  -0.00242 0.00766  105 ASP A CA  
827  C C   . ASP A 105 ? 0.22575 0.21721 0.18730 0.00463  -0.00266 0.00824  105 ASP A C   
828  O O   . ASP A 105 ? 0.23467 0.22291 0.19239 0.00560  -0.00207 0.00985  105 ASP A O   
829  C CB  . ASP A 105 ? 0.19681 0.19335 0.16771 0.00383  -0.00489 0.00733  105 ASP A CB  
830  C CG  . ASP A 105 ? 0.23372 0.23262 0.20505 0.00411  -0.00732 0.00583  105 ASP A CG  
831  O OD1 . ASP A 105 ? 0.21504 0.21370 0.18432 0.00390  -0.00728 0.00501  105 ASP A OD1 
832  O OD2 . ASP A 105 ? 0.22601 0.22702 0.20012 0.00447  -0.00912 0.00528  105 ASP A OD2 
833  N N   . THR A 106 ? 0.17176 0.16390 0.13149 0.00471  -0.00357 0.00692  106 THR A N   
834  C CA  . THR A 106 ? 0.22066 0.20967 0.17317 0.00591  -0.00377 0.00716  106 THR A CA  
835  C C   . THR A 106 ? 0.22755 0.21763 0.17825 0.00723  -0.00771 0.00611  106 THR A C   
836  O O   . THR A 106 ? 0.25352 0.24114 0.19794 0.00827  -0.00855 0.00583  106 THR A O   
837  C CB  . THR A 106 ? 0.27534 0.26356 0.22636 0.00503  -0.00132 0.00619  106 THR A CB  
838  O OG1 . THR A 106 ? 0.13502 0.12667 0.09043 0.00421  -0.00268 0.00420  106 THR A OG1 
839  C CG2 . THR A 106 ? 0.15927 0.14654 0.11265 0.00381  0.00260  0.00701  106 THR A CG2 
840  N N   . GLU A 107 ? 0.23171 0.22532 0.18779 0.00719  -0.01008 0.00535  107 GLU A N   
841  C CA  . GLU A 107 ? 0.23119 0.22628 0.18686 0.00842  -0.01391 0.00413  107 GLU A CA  
842  C C   . GLU A 107 ? 0.24255 0.23463 0.19310 0.01068  -0.01575 0.00555  107 GLU A C   
843  O O   . GLU A 107 ? 0.26164 0.25124 0.21085 0.01108  -0.01411 0.00753  107 GLU A O   
844  C CB  . GLU A 107 ? 0.22704 0.22666 0.19040 0.00763  -0.01533 0.00291  107 GLU A CB  
845  C CG  . GLU A 107 ? 0.21986 0.22188 0.18729 0.00567  -0.01435 0.00138  107 GLU A CG  
846  C CD  . GLU A 107 ? 0.24922 0.25510 0.22308 0.00489  -0.01578 0.00003  107 GLU A CD  
847  O OE1 . GLU A 107 ? 0.22152 0.22888 0.19692 0.00603  -0.01813 -0.00039 107 GLU A OE1 
848  O OE2 . GLU A 107 ? 0.32281 0.33004 0.30021 0.00318  -0.01447 -0.00062 107 GLU A OE2 
849  N N   . PRO A 108 ? 0.33780 0.32975 0.28533 0.01225  -0.01938 0.00452  108 PRO A N   
850  C CA  . PRO A 108 ? 0.20017 0.18850 0.14183 0.01478  -0.02165 0.00596  108 PRO A CA  
851  C C   . PRO A 108 ? 0.34163 0.33125 0.28791 0.01573  -0.02272 0.00690  108 PRO A C   
852  O O   . PRO A 108 ? 0.34038 0.32587 0.28233 0.01711  -0.02226 0.00910  108 PRO A O   
853  C CB  . PRO A 108 ? 0.27351 0.26257 0.21272 0.01613  -0.02605 0.00396  108 PRO A CB  
854  C CG  . PRO A 108 ? 0.30375 0.29485 0.24461 0.01419  -0.02485 0.00194  108 PRO A CG  
855  C CD  . PRO A 108 ? 0.25855 0.25289 0.20705 0.01189  -0.02164 0.00198  108 PRO A CD  
856  N N   . TYR A 109 ? 0.29445 0.28933 0.24928 0.01502  -0.02393 0.00527  109 TYR A N   
857  C CA  . TYR A 109 ? 0.32040 0.31657 0.27999 0.01587  -0.02448 0.00590  109 TYR A CA  
858  C C   . TYR A 109 ? 0.27614 0.27055 0.23643 0.01463  -0.02047 0.00771  109 TYR A C   
859  O O   . TYR A 109 ? 0.31226 0.30485 0.27263 0.01582  -0.02042 0.00911  109 TYR A O   
860  C CB  . TYR A 109 ? 0.34629 0.34842 0.31488 0.01512  -0.02599 0.00354  109 TYR A CB  
861  C CG  . TYR A 109 ? 0.32521 0.32909 0.29964 0.01543  -0.02542 0.00386  109 TYR A CG  
862  C CD1 . TYR A 109 ? 0.47632 0.47981 0.45143 0.01802  -0.02825 0.00414  109 TYR A CD1 
863  C CD2 . TYR A 109 ? 0.30800 0.31367 0.28705 0.01328  -0.02220 0.00375  109 TYR A CD2 
864  C CE1 . TYR A 109 ? 0.43627 0.44130 0.41693 0.01837  -0.02751 0.00420  109 TYR A CE1 
865  C CE2 . TYR A 109 ? 0.33762 0.34457 0.32143 0.01354  -0.02148 0.00383  109 TYR A CE2 
866  C CZ  . TYR A 109 ? 0.41518 0.42190 0.40000 0.01604  -0.02396 0.00399  109 TYR A CZ  
867  O OH  . TYR A 109 ? 0.51027 0.51820 0.50007 0.01635  -0.02302 0.00384  109 TYR A OH  
868  N N   . ALA A 110 ? 0.28054 0.27539 0.24163 0.01235  -0.01732 0.00754  110 ALA A N   
869  C CA  . ALA A 110 ? 0.27318 0.26672 0.23561 0.01106  -0.01385 0.00886  110 ALA A CA  
870  C C   . ALA A 110 ? 0.23011 0.21811 0.18609 0.01194  -0.01220 0.01119  110 ALA A C   
871  O O   . ALA A 110 ? 0.22304 0.20933 0.18011 0.01187  -0.01059 0.01250  110 ALA A O   
872  C CB  . ALA A 110 ? 0.23548 0.23070 0.20029 0.00870  -0.01145 0.00798  110 ALA A CB  
873  N N   . LYS A 111 ? 0.22340 0.20818 0.17236 0.01269  -0.01236 0.01168  111 LYS A N   
874  C CA  . LYS A 111 ? 0.33618 0.31494 0.27808 0.01343  -0.01035 0.01403  111 LYS A CA  
875  C C   . LYS A 111 ? 0.28909 0.26506 0.22892 0.01576  -0.01254 0.01556  111 LYS A C   
876  O O   . LYS A 111 ? 0.29550 0.26727 0.23298 0.01588  -0.01034 0.01762  111 LYS A O   
877  C CB  . LYS A 111 ? 0.24077 0.21629 0.17466 0.01387  -0.01012 0.01407  111 LYS A CB  
878  C CG  . LYS A 111 ? 0.35582 0.33346 0.29158 0.01173  -0.00755 0.01260  111 LYS A CG  
879  C CD  . LYS A 111 ? 0.33183 0.30592 0.25927 0.01227  -0.00706 0.01243  111 LYS A CD  
880  C CE  . LYS A 111 ? 0.30662 0.28298 0.23669 0.01030  -0.00453 0.01073  111 LYS A CE  
881  N NZ  . LYS A 111 ? 0.36647 0.33963 0.28858 0.01087  -0.00414 0.01009  111 LYS A NZ  
882  N N   . VAL A 112 ? 0.25745 0.23566 0.19857 0.01764  -0.01692 0.01448  112 VAL A N   
883  C CA  . VAL A 112 ? 0.30099 0.27692 0.24107 0.02020  -0.01952 0.01568  112 VAL A CA  
884  C C   . VAL A 112 ? 0.18881 0.16714 0.13652 0.01958  -0.01835 0.01563  112 VAL A C   
885  O O   . VAL A 112 ? 0.28148 0.25607 0.22774 0.02073  -0.01786 0.01742  112 VAL A O   
886  C CB  . VAL A 112 ? 0.24844 0.22661 0.18871 0.02249  -0.02487 0.01412  112 VAL A CB  
887  C CG1 . VAL A 112 ? 0.38717 0.36423 0.32883 0.02523  -0.02785 0.01491  112 VAL A CG1 
888  C CG2 . VAL A 112 ? 0.29479 0.26906 0.22560 0.02357  -0.02639 0.01441  112 VAL A CG2 
889  N N   . ARG A 113 ? 0.26215 0.24625 0.21760 0.01775  -0.01779 0.01358  113 ARG A N   
890  C CA  . ARG A 113 ? 0.24282 0.22905 0.20493 0.01703  -0.01650 0.01327  113 ARG A CA  
891  C C   . ARG A 113 ? 0.23810 0.22105 0.19900 0.01543  -0.01252 0.01481  113 ARG A C   
892  O O   . ARG A 113 ? 0.23461 0.21538 0.19658 0.01600  -0.01176 0.01582  113 ARG A O   
893  C CB  . ARG A 113 ? 0.24551 0.23786 0.21481 0.01532  -0.01656 0.01081  113 ARG A CB  
894  C CG  . ARG A 113 ? 0.23833 0.23254 0.21350 0.01412  -0.01463 0.01032  113 ARG A CG  
895  C CD  . ARG A 113 ? 0.22430 0.22277 0.20393 0.01179  -0.01354 0.00848  113 ARG A CD  
896  N NE  . ARG A 113 ? 0.20088 0.19824 0.17756 0.01008  -0.01171 0.00885  113 ARG A NE  
897  C CZ  . ARG A 113 ? 0.19765 0.19770 0.17655 0.00829  -0.01109 0.00754  113 ARG A CZ  
898  N NH1 . ARG A 113 ? 0.25842 0.26216 0.24203 0.00770  -0.01187 0.00589  113 ARG A NH1 
899  N NH2 . ARG A 113 ? 0.16064 0.15941 0.13706 0.00707  -0.00948 0.00789  113 ARG A NH2 
900  N N   . ASP A 114 ? 0.21892 0.20152 0.17811 0.01343  -0.00997 0.01483  114 ASP A N   
901  C CA  . ASP A 114 ? 0.23785 0.21827 0.19757 0.01165  -0.00627 0.01579  114 ASP A CA  
902  C C   . ASP A 114 ? 0.28601 0.26002 0.23981 0.01262  -0.00481 0.01826  114 ASP A C   
903  O O   . ASP A 114 ? 0.25016 0.22204 0.20560 0.01179  -0.00253 0.01912  114 ASP A O   
904  C CB  . ASP A 114 ? 0.22296 0.20497 0.18323 0.00947  -0.00412 0.01493  114 ASP A CB  
905  C CG  . ASP A 114 ? 0.17400 0.16144 0.14002 0.00829  -0.00514 0.01277  114 ASP A CG  
906  O OD1 . ASP A 114 ? 0.19405 0.18397 0.16392 0.00883  -0.00684 0.01195  114 ASP A OD1 
907  O OD2 . ASP A 114 ? 0.16301 0.15196 0.12967 0.00687  -0.00409 0.01188  114 ASP A OD2 
908  N N   . ALA A 115 ? 0.24588 0.21635 0.19248 0.01435  -0.00611 0.01942  115 ALA A N   
909  C CA  . ALA A 115 ? 0.25226 0.21571 0.19219 0.01553  -0.00487 0.02206  115 ALA A CA  
910  C C   . ALA A 115 ? 0.27950 0.24150 0.22154 0.01727  -0.00654 0.02285  115 ALA A C   
911  O O   . ALA A 115 ? 0.44167 0.39906 0.38238 0.01704  -0.00420 0.02458  115 ALA A O   
912  C CB  . ALA A 115 ? 0.29216 0.25170 0.22293 0.01737  -0.00653 0.02306  115 ALA A CB  
913  N N   . ALA A 116 ? 0.27377 0.23966 0.21960 0.01898  -0.01042 0.02143  116 ALA A N   
914  C CA  . ALA A 116 ? 0.27098 0.23593 0.21964 0.02085  -0.01206 0.02184  116 ALA A CA  
915  C C   . ALA A 116 ? 0.26458 0.23097 0.21960 0.01892  -0.00928 0.02123  116 ALA A C   
916  O O   . ALA A 116 ? 0.23981 0.20299 0.19545 0.01992  -0.00898 0.02223  116 ALA A O   
917  C CB  . ALA A 116 ? 0.34329 0.31306 0.29610 0.02286  -0.01650 0.01993  116 ALA A CB  
918  N N   . VAL A 117 ? 0.18486 0.15564 0.14431 0.01628  -0.00742 0.01957  117 VAL A N   
919  C CA  . VAL A 117 ? 0.28647 0.25854 0.25146 0.01447  -0.00521 0.01875  117 VAL A CA  
920  C C   . VAL A 117 ? 0.26702 0.23430 0.22967 0.01292  -0.00166 0.02033  117 VAL A C   
921  O O   . VAL A 117 ? 0.27309 0.23876 0.23854 0.01237  -0.00030 0.02040  117 VAL A O   
922  C CB  . VAL A 117 ? 0.23064 0.20871 0.20075 0.01245  -0.00499 0.01641  117 VAL A CB  
923  C CG1 . VAL A 117 ? 0.24926 0.22816 0.22409 0.01066  -0.00303 0.01549  117 VAL A CG1 
924  C CG2 . VAL A 117 ? 0.26670 0.24930 0.23977 0.01373  -0.00802 0.01477  117 VAL A CG2 
925  N N   A ARG A 118 ? 0.24709 0.21198 0.20490 0.01212  0.00009  0.02144  118 ARG A N   
926  N N   B ARG A 118 ? 0.24791 0.21285 0.20576 0.01210  0.00009  0.02142  118 ARG A N   
927  C CA  A ARG A 118 ? 0.29953 0.26000 0.25574 0.01042  0.00395  0.02281  118 ARG A CA  
928  C CA  B ARG A 118 ? 0.29894 0.25939 0.25507 0.01043  0.00394  0.02282  118 ARG A CA  
929  C C   A ARG A 118 ? 0.27673 0.23064 0.22931 0.01189  0.00444  0.02507  118 ARG A C   
930  C C   B ARG A 118 ? 0.27691 0.23088 0.22955 0.01190  0.00439  0.02505  118 ARG A C   
931  O O   A ARG A 118 ? 0.28066 0.23192 0.23540 0.01052  0.00703  0.02551  118 ARG A O   
932  O O   B ARG A 118 ? 0.28039 0.23183 0.23535 0.01055  0.00692  0.02544  118 ARG A O   
933  C CB  A ARG A 118 ? 0.30333 0.26232 0.25470 0.00949  0.00599  0.02348  118 ARG A CB  
934  C CB  B ARG A 118 ? 0.30321 0.26204 0.25427 0.00959  0.00591  0.02355  118 ARG A CB  
935  C CG  A ARG A 118 ? 0.30310 0.26781 0.25834 0.00779  0.00613  0.02132  118 ARG A CG  
936  C CG  B ARG A 118 ? 0.30398 0.26789 0.25936 0.00736  0.00706  0.02154  118 ARG A CG  
937  C CD  A ARG A 118 ? 0.32332 0.28601 0.27372 0.00702  0.00855  0.02192  118 ARG A CD  
938  C CD  B ARG A 118 ? 0.32247 0.28452 0.27235 0.00700  0.00886  0.02214  118 ARG A CD  
939  N NE  A ARG A 118 ? 0.30168 0.26950 0.25485 0.00605  0.00796  0.01988  118 ARG A NE  
940  N NE  B ARG A 118 ? 0.32152 0.28753 0.27578 0.00483  0.01063  0.02038  118 ARG A NE  
941  C CZ  A ARG A 118 ? 0.26846 0.23888 0.22647 0.00387  0.01019  0.01860  118 ARG A CZ  
942  C CZ  B ARG A 118 ? 0.27255 0.24371 0.22973 0.00469  0.00855  0.01847  118 ARG A CZ  
943  N NH1 A ARG A 118 ? 0.33560 0.30451 0.29681 0.00224  0.01316  0.01889  118 ARG A NH1 
944  N NH1 B ARG A 118 ? 0.29345 0.26698 0.25044 0.00627  0.00486  0.01784  118 ARG A NH1 
945  N NH2 A ARG A 118 ? 0.29701 0.27156 0.25700 0.00336  0.00926  0.01688  118 ARG A NH2 
946  N NH2 B ARG A 118 ? 0.29343 0.26733 0.25416 0.00291  0.01026  0.01707  118 ARG A NH2 
947  N N   . ARG A 119 ? 0.29031 0.24126 0.23738 0.01475  0.00176  0.02646  119 ARG A N   
948  C CA  . ARG A 119 ? 0.28248 0.22647 0.22543 0.01652  0.00185  0.02882  119 ARG A CA  
949  C C   . ARG A 119 ? 0.28676 0.23200 0.23596 0.01720  0.00073  0.02787  119 ARG A C   
950  O O   . ARG A 119 ? 0.21779 0.15771 0.16627 0.01728  0.00240  0.02929  119 ARG A O   
951  C CB  . ARG A 119 ? 0.30111 0.24159 0.23634 0.01975  -0.00142 0.03042  119 ARG A CB  
952  C CG  . ARG A 119 ? 0.30364 0.24119 0.23083 0.01929  -0.00002 0.03161  119 ARG A CG  
953  C CD  . ARG A 119 ? 0.30930 0.24365 0.22861 0.02269  -0.00410 0.03281  119 ARG A CD  
954  N NE  . ARG A 119 ? 0.30729 0.24862 0.23136 0.02413  -0.00875 0.03034  119 ARG A NE  
955  C CZ  . ARG A 119 ? 0.31065 0.25131 0.23013 0.02701  -0.01323 0.03042  119 ARG A CZ  
956  N NH1 . ARG A 119 ? 0.31111 0.24401 0.22003 0.02905  -0.01403 0.03299  119 ARG A NH1 
957  N NH2 . ARG A 119 ? 0.31122 0.25892 0.23673 0.02784  -0.01701 0.02781  119 ARG A NH2 
958  N N   . LEU A 120 ? 0.31264 0.26451 0.26788 0.01763  -0.00182 0.02541  120 LEU A N   
959  C CA  . LEU A 120 ? 0.23866 0.19211 0.20008 0.01799  -0.00234 0.02408  120 LEU A CA  
960  C C   . LEU A 120 ? 0.20573 0.15948 0.17130 0.01497  0.00101  0.02316  120 LEU A C   
961  O O   . LEU A 120 ? 0.27810 0.22969 0.24638 0.01506  0.00170  0.02295  120 LEU A O   
962  C CB  . LEU A 120 ? 0.23777 0.19820 0.20443 0.01886  -0.00523 0.02156  120 LEU A CB  
963  C CG  . LEU A 120 ? 0.22010 0.18115 0.18521 0.02217  -0.00926 0.02174  120 LEU A CG  
964  C CD1 . LEU A 120 ? 0.22597 0.19462 0.19721 0.02213  -0.01122 0.01893  120 LEU A CD1 
965  C CD2 . LEU A 120 ? 0.31718 0.27371 0.28194 0.02495  -0.01059 0.02288  120 LEU A CD2 
966  N N   . ALA A 121 ? 0.23970 0.19608 0.20607 0.01239  0.00288  0.02241  121 ALA A N   
967  C CA  . ALA A 121 ? 0.25768 0.21443 0.22824 0.00959  0.00561  0.02137  121 ALA A CA  
968  C C   . ALA A 121 ? 0.24934 0.19943 0.21721 0.00869  0.00872  0.02339  121 ALA A C   
969  O O   . ALA A 121 ? 0.25063 0.19922 0.22215 0.00725  0.01038  0.02276  121 ALA A O   
970  C CB  . ALA A 121 ? 0.21730 0.17889 0.18997 0.00739  0.00631  0.01989  121 ALA A CB  
971  N N   . ALA A 122 ? 0.24317 0.18890 0.20442 0.00942  0.00966  0.02576  122 ALA A N   
972  C CA  . ALA A 122 ? 0.29576 0.23429 0.25363 0.00857  0.01306  0.02798  122 ALA A CA  
973  C C   . ALA A 122 ? 0.22701 0.16050 0.18453 0.01025  0.01240  0.02907  122 ALA A C   
974  O O   . ALA A 122 ? 0.28527 0.21473 0.24449 0.00871  0.01515  0.02951  122 ALA A O   
975  C CB  . ALA A 122 ? 0.28725 0.22152 0.23667 0.00930  0.01414  0.03040  122 ALA A CB  
976  N N   . GLU A 123 ? 0.22783 0.16165 0.18390 0.01338  0.00875  0.02928  123 GLU A N   
977  C CA  . GLU A 123 ? 0.30087 0.22968 0.25699 0.01520  0.00812  0.03022  123 GLU A CA  
978  C C   . GLU A 123 ? 0.22025 0.15215 0.18435 0.01370  0.00866  0.02761  123 GLU A C   
979  O O   . GLU A 123 ? 0.25584 0.18279 0.22070 0.01379  0.00985  0.02820  123 GLU A O   
980  C CB  . GLU A 123 ? 0.28491 0.21362 0.23830 0.01916  0.00383  0.03084  123 GLU A CB  
981  C CG  . GLU A 123 ? 0.38211 0.30703 0.32670 0.02086  0.00279  0.03334  123 GLU A CG  
982  C CD  . GLU A 123 ? 0.39928 0.32658 0.34272 0.02449  -0.00226 0.03301  123 GLU A CD  
983  O OE1 . GLU A 123 ? 0.42698 0.36021 0.37739 0.02524  -0.00447 0.03054  123 GLU A OE1 
984  O OE2 . GLU A 123 ? 0.52705 0.45012 0.46261 0.02655  -0.00392 0.03513  123 GLU A OE2 
985  N N   . ALA A 124 ? 0.25074 0.19014 0.21999 0.01253  0.00766  0.02483  124 ALA A N   
986  C CA  . ALA A 124 ? 0.25720 0.19921 0.23291 0.01102  0.00815  0.02225  124 ALA A CA  
987  C C   . ALA A 124 ? 0.28464 0.22595 0.26288 0.00755  0.01129  0.02161  124 ALA A C   
988  O O   . ALA A 124 ? 0.30797 0.25120 0.29122 0.00610  0.01152  0.01930  124 ALA A O   
989  C CB  . ALA A 124 ? 0.21420 0.16378 0.19368 0.01118  0.00591  0.01964  124 ALA A CB  
990  N N   . GLY A 125 ? 0.29620 0.23484 0.27124 0.00621  0.01369  0.02339  125 GLY A N   
991  C CA  . GLY A 125 ? 0.27805 0.21677 0.25661 0.00286  0.01672  0.02252  125 GLY A CA  
992  C C   . GLY A 125 ? 0.23451 0.18041 0.21762 0.00110  0.01594  0.01990  125 GLY A C   
993  O O   . GLY A 125 ? 0.19461 0.14176 0.18278 -0.00132 0.01716  0.01811  125 GLY A O   
994  N N   . VAL A 126 ? 0.19274 0.14315 0.17422 0.00229  0.01377  0.01960  126 VAL A N   
995  C CA  . VAL A 126 ? 0.23088 0.18769 0.21604 0.00098  0.01269  0.01729  126 VAL A CA  
996  C C   . VAL A 126 ? 0.17431 0.13217 0.15820 -0.00032 0.01441  0.01792  126 VAL A C   
997  O O   . VAL A 126 ? 0.23515 0.19113 0.21372 0.00090  0.01472  0.01984  126 VAL A O   
998  C CB  . VAL A 126 ? 0.16635 0.12739 0.15110 0.00289  0.00949  0.01633  126 VAL A CB  
999  C CG1 . VAL A 126 ? 0.18406 0.15081 0.17146 0.00158  0.00856  0.01440  126 VAL A CG1 
1000 C CG2 . VAL A 126 ? 0.20949 0.16986 0.19630 0.00399  0.00828  0.01527  126 VAL A CG2 
1001 N N   . GLU A 127 ? 0.20915 0.16988 0.19788 -0.00266 0.01539  0.01615  127 GLU A N   
1002 C CA  . GLU A 127 ? 0.21622 0.17870 0.20501 -0.00390 0.01704  0.01621  127 GLU A CA  
1003 C C   . GLU A 127 ? 0.17519 0.14258 0.16296 -0.00294 0.01453  0.01539  127 GLU A C   
1004 O O   . GLU A 127 ? 0.13981 0.11068 0.12985 -0.00261 0.01197  0.01376  127 GLU A O   
1005 C CB  . GLU A 127 ? 0.22568 0.18979 0.22112 -0.00657 0.01864  0.01433  127 GLU A CB  
1006 C CG  . GLU A 127 ? 0.23849 0.20520 0.23536 -0.00777 0.02026  0.01390  127 GLU A CG  
1007 C CD  . GLU A 127 ? 0.25195 0.22136 0.25670 -0.01012 0.02098  0.01154  127 GLU A CD  
1008 O OE1 . GLU A 127 ? 0.24282 0.21220 0.25159 -0.01087 0.01985  0.01009  127 GLU A OE1 
1009 O OE2 . GLU A 127 ? 0.34733 0.31890 0.35444 -0.01114 0.02255  0.01094  127 GLU A OE2 
1010 N N   . VAL A 128 ? 0.25113 0.21840 0.23517 -0.00257 0.01548  0.01648  128 VAL A N   
1011 C CA  . VAL A 128 ? 0.15762 0.12888 0.14017 -0.00163 0.01328  0.01584  128 VAL A CA  
1012 C C   . VAL A 128 ? 0.14252 0.11637 0.12762 -0.00324 0.01478  0.01478  128 VAL A C   
1013 O O   . VAL A 128 ? 0.13589 0.10730 0.11948 -0.00401 0.01787  0.01570  128 VAL A O   
1014 C CB  . VAL A 128 ? 0.17301 0.14194 0.14865 0.00054  0.01246  0.01770  128 VAL A CB  
1015 C CG1 . VAL A 128 ? 0.24753 0.22079 0.22243 0.00139  0.00990  0.01668  128 VAL A CG1 
1016 C CG2 . VAL A 128 ? 0.22136 0.18722 0.19505 0.00231  0.01111  0.01882  128 VAL A CG2 
1017 N N   . VAL A 129 ? 0.16836 0.14683 0.15719 -0.00367 0.01274  0.01284  129 VAL A N   
1018 C CA  . VAL A 129 ? 0.16618 0.14757 0.15798 -0.00481 0.01344  0.01157  129 VAL A CA  
1019 C C   . VAL A 129 ? 0.15339 0.13769 0.14297 -0.00372 0.01109  0.01112  129 VAL A C   
1020 O O   . VAL A 129 ? 0.11689 0.10314 0.10690 -0.00310 0.00842  0.01042  129 VAL A O   
1021 C CB  . VAL A 129 ? 0.16229 0.14607 0.16098 -0.00636 0.01285  0.00955  129 VAL A CB  
1022 C CG1 . VAL A 129 ? 0.20869 0.19532 0.21109 -0.00731 0.01355  0.00821  129 VAL A CG1 
1023 C CG2 . VAL A 129 ? 0.20384 0.18475 0.20521 -0.00750 0.01475  0.00971  129 VAL A CG2 
1024 N N   . THR A 130 ? 0.12993 0.11430 0.11714 -0.00359 0.01234  0.01138  130 THR A N   
1025 C CA  . THR A 130 ? 0.13574 0.12226 0.12037 -0.00258 0.01034  0.01098  130 THR A CA  
1026 C C   . THR A 130 ? 0.11873 0.10729 0.10551 -0.00337 0.01139  0.00977  130 THR A C   
1027 O O   . THR A 130 ? 0.15126 0.13841 0.13461 -0.00313 0.01324  0.01024  130 THR A O   
1028 C CB  . THR A 130 ? 0.15056 0.13438 0.12835 -0.00098 0.01018  0.01258  130 THR A CB  
1029 O OG1 . THR A 130 ? 0.16601 0.14613 0.14058 -0.00130 0.01352  0.01381  130 THR A OG1 
1030 C CG2 . THR A 130 ? 0.18477 0.16713 0.16117 0.00019  0.00852  0.01351  130 THR A CG2 
1031 N N   . PRO A 131 ? 0.11578 0.10736 0.10783 -0.00416 0.01012  0.00814  131 PRO A N   
1032 C CA  . PRO A 131 ? 0.11310 0.10664 0.10790 -0.00468 0.01086  0.00685  131 PRO A CA  
1033 C C   . PRO A 131 ? 0.11197 0.10662 0.10343 -0.00373 0.00930  0.00657  131 PRO A C   
1034 O O   . PRO A 131 ? 0.12373 0.11854 0.11220 -0.00288 0.00710  0.00699  131 PRO A O   
1035 C CB  . PRO A 131 ? 0.15864 0.15456 0.15963 -0.00548 0.00911  0.00532  131 PRO A CB  
1036 C CG  . PRO A 131 ? 0.14286 0.13865 0.14222 -0.00499 0.00654  0.00567  131 PRO A CG  
1037 C CD  . PRO A 131 ? 0.12259 0.11563 0.11776 -0.00440 0.00770  0.00735  131 PRO A CD  
1038 N N   . ILE A 132 ? 0.12806 0.12351 0.12053 -0.00394 0.01062  0.00565  132 ILE A N   
1039 C CA  . ILE A 132 ? 0.11204 0.10843 0.10197 -0.00321 0.00931  0.00502  132 ILE A CA  
1040 C C   . ILE A 132 ? 0.10773 0.10674 0.10240 -0.00350 0.00719  0.00355  132 ILE A C   
1041 O O   . ILE A 132 ? 0.10672 0.10684 0.10649 -0.00409 0.00801  0.00250  132 ILE A O   
1042 C CB  . ILE A 132 ? 0.11621 0.11125 0.10347 -0.00308 0.01216  0.00482  132 ILE A CB  
1043 C CG1 . ILE A 132 ? 0.14067 0.13213 0.12148 -0.00257 0.01392  0.00657  132 ILE A CG1 
1044 C CG2 . ILE A 132 ? 0.13562 0.13176 0.12120 -0.00245 0.01064  0.00372  132 ILE A CG2 
1045 C CD1 . ILE A 132 ? 0.18314 0.17232 0.16339 -0.00327 0.01836  0.00682  132 ILE A CD1 
1046 N N   . SER A 133 ? 0.10569 0.10549 0.09881 -0.00306 0.00446  0.00344  133 SER A N   
1047 C CA  . SER A 133 ? 0.10270 0.10401 0.09899 -0.00326 0.00234  0.00237  133 SER A CA  
1048 C C   . SER A 133 ? 0.10209 0.10371 0.09567 -0.00286 0.00049  0.00215  133 SER A C   
1049 O O   . SER A 133 ? 0.10059 0.10274 0.09590 -0.00300 -0.00105 0.00140  133 SER A O   
1050 C CB  . SER A 133 ? 0.12621 0.12773 0.12501 -0.00371 0.00089  0.00246  133 SER A CB  
1051 O OG  . SER A 133 ? 0.19118 0.19171 0.18771 -0.00365 0.00118  0.00356  133 SER A OG  
1052 N N   . HIS A 134 ? 0.10374 0.10481 0.09318 -0.00236 0.00049  0.00273  134 HIS A N   
1053 C CA  . HIS A 134 ? 0.11681 0.11843 0.10449 -0.00216 -0.00119 0.00221  134 HIS A CA  
1054 C C   . HIS A 134 ? 0.10487 0.10635 0.09193 -0.00197 -0.00067 0.00112  134 HIS A C   
1055 O O   . HIS A 134 ? 0.10423 0.10609 0.09138 -0.00210 -0.00204 0.00030  134 HIS A O   
1056 C CB  . HIS A 134 ? 0.11209 0.11353 0.09644 -0.00155 -0.00188 0.00288  134 HIS A CB  
1057 C CG  . HIS A 134 ? 0.12249 0.12488 0.10602 -0.00151 -0.00366 0.00209  134 HIS A CG  
1058 N ND1 . HIS A 134 ? 0.11353 0.11683 0.09915 -0.00219 -0.00486 0.00172  134 HIS A ND1 
1059 C CD2 . HIS A 134 ? 0.11920 0.12158 0.10005 -0.00096 -0.00439 0.00149  134 HIS A CD2 
1060 C CE1 . HIS A 134 ? 0.14917 0.15322 0.13415 -0.00223 -0.00599 0.00090  134 HIS A CE1 
1061 N NE2 . HIS A 134 ? 0.11030 0.11398 0.09259 -0.00144 -0.00599 0.00064  134 HIS A NE2 
1062 N N   . THR A 135 ? 0.10730 0.10798 0.09371 -0.00176 0.00154  0.00101  135 THR A N   
1063 C CA  . THR A 135 ? 0.12099 0.12134 0.10697 -0.00154 0.00260  -0.00024 135 THR A CA  
1064 C C   . THR A 135 ? 0.10820 0.10919 0.09922 -0.00186 0.00401  -0.00101 135 THR A C   
1065 O O   . THR A 135 ? 0.11105 0.11253 0.10531 -0.00226 0.00445  -0.00051 135 THR A O   
1066 C CB  . THR A 135 ? 0.11821 0.11678 0.09894 -0.00098 0.00443  0.00000  135 THR A CB  
1067 O OG1 . THR A 135 ? 0.12261 0.12007 0.10284 -0.00110 0.00653  0.00129  135 THR A OG1 
1068 C CG2 . THR A 135 ? 0.14715 0.14531 0.12330 -0.00038 0.00227  0.00022  135 THR A CG2 
1069 N N   . LEU A 136 ? 0.10921 0.11024 0.10132 -0.00161 0.00459  -0.00245 136 LEU A N   
1070 C CA  . LEU A 136 ? 0.10860 0.11051 0.10628 -0.00167 0.00594  -0.00350 136 LEU A CA  
1071 C C   . LEU A 136 ? 0.11547 0.11708 0.11379 -0.00198 0.00946  -0.00324 136 LEU A C   
1072 O O   . LEU A 136 ? 0.12856 0.13131 0.13222 -0.00242 0.01016  -0.00339 136 LEU A O   
1073 C CB  . LEU A 136 ? 0.14278 0.14457 0.14137 -0.00116 0.00609  -0.00523 136 LEU A CB  
1074 C CG  . LEU A 136 ? 0.10822 0.10980 0.10687 -0.00100 0.00296  -0.00561 136 LEU A CG  
1075 C CD1 . LEU A 136 ? 0.11646 0.11737 0.11531 -0.00046 0.00355  -0.00739 136 LEU A CD1 
1076 C CD2 . LEU A 136 ? 0.10530 0.10757 0.10854 -0.00109 0.00078  -0.00531 136 LEU A CD2 
1077 N N   . TYR A 137 ? 0.11514 0.11490 0.10784 -0.00179 0.01169  -0.00287 137 TYR A N   
1078 C CA  . TYR A 137 ? 0.11883 0.11735 0.11089 -0.00218 0.01572  -0.00253 137 TYR A CA  
1079 C C   . TYR A 137 ? 0.12167 0.11786 0.10751 -0.00216 0.01609  -0.00049 137 TYR A C   
1080 O O   . TYR A 137 ? 0.12125 0.11696 0.10296 -0.00162 0.01332  0.00033  137 TYR A O   
1081 C CB  . TYR A 137 ? 0.12344 0.12075 0.11332 -0.00186 0.01878  -0.00392 137 TYR A CB  
1082 C CG  . TYR A 137 ? 0.19559 0.19491 0.19171 -0.00163 0.01870  -0.00612 137 TYR A CG  
1083 C CD1 . TYR A 137 ? 0.13213 0.13320 0.13585 -0.00206 0.02111  -0.00725 137 TYR A CD1 
1084 C CD2 . TYR A 137 ? 0.16685 0.16624 0.16171 -0.00094 0.01623  -0.00719 137 TYR A CD2 
1085 C CE1 . TYR A 137 ? 0.15065 0.15355 0.16053 -0.00154 0.02076  -0.00936 137 TYR A CE1 
1086 C CE2 . TYR A 137 ? 0.11980 0.12052 0.12025 -0.00053 0.01606  -0.00914 137 TYR A CE2 
1087 C CZ  . TYR A 137 ? 0.15944 0.16194 0.16737 -0.00070 0.01822  -0.01020 137 TYR A CZ  
1088 O OH  . TYR A 137 ? 0.20974 0.21358 0.22369 -0.00000 0.01777  -0.01223 137 TYR A OH  
1089 N N   . ASP A 138 ? 0.12569 0.12031 0.11130 -0.00274 0.01967  0.00025  138 ASP A N   
1090 C CA  . ASP A 138 ? 0.19118 0.18229 0.16939 -0.00249 0.02090  0.00217  138 ASP A CA  
1091 C C   . ASP A 138 ? 0.14687 0.13547 0.11723 -0.00158 0.02152  0.00184  138 ASP A C   
1092 O O   . ASP A 138 ? 0.14000 0.12736 0.10931 -0.00177 0.02506  0.00085  138 ASP A O   
1093 C CB  . ASP A 138 ? 0.19018 0.17961 0.17002 -0.00352 0.02518  0.00296  138 ASP A CB  
1094 C CG  . ASP A 138 ? 0.19080 0.17597 0.16313 -0.00322 0.02615  0.00534  138 ASP A CG  
1095 O OD1 . ASP A 138 ? 0.22803 0.21120 0.19290 -0.00199 0.02404  0.00615  138 ASP A OD1 
1096 O OD2 . ASP A 138 ? 0.22717 0.21081 0.20126 -0.00420 0.02895  0.00633  138 ASP A OD2 
1097 N N   . THR A 139 ? 0.14373 0.13165 0.10884 -0.00058 0.01806  0.00242  139 THR A N   
1098 C CA  . THR A 139 ? 0.15366 0.13942 0.11151 0.00036  0.01774  0.00171  139 THR A CA  
1099 C C   . THR A 139 ? 0.19818 0.17911 0.14805 0.00065  0.02133  0.00283  139 THR A C   
1100 O O   . THR A 139 ? 0.19323 0.17196 0.13785 0.00106  0.02299  0.00177  139 THR A O   
1101 C CB  . THR A 139 ? 0.21229 0.19866 0.16721 0.00131  0.01300  0.00194  139 THR A CB  
1102 O OG1 . THR A 139 ? 0.35339 0.33871 0.30664 0.00167  0.01187  0.00400  139 THR A OG1 
1103 C CG2 . THR A 139 ? 0.19795 0.18834 0.15967 0.00089  0.01009  0.00064  139 THR A CG2 
1104 N N   . ASP A 140 ? 0.22376 0.20247 0.17210 0.00043  0.02271  0.00497  140 ASP A N   
1105 C CA  . ASP A 140 ? 0.20620 0.17947 0.14658 0.00054  0.02663  0.00636  140 ASP A CA  
1106 C C   . ASP A 140 ? 0.23111 0.20406 0.17467 -0.00078 0.03228  0.00529  140 ASP A C   
1107 O O   . ASP A 140 ? 0.19484 0.16338 0.13114 -0.00070 0.03608  0.00552  140 ASP A O   
1108 C CB  . ASP A 140 ? 0.22624 0.19690 0.16472 0.00060  0.02667  0.00899  140 ASP A CB  
1109 C CG  . ASP A 140 ? 0.24209 0.21212 0.17598 0.00226  0.02160  0.01008  140 ASP A CG  
1110 O OD1 . ASP A 140 ? 0.36207 0.33095 0.28974 0.00354  0.01925  0.00942  140 ASP A OD1 
1111 O OD2 . ASP A 140 ? 0.29324 0.26398 0.23009 0.00231  0.01991  0.01138  140 ASP A OD2 
1112 N N   . MET A 141 ? 0.23637 0.21381 0.19069 -0.00194 0.03290  0.00403  141 MET A N   
1113 C CA  . MET A 141 ? 0.22315 0.20129 0.18243 -0.00309 0.03790  0.00247  141 MET A CA  
1114 C C   . MET A 141 ? 0.22022 0.19853 0.17731 -0.00245 0.03857  0.00023  141 MET A C   
1115 O O   . MET A 141 ? 0.21154 0.18728 0.16576 -0.00284 0.04356  -0.00050 141 MET A O   
1116 C CB  . MET A 141 ? 0.21238 0.19555 0.18411 -0.00417 0.03729  0.00142  141 MET A CB  
1117 C CG  . MET A 141 ? 0.15010 0.13518 0.12936 -0.00522 0.04175  -0.00066 141 MET A CG  
1118 S SD  . MET A 141 ? 0.31103 0.30018 0.29585 -0.00439 0.03958  -0.00372 141 MET A SD  
1119 C CE  . MET A 141 ? 0.13556 0.12898 0.12728 -0.00412 0.03312  -0.00357 141 MET A CE  
1120 N N   . LEU A 142 ? 0.18537 0.16636 0.14365 -0.00155 0.03387  -0.00096 142 LEU A N   
1121 C CA  . LEU A 142 ? 0.20931 0.19026 0.16558 -0.00092 0.03413  -0.00324 142 LEU A CA  
1122 C C   . LEU A 142 ? 0.18894 0.16443 0.13297 -0.00016 0.03602  -0.00284 142 LEU A C   
1123 O O   . LEU A 142 ? 0.21165 0.18546 0.15315 -0.00012 0.03954  -0.00455 142 LEU A O   
1124 C CB  . LEU A 142 ? 0.15201 0.13601 0.11079 -0.00021 0.02855  -0.00424 142 LEU A CB  
1125 C CG  . LEU A 142 ? 0.14283 0.13158 0.11234 -0.00068 0.02615  -0.00494 142 LEU A CG  
1126 C CD1 . LEU A 142 ? 0.18150 0.17185 0.15122 -0.00004 0.02135  -0.00581 142 LEU A CD1 
1127 C CD2 . LEU A 142 ? 0.21232 0.20296 0.18949 -0.00119 0.02951  -0.00687 142 LEU A CD2 
1128 N N   . VAL A 143 ? 0.17218 0.14462 0.10829 0.00059  0.03364  -0.00067 143 VAL A N   
1129 C CA  . VAL A 143 ? 0.20696 0.17354 0.13032 0.00157  0.03477  -0.00008 143 VAL A CA  
1130 C C   . VAL A 143 ? 0.21248 0.17470 0.13197 0.00070  0.04160  0.00073  143 VAL A C   
1131 O O   . VAL A 143 ? 0.25841 0.21658 0.17005 0.00103  0.04480  -0.00018 143 VAL A O   
1132 C CB  . VAL A 143 ? 0.23593 0.20038 0.15264 0.00279  0.03018  0.00211  143 VAL A CB  
1133 C CG1 . VAL A 143 ? 0.27685 0.23421 0.17960 0.00391  0.03155  0.00323  143 VAL A CG1 
1134 C CG2 . VAL A 143 ? 0.22642 0.19464 0.14579 0.00360  0.02408  0.00081  143 VAL A CG2 
1135 N N   . ALA A 144 ? 0.26519 0.22795 0.19007 -0.00052 0.04414  0.00233  144 ALA A N   
1136 C CA  . ALA A 144 ? 0.20502 0.16361 0.12711 -0.00168 0.05110  0.00316  144 ALA A CA  
1137 C C   . ALA A 144 ? 0.24152 0.20227 0.16983 -0.00268 0.05603  0.00035  144 ALA A C   
1138 O O   . ALA A 144 ? 0.26040 0.21673 0.18302 -0.00323 0.06202  0.00019  144 ALA A O   
1139 C CB  . ALA A 144 ? 0.26954 0.22855 0.19721 -0.00292 0.05235  0.00527  144 ALA A CB  
1140 N N   . ARG A 145 ? 0.21943 0.18664 0.15930 -0.00287 0.05376  -0.00189 145 ARG A N   
1141 C CA  . ARG A 145 ? 0.25448 0.22416 0.20133 -0.00350 0.05787  -0.00482 145 ARG A CA  
1142 C C   . ARG A 145 ? 0.23860 0.20584 0.17778 -0.00236 0.05833  -0.00679 145 ARG A C   
1143 O O   . ARG A 145 ? 0.27359 0.24064 0.21483 -0.00279 0.06340  -0.00899 145 ARG A O   
1144 C CB  . ARG A 145 ? 0.28854 0.26528 0.24951 -0.00373 0.05465  -0.00649 145 ARG A CB  
1145 C CG  . ARG A 145 ? 0.29173 0.27113 0.26131 -0.00496 0.05450  -0.00517 145 ARG A CG  
1146 C CD  . ARG A 145 ? 0.44630 0.42695 0.42420 -0.00653 0.06078  -0.00649 145 ARG A CD  
1147 N NE  . ARG A 145 ? 0.46991 0.45612 0.45962 -0.00637 0.06005  -0.00953 145 ARG A NE  
1148 C CZ  . ARG A 145 ? 0.41049 0.40174 0.41139 -0.00660 0.05666  -0.01015 145 ARG A CZ  
1149 N NH1 . ARG A 145 ? 0.36955 0.36126 0.37185 -0.00719 0.05403  -0.00815 145 ARG A NH1 
1150 N NH2 . ARG A 145 ? 0.48866 0.48425 0.49926 -0.00609 0.05573  -0.01291 145 ARG A NH2 
1151 N N   . ASN A 146 ? 0.25389 0.21935 0.18470 -0.00094 0.05320  -0.00628 146 ASN A N   
1152 C CA  . ASN A 146 ? 0.24192 0.20445 0.16423 0.00018  0.05305  -0.00818 146 ASN A CA  
1153 C C   . ASN A 146 ? 0.22543 0.18022 0.13288 0.00056  0.05649  -0.00681 146 ASN A C   
1154 O O   . ASN A 146 ? 0.25825 0.20957 0.15588 0.00176  0.05508  -0.00792 146 ASN A O   
1155 C CB  . ASN A 146 ? 0.25218 0.21678 0.17355 0.00142  0.04562  -0.00868 146 ASN A CB  
1156 C CG  . ASN A 146 ? 0.28996 0.25370 0.20772 0.00229  0.04505  -0.01171 146 ASN A CG  
1157 O OD1 . ASN A 146 ? 0.26988 0.23424 0.19145 0.00195  0.04925  -0.01407 146 ASN A OD1 
1158 N ND2 . ASN A 146 ? 0.23876 0.20112 0.14959 0.00343  0.03983  -0.01186 146 ASN A ND2 
1159 N N   . GLY A 147 ? 0.28513 0.23672 0.19037 -0.00044 0.06093  -0.00447 147 GLY A N   
1160 C CA  . GLY A 147 ? 0.29058 0.23391 0.18104 -0.00013 0.06463  -0.00281 147 GLY A CA  
1161 C C   . GLY A 147 ? 0.23775 0.17679 0.11773 0.00119  0.05982  0.00023  147 GLY A C   
1162 O O   . GLY A 147 ? 0.27452 0.20590 0.14045 0.00188  0.06187  0.00169  147 GLY A O   
1163 N N   . GLY A 148 ? 0.26958 0.21304 0.15568 0.00167  0.05352  0.00119  148 GLY A N   
1164 C CA  . GLY A 148 ? 0.29501 0.23514 0.17311 0.00302  0.04881  0.00394  148 GLY A CA  
1165 C C   . GLY A 148 ? 0.30065 0.24193 0.17480 0.00489  0.04147  0.00291  148 GLY A C   
1166 O O   . GLY A 148 ? 0.37349 0.31157 0.24005 0.00634  0.03740  0.00489  148 GLY A O   
1167 N N   . ALA A 149 ? 0.34675 0.29237 0.22612 0.00494  0.03960  -0.00022 149 ALA A N   
1168 C CA  . ALA A 149 ? 0.33759 0.28478 0.21472 0.00638  0.03282  -0.00159 149 ALA A CA  
1169 C C   . ALA A 149 ? 0.34148 0.29599 0.23140 0.00565  0.03060  -0.00405 149 ALA A C   
1170 O O   . ALA A 149 ? 0.30145 0.25807 0.19773 0.00461  0.03454  -0.00583 149 ALA A O   
1171 C CB  . ALA A 149 ? 0.29585 0.23740 0.15997 0.00761  0.03297  -0.00316 149 ALA A CB  
1172 N N   . ALA A 150 ? 0.31005 0.26817 0.20371 0.00623  0.02438  -0.00415 150 ALA A N   
1173 C CA  . ALA A 150 ? 0.29104 0.25536 0.19605 0.00551  0.02213  -0.00610 150 ALA A CA  
1174 C C   . ALA A 150 ? 0.32133 0.28533 0.22462 0.00577  0.02213  -0.00938 150 ALA A C   
1175 O O   . ALA A 150 ? 0.29807 0.25807 0.19131 0.00685  0.02077  -0.01030 150 ALA A O   
1176 C CB  . ALA A 150 ? 0.22721 0.19497 0.13605 0.00593  0.01598  -0.00541 150 ALA A CB  
1177 N N   . PRO A 151 ? 0.30454 0.27232 0.21720 0.00491  0.02350  -0.01128 151 PRO A N   
1178 C CA  . PRO A 151 ? 0.31221 0.27985 0.22420 0.00521  0.02293  -0.01453 151 PRO A CA  
1179 C C   . PRO A 151 ? 0.27958 0.24838 0.19036 0.00580  0.01660  -0.01544 151 PRO A C   
1180 O O   . PRO A 151 ? 0.23523 0.20720 0.15096 0.00558  0.01290  -0.01407 151 PRO A O   
1181 C CB  . PRO A 151 ? 0.25099 0.22291 0.17498 0.00429  0.02488  -0.01579 151 PRO A CB  
1182 C CG  . PRO A 151 ? 0.22449 0.19798 0.15391 0.00348  0.02770  -0.01346 151 PRO A CG  
1183 C CD  . PRO A 151 ? 0.30506 0.27721 0.22935 0.00377  0.02514  -0.01063 151 PRO A CD  
1184 N N   . LEU A 152 ? 0.24029 0.20644 0.14455 0.00648  0.01549  -0.01795 152 LEU A N   
1185 C CA  . LEU A 152 ? 0.34025 0.30741 0.24360 0.00691  0.00957  -0.01932 152 LEU A CA  
1186 C C   . LEU A 152 ? 0.21457 0.18432 0.12499 0.00628  0.00838  -0.02222 152 LEU A C   
1187 O O   . LEU A 152 ? 0.25521 0.22595 0.16599 0.00634  0.00377  -0.02370 152 LEU A O   
1188 C CB  . LEU A 152 ? 0.31744 0.27944 0.20771 0.00826  0.00790  -0.02014 152 LEU A CB  
1189 C CG  . LEU A 152 ? 0.41572 0.37460 0.29827 0.00917  0.00777  -0.01702 152 LEU A CG  
1190 C CD1 . LEU A 152 ? 0.43790 0.39117 0.30679 0.01077  0.00535  -0.01788 152 LEU A CD1 
1191 C CD2 . LEU A 152 ? 0.39975 0.36277 0.28910 0.00901  0.00387  -0.01484 152 LEU A CD2 
1192 N N   . THR A 153 ? 0.24333 0.21414 0.15979 0.00571  0.01231  -0.02312 153 THR A N   
1193 C CA  . THR A 153 ? 0.28070 0.25359 0.20439 0.00523  0.01131  -0.02556 153 THR A CA  
1194 C C   . THR A 153 ? 0.23422 0.21086 0.16893 0.00447  0.01284  -0.02435 153 THR A C   
1195 O O   . THR A 153 ? 0.20231 0.17942 0.13888 0.00433  0.01630  -0.02267 153 THR A O   
1196 C CB  . THR A 153 ? 0.25954 0.22925 0.17924 0.00571  0.01425  -0.02878 153 THR A CB  
1197 O OG1 . THR A 153 ? 0.30967 0.27872 0.23066 0.00572  0.02012  -0.02845 153 THR A OG1 
1198 C CG2 . THR A 153 ? 0.20448 0.16974 0.11188 0.00659  0.01282  -0.03010 153 THR A CG2 
1199 N N   . MET A 154 ? 0.19866 0.17765 0.14052 0.00396  0.01012  -0.02529 154 MET A N   
1200 C CA  . MET A 154 ? 0.20795 0.19000 0.15964 0.00343  0.01076  -0.02423 154 MET A CA  
1201 C C   . MET A 154 ? 0.23856 0.22028 0.19378 0.00381  0.01528  -0.02551 154 MET A C   
1202 O O   . MET A 154 ? 0.25767 0.24158 0.21931 0.00362  0.01696  -0.02418 154 MET A O   
1203 C CB  . MET A 154 ? 0.22463 0.20814 0.18180 0.00286  0.00703  -0.02499 154 MET A CB  
1204 C CG  . MET A 154 ? 0.22066 0.20627 0.18699 0.00259  0.00738  -0.02427 154 MET A CG  
1205 S SD  . MET A 154 ? 0.28738 0.27571 0.25754 0.00225  0.00807  -0.02089 154 MET A SD  
1206 C CE  . MET A 154 ? 0.16331 0.15272 0.13143 0.00151  0.00388  -0.01911 154 MET A CE  
1207 N N   . GLN A 155 ? 0.20383 0.18289 0.15523 0.00439  0.01726  -0.02829 155 GLN A N   
1208 C CA  . GLN A 155 ? 0.24494 0.22379 0.20013 0.00484  0.02191  -0.02990 155 GLN A CA  
1209 C C   . GLN A 155 ? 0.24377 0.22257 0.19752 0.00472  0.02637  -0.02830 155 GLN A C   
1210 O O   . GLN A 155 ? 0.22657 0.20781 0.18831 0.00458  0.02877  -0.02787 155 GLN A O   
1211 C CB  . GLN A 155 ? 0.22161 0.19713 0.17169 0.00550  0.02339  -0.03336 155 GLN A CB  
1212 C CG  . GLN A 155 ? 0.26352 0.23878 0.21782 0.00609  0.02846  -0.03553 155 GLN A CG  
1213 C CD  . GLN A 155 ? 0.24210 0.21950 0.20696 0.00644  0.02715  -0.03683 155 GLN A CD  
1214 O OE1 . GLN A 155 ? 0.24033 0.21982 0.21317 0.00680  0.02983  -0.03706 155 GLN A OE1 
