data_8Z44
# 
_entry.id   8Z44 
# 
_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   8Z44         pdb_00008z44 10.2210/pdb8z44/pdb 
WWPDB D_1300047006 ?            ?                   
# 
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                        8Z44 
_pdbx_database_status.recvd_initial_deposition_date   2024-04-16 
_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 
PDB 'The same protein 3 us after illumination of the dark-adapted form'   8Z3G unspecified 
PDB 'The same protein 10 us after illumination of the dark-adapted form'  8Z3L unspecified 
PDB 'The same protein 30 us after illumination of the dark-adapted form'  8Z3X unspecified 
PDB 'The same protein 100 us after illumination of the dark-adapted form' 8Z41 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    178 ? ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MAGVKNSIIWFRKGLRLHDNPALLEACKDAKHVYPVFVLDPHFLQQSSYKVSVNRYNFLLESLEDLQRSFQARGSRLLVL
RGKPEEVFPRVFREWGVTQLCFEHDTEPYAKVRDAAVRRLAAEAGVEVVTPISHTLYDTDMLVARNGGAAPLTMQSFTKL
VDRVGDPPAPAPDPPAAMPPPAEDMPSAAPAATGVPTWQEVGFKEPPLTVFKGGETEALARLEAAFQDPKWVAGFQKPDT
DPSAWEKPATTVLSPYLKFGCLSARLFHARLLEVYRRHPAHSQPPVSLRGQLLWREFFYTVGSTTPNFHRMAGNPVCKQI
DWDDNPEFLAAWREARTGFPWIDAIMTQLVTWGWMHHLARHSVACFLTRGDLYVSWERGMEVFEEHLIDQDHYLNAANWM
WLSASAFFSQYFRVYSPVVFGKKYDPEGRFIRKFLPVLKDMPAKYIYEPWTAPLEVQRKAGCVVGRDYPAPIVDHAVASK
ACIARMAAAYRRSKGEKLAAALEHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MAGVKNSIIWFRKGLRLHDNPALLEACKDAKHVYPVFVLDPHFLQQSSYKVSVNRYNFLLESLEDLQRSFQARGSRLLVL
RGKPEEVFPRVFREWGVTQLCFEHDTEPYAKVRDAAVRRLAAEAGVEVVTPISHTLYDTDMLVARNGGAAPLTMQSFTKL
VDRVGDPPAPAPDPPAAMPPPAEDMPSAAPAATGVPTWQEVGFKEPPLTVFKGGETEALARLEAAFQDPKWVAGFQKPDT
DPSAWEKPATTVLSPYLKFGCLSARLFHARLLEVYRRHPAHSQPPVSLRGQLLWREFFYTVGSTTPNFHRMAGNPVCKQI
DWDDNPEFLAAWREARTGFPWIDAIMTQLVTWGWMHHLARHSVACFLTRGDLYVSWERGMEVFEEHLIDQDHYLNAANWM
WLSASAFFSQYFRVYSPVVFGKKYDPEGRFIRKFLPVLKDMPAKYIYEPWTAPLEVQRKAGCVVGRDYPAPIVDHAVASK
ACIARMAAAYRRSKGEKLAAALEHHHHHH
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'FLAVIN-ADENINE DINUCLEOTIDE' FAD 
3 'CHLORIDE ION'                CL  
4 water                         HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ALA n 
1 3   GLY n 
1 4   VAL n 
1 5   LYS n 
1 6   ASN n 
1 7   SER n 
1 8   ILE n 
1 9   ILE n 
1 10  TRP n 
1 11  PHE n 
1 12  ARG n 
1 13  LYS n 
1 14  GLY n 
1 15  LEU n 
1 16  ARG n 
1 17  LEU n 
1 18  HIS n 
1 19  ASP n 
1 20  ASN n 
1 21  PRO n 
1 22  ALA n 
1 23  LEU n 
1 24  LEU n 
1 25  GLU n 
1 26  ALA n 
1 27  CYS n 
1 28  LYS n 
1 29  ASP n 
1 30  ALA n 
1 31  LYS n 
1 32  HIS n 
1 33  VAL n 
1 34  TYR n 
1 35  PRO n 
1 36  VAL n 
1 37  PHE n 
1 38  VAL n 
1 39  LEU n 
1 40  ASP n 
1 41  PRO n 
1 42  HIS n 
1 43  PHE n 
1 44  LEU n 
1 45  GLN n 
1 46  GLN n 
1 47  SER n 
1 48  SER n 
1 49  TYR n 
1 50  LYS n 
1 51  VAL n 
1 52  SER n 
1 53  VAL n 
1 54  ASN n 
1 55  ARG n 
1 56  TYR n 
1 57  ASN n 
1 58  PHE n 
1 59  LEU n 
1 60  LEU n 
1 61  GLU n 
1 62  SER n 
1 63  LEU n 
1 64  GLU n 
1 65  ASP n 
1 66  LEU n 
1 67  GLN n 
1 68  ARG n 
1 69  SER n 
1 70  PHE n 
1 71  GLN n 
1 72  ALA n 
1 73  ARG n 
1 74  GLY n 
1 75  SER n 
1 76  ARG n 
1 77  LEU n 
1 78  LEU n 
1 79  VAL n 
1 80  LEU n 
1 81  ARG n 
1 82  GLY n 
1 83  LYS n 
1 84  PRO n 
1 85  GLU n 
1 86  GLU n 
1 87  VAL n 
1 88  PHE n 
1 89  PRO n 
1 90  ARG n 
1 91  VAL n 
1 92  PHE n 
1 93  ARG n 
1 94  GLU n 
1 95  TRP n 
1 96  GLY n 
1 97  VAL n 
1 98  THR n 
1 99  GLN n 
1 100 LEU n 
1 101 CYS n 
1 102 PHE n 
1 103 GLU n 
1 104 HIS n 
1 105 ASP n 
1 106 THR n 
1 107 GLU n 
1 108 PRO n 
1 109 TYR n 
1 110 ALA n 
1 111 LYS n 
1 112 VAL n 
1 113 ARG n 
1 114 ASP n 
1 115 ALA n 
1 116 ALA n 
1 117 VAL n 
1 118 ARG n 
1 119 ARG n 
1 120 LEU n 
1 121 ALA n 
1 122 ALA n 
1 123 GLU n 
1 124 ALA n 
1 125 GLY n 
1 126 VAL n 
1 127 GLU n 
1 128 VAL n 
1 129 VAL n 
1 130 THR n 
1 131 PRO n 
1 132 ILE n 
1 133 SER n 
1 134 HIS n 
1 135 THR n 
1 136 LEU n 
1 137 TYR n 
1 138 ASP n 
1 139 THR n 
1 140 ASP n 
1 141 MET n 
1 142 LEU n 
1 143 VAL n 
1 144 ALA n 
1 145 ARG n 
1 146 ASN n 
1 147 GLY n 
1 148 GLY n 
1 149 ALA n 
1 150 ALA n 
1 151 PRO n 
1 152 LEU n 
1 153 THR n 
1 154 MET n 
1 155 GLN n 
1 156 SER n 
1 157 PHE n 
1 158 THR n 
1 159 LYS n 
1 160 LEU n 
1 161 VAL n 
1 162 ASP n 
1 163 ARG n 
1 164 VAL n 
1 165 GLY n 
1 166 ASP n 
1 167 PRO n 
1 168 PRO n 
1 169 ALA n 
1 170 PRO n 
1 171 ALA n 
1 172 PRO n 
1 173 ASP n 
1 174 PRO n 
1 175 PRO n 
1 176 ALA n 
1 177 ALA n 
1 178 MET n 
1 179 PRO n 
1 180 PRO n 
1 181 PRO n 
1 182 ALA n 
1 183 GLU n 
1 184 ASP n 
1 185 MET n 
1 186 PRO n 
1 187 SER n 
1 188 ALA n 
1 189 ALA n 
1 190 PRO n 
1 191 ALA n 
1 192 ALA n 
1 193 THR n 
1 194 GLY n 
1 195 VAL n 
1 196 PRO n 
1 197 THR n 
1 198 TRP n 
1 199 GLN n 
1 200 GLU n 
1 201 VAL n 
1 202 GLY n 
1 203 PHE n 
1 204 LYS n 
1 205 GLU n 
1 206 PRO n 
1 207 PRO n 
1 208 LEU n 
1 209 THR n 
1 210 VAL n 
1 211 PHE n 
1 212 LYS n 
1 213 GLY n 
1 214 GLY n 
1 215 GLU n 
1 216 THR n 
1 217 GLU n 
1 218 ALA n 
1 219 LEU n 
1 220 ALA n 
1 221 ARG n 
1 222 LEU n 
1 223 GLU n 
1 224 ALA n 
1 225 ALA n 
1 226 PHE n 
1 227 GLN n 
1 228 ASP n 
1 229 PRO n 
1 230 LYS n 
1 231 TRP n 
1 232 VAL n 
1 233 ALA n 
1 234 GLY n 
1 235 PHE n 
1 236 GLN n 
1 237 LYS n 
1 238 PRO n 
1 239 ASP n 
1 240 THR n 
1 241 ASP n 
1 242 PRO n 
1 243 SER n 
1 244 ALA n 
1 245 TRP n 
1 246 GLU n 
1 247 LYS n 
1 248 PRO n 
1 249 ALA n 
1 250 THR n 
1 251 THR n 
1 252 VAL n 
1 253 LEU n 
1 254 SER n 
1 255 PRO n 
1 256 TYR n 
1 257 LEU n 
1 258 LYS n 
1 259 PHE n 
1 260 GLY n 
1 261 CYS n 
1 262 LEU n 
1 263 SER n 
1 264 ALA n 
1 265 ARG n 
1 266 LEU n 
1 267 PHE n 
1 268 HIS n 
1 269 ALA n 
1 270 ARG n 
1 271 LEU n 
1 272 LEU n 
1 273 GLU n 
1 274 VAL n 
1 275 TYR n 
1 276 ARG n 
1 277 ARG n 
1 278 HIS n 
1 279 PRO n 
1 280 ALA n 
1 281 HIS n 
1 282 SER n 
1 283 GLN n 
1 284 PRO n 
1 285 PRO n 
1 286 VAL n 
1 287 SER n 
1 288 LEU n 
1 289 ARG n 
1 290 GLY n 
1 291 GLN n 
1 292 LEU n 
1 293 LEU n 
1 294 TRP n 
1 295 ARG n 
1 296 GLU n 
1 297 PHE n 
1 298 PHE n 
1 299 TYR n 
1 300 THR n 
1 301 VAL n 
1 302 GLY n 
1 303 SER n 
1 304 THR n 
1 305 THR n 
1 306 PRO n 
1 307 ASN n 
1 308 PHE n 
1 309 HIS n 
1 310 ARG n 
1 311 MET n 
1 312 ALA n 
1 313 GLY n 
1 314 ASN n 
1 315 PRO n 
1 316 VAL n 
1 317 CYS n 
1 318 LYS n 
1 319 GLN n 
1 320 ILE n 
1 321 ASP n 
1 322 TRP n 
1 323 ASP n 
1 324 ASP n 
1 325 ASN n 
1 326 PRO n 
1 327 GLU n 
1 328 PHE n 
1 329 LEU n 
1 330 ALA n 
1 331 ALA n 
1 332 TRP n 
1 333 ARG n 
1 334 GLU n 
1 335 ALA n 
1 336 ARG n 
1 337 THR n 
1 338 GLY n 
1 339 PHE n 
1 340 PRO n 
1 341 TRP n 
1 342 ILE n 
1 343 ASP n 
1 344 ALA n 
1 345 ILE n 
1 346 MET n 
1 347 THR n 
1 348 GLN n 
1 349 LEU n 
1 350 VAL n 
1 351 THR n 
1 352 TRP n 
1 353 GLY n 
1 354 TRP n 
1 355 MET n 
1 356 HIS n 
1 357 HIS n 
1 358 LEU n 
1 359 ALA n 
1 360 ARG n 
1 361 HIS n 
1 362 SER n 
1 363 VAL n 
1 364 ALA n 
1 365 CYS n 
1 366 PHE n 
1 367 LEU n 
1 368 THR n 
1 369 ARG n 
1 370 GLY n 
1 371 ASP n 
1 372 LEU n 
1 373 TYR n 
1 374 VAL n 
1 375 SER n 
1 376 TRP n 
1 377 GLU n 
1 378 ARG n 
1 379 GLY n 
1 380 MET n 
1 381 GLU n 
1 382 VAL n 
1 383 PHE n 
1 384 GLU n 
1 385 GLU n 
1 386 HIS n 
1 387 LEU n 
1 388 ILE n 
1 389 ASP n 
1 390 GLN n 
1 391 ASP n 
1 392 HIS n 
1 393 TYR n 
1 394 LEU n 
1 395 ASN n 
1 396 ALA n 
1 397 ALA n 
1 398 ASN n 
1 399 TRP n 
1 400 MET n 
1 401 TRP n 
1 402 LEU n 
1 403 SER n 
1 404 ALA n 
1 405 SER n 
1 406 ALA n 
1 407 PHE n 
1 408 PHE n 
1 409 SER n 
1 410 GLN n 
1 411 TYR n 
1 412 PHE n 
1 413 ARG n 
1 414 VAL n 
1 415 TYR n 
1 416 SER n 
1 417 PRO n 
1 418 VAL n 
1 419 VAL n 
1 420 PHE n 
1 421 GLY n 
1 422 LYS n 
1 423 LYS n 
1 424 TYR n 
1 425 ASP n 
1 426 PRO n 
1 427 GLU n 
1 428 GLY n 
1 429 ARG n 
1 430 PHE n 
1 431 ILE n 
1 432 ARG n 
1 433 LYS n 
1 434 PHE n 
1 435 LEU n 
1 436 PRO n 
1 437 VAL n 
1 438 LEU n 
1 439 LYS n 
1 440 ASP n 
1 441 MET n 
1 442 PRO n 
1 443 ALA n 
1 444 LYS n 
1 445 TYR n 
1 446 ILE n 
1 447 TYR n 
1 448 GLU n 
1 449 PRO n 
1 450 TRP n 
1 451 THR n 
1 452 ALA n 
1 453 PRO n 
1 454 LEU n 
1 455 GLU n 
1 456 VAL n 
1 457 GLN n 
1 458 ARG n 
1 459 LYS n 
1 460 ALA n 
1 461 GLY n 
1 462 CYS n 
1 463 VAL n 
1 464 VAL n 
1 465 GLY n 
1 466 ARG n 
1 467 ASP n 
1 468 TYR n 
1 469 PRO n 
1 470 ALA n 
1 471 PRO n 
1 472 ILE n 
1 473 VAL n 
1 474 ASP n 
1 475 HIS n 
1 476 ALA n 
1 477 VAL n 
1 478 ALA n 
1 479 SER n 
1 480 LYS n 
1 481 ALA n 
1 482 CYS n 
1 483 ILE n 
1 484 ALA n 
1 485 ARG n 
1 486 MET n 
1 487 ALA n 
1 488 ALA n 
1 489 ALA n 
1 490 TYR n 
1 491 ARG n 
1 492 ARG n 
1 493 SER n 
1 494 LYS n 
1 495 GLY n 
1 496 GLU n 
1 497 LYS n 
1 498 LEU n 
1 499 ALA n 
1 500 ALA n 
1 501 ALA n 
1 502 LEU n 
1 503 GLU n 
1 504 HIS n 
1 505 HIS n 
1 506 HIS n 
1 507 HIS n 
1 508 HIS n 
1 509 HIS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   509 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'UVR3, CHLRE_06g278251v5, CHLREDRAFT_206002' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Chlamydomonas reinhardtii' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     3055 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                       ? 'C3 H7 N O2'        89.093  
ARG 'L-peptide linking' y ARGININE                      ? 'C6 H15 N4 O2 1'    175.209 
ASN 'L-peptide linking' y ASPARAGINE                    ? 'C4 H8 N2 O3'       132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'               ? 'C4 H7 N O4'        133.103 
CL  non-polymer         . 'CHLORIDE ION'                ? 'Cl -1'             35.453  
CYS 'L-peptide linking' y CYSTEINE                      ? 'C3 H7 N O2 S'      121.158 
FAD non-polymer         . 'FLAVIN-ADENINE DINUCLEOTIDE' ? 'C27 H33 N9 O15 P2' 785.550 
GLN 'L-peptide linking' y GLUTAMINE                     ? 'C5 H10 N2 O3'      146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'               ? 'C5 H9 N O4'        147.129 
GLY 'peptide linking'   y GLYCINE                       ? 'C2 H5 N O2'        75.067  
HIS 'L-peptide linking' y HISTIDINE                     ? 'C6 H10 N3 O2 1'    156.162 
HOH non-polymer         . WATER                         ? 'H2 O'              18.015  
ILE 'L-peptide linking' y ISOLEUCINE                    ? 'C6 H13 N O2'       131.173 
LEU 'L-peptide linking' y LEUCINE                       ? 'C6 H13 N O2'       131.173 
LYS 'L-peptide linking' y LYSINE                        ? 'C6 H15 N2 O2 1'    147.195 
MET 'L-peptide linking' y METHIONINE                    ? 'C5 H11 N O2 S'     149.211 
PHE 'L-peptide linking' y PHENYLALANINE                 ? 'C9 H11 N O2'       165.189 
PRO 'L-peptide linking' y PROLINE                       ? 'C5 H9 N O2'        115.130 
SER 'L-peptide linking' y SERINE                        ? 'C3 H7 N O3'        105.093 
THR 'L-peptide linking' y THREONINE                     ? 'C4 H9 N O3'        119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                    ? 'C11 H12 N2 O2'     204.225 
TYR 'L-peptide linking' y TYROSINE                      ? 'C9 H11 N O3'       181.189 
VAL 'L-peptide linking' y VALINE                        ? 'C5 H11 N O2'       117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   ALA 2   2   ?   ?   ?   A . n 
A 1 3   GLY 3   3   3   GLY GLY A . n 
A 1 4   VAL 4   4   4   VAL VAL A . n 
A 1 5   LYS 5   5   5   LYS LYS A . n 
A 1 6   ASN 6   6   6   ASN ASN A . n 
A 1 7   SER 7   7   7   SER SER A . n 
A 1 8   ILE 8   8   8   ILE ILE A . n 
A 1 9   ILE 9   9   9   ILE ILE A . n 
A 1 10  TRP 10  10  10  TRP TRP A . n 
A 1 11  PHE 11  11  11  PHE PHE A . n 
A 1 12  ARG 12  12  12  ARG ARG A . n 
A 1 13  LYS 13  13  13  LYS LYS A . n 
A 1 14  GLY 14  14  14  GLY GLY A . n 
A 1 15  LEU 15  15  15  LEU LEU A . n 
A 1 16  ARG 16  16  16  ARG ARG A . n 
A 1 17  LEU 17  17  17  LEU LEU A . n 
A 1 18  HIS 18  18  18  HIS HIS A . n 
A 1 19  ASP 19  19  19  ASP ASP A . n 
A 1 20  ASN 20  20  20  ASN ASN A . n 
A 1 21  PRO 21  21  21  PRO PRO A . n 
A 1 22  ALA 22  22  22  ALA ALA A . n 
A 1 23  LEU 23  23  23  LEU LEU A . n 
A 1 24  LEU 24  24  24  LEU LEU A . n 
A 1 25  GLU 25  25  25  GLU GLU A . n 
A 1 26  ALA 26  26  26  ALA ALA A . n 
A 1 27  CYS 27  27  27  CYS CYS A . n 
A 1 28  LYS 28  28  28  LYS LYS A . n 
A 1 29  ASP 29  29  29  ASP ASP A . n 
A 1 30  ALA 30  30  30  ALA ALA A . n 
A 1 31  LYS 31  31  31  LYS LYS A . n 
A 1 32  HIS 32  32  32  HIS HIS A . n 
A 1 33  VAL 33  33  33  VAL VAL A . n 
A 1 34  TYR 34  34  34  TYR TYR A . n 
A 1 35  PRO 35  35  35  PRO PRO A . n 
A 1 36  VAL 36  36  36  VAL VAL A . n 
A 1 37  PHE 37  37  37  PHE PHE A . n 
A 1 38  VAL 38  38  38  VAL VAL A . n 
A 1 39  LEU 39  39  39  LEU LEU A . n 
A 1 40  ASP 40  40  40  ASP ASP A . n 
A 1 41  PRO 41  41  41  PRO PRO A . n 
A 1 42  HIS 42  42  42  HIS HIS A . n 
A 1 43  PHE 43  43  43  PHE PHE A . n 
A 1 44  LEU 44  44  44  LEU LEU A . n 
A 1 45  GLN 45  45  45  GLN GLN A . n 
A 1 46  GLN 46  46  46  GLN GLN A . n 
A 1 47  SER 47  47  ?   ?   ?   A . n 
A 1 48  SER 48  48  ?   ?   ?   A . n 
A 1 49  TYR 49  49  ?   ?   ?   A . n 
A 1 50  LYS 50  50  50  LYS LYS A . n 
A 1 51  VAL 51  51  51  VAL VAL A . n 
A 1 52  SER 52  52  52  SER SER A . n 
A 1 53  VAL 53  53  53  VAL VAL A . n 
A 1 54  ASN 54  54  54  ASN ASN A . n 
A 1 55  ARG 55  55  55  ARG ARG A . n 
A 1 56  TYR 56  56  56  TYR TYR A . n 
A 1 57  ASN 57  57  57  ASN ASN A . n 
A 1 58  PHE 58  58  58  PHE PHE A . n 
A 1 59  LEU 59  59  59  LEU LEU A . n 
A 1 60  LEU 60  60  60  LEU LEU A . n 
A 1 61  GLU 61  61  61  GLU GLU A . n 
A 1 62  SER 62  62  62  SER SER A . n 
A 1 63  LEU 63  63  63  LEU LEU A . n 
A 1 64  GLU 64  64  64  GLU GLU A . n 
A 1 65  ASP 65  65  65  ASP ASP A . n 
A 1 66  LEU 66  66  66  LEU LEU A . n 
A 1 67  GLN 67  67  67  GLN GLN A . n 
A 1 68  ARG 68  68  68  ARG ARG A . n 
A 1 69  SER 69  69  69  SER SER A . n 
A 1 70  PHE 70  70  70  PHE PHE A . n 
A 1 71  GLN 71  71  71  GLN GLN A . n 
A 1 72  ALA 72  72  72  ALA ALA A . n 
A 1 73  ARG 73  73  73  ARG ARG A . n 
A 1 74  GLY 74  74  74  GLY GLY A . n 
A 1 75  SER 75  75  75  SER SER A . n 
A 1 76  ARG 76  76  76  ARG ARG A . n 
A 1 77  LEU 77  77  77  LEU LEU A . n 
A 1 78  LEU 78  78  78  LEU LEU A . n 
A 1 79  VAL 79  79  79  VAL VAL A . n 
A 1 80  LEU 80  80  80  LEU LEU A . n 
A 1 81  ARG 81  81  81  ARG ARG A . n 
A 1 82  GLY 82  82  82  GLY GLY A . n 
A 1 83  LYS 83  83  83  LYS LYS A . n 
A 1 84  PRO 84  84  84  PRO PRO A . n 
A 1 85  GLU 85  85  85  GLU GLU A . n 
A 1 86  GLU 86  86  86  GLU GLU A . n 
A 1 87  VAL 87  87  87  VAL VAL A . n 
A 1 88  PHE 88  88  88  PHE PHE A . n 
A 1 89  PRO 89  89  89  PRO PRO A . n 
A 1 90  ARG 90  90  90  ARG ARG A . n 
A 1 91  VAL 91  91  91  VAL VAL A . n 
A 1 92  PHE 92  92  92  PHE PHE A . n 
A 1 93  ARG 93  93  93  ARG ARG A . n 
A 1 94  GLU 94  94  94  GLU GLU A . n 
A 1 95  TRP 95  95  95  TRP TRP A . n 
A 1 96  GLY 96  96  96  GLY GLY A . n 
A 1 97  VAL 97  97  97  VAL VAL A . n 
A 1 98  THR 98  98  98  THR THR A . n 
A 1 99  GLN 99  99  99  GLN GLN A . n 
A 1 100 LEU 100 100 100 LEU LEU A . n 
A 1 101 CYS 101 101 101 CYS CYS A . n 
A 1 102 PHE 102 102 102 PHE PHE A . n 
A 1 103 GLU 103 103 103 GLU GLU A . n 
A 1 104 HIS 104 104 104 HIS HIS A . n 
A 1 105 ASP 105 105 105 ASP ASP A . n 
A 1 106 THR 106 106 106 THR THR A . n 
A 1 107 GLU 107 107 107 GLU GLU A . n 
A 1 108 PRO 108 108 108 PRO PRO A . n 
A 1 109 TYR 109 109 109 TYR TYR A . n 
A 1 110 ALA 110 110 110 ALA ALA A . n 
A 1 111 LYS 111 111 111 LYS LYS A . n 
A 1 112 VAL 112 112 112 VAL VAL A . n 
A 1 113 ARG 113 113 113 ARG ARG A . n 
A 1 114 ASP 114 114 114 ASP ASP A . n 
A 1 115 ALA 115 115 115 ALA ALA A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 VAL 117 117 117 VAL VAL A . n 
A 1 118 ARG 118 118 118 ARG ARG A . n 
A 1 119 ARG 119 119 119 ARG ARG A . n 
A 1 120 LEU 120 120 120 LEU LEU A . n 
A 1 121 ALA 121 121 121 ALA ALA A . n 
A 1 122 ALA 122 122 122 ALA ALA A . n 
A 1 123 GLU 123 123 123 GLU GLU A . n 
A 1 124 ALA 124 124 124 ALA ALA A . n 
A 1 125 GLY 125 125 125 GLY GLY A . n 
A 1 126 VAL 126 126 126 VAL VAL A . n 
A 1 127 GLU 127 127 127 GLU GLU A . n 
A 1 128 VAL 128 128 128 VAL VAL A . n 
A 1 129 VAL 129 129 129 VAL VAL A . n 
A 1 130 THR 130 130 130 THR THR A . n 
A 1 131 PRO 131 131 131 PRO PRO A . n 
A 1 132 ILE 132 132 132 ILE ILE A . n 
A 1 133 SER 133 133 133 SER SER A . n 
A 1 134 HIS 134 134 134 HIS HIS A . n 
A 1 135 THR 135 135 135 THR THR A . n 
A 1 136 LEU 136 136 136 LEU LEU A . n 
A 1 137 TYR 137 137 137 TYR TYR A . n 
A 1 138 ASP 138 138 138 ASP ASP A . n 
A 1 139 THR 139 139 139 THR THR A . n 
A 1 140 ASP 140 140 140 ASP ASP A . n 
A 1 141 MET 141 141 141 MET MET A . n 
A 1 142 LEU 142 142 142 LEU LEU A . n 
A 1 143 VAL 143 143 143 VAL VAL A . n 
A 1 144 ALA 144 144 144 ALA ALA A . n 
A 1 145 ARG 145 145 145 ARG ARG A . n 
A 1 146 ASN 146 146 146 ASN ASN A . n 
A 1 147 GLY 147 147 147 GLY GLY A . n 
A 1 148 GLY 148 148 148 GLY GLY A . n 
A 1 149 ALA 149 149 149 ALA ALA A . n 
A 1 150 ALA 150 150 150 ALA ALA A . n 
A 1 151 PRO 151 151 151 PRO PRO A . n 
A 1 152 LEU 152 152 152 LEU LEU A . n 
A 1 153 THR 153 153 153 THR THR A . n 
A 1 154 MET 154 154 154 MET MET A . n 
A 1 155 GLN 155 155 155 GLN GLN A . n 
A 1 156 SER 156 156 156 SER SER A . n 
A 1 157 PHE 157 157 157 PHE PHE A . n 
A 1 158 THR 158 158 158 THR THR A . n 
A 1 159 LYS 159 159 159 LYS LYS A . n 
A 1 160 LEU 160 160 160 LEU LEU A . n 
A 1 161 VAL 161 161 161 VAL VAL A . n 
A 1 162 ASP 162 162 162 ASP ASP A . n 
A 1 163 ARG 163 163 163 ARG ARG A . n 
A 1 164 VAL 164 164 164 VAL VAL A . n 
A 1 165 GLY 165 165 165 GLY GLY A . n 
A 1 166 ASP 166 166 166 ASP ASP A . n 
A 1 167 PRO 167 167 167 PRO PRO A . n 
A 1 168 PRO 168 168 168 PRO PRO A . n 
A 1 169 ALA 169 169 169 ALA ALA A . n 
A 1 170 PRO 170 170 170 PRO PRO A . n 
A 1 171 ALA 171 171 171 ALA ALA A . n 
A 1 172 PRO 172 172 172 PRO PRO A . n 
A 1 173 ASP 173 173 173 ASP ASP A . n 
A 1 174 PRO 174 174 174 PRO PRO A . n 
A 1 175 PRO 175 175 175 PRO PRO A . n 
A 1 176 ALA 176 176 176 ALA ALA A . n 
A 1 177 ALA 177 177 177 ALA ALA A . n 
A 1 178 MET 178 178 178 MET MET A . n 
A 1 179 PRO 179 179 179 PRO PRO A . n 
A 1 180 PRO 180 180 180 PRO PRO A . n 
A 1 181 PRO 181 181 181 PRO PRO A . n 
A 1 182 ALA 182 182 182 ALA ALA A . n 
A 1 183 GLU 183 183 183 GLU GLU A . n 
A 1 184 ASP 184 184 184 ASP ASP A . n 
A 1 185 MET 185 185 185 MET MET A . n 
A 1 186 PRO 186 186 186 PRO PRO A . n 
A 1 187 SER 187 187 187 SER SER A . n 
A 1 188 ALA 188 188 188 ALA ALA A . n 
A 1 189 ALA 189 189 189 ALA ALA A . n 
A 1 190 PRO 190 190 190 PRO PRO A . n 
A 1 191 ALA 191 191 191 ALA ALA A . n 
A 1 192 ALA 192 192 192 ALA ALA A . n 
A 1 193 THR 193 193 193 THR THR A . n 
A 1 194 GLY 194 194 194 GLY GLY A . n 
A 1 195 VAL 195 195 195 VAL VAL A . n 
A 1 196 PRO 196 196 196 PRO PRO A . n 
A 1 197 THR 197 197 197 THR THR A . n 
A 1 198 TRP 198 198 198 TRP TRP A . n 
A 1 199 GLN 199 199 199 GLN GLN A . n 
A 1 200 GLU 200 200 200 GLU GLU A . n 
A 1 201 VAL 201 201 201 VAL VAL A . n 
A 1 202 GLY 202 202 202 GLY GLY A . n 
A 1 203 PHE 203 203 203 PHE PHE A . n 
A 1 204 LYS 204 204 204 LYS LYS A . n 
A 1 205 GLU 205 205 205 GLU GLU A . n 
A 1 206 PRO 206 206 206 PRO PRO A . n 
A 1 207 PRO 207 207 207 PRO PRO A . n 
A 1 208 LEU 208 208 208 LEU LEU A . n 
A 1 209 THR 209 209 209 THR THR A . n 
A 1 210 VAL 210 210 210 VAL VAL A . n 
A 1 211 PHE 211 211 211 PHE PHE A . n 
A 1 212 LYS 212 212 212 LYS LYS A . n 
A 1 213 GLY 213 213 213 GLY GLY A . n 
A 1 214 GLY 214 214 214 GLY GLY A . n 
A 1 215 GLU 215 215 215 GLU GLU A . n 
A 1 216 THR 216 216 216 THR THR A . n 
A 1 217 GLU 217 217 217 GLU GLU A . n 
A 1 218 ALA 218 218 218 ALA ALA A . n 
A 1 219 LEU 219 219 219 LEU LEU A . n 
A 1 220 ALA 220 220 220 ALA ALA A . n 
A 1 221 ARG 221 221 221 ARG ARG A . n 
A 1 222 LEU 222 222 222 LEU LEU A . n 
A 1 223 GLU 223 223 223 GLU GLU A . n 
A 1 224 ALA 224 224 224 ALA ALA A . n 
A 1 225 ALA 225 225 225 ALA ALA A . n 
A 1 226 PHE 226 226 226 PHE PHE A . n 
A 1 227 GLN 227 227 227 GLN GLN A . n 
A 1 228 ASP 228 228 228 ASP ASP A . n 
A 1 229 PRO 229 229 229 PRO PRO A . n 
A 1 230 LYS 230 230 230 LYS LYS A . n 
A 1 231 TRP 231 231 231 TRP TRP A . n 
A 1 232 VAL 232 232 232 VAL VAL A . n 
A 1 233 ALA 233 233 233 ALA ALA A . n 
A 1 234 GLY 234 234 234 GLY GLY A . n 
A 1 235 PHE 235 235 235 PHE PHE A . n 
A 1 236 GLN 236 236 236 GLN GLN A . n 
A 1 237 LYS 237 237 237 LYS LYS A . n 
A 1 238 PRO 238 238 238 PRO PRO A . n 
A 1 239 ASP 239 239 239 ASP ASP A . n 
A 1 240 THR 240 240 240 THR THR A . n 
A 1 241 ASP 241 241 241 ASP ASP A . n 
A 1 242 PRO 242 242 242 PRO PRO A . n 
A 1 243 SER 243 243 243 SER SER A . n 
A 1 244 ALA 244 244 244 ALA ALA A . n 
A 1 245 TRP 245 245 245 TRP TRP A . n 
A 1 246 GLU 246 246 246 GLU GLU A . n 
A 1 247 LYS 247 247 247 LYS LYS A . n 
A 1 248 PRO 248 248 248 PRO PRO A . n 
A 1 249 ALA 249 249 249 ALA ALA A . n 
A 1 250 THR 250 250 250 THR THR A . n 
A 1 251 THR 251 251 251 THR THR A . n 
A 1 252 VAL 252 252 252 VAL VAL A . n 
A 1 253 LEU 253 253 253 LEU LEU A . n 
A 1 254 SER 254 254 254 SER SER A . n 
A 1 255 PRO 255 255 255 PRO PRO A . n 
A 1 256 TYR 256 256 256 TYR TYR A . n 
A 1 257 LEU 257 257 257 LEU LEU A . n 
A 1 258 LYS 258 258 258 LYS LYS A . n 
A 1 259 PHE 259 259 259 PHE PHE A . n 
A 1 260 GLY 260 260 260 GLY GLY A . n 
A 1 261 CYS 261 261 261 CYS CYS A . n 
A 1 262 LEU 262 262 262 LEU LEU A . n 
A 1 263 SER 263 263 263 SER SER A . n 
A 1 264 ALA 264 264 264 ALA ALA A . n 
A 1 265 ARG 265 265 265 ARG ARG A . n 
A 1 266 LEU 266 266 266 LEU LEU A . n 
A 1 267 PHE 267 267 267 PHE PHE A . n 
A 1 268 HIS 268 268 268 HIS HIS A . n 
A 1 269 ALA 269 269 269 ALA ALA A . n 
A 1 270 ARG 270 270 270 ARG ARG A . n 
A 1 271 LEU 271 271 271 LEU LEU A . n 
A 1 272 LEU 272 272 272 LEU LEU A . n 
A 1 273 GLU 273 273 273 GLU GLU A . n 
A 1 274 VAL 274 274 274 VAL VAL A . n 
A 1 275 TYR 275 275 275 TYR TYR A . n 
A 1 276 ARG 276 276 276 ARG ARG A . n 
A 1 277 ARG 277 277 277 ARG ARG A . n 
A 1 278 HIS 278 278 278 HIS HIS A . n 
A 1 279 PRO 279 279 279 PRO PRO A . n 
A 1 280 ALA 280 280 280 ALA ALA A . n 
A 1 281 HIS 281 281 281 HIS HIS A . n 
A 1 282 SER 282 282 282 SER SER A . n 
A 1 283 GLN 283 283 283 GLN GLN A . n 
A 1 284 PRO 284 284 284 PRO PRO A . n 
A 1 285 PRO 285 285 285 PRO PRO A . n 
A 1 286 VAL 286 286 286 VAL VAL A . n 
A 1 287 SER 287 287 287 SER SER A . n 
A 1 288 LEU 288 288 288 LEU LEU A . n 
A 1 289 ARG 289 289 289 ARG ARG A . n 
A 1 290 GLY 290 290 290 GLY GLY A . n 
A 1 291 GLN 291 291 291 GLN GLN A . n 
A 1 292 LEU 292 292 292 LEU LEU A . n 
A 1 293 LEU 293 293 293 LEU LEU A . n 
A 1 294 TRP 294 294 294 TRP TRP A . n 
A 1 295 ARG 295 295 295 ARG ARG A . n 
A 1 296 GLU 296 296 296 GLU GLU A . n 
A 1 297 PHE 297 297 297 PHE PHE A . n 
A 1 298 PHE 298 298 298 PHE PHE A . n 
A 1 299 TYR 299 299 299 TYR TYR A . n 
A 1 300 THR 300 300 300 THR THR A . n 
A 1 301 VAL 301 301 301 VAL VAL A . n 
A 1 302 GLY 302 302 302 GLY GLY A . n 
A 1 303 SER 303 303 303 SER SER A . n 
A 1 304 THR 304 304 304 THR THR A . n 
A 1 305 THR 305 305 305 THR THR A . n 
A 1 306 PRO 306 306 306 PRO PRO A . n 
A 1 307 ASN 307 307 307 ASN ASN A . n 
A 1 308 PHE 308 308 308 PHE PHE A . n 
A 1 309 HIS 309 309 309 HIS HIS A . n 
A 1 310 ARG 310 310 310 ARG ARG A . n 
A 1 311 MET 311 311 311 MET MET A . n 
A 1 312 ALA 312 312 312 ALA ALA A . n 
A 1 313 GLY 313 313 313 GLY GLY A . n 
A 1 314 ASN 314 314 314 ASN ASN A . n 
A 1 315 PRO 315 315 315 PRO PRO A . n 
A 1 316 VAL 316 316 316 VAL VAL A . n 
A 1 317 CYS 317 317 317 CYS CYS A . n 
A 1 318 LYS 318 318 318 LYS LYS A . n 
A 1 319 GLN 319 319 319 GLN GLN A . n 
A 1 320 ILE 320 320 320 ILE ILE A . n 
A 1 321 ASP 321 321 321 ASP ASP A . n 
A 1 322 TRP 322 322 322 TRP TRP A . n 
A 1 323 ASP 323 323 323 ASP ASP A . n 
A 1 324 ASP 324 324 324 ASP ASP A . n 
A 1 325 ASN 325 325 325 ASN ASN A . n 
A 1 326 PRO 326 326 326 PRO PRO A . n 
A 1 327 GLU 327 327 327 GLU GLU A . n 
A 1 328 PHE 328 328 328 PHE PHE A . n 
A 1 329 LEU 329 329 329 LEU LEU A . n 
A 1 330 ALA 330 330 330 ALA ALA A . n 
A 1 331 ALA 331 331 331 ALA ALA A . n 
A 1 332 TRP 332 332 332 TRP TRP A . n 
A 1 333 ARG 333 333 333 ARG ARG A . n 
A 1 334 GLU 334 334 334 GLU GLU A . n 
A 1 335 ALA 335 335 335 ALA ALA A . n 
A 1 336 ARG 336 336 336 ARG ARG A . n 
A 1 337 THR 337 337 337 THR THR A . n 
A 1 338 GLY 338 338 338 GLY GLY A . n 
A 1 339 PHE 339 339 339 PHE PHE A . n 
A 1 340 PRO 340 340 340 PRO PRO A . n 
A 1 341 TRP 341 341 341 TRP TRP A . n 
A 1 342 ILE 342 342 342 ILE ILE A . n 
A 1 343 ASP 343 343 343 ASP ASP A . n 
A 1 344 ALA 344 344 344 ALA ALA A . n 
A 1 345 ILE 345 345 345 ILE ILE A . n 
A 1 346 MET 346 346 346 MET MET A . n 
A 1 347 THR 347 347 347 THR THR A . n 
A 1 348 GLN 348 348 348 GLN GLN A . n 
A 1 349 LEU 349 349 349 LEU LEU A . n 
A 1 350 VAL 350 350 350 VAL VAL A . n 
A 1 351 THR 351 351 351 THR THR A . n 
A 1 352 TRP 352 352 352 TRP TRP A . n 
A 1 353 GLY 353 353 353 GLY GLY A . n 
A 1 354 TRP 354 354 354 TRP TRP A . n 
A 1 355 MET 355 355 355 MET MET A . n 
A 1 356 HIS 356 356 356 HIS HIS A . n 
A 1 357 HIS 357 357 357 HIS HIS A . n 
A 1 358 LEU 358 358 358 LEU LEU A . n 
A 1 359 ALA 359 359 359 ALA ALA A . n 
A 1 360 ARG 360 360 360 ARG ARG A . n 
A 1 361 HIS 361 361 361 HIS HIS A . n 
A 1 362 SER 362 362 362 SER SER A . n 
A 1 363 VAL 363 363 363 VAL VAL A . n 
A 1 364 ALA 364 364 364 ALA ALA A . n 
A 1 365 CYS 365 365 365 CYS CYS A . n 
A 1 366 PHE 366 366 366 PHE PHE A . n 
A 1 367 LEU 367 367 367 LEU LEU A . n 
A 1 368 THR 368 368 368 THR THR A . n 
A 1 369 ARG 369 369 369 ARG ARG A . n 
A 1 370 GLY 370 370 370 GLY GLY A . n 
A 1 371 ASP 371 371 371 ASP ASP A . n 
A 1 372 LEU 372 372 372 LEU LEU A . n 
A 1 373 TYR 373 373 373 TYR TYR A . n 
A 1 374 VAL 374 374 374 VAL VAL A . n 
A 1 375 SER 375 375 375 SER SER A . n 
A 1 376 TRP 376 376 376 TRP TRP A . n 
A 1 377 GLU 377 377 377 GLU GLU A . n 
A 1 378 ARG 378 378 378 ARG ARG A . n 
A 1 379 GLY 379 379 379 GLY GLY A . n 
A 1 380 MET 380 380 380 MET MET A . n 
A 1 381 GLU 381 381 381 GLU GLU A . n 
A 1 382 VAL 382 382 382 VAL VAL A . n 
A 1 383 PHE 383 383 383 PHE PHE A . n 
A 1 384 GLU 384 384 384 GLU GLU A . n 
A 1 385 GLU 385 385 385 GLU GLU A . n 
A 1 386 HIS 386 386 386 HIS HIS A . n 
A 1 387 LEU 387 387 387 LEU LEU A . n 
A 1 388 ILE 388 388 388 ILE ILE A . n 
A 1 389 ASP 389 389 389 ASP ASP A . n 
A 1 390 GLN 390 390 390 GLN GLN A . n 
A 1 391 ASP 391 391 391 ASP ASP A . n 
A 1 392 HIS 392 392 392 HIS HIS A . n 
A 1 393 TYR 393 393 393 TYR TYR A . n 
A 1 394 LEU 394 394 394 LEU LEU A . n 
A 1 395 ASN 395 395 395 ASN ASN A . n 
A 1 396 ALA 396 396 396 ALA ALA A . n 
A 1 397 ALA 397 397 397 ALA ALA A . n 
A 1 398 ASN 398 398 398 ASN ASN A . n 
A 1 399 TRP 399 399 399 TRP TRP A . n 
A 1 400 MET 400 400 400 MET MET A . n 
A 1 401 TRP 401 401 401 TRP TRP A . n 
A 1 402 LEU 402 402 402 LEU LEU A . n 
A 1 403 SER 403 403 403 SER SER A . n 
A 1 404 ALA 404 404 404 ALA ALA A . n 
A 1 405 SER 405 405 405 SER SER A . n 
A 1 406 ALA 406 406 406 ALA ALA A . n 
A 1 407 PHE 407 407 407 PHE PHE A . n 
A 1 408 PHE 408 408 408 PHE PHE A . n 
A 1 409 SER 409 409 409 SER SER A . n 
A 1 410 GLN 410 410 410 GLN GLN A . n 
A 1 411 TYR 411 411 411 TYR TYR A . n 
A 1 412 PHE 412 412 412 PHE PHE A . n 
A 1 413 ARG 413 413 413 ARG ARG A . n 
A 1 414 VAL 414 414 414 VAL VAL A . n 
A 1 415 TYR 415 415 415 TYR TYR A . n 
A 1 416 SER 416 416 416 SER SER A . n 
A 1 417 PRO 417 417 417 PRO PRO A . n 
A 1 418 VAL 418 418 418 VAL VAL A . n 
A 1 419 VAL 419 419 419 VAL VAL A . n 
A 1 420 PHE 420 420 420 PHE PHE A . n 
A 1 421 GLY 421 421 421 GLY GLY A . n 
A 1 422 LYS 422 422 422 LYS LYS A . n 
A 1 423 LYS 423 423 423 LYS LYS A . n 
A 1 424 TYR 424 424 424 TYR TYR A . n 
A 1 425 ASP 425 425 425 ASP ASP A . n 
A 1 426 PRO 426 426 426 PRO PRO A . n 
A 1 427 GLU 427 427 427 GLU GLU A . n 
A 1 428 GLY 428 428 428 GLY GLY A . n 
A 1 429 ARG 429 429 429 ARG ARG A . n 
A 1 430 PHE 430 430 430 PHE PHE A . n 
A 1 431 ILE 431 431 431 ILE ILE A . n 
A 1 432 ARG 432 432 432 ARG ARG A . n 
A 1 433 LYS 433 433 433 LYS LYS A . n 
A 1 434 PHE 434 434 434 PHE PHE A . n 
A 1 435 LEU 435 435 435 LEU LEU A . n 
A 1 436 PRO 436 436 436 PRO PRO A . n 
A 1 437 VAL 437 437 437 VAL VAL A . n 
A 1 438 LEU 438 438 438 LEU LEU A . n 
A 1 439 LYS 439 439 439 LYS LYS A . n 
A 1 440 ASP 440 440 440 ASP ASP A . n 
A 1 441 MET 441 441 441 MET MET A . n 
A 1 442 PRO 442 442 442 PRO PRO A . n 
A 1 443 ALA 443 443 443 ALA ALA A . n 
A 1 444 LYS 444 444 444 LYS LYS A . n 
A 1 445 TYR 445 445 445 TYR TYR A . n 
A 1 446 ILE 446 446 446 ILE ILE A . n 
A 1 447 TYR 447 447 447 TYR TYR A . n 
A 1 448 GLU 448 448 448 GLU GLU A . n 
A 1 449 PRO 449 449 449 PRO PRO A . n 
A 1 450 TRP 450 450 450 TRP TRP A . n 
A 1 451 THR 451 451 451 THR THR A . n 
A 1 452 ALA 452 452 452 ALA ALA A . n 
A 1 453 PRO 453 453 453 PRO PRO A . n 
A 1 454 LEU 454 454 454 LEU LEU A . n 
A 1 455 GLU 455 455 455 GLU GLU A . n 
A 1 456 VAL 456 456 456 VAL VAL A . n 
A 1 457 GLN 457 457 457 GLN GLN A . n 
A 1 458 ARG 458 458 458 ARG ARG A . n 
A 1 459 LYS 459 459 459 LYS LYS A . n 
A 1 460 ALA 460 460 460 ALA ALA A . n 
A 1 461 GLY 461 461 461 GLY GLY A . n 
A 1 462 CYS 462 462 462 CYS CYS A . n 
A 1 463 VAL 463 463 463 VAL VAL A . n 
A 1 464 VAL 464 464 464 VAL VAL A . n 
A 1 465 GLY 465 465 465 GLY GLY A . n 
A 1 466 ARG 466 466 466 ARG ARG A . n 
A 1 467 ASP 467 467 467 ASP ASP A . n 
A 1 468 TYR 468 468 468 TYR TYR A . n 
A 1 469 PRO 469 469 469 PRO PRO A . n 
A 1 470 ALA 470 470 470 ALA ALA A . n 
A 1 471 PRO 471 471 471 PRO PRO A . n 
A 1 472 ILE 472 472 472 ILE ILE A . n 
A 1 473 VAL 473 473 473 VAL VAL A . n 
A 1 474 ASP 474 474 474 ASP ASP A . n 
A 1 475 HIS 475 475 475 HIS HIS A . n 
A 1 476 ALA 476 476 476 ALA ALA A . n 
A 1 477 VAL 477 477 477 VAL VAL A . n 
A 1 478 ALA 478 478 478 ALA ALA A . n 
A 1 479 SER 479 479 479 SER SER A . n 
A 1 480 LYS 480 480 480 LYS LYS A . n 
A 1 481 ALA 481 481 481 ALA ALA A . n 
A 1 482 CYS 482 482 482 CYS CYS A . n 
A 1 483 ILE 483 483 483 ILE ILE A . n 
A 1 484 ALA 484 484 484 ALA ALA A . n 
A 1 485 ARG 485 485 485 ARG ARG A . n 
A 1 486 MET 486 486 486 MET MET A . n 
A 1 487 ALA 487 487 487 ALA ALA A . n 
A 1 488 ALA 488 488 488 ALA ALA A . n 
A 1 489 ALA 489 489 489 ALA ALA A . n 
A 1 490 TYR 490 490 490 TYR TYR A . n 
A 1 491 ARG 491 491 491 ARG ARG A . n 
A 1 492 ARG 492 492 492 ARG ARG A . n 
A 1 493 SER 493 493 493 SER SER A . n 
A 1 494 LYS 494 494 494 LYS LYS A . n 
A 1 495 GLY 495 495 ?   ?   ?   A . n 
A 1 496 GLU 496 496 ?   ?   ?   A . n 
A 1 497 LYS 497 497 ?   ?   ?   A . n 
A 1 498 LEU 498 498 ?   ?   ?   A . n 
A 1 499 ALA 499 499 ?   ?   ?   A . n 
A 1 500 ALA 500 500 ?   ?   ?   A . n 
A 1 501 ALA 501 501 ?   ?   ?   A . n 
A 1 502 LEU 502 502 ?   ?   ?   A . n 
A 1 503 GLU 503 503 ?   ?   ?   A . n 
A 1 504 HIS 504 504 ?   ?   ?   A . n 
A 1 505 HIS 505 505 ?   ?   ?   A . n 
A 1 506 HIS 506 506 ?   ?   ?   A . n 
A 1 507 HIS 507 507 ?   ?   ?   A . n 
A 1 508 HIS 508 508 ?   ?   ?   A . n 
A 1 509 HIS 509 509 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        FAD 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   FAD 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 FAD 1   601 602 FAD FAD A . 