1215 N NE2 . GLN A 155 ? 0.24477 0.22143 0.20984 0.00637  0.02293  -0.03775 155 GLN A NE2 
1216 N N   . SER A 156 ? 0.24556 0.22134 0.18918 0.00478  0.02743  -0.02743 156 SER A N   
1217 C CA  . SER A 156 ? 0.25781 0.23270 0.19925 0.00450  0.03201  -0.02572 156 SER A CA  
1218 C C   . SER A 156 ? 0.19372 0.17181 0.14104 0.00380  0.03061  -0.02264 156 SER A C   
1219 O O   . SER A 156 ? 0.18352 0.16241 0.13437 0.00331  0.03448  -0.02164 156 SER A O   
1220 C CB  . SER A 156 ? 0.21982 0.18975 0.14776 0.00488  0.03308  -0.02524 156 SER A CB  
1221 O OG  . SER A 156 ? 0.30377 0.27334 0.22683 0.00509  0.02765  -0.02379 156 SER A OG  
1222 N N   . PHE A 157 ? 0.20741 0.18729 0.15608 0.00365  0.02532  -0.02129 157 PHE A N   
1223 C CA  . PHE A 157 ? 0.19660 0.17948 0.15112 0.00302  0.02388  -0.01866 157 PHE A CA  
1224 C C   . PHE A 157 ? 0.20741 0.19373 0.17326 0.00276  0.02461  -0.01926 157 PHE A C   
1225 O O   . PHE A 157 ? 0.19995 0.18813 0.17085 0.00225  0.02614  -0.01782 157 PHE A O   
1226 C CB  . PHE A 157 ? 0.20494 0.18885 0.15834 0.00294  0.01838  -0.01744 157 PHE A CB  
1227 C CG  . PHE A 157 ? 0.16212 0.14863 0.12038 0.00236  0.01690  -0.01485 157 PHE A CG  
1228 C CD1 . PHE A 157 ? 0.18928 0.17466 0.14314 0.00229  0.01761  -0.01255 157 PHE A CD1 
1229 C CD2 . PHE A 157 ? 0.19118 0.18076 0.15786 0.00195  0.01472  -0.01472 157 PHE A CD2 
1230 C CE1 . PHE A 157 ? 0.14628 0.13384 0.10454 0.00178  0.01628  -0.01040 157 PHE A CE1 
1231 C CE2 . PHE A 157 ? 0.13732 0.12893 0.10778 0.00144  0.01336  -0.01253 157 PHE A CE2 
1232 C CZ  . PHE A 157 ? 0.15663 0.14739 0.12312 0.00133  0.01420  -0.01049 157 PHE A CZ  
1233 N N   . THR A 158 ? 0.23694 0.22392 0.20694 0.00317  0.02326  -0.02144 158 THR A N   
1234 C CA  . THR A 158 ? 0.24144 0.23128 0.22194 0.00326  0.02322  -0.02203 158 THR A CA  
1235 C C   . THR A 158 ? 0.21188 0.20236 0.19673 0.00339  0.02842  -0.02319 158 THR A C   
1236 O O   . THR A 158 ? 0.28217 0.27552 0.27569 0.00327  0.02876  -0.02283 158 THR A O   
1237 C CB  . THR A 158 ? 0.25766 0.24721 0.24083 0.00382  0.02058  -0.02403 158 THR A CB  
1238 O OG1 . THR A 158 ? 0.19817 0.18713 0.17755 0.00342  0.01622  -0.02309 158 THR A OG1 
1239 C CG2 . THR A 158 ? 0.23652 0.22853 0.22995 0.00418  0.01959  -0.02428 158 THR A CG2 
1240 N N   . LYS A 159 ? 0.23038 0.21817 0.20939 0.00361  0.03256  -0.02472 159 LYS A N   
1241 C CA  . LYS A 159 ? 0.16772 0.15601 0.15071 0.00349  0.03832  -0.02582 159 LYS A CA  
1242 C C   . LYS A 159 ? 0.28106 0.26996 0.26409 0.00245  0.04046  -0.02331 159 LYS A C   
1243 O O   . LYS A 159 ? 0.32736 0.31857 0.31840 0.00203  0.04370  -0.02373 159 LYS A O   
1244 C CB  . LYS A 159 ? 0.21815 0.20270 0.19355 0.00388  0.04264  -0.02804 159 LYS A CB  
1245 C CG  . LYS A 159 ? 0.26423 0.24732 0.23777 0.00484  0.04045  -0.03066 159 LYS A CG  
1246 C CD  . LYS A 159 ? 0.25465 0.24090 0.23965 0.00551  0.03829  -0.03215 159 LYS A CD  
1247 C CE  . LYS A 159 ? 0.24096 0.22725 0.22547 0.00564  0.03201  -0.03147 159 LYS A CE  
1248 N NZ  . LYS A 159 ? 0.25620 0.24398 0.24973 0.00650  0.02997  -0.03309 159 LYS A NZ  
1249 N N   . LEU A 160 ? 0.25814 0.24500 0.23285 0.00207  0.03858  -0.02083 160 LEU A N   
1250 C CA  . LEU A 160 ? 0.25572 0.24258 0.23004 0.00113  0.04037  -0.01830 160 LEU A CA  
1251 C C   . LEU A 160 ? 0.24532 0.23652 0.23031 0.00067  0.03796  -0.01737 160 LEU A C   
1252 O O   . LEU A 160 ? 0.26773 0.26055 0.25890 -0.00009 0.04110  -0.01718 160 LEU A O   
1253 C CB  . LEU A 160 ? 0.26035 0.24406 0.22386 0.00118  0.03798  -0.01594 160 LEU A CB  
1254 C CG  . LEU A 160 ? 0.24517 0.22824 0.20733 0.00037  0.03904  -0.01302 160 LEU A CG  
1255 C CD1 . LEU A 160 ? 0.19719 0.17783 0.15766 -0.00036 0.04585  -0.01304 160 LEU A CD1 
1256 C CD2 . LEU A 160 ? 0.23230 0.21262 0.18472 0.00086  0.03549  -0.01092 160 LEU A CD2 
1257 N N   . VAL A 161 ? 0.26531 0.25823 0.25252 0.00105  0.03243  -0.01691 161 VAL A N   
1258 C CA  . VAL A 161 ? 0.24450 0.24084 0.24030 0.00071  0.02976  -0.01594 161 VAL A CA  
1259 C C   . VAL A 161 ? 0.23502 0.23421 0.24152 0.00102  0.03119  -0.01810 161 VAL A C   
1260 O O   . VAL A 161 ? 0.24052 0.24238 0.25470 0.00060  0.03082  -0.01768 161 VAL A O   
1261 C CB  . VAL A 161 ? 0.21175 0.20857 0.20640 0.00100  0.02397  -0.01496 161 VAL A CB  
1262 C CG1 . VAL A 161 ? 0.17392 0.16846 0.15922 0.00080  0.02255  -0.01308 161 VAL A CG1 
1263 C CG2 . VAL A 161 ? 0.24081 0.23738 0.23657 0.00184  0.02213  -0.01703 161 VAL A CG2 
1264 N N   . ASP A 162 ? 0.26110 0.25977 0.26858 0.00185  0.03271  -0.02061 162 ASP A N   
1265 C CA  . ASP A 162 ? 0.26343 0.26480 0.28150 0.00238  0.03446  -0.02296 162 ASP A CA  
1266 C C   . ASP A 162 ? 0.28191 0.28425 0.30376 0.00147  0.04019  -0.02342 162 ASP A C   
1267 O O   . ASP A 162 ? 0.25895 0.26471 0.29158 0.00145  0.04082  -0.02453 162 ASP A O   
1268 C CB  . ASP A 162 ? 0.25869 0.25883 0.27639 0.00354  0.03518  -0.02568 162 ASP A CB  
1269 C CG  . ASP A 162 ? 0.26143 0.26104 0.27852 0.00437  0.02960  -0.02559 162 ASP A CG  
1270 O OD1 . ASP A 162 ? 0.31598 0.31655 0.33407 0.00408  0.02537  -0.02357 162 ASP A OD1 
1271 O OD2 . ASP A 162 ? 0.32626 0.32418 0.34170 0.00522  0.02967  -0.02761 162 ASP A OD2 
1272 N N   . ARG A 163 ? 0.27358 0.27272 0.28671 0.00072  0.04442  -0.02266 163 ARG A N   
1273 C CA  . ARG A 163 ? 0.23905 0.23837 0.25483 -0.00047 0.05037  -0.02273 163 ARG A CA  
1274 C C   . ARG A 163 ? 0.27782 0.27845 0.29619 -0.00164 0.04911  -0.02028 163 ARG A C   
1275 O O   . ARG A 163 ? 0.26702 0.26969 0.29311 -0.00265 0.05258  -0.02082 163 ARG A O   
1276 C CB  . ARG A 163 ? 0.27752 0.27192 0.28174 -0.00085 0.05541  -0.02249 163 ARG A CB  
1277 C CG  . ARG A 163 ? 0.32429 0.31772 0.32871 -0.00017 0.05970  -0.02569 163 ARG A CG  
1278 C CD  . ARG A 163 ? 0.27438 0.26265 0.26777 -0.00082 0.06585  -0.02543 163 ARG A CD  
1279 N NE  . ARG A 163 ? 0.41237 0.39602 0.39183 -0.00010 0.06320  -0.02438 163 ARG A NE  
1280 C CZ  . ARG A 163 ? 0.31836 0.29902 0.28844 -0.00043 0.06115  -0.02133 163 ARG A CZ  
1281 N NH1 . ARG A 163 ? 0.34327 0.32467 0.31571 -0.00152 0.06160  -0.01886 163 ARG A NH1 
1282 N NH2 . ARG A 163 ? 0.42551 0.40234 0.38391 0.00043  0.05843  -0.02093 163 ARG A NH2 
1283 N N   . VAL A 164 ? 0.26137 0.26094 0.27392 -0.00157 0.04433  -0.01781 164 VAL A N   
1284 C CA  . VAL A 164 ? 0.29180 0.29234 0.30643 -0.00258 0.04294  -0.01559 164 VAL A CA  
1285 C C   . VAL A 164 ? 0.27215 0.27723 0.29872 -0.00244 0.03958  -0.01652 164 VAL A C   
1286 O O   . VAL A 164 ? 0.24523 0.25220 0.27832 -0.00345 0.04066  -0.01626 164 VAL A O   
1287 C CB  . VAL A 164 ? 0.24818 0.24620 0.25309 -0.00240 0.03903  -0.01292 164 VAL A CB  
1288 C CG1 . VAL A 164 ? 0.25301 0.25247 0.26123 -0.00315 0.03657  -0.01098 164 VAL A CG1 
1289 C CG2 . VAL A 164 ? 0.21771 0.21093 0.21098 -0.00255 0.04238  -0.01175 164 VAL A CG2 
1290 N N   . GLY A 165 ? 0.25715 0.26365 0.28654 -0.00117 0.03541  -0.01767 165 GLY A N   
1291 C CA  . GLY A 165 ? 0.32282 0.33283 0.36223 -0.00066 0.03159  -0.01852 165 GLY A CA  
1292 C C   . GLY A 165 ? 0.23246 0.24201 0.26852 -0.00032 0.02557  -0.01662 165 GLY A C   
1293 O O   . GLY A 165 ? 0.22507 0.23211 0.25213 -0.00029 0.02412  -0.01508 165 GLY A O   
1294 N N   . ASP A 166 ? 0.21264 0.22466 0.25631 -0.00003 0.02207  -0.01691 166 ASP A N   
1295 C CA  . ASP A 166 ? 0.15904 0.17048 0.20004 0.00024  0.01668  -0.01525 166 ASP A CA  
1296 C C   . ASP A 166 ? 0.19917 0.20922 0.23380 -0.00093 0.01680  -0.01279 166 ASP A C   
1297 O O   . ASP A 166 ? 0.14345 0.15360 0.17860 -0.00198 0.02031  -0.01240 166 ASP A O   
1298 C CB  . ASP A 166 ? 0.19379 0.20767 0.24373 0.00081  0.01312  -0.01615 166 ASP A CB  
1299 C CG  . ASP A 166 ? 0.20137 0.21629 0.25755 0.00237  0.01195  -0.01842 166 ASP A CG  
1300 O OD1 . ASP A 166 ? 0.24764 0.26061 0.29938 0.00314  0.01170  -0.01867 166 ASP A OD1 
1301 O OD2 . ASP A 166 ? 0.23351 0.25116 0.29936 0.00291  0.01111  -0.02012 166 ASP A OD2 
1302 N N   . PRO A 167 ? 0.18176 0.19033 0.21054 -0.00079 0.01322  -0.01114 167 PRO A N   
1303 C CA  . PRO A 167 ? 0.14180 0.14945 0.16607 -0.00167 0.01267  -0.00899 167 PRO A CA  
1304 C C   . PRO A 167 ? 0.13866 0.14805 0.16912 -0.00214 0.01111  -0.00893 167 PRO A C   
1305 O O   . PRO A 167 ? 0.13199 0.14321 0.16960 -0.00159 0.00930  -0.01042 167 PRO A O   
1306 C CB  . PRO A 167 ? 0.16299 0.16912 0.18117 -0.00127 0.00912  -0.00785 167 PRO A CB  
1307 C CG  . PRO A 167 ? 0.11533 0.12181 0.13685 -0.00032 0.00679  -0.00923 167 PRO A CG  
1308 C CD  . PRO A 167 ? 0.12770 0.13513 0.15367 0.00011  0.00995  -0.01126 167 PRO A CD  
1309 N N   . PRO A 168 ? 0.13913 0.14784 0.16716 -0.00305 0.01153  -0.00739 168 PRO A N   
1310 C CA  . PRO A 168 ? 0.15608 0.16620 0.18973 -0.00358 0.00986  -0.00754 168 PRO A CA  
1311 C C   . PRO A 168 ? 0.14814 0.15846 0.18258 -0.00281 0.00478  -0.00762 168 PRO A C   
1312 O O   . PRO A 168 ? 0.14845 0.15725 0.17733 -0.00229 0.00273  -0.00673 168 PRO A O   
1313 C CB  . PRO A 168 ? 0.14946 0.15791 0.17829 -0.00452 0.01115  -0.00563 168 PRO A CB  
1314 C CG  . PRO A 168 ? 0.10761 0.11418 0.13057 -0.00459 0.01487  -0.00489 168 PRO A CG  
1315 C CD  . PRO A 168 ? 0.17758 0.18402 0.19802 -0.00355 0.01374  -0.00562 168 PRO A CD  
1316 N N   . ALA A 169 ? 0.22354 0.23554 0.26498 -0.00277 0.00278  -0.00881 169 ALA A N   
1317 C CA  . ALA A 169 ? 0.17151 0.18300 0.21305 -0.00196 -0.00217 -0.00885 169 ALA A CA  
1318 C C   . ALA A 169 ? 0.16135 0.17085 0.19628 -0.00249 -0.00380 -0.00698 169 ALA A C   
1319 O O   . ALA A 169 ? 0.16676 0.17601 0.19999 -0.00346 -0.00172 -0.00610 169 ALA A O   
1320 C CB  . ALA A 169 ? 0.17650 0.19014 0.22689 -0.00169 -0.00429 -0.01070 169 ALA A CB  
1321 N N   . PRO A 170 ? 0.18001 0.18775 0.21103 -0.00185 -0.00727 -0.00634 170 PRO A N   
1322 C CA  . PRO A 170 ? 0.15559 0.16151 0.18073 -0.00237 -0.00850 -0.00481 170 PRO A CA  
1323 C C   . PRO A 170 ? 0.16360 0.16994 0.19159 -0.00294 -0.00952 -0.00519 170 PRO A C   
1324 O O   . PRO A 170 ? 0.15450 0.16201 0.18844 -0.00263 -0.01136 -0.00668 170 PRO A O   
1325 C CB  . PRO A 170 ? 0.13403 0.13780 0.15553 -0.00161 -0.01177 -0.00441 170 PRO A CB  
1326 C CG  . PRO A 170 ? 0.13017 0.13464 0.15702 -0.00051 -0.01338 -0.00590 170 PRO A CG  
1327 C CD  . PRO A 170 ? 0.15856 0.16547 0.18994 -0.00065 -0.00984 -0.00692 170 PRO A CD  
1328 N N   . ALA A 171 ? 0.14319 0.14859 0.16723 -0.00372 -0.00842 -0.00400 171 ALA A N   
1329 C CA  . ALA A 171 ? 0.11709 0.12252 0.14336 -0.00439 -0.00907 -0.00440 171 ALA A CA  
1330 C C   . ALA A 171 ? 0.16433 0.16834 0.18957 -0.00389 -0.01337 -0.00491 171 ALA A C   
1331 O O   . ALA A 171 ? 0.19618 0.19831 0.21644 -0.00330 -0.01515 -0.00417 171 ALA A O   
1332 C CB  . ALA A 171 ? 0.13513 0.13939 0.15691 -0.00509 -0.00697 -0.00296 171 ALA A CB  
1333 N N   . PRO A 172 ? 0.11746 0.12198 0.14706 -0.00417 -0.01508 -0.00622 172 PRO A N   
1334 C CA  . PRO A 172 ? 0.12525 0.12785 0.15290 -0.00358 -0.01949 -0.00679 172 PRO A CA  
1335 C C   . PRO A 172 ? 0.15682 0.15646 0.17623 -0.00384 -0.01971 -0.00538 172 PRO A C   
1336 O O   . PRO A 172 ? 0.14026 0.13982 0.15676 -0.00449 -0.01677 -0.00420 172 PRO A O   
1337 C CB  . PRO A 172 ? 0.17670 0.18077 0.21117 -0.00407 -0.02076 -0.00872 172 PRO A CB  
1338 C CG  . PRO A 172 ? 0.22674 0.23253 0.26443 -0.00536 -0.01626 -0.00848 172 PRO A CG  
1339 C CD  . PRO A 172 ? 0.09968 0.10629 0.13611 -0.00513 -0.01306 -0.00735 172 PRO A CD  
1340 N N   . ASP A 173 ? 0.20171 0.19870 0.21725 -0.00323 -0.02328 -0.00557 173 ASP A N   
1341 C CA  . ASP A 173 ? 0.24311 0.23703 0.25077 -0.00350 -0.02330 -0.00445 173 ASP A CA  
1342 C C   . ASP A 173 ? 0.20732 0.20098 0.21514 -0.00431 -0.02278 -0.00504 173 ASP A C   
1343 O O   . ASP A 173 ? 0.24806 0.24291 0.26129 -0.00453 -0.02403 -0.00660 173 ASP A O   
1344 C CB  . ASP A 173 ? 0.26819 0.25852 0.27071 -0.00263 -0.02699 -0.00439 173 ASP A CB  
1345 C CG  . ASP A 173 ? 0.29854 0.28833 0.30016 -0.00185 -0.02736 -0.00362 173 ASP A CG  
1346 O OD1 . ASP A 173 ? 0.44104 0.43282 0.44860 -0.00112 -0.02844 -0.00454 173 ASP A OD1 
1347 O OD2 . ASP A 173 ? 0.31031 0.29770 0.30573 -0.00200 -0.02641 -0.00222 173 ASP A OD2 
1348 N N   . PRO A 174 ? 0.22138 0.21359 0.22397 -0.00477 -0.02085 -0.00400 174 PRO A N   
1349 C CA  . PRO A 174 ? 0.24223 0.23376 0.24470 -0.00542 -0.02027 -0.00461 174 PRO A CA  
1350 C C   . PRO A 174 ? 0.13830 0.12724 0.13871 -0.00520 -0.02396 -0.00604 174 PRO A C   
1351 O O   . PRO A 174 ? 0.18366 0.17055 0.18070 -0.00445 -0.02680 -0.00609 174 PRO A O   
1352 C CB  . PRO A 174 ? 0.23085 0.22129 0.22788 -0.00562 -0.01767 -0.00320 174 PRO A CB  
1353 C CG  . PRO A 174 ? 0.23891 0.22832 0.23177 -0.00518 -0.01810 -0.00223 174 PRO A CG  
1354 C CD  . PRO A 174 ? 0.19312 0.18438 0.19035 -0.00473 -0.01904 -0.00241 174 PRO A CD  
1355 N N   . PRO A 175 ? 0.19563 0.18413 0.19758 -0.00579 -0.02419 -0.00726 175 PRO A N   
1356 C CA  . PRO A 175 ? 0.23191 0.21779 0.23182 -0.00554 -0.02811 -0.00898 175 PRO A CA  
1357 C C   . PRO A 175 ? 0.22222 0.20384 0.21239 -0.00512 -0.02892 -0.00830 175 PRO A C   
1358 O O   . PRO A 175 ? 0.19282 0.17384 0.17870 -0.00528 -0.02596 -0.00675 175 PRO A O   
1359 C CB  . PRO A 175 ? 0.28355 0.26983 0.28707 -0.00649 -0.02720 -0.01032 175 PRO A CB  
1360 C CG  . PRO A 175 ? 0.21286 0.20029 0.21635 -0.00700 -0.02256 -0.00867 175 PRO A CG  
1361 C CD  . PRO A 175 ? 0.23053 0.22034 0.23561 -0.00664 -0.02098 -0.00714 175 PRO A CD  
1362 N N   . ALA A 176 ? 0.13527 0.11376 0.12192 -0.00456 -0.03303 -0.00960 176 ALA A N   
1363 C CA  . ALA A 176 ? 0.16986 0.14340 0.14627 -0.00419 -0.03375 -0.00899 176 ALA A CA  
1364 C C   . ALA A 176 ? 0.24755 0.21927 0.21963 -0.00492 -0.03106 -0.00921 176 ALA A C   
1365 O O   . ALA A 176 ? 0.28091 0.24928 0.24506 -0.00491 -0.02969 -0.00833 176 ALA A O   
1366 C CB  . ALA A 176 ? 0.16204 0.13201 0.13491 -0.00323 -0.03916 -0.01035 176 ALA A CB  
1367 N N   . ALA A 177 ? 0.17881 0.15248 0.15611 -0.00556 -0.03008 -0.01043 177 ALA A N   
1368 C CA  . ALA A 177 ? 0.24225 0.21438 0.21659 -0.00610 -0.02748 -0.01082 177 ALA A CA  
1369 C C   . ALA A 177 ? 0.15407 0.12995 0.13531 -0.00668 -0.02399 -0.01021 177 ALA A C   
1370 O O   . ALA A 177 ? 0.23856 0.21721 0.22721 -0.00702 -0.02452 -0.01076 177 ALA A O   
1371 C CB  . ALA A 177 ? 0.19959 0.16866 0.17186 -0.00619 -0.03042 -0.01329 177 ALA A CB  
1372 N N   . MET A 178 ? 0.19185 0.16763 0.17064 -0.00676 -0.02041 -0.00913 178 MET A N   
1373 C CA  . MET A 178 ? 0.20508 0.18365 0.18889 -0.00700 -0.01720 -0.00819 178 MET A CA  
1374 C C   . MET A 178 ? 0.21669 0.19357 0.20008 -0.00722 -0.01574 -0.00921 178 MET A C   
1375 O O   . MET A 178 ? 0.24163 0.21541 0.21949 -0.00711 -0.01602 -0.01024 178 MET A O   
1376 C CB  . MET A 178 ? 0.21481 0.19496 0.19710 -0.00665 -0.01453 -0.00617 178 MET A CB  
1377 C CG  . MET A 178 ? 0.29810 0.27940 0.28008 -0.00643 -0.01568 -0.00517 178 MET A CG  
1378 S SD  . MET A 178 ? 0.42895 0.41422 0.41557 -0.00629 -0.01322 -0.00338 178 MET A SD  
1379 C CE  . MET A 178 ? 0.35218 0.33765 0.33820 -0.00613 -0.00998 -0.00282 178 MET A CE  
1380 N N   . PRO A 179 ? 0.17640 0.15479 0.16522 -0.00751 -0.01404 -0.00899 179 PRO A N   
1381 C CA  . PRO A 179 ? 0.15717 0.13376 0.14570 -0.00753 -0.01230 -0.00969 179 PRO A CA  
1382 C C   . PRO A 179 ? 0.26189 0.23825 0.24659 -0.00677 -0.00973 -0.00862 179 PRO A C   
1383 O O   . PRO A 179 ? 0.23613 0.21486 0.22217 -0.00634 -0.00803 -0.00681 179 PRO A O   
1384 C CB  . PRO A 179 ? 0.22659 0.20475 0.22167 -0.00796 -0.01080 -0.00904 179 PRO A CB  
1385 C CG  . PRO A 179 ? 0.21902 0.19932 0.21825 -0.00852 -0.01255 -0.00914 179 PRO A CG  
1386 C CD  . PRO A 179 ? 0.19064 0.17183 0.18607 -0.00792 -0.01375 -0.00835 179 PRO A CD  
1387 N N   . PRO A 180 ? 0.18206 0.15565 0.16211 -0.00659 -0.00939 -0.00990 180 PRO A N   
1388 C CA  . PRO A 180 ? 0.25917 0.23282 0.23620 -0.00594 -0.00680 -0.00923 180 PRO A CA  
1389 C C   . PRO A 180 ? 0.24011 0.21459 0.22078 -0.00529 -0.00440 -0.00874 180 PRO A C   
1390 O O   . PRO A 180 ? 0.23430 0.20804 0.21842 -0.00545 -0.00459 -0.00915 180 PRO A O   
1391 C CB  . PRO A 180 ? 0.21502 0.18488 0.18574 -0.00607 -0.00716 -0.01112 180 PRO A CB  
1392 C CG  . PRO A 180 ? 0.22923 0.19697 0.20119 -0.00651 -0.00929 -0.01299 180 PRO A CG  
1393 C CD  . PRO A 180 ? 0.26706 0.23725 0.24451 -0.00698 -0.01132 -0.01228 180 PRO A CD  
1394 N N   . PRO A 181 ? 0.21187 0.18775 0.19215 -0.00451 -0.00221 -0.00788 181 PRO A N   
1395 C CA  . PRO A 181 ? 0.19359 0.16971 0.17687 -0.00351 -0.00032 -0.00764 181 PRO A CA  
1396 C C   . PRO A 181 ? 0.20808 0.18088 0.18999 -0.00341 0.00024  -0.00972 181 PRO A C   
1397 O O   . PRO A 181 ? 0.23337 0.20384 0.21088 -0.00395 -0.00026 -0.01140 181 PRO A O   
1398 C CB  . PRO A 181 ? 0.24591 0.22437 0.22892 -0.00273 0.00144  -0.00687 181 PRO A CB  
1399 C CG  . PRO A 181 ? 0.23020 0.21013 0.21118 -0.00349 0.00050  -0.00607 181 PRO A CG  
1400 C CD  . PRO A 181 ? 0.14105 0.11836 0.11870 -0.00448 -0.00148 -0.00714 181 PRO A CD  
1401 N N   . ALA A 182 ? 0.24629 0.21839 0.23154 -0.00264 0.00123  -0.00961 182 ALA A N   
1402 C CA  . ALA A 182 ? 0.23073 0.19948 0.21517 -0.00243 0.00189  -0.01169 182 ALA A CA  
1403 C C   . ALA A 182 ? 0.22682 0.19528 0.20850 -0.00166 0.00393  -0.01291 182 ALA A C   
1404 O O   . ALA A 182 ? 0.22120 0.19241 0.20378 -0.00093 0.00526  -0.01188 182 ALA A O   
1405 C CB  . ALA A 182 ? 0.22426 0.19188 0.21298 -0.00167 0.00261  -0.01109 182 ALA A CB  
1406 N N   . GLU A 183 ? 0.22745 0.19250 0.20591 -0.00191 0.00428  -0.01532 183 GLU A N   
1407 C CA  . GLU A 183 ? 0.34280 0.30706 0.31816 -0.00138 0.00671  -0.01682 183 GLU A CA  
1408 C C   . GLU A 183 ? 0.29600 0.26062 0.27559 0.00026  0.00895  -0.01720 183 GLU A C   
1409 O O   . GLU A 183 ? 0.36580 0.32908 0.34878 0.00086  0.00847  -0.01713 183 GLU A O   
1410 C CB  . GLU A 183 ? 0.38424 0.34414 0.35343 -0.00222 0.00626  -0.01941 183 GLU A CB  
1411 C CG  . GLU A 183 ? 0.33961 0.29868 0.30395 -0.00353 0.00365  -0.01916 183 GLU A CG  
1412 C CD  . GLU A 183 ? 0.34951 0.30373 0.30654 -0.00413 0.00289  -0.02175 183 GLU A CD  
1413 O OE1 . GLU A 183 ? 0.35091 0.30231 0.30733 -0.00375 0.00400  -0.02394 183 GLU A OE1 
1414 O OE2 . GLU A 183 ? 0.35470 0.30757 0.30626 -0.00488 0.00105  -0.02163 183 GLU A OE2 
1415 N N   . ASP A 184 ? 0.33950 0.30594 0.31925 0.00101  0.01145  -0.01760 184 ASP A N   
1416 C CA  . ASP A 184 ? 0.40050 0.36752 0.38441 0.00280  0.01372  -0.01847 184 ASP A CA  
1417 C C   . ASP A 184 ? 0.25907 0.22846 0.24912 0.00429  0.01271  -0.01633 184 ASP A C   
1418 O O   . ASP A 184 ? 0.24647 0.21520 0.24020 0.00601  0.01357  -0.01686 184 ASP A O   
1419 C CB  . ASP A 184 ? 0.37673 0.33931 0.35898 0.00309  0.01464  -0.02113 184 ASP A CB  
1420 C CG  . ASP A 184 ? 0.45659 0.41624 0.43169 0.00184  0.01581  -0.02342 184 ASP A CG  
1421 O OD1 . ASP A 184 ? 0.40792 0.36921 0.38062 0.00137  0.01755  -0.02333 184 ASP A OD1 
1422 O OD2 . ASP A 184 ? 0.47186 0.42724 0.44344 0.00129  0.01497  -0.02531 184 ASP A OD2 
1423 N N   . MET A 185 ? 0.28624 0.25803 0.27708 0.00379  0.01087  -0.01392 185 MET A N   
1424 C CA  . MET A 185 ? 0.27923 0.25324 0.27470 0.00530  0.01008  -0.01181 185 MET A CA  
1425 C C   . MET A 185 ? 0.25654 0.23450 0.25497 0.00652  0.01134  -0.01190 185 MET A C   
1426 O O   . MET A 185 ? 0.22549 0.20585 0.22241 0.00545  0.01189  -0.01195 185 MET A O   
1427 C CB  . MET A 185 ? 0.26943 0.24446 0.26435 0.00430  0.00798  -0.00945 185 MET A CB  
1428 C CG  . MET A 185 ? 0.22448 0.19616 0.21826 0.00315  0.00676  -0.00936 185 MET A CG  
1429 S SD  . MET A 185 ? 0.31184 0.28013 0.30886 0.00464  0.00701  -0.00885 185 MET A SD  
1430 C CE  . MET A 185 ? 0.25670 0.22180 0.25291 0.00253  0.00582  -0.00895 185 MET A CE  
1431 N N   . PRO A 186 ? 0.24764 0.22629 0.25063 0.00876  0.01174  -0.01199 186 PRO A N   
1432 C CA  . PRO A 186 ? 0.21329 0.19601 0.22024 0.00995  0.01301  -0.01279 186 PRO A CA  
1433 C C   . PRO A 186 ? 0.15627 0.14313 0.16421 0.00955  0.01176  -0.01112 186 PRO A C   
1434 O O   . PRO A 186 ? 0.23287 0.22283 0.24199 0.00899  0.01325  -0.01214 186 PRO A O   
1435 C CB  . PRO A 186 ? 0.20446 0.18663 0.21634 0.01277  0.01265  -0.01288 186 PRO A CB  
1436 C CG  . PRO A 186 ? 0.23815 0.21649 0.24823 0.01292  0.01068  -0.01093 186 PRO A CG  
1437 C CD  . PRO A 186 ? 0.23248 0.20807 0.23751 0.01036  0.01097  -0.01145 186 PRO A CD  
1438 N N   . SER A 187 ? 0.17194 0.15872 0.17938 0.00973  0.00930  -0.00869 187 SER A N   
1439 C CA  . SER A 187 ? 0.23288 0.22331 0.24098 0.00941  0.00800  -0.00727 187 SER A CA  
1440 C C   . SER A 187 ? 0.19729 0.18823 0.20145 0.00689  0.00839  -0.00723 187 SER A C   
1441 O O   . SER A 187 ? 0.20547 0.19931 0.21007 0.00640  0.00760  -0.00635 187 SER A O   
1442 C CB  . SER A 187 ? 0.18862 0.17819 0.19653 0.01041  0.00554  -0.00477 187 SER A CB  
1443 O OG  . SER A 187 ? 0.18813 0.17673 0.19917 0.01299  0.00489  -0.00457 187 SER A OG  
1444 N N   . ALA A 188 ? 0.24965 0.23756 0.24984 0.00541  0.00933  -0.00821 188 ALA A N   
1445 C CA  . ALA A 188 ? 0.20068 0.18830 0.19656 0.00326  0.00948  -0.00826 188 ALA A CA  
1446 C C   . ALA A 188 ? 0.22076 0.20822 0.21493 0.00246  0.01216  -0.01027 188 ALA A C   
1447 O O   . ALA A 188 ? 0.18267 0.16836 0.17187 0.00079  0.01245  -0.01051 188 ALA A O   
1448 C CB  . ALA A 188 ? 0.19530 0.17935 0.18743 0.00216  0.00814  -0.00796 188 ALA A CB  
1449 N N   . ALA A 189 ? 0.18387 0.17290 0.18195 0.00369  0.01419  -0.01171 189 ALA A N   
1450 C CA  . ALA A 189 ? 0.20328 0.19195 0.19991 0.00287  0.01748  -0.01378 189 ALA A CA  
1451 C C   . ALA A 189 ? 0.19901 0.18944 0.19382 0.00115  0.01819  -0.01320 189 ALA A C   
1452 O O   . ALA A 189 ? 0.24970 0.24387 0.24841 0.00142  0.01707  -0.01209 189 ALA A O   
1453 C CB  . ALA A 189 ? 0.19058 0.18168 0.19352 0.00462  0.01958  -0.01549 189 ALA A CB  
1454 N N   . PRO A 190 ? 0.26742 0.25478 0.25594 -0.00059 0.01987  -0.01389 190 PRO A N   
1455 C CA  . PRO A 190 ? 0.21637 0.20446 0.20242 -0.00229 0.02043  -0.01303 190 PRO A CA  
1456 C C   . PRO A 190 ? 0.23554 0.22812 0.22760 -0.00231 0.02267  -0.01361 190 PRO A C   
1457 O O   . PRO A 190 ? 0.16197 0.15667 0.15496 -0.00317 0.02184  -0.01243 190 PRO A O   
1458 C CB  . PRO A 190 ? 0.22245 0.20546 0.20022 -0.00376 0.02239  -0.01403 190 PRO A CB  
1459 C CG  . PRO A 190 ? 0.14271 0.12227 0.11778 -0.00299 0.02086  -0.01475 190 PRO A CG  
1460 C CD  . PRO A 190 ? 0.20873 0.19109 0.19121 -0.00105 0.02081  -0.01530 190 PRO A CD  
1461 N N   . ALA A 191 ? 0.20589 0.20009 0.20264 -0.00136 0.02542  -0.01560 191 ALA A N   
1462 C CA  . ALA A 191 ? 0.16045 0.15933 0.16412 -0.00141 0.02767  -0.01663 191 ALA A CA  
1463 C C   . ALA A 191 ? 0.19761 0.20136 0.20845 0.00006  0.02441  -0.01560 191 ALA A C   
1464 O O   . ALA A 191 ? 0.19735 0.20513 0.21340 -0.00038 0.02514  -0.01605 191 ALA A O   
1465 C CB  . ALA A 191 ? 0.23850 0.23797 0.24606 -0.00057 0.03145  -0.01932 191 ALA A CB  
1466 N N   . ALA A 192 ? 0.13971 0.14291 0.15074 0.00173  0.02091  -0.01431 192 ALA A N   
1467 C CA  . ALA A 192 ? 0.18606 0.19293 0.20236 0.00329  0.01766  -0.01318 192 ALA A CA  
1468 C C   . ALA A 192 ? 0.15075 0.15681 0.16306 0.00250  0.01464  -0.01081 192 ALA A C   
1469 O O   . ALA A 192 ? 0.18072 0.18923 0.19606 0.00364  0.01193  -0.00976 192 ALA A O   
1470 C CB  . ALA A 192 ? 0.21272 0.21931 0.23229 0.00597  0.01603  -0.01327 192 ALA A CB  
1471 N N   . THR A 193 ? 0.16388 0.16640 0.16938 0.00071  0.01492  -0.01004 193 THR A N   
1472 C CA  . THR A 193 ? 0.19228 0.19395 0.19443 0.00007  0.01219  -0.00801 193 THR A CA  
1473 C C   . THR A 193 ? 0.20321 0.20424 0.20175 -0.00208 0.01300  -0.00764 193 THR A C   
1474 O O   . THR A 193 ? 0.14428 0.14409 0.13959 -0.00270 0.01096  -0.00617 193 THR A O   
1475 C CB  . THR A 193 ? 0.12551 0.12332 0.12342 0.00029  0.01073  -0.00720 193 THR A CB  
1476 O OG1 . THR A 193 ? 0.16255 0.15685 0.15600 -0.00071 0.01266  -0.00840 193 THR A OG1 
1477 C CG2 . THR A 193 ? 0.20967 0.20766 0.21098 0.00240  0.00960  -0.00703 193 THR A CG2 
1478 N N   . GLY A 194 ? 0.13954 0.14114 0.13868 -0.00323 0.01607  -0.00895 194 GLY A N   
1479 C CA  . GLY A 194 ? 0.12275 0.12287 0.11790 -0.00531 0.01708  -0.00844 194 GLY A CA  
1480 C C   . GLY A 194 ? 0.19081 0.19418 0.18928 -0.00564 0.01544  -0.00759 194 GLY A C   
1481 O O   . GLY A 194 ? 0.12328 0.13048 0.12745 -0.00430 0.01379  -0.00768 194 GLY A O   
1482 N N   . VAL A 195 ? 0.18820 0.18956 0.18256 -0.00737 0.01573  -0.00679 195 VAL A N   
1483 C CA  . VAL A 195 ? 0.18541 0.18928 0.18243 -0.00801 0.01458  -0.00622 195 VAL A CA  
1484 C C   . VAL A 195 ? 0.12964 0.13626 0.13164 -0.00910 0.01761  -0.00777 195 VAL A C   
1485 O O   . VAL A 195 ? 0.17913 0.18315 0.17814 -0.01077 0.02101  -0.00828 195 VAL A O   
1486 C CB  . VAL A 195 ? 0.17848 0.17876 0.16939 -0.00930 0.01353  -0.00475 195 VAL A CB  
1487 C CG1 . VAL A 195 ? 0.18472 0.18731 0.17852 -0.01007 0.01277  -0.00447 195 VAL A CG1 
1488 C CG2 . VAL A 195 ? 0.16509 0.16346 0.15268 -0.00824 0.01047  -0.00353 195 VAL A CG2 
1489 N N   . PRO A 196 ? 0.18167 0.19329 0.19116 -0.00826 0.01657  -0.00864 196 PRO A N   
1490 C CA  . PRO A 196 ? 0.18195 0.19677 0.19760 -0.00939 0.01942  -0.01048 196 PRO A CA  
1491 C C   . PRO A 196 ? 0.19054 0.20445 0.20492 -0.01171 0.02039  -0.01010 196 PRO A C   
1492 O O   . PRO A 196 ? 0.19998 0.21205 0.21039 -0.01196 0.01796  -0.00853 196 PRO A O   
1493 C CB  . PRO A 196 ? 0.17763 0.19794 0.20146 -0.00738 0.01676  -0.01147 196 PRO A CB  
1494 C CG  . PRO A 196 ? 0.10619 0.12565 0.12674 -0.00607 0.01253  -0.00962 196 PRO A CG  
1495 C CD  . PRO A 196 ? 0.19845 0.21288 0.21117 -0.00615 0.01274  -0.00812 196 PRO A CD  
1496 N N   . THR A 197 ? 0.18554 0.20060 0.20362 -0.01347 0.02426  -0.01165 197 THR A N   
1497 C CA  . THR A 197 ? 0.24463 0.25921 0.26312 -0.01584 0.02565  -0.01162 197 THR A CA  
1498 C C   . THR A 197 ? 0.24640 0.26698 0.27410 -0.01547 0.02345  -0.01301 197 THR A C   
1499 O O   . THR A 197 ? 0.19525 0.22026 0.22896 -0.01335 0.02118  -0.01408 197 THR A O   
1500 C CB  . THR A 197 ? 0.28634 0.29866 0.30406 -0.01823 0.03141  -0.01261 197 THR A CB  
1501 O OG1 . THR A 197 ? 0.29178 0.30869 0.31786 -0.01773 0.03382  -0.01507 197 THR A OG1 
1502 C CG2 . THR A 197 ? 0.28176 0.28722 0.28880 -0.01861 0.03317  -0.01118 197 THR A CG2 
1503 N N   . TRP A 198 ? 0.28878 0.30912 0.31733 -0.01748 0.02392  -0.01304 198 TRP A N   
1504 C CA  . TRP A 198 ? 0.29160 0.31735 0.32852 -0.01726 0.02148  -0.01458 198 TRP A CA  
1505 C C   . TRP A 198 ? 0.26949 0.30054 0.31679 -0.01765 0.02394  -0.01748 198 TRP A C   
1506 O O   . TRP A 198 ? 0.25475 0.29126 0.31002 -0.01631 0.02094  -0.01913 198 TRP A O   
1507 C CB  . TRP A 198 ? 0.29063 0.31442 0.32580 -0.01936 0.02127  -0.01401 198 TRP A CB  
1508 C CG  . TRP A 198 ? 0.32639 0.34735 0.36100 -0.02254 0.02642  -0.01438 198 TRP A CG  
1509 C CD1 . TRP A 198 ? 0.28351 0.29767 0.30898 -0.02406 0.02901  -0.01244 198 TRP A CD1 
1510 C CD2 . TRP A 198 ? 0.27538 0.29989 0.31886 -0.02462 0.02966  -0.01684 198 TRP A CD2 
1511 N NE1 . TRP A 198 ? 0.28599 0.29864 0.31321 -0.02700 0.03396  -0.01330 198 TRP A NE1 
1512 C CE2 . TRP A 198 ? 0.25459 0.27373 0.29326 -0.02754 0.03468  -0.01608 198 TRP A CE2 
1513 C CE3 . TRP A 198 ? 0.24270 0.27431 0.29790 -0.02427 0.02872  -0.01971 198 TRP A CE3 
1514 C CZ2 . TRP A 198 ? 0.21772 0.23833 0.26306 -0.03038 0.03934  -0.01803 198 TRP A CZ2 
1515 C CZ3 . TRP A 198 ? 0.30384 0.33755 0.36658 -0.02701 0.03298  -0.02192 198 TRP A CZ3 
1516 C CH2 . TRP A 198 ? 0.30175 0.32996 0.35962 -0.03016 0.03852  -0.02106 198 TRP A CH2 
1517 N N   . GLN A 199 ? 0.22174 0.25122 0.26914 -0.01939 0.02934  -0.01826 199 GLN A N   
1518 C CA  . GLN A 199 ? 0.27950 0.31430 0.33762 -0.01972 0.03215  -0.02128 199 GLN A CA  
1519 C C   . GLN A 199 ? 0.28932 0.32780 0.35176 -0.01645 0.02982  -0.02223 199 GLN A C   
1520 O O   . GLN A 199 ? 0.33840 0.38305 0.41157 -0.01542 0.02884  -0.02474 199 GLN A O   
1521 C CB  . GLN A 199 ? 0.27410 0.30567 0.33038 -0.02240 0.03912  -0.02184 199 GLN A CB  
1522 C CG  . GLN A 199 ? 0.31666 0.34397 0.36887 -0.02580 0.04216  -0.02093 199 GLN A CG  
1523 C CD  . GLN A 199 ? 0.38130 0.40024 0.41951 -0.02630 0.04282  -0.01784 199 GLN A CD  
1524 O OE1 . GLN A 199 ? 0.27101 0.28800 0.30301 -0.02401 0.03948  -0.01623 199 GLN A OE1 
1525 N NE2 . GLN A 199 ? 0.37881 0.39254 0.41207 -0.02928 0.04708  -0.01704 199 GLN A NE2 
1526 N N   . GLU A 200 ? 0.26831 0.30295 0.32277 -0.01473 0.02876  -0.02034 200 GLU A N   
1527 C CA  . GLU A 200 ? 0.25422 0.29125 0.31200 -0.01177 0.02718  -0.02111 200 GLU A CA  
1528 C C   . GLU A 200 ? 0.27719 0.31785 0.33870 -0.00900 0.02105  -0.02095 200 GLU A C   
1529 O O   . GLU A 200 ? 0.38700 0.43134 0.45497 -0.00656 0.01944  -0.02234 200 GLU A O   
1530 C CB  . GLU A 200 ? 0.21338 0.24477 0.26142 -0.01104 0.02802  -0.01926 200 GLU A CB  
1531 C CG  . GLU A 200 ? 0.25071 0.27808 0.29433 -0.01329 0.03398  -0.01964 200 GLU A CG  
1532 C CD  . GLU A 200 ? 0.29019 0.31141 0.32306 -0.01273 0.03400  -0.01778 200 GLU A CD  
1533 O OE1 . GLU A 200 ? 0.23526 0.25389 0.26196 -0.01205 0.03018  -0.01555 200 GLU A OE1 
1534 O OE2 . GLU A 200 ? 0.31161 0.33065 0.34248 -0.01297 0.03785  -0.01876 200 GLU A OE2 
1535 N N   . VAL A 201 ? 0.29461 0.33394 0.35184 -0.00920 0.01760  -0.01928 201 VAL A N   
1536 C CA  . VAL A 201 ? 0.21616 0.25788 0.27504 -0.00655 0.01193  -0.01891 201 VAL A CA  
1537 C C   . VAL A 201 ? 0.29453 0.34225 0.36352 -0.00627 0.00980  -0.02141 201 VAL A C   
1538 O O   . VAL A 201 ? 0.25564 0.30568 0.32688 -0.00367 0.00502  -0.02156 201 VAL A O   
1539 C CB  . VAL A 201 ? 0.31815 0.35603 0.36837 -0.00667 0.00912  -0.01633 201 VAL A CB  
1540 C CG1 . VAL A 201 ? 0.25268 0.28529 0.29395 -0.00626 0.01000  -0.01404 201 VAL A CG1 
1541 C CG2 . VAL A 201 ? 0.25569 0.29258 0.30486 -0.00956 0.01055  -0.01637 201 VAL A CG2 
1542 N N   . GLY A 202 ? 0.28054 0.33056 0.35554 -0.00889 0.01313  -0.02342 202 GLY A N   
1543 C CA  . GLY A 202 ? 0.31572 0.37207 0.40201 -0.00866 0.01125  -0.02637 202 GLY A CA  
1544 C C   . GLY A 202 ? 0.26215 0.31946 0.35140 -0.01180 0.01248  -0.02749 202 GLY A C   
1545 O O   . GLY A 202 ? 0.28284 0.34562 0.38283 -0.01234 0.01208  -0.03049 202 GLY A O   
1546 N N   . PHE A 203 ? 0.30532 0.35736 0.38566 -0.01386 0.01385  -0.02527 203 PHE A N   
1547 C CA  . PHE A 203 ? 0.27674 0.32881 0.35913 -0.01682 0.01489  -0.02611 203 PHE A CA  
1548 C C   . PHE A 203 ? 0.26060 0.31358 0.34895 -0.01996 0.02116  -0.02797 203 PHE A C   
1549 O O   . PHE A 203 ? 0.27715 0.32742 0.36232 -0.02061 0.02573  -0.02731 203 PHE A O   
1550 C CB  . PHE A 203 ? 0.21134 0.25708 0.28243 -0.01788 0.01460  -0.02314 203 PHE A CB  
1551 C CG  . PHE A 203 ? 0.20786 0.25264 0.27342 -0.01523 0.00906  -0.02150 203 PHE A CG  
1552 C CD1 . PHE A 203 ? 0.21418 0.26197 0.28333 -0.01445 0.00461  -0.02276 203 PHE A CD1 
1553 C CD2 . PHE A 203 ? 0.21722 0.25787 0.27389 -0.01364 0.00846  -0.01883 203 PHE A CD2 
1554 C CE1 . PHE A 203 ? 0.18186 0.22822 0.24514 -0.01211 0.00003  -0.02124 203 PHE A CE1 
1555 C CE2 . PHE A 203 ? 0.21388 0.25348 0.26566 -0.01143 0.00400  -0.01735 203 PHE A CE2 
1556 C CZ  . PHE A 203 ? 0.21445 0.25674 0.26919 -0.01066 -0.00004 -0.01848 203 PHE A CZ  
1557 N N   . LYS A 204 ? 0.28144 0.33800 0.37833 -0.02203 0.02151  -0.03042 204 LYS A N   
1558 C CA  . LYS A 204 ? 0.30467 0.36240 0.40847 -0.02537 0.02773  -0.03248 204 LYS A CA  
1559 C C   . LYS A 204 ? 0.33355 0.38610 0.43231 -0.02909 0.03113  -0.03130 204 LYS A C   
1560 O O   . LYS A 204 ? 0.35576 0.40579 0.45445 -0.03195 0.03755  -0.03148 204 LYS A O   
1561 C CB  . LYS A 204 ? 0.34038 0.40644 0.45975 -0.02535 0.02638  -0.03668 204 LYS A CB  
1562 C CG  . LYS A 204 ? 0.38521 0.45597 0.50847 -0.02171 0.01852  -0.03768 204 LYS A CG  
1563 C CD  . LYS A 204 ? 0.27458 0.34756 0.39912 -0.01795 0.01665  -0.03769 204 LYS A CD  
1564 C CE  . LYS A 204 ? 0.31128 0.38700 0.44386 -0.01891 0.02249  -0.03983 204 LYS A CE  
1565 N NZ  . LYS A 204 ? 0.31895 0.39959 0.45866 -0.01513 0.01949  -0.04148 204 LYS A NZ  
1566 N N   . GLU A 205 ? 0.34341 0.39395 0.43775 -0.02911 0.02718  -0.03014 205 GLU A N   
1567 C CA  . GLU A 205 ? 0.27388 0.31885 0.36302 -0.03242 0.03019  -0.02886 205 GLU A CA  
1568 C C   . GLU A 205 ? 0.22600 0.26343 0.30072 -0.03158 0.02944  -0.02491 205 GLU A C   
1569 O O   . GLU A 205 ? 0.26549 0.30292 0.33547 -0.02855 0.02475  -0.02353 205 GLU A O   
1570 C CB  . GLU A 205 ? 0.39795 0.44548 0.49283 -0.03348 0.02686  -0.03068 205 GLU A CB  
1571 C CG  . GLU A 205 ? 0.39125 0.44586 0.50118 -0.03510 0.02798  -0.03490 205 GLU A CG  
1572 C CD  . GLU A 205 ? 0.48829 0.54375 0.60295 -0.03728 0.02622  -0.03668 205 GLU A CD  
1573 O OE1 . GLU A 205 ? 0.46195 0.51108 0.56903 -0.03931 0.02783  -0.03467 205 GLU A OE1 
1574 O OE2 . GLU A 205 ? 0.56091 0.62326 0.68700 -0.03686 0.02298  -0.04020 205 GLU A OE2 
1575 N N   . PRO A 206 ? 0.24999 0.28075 0.31759 -0.03415 0.03399  -0.02307 206 PRO A N   
1576 C CA  . PRO A 206 ? 0.27260 0.29620 0.32690 -0.03320 0.03321  -0.01949 206 PRO A CA  
1577 C C   . PRO A 206 ? 0.26011 0.28194 0.31051 -0.03247 0.02850  -0.01833 206 PRO A C   
1578 O O   . PRO A 206 ? 0.27606 0.30034 0.33249 -0.03365 0.02712  -0.02006 206 PRO A O   
1579 C CB  . PRO A 206 ? 0.26651 0.28350 0.31531 -0.03635 0.03954  -0.01827 206 PRO A CB  
1580 C CG  . PRO A 206 ? 0.32019 0.33994 0.37873 -0.03947 0.04263  -0.02082 206 PRO A CG  
1581 C CD  . PRO A 206 ? 0.31659 0.34575 0.38797 -0.03805 0.04019  -0.02420 206 PRO A CD  
1582 N N   . PRO A 207 ? 0.28156 0.29921 0.32229 -0.03055 0.02599  -0.01565 207 PRO A N   
1583 C CA  . PRO A 207 ? 0.28399 0.29948 0.32067 -0.02988 0.02207  -0.01454 207 PRO A CA  
1584 C C   . PRO A 207 ? 0.24234 0.25161 0.27465 -0.03256 0.02463  -0.01340 207 PRO A C   
1585 O O   . PRO A 207 ? 0.22646 0.23074 0.25415 -0.03432 0.02899  -0.01215 207 PRO A O   
1586 C CB  . PRO A 207 ? 0.21576 0.22884 0.24426 -0.02713 0.01943  -0.01218 207 PRO A CB  
1587 C CG  . PRO A 207 ? 0.21394 0.22446 0.23876 -0.02747 0.02320  -0.01129 207 PRO A CG  
1588 C CD  . PRO A 207 ? 0.23314 0.24828 0.26697 -0.02880 0.02649  -0.01383 207 PRO A CD  
1589 N N   . LEU A 208 ? 0.20248 0.21159 0.23578 -0.03279 0.02184  -0.01382 208 LEU A N   
1590 C CA  . LEU A 208 ? 0.18223 0.18540 0.21205 -0.03517 0.02377  -0.01289 208 LEU A CA  
1591 C C   . LEU A 208 ? 0.15299 0.15120 0.17442 -0.03363 0.02068  -0.01060 208 LEU A C   
1592 O O   . LEU A 208 ? 0.13468 0.12703 0.15212 -0.03522 0.02198  -0.00947 208 LEU A O   
1593 C CB  . LEU A 208 ? 0.18358 0.19003 0.22240 -0.03727 0.02374  -0.01569 208 LEU A CB  
1594 C CG  . LEU A 208 ? 0.24450 0.25620 0.29359 -0.03924 0.02697  -0.01848 208 LEU A CG  
1595 C CD1 . LEU A 208 ? 0.25645 0.27085 0.31428 -0.04145 0.02649  -0.02134 208 LEU A CD1 
1596 C CD2 . LEU A 208 ? 0.24261 0.24980 0.28856 -0.04154 0.03328  -0.01725 208 LEU A CD2 
1597 N N   . THR A 209 ? 0.15878 0.15896 0.17766 -0.03062 0.01681  -0.00993 209 THR A N   
1598 C CA  . THR A 209 ? 0.12544 0.12178 0.13792 -0.02913 0.01389  -0.00822 209 THR A CA  
1599 C C   . THR A 209 ? 0.14574 0.13467 0.14945 -0.02949 0.01579  -0.00548 209 THR A C   
1600 O O   . THR A 209 ? 0.22290 0.21008 0.22393 -0.03006 0.01867  -0.00464 209 THR A O   
1601 C CB  . THR A 209 ? 0.15361 0.15360 0.16547 -0.02601 0.00997  -0.00812 209 THR A CB  
1602 O OG1 . THR A 209 ? 0.12008 0.11702 0.12738 -0.02479 0.00736  -0.00702 209 THR A OG1 
1603 C CG2 . THR A 209 ? 0.12115 0.12093 0.12950 -0.02470 0.01077  -0.00674 209 THR A CG2 
1604 N N   . VAL A 210 ? 0.13964 0.12394 0.13869 -0.02905 0.01404  -0.00421 210 VAL A N   
1605 C CA  . VAL A 210 ? 0.13860 0.11530 0.12907 -0.02910 0.01498  -0.00162 210 VAL A CA  
1606 C C   . VAL A 210 ? 0.19311 0.16908 0.17865 -0.02624 0.01169  -0.00017 210 VAL A C   
1607 O O   . VAL A 210 ? 0.17959 0.14946 0.15806 -0.02578 0.01147  0.00185  210 VAL A O   
1608 C CB  . VAL A 210 ? 0.20527 0.17629 0.19384 -0.03057 0.01543  -0.00107 210 VAL A CB  
1609 C CG1 . VAL A 210 ? 0.14708 0.11806 0.14046 -0.03382 0.01926  -0.00244 210 VAL A CG1 
1610 C CG2 . VAL A 210 ? 0.15363 0.12655 0.14444 -0.02901 0.01155  -0.00196 210 VAL A CG2 
1611 N N   . PHE A 211 ? 0.13764 0.11936 0.12668 -0.02430 0.00906  -0.00118 211 PHE A N   
1612 C CA  . PHE A 211 ? 0.13529 0.11688 0.12088 -0.02178 0.00617  -0.00009 211 PHE A CA  
1613 C C   . PHE A 211 ? 0.14487 0.12902 0.13009 -0.02088 0.00668  0.00007  211 PHE A C   
1614 O O   . PHE A 211 ? 0.19053 0.17989 0.18084 -0.02086 0.00714  -0.00135 211 PHE A O   
1615 C CB  . PHE A 211 ? 0.13698 0.12227 0.12592 -0.02026 0.00313  -0.00120 211 PHE A CB  
1616 C CG  . PHE A 211 ? 0.14699 0.13010 0.13684 -0.02108 0.00262  -0.00179 211 PHE A CG  
1617 C CD1 . PHE A 211 ? 0.14811 0.12535 0.13340 -0.02089 0.00209  -0.00037 211 PHE A CD1 
1618 C CD2 . PHE A 211 ? 0.18049 0.16723 0.17584 -0.02194 0.00241  -0.00391 211 PHE A CD2 
1619 C CE1 . PHE A 211 ? 0.17299 0.14785 0.15922 -0.02157 0.00166  -0.00099 211 PHE A CE1 
1620 C CE2 . PHE A 211 ? 0.12958 0.11408 0.12581 -0.02276 0.00194  -0.00469 211 PHE A CE2 
1621 C CZ  . PHE A 211 ? 0.17831 0.15679 0.16999 -0.02259 0.00171  -0.00319 211 PHE A CZ  
1622 N N   . LYS A 212 ? 0.14582 0.12614 0.12513 -0.02004 0.00634  0.00168  212 LYS A N   
1623 C CA  . LYS A 212 ? 0.23684 0.21838 0.21486 -0.01934 0.00703  0.00186  212 LYS A CA  
1624 C C   . LYS A 212 ? 0.12189 0.10672 0.10106 -0.01705 0.00406  0.00180  212 LYS A C   
1625 O O   . LYS A 212 ? 0.17523 0.15877 0.15290 -0.01588 0.00161  0.00240  212 LYS A O   
1626 C CB  . LYS A 212 ? 0.22664 0.20172 0.19702 -0.01977 0.00823  0.00344  212 LYS A CB  
1627 C CG  . LYS A 212 ? 0.28030 0.25094 0.24826 -0.02219 0.01177  0.00381  212 LYS A CG  
1628 C CD  . LYS A 212 ? 0.28642 0.26070 0.25908 -0.02375 0.01544  0.00233  212 LYS A CD  
1629 C CE  . LYS A 212 ? 0.22752 0.20214 0.19774 -0.02304 0.01654  0.00232  212 LYS A CE  
1630 N NZ  . LYS A 212 ? 0.23742 0.20832 0.20440 -0.02510 0.02126  0.00240  212 LYS A NZ  
1631 N N   . GLY A 213 ? 0.11859 0.10749 0.10064 -0.01643 0.00448  0.00104  213 GLY A N   
1632 C CA  . GLY A 213 ? 0.13521 0.12682 0.11826 -0.01446 0.00217  0.00107  213 GLY A CA  
1633 C C   . GLY A 213 ? 0.15802 0.14642 0.13626 -0.01358 0.00127  0.00218  213 GLY A C   
1634 O O   . GLY A 213 ? 0.19406 0.17826 0.16768 -0.01433 0.00246  0.00284  213 GLY A O   
1635 N N   . GLY A 214 ? 0.11301 0.10320 0.09224 -0.01200 -0.00086 0.00228  214 GLY A N   
1636 C CA  . GLY A 214 ? 0.12311 0.11114 0.09917 -0.01112 -0.00203 0.00292  214 GLY A CA  
1637 C C   . GLY A 214 ? 0.14130 0.12811 0.11678 -0.01011 -0.00456 0.00337  214 GLY A C   
1638 O O   . GLY A 214 ? 0.14073 0.12652 0.11641 -0.01026 -0.00524 0.00349  214 GLY A O   
1639 N N   . GLU A 215 ? 0.15164 0.13862 0.12693 -0.00909 -0.00590 0.00344  215 GLU A N   
1640 C CA  . GLU A 215 ? 0.12947 0.11560 0.10514 -0.00812 -0.00825 0.00359  215 GLU A CA  
1641 C C   . GLU A 215 ? 0.13787 0.11914 0.10930 -0.00823 -0.00957 0.00422  215 GLU A C   
1642 O O   . GLU A 215 ? 0.11830 0.09872 0.09064 -0.00755 -0.01133 0.00428  215 GLU A O   
1643 C CB  . GLU A 215 ? 0.13782 0.12513 0.11470 -0.00729 -0.00917 0.00332  215 GLU A CB  
1644 C CG  . GLU A 215 ? 0.12811 0.11450 0.10593 -0.00638 -0.01164 0.00319  215 GLU A CG  
1645 C CD  . GLU A 215 ? 0.13555 0.12251 0.11439 -0.00593 -0.01245 0.00273  215 GLU A CD  
1646 O OE1 . GLU A 215 ? 0.11203 0.09866 0.08911 -0.00631 -0.01134 0.00267  215 GLU A OE1 
1647 O OE2 . GLU A 215 ? 0.12582 0.11358 0.10767 -0.00524 -0.01406 0.00227  215 GLU A OE2 
1648 N N   . THR A 216 ? 0.12264 0.10034 0.08915 -0.00897 -0.00868 0.00468  216 THR A N   
1649 C CA  . THR A 216 ? 0.17864 0.15061 0.13962 -0.00901 -0.00993 0.00553  216 THR A CA  
1650 C C   . THR A 216 ? 0.14750 0.11789 0.10849 -0.00962 -0.00941 0.00601  216 THR A C   
1651 O O   . THR A 216 ? 0.17955 0.14694 0.13919 -0.00886 -0.01159 0.00649  216 THR A O   
1652 C CB  . THR A 216 ? 0.15723 0.12535 0.11212 -0.00987 -0.00835 0.00591  216 THR A CB  
1653 O OG1 . THR A 216 ? 0.17484 0.14397 0.12957 -0.00920 -0.00920 0.00528  216 THR A OG1 
1654 C CG2 . THR A 216 ? 0.18180 0.14298 0.12954 -0.00991 -0.00951 0.00705  216 THR A CG2 
1655 N N   . GLU A 217 ? 0.18218 0.15452 0.14510 -0.01094 -0.00666 0.00572  217 GLU A N   
1656 C CA  . GLU A 217 ? 0.17950 0.15064 0.14318 -0.01174 -0.00600 0.00587  217 GLU A CA  
1657 C C   . GLU A 217 ? 0.17343 0.14740 0.14172 -0.01063 -0.00788 0.00525  217 GLU A C   
1658 O O   . GLU A 217 ? 0.17222 0.14367 0.14013 -0.01062 -0.00860 0.00548  217 GLU A O   
1659 C CB  . GLU A 217 ? 0.15902 0.13247 0.12500 -0.01344 -0.00281 0.00525  217 GLU A CB  
1660 C CG  . GLU A 217 ? 0.28349 0.25354 0.24502 -0.01487 -0.00012 0.00576  217 GLU A CG  
1661 C CD  . GLU A 217 ? 0.27530 0.23840 0.23094 -0.01577 0.00040  0.00704  217 GLU A CD  
1662 O OE1 . GLU A 217 ? 0.27037 0.23209 0.22693 -0.01566 -0.00079 0.00729  217 GLU A OE1 
1663 O OE2 . GLU A 217 ? 0.32111 0.27968 0.27079 -0.01654 0.00209  0.00782  217 GLU A OE2 
1664 N N   . ALA A 218 ? 0.14413 0.12291 0.11653 -0.00972 -0.00844 0.00445  218 ALA A N   
1665 C CA  . ALA A 218 ? 0.11707 0.09833 0.09338 -0.00867 -0.00976 0.00377  218 ALA A CA  
1666 C C   . ALA A 218 ? 0.14172 0.12012 0.11713 -0.00741 -0.01229 0.00410  218 ALA A C   
1667 O O   . ALA A 218 ? 0.13587 0.11335 0.11262 -0.00693 -0.01315 0.00384  218 ALA A O   
1668 C CB  . ALA A 218 ? 0.13035 0.11643 0.11018 -0.00801 -0.00950 0.00309  218 ALA A CB  
1669 N N   . LEU A 219 ? 0.12122 0.09813 0.09457 -0.00677 -0.01368 0.00450  219 LEU A N   
1670 C CA  . LEU A 219 ? 0.14677 0.12123 0.11986 -0.00537 -0.01665 0.00459  219 LEU A CA  
1671 C C   . LEU A 219 ? 0.14302 0.11160 0.11151 -0.00542 -0.01762 0.00558  219 LEU A C   
1672 O O   . LEU A 219 ? 0.13933 0.10621 0.10897 -0.00419 -0.01984 0.00549  219 LEU A O   
1673 C CB  . LEU A 219 ? 0.12513 0.09932 0.09706 -0.00476 -0.01820 0.00453  219 LEU A CB  
1674 C CG  . LEU A 219 ? 0.15708 0.13646 0.13368 -0.00467 -0.01729 0.00363  219 LEU A CG  
1675 C CD1 . LEU A 219 ? 0.12046 0.09910 0.09571 -0.00434 -0.01868 0.00343  219 LEU A CD1 
1676 C CD2 . LEU A 219 ? 0.19264 0.17536 0.17520 -0.00376 -0.01777 0.00271  219 LEU A CD2 
1677 N N   . ALA A 220 ? 0.13956 0.10472 0.10287 -0.00683 -0.01581 0.00653  220 ALA A N   
1678 C CA  . ALA A 220 ? 0.17227 0.13102 0.13048 -0.00713 -0.01618 0.00773  220 ALA A CA  
1679 C C   . ALA A 220 ? 0.17314 0.13227 0.13452 -0.00746 -0.01545 0.00738  220 ALA A C   
1680 O O   . ALA A 220 ? 0.14636 0.10102 0.10594 -0.00675 -0.01708 0.00798  220 ALA A O   
1681 C CB  . ALA A 220 ? 0.20516 0.16025 0.15730 -0.00886 -0.01356 0.00872  220 ALA A CB  
1682 N N   . ARG A 221 ? 0.16744 0.13153 0.13331 -0.00846 -0.01320 0.00633  221 ARG A N   
1683 C CA  . ARG A 221 ? 0.19618 0.16085 0.16518 -0.00875 -0.01272 0.00561  221 ARG A CA  
1684 C C   . ARG A 221 ? 0.17012 0.13662 0.14317 -0.00682 -0.01500 0.00471  221 ARG A C   
1685 O O   . ARG A 221 ? 0.16776 0.13226 0.14183 -0.00645 -0.01558 0.00440  221 ARG A O   
1686 C CB  . ARG A 221 ? 0.15394 0.12342 0.12645 -0.01015 -0.01020 0.00451  221 ARG A CB  
1687 C CG  . ARG A 221 ? 0.21507 0.18430 0.18985 -0.01091 -0.00950 0.00364  221 ARG A CG  
1688 C CD  . ARG A 221 ? 0.20768 0.17981 0.18447 -0.01280 -0.00706 0.00279  221 ARG A CD  
1689 N NE  . ARG A 221 ? 0.24612 0.21638 0.22407 -0.01400 -0.00631 0.00210  221 ARG A NE  
1690 C CZ  . ARG A 221 ? 0.20820 0.17376 0.18357 -0.01571 -0.00474 0.00289  221 ARG A CZ  
1691 N NH1 . ARG A 221 ? 0.23669 0.19875 0.20753 -0.01641 -0.00358 0.00443  221 ARG A NH1 
1692 N NH2 . ARG A 221 ? 0.26029 0.22426 0.23737 -0.01681 -0.00415 0.00205  221 ARG A NH2 
1693 N N   . LEU A 222 ? 0.14928 0.11940 0.12492 -0.00566 -0.01607 0.00417  222 LEU A N   
1694 C CA  . LEU A 222 ? 0.17286 0.14499 0.15301 -0.00394 -0.01777 0.00313  222 LEU A CA  
1695 C C   . LEU A 222 ? 0.15261 0.11995 0.13129 -0.00248 -0.02067 0.00367  222 LEU A C   
1696 O O   . LEU A 222 ? 0.13143 0.09792 0.11261 -0.00156 -0.02145 0.00301  222 LEU A O   
1697 C CB  . LEU A 222 ? 0.12218 0.09877 0.10539 -0.00331 -0.01796 0.00252  222 LEU A CB  
1698 C CG  . LEU A 222 ? 0.14691 0.12618 0.13561 -0.00175 -0.01908 0.00126  222 LEU A CG  
1699 C CD1 . LEU A 222 ? 0.11602 0.09786 0.10779 -0.00186 -0.01726 0.00009  222 LEU A CD1 
1700 C CD2 . LEU A 222 ? 0.17793 0.16060 0.16909 -0.00146 -0.01917 0.00088  222 LEU A CD2 
1701 N N   . GLU A 223 ? 0.13473 0.09854 0.10906 -0.00212 -0.02246 0.00481  223 GLU A N   
1702 C CA  . GLU A 223 ? 0.14081 0.09946 0.11296 -0.00047 -0.02582 0.00544  223 GLU A CA  
1703 C C   . GLU A 223 ? 0.20816 0.16129 0.17688 -0.00089 -0.02543 0.00638  223 GLU A C   
1704 O O   . GLU A 223 ? 0.19580 0.14565 0.16510 0.00076  -0.02793 0.00642  223 GLU A O   
1705 C CB  . GLU A 223 ? 0.21956 0.17473 0.18612 -0.00015 -0.02781 0.00651  223 GLU A CB  
1706 C CG  . GLU A 223 ? 0.18793 0.14780 0.15791 0.00035  -0.02869 0.00547  223 GLU A CG  
1707 C CD  . GLU A 223 ? 0.21920 0.18156 0.19569 0.00243  -0.03174 0.00407  223 GLU A CD  
1708 O OE1 . GLU A 223 ? 0.33225 0.29166 0.30941 0.00389  -0.03401 0.00410  223 GLU A OE1 
1709 O OE2 . GLU A 223 ? 0.25125 0.21846 0.23258 0.00259  -0.03175 0.00286  223 GLU A OE2 
1710 N N   . ALA A 224 ? 0.19461 0.14653 0.16016 -0.00309 -0.02230 0.00706  224 ALA A N   
1711 C CA  . ALA A 224 ? 0.22127 0.16788 0.18400 -0.00388 -0.02144 0.00786  224 ALA A CA  
1712 C C   . ALA A 224 ? 0.20672 0.15561 0.17530 -0.00323 -0.02146 0.00633  224 ALA A C   
1713 O O   . ALA A 224 ? 0.20030 0.14434 0.16789 -0.00251 -0.02262 0.00670  224 ALA A O   
1714 C CB  . ALA A 224 ? 0.18847 0.13432 0.14808 -0.00663 -0.01772 0.00848  224 ALA A CB  
1715 N N   . ALA A 225 ? 0.18616 0.14193 0.16041 -0.00338 -0.02017 0.00460  225 ALA A N   
1716 C CA  . ALA A 225 ? 0.20555 0.16352 0.18483 -0.00275 -0.01993 0.00290  225 ALA A CA  
1717 C C   . ALA A 225 ? 0.24109 0.19856 0.22363 -0.00015 -0.02279 0.00225  225 ALA A C   
1718 O O   . ALA A 225 ? 0.20406 0.16001 0.18897 0.00071  -0.02322 0.00134  225 ALA A O   
1719 C CB  . ALA A 225 ? 0.16314 0.12796 0.14640 -0.00347 -0.01783 0.00135  225 ALA A CB  
1720 N N   . PHE A 226 ? 0.16650 0.12528 0.14969 0.00112  -0.02482 0.00249  226 PHE A N   
1721 C CA  . PHE A 226 ? 0.18922 0.14830 0.17676 0.00364  -0.02774 0.00158  226 PHE A CA  
1722 C C   . PHE A 226 ? 0.19065 0.14277 0.17415 0.00514  -0.03127 0.00300  226 PHE A C   
1723 O O   . PHE A 226 ? 0.20858 0.16066 0.19571 0.00748  -0.03443 0.00228  226 PHE A O   
1724 C CB  . PHE A 226 ? 0.21437 0.17882 0.20582 0.00422  -0.02827 0.00073  226 PHE A CB  
1725 C CG  . PHE A 226 ? 0.16827 0.13912 0.16507 0.00368  -0.02543 -0.00099 226 PHE A CG  
1726 C CD1 . PHE A 226 ? 0.21134 0.18460 0.20619 0.00171  -0.02240 -0.00079 226 PHE A CD1 
1727 C CD2 . PHE A 226 ? 0.18604 0.16022 0.18970 0.00522  -0.02575 -0.00284 226 PHE A CD2 
1728 C CE1 . PHE A 226 ? 0.16520 0.14349 0.16381 0.00140  -0.02004 -0.00219 226 PHE A CE1 
1729 C CE2 . PHE A 226 ? 0.12198 0.10121 0.12945 0.00468  -0.02279 -0.00428 226 PHE A CE2 
1730 C CZ  . PHE A 226 ? 0.15664 0.13763 0.16105 0.00282  -0.02008 -0.00385 226 PHE A CZ  
1731 N N   . GLN A 227 ? 0.27371 0.21973 0.24983 0.00389  -0.03078 0.00496  227 GLN A N   
1732 C CA  . GLN A 227 ? 0.29892 0.23705 0.26988 0.00536  -0.03402 0.00659  227 GLN A CA  
1733 C C   . GLN A 227 ? 0.20535 0.14112 0.18001 0.00723  -0.03564 0.00578  227 GLN A C   
1734 O O   . GLN A 227 ? 0.28303 0.21434 0.25675 0.00965  -0.03959 0.00633  227 GLN A O   
1735 C CB  . GLN A 227 ? 0.29643 0.22811 0.25851 0.00327  -0.03217 0.00887  227 GLN A CB  
1736 C CG  . GLN A 227 ? 0.25815 0.18972 0.21486 0.00216  -0.03167 0.00998  227 GLN A CG  
1737 C CD  . GLN A 227 ? 0.40719 0.33522 0.36043 0.00443  -0.03621 0.01074  227 GLN A CD  
1738 O OE1 . GLN A 227 ? 0.49028 0.41437 0.44370 0.00680  -0.03989 0.01094  227 GLN A OE1 
1739 N NE2 . GLN A 227 ? 0.47812 0.40744 0.42827 0.00384  -0.03621 0.01102  227 GLN A NE2 
1740 N N   . ASP A 228 ? 0.23259 0.24406 0.22066 0.00759  -0.01945 0.02369  228 ASP A N   
1741 C CA  . ASP A 228 ? 0.24719 0.25681 0.24231 0.00951  -0.02003 0.02586  228 ASP A CA  
1742 C C   . ASP A 228 ? 0.20305 0.21220 0.20409 0.01074  -0.01809 0.02254  228 ASP A C   
1743 O O   . ASP A 228 ? 0.19077 0.19710 0.19184 0.01101  -0.01493 0.02027  228 ASP A O   
1744 C CB  . ASP A 228 ? 0.22345 0.22913 0.21786 0.00976  -0.01853 0.02780  228 ASP A CB  
1745 C CG  . ASP A 228 ? 0.18055 0.18393 0.18254 0.01177  -0.01928 0.02993  228 ASP A CG  
1746 O OD1 . ASP A 228 ? 0.24702 0.25235 0.25471 0.01304  -0.02137 0.03058  228 ASP A OD1 
1747 O OD2 . ASP A 228 ? 0.22105 0.22069 0.22382 0.01208  -0.01778 0.03074  228 ASP A OD2 
1748 N N   . PRO A 229 ? 0.21608 0.22823 0.22221 0.01136  -0.01987 0.02218  229 PRO A N   
1749 C CA  . PRO A 229 ? 0.14421 0.15639 0.15582 0.01222  -0.01762 0.01902  229 PRO A CA  
1750 C C   . PRO A 229 ? 0.15048 0.15959 0.16741 0.01405  -0.01550 0.01890  229 PRO A C   
1751 O O   . PRO A 229 ? 0.17112 0.17930 0.18993 0.01433  -0.01249 0.01591  229 PRO A O   
1752 C CB  . PRO A 229 ? 0.13534 0.15199 0.15199 0.01240  -0.02050 0.01937  229 PRO A CB  
1753 C CG  . PRO A 229 ? 0.15864 0.17683 0.17412 0.01243  -0.02458 0.02348  229 PRO A CG  
1754 C CD  . PRO A 229 ? 0.19298 0.20908 0.19964 0.01100  -0.02401 0.02448  229 PRO A CD  
1755 N N   . LYS A 230 ? 0.18452 0.19192 0.20383 0.01520  -0.01695 0.02201  230 LYS A N   
1756 C CA  . LYS A 230 ? 0.21064 0.21464 0.23495 0.01687  -0.01483 0.02137  230 LYS A CA  
1757 C C   . LYS A 230 ? 0.16600 0.16647 0.18527 0.01602  -0.01151 0.01918  230 LYS A C   
1758 O O   . LYS A 230 ? 0.19037 0.18904 0.21230 0.01679  -0.00872 0.01649  230 LYS A O   
1759 C CB  . LYS A 230 ? 0.18417 0.18650 0.21219 0.01814  -0.01734 0.02541  230 LYS A CB  
1760 C CG  . LYS A 230 ? 0.23046 0.23623 0.26472 0.01936  -0.02100 0.02789  230 LYS A CG  
1761 C CD  . LYS A 230 ? 0.23480 0.23804 0.27458 0.02111  -0.02311 0.03170  230 LYS A CD  
1762 C CE  . LYS A 230 ? 0.28124 0.28811 0.32828 0.02262  -0.02708 0.03431  230 LYS A CE  
1763 N NZ  . LYS A 230 ? 0.18469 0.19516 0.23823 0.02360  -0.02577 0.03061  230 LYS A NZ  
1764 N N   . TRP A 231 ? 0.12382 0.12356 0.13585 0.01439  -0.01177 0.02021  231 TRP A N   
1765 C CA  . TRP A 231 ? 0.20470 0.20160 0.21234 0.01356  -0.00897 0.01824  231 TRP A CA  
1766 C C   . TRP A 231 ? 0.18237 0.18002 0.18862 0.01309  -0.00663 0.01448  231 TRP A C   
1767 O O   . TRP A 231 ? 0.20768 0.20298 0.21326 0.01314  -0.00413 0.01233  231 TRP A O   
1768 C CB  . TRP A 231 ? 0.19734 0.19418 0.19821 0.01189  -0.00967 0.02002  231 TRP A CB  
1769 C CG  . TRP A 231 ? 0.17710 0.17170 0.17398 0.01101  -0.00708 0.01801  231 TRP A CG  
1770 C CD1 . TRP A 231 ? 0.24517 0.23658 0.24225 0.01097  -0.00602 0.01856  231 TRP A CD1 
1771 C CD2 . TRP A 231 ? 0.14614 0.14157 0.13888 0.01004  -0.00551 0.01521  231 TRP A CD2 
1772 N NE1 . TRP A 231 ? 0.20522 0.19588 0.19852 0.01004  -0.00401 0.01628  231 TRP A NE1 
1773 C CE2 . TRP A 231 ? 0.21032 0.20331 0.20100 0.00958  -0.00369 0.01432  231 TRP A CE2 
1774 C CE3 . TRP A 231 ? 0.15657 0.15445 0.14765 0.00950  -0.00561 0.01339  231 TRP A CE3 
1775 C CZ2 . TRP A 231 ? 0.13625 0.12932 0.12343 0.00883  -0.00215 0.01191  231 TRP A CZ2 
1776 C CZ3 . TRP A 231 ? 0.14914 0.14659 0.13677 0.00873  -0.00392 0.01097  231 TRP A CZ3 
1777 C CH2 . TRP A 231 ? 0.17668 0.17182 0.16245 0.00850  -0.00229 0.01037  231 TRP A CH2 
1778 N N   . VAL A 232 ? 0.14153 0.14235 0.14719 0.01246  -0.00754 0.01376  232 VAL A N   
1779 C CA  . VAL A 232 ? 0.14924 0.15054 0.15403 0.01187  -0.00546 0.01066  232 VAL A CA  
1780 C C   . VAL A 232 ? 0.10829 0.10932 0.11873 0.01304  -0.00356 0.00904  232 VAL A C   
1781 O O   . VAL A 232 ? 0.11184 0.11118 0.12100 0.01284  -0.00092 0.00689  232 VAL A O   
1782 C CB  . VAL A 232 ? 0.14472 0.14931 0.14830 0.01077  -0.00704 0.01023  232 VAL A CB  
1783 C CG1 . VAL A 232 ? 0.14604 0.15072 0.14959 0.01007  -0.00492 0.00742  232 VAL A CG1 
1784 C CG2 . VAL A 232 ? 0.15475 0.15968 0.15211 0.00951  -0.00836 0.01113  232 VAL A CG2 
1785 N N   . ALA A 233 ? 0.18206 0.18498 0.19889 0.01429  -0.00487 0.01006  233 ALA A N   
1786 C CA  . ALA A 233 ? 0.17223 0.17587 0.19515 0.01537  -0.00281 0.00813  233 ALA A CA  
1787 C C   . ALA A 233 ? 0.19299 0.19317 0.21674 0.01635  -0.00046 0.00692  233 ALA A C   
1788 O O   . ALA A 233 ? 0.15164 0.15162 0.17671 0.01649  0.00246  0.00429  233 ALA A O   
1789 C CB  . ALA A 233 ? 0.19219 0.19905 0.22273 0.01668  -0.00501 0.00951  233 ALA A CB  
1790 N N   . GLY A 234 ? 0.12777 0.12526 0.15079 0.01687  -0.00165 0.00878  234 GLY A N   
1791 C CA  . GLY A 234 ? 0.14288 0.13683 0.16703 0.01767  0.00025  0.00749  234 GLY A CA  
1792 C C   . GLY A 234 ? 0.12045 0.11171 0.13781 0.01631  0.00177  0.00629  234 GLY A C   
1793 O O   . GLY A 234 ? 0.12686 0.11503 0.14456 0.01667  0.00287  0.00535  234 GLY A O   
1794 N N   . PHE A 235 ? 0.09304 0.08541 0.10474 0.01480  0.00175  0.00614  235 PHE A N   
1795 C CA  . PHE A 235 ? 0.11775 0.10797 0.12354 0.01362  0.00270  0.00538  235 PHE A CA  
1796 C C   . PHE A 235 ? 0.11493 0.10342 0.12039 0.01371  0.00535  0.00248  235 PHE A C   
1797 O O   . PHE A 235 ? 0.10985 0.09974 0.11630 0.01373  0.00701  0.00069  235 PHE A O   
1798 C CB  . PHE A 235 ? 0.12990 0.12184 0.13094 0.01229  0.00222  0.00545  235 PHE A CB  
1799 C CG  . PHE A 235 ? 0.11922 0.10945 0.11497 0.01126  0.00299  0.00472  235 PHE A CG  
1800 C CD1 . PHE A 235 ? 0.15175 0.14115 0.14542 0.01083  0.00483  0.00262  235 PHE A CD1 
1801 C CD2 . PHE A 235 ? 0.10492 0.09473 0.09789 0.01064  0.00185  0.00628  235 PHE A CD2 
1802 C CE1 . PHE A 235 ? 0.08928 0.07737 0.07874 0.01003  0.00513  0.00212  235 PHE A CE1 
1803 C CE2 . PHE A 235 ? 0.13035 0.11909 0.11944 0.00981  0.00255  0.00549  235 PHE A CE2 
1804 C CZ  . PHE A 235 ? 0.11185 0.09972 0.09945 0.00961  0.00401  0.00342  235 PHE A CZ  
1805 N N   . GLN A 236 ? 0.10923 0.09485 0.11331 0.01358  0.00576  0.00202  236 GLN A N   
1806 C CA  . GLN A 236 ? 0.13828 0.12220 0.14090 0.01336  0.00795  -0.00086 236 GLN A CA  
1807 C C   . GLN A 236 ? 0.16958 0.15193 0.16701 0.01211  0.00760  -0.00081 236 GLN A C   
1808 O O   . GLN A 236 ? 0.17057 0.15106 0.16842 0.01196  0.00668  0.00019  236 GLN A O   
1809 C CB  . GLN A 236 ? 0.10337 0.08534 0.11099 0.01459  0.00882  -0.00229 236 GLN A CB  
1810 C CG  . GLN A 236 ? 0.15835 0.14226 0.17217 0.01607  0.00942  -0.00277 236 GLN A CG  
1811 C CD  . GLN A 236 ? 0.20529 0.18755 0.22361 0.01725  0.01139  -0.00572 236 GLN A CD  
1812 O OE1 . GLN A 236 ? 0.25508 0.23732 0.28033 0.01892  0.01097  -0.00538 236 GLN A OE1 
1813 N NE2 . GLN A 236 ? 0.25065 0.23166 0.26518 0.01642  0.01349  -0.00878 236 GLN A NE2 
1814 N N   . LYS A 237 ? 0.09363 0.07677 0.08671 0.01118  0.00828  -0.00171 237 LYS A N   
1815 C CA  . LYS A 237 ? 0.09909 0.08147 0.08788 0.01014  0.00763  -0.00143 237 LYS A CA  
1816 C C   . LYS A 237 ? 0.09777 0.07779 0.08615 0.00981  0.00780  -0.00259 237 LYS A C   
1817 O O   . LYS A 237 ? 0.09473 0.07422 0.08221 0.00921  0.00672  -0.00143 237 LYS A O   
1818 C CB  . LYS A 237 ? 0.09237 0.07565 0.07739 0.00943  0.00827  -0.00221 237 LYS A CB  
1819 C CG  . LYS A 237 ? 0.09190 0.07472 0.07331 0.00861  0.00744  -0.00194 237 LYS A CG  
1820 C CD  . LYS A 237 ? 0.09035 0.07414 0.07199 0.00850  0.00608  -0.00015 237 LYS A CD  
1821 C CE  . LYS A 237 ? 0.08966 0.07374 0.06849 0.00788  0.00554  -0.00017 237 LYS A CE  
1822 N NZ  . LYS A 237 ? 0.09582 0.08028 0.07290 0.00775  0.00583  -0.00062 237 LYS A NZ  
1823 N N   . PRO A 238 ? 0.16964 0.14837 0.15865 0.01002  0.00917  -0.00504 238 PRO A N   
1824 C CA  . PRO A 238 ? 0.14089 0.11733 0.12951 0.00947  0.00907  -0.00647 238 PRO A CA  
1825 C C   . PRO A 238 ? 0.10041 0.07503 0.09314 0.00977  0.00809  -0.00514 238 PRO A C   
1826 O O   . PRO A 238 ? 0.13520 0.10801 0.12782 0.00897  0.00763  -0.00574 238 PRO A O   
1827 C CB  . PRO A 238 ? 0.17485 0.15063 0.16339 0.00968  0.01098  -0.00977 238 PRO A CB  
1828 C CG  . PRO A 238 ? 0.15614 0.13420 0.14301 0.00979  0.01212  -0.00977 238 PRO A CG  
1829 C CD  . PRO A 238 ? 0.14135 0.12097 0.13071 0.01041  0.01107  -0.00698 238 PRO A CD  
1830 N N   . ASP A 239 ? 0.14622 0.12128 0.14271 0.01078  0.00758  -0.00315 239 ASP A N   
1831 C CA  . ASP A 239 ? 0.12577 0.09884 0.12637 0.01109  0.00649  -0.00125 239 ASP A CA  
1832 C C   . ASP A 239 ? 0.17453 0.14855 0.17355 0.01022  0.00491  0.00222  239 ASP A C   
1833 O O   . ASP A 239 ? 0.19658 0.16917 0.19851 0.01023  0.00388  0.00461  239 ASP A O   
1834 C CB  . ASP A 239 ? 0.11226 0.08531 0.11835 0.01279  0.00650  -0.00069 239 ASP A CB  
1835 C CG  . ASP A 239 ? 0.19737 0.16961 0.20598 0.01374  0.00850  -0.00445 239 ASP A CG  
1836 O OD1 . ASP A 239 ? 0.19929 0.16997 0.20582 0.01300  0.00959  -0.00737 239 ASP A OD1 
1837 O OD2 . ASP A 239 ? 0.26147 0.23495 0.27425 0.01517  0.00900  -0.00463 239 ASP A OD2 
1838 N N   . THR A 240 ? 0.10305 0.07941 0.09768 0.00943  0.00478  0.00257  240 THR A N   
1839 C CA  . THR A 240 ? 0.11129 0.08911 0.10425 0.00860  0.00369  0.00536  240 THR A CA  
1840 C C   . THR A 240 ? 0.12271 0.09953 0.11475 0.00723  0.00365  0.00547  240 THR A C   
1841 O O   . THR A 240 ? 0.11744 0.09300 0.10908 0.00682  0.00420  0.00312  240 THR A O   
1842 C CB  . THR A 240 ? 0.10329 0.08404 0.09275 0.00847  0.00367  0.00532  240 THR A CB  
1843 O OG1 . THR A 240 ? 0.12292 0.10374 0.10991 0.00823  0.00454  0.00286  240 THR A OG1 
1844 C CG2 . THR A 240 ? 0.16654 0.14869 0.15759 0.00949  0.00334  0.00585  240 THR A CG2 
1845 N N   . ASP A 241 ? 0.15074 0.12845 0.14239 0.00636  0.00298  0.00826  241 ASP A N   
1846 C CA  . ASP A 241 ? 0.16626 0.14310 0.15838 0.00490  0.00301  0.00899  241 ASP A CA  
1847 C C   . ASP A 241 ? 0.10847 0.08797 0.09741 0.00398  0.00343  0.00811  241 ASP A C   
1848 O O   . ASP A 241 ? 0.13411 0.11631 0.12077 0.00380  0.00343  0.00933  241 ASP A O   
1849 C CB  . ASP A 241 ? 0.15470 0.13121 0.14822 0.00422  0.00230  0.01283  241 ASP A CB  
1850 C CG  . ASP A 241 ? 0.12185 0.09686 0.11708 0.00251  0.00249  0.01383  241 ASP A CG  
1851 O OD1 . ASP A 241 ? 0.12694 0.10237 0.12164 0.00167  0.00307  0.01163  241 ASP A OD1 
1852 O OD2 . ASP A 241 ? 0.20364 0.17707 0.20103 0.00192  0.00190  0.01704  241 ASP A OD2 
1853 N N   . PRO A 242 ? 0.09839 0.07738 0.08736 0.00341  0.00368  0.00590  242 PRO A N   
1854 C CA  . PRO A 242 ? 0.10713 0.08881 0.09413 0.00275  0.00386  0.00519  242 PRO A CA  
1855 C C   . PRO A 242 ? 0.11931 0.10266 0.10712 0.00127  0.00417  0.00716  242 PRO A C   
1856 O O   . PRO A 242 ? 0.11004 0.09637 0.09653 0.00095  0.00458  0.00689  242 PRO A O   
1857 C CB  . PRO A 242 ? 0.11076 0.09129 0.09798 0.00256  0.00361  0.00247  242 PRO A CB  
1858 C CG  . PRO A 242 ? 0.10404 0.08132 0.09399 0.00229  0.00352  0.00210  242 PRO A CG  
1859 C CD  . PRO A 242 ? 0.12520 0.10131 0.11610 0.00337  0.00368  0.00369  242 PRO A CD  
1860 N N   . SER A 243 ? 0.12700 0.10852 0.11722 0.00033  0.00410  0.00911  243 SER A N   
1861 C CA  . SER A 243 ? 0.13964 0.12282 0.13064 -0.00145 0.00466  0.01132  243 SER A CA  
1862 C C   . SER A 243 ? 0.13957 0.12486 0.12821 -0.00164 0.00498  0.01423  243 SER A C   
1863 O O   . SER A 243 ? 0.19156 0.17887 0.18001 -0.00327 0.00580  0.01618  243 SER A O   
1864 C CB  . SER A 243 ? 0.12306 0.10304 0.11788 -0.00272 0.00442  0.01244  243 SER A CB  
1865 O OG  . SER A 243 ? 0.17575 0.15286 0.17177 -0.00213 0.00383  0.01471  243 SER A OG  
1866 N N   . ALA A 244 ? 0.10140 0.08660 0.08820 -0.00021 0.00437  0.01452  244 ALA A N   
1867 C CA  . ALA A 244 ? 0.19349 0.18090 0.17757 -0.00046 0.00426  0.01707  244 ALA A CA  
1868 C C   . ALA A 244 ? 0.13263 0.12411 0.11354 -0.00070 0.00526  0.01558  244 ALA A C   
1869 O O   . ALA A 244 ? 0.15136 0.14346 0.13142 0.00050  0.00523  0.01286  244 ALA A O   
1870 C CB  . ALA A 244 ? 0.13354 0.11976 0.11747 0.00112  0.00300  0.01759  244 ALA A CB  
1871 N N   . TRP A 245 ? 0.12885 0.12305 0.10816 -0.00230 0.00625  0.01736  245 TRP A N   
1872 C CA  . TRP A 245 ? 0.18112 0.17937 0.15802 -0.00257 0.00757  0.01553  245 TRP A CA  
1873 C C   . TRP A 245 ? 0.21708 0.21817 0.18983 -0.00346 0.00789  0.01749  245 TRP A C   
1874 O O   . TRP A 245 ? 0.16612 0.16997 0.13626 -0.00306 0.00844  0.01542  245 TRP A O   
1875 C CB  . TRP A 245 ? 0.14235 0.14239 0.12154 -0.00382 0.00910  0.01467  245 TRP A CB  
1876 C CG  . TRP A 245 ? 0.23843 0.23876 0.21846 -0.00602 0.00991  0.01793  245 TRP A CG  
1877 C CD1 . TRP A 245 ? 0.19901 0.19618 0.18253 -0.00688 0.00938  0.01954  245 TRP A CD1 
1878 C CD2 . TRP A 245 ? 0.22493 0.22887 0.20225 -0.00786 0.01152  0.02001  245 TRP A CD2 
1879 N NE1 . TRP A 245 ? 0.14748 0.14579 0.13099 -0.00918 0.01046  0.02285  245 TRP A NE1 
1880 C CE2 . TRP A 245 ? 0.22437 0.22704 0.20378 -0.00987 0.01188  0.02333  245 TRP A CE2 
1881 C CE3 . TRP A 245 ? 0.29377 0.30190 0.26697 -0.00812 0.01280  0.01924  245 TRP A CE3 
1882 C CZ2 . TRP A 245 ? 0.28997 0.29558 0.26719 -0.01227 0.01355  0.02636  245 TRP A CZ2 
1883 C CZ3 . TRP A 245 ? 0.28039 0.29169 0.25107 -0.01041 0.01454  0.02177  245 TRP A CZ3 
1884 C CH2 . TRP A 245 ? 0.32248 0.33259 0.29503 -0.01252 0.01494  0.02554  245 TRP A CH2 
1885 N N   . GLU A 246 ? 0.19793 0.19832 0.16996 -0.00474 0.00743  0.02146  246 GLU A N   
1886 C CA  . GLU A 246 ? 0.18287 0.18588 0.15019 -0.00563 0.00719  0.02371  246 GLU A CA  
1887 C C   . GLU A 246 ? 0.20099 0.20377 0.16663 -0.00396 0.00538  0.02257  246 GLU A C   
1888 O O   . GLU A 246 ? 0.22137 0.22725 0.18334 -0.00402 0.00569  0.02088  246 GLU A O   
1889 C CB  . GLU A 246 ? 0.23175 0.23330 0.19899 -0.00716 0.00645  0.02885  246 GLU A CB  
1890 C CG  . GLU A 246 ? 0.30935 0.31220 0.27720 -0.00955 0.00853  0.03063  246 GLU A CG  
1891 C CD  . GLU A 246 ? 0.35768 0.35842 0.32568 -0.01116 0.00761  0.03623  246 GLU A CD  
1892 O OE1 . GLU A 246 ? 0.51167 0.50776 0.48427 -0.01051 0.00620  0.03759  246 GLU A OE1 
1893 O OE2 . GLU A 246 ? 0.37627 0.37994 0.33976 -0.01312 0.00829  0.03930  246 GLU A OE2 
1894 N N   . LYS A 247 ? 0.23309 0.23233 0.20175 -0.00255 0.00359  0.02324  247 LYS A N   
1895 C CA  . LYS A 247 ? 0.21550 0.21446 0.18402 -0.00089 0.00203  0.02180  247 LYS A CA  
1896 C C   . LYS A 247 ? 0.11533 0.11151 0.08770 0.00069  0.00220  0.01892  247 LYS A C   
1897 O O   . LYS A 247 ? 0.16393 0.15688 0.13985 0.00134  0.00152  0.01990  247 LYS A O   
1898 C CB  . LYS A 247 ? 0.26164 0.25957 0.23050 -0.00063 -0.00029 0.02545  247 LYS A CB  
1899 C CG  . LYS A 247 ? 0.21648 0.21527 0.18517 0.00072  -0.00200 0.02423  247 LYS A CG  
1900 C CD  . LYS A 247 ? 0.21086 0.21376 0.17420 -0.00026 -0.00220 0.02352  247 LYS A CD  
1901 C CE  . LYS A 247 ? 0.22196 0.22697 0.18108 -0.00227 -0.00223 0.02713  247 LYS A CE  
1902 N NZ  . LYS A 247 ? 0.22942 0.23265 0.19008 -0.00231 -0.00452 0.03213  247 LYS A NZ  
1903 N N   . PRO A 248 ? 0.10929 0.10650 0.08110 0.00129  0.00310  0.01539  248 PRO A N   
1904 C CA  . PRO A 248 ? 0.09861 0.09336 0.07328 0.00254  0.00322  0.01300  248 PRO A CA  
1905 C C   . PRO A 248 ? 0.15727 0.15002 0.13392 0.00381  0.00193  0.01334  248 PRO A C   
1906 O O   . PRO A 248 ? 0.13535 0.12935 0.11105 0.00410  0.00083  0.01415  248 PRO A O   
1907 C CB  . PRO A 248 ? 0.12045 0.11700 0.09365 0.00291  0.00399  0.00989  248 PRO A CB  
1908 C CG  . PRO A 248 ? 0.14806 0.14785 0.11866 0.00169  0.00498  0.01011  248 PRO A CG  
1909 C CD  . PRO A 248 ? 0.13479 0.13538 0.10345 0.00078  0.00412  0.01339  248 PRO A CD  
1910 N N   . ALA A 249 ? 0.11298 0.10287 0.09258 0.00449  0.00212  0.01249  249 ALA A N   
1911 C CA  . ALA A 249 ? 0.11267 0.10061 0.09509 0.00569  0.00134  0.01271  249 ALA A CA  
1912 C C   . ALA A 249 ? 0.09957 0.08844 0.08169 0.00664  0.00129  0.01070  249 ALA A C   
1913 O O   . ALA A 249 ? 0.11047 0.09880 0.09508 0.00759  0.00070  0.01094  249 ALA A O   
1914 C CB  . ALA A 249 ? 0.12774 0.11254 0.11307 0.00596  0.00191  0.01172  249 ALA A CB  
1915 N N   . THR A 250 ? 0.09245 0.08266 0.07221 0.00640  0.00193  0.00877  250 THR A N   
1916 C CA  . THR A 250 ? 0.09084 0.08171 0.07042 0.00699  0.00192  0.00709  250 THR A CA  
1917 C C   . THR A 250 ? 0.10409 0.09761 0.08119 0.00644  0.00143  0.00695  250 THR A C   
1918 O O   . THR A 250 ? 0.10211 0.09717 0.07737 0.00566  0.00114  0.00824  250 THR A O   
1919 C CB  . THR A 250 ? 0.08927 0.07875 0.06863 0.00721  0.00294  0.00492  250 THR A CB  
1920 O OG1 . THR A 250 ? 0.08903 0.07899 0.06681 0.00663  0.00335  0.00435  250 THR A OG1 
1921 C CG2 . THR A 250 ? 0.09304 0.08017 0.07445 0.00764  0.00340  0.00460  250 THR A CG2 
1922 N N   . THR A 251 ? 0.09005 0.08409 0.06706 0.00669  0.00141  0.00528  251 THR A N   
1923 C CA  . THR A 251 ? 0.09090 0.08726 0.06610 0.00616  0.00074  0.00467  251 THR A CA  
1924 C C   . THR A 251 ? 0.10169 0.09896 0.07452 0.00563  0.00158  0.00317  251 THR A C   
1925 O O   . THR A 251 ? 0.09299 0.09251 0.06366 0.00497  0.00125  0.00271  251 THR A O   
1926 C CB  . THR A 251 ? 0.08990 0.08628 0.06656 0.00643  0.00046  0.00329  251 THR A CB  
1927 O OG1 . THR A 251 ? 0.08845 0.08302 0.06536 0.00667  0.00159  0.00172  251 THR A OG1 
1928 C CG2 . THR A 251 ? 0.08970 0.08587 0.06949 0.00703  -0.00014 0.00448  251 THR A CG2 
1929 N N   . VAL A 252 ? 0.08988 0.08572 0.06325 0.00592  0.00260  0.00223  252 VAL A N   
1930 C CA  . VAL A 252 ? 0.09068 0.08735 0.06316 0.00577  0.00342  0.00052  252 VAL A CA  
1931 C C   . VAL A 252 ? 0.09035 0.08759 0.06250 0.00581  0.00319  -0.00151 252 VAL A C   
1932 O O   . VAL A 252 ? 0.09172 0.09071 0.06270 0.00549  0.00364  -0.00308 252 VAL A O   
1933 C CB  . VAL A 252 ? 0.10922 0.10814 0.08010 0.00495  0.00403  0.00124  252 VAL A CB  
1934 C CG1 . VAL A 252 ? 0.10234 0.10202 0.07383 0.00504  0.00521  -0.00050 252 VAL A CG1 
1935 C CG2 . VAL A 252 ? 0.09215 0.09025 0.06362 0.00461  0.00388  0.00382  252 VAL A CG2 
1936 N N   . LEU A 253 ? 0.08952 0.08533 0.06295 0.00611  0.00265  -0.00171 253 LEU A N   
1937 C CA  . LEU A 253 ? 0.09006 0.08578 0.06393 0.00600  0.00240  -0.00361 253 LEU A CA  
1938 C C   . LEU A 253 ? 0.08943 0.08292 0.06465 0.00655  0.00290  -0.00466 253 LEU A C   
1939 O O   . LEU A 253 ? 0.10791 0.10067 0.08406 0.00647  0.00271  -0.00617 253 LEU A O   
1940 C CB  . LEU A 253 ? 0.08997 0.08573 0.06502 0.00574  0.00152  -0.00309 253 LEU A CB  
1941 C CG  . LEU A 253 ? 0.09145 0.08980 0.06547 0.00517  0.00035  -0.00231 253 LEU A CG  
1942 C CD1 . LEU A 253 ? 0.09108 0.08976 0.06750 0.00509  -0.00062 -0.00169 253 LEU A CD1 
1943 C CD2 . LEU A 253 ? 0.11760 0.11790 0.08945 0.00445  0.00008  -0.00432 253 LEU A CD2 
1944 N N   . SER A 254 ? 0.09603 0.08838 0.07153 0.00703  0.00331  -0.00384 254 SER A N   
1945 C CA  . SER A 254 ? 0.09747 0.08772 0.07409 0.00756  0.00333  -0.00425 254 SER A CA  
1946 C C   . SER A 254 ? 0.08948 0.07990 0.06728 0.00796  0.00341  -0.00616 254 SER A C   
1947 O O   . SER A 254 ? 0.09031 0.07866 0.06950 0.00823  0.00304  -0.00658 254 SER A O   
1948 C CB  . SER A 254 ? 0.08767 0.07716 0.06412 0.00785  0.00341  -0.00312 254 SER A CB  
1949 O OG  . SER A 254 ? 0.08745 0.07871 0.06386 0.00781  0.00375  -0.00320 254 SER A OG  
1950 N N   . PRO A 255 ? 0.10169 0.09440 0.07931 0.00800  0.00399  -0.00738 255 PRO A N   
1951 C CA  . PRO A 255 ? 0.12136 0.11422 0.10086 0.00859  0.00430  -0.00975 255 PRO A CA  
1952 C C   . PRO A 255 ? 0.09979 0.09210 0.07953 0.00822  0.00404  -0.01158 255 PRO A C   
1953 O O   . PRO A 255 ? 0.09446 0.08515 0.07667 0.00882  0.00391  -0.01325 255 PRO A O   
1954 C CB  . PRO A 255 ? 0.09186 0.08803 0.07080 0.00844  0.00545  -0.01073 255 PRO A CB  
1955 C CG  . PRO A 255 ? 0.10548 0.10248 0.08263 0.00781  0.00548  -0.00827 255 PRO A CG  
1956 C CD  . PRO A 255 ? 0.09060 0.08588 0.06655 0.00745  0.00457  -0.00673 255 PRO A CD  
1957 N N   . TYR A 256 ? 0.09332 0.08684 0.07097 0.00725  0.00374  -0.01128 256 TYR A N   
1958 C CA  . TYR A 256 ? 0.09513 0.08844 0.07309 0.00662  0.00321  -0.01312 256 TYR A CA  
1959 C C   . TYR A 256 ? 0.09477 0.08501 0.07477 0.00651  0.00251  -0.01217 256 TYR A C   
1960 O O   . TYR A 256 ? 0.09662 0.08544 0.07846 0.00622  0.00217  -0.01395 256 TYR A O   
1961 C CB  . TYR A 256 ? 0.09585 0.09197 0.07104 0.00556  0.00273  -0.01283 256 TYR A CB  
1962 C CG  . TYR A 256 ? 0.11051 0.10970 0.08302 0.00534  0.00353  -0.01298 256 TYR A CG  
1963 C CD1 . TYR A 256 ? 0.10862 0.10980 0.08009 0.00507  0.00435  -0.01603 256 TYR A CD1 
1964 C CD2 . TYR A 256 ? 0.11450 0.11456 0.08566 0.00528  0.00366  -0.01019 256 TYR A CD2 
1965 C CE1 . TYR A 256 ? 0.14412 0.14847 0.11287 0.00461  0.00545  -0.01605 256 TYR A CE1 
1966 C CE2 . TYR A 256 ? 0.13093 0.13374 0.09974 0.00479  0.00453  -0.00993 256 TYR A CE2 
1967 C CZ  . TYR A 256 ? 0.09967 0.10481 0.06709 0.00438  0.00551  -0.01275 256 TYR A CZ  
1968 O OH  . TYR A 256 ? 0.14025 0.14849 0.10501 0.00363  0.00672  -0.01242 256 TYR A OH  
1969 N N   . LEU A 257 ? 0.09291 0.08210 0.07268 0.00660  0.00243  -0.00952 257 LEU A N   
1970 C CA  . LEU A 257 ? 0.09898 0.08550 0.08031 0.00633  0.00218  -0.00840 257 LEU A CA  
1971 C C   . LEU A 257 ? 0.09424 0.07793 0.07723 0.00707  0.00210  -0.00830 257 LEU A C   
1972 O O   . LEU A 257 ? 0.15727 0.13845 0.14202 0.00668  0.00180  -0.00805 257 LEU A O   
1973 C CB  . LEU A 257 ? 0.09144 0.07812 0.07174 0.00615  0.00243  -0.00600 257 LEU A CB  
1974 C CG  . LEU A 257 ? 0.09077 0.07974 0.07084 0.00551  0.00218  -0.00569 257 LEU A CG  
1975 C CD1 . LEU A 257 ? 0.16010 0.14921 0.13972 0.00574  0.00266  -0.00375 257 LEU A CD1 
1976 C CD2 . LEU A 257 ? 0.09297 0.08176 0.07507 0.00454  0.00176  -0.00643 257 LEU A CD2 
1977 N N   . LYS A 258 ? 0.10586 0.08997 0.08873 0.00806  0.00225  -0.00835 258 LYS A N   
1978 C CA  . LYS A 258 ? 0.09511 0.07686 0.08012 0.00899  0.00175  -0.00809 258 LYS A CA  
1979 C C   . LYS A 258 ? 0.12425 0.10472 0.11234 0.00934  0.00158  -0.01056 258 LYS A C   
1980 O O   . LYS A 258 ? 0.09963 0.07686 0.09002 0.00949  0.00089  -0.00991 258 LYS A O   
1981 C CB  . LYS A 258 ? 0.09397 0.07725 0.07887 0.00993  0.00183  -0.00783 258 LYS A CB  
1982 C CG  . LYS A 258 ? 0.13287 0.11450 0.12077 0.01117  0.00098  -0.00774 258 LYS A CG  
1983 C CD  . LYS A 258 ? 0.09975 0.08285 0.09076 0.01212  0.00154  -0.01078 258 LYS A CD  
1984 C CE  . LYS A 258 ? 0.11289 0.09484 0.10797 0.01366  0.00059  -0.01070 258 LYS A CE  
1985 N NZ  . LYS A 258 ? 0.20430 0.18227 0.20001 0.01374  -0.00101 -0.00810 258 LYS A NZ  
1986 N N   . PHE A 259 ? 0.10726 0.09016 0.09540 0.00940  0.00225  -0.01344 259 PHE A N   
1987 C CA  . PHE A 259 ? 0.10258 0.08448 0.09364 0.00970  0.00231  -0.01663 259 PHE A CA  
1988 C C   . PHE A 259 ? 0.10832 0.08921 0.09945 0.00832  0.00193  -0.01771 259 PHE A C   
1989 O O   . PHE A 259 ? 0.11672 0.09622 0.11052 0.00834  0.00185  -0.02061 259 PHE A O   
1990 C CB  . PHE A 259 ? 0.14415 0.12952 0.13487 0.01016  0.00347  -0.01973 259 PHE A CB  
1991 C CG  . PHE A 259 ? 0.10067 0.08680 0.09368 0.01168  0.00391  -0.01976 259 PHE A CG  
1992 C CD1 . PHE A 259 ? 0.16305 0.14695 0.16099 0.01311  0.00357  -0.02114 259 PHE A CD1 