C 3 CL  1   602 1   CL  CL  A . 
D 4 HOH 1   701 164 HOH HOH A . 
D 4 HOH 2   702 138 HOH HOH A . 
D 4 HOH 3   703 167 HOH HOH A . 
D 4 HOH 4   704 44  HOH HOH A . 
D 4 HOH 5   705 150 HOH HOH A . 
D 4 HOH 6   706 25  HOH HOH A . 
D 4 HOH 7   707 95  HOH HOH A . 
D 4 HOH 8   708 107 HOH HOH A . 
D 4 HOH 9   709 53  HOH HOH A . 
D 4 HOH 10  710 26  HOH HOH A . 
D 4 HOH 11  711 148 HOH HOH A . 
D 4 HOH 12  712 93  HOH HOH A . 
D 4 HOH 13  713 100 HOH HOH A . 
D 4 HOH 14  714 124 HOH HOH A . 
D 4 HOH 15  715 99  HOH HOH A . 
D 4 HOH 16  716 39  HOH HOH A . 
D 4 HOH 17  717 9   HOH HOH A . 
D 4 HOH 18  718 108 HOH HOH A . 
D 4 HOH 19  719 80  HOH HOH A . 
D 4 HOH 20  720 20  HOH HOH A . 
D 4 HOH 21  721 24  HOH HOH A . 
D 4 HOH 22  722 140 HOH HOH A . 
D 4 HOH 23  723 38  HOH HOH A . 
D 4 HOH 24  724 36  HOH HOH A . 
D 4 HOH 25  725 161 HOH HOH A . 
D 4 HOH 26  726 7   HOH HOH A . 
D 4 HOH 27  727 31  HOH HOH A . 
D 4 HOH 28  728 84  HOH HOH A . 
D 4 HOH 29  729 76  HOH HOH A . 
D 4 HOH 30  730 137 HOH HOH A . 
D 4 HOH 31  731 6   HOH HOH A . 
D 4 HOH 32  732 86  HOH HOH A . 
D 4 HOH 33  733 141 HOH HOH A . 
D 4 HOH 34  734 28  HOH HOH A . 
D 4 HOH 35  735 22  HOH HOH A . 
D 4 HOH 36  736 165 HOH HOH A . 
D 4 HOH 37  737 149 HOH HOH A . 
D 4 HOH 38  738 144 HOH HOH A . 
D 4 HOH 39  739 166 HOH HOH A . 
D 4 HOH 40  740 2   HOH HOH A . 
D 4 HOH 41  741 109 HOH HOH A . 
D 4 HOH 42  742 169 HOH HOH A . 
D 4 HOH 43  743 13  HOH HOH A . 
D 4 HOH 44  744 156 HOH HOH A . 
D 4 HOH 45  745 91  HOH HOH A . 
D 4 HOH 46  746 37  HOH HOH A . 
D 4 HOH 47  747 3   HOH HOH A . 
D 4 HOH 48  748 172 HOH HOH A . 
D 4 HOH 49  749 142 HOH HOH A . 
D 4 HOH 50  750 4   HOH HOH A . 
D 4 HOH 51  751 35  HOH HOH A . 
D 4 HOH 52  752 52  HOH HOH A . 
D 4 HOH 53  753 168 HOH HOH A . 
D 4 HOH 54  754 147 HOH HOH A . 
D 4 HOH 55  755 174 HOH HOH A . 
D 4 HOH 56  756 32  HOH HOH A . 
D 4 HOH 57  757 157 HOH HOH A . 
D 4 HOH 58  758 48  HOH HOH A . 
D 4 HOH 59  759 171 HOH HOH A . 
D 4 HOH 60  760 67  HOH HOH A . 
D 4 HOH 61  761 136 HOH HOH A . 
D 4 HOH 62  762 45  HOH HOH A . 
D 4 HOH 63  763 133 HOH HOH A . 
D 4 HOH 64  764 119 HOH HOH A . 
D 4 HOH 65  765 63  HOH HOH A . 
D 4 HOH 66  766 41  HOH HOH A . 
D 4 HOH 67  767 1   HOH HOH A . 
D 4 HOH 68  768 87  HOH HOH A . 
D 4 HOH 69  769 72  HOH HOH A . 
D 4 HOH 70  770 88  HOH HOH A . 
D 4 HOH 71  771 58  HOH HOH A . 
D 4 HOH 72  772 71  HOH HOH A . 
D 4 HOH 73  773 155 HOH HOH A . 
D 4 HOH 74  774 10  HOH HOH A . 
D 4 HOH 75  775 105 HOH HOH A . 
D 4 HOH 76  776 112 HOH HOH A . 
D 4 HOH 77  777 135 HOH HOH A . 
D 4 HOH 78  778 15  HOH HOH A . 
D 4 HOH 79  779 16  HOH HOH A . 
D 4 HOH 80  780 122 HOH HOH A . 
D 4 HOH 81  781 11  HOH HOH A . 
D 4 HOH 82  782 23  HOH HOH A . 
D 4 HOH 83  783 163 HOH HOH A . 
D 4 HOH 84  784 62  HOH HOH A . 
D 4 HOH 85  785 151 HOH HOH A . 
D 4 HOH 86  786 146 HOH HOH A . 
D 4 HOH 87  787 134 HOH HOH A . 
D 4 HOH 88  788 19  HOH HOH A . 
D 4 HOH 89  789 21  HOH HOH A . 
D 4 HOH 90  790 30  HOH HOH A . 
D 4 HOH 91  791 120 HOH HOH A . 
D 4 HOH 92  792 12  HOH HOH A . 
D 4 HOH 93  793 51  HOH HOH A . 
D 4 HOH 94  794 118 HOH HOH A . 
D 4 HOH 95  795 154 HOH HOH A . 
D 4 HOH 96  796 81  HOH HOH A . 
D 4 HOH 97  797 8   HOH HOH A . 
D 4 HOH 98  798 74  HOH HOH A . 
D 4 HOH 99  799 114 HOH HOH A . 
D 4 HOH 100 800 59  HOH HOH A . 
D 4 HOH 101 801 56  HOH HOH A . 
D 4 HOH 102 802 159 HOH HOH A . 
D 4 HOH 103 803 143 HOH HOH A . 
D 4 HOH 104 804 29  HOH HOH A . 
D 4 HOH 105 805 5   HOH HOH A . 
D 4 HOH 106 806 152 HOH HOH A . 
D 4 HOH 107 807 90  HOH HOH A . 
D 4 HOH 108 808 61  HOH HOH A . 
D 4 HOH 109 809 57  HOH HOH A . 
D 4 HOH 110 810 116 HOH HOH A . 
D 4 HOH 111 811 60  HOH HOH A . 
D 4 HOH 112 812 111 HOH HOH A . 
D 4 HOH 113 813 65  HOH HOH A . 
D 4 HOH 114 814 68  HOH HOH A . 
D 4 HOH 115 815 14  HOH HOH A . 
D 4 HOH 116 816 42  HOH HOH A . 
D 4 HOH 117 817 130 HOH HOH A . 
D 4 HOH 118 818 158 HOH HOH A . 
D 4 HOH 119 819 173 HOH HOH A . 
D 4 HOH 120 820 128 HOH HOH A . 
D 4 HOH 121 821 33  HOH HOH A . 
D 4 HOH 122 822 82  HOH HOH A . 
D 4 HOH 123 823 94  HOH HOH A . 
D 4 HOH 124 824 162 HOH HOH A . 
D 4 HOH 125 825 113 HOH HOH A . 
D 4 HOH 126 826 83  HOH HOH A . 
D 4 HOH 127 827 177 HOH HOH A . 
D 4 HOH 128 828 123 HOH HOH A . 
D 4 HOH 129 829 178 HOH HOH A . 
D 4 HOH 130 830 96  HOH HOH A . 
D 4 HOH 131 831 18  HOH HOH A . 
D 4 HOH 132 832 27  HOH HOH A . 
D 4 HOH 133 833 117 HOH HOH A . 
D 4 HOH 134 834 40  HOH HOH A . 
D 4 HOH 135 835 106 HOH HOH A . 
D 4 HOH 136 836 78  HOH HOH A . 
D 4 HOH 137 837 73  HOH HOH A . 
D 4 HOH 138 838 127 HOH HOH A . 
D 4 HOH 139 839 160 HOH HOH A . 
D 4 HOH 140 840 46  HOH HOH A . 
D 4 HOH 141 841 125 HOH HOH A . 
D 4 HOH 142 842 92  HOH HOH A . 
D 4 HOH 143 843 75  HOH HOH A . 
D 4 HOH 144 844 131 HOH HOH A . 
D 4 HOH 145 845 104 HOH HOH A . 
D 4 HOH 146 846 145 HOH HOH A . 
D 4 HOH 147 847 43  HOH HOH A . 
D 4 HOH 148 848 126 HOH HOH A . 
D 4 HOH 149 849 79  HOH HOH A . 
D 4 HOH 150 850 89  HOH HOH A . 
D 4 HOH 151 851 176 HOH HOH A . 
D 4 HOH 152 852 49  HOH HOH A . 
D 4 HOH 153 853 17  HOH HOH A . 
D 4 HOH 154 854 132 HOH HOH A . 
D 4 HOH 155 855 97  HOH HOH A . 
D 4 HOH 156 856 103 HOH HOH A . 
D 4 HOH 157 857 153 HOH HOH A . 
D 4 HOH 158 858 85  HOH HOH A . 
D 4 HOH 159 859 50  HOH HOH A . 
D 4 HOH 160 860 54  HOH HOH A . 
D 4 HOH 161 861 47  HOH HOH A . 
D 4 HOH 162 862 55  HOH HOH A . 
D 4 HOH 163 863 34  HOH HOH A . 
D 4 HOH 164 864 121 HOH HOH A . 
D 4 HOH 165 865 77  HOH HOH A . 
D 4 HOH 166 866 64  HOH HOH A . 
D 4 HOH 167 867 101 HOH HOH A . 
D 4 HOH 168 868 70  HOH HOH A . 
D 4 HOH 169 869 66  HOH HOH A . 
D 4 HOH 170 870 69  HOH HOH A . 
D 4 HOH 171 871 110 HOH HOH A . 
D 4 HOH 172 872 115 HOH HOH A . 
D 4 HOH 173 873 139 HOH HOH A . 
D 4 HOH 174 874 129 HOH HOH A . 
D 4 HOH 175 875 175 HOH HOH A . 
D 4 HOH 176 876 170 HOH HOH A . 
D 4 HOH 177 877 98  HOH HOH A . 
D 4 HOH 178 878 102 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 0 A GLY 3   ? N   ? A GLY 3   N   
2   1 Y 0 A GLY 3   ? CA  ? A GLY 3   CA  
3   1 Y 0 A GLY 3   ? O   ? A GLY 3   O   
4   1 Y 0 A LYS 28  ? CD  ? A LYS 28  CD  
5   1 Y 0 A LYS 28  ? CE  ? A LYS 28  CE  
6   1 Y 0 A LYS 28  ? NZ  ? A LYS 28  NZ  
7   1 Y 0 A LEU 44  ? CG  ? A LEU 44  CG  
8   1 Y 0 A LEU 44  ? CD1 ? A LEU 44  CD1 
9   1 Y 0 A LEU 44  ? CD2 ? A LEU 44  CD2 
10  1 Y 0 A GLN 45  ? CG  ? A GLN 45  CG  
11  1 Y 0 A GLN 45  ? CD  ? A GLN 45  CD  
12  1 Y 0 A GLN 45  ? OE1 ? A GLN 45  OE1 
13  1 Y 0 A GLN 45  ? NE2 ? A GLN 45  NE2 
14  1 Y 0 A GLN 46  ? 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 0 A LYS 50  ? CG  ? A LYS 50  CG  
18  1 Y 0 A LYS 50  ? CD  ? A LYS 50  CD  
19  1 Y 0 A LYS 50  ? CE  ? A LYS 50  CE  
20  1 Y 0 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 ARG 145 ? CZ  ? A ARG 145 CZ  
31  1 Y 0 A ARG 145 ? NH1 ? A ARG 145 NH1 
32  1 Y 0 A ARG 145 ? NH2 ? A ARG 145 NH2 
33  1 Y 0 A GLN 155 ? OE1 ? A GLN 155 OE1 
34  1 Y 0 A GLN 155 ? NE2 ? A GLN 155 NE2 
35  1 Y 0 A LYS 159 ? CD  ? A LYS 159 CD  
36  1 Y 0 A LYS 159 ? CE  ? A LYS 159 CE  
37  1 Y 0 A LYS 159 ? NZ  ? A LYS 159 NZ  
38  1 Y 0 A GLU 183 ? CD  ? A GLU 183 CD  
39  1 Y 0 A GLU 183 ? OE1 ? A GLU 183 OE1 
40  1 Y 0 A GLU 183 ? OE2 ? A GLU 183 OE2 
41  1 Y 0 A LYS 204 ? CD  ? A LYS 204 CD  
42  1 Y 0 A LYS 204 ? CE  ? A LYS 204 CE  
43  1 Y 0 A LYS 204 ? NZ  ? A LYS 204 NZ  
44  1 Y 0 A LYS 212 ? CE  ? A LYS 212 CE  
45  1 Y 0 A LYS 212 ? NZ  ? A LYS 212 NZ  
46  1 Y 0 A LYS 247 ? CD  ? A LYS 247 CD  
47  1 Y 0 A LYS 247 ? CE  ? A LYS 247 CE  
48  1 Y 0 A LYS 247 ? NZ  ? A LYS 247 NZ  
49  1 Y 0 A ARG 276 ? CD  ? A ARG 276 CD  
50  1 Y 0 A ARG 276 ? NE  ? A ARG 276 NE  
51  1 Y 0 A ARG 276 ? CZ  ? A ARG 276 CZ  
52  1 Y 0 A ARG 276 ? NH1 ? A ARG 276 NH1 
53  1 Y 0 A ARG 276 ? NH2 ? A ARG 276 NH2 
54  1 Y 0 A ARG 277 ? NE  ? A ARG 277 NE  
55  1 Y 0 A ARG 277 ? CZ  ? A ARG 277 CZ  
56  1 Y 0 A ARG 277 ? NH1 ? A ARG 277 NH1 
57  1 Y 0 A ARG 277 ? NH2 ? A ARG 277 NH2 
58  1 Y 0 A ARG 310 ? CD  ? A ARG 310 CD  
59  1 Y 0 A ARG 310 ? NE  ? A ARG 310 NE  
60  1 Y 0 A ARG 310 ? CZ  ? A ARG 310 CZ  
61  1 Y 0 A ARG 310 ? NH1 ? A ARG 310 NH1 
62  1 Y 0 A ARG 310 ? NH2 ? A ARG 310 NH2 
63  1 Y 0 A LYS 423 ? CG  ? A LYS 423 CG  
64  1 Y 0 A LYS 423 ? CD  ? A LYS 423 CD  
65  1 Y 0 A LYS 423 ? CE  ? A LYS 423 CE  
66  1 Y 0 A LYS 423 ? NZ  ? A LYS 423 NZ  
67  1 Y 0 A ARG 429 ? NE  ? A ARG 429 NE  
68  1 Y 0 A ARG 429 ? CZ  ? A ARG 429 CZ  
69  1 Y 0 A ARG 429 ? NH1 ? A ARG 429 NH1 
70  1 Y 0 A ARG 429 ? NH2 ? A ARG 429 NH2 
71  1 Y 0 A LYS 439 ? CD  ? A LYS 439 CD  
72  1 Y 0 A LYS 439 ? CE  ? A LYS 439 CE  
73  1 Y 0 A LYS 439 ? NZ  ? A LYS 439 NZ  
74  1 Y 0 A LYS 444 ? CE  ? A LYS 444 CE  
75  1 Y 0 A LYS 444 ? NZ  ? A LYS 444 NZ  
76  1 Y 0 A GLU 455 ? CG  ? A GLU 455 CG  
77  1 Y 0 A GLU 455 ? CD  ? A GLU 455 CD  
78  1 Y 0 A GLU 455 ? OE1 ? A GLU 455 OE1 
79  1 Y 0 A GLU 455 ? OE2 ? A GLU 455 OE2 
80  1 Y 0 A ARG 458 ? CD  ? A ARG 458 CD  
81  1 Y 0 A ARG 458 ? NE  ? A ARG 458 NE  
82  1 Y 0 A ARG 458 ? CZ  ? A ARG 458 CZ  
83  1 Y 0 A ARG 458 ? NH1 ? A ARG 458 NH1 
84  1 Y 0 A ARG 458 ? NH2 ? A ARG 458 NH2 
85  1 Y 0 A LYS 459 ? CG  ? A LYS 459 CG  
86  1 Y 0 A LYS 459 ? CD  ? A LYS 459 CD  
87  1 Y 0 A LYS 459 ? CE  ? A LYS 459 CE  
88  1 Y 0 A LYS 459 ? NZ  ? A LYS 459 NZ  
89  1 Y 0 A LYS 480 ? CD  ? A LYS 480 CD  
90  1 Y 0 A LYS 480 ? CE  ? A LYS 480 CE  
91  1 Y 0 A LYS 480 ? NZ  ? A LYS 480 NZ  
92  1 Y 1 A ARG 492 ? CG  ? A ARG 492 CG  
93  1 Y 1 A ARG 492 ? CD  ? A ARG 492 CD  
94  1 Y 1 A ARG 492 ? NE  ? A ARG 492 NE  
95  1 Y 1 A ARG 492 ? CZ  ? A ARG 492 CZ  
96  1 Y 1 A ARG 492 ? NH1 ? A ARG 492 NH1 
97  1 Y 1 A ARG 492 ? NH2 ? A ARG 492 NH2 
98  1 Y 1 A LYS 494 ? CG  ? A LYS 494 CG  
99  1 Y 1 A LYS 494 ? CD  ? A LYS 494 CD  
100 1 Y 1 A LYS 494 ? CE  ? A LYS 494 CE  
101 1 Y 1 A LYS 494 ? NZ  ? A LYS 494 NZ  
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX    ? ? ? 1.20.1_4487 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? CrystFEL  ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? pointless ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? REFMAC    ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8Z44 
_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                         8Z44 
_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                   8Z44 
_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             2.21 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          44.31 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          '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                          13.05 
_reflns.entry_id                                       8Z44 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.83 
_reflns.d_resolution_low                               33.1 
_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                                     46189 
_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                                374 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          7.133 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.993 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.83 
_reflns_shell.d_res_low                                     1.87 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.38 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2258 
_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                                  0.515 
_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                               13.86 
_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                                 8Z44 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.00 
_refine.ls_d_res_low                             30.58 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     35460 
_refine.ls_number_reflns_R_free                  1105 
_refine.ls_number_reflns_R_work                  34355 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.99 
_refine.ls_percent_reflns_R_free                 3.12 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2100 
_refine.ls_R_factor_R_free                       0.2315 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2093 
_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                 23.9260 
_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                            0.2258 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.00 
_refine_hist.d_res_low                        30.58 
_refine_hist.number_atoms_solvent             178 
_refine_hist.number_atoms_total               4146 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        3914 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         54 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0025  ? 4124 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.4936  ? 5637 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0382  ? 588  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0071  ? 725  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 12.0263 ? 1488 ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.00 2.09  . . 132 4220 100.00 . . . . 0.3228 . . . . . . . . . . . 0.3287 
'X-RAY DIFFRACTION' 2.09 2.20  . . 140 4235 100.00 . . . . 0.3049 . . . . . . . . . . . 0.3114 
'X-RAY DIFFRACTION' 2.20 2.34  . . 141 4222 100.00 . . . . 0.2811 . . . . . . . . . . . 0.2724 
'X-RAY DIFFRACTION' 2.34 2.52  . . 123 4284 100.00 . . . . 0.2633 . . . . . . . . . . . 0.3104 
'X-RAY DIFFRACTION' 2.52 2.77  . . 154 4227 100.00 . . . . 0.2425 . . . . . . . . . . . 0.2650 
'X-RAY DIFFRACTION' 2.77 3.17  . . 143 4299 100.00 . . . . 0.2168 . . . . . . . . . . . 0.2324 
'X-RAY DIFFRACTION' 3.17 4.00  . . 139 4322 100.00 . . . . 0.1578 . . . . . . . . . . . 0.1818 
'X-RAY DIFFRACTION' 4.00 30.58 . . 133 4546 99.96  . . . . 0.1197 . . . . . . . . . . . 0.1371 
# 
_struct.entry_id                     8Z44 
_struct.title                        'SFX structure of CraCRY 300 ns after photoexcitation of the oxidized protein' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        8Z44 
_struct_keywords.text            'photoreceptor, FLAVOPROTEIN, time-resolved crystallography, 300 ns time-point' 
_struct_keywords.pdbx_keywords   FLAVOPROTEIN 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A8J8W0_CHLRE 
_struct_ref.pdbx_db_accession          A8J8W0 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MAGVKNSIIWFRKGLRLHDNPALLEACKDAKHVYPVFVLDPHFLQQSSYKVSVNRYNFLLESLEDLQRSFQARGSRLLVL
RGKPEEVFPRVFREWGVTQLCFEHDTEPYAKVRDAAVRRLAAEAGVEVVTPISHTLYDTDMLVARNGGAAPLTMQSFTKL
VDRVGDPPAPAPDPPAAMPPPAEDMPSAAPAATGVPTWQEVGFKEPPLTVFKGGETEALARLEAAFQDPKWVAGFQKPDT
DPSAWEKPATTVLSPYLKFGCLSARLFHARLLEVYRRHPAHSQPPVSLRGQLLWREFFYTVGSTTPNFHRMAGNPVCKQI
DWDDNPEFLAAWREARTGFPWIDAIMTQLVTWGWMHHLARHSVACFLTRGDLYVSWERGMEVFEEHLIDQDHYLNAANWM
WLSASAFFSQYFRVYSPVVFGKKYDPEGRFIRKFLPVLKDMPAKYIYEPWTAPLEVQRKAGCVVGRDYPAPIVDHAVASK
ACIARMAAAYRRSKGE
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8Z44 
_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 8Z44 LYS A 497 ? UNP A8J8W0 ? ? 'expression tag' 497 1  
1 8Z44 LEU A 498 ? UNP A8J8W0 ? ? 'expression tag' 498 2  
1 8Z44 ALA A 499 ? UNP A8J8W0 ? ? 'expression tag' 499 3  
1 8Z44 ALA A 500 ? UNP A8J8W0 ? ? 'expression tag' 500 4  
1 8Z44 ALA A 501 ? UNP A8J8W0 ? ? 'expression tag' 501 5  
1 8Z44 LEU A 502 ? UNP A8J8W0 ? ? 'expression tag' 502 6  
1 8Z44 GLU A 503 ? UNP A8J8W0 ? ? 'expression tag' 503 7  
1 8Z44 HIS A 504 ? UNP A8J8W0 ? ? 'expression tag' 504 8  
1 8Z44 HIS A 505 ? UNP A8J8W0 ? ? 'expression tag' 505 9  
1 8Z44 HIS A 506 ? UNP A8J8W0 ? ? 'expression tag' 506 10 
1 8Z44 HIS A 507 ? UNP A8J8W0 ? ? 'expression tag' 507 11 
1 8Z44 HIS A 508 ? UNP A8J8W0 ? ? 'expression tag' 508 12 
1 8Z44 HIS A 509 ? UNP A8J8W0 ? ? 'expression tag' 509 13 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 1390  ? 
1 MORE         -17   ? 
1 'SSA (A^2)'  20480 ? 
# 
_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  ? ALA A 72  ? SER A 52  ALA A 72  1 ? 21 
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 189 ? MET A 185 ALA A 189 5 ? 5  
HELX_P HELX_P8  AA8 GLY A 214 ? PHE A 226 ? GLY A 214 PHE A 226 1 ? 13 
HELX_P HELX_P9  AA9 ASP A 228 ? GLY A 234 ? ASP A 228 GLY A 234 1 ? 7  
HELX_P HELX_P10 AB1 GLN A 236 ? THR A 240 ? GLN A 236 THR A 240 5 ? 5  
HELX_P HELX_P11 AB2 LEU A 253 ? PHE A 259 ? LEU A 253 PHE A 259 1 ? 7  
HELX_P HELX_P12 AB3 SER A 263 ? ARG A 276 ? SER A 263 ARG A 276 1 ? 14 
HELX_P HELX_P13 AB4 SER A 287 ? THR A 304 ? SER A 287 THR A 304 1 ? 18 
HELX_P HELX_P14 AB5 ASN A 325 ? GLU A 334 ? ASN A 325 GLU A 334 1 ? 10 
HELX_P HELX_P15 AB6 PHE A 339 ? GLY A 353 ? PHE A 339 GLY A 353 1 ? 15 
HELX_P HELX_P16 AB7 HIS A 356 ? THR A 368 ? HIS A 356 THR A 368 1 ? 13 
HELX_P HELX_P17 AB8 SER A 375 ? LEU A 387 ? SER A 375 LEU A 387 1 ? 13 
HELX_P HELX_P18 AB9 ASP A 391 ? SER A 403 ? ASP A 391 SER A 403 1 ? 13 
HELX_P HELX_P19 AC1 PHE A 420 ? TYR A 424 ? PHE A 420 TYR A 424 5 ? 5  
HELX_P HELX_P20 AC2 GLY A 428 ? LEU A 435 ? GLY A 428 LEU A 435 1 ? 8  
HELX_P HELX_P21 AC3 PRO A 436 ? LYS A 439 ? PRO A 436 LYS A 439 5 ? 4  
HELX_P HELX_P22 AC4 PRO A 442 ? ILE A 446 ? PRO A 442 ILE A 446 5 ? 5  
HELX_P HELX_P23 AC5 GLU A 448 ? ALA A 452 ? GLU A 448 ALA A 452 5 ? 5  
HELX_P HELX_P24 AC6 PRO A 453 ? ALA A 460 ? PRO A 453 ALA A 460 1 ? 8  
HELX_P HELX_P25 AC7 ASP A 474 ? SER A 493 ? ASP A 474 SER A 493 1 ? 20 
# 
_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       2.27 
# 
_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  ? CYS A 101 ? GLN A 99  CYS A 101 
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 ILE A 8   ? N ILE A 8   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                   8Z44 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ARG A 12  ? ? -129.03 -68.64  
2  1 LYS A 13  ? ? -100.10 -159.68 
3  1 GLN A 45  ? ? -102.96 53.42   
4  1 SER A 75  ? ? -115.64 -166.38 
5  1 SER A 133 ? ? -149.63 -2.31   
6  1 THR A 250 ? ? -115.78 -169.97 
7  1 TRP A 322 ? ? -47.92  154.25  
8  1 ASP A 324 ? ? -108.13 77.96   
9  1 THR A 368 ? ? -93.03  -115.44 
10 1 ARG A 369 ? ? -67.19  9.78    
11 1 ASP A 371 ? ? -143.69 -56.70  
12 1 PHE A 407 ? ? 62.23   -57.47  
# 
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 20.0221939241 9.22985985101  -15.7505613519 0.0835067381841 ? -0.00317918454058 ? -0.0124797183865 
? 0.0751734918281 ? -0.00209755331264 ? 0.0725950147484 ? 0.567641198878 ? -0.0788217308619 ? -0.247955901676 ? 0.668350012434 ? 
0.114050745642   ? 0.608874191705 ? 0.00562674087198 ? 0.02413864101   ? 0.0306830983109  ? -0.0158011082521 ? -0.0123145258641 ? 
0.00251444808948 ? -0.0178207387032 ? -0.0495960706455 ? 0.00219975221576 ? 