1993 C CD2 . PHE A 259 ? 0.12812 0.11724 0.11906 0.01168  0.00453  -0.01841 259 PHE A CD2 
1994 C CE1 . PHE A 259 ? 0.12921 0.11430 0.13011 0.01461  0.00376  -0.02120 259 PHE A CE1 
1995 C CE2 . PHE A 259 ? 0.12860 0.11889 0.12232 0.01292  0.00485  -0.01856 259 PHE A CE2 
1996 C CZ  . PHE A 259 ? 0.14379 0.13229 0.14256 0.01444  0.00441  -0.01996 259 PHE A CZ  
1997 N N   . GLY A 260 ? 0.10263 0.08424 0.09147 0.00713  0.00167  -0.01571 260 GLY A N   
1998 C CA  . GLY A 260 ? 0.12171 0.10310 0.11112 0.00570  0.00119  -0.01674 260 GLY A CA  
1999 C C   . GLY A 260 ? 0.10315 0.08777 0.09090 0.00499  0.00116  -0.01981 260 GLY A C   
2000 O O   . GLY A 260 ? 0.10524 0.08958 0.09417 0.00381  0.00049  -0.02165 260 GLY A O   
2001 N N   . CYS A 261 ? 0.10236 0.09017 0.08726 0.00547  0.00180  -0.02035 261 CYS A N   
2002 C CA  . CYS A 261 ? 0.10976 0.10113 0.09182 0.00449  0.00165  -0.02254 261 CYS A CA  
2003 C C   . CYS A 261 ? 0.10296 0.09594 0.08351 0.00329  0.00048  -0.02056 261 CYS A C   
2004 O O   . CYS A 261 ? 0.13488 0.13020 0.11394 0.00214  -0.00040 -0.02234 261 CYS A O   
2005 C CB  . CYS A 261 ? 0.10679 0.10131 0.08589 0.00502  0.00277  -0.02277 261 CYS A CB  
2006 S SG  . CYS A 261 ? 0.11712 0.11078 0.09896 0.00663  0.00431  -0.02509 261 CYS A SG  
2007 N N   . LEU A 262 ? 0.12389 0.11593 0.10494 0.00355  0.00041  -0.01708 262 LEU A N   
2008 C CA  . LEU A 262 ? 0.09894 0.09242 0.07994 0.00269  -0.00054 -0.01523 262 LEU A CA  
2009 C C   . LEU A 262 ? 0.09816 0.08887 0.08243 0.00238  -0.00047 -0.01387 262 LEU A C   
2010 O O   . LEU A 262 ? 0.09725 0.08533 0.08225 0.00311  0.00036  -0.01244 262 LEU A O   
2011 C CB  . LEU A 262 ? 0.09672 0.09208 0.07547 0.00321  -0.00039 -0.01245 262 LEU A CB  
2012 C CG  . LEU A 262 ? 0.09564 0.09254 0.07526 0.00272  -0.00135 -0.01044 262 LEU A CG  
2013 C CD1 . LEU A 262 ? 0.10695 0.10684 0.08597 0.00158  -0.00304 -0.01178 262 LEU A CD1 
2014 C CD2 . LEU A 262 ? 0.15358 0.15121 0.13194 0.00351  -0.00102 -0.00773 262 LEU A CD2 
2015 N N   . SER A 263 ? 0.12127 0.11284 0.10743 0.00113  -0.00138 -0.01423 263 SER A N   
2016 C CA  . SER A 263 ? 0.09866 0.08828 0.08802 0.00046  -0.00104 -0.01276 263 SER A CA  
2017 C C   . SER A 263 ? 0.09608 0.08666 0.08513 0.00093  -0.00034 -0.00976 263 SER A C   
2018 O O   . SER A 263 ? 0.09478 0.08835 0.08317 0.00107  -0.00095 -0.00907 263 SER A O   
2019 C CB  . SER A 263 ? 0.11379 0.10460 0.10598 -0.00122 -0.00221 -0.01433 263 SER A CB  
2020 O OG  . SER A 263 ? 0.09991 0.08983 0.09534 -0.00209 -0.00162 -0.01250 263 SER A OG  
2021 N N   . ALA A 264 ? 0.09548 0.08345 0.08506 0.00115  0.00088  -0.00799 264 ALA A N   
2022 C CA  . ALA A 264 ? 0.10673 0.09549 0.09625 0.00140  0.00186  -0.00572 264 ALA A CA  
2023 C C   . ALA A 264 ? 0.11701 0.10812 0.10979 0.00031  0.00174  -0.00550 264 ALA A C   
2024 O O   . ALA A 264 ? 0.09206 0.08542 0.08542 0.00076  0.00203  -0.00447 264 ALA A O   
2025 C CB  . ALA A 264 ? 0.14553 0.13122 0.13436 0.00150  0.00313  -0.00409 264 ALA A CB  
2026 N N   . ARG A 265 ? 0.10775 0.09840 0.10336 -0.00113 0.00128  -0.00657 265 ARG A N   
2027 C CA  . ARG A 265 ? 0.14268 0.13600 0.14225 -0.00236 0.00108  -0.00649 265 ARG A CA  
2028 C C   . ARG A 265 ? 0.11434 0.11159 0.11429 -0.00211 -0.00083 -0.00743 265 ARG A C   
2029 O O   . ARG A 265 ? 0.09607 0.09636 0.09881 -0.00214 -0.00099 -0.00655 265 ARG A O   
2030 C CB  . ARG A 265 ? 0.11655 0.10820 0.11936 -0.00422 0.00094  -0.00746 265 ARG A CB  
2031 C CG  . ARG A 265 ? 0.12325 0.11155 0.12643 -0.00486 0.00285  -0.00554 265 ARG A CG  
2032 C CD  . ARG A 265 ? 0.13001 0.11564 0.13633 -0.00669 0.00253  -0.00628 265 ARG A CD  
2033 N NE  . ARG A 265 ? 0.12609 0.10827 0.13215 -0.00735 0.00420  -0.00376 265 ARG A NE  
2034 C CZ  . ARG A 265 ? 0.14282 0.12134 0.15113 -0.00876 0.00414  -0.00345 265 ARG A CZ  
2035 N NH1 . ARG A 265 ? 0.11005 0.08767 0.12143 -0.00965 0.00262  -0.00600 265 ARG A NH1 
2036 N NH2 . ARG A 265 ? 0.18311 0.15869 0.19050 -0.00938 0.00556  -0.00047 265 ARG A NH2 
2037 N N   . LEU A 266 ? 0.09971 0.09714 0.09698 -0.00187 -0.00229 -0.00915 266 LEU A N   
2038 C CA  . LEU A 266 ? 0.10697 0.10812 0.10332 -0.00169 -0.00426 -0.00953 266 LEU A CA  
2039 C C   . LEU A 266 ? 0.10704 0.10938 0.10204 -0.00016 -0.00388 -0.00719 266 LEU A C   
2040 O O   . LEU A 266 ? 0.13890 0.14433 0.13592 0.00003  -0.00506 -0.00616 266 LEU A O   
2041 C CB  . LEU A 266 ? 0.09813 0.09920 0.09084 -0.00184 -0.00537 -0.01188 266 LEU A CB  
2042 C CG  . LEU A 266 ? 0.20691 0.21197 0.19747 -0.00199 -0.00758 -0.01214 266 LEU A CG  
2043 C CD1 . LEU A 266 ? 0.15581 0.16400 0.15023 -0.00334 -0.00963 -0.01263 266 LEU A CD1 
2044 C CD2 . LEU A 266 ? 0.16538 0.17053 0.15154 -0.00224 -0.00804 -0.01467 266 LEU A CD2 
2045 N N   . PHE A 267 ? 0.12549 0.12535 0.11755 0.00095  -0.00240 -0.00639 267 PHE A N   
2046 C CA  . PHE A 267 ? 0.13220 0.13245 0.12340 0.00227  -0.00182 -0.00438 267 PHE A CA  
2047 C C   . PHE A 267 ? 0.11763 0.11895 0.11293 0.00239  -0.00099 -0.00319 267 PHE A C   
2048 O O   . PHE A 267 ? 0.14077 0.14432 0.13788 0.00312  -0.00174 -0.00207 267 PHE A O   
2049 C CB  . PHE A 267 ? 0.11678 0.11399 0.10492 0.00308  -0.00029 -0.00404 267 PHE A CB  
2050 C CG  . PHE A 267 ? 0.13150 0.12887 0.11808 0.00425  0.00001  -0.00251 267 PHE A CG  
2051 C CD1 . PHE A 267 ? 0.12704 0.12661 0.11524 0.00471  -0.00089 -0.00123 267 PHE A CD1 
2052 C CD2 . PHE A 267 ? 0.17499 0.17018 0.15902 0.00487  0.00103  -0.00230 267 PHE A CD2 
2053 C CE1 . PHE A 267 ? 0.16997 0.16908 0.15725 0.00571  -0.00063 0.00021  267 PHE A CE1 
2054 C CE2 . PHE A 267 ? 0.13170 0.12680 0.11470 0.00570  0.00129  -0.00104 267 PHE A CE2 
2055 C CZ  . PHE A 267 ? 0.12351 0.12033 0.10812 0.00609  0.00052  0.00020  267 PHE A CZ  
2056 N N   . HIS A 268 ? 0.10364 0.10350 0.10076 0.00164  0.00062  -0.00338 268 HIS A N   
2057 C CA  . HIS A 268 ? 0.08929 0.09052 0.09030 0.00159  0.00202  -0.00255 268 HIS A CA  
2058 C C   . HIS A 268 ? 0.12680 0.13197 0.13269 0.00109  0.00047  -0.00278 268 HIS A C   
2059 O O   . HIS A 268 ? 0.10164 0.10911 0.11103 0.00190  0.00079  -0.00200 268 HIS A O   
2060 C CB  . HIS A 268 ? 0.09456 0.09360 0.09592 0.00046  0.00412  -0.00247 268 HIS A CB  
2061 C CG  . HIS A 268 ? 0.16784 0.16805 0.17182 0.00043  0.00641  -0.00170 268 HIS A CG  
2062 N ND1 . HIS A 268 ? 0.09020 0.09369 0.09970 -0.00035 0.00677  -0.00186 268 HIS A ND1 
2063 C CD2 . HIS A 268 ? 0.12687 0.12572 0.12877 0.00100  0.00858  -0.00105 268 HIS A CD2 
2064 C CE1 . HIS A 268 ? 0.10003 0.10422 0.11086 -0.00018 0.00938  -0.00142 268 HIS A CE1 
2065 N NE2 . HIS A 268 ? 0.12750 0.12882 0.13342 0.00059  0.01049  -0.00101 268 HIS A NE2 
2066 N N   . ALA A 269 ? 0.09833 0.10447 0.10491 -0.00018 -0.00136 -0.00404 269 ALA A N   
2067 C CA  . ALA A 269 ? 0.16139 0.17164 0.17287 -0.00088 -0.00325 -0.00435 269 ALA A CA  
2068 C C   . ALA A 269 ? 0.14554 0.15851 0.15679 0.00043  -0.00554 -0.00331 269 ALA A C   
2069 O O   . ALA A 269 ? 0.09244 0.10885 0.10876 0.00080  -0.00652 -0.00254 269 ALA A O   
2070 C CB  . ALA A 269 ? 0.12640 0.13683 0.13829 -0.00276 -0.00485 -0.00633 269 ALA A CB  
2071 N N   . ARG A 270 ? 0.12473 0.13632 0.13054 0.00112  -0.00642 -0.00308 270 ARG A N   
2072 C CA  . ARG A 270 ? 0.14372 0.15738 0.14876 0.00223  -0.00848 -0.00143 270 ARG A CA  
2073 C C   . ARG A 270 ? 0.14094 0.15421 0.14863 0.00394  -0.00712 0.00040  270 ARG A C   
2074 O O   . ARG A 270 ? 0.19412 0.20983 0.20496 0.00489  -0.00885 0.00195  270 ARG A O   
2075 C CB  . ARG A 270 ? 0.13501 0.14723 0.13343 0.00228  -0.00913 -0.00153 270 ARG A CB  
2076 C CG  . ARG A 270 ? 0.16900 0.18199 0.16467 0.00072  -0.01057 -0.00382 270 ARG A CG  
2077 C CD  . ARG A 270 ? 0.23131 0.24856 0.22809 -0.00002 -0.01397 -0.00362 270 ARG A CD  
2078 N NE  . ARG A 270 ? 0.28741 0.30612 0.28161 0.00090  -0.01560 -0.00107 270 ARG A NE  
2079 C CZ  . ARG A 270 ? 0.27894 0.29762 0.26693 0.00058  -0.01617 -0.00100 270 ARG A CZ  
2080 N NH1 . ARG A 270 ? 0.20758 0.22499 0.19153 -0.00039 -0.01515 -0.00377 270 ARG A NH1 
2081 N NH2 . ARG A 270 ? 0.32551 0.34548 0.31159 0.00123  -0.01770 0.00194  270 ARG A NH2 
2082 N N   . LEU A 271 ? 0.10527 0.11546 0.11184 0.00438  -0.00418 0.00017  271 LEU A N   
2083 C CA  . LEU A 271 ? 0.08899 0.09865 0.09807 0.00586  -0.00255 0.00117  271 LEU A CA  
2084 C C   . LEU A 271 ? 0.14307 0.15594 0.15940 0.00609  -0.00232 0.00115  271 LEU A C   
2085 O O   . LEU A 271 ? 0.19015 0.20446 0.21033 0.00757  -0.00293 0.00223  271 LEU A O   
2086 C CB  . LEU A 271 ? 0.08723 0.09341 0.09335 0.00585  0.00043  0.00053  271 LEU A CB  
2087 C CG  . LEU A 271 ? 0.08783 0.09103 0.08809 0.00616  0.00046  0.00077  271 LEU A CG  
2088 C CD1 . LEU A 271 ? 0.11249 0.11282 0.11033 0.00586  0.00287  0.00008  271 LEU A CD1 
2089 C CD2 . LEU A 271 ? 0.10768 0.11059 0.10789 0.00754  -0.00018 0.00218  271 LEU A CD2 
2090 N N   . LEU A 272 ? 0.09519 0.10925 0.11406 0.00464  -0.00137 -0.00004 272 LEU A N   
2091 C CA  . LEU A 272 ? 0.13722 0.15489 0.16364 0.00466  -0.00076 -0.00023 272 LEU A CA  
2092 C C   . LEU A 272 ? 0.12212 0.14381 0.15309 0.00526  -0.00429 0.00066  272 LEU A C   
2093 O O   . LEU A 272 ? 0.12786 0.15239 0.16550 0.00645  -0.00424 0.00112  272 LEU A O   
2094 C CB  . LEU A 272 ? 0.12697 0.14518 0.15514 0.00255  0.00076  -0.00143 272 LEU A CB  
2095 C CG  . LEU A 272 ? 0.17544 0.19021 0.20014 0.00188  0.00432  -0.00178 272 LEU A CG  
2096 C CD1 . LEU A 272 ? 0.17930 0.19473 0.20654 -0.00042 0.00566  -0.00239 272 LEU A CD1 
2097 C CD2 . LEU A 272 ? 0.20585 0.22054 0.23180 0.00333  0.00707  -0.00163 272 LEU A CD2 
2098 N N   . GLU A 273 ? 0.15405 0.17621 0.18157 0.00446  -0.00746 0.00084  273 GLU A N   
2099 C CA  . GLU A 273 ? 0.19404 0.22012 0.22484 0.00486  -0.01133 0.00202  273 GLU A CA  
2100 C C   . GLU A 273 ? 0.12541 0.15128 0.15741 0.00716  -0.01220 0.00430  273 GLU A C   
2101 O O   . GLU A 273 ? 0.21014 0.23945 0.24840 0.00820  -0.01438 0.00559  273 GLU A O   
2102 C CB  . GLU A 273 ? 0.26368 0.29004 0.28888 0.00343  -0.01430 0.00159  273 GLU A CB  
2103 C CG  . GLU A 273 ? 0.25560 0.28289 0.28144 0.00112  -0.01451 -0.00080 273 GLU A CG  
2104 C CD  . GLU A 273 ? 0.33874 0.36557 0.35811 -0.00019 -0.01679 -0.00195 273 GLU A CD  
2105 O OE1 . GLU A 273 ? 0.33033 0.35742 0.34531 0.00055  -0.01871 -0.00051 273 GLU A OE1 
2106 O OE2 . GLU A 273 ? 0.43504 0.46118 0.45375 -0.00202 -0.01651 -0.00434 273 GLU A OE2 
2107 N N   . VAL A 274 ? 0.16032 0.18216 0.18696 0.00796  -0.01068 0.00490  274 VAL A N   
2108 C CA  . VAL A 274 ? 0.17156 0.19245 0.19949 0.00997  -0.01134 0.00706  274 VAL A CA  
2109 C C   . VAL A 274 ? 0.14909 0.16992 0.18360 0.01152  -0.00863 0.00644  274 VAL A C   
2110 O O   . VAL A 274 ? 0.14145 0.16366 0.18183 0.01330  -0.00987 0.00785  274 VAL A O   
2111 C CB  . VAL A 274 ? 0.18864 0.20544 0.20892 0.01000  -0.01070 0.00779  274 VAL A CB  
2112 C CG1 . VAL A 274 ? 0.16884 0.18397 0.19111 0.01190  -0.01092 0.00989  274 VAL A CG1 
2113 C CG2 . VAL A 274 ? 0.18681 0.20442 0.20109 0.00863  -0.01336 0.00840  274 VAL A CG2 
2114 N N   . TYR A 275 ? 0.12608 0.14544 0.15989 0.01086  -0.00491 0.00432  275 TYR A N   
2115 C CA  . TYR A 275 ? 0.14078 0.16038 0.18007 0.01208  -0.00182 0.00321  275 TYR A CA  
2116 C C   . TYR A 275 ? 0.08815 0.11272 0.13695 0.01266  -0.00255 0.00305  275 TYR A C   
2117 O O   . TYR A 275 ? 0.10450 0.13003 0.15967 0.01450  -0.00128 0.00274  275 TYR A O   
2118 C CB  . TYR A 275 ? 0.12600 0.14358 0.16176 0.01079  0.00210  0.00122  275 TYR A CB  
2119 C CG  . TYR A 275 ? 0.08723 0.10009 0.11523 0.01070  0.00330  0.00115  275 TYR A CG  
2120 C CD1 . TYR A 275 ? 0.13530 0.14593 0.16080 0.01185  0.00164  0.00254  275 TYR A CD1 
2121 C CD2 . TYR A 275 ? 0.09281 0.10357 0.11629 0.00937  0.00596  -0.00008 275 TYR A CD2 
2122 C CE1 . TYR A 275 ? 0.14922 0.15599 0.16838 0.01164  0.00269  0.00237  275 TYR A CE1 
2123 C CE2 . TYR A 275 ? 0.08718 0.09407 0.10420 0.00934  0.00672  -0.00011 275 TYR A CE2 
2124 C CZ  . TYR A 275 ? 0.08930 0.09436 0.10439 0.01046  0.00514  0.00094  275 TYR A CZ  
2125 O OH  . TYR A 275 ? 0.11227 0.11389 0.12159 0.01029  0.00584  0.00080  275 TYR A OH  
2126 N N   . ARG A 276 ? 0.10876 0.13667 0.15919 0.01113  -0.00460 0.00302  276 ARG A N   
2127 C CA  . ARG A 276 ? 0.15582 0.18904 0.21593 0.01141  -0.00535 0.00273  276 ARG A CA  
2128 C C   . ARG A 276 ? 0.12956 0.16503 0.19556 0.01367  -0.00886 0.00483  276 ARG A C   
2129 O O   . ARG A 276 ? 0.13204 0.17137 0.20764 0.01493  -0.00871 0.00455  276 ARG A O   
2130 C CB  . ARG A 276 ? 0.11324 0.14933 0.17352 0.00896  -0.00715 0.00211  276 ARG A CB  
2131 C CG  . ARG A 276 ? 0.18629 0.22144 0.24500 0.00681  -0.00342 0.00014  276 ARG A CG  
2132 C CD  . ARG A 276 ? 0.15680 0.19559 0.22421 0.00693  -0.00027 -0.00103 276 ARG A CD  
2133 N NE  . ARG A 276 ? 0.15647 0.19908 0.22853 0.00460  -0.00073 -0.00186 276 ARG A NE  
2134 C CZ  . ARG A 276 ? 0.15230 0.19996 0.23146 0.00451  -0.00418 -0.00153 276 ARG A CZ  
2135 N NH1 . ARG A 276 ? 0.15608 0.20565 0.23843 0.00671  -0.00770 -0.00004 276 ARG A NH1 
2136 N NH2 . ARG A 276 ? 0.14608 0.19694 0.22941 0.00204  -0.00432 -0.00255 276 ARG A NH2 
2137 N N   . ARG A 277 ? 0.17979 0.21304 0.24053 0.01418  -0.01200 0.00710  277 ARG A N   
2138 C CA  . ARG A 277 ? 0.17372 0.20843 0.23919 0.01622  -0.01569 0.00986  277 ARG A CA  
2139 C C   . ARG A 277 ? 0.16801 0.19864 0.23380 0.01846  -0.01423 0.01077  277 ARG A C   
2140 O O   . ARG A 277 ? 0.14207 0.17303 0.21201 0.02031  -0.01719 0.01341  277 ARG A O   
2141 C CB  . ARG A 277 ? 0.22441 0.25970 0.28396 0.01510  -0.02042 0.01225  277 ARG A CB  
2142 C CG  . ARG A 277 ? 0.25678 0.29622 0.31638 0.01287  -0.02255 0.01114  277 ARG A CG  
2143 C CD  . ARG A 277 ? 0.27752 0.31753 0.33025 0.01169  -0.02701 0.01310  277 ARG A CD  
2144 N NE  . ARG A 277 ? 0.29303 0.33700 0.34590 0.00945  -0.02929 0.01158  277 ARG A NE  
2145 C CZ  . ARG A 277 ? 0.30430 0.34976 0.35138 0.00795  -0.03315 0.01236  277 ARG A CZ  
2146 N NH1 . ARG A 277 ? 0.31141 0.35499 0.35179 0.00834  -0.03507 0.01501  277 ARG A NH1 
2147 N NH2 . ARG A 277 ? 0.30813 0.35714 0.35609 0.00582  -0.03504 0.01035  277 ARG A NH2 
2148 N N   . HIS A 278 ? 0.14206 0.16881 0.20374 0.01825  -0.00997 0.00873  278 HIS A N   
2149 C CA  . HIS A 278 ? 0.16873 0.19131 0.23042 0.02006  -0.00837 0.00898  278 HIS A CA  
2150 C C   . HIS A 278 ? 0.13299 0.15504 0.19768 0.02051  -0.00338 0.00556  278 HIS A C   
2151 O O   . HIS A 278 ? 0.09113 0.11036 0.14915 0.01922  -0.00035 0.00380  278 HIS A O   
2152 C CB  . HIS A 278 ? 0.14281 0.16077 0.19448 0.01906  -0.00868 0.01012  278 HIS A CB  
2153 C CG  . HIS A 278 ? 0.12832 0.14681 0.17660 0.01860  -0.01318 0.01354  278 HIS A CG  
2154 N ND1 . HIS A 278 ? 0.18110 0.19822 0.23152 0.02013  -0.01581 0.01674  278 HIS A ND1 
2155 C CD2 . HIS A 278 ? 0.18046 0.20076 0.22324 0.01668  -0.01548 0.01422  278 HIS A CD2 
2156 C CE1 . HIS A 278 ? 0.24871 0.26703 0.29450 0.01904  -0.01950 0.01953  278 HIS A CE1 
2157 N NE2 . HIS A 278 ? 0.18535 0.20571 0.22636 0.01696  -0.01930 0.01778  278 HIS A NE2 
2158 N N   . PRO A 279 ? 0.11311 0.13798 0.18782 0.02237  -0.00239 0.00453  279 PRO A N   
2159 C CA  . PRO A 279 ? 0.15309 0.17866 0.23063 0.02241  0.00273  0.00090  279 PRO A CA  
2160 C C   . PRO A 279 ? 0.13437 0.15498 0.20764 0.02299  0.00589  -0.00086 279 PRO A C   
2161 O O   . PRO A 279 ? 0.09307 0.11363 0.16480 0.02220  0.01022  -0.00384 279 PRO A O   
2162 C CB  . PRO A 279 ? 0.18409 0.21424 0.27440 0.02460  0.00254  0.00037  279 PRO A CB  
2163 C CG  . PRO A 279 ? 0.24470 0.27426 0.33841 0.02648  -0.00247 0.00389  279 PRO A CG  
2164 C CD  . PRO A 279 ? 0.18573 0.21377 0.26991 0.02445  -0.00594 0.00663  279 PRO A CD  
2165 N N   . ALA A 280 ? 0.13570 0.15222 0.20682 0.02411  0.00385  0.00093  280 ALA A N   
2166 C CA  . ALA A 280 ? 0.15955 0.17124 0.22692 0.02451  0.00639  -0.00078 280 ALA A CA  
2167 C C   . ALA A 280 ? 0.11979 0.12795 0.17588 0.02240  0.00625  -0.00010 280 ALA A C   
2168 O O   . ALA A 280 ? 0.10936 0.11324 0.16195 0.02264  0.00674  -0.00034 280 ALA A O   
2169 C CB  . ALA A 280 ? 0.11810 0.12715 0.19115 0.02698  0.00448  0.00061  280 ALA A CB  
2170 N N   . HIS A 281 ? 0.09287 0.10278 0.14388 0.02036  0.00552  0.00061  281 HIS A N   
2171 C CA  . HIS A 281 ? 0.13344 0.14039 0.17466 0.01852  0.00537  0.00112  281 HIS A CA  
2172 C C   . HIS A 281 ? 0.10550 0.10987 0.14238 0.01788  0.00915  -0.00164 281 HIS A C   
2173 O O   . HIS A 281 ? 0.09873 0.10460 0.13854 0.01803  0.01230  -0.00414 281 HIS A O   
2174 C CB  . HIS A 281 ? 0.10648 0.11589 0.14440 0.01661  0.00411  0.00184  281 HIS A CB  
2175 C CG  . HIS A 281 ? 0.08945 0.10151 0.12916 0.01554  0.00689  -0.00027 281 HIS A CG  
2176 N ND1 . HIS A 281 ? 0.14063 0.15095 0.17464 0.01403  0.00978  -0.00184 281 HIS A ND1 
2177 C CD2 . HIS A 281 ? 0.11560 0.13205 0.16229 0.01559  0.00718  -0.00080 281 HIS A CD2 
2178 C CE1 . HIS A 281 ? 0.13213 0.14543 0.16918 0.01309  0.01190  -0.00307 281 HIS A CE1 
2179 N NE2 . HIS A 281 ? 0.14588 0.16305 0.19084 0.01397  0.01051  -0.00263 281 HIS A NE2 
2180 N N   . SER A 282 ? 0.13465 0.13543 0.16445 0.01707  0.00880  -0.00118 282 SER A N   
2181 C CA  . SER A 282 ? 0.15233 0.15072 0.17733 0.01632  0.01173  -0.00353 282 SER A CA  
2182 C C   . SER A 282 ? 0.14336 0.14357 0.16523 0.01463  0.01379  -0.00466 282 SER A C   
2183 O O   . SER A 282 ? 0.14169 0.14396 0.16329 0.01366  0.01254  -0.00341 282 SER A O   
2184 C CB  . SER A 282 ? 0.13240 0.12715 0.15099 0.01566  0.01048  -0.00254 282 SER A CB  
2185 O OG  . SER A 282 ? 0.11484 0.11018 0.12974 0.01462  0.00811  -0.00030 282 SER A OG  
2186 N N   . GLN A 283 ? 0.13970 0.13901 0.15909 0.01413  0.01693  -0.00702 283 GLN A N   
2187 C CA  . GLN A 283 ? 0.16392 0.16456 0.18005 0.01240  0.01927  -0.00787 283 GLN A CA  
2188 C C   . GLN A 283 ? 0.15124 0.14882 0.15895 0.01106  0.01954  -0.00791 283 GLN A C   
2189 O O   . GLN A 283 ? 0.17191 0.16669 0.17700 0.01155  0.01869  -0.00816 283 GLN A O   
2190 C CB  . GLN A 283 ? 0.21437 0.21726 0.23445 0.01272  0.02301  -0.01053 283 GLN A CB  
2191 C CG  . GLN A 283 ? 0.15558 0.16213 0.18526 0.01418  0.02297  -0.01072 283 GLN A CG  
2192 C CD  . GLN A 283 ? 0.13748 0.14750 0.16960 0.01301  0.02217  -0.00920 283 GLN A CD  
2193 O OE1 . GLN A 283 ? 0.21689 0.23015 0.25670 0.01402  0.02112  -0.00878 283 GLN A OE1 
2194 N NE2 . GLN A 283 ? 0.21158 0.22089 0.23762 0.01085  0.02250  -0.00837 283 GLN A NE2 
2195 N N   . PRO A 284 ? 0.14639 0.14444 0.15014 0.00931  0.02053  -0.00748 284 PRO A N   
2196 C CA  . PRO A 284 ? 0.17589 0.17124 0.17214 0.00817  0.02062  -0.00736 284 PRO A CA  
2197 C C   . PRO A 284 ? 0.18419 0.17836 0.17820 0.00839  0.02272  -0.00973 284 PRO A C   
2198 O O   . PRO A 284 ? 0.21138 0.20729 0.20893 0.00890  0.02528  -0.01181 284 PRO A O   
2199 C CB  . PRO A 284 ? 0.18660 0.18304 0.18067 0.00633  0.02179  -0.00644 284 PRO A CB  
2200 C CG  . PRO A 284 ? 0.21118 0.21029 0.21111 0.00643  0.02097  -0.00557 284 PRO A CG  
2201 C CD  . PRO A 284 ? 0.15046 0.15137 0.15681 0.00823  0.02113  -0.00673 284 PRO A CD  
2202 N N   . PRO A 285 ? 0.19937 0.19081 0.18776 0.00796  0.02175  -0.00976 285 PRO A N   
2203 C CA  . PRO A 285 ? 0.17895 0.16860 0.16331 0.00738  0.01914  -0.00770 285 PRO A CA  
2204 C C   . PRO A 285 ? 0.17419 0.16255 0.16039 0.00848  0.01655  -0.00684 285 PRO A C   
2205 O O   . PRO A 285 ? 0.16843 0.15575 0.15197 0.00810  0.01461  -0.00540 285 PRO A O   
2206 C CB  . PRO A 285 ? 0.11068 0.09870 0.08861 0.00632  0.01979  -0.00851 285 PRO A CB  
2207 C CG  . PRO A 285 ? 0.19590 0.18378 0.17495 0.00695  0.02162  -0.01144 285 PRO A CG  
2208 C CD  . PRO A 285 ? 0.18400 0.17433 0.16948 0.00784  0.02353  -0.01235 285 PRO A CD  
2209 N N   . VAL A 286 ? 0.15671 0.14517 0.14765 0.00981  0.01653  -0.00759 286 VAL A N   
2210 C CA  . VAL A 286 ? 0.11364 0.10064 0.10586 0.01057  0.01422  -0.00643 286 VAL A CA  
2211 C C   . VAL A 286 ? 0.11475 0.10325 0.10952 0.01090  0.01221  -0.00413 286 VAL A C   
2212 O O   . VAL A 286 ? 0.12648 0.11409 0.12040 0.01097  0.01025  -0.00264 286 VAL A O   
2213 C CB  . VAL A 286 ? 0.13006 0.11585 0.12637 0.01180  0.01479  -0.00790 286 VAL A CB  
2214 C CG1 . VAL A 286 ? 0.10248 0.08654 0.09560 0.01129  0.01644  -0.01061 286 VAL A CG1 
2215 C CG2 . VAL A 286 ? 0.09761 0.08554 0.10026 0.01298  0.01591  -0.00847 286 VAL A CG2 
2216 N N   . SER A 287 ? 0.10293 0.09394 0.10069 0.01092  0.01267  -0.00389 287 SER A N   
2217 C CA  . SER A 287 ? 0.09429 0.08708 0.09471 0.01117  0.01054  -0.00205 287 SER A CA  
2218 C C   . SER A 287 ? 0.10250 0.09491 0.09845 0.01009  0.00905  -0.00092 287 SER A C   
2219 O O   . SER A 287 ? 0.13833 0.12925 0.12993 0.00926  0.00966  -0.00138 287 SER A O   
2220 C CB  . SER A 287 ? 0.09820 0.09408 0.10330 0.01123  0.01138  -0.00240 287 SER A CB  
2221 O OG  . SER A 287 ? 0.09023 0.08669 0.09266 0.00978  0.01266  -0.00281 287 SER A OG  
2222 N N   . LEU A 288 ? 0.09109 0.08495 0.08826 0.01014  0.00694  0.00050  288 LEU A N   
2223 C CA  . LEU A 288 ? 0.09440 0.08826 0.08793 0.00916  0.00573  0.00100  288 LEU A CA  
2224 C C   . LEU A 288 ? 0.08732 0.08169 0.08022 0.00812  0.00670  0.00021  288 LEU A C   
2225 O O   . LEU A 288 ? 0.10949 0.10249 0.09889 0.00739  0.00669  0.00003  288 LEU A O   
2226 C CB  . LEU A 288 ? 0.14894 0.14463 0.14353 0.00925  0.00337  0.00236  288 LEU A CB  
2227 C CG  . LEU A 288 ? 0.13575 0.13056 0.12671 0.00904  0.00218  0.00330  288 LEU A CG  
2228 C CD1 . LEU A 288 ? 0.16969 0.16686 0.16061 0.00871  -0.00003 0.00445  288 LEU A CD1 
2229 C CD2 . LEU A 288 ? 0.13337 0.12670 0.12035 0.00831  0.00300  0.00225  288 LEU A CD2 
2230 N N   . ARG A 289 ? 0.08746 0.08381 0.08427 0.00801  0.00753  -0.00016 289 ARG A N   
2231 C CA  . ARG A 289 ? 0.08795 0.08453 0.08441 0.00675  0.00884  -0.00067 289 ARG A CA  
2232 C C   . ARG A 289 ? 0.08933 0.08359 0.08194 0.00632  0.01079  -0.00110 289 ARG A C   
2233 O O   . ARG A 289 ? 0.09014 0.08310 0.08003 0.00526  0.01102  -0.00083 289 ARG A O   
2234 C CB  . ARG A 289 ? 0.11962 0.11918 0.12158 0.00660  0.00979  -0.00101 289 ARG A CB  
2235 C CG  . ARG A 289 ? 0.12290 0.12265 0.12475 0.00505  0.01177  -0.00133 289 ARG A CG  
2236 C CD  . ARG A 289 ? 0.10875 0.11208 0.11682 0.00470  0.01281  -0.00173 289 ARG A CD  
2237 N NE  . ARG A 289 ? 0.10167 0.10513 0.10947 0.00288  0.01498  -0.00172 289 ARG A NE  
2238 C CZ  . ARG A 289 ? 0.12148 0.12543 0.12914 0.00243  0.01815  -0.00221 289 ARG A CZ  
2239 N NH1 . ARG A 289 ? 0.16980 0.17421 0.17806 0.00379  0.01963  -0.00329 289 ARG A NH1 
2240 N NH2 . ARG A 289 ? 0.09504 0.09897 0.10192 0.00045  0.01997  -0.00165 289 ARG A NH2 
2241 N N   . GLY A 290 ? 0.09014 0.08376 0.08253 0.00712  0.01201  -0.00178 290 GLY A N   
2242 C CA  . GLY A 290 ? 0.09211 0.08378 0.08022 0.00661  0.01353  -0.00234 290 GLY A CA  
2243 C C   . GLY A 290 ? 0.09193 0.08131 0.07554 0.00635  0.01203  -0.00168 290 GLY A C   
2244 O O   . GLY A 290 ? 0.09374 0.08174 0.07369 0.00555  0.01261  -0.00150 290 GLY A O   
2245 N N   . GLN A 291 ? 0.09015 0.07935 0.07410 0.00697  0.01008  -0.00118 291 GLN A N   
2246 C CA  . GLN A 291 ? 0.08991 0.07753 0.07053 0.00680  0.00884  -0.00077 291 GLN A CA  
2247 C C   . GLN A 291 ? 0.09012 0.07739 0.06988 0.00600  0.00838  -0.00031 291 GLN A C   
2248 O O   . GLN A 291 ? 0.09101 0.07667 0.06813 0.00576  0.00797  -0.00003 291 GLN A O   
2249 C CB  . GLN A 291 ? 0.08846 0.07645 0.06975 0.00745  0.00731  -0.00038 291 GLN A CB  
2250 C CG  . GLN A 291 ? 0.08874 0.07642 0.07137 0.00818  0.00752  -0.00052 291 GLN A CG  
2251 C CD  . GLN A 291 ? 0.09034 0.07633 0.07089 0.00807  0.00856  -0.00151 291 GLN A CD  
2252 O OE1 . GLN A 291 ? 0.10375 0.08865 0.08156 0.00774  0.00799  -0.00152 291 GLN A OE1 
2253 N NE2 . GLN A 291 ? 0.10215 0.08818 0.08422 0.00835  0.01005  -0.00255 291 GLN A NE2 
2254 N N   . LEU A 292 ? 0.08963 0.07834 0.07207 0.00559  0.00825  -0.00026 292 LEU A N   
2255 C CA  . LEU A 292 ? 0.09049 0.07845 0.07277 0.00464  0.00801  -0.00001 292 LEU A CA  
2256 C C   . LEU A 292 ? 0.09286 0.07970 0.07383 0.00369  0.00961  0.00061  292 LEU A C   
2257 O O   . LEU A 292 ? 0.09446 0.07954 0.07429 0.00295  0.00931  0.00134  292 LEU A O   
2258 C CB  . LEU A 292 ? 0.08978 0.07971 0.07554 0.00417  0.00734  -0.00036 292 LEU A CB  
2259 C CG  . LEU A 292 ? 0.12244 0.11359 0.10858 0.00466  0.00547  -0.00086 292 LEU A CG  
2260 C CD1 . LEU A 292 ? 0.16594 0.15944 0.15547 0.00399  0.00463  -0.00129 292 LEU A CD1 
2261 C CD2 . LEU A 292 ? 0.13789 0.12734 0.12166 0.00468  0.00463  -0.00134 292 LEU A CD2 
2262 N N   . LEU A 293 ? 0.10199 0.08981 0.08315 0.00366  0.01138  0.00037  293 LEU A N   
2263 C CA  . LEU A 293 ? 0.11084 0.09798 0.08986 0.00251  0.01322  0.00100  293 LEU A CA  
2264 C C   . LEU A 293 ? 0.11697 0.10193 0.09104 0.00255  0.01285  0.00149  293 LEU A C   
2265 O O   . LEU A 293 ? 0.12816 0.11179 0.09948 0.00145  0.01330  0.00279  293 LEU A O   
2266 C CB  . LEU A 293 ? 0.13374 0.12318 0.11481 0.00239  0.01562  0.00009  293 LEU A CB  
2267 C CG  . LEU A 293 ? 0.10611 0.09820 0.09271 0.00205  0.01606  -0.00012 293 LEU A CG  
2268 C CD1 . LEU A 293 ? 0.12366 0.11837 0.11315 0.00217  0.01863  -0.00124 293 LEU A CD1 
2269 C CD2 . LEU A 293 ? 0.14148 0.13298 0.12851 0.00036  0.01609  0.00110  293 LEU A CD2 
2270 N N   . TRP A 294 ? 0.09763 0.08225 0.07062 0.00365  0.01189  0.00067  294 TRP A N   
2271 C CA  . TRP A 294 ? 0.09923 0.08207 0.06819 0.00368  0.01091  0.00109  294 TRP A CA  
2272 C C   . TRP A 294 ? 0.09952 0.08075 0.06806 0.00352  0.00921  0.00246  294 TRP A C   
2273 O O   . TRP A 294 ? 0.12779 0.10749 0.09335 0.00295  0.00873  0.00375  294 TRP A O   
2274 C CB  . TRP A 294 ? 0.11735 0.10028 0.08643 0.00475  0.01000  -0.00004 294 TRP A CB  
2275 C CG  . TRP A 294 ? 0.10791 0.09144 0.07683 0.00493  0.01146  -0.00154 294 TRP A CG  
2276 C CD1 . TRP A 294 ? 0.12700 0.11155 0.09943 0.00576  0.01197  -0.00255 294 TRP A CD1 
2277 C CD2 . TRP A 294 ? 0.12564 0.10868 0.09083 0.00429  0.01251  -0.00235 294 TRP A CD2 
2278 N NE1 . TRP A 294 ? 0.09891 0.08339 0.07070 0.00582  0.01342  -0.00418 294 TRP A NE1 
2279 C CE2 . TRP A 294 ? 0.14860 0.13231 0.11565 0.00484  0.01388  -0.00432 294 TRP A CE2 
2280 C CE3 . TRP A 294 ? 0.19132 0.17347 0.15170 0.00327  0.01230  -0.00157 294 TRP A CE3 
2281 C CZ2 . TRP A 294 ? 0.20902 0.19255 0.17319 0.00435  0.01530  -0.00611 294 TRP A CZ2 
2282 C CZ3 . TRP A 294 ? 0.18684 0.16909 0.14365 0.00263  0.01353  -0.00301 294 TRP A CZ3 
2283 C CH2 . TRP A 294 ? 0.21876 0.20173 0.17745 0.00315  0.01515  -0.00554 294 TRP A CH2 
2284 N N   . ARG A 295 ? 0.09692 0.07849 0.06848 0.00404  0.00818  0.00214  295 ARG A N   
2285 C CA  . ARG A 295 ? 0.11097 0.09098 0.08313 0.00403  0.00679  0.00285  295 ARG A CA  
2286 C C   . ARG A 295 ? 0.10050 0.07911 0.07250 0.00275  0.00741  0.00436  295 ARG A C   
2287 O O   . ARG A 295 ? 0.10315 0.07958 0.07373 0.00254  0.00647  0.00583  295 ARG A O   
2288 C CB  . ARG A 295 ? 0.09477 0.07586 0.06999 0.00457  0.00602  0.00165  295 ARG A CB  
2289 C CG  . ARG A 295 ? 0.09552 0.07510 0.07211 0.00466  0.00483  0.00155  295 ARG A CG  
2290 C CD  . ARG A 295 ? 0.09349 0.07467 0.07222 0.00505  0.00426  -0.00017 295 ARG A CD  
2291 N NE  . ARG A 295 ? 0.09457 0.07441 0.07488 0.00523  0.00335  -0.00103 295 ARG A NE  
2292 C CZ  . ARG A 295 ? 0.09594 0.07490 0.07846 0.00443  0.00321  -0.00154 295 ARG A CZ  
2293 N NH1 . ARG A 295 ? 0.11016 0.08977 0.09371 0.00327  0.00390  -0.00109 295 ARG A NH1 
2294 N NH2 . ARG A 295 ? 0.09733 0.07478 0.08160 0.00477  0.00241  -0.00275 295 ARG A NH2 
2295 N N   . GLU A 296 ? 0.10049 0.08039 0.07434 0.00184  0.00893  0.00423  296 GLU A N   
2296 C CA  . GLU A 296 ? 0.10583 0.08463 0.07988 0.00026  0.00985  0.00583  296 GLU A CA  
2297 C C   . GLU A 296 ? 0.10774 0.08557 0.07723 -0.00056 0.01076  0.00754  296 GLU A C   
2298 O O   . GLU A 296 ? 0.13501 0.11067 0.10313 -0.00164 0.01049  0.00977  296 GLU A O   
2299 C CB  . GLU A 296 ? 0.10277 0.08396 0.08029 -0.00063 0.01148  0.00514  296 GLU A CB  
2300 C CG  . GLU A 296 ? 0.10544 0.08564 0.08505 -0.00244 0.01209  0.00650  296 GLU A CG  
2301 C CD  . GLU A 296 ? 0.13149 0.11012 0.11427 -0.00237 0.01016  0.00593  296 GLU A CD  
2302 O OE1 . GLU A 296 ? 0.10198 0.08097 0.08529 -0.00094 0.00861  0.00427  296 GLU A OE1 
2303 O OE2 . GLU A 296 ? 0.13339 0.11044 0.11819 -0.00390 0.01034  0.00703  296 GLU A OE2 
2304 N N   . PHE A 297 ? 0.12099 0.10031 0.08797 -0.00016 0.01173  0.00654  297 PHE A N   
2305 C CA  . PHE A 297 ? 0.12263 0.10146 0.08447 -0.00108 0.01259  0.00767  297 PHE A CA  
2306 C C   . PHE A 297 ? 0.11433 0.09069 0.07319 -0.00080 0.01014  0.00941  297 PHE A C   
2307 O O   . PHE A 297 ? 0.11917 0.09402 0.07484 -0.00202 0.01001  0.01189  297 PHE A O   
2308 C CB  . PHE A 297 ? 0.15276 0.13351 0.11308 -0.00051 0.01388  0.00547  297 PHE A CB  
2309 C CG  . PHE A 297 ? 0.16725 0.14778 0.12165 -0.00147 0.01464  0.00592  297 PHE A CG  
2310 C CD1 . PHE A 297 ? 0.16594 0.14694 0.11757 -0.00332 0.01681  0.00727  297 PHE A CD1 
2311 C CD2 . PHE A 297 ? 0.16164 0.14177 0.11314 -0.00074 0.01321  0.00493  297 PHE A CD2 
2312 C CE1 . PHE A 297 ? 0.26905 0.25014 0.21428 -0.00441 0.01751  0.00761  297 PHE A CE1 
2313 C CE2 . PHE A 297 ? 0.21117 0.19133 0.15676 -0.00179 0.01364  0.00504  297 PHE A CE2 
2314 C CZ  . PHE A 297 ? 0.20343 0.18409 0.14550 -0.00362 0.01578  0.00638  297 PHE A CZ  
2315 N N   . PHE A 298 ? 0.11126 0.08735 0.07138 0.00077  0.00812  0.00833  298 PHE A N   
2316 C CA  . PHE A 298 ? 0.11323 0.08753 0.07153 0.00128  0.00564  0.00974  298 PHE A CA  
2317 C C   . PHE A 298 ? 0.11478 0.08663 0.07543 0.00118  0.00432  0.01175  298 PHE A C   
2318 O O   . PHE A 298 ? 0.11875 0.08867 0.07741 0.00099  0.00266  0.01412  298 PHE A O   
2319 C CB  . PHE A 298 ? 0.10951 0.08471 0.06934 0.00286  0.00422  0.00786  298 PHE A CB  
2320 C CG  . PHE A 298 ? 0.10920 0.08598 0.06662 0.00288  0.00499  0.00619  298 PHE A CG  
2321 C CD1 . PHE A 298 ? 0.14227 0.11918 0.09492 0.00173  0.00583  0.00661  298 PHE A CD1 
2322 C CD2 . PHE A 298 ? 0.10696 0.08502 0.06681 0.00389  0.00493  0.00415  298 PHE A CD2 
2323 C CE1 . PHE A 298 ? 0.11376 0.09187 0.06450 0.00173  0.00655  0.00454  298 PHE A CE1 
2324 C CE2 . PHE A 298 ? 0.10539 0.08438 0.06369 0.00386  0.00556  0.00257  298 PHE A CE2 
2325 C CZ  . PHE A 298 ? 0.13789 0.11683 0.09183 0.00284  0.00637  0.00251  298 PHE A CZ  
2326 N N   . TYR A 299 ? 0.14326 0.11503 0.10830 0.00129  0.00482  0.01083  299 TYR A N   
2327 C CA  . TYR A 299 ? 0.13416 0.10322 0.10189 0.00098  0.00381  0.01239  299 TYR A CA  
2328 C C   . TYR A 299 ? 0.11974 0.08718 0.08510 -0.00098 0.00471  0.01546  299 TYR A C   
2329 O O   . TYR A 299 ? 0.14677 0.11119 0.11227 -0.00126 0.00320  0.01807  299 TYR A O   
2330 C CB  . TYR A 299 ? 0.11114 0.08076 0.08368 0.00114  0.00429  0.01032  299 TYR A CB  
2331 C CG  . TYR A 299 ? 0.14617 0.11557 0.12168 0.00282  0.00266  0.00840  299 TYR A CG  
2332 C CD1 . TYR A 299 ? 0.15047 0.12233 0.12568 0.00403  0.00256  0.00631  299 TYR A CD1 
2333 C CD2 . TYR A 299 ? 0.13265 0.09938 0.11150 0.00313  0.00140  0.00859  299 TYR A CD2 
2334 C CE1 . TYR A 299 ? 0.10292 0.07506 0.08062 0.00536  0.00149  0.00452  299 TYR A CE1 
2335 C CE2 . TYR A 299 ? 0.11998 0.08690 0.10167 0.00469  0.00031  0.00634  299 TYR A CE2 
2336 C CZ  . TYR A 299 ? 0.10475 0.07463 0.08561 0.00573  0.00049  0.00434  299 TYR A CZ  
2337 O OH  . TYR A 299 ? 0.11301 0.08355 0.09645 0.00706  -0.00018 0.00208  299 TYR A OH  
2338 N N   . THR A 300 ? 0.13113 0.10063 0.09448 -0.00235 0.00724  0.01530  300 THR A N   
2339 C CA  . THR A 300 ? 0.13213 0.10074 0.09299 -0.00457 0.00873  0.01816  300 THR A CA  
2340 C C   . THR A 300 ? 0.13948 0.10687 0.09432 -0.00503 0.00763  0.02085  300 THR A C   
2341 O O   . THR A 300 ? 0.15685 0.12162 0.11027 -0.00627 0.00687  0.02442  300 THR A O   
2342 C CB  . THR A 300 ? 0.16814 0.14003 0.12882 -0.00577 0.01204  0.01676  300 THR A CB  
2343 O OG1 . THR A 300 ? 0.17717 0.15035 0.14371 -0.00542 0.01255  0.01462  300 THR A OG1 
2344 C CG2 . THR A 300 ? 0.15635 0.12788 0.11440 -0.00833 0.01409  0.01967  300 THR A CG2 
2345 N N   . VAL A 301 ? 0.17177 0.14096 0.12306 -0.00416 0.00729  0.01931  301 VAL A N   
2346 C CA  . VAL A 301 ? 0.16718 0.13576 0.11222 -0.00478 0.00604  0.02155  301 VAL A CA  
2347 C C   . VAL A 301 ? 0.13722 0.10303 0.08350 -0.00358 0.00227  0.02372  301 VAL A C   
2348 O O   . VAL A 301 ? 0.14345 0.10716 0.08667 -0.00456 0.00080  0.02751  301 VAL A O   
2349 C CB  . VAL A 301 ? 0.13461 0.10590 0.07603 -0.00431 0.00666  0.01875  301 VAL A CB  
2350 C CG1 . VAL A 301 ? 0.16535 0.13635 0.09972 -0.00526 0.00519  0.02081  301 VAL A CG1 
2351 C CG2 . VAL A 301 ? 0.17762 0.15158 0.11902 -0.00517 0.01042  0.01636  301 VAL A CG2 
2352 N N   . GLY A 302 ? 0.15786 0.12374 0.10886 -0.00146 0.00070  0.02146  302 GLY A N   
2353 C CA  . GLY A 302 ? 0.13297 0.09688 0.08596 -0.00000 -0.00271 0.02289  302 GLY A CA  
2354 C C   . GLY A 302 ? 0.17034 0.13057 0.12650 -0.00027 -0.00386 0.02591  302 GLY A C   
2355 O O   . GLY A 302 ? 0.18600 0.14404 0.14182 0.00015  -0.00665 0.02892  302 GLY A O   
2356 N N   . SER A 303 ? 0.18961 0.14903 0.14932 -0.00100 -0.00195 0.02520  303 SER A N   
2357 C CA  . SER A 303 ? 0.21059 0.16609 0.17417 -0.00137 -0.00297 0.02768  303 SER A CA  
2358 C C   . SER A 303 ? 0.23477 0.18809 0.19403 -0.00358 -0.00301 0.03260  303 SER A C   
2359 O O   . SER A 303 ? 0.29251 0.24186 0.25444 -0.00379 -0.00470 0.03572  303 SER A O   
2360 C CB  . SER A 303 ? 0.24001 0.19549 0.20860 -0.00184 -0.00102 0.02527  303 SER A CB  
2361 O OG  . SER A 303 ? 0.22987 0.18714 0.19608 -0.00404 0.00194  0.02551  303 SER A OG  
2362 N N   . THR A 304 ? 0.20420 0.15993 0.15687 -0.00529 -0.00114 0.03336  304 THR A N   
2363 C CA  . THR A 304 ? 0.24799 0.20227 0.19524 -0.00772 -0.00085 0.03811  304 THR A CA  
2364 C C   . THR A 304 ? 0.20300 0.15803 0.14347 -0.00762 -0.00307 0.04013  304 THR A C   
2365 O O   . THR A 304 ? 0.27771 0.23222 0.21199 -0.00981 -0.00283 0.04400  304 THR A O   
2366 C CB  . THR A 304 ? 0.22238 0.17914 0.16687 -0.01023 0.00339  0.03760  304 THR A CB  
2367 O OG1 . THR A 304 ? 0.22149 0.18247 0.16275 -0.00975 0.00516  0.03385  304 THR A OG1 
2368 C CG2 . THR A 304 ? 0.21651 0.17268 0.16795 -0.01066 0.00521  0.03601  304 THR A CG2 
2369 N N   . THR A 305 ? 0.20512 0.16155 0.14648 -0.00535 -0.00524 0.03763  305 THR A N   
2370 C CA  . THR A 305 ? 0.25968 0.21727 0.19516 -0.00524 -0.00771 0.03900  305 THR A CA  
2371 C C   . THR A 305 ? 0.29034 0.24567 0.22995 -0.00310 -0.01221 0.04087  305 THR A C   
2372 O O   . THR A 305 ? 0.22026 0.17591 0.16640 -0.00076 -0.01301 0.03777  305 THR A O   
2373 C CB  . THR A 305 ? 0.24449 0.20611 0.17767 -0.00463 -0.00647 0.03436  305 THR A CB  
2374 O OG1 . THR A 305 ? 0.20799 0.17168 0.13874 -0.00627 -0.00220 0.03234  305 THR A OG1 
2375 C CG2 . THR A 305 ? 0.18006 0.14304 0.10669 -0.00499 -0.00897 0.03552  305 THR A CG2 
2376 N N   . PRO A 306 ? 0.29723 0.25048 0.23351 -0.00378 -0.01520 0.04590  306 PRO A N   
2377 C CA  . PRO A 306 ? 0.28348 0.23480 0.22463 -0.00147 -0.01975 0.04775  306 PRO A CA  
2378 C C   . PRO A 306 ? 0.26137 0.21621 0.20219 0.00019  -0.02181 0.04483  306 PRO A C   
2379 O O   . PRO A 306 ? 0.29329 0.25120 0.22729 -0.00105 -0.02113 0.04356  306 PRO A O   
2380 C CB  . PRO A 306 ? 0.30764 0.25616 0.24399 -0.00309 -0.02235 0.05442  306 PRO A CB  
2381 C CG  . PRO A 306 ? 0.33006 0.28085 0.25644 -0.00620 -0.01954 0.05513  306 PRO A CG  
2382 C CD  . PRO A 306 ? 0.26216 0.21479 0.19030 -0.00675 -0.01454 0.05037  306 PRO A CD  
2383 N N   . ASN A 307 ? 0.20050 0.15493 0.14917 0.00294  -0.02420 0.04351  307 ASN A N   
2384 C CA  . ASN A 307 ? 0.22957 0.18734 0.17968 0.00461  -0.02641 0.04097  307 ASN A CA  
2385 C C   . ASN A 307 ? 0.26627 0.22774 0.21420 0.00414  -0.02319 0.03583  307 ASN A C   
2386 O O   . ASN A 307 ? 0.22403 0.18851 0.16861 0.00394  -0.02425 0.03434  307 ASN A O   
2387 C CB  . ASN A 307 ? 0.34111 0.29958 0.28581 0.00399  -0.03052 0.04478  307 ASN A CB  
2388 C CG  . ASN A 307 ? 0.23180 0.18647 0.17947 0.00475  -0.03430 0.05032  307 ASN A CG  
2389 O OD1 . ASN A 307 ? 0.31769 0.27075 0.25891 0.00287  -0.03582 0.05528  307 ASN A OD1 
2390 N ND2 . ASN A 307 ? 0.29911 0.25226 0.25669 0.00748  -0.03575 0.04952  307 ASN A ND2 
2391 N N   . PHE A 308 ? 0.26321 0.22436 0.21357 0.00399  -0.01945 0.03311  308 PHE A N   
2392 C CA  . PHE A 308 ? 0.25070 0.21487 0.19911 0.00345  -0.01629 0.02881  308 PHE A CA  
2393 C C   . PHE A 308 ? 0.22050 0.18742 0.17294 0.00523  -0.01722 0.02528  308 PHE A C   
2394 O O   . PHE A 308 ? 0.20596 0.17546 0.15562 0.00465  -0.01592 0.02254  308 PHE A O   
2395 C CB  . PHE A 308 ? 0.21752 0.18080 0.16843 0.00300  -0.01265 0.02714  308 PHE A CB  
2396 C CG  . PHE A 308 ? 0.14817 0.11420 0.09699 0.00233  -0.00944 0.02346  308 PHE A CG  
2397 C CD1 . PHE A 308 ? 0.15449 0.12168 0.09659 0.00037  -0.00762 0.02367  308 PHE A CD1 
2398 C CD2 . PHE A 308 ? 0.14243 0.10993 0.09606 0.00365  -0.00822 0.01982  308 PHE A CD2 
2399 C CE1 . PHE A 308 ? 0.17924 0.14874 0.12038 0.00001  -0.00474 0.02020  308 PHE A CE1 
2400 C CE2 . PHE A 308 ? 0.17266 0.14237 0.12488 0.00315  -0.00559 0.01688  308 PHE A CE2 
2401 C CZ  . PHE A 308 ? 0.20014 0.17074 0.14655 0.00145  -0.00389 0.01700  308 PHE A CZ  
2402 N N   A HIS A 309 ? 0.25431 0.22075 0.21365 0.00731  -0.01929 0.02521  309 HIS A N   
2403 N N   B HIS A 309 ? 0.25397 0.22040 0.21329 0.00731  -0.01931 0.02523  309 HIS A N   
2404 C CA  A HIS A 309 ? 0.26534 0.23469 0.22919 0.00888  -0.01991 0.02202  309 HIS A CA  
2405 C CA  B HIS A 309 ? 0.26442 0.23377 0.22825 0.00887  -0.01990 0.02202  309 HIS A CA  
2406 C C   A HIS A 309 ? 0.25364 0.22493 0.21649 0.00917  -0.02353 0.02310  309 HIS A C   
2407 C C   B HIS A 309 ? 0.25356 0.22488 0.21632 0.00915  -0.02349 0.02307  309 HIS A C   
2408 O O   A HIS A 309 ? 0.24857 0.22257 0.21563 0.01031  -0.02424 0.02070  309 HIS A O   
2409 O O   B HIS A 309 ? 0.24850 0.22259 0.21525 0.01021  -0.02413 0.02060  309 HIS A O   
2410 C CB  A HIS A 309 ? 0.26975 0.23832 0.24194 0.01098  -0.01997 0.02081  309 HIS A CB  
2411 C CB  B HIS A 309 ? 0.26894 0.23751 0.24113 0.01097  -0.01995 0.02079  309 HIS A CB  
2412 C CG  A HIS A 309 ? 0.24597 0.21185 0.22179 0.01215  -0.02302 0.02410  309 HIS A CG  
2413 C CG  B HIS A 309 ? 0.24670 0.21797 0.22231 0.01170  -0.01770 0.01656  309 HIS A CG  
2414 N ND1 A HIS A 309 ? 0.25864 0.22065 0.23242 0.01120  -0.02326 0.02763  309 HIS A ND1 
2415 N ND1 B HIS A 309 ? 0.24333 0.21659 0.21513 0.01048  -0.01540 0.01437  309 HIS A ND1 
2416 C CD2 A HIS A 309 ? 0.28455 0.25098 0.26649 0.01421  -0.02597 0.02456  309 HIS A CD2 
2417 C CD2 B HIS A 309 ? 0.24925 0.22157 0.23155 0.01342  -0.01734 0.01423  309 HIS A CD2 
2418 C CE1 A HIS A 309 ? 0.30013 0.25997 0.27848 0.01266  -0.02642 0.03032  309 HIS A CE1 
2419 C CE1 B HIS A 309 ? 0.24738 0.22266 0.22315 0.01132  -0.01392 0.01136  309 HIS A CE1 
2420 N NE2 A HIS A 309 ? 0.29324 0.25586 0.27685 0.01466  -0.02817 0.02839  309 HIS A NE2 
2421 N NE2 B HIS A 309 ? 0.23387 0.20885 0.21579 0.01303  -0.01491 0.01109  309 HIS A NE2 
2422 N N   . ARG A 310 ? 0.25678 0.22698 0.21425 0.00805  -0.02588 0.02673  310 ARG A N   
2423 C CA  . ARG A 310 ? 0.25038 0.22257 0.20642 0.00813  -0.02988 0.02805  310 ARG A CA  
2424 C C   . ARG A 310 ? 0.29671 0.26995 0.24303 0.00564  -0.02965 0.02835  310 ARG A C   
2425 O O   . ARG A 310 ? 0.28020 0.25246 0.22133 0.00400  -0.02636 0.02795  310 ARG A O   
2426 C CB  . ARG A 310 ? 0.28049 0.25054 0.23948 0.00931  -0.03395 0.03257  310 ARG A CB  
2427 C CG  . ARG A 310 ? 0.33149 0.30053 0.30081 0.01199  -0.03425 0.03178  310 ARG A CG  
2428 C CD  . ARG A 310 ? 0.32372 0.29062 0.29699 0.01344  -0.03867 0.03618  310 ARG A CD  
2429 N NE  . ARG A 310 ? 0.31864 0.28067 0.29228 0.01324  -0.03793 0.03923  310 ARG A NE  
2430 C CZ  . ARG A 310 ? 0.32286 0.28177 0.30106 0.01461  -0.04120 0.04317  310 ARG A CZ  
2431 N NH1 . ARG A 310 ? 0.32560 0.28598 0.30859 0.01649  -0.04562 0.04469  310 ARG A NH1 
2432 N NH2 . ARG A 310 ? 0.32416 0.27835 0.30273 0.01409  -0.04013 0.04571  310 ARG A NH2 
2433 N N   . MET A 311 ? 0.27134 0.24691 0.21553 0.00534  -0.03316 0.02875  311 MET A N   
2434 C CA  . MET A 311 ? 0.27468 0.25146 0.20930 0.00291  -0.03343 0.02877  311 MET A CA  
2435 C C   . MET A 311 ? 0.29484 0.26987 0.22315 0.00170  -0.03615 0.03407  311 MET A C   
2436 O O   . MET A 311 ? 0.28021 0.25434 0.20045 -0.00049 -0.03400 0.03509  311 MET A O   
2437 C CB  . MET A 311 ? 0.27685 0.25726 0.21192 0.00282  -0.03589 0.02607  311 MET A CB  
2438 C CG  . MET A 311 ? 0.29381 0.27567 0.21950 0.00026  -0.03532 0.02431  311 MET A CG  
2439 S SD  . MET A 311 ? 0.28436 0.27011 0.20989 -0.00022 -0.03995 0.02252  311 MET A SD  
2440 C CE  . MET A 311 ? 0.40324 0.38876 0.32853 0.00044  -0.04611 0.02864  311 MET A CE  
2441 N N   . ALA A 312 ? 0.30299 0.27761 0.23517 0.00310  -0.04083 0.03762  312 ALA A N   
2442 C CA  . ALA A 312 ? 0.25577 0.22851 0.18246 0.00206  -0.04407 0.04344  312 ALA A CA  
2443 C C   . ALA A 312 ? 0.33708 0.30554 0.26398 0.00179  -0.04155 0.04654  312 ALA A C   
2444 O O   . ALA A 312 ? 0.32852 0.29517 0.26329 0.00352  -0.03946 0.04519  312 ALA A O   
2445 C CB  . ALA A 312 ? 0.34746 0.32085 0.27990 0.00401  -0.05003 0.04646  312 ALA A CB  
2446 N N   . GLY A 313 ? 0.39549 0.36246 0.31351 -0.00061 -0.04170 0.05067  313 GLY A N   
2447 C CA  . GLY A 313 ? 0.36253 0.32559 0.28011 -0.00146 -0.03909 0.05381  313 GLY A CA  
2448 C C   . GLY A 313 ? 0.35444 0.31750 0.27183 -0.00235 -0.03299 0.04980  313 GLY A C   
2449 O O   . GLY A 313 ? 0.33676 0.29686 0.25451 -0.00320 -0.03057 0.05200  313 GLY A O   
2450 N N   . ASN A 314 ? 0.34176 0.30800 0.25907 -0.00220 -0.03061 0.04415  314 ASN A N   
2451 C CA  . ASN A 314 ? 0.29298 0.25958 0.21030 -0.00292 -0.02514 0.04033  314 ASN A CA  
2452 C C   . ASN A 314 ? 0.29319 0.26136 0.20019 -0.00586 -0.02254 0.04001  314 ASN A C   
2453 O O   . ASN A 314 ? 0.26399 0.23493 0.16585 -0.00662 -0.02349 0.03780  314 ASN A O   
2454 C CB  . ASN A 314 ? 0.23601 0.20494 0.15901 -0.00120 -0.02395 0.03472  314 ASN A CB  
2455 C CG  . ASN A 314 ? 0.22988 0.19880 0.15504 -0.00136 -0.01894 0.03130  314 ASN A CG  
2456 O OD1 . ASN A 314 ? 0.24403 0.21207 0.16540 -0.00307 -0.01597 0.03230  314 ASN A OD1 
2457 N ND2 . ASN A 314 ? 0.20940 0.17956 0.14080 0.00034  -0.01805 0.02738  314 ASN A ND2 
2458 N N   . PRO A 315 ? 0.22311 0.18980 0.12706 -0.00766 -0.01916 0.04187  315 PRO A N   
2459 C CA  . PRO A 315 ? 0.30972 0.27837 0.20382 -0.01054 -0.01628 0.04140  315 PRO A CA  
2460 C C   . PRO A 315 ? 0.26594 0.23744 0.15976 -0.01062 -0.01230 0.03512  315 PRO A C   
2461 O O   . PRO A 315 ? 0.35885 0.33262 0.24471 -0.01258 -0.01067 0.03347  315 PRO A O   
2462 C CB  . PRO A 315 ? 0.22801 0.19427 0.12097 -0.01229 -0.01366 0.04537  315 PRO A CB  
2463 C CG  . PRO A 315 ? 0.27138 0.23497 0.17488 -0.01014 -0.01354 0.04525  315 PRO A CG  
2464 C CD  . PRO A 315 ? 0.33436 0.29757 0.24356 -0.00738 -0.01810 0.04483  315 PRO A CD  
2465 N N   . VAL A 316 ? 0.25023 0.22169 0.15233 -0.00861 -0.01068 0.03154  316 VAL A N   
2466 C CA  . VAL A 316 ? 0.25383 0.22768 0.15618 -0.00856 -0.00723 0.02598  316 VAL A CA  
2467 C C   . VAL A 316 ? 0.22840 0.20393 0.13228 -0.00728 -0.00955 0.02247  316 VAL A C   
2468 O O   . VAL A 316 ? 0.25543 0.23275 0.15858 -0.00747 -0.00720 0.01800  316 VAL A O   
2469 C CB  . VAL A 316 ? 0.25347 0.22673 0.16331 -0.00742 -0.00392 0.02397  316 VAL A CB  
2470 C CG1 . VAL A 316 ? 0.31383 0.28553 0.22319 -0.00885 -0.00162 0.02725  316 VAL A CG1 
2471 C CG2 . VAL A 316 ? 0.28065 0.25283 0.19898 -0.00484 -0.00625 0.02336  316 VAL A CG2 
2472 N N   . CYS A 317 ? 0.23993 0.21498 0.14645 -0.00602 -0.01405 0.02431  317 CYS A N   
2473 C CA  . CYS A 317 ? 0.23723 0.21409 0.14646 -0.00488 -0.01627 0.02110  317 CYS A CA  
2474 C C   . CYS A 317 ? 0.21691 0.19553 0.11842 -0.00648 -0.01908 0.02126  317 CYS A C   
2475 O O   . CYS A 317 ? 0.27049 0.24857 0.16752 -0.00733 -0.02209 0.02555  317 CYS A O   
2476 C CB  . CYS A 317 ? 0.23445 0.21053 0.15208 -0.00252 -0.01936 0.02241  317 CYS A CB  
2477 S SG  . CYS A 317 ? 0.21006 0.18881 0.13177 -0.00139 -0.02207 0.01888  317 CYS A SG  
2478 N N   . LYS A 318 ? 0.23684 0.21746 0.13687 -0.00696 -0.01829 0.01661  318 LYS A N   
2479 C CA  . LYS A 318 ? 0.28872 0.27129 0.18160 -0.00861 -0.02103 0.01580  318 LYS A CA  
2480 C C   . LYS A 318 ? 0.28535 0.26880 0.18194 -0.00749 -0.02661 0.01744  318 LYS A C   
2481 O O   . LYS A 318 ? 0.28426 0.26777 0.18967 -0.00548 -0.02737 0.01635  318 LYS A O   
2482 C CB  . LYS A 318 ? 0.33366 0.31775 0.22496 -0.00941 -0.01847 0.00984  318 LYS A CB  
2483 C CG  . LYS A 318 ? 0.40669 0.39280 0.28956 -0.01152 -0.02081 0.00828  318 LYS A CG  
2484 C CD  . LYS A 318 ? 0.33518 0.32237 0.21846 -0.01200 -0.01890 0.00198  318 LYS A CD  
2485 C CE  . LYS A 318 ? 0.44117 0.43022 0.31432 -0.01457 -0.02004 -0.00004 318 LYS A CE  
2486 N NZ  . LYS A 318 ? 0.47879 0.46788 0.34284 -0.01637 -0.01778 0.00247  318 LYS A NZ  
2487 N N   . GLN A 319 ? 0.27005 0.25453 0.15984 -0.00889 -0.03051 0.02008  319 GLN A N   
2488 C CA  . GLN A 319 ? 0.28324 0.26897 0.17634 -0.00793 -0.03637 0.02222  319 GLN A CA  
2489 C C   . GLN A 319 ? 0.27087 0.25950 0.16337 -0.00872 -0.03817 0.01759  319 GLN A C   
2490 O O   . GLN A 319 ? 0.29242 0.28266 0.17612 -0.01099 -0.03949 0.01655  319 GLN A O   
2491 C CB  . GLN A 319 ? 0.37137 0.35670 0.25765 -0.00906 -0.04018 0.02800  319 GLN A CB  
2492 C CG  . GLN A 319 ? 0.33511 0.31730 0.21991 -0.00918 -0.03776 0.03245  319 GLN A CG  
2493 C CD  . GLN A 319 ? 0.33838 0.31820 0.23414 -0.00638 -0.03776 0.03428  319 GLN A CD  
2494 O OE1 . GLN A 319 ? 0.33012 0.31032 0.23258 -0.00446 -0.04188 0.03575  319 GLN A OE1 
2495 N NE2 . GLN A 319 ? 0.35592 0.33354 0.25388 -0.00614 -0.03309 0.03392  319 GLN A NE2 
2496 N N   . ILE A 320 ? 0.31667 0.30607 0.21853 -0.00703 -0.03826 0.01480  320 ILE A N   
2497 C CA  . ILE A 320 ? 0.22975 0.22168 0.13319 -0.00770 -0.03986 0.01038  320 ILE A CA  
2498 C C   . ILE A 320 ? 0.30234 0.29631 0.21310 -0.00629 -0.04502 0.01222  320 ILE A C   
2499 O O   . ILE A 320 ? 0.26856 0.26169 0.18688 -0.00404 -0.04536 0.01487  320 ILE A O   
2500 C CB  . ILE A 320 ? 0.26322 0.25443 0.17186 -0.00717 -0.03520 0.00563  320 ILE A CB  
2501 C CG1 . ILE A 320 ? 0.30432 0.29412 0.20595 -0.00863 -0.03047 0.00322  320 ILE A CG1 
2502 C CG2 . ILE A 320 ? 0.29803 0.29143 0.21100 -0.00757 -0.03705 0.00169  320 ILE A CG2 
2503 C CD1 . ILE A 320 ? 0.27832 0.26686 0.18545 -0.00773 -0.02584 -0.00028 320 ILE A CD1 
2504 N N   . ASP A 321 ? 0.33912 0.33599 0.24813 -0.00760 -0.04904 0.01056  321 ASP A N   
2505 C CA  . ASP A 321 ? 0.41145 0.41088 0.32765 -0.00628 -0.05447 0.01276  321 ASP A CA  
2506 C C   . ASP A 321 ? 0.32929 0.33027 0.25645 -0.00506 -0.05341 0.00931  321 ASP A C   
2507 O O   . ASP A 321 ? 0.41833 0.42253 0.34869 -0.00567 -0.05702 0.00771  321 ASP A O   
2508 C CB  . ASP A 321 ? 0.47953 0.48189 0.38917 -0.00835 -0.05995 0.01302  321 ASP A CB  
2509 C CG  . ASP A 321 ? 0.56827 0.56961 0.46529 -0.01021 -0.06101 0.01622  321 ASP A CG  
2510 O OD1 . ASP A 321 ? 0.49892 0.49786 0.39507 -0.00914 -0.06054 0.02111  321 ASP A OD1 
2511 O OD2 . ASP A 321 ? 0.52731 0.53024 0.41529 -0.01287 -0.06218 0.01377  321 ASP A OD2 
2512 N N   . TRP A 322 ? 0.23120 0.23025 0.16434 -0.00334 -0.04918 0.00893  322 TRP A N   
2513 C CA  . TRP A 322 ? 0.28676 0.28726 0.22977 -0.00236 -0.04764 0.00599  322 TRP A CA  
2514 C C   . TRP A 322 ? 0.24861 0.25310 0.19913 -0.00177 -0.05246 0.00641  322 TRP A C   
2515 O O   . TRP A 322 ? 0.29505 0.30062 0.24652 -0.00077 -0.05664 0.01010  322 TRP A O   
2516 C CB  . TRP A 322 ? 0.25298 0.25121 0.20132 -0.00024 -0.04355 0.00696  322 TRP A CB  
2517 C CG  . TRP A 322 ? 0.20224 0.19707 0.14456 -0.00080 -0.03887 0.00638  322 TRP A CG  
2518 C CD1 . TRP A 322 ? 0.22085 0.21306 0.15920 -0.00032 -0.03762 0.00946  322 TRP A CD1 
2519 C CD2 . TRP A 322 ? 0.21377 0.20757 0.15439 -0.00189 -0.03480 0.00249  322 TRP A CD2 
2520 N NE1 . TRP A 322 ? 0.21356 0.20367 0.14794 -0.00108 -0.03303 0.00762  322 TRP A NE1 
2521 C CE2 . TRP A 322 ? 0.17538 0.16636 0.11114 -0.00189 -0.03130 0.00338  322 TRP A CE2 
2522 C CE3 . TRP A 322 ? 0.20814 0.20301 0.15138 -0.00287 -0.03387 -0.00150 322 TRP A CE3 
2523 C CZ2 . TRP A 322 ? 0.19531 0.18483 0.12912 -0.00260 -0.02705 0.00034  322 TRP A CZ2 
2524 C CZ3 . TRP A 322 ? 0.21365 0.20652 0.15474 -0.00357 -0.02972 -0.00433 322 TRP A CZ3 
2525 C CH2 . TRP A 322 ? 0.17727 0.16764 0.11386 -0.00331 -0.02640 -0.00345 322 TRP A CH2 
2526 N N   . ASP A 323 ? 0.24277 0.24939 0.19924 -0.00234 -0.05173 0.00284  323 ASP A N   
2527 C CA  . ASP A 323 ? 0.25320 0.26417 0.21812 -0.00192 -0.05575 0.00277  323 ASP A CA  
2528 C C   . ASP A 323 ? 0.27055 0.28243 0.24544 0.00095  -0.05511 0.00487  323 ASP A C   
2529 O O   . ASP A 323 ? 0.32396 0.33352 0.30086 0.00218  -0.05062 0.00473  323 ASP A O   
2530 C CB  . ASP A 323 ? 0.28555 0.29844 0.25405 -0.00376 -0.05482 -0.00172 323 ASP A CB  
2531 C CG  . ASP A 323 ? 0.30015 0.31289 0.26018 -0.00664 -0.05649 -0.00441 323 ASP A CG  
2532 O OD1 . ASP A 323 ? 0.35578 0.36765 0.30691 -0.00727 -0.05871 -0.00263 323 ASP A OD1 
2533 O OD2 . ASP A 323 ? 0.23599 0.24940 0.19818 -0.00838 -0.05550 -0.00834 323 ASP A OD2 
2534 N N   . ASP A 324 ? 0.30858 0.32414 0.28994 0.00199  -0.05977 0.00659  324 ASP A N   
2535 C CA  . ASP A 324 ? 0.32887 0.34622 0.32100 0.00477  -0.05974 0.00804  324 ASP A CA  
2536 C C   . ASP A 324 ? 0.29777 0.31987 0.29949 0.00429  -0.05975 0.00502  324 ASP A C   
2537 O O   . ASP A 324 ? 0.34824 0.37478 0.35604 0.00448  -0.06428 0.00546  324 ASP A O   
2538 C CB  . ASP A 324 ? 0.34235 0.36047 0.33588 0.00654  -0.06510 0.01243  324 ASP A CB  
2539 C CG  . ASP A 324 ? 0.38302 0.40255 0.38809 0.00975  -0.06486 0.01370  324 ASP A CG  
2540 O OD1 . ASP A 324 ? 0.46123 0.48028 0.47104 0.01063  -0.05998 0.01160  324 ASP A OD1 
2541 O OD2 . ASP A 324 ? 0.50567 0.52689 0.51513 0.01141  -0.06971 0.01677  324 ASP A OD2 
2542 N N   . ASN A 325 ? 0.34518 0.36645 0.34841 0.00353  -0.05469 0.00211  325 ASN A N   
2543 C CA  . ASN A 325 ? 0.29455 0.31982 0.30612 0.00256  -0.05378 -0.00070 325 ASN A CA  
2544 C C   . ASN A 325 ? 0.20735 0.23353 0.22710 0.00455  -0.04969 -0.00085 325 ASN A C   
2545 O O   . ASN A 325 ? 0.20901 0.23256 0.22674 0.00423  -0.04477 -0.00205 325 ASN A O   
2546 C CB  . ASN A 325 ? 0.28610 0.30965 0.29265 -0.00034 -0.05142 -0.00389 325 ASN A CB  
2547 C CG  . ASN A 325 ? 0.24970 0.27757 0.26371 -0.00220 -0.05240 -0.00649 325 ASN A CG  
2548 O OD1 . ASN A 325 ? 0.34547 0.37328 0.35596 -0.00477 -0.05398 -0.00871 325 ASN A OD1 
2549 N ND2 . ASN A 325 ? 0.27278 0.30451 0.29730 -0.00105 -0.05132 -0.00643 325 ASN A ND2 
2550 N N   . PRO A 326 ? 0.19773 0.22779 0.22691 0.00665  -0.05154 0.00021  326 PRO A N   
2551 C CA  . PRO A 326 ? 0.23913 0.27041 0.27587 0.00847  -0.04732 -0.00046 326 PRO A CA  
2552 C C   . PRO A 326 ? 0.25632 0.29001 0.29721 0.00661  -0.04356 -0.00329 326 PRO A C   
2553 O O   . PRO A 326 ? 0.20790 0.24106 0.25076 0.00727  -0.03883 -0.00405 326 PRO A O   
2554 C CB  . PRO A 326 ? 0.29494 0.33055 0.34163 0.01094  -0.05083 0.00087  326 PRO A CB  
2555 C CG  . PRO A 326 ? 0.31228 0.34730 0.35455 0.01087  -0.05691 0.00337  326 PRO A CG  
2556 C CD  . PRO A 326 ? 0.21877 0.25246 0.25236 0.00754  -0.05758 0.00199  326 PRO A CD  
2557 N N   . GLU A 327 ? 0.19735 0.23368 0.23953 0.00413  -0.04563 -0.00478 327 GLU A N   
2558 C CA  . GLU A 327 ? 0.22220 0.26065 0.26876 0.00206  -0.04221 -0.00710 327 GLU A CA  
2559 C C   . GLU A 327 ? 0.21033 0.24353 0.24888 0.00064  -0.03798 -0.00787 327 GLU A C   
2560 O O   . GLU A 327 ? 0.21743 0.25069 0.25839 0.00039  -0.03346 -0.00851 327 GLU A O   
2561 C CB  . GLU A 327 ? 0.25612 0.29849 0.30658 -0.00041 -0.04587 -0.00856 327 GLU A CB  
2562 C CG  . GLU A 327 ? 0.28242 0.33101 0.34261 0.00087  -0.05014 -0.00794 327 GLU A CG  
2563 C CD  . GLU A 327 ? 0.39278 0.44043 0.44872 0.00232  -0.05578 -0.00570 327 GLU A CD  
2564 O OE1 . GLU A 327 ? 0.34551 0.38842 0.39050 0.00138  -0.05687 -0.00517 327 GLU A OE1 
2565 O OE2 . GLU A 327 ? 0.39528 0.44707 0.45901 0.00438  -0.05910 -0.00437 327 GLU A OE2 
2566 N N   . PHE A 328 ? 0.24221 0.27103 0.27120 -0.00027 -0.03938 -0.00776 328 PHE A N   
2567 C CA  . PHE A 328 ? 0.17223 0.19607 0.19415 -0.00127 -0.03554 -0.00847 328 PHE A CA  
2568 C C   . PHE A 328 ? 0.17031 0.19171 0.19067 0.00089  -0.03185 -0.00710 328 PHE A C   
2569 O O   . PHE A 328 ? 0.23031 0.24967 0.24934 0.00037  -0.02779 -0.00764 328 PHE A O   
2570 C CB  . PHE A 328 ? 0.22949 0.24962 0.24182 -0.00243 -0.03767 -0.00887 328 PHE A CB  
2571 C CG  . PHE A 328 ? 0.25466 0.27580 0.26691 -0.00527 -0.03985 -0.01132 328 PHE A CG  
2572 C CD1 . PHE A 328 ? 0.21274 0.23716 0.23304 -0.00685 -0.03930 -0.01282 328 PHE A CD1 
2573 C CD2 . PHE A 328 ? 0.23729 0.25613 0.24139 -0.00655 -0.04228 -0.01229 328 PHE A CD2 
2574 C CE1 . PHE A 328 ? 0.19356 0.21865 0.21426 -0.00964 -0.04140 -0.01528 328 PHE A CE1 
2575 C CE2 . PHE A 328 ? 0.20593 0.22558 0.20993 -0.00925 -0.04433 -0.01508 328 PHE A CE2 
2576 C CZ  . PHE A 328 ? 0.22099 0.24360 0.23354 -0.01080 -0.04401 -0.01660 328 PHE A CZ  
2577 N N   . LEU A 329 ? 0.21217 0.23367 0.23286 0.00328  -0.03341 -0.00525 329 LEU A N   
2578 C CA  . LEU A 329 ? 0.19326 0.21239 0.21276 0.00524  -0.03018 -0.00425 329 LEU A CA  
2579 C C   . LEU A 329 ? 0.18950 0.21188 0.21671 0.00588  -0.02684 -0.00516 329 LEU A C   
2580 O O   . LEU A 329 ? 0.13555 0.15604 0.16085 0.00610  -0.02289 -0.00540 329 LEU A O   
2581 C CB  . LEU A 329 ? 0.21673 0.23481 0.23526 0.00749  -0.03294 -0.00202 329 LEU A CB  
2582 C CG  . LEU A 329 ? 0.21767 0.23294 0.23514 0.00951  -0.03017 -0.00106 329 LEU A CG  
2583 C CD1 . LEU A 329 ? 0.20988 0.22076 0.21936 0.00843  -0.02702 -0.00134 329 LEU A CD1 
2584 C CD2 . LEU A 329 ? 0.23945 0.25336 0.25653 0.01146  -0.03350 0.00145  329 LEU A CD2 
2585 N N   . ALA A 330 ? 0.15294 0.18059 0.18889 0.00608  -0.02835 -0.00574 330 ALA A N   
2586 C CA  . ALA A 330 ? 0.14155 0.17305 0.18504 0.00653  -0.02489 -0.00681 330 ALA A CA  
2587 C C   . ALA A 330 ? 0.12568 0.15695 0.16795 0.00402  -0.02120 -0.00786 330 ALA A C   
2588 O O   . ALA A 330 ? 0.12892 0.16040 0.17174 0.00424  -0.01710 -0.00816 330 ALA A O   
2589 C CB  . ALA A 330 ? 0.16215 0.19986 0.21594 0.00714  -0.02734 -0.00732 330 ALA A CB  
2590 N N   . ALA A 331 ? 0.13475 0.16544 0.17524 0.00155  -0.02273 -0.00840 331 ALA A N   
2591 C CA  . ALA A 331 ? 0.10341 0.13327 0.14319 -0.00090 -0.01954 -0.00907 331 ALA A CA  
2592 C C   . ALA A 331 ? 0.11528 0.13981 0.14718 -0.00067 -0.01664 -0.00842 331 ALA A C   
2593 O O   . ALA A 331 ? 0.09403 0.11838 0.12618 -0.00152 -0.01298 -0.00827 331 ALA A O   
2594 C CB  . ALA A 331 ? 0.09932 0.12906 0.13908 -0.00353 -0.02213 -0.01010 331 ALA A CB  
2595 N N   . TRP A 332 ? 0.09716 0.11759 0.12214 0.00039  -0.01828 -0.00785 332 TRP A N   
2596 C CA  . TRP A 332 ? 0.11051 0.12629 0.12868 0.00081  -0.01574 -0.00725 332 TRP A CA  
2597 C C   . TRP A 332 ? 0.13037 0.14684 0.14970 0.00268  -0.01305 -0.00662 332 TRP A C   
2598 O O   . TRP A 332 ? 0.19333 0.20829 0.21043 0.00233  -0.00987 -0.00639 332 TRP A O   
2599 C CB  . TRP A 332 ? 0.09903 0.11100 0.11015 0.00132  -0.01809 -0.00687 332 TRP A CB  
2600 C CG  . TRP A 332 ? 0.12443 0.13198 0.12904 0.00183  -0.01575 -0.00631 332 TRP A CG  
2601 C CD1 . TRP A 332 ? 0.14672 0.15115 0.14749 0.00054  -0.01408 -0.00687 332 TRP A CD1 
2602 C CD2 . TRP A 332 ? 0.09754 0.10336 0.09941 0.00376  -0.01503 -0.00516 332 TRP A CD2 
2603 N NE1 . TRP A 332 ? 0.16212 0.16347 0.15814 0.00160  -0.01236 -0.00610 332 TRP A NE1 
2604 C CE2 . TRP A 332 ? 0.11893 0.12106 0.11539 0.00344  -0.01289 -0.00507 332 TRP A CE2 
2605 C CE3 . TRP A 332 ? 0.13637 0.14335 0.14051 0.00575  -0.01602 -0.00425 332 TRP A CE3 
2606 C CZ2 . TRP A 332 ? 0.10066 0.10053 0.09378 0.00480  -0.01174 -0.00413 332 TRP A CZ2 
2607 C CZ3 . TRP A 332 ? 0.10015 0.10435 0.10081 0.00707  -0.01485 -0.00335 332 TRP A CZ3 
2608 C CH2 . TRP A 332 ? 0.13350 0.13434 0.12864 0.00648  -0.01273 -0.00330 332 TRP A CH2 
2609 N N   . ARG A 333 ? 0.12665 0.14541 0.14969 0.00466  -0.01444 -0.00644 333 ARG A N   
2610 C CA  . ARG A 333 ? 0.10840 0.12773 0.13295 0.00653  -0.01205 -0.00643 333 ARG A CA  
2611 C C   . ARG A 333 ? 0.13135 0.15451 0.16065 0.00573  -0.00853 -0.00736 333 ARG A C   
2612 O O   . ARG A 333 ? 0.08851 0.11103 0.11590 0.00613  -0.00543 -0.00751 333 ARG A O   
2613 C CB  . ARG A 333 ? 0.12349 0.14432 0.15218 0.00887  -0.01464 -0.00616 333 ARG A CB  
2614 C CG  . ARG A 333 ? 0.16929 0.19072 0.20065 0.01097  -0.01238 -0.00673 333 ARG A CG  
2615 C CD  . ARG A 333 ? 0.21146 0.23397 0.24802 0.01343  -0.01526 -0.00637 333 ARG A CD  
2616 N NE  . ARG A 333 ? 0.24943 0.27752 0.29489 0.01367  -0.01655 -0.00721 333 ARG A NE  
2617 C CZ  . ARG A 333 ? 0.17275 0.20230 0.22078 0.01366  -0.02082 -0.00628 333 ARG A CZ  
2618 N NH1 . ARG A 333 ? 0.21445 0.24027 0.25624 0.01337  -0.02418 -0.00446 333 ARG A NH1 
2619 N NH2 . ARG A 333 ? 0.25780 0.29305 0.31492 0.01386  -0.02175 -0.00724 333 ARG A NH2 
2620 N N   . GLU A 334 ? 0.18666 0.21402 0.22201 0.00442  -0.00895 -0.00798 334 GLU A N   
2621 C CA  . GLU A 334 ? 0.12182 0.15358 0.16227 0.00338  -0.00551 -0.00871 334 GLU A CA  
2622 C C   . GLU A 334 ? 0.15382 0.18413 0.19122 0.00063  -0.00329 -0.00804 334 GLU A C   
2623 O O   . GLU A 334 ? 0.12823 0.16221 0.16962 -0.00089 -0.00057 -0.00818 334 GLU A O   
2624 C CB  . GLU A 334 ? 0.13088 0.16850 0.18063 0.00329  -0.00694 -0.00964 334 GLU A CB  
2625 C CG  . GLU A 334 ? 0.19904 0.23852 0.25338 0.00629  -0.00900 -0.01018 334 GLU A CG  
2626 C CD  . GLU A 334 ? 0.19430 0.23967 0.25840 0.00639  -0.01117 -0.01095 334 GLU A CD  
2627 O OE1 . GLU A 334 ? 0.14706 0.19576 0.21496 0.00396  -0.01040 -0.01134 334 GLU A OE1 
2628 O OE2 . GLU A 334 ? 0.26460 0.31129 0.33307 0.00888  -0.01380 -0.01103 334 GLU A OE2 
2629 N N   . ALA A 335 ? 0.16053 0.18563 0.19128 -0.00006 -0.00433 -0.00723 335 ALA A N   
2630 C CA  . ALA A 335 ? 0.14121 0.16394 0.16908 -0.00234 -0.00252 -0.00639 335 ALA A CA  
2631 C C   . ALA A 335 ? 0.12314 0.14879 0.15670 -0.00490 -0.00259 -0.00661 335 ALA A C   
2632 O O   . ALA A 335 ? 0.15756 0.18411 0.19233 -0.00679 0.00016  -0.00573 335 ALA A O   
2633 C CB  . ALA A 335 ? 0.20495 0.22746 0.23016 -0.00227 0.00118  -0.00552 335 ALA A CB  
2634 N N   . ARG A 336 ? 0.12198 0.14917 0.15906 -0.00515 -0.00589 -0.00762 336 ARG A N   
2635 C CA  . ARG A 336 ? 0.09384 0.12358 0.13658 -0.00779 -0.00659 -0.00812 336 ARG A CA  
2636 C C   . ARG A 336 ? 0.13066 0.15723 0.17097 -0.00873 -0.01030 -0.00905 336 ARG A C   
2637 O O   . ARG A 336 ? 0.13376 0.16318 0.17877 -0.00972 -0.01312 -0.01016 336 ARG A O   
2638 C CB  . ARG A 336 ? 0.10548 0.14213 0.15706 -0.00754 -0.00685 -0.00893 336 ARG A CB  
2639 C CG  . ARG A 336 ? 0.13157 0.16991 0.18464 -0.00473 -0.00990 -0.00961 336 ARG A CG  
2640 C CD  . ARG A 336 ? 0.09186 0.13738 0.15512 -0.00450 -0.01027 -0.01053 336 ARG A CD  
2641 N NE  . ARG A 336 ? 0.16296 0.20994 0.22844 -0.00155 -0.01336 -0.01084 336 ARG A NE  
2642 C CZ  . ARG A 336 ? 0.10552 0.15297 0.17236 -0.00128 -0.01824 -0.01098 336 ARG A CZ  
2643 N NH1 . ARG A 336 ? 0.17169 0.21842 0.23780 -0.00382 -0.02060 -0.01137 336 ARG A NH1 
2644 N NH2 . ARG A 336 ? 0.16157 0.21015 0.23055 0.00154  -0.02096 -0.01071 336 ARG A NH2 
2645 N N   . THR A 337 ? 0.09722 0.11805 0.13013 -0.00849 -0.01033 -0.00881 337 THR A N   
2646 C CA  . THR A 337 ? 0.10920 0.12681 0.13913 -0.00958 -0.01323 -0.01015 337 THR A CA  
2647 C C   . THR A 337 ? 0.10244 0.11897 0.13535 -0.01263 -0.01275 -0.01079 337 THR A C   
2648 O O   . THR A 337 ? 0.11465 0.12951 0.14679 -0.01397 -0.01536 -0.01259 337 THR A O   
2649 C CB  . THR A 337 ? 0.10083 0.11298 0.12234 -0.00824 -0.01308 -0.01000 337 THR A CB  
2650 O OG1 . THR A 337 ? 0.11649 0.12559 0.13605 -0.00866 -0.00981 -0.00889 337 THR A OG1 
2651 C CG2 . THR A 337 ? 0.09919 0.11185 0.11778 -0.00547 -0.01363 -0.00922 337 THR A CG2 
2652 N N   . GLY A 338 ? 0.10555 0.12291 0.14171 -0.01392 -0.00952 -0.00937 338 GLY A N   
2653 C CA  . GLY A 338 ? 0.12409 0.13953 0.16302 -0.01687 -0.00883 -0.00944 338 GLY A CA  
2654 C C   . GLY A 338 ? 0.11138 0.12025 0.14496 -0.01701 -0.00782 -0.00906 338 GLY A C   
2655 O O   . GLY A 338 ? 0.16456 0.17096 0.20063 -0.01936 -0.00719 -0.00893 338 GLY A O   
2656 N N   . PHE A 339 ? 0.11397 0.11992 0.14089 -0.01459 -0.00769 -0.00890 339 PHE A N   
2657 C CA  . PHE A 339 ? 0.11803 0.11832 0.14051 -0.01431 -0.00642 -0.00839 339 PHE A CA  
2658 C C   . PHE A 339 ? 0.10353 0.10403 0.12442 -0.01323 -0.00342 -0.00557 339 PHE A C   
2659 O O   . PHE A 339 ? 0.11061 0.11231 0.12816 -0.01099 -0.00310 -0.00519 339 PHE A O   
2660 C CB  . PHE A 339 ? 0.10675 0.10401 0.12309 -0.01260 -0.00814 -0.01022 339 PHE A CB  
2661 C CG  . PHE A 339 ? 0.14605 0.14260 0.16257 -0.01391 -0.01107 -0.01324 339 PHE A CG  
2662 C CD1 . PHE A 339 ? 0.15154 0.14384 0.16829 -0.01550 -0.01118 -0.01499 339 PHE A CD1 
2663 C CD2 . PHE A 339 ? 0.14276 0.14287 0.15936 -0.01356 -0.01388 -0.01441 339 PHE A CD2 
2664 C CE1 . PHE A 339 ? 0.11800 0.10976 0.13453 -0.01688 -0.01388 -0.01827 339 PHE A CE1 
2665 C CE2 . PHE A 339 ? 0.11443 0.11423 0.13060 -0.01496 -0.01686 -0.01720 339 PHE A CE2 
2666 C CZ  . PHE A 339 ? 0.13636 0.13204 0.15224 -0.01670 -0.01678 -0.01936 339 PHE A CZ  
2667 N N   . PRO A 340 ? 0.10476 0.10413 0.12782 -0.01485 -0.00132 -0.00347 340 PRO A N   
2668 C CA  . PRO A 340 ? 0.13185 0.13226 0.15307 -0.01412 0.00136  -0.00067 340 PRO A CA  
2669 C C   . PRO A 340 ? 0.12914 0.12683 0.14423 -0.01160 0.00159  -0.00034 340 PRO A C   
2670 O O   . PRO A 340 ? 0.11798 0.11797 0.13099 -0.01032 0.00297  0.00077  340 PRO A O   
2671 C CB  . PRO A 340 ? 0.15802 0.15624 0.18190 -0.01655 0.00287  0.00169  340 PRO A CB  
2672 C CG  . PRO A 340 ? 0.11150 0.11014 0.14094 -0.01895 0.00148  0.00010  340 PRO A CG  
2673 C CD  . PRO A 340 ? 0.12123 0.11880 0.14894 -0.01772 -0.00140 -0.00340 340 PRO A CD  
2674 N N   . TRP A 341 ? 0.10309 0.09615 0.11554 -0.01096 0.00041  -0.00151 341 TRP A N   
2675 C CA  . TRP A 341 ? 0.11709 0.10798 0.12437 -0.00868 0.00069  -0.00130 341 TRP A CA  
2676 C C   . TRP A 341 ? 0.09902 0.09269 0.10382 -0.00682 -0.00003 -0.00238 341 TRP A C   
2677 O O   . TRP A 341 ? 0.10089 0.09524 0.10295 -0.00532 0.00101  -0.00134 341 TRP A O   
2678 C CB  . TRP A 341 ? 0.14290 0.12893 0.14854 -0.00839 -0.00026 -0.00292 341 TRP A CB  
2679 C CG  . TRP A 341 ? 0.10285 0.08697 0.10389 -0.00620 0.00015  -0.00283 341 TRP A CG  
2680 C CD1 . TRP A 341 ? 0.12667 0.11003 0.12415 -0.00487 -0.00080 -0.00491 341 TRP A CD1 
2681 C CD2 . TRP A 341 ? 0.10910 0.09215 0.10875 -0.00530 0.00157  -0.00043 341 TRP A CD2 
2682 N NE1 . TRP A 341 ? 0.10405 0.08599 0.09855 -0.00324 0.00016  -0.00407 341 TRP A NE1 
2683 C CE2 . TRP A 341 ? 0.10109 0.08288 0.09699 -0.00339 0.00143  -0.00142 341 TRP A CE2 
2684 C CE3 . TRP A 341 ? 0.10272 0.08597 0.10377 -0.00606 0.00283  0.00263  341 TRP A CE3 
2685 C CZ2 . TRP A 341 ? 0.10027 0.08115 0.09446 -0.00217 0.00234  0.00031  341 TRP A CZ2 
2686 C CZ3 . TRP A 341 ? 0.10224 0.08452 0.10093 -0.00480 0.00352  0.00448  341 TRP A CZ3 
2687 C CH2 . TRP A 341 ? 0.13773 0.11890 0.13335 -0.00283 0.00319  0.00320  341 TRP A CH2 
2688 N N   . ILE A 342 ? 0.09929 0.09456 0.10528 -0.00698 -0.00200 -0.00437 342 ILE A N   
2689 C CA  . ILE A 342 ? 0.10056 0.09812 0.10477 -0.00522 -0.00309 -0.00506 342 ILE A CA  
2690 C C   . ILE A 342 ? 0.10133 0.10332 0.10840 -0.00481 -0.00181 -0.00401 342 ILE A C   
2691 O O   . ILE A 342 ? 0.10296 0.10579 0.10795 -0.00303 -0.00126 -0.00367 342 ILE A O   
2692 C CB  . ILE A 342 ? 0.11409 0.11231 0.11890 -0.00566 -0.00596 -0.00712 342 ILE A CB  
2693 C CG1 . ILE A 342 ? 0.11191 0.10588 0.11328 -0.00613 -0.00687 -0.00873 342 ILE A CG1 
2694 C CG2 . ILE A 342 ? 0.14795 0.14839 0.15140 -0.00384 -0.00742 -0.00722 342 ILE A CG2 
2695 C CD1 . ILE A 342 ? 0.10179 0.09298 0.09761 -0.00440 -0.00612 -0.00853 342 ILE A CD1 
2696 N N   . ASP A 343 ? 0.09557 0.10056 0.10775 -0.00654 -0.00116 -0.00371 343 ASP A N   
2697 C CA  . ASP A 343 ? 0.11910 0.12896 0.13459 -0.00627 0.00042  -0.00320 343 ASP A CA  
2698 C C   . ASP A 343 ? 0.09343 0.10315 0.10605 -0.00578 0.00319  -0.00157 343 ASP A C   
2699 O O   . ASP A 343 ? 0.12283 0.13564 0.13584 -0.00459 0.00437  -0.00181 343 ASP A O   
2700 C CB  . ASP A 343 ? 0.09495 0.10828 0.11680 -0.00860 0.00084  -0.00320 343 ASP A CB  
2701 C CG  . ASP A 343 ? 0.10306 0.11777 0.12841 -0.00902 -0.00225 -0.00506 343 ASP A CG  
2702 O OD1 . ASP A 343 ? 0.09519 0.10940 0.11831 -0.00719 -0.00452 -0.00611 343 ASP A OD1 
2703 O OD2 . ASP A 343 ? 0.09720 0.11357 0.12753 -0.01132 -0.00253 -0.00533 343 ASP A OD2 
2704 N N   . ALA A 344 ? 0.09452 0.10074 0.10444 -0.00662 0.00407  -0.00002 344 ALA A N   
2705 C CA  . ALA A 344 ? 0.09970 0.10590 0.10645 -0.00626 0.00621  0.00175  344 ALA A CA  
2706 C C   . ALA A 344 ? 0.09270 0.09753 0.09506 -0.00388 0.00574  0.00106  344 ALA A C   
2707 O O   . ALA A 344 ? 0.10840 0.11508 0.10901 -0.00318 0.00725  0.00144  344 ALA A O   
2708 C CB  . ALA A 344 ? 0.09686 0.09957 0.10250 -0.00771 0.00679  0.00397  344 ALA A CB  
2709 N N   . ILE A 345 ? 0.09234 0.09408 0.09281 -0.00280 0.00378  -0.00005 345 ILE A N   
2710 C CA  . ILE A 345 ? 0.09098 0.09145 0.08772 -0.00079 0.00337  -0.00056 345 ILE A CA  
2711 C C   . ILE A 345 ? 0.10423 0.10779 0.10253 0.00049  0.00305  -0.00177 345 ILE A C   
2712 O O   . ILE A 345 ? 0.10292 0.10705 0.09954 0.00172  0.00387  -0.00190 345 ILE A O   
2713 C CB  . ILE A 345 ? 0.09166 0.08829 0.08590 -0.00026 0.00170  -0.00134 345 ILE A CB  
2714 C CG1 . ILE A 345 ? 0.13127 0.12472 0.12506 -0.00129 0.00211  -0.00049 345 ILE A CG1 
2715 C CG2 . ILE A 345 ? 0.12581 0.12123 0.11647 0.00150  0.00151  -0.00156 345 ILE A CG2 
2716 C CD1 . ILE A 345 ? 0.09468 0.08472 0.08648 -0.00092 0.00089  -0.00185 345 ILE A CD1 
2717 N N   . MET A 346 ? 0.10760 0.11318 0.10962 0.00022  0.00170  -0.00276 346 MET A N   
2718 C CA  . MET A 346 ? 0.14442 0.15298 0.14915 0.00163  0.00110  -0.00381 346 MET A CA  
2719 C C   . MET A 346 ? 0.15037 0.16287 0.15772 0.00162  0.00364  -0.00400 346 MET A C   
2720 O O   . MET A 346 ? 0.13075 0.14498 0.13947 0.00323  0.00386  -0.00504 346 MET A O   
2721 C CB  . MET A 346 ? 0.13710 0.14737 0.14581 0.00124  -0.00124 -0.00462 346 MET A CB  
2722 C CG  . MET A 346 ? 0.12062 0.12746 0.12602 0.00127  -0.00386 -0.00484 346 MET A CG  
2723 S SD  . MET A 346 ? 0.13739 0.14140 0.13795 0.00345  -0.00472 -0.00456 346 MET A SD  
2724 C CE  . MET A 346 ? 0.11291 0.12066 0.11858 0.00518  -0.00556 -0.00497 346 MET A CE  
2725 N N   . THR A 347 ? 0.11709 0.13077 0.12492 -0.00021 0.00562  -0.00299 347 THR A N   
2726 C CA  . THR A 347 ? 0.10084 0.11858 0.11014 -0.00057 0.00849  -0.00314 347 THR A CA  
2727 C C   . THR A 347 ? 0.08937 0.10547 0.09336 0.00022  0.00969  -0.00277 347 THR A C   
2728 O O   . THR A 347 ? 0.11107 0.12987 0.11536 0.00098  0.01131  -0.00400 347 THR A O   
2729 C CB  . THR A 347 ? 0.16321 0.18347 0.17553 -0.00312 0.01009  -0.00199 347 THR A CB  
2730 O OG1 . THR A 347 ? 0.14887 0.17174 0.16719 -0.00357 0.00888  -0.00301 347 THR A OG1 
2731 C CG2 . THR A 347 ? 0.13540 0.15958 0.14752 -0.00399 0.01348  -0.00168 347 THR A CG2 
2732 N N   . GLN A 348 ? 0.13613 0.14807 0.13581 0.00004  0.00887  -0.00136 348 GLN A N   
2733 C CA  . GLN A 348 ? 0.10160 0.11204 0.09666 0.00083  0.00946  -0.00105 348 GLN A CA  
2734 C C   . GLN A 348 ? 0.11938 0.12928 0.11416 0.00295  0.00854  -0.00291 348 GLN A C   
2735 O O   . GLN A 348 ? 0.08881 0.09959 0.08183 0.00362  0.00961  -0.00377 348 GLN A O   
2736 C CB  . GLN A 348 ? 0.10480 0.11102 0.09654 0.00043  0.00848  0.00073  348 GLN A CB  
2737 C CG  . GLN A 348 ? 0.10007 0.10524 0.08759 0.00092  0.00893  0.00143  348 GLN A CG  
2738 C CD  . GLN A 348 ? 0.09746 0.09866 0.08290 0.00094  0.00777  0.00291  348 GLN A CD  
2739 O OE1 . GLN A 348 ? 0.14895 0.14763 0.13542 0.00114  0.00653  0.00261  348 GLN A OE1 
2740 N NE2 . GLN A 348 ? 0.14592 0.14679 0.12858 0.00073  0.00814  0.00438  348 GLN A NE2 
2741 N N   . LEU A 349 ? 0.09309 0.10146 0.08953 0.00388  0.00645  -0.00352 349 LEU A N   
2742 C CA  . LEU A 349 ? 0.10755 0.11517 0.10433 0.00577  0.00536  -0.00479 349 LEU A CA  
2743 C C   . LEU A 349 ? 0.13124 0.14258 0.13164 0.00662  0.00672  -0.00658 349 LEU A C   
2744 O O   . LEU A 349 ? 0.08735 0.09826 0.08684 0.00778  0.00721  -0.00774 349 LEU A O   
2745 C CB  . LEU A 349 ? 0.09965 0.10566 0.09769 0.00630  0.00275  -0.00470 349 LEU A CB  
2746 C CG  . LEU A 349 ? 0.09216 0.09759 0.09161 0.00816  0.00121  -0.00544 349 LEU A CG  
2747 C CD1 . LEU A 349 ? 0.11034 0.11224 0.10561 0.00890  0.00099  -0.00506 349 LEU A CD1 
2748 C CD2 . LEU A 349 ? 0.12067 0.12589 0.12196 0.00832  -0.00149 -0.00509 349 LEU A CD2 
2749 N N   . VAL A 350 ? 0.09623 0.11135 0.10127 0.00604  0.00744  -0.00711 350 VAL A N   
2750 C CA  . VAL A 350 ? 0.14486 0.16390 0.15440 0.00708  0.00887  -0.00925 350 VAL A CA  
2751 C C   . VAL A 350 ? 0.13815 0.15983 0.14571 0.00621  0.01215  -0.01006 350 VAL A C   
2752 O O   . VAL A 350 ? 0.15237 0.17634 0.16192 0.00733  0.01363  -0.01243 350 VAL A O   
2753 C CB  . VAL A 350 ? 0.12970 0.15247 0.14586 0.00687  0.00843  -0.00971 350 VAL A CB  
2754 C CG1 . VAL A 350 ? 0.15399 0.17445 0.17160 0.00775  0.00481  -0.00903 350 VAL A CG1 
2755 C CG2 . VAL A 350 ? 0.16949 0.19447 0.18597 0.00434  0.00999  -0.00850 350 VAL A CG2 
2756 N N   . THR A 351 ? 0.09678 0.11821 0.10043 0.00422  0.01328  -0.00819 351 THR A N   
2757 C CA  . THR A 351 ? 0.11295 0.13694 0.11360 0.00315  0.01612  -0.00851 351 THR A CA  
2758 C C   . THR A 351 ? 0.11913 0.14020 0.11417 0.00370  0.01567  -0.00854 351 THR A C   
2759 O O   . THR A 351 ? 0.12924 0.15209 0.12314 0.00418  0.01718  -0.01069 351 THR A O   
2760 C CB  . THR A 351 ? 0.11455 0.13991 0.11389 0.00056  0.01746  -0.00597 351 THR A CB  
2761 O OG1 . THR A 351 ? 0.19292 0.21374 0.18935 -0.00000 0.01542  -0.00340 351 THR A OG1 
2762 C CG2 . THR A 351 ? 0.10794 0.13699 0.11344 -0.00036 0.01830  -0.00619 351 THR A CG2 
2763 N N   . TRP A 352 ? 0.10907 0.12588 0.10093 0.00360  0.01367  -0.00648 352 TRP A N   
2764 C CA  . TRP A 352 ? 0.15291 0.16730 0.14010 0.00397  0.01311  -0.00634 352 TRP A CA  
2765 C C   . TRP A 352 ? 0.11238 0.12387 0.10031 0.00587  0.01139  -0.00775 352 TRP A C   
2766 O O   . TRP A 352 ? 0.16477 0.17560 0.15050 0.00637  0.01149  -0.00896 352 TRP A O   
2767 C CB  . TRP A 352 ? 0.12633 0.13795 0.11022 0.00291  0.01208  -0.00336 352 TRP A CB  
2768 C CG  . TRP A 352 ? 0.12783 0.14147 0.10967 0.00095  0.01354  -0.00133 352 TRP A CG  
2769 C CD1 . TRP A 352 ? 0.15074 0.16858 0.13347 -0.00028 0.01585  -0.00165 352 TRP A CD1 
2770 C CD2 . TRP A 352 ? 0.12891 0.14049 0.10760 -0.00005 0.01280  0.00160  352 TRP A CD2 