2 'X-RAY DIFFRACTION' ? refined 11.8210506512 -17.8139427827 -24.5307964469 0.0933710532999 ? 0.00567596509756  ? 0.00238380827135 
? 0.0661515994619 ? -0.00231204871242 ? 0.0607744632035 ? 0.580962428745 ? 0.163333397271   ? 0.039512518246  ? 0.419868551689 ? 
-0.0300188078808 ? 0.245527950764 ? -0.0057869939234 ? 0.0276528736154 ? -0.0285929366344 ? -0.0450186514765 ? 0.0164252048356  ? 
0.0385262017465  ? 0.027979989717   ? -0.026984125576  ? -0.0100911394429 ? 
# 
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 198 A 203 ? ? 
;chain 'A' and (resid 3 through 203 )
;
2 'X-RAY DIFFRACTION' 2 A 199 A 204 ? A 489 A 494 ? ? 
;chain 'A' and (resid 204 through 494 )
;
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 1   ? A MET 1   
2  1 Y 1 A ALA 2   ? A ALA 2   
3  1 Y 1 A SER 47  ? A SER 47  
4  1 Y 1 A SER 48  ? A SER 48  
5  1 Y 1 A TYR 49  ? A TYR 49  
6  1 Y 1 A GLY 495 ? A GLY 495 
7  1 Y 1 A GLU 496 ? A GLU 496 
8  1 Y 1 A LYS 497 ? A LYS 497 
9  1 Y 1 A LEU 498 ? A LEU 498 
10 1 Y 1 A ALA 499 ? A ALA 499 
11 1 Y 1 A ALA 500 ? A ALA 500 
12 1 Y 1 A ALA 501 ? A ALA 501 
13 1 Y 1 A LEU 502 ? A LEU 502 
14 1 Y 1 A GLU 503 ? A GLU 503 
15 1 Y 1 A HIS 504 ? A HIS 504 
16 1 Y 1 A HIS 505 ? A HIS 505 
17 1 Y 1 A HIS 506 ? A HIS 506 
18 1 Y 1 A HIS 507 ? A HIS 507 
19 1 Y 1 A HIS 508 ? A HIS 508 
20 1 Y 1 A HIS 509 ? A HIS 509 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N      N  N N 1   
ALA CA     C  N S 2   
ALA C      C  N N 3   
ALA O      O  N N 4   
ALA CB     C  N N 5   
ALA OXT    O  N N 6   
ALA H      H  N N 7   
ALA H2     H  N N 8   
ALA HA     H  N N 9   
ALA HB1    H  N N 10  
ALA HB2    H  N N 11  
ALA HB3    H  N N 12  
ALA HXT    H  N N 13  
ARG N      N  N N 14  
ARG CA     C  N S 15  
ARG C      C  N N 16  
ARG O      O  N N 17  
ARG CB     C  N N 18  
ARG CG     C  N N 19  
ARG CD     C  N N 20  
ARG NE     N  N N 21  
ARG CZ     C  N N 22  
ARG NH1    N  N N 23  
ARG NH2    N  N N 24  
ARG OXT    O  N N 25  
ARG H      H  N N 26  
ARG H2     H  N N 27  
ARG HA     H  N N 28  
ARG HB2    H  N N 29  
ARG HB3    H  N N 30  
ARG HG2    H  N N 31  
ARG HG3    H  N N 32  
ARG HD2    H  N N 33  
ARG HD3    H  N N 34  
ARG HE     H  N N 35  
ARG HH11   H  N N 36  
ARG HH12   H  N N 37  
ARG HH21   H  N N 38  
ARG HH22   H  N N 39  
ARG HXT    H  N N 40  
ASN N      N  N N 41  
ASN CA     C  N S 42  
ASN C      C  N N 43  
ASN O      O  N N 44  
ASN CB     C  N N 45  
ASN CG     C  N N 46  
ASN OD1    O  N N 47  
ASN ND2    N  N N 48  
ASN OXT    O  N N 49  
ASN H      H  N N 50  
ASN H2     H  N N 51  
ASN HA     H  N N 52  
ASN HB2    H  N N 53  
ASN HB3    H  N N 54  
ASN HD21   H  N N 55  
ASN HD22   H  N N 56  
ASN HXT    H  N N 57  
ASP N      N  N N 58  
ASP CA     C  N S 59  
ASP C      C  N N 60  
ASP O      O  N N 61  
ASP CB     C  N N 62  
ASP CG     C  N N 63  
ASP OD1    O  N N 64  
ASP OD2    O  N N 65  
ASP OXT    O  N N 66  
ASP H      H  N N 67  
ASP H2     H  N N 68  
ASP HA     H  N N 69  
ASP HB2    H  N N 70  
ASP HB3    H  N N 71  
ASP HD2    H  N N 72  
ASP HXT    H  N N 73  
CL  CL     CL N N 74  
CYS N      N  N N 75  
CYS CA     C  N R 76  
CYS C      C  N N 77  
CYS O      O  N N 78  
CYS CB     C  N N 79  
CYS SG     S  N N 80  
CYS OXT    O  N N 81  
CYS H      H  N N 82  
CYS H2     H  N N 83  
CYS HA     H  N N 84  
CYS HB2    H  N N 85  
CYS HB3    H  N N 86  
CYS HG     H  N N 87  
CYS HXT    H  N N 88  
FAD PA     P  N R 89  
FAD O1A    O  N N 90  
FAD O2A    O  N N 91  
FAD O5B    O  N N 92  
FAD C5B    C  N N 93  
FAD C4B    C  N R 94  
FAD O4B    O  N N 95  
FAD C3B    C  N S 96  
FAD O3B    O  N N 97  
FAD C2B    C  N R 98  
FAD O2B    O  N N 99  
FAD C1B    C  N R 100 
FAD N9A    N  Y N 101 
FAD C8A    C  Y N 102 
FAD N7A    N  Y N 103 
FAD C5A    C  Y N 104 
FAD C6A    C  Y N 105 
FAD N6A    N  N N 106 
FAD N1A    N  Y N 107 
FAD C2A    C  Y N 108 
FAD N3A    N  Y N 109 
FAD C4A    C  Y N 110 
FAD N1     N  N N 111 
FAD C2     C  N N 112 
FAD O2     O  N N 113 
FAD N3     N  N N 114 
FAD C4     C  N N 115 
FAD O4     O  N N 116 
FAD C4X    C  N N 117 
FAD N5     N  N N 118 
FAD C5X    C  Y N 119 
FAD C6     C  Y N 120 
FAD C7     C  Y N 121 
FAD C7M    C  N N 122 
FAD C8     C  Y N 123 
FAD C8M    C  N N 124 
FAD C9     C  Y N 125 
FAD C9A    C  Y N 126 
FAD N10    N  N N 127 
FAD C10    C  N N 128 
FAD "C1'"  C  N N 129 
FAD "C2'"  C  N S 130 
FAD "O2'"  O  N N 131 
FAD "C3'"  C  N S 132 
FAD "O3'"  O  N N 133 
FAD "C4'"  C  N R 134 
FAD "O4'"  O  N N 135 
FAD "C5'"  C  N N 136 
FAD "O5'"  O  N N 137 
FAD P      P  N R 138 
FAD O1P    O  N N 139 
FAD O2P    O  N N 140 
FAD O3P    O  N N 141 
FAD HOA2   H  N N 142 
FAD H51A   H  N N 143 
FAD H52A   H  N N 144 
FAD H4B    H  N N 145 
FAD H3B    H  N N 146 
FAD HO3A   H  N N 147 
FAD H2B    H  N N 148 
FAD HO2A   H  N N 149 
FAD H1B    H  N N 150 
FAD H8A    H  N N 151 
FAD H61A   H  N N 152 
FAD H62A   H  N N 153 
FAD H2A    H  N N 154 
FAD HN3    H  N N 155 
FAD H6     H  N N 156 
FAD HM71   H  N N 157 
FAD HM72   H  N N 158 
FAD HM73   H  N N 159 
FAD HM81   H  N N 160 
FAD HM82   H  N N 161 
FAD HM83   H  N N 162 
FAD H9     H  N N 163 
FAD "H1'1" H  N N 164 
FAD "H1'2" H  N N 165 
FAD "H2'"  H  N N 166 
FAD "HO2'" H  N N 167 
FAD "H3'"  H  N N 168 
FAD "HO3'" H  N N 169 
FAD "H4'"  H  N N 170 
FAD "HO4'" H  N N 171 
FAD "H5'1" H  N N 172 
FAD "H5'2" H  N N 173 
FAD HOP2   H  N N 174 
GLN N      N  N N 175 
GLN CA     C  N S 176 
GLN C      C  N N 177 
GLN O      O  N N 178 
GLN CB     C  N N 179 
GLN CG     C  N N 180 
GLN CD     C  N N 181 
GLN OE1    O  N N 182 
GLN NE2    N  N N 183 
GLN OXT    O  N N 184 
GLN H      H  N N 185 
GLN H2     H  N N 186 
GLN HA     H  N N 187 
GLN HB2    H  N N 188 
GLN HB3    H  N N 189 
GLN HG2    H  N N 190 
GLN HG3    H  N N 191 
GLN HE21   H  N N 192 
GLN HE22   H  N N 193 
GLN HXT    H  N N 194 
GLU N      N  N N 195 
GLU CA     C  N S 196 
GLU C      C  N N 197 
GLU O      O  N N 198 
GLU CB     C  N N 199 
GLU CG     C  N N 200 
GLU CD     C  N N 201 
GLU OE1    O  N N 202 
GLU OE2    O  N N 203 
GLU OXT    O  N N 204 
GLU H      H  N N 205 
GLU H2     H  N N 206 
GLU HA     H  N N 207 
GLU HB2    H  N N 208 
GLU HB3    H  N N 209 
GLU HG2    H  N N 210 
GLU HG3    H  N N 211 
GLU HE2    H  N N 212 
GLU HXT    H  N N 213 
GLY N      N  N N 214 
GLY CA     C  N N 215 
GLY C      C  N N 216 
GLY O      O  N N 217 
GLY OXT    O  N N 218 
GLY H      H  N N 219 
GLY H2     H  N N 220 
GLY HA2    H  N N 221 
GLY HA3    H  N N 222 
GLY HXT    H  N N 223 
HIS N      N  N N 224 
HIS CA     C  N S 225 
HIS C      C  N N 226 
HIS O      O  N N 227 
HIS CB     C  N N 228 
HIS CG     C  Y N 229 
HIS ND1    N  Y N 230 
HIS CD2    C  Y N 231 
HIS CE1    C  Y N 232 
HIS NE2    N  Y N 233 
HIS OXT    O  N N 234 
HIS H      H  N N 235 
HIS H2     H  N N 236 
HIS HA     H  N N 237 
HIS HB2    H  N N 238 
HIS HB3    H  N N 239 
HIS HD1    H  N N 240 
HIS HD2    H  N N 241 
HIS HE1    H  N N 242 
HIS HE2    H  N N 243 
HIS HXT    H  N N 244 
HOH O      O  N N 245 
HOH H1     H  N N 246 
HOH H2     H  N N 247 
ILE N      N  N N 248 
ILE CA     C  N S 249 
ILE C      C  N N 250 
ILE O      O  N N 251 
ILE CB     C  N S 252 
ILE CG1    C  N N 253 
ILE CG2    C  N N 254 
ILE CD1    C  N N 255 
ILE OXT    O  N N 256 
ILE H      H  N N 257 
ILE H2     H  N N 258 
ILE HA     H  N N 259 
ILE HB     H  N N 260 
ILE HG12   H  N N 261 
ILE HG13   H  N N 262 
ILE HG21   H  N N 263 
ILE HG22   H  N N 264 
ILE HG23   H  N N 265 
ILE HD11   H  N N 266 
ILE HD12   H  N N 267 
ILE HD13   H  N N 268 
ILE HXT    H  N N 269 
LEU N      N  N N 270 
LEU CA     C  N S 271 
LEU C      C  N N 272 
LEU O      O  N N 273 
LEU CB     C  N N 274 
LEU CG     C  N N 275 
LEU CD1    C  N N 276 
LEU CD2    C  N N 277 
LEU OXT    O  N N 278 
LEU H      H  N N 279 
LEU H2     H  N N 280 
LEU HA     H  N N 281 
LEU HB2    H  N N 282 
LEU HB3    H  N N 283 
LEU HG     H  N N 284 
LEU HD11   H  N N 285 
LEU HD12   H  N N 286 
LEU HD13   H  N N 287 
LEU HD21   H  N N 288 
LEU HD22   H  N N 289 
LEU HD23   H  N N 290 
LEU HXT    H  N N 291 
LYS N      N  N N 292 
LYS CA     C  N S 293 
LYS C      C  N N 294 
LYS O      O  N N 295 
LYS CB     C  N N 296 
LYS CG     C  N N 297 
LYS CD     C  N N 298 
LYS CE     C  N N 299 
LYS NZ     N  N N 300 
LYS OXT    O  N N 301 
LYS H      H  N N 302 
LYS H2     H  N N 303 
LYS HA     H  N N 304 
LYS HB2    H  N N 305 
LYS HB3    H  N N 306 
LYS HG2    H  N N 307 
LYS HG3    H  N N 308 
LYS HD2    H  N N 309 
LYS HD3    H  N N 310 
LYS HE2    H  N N 311 
LYS HE3    H  N N 312 
LYS HZ1    H  N N 313 
LYS HZ2    H  N N 314 
LYS HZ3    H  N N 315 
LYS HXT    H  N N 316 
MET N      N  N N 317 
MET CA     C  N S 318 
MET C      C  N N 319 
MET O      O  N N 320 
MET CB     C  N N 321 
MET CG     C  N N 322 
MET SD     S  N N 323 
MET CE     C  N N 324 
MET OXT    O  N N 325 
MET H      H  N N 326 
MET H2     H  N N 327 
MET HA     H  N N 328 
MET HB2    H  N N 329 
MET HB3    H  N N 330 
MET HG2    H  N N 331 
MET HG3    H  N N 332 
MET HE1    H  N N 333 
MET HE2    H  N N 334 
MET HE3    H  N N 335 
MET HXT    H  N N 336 
PHE N      N  N N 337 
PHE CA     C  N S 338 
PHE C      C  N N 339 
PHE O      O  N N 340 
PHE CB     C  N N 341 
PHE CG     C  Y N 342 
PHE CD1    C  Y N 343 
PHE CD2    C  Y N 344 
PHE CE1    C  Y N 345 
PHE CE2    C  Y N 346 
PHE CZ     C  Y N 347 
PHE OXT    O  N N 348 
PHE H      H  N N 349 
PHE H2     H  N N 350 
PHE HA     H  N N 351 
PHE HB2    H  N N 352 
PHE HB3    H  N N 353 
PHE HD1    H  N N 354 
PHE HD2    H  N N 355 
PHE HE1    H  N N 356 
PHE HE2    H  N N 357 
PHE HZ     H  N N 358 
PHE HXT    H  N N 359 
PRO N      N  N N 360 
PRO CA     C  N S 361 
PRO C      C  N N 362 
PRO O      O  N N 363 
PRO CB     C  N N 364 
PRO CG     C  N N 365 
PRO CD     C  N N 366 
PRO OXT    O  N N 367 
PRO H      H  N N 368 
PRO HA     H  N N 369 
PRO HB2    H  N N 370 
PRO HB3    H  N N 371 
PRO HG2    H  N N 372 
PRO HG3    H  N N 373 
PRO HD2    H  N N 374 
PRO HD3    H  N N 375 
PRO HXT    H  N N 376 
SER N      N  N N 377 
SER CA     C  N S 378 
SER C      C  N N 379 
SER O      O  N N 380 
SER CB     C  N N 381 
SER OG     O  N N 382 
SER OXT    O  N N 383 
SER H      H  N N 384 
SER H2     H  N N 385 
SER HA     H  N N 386 
SER HB2    H  N N 387 
SER HB3    H  N N 388 
SER HG     H  N N 389 
SER HXT    H  N N 390 
THR N      N  N N 391 
THR CA     C  N S 392 
THR C      C  N N 393 
THR O      O  N N 394 
THR CB     C  N R 395 
THR OG1    O  N N 396 
THR CG2    C  N N 397 
THR OXT    O  N N 398 
THR H      H  N N 399 
THR H2     H  N N 400 
THR HA     H  N N 401 
THR HB     H  N N 402 
THR HG1    H  N N 403 
THR HG21   H  N N 404 
THR HG22   H  N N 405 
THR HG23   H  N N 406 
THR HXT    H  N N 407 
TRP N      N  N N 408 
TRP CA     C  N S 409 
TRP C      C  N N 410 
TRP O      O  N N 411 
TRP CB     C  N N 412 
TRP CG     C  Y N 413 
TRP CD1    C  Y N 414 
TRP CD2    C  Y N 415 
TRP NE1    N  Y N 416 
TRP CE2    C  Y N 417 
TRP CE3    C  Y N 418 
TRP CZ2    C  Y N 419 
TRP CZ3    C  Y N 420 
TRP CH2    C  Y N 421 
TRP OXT    O  N N 422 
TRP H      H  N N 423 
TRP H2     H  N N 424 
TRP HA     H  N N 425 
TRP HB2    H  N N 426 
TRP HB3    H  N N 427 
TRP HD1    H  N N 428 
TRP HE1    H  N N 429 
TRP HE3    H  N N 430 
TRP HZ2    H  N N 431 
TRP HZ3    H  N N 432 
TRP HH2    H  N N 433 
TRP HXT    H  N N 434 
TYR N      N  N N 435 
TYR CA     C  N S 436 
TYR C      C  N N 437 
TYR O      O  N N 438 
TYR CB     C  N N 439 
TYR CG     C  Y N 440 
TYR CD1    C  Y N 441 
TYR CD2    C  Y N 442 
TYR CE1    C  Y N 443 
TYR CE2    C  Y N 444 
TYR CZ     C  Y N 445 
TYR OH     O  N N 446 
TYR OXT    O  N N 447 
TYR H      H  N N 448 
TYR H2     H  N N 449 
TYR HA     H  N N 450 
TYR HB2    H  N N 451 
TYR HB3    H  N N 452 
TYR HD1    H  N N 453 
TYR HD2    H  N N 454 
TYR HE1    H  N N 455 
TYR HE2    H  N N 456 
TYR HH     H  N N 457 
TYR HXT    H  N N 458 
VAL N      N  N N 459 
VAL CA     C  N S 460 
VAL C      C  N N 461 
VAL O      O  N N 462 
VAL CB     C  N N 463 
VAL CG1    C  N N 464 
VAL CG2    C  N N 465 
VAL OXT    O  N N 466 
VAL H      H  N N 467 
VAL H2     H  N N 468 
VAL HA     H  N N 469 
VAL HB     H  N N 470 
VAL HG11   H  N N 471 
VAL HG12   H  N N 472 
VAL HG13   H  N N 473 
VAL HG21   H  N N 474 
VAL HG22   H  N N 475 
VAL HG23   H  N N 476 
VAL HXT    H  N N 477 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N     CA     sing N N 1   
ALA N     H      sing N N 2   
ALA N     H2     sing N N 3   
ALA CA    C      sing N N 4   
ALA CA    CB     sing N N 5   
ALA CA    HA     sing N N 6   
ALA C     O      doub N N 7   
ALA C     OXT    sing N N 8   
ALA CB    HB1    sing N N 9   
ALA CB    HB2    sing N N 10  
ALA CB    HB3    sing N N 11  
ALA OXT   HXT    sing N N 12  
ARG N     CA     sing N N 13  
ARG N     H      sing N N 14  
ARG N     H2     sing N N 15  
ARG CA    C      sing N N 16  
ARG CA    CB     sing N N 17  
ARG CA    HA     sing N N 18  
ARG C     O      doub N N 19  
ARG C     OXT    sing N N 20  
ARG CB    CG     sing N N 21  
ARG CB    HB2    sing N N 22  
ARG CB    HB3    sing N N 23  
ARG CG    CD     sing N N 24  
ARG CG    HG2    sing N N 25  
ARG CG    HG3    sing N N 26  
ARG CD    NE     sing N N 27  
ARG CD    HD2    sing N N 28  
ARG CD    HD3    sing N N 29  
ARG NE    CZ     sing N N 30  
ARG NE    HE     sing N N 31  
ARG CZ    NH1    sing N N 32  
ARG CZ    NH2    doub N N 33  
ARG NH1   HH11   sing N N 34  
ARG NH1   HH12   sing N N 35  
ARG NH2   HH21   sing N N 36  
ARG NH2   HH22   sing N N 37  
ARG OXT   HXT    sing N N 38  
ASN N     CA     sing N N 39  
ASN N     H      sing N N 40  
ASN N     H2     sing N N 41  
ASN CA    C      sing N N 42  
ASN CA    CB     sing N N 43  
ASN CA    HA     sing N N 44  
ASN C     O      doub N N 45  
ASN C     OXT    sing N N 46  
ASN CB    CG     sing N N 47  
ASN CB    HB2    sing N N 48  
ASN CB    HB3    sing N N 49  
ASN CG    OD1    doub N N 50  
ASN CG    ND2    sing N N 51  
ASN ND2   HD21   sing N N 52  
ASN ND2   HD22   sing N N 53  
ASN OXT   HXT    sing N N 54  
ASP N     CA     sing N N 55  
ASP N     H      sing N N 56  
ASP N     H2     sing N N 57  
ASP CA    C      sing N N 58  
ASP CA    CB     sing N N 59  
ASP CA    HA     sing N N 60  
ASP C     O      doub N N 61  
ASP C     OXT    sing N N 62  
ASP CB    CG     sing N N 63  
ASP CB    HB2    sing N N 64  
ASP CB    HB3    sing N N 65  
ASP CG    OD1    doub N N 66  
ASP CG    OD2    sing N N 67  
ASP OD2   HD2    sing N N 68  
ASP OXT   HXT    sing N N 69  
CYS N     CA     sing N N 70  
CYS N     H      sing N N 71  
CYS N     H2     sing N N 72  
CYS CA    C      sing N N 73  
CYS CA    CB     sing N N 74  
CYS CA    HA     sing N N 75  
CYS C     O      doub N N 76  
CYS C     OXT    sing N N 77  
CYS CB    SG     sing N N 78  
CYS CB    HB2    sing N N 79  
CYS CB    HB3    sing N N 80  
CYS SG    HG     sing N N 81  
CYS OXT   HXT    sing N N 82  
FAD PA    O1A    doub N N 83  
FAD PA    O2A    sing N N 84  
FAD PA    O5B    sing N N 85  
FAD PA    O3P    sing N N 86  
FAD O2A   HOA2   sing N N 87  
FAD O5B   C5B    sing N N 88  
FAD C5B   C4B    sing N N 89  
FAD C5B   H51A   sing N N 90  
FAD C5B   H52A   sing N N 91  
FAD C4B   O4B    sing N N 92  
FAD C4B   C3B    sing N N 93  
FAD C4B   H4B    sing N N 94  
FAD O4B   C1B    sing N N 95  
FAD C3B   O3B    sing N N 96  
FAD C3B   C2B    sing N N 97  
FAD C3B   H3B    sing N N 98  
FAD O3B   HO3A   sing N N 99  
FAD C2B   O2B    sing N N 100 
FAD C2B   C1B    sing N N 101 
FAD C2B   H2B    sing N N 102 
FAD O2B   HO2A   sing N N 103 
FAD C1B   N9A    sing N N 104 
FAD C1B   H1B    sing N N 105 
FAD N9A   C8A    sing Y N 106 
FAD N9A   C4A    sing Y N 107 
FAD C8A   N7A    doub Y N 108 
FAD C8A   H8A    sing N N 109 
FAD N7A   C5A    sing Y N 110 
FAD C5A   C6A    sing Y N 111 
FAD C5A   C4A    doub Y N 112 
FAD C6A   N6A    sing N N 113 
FAD C6A   N1A    doub Y N 114 
FAD N6A   H61A   sing N N 115 
FAD N6A   H62A   sing N N 116 
FAD N1A   C2A    sing Y N 117 
FAD C2A   N3A    doub Y N 118 
FAD C2A   H2A    sing N N 119 
FAD N3A   C4A    sing Y N 120 
FAD N1    C2     sing N N 121 
FAD N1    C10    doub N N 122 
FAD C2    O2     doub N N 123 
FAD C2    N3     sing N N 124 
FAD N3    C4     sing N N 125 
FAD N3    HN3    sing N N 126 
FAD C4    O4     doub N N 127 
FAD C4    C4X    sing N N 128 
FAD C4X   N5     doub N N 129 
FAD C4X   C10    sing N N 130 
FAD N5    C5X    sing N N 131 
FAD C5X   C6     doub Y N 132 
FAD C5X   C9A    sing Y N 133 
FAD C6    C7     sing Y N 134 
FAD C6    H6     sing N N 135 
FAD C7    C7M    sing N N 136 
FAD C7    C8     doub Y N 137 
FAD C7M   HM71   sing N N 138 
FAD C7M   HM72   sing N N 139 
FAD C7M   HM73   sing N N 140 
FAD C8    C8M    sing N N 141 
FAD C8    C9     sing Y N 142 
FAD C8M   HM81   sing N N 143 
FAD C8M   HM82   sing N N 144 
FAD C8M   HM83   sing N N 145 
FAD C9    C9A    doub Y N 146 
FAD C9    H9     sing N N 147 
FAD C9A   N10    sing N N 148 
FAD N10   C10    sing N N 149 
FAD N10   "C1'"  sing N N 150 
FAD "C1'" "C2'"  sing N N 151 
FAD "C1'" "H1'1" sing N N 152 
FAD "C1'" "H1'2" sing N N 153 
FAD "C2'" "O2'"  sing N N 154 
FAD "C2'" "C3'"  sing N N 155 
FAD "C2'" "H2'"  sing N N 156 
FAD "O2'" "HO2'" sing N N 157 
FAD "C3'" "O3'"  sing N N 158 
FAD "C3'" "C4'"  sing N N 159 
FAD "C3'" "H3'"  sing N N 160 
FAD "O3'" "HO3'" sing N N 161 
FAD "C4'" "O4'"  sing N N 162 
FAD "C4'" "C5'"  sing N N 163 
FAD "C4'" "H4'"  sing N N 164 
FAD "O4'" "HO4'" sing N N 165 
FAD "C5'" "O5'"  sing N N 166 
FAD "C5'" "H5'1" sing N N 167 
FAD "C5'" "H5'2" sing N N 168 
FAD "O5'" P      sing N N 169 
FAD P     O1P    doub N N 170 
FAD P     O2P    sing N N 171 
FAD P     O3P    sing N N 172 
FAD O2P   HOP2   sing N N 173 
GLN N     CA     sing N N 174 
GLN N     H      sing N N 175 
GLN N     H2     sing N N 176 
GLN CA    C      sing N N 177 
GLN CA    CB     sing N N 178 
GLN CA    HA     sing N N 179 
GLN C     O      doub N N 180 
GLN C     OXT    sing N N 181 
GLN CB    CG     sing N N 182 
GLN CB    HB2    sing N N 183 
GLN CB    HB3    sing N N 184 
GLN CG    CD     sing N N 185 
GLN CG    HG2    sing N N 186 
GLN CG    HG3    sing N N 187 
GLN CD    OE1    doub N N 188 
GLN CD    NE2    sing N N 189 
GLN NE2   HE21   sing N N 190 
GLN NE2   HE22   sing N N 191 
GLN OXT   HXT    sing N N 192 
GLU N     CA     sing N N 193 
GLU N     H      sing N N 194 
GLU N     H2     sing N N 195 
GLU CA    C      sing N N 196 
GLU CA    CB     sing N N 197 
GLU CA    HA     sing N N 198 
GLU C     O      doub N N 199 
GLU C     OXT    sing N N 200 
GLU CB    CG     sing N N 201 
GLU CB    HB2    sing N N 202 
GLU CB    HB3    sing N N 203 
GLU CG    CD     sing N N 204 
GLU CG    HG2    sing N N 205 
GLU CG    HG3    sing N N 206 
GLU CD    OE1    doub N N 207 
GLU CD    OE2    sing N N 208 
GLU OE2   HE2    sing N N 209 
GLU OXT   HXT    sing N N 210 
GLY N     CA     sing N N 211 
GLY N     H      sing N N 212 
GLY N     H2     sing N N 213 
GLY CA    C      sing N N 214 
GLY CA    HA2    sing N N 215 
GLY CA    HA3    sing N N 216 
GLY C     O      doub N N 217 
GLY C     OXT    sing N N 218 
GLY OXT   HXT    sing N N 219 
HIS N     CA     sing N N 220 
HIS N     H      sing N N 221 
HIS N     H2     sing N N 222 
HIS CA    C      sing N N 223 
HIS CA    CB     sing N N 224 
HIS CA    HA     sing N N 225 
HIS C     O      doub N N 226 
HIS C     OXT    sing N N 227 
HIS CB    CG     sing N N 228 
HIS CB    HB2    sing N N 229 
HIS CB    HB3    sing N N 230 
HIS CG    ND1    sing Y N 231 
HIS CG    CD2    doub Y N 232 
HIS ND1   CE1    doub Y N 233 
HIS ND1   HD1    sing N N 234 
HIS CD2   NE2    sing Y N 235 
HIS CD2   HD2    sing N N 236 
HIS CE1   NE2    sing Y N 237 
HIS CE1   HE1    sing N N 238 
HIS NE2   HE2    sing N N 239 
HIS OXT   HXT    sing N N 240 
HOH O     H1     sing N N 241 
HOH O     H2     sing N N 242 
ILE N     CA     sing N N 243 
ILE N     H      sing N N 244 
ILE N     H2     sing N N 245 
ILE CA    C      sing N N 246 
ILE CA    CB     sing N N 247 
ILE CA    HA     sing N N 248 
ILE C     O      doub N N 249 
ILE C     OXT    sing N N 250 
ILE CB    CG1    sing N N 251 
ILE CB    CG2    sing N N 252 
ILE CB    HB     sing N N 253 
ILE CG1   CD1    sing N N 254 
ILE CG1   HG12   sing N N 255 
ILE CG1   HG13   sing N N 256 
ILE CG2   HG21   sing N N 257 
ILE CG2   HG22   sing N N 258 
ILE CG2   HG23   sing N N 259 
ILE CD1   HD11   sing N N 260 
ILE CD1   HD12   sing N N 261 
ILE CD1   HD13   sing N N 262 
ILE OXT   HXT    sing N N 263 
LEU N     CA     sing N N 264 
LEU N     H      sing N N 265 
LEU N     H2     sing N N 266 
LEU CA    C      sing N N 267 
LEU CA    CB     sing N N 268 
LEU CA    HA     sing N N 269 
LEU C     O      doub N N 270 
LEU C     OXT    sing N N 271 
LEU CB    CG     sing N N 272 
LEU CB    HB2    sing N N 273 
LEU CB    HB3    sing N N 274 
LEU CG    CD1    sing N N 275 
LEU CG    CD2    sing N N 276 
LEU CG    HG     sing N N 277 
LEU CD1   HD11   sing N N 278 
LEU CD1   HD12   sing N N 279 
LEU CD1   HD13   sing N N 280 
LEU CD2   HD21   sing N N 281 
LEU CD2   HD22   sing N N 282 
LEU CD2   HD23   sing N N 283 
LEU OXT   HXT    sing N N 284 
LYS N     CA     sing N N 285 
LYS N     H      sing N N 286 
LYS N     H2     sing N N 287 
LYS CA    C      sing N N 288 
LYS CA    CB     sing N N 289 
LYS CA    HA     sing N N 290 
LYS C     O      doub N N 291 
LYS C     OXT    sing N N 292 
LYS CB    CG     sing N N 293 
LYS CB    HB2    sing N N 294 
LYS CB    HB3    sing N N 295 
LYS CG    CD     sing N N 296 
LYS CG    HG2    sing N N 297 
LYS CG    HG3    sing N N 298 
LYS CD    CE     sing N N 299 
LYS CD    HD2    sing N N 300 
LYS CD    HD3    sing N N 301 
LYS CE    NZ     sing N N 302 
LYS CE    HE2    sing N N 303 
LYS CE    HE3    sing N N 304 
LYS NZ    HZ1    sing N N 305 
LYS NZ    HZ2    sing N N 306 
LYS NZ    HZ3    sing N N 307 
LYS OXT   HXT    sing N N 308 
MET N     CA     sing N N 309 
MET N     H      sing N N 310 
MET N     H2     sing N N 311 
MET CA    C      sing N N 312 
MET CA    CB     sing N N 313 
MET CA    HA     sing N N 314 
MET C     O      doub N N 315 
MET C     OXT    sing N N 316 
MET CB    CG     sing N N 317 
MET CB    HB2    sing N N 318 
MET CB    HB3    sing N N 319 
MET CG    SD     sing N N 320 
MET CG    HG2    sing N N 321 
MET CG    HG3    sing N N 322 
MET SD    CE     sing N N 323 
MET CE    HE1    sing N N 324 
MET CE    HE2    sing N N 325 
MET CE    HE3    sing N N 326 
MET OXT   HXT    sing N N 327 
PHE N     CA     sing N N 328 
PHE N     H      sing N N 329 
PHE N     H2     sing N N 330 
PHE CA    C      sing N N 331 
PHE CA    CB     sing N N 332 
PHE CA    HA     sing N N 333 
PHE C     O      doub N N 334 
PHE C     OXT    sing N N 335 
PHE CB    CG     sing N N 336 
PHE CB    HB2    sing N N 337 
PHE CB    HB3    sing N N 338 
PHE CG    CD1    doub Y N 339 
PHE CG    CD2    sing Y N 340 
PHE CD1   CE1    sing Y N 341 
PHE CD1   HD1    sing N N 342 
PHE CD2   CE2    doub Y N 343 
PHE CD2   HD2    sing N N 344 
PHE CE1   CZ     doub Y N 345 
PHE CE1   HE1    sing N N 346 
PHE CE2   CZ     sing Y N 347 
PHE CE2   HE2    sing N N 348 
PHE CZ    HZ     sing N N 349 
PHE OXT   HXT    sing N N 350 
PRO N     CA     sing N N 351 
PRO N     CD     sing N N 352 
PRO N     H      sing N N 353 
PRO CA    C      sing N N 354 
PRO CA    CB     sing N N 355 
PRO CA    HA     sing N N 356 
PRO C     O      doub N N 357 
PRO C     OXT    sing N N 358 
PRO CB    CG     sing N N 359 
PRO CB    HB2    sing N N 360 
PRO CB    HB3    sing N N 361 
PRO CG    CD     sing N N 362 
PRO CG    HG2    sing N N 363 
PRO CG    HG3    sing N N 364 
PRO CD    HD2    sing N N 365 
PRO CD    HD3    sing N N 366 
PRO OXT   HXT    sing N N 367 
SER N     CA     sing N N 368 
SER N     H      sing N N 369 
SER N     H2     sing N N 370 
SER CA    C      sing N N 371 
SER CA    CB     sing N N 372 
SER CA    HA     sing N N 373 
SER C     O      doub N N 374 
SER C     OXT    sing N N 375 
SER CB    OG     sing N N 376 
SER CB    HB2    sing N N 377 
SER CB    HB3    sing N N 378 
SER OG    HG     sing N N 379 
SER OXT   HXT    sing N N 380 
THR N     CA     sing N N 381 
THR N     H      sing N N 382 
THR N     H2     sing N N 383 
THR CA    C      sing N N 384 
THR CA    CB     sing N N 385 
THR CA    HA     sing N N 386 
THR C     O      doub N N 387 
THR C     OXT    sing N N 388 
THR CB    OG1    sing N N 389 
THR CB    CG2    sing N N 390 
THR CB    HB     sing N N 391 
THR OG1   HG1    sing N N 392 
THR CG2   HG21   sing N N 393 
THR CG2   HG22   sing N N 394 
THR CG2   HG23   sing N N 395 
THR OXT   HXT    sing N N 396 
TRP N     CA     sing N N 397 
TRP N     H      sing N N 398 
TRP N     H2     sing N N 399 
TRP CA    C      sing N N 400 
TRP CA    CB     sing N N 401 
TRP CA    HA     sing N N 402 
TRP C     O      doub N N 403 
TRP C     OXT    sing N N 404 
TRP CB    CG     sing N N 405 
TRP CB    HB2    sing N N 406 
TRP CB    HB3    sing N N 407 
TRP CG    CD1    doub Y N 408 
TRP CG    CD2    sing Y N 409 
TRP CD1   NE1    sing Y N 410 
TRP CD1   HD1    sing N N 411 
TRP CD2   CE2    doub Y N 412 
TRP CD2   CE3    sing Y N 413 
TRP NE1   CE2    sing Y N 414 
TRP NE1   HE1    sing N N 415 
TRP CE2   CZ2    sing Y N 416 
TRP CE3   CZ3    doub Y N 417 
TRP CE3   HE3    sing N N 418 
TRP CZ2   CH2    doub Y N 419 
TRP CZ2   HZ2    sing N N 420 
TRP CZ3   CH2    sing Y N 421 
TRP CZ3   HZ3    sing N N 422 
TRP CH2   HH2    sing N N 423 
TRP OXT   HXT    sing N N 424 
TYR N     CA     sing N N 425 
TYR N     H      sing N N 426 
TYR N     H2     sing N N 427 
TYR CA    C      sing N N 428 
TYR CA    CB     sing N N 429 
TYR CA    HA     sing N N 430 
TYR C     O      doub N N 431 
TYR C     OXT    sing N N 432 
TYR CB    CG     sing N N 433 
TYR CB    HB2    sing N N 434 
TYR CB    HB3    sing N N 435 
TYR CG    CD1    doub Y N 436 
TYR CG    CD2    sing Y N 437 
TYR CD1   CE1    sing Y N 438 
TYR CD1   HD1    sing N N 439 
TYR CD2   CE2    doub Y N 440 
TYR CD2   HD2    sing N N 441 
TYR CE1   CZ     doub Y N 442 
TYR CE1   HE1    sing N N 443 
TYR CE2   CZ     sing Y N 444 
TYR CE2   HE2    sing N N 445 
TYR CZ    OH     sing N N 446 
TYR OH    HH     sing N N 447 
TYR OXT   HXT    sing N N 448 
VAL N     CA     sing N N 449 
VAL N     H      sing N N 450 
VAL N     H2     sing N N 451 
VAL CA    C      sing N N 452 
VAL CA    CB     sing N N 453 
VAL CA    HA     sing N N 454 
VAL C     O      doub N N 455 
VAL C     OXT    sing N N 456 
VAL CB    CG1    sing N N 457 
VAL CB    CG2    sing N N 458 
VAL CB    HB     sing N N 459 
VAL CG1   HG11   sing N N 460 
VAL CG1   HG12   sing N N 461 
VAL CG1   HG13   sing N N 462 
VAL CG2   HG21   sing N N 463 
VAL CG2   HG22   sing N N 464 
VAL CG2   HG23   sing N N 465 
VAL OXT   HXT    sing N N 466 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Ministry of Science and Technology (MoST, Taiwan)'                      Taiwan AS-KPQ-105-TPP         1 
'Ministry of Science and Technology (MoST, Taiwan)'                      Taiwan AS-KPQ-109-TPP2        2 
'Ministry of Education, Culture, Sports, Science and Technology (Japan)' Japan  JP20H05442             3 
'Ministry of Education, Culture, Sports, Science and Technology (Japan)' Japan  JP22H04751             4 
'Japan Science and Technology'                                           Japan  JPMJFR2057             5 
'Japan Society for the Promotion of Science (JSPS)'                      Japan  JP19H05776             6 
'National Science Council (NSC, Taiwan)'                                 Taiwan 111-2113-M-002-029-MY3 7 
'Japan Society for the Promotion of Science (JSPS)'                      Japan  JP21J13329             8 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   6fn3 
_pdbx_initial_refinement_model.details          ? 