2771 N NE1 . TRP A 352 ? 0.20574 0.22412 0.18550 -0.00222 0.01657  0.00126  352 TRP A NE1 
2772 C CE2 . TRP A 352 ? 0.16502 0.17943 0.14247 -0.00199 0.01454  0.00336  352 TRP A CE2 
2773 C CE3 . TRP A 352 ? 0.20079 0.20858 0.17797 0.00053  0.01091  0.00296  352 TRP A CE3 
2774 C CZ2 . TRP A 352 ? 0.16488 0.17801 0.13963 -0.00331 0.01406  0.00680  352 TRP A CZ2 
2775 C CZ3 . TRP A 352 ? 0.17196 0.17870 0.14709 -0.00055 0.01052  0.00596  352 TRP A CZ3 
2776 C CH2 . TRP A 352 ? 0.12666 0.13585 0.10058 -0.00242 0.01191  0.00803  352 TRP A CH2 
2777 N N   . GLY A 353 ? 0.12300 0.13267 0.11374 0.00673  0.00967  -0.00748 353 GLY A N   
2778 C CA  . GLY A 353 ? 0.09832 0.10481 0.08909 0.00820  0.00792  -0.00800 353 GLY A CA  
2779 C C   . GLY A 353 ? 0.10857 0.11144 0.09556 0.00792  0.00671  -0.00633 353 GLY A C   
2780 O O   . GLY A 353 ? 0.14000 0.14034 0.12647 0.00882  0.00561  -0.00658 353 GLY A O   
2781 N N   . TRP A 354 ? 0.08779 0.09036 0.07258 0.00667  0.00696  -0.00459 354 TRP A N   
2782 C CA  . TRP A 354 ? 0.11664 0.11617 0.09867 0.00651  0.00604  -0.00319 354 TRP A CA  
2783 C C   . TRP A 354 ? 0.11316 0.11206 0.09510 0.00545  0.00592  -0.00150 354 TRP A C   
2784 O O   . TRP A 354 ? 0.08852 0.08934 0.07069 0.00436  0.00696  -0.00068 354 TRP A O   
2785 C CB  . TRP A 354 ? 0.08824 0.08794 0.06754 0.00630  0.00653  -0.00315 354 TRP A CB  
2786 C CG  . TRP A 354 ? 0.08790 0.08502 0.06540 0.00626  0.00563  -0.00180 354 TRP A CG  
2787 C CD1 . TRP A 354 ? 0.08742 0.08251 0.06441 0.00693  0.00489  -0.00218 354 TRP A CD1 
2788 C CD2 . TRP A 354 ? 0.09699 0.09341 0.07365 0.00553  0.00552  0.00013  354 TRP A CD2 
2789 N NE1 . TRP A 354 ? 0.08731 0.08095 0.06332 0.00670  0.00450  -0.00087 354 TRP A NE1 
2790 C CE2 . TRP A 354 ? 0.08788 0.08214 0.06385 0.00600  0.00477  0.00052  354 TRP A CE2 
2791 C CE3 . TRP A 354 ? 0.11884 0.11617 0.09570 0.00450  0.00601  0.00167  354 TRP A CE3 
2792 C CZ2 . TRP A 354 ? 0.08834 0.08141 0.06427 0.00576  0.00446  0.00209  354 TRP A CZ2 
2793 C CZ3 . TRP A 354 ? 0.09046 0.08609 0.06707 0.00417  0.00550  0.00354  354 TRP A CZ3 
2794 C CH2 . TRP A 354 ? 0.09126 0.08480 0.06761 0.00494  0.00471  0.00360  354 TRP A CH2 
2795 N N   . MET A 355 ? 0.08724 0.08343 0.06885 0.00564  0.00478  -0.00104 355 MET A N   
2796 C CA  . MET A 355 ? 0.08963 0.08446 0.07131 0.00475  0.00461  0.00014  355 MET A CA  
2797 C C   . MET A 355 ? 0.10917 0.10126 0.08902 0.00516  0.00416  0.00059  355 MET A C   
2798 O O   . MET A 355 ? 0.08742 0.07866 0.06609 0.00597  0.00385  -0.00001 355 MET A O   
2799 C CB  . MET A 355 ? 0.09963 0.09423 0.08333 0.00439  0.00376  -0.00041 355 MET A CB  
2800 C CG  . MET A 355 ? 0.13254 0.13017 0.11909 0.00436  0.00389  -0.00124 355 MET A CG  
2801 S SD  . MET A 355 ? 0.14973 0.14720 0.13690 0.00589  0.00244  -0.00250 355 MET A SD  
2802 C CE  . MET A 355 ? 0.17940 0.17458 0.16576 0.00549  0.00051  -0.00246 355 MET A CE  
2803 N N   . HIS A 356 ? 0.10833 0.09905 0.08851 0.00457  0.00423  0.00166  356 HIS A N   
2804 C CA  . HIS A 356 ? 0.08917 0.07754 0.06863 0.00508  0.00399  0.00180  356 HIS A CA  
2805 C C   . HIS A 356 ? 0.08933 0.07611 0.06818 0.00544  0.00350  0.00035  356 HIS A C   
2806 O O   . HIS A 356 ? 0.09386 0.08086 0.07316 0.00507  0.00296  -0.00043 356 HIS A O   
2807 C CB  . HIS A 356 ? 0.09067 0.07765 0.07158 0.00452  0.00408  0.00313  356 HIS A CB  
2808 C CG  . HIS A 356 ? 0.09743 0.08237 0.07866 0.00527  0.00400  0.00312  356 HIS A CG  
2809 N ND1 . HIS A 356 ? 0.10732 0.09008 0.08914 0.00547  0.00404  0.00168  356 HIS A ND1 
2810 C CD2 . HIS A 356 ? 0.11649 0.10158 0.09784 0.00586  0.00392  0.00419  356 HIS A CD2 
2811 C CE1 . HIS A 356 ? 0.12438 0.10610 0.10702 0.00625  0.00430  0.00174  356 HIS A CE1 
2812 N NE2 . HIS A 356 ? 0.10273 0.08586 0.08538 0.00654  0.00408  0.00338  356 HIS A NE2 
2813 N N   . HIS A 357 ? 0.09552 0.08101 0.07331 0.00604  0.00368  0.00004  357 HIS A N   
2814 C CA  . HIS A 357 ? 0.09038 0.07458 0.06665 0.00618  0.00350  -0.00116 357 HIS A CA  
2815 C C   . HIS A 357 ? 0.09217 0.07522 0.06876 0.00554  0.00314  -0.00216 357 HIS A C   
2816 O O   . HIS A 357 ? 0.09324 0.07627 0.06844 0.00527  0.00235  -0.00302 357 HIS A O   
2817 C CB  . HIS A 357 ? 0.09065 0.07398 0.06635 0.00668  0.00426  -0.00130 357 HIS A CB  
2818 C CG  . HIS A 357 ? 0.09232 0.07465 0.06584 0.00658  0.00448  -0.00239 357 HIS A CG  
2819 N ND1 . HIS A 357 ? 0.09678 0.07931 0.06824 0.00647  0.00381  -0.00232 357 HIS A ND1 
2820 C CD2 . HIS A 357 ? 0.10396 0.08516 0.07691 0.00653  0.00537  -0.00353 357 HIS A CD2 
2821 C CE1 . HIS A 357 ? 0.10768 0.08930 0.07674 0.00615  0.00419  -0.00304 357 HIS A CE1 
2822 N NE2 . HIS A 357 ? 0.09604 0.07702 0.06586 0.00616  0.00533  -0.00405 357 HIS A NE2 
2823 N N   . LEU A 358 ? 0.09302 0.07499 0.07156 0.00524  0.00350  -0.00204 358 LEU A N   
2824 C CA  . LEU A 358 ? 0.10524 0.08578 0.08453 0.00448  0.00316  -0.00340 358 LEU A CA  
2825 C C   . LEU A 358 ? 0.09510 0.07691 0.07574 0.00352  0.00227  -0.00320 358 LEU A C   
2826 O O   . LEU A 358 ? 0.10497 0.08618 0.08578 0.00273  0.00151  -0.00466 358 LEU A O   
2827 C CB  . LEU A 358 ? 0.09667 0.07515 0.07850 0.00453  0.00380  -0.00336 358 LEU A CB  
2828 C CG  . LEU A 358 ? 0.11173 0.08900 0.09321 0.00546  0.00478  -0.00442 358 LEU A CG  
2829 C CD1 . LEU A 358 ? 0.11683 0.09193 0.10199 0.00576  0.00523  -0.00449 358 LEU A CD1 
2830 C CD2 . LEU A 358 ? 0.14552 0.12241 0.12397 0.00520  0.00496  -0.00682 358 LEU A CD2 
2831 N N   . ALA A 359 ? 0.09330 0.07714 0.07501 0.00346  0.00241  -0.00167 359 ALA A N   
2832 C CA  . ALA A 359 ? 0.09304 0.07890 0.07641 0.00265  0.00182  -0.00170 359 ALA A CA  
2833 C C   . ALA A 359 ? 0.09286 0.07980 0.07493 0.00307  0.00066  -0.00277 359 ALA A C   
2834 O O   . ALA A 359 ? 0.09387 0.08160 0.07716 0.00236  -0.00050 -0.00361 359 ALA A O   
2835 C CB  . ALA A 359 ? 0.09164 0.07986 0.07617 0.00252  0.00268  -0.00010 359 ALA A CB  
2836 N N   . ARG A 360 ? 0.09202 0.07891 0.07184 0.00414  0.00073  -0.00260 360 ARG A N   
2837 C CA  . ARG A 360 ? 0.09262 0.07999 0.07110 0.00457  -0.00059 -0.00308 360 ARG A CA  
2838 C C   . ARG A 360 ? 0.09543 0.08127 0.07165 0.00399  -0.00158 -0.00423 360 ARG A C   
2839 O O   . ARG A 360 ? 0.09687 0.08353 0.07263 0.00378  -0.00329 -0.00458 360 ARG A O   
2840 C CB  . ARG A 360 ? 0.09173 0.07880 0.06850 0.00561  -0.00019 -0.00245 360 ARG A CB  
2841 C CG  . ARG A 360 ? 0.08964 0.07811 0.06797 0.00605  0.00087  -0.00182 360 ARG A CG  
2842 C CD  . ARG A 360 ? 0.10568 0.09393 0.08307 0.00696  0.00088  -0.00163 360 ARG A CD  
2843 N NE  . ARG A 360 ? 0.09145 0.08090 0.06964 0.00718  0.00195  -0.00150 360 ARG A NE  
2844 C CZ  . ARG A 360 ? 0.08757 0.07715 0.06574 0.00781  0.00209  -0.00174 360 ARG A CZ  
2845 N NH1 . ARG A 360 ? 0.08842 0.07674 0.06626 0.00836  0.00125  -0.00174 360 ARG A NH1 
2846 N NH2 . ARG A 360 ? 0.09014 0.08105 0.06854 0.00777  0.00299  -0.00195 360 ARG A NH2 
2847 N N   . HIS A 361 ? 0.09668 0.08050 0.07153 0.00375  -0.00057 -0.00496 361 HIS A N   
2848 C CA  . HIS A 361 ? 0.10007 0.08256 0.07266 0.00301  -0.00114 -0.00671 361 HIS A CA  
2849 C C   . HIS A 361 ? 0.11335 0.09646 0.08799 0.00186  -0.00254 -0.00777 361 HIS A C   
2850 O O   . HIS A 361 ? 0.12126 0.10457 0.09383 0.00118  -0.00411 -0.00898 361 HIS A O   
2851 C CB  . HIS A 361 ? 0.12038 0.10077 0.09266 0.00308  0.00055  -0.00773 361 HIS A CB  
2852 C CG  . HIS A 361 ? 0.11888 0.09874 0.08822 0.00375  0.00170  -0.00767 361 HIS A CG  
2853 N ND1 . HIS A 361 ? 0.14154 0.12027 0.10820 0.00342  0.00253  -0.00956 361 HIS A ND1 
2854 C CD2 . HIS A 361 ? 0.13346 0.11394 0.10239 0.00456  0.00233  -0.00613 361 HIS A CD2 
2855 C CE1 . HIS A 361 ? 0.17714 0.15603 0.14197 0.00395  0.00375  -0.00893 361 HIS A CE1 
2856 N NE2 . HIS A 361 ? 0.15591 0.13572 0.12223 0.00461  0.00351  -0.00681 361 HIS A NE2 
2857 N N   . SER A 362 ? 0.09999 0.08349 0.07859 0.00140  -0.00206 -0.00726 362 SER A N   
2858 C CA  . SER A 362 ? 0.12424 0.10822 0.10556 -0.00000 -0.00319 -0.00830 362 SER A CA  
2859 C C   . SER A 362 ? 0.10125 0.08817 0.08351 -0.00019 -0.00516 -0.00812 362 SER A C   
2860 O O   . SER A 362 ? 0.10387 0.09125 0.08600 -0.00119 -0.00701 -0.00959 362 SER A O   
2861 C CB  . SER A 362 ? 0.12643 0.11023 0.11190 -0.00063 -0.00201 -0.00719 362 SER A CB  
2862 O OG  . SER A 362 ? 0.13342 0.11414 0.11906 -0.00064 -0.00086 -0.00760 362 SER A OG  
2863 N N   . VAL A 363 ? 0.09844 0.08748 0.08197 0.00079  -0.00490 -0.00652 363 VAL A N   
2864 C CA  . VAL A 363 ? 0.11930 0.11132 0.10502 0.00091  -0.00674 -0.00636 363 VAL A CA  
2865 C C   . VAL A 363 ? 0.11399 0.10568 0.09603 0.00157  -0.00871 -0.00642 363 VAL A C   
2866 O O   . VAL A 363 ? 0.12498 0.11849 0.10810 0.00125  -0.01116 -0.00671 363 VAL A O   
2867 C CB  . VAL A 363 ? 0.09504 0.08950 0.08392 0.00181  -0.00556 -0.00508 363 VAL A CB  
2868 C CG1 . VAL A 363 ? 0.10966 0.10515 0.10203 0.00068  -0.00390 -0.00475 363 VAL A CG1 
2869 C CG2 . VAL A 363 ? 0.09364 0.08674 0.07968 0.00317  -0.00422 -0.00419 363 VAL A CG2 
2870 N N   . ALA A 364 ? 0.10067 0.09024 0.07848 0.00235  -0.00783 -0.00594 364 ALA A N   
2871 C CA  . ALA A 364 ? 0.12357 0.11266 0.09738 0.00268  -0.00954 -0.00551 364 ALA A CA  
2872 C C   . ALA A 364 ? 0.12051 0.10883 0.09089 0.00132  -0.01090 -0.00718 364 ALA A C   
2873 O O   . ALA A 364 ? 0.12333 0.11261 0.09173 0.00103  -0.01348 -0.00694 364 ALA A O   
2874 C CB  . ALA A 364 ? 0.10299 0.09019 0.07354 0.00356  -0.00791 -0.00449 364 ALA A CB  
2875 N N   . CYS A 365 ? 0.10866 0.09524 0.07833 0.00047  -0.00932 -0.00896 365 CYS A N   
2876 C CA  . CYS A 365 ? 0.14367 0.12951 0.11033 -0.00094 -0.01042 -0.01130 365 CYS A CA  
2877 C C   . CYS A 365 ? 0.15721 0.14514 0.12709 -0.00207 -0.01302 -0.01218 365 CYS A C   
2878 O O   . CYS A 365 ? 0.24485 0.23361 0.21180 -0.00300 -0.01551 -0.01317 365 CYS A O   
2879 C CB  . CYS A 365 ? 0.17550 0.15880 0.14207 -0.00139 -0.00802 -0.01331 365 CYS A CB  
2880 S SG  . CYS A 365 ? 0.12060 0.10265 0.08346 -0.00313 -0.00884 -0.01715 365 CYS A SG  
2881 N N   . PHE A 366 ? 0.11115 0.10026 0.08702 -0.00217 -0.01250 -0.01175 366 PHE A N   
2882 C CA  . PHE A 366 ? 0.12289 0.11438 0.10297 -0.00344 -0.01467 -0.01260 366 PHE A CA  
2883 C C   . PHE A 366 ? 0.12441 0.11887 0.10456 -0.00296 -0.01780 -0.01152 366 PHE A C   
2884 O O   . PHE A 366 ? 0.12644 0.12249 0.10680 -0.00418 -0.02067 -0.01275 366 PHE A O   
2885 C CB  . PHE A 366 ? 0.11703 0.10966 0.10347 -0.00360 -0.01303 -0.01174 366 PHE A CB  
2886 C CG  . PHE A 366 ? 0.16113 0.15649 0.15292 -0.00515 -0.01479 -0.01257 366 PHE A CG  
2887 C CD1 . PHE A 366 ? 0.15317 0.14711 0.14664 -0.00713 -0.01490 -0.01459 366 PHE A CD1 
2888 C CD2 . PHE A 366 ? 0.16251 0.16190 0.15839 -0.00463 -0.01627 -0.01145 366 PHE A CD2 
2889 C CE1 . PHE A 366 ? 0.23570 0.23232 0.23465 -0.00883 -0.01654 -0.01538 366 PHE A CE1 
2890 C CE2 . PHE A 366 ? 0.11785 0.12032 0.11944 -0.00614 -0.01785 -0.01227 366 PHE A CE2 
2891 C CZ  . PHE A 366 ? 0.13104 0.13219 0.13408 -0.00837 -0.01801 -0.01417 366 PHE A CZ  
2892 N N   . LEU A 367 ? 0.12846 0.12362 0.10868 -0.00118 -0.01750 -0.00924 367 LEU A N   
2893 C CA  . LEU A 367 ? 0.11765 0.11536 0.09896 -0.00040 -0.02057 -0.00786 367 LEU A CA  
2894 C C   . LEU A 367 ? 0.14980 0.14649 0.12439 -0.00080 -0.02300 -0.00771 367 LEU A C   
2895 O O   . LEU A 367 ? 0.18326 0.18215 0.15816 -0.00123 -0.02660 -0.00749 367 LEU A O   
2896 C CB  . LEU A 367 ? 0.10803 0.10624 0.09175 0.00164  -0.01940 -0.00574 367 LEU A CB  
2897 C CG  . LEU A 367 ? 0.10945 0.10969 0.09492 0.00286  -0.02254 -0.00407 367 LEU A CG  
2898 C CD1 . LEU A 367 ? 0.11486 0.11931 0.10793 0.00276  -0.02424 -0.00458 367 LEU A CD1 
2899 C CD2 . LEU A 367 ? 0.10735 0.10644 0.09311 0.00479  -0.02116 -0.00229 367 LEU A CD2 
2900 N N   . THR A 368 ? 0.15941 0.15311 0.12788 -0.00076 -0.02112 -0.00772 368 THR A N   
2901 C CA  . THR A 368 ? 0.13807 0.13098 0.09948 -0.00118 -0.02292 -0.00707 368 THR A CA  
2902 C C   . THR A 368 ? 0.16554 0.15778 0.12215 -0.00320 -0.02340 -0.01005 368 THR A C   
2903 O O   . THR A 368 ? 0.16367 0.15779 0.12175 -0.00444 -0.02608 -0.01158 368 THR A O   
2904 C CB  . THR A 368 ? 0.15334 0.14382 0.11078 -0.00019 -0.02051 -0.00536 368 THR A CB  
2905 O OG1 . THR A 368 ? 0.15099 0.13946 0.10788 -0.00043 -0.01687 -0.00715 368 THR A OG1 
2906 C CG2 . THR A 368 ? 0.16342 0.15437 0.12540 0.00171  -0.02035 -0.00276 368 THR A CG2 
2907 N N   . ARG A 369 ? 0.13094 0.12069 0.08213 -0.00357 -0.02077 -0.01115 369 ARG A N   
2908 C CA  . ARG A 369 ? 0.17187 0.16088 0.11731 -0.00537 -0.02090 -0.01424 369 ARG A CA  
2909 C C   . ARG A 369 ? 0.17009 0.15845 0.11926 -0.00647 -0.02003 -0.01789 369 ARG A C   
2910 O O   . ARG A 369 ? 0.14197 0.12963 0.08711 -0.00804 -0.02020 -0.02117 369 ARG A O   
2911 C CB  . ARG A 369 ? 0.15594 0.14283 0.09534 -0.00525 -0.01780 -0.01438 369 ARG A CB  
2912 C CG  . ARG A 369 ? 0.15067 0.13560 0.09383 -0.00413 -0.01378 -0.01479 369 ARG A CG  
2913 C CD  . ARG A 369 ? 0.13655 0.11988 0.07447 -0.00430 -0.01066 -0.01590 369 ARG A CD  
2914 N NE  . ARG A 369 ? 0.20256 0.18431 0.14473 -0.00315 -0.00728 -0.01625 369 ARG A NE  
2915 C CZ  . ARG A 369 ? 0.18849 0.16884 0.13341 -0.00336 -0.00551 -0.01924 369 ARG A CZ  
2916 N NH1 . ARG A 369 ? 0.13854 0.11861 0.08251 -0.00475 -0.00649 -0.02261 369 ARG A NH1 
2917 N NH2 . ARG A 369 ? 0.20769 0.18679 0.15662 -0.00216 -0.00289 -0.01882 369 ARG A NH2 
2918 N N   . GLY A 370 ? 0.16848 0.15696 0.12505 -0.00586 -0.01906 -0.01747 370 GLY A N   
2919 C CA  . GLY A 370 ? 0.16386 0.15107 0.12421 -0.00698 -0.01797 -0.02041 370 GLY A CA  
2920 C C   . GLY A 370 ? 0.16216 0.15157 0.12684 -0.00849 -0.02097 -0.02164 370 GLY A C   
2921 O O   . GLY A 370 ? 0.19476 0.18329 0.15914 -0.01026 -0.02160 -0.02506 370 GLY A O   
2922 N N   . ASP A 371 ? 0.14787 0.14026 0.11712 -0.00784 -0.02277 -0.01915 371 ASP A N   
2923 C CA  . ASP A 371 ? 0.12916 0.12420 0.10422 -0.00924 -0.02526 -0.02014 371 ASP A CA  
2924 C C   . ASP A 371 ? 0.15294 0.15196 0.12909 -0.00885 -0.02916 -0.01830 371 ASP A C   
2925 O O   . ASP A 371 ? 0.21892 0.21983 0.19403 -0.01037 -0.03271 -0.01985 371 ASP A O   
2926 C CB  . ASP A 371 ? 0.12614 0.12130 0.10889 -0.00910 -0.02290 -0.01931 371 ASP A CB  
2927 C CG  . ASP A 371 ? 0.12895 0.12017 0.11185 -0.00974 -0.01980 -0.02104 371 ASP A CG  
2928 O OD1 . ASP A 371 ? 0.14659 0.13545 0.12718 -0.00832 -0.01701 -0.01994 371 ASP A OD1 
2929 O OD2 . ASP A 371 ? 0.21556 0.20598 0.20135 -0.01166 -0.02032 -0.02349 371 ASP A OD2 
2930 N N   . LEU A 372 ? 0.19425 0.19464 0.17286 -0.00682 -0.02875 -0.01512 372 LEU A N   
2931 C CA  . LEU A 372 ? 0.13953 0.14389 0.12188 -0.00613 -0.03228 -0.01331 372 LEU A CA  
2932 C C   . LEU A 372 ? 0.19070 0.19517 0.16666 -0.00550 -0.03530 -0.01162 372 LEU A C   
2933 O O   . LEU A 372 ? 0.18410 0.19182 0.16248 -0.00531 -0.03930 -0.01044 372 LEU A O   
2934 C CB  . LEU A 372 ? 0.16076 0.16666 0.14967 -0.00420 -0.03037 -0.01109 372 LEU A CB  
2935 C CG  . LEU A 372 ? 0.15248 0.15892 0.14774 -0.00495 -0.02744 -0.01208 372 LEU A CG  
2936 C CD1 . LEU A 372 ? 0.12624 0.13451 0.12677 -0.00312 -0.02536 -0.01013 372 LEU A CD1 
2937 C CD2 . LEU A 372 ? 0.18836 0.19769 0.18878 -0.00709 -0.02973 -0.01398 372 LEU A CD2 
2938 N N   . TYR A 373 ? 0.21037 0.21154 0.17853 -0.00526 -0.03355 -0.01128 373 TYR A N   
2939 C CA  . TYR A 373 ? 0.20519 0.20609 0.16625 -0.00502 -0.03600 -0.00930 373 TYR A CA  
2940 C C   . TYR A 373 ? 0.21036 0.21294 0.17514 -0.00294 -0.03809 -0.00550 373 TYR A C   
2941 O O   . TYR A 373 ? 0.20988 0.21408 0.17264 -0.00292 -0.04224 -0.00360 373 TYR A O   
2942 C CB  . TYR A 373 ? 0.25687 0.25926 0.21315 -0.00718 -0.03982 -0.01117 373 TYR A CB  
2943 C CG  . TYR A 373 ? 0.25210 0.25248 0.19762 -0.00800 -0.03970 -0.01100 373 TYR A CG  
2944 C CD1 . TYR A 373 ? 0.23638 0.23380 0.17701 -0.00884 -0.03579 -0.01372 373 TYR A CD1 
2945 C CD2 . TYR A 373 ? 0.24552 0.24708 0.18600 -0.00793 -0.04340 -0.00799 373 TYR A CD2 
2946 C CE1 . TYR A 373 ? 0.28286 0.27895 0.21387 -0.00971 -0.03517 -0.01381 373 TYR A CE1 
2947 C CE2 . TYR A 373 ? 0.29179 0.29175 0.22195 -0.00898 -0.04296 -0.00761 373 TYR A CE2 
2948 C CZ  . TYR A 373 ? 0.27643 0.27385 0.20186 -0.00992 -0.03863 -0.01070 373 TYR A CZ  
2949 O OH  . TYR A 373 ? 0.25656 0.25289 0.17189 -0.01108 -0.03771 -0.01059 373 TYR A OH  
2950 N N   . VAL A 374 ? 0.24311 0.24523 0.21335 -0.00117 -0.03532 -0.00439 374 VAL A N   
2951 C CA  . VAL A 374 ? 0.22238 0.22539 0.19656 0.00105  -0.03652 -0.00125 374 VAL A CA  
2952 C C   . VAL A 374 ? 0.16016 0.15955 0.12903 0.00199  -0.03419 0.00070  374 VAL A C   
2953 O O   . VAL A 374 ? 0.16300 0.15989 0.12851 0.00148  -0.03051 -0.00059 374 VAL A O   
2954 C CB  . VAL A 374 ? 0.21990 0.22522 0.20383 0.00229  -0.03491 -0.00173 374 VAL A CB  
2955 C CG1 . VAL A 374 ? 0.30260 0.30858 0.29101 0.00476  -0.03581 0.00091  374 VAL A CG1 
2956 C CG2 . VAL A 374 ? 0.22269 0.23194 0.21233 0.00105  -0.03715 -0.00356 374 VAL A CG2 
2957 N N   . SER A 375 ? 0.17832 0.17741 0.14687 0.00332  -0.03652 0.00395  375 SER A N   
2958 C CA  . SER A 375 ? 0.17191 0.16756 0.13562 0.00394  -0.03473 0.00618  375 SER A CA  
2959 C C   . SER A 375 ? 0.16180 0.15581 0.12871 0.00499  -0.03024 0.00532  375 SER A C   
2960 O O   . SER A 375 ? 0.14612 0.14178 0.12034 0.00613  -0.02930 0.00442  375 SER A O   
2961 C CB  . SER A 375 ? 0.18566 0.18115 0.15069 0.00539  -0.03818 0.01006  375 SER A CB  
2962 O OG  . SER A 375 ? 0.19143 0.18351 0.15414 0.00616  -0.03598 0.01215  375 SER A OG  
2963 N N   . TRP A 376 ? 0.16334 0.15438 0.12463 0.00450  -0.02745 0.00560  376 TRP A N   
2964 C CA  . TRP A 376 ? 0.14551 0.13499 0.10919 0.00541  -0.02358 0.00507  376 TRP A CA  
2965 C C   . TRP A 376 ? 0.17702 0.16601 0.14567 0.00738  -0.02400 0.00712  376 TRP A C   
2966 O O   . TRP A 376 ? 0.13365 0.12237 0.10609 0.00828  -0.02134 0.00615  376 TRP A O   
2967 C CB  . TRP A 376 ? 0.12325 0.11009 0.08033 0.00441  -0.02083 0.00499  376 TRP A CB  
2968 C CG  . TRP A 376 ? 0.16973 0.15487 0.12136 0.00405  -0.02219 0.00795  376 TRP A CG  
2969 C CD1 . TRP A 376 ? 0.16565 0.15095 0.11058 0.00255  -0.02416 0.00870  376 TRP A CD1 
2970 C CD2 . TRP A 376 ? 0.14680 0.12979 0.09905 0.00498  -0.02166 0.01067  376 TRP A CD2 
2971 N NE1 . TRP A 376 ? 0.18784 0.17128 0.12892 0.00243  -0.02483 0.01214  376 TRP A NE1 
2972 C CE2 . TRP A 376 ? 0.19129 0.17310 0.13713 0.00391  -0.02332 0.01342  376 TRP A CE2 
2973 C CE3 . TRP A 376 ? 0.13414 0.11607 0.09160 0.00644  -0.01995 0.01095  376 TRP A CE3 
2974 C CZ2 . TRP A 376 ? 0.16256 0.14189 0.10760 0.00424  -0.02331 0.01675  376 TRP A CZ2 
2975 C CZ3 . TRP A 376 ? 0.15089 0.13034 0.10774 0.00682  -0.02003 0.01374  376 TRP A CZ3 
2976 C CH2 . TRP A 376 ? 0.14975 0.12779 0.10071 0.00572  -0.02170 0.01678  376 TRP A CH2 
2977 N N   . GLU A 377 ? 0.12334 0.11212 0.09210 0.00805  -0.02736 0.00988  377 GLU A N   
2978 C CA  . GLU A 377 ? 0.14001 0.12811 0.11470 0.01012  -0.02791 0.01149  377 GLU A CA  
2979 C C   . GLU A 377 ? 0.19517 0.18645 0.17850 0.01148  -0.02787 0.00951  377 GLU A C   
2980 O O   . GLU A 377 ? 0.17265 0.16360 0.16102 0.01298  -0.02614 0.00897  377 GLU A O   
2981 C CB  . GLU A 377 ? 0.18421 0.17128 0.15782 0.01063  -0.03195 0.01521  377 GLU A CB  
2982 C CG  . GLU A 377 ? 0.14485 0.12941 0.10923 0.00888  -0.03222 0.01749  377 GLU A CG  
2983 C CD  . GLU A 377 ? 0.19586 0.17881 0.15943 0.00944  -0.03599 0.02194  377 GLU A CD  
2984 O OE1 . GLU A 377 ? 0.23639 0.21736 0.20518 0.01116  -0.03609 0.02357  377 GLU A OE1 
2985 O OE2 . GLU A 377 ? 0.19754 0.18113 0.15533 0.00812  -0.03899 0.02380  377 GLU A OE2 
2986 N N   . ARG A 378 ? 0.19682 0.19138 0.18196 0.01081  -0.02959 0.00820  378 ARG A N   
2987 C CA  . ARG A 378 ? 0.19144 0.18962 0.18501 0.01178  -0.02928 0.00632  378 ARG A CA  
2988 C C   . ARG A 378 ? 0.14184 0.14023 0.13636 0.01133  -0.02483 0.00379  378 ARG A C   
2989 O O   . ARG A 378 ? 0.12592 0.12582 0.12636 0.01258  -0.02306 0.00273  378 ARG A O   
2990 C CB  . ARG A 378 ? 0.19518 0.19690 0.19046 0.01077  -0.03232 0.00562  378 ARG A CB  
2991 C CG  . ARG A 378 ? 0.19219 0.19453 0.18700 0.01117  -0.03741 0.00824  378 ARG A CG  
2992 C CD  . ARG A 378 ? 0.26890 0.27260 0.27225 0.01379  -0.03931 0.00967  378 ARG A CD  
2993 N NE  . ARG A 378 ? 0.25207 0.25172 0.25399 0.01517  -0.03858 0.01188  378 ARG A NE  
2994 C CZ  . ARG A 378 ? 0.27603 0.27321 0.27443 0.01545  -0.04176 0.01545  378 ARG A CZ  
2995 N NH1 . ARG A 378 ? 0.23917 0.23772 0.23461 0.01456  -0.04613 0.01730  378 ARG A NH1 
2996 N NH2 . ARG A 378 ? 0.25475 0.24798 0.25245 0.01648  -0.04065 0.01731  378 ARG A NH2 
2997 N N   . GLY A 379 ? 0.10819 0.10523 0.09702 0.00955  -0.02302 0.00277  379 GLY A N   
2998 C CA  . GLY A 379 ? 0.15495 0.15181 0.14426 0.00913  -0.01916 0.00098  379 GLY A CA  
2999 C C   . GLY A 379 ? 0.11870 0.11333 0.10754 0.01023  -0.01684 0.00148  379 GLY A C   
3000 O O   . GLY A 379 ? 0.16355 0.15909 0.15523 0.01058  -0.01425 0.00023  379 GLY A O   
3001 N N   . MET A 380 ? 0.12276 0.11454 0.10790 0.01058  -0.01777 0.00335  380 MET A N   
3002 C CA  . MET A 380 ? 0.15987 0.14948 0.14534 0.01153  -0.01594 0.00381  380 MET A CA  
3003 C C   . MET A 380 ? 0.16462 0.15584 0.15726 0.01335  -0.01595 0.00314  380 MET A C   
3004 O O   . MET A 380 ? 0.16015 0.15164 0.15471 0.01376  -0.01333 0.00162  380 MET A O   
3005 C CB  . MET A 380 ? 0.13689 0.12332 0.11796 0.01141  -0.01729 0.00631  380 MET A CB  
3006 C CG  . MET A 380 ? 0.16101 0.14481 0.14138 0.01173  -0.01517 0.00667  380 MET A CG  
3007 S SD  . MET A 380 ? 0.26048 0.24096 0.23485 0.01085  -0.01664 0.00994  380 MET A SD  
3008 C CE  . MET A 380 ? 0.24254 0.22304 0.22101 0.01235  -0.02089 0.01243  380 MET A CE  
3009 N N   . GLU A 381 ? 0.15599 0.14853 0.15279 0.01446  -0.01892 0.00412  381 GLU A N   
3010 C CA  . GLU A 381 ? 0.11502 0.10931 0.11960 0.01643  -0.01893 0.00318  381 GLU A CA  
3011 C C   . GLU A 381 ? 0.13536 0.13321 0.14370 0.01627  -0.01607 0.00032  381 GLU A C   
3012 O O   . GLU A 381 ? 0.13768 0.13649 0.15060 0.01753  -0.01431 -0.00129 381 GLU A O   
3013 C CB  . GLU A 381 ? 0.14006 0.13595 0.14915 0.01758  -0.02291 0.00468  381 GLU A CB  
3014 C CG  . GLU A 381 ? 0.21038 0.20270 0.21618 0.01789  -0.02597 0.00809  381 GLU A CG  
3015 C CD  . GLU A 381 ? 0.25553 0.24972 0.26367 0.01837  -0.03054 0.01005  381 GLU A CD  
3016 O OE1 . GLU A 381 ? 0.24830 0.24673 0.26070 0.01833  -0.03126 0.00847  381 GLU A OE1 
3017 O OE2 . GLU A 381 ? 0.36063 0.35220 0.36640 0.01866  -0.03353 0.01334  381 GLU A OE2 
3018 N N   . VAL A 382 ? 0.13450 0.13427 0.14091 0.01460  -0.01548 -0.00040 382 VAL A N   
3019 C CA  . VAL A 382 ? 0.10014 0.10300 0.10934 0.01404  -0.01257 -0.00254 382 VAL A CA  
3020 C C   . VAL A 382 ? 0.11368 0.11459 0.11901 0.01355  -0.00937 -0.00324 382 VAL A C   
3021 O O   . VAL A 382 ? 0.09144 0.09413 0.09946 0.01398  -0.00696 -0.00484 382 VAL A O   
3022 C CB  . VAL A 382 ? 0.10461 0.10963 0.11337 0.01224  -0.01309 -0.00285 382 VAL A CB  
3023 C CG1 . VAL A 382 ? 0.12409 0.13193 0.13524 0.01132  -0.00993 -0.00446 382 VAL A CG1 
3024 C CG2 . VAL A 382 ? 0.13645 0.14413 0.14985 0.01269  -0.01651 -0.00240 382 VAL A CG2 
3025 N N   . PHE A 383 ? 0.09441 0.09193 0.09345 0.01263  -0.00935 -0.00212 383 PHE A N   
3026 C CA  . PHE A 383 ? 0.10312 0.09888 0.09883 0.01222  -0.00680 -0.00256 383 PHE A CA  
3027 C C   . PHE A 383 ? 0.13087 0.12551 0.12849 0.01361  -0.00618 -0.00306 383 PHE A C   
3028 O O   . PHE A 383 ? 0.12332 0.11864 0.12110 0.01357  -0.00389 -0.00447 383 PHE A O   
3029 C CB  . PHE A 383 ? 0.13502 0.12768 0.12462 0.01114  -0.00702 -0.00135 383 PHE A CB  
3030 C CG  . PHE A 383 ? 0.09259 0.08579 0.07997 0.00963  -0.00617 -0.00175 383 PHE A CG  
3031 C CD1 . PHE A 383 ? 0.09185 0.08781 0.08232 0.00903  -0.00630 -0.00250 383 PHE A CD1 
3032 C CD2 . PHE A 383 ? 0.09281 0.08372 0.07568 0.00880  -0.00517 -0.00144 383 PHE A CD2 
3033 C CE1 . PHE A 383 ? 0.09161 0.08750 0.08056 0.00757  -0.00559 -0.00282 383 PHE A CE1 
3034 C CE2 . PHE A 383 ? 0.09249 0.08346 0.07408 0.00761  -0.00443 -0.00193 383 PHE A CE2 
3035 C CZ  . PHE A 383 ? 0.09201 0.08520 0.07656 0.00696  -0.00471 -0.00257 383 PHE A CZ  
3036 N N   . GLU A 384 ? 0.14067 0.13343 0.13963 0.01475  -0.00833 -0.00187 384 GLU A N   
3037 C CA  . GLU A 384 ? 0.15717 0.14818 0.15847 0.01604  -0.00788 -0.00242 384 GLU A CA  
3038 C C   . GLU A 384 ? 0.14622 0.14033 0.15347 0.01722  -0.00644 -0.00502 384 GLU A C   
3039 O O   . GLU A 384 ? 0.18255 0.17585 0.19116 0.01787  -0.00499 -0.00666 384 GLU A O   
3040 C CB  . GLU A 384 ? 0.19532 0.18352 0.19757 0.01701  -0.01073 -0.00017 384 GLU A CB  
3041 C CG  . GLU A 384 ? 0.27089 0.25702 0.26713 0.01568  -0.01228 0.00243  384 GLU A CG  
3042 C CD  . GLU A 384 ? 0.29354 0.27554 0.28624 0.01527  -0.01247 0.00437  384 GLU A CD  
3043 O OE1 . GLU A 384 ? 0.40250 0.38232 0.39755 0.01629  -0.01442 0.00610  384 GLU A OE1 
3044 O OE2 . GLU A 384 ? 0.29152 0.27253 0.27943 0.01388  -0.01073 0.00434  384 GLU A OE2 
3045 N N   . GLU A 385 ? 0.11275 0.11063 0.12371 0.01736  -0.00669 -0.00569 385 GLU A N   
3046 C CA  . GLU A 385 ? 0.14167 0.14322 0.15862 0.01839  -0.00492 -0.00834 385 GLU A CA  
3047 C C   . GLU A 385 ? 0.15559 0.15901 0.16989 0.01712  -0.00148 -0.01019 385 GLU A C   
3048 O O   . GLU A 385 ? 0.15967 0.16447 0.17633 0.01781  0.00058  -0.01268 385 GLU A O   
3049 C CB  . GLU A 385 ? 0.16656 0.17205 0.18876 0.01871  -0.00621 -0.00834 385 GLU A CB  
3050 C CG  . GLU A 385 ? 0.13925 0.14897 0.16918 0.02011  -0.00460 -0.01107 385 GLU A CG  
3051 C CD  . GLU A 385 ? 0.26101 0.27499 0.29690 0.02035  -0.00613 -0.01089 385 GLU A CD  
3052 O OE1 . GLU A 385 ? 0.30033 0.31325 0.33488 0.01993  -0.00935 -0.00854 385 GLU A OE1 
3053 O OE2 . GLU A 385 ? 0.20366 0.22233 0.24555 0.02081  -0.00408 -0.01322 385 GLU A OE2 
3054 N N   . HIS A 386 ? 0.10611 0.10949 0.11543 0.01524  -0.00090 -0.00903 386 HIS A N   
3055 C CA  . HIS A 386 ? 0.11519 0.12105 0.12261 0.01388  0.00194  -0.01009 386 HIS A CA  
3056 C C   . HIS A 386 ? 0.08874 0.09209 0.09015 0.01286  0.00292  -0.00955 386 HIS A C   
3057 O O   . HIS A 386 ? 0.11467 0.11982 0.11467 0.01215  0.00513  -0.01069 386 HIS A O   
3058 C CB  . HIS A 386 ? 0.11364 0.12198 0.12149 0.01243  0.00197  -0.00918 386 HIS A CB  
3059 C CG  . HIS A 386 ? 0.08809 0.10022 0.10262 0.01310  0.00143  -0.01002 386 HIS A CG  
3060 N ND1 . HIS A 386 ? 0.11122 0.12780 0.13011 0.01323  0.00390  -0.01206 386 HIS A ND1 
3061 C CD2 . HIS A 386 ? 0.17042 0.18294 0.18821 0.01360  -0.00132 -0.00914 386 HIS A CD2 
3062 C CE1 . HIS A 386 ? 0.10229 0.12194 0.12760 0.01391  0.00278  -0.01246 386 HIS A CE1 
3063 N NE2 . HIS A 386 ? 0.13535 0.15258 0.16011 0.01415  -0.00062 -0.01062 386 HIS A NE2 
3064 N N   . LEU A 387 ? 0.08889 0.08851 0.08676 0.01268  0.00137  -0.00783 387 LEU A N   
3065 C CA  . LEU A 387 ? 0.08857 0.08625 0.08163 0.01175  0.00221  -0.00731 387 LEU A CA  
3066 C C   . LEU A 387 ? 0.08946 0.08662 0.08263 0.01232  0.00318  -0.00900 387 LEU A C   
3067 O O   . LEU A 387 ? 0.14377 0.13918 0.13926 0.01350  0.00227  -0.00956 387 LEU A O   
3068 C CB  . LEU A 387 ? 0.08888 0.08312 0.07882 0.01146  0.00062  -0.00539 387 LEU A CB  
3069 C CG  . LEU A 387 ? 0.08841 0.08240 0.07609 0.01036  0.00014  -0.00408 387 LEU A CG  
3070 C CD1 . LEU A 387 ? 0.08949 0.08030 0.07395 0.01019  -0.00098 -0.00276 387 LEU A CD1 
3071 C CD2 . LEU A 387 ? 0.08738 0.08247 0.07330 0.00924  0.00180  -0.00406 387 LEU A CD2 
3072 N N   . ILE A 388 ? 0.11553 0.11405 0.10616 0.01140  0.00482  -0.00974 388 ILE A N   
3073 C CA  . ILE A 388 ? 0.10291 0.10095 0.09305 0.01164  0.00552  -0.01161 388 ILE A CA  
3074 C C   . ILE A 388 ? 0.13368 0.12817 0.12155 0.01143  0.00440  -0.01051 388 ILE A C   
3075 O O   . ILE A 388 ? 0.13823 0.13160 0.12649 0.01165  0.00449  -0.01203 388 ILE A O   
3076 C CB  . ILE A 388 ? 0.14189 0.14303 0.12961 0.01055  0.00742  -0.01279 388 ILE A CB  
3077 C CG1 . ILE A 388 ? 0.13221 0.13323 0.11591 0.00917  0.00730  -0.01038 388 ILE A CG1 
3078 C CG2 . ILE A 388 ? 0.12538 0.13048 0.11575 0.01065  0.00909  -0.01433 388 ILE A CG2 
3079 C CD1 . ILE A 388 ? 0.12764 0.13147 0.10833 0.00797  0.00871  -0.01086 388 ILE A CD1 
3080 N N   . ASP A 389 ? 0.12144 0.11421 0.10724 0.01093  0.00346  -0.00814 389 ASP A N   
3081 C CA  . ASP A 389 ? 0.09948 0.08929 0.08351 0.01063  0.00270  -0.00700 389 ASP A CA  
3082 C C   . ASP A 389 ? 0.09104 0.07822 0.07602 0.01122  0.00124  -0.00558 389 ASP A C   
3083 O O   . ASP A 389 ? 0.09156 0.07654 0.07459 0.01070  0.00080  -0.00415 389 ASP A O   
3084 C CB  . ASP A 389 ? 0.08893 0.07890 0.06983 0.00959  0.00301  -0.00559 389 ASP A CB  
3085 C CG  . ASP A 389 ? 0.08808 0.07841 0.06840 0.00934  0.00277  -0.00426 389 ASP A CG  
3086 O OD1 . ASP A 389 ? 0.09296 0.08334 0.07488 0.00983  0.00206  -0.00416 389 ASP A OD1 
3087 O OD2 . ASP A 389 ? 0.08745 0.07797 0.06605 0.00864  0.00314  -0.00338 389 ASP A OD2 
3088 N N   . GLN A 390 ? 0.09170 0.07934 0.07972 0.01223  0.00046  -0.00587 390 GLN A N   
3089 C CA  . GLN A 390 ? 0.09340 0.07880 0.08237 0.01284  -0.00139 -0.00420 390 GLN A CA  
3090 C C   . GLN A 390 ? 0.10513 0.08709 0.09335 0.01267  -0.00190 -0.00320 390 GLN A C   
3091 O O   . GLN A 390 ? 0.10027 0.08112 0.09115 0.01325  -0.00176 -0.00448 390 GLN A O   
3092 C CB  . GLN A 390 ? 0.10607 0.09268 0.09996 0.01430  -0.00222 -0.00511 390 GLN A CB  
3093 C CG  . GLN A 390 ? 0.15520 0.13954 0.15060 0.01511  -0.00466 -0.00306 390 GLN A CG  
3094 C CD  . GLN A 390 ? 0.21177 0.19293 0.20969 0.01595  -0.00528 -0.00299 390 GLN A CD  
3095 O OE1 . GLN A 390 ? 0.20290 0.18108 0.20013 0.01597  -0.00705 -0.00047 390 GLN A OE1 
3096 N NE2 . GLN A 390 ? 0.14172 0.12343 0.14246 0.01651  -0.00383 -0.00577 390 GLN A NE2 
3097 N N   . ASP A 391 ? 0.15988 0.14019 0.14463 0.01175  -0.00232 -0.00111 391 ASP A N   
3098 C CA  . ASP A 391 ? 0.10523 0.08251 0.08899 0.01118  -0.00256 0.00031  391 ASP A CA  
3099 C C   . ASP A 391 ? 0.11381 0.08931 0.09593 0.01109  -0.00424 0.00301  391 ASP A C   
3100 O O   . ASP A 391 ? 0.10724 0.08373 0.08624 0.01052  -0.00443 0.00381  391 ASP A O   
3101 C CB  . ASP A 391 ? 0.10075 0.07832 0.08164 0.00988  -0.00106 0.00025  391 ASP A CB  
3102 C CG  . ASP A 391 ? 0.12025 0.09521 0.10087 0.00904  -0.00093 0.00145  391 ASP A CG  
3103 O OD1 . ASP A 391 ? 0.11789 0.09102 0.09670 0.00856  -0.00159 0.00377  391 ASP A OD1 
3104 O OD2 . ASP A 391 ? 0.13480 0.10971 0.11689 0.00866  -0.00019 0.00011  391 ASP A OD2 
3105 N N   . HIS A 392 ? 0.13266 0.10543 0.11686 0.01157  -0.00556 0.00440  392 HIS A N   
3106 C CA  . HIS A 392 ? 0.12082 0.09184 0.10359 0.01155  -0.00764 0.00743  392 HIS A CA  
3107 C C   . HIS A 392 ? 0.13304 0.10413 0.10982 0.00992  -0.00714 0.00912  392 HIS A C   
3108 O O   . HIS A 392 ? 0.15679 0.12900 0.13099 0.00976  -0.00829 0.00994  392 HIS A O   
3109 C CB  . HIS A 392 ? 0.19790 0.16521 0.18336 0.01184  -0.00870 0.00914  392 HIS A CB  
3110 C CG  . HIS A 392 ? 0.24094 0.20625 0.22536 0.01196  -0.01130 0.01278  392 HIS A CG  
3111 N ND1 . HIS A 392 ? 0.28642 0.25202 0.27467 0.01368  -0.01377 0.01330  392 HIS A ND1 
3112 C CD2 . HIS A 392 ? 0.27778 0.24103 0.25772 0.01049  -0.01189 0.01622  392 HIS A CD2 
3113 C CE1 . HIS A 392 ? 0.24278 0.20643 0.22880 0.01332  -0.01615 0.01714  392 HIS A CE1 
3114 N NE2 . HIS A 392 ? 0.25703 0.21920 0.23760 0.01129  -0.01495 0.01901  392 HIS A NE2 
3115 N N   . TYR A 393 ? 0.14552 0.11570 0.12028 0.00862  -0.00534 0.00933  393 TYR A N   
3116 C CA  . TYR A 393 ? 0.11331 0.08363 0.08279 0.00707  -0.00441 0.01069  393 TYR A CA  
3117 C C   . TYR A 393 ? 0.10812 0.08118 0.07558 0.00685  -0.00311 0.00864  393 TYR A C   
3118 O O   . TYR A 393 ? 0.11002 0.08362 0.07337 0.00603  -0.00304 0.00921  393 TYR A O   
3119 C CB  . TYR A 393 ? 0.11267 0.08145 0.08168 0.00573  -0.00274 0.01154  393 TYR A CB  
3120 C CG  . TYR A 393 ? 0.13364 0.09905 0.10396 0.00544  -0.00398 0.01427  393 TYR A CG  
3121 C CD1 . TYR A 393 ? 0.15480 0.11869 0.12258 0.00528  -0.00598 0.01739  393 TYR A CD1 
3122 C CD2 . TYR A 393 ? 0.11952 0.08314 0.09371 0.00525  -0.00339 0.01383  393 TYR A CD2 
3123 C CE1 . TYR A 393 ? 0.14127 0.10168 0.11050 0.00500  -0.00733 0.02043  393 TYR A CE1 
3124 C CE2 . TYR A 393 ? 0.18693 0.14694 0.16290 0.00490  -0.00457 0.01643  393 TYR A CE2 
3125 C CZ  . TYR A 393 ? 0.17671 0.13497 0.15027 0.00483  -0.00654 0.01994  393 TYR A CZ  
3126 O OH  . TYR A 393 ? 0.20074 0.15502 0.17634 0.00448  -0.00790 0.02303  393 TYR A OH  
3127 N N   . LEU A 394 ? 0.12794 0.10266 0.09811 0.00747  -0.00211 0.00629  394 LEU A N   
3128 C CA  . LEU A 394 ? 0.10135 0.07820 0.07014 0.00724  -0.00096 0.00473  394 LEU A CA  
3129 C C   . LEU A 394 ? 0.10123 0.07930 0.06971 0.00770  -0.00232 0.00434  394 LEU A C   
3130 O O   . LEU A 394 ? 0.10182 0.08056 0.06759 0.00707  -0.00204 0.00397  394 LEU A O   
3131 C CB  . LEU A 394 ? 0.09772 0.07594 0.06920 0.00759  0.00024  0.00292  394 LEU A CB  
3132 C CG  . LEU A 394 ? 0.09779 0.07521 0.07033 0.00706  0.00124  0.00295  394 LEU A CG  
3133 C CD1 . LEU A 394 ? 0.09477 0.07403 0.06921 0.00726  0.00206  0.00119  394 LEU A CD1 
3134 C CD2 . LEU A 394 ? 0.13911 0.11595 0.10906 0.00588  0.00241  0.00408  394 LEU A CD2 
3135 N N   . ASN A 395 ? 0.10071 0.07923 0.07243 0.00877  -0.00375 0.00416  395 ASN A N   
3136 C CA  . ASN A 395 ? 0.10074 0.08082 0.07313 0.00915  -0.00526 0.00386  395 ASN A CA  
3137 C C   . ASN A 395 ? 0.11726 0.09646 0.08601 0.00851  -0.00702 0.00560  395 ASN A C   
3138 O O   . ASN A 395 ? 0.10585 0.08626 0.07281 0.00797  -0.00763 0.00499  395 ASN A O   
3139 C CB  . ASN A 395 ? 0.09982 0.08075 0.07723 0.01054  -0.00627 0.00333  395 ASN A CB  
3140 C CG  . ASN A 395 ? 0.12611 0.10994 0.10618 0.01090  -0.00649 0.00189  395 ASN A CG  
3141 O OD1 . ASN A 395 ? 0.13697 0.12175 0.11771 0.01104  -0.00839 0.00242  395 ASN A OD1 
3142 N ND2 . ASN A 395 ? 0.18206 0.16751 0.16362 0.01088  -0.00461 0.00023  395 ASN A ND2 
3143 N N   . ALA A 396 ? 0.11436 0.09138 0.08172 0.00836  -0.00785 0.00780  396 ALA A N   
3144 C CA  . ALA A 396 ? 0.15739 0.13357 0.12025 0.00748  -0.00954 0.00994  396 ALA A CA  
3145 C C   . ALA A 396 ? 0.13316 0.10981 0.09067 0.00596  -0.00789 0.00913  396 ALA A C   
3146 O O   . ALA A 396 ? 0.12489 0.10252 0.07927 0.00531  -0.00904 0.00882  396 ALA A O   
3147 C CB  . ALA A 396 ? 0.16289 0.13632 0.12508 0.00730  -0.01020 0.01283  396 ALA A CB  
3148 N N   . ALA A 397 ? 0.14543 0.12146 0.10208 0.00535  -0.00524 0.00867  397 ALA A N   
3149 C CA  . ALA A 397 ? 0.15035 0.12677 0.10249 0.00402  -0.00331 0.00788  397 ALA A CA  
3150 C C   . ALA A 397 ? 0.12093 0.09899 0.07320 0.00407  -0.00286 0.00519  397 ALA A C   
3151 O O   . ALA A 397 ? 0.11685 0.09533 0.06504 0.00309  -0.00274 0.00435  397 ALA A O   
3152 C CB  . ALA A 397 ? 0.17622 0.15218 0.12917 0.00360  -0.00060 0.00772  397 ALA A CB  
3153 N N   . ASN A 398 ? 0.10841 0.08735 0.06523 0.00505  -0.00256 0.00377  398 ASN A N   
3154 C CA  . ASN A 398 ? 0.11950 0.09958 0.07700 0.00495  -0.00200 0.00156  398 ASN A CA  
3155 C C   . ASN A 398 ? 0.10836 0.08930 0.06541 0.00477  -0.00435 0.00119  398 ASN A C   
3156 O O   . ASN A 398 ? 0.10920 0.09059 0.06516 0.00411  -0.00415 -0.00059 398 ASN A O   
3157 C CB  . ASN A 398 ? 0.10187 0.08270 0.06389 0.00579  -0.00098 0.00068  398 ASN A CB  
3158 C CG  . ASN A 398 ? 0.10042 0.08093 0.06285 0.00574  0.00128  0.00040  398 ASN A CG  