# 
_pdbx_serial_crystallography_measurement.diffrn_id                    1 
_pdbx_serial_crystallography_measurement.pulse_energy                 ? 
_pdbx_serial_crystallography_measurement.pulse_duration               10 
_pdbx_serial_crystallography_measurement.xfel_pulse_repetition_rate   30 
_pdbx_serial_crystallography_measurement.pulse_photon_energy          10 
_pdbx_serial_crystallography_measurement.photons_per_pulse            ? 
_pdbx_serial_crystallography_measurement.source_size                  ? 
_pdbx_serial_crystallography_measurement.source_distance              ? 
_pdbx_serial_crystallography_measurement.focal_spot_size              1.77 
_pdbx_serial_crystallography_measurement.collimation                  ? 
_pdbx_serial_crystallography_measurement.collection_time_total        ? 
# 
_pdbx_serial_crystallography_sample_delivery.diffrn_id     1 
_pdbx_serial_crystallography_sample_delivery.description   ? 
_pdbx_serial_crystallography_sample_delivery.method        injection 
# 
_pdbx_serial_crystallography_sample_delivery_injection.diffrn_id               1 
_pdbx_serial_crystallography_sample_delivery_injection.description             'High viscosity injector' 
_pdbx_serial_crystallography_sample_delivery_injection.injector_diameter       75 
_pdbx_serial_crystallography_sample_delivery_injection.injector_temperature    293 
_pdbx_serial_crystallography_sample_delivery_injection.injector_pressure       ? 
_pdbx_serial_crystallography_sample_delivery_injection.flow_rate               2.8 
_pdbx_serial_crystallography_sample_delivery_injection.carrier_solvent         grease 
_pdbx_serial_crystallography_sample_delivery_injection.crystal_concentration   ? 
_pdbx_serial_crystallography_sample_delivery_injection.preparation             ? 
_pdbx_serial_crystallography_sample_delivery_injection.power_by                ? 
_pdbx_serial_crystallography_sample_delivery_injection.injector_nozzle         ? 
_pdbx_serial_crystallography_sample_delivery_injection.jet_diameter            ? 
_pdbx_serial_crystallography_sample_delivery_injection.filter_size             50 
# 
_space_group.name_H-M_alt     'P 21 21 21' 
_space_group.name_Hall        'P 2ac 2ab' 
_space_group.IT_number        19 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    8Z44 
_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    N  N     . GLY A 1 3   ? 28.76627  31.62050  -8.89479  0.000 25.79829 ? 3   GLY A N     1 
ATOM   2    C  CA    . GLY A 1 3   ? 30.19428  31.49752  -8.62582  0.000 26.14036 ? 3   GLY A CA    1 
ATOM   3    C  C     . GLY A 1 3   ? 30.52830  30.12854  -8.04378  1.000 26.76119 ? 3   GLY A C     1 
ATOM   4    O  O     . GLY A 1 3   ? 31.58632  29.89656  -7.45080  0.000 25.34627 ? 3   GLY A O     1 
ATOM   5    N  N     . VAL A 1 4   ? 29.62031  29.17853  -8.20874  1.000 27.06673 ? 4   VAL A N     1 
ATOM   6    C  CA    . VAL A 1 4   ? 29.82133  27.82654  -7.69970  1.000 22.41510 ? 4   VAL A CA    1 
ATOM   7    C  C     . VAL A 1 4   ? 29.22632  26.82951  -8.68266  1.000 22.19840 ? 4   VAL A C     1 
ATOM   8    O  O     . VAL A 1 4   ? 28.46029  27.20447  -9.57865  1.000 21.33100 ? 4   VAL A O     1 
ATOM   9    C  CB    . VAL A 1 4   ? 29.20436  27.65758  -6.29868  1.000 20.63429 ? 4   VAL A CB    1 
ATOM   10   C  CG1   . VAL A 1 4   ? 29.72737  28.73261  -5.35672  1.000 18.22182 ? 4   VAL A CG1   1 
ATOM   11   C  CG2   . VAL A 1 4   ? 27.68536  27.69857  -6.37865  1.000 22.70513 ? 4   VAL A CG2   1 
ATOM   12   N  N     . LYS A 1 5   ? 29.57133  25.55352  -8.52263  1.000 18.97493 ? 5   LYS A N     1 
ATOM   13   C  CA    . LYS A 1 5   ? 29.11132  24.49548  -9.41458  1.000 13.93735 ? 5   LYS A CA    1 
ATOM   14   C  C     . LYS A 1 5   ? 27.93634  23.77150  -8.76654  1.000 15.83017 ? 5   LYS A C     1 
ATOM   15   O  O     . LYS A 1 5   ? 28.09836  23.10053  -7.74252  1.000 14.32332 ? 5   LYS A O     1 
ATOM   16   C  CB    . LYS A 1 5   ? 30.24032  23.51748  -9.73358  1.000 16.04159 ? 5   LYS A CB    1 
ATOM   17   C  CG    . LYS A 1 5   ? 29.78931  22.31746  -10.55353 1.000 15.79328 ? 5   LYS A CG    1 
ATOM   18   C  CD    . LYS A 1 5   ? 30.91132  21.31046  -10.75052 1.000 13.33667 ? 5   LYS A CD    1 
ATOM   19   C  CE    . LYS A 1 5   ? 30.41331  20.08643  -11.49948 1.000 11.61017 ? 5   LYS A CE    1 
ATOM   20   N  NZ    . LYS A 1 5   ? 31.48531  19.07443  -11.70747 1.000 12.64580 ? 5   LYS A NZ    1 
ATOM   21   N  N     . ASN A 1 6   ? 26.75732  23.91147  -9.36552  1.000 11.72581 ? 6   ASN A N     1 
ATOM   22   C  CA    . ASN A 1 6   ? 25.57134  23.15647  -8.98547  1.000 11.03783 ? 6   ASN A CA    1 
ATOM   23   C  C     . ASN A 1 6   ? 25.19932  22.25243  -10.15143 1.000 10.66238 ? 6   ASN A C     1 
ATOM   24   O  O     . ASN A 1 6   ? 24.87029  22.74140  -11.23744 1.000 9.38945  ? 6   ASN A O     1 
ATOM   25   C  CB    . ASN A 1 6   ? 24.41434  24.08747  -8.62447  1.000 12.94729 ? 6   ASN A CB    1 
ATOM   26   C  CG    . ASN A 1 6   ? 24.69836  24.91851  -7.39050  1.000 13.53252 ? 6   ASN A CG    1 
ATOM   27   O  OD1   . ASN A 1 6   ? 25.33438  24.45055  -6.44450  1.000 15.32872 ? 6   ASN A OD1   1 
ATOM   28   N  ND2   . ASN A 1 6   ? 24.22935  26.16051  -7.39153  1.000 14.81299 ? 6   ASN A ND2   1 
ATOM   29   N  N     . SER A 1 7   ? 25.25934  20.94344  -9.93139  1.000 10.92861 ? 7   SER A N     1 
ATOM   30   C  CA    . SER A 1 7   ? 25.08232  19.96941  -10.99536 1.000 11.22249 ? 7   SER A CA    1 
ATOM   31   C  C     . SER A 1 7   ? 23.83633  19.12740  -10.75531 1.000 7.82705  ? 7   SER A C     1 
ATOM   32   O  O     . SER A 1 7   ? 23.34636  19.00243  -9.63029  1.000 7.53647  ? 7   SER A O     1 
ATOM   33   C  CB    . SER A 1 7   ? 26.30933  19.05441  -11.11736 1.000 10.81585 ? 7   SER A CB    1 
ATOM   34   O  OG    . SER A 1 7   ? 26.54836  18.35645  -9.90834  1.000 10.47367 ? 7   SER A OG    1 
ATOM   35   N  N     . ILE A 1 8   ? 23.32831  18.55237  -11.84328 1.000 7.30744  ? 8   ILE A N     1 
ATOM   36   C  CA    . ILE A 1 8   ? 22.21332  17.61536  -11.81223 1.000 7.07450  ? 8   ILE A CA    1 
ATOM   37   C  C     . ILE A 1 8   ? 22.66332  16.32134  -12.47220 1.000 6.82412  ? 8   ILE A C     1 
ATOM   38   O  O     . ILE A 1 8   ? 23.18629  16.34031  -13.59221 1.000 7.10170  ? 8   ILE A O     1 
ATOM   39   C  CB    . ILE A 1 8   ? 20.96930  18.17533  -12.52622 1.000 9.31853  ? 8   ILE A CB    1 
ATOM   40   C  CG1   . ILE A 1 8   ? 20.40931  19.38734  -11.78324 1.000 9.00142  ? 8   ILE A CG1   1 
ATOM   41   C  CG2   . ILE A 1 8   ? 19.90231  17.09731  -12.66416 1.000 7.57928  ? 8   ILE A CG2   1 
ATOM   42   C  CD1   . ILE A 1 8   ? 19.11929  19.90932  -12.37923 1.000 12.55915 ? 8   ILE A CD1   1 
ATOM   43   N  N     . ILE A 1 9   ? 22.46734  15.20536  -11.78016 1.000 7.17269  ? 9   ILE A N     1 
ATOM   44   C  CA    . ILE A 1 9   ? 22.69034  13.87935  -12.34213 1.000 8.09287  ? 9   ILE A CA    1 
ATOM   45   C  C     . ILE A 1 9   ? 21.31934  13.28133  -12.62808 1.000 6.98604  ? 9   ILE A C     1 
ATOM   46   O  O     . ILE A 1 9   ? 20.57836  12.91635  -11.70605 1.000 6.40981  ? 9   ILE A O     1 
ATOM   47   C  CB    . ILE A 1 9   ? 23.52937  12.98938  -11.41212 1.000 6.89405  ? 9   ILE A CB    1 
ATOM   48   C  CG1   . ILE A 1 9   ? 23.45237  11.52237  -11.85007 1.000 7.18132  ? 9   ILE A CG1   1 
ATOM   49   C  CG2   . ILE A 1 9   ? 23.12340  13.17542  -9.95411  1.000 6.71038  ? 9   ILE A CG2   1 
ATOM   50   C  CD1   . ILE A 1 9   ? 24.08434  11.25233  -13.20108 1.000 7.85754  ? 9   ILE A CD1   1 
ATOM   51   N  N     . TRP A 1 10  ? 20.97231  13.19828  -13.90907 1.000 7.23298  ? 10  TRP A N     1 
ATOM   52   C  CA    . TRP A 1 10  ? 19.64531  12.77526  -14.33803 1.000 6.33802  ? 10  TRP A CA    1 
ATOM   53   C  C     . TRP A 1 10  ? 19.64431  11.27025  -14.57798 1.000 6.69937  ? 10  TRP A C     1 
ATOM   54   O  O     . TRP A 1 10  ? 20.34430  10.77623  -15.46798 1.000 6.34910  ? 10  TRP A O     1 
ATOM   55   C  CB    . TRP A 1 10  ? 19.23427  13.52622  -15.60504 1.000 6.99895  ? 10  TRP A CB    1 
ATOM   56   C  CG    . TRP A 1 10  ? 17.88127  13.15619  -16.13600 1.000 7.78801  ? 10  TRP A CG    1 
ATOM   57   C  CD1   . TRP A 1 10  ? 16.86428  12.55121  -15.45296 1.000 8.29854  ? 10  TRP A CD1   1 
ATOM   58   C  CD2   . TRP A 1 10  ? 17.40224  13.36315  -17.46900 1.000 8.90166  ? 10  TRP A CD2   1 
ATOM   59   N  NE1   . TRP A 1 10  ? 15.78127  12.37217  -16.27893 1.000 8.90304  ? 10  TRP A NE1   1 
ATOM   60   C  CE2   . TRP A 1 10  ? 16.08624  12.86014  -17.52296 1.000 7.72979  ? 10  TRP A CE2   1 
ATOM   61   C  CE3   . TRP A 1 10  ? 17.95721  13.92412  -18.62303 1.000 7.28906  ? 10  TRP A CE3   1 
ATOM   62   C  CZ2   . TRP A 1 10  ? 15.31821  12.90410  -18.68294 1.000 9.77279  ? 10  TRP A CZ2   1 
ATOM   63   C  CZ3   . TRP A 1 10  ? 17.19218  13.96608  -19.77401 1.000 8.90688  ? 10  TRP A CZ3   1 
ATOM   64   C  CH2   . TRP A 1 10  ? 15.88819  13.45907  -19.79597 1.000 11.94173 ? 10  TRP A CH2   1 
ATOM   65   N  N     . PHE A 1 11  ? 18.85334  10.54827  -13.79094 1.000 6.95845  ? 11  PHE A N     1 
ATOM   66   C  CA    . PHE A 1 11  ? 18.73034  9.10527   -13.93690 1.000 6.43193  ? 11  PHE A CA    1 
ATOM   67   C  C     . PHE A 1 11  ? 17.58733  8.77123   -14.88586 1.000 6.42419  ? 11  PHE A C     1 
ATOM   68   O  O     . PHE A 1 11  ? 16.47633  9.29122   -14.74086 1.000 7.63769  ? 11  PHE A O     1 
ATOM   69   C  CB    . PHE A 1 11  ? 18.50238  8.43831   -12.57887 1.000 6.12430  ? 11  PHE A CB    1 
ATOM   70   C  CG    . PHE A 1 11  ? 19.71340  8.43634   -11.69190 1.000 6.41177  ? 11  PHE A CG    1 
ATOM   71   C  CD1   . PHE A 1 11  ? 20.68640  7.45935   -11.82889 1.000 6.04046  ? 11  PHE A CD1   1 
ATOM   72   C  CD2   . PHE A 1 11  ? 19.88041  9.41037   -10.72093 1.000 8.25468  ? 11  PHE A CD2   1 
ATOM   73   C  CE1   . PHE A 1 11  ? 21.80242  7.45538   -11.01491 1.000 6.87265  ? 11  PHE A CE1   1 
ATOM   74   C  CE2   . PHE A 1 11  ? 20.99443  9.41141   -9.90395  1.000 7.13303  ? 11  PHE A CE2   1 
ATOM   75   C  CZ    . PHE A 1 11  ? 21.95743  8.43141   -10.05095 1.000 7.68189  ? 11  PHE A CZ    1 
ATOM   76   N  N     . ARG A 1 12  ? 17.87594  7.92347   -15.87028 1.000 6.20362  ? 12  ARG A N     1 
ATOM   77   C  CA    . ARG A 1 12  ? 16.85390  7.32968   -16.72262 1.000 8.15814  ? 12  ARG A CA    1 
ATOM   78   C  C     . ARG A 1 12  ? 17.08771  5.82699   -16.73097 1.000 6.33671  ? 12  ARG A C     1 
ATOM   79   O  O     . ARG A 1 12  ? 16.28934  5.05662   -16.18809 1.000 6.46346  ? 12  ARG A O     1 
ATOM   80   C  CB    . ARG A 1 12  ? 16.90290  7.90176   -18.14200 1.000 7.94149  ? 12  ARG A CB    1 
ATOM   81   C  CG    . ARG A 1 12  ? 16.82546  9.42084   -18.22167 1.000 8.23391  ? 12  ARG A CG    1 
ATOM   82   C  CD    . ARG A 1 12  ? 18.21060  10.04950  -18.22142 1.000 8.28452  ? 12  ARG A CD    1 
ATOM   83   N  NE    . ARG A 1 12  ? 19.03755  9.53769   -19.30770 1.000 8.30330  ? 12  ARG A NE    1 
ATOM   84   C  CZ    . ARG A 1 12  ? 19.07620  10.05603  -20.52759 1.000 10.41850 ? 12  ARG A CZ    1 
ATOM   85   N  NH1   . ARG A 1 12  ? 18.34613  11.11033  -20.85373 1.000 9.35565  ? 12  ARG A NH1   1 
ATOM   86   N  NH2   . ARG A 1 12  ? 19.86739  9.50285   -21.44286 1.000 9.25456  ? 12  ARG A NH2   1 
ATOM   87   N  N     . LYS A 1 13  ? 18.18530  5.41116   -17.34677 1.000 7.29921  ? 13  LYS A N     1 
ATOM   88   C  CA    . LYS A 1 13  ? 18.78332  4.11317   -17.10875 1.000 6.30163  ? 13  LYS A CA    1 
ATOM   89   C  C     . LYS A 1 13  ? 19.96133  4.31121   -16.15178 1.000 7.09160  ? 13  LYS A C     1 
ATOM   90   O  O     . LYS A 1 13  ? 20.04034  5.32923   -15.45181 1.000 7.47484  ? 13  LYS A O     1 
ATOM   91   C  CB    . LYS A 1 13  ? 19.19029  3.47213   -18.44074 1.000 9.47653  ? 13  LYS A CB    1 
ATOM   92   C  CG    . LYS A 1 13  ? 18.02928  3.20510   -19.38570 1.000 8.32871  ? 13  LYS A CG    1 
ATOM   93   C  CD    . LYS A 1 13  ? 18.51625  2.60606   -20.69470 1.000 9.64717  ? 13  LYS A CD    1 
ATOM   94   C  CE    . LYS A 1 13  ? 17.37323  2.43202   -21.68067 1.000 12.87169 ? 13  LYS A CE    1 
ATOM   95   N  NZ    . LYS A 1 13  ? 17.84821  1.90398   -22.98966 1.000 11.96306 ? 13  LYS A NZ    1 
ATOM   96   N  N     . GLY A 1 14  ? 20.88634  3.35822   -16.12277 1.000 6.80129  ? 14  GLY A N     1 
ATOM   97   C  CA    . GLY A 1 14  ? 22.03636  3.47225   -15.23780 1.000 6.06687  ? 14  GLY A CA    1 
ATOM   98   C  C     . GLY A 1 14  ? 21.66739  3.66429   -13.78279 1.000 6.89091  ? 14  GLY A C     1 
ATOM   99   O  O     . GLY A 1 14  ? 22.30040  4.46332   -13.08283 1.000 6.03931  ? 14  GLY A O     1 
ATOM   100  N  N     . LEU A 1 15  ? 20.64241  2.95330   -13.31275 1.000 6.15166  ? 15  LEU A N     1 
ATOM   101  C  CA    . LEU A 1 15  ? 20.17643  3.08934   -11.93875 1.000 6.20995  ? 15  LEU A CA    1 
ATOM   102  C  C     . LEU A 1 15  ? 21.15546  2.44138   -10.96975 1.000 6.30031  ? 15  LEU A C     1 
ATOM   103  O  O     . LEU A 1 15  ? 20.86148  1.39239   -10.38971 1.000 6.45866  ? 15  LEU A O     1 
ATOM   104  C  CB    . LEU A 1 15  ? 18.78444  2.47233   -11.78970 1.000 6.81620  ? 15  LEU A CB    1 
ATOM   105  C  CG    . LEU A 1 15  ? 17.71942  3.03729   -12.73069 1.000 6.34144  ? 15  LEU A CG    1 
ATOM   106  C  CD1   . LEU A 1 15  ? 16.41643  2.26629   -12.60064 1.000 6.54927  ? 15  LEU A CD1   1 
ATOM   107  C  CD2   . LEU A 1 15  ? 17.49941  4.51730   -12.46273 1.000 6.41665  ? 15  LEU A CD2   1 
ATOM   108  N  N     . ARG A 1 16  ? 22.31898  3.05987   -10.78673 1.000 6.26065  ? 16  ARG A N     1 
ATOM   109  C  CA    . ARG A 1 16  ? 23.36049  2.48697   -9.94795  1.000 6.93127  ? 16  ARG A CA    1 
ATOM   110  C  C     . ARG A 1 16  ? 24.32388  3.58793   -9.53575  1.000 6.79299  ? 16  ARG A C     1 
ATOM   111  O  O     . ARG A 1 16  ? 24.34348  4.67430   -10.12025 1.000 6.29038  ? 16  ARG A O     1 
ATOM   112  C  CB    . ARG A 1 16  ? 24.11207  1.36800   -10.67654 1.000 7.43059  ? 16  ARG A CB    1 
ATOM   113  C  CG    . ARG A 1 16  ? 24.87107  1.85130   -11.90111 1.000 8.37117  ? 16  ARG A CG    1 
ATOM   114  C  CD    . ARG A 1 16  ? 25.52175  0.70693   -12.65862 1.000 6.65894  ? 16  ARG A CD    1 
ATOM   115  N  NE    . ARG A 1 16  ? 26.32686  1.19530   -13.77172 1.000 6.42391  ? 16  ARG A NE    1 
ATOM   116  C  CZ    . ARG A 1 16  ? 25.85913  1.42282   -14.99124 1.000 6.33216  ? 16  ARG A CZ    1 
ATOM   117  N  NH1   . ARG A 1 16  ? 24.59010  1.20869   -15.29553 1.000 7.47054  ? 16  ARG A NH1   1 
ATOM   118  N  NH2   . ARG A 1 16  ? 26.68503  1.87833   -15.92870 1.000 6.95044  ? 16  ARG A NH2   1 
ATOM   119  N  N     . LEU A 1 17  ? 25.12550  3.28748   -8.51586  1.000 7.12605  ? 17  LEU A N     1 
ATOM   120  C  CA    . LEU A 1 17  ? 26.19851  4.17450   -8.08391  1.000 8.62583  ? 17  LEU A CA    1 
ATOM   121  C  C     . LEU A 1 17  ? 27.57050  3.71850   -8.55392  1.000 7.99088  ? 17  LEU A C     1 
ATOM   122  O  O     . LEU A 1 17  ? 28.44449  4.56050   -8.78597  1.000 8.07287  ? 17  LEU A O     1 
ATOM   123  C  CB    . LEU A 1 17  ? 26.20954  4.30055   -6.55491  1.000 8.82731  ? 17  LEU A CB    1 
ATOM   124  C  CG    . LEU A 1 17  ? 25.38754  5.43656   -5.93993  1.000 9.07231  ? 17  LEU A CG    1 
ATOM   125  C  CD1   . LEU A 1 17  ? 23.90754  5.28854   -6.25589  1.000 8.65631  ? 17  LEU A CD1   1 
ATOM   126  C  CD2   . LEU A 1 17  ? 25.61257  5.50261   -4.43693  1.000 12.55750 ? 17  LEU A CD2   1 
ATOM   127  N  N     . HIS A 1 18  ? 27.77751  2.41250   -8.70289  1.000 6.93812  ? 18  HIS A N     1 
ATOM   128  C  CA    . HIS A 1 18  ? 29.04150  1.89449   -9.20390  1.000 8.96346  ? 18  HIS A CA    1 
ATOM   129  C  C     . HIS A 1 18  ? 29.12347  2.07245   -10.71290 1.000 8.20442  ? 18  HIS A C     1 
ATOM   130  O  O     . HIS A 1 18  ? 28.12045  1.94542   -11.42088 1.000 8.22782  ? 18  HIS A O     1 
ATOM   131  C  CB    . HIS A 1 18  ? 29.19452  0.41550   -8.84486  1.000 8.81547  ? 18  HIS A CB    1 
ATOM   132  C  CG    . HIS A 1 18  ? 28.25651  -0.48653  -9.58681  1.000 7.42424  ? 18  HIS A CG    1 
ATOM   133  N  ND1   . HIS A 1 18  ? 26.99352  -0.79152  -9.12477  1.000 8.49054  ? 18  HIS A ND1   1 
ATOM   134  C  CD2   . HIS A 1 18  ? 28.39749  -1.15056  -10.75879 1.000 7.60801  ? 18  HIS A CD2   1 
ATOM   135  C  CE1   . HIS A 1 18  ? 26.39851  -1.60355  -9.97974  1.000 7.11390  ? 18  HIS A CE1   1 
ATOM   136  N  NE2   . HIS A 1 18  ? 27.22849  -1.83758  -10.97975 1.000 7.11888  ? 18  HIS A NE2   1 
ATOM   137  N  N     . ASP A 1 19  ? 30.32846  2.36744   -11.19994 1.000 7.01207  ? 19  ASP A N     1 
ATOM   138  C  CA    . ASP A 1 19  ? 30.59642  2.55140   -12.62595 1.000 8.58542  ? 19  ASP A CA    1 
ATOM   139  C  C     . ASP A 1 19  ? 29.59740  3.52837   -13.24796 1.000 7.23154  ? 19  ASP A C     1 
ATOM   140  O  O     . ASP A 1 19  ? 28.88938  3.22234   -14.20793 1.000 6.51132  ? 19  ASP A O     1 
ATOM   141  C  CB    . ASP A 1 19  ? 30.58742  1.20638   -13.35791 1.000 8.93645  ? 19  ASP A CB    1 
ATOM   142  C  CG    . ASP A 1 19  ? 31.11339  1.31134   -14.77792 1.000 8.75758  ? 19  ASP A CG    1 
ATOM   143  O  OD1   . ASP A 1 19  ? 31.72737  2.34533   -15.11397 1.000 8.84700  ? 19  ASP A OD1   1 
ATOM   144  O  OD2   . ASP A 1 19  ? 30.90738  0.36131   -15.56089 1.000 9.24471  ? 19  ASP A OD2   1 
ATOM   145  N  N     . ASN A 1 20  ? 29.54241  4.72639   -12.66199 1.000 6.61928  ? 20  ASN A N     1 
ATOM   146  C  CA    . ASN A 1 20  ? 28.66239  5.79837   -13.11801 1.000 7.61095  ? 20  ASN A CA    1 
ATOM   147  C  C     . ASN A 1 20  ? 29.53237  7.01937   -13.39806 1.000 7.54386  ? 20  ASN A C     1 
ATOM   148  O  O     . ASN A 1 20  ? 29.67538  7.90439   -12.53909 1.000 6.63578  ? 20  ASN A O     1 
ATOM   149  C  CB    . ASN A 1 20  ? 27.57941  6.11039   -12.08599 1.000 7.51095  ? 20  ASN A CB    1 
ATOM   150  C  CG    . ASN A 1 20  ? 26.33539  6.72136   -12.70799 1.000 8.99986  ? 20  ASN A CG    1 
ATOM   151  O  OD1   . ASN A 1 20  ? 25.21240  6.34536   -12.36995 1.000 11.64006 ? 20  ASN A OD1   1 
ATOM   152  N  ND2   . ASN A 1 20  ? 26.52836  7.66034   -13.62702 1.000 7.41763  ? 20  ASN A ND2   1 
ATOM   153  N  N     . PRO A 1 21  ? 30.13635  7.09934   -14.58608 1.000 6.67141  ? 21  PRO A N     1 
ATOM   154  C  CA    . PRO A 1 21  ? 30.95533  8.28033   -14.90813 1.000 10.82566 ? 21  PRO A CA    1 
ATOM   155  C  C     . PRO A 1 21  ? 30.15932  9.57133   -14.94115 1.000 9.08530  ? 21  PRO A C     1 
ATOM   156  O  O     . PRO A 1 21  ? 30.73232  10.64534  -14.72520 1.000 8.69785  ? 21  PRO A O     1 
ATOM   157  C  CB    . PRO A 1 21  ? 31.54030  7.93630   -16.28613 1.000 11.01691 ? 21  PRO A CB    1 
ATOM   158  C  CG    . PRO A 1 21  ? 30.61330  6.90727   -16.85108 1.000 10.67604 ? 21  PRO A CG    1 
ATOM   159  C  CD    . PRO A 1 21  ? 30.13333  6.11130   -15.67705 1.000 7.73053  ? 21  PRO A CD    1 
ATOM   160  N  N     . ALA A 1 22  ? 28.85231  9.50031   -15.20612 1.000 10.08634 ? 22  ALA A N     1 
ATOM   161  C  CA    . ALA A 1 22  ? 28.02631  10.70230  -15.17114 1.000 8.52206  ? 22  ALA A CA    1 
ATOM   162  C  C     . ALA A 1 22  ? 27.85033  11.20434  -13.74415 1.000 9.53191  ? 22  ALA A C     1 
ATOM   163  O  O     . ALA A 1 22  ? 27.82133  12.41735  -13.50719 1.000 8.85966  ? 22  ALA A O     1 
ATOM   164  C  CB    . ALA A 1 22  ? 26.66829  10.42727  -15.81811 1.000 7.94235  ? 22  ALA A CB    1 
ATOM   165  N  N     . LEU A 1 23  ? 27.73136  10.28437  -12.78312 1.000 8.41322  ? 23  LEU A N     1 
ATOM   166  C  CA    . LEU A 1 23  ? 27.60439  10.68441  -11.38613 1.000 8.96799  ? 23  LEU A CA    1 
ATOM   167  C  C     . LEU A 1 23  ? 28.90939  11.26544  -10.85618 1.000 9.21558  ? 23  LEU A C     1 
ATOM   168  O  O     . LEU A 1 23  ? 28.89740  12.22246  -10.07521 1.000 8.60175  ? 23  LEU A O     1 
ATOM   169  C  CB    . LEU A 1 23  ? 27.16441  9.49044   -10.53909 1.000 7.75445  ? 23  LEU A CB    1 
ATOM   170  C  CG    . LEU A 1 23  ? 27.15644  9.68348   -9.02109  1.000 8.54892  ? 23  LEU A CG    1 
ATOM   171  C  CD1   . LEU A 1 23  ? 26.20444  10.80149  -8.62311  1.000 9.57232  ? 23  LEU A CD1   1 
ATOM   172  C  CD2   . LEU A 1 23  ? 26.79347  8.38450   -8.31605  1.000 8.93402  ? 23  LEU A CD2   1 
ATOM   173  N  N     . LEU A 1 24  ? 30.04539  10.69944  -11.27319 1.000 7.17764  ? 24  LEU A N     1 
ATOM   174  C  CA    . LEU A 1 24  ? 31.33539  11.18046  -10.78923 1.000 9.00531  ? 24  LEU A CA    1 
ATOM   175  C  C     . LEU A 1 24  ? 31.61637  12.59745  -11.27328 1.000 10.23513 ? 24  LEU A C     1 
ATOM   176  O  O     . LEU A 1 24  ? 32.07738  13.44248  -10.49631 1.000 11.89809 ? 24  LEU A O     1 
ATOM   177  C  CB    . LEU A 1 24  ? 32.44639  10.23246  -11.23422 1.000 7.39394  ? 24  LEU A CB    1 
ATOM   178  C  CG    . LEU A 1 24  ? 32.33341  8.78647   -10.75118 1.000 9.47722  ? 24  LEU A CG    1 
ATOM   179  C  CD1   . LEU A 1 24  ? 33.46741  7.94246   -11.31417 1.000 9.81243  ? 24  LEU A CD1   1 
ATOM   180  C  CD2   . LEU A 1 24  ? 32.32045  8.72652   -9.23217  1.000 9.39975  ? 24  LEU A CD2   1 
ATOM   181  N  N     . GLU A 1 25  ? 31.34634  12.87541  -12.55128 1.000 10.33230 ? 25  GLU A N     1 
ATOM   182  C  CA    . GLU A 1 25  ? 31.55432  14.22139  -13.07532 1.000 10.27192 ? 25  GLU A CA    1 
ATOM   183  C  C     . GLU A 1 25  ? 30.62933  15.22441  -12.39633 1.000 13.07765 ? 25  GLU A C     1 
ATOM   184  O  O     . GLU A 1 25  ? 31.01132  16.37942  -12.16938 1.000 9.85372  ? 25  GLU A O     1 
ATOM   185  C  CB    . GLU A 1 25  ? 31.34029  14.23035  -14.59032 1.000 14.07993 ? 25  GLU A CB    1 
ATOM   186  C  CG    . GLU A 1 25  ? 31.47327  15.60533  -15.23536 1.000 14.64998 ? 25  GLU A CG    1 
ATOM   187  C  CD    . GLU A 1 25  ? 32.88526  16.15034  -15.16441 1.000 12.58328 ? 25  GLU A CD    1 
ATOM   188  O  OE1   . GLU A 1 25  ? 33.83627  15.34235  -15.14741 1.000 13.73038 ? 25  GLU A OE1   1 
ATOM   189  O  OE2   . GLU A 1 25  ? 33.04425  17.38834  -15.12045 1.000 15.73493 ? 25  GLU A OE2   1 
ATOM   190  N  N     . ALA A 1 26  ? 29.40834  14.80041  -12.06130 1.000 12.42059 ? 26  ALA A N     1 
ATOM   191  C  CA    . ALA A 1 26  ? 28.46235  15.69042  -11.39930 1.000 10.04362 ? 26  ALA A CA    1 
ATOM   192  C  C     . ALA A 1 26  ? 28.88437  16.03947  -9.97832  1.000 11.30454 ? 26  ALA A C     1 
ATOM   193  O  O     . ALA A 1 26  ? 28.48138  17.09048  -9.46935  1.000 10.58503 ? 26  ALA A O     1 
ATOM   194  C  CB    . ALA A 1 26  ? 27.07035  15.06241  -11.38525 1.000 7.27024  ? 26  ALA A CB    1 
ATOM   195  N  N     . CYS A 1 27  ? 29.69639  15.19849  -9.33531  1.000 11.32116 ? 27  CYS A N     1 
ATOM   196  C  CA    . CYS A 1 27  ? 30.09542  15.42654  -7.95333  1.000 12.56793 ? 27  CYS A CA    1 
ATOM   197  C  C     . CYS A 1 27  ? 31.43242  16.14055  -7.81738  1.000 13.33512 ? 27  CYS A C     1 
ATOM   198  O  O     . CYS A 1 27  ? 31.70144  16.70859  -6.75340  1.000 12.34205 ? 27  CYS A O     1 
ATOM   199  C  CB    . CYS A 1 27  ? 30.16345  14.09756  -7.19529  1.000 10.73061 ? 27  CYS A CB    1 
ATOM   200  S  SG    . CYS A 1 27  ? 28.56446  13.30056  -6.92523  1.000 11.97059 ? 27  CYS A SG    1 
ATOM   201  N  N     . LYS A 1 28  ? 32.27140  16.12553  -8.85140  1.000 15.39171 ? 28  LYS A N     1 
ATOM   202  C  CA    . LYS A 1 28  ? 33.58839  16.74054  -8.74544  1.000 16.82848 ? 28  LYS A CA    1 
ATOM   203  C  C     . LYS A 1 28  ? 33.46738  18.25754  -8.66749  1.000 14.53103 ? 28  LYS A C     1 
ATOM   204  O  O     . LYS A 1 28  ? 32.82336  18.88351  -9.51649  1.000 14.29140 ? 28  LYS A O     1 
ATOM   205  C  CB    . LYS A 1 28  ? 34.46537  16.34851  -9.93245  1.000 15.63388 ? 28  LYS A CB    1 
ATOM   206  C  CG    . LYS A 1 28  ? 35.84137  16.99252  -9.89050  1.000 20.46657 ? 28  LYS A CG    1 
ATOM   207  C  CD    . LYS A 1 28  ? 36.62334  16.76649  -11.17151 0.000 19.79642 ? 28  LYS A CD    1 
ATOM   208  C  CE    . LYS A 1 28  ? 37.96234  17.48750  -11.11756 0.000 21.09330 ? 28  LYS A CE    1 
ATOM   209  N  NZ    . LYS A 1 28  ? 38.74531  17.31247  -12.36957 0.000 21.30633 ? 28  LYS A NZ    1 
ATOM   210  N  N     . ASP A 1 29  ? 34.09540  18.84458  -7.64652  1.000 17.11317 ? 29  ASP A N     1 
ATOM   211  C  CA    . ASP A 1 29  ? 34.06839  20.29058  -7.41056  1.000 18.57081 ? 29  ASP A CA    1 
ATOM   212  C  C     . ASP A 1 29  ? 32.64239  20.82558  -7.34455  1.000 20.45358 ? 29  ASP A C     1 
ATOM   213  O  O     . ASP A 1 29  ? 32.38137  21.97756  -7.69958  1.000 21.97050 ? 29  ASP A O     1 
ATOM   214  C  CB    . ASP A 1 29  ? 34.87637  21.04256  -8.47160  1.000 23.26910 ? 29  ASP A CB    1 
ATOM   215  C  CG    . ASP A 1 29  ? 36.36837  20.82158  -8.32963  1.000 24.94951 ? 29  ASP A CG    1 
ATOM   216  O  OD1   . ASP A 1 29  ? 36.86539  20.83961  -7.18264  1.000 29.22270 ? 29  ASP A OD1   1 
ATOM   217  O  OD2   . ASP A 1 29  ? 37.04635  20.62755  -9.36163  1.000 28.37278 ? 29  ASP A OD2   1 
ATOM   218  N  N     . ALA A 1 30  ? 31.71341  19.99658  -6.88150  1.000 15.14295 ? 30  ALA A N     1 
ATOM   219  C  CA    . ALA A 1 30  ? 30.30141  20.34257  -6.86748  1.000 14.48672 ? 30  ALA A CA    1 
ATOM   220  C  C     . ALA A 1 30  ? 29.91243  20.91261  -5.51249  1.000 14.29128 ? 30  ALA A C     1 
ATOM   221  O  O     . ALA A 1 30  ? 30.26646  20.35464  -4.46948  1.000 15.41599 ? 30  ALA A O     1 
ATOM   222  C  CB    . ALA A 1 30  ? 29.44241  19.11956  -7.18843  1.000 13.15746 ? 30  ALA A CB    1 
ATOM   223  N  N     . LYS A 1 31  ? 29.18842  22.03160  -5.53551  1.000 17.04382 ? 31  LYS A N     1 
ATOM   224  C  CA    . LYS A 1 31  ? 28.63944  22.59564  -4.30852  1.000 14.96787 ? 31  LYS A CA    1 
ATOM   225  C  C     . LYS A 1 31  ? 27.37846  21.84964  -3.89147  1.000 14.43086 ? 31  LYS A C     1 
ATOM   226  O  O     . LYS A 1 31  ? 27.23848  21.44567  -2.73145  1.000 13.20160 ? 31  LYS A O     1 