3159 O OD1 . ASN A 398 ? 0.10032 0.08097 0.06243 0.00545  0.00265  -0.00083 398 ASN A OD1 
3160 N ND2 . ASN A 398 ? 0.09955 0.07965 0.06328 0.00604  0.00154  0.00140  398 ASN A ND2 
3161 N N   . TRP A 399 ? 0.10913 0.09034 0.06757 0.00536  -0.00669 0.00271  399 TRP A N   
3162 C CA  . TRP A 399 ? 0.11128 0.09372 0.06950 0.00510  -0.00932 0.00254  399 TRP A CA  
3163 C C   . TRP A 399 ? 0.13820 0.12013 0.09014 0.00377  -0.01029 0.00293  399 TRP A C   
3164 O O   . TRP A 399 ? 0.11918 0.10215 0.06955 0.00294  -0.01157 0.00151  399 TRP A O   
3165 C CB  . TRP A 399 ? 0.13366 0.11677 0.09582 0.00630  -0.01171 0.00411  399 TRP A CB  
3166 C CG  . TRP A 399 ? 0.10683 0.09184 0.07497 0.00719  -0.01140 0.00276  399 TRP A CG  
3167 C CD1 . TRP A 399 ? 0.12056 0.10574 0.09272 0.00829  -0.01010 0.00262  399 TRP A CD1 
3168 C CD2 . TRP A 399 ? 0.11842 0.10564 0.08898 0.00679  -0.01217 0.00124  399 TRP A CD2 
3169 N NE1 . TRP A 399 ? 0.13477 0.12235 0.11132 0.00859  -0.00984 0.00122  399 TRP A NE1 
3170 C CE2 . TRP A 399 ? 0.10145 0.09027 0.07742 0.00765  -0.01108 0.00052  399 TRP A CE2 
3171 C CE3 . TRP A 399 ? 0.10793 0.09602 0.07664 0.00560  -0.01367 0.00028  399 TRP A CE3 
3172 C CZ2 . TRP A 399 ? 0.09981 0.09112 0.07953 0.00729  -0.01125 -0.00075 399 TRP A CZ2 
3173 C CZ3 . TRP A 399 ? 0.10613 0.09644 0.07898 0.00528  -0.01410 -0.00114 399 TRP A CZ3 
3174 C CH2 . TRP A 399 ? 0.12073 0.11267 0.09914 0.00608  -0.01279 -0.00147 399 TRP A CH2 
3175 N N   . MET A 400 ? 0.12012 0.10059 0.06827 0.00334  -0.00964 0.00479  400 MET A N   
3176 C CA  . MET A 400 ? 0.15873 0.13899 0.09996 0.00180  -0.00997 0.00513  400 MET A CA  
3177 C C   . MET A 400 ? 0.16771 0.14822 0.10653 0.00086  -0.00722 0.00203  400 MET A C   
3178 O O   . MET A 400 ? 0.17821 0.15931 0.11239 -0.00039 -0.00775 0.00058  400 MET A O   
3179 C CB  . MET A 400 ? 0.14824 0.12692 0.08629 0.00136  -0.00958 0.00823  400 MET A CB  
3180 C CG  . MET A 400 ? 0.16353 0.14152 0.10272 0.00202  -0.01297 0.01161  400 MET A CG  
3181 S SD  . MET A 400 ? 0.21906 0.19469 0.15403 0.00104  -0.01263 0.01575  400 MET A SD  
3182 C CE  . MET A 400 ? 0.14034 0.11459 0.08113 0.00200  -0.00952 0.01521  400 MET A CE  
3183 N N   . TRP A 401 ? 0.13747 0.11760 0.07962 0.00148  -0.00441 0.00087  401 TRP A N   
3184 C CA  . TRP A 401 ? 0.19387 0.17411 0.13555 0.00103  -0.00185 -0.00210 401 TRP A CA  
3185 C C   . TRP A 401 ? 0.16939 0.15024 0.11260 0.00086  -0.00305 -0.00456 401 TRP A C   
3186 O O   . TRP A 401 ? 0.13917 0.12007 0.07908 -0.00019 -0.00262 -0.00695 401 TRP A O   
3187 C CB  . TRP A 401 ? 0.13355 0.11346 0.07972 0.00200  0.00057  -0.00228 401 TRP A CB  
3188 C CG  . TRP A 401 ? 0.15823 0.13812 0.10501 0.00188  0.00322  -0.00487 401 TRP A CG  
3189 C CD1 . TRP A 401 ? 0.21341 0.19322 0.16218 0.00196  0.00337  -0.00735 401 TRP A CD1 
3190 C CD2 . TRP A 401 ? 0.18743 0.16738 0.13381 0.00175  0.00608  -0.00522 401 TRP A CD2 
3191 N NE1 . TRP A 401 ? 0.19624 0.17580 0.14593 0.00208  0.00605  -0.00924 401 TRP A NE1 
3192 C CE2 . TRP A 401 ? 0.22267 0.20262 0.17105 0.00199  0.00779  -0.00805 401 TRP A CE2 
3193 C CE3 . TRP A 401 ? 0.21206 0.19210 0.15712 0.00138  0.00736  -0.00339 401 TRP A CE3 
3194 C CZ2 . TRP A 401 ? 0.25531 0.23568 0.20470 0.00211  0.01071  -0.00923 401 TRP A CZ2 
3195 C CZ3 . TRP A 401 ? 0.18092 0.16162 0.12679 0.00123  0.01039  -0.00454 401 TRP A CZ3 
3196 C CH2 . TRP A 401 ? 0.32053 0.30156 0.26869 0.00170  0.01202  -0.00749 401 TRP A CH2 
3197 N N   . LEU A 402 ? 0.14780 0.12918 0.09614 0.00174  -0.00441 -0.00420 402 LEU A N   
3198 C CA  . LEU A 402 ? 0.14926 0.13125 0.10012 0.00140  -0.00535 -0.00627 402 LEU A CA  
3199 C C   . LEU A 402 ? 0.14577 0.12870 0.09358 0.00032  -0.00823 -0.00681 402 LEU A C   
3200 O O   . LEU A 402 ? 0.12250 0.10568 0.07098 -0.00053 -0.00877 -0.00926 402 LEU A O   
3201 C CB  . LEU A 402 ? 0.12847 0.11129 0.08546 0.00240  -0.00579 -0.00544 402 LEU A CB  
3202 C CG  . LEU A 402 ? 0.10759 0.08986 0.06831 0.00284  -0.00351 -0.00629 402 LEU A CG  
3203 C CD1 . LEU A 402 ? 0.13033 0.11182 0.09136 0.00193  -0.00301 -0.00882 402 LEU A CD1 
3204 C CD2 . LEU A 402 ? 0.12927 0.11061 0.08915 0.00346  -0.00126 -0.00557 402 LEU A CD2 
3205 N N   . SER A 403 ? 0.16977 0.15316 0.11451 0.00026  -0.01030 -0.00450 403 SER A N   
3206 C CA  . SER A 403 ? 0.13760 0.12217 0.07892 -0.00082 -0.01353 -0.00460 403 SER A CA  
3207 C C   . SER A 403 ? 0.15012 0.13425 0.08348 -0.00237 -0.01293 -0.00563 403 SER A C   
3208 O O   . SER A 403 ? 0.17599 0.16120 0.10510 -0.00350 -0.01577 -0.00556 403 SER A O   
3209 C CB  . SER A 403 ? 0.15451 0.13990 0.09706 0.00002  -0.01661 -0.00119 403 SER A CB  
3210 O OG  . SER A 403 ? 0.19524 0.17919 0.13505 0.00039  -0.01564 0.00149  403 SER A OG  
3211 N N   . ALA A 404 ? 0.16787 0.15078 0.09921 -0.00250 -0.00932 -0.00668 404 ALA A N   
3212 C CA  . ALA A 404 ? 0.18684 0.16967 0.11060 -0.00399 -0.00793 -0.00778 404 ALA A CA  
3213 C C   . ALA A 404 ? 0.21169 0.19493 0.12977 -0.00470 -0.01007 -0.00417 404 ALA A C   
3214 O O   . ALA A 404 ? 0.22830 0.21229 0.13911 -0.00637 -0.01091 -0.00468 404 ALA A O   
3215 C CB  . ALA A 404 ? 0.23350 0.21684 0.15460 -0.00537 -0.00829 -0.01199 404 ALA A CB  
3216 N N   . SER A 405 ? 0.14487 0.12751 0.06621 -0.00348 -0.01105 -0.00045 405 SER A N   
3217 C CA  . SER A 405 ? 0.20688 0.18927 0.12380 -0.00399 -0.01307 0.00361  405 SER A CA  
3218 C C   . SER A 405 ? 0.23268 0.21380 0.14713 -0.00438 -0.00992 0.00554  405 SER A C   
3219 O O   . SER A 405 ? 0.26355 0.24442 0.17202 -0.00561 -0.01069 0.00845  405 SER A O   
3220 C CB  . SER A 405 ? 0.22237 0.20469 0.14493 -0.00242 -0.01649 0.00659  405 SER A CB  
3221 O OG  . SER A 405 ? 0.16264 0.14669 0.08781 -0.00225 -0.01954 0.00504  405 SER A OG  
3222 N N   . ALA A 406 ? 0.22197 0.20243 0.14096 -0.00349 -0.00654 0.00422  406 ALA A N   
3223 C CA  . ALA A 406 ? 0.22460 0.20432 0.14202 -0.00404 -0.00332 0.00555  406 ALA A CA  
3224 C C   . ALA A 406 ? 0.21306 0.19306 0.13436 -0.00345 0.00041  0.00224  406 ALA A C   
3225 O O   . ALA A 406 ? 0.22338 0.20346 0.15003 -0.00220 0.00016  0.00019  406 ALA A O   
3226 C CB  . ALA A 406 ? 0.29410 0.27225 0.21493 -0.00320 -0.00435 0.00956  406 ALA A CB  
3227 N N   . PHE A 407 ? 0.28662 0.26695 0.20534 -0.00443 0.00386  0.00192  407 PHE A N   
3228 C CA  . PHE A 407 ? 0.25861 0.23945 0.18140 -0.00382 0.00746  -0.00078 407 PHE A CA  
3229 C C   . PHE A 407 ? 0.26149 0.24295 0.18485 -0.00360 0.00833  -0.00525 407 PHE A C   
3230 O O   . PHE A 407 ? 0.44562 0.42790 0.36855 -0.00395 0.01162  -0.00794 407 PHE A O   
3231 C CB  . PHE A 407 ? 0.25326 0.23332 0.18355 -0.00215 0.00723  0.00034  407 PHE A CB  
3232 C CG  . PHE A 407 ? 0.22655 0.20547 0.15736 -0.00221 0.00597  0.00430  407 PHE A CG  
3233 C CD1 . PHE A 407 ? 0.22775 0.20661 0.15643 -0.00345 0.00804  0.00622  407 PHE A CD1 
3234 C CD2 . PHE A 407 ? 0.22188 0.19981 0.15592 -0.00106 0.00289  0.00596  407 PHE A CD2 
3235 C CE1 . PHE A 407 ? 0.27361 0.25090 0.20330 -0.00361 0.00681  0.00988  407 PHE A CE1 
3236 C CE2 . PHE A 407 ? 0.26512 0.24160 0.20034 -0.00097 0.00174  0.00928  407 PHE A CE2 
3237 C CZ  . PHE A 407 ? 0.24757 0.22347 0.18064 -0.00227 0.00359  0.01131  407 PHE A CZ  
3238 N N   . PHE A 408 ? 0.28079 0.26189 0.20577 -0.00303 0.00552  -0.00620 408 PHE A N   
3239 C CA  . PHE A 408 ? 0.25517 0.23636 0.18126 -0.00297 0.00596  -0.01030 408 PHE A CA  
3240 C C   . PHE A 408 ? 0.30654 0.28832 0.22610 -0.00453 0.00405  -0.01171 408 PHE A C   
3241 O O   . PHE A 408 ? 0.26626 0.24828 0.18326 -0.00497 0.00072  -0.00920 408 PHE A O   
3242 C CB  . PHE A 408 ? 0.29585 0.27636 0.22889 -0.00153 0.00433  -0.01048 408 PHE A CB  
3243 C CG  . PHE A 408 ? 0.22585 0.20589 0.16134 -0.00145 0.00490  -0.01432 408 PHE A CG  
3244 C CD1 . PHE A 408 ? 0.17709 0.15669 0.11554 -0.00087 0.00799  -0.01667 408 PHE A CD1 
3245 C CD2 . PHE A 408 ? 0.21080 0.19080 0.14646 -0.00195 0.00220  -0.01548 408 PHE A CD2 
3246 C CE1 . PHE A 408 ? 0.25799 0.23660 0.19936 -0.00073 0.00840  -0.02007 408 PHE A CE1 
3247 C CE2 . PHE A 408 ? 0.26191 0.24105 0.20033 -0.00207 0.00268  -0.01895 408 PHE A CE2 
3248 C CZ  . PHE A 408 ? 0.21074 0.18892 0.15200 -0.00142 0.00578  -0.02120 408 PHE A CZ  
3249 N N   . SER A 409 ? 0.29250 0.27461 0.20961 -0.00535 0.00603  -0.01590 409 SER A N   
3250 C CA  . SER A 409 ? 0.29722 0.28014 0.20731 -0.00714 0.00444  -0.01789 409 SER A CA  
3251 C C   . SER A 409 ? 0.28371 0.26614 0.19549 -0.00736 0.00463  -0.02304 409 SER A C   
3252 O O   . SER A 409 ? 0.21734 0.20050 0.12344 -0.00898 0.00316  -0.02536 409 SER A O   
3253 C CB  . SER A 409 ? 0.31348 0.29768 0.21546 -0.00882 0.00691  -0.01795 409 SER A CB  
3254 O OG  . SER A 409 ? 0.34901 0.33346 0.25289 -0.00849 0.01158  -0.02101 409 SER A OG  
3255 N N   . GLN A 410 ? 0.24248 0.22359 0.16188 -0.00590 0.00618  -0.02480 410 GLN A N   
3256 C CA  . GLN A 410 ? 0.21194 0.19196 0.13386 -0.00610 0.00644  -0.02956 410 GLN A CA  
3257 C C   . GLN A 410 ? 0.15176 0.13131 0.07710 -0.00616 0.00252  -0.02882 410 GLN A C   
3258 O O   . GLN A 410 ? 0.17969 0.15806 0.11230 -0.00497 0.00224  -0.02817 410 GLN A O   
3259 C CB  . GLN A 410 ? 0.22823 0.20689 0.15696 -0.00454 0.00979  -0.03143 410 GLN A CB  
3260 C CG  . GLN A 410 ? 0.23168 0.20870 0.16315 -0.00475 0.01043  -0.03652 410 GLN A CG  
3261 C CD  . GLN A 410 ? 0.24685 0.22472 0.17074 -0.00672 0.01071  -0.04071 410 GLN A CD  
3262 O OE1 . GLN A 410 ? 0.29446 0.27191 0.21696 -0.00796 0.00808  -0.04285 410 GLN A OE1 
3263 N NE2 . GLN A 410 ? 0.28302 0.26238 0.20187 -0.00720 0.01393  -0.04199 410 GLN A NE2 
3264 N N   . TYR A 411 ? 0.20906 0.18986 0.12899 -0.00770 -0.00060 -0.02882 411 TYR A N   
3265 C CA  . TYR A 411 ? 0.20440 0.18551 0.12748 -0.00798 -0.00454 -0.02814 411 TYR A CA  
3266 C C   . TYR A 411 ? 0.18907 0.16893 0.11559 -0.00874 -0.00480 -0.03276 411 TYR A C   
3267 O O   . TYR A 411 ? 0.23947 0.21974 0.16939 -0.00923 -0.00786 -0.03258 411 TYR A O   
3268 C CB  . TYR A 411 ? 0.23568 0.21888 0.15218 -0.00932 -0.00822 -0.02626 411 TYR A CB  
3269 C CG  . TYR A 411 ? 0.25996 0.24400 0.16760 -0.01136 -0.00799 -0.02955 411 TYR A CG  
3270 C CD1 . TYR A 411 ? 0.28977 0.27400 0.19626 -0.01294 -0.00972 -0.03399 411 TYR A CD1 
3271 C CD2 . TYR A 411 ? 0.24987 0.23467 0.15017 -0.01194 -0.00595 -0.02834 411 TYR A CD2 
3272 C CE1 . TYR A 411 ? 0.29637 0.28158 0.19419 -0.01495 -0.00948 -0.03745 411 TYR A CE1 
3273 C CE2 . TYR A 411 ? 0.33682 0.32278 0.22828 -0.01402 -0.00547 -0.03146 411 TYR A CE2 
3274 C CZ  . TYR A 411 ? 0.33724 0.32343 0.22726 -0.01548 -0.00727 -0.03617 411 TYR A CZ  
3275 O OH  . TYR A 411 ? 0.41954 0.40709 0.30020 -0.01770 -0.00677 -0.03973 411 TYR A OH  
3276 N N   . PHE A 412 ? 0.20104 0.17940 0.12733 -0.00888 -0.00164 -0.03700 412 PHE A N   
3277 C CA  . PHE A 412 ? 0.18584 0.16221 0.11689 -0.00938 -0.00166 -0.04126 412 PHE A CA  
3278 C C   . PHE A 412 ? 0.21048 0.18476 0.15093 -0.00773 -0.00059 -0.03972 412 PHE A C   
3279 O O   . PHE A 412 ? 0.24047 0.21296 0.18613 -0.00820 -0.00134 -0.04187 412 PHE A O   
3280 C CB  . PHE A 412 ? 0.23558 0.21096 0.16325 -0.01010 0.00127  -0.04688 412 PHE A CB  
3281 C CG  . PHE A 412 ? 0.26237 0.23975 0.18040 -0.01230 -0.00005 -0.04946 412 PHE A CG  
3282 C CD1 . PHE A 412 ? 0.28197 0.25947 0.19876 -0.01421 -0.00319 -0.05268 412 PHE A CD1 
3283 C CD2 . PHE A 412 ? 0.23950 0.21879 0.14960 -0.01268 0.00182  -0.04867 412 PHE A CD2 
3284 C CE1 . PHE A 412 ? 0.26889 0.24849 0.17622 -0.01639 -0.00471 -0.05511 412 PHE A CE1 
3285 C CE2 . PHE A 412 ? 0.25168 0.23296 0.15211 -0.01491 0.00060  -0.05078 412 PHE A CE2 
3286 C CZ  . PHE A 412 ? 0.29794 0.27943 0.19674 -0.01673 -0.00279 -0.05407 412 PHE A CZ  
3287 N N   . ARG A 413 ? 0.21253 0.18702 0.15514 -0.00599 0.00105  -0.03597 413 ARG A N   
3288 C CA  . ARG A 413 ? 0.20465 0.17762 0.15525 -0.00451 0.00177  -0.03387 413 ARG A CA  
3289 C C   . ARG A 413 ? 0.21127 0.18555 0.16440 -0.00463 -0.00121 -0.03030 413 ARG A C   
3290 O O   . ARG A 413 ? 0.18347 0.15952 0.13508 -0.00396 -0.00191 -0.02668 413 ARG A O   
3291 C CB  . ARG A 413 ? 0.22421 0.19726 0.17581 -0.00276 0.00456  -0.03171 413 ARG A CB  
3292 C CG  . ARG A 413 ? 0.18035 0.15218 0.13938 -0.00130 0.00505  -0.02919 413 ARG A CG  
3293 C CD  . ARG A 413 ? 0.21075 0.17969 0.17530 -0.00104 0.00624  -0.03209 413 ARG A CD  
3294 N NE  . ARG A 413 ? 0.20387 0.17169 0.17500 0.00012  0.00629  -0.02910 413 ARG A NE  
3295 C CZ  . ARG A 413 ? 0.22865 0.19556 0.20382 -0.00049 0.00458  -0.02780 413 ARG A CZ  
3296 N NH1 . ARG A 413 ? 0.23607 0.20309 0.21032 -0.00219 0.00258  -0.02938 413 ARG A NH1 
3297 N NH2 . ARG A 413 ? 0.26076 0.22688 0.24100 0.00046  0.00484  -0.02477 413 ARG A NH2 
3298 N N   . VAL A 414 ? 0.17069 0.14415 0.12819 -0.00555 -0.00283 -0.03146 414 VAL A N   
3299 C CA  . VAL A 414 ? 0.20593 0.18110 0.16657 -0.00591 -0.00545 -0.02871 414 VAL A CA  
3300 C C   . VAL A 414 ? 0.19909 0.17265 0.16725 -0.00545 -0.00455 -0.02744 414 VAL A C   
3301 O O   . VAL A 414 ? 0.13966 0.11087 0.11136 -0.00629 -0.00423 -0.02996 414 VAL A O   
3302 C CB  . VAL A 414 ? 0.21930 0.19578 0.17835 -0.00791 -0.00860 -0.03094 414 VAL A CB  
3303 C CG1 . VAL A 414 ? 0.23645 0.21516 0.20009 -0.00818 -0.01104 -0.02822 414 VAL A CG1 
3304 C CG2 . VAL A 414 ? 0.25059 0.22878 0.20132 -0.00852 -0.00977 -0.03173 414 VAL A CG2 
3305 N N   . TYR A 415 ? 0.15634 0.13109 0.12681 -0.00425 -0.00418 -0.02355 415 TYR A N   
3306 C CA  . TYR A 415 ? 0.20577 0.17950 0.18248 -0.00399 -0.00341 -0.02171 415 TYR A CA  
3307 C C   . TYR A 415 ? 0.20280 0.17719 0.18353 -0.00572 -0.00531 -0.02212 415 TYR A C   
3308 O O   . TYR A 415 ? 0.15001 0.12709 0.12964 -0.00651 -0.00753 -0.02207 415 TYR A O   
3309 C CB  . TYR A 415 ? 0.20618 0.18165 0.18351 -0.00258 -0.00276 -0.01780 415 TYR A CB  
3310 C CG  . TYR A 415 ? 0.27585 0.25102 0.24994 -0.00104 -0.00102 -0.01711 415 TYR A CG  
3311 C CD1 . TYR A 415 ? 0.20702 0.17998 0.18279 -0.00019 0.00104  -0.01762 415 TYR A CD1 
3312 C CD2 . TYR A 415 ? 0.18801 0.16513 0.15804 -0.00048 -0.00155 -0.01580 415 TYR A CD2 
3313 C CE1 . TYR A 415 ? 0.22984 0.20301 0.20340 0.00108  0.00262  -0.01705 415 TYR A CE1 
3314 C CE2 . TYR A 415 ? 0.20214 0.17905 0.16969 0.00062  0.00009  -0.01510 415 TYR A CE2 
3315 C CZ  . TYR A 415 ? 0.25982 0.23499 0.22918 0.00134  0.00223  -0.01582 415 TYR A CZ  
3316 O OH  . TYR A 415 ? 0.24783 0.22326 0.21545 0.00232  0.00389  -0.01521 415 TYR A OH  
3317 N N   . SER A 416 ? 0.13747 0.10943 0.12343 -0.00635 -0.00451 -0.02230 416 SER A N   
3318 C CA  . SER A 416 ? 0.14084 0.11336 0.13149 -0.00827 -0.00599 -0.02244 416 SER A CA  
3319 C C   . SER A 416 ? 0.15191 0.12674 0.14607 -0.00809 -0.00563 -0.01840 416 SER A C   
3320 O O   . SER A 416 ? 0.16743 0.14108 0.16298 -0.00709 -0.00384 -0.01597 416 SER A O   
3321 C CB  . SER A 416 ? 0.17033 0.13876 0.16519 -0.00938 -0.00537 -0.02459 416 SER A CB  
3322 O OG  . SER A 416 ? 0.17813 0.14711 0.17832 -0.01139 -0.00649 -0.02394 416 SER A OG  
3323 N N   . PRO A 417 ? 0.17376 0.15214 0.16960 -0.00907 -0.00727 -0.01772 417 PRO A N   
3324 C CA  . PRO A 417 ? 0.12723 0.10823 0.12662 -0.00903 -0.00649 -0.01434 417 PRO A CA  
3325 C C   . PRO A 417 ? 0.15573 0.13493 0.16048 -0.01051 -0.00533 -0.01306 417 PRO A C   
3326 O O   . PRO A 417 ? 0.18423 0.16544 0.19137 -0.01064 -0.00418 -0.01008 417 PRO A O   
3327 C CB  . PRO A 417 ? 0.15699 0.14236 0.15757 -0.00974 -0.00868 -0.01470 417 PRO A CB  
3328 C CG  . PRO A 417 ? 0.16002 0.14439 0.15981 -0.01122 -0.01087 -0.01820 417 PRO A CG  
3329 C CD  . PRO A 417 ? 0.22838 0.20885 0.22327 -0.01034 -0.00997 -0.02013 417 PRO A CD  
3330 N N   . VAL A 418 ? 0.19951 0.17486 0.20607 -0.01167 -0.00550 -0.01520 418 VAL A N   
3331 C CA  . VAL A 418 ? 0.16041 0.13316 0.17241 -0.01323 -0.00459 -0.01383 418 VAL A CA  
3332 C C   . VAL A 418 ? 0.17037 0.13873 0.18212 -0.01188 -0.00295 -0.01276 418 VAL A C   
3333 O O   . VAL A 418 ? 0.24727 0.21490 0.26142 -0.01195 -0.00172 -0.00920 418 VAL A O   
3334 C CB  . VAL A 418 ? 0.19707 0.16825 0.21272 -0.01568 -0.00618 -0.01707 418 VAL A CB  
3335 C CG1 . VAL A 418 ? 0.23965 0.20631 0.26067 -0.01705 -0.00517 -0.01607 418 VAL A CG1 
3336 C CG2 . VAL A 418 ? 0.20628 0.18230 0.22449 -0.01740 -0.00778 -0.01710 418 VAL A CG2 
3337 N N   . VAL A 419 ? 0.15192 0.11762 0.16079 -0.01063 -0.00292 -0.01576 419 VAL A N   
3338 C CA  . VAL A 419 ? 0.20876 0.17011 0.21897 -0.00940 -0.00156 -0.01544 419 VAL A CA  
3339 C C   . VAL A 419 ? 0.12216 0.08474 0.12922 -0.00702 -0.00033 -0.01274 419 VAL A C   
3340 O O   . VAL A 419 ? 0.15204 0.11217 0.16131 -0.00608 0.00062  -0.01058 419 VAL A O   
3341 C CB  . VAL A 419 ? 0.18084 0.13900 0.19022 -0.00925 -0.00174 -0.02045 419 VAL A CB  
3342 C CG1 . VAL A 419 ? 0.15166 0.10545 0.16354 -0.00766 -0.00026 -0.02045 419 VAL A CG1 
3343 C CG2 . VAL A 419 ? 0.21034 0.16720 0.22306 -0.01182 -0.00318 -0.02337 419 VAL A CG2 
3344 N N   . PHE A 420 ? 0.14448 0.11075 0.14673 -0.00606 -0.00052 -0.01269 420 PHE A N   
3345 C CA  . PHE A 420 ? 0.14354 0.11059 0.14263 -0.00388 0.00056  -0.01120 420 PHE A CA  
3346 C C   . PHE A 420 ? 0.15455 0.12198 0.15561 -0.00347 0.00134  -0.00690 420 PHE A C   
3347 O O   . PHE A 420 ? 0.15276 0.11839 0.15444 -0.00211 0.00211  -0.00569 420 PHE A O   
3348 C CB  . PHE A 420 ? 0.17326 0.14396 0.16747 -0.00326 0.00002  -0.01161 420 PHE A CB  
3349 C CG  . PHE A 420 ? 0.15984 0.13123 0.15093 -0.00130 0.00107  -0.01048 420 PHE A CG  
3350 C CD1 . PHE A 420 ? 0.18497 0.15467 0.17408 -0.00026 0.00190  -0.01266 420 PHE A CD1 
3351 C CD2 . PHE A 420 ? 0.16406 0.13798 0.15440 -0.00064 0.00136  -0.00752 420 PHE A CD2 
3352 C CE1 . PHE A 420 ? 0.17768 0.14827 0.16458 0.00131  0.00291  -0.01161 420 PHE A CE1 
3353 C CE2 . PHE A 420 ? 0.13472 0.10925 0.12262 0.00093  0.00216  -0.00668 420 PHE A CE2 
3354 C CZ  . PHE A 420 ? 0.18662 0.15952 0.17298 0.00186  0.00288  -0.00858 420 PHE A CZ  
3355 N N   . GLY A 421 ? 0.15245 0.12255 0.15452 -0.00468 0.00113  -0.00459 421 GLY A N   
3356 C CA  . GLY A 421 ? 0.13946 0.11048 0.14237 -0.00460 0.00194  -0.00055 421 GLY A CA  
3357 C C   . GLY A 421 ? 0.12936 0.09701 0.13665 -0.00563 0.00214  0.00161  421 GLY A C   
3358 O O   . GLY A 421 ? 0.15670 0.12418 0.16411 -0.00520 0.00262  0.00507  421 GLY A O   
3359 N N   . LYS A 422 ? 0.16689 0.13172 0.17778 -0.00708 0.00160  -0.00028 422 LYS A N   
3360 C CA  . LYS A 422 ? 0.16629 0.12722 0.18207 -0.00820 0.00167  0.00189  422 LYS A CA  
3361 C C   . LYS A 422 ? 0.18433 0.14155 0.20116 -0.00620 0.00184  0.00255  422 LYS A C   
3362 O O   . LYS A 422 ? 0.20396 0.15859 0.22408 -0.00650 0.00181  0.00605  422 LYS A O   
3363 C CB  . LYS A 422 ? 0.21288 0.17133 0.23261 -0.01019 0.00094  -0.00105 422 LYS A CB  
3364 C CG  . LYS A 422 ? 0.19870 0.15239 0.22435 -0.01160 0.00090  0.00094  422 LYS A CG  
3365 C CD  . LYS A 422 ? 0.28949 0.24063 0.31910 -0.01364 0.00007  -0.00276 422 LYS A CD  
3366 C CE  . LYS A 422 ? 0.23725 0.19286 0.26685 -0.01594 -0.00038 -0.00316 422 LYS A CE  
3367 N NZ  . LYS A 422 ? 0.16997 0.12335 0.20377 -0.01821 -0.00151 -0.00683 422 LYS A NZ  
3368 N N   . LYS A 423 ? 0.18500 0.14209 0.19934 -0.00419 0.00201  -0.00053 423 LYS A N   
3369 C CA  . LYS A 423 ? 0.26774 0.22183 0.28403 -0.00216 0.00228  -0.00026 423 LYS A CA  
3370 C C   . LYS A 423 ? 0.15828 0.11434 0.17313 -0.00101 0.00233  0.00421  423 LYS A C   
3371 O O   . LYS A 423 ? 0.19651 0.14996 0.21468 0.00001  0.00203  0.00651  423 LYS A O   
3372 C CB  . LYS A 423 ? 0.23373 0.18771 0.24782 -0.00056 0.00284  -0.00494 423 LYS A CB  
3373 C CG  . LYS A 423 ? 0.27359 0.23175 0.28220 0.00071  0.00326  -0.00485 423 LYS A CG  
3374 C CD  . LYS A 423 ? 0.19579 0.15356 0.20277 0.00222  0.00414  -0.00880 423 LYS A CD  
3375 C CE  . LYS A 423 ? 0.18856 0.14767 0.19158 0.00117  0.00399  -0.01254 423 LYS A CE  
3376 N NZ  . LYS A 423 ? 0.17512 0.13831 0.17391 0.00065  0.00339  -0.01075 423 LYS A NZ  
3377 N N   . TYR A 424 ? 0.15335 0.11393 0.16360 -0.00116 0.00252  0.00544  424 TYR A N   
3378 C CA  . TYR A 424 ? 0.13175 0.09449 0.14020 -0.00043 0.00245  0.00936  424 TYR A CA  
3379 C C   . TYR A 424 ? 0.18530 0.14861 0.19462 -0.00236 0.00233  0.01370  424 TYR A C   
3380 O O   . TYR A 424 ? 0.17832 0.14138 0.18792 -0.00205 0.00188  0.01760  424 TYR A O   
3381 C CB  . TYR A 424 ? 0.16314 0.13030 0.16639 0.00030  0.00284  0.00839  424 TYR A CB  
3382 C CG  . TYR A 424 ? 0.12282 0.08993 0.12445 0.00185  0.00314  0.00460  424 TYR A CG  
3383 C CD1 . TYR A 424 ? 0.15163 0.11814 0.15377 0.00374  0.00327  0.00453  424 TYR A CD1 
3384 C CD2 . TYR A 424 ? 0.15612 0.12412 0.15573 0.00131  0.00326  0.00129  424 TYR A CD2 
3385 C CE1 . TYR A 424 ? 0.13120 0.09799 0.13179 0.00489  0.00394  0.00119  424 TYR A CE1 
3386 C CE2 . TYR A 424 ? 0.14123 0.10932 0.13862 0.00246  0.00365  -0.00180 424 TYR A CE2 
3387 C CZ  . TYR A 424 ? 0.12795 0.09545 0.12581 0.00416  0.00420  -0.00186 424 TYR A CZ  
3388 O OH  . TYR A 424 ? 0.16396 0.13186 0.15958 0.00504  0.00495  -0.00479 424 TYR A OH  
3389 N N   . ASP A 425 ? 0.20244 0.16679 0.21224 -0.00447 0.00268  0.01319  425 ASP A N   
3390 C CA  . ASP A 425 ? 0.16091 0.12726 0.17068 -0.00661 0.00314  0.01699  425 ASP A CA  
3391 C C   . ASP A 425 ? 0.15812 0.12238 0.17232 -0.00898 0.00318  0.01659  425 ASP A C   
3392 O O   . ASP A 425 ? 0.18927 0.15634 0.20338 -0.01041 0.00361  0.01489  425 ASP A O   
3393 C CB  . ASP A 425 ? 0.20142 0.17337 0.20672 -0.00676 0.00397  0.01662  425 ASP A CB  
3394 C CG  . ASP A 425 ? 0.21792 0.19276 0.22269 -0.00893 0.00496  0.02022  425 ASP A CG  
3395 O OD1 . ASP A 425 ? 0.19125 0.16378 0.19848 -0.01042 0.00490  0.02377  425 ASP A OD1 
3396 O OD2 . ASP A 425 ? 0.16616 0.14565 0.16816 -0.00916 0.00589  0.01949  425 ASP A OD2 
3397 N N   . PRO A 426 ? 0.18558 0.14482 0.20439 -0.00948 0.00261  0.01814  426 PRO A N   
3398 C CA  . PRO A 426 ? 0.19640 0.15312 0.22008 -0.01194 0.00254  0.01746  426 PRO A CA  
3399 C C   . PRO A 426 ? 0.21230 0.17184 0.23651 -0.01485 0.00345  0.02103  426 PRO A C   
3400 O O   . PRO A 426 ? 0.26236 0.22152 0.29022 -0.01715 0.00356  0.01979  426 PRO A O   
3401 C CB  . PRO A 426 ? 0.16832 0.11859 0.19704 -0.01141 0.00170  0.01866  426 PRO A CB  
3402 C CG  . PRO A 426 ? 0.24284 0.19335 0.26937 -0.00944 0.00136  0.02235  426 PRO A CG  
3403 C CD  . PRO A 426 ? 0.15589 0.11136 0.17646 -0.00770 0.00181  0.02020  426 PRO A CD  
3404 N N   . GLU A 427 ? 0.20637 0.16896 0.22714 -0.01503 0.00417  0.02526  427 GLU A N   
3405 C CA  . GLU A 427 ? 0.24168 0.20760 0.26250 -0.01794 0.00554  0.02856  427 GLU A CA  
3406 C C   . GLU A 427 ? 0.22227 0.19457 0.24033 -0.01825 0.00674  0.02599  427 GLU A C   
3407 O O   . GLU A 427 ? 0.25212 0.22778 0.27137 -0.02076 0.00816  0.02750  427 GLU A O   
3408 C CB  . GLU A 427 ? 0.19472 0.16117 0.21270 -0.01832 0.00585  0.03439  427 GLU A CB  
3409 C CG  . GLU A 427 ? 0.28903 0.24920 0.31098 -0.01855 0.00454  0.03808  427 GLU A CG  
3410 C CD  . GLU A 427 ? 0.41043 0.36674 0.43900 -0.02107 0.00457  0.03792  427 GLU A CD  
3411 O OE1 . GLU A 427 ? 0.45617 0.41479 0.48567 -0.02422 0.00594  0.04040  427 GLU A OE1 
3412 O OE2 . GLU A 427 ? 0.43885 0.39001 0.47187 -0.02001 0.00335  0.03501  427 GLU A OE2 
3413 N N   . GLY A 428 ? 0.15504 0.12907 0.16995 -0.01577 0.00627  0.02224  428 GLY A N   
3414 C CA  . GLY A 428 ? 0.18997 0.16963 0.20278 -0.01566 0.00713  0.01983  428 GLY A CA  
3415 C C   . GLY A 428 ? 0.18904 0.17338 0.19763 -0.01569 0.00865  0.02227  428 GLY A C   
3416 O O   . GLY A 428 ? 0.20426 0.19347 0.21302 -0.01682 0.01008  0.02166  428 GLY A O   
3417 N N   . ARG A 429 ? 0.18407 0.16729 0.18911 -0.01449 0.00837  0.02480  429 ARG A N   
3418 C CA  . ARG A 429 ? 0.19844 0.18616 0.19882 -0.01468 0.00971  0.02682  429 ARG A CA  
3419 C C   . ARG A 429 ? 0.20614 0.19816 0.20407 -0.01314 0.01030  0.02301  429 ARG A C   
3420 O O   . ARG A 429 ? 0.15705 0.15395 0.15362 -0.01409 0.01210  0.02299  429 ARG A O   
3421 C CB  . ARG A 429 ? 0.22959 0.21526 0.22669 -0.01354 0.00866  0.02992  429 ARG A CB  
3422 C CG  . ARG A 429 ? 0.26392 0.24722 0.26211 -0.01558 0.00855  0.03534  429 ARG A CG  
3423 C CD  . ARG A 429 ? 0.24105 0.21784 0.24364 -0.01475 0.00661  0.03615  429 ARG A CD  
3424 N NE  . ARG A 429 ? 0.25488 0.22897 0.25905 -0.01668 0.00627  0.04178  429 ARG A NE  
3425 C CZ  . ARG A 429 ? 0.26572 0.23933 0.26702 -0.01630 0.00521  0.04613  429 ARG A CZ  
3426 N NH1 . ARG A 429 ? 0.26878 0.24460 0.26570 -0.01413 0.00442  0.04527  429 ARG A NH1 
3427 N NH2 . ARG A 429 ? 0.27171 0.24258 0.27474 -0.01826 0.00476  0.05166  429 ARG A NH2 
3428 N N   . PHE A 430 ? 0.19708 0.18731 0.19460 -0.01079 0.00890  0.01978  430 PHE A N   
3429 C CA  . PHE A 430 ? 0.14676 0.14027 0.14261 -0.00931 0.00914  0.01635  430 PHE A CA  
3430 C C   . PHE A 430 ? 0.10546 0.10226 0.10465 -0.01057 0.00999  0.01457  430 PHE A C   
3431 O O   . PHE A 430 ? 0.18026 0.18148 0.17867 -0.01028 0.01114  0.01327  430 PHE A O   
3432 C CB  . PHE A 430 ? 0.11809 0.10856 0.11342 -0.00706 0.00747  0.01365  430 PHE A CB  
3433 C CG  . PHE A 430 ? 0.13930 0.13229 0.13314 -0.00554 0.00735  0.01052  430 PHE A CG  
3434 C CD1 . PHE A 430 ? 0.16444 0.15908 0.15472 -0.00413 0.00763  0.01026  430 PHE A CD1 
3435 C CD2 . PHE A 430 ? 0.16362 0.15706 0.15983 -0.00554 0.00666  0.00791  430 PHE A CD2 
3436 C CE1 . PHE A 430 ? 0.10265 0.09897 0.09211 -0.00274 0.00740  0.00761  430 PHE A CE1 
3437 C CE2 . PHE A 430 ? 0.10139 0.09679 0.09648 -0.00407 0.00624  0.00556  430 PHE A CE2 
3438 C CZ  . PHE A 430 ? 0.09466 0.09128 0.08656 -0.00265 0.00669  0.00548  430 PHE A CZ  
3439 N N   . ILE A 431 ? 0.15692 0.15172 0.16041 -0.01200 0.00939  0.01433  431 ILE A N   
3440 C CA  . ILE A 431 ? 0.18035 0.17842 0.18791 -0.01332 0.00980  0.01258  431 ILE A CA  
3441 C C   . ILE A 431 ? 0.15966 0.16240 0.16816 -0.01537 0.01228  0.01470  431 ILE A C   
3442 O O   . ILE A 431 ? 0.13354 0.14121 0.14347 -0.01533 0.01337  0.01296  431 ILE A O   
3443 C CB  . ILE A 431 ? 0.19888 0.19350 0.21084 -0.01468 0.00840  0.01177  431 ILE A CB  
3444 C CG1 . ILE A 431 ? 0.18827 0.17934 0.19886 -0.01266 0.00627  0.00881  431 ILE A CG1 
3445 C CG2 . ILE A 431 ? 0.17696 0.17542 0.19396 -0.01661 0.00878  0.01057  431 ILE A CG2 
3446 C CD1 . ILE A 431 ? 0.13399 0.12175 0.14838 -0.01393 0.00483  0.00715  431 ILE A CD1 
3447 N N   . ARG A 432 ? 0.15985 0.16122 0.16767 -0.01719 0.01328  0.01856  432 ARG A N   
3448 C CA  . ARG A 432 ? 0.19466 0.20057 0.20280 -0.01958 0.01596  0.02093  432 ARG A CA  
3449 C C   . ARG A 432 ? 0.15274 0.16333 0.15635 -0.01840 0.01763  0.02016  432 ARG A C   
3450 O O   . ARG A 432 ? 0.13881 0.15481 0.14344 -0.01974 0.02012  0.01994  432 ARG A O   
3451 C CB  . ARG A 432 ? 0.20374 0.20665 0.21129 -0.02178 0.01637  0.02584  432 ARG A CB  
3452 C CG  . ARG A 432 ? 0.23814 0.23602 0.25089 -0.02316 0.01489  0.02654  432 ARG A CG  
3453 C CD  . ARG A 432 ? 0.20802 0.20158 0.22008 -0.02457 0.01465  0.03157  432 ARG A CD  
3454 N NE  . ARG A 432 ? 0.18023 0.16765 0.19714 -0.02498 0.01276  0.03141  432 ARG A NE  
3455 C CZ  . ARG A 432 ? 0.22738 0.21374 0.25004 -0.02778 0.01310  0.03207  432 ARG A CZ  
3456 N NH1 . ARG A 432 ? 0.24906 0.24037 0.27369 -0.03052 0.01536  0.03318  432 ARG A NH1 
3457 N NH2 . ARG A 432 ? 0.35018 0.33047 0.37706 -0.02792 0.01125  0.03136  432 ARG A NH2 
3458 N N   . LYS A 433 ? 0.18753 0.19628 0.18648 -0.01598 0.01642  0.01948  433 LYS A N   
3459 C CA  . LYS A 433 ? 0.20952 0.22227 0.20419 -0.01490 0.01781  0.01835  433 LYS A CA  
3460 C C   . LYS A 433 ? 0.18246 0.19908 0.17989 -0.01364 0.01843  0.01420  433 LYS A C   
3461 O O   . LYS A 433 ? 0.21169 0.23352 0.20917 -0.01424 0.02088  0.01327  433 LYS A O   
3462 C CB  . LYS A 433 ? 0.19892 0.20859 0.18880 -0.01274 0.01606  0.01846  433 LYS A CB  
3463 C CG  . LYS A 433 ? 0.27064 0.28365 0.25672 -0.01119 0.01687  0.01610  433 LYS A CG  
3464 C CD  . LYS A 433 ? 0.27972 0.29773 0.26283 -0.01298 0.01964  0.01724  433 LYS A CD  
3465 C CE  . LYS A 433 ? 0.33847 0.35936 0.31805 -0.01136 0.02033  0.01418  433 LYS A CE  
3466 N NZ  . LYS A 433 ? 0.40323 0.42939 0.37945 -0.01315 0.02330  0.01457  433 LYS A NZ  
3467 N N   . PHE A 434 ? 0.15737 0.17163 0.15721 -0.01188 0.01624  0.01167  434 PHE A N   
3468 C CA  . PHE A 434 ? 0.12027 0.13760 0.12267 -0.01030 0.01616  0.00811  434 PHE A CA  
3469 C C   . PHE A 434 ? 0.14032 0.16021 0.14924 -0.01157 0.01626  0.00709  434 PHE A C   
3470 O O   . PHE A 434 ? 0.16619 0.18983 0.17832 -0.01053 0.01653  0.00452  434 PHE A O   
3471 C CB  . PHE A 434 ? 0.15991 0.17363 0.16069 -0.00770 0.01357  0.00619  434 PHE A CB  
3472 C CG  . PHE A 434 ? 0.15651 0.16842 0.15179 -0.00633 0.01341  0.00665  434 PHE A CG  
3473 C CD1 . PHE A 434 ? 0.16722 0.18202 0.16055 -0.00517 0.01454  0.00501  434 PHE A CD1 
3474 C CD2 . PHE A 434 ? 0.13200 0.13945 0.12467 -0.00619 0.01208  0.00849  434 PHE A CD2 
3475 C CE1 . PHE A 434 ? 0.14670 0.15998 0.13528 -0.00413 0.01418  0.00524  434 PHE A CE1 
3476 C CE2 . PHE A 434 ? 0.15110 0.15739 0.13940 -0.00501 0.01175  0.00891  434 PHE A CE2 
3477 C CZ  . PHE A 434 ? 0.12199 0.13121 0.10811 -0.00409 0.01272  0.00730  434 PHE A CZ  
3478 N N   . LEU A 435 ? 0.15854 0.17650 0.17007 -0.01376 0.01588  0.00895  435 LEU A N   
3479 C CA  . LEU A 435 ? 0.16947 0.19020 0.18764 -0.01556 0.01605  0.00824  435 LEU A CA  
3480 C C   . LEU A 435 ? 0.15321 0.17567 0.17278 -0.01883 0.01861  0.01140  435 LEU A C   
3481 O O   . LEU A 435 ? 0.17494 0.19430 0.19685 -0.02086 0.01787  0.01322  435 LEU A O   
3482 C CB  . LEU A 435 ? 0.17180 0.18844 0.19246 -0.01555 0.01298  0.00715  435 LEU A CB  
3483 C CG  . LEU A 435 ? 0.17094 0.18779 0.19278 -0.01334 0.01042  0.00388  435 LEU A CG  
3484 C CD1 . LEU A 435 ? 0.18204 0.19367 0.20336 -0.01334 0.00762  0.00315  435 LEU A CD1 
3485 C CD2 . LEU A 435 ? 0.26720 0.28971 0.29563 -0.01400 0.01061  0.00221  435 LEU A CD2 
3486 N N   . PRO A 436 ? 0.19985 0.22718 0.21802 -0.01954 0.02175  0.01210  436 PRO A N   
3487 C CA  . PRO A 436 ? 0.17079 0.19991 0.18930 -0.02293 0.02443  0.01565  436 PRO A CA  
3488 C C   . PRO A 436 ? 0.16412 0.19579 0.19036 -0.02561 0.02513  0.01575  436 PRO A C   
3489 O O   . PRO A 436 ? 0.13254 0.16504 0.15970 -0.02881 0.02720  0.01909  436 PRO A O   
3490 C CB  . PRO A 436 ? 0.15080 0.18550 0.16584 -0.02280 0.02774  0.01525  436 PRO A CB  
3491 C CG  . PRO A 436 ? 0.19165 0.22893 0.20853 -0.01978 0.02711  0.01070  436 PRO A CG  
3492 C CD  . PRO A 436 ? 0.11127 0.14280 0.12766 -0.01745 0.02312  0.00951  436 PRO A CD  
3493 N N   . VAL A 437 ? 0.13988 0.17286 0.17178 -0.02461 0.02331  0.01243  437 VAL A N   
3494 C CA  . VAL A 437 ? 0.14521 0.18036 0.18487 -0.02736 0.02346  0.01249  437 VAL A CA  
3495 C C   . VAL A 437 ? 0.21325 0.24194 0.25333 -0.02934 0.02163  0.01493  437 VAL A C   
3496 O O   . VAL A 437 ? 0.19550 0.22500 0.24053 -0.03270 0.02270  0.01678  437 VAL A O   
3497 C CB  . VAL A 437 ? 0.16275 0.20099 0.20834 -0.02572 0.02136  0.00841  437 VAL A CB  
3498 C CG1 . VAL A 437 ? 0.19104 0.22356 0.23433 -0.02338 0.01713  0.00664  437 VAL A CG1 
3499 C CG2 . VAL A 437 ? 0.21614 0.25838 0.27064 -0.02878 0.02189  0.00825  437 VAL A CG2 
3500 N N   . LEU A 438 ? 0.18997 0.21219 0.22525 -0.02739 0.01910  0.01501  438 LEU A N   
3501 C CA  . LEU A 438 ? 0.13957 0.15511 0.17535 -0.02873 0.01732  0.01683  438 LEU A CA  
3502 C C   . LEU A 438 ? 0.16728 0.17948 0.19839 -0.02966 0.01862  0.02140  438 LEU A C   
3503 O O   . LEU A 438 ? 0.22588 0.23164 0.25616 -0.02958 0.01682  0.02276  438 LEU A O   
3504 C CB  . LEU A 438 ? 0.14360 0.15426 0.17758 -0.02605 0.01383  0.01389  438 LEU A CB  
3505 C CG  . LEU A 438 ? 0.17997 0.19236 0.21828 -0.02546 0.01150  0.00980  438 LEU A CG  
3506 C CD1 . LEU A 438 ? 0.23086 0.24063 0.26452 -0.02205 0.00911  0.00720  438 LEU A CD1 
3507 C CD2 . LEU A 438 ? 0.17197 0.18136 0.21571 -0.02809 0.00995  0.00940  438 LEU A CD2 
3508 N N   . LYS A 439 ? 0.17820 0.19475 0.20629 -0.03053 0.02165  0.02372  439 LYS A N   
3509 C CA  . LYS A 439 ? 0.24157 0.25530 0.26416 -0.03119 0.02244  0.02825  439 LYS A CA  
3510 C C   . LYS A 439 ? 0.17234 0.18176 0.19821 -0.03437 0.02229  0.03240  439 LYS A C   
3511 O O   . LYS A 439 ? 0.19289 0.19698 0.21569 -0.03414 0.02112  0.03569  439 LYS A O   
3512 C CB  . LYS A 439 ? 0.27241 0.29233 0.29081 -0.03195 0.02585  0.02967  439 LYS A CB  
3513 C CG  . LYS A 439 ? 0.24137 0.26721 0.26444 -0.03541 0.02919  0.03065  439 LYS A CG  
3514 C CD  . LYS A 439 ? 0.23698 0.26687 0.25460 -0.03734 0.03269  0.03415  439 LYS A CD  
3515 C CE  . LYS A 439 ? 0.22904 0.26158 0.23986 -0.03445 0.03320  0.03184  439 LYS A CE  
3516 N NZ  . LYS A 439 ? 0.22959 0.26708 0.23489 -0.03656 0.03686  0.03448  439 LYS A NZ  
3517 N N   . ASP A 440 ? 0.19625 0.20775 0.22891 -0.03732 0.02330  0.03232  440 ASP A N   
3518 C CA  . ASP A 440 ? 0.24237 0.25015 0.27892 -0.04086 0.02354  0.03645  440 ASP A CA  
3519 C C   . ASP A 440 ? 0.23191 0.23371 0.27416 -0.04093 0.02048  0.03429  440 ASP A C   
3520 O O   . ASP A 440 ? 0.27906 0.27740 0.32604 -0.04399 0.02046  0.03701  440 ASP A O   
3521 C CB  . ASP A 440 ? 0.30629 0.32039 0.34704 -0.04475 0.02704  0.03818  440 ASP A CB  
3522 C CG  . ASP A 440 ? 0.33329 0.35289 0.36793 -0.04540 0.03053  0.04092  440 ASP A CG  
3523 O OD1 . ASP A 440 ? 0.28504 0.30296 0.31217 -0.04310 0.02990  0.04196  440 ASP A OD1 
3524 O OD2 . ASP A 440 ? 0.40302 0.42889 0.44046 -0.04833 0.03397  0.04183  440 ASP A OD2 
3525 N N   . MET A 441 ? 0.18861 0.18910 0.23041 -0.03780 0.01797  0.02944  441 MET A N   
3526 C CA  . MET A 441 ? 0.21027 0.20539 0.25656 -0.03778 0.01510  0.02671  441 MET A CA  
3527 C C   . MET A 441 ? 0.24638 0.23341 0.29073 -0.03695 0.01357  0.02906  441 MET A C   
3528 O O   . MET A 441 ? 0.24506 0.23065 0.28343 -0.03414 0.01317  0.02980  441 MET A O   
3529 C CB  . MET A 441 ? 0.21336 0.21000 0.25870 -0.03474 0.01300  0.02107  441 MET A CB  
3530 C CG  . MET A 441 ? 0.20789 0.20042 0.25764 -0.03511 0.01016  0.01746  441 MET A CG  
3531 S SD  . MET A 441 ? 0.27093 0.26627 0.33019 -0.03954 0.01038  0.01684  441 MET A SD  
3532 C CE  . MET A 441 ? 0.24646 0.25214 0.30650 -0.03946 0.01263  0.01621  441 MET A CE  
3533 N N   . PRO A 442 ? 0.16462 0.14630 0.21441 -0.03928 0.01268  0.03028  442 PRO A N   
3534 C CA  . PRO A 442 ? 0.25953 0.23323 0.30866 -0.03816 0.01107  0.03214  442 PRO A CA  
3535 C C   . PRO A 442 ? 0.21294 0.18387 0.25904 -0.03422 0.00885  0.02755  442 PRO A C   
3536 O O   . PRO A 442 ? 0.18233 0.15570 0.22858 -0.03314 0.00788  0.02252  442 PRO A O   
3537 C CB  . PRO A 442 ? 0.25256 0.22153 0.30962 -0.04147 0.01040  0.03266  442 PRO A CB  
3538 C CG  . PRO A 442 ? 0.20644 0.18152 0.26717 -0.04517 0.01262  0.03404  442 PRO A CG  
3539 C CD  . PRO A 442 ? 0.18055 0.16340 0.23792 -0.04329 0.01331  0.03045  442 PRO A CD  
3540 N N   . ALA A 443 ? 0.14408 0.10999 0.18761 -0.03217 0.00800  0.02956  443 ALA A N   
3541 C CA  . ALA A 443 ? 0.16594 0.12987 0.20601 -0.02838 0.00643  0.02580  443 ALA A CA  
3542 C C   . ALA A 443 ? 0.22121 0.18180 0.26501 -0.02812 0.00469  0.02027  443 ALA A C   
3543 O O   . ALA A 443 ? 0.26867 0.22987 0.30931 -0.02554 0.00374  0.01602  443 ALA A O   
3544 C CB  . ALA A 443 ? 0.20064 0.15983 0.23882 -0.02652 0.00581  0.02923  443 ALA A CB  
3545 N N   . LYS A 444 ? 0.21304 0.17015 0.26337 -0.03096 0.00427  0.02021  444 LYS A N   
3546 C CA  . LYS A 444 ? 0.23661 0.19015 0.29046 -0.03100 0.00251  0.01467  444 LYS A CA  
3547 C C   . LYS A 444 ? 0.17888 0.13793 0.23095 -0.03074 0.00184  0.00979  444 LYS A C   