ATOM   227  C  CB    . LYS A 1 31  ? 28.35043  24.08463  -4.50655  1.000 16.21228 ? 31  LYS A CB    1 
ATOM   228  C  CG    . LYS A 1 31  ? 28.68244  24.96067  -3.31059  1.000 20.99856 ? 31  LYS A CG    1 
ATOM   229  C  CD    . LYS A 1 31  ? 27.73347  24.71869  -2.15356  1.000 21.11122 ? 31  LYS A CD    1 
ATOM   230  C  CE    . LYS A 1 31  ? 28.01349  25.67973  -1.01660  1.000 24.50033 ? 31  LYS A CE    1 
ATOM   231  N  NZ    . LYS A 1 31  ? 29.41550  25.56476  -0.52762  1.000 30.22221 ? 31  LYS A NZ    1 
ATOM   232  N  N     . HIS A 1 32  ? 26.45444  21.65360  -4.82944  1.000 13.84914 ? 32  HIS A N     1 
ATOM   233  C  CA    . HIS A 1 32  ? 25.22045  20.92260  -4.58739  1.000 12.21044 ? 32  HIS A CA    1 
ATOM   234  C  C     . HIS A 1 32  ? 24.96443  19.98756  -5.75936  1.000 10.58305 ? 32  HIS A C     1 
ATOM   235  O  O     . HIS A 1 32  ? 25.15740  20.36553  -6.91737  1.000 10.56625 ? 32  HIS A O     1 
ATOM   236  C  CB    . HIS A 1 32  ? 24.03045  21.87460  -4.40540  1.000 13.90865 ? 32  HIS A CB    1 
ATOM   237  C  CG    . HIS A 1 32  ? 24.17046  22.80563  -3.24043  1.000 13.54254 ? 32  HIS A CG    1 
ATOM   238  N  ND1   . HIS A 1 32  ? 23.92145  24.15863  -3.33446  1.000 17.06777 ? 32  HIS A ND1   1 
ATOM   239  C  CD2   . HIS A 1 32  ? 24.52449  22.57767  -1.95343  1.000 14.58250 ? 32  HIS A CD2   1 
ATOM   240  C  CE1   . HIS A 1 32  ? 24.12147  24.72367  -2.15748  1.000 16.48181 ? 32  HIS A CE1   1 
ATOM   241  N  NE2   . HIS A 1 32  ? 24.48950  23.78569  -1.30146  1.000 17.93896 ? 32  HIS A NE2   1 
ATOM   242  N  N     . VAL A 1 33  ? 24.53445  18.76557  -5.45231  1.000 9.84252  ? 33  VAL A N     1 
ATOM   243  C  CA    . VAL A 1 33  ? 24.20443  17.76254  -6.45628  1.000 9.77236  ? 33  VAL A CA    1 
ATOM   244  C  C     . VAL A 1 33  ? 22.73644  17.39453  -6.30023  1.000 7.72477  ? 33  VAL A C     1 
ATOM   245  O  O     . VAL A 1 33  ? 22.25147  17.19856  -5.18022  1.000 8.63294  ? 33  VAL A O     1 
ATOM   246  C  CB    . VAL A 1 33  ? 25.09945  16.51155  -6.33326  1.000 9.66977  ? 33  VAL A CB    1 
ATOM   247  C  CG1   . VAL A 1 33  ? 24.71743  15.47451  -7.38022  1.000 7.21890  ? 33  VAL A CG1   1 
ATOM   248  C  CG2   . VAL A 1 33  ? 26.56544  16.89155  -6.46730  1.000 8.87595  ? 33  VAL A CG2   1 
ATOM   249  N  N     . TYR A 1 34  ? 22.02642  17.30949  -7.42722  1.000 7.35286  ? 34  TYR A N     1 
ATOM   250  C  CA    . TYR A 1 34  ? 20.59942  16.99448  -7.45118  1.000 7.48522  ? 34  TYR A CA    1 
ATOM   251  C  C     . TYR A 1 34  ? 20.38741  15.68745  -8.20313  1.000 6.96431  ? 34  TYR A C     1 
ATOM   252  O  O     . TYR A 1 34  ? 20.25239  15.68541  -9.43713  1.000 6.85371  ? 34  TYR A O     1 
ATOM   253  C  CB    . TYR A 1 34  ? 19.79840  18.12645  -8.09319  1.000 7.40738  ? 34  TYR A CB    1 
ATOM   254  C  CG    . TYR A 1 34  ? 19.80540  19.42048  -7.30823  1.000 9.10085  ? 34  TYR A CG    1 
ATOM   255  C  CD1   . TYR A 1 34  ? 20.83139  20.34448  -7.46128  1.000 8.05375  ? 34  TYR A CD1   1 
ATOM   256  C  CD2   . TYR A 1 34  ? 18.77942  19.72349  -6.42122  1.000 9.92646  ? 34  TYR A CD2   1 
ATOM   257  C  CE1   . TYR A 1 34  ? 20.83940  21.53050  -6.75032  1.000 9.13240  ? 34  TYR A CE1   1 
ATOM   258  C  CE2   . TYR A 1 34  ? 18.77743  20.90752  -5.70626  1.000 9.94941  ? 34  TYR A CE2   1 
ATOM   259  C  CZ    . TYR A 1 34  ? 19.80941  21.80652  -5.87330  1.000 10.97073 ? 34  TYR A CZ    1 
ATOM   260  O  OH    . TYR A 1 34  ? 19.81242  22.98554  -5.16334  1.000 9.90793  ? 34  TYR A OH    1 
ATOM   261  N  N     . PRO A 1 35  ? 20.36744  14.54747  -7.50610  1.000 8.51616  ? 35  PRO A N     1 
ATOM   262  C  CA    . PRO A 1 35  ? 19.97343  13.29245  -8.16105  1.000 7.94838  ? 35  PRO A CA    1 
ATOM   263  C  C     . PRO A 1 35  ? 18.49743  13.31043  -8.52102  1.000 7.75195  ? 35  PRO A C     1 
ATOM   264  O  O     . PRO A 1 35  ? 17.63844  13.33145  -7.63400  1.000 6.99610  ? 35  PRO A O     1 
ATOM   265  C  CB    . PRO A 1 35  ? 20.28746  12.22349  -7.10302  1.000 8.43367  ? 35  PRO A CB    1 
ATOM   266  C  CG    . PRO A 1 35  ? 21.23048  12.88352  -6.14506  1.000 8.00037  ? 35  PRO A CG    1 
ATOM   267  C  CD    . PRO A 1 35  ? 20.83647  14.32652  -6.13010  1.000 8.99053  ? 35  PRO A CD    1 
ATOM   268  N  N     . VAL A 1 36  ? 18.18940  13.30439  -9.81601  1.000 7.46123  ? 36  VAL A N     1 
ATOM   269  C  CA    . VAL A 1 36  ? 16.83339  13.52536  -10.30199 1.000 7.01274  ? 36  VAL A CA    1 
ATOM   270  C  C     . VAL A 1 36  ? 16.42038  12.36533  -11.19695 1.000 6.71402  ? 36  VAL A C     1 
ATOM   271  O  O     . VAL A 1 36  ? 17.17536  11.96231  -12.08795 1.000 6.42741  ? 36  VAL A O     1 
ATOM   272  C  CB    . VAL A 1 36  ? 16.71836  14.85834  -11.06603 1.000 7.17871  ? 36  VAL A CB    1 
ATOM   273  C  CG1   . VAL A 1 36  ? 15.35634  14.97631  -11.73100 1.000 11.71679 ? 36  VAL A CG1   1 
ATOM   274  C  CG2   . VAL A 1 36  ? 16.96537  16.03237  -10.13007 1.000 9.24459  ? 36  VAL A CG2   1 
ATOM   275  N  N     . PHE A 1 37  ? 15.22539  11.83033  -10.95191 1.000 7.86312  ? 37  PHE A N     1 
ATOM   276  C  CA    . PHE A 1 37  ? 14.55337  10.91230  -11.86186 1.000 8.48647  ? 37  PHE A CA    1 
ATOM   277  C  C     . PHE A 1 37  ? 13.21336  11.52127  -12.24085 1.000 9.29981  ? 37  PHE A C     1 
ATOM   278  O  O     . PHE A 1 37  ? 12.42038  11.87929  -11.36285 1.000 9.90018  ? 37  PHE A O     1 
ATOM   279  C  CB    . PHE A 1 37  ? 14.35140  9.53131   -11.22682 1.000 7.49748  ? 37  PHE A CB    1 
ATOM   280  C  CG    . PHE A 1 37  ? 13.77439  8.50728   -12.16777 1.000 9.10811  ? 37  PHE A CG    1 
ATOM   281  C  CD1   . PHE A 1 37  ? 12.40238  8.36827   -12.31474 1.000 9.82905  ? 37  PHE A CD1   1 
ATOM   282  C  CD2   . PHE A 1 37  ? 14.60538  7.68226   -12.90677 1.000 8.77145  ? 37  PHE A CD2   1 
ATOM   283  C  CE1   . PHE A 1 37  ? 11.87337  7.43023   -13.18270 1.000 11.51129 ? 37  PHE A CE1   1 
ATOM   284  C  CE2   . PHE A 1 37  ? 14.08237  6.74223   -13.77573 1.000 9.36907  ? 37  PHE A CE2   1 
ATOM   285  C  CZ    . PHE A 1 37  ? 12.71436  6.61622   -13.91269 1.000 7.29879  ? 37  PHE A CZ    1 
ATOM   286  N  N     . VAL A 1 38  ? 12.96233  11.64323  -13.53985 1.000 10.62788 ? 38  VAL A N     1 
ATOM   287  C  CA    . VAL A 1 38  ? 11.73932  12.26421  -14.03684 1.000 12.55874 ? 38  VAL A CA    1 
ATOM   288  C  C     . VAL A 1 38  ? 10.67932  11.18419  -14.20879 1.000 11.39854 ? 38  VAL A C     1 
ATOM   289  O  O     . VAL A 1 38  ? 10.85931  10.23917  -14.98377 1.000 11.24470 ? 38  VAL A O     1 
ATOM   290  C  CB    . VAL A 1 38  ? 11.99028  13.01017  -15.35487 1.000 13.28113 ? 38  VAL A CB    1 
ATOM   291  C  CG1   . VAL A 1 38  ? 10.69227  13.60014  -15.88286 1.000 15.06377 ? 38  VAL A CG1   1 
ATOM   292  C  CG2   . VAL A 1 38  ? 13.02828  14.10218  -15.15093 1.000 10.47986 ? 38  VAL A CG2   1 
ATOM   293  N  N     . LEU A 1 39  ? 9.57334   11.32521  -13.48377 1.000 14.67436 ? 39  LEU A N     1 
ATOM   294  C  CA    . LEU A 1 39  ? 8.47334   10.37220  -13.51672 1.000 16.20890 ? 39  LEU A CA    1 
ATOM   295  C  C     . LEU A 1 39  ? 7.23833   11.05217  -14.08871 1.000 20.43483 ? 39  LEU A C     1 
ATOM   296  O  O     . LEU A 1 39  ? 6.88933   12.16218  -13.67574 1.000 20.20161 ? 39  LEU A O     1 
ATOM   297  C  CB    . LEU A 1 39  ? 8.17438   9.82924   -12.11670 1.000 16.68768 ? 39  LEU A CB    1 
ATOM   298  C  CG    . LEU A 1 39  ? 7.17739   8.67323   -12.02864 1.000 20.12265 ? 39  LEU A CG    1 
ATOM   299  C  CD1   . LEU A 1 39  ? 7.85939   7.35223   -12.35061 1.000 19.18512 ? 39  LEU A CD1   1 
ATOM   300  C  CD2   . LEU A 1 39  ? 6.51742   8.62727   -10.66062 1.000 17.12922 ? 39  LEU A CD2   1 
ATOM   301  N  N     . ASP A 1 40  ? 6.58131   10.38514  -15.03768 1.000 24.94821 ? 40  ASP A N     1 
ATOM   302  C  CA    . ASP A 1 40  ? 5.34829   10.90111  -15.61167 1.000 27.52085 ? 40  ASP A CA    1 
ATOM   303  C  C     . ASP A 1 40  ? 4.16831   10.23312  -14.92362 1.000 31.93583 ? 40  ASP A C     1 
ATOM   304  O  O     . ASP A 1 40  ? 3.91432   9.04411   -15.17258 1.000 33.97601 ? 40  ASP A O     1 
ATOM   305  C  CB    . ASP A 1 40  ? 5.30426   10.64806  -17.11766 1.000 31.11453 ? 40  ASP A CB    1 
ATOM   306  C  CG    . ASP A 1 40  ? 4.15224   11.36603  -17.79566 1.000 36.31039 ? 40  ASP A CG    1 
ATOM   307  O  OD1   . ASP A 1 40  ? 4.16623   12.61403  -17.83370 1.000 36.04206 ? 40  ASP A OD1   1 
ATOM   308  O  OD2   . ASP A 1 40  ? 3.23324   10.68201  -18.29362 1.000 39.16342 ? 40  ASP A OD2   1 
ATOM   309  N  N     . PRO A 1 41  ? 3.42433   10.93614  -14.06463 1.000 35.12615 ? 41  PRO A N     1 
ATOM   310  C  CA    . PRO A 1 41  ? 2.31535   10.29415  -13.34159 1.000 37.39420 ? 41  PRO A CA    1 
ATOM   311  C  C     . PRO A 1 41  ? 1.12333   9.94312   -14.21755 1.000 40.34720 ? 41  PRO A C     1 
ATOM   312  O  O     . PRO A 1 41  ? 0.12235   9.44013   -13.69451 1.000 44.33504 ? 41  PRO A O     1 
ATOM   313  C  CB    . PRO A 1 41  ? 1.93336   11.34618  -12.29061 1.000 39.55096 ? 41  PRO A CB    1 
ATOM   314  C  CG    . PRO A 1 41  ? 2.32734   12.64217  -12.91066 1.000 34.76051 ? 41  PRO A CG    1 
ATOM   315  C  CD    . PRO A 1 41  ? 3.56832   12.35915  -13.71167 1.000 32.03674 ? 41  PRO A CD    1 
ATOM   316  N  N     . HIS A 1 42  ? 1.19130   10.19208  -15.52456 1.000 40.95180 ? 42  HIS A N     1 
ATOM   317  C  CA    . HIS A 1 42  ? 0.13328   9.82604   -16.45653 1.000 44.19085 ? 42  HIS A CA    1 
ATOM   318  C  C     . HIS A 1 42  ? 0.60127   8.75902   -17.44150 1.000 41.80364 ? 42  HIS A C     1 
ATOM   319  O  O     . HIS A 1 42  ? 0.10525   8.68098   -18.56749 1.000 41.25095 ? 42  HIS A O     1 
ATOM   320  C  CB    . HIS A 1 42  ? -0.37374  11.06002  -17.20055 1.000 43.39435 ? 42  HIS A CB    1 
ATOM   321  C  CG    . HIS A 1 42  ? -0.65873  12.22704  -16.30758 1.000 45.00044 ? 42  HIS A CG    1 
ATOM   322  N  ND1   . HIS A 1 42  ? -1.84172  12.36405  -15.61456 1.000 47.66851 ? 42  HIS A ND1   1 
ATOM   323  C  CD2   . HIS A 1 42  ? 0.09027   13.30906  -15.98963 1.000 44.76272 ? 42  HIS A CD2   1 
ATOM   324  C  CE1   . HIS A 1 42  ? -1.80971  13.48107  -14.91060 1.000 51.85606 ? 42  HIS A CE1   1 
ATOM   325  N  NE2   . HIS A 1 42  ? -0.64772  14.07308  -15.12064 1.000 50.81109 ? 42  HIS A NE2   1 
ATOM   326  N  N     . PHE A 1 43  ? 1.56029   7.92904   -17.02250 1.000 42.42035 ? 43  PHE A N     1 
ATOM   327  C  CA    . PHE A 1 43  ? 2.13428   6.94101   -17.92848 1.000 40.96353 ? 43  PHE A CA    1 
ATOM   328  C  C     . PHE A 1 43  ? 1.18028   5.77600   -18.15542 1.000 42.26154 ? 43  PHE A C     1 
ATOM   329  O  O     . PHE A 1 43  ? 1.12426   5.21997   -19.25841 1.000 42.76250 ? 43  PHE A O     1 
ATOM   330  C  CB    . PHE A 1 43  ? 3.47129   6.44304   -17.38049 1.000 41.00617 ? 43  PHE A CB    1 
ATOM   331  C  CG    . PHE A 1 43  ? 4.37127   5.85102   -18.42449 1.000 41.61046 ? 43  PHE A CG    1 
ATOM   332  C  CD1   . PHE A 1 43  ? 5.20325   6.66300   -19.17654 1.000 39.72752 ? 43  PHE A CD1   1 
ATOM   333  C  CD2   . PHE A 1 43  ? 4.38728   4.48601   -18.65545 1.000 38.86249 ? 43  PHE A CD2   1 
ATOM   334  C  CE1   . PHE A 1 43  ? 6.03524   6.12498   -20.13954 1.000 43.03787 ? 43  PHE A CE1   1 
ATOM   335  C  CE2   . PHE A 1 43  ? 5.21626   3.94299   -19.61745 1.000 39.30732 ? 43  PHE A CE2   1 
ATOM   336  C  CZ    . PHE A 1 43  ? 6.04124   4.76297   -20.36050 1.000 42.46721 ? 43  PHE A CZ    1 
ATOM   337  N  N     . LEU A 1 44  ? 0.42931   5.38503   -17.12740 1.000 41.95028 ? 44  LEU A N     1 
ATOM   338  C  CA    . LEU A 1 44  ? -0.56669  4.33301   -17.28034 1.000 41.42185 ? 44  LEU A CA    1 
ATOM   339  C  C     . LEU A 1 44  ? -1.83871  4.82798   -17.95133 1.000 45.05558 ? 44  LEU A C     1 
ATOM   340  O  O     . LEU A 1 44  ? -2.69571  4.00996   -18.30529 1.000 46.60493 ? 44  LEU A O     1 
ATOM   341  C  CB    . LEU A 1 44  ? -0.90966  3.72905   -15.91632 1.000 39.28933 ? 44  LEU A CB    1 
ATOM   342  C  CG    . LEU A 1 44  ? 0.26437   3.42909   -14.98033 0.000 33.30641 ? 44  LEU A CG    1 
ATOM   343  C  CD1   . LEU A 1 44  ? -0.23060  2.77612   -13.69930 0.000 27.33682 ? 44  LEU A CD1   1 
ATOM   344  C  CD2   . LEU A 1 44  ? 1.30536   2.55808   -15.66833 0.000 30.96543 ? 44  LEU A CD2   1 
ATOM   345  N  N     . GLN A 1 45  ? -1.97672  6.13598   -18.13937 1.000 46.47837 ? 45  GLN A N     1 
ATOM   346  C  CA    . GLN A 1 45  ? -3.17274  6.74695   -18.71936 1.000 44.81951 ? 45  GLN A CA    1 
ATOM   347  C  C     . GLN A 1 45  ? -2.93777  7.14091   -20.17438 1.000 45.52710 ? 45  GLN A C     1 
ATOM   348  O  O     . GLN A 1 45  ? -3.14979  8.28589   -20.57141 1.000 46.14136 ? 45  GLN A O     1 
ATOM   349  C  CB    . GLN A 1 45  ? -3.59173  7.95097   -17.88339 1.000 47.03660 ? 45  GLN A CB    1 
ATOM   350  C  CG    . GLN A 1 45  ? -5.01674  8.43695   -18.11237 0.000 47.94453 ? 45  GLN A CG    1 
ATOM   351  C  CD    . GLN A 1 45  ? -5.28874  9.76397   -17.42841 0.000 48.64596 ? 45  GLN A CD    1 
ATOM   352  O  OE1   . GLN A 1 45  ? -4.40073  10.35100  -16.80945 0.000 48.48405 ? 45  GLN A OE1   1 
ATOM   353  N  NE2   . GLN A 1 45  ? -6.52174  10.24596  -17.54240 0.000 48.95686 ? 45  GLN A NE2   1 
ATOM   354  N  N     . GLN A 1 46  ? -2.48578  6.19389   -20.99136 1.000 41.18344 ? 46  GLN A N     1 
ATOM   355  C  CA    . GLN A 1 46  ? -2.24681  6.46684   -22.40537 1.000 44.17388 ? 46  GLN A CA    1 
ATOM   356  C  C     . GLN A 1 46  ? -2.99383  5.48081   -23.30533 1.000 43.46926 ? 46  GLN A C     1 
ATOM   357  O  O     . GLN A 1 46  ? -2.56682  4.34481   -23.50930 1.000 44.98678 ? 46  GLN A O     1 
ATOM   358  C  CB    . GLN A 1 46  ? -0.74282  6.44685   -22.71240 1.000 41.91468 ? 46  GLN A CB    1 
ATOM   359  C  CG    . GLN A 1 46  ? 0.01520   5.24287   -22.16638 1.000 43.53783 ? 46  GLN A CG    1 
ATOM   360  C  CD    . GLN A 1 46  ? 1.52120   5.39288   -22.29542 0.000 40.97553 ? 46  GLN A CD    1 
ATOM   361  O  OE1   . GLN A 1 46  ? 2.27621   4.46089   -22.01841 0.000 39.73871 ? 46  GLN A OE1   1 
ATOM   362  N  NE2   . GLN A 1 46  ? 1.96518   6.57387   -22.71047 0.000 41.47514 ? 46  GLN A NE2   1 
ATOM   363  N  N     . LYS A 1 50  ? 0.38126   -1.94912  -21.94117 1.000 23.44833 ? 50  LYS A N     1 
ATOM   364  C  CA    . LYS A 1 50  ? 1.54425   -1.05512  -22.09923 1.000 22.70577 ? 50  LYS A CA    1 
ATOM   365  C  C     . LYS A 1 50  ? 2.62228   -1.43808  -21.08524 1.000 21.02368 ? 50  LYS A C     1 
ATOM   366  O  O     . LYS A 1 50  ? 3.70327   -1.82808  -21.51425 1.000 20.96051 ? 50  LYS A O     1 
ATOM   367  C  CB    . LYS A 1 50  ? 1.15924   0.41189   -21.89726 1.000 26.05244 ? 50  LYS A CB    1 
ATOM   368  C  CG    . LYS A 1 50  ? -0.32176  0.76087   -21.96924 0.000 29.34748 ? 50  LYS A CG    1 
ATOM   369  C  CD    . LYS A 1 50  ? -0.80279  1.11283   -23.36724 0.000 31.83919 ? 50  LYS A CD    1 
ATOM   370  C  CE    . LYS A 1 50  ? 0.00118   2.21881   -24.01629 0.000 33.82502 ? 50  LYS A CE    1 
ATOM   371  N  NZ    . LYS A 1 50  ? 0.93717   1.70479   -25.04230 0.000 32.90893 ? 50  LYS A NZ    1 
ATOM   372  N  N     . VAL A 1 51  ? 2.31430   -1.32604  -19.79523 1.000 21.91052 ? 51  VAL A N     1 
ATOM   373  C  CA    . VAL A 1 51  ? 3.29733   -1.65200  -18.77024 1.000 21.28182 ? 51  VAL A CA    1 
ATOM   374  C  C     . VAL A 1 51  ? 2.61936   -2.51198  -17.71420 1.000 19.36620 ? 51  VAL A C     1 
ATOM   375  O  O     . VAL A 1 51  ? 1.54936   -2.15297  -17.21019 1.000 22.14406 ? 51  VAL A O     1 
ATOM   376  C  CB    . VAL A 1 51  ? 3.89733   -0.38798  -18.12130 1.000 22.25525 ? 51  VAL A CB    1 
ATOM   377  C  CG1   . VAL A 1 51  ? 5.34934   -0.62695  -17.72832 1.000 21.28780 ? 51  VAL A CG1   1 
ATOM   378  C  CG2   . VAL A 1 51  ? 3.76730   0.81199   -19.04733 1.000 23.28272 ? 51  VAL A CG2   1 
ATOM   379  N  N     . SER A 1 52  ? 3.23437   -3.64296  -17.38518 1.000 16.46954 ? 52  SER A N     1 
ATOM   380  C  CA    A SER A 1 52  ? 2.71340   -4.49893  -16.33315 0.418 13.47943 ? 52  SER A CA    1 
ATOM   381  C  CA    B SER A 1 52  ? 2.70840   -4.49493  -16.33315 0.582 13.47756 ? 52  SER A CA    1 
ATOM   382  C  C     . SER A 1 52  ? 3.19643   -4.01789  -14.96917 1.000 11.54444 ? 52  SER A C     1 
ATOM   383  O  O     . SER A 1 52  ? 4.19842   -3.30888  -14.84721 1.000 11.06451 ? 52  SER A O     1 
ATOM   384  C  CB    A SER A 1 52  ? 3.13441   -5.95094  -16.55611 0.418 11.70486 ? 52  SER A CB    1 
ATOM   385  C  CB    B SER A 1 52  ? 3.11841   -5.95094  -16.55511 0.582 11.71143 ? 52  SER A CB    1 
ATOM   386  O  OG    A SER A 1 52  ? 2.71644   -6.77391  -15.48008 0.418 12.01503 ? 52  SER A OG    1 
ATOM   387  O  OG    B SER A 1 52  ? 4.52541   -6.10092  -16.48514 0.582 11.17898 ? 52  SER A OG    1 
ATOM   388  N  N     . VAL A 1 53  ? 2.46445   -4.42486  -13.92814 1.000 11.98398 ? 53  VAL A N     1 
ATOM   389  C  CA    . VAL A 1 53  ? 2.83848   -4.04382  -12.57316 1.000 12.30045 ? 53  VAL A CA    1 
ATOM   390  C  C     . VAL A 1 53  ? 4.14249   -4.70979  -12.14917 1.000 10.78160 ? 53  VAL A C     1 
ATOM   391  O  O     . VAL A 1 53  ? 4.77451   -4.26776  -11.18420 1.000 10.71906 ? 53  VAL A O     1 
ATOM   392  C  CB    . VAL A 1 53  ? 1.69350   -4.37680  -11.59713 1.000 13.96042 ? 53  VAL A CB    1 
ATOM   393  C  CG1   . VAL A 1 53  ? 1.59352   -5.87979  -11.37808 1.000 15.67435 ? 53  VAL A CG1   1 
ATOM   394  C  CG2   . VAL A 1 53  ? 1.86752   -3.63476  -10.27815 1.000 14.47102 ? 53  VAL A CG2   1 
ATOM   395  N  N     . ASN A 1 54  ? 4.57448   -5.75481  -12.85915 1.000 10.89126 ? 54  ASN A N     1 
ATOM   396  C  CA    . ASN A 1 54  ? 5.81950   -6.42879  -12.50215 1.000 10.62351 ? 54  ASN A CA    1 
ATOM   397  C  C     . ASN A 1 54  ? 7.03648   -5.58779  -12.86920 1.000 9.99516  ? 54  ASN A C     1 
ATOM   398  O  O     . ASN A 1 54  ? 7.97550   -5.46876  -12.07323 1.000 9.67821  ? 54  ASN A O     1 
ATOM   399  C  CB    . ASN A 1 54  ? 5.89049   -7.79781  -13.18011 1.000 10.99545 ? 54  ASN A CB    1 
ATOM   400  C  CG    . ASN A 1 54  ? 5.02652   -8.83280  -12.48906 1.000 11.62139 ? 54  ASN A CG    1 
ATOM   401  O  OD1   . ASN A 1 54  ? 4.22153   -8.50478  -11.61806 1.000 12.11471 ? 54  ASN A OD1   1 
ATOM   402  N  ND2   . ASN A 1 54  ? 5.18752   -10.09281 -12.87603 1.000 11.98205 ? 54  ASN A ND2   1 
ATOM   403  N  N     . ARG A 1 55  ? 7.04443   -4.99907  -14.06715 1.000 9.86519  ? 55  ARG A N     1 
ATOM   404  C  CA    . ARG A 1 55  ? 8.19719   -4.20594  -14.48054 1.000 9.33065  ? 55  ARG A CA    1 
ATOM   405  C  C     . ARG A 1 55  ? 8.18303   -2.81843  -13.85039 1.000 9.02015  ? 55  ARG A C     1 
ATOM   406  O  O     . ARG A 1 55  ? 9.23922   -2.29462  -13.47914 1.000 9.30220  ? 55  ARG A O     1 
ATOM   407  C  CB    . ARG A 1 55  ? 8.25362   -4.09357  -16.00614 1.000 9.67912  ? 55  ARG A CB    1 
ATOM   408  C  CG    . ARG A 1 55  ? 9.46117   -3.30468  -16.50503 1.000 9.07647  ? 55  ARG A CG    1 
ATOM   409  C  CD    . ARG A 1 55  ? 9.66880   -3.42850  -18.00756 1.000 11.61294 ? 55  ARG A CD    1 
ATOM   410  N  NE    . ARG A 1 55  ? 8.68911   -2.67495  -18.78091 1.000 11.61100 ? 55  ARG A NE    1 
ATOM   411  C  CZ    . ARG A 1 55  ? 7.65014   -3.21373  -19.40406 1.000 13.23564 ? 55  ARG A CZ    1 
ATOM   412  N  NH1   . ARG A 1 55  ? 7.41547   -4.51524  -19.35861 1.000 11.04413 ? 55  ARG A NH1   1 
ATOM   413  N  NH2   . ARG A 1 55  ? 6.82976   -2.42782  -20.09583 1.000 15.77961 ? 55  ARG A NH2   1 
ATOM   414  N  N     . TYR A 1 56  ? 7.00344   -2.20682  -13.72131 1.000 9.26182  ? 56  TYR A N     1 
ATOM   415  C  CA    . TYR A 1 56  ? 6.93844   -0.86580  -13.15135 1.000 9.02906  ? 56  TYR A CA    1 
ATOM   416  C  C     . TYR A 1 56  ? 7.30947   -0.87676  -11.67335 1.000 8.91038  ? 56  TYR A C     1 
ATOM   417  O  O     . TYR A 1 56  ? 7.95447   0.05826   -11.18440 1.000 10.13133 ? 56  TYR A O     1 
ATOM   418  C  CB    . TYR A 1 56  ? 5.54743   -0.26682  -13.35133 1.000 9.85497  ? 56  TYR A CB    1 
ATOM   419  C  CG    . TYR A 1 56  ? 5.54842   1.24518   -13.36738 1.000 13.98359 ? 56  TYR A CG    1 
ATOM   420  C  CD1   . TYR A 1 56  ? 5.45644   1.97321   -12.18840 1.000 14.69928 ? 56  TYR A CD1   1 
ATOM   421  C  CD2   . TYR A 1 56  ? 5.65139   1.94414   -14.56340 1.000 14.41910 ? 56  TYR A CD2   1 
ATOM   422  C  CE1   . TYR A 1 56  ? 5.46243   3.35621   -12.20144 1.000 14.53722 ? 56  TYR A CE1   1 
ATOM   423  C  CE2   . TYR A 1 56  ? 5.65738   3.32614   -14.58645 1.000 16.77594 ? 56  TYR A CE2   1 
ATOM   424  C  CZ    . TYR A 1 56  ? 5.56240   4.02618   -13.40346 1.000 18.85396 ? 56  TYR A CZ    1 
ATOM   425  O  OH    . TYR A 1 56  ? 5.56738   5.40118   -13.42351 1.000 16.20564 ? 56  TYR A OH    1 
ATOM   426  N  N     . ASN A 1 57  ? 6.91349   -1.92474  -10.94531 1.000 9.23559  ? 57  ASN A N     1 
ATOM   427  C  CA    . ASN A 1 57  ? 7.33752   -2.04669  -9.55532  1.000 9.18789  ? 57  ASN A CA    1 
ATOM   428  C  C     . ASN A 1 57  ? 8.81553   -2.39868  -9.45734  1.000 8.84648  ? 57  ASN A C     1 
ATOM   429  O  O     . ASN A 1 57  ? 9.47555   -2.02564  -8.48136  1.000 8.67603  ? 57  ASN A O     1 
ATOM   430  C  CB    . ASN A 1 57  ? 6.48755   -3.08968  -8.83027  1.000 9.94569  ? 57  ASN A CB    1 
ATOM   431  C  CG    . ASN A 1 57  ? 6.80158   -3.16963  -7.34927  1.000 11.40154 ? 57  ASN A CG    1 
ATOM   432  O  OD1   . ASN A 1 57  ? 6.38859   -2.31261  -6.56729  1.000 9.77900  ? 57  ASN A OD1   1 
ATOM   433  N  ND2   . ASN A 1 57  ? 7.53060   -4.20661  -6.95326  1.000 12.92235 ? 57  ASN A ND2   1 
ATOM   434  N  N     . PHE A 1 58  ? 9.34951   -3.11070  -10.45133 1.000 8.79588  ? 58  PHE A N     1 
ATOM   435  C  CA    . PHE A 1 58  ? 10.78751  -3.35069  -10.50035 1.000 8.48996  ? 58  PHE A CA    1 
ATOM   436  C  C     . PHE A 1 58  ? 11.55150  -2.03869  -10.62941 1.000 8.04852  ? 58  PHE A C     1 
ATOM   437  O  O     . PHE A 1 58  ? 12.60451  -1.85866  -10.00544 1.000 7.83846  ? 58  PHE A O     1 
ATOM   438  C  CB    . PHE A 1 58  ? 11.12250  -4.28972  -11.66133 1.000 8.56983  ? 58  PHE A CB    1 
ATOM   439  C  CG    . PHE A 1 58  ? 12.51550  -4.85571  -11.61034 1.000 10.43764 ? 58  PHE A CG    1 
ATOM   440  C  CD1   . PHE A 1 58  ? 13.58749  -4.15072  -12.13339 1.000 8.22515  ? 58  PHE A CD1   1 
ATOM   441  C  CD2   . PHE A 1 58  ? 12.74952  -6.10169  -11.05031 1.000 8.75118  ? 58  PHE A CD2   1 
ATOM   442  C  CE1   . PHE A 1 58  ? 14.86649  -4.67271  -12.08940 1.000 8.03731  ? 58  PHE A CE1   1 
ATOM   443  C  CE2   . PHE A 1 58  ? 14.02553  -6.62868  -11.00432 1.000 8.74117  ? 58  PHE A CE2   1 
ATOM   444  C  CZ    . PHE A 1 58  ? 15.08451  -5.91369  -11.52437 1.000 8.88983  ? 58  PHE A CZ    1 
ATOM   445  N  N     . LEU A 1 59  ? 11.03048  -1.10872  -11.43342 1.000 8.28504  ? 59  LEU A N     1 
ATOM   446  C  CA    . LEU A 1 59  ? 11.63946  0.21328   -11.54148 1.000 9.49958  ? 59  LEU A CA    1 
ATOM   447  C  C     . LEU A 1 59  ? 11.52049  0.98232   -10.23150 1.000 8.49702  ? 59  LEU A C     1 
ATOM   448  O  O     . LEU A 1 59  ? 12.46949  1.65634   -9.81154  1.000 9.49344  ? 59  LEU A O     1 
ATOM   449  C  CB    . LEU A 1 59  ? 10.99243  0.99624   -12.68349 1.000 8.48537  ? 59  LEU A CB    1 
ATOM   450  C  CG    . LEU A 1 59  ? 11.33442  2.48324   -12.80054 1.000 10.70865 ? 59  LEU A CG    1 
ATOM   451  C  CD1   . LEU A 1 59  ? 12.80141  2.68024   -13.15158 1.000 10.06425 ? 59  LEU A CD1   1 
ATOM   452  C  CD2   . LEU A 1 59  ? 10.43739  3.16120   -13.82354 1.000 10.33324 ? 59  LEU A CD2   1 
ATOM   453  N  N     . LEU A 1 60  ? 10.36350  0.89333   -9.57047  1.000 9.28390  ? 60  LEU A N     1 
ATOM   454  C  CA    . LEU A 1 60  ? 10.17452  1.59137   -8.30249  1.000 11.24561 ? 60  LEU A CA    1 
ATOM   455  C  C     . LEU A 1 60  ? 11.09955  1.04341   -7.22449  1.000 8.72920  ? 60  LEU A C     1 
ATOM   456  O  O     . LEU A 1 60  ? 11.66556  1.80944   -6.43553  1.000 7.80723  ? 60  LEU A O     1 
ATOM   457  C  CB    . LEU A 1 60  ? 8.71453   1.49237   -7.86145  1.000 8.35234  ? 60  LEU A CB    1 
ATOM   458  C  CG    . LEU A 1 60  ? 7.69451   2.22734   -8.73446  1.000 9.10311  ? 60  LEU A CG    1 
ATOM   459  C  CD1   . LEU A 1 60  ? 6.27652   1.95434   -8.25942  1.000 10.31056 ? 60  LEU A CD1   1 
ATOM   460  C  CD2   . LEU A 1 60  ? 7.98050   3.72134   -8.74851  1.000 10.75925 ? 60  LEU A CD2   1 
ATOM   461  N  N     . GLU A 1 61  ? 11.26756  -0.28059  -7.17345  1.000 9.32858  ? 61  GLU A N     1 
ATOM   462  C  CA    . GLU A 1 61  ? 12.18159  -0.86855  -6.19946  1.000 8.73510  ? 61  GLU A CA    1 
ATOM   463  C  C     . GLU A 1 61  ? 13.62958  -0.51455  -6.50750  1.000 7.78886  ? 61  GLU A C     1 
ATOM   464  O  O     . GLU A 1 61  ? 14.46660  -0.49151  -5.59852  1.000 7.80051  ? 61  GLU A O     1 
ATOM   465  C  CB    . GLU A 1 61  ? 12.00060  -2.38555  -6.15541  1.000 9.14483  ? 61  GLU A CB    1 
ATOM   466  C  CG    . GLU A 1 61  ? 10.65761  -2.82555  -5.60336  1.000 9.47342  ? 61  GLU A CG    1 
ATOM   467  C  CD    . GLU A 1 61  ? 10.47463  -4.32755  -5.64632  1.000 9.48669  ? 61  GLU A CD    1 
ATOM   468  O  OE1   . GLU A 1 61  ? 11.37962  -5.02456  -6.14931  1.000 9.18421  ? 61  GLU A OE1   1 
ATOM   469  O  OE2   . GLU A 1 61  ? 9.42264   -4.81054  -5.17728  1.000 12.49148 ? 61  GLU A OE2   1 
ATOM   470  N  N     . SER A 1 62  ? 13.94455  -0.24058  -7.77551  1.000 7.53594  ? 62  SER A N     1 
ATOM   471  C  CA    . SER A 1 62  ? 15.28654  0.22042   -8.11456  1.000 9.30699  ? 62  SER A CA    1 
ATOM   472  C  C     . SER A 1 62  ? 15.52354  1.64543   -7.63360  1.000 8.89599  ? 62  SER A C     1 
ATOM   473  O  O     . SER A 1 62  ? 16.64554  1.98845   -7.24264  1.000 7.51432  ? 62  SER A O     1 
ATOM   474  C  CB    . SER A 1 62  ? 15.51251  0.12237   -9.62356  1.000 7.22214  ? 62  SER A CB    1 
ATOM   475  O  OG    . SER A 1 62  ? 15.39751  -1.21564  -10.07251 1.000 7.41384  ? 62  SER A OG    1 
ATOM   476  N  N     . LEU A 1 63  ? 14.48453  2.48642   -7.65261  1.000 7.68962  ? 63  LEU A N     1 
ATOM   477  C  CA    . LEU A 1 63  ? 14.63153  3.85344   -7.16665  1.000 9.15863  ? 63  LEU A CA    1 
ATOM   478  C  C     . LEU A 1 63  ? 14.72956  3.90149   -5.64865  1.000 8.83507  ? 63  LEU A C     1 
ATOM   479  O  O     . LEU A 1 63  ? 15.44857  4.74651   -5.10370  1.000 11.19016 ? 63  LEU A O     1 
ATOM   480  C  CB    . LEU A 1 63  ? 13.46451  4.71342   -7.65065  1.000 11.16822 ? 63  LEU A CB    1 
ATOM   481  C  CG    . LEU A 1 63  ? 13.32348  4.87737   -9.16565  1.000 11.01679 ? 63  LEU A CG    1 
ATOM   482  C  CD1   . LEU A 1 63  ? 12.18346  5.82735   -9.49466  1.000 12.95197 ? 63  LEU A CD1   1 
ATOM   483  C  CD2   . LEU A 1 63  ? 14.62746  5.36636   -9.77970  1.000 10.13538 ? 63  LEU A CD2   1 
ATOM   484  N  N     . GLU A 1 64  ? 14.02158  3.01050   -4.95061  1.000 10.01519 ? 64  GLU A N     1 
ATOM   485  C  CA    . GLU A 1 64  ? 14.16461  2.93555   -3.50161  1.000 11.54805 ? 64  GLU A CA    1 
ATOM   486  C  C     . GLU A 1 64  ? 15.56063  2.47757   -3.10463  1.000 10.35023 ? 64  GLU A C     1 
ATOM   487  O  O     . GLU A 1 64  ? 16.05964  2.86661   -2.04265  1.000 9.41381  ? 64  GLU A O     1 
ATOM   488  C  CB    . GLU A 1 64  ? 13.11063  1.99856   -2.91256  1.000 11.61020 ? 64  GLU A CB    1 
ATOM   489  C  CG    . GLU A 1 64  ? 11.68163  2.47954   -3.09255  1.000 15.13592 ? 64  GLU A CG    1 
ATOM   490  C  CD    . GLU A 1 64  ? 10.67565  1.57155   -2.41750  1.000 18.26216 ? 64  GLU A CD    1 
ATOM   491  O  OE1   . GLU A 1 64  ? 11.08267  0.50657   -1.90547  1.000 20.75684 ? 64  GLU A OE1   1 
ATOM   492  O  OE2   . GLU A 1 64  ? 9.47664   1.92254   -2.39548  1.000 20.50459 ? 64  GLU A OE2   1 
ATOM   493  N  N     . ASP A 1 65  ? 16.19961  1.65355   -3.93762  1.000 10.40379 ? 65  ASP A N     1 
ATOM   494  C  CA    . ASP A 1 65  ? 17.57762  1.25757   -3.67264  1.000 11.34598 ? 65  ASP A CA    1 
ATOM   495  C  C     . ASP A 1 65  ? 18.52061  2.44557   -3.80869  1.000 8.89883  ? 65  ASP A C     1 
ATOM   496  O  O     . ASP A 1 65  ? 19.44963  2.60360   -3.00872  1.000 10.29521 ? 65  ASP A O     1 
ATOM   497  C  CB    . ASP A 1 65  ? 17.98761  0.12954   -4.61861  1.000 9.77767  ? 65  ASP A CB    1 
ATOM   498  C  CG    . ASP A 1 65  ? 19.27963  -0.54043  -4.20162  1.000 10.00918 ? 65  ASP A CG    1 
ATOM   499  O  OD1   . ASP A 1 65  ? 19.27165  -1.25840  -3.18059  1.000 11.00381 ? 65  ASP A OD1   1 
ATOM   500  O  OD2   . ASP A 1 65  ? 20.30061  -0.35445  -4.89564  1.000 12.75938 ? 65  ASP A OD2   1 
ATOM   501  N  N     . LEU A 1 66  ? 18.29658  3.29054   -4.81771  1.000 8.69009  ? 66  LEU A N     1 
ATOM   502  C  CA    . LEU A 1 66  ? 19.09457  4.50454   -4.95477  1.000 8.88707  ? 66  LEU A CA    1 
ATOM   503  C  C     . LEU A 1 66  ? 18.82059  5.47257   -3.81179  1.000 9.17834  ? 66  LEU A C     1 
ATOM   504  O  O     . LEU A 1 66  ? 19.73059  6.17059   -3.35183  1.000 7.45970  ? 66  LEU A O     1 
ATOM   505  C  CB    . LEU A 1 66  ? 18.81054  5.17550   -6.29978  1.000 9.02334  ? 66  LEU A CB    1 
ATOM   506  C  CG    . LEU A 1 66  ? 19.18752  4.40346   -7.56576  1.000 9.52129  ? 66  LEU A CG    1 
ATOM   507  C  CD1   . LEU A 1 66  ? 18.75748  5.17642   -8.80178  1.000 8.15178  ? 66  LEU A CD1   1 
ATOM   508  C  CD2   . LEU A 1 66  ? 20.67852  4.12347   -7.59879  1.000 9.97248  ? 66  LEU A CD2   1 
ATOM   509  N  N     . GLN A 1 67  ? 17.57060  5.52858   -3.34276  1.000 8.34281  ? 67  GLN A N     1 
ATOM   510  C  CA    . GLN A 1 67  ? 17.22361  6.44761   -2.26278  1.000 9.50993  ? 67  GLN A CA    1 
ATOM   511  C  C     . GLN A 1 67  ? 17.98264  6.11065   -0.98479  1.000 10.59772 ? 67  GLN A C     1 
ATOM   512  O  O     . GLN A 1 67  ? 18.50465  7.00468   -0.30983  1.000 8.95710  ? 67  GLN A O     1 
ATOM   513  C  CB    . GLN A 1 67  ? 15.71562  6.42060   -2.01675  1.000 9.29598  ? 67  GLN A CB    1 
ATOM   514  C  CG    . GLN A 1 67  ? 15.22763  7.48163   -1.04377  1.000 10.27816 ? 67  GLN A CG    1 
ATOM   515  C  CD    . GLN A 1 67  ? 15.42961  8.89061   -1.56882  1.000 9.44169  ? 67  GLN A CD    1 
ATOM   516  O  OE1   . GLN A 1 67  ? 16.41161  9.55563   -1.23586  1.000 12.23723 ? 67  GLN A OE1   1 
ATOM   517  N  NE2   . GLN A 1 67  ? 14.49659  9.35258   -2.39282  1.000 11.95687 ? 67  GLN A NE2   1 
ATOM   518  N  N     . ARG A 1 68  ? 18.05811  4.82320   -0.63811  1.000 10.37344 ? 68  ARG A N     1 
ATOM   519  C  CA    . ARG A 1 68  ? 18.81087  4.42373   0.54608   1.000 11.07947 ? 68  ARG A CA    1 
ATOM   520  C  C     . ARG A 1 68  ? 20.30995  4.60722   0.34775   1.000 12.08272 ? 68  ARG A C     1 
ATOM   521  O  O     . ARG A 1 68  ? 21.04102  4.82199   1.32148   1.000 11.78367 ? 68  ARG A O     1 
ATOM   522  C  CB    . ARG A 1 68  ? 18.49762  2.97119   0.90423   1.000 11.79249 ? 68  ARG A CB    1 
ATOM   523  C  CG    . ARG A 1 68  ? 17.02716  2.70586   1.18782   1.000 17.35629 ? 68  ARG A CG    1 
ATOM   524  C  CD    . ARG A 1 68  ? 16.79628  1.26118   1.60440   1.000 19.15307 ? 68  ARG A CD    1 
ATOM   525  N  NE    . ARG A 1 68  ? 17.17627  0.32001   0.55753   1.000 18.51549 ? 68  ARG A NE    1 
ATOM   526  C  CZ    . ARG A 1 68  ? 16.35247  -0.13161  -0.37827  1.000 18.33488 ? 68  ARG A CZ    1 
ATOM   527  N  NH1   . ARG A 1 68  ? 15.08874  0.25583   -0.43224  1.000 18.80468 ? 68  ARG A NH1   1 
ATOM   528  N  NH2   . ARG A 1 68  ? 16.80792  -0.99383  -1.28282  1.000 16.91888 ? 68  ARG A NH2   1 
ATOM   529  N  N     . SER A 1 69  ? 20.78466  4.52668   -0.89680  1.000 12.25458 ? 69  SER A N     1 
ATOM   530  C  CA    . SER A 1 69  ? 22.20665  4.71168   -1.16484  1.000 12.34344 ? 69  SER A CA    1 
ATOM   531  C  C     . SER A 1 69  ? 22.60464  6.18169   -1.08389  1.000 12.04594 ? 69  SER A C     1 
ATOM   532  O  O     . SER A 1 69  ? 23.67665  6.50771   -0.56192  1.000 11.92522 ? 69  SER A O     1 
ATOM   533  C  CB    . SER A 1 69  ? 22.56462  4.13664   -2.53583  1.000 10.65861 ? 69  SER A CB    1 
ATOM   534  O  OG    . SER A 1 69  ? 22.31563  2.74264   -2.58478  1.000 12.20994 ? 69  SER A OG    1 
ATOM   535  N  N     . PHE A 1 70  ? 21.75862  7.07966   -1.59590  1.000 9.81087  ? 70  PHE A N     1 
ATOM   536  C  CA    . PHE A 1 70  ? 22.06161  8.50467   -1.51095  1.000 11.38326 ? 70  PHE A CA    1 
ATOM   537  C  C     . PHE A 1 70  ? 21.93964  9.01171   -0.07896  1.000 10.97011 ? 70  PHE A C     1 
ATOM   538  O  O     . PHE A 1 70  ? 22.71364  9.87873   0.34399   1.000 12.20036 ? 70  PHE A O     1 
ATOM   539  C  CB    . PHE A 1 70  ? 21.14659  9.30163   -2.44095  1.000 10.65805 ? 70  PHE A CB    1 
ATOM   540  C  CG    . PHE A 1 70  ? 21.54856  9.24159   -3.88996  1.000 10.17222 ? 70  PHE A CG    1 
ATOM   541  C  CD1   . PHE A 1 70  ? 22.72654  9.82759   -4.32000  1.000 9.87204  ? 70  PHE A CD1   1 
ATOM   542  C  CD2   . PHE A 1 70  ? 20.74154  8.61656   -4.82393  1.000 10.79519 ? 70  PHE A CD2   1 
ATOM   543  C  CE1   . PHE A 1 70  ? 23.09751  9.77855   -5.65201  1.000 11.90096 ? 70  PHE A CE1   1 
ATOM   544  C  CE2   . PHE A 1 70  ? 21.10651  8.56452   -6.15693  1.000 9.94818  ? 70  PHE A CE2   1 
ATOM   545  C  CZ    . PHE A 1 70  ? 22.28550  9.14752   -6.57097  1.000 7.65556  ? 70  PHE A CZ    1 
ATOM   546  N  N     . GLN A 1 71  ? 20.97566  8.48673   0.68107   1.000 11.47388 ? 71  GLN A N     1 
ATOM   547  C  CA    . GLN A 1 71  ? 20.81168  8.91977   2.06506   1.000 13.58467 ? 71  GLN A CA    1 
ATOM   548  C  C     . GLN A 1 71  ? 21.97771  8.47680   2.93805   1.000 12.35060 ? 71  GLN A C     1 
ATOM   549  O  O     . GLN A 1 71  ? 22.36472  9.19883   3.86402   1.000 9.69434  ? 71  GLN A O     1 
ATOM   550  C  CB    . GLN A 1 71  ? 19.49370  8.39377   2.63311   1.000 12.64138 ? 71  GLN A CB    1 
ATOM   551  C  CG    . GLN A 1 71  ? 18.26068  9.10775   2.10311   1.000 15.24721 ? 71  GLN A CG    1 
ATOM   552  C  CD    . GLN A 1 71  ? 16.98070  8.60676   2.74415   1.000 20.33755 ? 71  GLN A CD    1 
ATOM   553  O  OE1   . GLN A 1 71  ? 16.99172  7.63878   3.50418   1.000 20.56341 ? 71  GLN A OE1   1 
ATOM   554  N  NE2   . GLN A 1 71  ? 15.86869  9.26674   2.44016   1.000 21.09626 ? 71  GLN A NE2   1 
ATOM   555  N  N     . ALA A 1 72  ? 22.54771  7.30080   2.66508   1.000 11.15770 ? 72  ALA A N     1 
ATOM   556  C  CA    . ALA A 1 72  ? 23.71873  6.85283   3.40607   1.000 11.35145 ? 72  ALA A CA    1 
ATOM   557  C  C     . ALA A 1 72  ? 24.94572  7.70483   3.11401   1.000 14.30383 ? 72  ALA A C     1 
ATOM   558  O  O     . ALA A 1 72  ? 25.91973  7.64986   3.87299   1.000 11.79700 ? 72  ALA A O     1 
ATOM   559  C  CB    . ALA A 1 72  ? 24.01373  5.38582   3.08910   1.000 12.36303 ? 72  ALA A CB    1 
ATOM   560  N  N     . ARG A 1 73  ? 24.91923  8.49113   2.03679   1.000 13.27304 ? 73  ARG A N     1 
ATOM   561  C  CA    . ARG A 1 73  ? 26.02494  9.36288   1.66312   1.000 13.52258 ? 73  ARG A CA    1 
ATOM   562  C  C     . ARG A 1 73  ? 25.68476  10.83772  1.85200   1.000 14.20608 ? 73  ARG A C     1 
ATOM   563  O  O     . ARG A 1 73  ? 26.33869  11.70376  1.26207   1.000 12.52788 ? 73  ARG A O     1 
ATOM   564  C  CB    . ARG A 1 73  ? 26.44226  9.08739   0.21875   1.000 12.72054 ? 73  ARG A CB    1 
ATOM   565  C  CG    . ARG A 1 73  ? 26.87995  7.65133   -0.01889  1.000 15.11511 ? 73  ARG A CG    1 
ATOM   566  C  CD    . ARG A 1 73  ? 27.08451  7.35743   -1.49440  1.000 14.88933 ? 73  ARG A CD    1 
ATOM   567  N  NE    . ARG A 1 73  ? 27.49397  5.97524   -1.71280  1.000 17.34109 ? 73  ARG A NE    1 
ATOM   568  C  CZ    . ARG A 1 73  ? 28.75439  5.57120   -1.79241  1.000 19.59920 ? 73  ARG A CZ    1 
ATOM   569  N  NH1   . ARG A 1 73  ? 29.76082  6.42348   -1.68867  1.000 18.56890 ? 73  ARG A NH1   1 
ATOM   570  N  NH2   . ARG A 1 73  ? 29.01121  4.27998   -1.98264  1.000 20.43931 ? 73  ARG A NH2   1 
ATOM   571  N  N     . GLY A 1 74  ? 24.67168  11.13782  2.66192   1.000 11.67212 ? 74  GLY A N     1 
ATOM   572  C  CA    . GLY A 1 74  ? 24.30167  12.50682  2.95688   1.000 13.37907 ? 74  GLY A CA    1 
ATOM   573  C  C     . GLY A 1 74  ? 23.47465  13.20378  1.90088   1.000 16.22264 ? 74  GLY A C     1 
ATOM   574  O  O     . GLY A 1 74  ? 23.28364  14.42178  1.99385   1.000 15.16925 ? 74  GLY A O     1 
ATOM   575  N  N     . SER A 1 75  ? 22.97063  12.47875  0.90891   1.000 11.60293 ? 75  SER A N     1 
ATOM   576  C  CA    . SER A 1 75  ? 22.20860  13.06171  -0.18609  1.000 14.01793 ? 75  SER A CA    1 
ATOM   577  C  C     . SER A 1 75  ? 20.77061  12.54070  -0.15104  1.000 12.93760 ? 75  SER A C     1 
ATOM   578  O  O     . SER A 1 75  ? 20.32363  11.94473  0.83298   1.000 12.23650 ? 75  SER A O     1 
ATOM   579  C  CB    . SER A 1 75  ? 22.88858  12.76367  -1.52410  1.000 13.01404 ? 75  SER A CB    1 
ATOM   580  O  OG    . SER A 1 75  ? 22.19355  13.37464  -2.59710  1.000 14.16138 ? 75  SER A OG    1 
ATOM   581  N  N     . ARG A 1 76  ? 20.04755  12.76720  -1.24616  1.000 13.08703 ? 76  ARG A N     1 
ATOM   582  C  CA    . ARG A 1 76  ? 18.64797  12.37786  -1.33573  1.000 11.48145 ? 76  ARG A CA    1 
ATOM   583  C  C     . ARG A 1 76  ? 18.24211  12.32406  -2.80147  1.000 12.73493 ? 76  ARG A C     1 
ATOM   584  O  O     . ARG A 1 76  ? 18.58943  13.21636  -3.57914  1.000 11.91148 ? 76  ARG A O     1 
ATOM   585  C  CB    . ARG A 1 76  ? 17.75360  13.35567  -0.56320  1.000 16.21037 ? 76  ARG A CB    1 
ATOM   586  C  CG    . ARG A 1 76  ? 16.26694  13.05409  -0.64302  1.000 14.89728 ? 76  ARG A CG    1 
ATOM   587  C  CD    . ARG A 1 76  ? 15.49190  13.87891  0.37207   1.000 15.05217 ? 76  ARG A CD    1 
ATOM   588  N  NE    . ARG A 1 76  ? 15.75762  15.30660  0.23876   1.000 18.09459 ? 76  ARG A NE    1 
ATOM   589  C  CZ    . ARG A 1 76  ? 14.97534  16.15788  -0.41060  1.000 15.17087 ? 76  ARG A CZ    1 
ATOM   590  N  NH1   . ARG A 1 76  ? 13.85774  15.76082  -0.99637  1.000 14.02001 ? 76  ARG A NH1   1 
ATOM   591  N  NH2   . ARG A 1 76  ? 15.32134  17.44075  -0.47064  1.000 17.38389 ? 76  ARG A NH2   1 
ATOM   592  N  N     . LEU A 1 77  ? 17.51255  11.27258  -3.16894  1.000 11.06866 ? 77  LEU A N     1 
ATOM   593  C  CA    . LEU A 1 77  ? 17.04153  11.11354  -4.53892  1.000 10.97317 ? 77  LEU A CA    1 
ATOM   594  C  C     . LEU A 1 77  ? 15.74952  11.89652  -4.73992  1.000 9.40770  ? 77  LEU A C     1 
ATOM   595  O  O     . LEU A 1 77  ? 14.82153  11.80054  -3.93090  1.000 8.89856  ? 77  LEU A O     1 
ATOM   596  C  CB    . LEU A 1 77  ? 16.82153  9.63553   -4.85887  1.000 8.03252  ? 77  LEU A CB    1 
ATOM   597  C  CG    . LEU A 1 77  ? 16.30050  9.31748   -6.26185  1.000 8.87088  ? 77  LEU A CG    1 
ATOM   598  C  CD1   . LEU A 1 77  ? 17.28448  9.79046   -7.32189  1.000 8.18330  ? 77  LEU A CD1   1 
ATOM   599  C  CD2   . LEU A 1 77  ? 16.01751  7.83047   -6.41080  1.000 12.99684 ? 77  LEU A CD2   1 
ATOM   600  N  N     . LEU A 1 78  ? 15.69249  12.66949  -5.82094  1.000 8.98656  ? 78  LEU A N     1 
ATOM   601  C  CA    . LEU A 1 78  ? 14.54047  13.50547  -6.13894  1.000 9.30638  ? 78  LEU A CA    1 
ATOM   602  C  C     . LEU A 1 78  ? 13.77445  12.87643  -7.29391  1.000 10.16996 ? 78  LEU A C     1 
ATOM   603  O  O     . LEU A 1 78  ? 14.33543  12.66540  -8.37391  1.000 10.65182 ? 78  LEU A O     1 
ATOM   604  C  CB    . LEU A 1 78  ? 14.97546  14.92746  -6.49499  1.000 9.57450  ? 78  LEU A CB    1 
ATOM   605  C  CG    . LEU A 1 78  ? 15.80247  15.68150  -5.45303  1.000 10.42722 ? 78  LEU A CG    1 
ATOM   606  C  CD1   . LEU A 1 78  ? 16.17245  17.06549  -5.96408  1.000 10.93231 ? 78  LEU A CD1   1 
ATOM   607  C  CD2   . LEU A 1 78  ? 15.05150  15.78053  -4.13702  1.000 11.55009 ? 78  LEU A CD2   1 
ATOM   608  N  N     . VAL A 1 79  ? 12.49646  12.57943  -7.06487  1.000 10.45137 ? 79  VAL A N     1 
ATOM   609  C  CA    . VAL A 1 79  ? 11.63444  12.03439  -8.10784  1.000 10.16798 ? 79  VAL A CA    1 
ATOM   610  C  C     . VAL A 1 79  ? 10.67743  13.12337  -8.57085  1.000 12.24899 ? 79  VAL A C     1 
ATOM   611  O  O     . VAL A 1 79  ? 9.61744   13.33138  -7.97183  1.000 12.77286 ? 79  VAL A O     1 
ATOM   612  C  CB    . VAL A 1 79  ? 10.86946  10.79240  -7.61178  1.000 11.64926 ? 79  VAL A CB    1 
ATOM   613  C  CG1   . VAL A 1 79  ? 10.02445  10.20336  -8.73375  1.000 10.96104 ? 79  VAL A CG1   1 
ATOM   614  C  CG2   . VAL A 1 79  ? 11.83948  9.75542   -7.07077  1.000 10.77622 ? 79  VAL A CG2   1 
ATOM   615  N  N     . LEU A 1 80  ? 11.04740  13.82934  -9.63488  1.000 12.20549 ? 80  LEU A N     1 
ATOM   616  C  CA    . LEU A 1 80  ? 10.24338  14.93631  -10.13089 1.000 12.33522 ? 80  LEU A CA    1 
ATOM   617  C  C     . LEU A 1 80  ? 9.12036   14.42828  -11.02486 1.000 16.39117 ? 80  LEU A C     1 
ATOM   618  O  O     . LEU A 1 80  ? 9.31835   13.52926  -11.84783 1.000 14.87360 ? 80  LEU A O     1 
ATOM   619  C  CB    . LEU A 1 80  ? 11.11835  15.92730  -10.89794 1.000 14.90164 ? 80  LEU A CB    1 
ATOM   620  C  CG    . LEU A 1 80  ? 12.26937  16.56633  -10.11599 1.000 14.58120 ? 80  LEU A CG    1 
ATOM   621  C  CD1   . LEU A 1 80  ? 12.99134  17.60231  -10.96503 1.000 15.01155 ? 80  LEU A CD1   1 
ATOM   622  C  CD2   . LEU A 1 80  ? 11.76139  17.18937  -8.82799  1.000 15.60424 ? 80  LEU A CD2   1 
ATOM   623  N  N     . ARG A 1 81  ? 7.93169   14.99738  -10.84663 1.000 15.39775 ? 81  ARG A N     1 
ATOM   624  C  CA    . ARG A 1 81  ? 6.77392   14.63343  -11.65058 1.000 15.77803 ? 81  ARG A CA    1 
ATOM   625  C  C     . ARG A 1 81  ? 6.68876   15.52809  -12.87886 1.000 15.15547 ? 81  ARG A C     1 
ATOM   626  O  O     . ARG A 1 81  ? 7.03018   16.71288  -12.82303 1.000 20.27649 ? 81  ARG A O     1 
ATOM   627  C  CB    . ARG A 1 81  ? 5.48398   14.74578  -10.83467 1.000 14.52035 ? 81  ARG A CB    1 
ATOM   628  C  CG    . ARG A 1 81  ? 5.07848   13.47316  -10.10365 1.000 16.70618 ? 81  ARG A CG    1 
ATOM   629  C  CD    . ARG A 1 81  ? 5.97846   13.18123  -8.91421  1.000 14.35932 ? 81  ARG A CD    1 
ATOM   630  N  NE    . ARG A 1 81  ? 5.52264   12.01298  -8.16992  1.000 13.69400 ? 81  ARG A NE    1 
ATOM   631  C  CZ    . ARG A 1 81  ? 6.06882   11.58247  -7.04083  1.000 13.63222 ? 81  ARG A CZ    1 
ATOM   632  N  NH1   . ARG A 1 81  ? 7.09870   12.20415  -6.49028  1.000 15.09600 ? 81  ARG A NH1   1 
ATOM   633  N  NH2   . ARG A 1 81  ? 5.56792   10.50197  -6.44852  1.000 12.82242 ? 81  ARG A NH2   1 
ATOM   634  N  N     . GLY A 1 82  ? 6.23330   14.95817  -13.98681 1.000 18.48847 ? 82  GLY A N     1 
ATOM   635  C  CA    . GLY A 1 82  ? 6.06126   15.71113  -15.21283 1.000 20.80859 ? 82  GLY A CA    1 
ATOM   636  C  C     . GLY A 1 82  ? 6.91624   15.22010  -16.36083 1.000 19.87349 ? 82  GLY A C     1 
ATOM   637  O  O     . GLY A 1 82  ? 7.48025   14.12311  -16.29881 1.000 18.52840 ? 82  GLY A O     1 
ATOM   638  N  N     . LYS A 1 83  ? 7.01922   16.03007  -17.42186 1.000 19.32154 ? 83  LYS A N     1 
ATOM   639  C  CA    . LYS A 1 83  ? 7.83219   15.70404  -18.57987 1.000 19.87320 ? 83  LYS A CA    1 
ATOM   640  C  C     . LYS A 1 83  ? 9.16119   16.44905  -18.52692 1.000 18.51657 ? 83  LYS A C     1 
ATOM   641  O  O     . LYS A 1 83  ? 9.23819   17.55407  -17.97995 1.000 19.80761 ? 83  LYS A O     1 
ATOM   642  C  CB    . LYS A 1 83  ? 7.09216   16.05799  -19.87286 1.000 20.36482 ? 83  LYS A CB    1 
ATOM   643  C  CG    . LYS A 1 83  ? 5.81717   15.25898  -20.08981 1.000 22.46450 ? 83  LYS A CG    1 
ATOM   644  C  CD    . LYS A 1 83  ? 5.14213   15.62793  -21.39981 0.000 23.08831 ? 83  LYS A CD    1 
ATOM   645  C  CE    . LYS A 1 83  ? 3.89714   14.78692  -21.62876 0.000 23.32055 ? 83  LYS A CE    1 
ATOM   646  N  NZ    . LYS A 1 83  ? 3.21511   15.13887  -22.90375 0.000 22.88118 ? 83  LYS A NZ    1 
ATOM   647  N  N     . PRO A 1 84  ? 10.22518  15.86104  -19.08292 1.000 16.46390 ? 84  PRO A N     1 
ATOM   648  C  CA    . PRO A 1 84  ? 11.54418  16.51406  -18.99097 1.000 19.51831 ? 84  PRO A CA    1 
ATOM   649  C  C     . PRO A 1 84  ? 11.59915  17.88604  -19.64201 1.000 17.63931 ? 84  PRO A C     1 
ATOM   650  O  O     . PRO A 1 84  ? 12.21216  18.80406  -19.08205 1.000 16.80646 ? 84  PRO A O     1 
ATOM   651  C  CB    . PRO A 1 84  ? 12.47317  15.51404  -19.69396 1.000 14.85290 ? 84  PRO A CB    1 
ATOM   652  C  CG    . PRO A 1 84  ? 11.77318  14.20004  -19.58290 1.000 15.68254 ? 84  PRO A CG    1 
ATOM   653  C  CD    . PRO A 1 84  ? 10.31018  14.52103  -19.68888 1.000 16.67755 ? 84  PRO A CD    1 
ATOM   654  N  N     . GLU A 1 85  ? 10.97513  18.05700  -20.80900 1.000 15.95832 ? 85  GLU A N     1 
ATOM   655  C  CA    . GLU A 1 85  ? 11.03310  19.33898  -21.50204 1.000 20.56240 ? 85  GLU A CA    1 
ATOM   656  C  C     . GLU A 1 85  ? 10.31211  20.44699  -20.74506 1.000 18.81268 ? 85  GLU A C     1 
ATOM   657  O  O     . GLU A 1 85  ? 10.56510  21.62699  -21.01210 1.000 17.77328 ? 85  GLU A O     1 
ATOM   658  C  CB    . GLU A 1 85  ? 10.44307  19.21293  -22.90903 1.000 24.40393 ? 85  GLU A CB    1 
ATOM   659  C  CG    . GLU A 1 85  ? 11.12006  18.17091  -23.78901 1.000 25.89870 ? 85  GLU A CG    1 
ATOM   660  C  CD    . GLU A 1 85  ? 10.52008  16.78691  -23.62796 1.000 22.77894 ? 85  GLU A CD    1 
ATOM   661  O  OE1   . GLU A 1 85  ? 9.56610   16.63992  -22.83593 1.000 27.70678 ? 85  GLU A OE1   1 
ATOM   662  O  OE2   . GLU A 1 85  ? 11.00007  15.84789  -24.29594 1.000 26.23866 ? 85  GLU A OE2   1 
ATOM   663  N  N     . GLU A 1 86  ? 9.42313   20.10001  -19.81303 1.000 20.10101 ? 86  GLU A N     1 
ATOM   664  C  CA    . GLU A 1 86  ? 8.69514   21.09403  -19.03605 1.000 19.27444 ? 86  GLU A CA    1 
ATOM   665  C  C     . GLU A 1 86  ? 9.27017   21.31208  -17.64207 1.000 15.91164 ? 86  GLU A C     1 
ATOM   666  O  O     . GLU A 1 86  ? 9.04317   22.37610  -17.05809 1.000 20.06835 ? 86  GLU A O     1 
ATOM   667  C  CB    . GLU A 1 86  ? 7.22115   20.69002  -18.90200 1.000 21.30625 ? 86  GLU A CB    1 
ATOM   668  C  CG    . GLU A 1 86  ? 6.49012   20.54898  -20.22498 1.000 22.66329 ? 86  GLU A CG    1 
ATOM   669  C  CD    . GLU A 1 86  ? 5.07113   20.04597  -20.04994 1.000 23.59608 ? 86  GLU A CD    1 
ATOM   670  O  OE1   . GLU A 1 86  ? 4.68316   19.74000  -18.90292 1.000 22.22637 ? 86  GLU A OE1   1 
ATOM   671  O  OE2   . GLU A 1 86  ? 4.34411   19.95494  -21.06092 1.000 27.04622 ? 86  GLU A OE2   1 
ATOM   672  N  N     . VAL A 1 87  ? 10.00219  20.34110  -17.10105 1.000 15.51452 ? 87  VAL A N     1 
ATOM   673  C  CA    . VAL A 1 87  ? 10.48522  20.43215  -15.72607 1.000 17.73574 ? 87  VAL A CA    1 
ATOM   674  C  C     . VAL A 1 87  ? 11.90221  20.98916  -15.65911 1.000 15.38649 ? 87  VAL A C     1 
ATOM   675  O  O     . VAL A 1 87  ? 12.21923  21.78519  -14.77314 1.000 16.19647 ? 87  VAL A O     1 
ATOM   676  C  CB    . VAL A 1 87  ? 10.38924  19.04817  -15.05202 1.000 20.00741 ? 87  VAL A CB    1 
ATOM   677  C  CG1   . VAL A 1 87  ? 11.05527  19.07321  -13.68604 1.000 18.54172 ? 87  VAL A CG1   1 
ATOM   678  C  CG2   . VAL A 1 87  ? 8.93625   18.62016  -14.92698 1.000 18.64632 ? 87  VAL A CG2   1 
ATOM   679  N  N     . PHE A 1 88  ? 12.76720  20.59814  -16.59312 1.000 14.13106 ? 88  PHE A N     1 
ATOM   680  C  CA    . PHE A 1 88  ? 14.17720  20.97415  -16.53116 1.000 13.29759 ? 88  PHE A CA    1 
ATOM   681  C  C     . PHE A 1 88  ? 14.40818  22.47815  -16.68021 1.000 13.25020 ? 88  PHE A C     1 
ATOM   682  O  O     . PHE A 1 88  ? 15.21019  23.03818  -15.92224 1.000 13.65103 ? 88  PHE A O     1 
ATOM   683  C  CB    . PHE A 1 88  ? 14.98318  20.19913  -17.57915 1.000 11.20227 ? 88  PHE A CB    1 
ATOM   684  C  CG    . PHE A 1 88  ? 15.32820  18.79814  -17.15612 1.000 12.80988 ? 88  PHE A CG    1 
ATOM   685  C  CD1   . PHE A 1 88  ? 16.19522  18.57918  -16.10013 1.000 12.77668 ? 88  PHE A CD1   1 
ATOM   686  C  CD2   . PHE A 1 88  ? 14.78119  17.70312  -17.80707 1.000 15.80834 ? 88  PHE A CD2   1 
ATOM   687  C  CE1   . PHE A 1 88  ? 16.51324  17.29520  -15.69910 1.000 12.64575 ? 88  PHE A CE1   1 
ATOM   688  C  CE2   . PHE A 1 88  ? 15.09721  16.41613  -17.41004 1.000 13.08842 ? 88  PHE A CE2   1 
ATOM   689  C  CZ    . PHE A 1 88  ? 15.96424  16.21417  -16.35605 1.000 11.98764 ? 88  PHE A CZ    1 
ATOM   690  N  N     . PRO A 1 89  ? 13.75416  23.17612  -17.61822 1.000 12.24325 ? 89  PRO A N     1 
ATOM   691  C  CA    . PRO A 1 89  ? 13.91214  24.64212  -17.66227 1.000 15.53653 ? 89  PRO A CA    1 
ATOM   692  C  C     . PRO A 1 89  ? 13.50916  25.33615  -16.37228 1.000 14.86916 ? 89  PRO A C     1 
ATOM   693  O  O     . PRO A 1 89  ? 13.98816  26.44516  -16.10732 1.000 15.11110 ? 89  PRO A O     1 
ATOM   694  C  CB    . PRO A 1 89  ? 13.00711  25.05907  -18.82826 1.000 14.90719 ? 89  PRO A CB    1 
ATOM   695  C  CG    . PRO A 1 89  ? 12.95711  23.86905  -19.69422 1.000 12.05909 ? 89  PRO A CG    1 
ATOM   696  C  CD    . PRO A 1 89  ? 12.95413  22.69507  -18.76119 1.000 16.51232 ? 89  PRO A CD    1 
ATOM   697  N  N     . ARG A 1 90  ? 12.64782  24.72003  -15.56145 1.000 15.23738 ? 90  ARG A N     1 
ATOM   698  C  CA    . ARG A 1 90  ? 12.27726  25.30093  -14.27651 1.000 14.27339 ? 90  ARG A CA    1 
ATOM   699  C  C     . ARG A 1 90  ? 13.36698  25.08142  -13.23395 1.000 15.59777 ? 90  ARG A C     1 
ATOM   700  O  O     . ARG A 1 90  ? 13.79239  26.02658  -12.56077 1.000 14.61900 ? 90  ARG A O     1 
ATOM   701  C  CB    . ARG A 1 90  ? 10.95364  24.70503  -13.79607 1.000 18.09067 ? 90  ARG A CB    1 
ATOM   702  C  CG    . ARG A 1 90  ? 10.54486  25.14108  -12.39886 1.000 16.56962 ? 90  ARG A CG    1 
ATOM   703  C  CD    . ARG A 1 90  ? 9.35144   24.33933  -11.91010 1.000 23.50645 ? 90  ARG A CD    1 
ATOM   704  N  NE    . ARG A 1 90  ? 9.67772   22.92772  -11.74582 1.000 24.37807 ? 90  ARG A NE    1 
ATOM   705  C  CZ    . ARG A 1 90  ? 8.78283   21.96995  -11.54575 1.000 27.63353 ? 90  ARG A CZ    1 
ATOM   706  N  NH1   . ARG A 1 90  ? 7.48713   22.23315  -11.49949 1.000 38.10213 ? 90  ARG A NH1   1 
ATOM   707  N  NH2   . ARG A 1 90  ? 9.19792   20.71588  -11.39122 1.000 30.20852 ? 90  ARG A NH2   1 
ATOM   708  N  N     . VAL A 1 91  ? 13.83125  23.83725  -13.08824 1.000 15.55940 ? 91  VAL A N     1 
ATOM   709  C  CA    . VAL A 1 91  ? 14.82627  23.52929  -12.06725 1.000 15.70724 ? 91  VAL A CA    1 
ATOM   710  C  C     . VAL A 1 91  ? 16.20726  24.05029  -12.44030 1.000 13.12126 ? 91  VAL A C     1 
ATOM   711  O  O     . VAL A 1 91  ? 17.08828  24.12532  -11.57632 1.000 12.87350 ? 91  VAL A O     1 
ATOM   712  C  CB    . VAL A 1 91  ? 14.87229  22.01230  -11.80221 1.000 13.15632 ? 91  VAL A CB    1 
ATOM   713  C  CG1   . VAL A 1 91  ? 13.50630  21.50930  -11.36216 1.000 13.65999 ? 91  VAL A CG1   1 
ATOM   714  C  CG2   . VAL A 1 91  ? 15.34627  21.26827  -13.04019 1.000 13.54090 ? 91  VAL A CG2   1 
ATOM   715  N  N     . PHE A 1 92  ? 16.42623  24.40925  -13.70731 1.000 13.33404 ? 92  PHE A N     1 
ATOM   716  C  CA    . PHE A 1 92  ? 17.70322  24.99825  -14.09636 1.000 13.16797 ? 92  PHE A CA    1 
ATOM   717  C  C     . PHE A 1 92  ? 17.88922  26.36927  -13.45840 1.000 13.40147 ? 92  PHE A C     1 
ATOM   718  O  O     . PHE A 1 92  ? 18.93023  26.64830  -12.85043 1.000 11.95254 ? 92  PHE A O     1 
ATOM   719  C  CB    . PHE A 1 92  ? 17.80018  25.09721  -15.62036 1.000 12.87111 ? 92  PHE A CB    1 
ATOM   720  C  CG    . PHE A 1 92  ? 18.07918  23.78619  -16.29933 1.000 13.75929 ? 92  PHE A CG    1 
ATOM   721  C  CD1   . PHE A 1 92  ? 18.53020  22.69621  -15.57530 1.000 13.16865 ? 92  PHE A CD1   1 
ATOM   722  C  CD2   . PHE A 1 92  ? 17.89315  23.64615  -17.66532 1.000 14.03382 ? 92  PHE A CD2   1 
ATOM   723  C  CE1   . PHE A 1 92  ? 18.78820  21.49120  -16.19827 1.000 14.10925 ? 92  PHE A CE1   1 