3548 O O   . LYS A 444 ? 0.24665 0.20403 0.29792 -0.02943 0.00027  0.00471  444 LYS A O   
3549 C CB  . LYS A 444 ? 0.28778 0.23695 0.34946 -0.03458 0.00224  0.01572  444 LYS A CB  
3550 C CG  . LYS A 444 ? 0.29992 0.24498 0.36575 -0.03511 0.00039  0.00975  444 LYS A CG  
3551 C CD  . LYS A 444 ? 0.33696 0.27476 0.41032 -0.03755 0.00005  0.01147  444 LYS A CD  
3552 C CE  . LYS A 444 ? 0.30313 0.23755 0.38137 -0.03898 -0.00168 0.00517  444 LYS A CE  
3553 N NZ  . LYS A 444 ? 0.29586 0.23445 0.37837 -0.04287 -0.00188 0.00425  444 LYS A NZ  
3554 N N   . TYR A 445 ? 0.25389 0.21968 0.30522 -0.03186 0.00300  0.01127  445 TYR A N   
3555 C CA  . TYR A 445 ? 0.18534 0.15656 0.23648 -0.03187 0.00210  0.00721  445 TYR A CA  
3556 C C   . TYR A 445 ? 0.20248 0.17944 0.24781 -0.02935 0.00289  0.00742  445 TYR A C   
3557 O O   . TYR A 445 ? 0.20068 0.18249 0.24609 -0.02914 0.00210  0.00464  445 TYR A O   
3558 C CB  . TYR A 445 ? 0.16419 0.13881 0.22189 -0.03569 0.00253  0.00778  445 TYR A CB  
3559 C CG  . TYR A 445 ? 0.24041 0.20937 0.30466 -0.03872 0.00200  0.00820  445 TYR A CG  
3560 C CD1 . TYR A 445 ? 0.24571 0.21107 0.31284 -0.03928 -0.00036 0.00322  445 TYR A CD1 
3561 C CD2 . TYR A 445 ? 0.25253 0.21962 0.32001 -0.04118 0.00382  0.01355  445 TYR A CD2 
3562 C CE1 . TYR A 445 ? 0.22564 0.18544 0.29927 -0.04210 -0.00089 0.00318  445 TYR A CE1 
3563 C CE2 . TYR A 445 ? 0.21822 0.17958 0.29230 -0.04405 0.00325  0.01414  445 TYR A CE2 
3564 C CZ  . TYR A 445 ? 0.25350 0.21112 0.33093 -0.04444 0.00089  0.00874  445 TYR A CZ  
3565 O OH  . TYR A 445 ? 0.37330 0.32485 0.45777 -0.04733 0.00028  0.00887  445 TYR A OH  
3566 N N   . ILE A 446 ? 0.16918 0.14572 0.20980 -0.02744 0.00420  0.01055  446 ILE A N   
3567 C CA  . ILE A 446 ? 0.19654 0.17874 0.23244 -0.02555 0.00521  0.01088  446 ILE A CA  
3568 C C   . ILE A 446 ? 0.21366 0.19667 0.24596 -0.02279 0.00350  0.00660  446 ILE A C   
3569 O O   . ILE A 446 ? 0.19701 0.18508 0.22734 -0.02165 0.00374  0.00569  446 ILE A O   
3570 C CB  . ILE A 446 ? 0.18592 0.16753 0.21748 -0.02443 0.00679  0.01510  446 ILE A CB  
3571 C CG1 . ILE A 446 ? 0.17876 0.16682 0.20662 -0.02336 0.00830  0.01549  446 ILE A CG1 
3572 C CG2 . ILE A 446 ? 0.16617 0.14265 0.19434 -0.02170 0.00558  0.01443  446 ILE A CG2 
3573 C CD1 . ILE A 446 ? 0.20901 0.19743 0.23231 -0.02269 0.00980  0.01937  446 ILE A CD1 
3574 N N   . TYR A 447 ? 0.23610 0.21421 0.26761 -0.02174 0.00187  0.00392  447 TYR A N   
3575 C CA  . TYR A 447 ? 0.17654 0.15544 0.20455 -0.01968 0.00025  -0.00007 447 TYR A CA  
3576 C C   . TYR A 447 ? 0.21769 0.19822 0.24888 -0.02129 -0.00169 -0.00366 447 TYR A C   
3577 O O   . TYR A 447 ? 0.19067 0.17349 0.21900 -0.01994 -0.00317 -0.00635 447 TYR A O   
3578 C CB  . TYR A 447 ? 0.23697 0.21051 0.26201 -0.01773 -0.00027 -0.00154 447 TYR A CB  
3579 C CG  . TYR A 447 ? 0.20641 0.17944 0.22744 -0.01548 0.00102  0.00125  447 TYR A CG  
3580 C CD1 . TYR A 447 ? 0.14016 0.11589 0.15616 -0.01316 0.00104  0.00049  447 TYR A CD1 
3581 C CD2 . TYR A 447 ? 0.17743 0.14728 0.19997 -0.01580 0.00198  0.00479  447 TYR A CD2 
3582 C CE1 . TYR A 447 ? 0.13855 0.11399 0.15123 -0.01131 0.00202  0.00279  447 TYR A CE1 
3583 C CE2 . TYR A 447 ? 0.17641 0.14617 0.19540 -0.01386 0.00274  0.00732  447 TYR A CE2 
3584 C CZ  . TYR A 447 ? 0.15249 0.12516 0.16662 -0.01167 0.00279  0.00612  447 TYR A CZ  
3585 O OH  . TYR A 447 ? 0.19157 0.16428 0.20252 -0.00994 0.00338  0.00843  447 TYR A OH  
3586 N N   . GLU A 448 ? 0.22786 0.20732 0.26496 -0.02425 -0.00189 -0.00357 448 GLU A N   
3587 C CA  . GLU A 448 ? 0.19951 0.18054 0.24044 -0.02622 -0.00400 -0.00703 448 GLU A CA  
3588 C C   . GLU A 448 ? 0.25780 0.24225 0.30545 -0.02936 -0.00311 -0.00494 448 GLU A C   
3589 O O   . GLU A 448 ? 0.22330 0.20509 0.27636 -0.03218 -0.00359 -0.00546 448 GLU A O   
3590 C CB  . GLU A 448 ? 0.25344 0.22847 0.29533 -0.02697 -0.00550 -0.01042 448 GLU A CB  
3591 C CG  . GLU A 448 ? 0.31610 0.28815 0.35167 -0.02411 -0.00608 -0.01298 448 GLU A CG  
3592 C CD  . GLU A 448 ? 0.33736 0.30319 0.37440 -0.02479 -0.00682 -0.01629 448 GLU A CD  
3593 O OE1 . GLU A 448 ? 0.41268 0.37402 0.45383 -0.02576 -0.00573 -0.01442 448 GLU A OE1 
3594 O OE2 . GLU A 448 ? 0.37844 0.34385 0.41254 -0.02439 -0.00850 -0.02081 448 GLU A OE2 
3595 N N   . PRO A 449 ? 0.19392 0.18438 0.24180 -0.02908 -0.00166 -0.00276 449 PRO A N   
3596 C CA  . PRO A 449 ? 0.19381 0.18794 0.24809 -0.03217 -0.00005 -0.00039 449 PRO A CA  
3597 C C   . PRO A 449 ? 0.22323 0.21958 0.28418 -0.03487 -0.00210 -0.00324 449 PRO A C   
3598 O O   . PRO A 449 ? 0.26288 0.26005 0.33019 -0.03818 -0.00102 -0.00160 449 PRO A O   
3599 C CB  . PRO A 449 ? 0.21990 0.22046 0.27231 -0.03065 0.00184  0.00132  449 PRO A CB  
3600 C CG  . PRO A 449 ? 0.19578 0.19696 0.24289 -0.02727 -0.00001 -0.00137 449 PRO A CG  
3601 C CD  . PRO A 449 ? 0.18696 0.18122 0.22976 -0.02607 -0.00130 -0.00263 449 PRO A CD  
3602 N N   . TRP A 450 ? 0.17578 0.17312 0.23542 -0.03376 -0.00515 -0.00733 450 TRP A N   
3603 C CA  . TRP A 450 ? 0.17675 0.17629 0.24249 -0.03637 -0.00769 -0.01034 450 TRP A CA  
3604 C C   . TRP A 450 ? 0.16952 0.16297 0.23877 -0.03916 -0.00842 -0.01162 450 TRP A C   
3605 O O   . TRP A 450 ? 0.15994 0.15510 0.23595 -0.04229 -0.00984 -0.01325 450 TRP A O   
3606 C CB  . TRP A 450 ? 0.22776 0.22949 0.29013 -0.03448 -0.01116 -0.01418 450 TRP A CB  
3607 C CG  . TRP A 450 ? 0.18009 0.17601 0.23512 -0.03244 -0.01243 -0.01649 450 TRP A CG  
3608 C CD1 . TRP A 450 ? 0.28883 0.28040 0.34343 -0.03365 -0.01462 -0.02025 450 TRP A CD1 
3609 C CD2 . TRP A 450 ? 0.19153 0.18569 0.23889 -0.02896 -0.01138 -0.01551 450 TRP A CD2 
3610 N NE1 . TRP A 450 ? 0.17588 0.16334 0.22295 -0.03109 -0.01472 -0.02164 450 TRP A NE1 
3611 C CE2 . TRP A 450 ? 0.18781 0.17680 0.23054 -0.02824 -0.01282 -0.01863 450 TRP A CE2 
3612 C CE3 . TRP A 450 ? 0.20935 0.20591 0.25348 -0.02652 -0.00931 -0.01255 450 TRP A CE3 
3613 C CZ2 . TRP A 450 ? 0.26538 0.25183 0.30078 -0.02523 -0.01212 -0.01858 450 TRP A CZ2 
3614 C CZ3 . TRP A 450 ? 0.23382 0.22753 0.27068 -0.02358 -0.00892 -0.01254 450 TRP A CZ3 
3615 C CH2 . TRP A 450 ? 0.22202 0.21087 0.25477 -0.02299 -0.01028 -0.01539 450 TRP A CH2 
3616 N N   . THR A 451 ? 0.16864 0.15507 0.23416 -0.03812 -0.00756 -0.01101 451 THR A N   
3617 C CA  . THR A 451 ? 0.26587 0.24573 0.33512 -0.04043 -0.00820 -0.01244 451 THR A CA  
3618 C C   . THR A 451 ? 0.20415 0.18207 0.27920 -0.04322 -0.00574 -0.00796 451 THR A C   
3619 O O   . THR A 451 ? 0.17554 0.14778 0.25502 -0.04547 -0.00620 -0.00867 451 THR A O   
3620 C CB  . THR A 451 ? 0.18288 0.15600 0.24636 -0.03786 -0.00847 -0.01422 451 THR A CB  
3621 O OG1 . THR A 451 ? 0.21824 0.19012 0.27764 -0.03548 -0.00598 -0.00999 451 THR A OG1 
3622 C CG2 . THR A 451 ? 0.16836 0.14308 0.22600 -0.03569 -0.01086 -0.01873 451 THR A CG2 
3623 N N   . ALA A 452 ? 0.21659 0.19894 0.29162 -0.04323 -0.00312 -0.00343 452 ALA A N   
3624 C CA  . ALA A 452 ? 0.19530 0.17638 0.27494 -0.04608 -0.00057 0.00144  452 ALA A CA  
3625 C C   . ALA A 452 ? 0.17436 0.15912 0.26286 -0.05035 -0.00083 0.00091  452 ALA A C   
3626 O O   . ALA A 452 ? 0.16549 0.15718 0.25598 -0.05054 -0.00176 -0.00132 452 ALA A O   
3627 C CB  . ALA A 452 ? 0.23197 0.21704 0.30759 -0.04473 0.00250  0.00618  452 ALA A CB  
3628 N N   . PRO A 453 ? 0.21406 0.19433 0.30851 -0.05382 -0.00015 0.00299  453 PRO A N   
3629 C CA  . PRO A 453 ? 0.19804 0.18193 0.30161 -0.05828 -0.00016 0.00281  453 PRO A CA  
3630 C C   . PRO A 453 ? 0.23001 0.22297 0.33510 -0.05911 0.00260  0.00588  453 PRO A C   
3631 O O   . PRO A 453 ? 0.26796 0.26262 0.36792 -0.05738 0.00534  0.00975  453 PRO A O   
3632 C CB  . PRO A 453 ? 0.30056 0.27704 0.40901 -0.06146 0.00083  0.00606  453 PRO A CB  
3633 C CG  . PRO A 453 ? 0.24618 0.21429 0.34903 -0.05833 -0.00014 0.00541  453 PRO A CG  
3634 C CD  . PRO A 453 ? 0.22981 0.20136 0.32357 -0.05383 0.00051  0.00573  453 PRO A CD  
3635 N N   . LEU A 454 ? 0.24712 0.24626 0.35962 -0.06181 0.00183  0.00380  454 LEU A N   
3636 C CA  . LEU A 454 ? 0.24940 0.25803 0.36448 -0.06244 0.00446  0.00578  454 LEU A CA  
3637 C C   . LEU A 454 ? 0.31479 0.32368 0.43024 -0.06464 0.00900  0.01211  454 LEU A C   
3638 O O   . LEU A 454 ? 0.30187 0.31710 0.41494 -0.06363 0.01200  0.01434  454 LEU A O   
3639 C CB  . LEU A 454 ? 0.21151 0.22627 0.33626 -0.06553 0.00279  0.00271  454 LEU A CB  
3640 C CG  . LEU A 454 ? 0.22027 0.24589 0.34960 -0.06604 0.00508  0.00355  454 LEU A CG  
3641 C CD1 . LEU A 454 ? 0.23521 0.26504 0.35786 -0.06109 0.00468  0.00199  454 LEU A CD1 
3642 C CD2 . LEU A 454 ? 0.14510 0.17609 0.28514 -0.06935 0.00283  0.00037  454 LEU A CD2 
3643 N N   . GLU A 455 ? 0.27806 0.28001 0.39624 -0.06764 0.00953  0.01506  455 GLU A N   
3644 C CA  . GLU A 455 ? 0.29869 0.30044 0.41674 -0.07004 0.01358  0.02170  455 GLU A CA  
3645 C C   . GLU A 455 ? 0.27398 0.27476 0.38177 -0.06632 0.01532  0.02477  455 GLU A C   
3646 O O   . GLU A 455 ? 0.28756 0.29359 0.39307 -0.06692 0.01895  0.02861  455 GLU A O   
3647 C CB  . GLU A 455 ? 0.31723 0.31042 0.44011 -0.07361 0.01314  0.02435  455 GLU A CB  
3648 C CG  . GLU A 455 ? 0.22300 0.21397 0.34397 -0.07564 0.01670  0.03199  455 GLU A CG  
3649 C CD  . GLU A 455 ? 0.26255 0.24330 0.38734 -0.07813 0.01562  0.03475  455 GLU A CD  
3650 O OE1 . GLU A 455 ? 0.25888 0.23719 0.39220 -0.08124 0.01385  0.03210  455 GLU A OE1 
3651 O OE2 . GLU A 455 ? 0.26622 0.24130 0.38584 -0.07696 0.01635  0.03951  455 GLU A OE2 
3652 N N   . VAL A 456 ? 0.32867 0.32310 0.43023 -0.06257 0.01285  0.02289  456 VAL A N   
3653 C CA  . VAL A 456 ? 0.29260 0.28584 0.38485 -0.05912 0.01413  0.02567  456 VAL A CA  
3654 C C   . VAL A 456 ? 0.27613 0.27747 0.36397 -0.05619 0.01510  0.02358  456 VAL A C   
3655 O O   . VAL A 456 ? 0.31682 0.32080 0.39888 -0.05493 0.01765  0.02671  456 VAL A O   
3656 C CB  . VAL A 456 ? 0.30484 0.28934 0.39272 -0.05601 0.01131  0.02401  456 VAL A CB  
3657 C CG1 . VAL A 456 ? 0.33619 0.31944 0.41529 -0.05280 0.01250  0.02730  456 VAL A CG1 
3658 C CG2 . VAL A 456 ? 0.24699 0.22325 0.34056 -0.05880 0.01021  0.02539  456 VAL A CG2 
3659 N N   . GLN A 457 ? 0.23231 0.23764 0.32285 -0.05507 0.01295  0.01829  457 GLN A N   
3660 C CA  . GLN A 457 ? 0.25930 0.27237 0.34720 -0.05242 0.01375  0.01635  457 GLN A CA  
3661 C C   . GLN A 457 ? 0.23500 0.25581 0.32587 -0.05477 0.01794  0.01935  457 GLN A C   
3662 O O   . GLN A 457 ? 0.21955 0.24458 0.30536 -0.05269 0.02025  0.02031  457 GLN A O   
3663 C CB  . GLN A 457 ? 0.23926 0.25537 0.33099 -0.05144 0.01038  0.01076  457 GLN A CB  
3664 C CG  . GLN A 457 ? 0.24746 0.25756 0.33433 -0.04845 0.00661  0.00720  457 GLN A CG  
3665 C CD  . GLN A 457 ? 0.23306 0.24697 0.32274 -0.04757 0.00323  0.00218  457 GLN A CD  
3666 O OE1 . GLN A 457 ? 0.24375 0.26534 0.33839 -0.04821 0.00365  0.00138  457 GLN A OE1 
3667 N NE2 . GLN A 457 ? 0.30874 0.31752 0.39539 -0.04614 -0.00018 -0.00123 457 GLN A NE2 
3668 N N   . ARG A 458 ? 0.27234 0.29523 0.37156 -0.05927 0.01912  0.02067  458 ARG A N   
3669 C CA  . ARG A 458 ? 0.32611 0.35678 0.42866 -0.06195 0.02357  0.02353  458 ARG A CA  
3670 C C   . ARG A 458 ? 0.30235 0.33089 0.39827 -0.06272 0.02702  0.02934  458 ARG A C   
3671 O O   . ARG A 458 ? 0.34775 0.38274 0.44096 -0.06260 0.03072  0.03091  458 ARG A O   
3672 C CB  . ARG A 458 ? 0.28035 0.31341 0.39382 -0.06694 0.02397  0.02375  458 ARG A CB  
3673 C CG  . ARG A 458 ? 0.22088 0.25801 0.34171 -0.06665 0.02068  0.01816  458 ARG A CG  
3674 C CD  . ARG A 458 ? 0.25682 0.29458 0.38844 -0.07189 0.02044  0.01842  458 ARG A CD  
3675 N NE  . ARG A 458 ? 0.24953 0.29196 0.38858 -0.07189 0.01703  0.01314  458 ARG A NE  
3676 C CZ  . ARG A 458 ? 0.24716 0.29956 0.39390 -0.07303 0.01840  0.01178  458 ARG A CZ  
3677 N NH1 . ARG A 458 ? 0.25401 0.31307 0.40209 -0.07434 0.02355  0.01490  458 ARG A NH1 
3678 N NH2 . ARG A 458 ? 0.24177 0.29783 0.39510 -0.07286 0.01449  0.00710  458 ARG A NH2 
3679 N N   . LYS A 459 ? 0.34182 0.36145 0.43515 -0.06351 0.02581  0.03253  459 LYS A N   
3680 C CA  A LYS A 459 ? 0.29586 0.31300 0.38265 -0.06418 0.02839  0.03852  459 LYS A CA  
3681 C CA  B LYS A 459 ? 0.29585 0.31316 0.38268 -0.06420 0.02844  0.03851  459 LYS A CA  
3682 C C   . LYS A 459 ? 0.28355 0.30128 0.36035 -0.05965 0.02847  0.03800  459 LYS A C   
3683 O O   . LYS A 459 ? 0.29155 0.31076 0.36244 -0.06007 0.03124  0.04222  459 LYS A O   
3684 C CB  A LYS A 459 ? 0.33796 0.34497 0.42546 -0.06573 0.02646  0.04193  459 LYS A CB  
3685 C CB  B LYS A 459 ? 0.33767 0.34502 0.42542 -0.06596 0.02667  0.04209  459 LYS A CB  
3686 C CG  A LYS A 459 ? 0.33664 0.34280 0.42636 -0.07058 0.02947  0.04879  459 LYS A CG  
3687 C CG  B LYS A 459 ? 0.33574 0.34299 0.42640 -0.07103 0.02981  0.04864  459 LYS A CG  
3688 C CD  A LYS A 459 ? 0.38806 0.39694 0.46892 -0.07015 0.03261  0.05380  459 LYS A CD  
3689 C CD  B LYS A 459 ? 0.31795 0.33343 0.41694 -0.07495 0.03249  0.04776  459 LYS A CD  
3690 C CE  A LYS A 459 ? 0.35518 0.35568 0.42895 -0.06764 0.03040  0.05698  459 LYS A CE  
3691 C CE  B LYS A 459 ? 0.34808 0.35953 0.45732 -0.07853 0.03053  0.04682  459 LYS A CE  
3692 N NZ  A LYS A 459 ? 0.25366 0.24655 0.33086 -0.07104 0.02988  0.06280  459 LYS A NZ  
3693 N NZ  B LYS A 459 ? 0.34415 0.34782 0.45440 -0.08192 0.03096  0.05319  459 LYS A NZ  
3694 N N   . ALA A 460 ? 0.31710 0.33375 0.39179 -0.05555 0.02544  0.03301  460 ALA A N   
3695 C CA  . ALA A 460 ? 0.18364 0.20087 0.24969 -0.05128 0.02528  0.03199  460 ALA A CA  
3696 C C   . ALA A 460 ? 0.16762 0.19375 0.23370 -0.04968 0.02707  0.02877  460 ALA A C   
3697 O O   . ALA A 460 ? 0.23443 0.26165 0.29386 -0.04629 0.02720  0.02764  460 ALA A O   
3698 C CB  . ALA A 460 ? 0.19060 0.20121 0.25397 -0.04773 0.02114  0.02872  460 ALA A CB  
3699 N N   . GLY A 461 ? 0.21077 0.24323 0.28479 -0.05197 0.02835  0.02712  461 GLY A N   
3700 C CA  . GLY A 461 ? 0.17184 0.21299 0.24733 -0.05040 0.03016  0.02401  461 GLY A CA  
3701 C C   . GLY A 461 ? 0.24077 0.28179 0.31494 -0.04597 0.02678  0.01905  461 GLY A C   
3702 O O   . GLY A 461 ? 0.23423 0.28040 0.30650 -0.04341 0.02802  0.01698  461 GLY A O   
3703 N N   . CYS A 462 ? 0.20454 0.23968 0.27962 -0.04509 0.02257  0.01705  462 CYS A N   
3704 C CA  . CYS A 462 ? 0.17757 0.21192 0.25075 -0.04118 0.01906  0.01276  462 CYS A CA  
3705 C C   . CYS A 462 ? 0.14700 0.17959 0.22654 -0.04249 0.01543  0.01001  462 CYS A C   
3706 O O   . CYS A 462 ? 0.23955 0.26496 0.31715 -0.04255 0.01288  0.00973  462 CYS A O   
3707 C CB  . CYS A 462 ? 0.18952 0.21732 0.25350 -0.03808 0.01772  0.01331  462 CYS A CB  
3708 S SG  . CYS A 462 ? 0.20081 0.22741 0.26146 -0.03349 0.01381  0.00866  462 CYS A SG  
3709 N N   . VAL A 463 ? 0.17651 0.21588 0.26388 -0.04356 0.01517  0.00778  463 VAL A N   
3710 C CA  . VAL A 463 ? 0.17000 0.20895 0.26367 -0.04486 0.01137  0.00475  463 VAL A CA  
3711 C C   . VAL A 463 ? 0.17860 0.21715 0.26897 -0.04096 0.00749  0.00101  463 VAL A C   
3712 O O   . VAL A 463 ? 0.22232 0.26619 0.31262 -0.03836 0.00784  -0.00019 463 VAL A O   
3713 C CB  . VAL A 463 ? 0.15576 0.20270 0.26009 -0.04796 0.01261  0.00424  463 VAL A CB  
3714 C CG1 . VAL A 463 ? 0.20105 0.24832 0.31168 -0.04898 0.00804  0.00063  463 VAL A CG1 
3715 C CG2 . VAL A 463 ? 0.30588 0.35270 0.41345 -0.05238 0.01643  0.00829  463 VAL A CG2 
3716 N N   . VAL A 464 ? 0.16575 0.19791 0.25335 -0.04058 0.00388  -0.00082 464 VAL A N   
3717 C CA  . VAL A 464 ? 0.18249 0.21420 0.26653 -0.03734 0.00009  -0.00413 464 VAL A CA  
3718 C C   . VAL A 464 ? 0.15229 0.19117 0.24402 -0.03778 -0.00224 -0.00668 464 VAL A C   
3719 O O   . VAL A 464 ? 0.16012 0.20088 0.25935 -0.04108 -0.00335 -0.00759 464 VAL A O   
3720 C CB  . VAL A 464 ? 0.22429 0.24814 0.30403 -0.03733 -0.00293 -0.00586 464 VAL A CB  
3721 C CG1 . VAL A 464 ? 0.23763 0.26149 0.31306 -0.03428 -0.00668 -0.00903 464 VAL A CG1 
3722 C CG2 . VAL A 464 ? 0.22138 0.23848 0.29459 -0.03662 -0.00076 -0.00325 464 VAL A CG2 
3723 N N   . GLY A 465 ? 0.19899 0.24189 0.28936 -0.03444 -0.00317 -0.00780 465 GLY A N   
3724 C CA  . GLY A 465 ? 0.12501 0.17530 0.22302 -0.03420 -0.00538 -0.00982 465 GLY A CA  
3725 C C   . GLY A 465 ? 0.14144 0.19961 0.24604 -0.03430 -0.00166 -0.00872 465 GLY A C   
3726 O O   . GLY A 465 ? 0.16579 0.23061 0.27702 -0.03326 -0.00329 -0.01037 465 GLY A O   
3727 N N   . ARG A 466 ? 0.16490 0.22275 0.26797 -0.03553 0.00324  -0.00602 466 ARG A N   
3728 C CA  . ARG A 466 ? 0.19522 0.26062 0.30350 -0.03576 0.00754  -0.00514 466 ARG A CA  
3729 C C   . ARG A 466 ? 0.22168 0.28577 0.32213 -0.03330 0.01110  -0.00357 466 ARG A C   
3730 O O   . ARG A 466 ? 0.10222 0.17132 0.20402 -0.03068 0.01239  -0.00473 466 ARG A O   
3731 C CB  . ARG A 466 ? 0.24414 0.31212 0.35914 -0.04057 0.01063  -0.00326 466 ARG A CB  
3732 C CG  . ARG A 466 ? 0.23539 0.31222 0.35674 -0.04135 0.01538  -0.00267 466 ARG A CG  
3733 C CD  . ARG A 466 ? 0.23951 0.31890 0.36770 -0.04652 0.01833  -0.00058 466 ARG A CD  
3734 N NE  . ARG A 466 ? 0.36411 0.43641 0.48534 -0.04872 0.02042  0.00308  466 ARG A NE  
3735 C CZ  . ARG A 466 ? 0.31849 0.39097 0.43432 -0.04903 0.02510  0.00606  466 ARG A CZ  
3736 N NH1 . ARG A 466 ? 0.35868 0.43796 0.47481 -0.04735 0.02860  0.00539  466 ARG A NH1 
3737 N NH2 . ARG A 466 ? 0.25942 0.32512 0.36948 -0.05107 0.02620  0.00971  466 ARG A NH2 
3738 N N   . ASP A 467 ? 0.14127 0.19873 0.23393 -0.03404 0.01256  -0.00108 467 ASP A N   
3739 C CA  . ASP A 467 ? 0.16889 0.22443 0.25328 -0.03192 0.01537  0.00047  467 ASP A CA  
3740 C C   . ASP A 467 ? 0.15750 0.20678 0.23363 -0.02843 0.01231  -0.00047 467 ASP A C   
3741 O O   . ASP A 467 ? 0.15099 0.20079 0.22250 -0.02549 0.01332  -0.00085 467 ASP A O   
3742 C CB  . ASP A 467 ? 0.17258 0.22505 0.25358 -0.03490 0.01874  0.00429  467 ASP A CB  
3743 C CG  . ASP A 467 ? 0.20067 0.25913 0.28935 -0.03885 0.02221  0.00578  467 ASP A CG  
3744 O OD1 . ASP A 467 ? 0.20537 0.27166 0.29875 -0.03843 0.02472  0.00450  467 ASP A OD1 
3745 O OD2 . ASP A 467 ? 0.16647 0.22181 0.25690 -0.04241 0.02252  0.00817  467 ASP A OD2 
3746 N N   . TYR A 468 ? 0.14662 0.19008 0.22093 -0.02886 0.00877  -0.00103 468 TYR A N   
3747 C CA  . TYR A 468 ? 0.22561 0.26343 0.29258 -0.02592 0.00590  -0.00210 468 TYR A CA  
3748 C C   . TYR A 468 ? 0.18978 0.22705 0.25949 -0.02582 0.00126  -0.00483 468 TYR A C   
3749 O O   . TYR A 468 ? 0.17853 0.21603 0.25356 -0.02876 0.00006  -0.00538 468 TYR A O   
3750 C CB  . TYR A 468 ? 0.18868 0.21904 0.24892 -0.02649 0.00659  0.00003  468 TYR A CB  
3751 C CG  . TYR A 468 ? 0.12830 0.15359 0.18083 -0.02334 0.00455  -0.00090 468 TYR A CG  
3752 C CD1 . TYR A 468 ? 0.16404 0.19006 0.21159 -0.02050 0.00583  -0.00055 468 TYR A CD1 
3753 C CD2 . TYR A 468 ? 0.16694 0.18690 0.21733 -0.02335 0.00149  -0.00236 468 TYR A CD2 
3754 C CE1 . TYR A 468 ? 0.14191 0.16352 0.18290 -0.01787 0.00409  -0.00128 468 TYR A CE1 
3755 C CE2 . TYR A 468 ? 0.16843 0.18422 0.21194 -0.02066 0.00001  -0.00321 468 TYR A CE2 
3756 C CZ  . TYR A 468 ? 0.10189 0.11856 0.14088 -0.01799 0.00131  -0.00248 468 TYR A CZ  
3757 O OH  . TYR A 468 ? 0.10099 0.11373 0.13363 -0.01557 -0.00005 -0.00321 468 TYR A OH  
3758 N N   . PRO A 469 ? 0.14612 0.18284 0.21236 -0.02271 -0.00148 -0.00652 469 PRO A N   
3759 C CA  . PRO A 469 ? 0.20288 0.23994 0.27129 -0.02268 -0.00610 -0.00897 469 PRO A CA  
3760 C C   . PRO A 469 ? 0.17733 0.20772 0.24155 -0.02404 -0.00824 -0.00982 469 PRO A C   
3761 O O   . PRO A 469 ? 0.20683 0.23158 0.26542 -0.02397 -0.00660 -0.00861 469 PRO A O   
3762 C CB  . PRO A 469 ? 0.20575 0.24354 0.27046 -0.01887 -0.00794 -0.00973 469 PRO A CB  
3763 C CG  . PRO A 469 ? 0.15928 0.19385 0.21723 -0.01708 -0.00483 -0.00808 469 PRO A CG  
3764 C CD  . PRO A 469 ? 0.12863 0.16517 0.18949 -0.01924 -0.00052 -0.00623 469 PRO A CD  
3765 N N   . ALA A 470 ? 0.20928 0.24067 0.27675 -0.02531 -0.01204 -0.01214 470 ALA A N   
3766 C CA  . ALA A 470 ? 0.14536 0.17103 0.20881 -0.02635 -0.01462 -0.01401 470 ALA A CA  
3767 C C   . ALA A 470 ? 0.16287 0.18536 0.21772 -0.02328 -0.01656 -0.01486 470 ALA A C   
3768 O O   . ALA A 470 ? 0.20326 0.22886 0.25705 -0.02072 -0.01731 -0.01441 470 ALA A O   
3769 C CB  . ALA A 470 ? 0.17308 0.20160 0.24284 -0.02893 -0.01818 -0.01651 470 ALA A CB  
3770 N N   . PRO A 471 ? 0.17969 0.19598 0.22862 -0.02349 -0.01723 -0.01608 471 PRO A N   
3771 C CA  . PRO A 471 ? 0.12926 0.14271 0.16985 -0.02086 -0.01869 -0.01682 471 PRO A CA  
3772 C C   . PRO A 471 ? 0.17054 0.18756 0.21102 -0.02025 -0.02300 -0.01848 471 PRO A C   
3773 O O   . PRO A 471 ? 0.24687 0.26552 0.29077 -0.02241 -0.02596 -0.02064 471 PRO A O   
3774 C CB  . PRO A 471 ? 0.21779 0.22465 0.25407 -0.02192 -0.01851 -0.01849 471 PRO A CB  
3775 C CG  . PRO A 471 ? 0.18897 0.19575 0.23202 -0.02536 -0.01881 -0.01963 471 PRO A CG  
3776 C CD  . PRO A 471 ? 0.23779 0.24929 0.28777 -0.02616 -0.01656 -0.01694 471 PRO A CD  
3777 N N   . ILE A 472 ? 0.21500 0.23320 0.25163 -0.01734 -0.02356 -0.01732 472 ILE A N   
3778 C CA  . ILE A 472 ? 0.18539 0.20692 0.22177 -0.01648 -0.02787 -0.01810 472 ILE A CA  
3779 C C   . ILE A 472 ? 0.15811 0.17643 0.18792 -0.01738 -0.03100 -0.02050 472 ILE A C   
3780 O O   . ILE A 472 ? 0.24097 0.26224 0.27114 -0.01777 -0.03526 -0.02156 472 ILE A O   
3781 C CB  . ILE A 472 ? 0.22729 0.25009 0.26130 -0.01314 -0.02757 -0.01597 472 ILE A CB  
3782 C CG1 . ILE A 472 ? 0.17356 0.19110 0.20017 -0.01162 -0.02441 -0.01491 472 ILE A CG1 
3783 C CG2 . ILE A 472 ? 0.26640 0.29466 0.30876 -0.01237 -0.02601 -0.01459 472 ILE A CG2 
3784 C CD1 . ILE A 472 ? 0.17081 0.18809 0.19301 -0.00869 -0.02502 -0.01339 472 ILE A CD1 
3785 N N   . VAL A 473 ? 0.17813 0.19073 0.20192 -0.01768 -0.02905 -0.02146 473 VAL A N   
3786 C CA  . VAL A 473 ? 0.22611 0.23562 0.24363 -0.01875 -0.03133 -0.02438 473 VAL A CA  
3787 C C   . VAL A 473 ? 0.27106 0.27571 0.28880 -0.02063 -0.02901 -0.02638 473 VAL A C   
3788 O O   . VAL A 473 ? 0.24557 0.24826 0.26607 -0.02048 -0.02545 -0.02473 473 VAL A O   
3789 C CB  . VAL A 473 ? 0.19051 0.19766 0.19863 -0.01651 -0.03151 -0.02377 473 VAL A CB  
3790 C CG1 . VAL A 473 ? 0.19120 0.20248 0.19901 -0.01469 -0.03434 -0.02164 473 VAL A CG1 
3791 C CG2 . VAL A 473 ? 0.19048 0.19374 0.19585 -0.01482 -0.02709 -0.02211 473 VAL A CG2 
3792 N N   . ASP A 474 ? 0.18070 0.18340 0.19549 -0.02244 -0.03123 -0.03002 474 ASP A N   
3793 C CA  . ASP A 474 ? 0.28246 0.27949 0.29557 -0.02362 -0.02924 -0.03258 474 ASP A CA  
3794 C C   . ASP A 474 ? 0.19210 0.18561 0.19626 -0.02147 -0.02768 -0.03281 474 ASP A C   
3795 O O   . ASP A 474 ? 0.21762 0.21231 0.21530 -0.02091 -0.02994 -0.03377 474 ASP A O   
3796 C CB  . ASP A 474 ? 0.27369 0.27047 0.28809 -0.02665 -0.03229 -0.03702 474 ASP A CB  
3797 C CG  . ASP A 474 ? 0.28344 0.27408 0.29743 -0.02794 -0.03027 -0.04018 474 ASP A CG  
3798 O OD1 . ASP A 474 ? 0.30372 0.29030 0.31276 -0.02614 -0.02753 -0.04008 474 ASP A OD1 
3799 O OD2 . ASP A 474 ? 0.34137 0.33125 0.36058 -0.03078 -0.03152 -0.04294 474 ASP A OD2 
3800 N N   . HIS A 475 ? 0.26127 0.25069 0.26519 -0.02038 -0.02390 -0.03172 475 HIS A N   
3801 C CA  . HIS A 475 ? 0.21326 0.19996 0.20981 -0.01822 -0.02206 -0.03156 475 HIS A CA  
3802 C C   . HIS A 475 ? 0.20479 0.18893 0.19544 -0.01914 -0.02300 -0.03606 475 HIS A C   
3803 O O   . HIS A 475 ? 0.27729 0.26168 0.26053 -0.01797 -0.02325 -0.03635 475 HIS A O   
3804 C CB  . HIS A 475 ? 0.17554 0.15877 0.17402 -0.01695 -0.01816 -0.02948 475 HIS A CB  
3805 C CG  . HIS A 475 ? 0.18264 0.16373 0.17475 -0.01468 -0.01617 -0.02900 475 HIS A CG  
3806 N ND1 . HIS A 475 ? 0.18569 0.16921 0.17298 -0.01294 -0.01665 -0.02703 475 HIS A ND1 
3807 C CD2 . HIS A 475 ? 0.18527 0.16213 0.17564 -0.01392 -0.01371 -0.03026 475 HIS A CD2 
3808 C CE1 . HIS A 475 ? 0.22165 0.20268 0.20434 -0.01142 -0.01448 -0.02707 475 HIS A CE1 
3809 N NE2 . HIS A 475 ? 0.25889 0.23611 0.24346 -0.01190 -0.01265 -0.02909 475 HIS A NE2 
3810 N N   . ALA A 476 ? 0.25032 0.23193 0.24413 -0.02134 -0.02333 -0.03970 476 ALA A N   
3811 C CA  . ALA A 476 ? 0.24534 0.22460 0.23369 -0.02237 -0.02404 -0.04477 476 ALA A CA  
3812 C C   . ALA A 476 ? 0.28080 0.26406 0.26309 -0.02316 -0.02786 -0.04608 476 ALA A C   
3813 O O   . ALA A 476 ? 0.31260 0.29525 0.28670 -0.02283 -0.02785 -0.04822 476 ALA A O   
3814 C CB  . ALA A 476 ? 0.24664 0.22265 0.24069 -0.02484 -0.02417 -0.04862 476 ALA A CB  
3815 N N   . VAL A 477 ? 0.27798 0.26563 0.26430 -0.02424 -0.03115 -0.04463 477 VAL A N   
3816 C CA  . VAL A 477 ? 0.22586 0.21763 0.20727 -0.02502 -0.03548 -0.04539 477 VAL A CA  
3817 C C   . VAL A 477 ? 0.25950 0.25327 0.23509 -0.02249 -0.03549 -0.04141 477 VAL A C   
3818 O O   . VAL A 477 ? 0.33414 0.32867 0.30129 -0.02250 -0.03717 -0.04228 477 VAL A O   
3819 C CB  . VAL A 477 ? 0.29649 0.29260 0.28551 -0.02688 -0.03911 -0.04504 477 VAL A CB  
3820 C CG1 . VAL A 477 ? 0.29448 0.29568 0.27955 -0.02684 -0.04381 -0.04399 477 VAL A CG1 
3821 C CG2 . VAL A 477 ? 0.30890 0.30312 0.30201 -0.03003 -0.04006 -0.04991 477 VAL A CG2 
3822 N N   . ALA A 478 ? 0.29072 0.28529 0.27060 -0.02043 -0.03358 -0.03700 478 ALA A N   
3823 C CA  . ALA A 478 ? 0.27129 0.26767 0.24702 -0.01807 -0.03377 -0.03314 478 ALA A CA  
3824 C C   . ALA A 478 ? 0.30038 0.29336 0.26810 -0.01676 -0.03087 -0.03333 478 ALA A C   
3825 O O   . ALA A 478 ? 0.27011 0.26416 0.23084 -0.01609 -0.03219 -0.03211 478 ALA A O   
3826 C CB  . ALA A 478 ? 0.20125 0.19928 0.18403 -0.01635 -0.03221 -0.02909 478 ALA A CB  
3827 N N   . SER A 479 ? 0.22379 0.21280 0.19275 -0.01642 -0.02698 -0.03463 479 SER A N   
3828 C CA  . SER A 479 ? 0.24982 0.23606 0.21233 -0.01512 -0.02398 -0.03492 479 SER A CA  
3829 C C   . SER A 479 ? 0.27483 0.26057 0.22927 -0.01658 -0.02502 -0.03891 479 SER A C   
3830 O O   . SER A 479 ? 0.20779 0.19346 0.15490 -0.01579 -0.02405 -0.03826 479 SER A O   
3831 C CB  . SER A 479 ? 0.25783 0.24020 0.22452 -0.01436 -0.01994 -0.03544 479 SER A CB  
3832 O OG  . SER A 479 ? 0.31556 0.29562 0.28552 -0.01622 -0.01995 -0.03951 479 SER A OG  
3833 N N   . LYS A 480 ? 0.28331 0.26883 0.23886 -0.01890 -0.02689 -0.04318 480 LYS A N   
3834 C CA  . LYS A 480 ? 0.34886 0.33444 0.29618 -0.02057 -0.02817 -0.04742 480 LYS A CA  
3835 C C   . LYS A 480 ? 0.35057 0.34004 0.29091 -0.02071 -0.03174 -0.04495 480 LYS A C   
3836 O O   . LYS A 480 ? 0.27650 0.26600 0.20769 -0.02090 -0.03123 -0.04577 480 LYS A O   
3837 C CB  . LYS A 480 ? 0.30245 0.28739 0.25301 -0.02323 -0.03013 -0.05249 480 LYS A CB  
3838 C CG  . LYS A 480 ? 0.28686 0.27124 0.22918 -0.02515 -0.03076 -0.05813 480 LYS A CG  
3839 C CD  . LYS A 480 ? 0.30802 0.28790 0.24930 -0.02449 -0.02596 -0.06181 480 LYS A CD  
3840 C CE  . LYS A 480 ? 0.31270 0.29177 0.24812 -0.02682 -0.02647 -0.06883 480 LYS A CE  
3841 N NZ  . LYS A 480 ? 0.32214 0.29645 0.25984 -0.02626 -0.02197 -0.07330 480 LYS A NZ  
3842 N N   . ALA A 481 ? 0.37214 0.36502 0.31696 -0.02060 -0.03529 -0.04168 481 ALA A N   
3843 C CA  . ALA A 481 ? 0.31400 0.31049 0.25334 -0.02057 -0.03924 -0.03886 481 ALA A CA  
3844 C C   . ALA A 481 ? 0.27386 0.26975 0.20870 -0.01830 -0.03716 -0.03450 481 ALA A C   
3845 O O   . ALA A 481 ? 0.31868 0.31568 0.24500 -0.01861 -0.03875 -0.03330 481 ALA A O   
3846 C CB  . ALA A 481 ? 0.27995 0.28032 0.22697 -0.02066 -0.04333 -0.03648 481 ALA A CB  
3847 N N   . CYS A 482 ? 0.30313 0.29726 0.24344 -0.01620 -0.03367 -0.03202 482 CYS A N   
3848 C CA  . CYS A 482 ? 0.25921 0.25270 0.19623 -0.01415 -0.03172 -0.02801 482 CYS A CA  
3849 C C   . CYS A 482 ? 0.25754 0.24868 0.18628 -0.01445 -0.02853 -0.02993 482 CYS A C   
3850 O O   . CYS A 482 ? 0.29296 0.28452 0.21513 -0.01402 -0.02852 -0.02735 482 CYS A O   
3851 C CB  . CYS A 482 ? 0.25357 0.24597 0.19844 -0.01207 -0.02886 -0.02546 482 CYS A CB  
3852 S SG  . CYS A 482 ? 0.24065 0.23643 0.19538 -0.01141 -0.03173 -0.02278 482 CYS A SG  
3853 N N   . ILE A 483 ? 0.27737 0.26603 0.20680 -0.01520 -0.02566 -0.03438 483 ILE A N   
3854 C CA  . ILE A 483 ? 0.27546 0.26229 0.19790 -0.01547 -0.02227 -0.03691 483 ILE A CA  
3855 C C   . ILE A 483 ? 0.30982 0.29862 0.22213 -0.01745 -0.02470 -0.03843 483 ILE A C   
3856 O O   . ILE A 483 ? 0.33624 0.32521 0.24093 -0.01742 -0.02306 -0.03731 483 ILE A O   
3857 C CB  . ILE A 483 ? 0.26963 0.25338 0.19612 -0.01578 -0.01910 -0.04178 483 ILE A CB  
3858 C CG1 . ILE A 483 ? 0.27900 0.26075 0.21407 -0.01372 -0.01639 -0.03942 483 ILE A CG1 
3859 C CG2 . ILE A 483 ? 0.28350 0.26596 0.20296 -0.01628 -0.01581 -0.04550 483 ILE A CG2 
3860 C CD1 . ILE A 483 ? 0.28992 0.26839 0.23037 -0.01389 -0.01388 -0.04335 483 ILE A CD1 
3861 N N   . ALA A 484 ? 0.29378 0.28437 0.20576 -0.01939 -0.02878 -0.04079 484 ALA A N   
3862 C CA  . ALA A 484 ? 0.30352 0.29631 0.20540 -0.02155 -0.03162 -0.04241 484 ALA A CA  
3863 C C   . ALA A 484 ? 0.36780 0.36306 0.26474 -0.02101 -0.03457 -0.03651 484 ALA A C   
3864 O O   . ALA A 484 ? 0.41084 0.40729 0.29746 -0.02235 -0.03532 -0.03633 484 ALA A O   
3865 C CB  . ALA A 484 ? 0.36236 0.35669 0.26608 -0.02380 -0.03575 -0.04630 484 ALA A CB  
3866 N N   . ARG A 485 ? 0.35617 0.35219 0.26030 -0.01913 -0.03622 -0.03167 485 ARG A N   
3867 C CA  . ARG A 485 ? 0.34452 0.34228 0.24533 -0.01829 -0.03895 -0.02587 485 ARG A CA  
3868 C C   . ARG A 485 ? 0.30963 0.30531 0.20738 -0.01681 -0.03481 -0.02278 485 ARG A C   
3869 O O   . ARG A 485 ? 0.31596 0.31237 0.20670 -0.01705 -0.03608 -0.01916 485 ARG A O   
3870 C CB  . ARG A 485 ? 0.29628 0.29584 0.20665 -0.01678 -0.04231 -0.02241 485 ARG A CB  
3871 C CG  . ARG A 485 ? 0.26787 0.27038 0.18146 -0.01840 -0.04714 -0.02469 485 ARG A CG  
3872 C CD  . ARG A 485 ? 0.27177 0.27637 0.19627 -0.01676 -0.04954 -0.02168 485 ARG A CD  
3873 N NE  . ARG A 485 ? 0.30634 0.31231 0.23029 -0.01507 -0.05214 -0.01599 485 ARG A NE  
3874 C CZ  . ARG A 485 ? 0.36519 0.37318 0.29808 -0.01328 -0.05425 -0.01292 485 ARG A CZ  
3875 N NH1 . ARG A 485 ? 0.33145 0.34076 0.27424 -0.01308 -0.05388 -0.01474 485 ARG A NH1 
3876 N NH2 . ARG A 485 ? 0.31394 0.32265 0.24610 -0.01169 -0.05664 -0.00792 485 ARG A NH2 
3877 N N   . MET A 486 ? 0.27028 0.26341 0.17334 -0.01539 -0.03006 -0.02393 486 MET A N   
3878 C CA  . MET A 486 ? 0.29077 0.28214 0.19115 -0.01426 -0.02593 -0.02171 486 MET A CA  
3879 C C   . MET A 486 ? 0.32700 0.31829 0.21708 -0.01606 -0.02364 -0.02427 486 MET A C   
3880 O O   . MET A 486 ? 0.34261 0.33389 0.22685 -0.01609 -0.02231 -0.02116 486 MET A O   
3881 C CB  . MET A 486 ? 0.25895 0.24801 0.16743 -0.01250 -0.02176 -0.02273 486 MET A CB  
3882 C CG  . MET A 486 ? 0.28358 0.27284 0.20129 -0.01061 -0.02303 -0.01950 486 MET A CG  
3883 S SD  . MET A 486 ? 0.32653 0.31627 0.24356 -0.00903 -0.02435 -0.01307 486 MET A SD  
3884 C CE  . MET A 486 ? 0.25303 0.24043 0.16677 -0.00847 -0.01888 -0.01271 486 MET A CE  
3885 N N   . ALA A 487 ? 0.35387 0.34511 0.24174 -0.01769 -0.02299 -0.03009 487 ALA A N   
3886 C CA  . ALA A 487 ? 0.38473 0.37627 0.26275 -0.01952 -0.02048 -0.03341 487 ALA A CA  
3887 C C   . ALA A 487 ? 0.45942 0.45351 0.32696 -0.02139 -0.02408 -0.03073 487 ALA A C   
3888 O O   . ALA A 487 ? 0.48945 0.48404 0.34825 -0.02243 -0.02170 -0.03011 487 ALA A O   
3889 C CB  . ALA A 487 ? 0.28456 0.27539 0.16317 -0.02086 -0.01945 -0.04069 487 ALA A CB  
3890 N N   . ALA A 488 ? 0.46232 0.45830 0.33071 -0.02192 -0.02988 -0.02894 488 ALA A N   
3891 C CA  . ALA A 488 ? 0.49130 0.48975 0.35014 -0.02356 -0.03404 -0.02558 488 ALA A CA  
3892 C C   . ALA A 488 ? 0.47006 0.46797 0.32804 -0.02216 -0.03390 -0.01841 488 ALA A C   
3893 O O   . ALA A 488 ? 0.47986 0.47870 0.32795 -0.02361 -0.03435 -0.01562 488 ALA A O   
3894 C CB  . ALA A 488 ? 0.49786 0.49874 0.35923 -0.02427 -0.04064 -0.02539 488 ALA A CB  
3895 N N   . ALA A 489 ? 0.38770 0.38402 0.25582 -0.01952 -0.03315 -0.01543 489 ALA A N   
3896 C CA  . ALA A 489 ? 0.45552 0.45085 0.32387 -0.01813 -0.03284 -0.00907 489 ALA A CA  
3897 C C   . ALA A 489 ? 0.41994 0.41389 0.28258 -0.01866 -0.02730 -0.00903 489 ALA A C   
3898 O O   . ALA A 489 ? 0.47608 0.46996 0.33291 -0.01920 -0.02750 -0.00430 489 ALA A O   
3899 C CB  . ALA A 489 ? 0.35628 0.35032 0.23681 -0.01529 -0.03282 -0.00691 489 ALA A CB  
3900 N N   . TYR A 490 ? 0.43841 0.43132 0.30305 -0.01855 -0.02236 -0.01413 490 TYR A N   
3901 C CA  . TYR A 490 ? 0.40588 0.39797 0.26655 -0.01890 -0.01681 -0.01451 490 TYR A CA  
3902 C C   . TYR A 490 ? 0.47109 0.46503 0.31897 -0.02176 -0.01598 -0.01571 490 TYR A C   
3903 O O   . TYR A 490 ? 0.51675 0.51064 0.35998 -0.02241 -0.01211 -0.01418 490 TYR A O   
3904 C CB  . TYR A 490 ? 0.35196 0.34262 0.21928 -0.01775 -0.01205 -0.01964 490 TYR A CB  
3905 C CG  . TYR A 490 ? 0.33044 0.31923 0.20689 -0.01526 -0.00990 -0.01687 490 TYR A CG  
3906 C CD1 . TYR A 490 ? 0.29889 0.28687 0.18446 -0.01340 -0.01239 -0.01549 490 TYR A CD1 
3907 C CD2 . TYR A 490 ? 0.33795 0.32613 0.21380 -0.01492 -0.00538 -0.01569 490 TYR A CD2 
3908 C CE1 . TYR A 490 ? 0.30720 0.29371 0.20035 -0.01130 -0.01052 -0.01320 490 TYR A CE1 
3909 C CE2 . TYR A 490 ? 0.27505 0.26173 0.15899 -0.01282 -0.00375 -0.01334 490 TYR A CE2 
3910 C CZ  . TYR A 490 ? 0.33662 0.32241 0.22884 -0.01102 -0.00638 -0.01217 490 TYR A CZ  
3911 O OH  . TYR A 490 ? 0.30311 0.28762 0.20275 -0.00909 -0.00485 -0.01010 490 TYR A OH  
3912 N N   . ARG A 491 ? 0.52928 0.52509 0.37124 -0.02367 -0.01950 -0.01842 491 ARG A N   
3913 C CA  . ARG A 491 ? 0.57559 0.57360 0.40697 -0.02574 -0.01873 -0.01956 491 ARG A CA  
3914 C C   . ARG A 491 ? 0.51406 0.51363 0.34036 -0.02612 -0.02328 -0.01309 491 ARG A C   
3915 O O   . ARG A 491 ? 0.60767 0.60870 0.42670 -0.02707 -0.02179 -0.01210 491 ARG A O   
3916 C CB  . ARG A 491 ? 0.59671 0.59593 0.42683 -0.02669 -0.01935 -0.02664 491 ARG A CB  
3917 C CG  . ARG A 491 ? 0.66435 0.66544 0.49306 -0.02743 -0.02616 -0.02586 491 ARG A CG  
3918 C CD  . ARG A 491 ? 0.62684 0.62912 0.45247 -0.02867 -0.02629 -0.03274 491 ARG A CD  
3919 N NE  . ARG A 491 ? 0.61914 0.61955 0.45159 -0.02848 -0.02413 -0.03919 491 ARG A NE  
3920 C CZ  . ARG A 491 ? 0.69060 0.69083 0.52875 -0.02881 -0.02798 -0.04149 491 ARG A CZ  
3921 N NH1 . ARG A 491 ? 0.57116 0.57338 0.40943 -0.02924 -0.03432 -0.03815 491 ARG A NH1 
3922 N NH2 . ARG A 491 ? 0.75102 0.74910 0.59558 -0.02869 -0.02541 -0.04717 491 ARG A NH2 
3923 N N   . ARG A 492 ? 0.43299 0.43223 0.26321 -0.02535 -0.02874 -0.00866 492 ARG A N   
3924 C CA  . ARG A 492 ? 0.51097 0.51130 0.33791 -0.02529 -0.03315 -0.00194 492 ARG A CA  
3925 C C   . ARG A 492 ? 0.60192 0.60005 0.43032 -0.02436 -0.03154 0.00452  492 ARG A C   
3926 O O   . ARG A 492 ? 0.51658 0.51400 0.34795 -0.02332 -0.03583 0.01040  492 ARG A O   
3927 C CB  . ARG A 492 ? 0.49598 0.49749 0.32730 -0.02473 -0.04018 -0.00056 492 ARG A CB  
3928 C CG  . ARG A 492 ? 0.45038 0.44995 0.29154 -0.02317 -0.04170 0.00010  492 ARG A CG  
3929 C CD  . ARG A 492 ? 0.42936 0.43098 0.27557 -0.02263 -0.04852 0.00098  492 ARG A CD  
3930 N NE  . ARG A 492 ? 0.39478 0.39529 0.25475 -0.01965 -0.04878 0.00176  492 ARG A NE  
3931 N N   . SER A 493 ? 0.56645 0.56347 0.39347 -0.02465 -0.02535 0.00338  493 SER A N   
3932 C CA  . SER A 493 ? 0.55722 0.55208 0.38578 -0.02406 -0.02317 0.00891  493 SER A CA  
3933 C C   . SER A 493 ? 0.63945 0.63545 0.46062 -0.02544 -0.02006 0.01117  493 SER A C   
3934 O O   . SER A 493 ? 0.59870 0.59316 0.42046 -0.02541 -0.01764 0.01553  493 SER A O   
3935 C CB  . SER A 493 ? 0.53971 0.53242 0.37455 -0.02307 -0.01842 0.00614  493 SER A CB  
3936 O OG  . SER A 493 ? 0.56186 0.55446 0.40507 -0.02134 -0.01952 0.00150  493 SER A OG  
# 