ATOM   724  C  CE2   . PHE A 1 92  ? 18.15015  22.44413  -18.29429 1.000 13.22424 ? 92  PHE A CE2   1 
ATOM   725  C  CZ    . PHE A 1 92  ? 18.59817  21.36616  -17.56027 1.000 13.36159 ? 92  PHE A CZ    1 
ATOM   726  N  N     . ARG A 1 93  ? 16.88463  27.23875  -13.58187 1.000 13.18436 ? 93  ARG A N     1 
ATOM   727  C  CA    . ARG A 1 93  ? 16.97732  28.57441  -13.00454 1.000 14.77274 ? 93  ARG A CA    1 
ATOM   728  C  C     . ARG A 1 93  ? 16.78439  28.56180  -11.49432 1.000 13.37085 ? 93  ARG A C     1 
ATOM   729  O  O     . ARG A 1 93  ? 17.37162  29.39320  -10.79319 1.000 13.32339 ? 93  ARG A O     1 
ATOM   730  C  CB    . ARG A 1 93  ? 15.94650  29.50533  -13.64767 1.000 14.23036 ? 93  ARG A CB    1 
ATOM   731  C  CG    . ARG A 1 93  ? 16.33263  30.04195  -15.02061 1.000 17.54809 ? 93  ARG A CG    1 
ATOM   732  C  CD    . ARG A 1 93  ? 16.11251  29.01716  -16.12119 1.000 16.43045 ? 93  ARG A CD    1 
ATOM   733  N  NE    . ARG A 1 93  ? 16.37895  29.57570  -17.44128 1.000 17.90676 ? 93  ARG A NE    1 
ATOM   734  C  CZ    . ARG A 1 93  ? 16.28301  28.89682  -18.57608 1.000 16.00909 ? 93  ARG A CZ    1 
ATOM   735  N  NH1   . ARG A 1 93  ? 15.93053  27.62173  -18.59119 1.000 15.37663 ? 93  ARG A NH1   1 
ATOM   736  N  NH2   . ARG A 1 93  ? 16.54767  29.51265  -19.72494 1.000 15.06510 ? 93  ARG A NH2   1 
ATOM   737  N  N     . GLU A 1 94  ? 15.97226  27.63633  -10.97840 1.000 15.30443 ? 94  GLU A N     1 
ATOM   738  C  CA    . GLU A 1 94  ? 15.70229  27.60638  -9.54439  1.000 12.97605 ? 94  GLU A CA    1 
ATOM   739  C  C     . GLU A 1 94  ? 16.91531  27.12841  -8.75640  1.000 12.05704 ? 94  GLU A C     1 
ATOM   740  O  O     . GLU A 1 94  ? 17.26333  27.71644  -7.72543  1.000 11.27669 ? 94  GLU A O     1 
ATOM   741  C  CB    . GLU A 1 94  ? 14.49430  26.71437  -9.25934  1.000 14.43897 ? 94  GLU A CB    1 
ATOM   742  C  CG    . GLU A 1 94  ? 14.26534  26.42642  -7.78433  1.000 14.91790 ? 94  GLU A CG    1 
ATOM   743  C  CD    . GLU A 1 94  ? 13.11235  25.47042  -7.55227  1.000 14.28216 ? 94  GLU A CD    1 
ATOM   744  O  OE1   . GLU A 1 94  ? 12.11533  25.54638  -8.30026  1.000 13.45915 ? 94  GLU A OE1   1 
ATOM   745  O  OE2   . GLU A 1 94  ? 13.20838  24.63744  -6.62725  1.000 15.19855 ? 94  GLU A OE2   1 
ATOM   746  N  N     . TRP A 1 95  ? 17.56931  26.06840  -9.22039  1.000 11.12764 ? 95  TRP A N     1 
ATOM   747  C  CA    . TRP A 1 95  ? 18.68733  25.46843  -8.50639  1.000 13.37282 ? 95  TRP A CA    1 
ATOM   748  C  C     . TRP A 1 95  ? 20.03632  26.05643  -8.90144  1.000 13.72942 ? 95  TRP A C     1 
ATOM   749  O  O     . TRP A 1 95  ? 21.05933  25.64145  -8.34545  1.000 13.25095 ? 95  TRP A O     1 
ATOM   750  C  CB    . TRP A 1 95  ? 18.69834  23.95242  -8.73035  1.000 12.88723 ? 95  TRP A CB    1 
ATOM   751  C  CG    . TRP A 1 95  ? 17.46435  23.26643  -8.22030  1.000 11.29454 ? 95  TRP A CG    1 
ATOM   752  C  CD1   . TRP A 1 95  ? 16.54837  23.77345  -7.34530  1.000 12.13594 ? 95  TRP A CD1   1 
ATOM   753  C  CD2   . TRP A 1 95  ? 17.00836  21.95042  -8.55925  1.000 10.51313 ? 95  TRP A CD2   1 
ATOM   754  N  NE1   . TRP A 1 95  ? 15.55338  22.85545  -7.11625  1.000 11.69688 ? 95  TRP A NE1   1 
ATOM   755  C  CE2   . TRP A 1 95  ? 15.81237  21.72743  -7.84922  1.000 11.32008 ? 95  TRP A CE2   1 
ATOM   756  C  CE3   . TRP A 1 95  ? 17.49735  20.94039  -9.39323  1.000 10.79113 ? 95  TRP A CE3   1 
ATOM   757  C  CZ2   . TRP A 1 95  ? 15.09638  20.53642  -7.94717  1.000 10.80593 ? 95  TRP A CZ2   1 
ATOM   758  C  CZ3   . TRP A 1 95  ? 16.78535  19.75739  -9.48918  1.000 12.11528 ? 95  TRP A CZ3   1 
ATOM   759  C  CH2   . TRP A 1 95  ? 15.59937  19.56540  -8.77015  1.000 11.59550 ? 95  TRP A CH2   1 
ATOM   760  N  N     . GLY A 1 96  ? 20.06429  27.00840  -9.83347  1.000 13.72458 ? 96  GLY A N     1 
ATOM   761  C  CA    . GLY A 1 96  ? 21.31328  27.58740  -10.28851 1.000 16.09143 ? 96  GLY A CA    1 
ATOM   762  C  C     . GLY A 1 96  ? 22.22827  26.55539  -10.91450 1.000 14.43323 ? 96  GLY A C     1 
ATOM   763  O  O     . GLY A 1 96  ? 23.42228  26.50240  -10.61152 1.000 14.39584 ? 96  GLY A O     1 
ATOM   764  N  N     . VAL A 1 97  ? 21.66726  25.72535  -11.79446 1.000 13.13986 ? 97  VAL A N     1 
ATOM   765  C  CA    . VAL A 1 97  ? 22.41026  24.60534  -12.35444 1.000 12.59173 ? 97  VAL A CA    1 
ATOM   766  C  C     . VAL A 1 97  ? 23.42223  25.10532  -13.37648 1.000 9.64217  ? 97  VAL A C     1 
ATOM   767  O  O     . VAL A 1 97  ? 23.12021  25.96629  -14.21450 1.000 9.42929  ? 97  VAL A O     1 
ATOM   768  C  CB    . VAL A 1 97  ? 21.44325  23.58632  -12.98139 1.000 10.98145 ? 97  VAL A CB    1 
ATOM   769  C  CG1   . VAL A 1 97  ? 22.18125  22.31131  -13.36137 1.000 9.67446  ? 97  VAL A CG1   1 
ATOM   770  C  CG2   . VAL A 1 97  ? 20.30327  23.28934  -12.02436 1.000 11.03474 ? 97  VAL A CG2   1 
ATOM   771  N  N     . THR A 1 98  ? 24.63924  24.56533  -13.30449 1.000 10.02197 ? 98  THR A N     1 
ATOM   772  C  CA    . THR A 1 98  ? 25.68621  24.86731  -14.26552 1.000 9.21793  ? 98  THR A CA    1 
ATOM   773  C  C     . THR A 1 98  ? 26.14821  23.65329  -15.05650 1.000 11.34181 ? 98  THR A C     1 
ATOM   774  O  O     . THR A 1 98  ? 26.93618  23.81627  -15.99552 1.000 12.41494 ? 98  THR A O     1 
ATOM   775  C  CB    . THR A 1 98  ? 26.90422  25.48934  -13.56257 1.000 11.36073 ? 98  THR A CB    1 
ATOM   776  O  OG1   . THR A 1 98  ? 27.44625  24.55237  -12.62255 1.000 11.68161 ? 98  THR A OG1   1 
ATOM   777  C  CG2   . THR A 1 98  ? 26.50923  26.76336  -12.83260 1.000 14.17475 ? 98  THR A CG2   1 
ATOM   778  N  N     . GLN A 1 99  ? 25.68722  22.45230  -14.71245 1.000 11.05035 ? 99  GLN A N     1 
ATOM   779  C  CA    . GLN A 1 99  ? 26.12422  21.23928  -15.39142 1.000 10.92888 ? 99  GLN A CA    1 
ATOM   780  C  C     . GLN A 1 99  ? 25.04523  20.17528  -15.26437 1.000 9.82510  ? 99  GLN A C     1 
ATOM   781  O  O     . GLN A 1 99  ? 24.55725  19.91231  -14.16135 1.000 10.28101 ? 99  GLN A O     1 
ATOM   782  C  CB    . GLN A 1 99  ? 27.44423  20.72431  -14.80743 1.000 10.22015 ? 99  GLN A CB    1 
ATOM   783  C  CG    . GLN A 1 99  ? 27.97923  19.47729  -15.49541 1.000 12.70264 ? 99  GLN A CG    1 
ATOM   784  C  CD    . GLN A 1 99  ? 29.13025  18.84032  -14.74041 1.000 14.27105 ? 99  GLN A CD    1 
ATOM   785  O  OE1   . GLN A 1 99  ? 28.93528  18.22535  -13.69239 1.000 11.23248 ? 99  GLN A OE1   1 
ATOM   786  N  NE2   . GLN A 1 99  ? 30.33924  18.98332  -15.27244 1.000 13.35166 ? 99  GLN A NE2   1 
ATOM   787  N  N     . LEU A 1 100 ? 24.68121  19.56924  -16.39034 1.000 9.00870  ? 100 LEU A N     1 
ATOM   788  C  CA    . LEU A 1 100 ? 23.73522  18.46223  -16.42929 1.000 10.13731 ? 100 LEU A CA    1 
ATOM   789  C  C     . LEU A 1 100 ? 24.45122  17.22422  -16.94426 1.000 9.77166  ? 100 LEU A C     1 
ATOM   790  O  O     . LEU A 1 100 ? 25.10419  17.27219  -17.99228 1.000 10.40291 ? 100 LEU A O     1 
ATOM   791  C  CB    . LEU A 1 100 ? 22.52920  18.79019  -17.31527 1.000 9.00507  ? 100 LEU A CB    1 
ATOM   792  C  CG    . LEU A 1 100 ? 21.53520  17.65218  -17.55122 1.000 8.33607  ? 100 LEU A CG    1 
ATOM   793  C  CD1   . LEU A 1 100 ? 20.97223  17.14321  -16.23419 1.000 7.56654  ? 100 LEU A CD1   1 
ATOM   794  C  CD2   . LEU A 1 100 ? 20.41718  18.09914  -18.47821 1.000 8.76947  ? 100 LEU A CD2   1 
ATOM   795  N  N     . CYS A 1 101 ? 24.33324  16.12224  -16.20623 1.000 7.48575  ? 101 CYS A N     1 
ATOM   796  C  CA    . CYS A 1 101 ? 25.01024  14.87824  -16.54621 1.000 8.39151  ? 101 CYS A CA    1 
ATOM   797  C  C     . CYS A 1 101 ? 24.00625  13.73723  -16.54515 1.000 8.04285  ? 101 CYS A C     1 
ATOM   798  O  O     . CYS A 1 101 ? 23.19727  13.61925  -15.61913 1.000 8.69654  ? 101 CYS A O     1 
ATOM   799  C  CB    . CYS A 1 101 ? 26.14627  14.57828  -15.56022 1.000 10.03076 ? 101 CYS A CB    1 
ATOM   800  S  SG    . CYS A 1 101 ? 27.40426  15.87229  -15.43929 1.000 15.20743 ? 101 CYS A SG    1 
ATOM   801  N  N     . PHE A 1 102 ? 24.06024  12.90420  -17.58013 1.000 9.08713  ? 102 PHE A N     1 
ATOM   802  C  CA    . PHE A 1 102 ? 23.23225  11.70819  -17.64007 1.000 7.92835  ? 102 PHE A CA    1 
ATOM   803  C  C     . PHE A 1 102 ? 23.87323  10.71317  -18.59505 1.000 7.83291  ? 102 PHE A C     1 
ATOM   804  O  O     . PHE A 1 102 ? 24.60421  11.09214  -19.51308 1.000 7.82544  ? 102 PHE A O     1 
ATOM   805  C  CB    . PHE A 1 102 ? 21.79223  12.02717  -18.06805 1.000 8.35687  ? 102 PHE A CB    1 
ATOM   806  C  CG    . PHE A 1 102 ? 21.69120  12.86513  -19.31007 1.000 7.54730  ? 102 PHE A CG    1 
ATOM   807  C  CD1   . PHE A 1 102 ? 21.64418  12.27409  -20.56205 1.000 9.09378  ? 102 PHE A CD1   1 
ATOM   808  C  CD2   . PHE A 1 102 ? 21.61819  14.24613  -19.22511 1.000 9.32699  ? 102 PHE A CD2   1 
ATOM   809  C  CE1   . PHE A 1 102 ? 21.53915  13.04305  -21.70408 1.000 10.15286 ? 102 PHE A CE1   1 
ATOM   810  C  CE2   . PHE A 1 102 ? 21.51516  15.02109  -20.36514 1.000 9.52756  ? 102 PHE A CE2   1 
ATOM   811  C  CZ    . PHE A 1 102 ? 21.47514  14.41906  -21.60712 1.000 11.91431 ? 102 PHE A CZ    1 
ATOM   812  N  N     . GLU A 1 103 ? 23.59025  9.43417   -18.35801 1.000 6.73799  ? 103 GLU A N     1 
ATOM   813  C  CA    . GLU A 1 103 ? 24.16724  8.36915   -19.16399 1.000 7.97839  ? 103 GLU A CA    1 
ATOM   814  C  C     . GLU A 1 103 ? 23.64421  8.43310   -20.59498 1.000 7.87555  ? 103 GLU A C     1 
ATOM   815  O  O     . GLU A 1 103 ? 22.46420  8.70709   -20.82996 1.000 10.47667 ? 103 GLU A O     1 
ATOM   816  C  CB    . GLU A 1 103 ? 23.84226  7.01117   -18.54294 1.000 6.97789  ? 103 GLU A CB    1 
ATOM   817  C  CG    . GLU A 1 103 ? 24.58026  5.83615   -19.15792 1.000 6.21920  ? 103 GLU A CG    1 
ATOM   818  C  CD    . GLU A 1 103 ? 24.22528  4.52317   -18.48887 1.000 7.20080  ? 103 GLU A CD    1 
ATOM   819  O  OE1   . GLU A 1 103 ? 23.02029  4.20816   -18.39784 1.000 6.14129  ? 103 GLU A OE1   1 
ATOM   820  O  OE2   . GLU A 1 103 ? 25.14730  3.81319   -18.04087 1.000 8.97736  ? 103 GLU A OE2   1 
ATOM   821  N  N     . HIS A 1 104 ? 24.53219  8.18208   -21.55299 1.000 7.74696  ? 104 HIS A N     1 
ATOM   822  C  CA    . HIS A 1 104 ? 24.14416  8.22404   -22.95599 1.000 9.53267  ? 104 HIS A CA    1 
ATOM   823  C  C     . HIS A 1 104 ? 23.19816  7.07602   -23.28693 1.000 10.87868 ? 104 HIS A C     1 
ATOM   824  O  O     . HIS A 1 104 ? 23.40918  5.93303   -22.86990 1.000 8.72700  ? 104 HIS A O     1 
ATOM   825  C  CB    . HIS A 1 104 ? 25.37714  8.16002   -23.85601 1.000 11.03811 ? 104 HIS A CB    1 
ATOM   826  C  CG    . HIS A 1 104 ? 25.05711  8.19797   -25.31800 1.000 10.91490 ? 104 HIS A CG    1 
ATOM   827  N  ND1   . HIS A 1 104 ? 24.70309  9.35895   -25.97303 1.000 13.89400 ? 104 HIS A ND1   1 
ATOM   828  C  CD2   . HIS A 1 104 ? 25.03210  7.21794   -26.25097 1.000 10.30250 ? 104 HIS A CD2   1 
ATOM   829  C  CE1   . HIS A 1 104 ? 24.47606  9.09091   -27.24702 1.000 13.96710 ? 104 HIS A CE1   1 
ATOM   830  N  NE2   . HIS A 1 104 ? 24.66807  7.79890   -27.44098 1.000 14.55184 ? 104 HIS A NE2   1 
ATOM   831  N  N     . ASP A 1 105 ? 22.14814  7.38799   -24.04292 1.000 12.82995 ? 105 ASP A N     1 
ATOM   832  C  CA    . ASP A 1 105 ? 21.15514  6.40897   -24.45587 1.000 12.32871 ? 105 ASP A CA    1 
ATOM   833  C  C     . ASP A 1 105 ? 20.97811  6.48692   -25.96387 1.000 12.28284 ? 105 ASP A C     1 
ATOM   834  O  O     . ASP A 1 105 ? 21.04909  7.57090   -26.54890 1.000 15.16004 ? 105 ASP A O     1 
ATOM   835  C  CB    . ASP A 1 105 ? 19.81516  6.64298   -23.74685 1.000 13.50897 ? 105 ASP A CB    1 
ATOM   836  C  CG    . ASP A 1 105 ? 18.89516  5.44097   -23.82579 1.000 14.79152 ? 105 ASP A CG    1 
ATOM   837  O  OD1   . ASP A 1 105 ? 19.32716  4.39596   -24.35677 1.000 16.65339 ? 105 ASP A OD1   1 
ATOM   838  O  OD2   . ASP A 1 105 ? 17.74317  5.53997   -23.35377 1.000 13.00906 ? 105 ASP A OD2   1 
ATOM   839  N  N     . THR A 1 106 ? 20.74911  5.33190   -26.59083 1.000 15.28444 ? 106 THR A N     1 
ATOM   840  C  CA    . THR A 1 106 ? 20.63508  5.24985   -28.04182 1.000 16.65102 ? 106 THR A CA    1 
ATOM   841  C  C     . THR A 1 106 ? 19.26107  4.78283   -28.50678 1.000 14.57511 ? 106 THR A C     1 
ATOM   842  O  O     . THR A 1 106 ? 19.10205  4.44279   -29.68576 1.000 14.91636 ? 106 THR A O     1 
ATOM   843  C  CB    . THR A 1 106 ? 21.71507  4.32485   -28.61382 1.000 15.30450 ? 106 THR A CB    1 
ATOM   844  O  OG1   . THR A 1 106 ? 21.64109  3.04386   -27.97578 1.000 15.59912 ? 106 THR A OG1   1 
ATOM   845  C  CG2   . THR A 1 106 ? 23.09707  4.91886   -28.38986 1.000 14.71622 ? 106 THR A CG2   1 
ATOM   846  N  N     . GLU A 1 107 ? 18.26809  4.75285   -27.62376 1.000 16.59477 ? 107 GLU A N     1 
ATOM   847  C  CA    . GLU A 1 107 ? 16.92708  4.37482   -28.03572 1.000 17.97393 ? 107 GLU A CA    1 
ATOM   848  C  C     . GLU A 1 107 ? 16.30106  5.48679   -28.87774 1.000 19.47892 ? 107 GLU A C     1 
ATOM   849  O  O     . GLU A 1 107 ? 16.67105  6.65680   -28.74678 1.000 17.82378 ? 107 GLU A O     1 
ATOM   850  C  CB    . GLU A 1 107 ? 16.05411  4.07885   -26.81769 1.000 16.61827 ? 107 GLU A CB    1 
ATOM   851  C  CG    . GLU A 1 107 ? 16.50814  2.86588   -26.01666 1.000 16.09572 ? 107 GLU A CG    1 
ATOM   852  C  CD    . GLU A 1 107 ? 15.40816  2.29390   -25.14462 1.000 16.12597 ? 107 GLU A CD    1 
ATOM   853  O  OE1   . GLU A 1 107 ? 14.28116  2.82789   -25.17661 1.000 17.26917 ? 107 GLU A OE1   1 
ATOM   854  O  OE2   . GLU A 1 107 ? 15.67018  1.30492   -24.42760 1.000 17.43802 ? 107 GLU A OE2   1 
ATOM   855  N  N     . PRO A 1 108 ? 15.36104  5.14176   -29.76571 1.000 20.78081 ? 108 PRO A N     1 
ATOM   856  C  CA    . PRO A 1 108 ? 14.76701  6.17873   -30.63272 1.000 18.50009 ? 108 PRO A CA    1 
ATOM   857  C  C     . PRO A 1 108 ? 14.08702  7.29975   -29.86474 1.000 20.19371 ? 108 PRO A C     1 
ATOM   858  O  O     . PRO A 1 108 ? 14.29000  8.47774   -30.18678 1.000 22.56070 ? 108 PRO A O     1 
ATOM   859  C  CB    . PRO A 1 108 ? 13.77500  5.37970   -31.49068 1.000 23.82675 ? 108 PRO A CB    1 
ATOM   860  C  CG    . PRO A 1 108 ? 14.32101  3.99070   -31.50065 1.000 24.62966 ? 108 PRO A CG    1 
ATOM   861  C  CD    . PRO A 1 108 ? 14.91604  3.78775   -30.13766 1.000 17.61067 ? 108 PRO A CD    1 
ATOM   862  N  N     . TYR A 1 109 ? 13.27504  6.96977   -28.85772 1.000 21.42129 ? 109 TYR A N     1 
ATOM   863  C  CA    . TYR A 1 109 ? 12.64405  8.01279   -28.05874 1.000 21.09291 ? 109 TYR A CA    1 
ATOM   864  C  C     . TYR A 1 109 ? 13.66706  8.78882   -27.23978 1.000 20.01704 ? 109 TYR A C     1 
ATOM   865  O  O     . TYR A 1 109 ? 13.45906  9.97283   -26.95181 1.000 20.22083 ? 109 TYR A O     1 
ATOM   866  C  CB    . TYR A 1 109 ? 11.57908  7.40881   -27.14069 1.000 24.36917 ? 109 TYR A CB    1 
ATOM   867  C  CG    . TYR A 1 109 ? 11.07309  8.36784   -26.08471 1.000 23.46335 ? 109 TYR A CG    1 
ATOM   868  C  CD1   . TYR A 1 109 ? 10.19208  9.39082   -26.41173 1.000 25.11630 ? 109 TYR A CD1   1 
ATOM   869  C  CD2   . TYR A 1 109 ? 11.47712  8.25188   -24.76172 1.000 24.32003 ? 109 TYR A CD2   1 
ATOM   870  C  CE1   . TYR A 1 109 ? 9.73009   10.27185  -25.45074 1.000 27.81381 ? 109 TYR A CE1   1 
ATOM   871  C  CE2   . TYR A 1 109 ? 11.02114  9.12691   -23.79373 1.000 26.54226 ? 109 TYR A CE2   1 
ATOM   872  C  CZ    . TYR A 1 109 ? 10.14812  10.13489  -24.14375 1.000 27.68600 ? 109 TYR A CZ    1 
ATOM   873  O  OH    . TYR A 1 109 ? 9.69113   11.00791  -23.18276 1.000 34.50176 ? 109 TYR A OH    1 
ATOM   874  N  N     . ALA A 1 110 ? 14.77508  8.14484   -26.86278 1.000 18.15390 ? 110 ALA A N     1 
ATOM   875  C  CA    . ALA A 1 110 ? 15.77909  8.81488   -26.04483 1.000 17.14610 ? 110 ALA A CA    1 
ATOM   876  C  C     . ALA A 1 110 ? 16.48206  9.92286   -26.81887 1.000 16.31661 ? 110 ALA A C     1 
ATOM   877  O  O     . ALA A 1 110 ? 16.70707  11.01288  -26.28291 1.000 17.86357 ? 110 ALA A O     1 
ATOM   878  C  CB    . ALA A 1 110 ? 16.79411  7.79890   -25.52482 1.000 17.20831 ? 110 ALA A CB    1 
ATOM   879  N  N     . LYS A 1 111 ? 16.83104  9.66482   -28.08187 1.000 16.11677 ? 111 LYS A N     1 
ATOM   880  C  CA    . LYS A 1 111 ? 17.55802  10.65980  -28.86592 1.000 19.78190 ? 111 LYS A CA    1 
ATOM   881  C  C     . LYS A 1 111 ? 16.72400  11.91679  -29.07894 1.000 19.34735 ? 111 LYS A C     1 
ATOM   882  O  O     . LYS A 1 111 ? 17.23599  13.03680  -28.96198 1.000 18.68692 ? 111 LYS A O     1 
ATOM   883  C  CB    . LYS A 1 111 ? 17.98299  10.05977  -30.20491 1.000 19.15481 ? 111 LYS A CB    1 
ATOM   884  C  CG    . LYS A 1 111 ? 18.90400  8.85778   -30.07189 1.000 22.76071 ? 111 LYS A CG    1 
ATOM   885  C  CD    . LYS A 1 111 ? 19.27798  8.29274   -31.42988 1.000 27.65018 ? 111 LYS A CD    1 
ATOM   886  C  CE    . LYS A 1 111 ? 20.21099  7.10275   -31.29087 1.000 19.99188 ? 111 LYS A CE    1 
ATOM   887  N  NZ    . LYS A 1 111 ? 20.56397  6.51971   -32.61286 1.000 24.78592 ? 111 LYS A NZ    1 
ATOM   888  N  N     . VAL A 1 112 ? 15.43700  11.75477  -29.39191 1.000 16.64350 ? 112 VAL A N     1 
ATOM   889  C  CA    . VAL A 1 112 ? 14.55998  12.91176  -29.54192 1.000 17.42609 ? 112 VAL A CA    1 
ATOM   890  C  C     . VAL A 1 112 ? 14.38001  13.61880  -28.20394 1.000 15.58210 ? 112 VAL A C     1 
ATOM   891  O  O     . VAL A 1 112 ? 14.33400  14.85380  -28.13898 1.000 15.92985 ? 112 VAL A O     1 
ATOM   892  C  CB    . VAL A 1 112 ? 13.20997  12.48173  -30.14388 1.000 18.06594 ? 112 VAL A CB    1 
ATOM   893  C  CG1   . VAL A 1 112 ? 12.30996  13.68872  -30.35590 1.000 20.95134 ? 112 VAL A CG1   1 
ATOM   894  C  CG2   . VAL A 1 112 ? 13.42895  11.73469  -31.45086 1.000 22.86624 ? 112 VAL A CG2   1 
ATOM   895  N  N     . ARG A 1 113 ? 14.28093  12.85029  -27.11769 1.000 18.09221 ? 113 ARG A N     1 
ATOM   896  C  CA    . ARG A 1 113 ? 14.14402  13.44454  -25.79194 1.000 18.49397 ? 113 ARG A CA    1 
ATOM   897  C  C     . ARG A 1 113 ? 15.42585  14.15309  -25.37189 1.000 17.11517 ? 113 ARG A C     1 
ATOM   898  O  O     . ARG A 1 113 ? 15.38924  15.29175  -24.89115 1.000 18.24765 ? 113 ARG A O     1 
ATOM   899  C  CB    . ARG A 1 113 ? 13.76835  12.36702  -24.77461 1.000 18.01276 ? 113 ARG A CB    1 
ATOM   900  C  CG    . ARG A 1 113 ? 13.78915  12.83507  -23.32958 1.000 18.83049 ? 113 ARG A CG    1 
ATOM   901  C  CD    . ARG A 1 113 ? 13.84941  11.64979  -22.38109 1.000 15.76910 ? 113 ARG A CD    1 
ATOM   902  N  NE    . ARG A 1 113 ? 15.04421  10.84462  -22.60659 1.000 16.03197 ? 113 ARG A NE    1 
ATOM   903  C  CZ    . ARG A 1 113 ? 15.30793  9.70123   -21.98891 1.000 17.12481 ? 113 ARG A CZ    1 
ATOM   904  N  NH1   . ARG A 1 113 ? 14.47578  9.18907   -21.09704 1.000 16.76599 ? 113 ARG A NH1   1 
ATOM   905  N  NH2   . ARG A 1 113 ? 16.43475  9.05466   -22.27429 1.000 13.53492 ? 113 ARG A NH2   1 
ATOM   906  N  N     . ASP A 1 114 ? 16.57306  13.49190  -25.54598 1.000 15.82439 ? 114 ASP A N     1 
ATOM   907  C  CA    . ASP A 1 114 ? 17.83807  14.08292  -25.12103 1.000 17.40041 ? 114 ASP A CA    1 
ATOM   908  C  C     . ASP A 1 114 ? 18.21104  15.29390  -25.96607 1.000 18.14179 ? 114 ASP A C     1 
ATOM   909  O  O     . ASP A 1 114 ? 18.85904  16.21892  -25.46412 1.000 17.80779 ? 114 ASP A O     1 
ATOM   910  C  CB    . ASP A 1 114 ? 18.95008  13.03593  -25.16902 1.000 16.05292 ? 114 ASP A CB    1 
ATOM   911  C  CG    . ASP A 1 114 ? 18.72310  11.89796  -24.18898 1.000 15.56916 ? 114 ASP A CG    1 
ATOM   912  O  OD1   . ASP A 1 114 ? 17.71612  11.93897  -23.45296 1.000 16.41920 ? 114 ASP A OD1   1 
ATOM   913  O  OD2   . ASP A 1 114 ? 19.55011  10.96196  -24.15797 1.000 12.82895 ? 114 ASP A OD2   1 
ATOM   914  N  N     . ALA A 1 115 ? 17.81301  15.31086  -27.24007 1.000 18.06083 ? 115 ALA A N     1 
ATOM   915  C  CA    . ALA A 1 115 ? 18.11399  16.45983  -28.08811 1.000 17.45076 ? 115 ALA A CA    1 
ATOM   916  C  C     . ALA A 1 115 ? 17.37899  17.70684  -27.61313 1.000 19.94204 ? 115 ALA A C     1 
ATOM   917  O  O     . ALA A 1 115 ? 17.94298  18.80685  -27.62017 1.000 24.71428 ? 115 ALA A O     1 
ATOM   918  C  CB    . ALA A 1 115 ? 17.76196  16.14979  -29.54209 1.000 18.69347 ? 115 ALA A CB    1 
ATOM   919  N  N     . ALA A 1 116 ? 16.12000  17.55584  -27.19510 1.000 16.66719 ? 116 ALA A N     1 
ATOM   920  C  CA    . ALA A 1 116 ? 15.35500  18.70785  -26.73412 1.000 19.07229 ? 116 ALA A CA    1 
ATOM   921  C  C     . ALA A 1 116 ? 15.88902  19.24890  -25.41514 1.000 15.95048 ? 116 ALA A C     1 
ATOM   922  O  O     . ALA A 1 116 ? 15.84802  20.46290  -25.18518 1.000 16.40560 ? 116 ALA A O     1 
ATOM   923  C  CB    . ALA A 1 116 ? 13.87900  18.33884  -26.59607 1.000 20.89950 ? 116 ALA A CB    1 
ATOM   924  N  N     . VAL A 1 117 ? 16.40305  18.37593  -24.54613 1.000 15.08175 ? 117 VAL A N     1 
ATOM   925  C  CA    . VAL A 1 117 ? 16.89807  18.82297  -23.24715 1.000 16.70198 ? 117 VAL A CA    1 
ATOM   926  C  C     . VAL A 1 117 ? 18.21506  19.57598  -23.40220 1.000 16.76629 ? 117 VAL A C     1 
ATOM   927  O  O     . VAL A 1 117 ? 18.45807  20.57400  -22.71224 1.000 16.42080 ? 117 VAL A O     1 
ATOM   928  C  CB    . VAL A 1 117 ? 17.02910  17.62600  -22.28712 1.000 17.71158 ? 117 VAL A CB    1 
ATOM   929  C  CG1   . VAL A 1 117 ? 17.59812  18.07104  -20.94914 1.000 17.82974 ? 117 VAL A CG1   1 
ATOM   930  C  CG2   . VAL A 1 117 ? 15.67811  16.95499  -22.09407 1.000 18.19322 ? 117 VAL A CG2   1 
ATOM   931  N  N     . ARG A 1 118 ? 19.08522  19.11320  -24.30603 1.000 15.42809 ? 118 ARG A N     1 
ATOM   932  C  CA    . ARG A 1 118 ? 20.32462  19.83689  -24.57750 1.000 18.53922 ? 118 ARG A CA    1 
ATOM   933  C  C     . ARG A 1 118 ? 20.03792  21.23438  -25.11121 1.000 17.74260 ? 118 ARG A C     1 
ATOM   934  O  O     . ARG A 1 118 ? 20.77683  22.18300  -24.82231 1.000 21.49168 ? 118 ARG A O     1 
ATOM   935  C  CB    . ARG A 1 118 ? 21.18809  19.05860  -25.57059 1.000 19.39584 ? 118 ARG A CB    1 
ATOM   936  C  CG    . ARG A 1 118 ? 21.69393  17.71978  -25.06381 1.000 19.47140 ? 118 ARG A CG    1 
ATOM   937  C  CD    . ARG A 1 118 ? 22.64295  17.08682  -26.07037 1.000 21.62340 ? 118 ARG A CD    1 
ATOM   938  N  NE    . ARG A 1 118 ? 23.11383  15.77637  -25.63826 1.000 24.21168 ? 118 ARG A NE    1 
ATOM   939  C  CZ    . ARG A 1 118 ? 22.55694  14.62610  -25.99206 1.000 24.99595 ? 118 ARG A CZ    1 
ATOM   940  N  NH1   . ARG A 1 118 ? 21.50166  14.58520  -26.78919 1.000 28.05174 ? 118 ARG A NH1   1 
ATOM   941  N  NH2   . ARG A 1 118 ? 23.07267  13.48807  -25.53602 1.000 22.97789 ? 118 ARG A NH2   1 
ATOM   942  N  N     . ARG A 1 119 ? 18.97148  21.37564  -25.90029 1.000 20.81523 ? 119 ARG A N     1 
ATOM   943  C  CA    . ARG A 1 119 ? 18.56157  22.69116  -26.38038 1.000 17.48058 ? 119 ARG A CA    1 
ATOM   944  C  C     . ARG A 1 119 ? 18.15722  23.59048  -25.21941 1.000 18.49158 ? 119 ARG A C     1 
ATOM   945  O  O     . ARG A 1 119 ? 18.55709  24.75860  -25.14980 1.000 19.39620 ? 119 ARG A O     1 
ATOM   946  C  CB    . ARG A 1 119 ? 17.40875  22.53570  -27.37200 1.000 23.24227 ? 119 ARG A CB    1 
ATOM   947  C  CG    . ARG A 1 119 ? 16.89868  23.83035  -27.97051 0.000 21.80906 ? 119 ARG A CG    1 
ATOM   948  C  CD    . ARG A 1 119 ? 15.54985  23.60829  -28.63457 0.000 23.31474 ? 119 ARG A CD    1 
ATOM   949  N  NE    . ARG A 1 119 ? 15.50393  22.34579  -29.36253 0.000 24.72785 ? 119 ARG A NE    1 
ATOM   950  C  CZ    . ARG A 1 119 ? 15.88751  22.19075  -30.62222 0.000 26.41875 ? 119 ARG A CZ    1 
ATOM   951  N  NH1   . ARG A 1 119 ? 16.35581  23.20407  -31.33204 0.000 26.81722 ? 119 ARG A NH1   1 
ATOM   952  N  NH2   . ARG A 1 119 ? 15.79981  20.98823  -31.18356 0.000 27.16069 ? 119 ARG A NH2   1 
ATOM   953  N  N     . LEU A 1 120 ? 17.36001  23.05394  -24.29329 1.000 20.02740 ? 120 LEU A N     1 
ATOM   954  C  CA    . LEU A 1 120 ? 16.93403  23.81597  -23.12530 1.000 16.96394 ? 120 LEU A CA    1 
ATOM   955  C  C     . LEU A 1 120 ? 18.10105  24.11701  -22.19534 1.000 13.73373 ? 120 LEU A C     1 
ATOM   956  O  O     . LEU A 1 120 ? 18.12606  25.17703  -21.55937 1.000 14.07017 ? 120 LEU A O     1 
ATOM   957  C  CB    . LEU A 1 120 ? 15.84106  23.05399  -22.37726 1.000 15.88476 ? 120 LEU A CB    1 
ATOM   958  C  CG    . LEU A 1 120 ? 14.58304  22.73695  -23.18622 1.000 15.34887 ? 120 LEU A CG    1 
ATOM   959  C  CD1   . LEU A 1 120 ? 13.72806  21.70497  -22.47017 1.000 13.87029 ? 120 LEU A CD1   1 
ATOM   960  C  CD2   . LEU A 1 120 ? 13.78503  24.00494  -23.45424 1.000 19.73163 ? 120 LEU A CD2   1 
ATOM   961  N  N     . ALA A 1 121 ? 19.07406  23.20702  -22.10633 1.000 14.41843 ? 121 ALA A N     1 
ATOM   962  C  CA    . ALA A 1 121 ? 20.23908  23.45206  -21.26336 1.000 15.94223 ? 121 ALA A CA    1 
ATOM   963  C  C     . ALA A 1 121 ? 21.16705  24.49104  -21.87741 1.000 15.67206 ? 121 ALA A C     1 
ATOM   964  O  O     . ALA A 1 121 ? 21.79606  25.26607  -21.14745 1.000 13.48438 ? 121 ALA A O     1 
ATOM   965  C  CB    . ALA A 1 121 ? 20.99209  22.14607  -21.01634 1.000 13.63450 ? 121 ALA A CB    1 
ATOM   966  N  N     . ALA A 1 122 ? 21.26703  24.52401  -23.20842 1.000 18.26337 ? 122 ALA A N     1 
ATOM   967  C  CA    . ALA A 1 122 ? 22.10800  25.52199  -23.86147 1.000 16.44082 ? 122 ALA A CA    1 
ATOM   968  C  C     . ALA A 1 122 ? 21.52900  26.92199  -23.69850 1.000 17.60840 ? 122 ALA A C     1 
ATOM   969  O  O     . ALA A 1 122 ? 22.27499  27.89000  -23.50754 1.000 17.98835 ? 122 ALA A O     1 
ATOM   970  C  CB    . ALA A 1 122 ? 22.27998  25.17995  -25.34046 1.000 14.40441 ? 122 ALA A CB    1 
ATOM   971  N  N     . GLU A 1 123 ? 20.20199  27.05098  -23.77347 1.000 15.64278 ? 123 GLU A N     1 
ATOM   972  C  CA    . GLU A 1 123 ? 19.56499  28.34498  -23.56550 1.000 17.84929 ? 123 GLU A CA    1 
ATOM   973  C  C     . GLU A 1 123 ? 19.67002  28.81103  -22.12051 1.000 16.28612 ? 123 GLU A C     1 
ATOM   974  O  O     . GLU A 1 123 ? 19.52501  30.01003  -21.85755 1.000 17.78584 ? 123 GLU A O     1 
ATOM   975  C  CB    . GLU A 1 123 ? 18.09598  28.28096  -23.98946 1.000 19.69755 ? 123 GLU A CB    1 
ATOM   976  C  CG    . GLU A 1 123 ? 17.88895  27.97591  -25.46445 1.000 18.88828 ? 123 GLU A CG    1 
ATOM   977  C  CD    . GLU A 1 123 ? 16.42895  27.76489  -25.81741 1.000 18.70909 ? 123 GLU A CD    1 
ATOM   978  O  OE1   . GLU A 1 123 ? 15.58696  27.76991  -24.89640 1.000 19.72691 ? 123 GLU A OE1   1 
ATOM   979  O  OE2   . GLU A 1 123 ? 16.12492  27.59385  -27.01740 1.000 18.34582 ? 123 GLU A OE2   1 
ATOM   980  N  N     . ALA A 1 124 ? 19.91504  27.89806  -21.18249 1.000 15.45625 ? 124 ALA A N     1 
ATOM   981  C  CA    . ALA A 1 124 ? 20.08807  28.23610  -19.77751 1.000 16.42678 ? 124 ALA A CA    1 
ATOM   982  C  C     . ALA A 1 124 ? 21.55108  28.30012  -19.36154 1.000 14.05732 ? 124 ALA A C     1 
ATOM   983  O  O     . ALA A 1 124 ? 21.83610  28.57516  -18.19155 1.000 15.42025 ? 124 ALA A O     1 
ATOM   984  C  CB    . ALA A 1 124 ? 19.34510  27.22712  -18.89646 1.000 16.17836 ? 124 ALA A CB    1 
ATOM   985  N  N     . GLY A 1 125 ? 22.47906  28.05210  -20.28255 1.000 16.61296 ? 125 GLY A N     1 
ATOM   986  C  CA    . GLY A 1 125 ? 23.89107  28.08812  -19.95158 1.000 15.44843 ? 125 GLY A CA    1 
ATOM   987  C  C     . GLY A 1 125 ? 24.37809  26.89715  -19.16056 1.000 14.73646 ? 125 GLY A C     1 
ATOM   988  O  O     . GLY A 1 125 ? 25.35011  27.01718  -18.40758 1.000 15.89384 ? 125 GLY A O     1 
ATOM   989  N  N     . VAL A 1 126 ? 23.73310  25.74314  -19.31451 1.000 15.97669 ? 126 VAL A N     1 
ATOM   990  C  CA    . VAL A 1 126 ? 24.06712  24.54117  -18.56048 1.000 11.50131 ? 126 VAL A CA    1 
ATOM   991  C  C     . VAL A 1 126 ? 24.93011  23.63815  -19.42847 1.000 12.01055 ? 126 VAL A C     1 
ATOM   992  O  O     . VAL A 1 126 ? 24.57009  23.33211  -20.57245 1.000 12.80011 ? 126 VAL A O     1 
ATOM   993  C  CB    . VAL A 1 126 ? 22.79814  23.80617  -18.09543 1.000 12.31804 ? 126 VAL A CB    1 
ATOM   994  C  CG1   . VAL A 1 126 ? 23.16417  22.52620  -17.35940 1.000 10.42084 ? 126 VAL A CG1   1 
ATOM   995  C  CG2   . VAL A 1 126 ? 21.95615  24.71119  -17.21244 1.000 11.79962 ? 126 VAL A CG2   1 
ATOM   996  N  N     . GLU A 1 127 ? 26.07113  23.21717  -18.88948 1.000 10.70489 ? 127 GLU A N     1 
ATOM   997  C  CA    . GLU A 1 127 ? 26.93512  22.27916  -19.59047 1.000 11.93535 ? 127 GLU A CA    1 
ATOM   998  C  C     . GLU A 1 127 ? 26.33713  20.87916  -19.54942 1.000 13.09093 ? 127 GLU A C     1 
ATOM   999  O  O     . GLU A 1 127 ? 25.80316  20.44418  -18.52539 1.000 11.69925 ? 127 GLU A O     1 
ATOM   1000 C  CB    . GLU A 1 127 ? 28.33013  22.27619  -18.96350 1.000 14.65254 ? 127 GLU A CB    1 
ATOM   1001 C  CG    . GLU A 1 127 ? 29.29613  21.27618  -19.58049 1.000 16.79009 ? 127 GLU A CG    1 
ATOM   1002 C  CD    . GLU A 1 127 ? 30.58515  21.14921  -18.79251 1.000 18.20287 ? 127 GLU A CD    1 
ATOM   1003 O  OE1   . GLU A 1 127 ? 30.70816  21.81225  -17.74054 1.000 22.05519 ? 127 GLU A OE1   1 
ATOM   1004 O  OE2   . GLU A 1 127 ? 31.47614  20.38521  -19.22151 1.000 20.13556 ? 127 GLU A OE2   1 
ATOM   1005 N  N     . VAL A 1 128 ? 26.42511  20.17012  -20.67240 1.000 13.92104 ? 128 VAL A N     1 
ATOM   1006 C  CA    . VAL A 1 128 ? 25.87312  18.82711  -20.80834 1.000 12.79735 ? 128 VAL A CA    1 
ATOM   1007 C  C     . VAL A 1 128 ? 27.02713  17.85112  -20.99234 1.000 11.55073 ? 128 VAL A C     1 
ATOM   1008 O  O     . VAL A 1 128 ? 27.82510  17.99010  -21.92736 1.000 13.10469 ? 128 VAL A O     1 
ATOM   1009 C  CB    . VAL A 1 128 ? 24.88110  18.73807  -21.97832 1.000 13.00082 ? 128 VAL A CB    1 
ATOM   1010 C  CG1   . VAL A 1 128 ? 24.35011  17.31906  -22.11527 1.000 15.33763 ? 128 VAL A CG1   1 
ATOM   1011 C  CG2   . VAL A 1 128 ? 23.73909  19.72007  -21.77532 1.000 13.33400 ? 128 VAL A CG2   1 
ATOM   1012 N  N     . VAL A 1 129 ? 27.11415  16.86815  -20.10031 1.000 10.18314 ? 129 VAL A N     1 
ATOM   1013 C  CA    . VAL A 1 129 ? 28.12016  15.81415  -20.16430 1.000 11.72558 ? 129 VAL A CA    1 
ATOM   1014 C  C     . VAL A 1 129 ? 27.39017  14.48114  -20.23124 1.000 11.62421 ? 129 VAL A C     1 
ATOM   1015 O  O     . VAL A 1 129 ? 26.65819  14.12217  -19.30022 1.000 10.97998 ? 129 VAL A O     1 
ATOM   1016 C  CB    . VAL A 1 129 ? 29.07418  15.85720  -18.96032 1.000 9.70863  ? 129 VAL A CB    1 
ATOM   1017 C  CG1   . VAL A 1 129 ? 30.09619  14.73420  -19.05431 1.000 16.03007 ? 129 VAL A CG1   1 
ATOM   1018 C  CG2   . VAL A 1 129 ? 29.76418  17.21020  -18.87738 1.000 14.02332 ? 129 VAL A CG2   1 
ATOM   1019 N  N     . THR A 1 130 ? 27.58615  13.74811  -21.33023 1.000 11.19974 ? 130 THR A N     1 
ATOM   1020 C  CA    . THR A 1 130 ? 26.89116  12.48810  -21.58717 1.000 9.48681  ? 130 THR A CA    1 
ATOM   1021 C  C     . THR A 1 130 ? 27.92016  11.38810  -21.82416 1.000 9.59878  ? 130 THR A C     1 
ATOM   1022 O  O     . THR A 1 130 ? 28.25414  11.07407  -22.97516 1.000 9.94380  ? 130 THR A O     1 
ATOM   1023 C  CB    . THR A 1 130 ? 25.94613  12.60806  -22.78216 1.000 9.99898  ? 130 THR A CB    1 
ATOM   1024 O  OG1   . THR A 1 130 ? 26.69710  12.94803  -23.95418 1.000 7.35709  ? 130 THR A OG1   1 
ATOM   1025 C  CG2   . THR A 1 130 ? 24.90213  13.68205  -22.52917 1.000 9.68761  ? 130 THR A CG2   1 
ATOM   1026 N  N     . PRO A 1 131 ? 28.44319  10.78214  -20.76215 1.000 8.53071  ? 131 PRO A N     1 
ATOM   1027 C  CA    . PRO A 1 131 ? 29.36919  9.66114   -20.93414 1.000 9.48439  ? 131 PRO A CA    1 
ATOM   1028 C  C     . PRO A 1 131 ? 28.63219  8.37812   -21.28608 1.000 11.12319 ? 131 PRO A C     1 
ATOM   1029 O  O     . PRO A 1 131 ? 27.42720  8.23312   -21.07105 1.000 10.50623 ? 131 PRO A O     1 
ATOM   1030 C  CB    . PRO A 1 131 ? 30.04522  9.55118   -19.56315 1.000 9.70934  ? 131 PRO A CB    1 
ATOM   1031 C  CG    . PRO A 1 131 ? 29.01224  10.04721  -18.61614 1.000 10.41185 ? 131 PRO A CG    1 
ATOM   1032 C  CD    . PRO A 1 131 ? 28.25721  11.13418  -19.34316 1.000 10.02931 ? 131 PRO A CD    1 
ATOM   1033 N  N     . ILE A 1 132 ? 29.38919  7.43711   -21.83907 1.000 8.09823  ? 132 ILE A N     1 
ATOM   1034 C  CA    . ILE A 1 132 ? 28.85719  6.15109   -22.27102 1.000 9.02443  ? 132 ILE A CA    1 
ATOM   1035 C  C     . ILE A 1 132 ? 29.20322  5.11013   -21.21700 1.000 8.33407  ? 132 ILE A C     1 
ATOM   1036 O  O     . ILE A 1 132 ? 30.38223  4.87515   -20.92502 1.000 7.72285  ? 132 ILE A O     1 
ATOM   1037 C  CB    . ILE A 1 132 ? 29.40516  5.75306   -23.64902 1.000 11.14958 ? 132 ILE A CB    1 
ATOM   1038 C  CG1   . ILE A 1 132 ? 28.95113  6.76702   -24.70204 1.000 10.47974 ? 132 ILE A CG1   1 
ATOM   1039 C  CG2   . ILE A 1 132 ? 28.95517  4.34504   -24.01297 1.000 8.76764  ? 132 ILE A CG2   1 
ATOM   1040 C  CD1   . ILE A 1 132 ? 29.65611  6.63099   -26.02705 1.000 9.93951  ? 132 ILE A CD1   1 
ATOM   1041 N  N     . SER A 1 133 ? 28.17624  4.49214   -20.64396 1.000 7.22318  ? 133 SER A N     1 
ATOM   1042 C  CA    . SER A 1 133 ? 28.38727  3.45517   -19.64293 1.000 7.97769  ? 133 SER A CA    1 
ATOM   1043 C  C     . SER A 1 133 ? 27.29328  2.39716   -19.62788 1.000 6.71773  ? 133 SER A C     1 
ATOM   1044 O  O     . SER A 1 133 ? 27.39730  1.45119   -18.84385 1.000 8.44111  ? 133 SER A O     1 
ATOM   1045 C  CB    . SER A 1 133 ? 28.51829  4.09121   -18.24695 1.000 7.69155  ? 133 SER A CB    1 
ATOM   1046 O  OG    . SER A 1 133 ? 27.40529  4.91421   -17.95395 1.000 6.28170  ? 133 SER A OG    1 
ATOM   1047 N  N     . HIS A 1 134 ? 26.25126  2.51613   -20.45486 1.000 6.47688  ? 134 HIS A N     1 
ATOM   1048 C  CA    . HIS A 1 134 ? 25.21227  1.49312   -20.49780 1.000 6.53899  ? 134 HIS A CA    1 
ATOM   1049 C  C     . HIS A 1 134 ? 25.66326  0.27610   -21.29578 1.000 6.72916  ? 134 HIS A C     1 
ATOM   1050 O  O     . HIS A 1 134 ? 25.33927  -0.86089  -20.93574 1.000 6.81629  ? 134 HIS A O     1 
ATOM   1051 C  CB    . HIS A 1 134 ? 23.92725  2.07409   -21.08979 1.000 6.51063  ? 134 HIS A CB    1 
ATOM   1052 C  CG    . HIS A 1 134 ? 22.80625  1.08608   -21.18474 1.000 6.78047  ? 134 HIS A CG    1 
ATOM   1053 N  ND1   . HIS A 1 134 ? 22.26728  0.46311   -20.07871 1.000 6.57695  ? 134 HIS A ND1   1 
ATOM   1054 C  CD2   . HIS A 1 134 ? 22.12223  0.61404   -22.25271 1.000 6.82580  ? 134 HIS A CD2   1 
ATOM   1055 C  CE1   . HIS A 1 134 ? 21.29928  -0.34991  -20.46267 1.000 6.89502  ? 134 HIS A CE1   1 
ATOM   1056 N  NE2   . HIS A 1 134 ? 21.19125  -0.27695  -21.77767 1.000 6.90816  ? 134 HIS A NE2   1 
ATOM   1057 N  N     . THR A 1 135 ? 26.40223  0.49507   -22.37680 1.000 7.01133  ? 135 THR A N     1 
ATOM   1058 C  CA    . THR A 1 135 ? 26.95522  -0.57895  -23.18678 1.000 7.49172  ? 135 THR A CA    1 
ATOM   1059 C  C     . THR A 1 135 ? 28.44623  -0.73893  -22.90080 1.000 7.19652  ? 135 THR A C     1 
ATOM   1060 O  O     . THR A 1 135 ? 29.07524  0.09710   -22.24884 1.000 7.08255  ? 135 THR A O     1 
ATOM   1061 C  CB    . THR A 1 135 ? 26.71819  -0.30900  -24.67578 1.000 7.30157  ? 135 THR A CB    1 
ATOM   1062 O  OG1   . THR A 1 135 ? 27.29617  0.95200   -25.03383 1.000 7.78264  ? 135 THR A OG1   1 
ATOM   1063 C  CG2   . THR A 1 135 ? 25.22818  -0.28302  -24.98075 1.000 7.31367  ? 135 THR A CG2   1 
ATOM   1064 N  N     . LEU A 1 136 ? 29.00823  -1.84094  -23.40178 1.000 8.03251  ? 136 LEU A N     1 
ATOM   1065 C  CA    . LEU A 1 136 ? 30.42224  -2.12692  -23.16880 1.000 7.61456  ? 136 LEU A CA    1 
ATOM   1066 C  C     . LEU A 1 136 ? 31.31121  -1.09394  -23.85185 1.000 7.68055  ? 136 LEU A C     1 
ATOM   1067 O  O     . LEU A 1 136 ? 32.14922  -0.45291  -23.20789 1.000 7.79643  ? 136 LEU A O     1 
ATOM   1068 C  CB    . LEU A 1 136 ? 30.75924  -3.53693  -23.65677 1.000 7.93612  ? 136 LEU A CB    1 
ATOM   1069 C  CG    . LEU A 1 136 ? 30.26327  -4.69591  -22.79272 1.000 7.98280  ? 136 LEU A CG    1 
ATOM   1070 C  CD1   . LEU A 1 136 ? 30.62226  -6.02493  -23.43569 1.000 9.25818  ? 136 LEU A CD1   1 
ATOM   1071 C  CD2   . LEU A 1 136 ? 30.84929  -4.59986  -21.39374 1.000 7.90456  ? 136 LEU A CD2   1 
ATOM   1072 N  N     . TYR A 1 137 ? 31.14419  -0.91998  -25.15786 1.000 7.82947  ? 137 TYR A N     1 
ATOM   1073 C  CA    . TYR A 1 137 ? 31.93816  0.01401   -25.93890 1.000 7.97018  ? 137 TYR A CA    1 
ATOM   1074 C  C     . TYR A 1 137 ? 31.08214  1.18899   -26.39292 1.000 7.83757  ? 137 TYR A C     1 
ATOM   1075 O  O     . TYR A 1 137 ? 29.86315  1.21598   -26.21289 1.000 7.66241  ? 137 TYR A O     1 
ATOM   1076 C  CB    . TYR A 1 137 ? 32.55214  -0.67403  -27.16389 1.000 8.48421  ? 137 TYR A CB    1 
ATOM   1077 C  CG    . TYR A 1 137 ? 33.39816  -1.88701  -26.85987 1.000 8.57503  ? 137 TYR A CG    1 
ATOM   1078 C  CD1   . TYR A 1 137 ? 32.83017  -3.15301  -26.79182 1.000 10.01299 ? 137 TYR A CD1   1 
ATOM   1079 C  CD2   . TYR A 1 137 ? 34.76716  -1.77099  -26.66191 1.000 8.93358  ? 137 TYR A CD2   1 
ATOM   1080 C  CE1   . TYR A 1 137 ? 33.60018  -4.26800  -26.52281 1.000 9.85798  ? 137 TYR A CE1   1 
ATOM   1081 C  CE2   . TYR A 1 137 ? 35.54617  -2.88098  -26.39389 1.000 9.11937  ? 137 TYR A CE2   1 
ATOM   1082 C  CZ    . TYR A 1 137 ? 34.95719  -4.12598  -26.32484 1.000 9.89889  ? 137 TYR A CZ    1 
ATOM   1083 O  OH    . TYR A 1 137 ? 35.72620  -5.23497  -26.05782 1.000 12.77679 ? 137 TYR A OH    1 
ATOM   1084 N  N     . ASP A 1 138 ? 31.75112  2.17197   -26.98796 1.000 8.48946  ? 138 ASP A N     1 
ATOM   1085 C  CA    . ASP A 1 138 ? 31.07210  3.20594   -27.75798 1.000 9.76726  ? 138 ASP A CA    1 
ATOM   1086 C  C     . ASP A 1 138 ? 30.55908  2.57590   -29.04595 1.000 9.84947  ? 138 ASP A C     1 
ATOM   1087 O  O     . ASP A 1 138 ? 31.34206  2.28788   -29.95596 1.000 10.82225 ? 138 ASP A O     1 
ATOM   1088 C  CB    . ASP A 1 138 ? 32.02908  4.35994   -28.04304 1.000 10.81987 ? 138 ASP A CB    1 
ATOM   1089 C  CG    . ASP A 1 138 ? 31.37406  5.49592   -28.81206 1.000 13.83195 ? 138 ASP A CG    1 
ATOM   1090 O  OD1   . ASP A 1 138 ? 30.14005  5.46590   -29.01603 1.000 11.84870 ? 138 ASP A OD1   1 
ATOM   1091 O  OD2   . ASP A 1 138 ? 32.10004  6.42891   -29.21310 1.000 14.87339 ? 138 ASP A OD2   1 
ATOM   1092 N  N     . THR A 1 139 ? 29.24608  2.33789   -29.11591 1.000 8.54979  ? 139 THR A N     1 
ATOM   1093 C  CA    . THR A 1 139 ? 28.68406  1.63985   -30.26888 1.000 11.42411 ? 139 THR A CA    1 
ATOM   1094 C  C     . THR A 1 139 ? 28.89502  2.42081   -31.55991 1.000 10.64708 ? 139 THR A C     1 
ATOM   1095 O  O     . THR A 1 139 ? 28.97901  1.82278   -32.63789 1.000 12.25552 ? 139 THR A O     1 
ATOM   1096 C  CB    . THR A 1 139 ? 27.19506  1.36284   -30.04984 1.000 11.23996 ? 139 THR A CB    1 
ATOM   1097 O  OG1   . THR A 1 139 ? 26.52606  2.57385   -29.67486 1.000 15.41077 ? 139 THR A OG1   1 
ATOM   1098 C  CG2   . THR A 1 139 ? 27.00410  0.32288   -28.95581 1.000 10.59788 ? 139 THR A CG2   1 
ATOM   1099 N  N     . ASP A 1 140 ? 28.98601  3.74982   -31.47495 1.000 12.61757 ? 140 ASP A N     1 
ATOM   1100 C  CA    . ASP A 1 140 ? 29.30498  4.54278   -32.65398 1.000 11.54472 ? 140 ASP A CA    1 
ATOM   1101 C  C     . ASP A 1 140 ? 30.77298  4.42378   -33.04401 1.000 12.70972 ? 140 ASP A C     1 
ATOM   1102 O  O     . ASP A 1 140 ? 31.11295  4.65175   -34.21002 1.000 11.92537 ? 140 ASP A O     1 
ATOM   1103 C  CB    . ASP A 1 140 ? 28.93498  6.00779   -32.41902 1.000 12.74837 ? 140 ASP A CB    1 
ATOM   1104 C  CG    . ASP A 1 140 ? 27.44598  6.20378   -32.21299 1.000 15.88147 ? 140 ASP A CG    1 
ATOM   1105 O  OD1   . ASP A 1 140 ? 26.66398  5.36076   -32.70095 1.000 19.02744 ? 140 ASP A OD1   1 
ATOM   1106 O  OD2   . ASP A 1 140 ? 27.05599  7.19780   -31.56602 1.000 15.21094 ? 140 ASP A OD2   1 
ATOM   1107 N  N     . MET A 1 141 ? 31.64500  4.07082   -32.09802 1.000 12.70448 ? 141 MET A N     1 
ATOM   1108 C  CA    . MET A 1 141 ? 33.04899  3.84882   -32.42504 1.000 12.18294 ? 141 MET A CA    1 
ATOM   1109 C  C     . MET A 1 141 ? 33.24899  2.51780   -33.14101 1.000 12.39396 ? 141 MET A C     1 
ATOM   1110 O  O     . MET A 1 141 ? 34.07497  2.42078   -34.05602 1.000 13.64570 ? 141 MET A O     1 
ATOM   1111 C  CB    . MET A 1 141 ? 33.90002  3.91486   -31.15306 1.000 14.81185 ? 141 MET A CB    1 
ATOM   1112 C  CG    . MET A 1 141 ? 35.37602  3.60387   -31.35808 1.000 15.60066 ? 141 MET A CG    1 
ATOM   1113 S  SD    . MET A 1 141 ? 35.80004  1.88688   -31.00404 1.000 18.79007 ? 141 MET A SD    1 
ATOM   1114 C  CE    . MET A 1 141 ? 35.45508  1.81093   -29.24803 1.000 9.76568  ? 141 MET A CE    1 
ATOM   1115 N  N     . LEU A 1 142 ? 32.50101  1.48481   -32.73996 1.000 12.13900 ? 142 LEU A N     1 
ATOM   1116 C  CA    . LEU A 1 142 ? 32.59200  0.19879   -33.42292 1.000 13.16410 ? 142 LEU A CA    1 
ATOM   1117 C  C     . LEU A 1 142 ? 32.13097  0.30374   -34.86991 1.000 12.83963 ? 142 LEU A C     1 
ATOM   1118 O  O     . LEU A 1 142 ? 32.65696  -0.39928  -35.74090 1.000 14.88494 ? 142 LEU A O     1 
ATOM   1119 C  CB    . LEU A 1 142 ? 31.76703  -0.85320  -32.67887 1.000 9.96112  ? 142 LEU A CB    1 
ATOM   1120 C  CG    . LEU A 1 142 ? 32.17706  -1.14515  -31.23287 1.000 12.07449 ? 142 LEU A CG    1 
ATOM   1121 C  CD1   . LEU A 1 142 ? 31.29808  -2.23114  -30.63182 1.000 9.17547  ? 142 LEU A CD1   1 
ATOM   1122 C  CD2   . LEU A 1 142 ? 33.64506  -1.53814  -31.16189 1.000 13.41996 ? 142 LEU A CD2   1 
ATOM   1123 N  N     . VAL A 1 143 ? 31.15396  1.17072   -35.14492 1.000 12.93536 ? 143 VAL A N     1 
ATOM   1124 C  CA    . VAL A 1 143 ? 30.70993  1.37668   -36.51892 1.000 13.36180 ? 143 VAL A CA    1 
ATOM   1125 C  C     . VAL A 1 143 ? 31.79990  2.06166   -37.33396 1.000 14.19123 ? 143 VAL A C     1 
ATOM   1126 O  O     . VAL A 1 143 ? 32.04588  1.70463   -38.49195 1.000 15.07620 ? 143 VAL A O     1 
ATOM   1127 C  CB    . VAL A 1 143 ? 29.39492  2.17867   -36.53691 1.000 12.76909 ? 143 VAL A CB    1 
ATOM   1128 C  CG1   . VAL A 1 143 ? 28.97589  2.48962   -37.96591 1.000 11.49624 ? 143 VAL A CG1   1 
ATOM   1129 C  CG2   . VAL A 1 143 ? 28.29894  1.41168   -35.81487 1.000 14.14293 ? 143 VAL A CG2   1 
ATOM   1130 N  N     . ALA A 1 144 ? 32.47691  3.04868   -36.74200 1.000 14.09440 ? 144 ALA A N     1 
ATOM   1131 C  CA    . ALA A 1 144 ? 33.54089  3.74667   -37.45505 1.000 13.67672 ? 144 ALA A CA    1 
ATOM   1132 C  C     . ALA A 1 144 ? 34.74789  2.84267   -37.67605 1.000 14.70549 ? 144 ALA A C     1 
ATOM   1133 O  O     . ALA A 1 144 ? 35.41587  2.93165   -38.71106 1.000 15.57260 ? 144 ALA A O     1 
ATOM   1134 C  CB    . ALA A 1 144 ? 33.94489  5.00770   -36.69310 1.000 14.33850 ? 144 ALA A CB    1 
ATOM   1135 N  N     . ARG A 1 145 ? 35.04759  1.97109   -36.70932 1.000 15.09220 ? 145 ARG A N     1 
ATOM   1136 C  CA    . ARG A 1 145 ? 36.17891  1.06085   -36.84732 1.000 18.34447 ? 145 ARG A CA    1 
ATOM   1137 C  C     . ARG A 1 145 ? 35.92619  -0.02536  -37.88386 1.000 16.55343 ? 145 ARG A C     1 
ATOM   1138 O  O     . ARG A 1 145 ? 36.88681  -0.60002  -38.40732 1.000 17.81403 ? 145 ARG A O     1 
ATOM   1139 C  CB    . ARG A 1 145 ? 36.51044  0.42250   -35.49634 1.000 15.15004 ? 145 ARG A CB    1 
ATOM   1140 C  CG    . ARG A 1 145 ? 37.06284  1.39577   -34.46710 1.000 17.66158 ? 145 ARG A CG    1 
ATOM   1141 C  CD    . ARG A 1 145 ? 38.50868  1.75965   -34.76162 1.000 23.17215 ? 145 ARG A CD    1 
ATOM   1142 N  NE    . ARG A 1 145 ? 39.43740  1.01551   -33.91906 1.000 29.75280 ? 145 ARG A NE    1 
ATOM   1143 C  CZ    . ARG A 1 145 ? 39.90878  1.45332   -32.75941 0.000 23.90251 ? 145 ARG A CZ    1 
ATOM   1144 N  NH1   . ARG A 1 145 ? 39.56581  2.63646   -32.27645 0.000 21.91235 ? 145 ARG A NH1   1 
ATOM   1145 N  NH2   . ARG A 1 145 ? 40.74581  0.68549   -32.06729 0.000 23.51306 ? 145 ARG A NH2   1 
ATOM   1146 N  N     . ASN A 1 146 ? 34.66290  -0.31734  -38.19295 1.000 14.23783 ? 146 ASN A N     1 
ATOM   1147 C  CA    . ASN A 1 146 ? 34.30789  -1.33838  -39.17091 1.000 15.38889 ? 146 ASN A CA    1 
ATOM   1148 C  C     . ASN A 1 146 ? 34.04486  -0.74542  -40.55292 1.000 13.37081 ? 146 ASN A C     1 
ATOM   1149 O  O     . ASN A 1 146 ? 33.31085  -1.33345  -41.35389 1.000 15.71802 ? 146 ASN A O     1 
ATOM   1150 C  CB    . ASN A 1 146 ? 33.09291  -2.13337  -38.68786 1.000 16.47581 ? 146 ASN A CB    1 
ATOM   1151 C  CG    . ASN A 1 146 ? 32.96190  -3.47839  -39.37782 1.000 15.56066 ? 146 ASN A CG    1 
ATOM   1152 O  OD1   . ASN A 1 146 ? 33.95990  -4.12039  -39.70682 1.000 13.11641 ? 146 ASN A OD1   1 
ATOM   1153 N  ND2   . ASN A 1 146 ? 31.72690  -3.90841  -39.60678 1.000 17.71367 ? 146 ASN A ND2   1 
ATOM   1154 N  N     . GLY A 1 147 ? 34.62484  0.41558   -40.84497 1.000 17.27953 ? 147 GLY A N     1 
ATOM   1155 C  CA    . GLY A 1 147 ? 34.48481  1.03554   -42.14599 1.000 16.92941 ? 147 GLY A CA    1 
ATOM   1156 C  C     . GLY A 1 147 ? 33.25080  1.89152   -42.33399 1.000 15.55261 ? 147 GLY A C     1 
ATOM   1157 O  O     . GLY A 1 147 ? 33.03577  2.39949   -43.44100 1.000 15.93438 ? 147 GLY A O     1 
ATOM   1158 N  N     . GLY A 1 148 ? 32.43282  2.06755   -41.29797 1.000 16.25474 ? 148 GLY A N     1 
ATOM   1159 C  CA    . GLY A 1 148 ? 31.24981  2.90153   -41.38297 1.000 15.15838 ? 148 GLY A CA    1 
ATOM   1160 C  C     . GLY A 1 148 ? 29.93182  2.16152   -41.31592 1.000 18.29184 ? 148 GLY A C     1 
ATOM   1161 O  O     . GLY A 1 148 ? 28.87981  2.81052   -41.32892 1.000 21.11782 ? 148 GLY A O     1 
ATOM   1162 N  N     . ALA A 1 149 ? 29.94683  0.83253   -41.24488 1.000 19.55434 ? 149 ALA A N     1 
ATOM   1163 C  CA    . ALA A 1 149 ? 28.73084  0.03852   -41.16383 1.000 17.00753 ? 149 ALA A CA    1 
ATOM   1164 C  C     . ALA A 1 149 ? 28.83287  -0.93644  -40.00081 1.000 16.49102 ? 149 ALA A C     1 
ATOM   1165 O  O     . ALA A 1 149 ? 29.92388  -1.37942  -39.63382 1.000 18.48760 ? 149 ALA A O     1 
ATOM   1166 C  CB    . ALA A 1 149 ? 28.46782  -0.72652  -42.46781 1.000 19.89156 ? 149 ALA A CB    1 
ATOM   1167 N  N     . ALA A 1 150 ? 27.68089  -1.26644  -39.42377 1.000 12.57499 ? 150 ALA A N     1 
ATOM   1168 C  CA    . ALA A 1 150 ? 27.65092  -2.20040  -38.30874 1.000 14.61093 ? 150 ALA A CA    1 
ATOM   1169 C  C     . ALA A 1 150 ? 27.71992  -3.63842  -38.82170 1.000 16.57779 ? 150 ALA A C     1 
ATOM   1170 O  O     . ALA A 1 150 ? 27.13090  -3.95745  -39.85768 1.000 13.12279 ? 150 ALA A O     1 
ATOM   1171 C  CB    . ALA A 1 150 ? 26.38493  -2.00839  -37.47772 1.000 12.78727 ? 150 ALA A CB    1 
ATOM   1172 N  N     . PRO A 1 151 ? 28.43994  -4.51839  -38.12569 1.000 14.81582 ? 151 PRO A N     1 
ATOM   1173 C  CA    . PRO A 1 151 ? 28.47094  -5.92640  -38.53465 1.000 14.26990 ? 151 PRO A CA    1 
ATOM   1174 C  C     . PRO A 1 151 ? 27.09295  -6.55841  -38.41460 1.000 15.17446 ? 151 PRO A C     1 
ATOM   1175 O  O     . PRO A 1 151 ? 26.31297  -6.23539  -37.51659 1.000 16.28470 ? 151 PRO A O     1 
ATOM   1176 C  CB    . PRO A 1 151 ? 29.46497  -6.56336  -37.55565 1.000 17.61546 ? 151 PRO A CB    1 
ATOM   1177 C  CG    . PRO A 1 151 ? 30.26797  -5.42134  -37.01870 1.000 15.75962 ? 151 PRO A CG    1 
ATOM   1178 C  CD    . PRO A 1 151 ? 29.33496  -4.25135  -36.98772 1.000 16.38771 ? 151 PRO A CD    1 
ATOM   1179 N  N     . LEU A 1 152 ? 26.79594  -7.47044  -39.34057 1.000 17.56133 ? 152 LEU A N     1 
ATOM   1180 C  CA    . LEU A 1 152 ? 25.50094  -8.13445  -39.37652 1.000 17.97515 ? 152 LEU A CA    1 
ATOM   1181 C  C     . LEU A 1 152 ? 25.54196  -9.57844  -38.89848 1.000 16.65073 ? 152 LEU A C     1 
ATOM   1182 O  O     . LEU A 1 152 ? 24.47797  -10.16744 -38.67944 1.000 15.99272 ? 152 LEU A O     1 
ATOM   1183 C  CB    . LEU A 1 152 ? 24.91891  -8.08450  -40.79751 1.000 18.67731 ? 152 LEU A CB    1 
ATOM   1184 C  CG    . LEU A 1 152 ? 24.67189  -6.68352  -41.36354 1.000 18.52174 ? 152 LEU A CG    1 
ATOM   1185 C  CD1   . LEU A 1 152 ? 24.00386  -6.76356  -42.72653 1.000 23.38581 ? 152 LEU A CD1   1 
ATOM   1186 C  CD2   . LEU A 1 152 ? 23.84090  -5.84950  -40.40055 1.000 14.84551 ? 152 LEU A CD2   1 
ATOM   1187 N  N     . THR A 1 153 ? 26.72597  -10.16142 -38.72948 1.000 17.36201 ? 153 THR A N     1 
ATOM   1188 C  CA    . THR A 1 153 ? 26.86899  -11.51941 -38.22744 1.000 19.56076 ? 153 THR A CA    1 
ATOM   1189 C  C     . THR A 1 153 ? 27.64902  -11.50236 -36.92046 1.000 16.89191 ? 153 THR A C     1 
ATOM   1190 O  O     . THR A 1 153 ? 28.54502  -10.67635 -36.72251 1.000 18.58566 ? 153 THR A O     1 
ATOM   1191 C  CB    . THR A 1 153 ? 27.57998  -12.42843 -39.23943 1.000 17.11974 ? 153 THR A CB    1 
ATOM   1192 O  OG1   . THR A 1 153 ? 28.94297  -12.01142 -39.38647 1.000 20.04401 ? 153 THR A OG1   1 
ATOM   1193 C  CG2   . THR A 1 153 ? 26.88895  -12.36548 -40.59242 1.000 17.93642 ? 153 THR A CG2   1 
ATOM   1194 N  N     . MET A 1 154 ? 27.29605  -12.42834 -36.02343 1.000 15.26082 ? 154 MET A N     1 
ATOM   1195 C  CA    . MET A 1 154 ? 27.97407  -12.49929 -34.73244 1.000 15.32269 ? 154 MET A CA    1 
ATOM   1196 C  C     . MET A 1 154 ? 29.43807  -12.88828 -34.88546 1.000 16.62990 ? 154 MET A C     1 
ATOM   1197 O  O     . MET A 1 154 ? 30.28309  -12.42325 -34.11249 1.000 18.24661 ? 154 MET A O     1 
ATOM   1198 C  CB    . MET A 1 154 ? 27.25910  -13.49227 -33.81539 1.000 14.92596 ? 154 MET A CB    1 
ATOM   1199 C  CG    . MET A 1 154 ? 27.81513  -13.53722 -32.40140 1.000 14.91419 ? 154 MET A CG    1 
ATOM   1200 S  SD    . MET A 1 154 ? 27.54614  -11.99320 -31.51044 1.000 21.96810 ? 154 MET A SD    1 
ATOM   1201 C  CE    . MET A 1 154 ? 29.14815  -11.75316 -30.75049 1.000 12.27159 ? 154 MET A CE    1 
ATOM   1202 N  N     . GLN A 1 155 ? 29.75606  -13.73131 -35.87144 1.000 16.38497 ? 155 GLN A N     1 
ATOM   1203 C  CA    . GLN A 1 155 ? 31.14506  -14.12331 -36.08946 1.000 18.10942 ? 155 GLN A CA    1 
ATOM   1204 C  C     . GLN A 1 155 ? 32.00004  -12.92031 -36.46751 1.000 17.11163 ? 155 GLN A C     1 
ATOM   1205 O  O     . GLN A 1 155 ? 33.11905  -12.76029 -35.96554 1.000 18.32804 ? 155 GLN A O     1 
ATOM   1206 C  CB    . GLN A 1 155 ? 31.21904  -15.20234 -37.17043 1.000 14.75079 ? 155 GLN A CB    1 
ATOM   1207 C  CG    . GLN A 1 155 ? 32.22706  -16.31132 -36.89541 1.000 22.45152 ? 155 GLN A CG    1 
ATOM   1208 C  CD    . GLN A 1 155 ? 33.66505  -15.87932 -37.11846 1.000 22.04125 ? 155 GLN A CD    1 
ATOM   1209 O  OE1   . GLN A 1 155 ? 34.25003  -16.15135 -38.16646 0.000 20.13474 ? 155 GLN A OE1   1 
ATOM   1210 N  NE2   . GLN A 1 155 ? 34.24607  -15.21228 -36.12649 0.000 19.78137 ? 155 GLN A NE2   1 
ATOM   1211 N  N     . SER A 1 156 ? 31.48202  -12.05234 -37.34053 1.000 18.93788 ? 156 SER A N     1 
ATOM   1212 C  CA    . SER A 1 156 ? 32.21900  -10.85235 -37.71958 1.000 18.62074 ? 156 SER A CA    1 
ATOM   1213 C  C     . SER A 1 156 ? 32.26801  -9.83731  -36.58461 1.000 17.27957 ? 156 SER A C     1 
ATOM   1214 O  O     . SER A 1 156 ? 33.22001  -9.05230  -36.49765 1.000 18.83632 ? 156 SER A O     1 
ATOM   1215 C  CB    . SER A 1 156 ? 31.59597  -10.22139 -38.96458 1.000 19.07662 ? 156 SER A CB    1 
ATOM   1216 O  OG    . SER A 1 156 ? 32.22795  -8.99540  -39.28763 1.000 19.22812 ? 156 SER A OG    1 
ATOM   1217 N  N     . PHE A 1 157 ? 31.25703  -9.82929  -35.71259 1.000 17.59914 ? 157 PHE A N     1 
ATOM   1218 C  CA    . PHE A 1 157 ? 31.25505  -8.89026  -34.59662 1.000 14.58893 ? 157 PHE A CA    1 
ATOM   1219 C  C     . PHE A 1 157 ? 32.29507  -9.27522  -33.55163 1.000 16.10951 ? 157 PHE A C     1 
ATOM   1220 O  O     . PHE A 1 157 ? 32.91808  -8.40120  -32.93767 1.000 14.71590 ? 157 PHE A O     1 
ATOM   1221 C  CB    . PHE A 1 157 ? 29.86106  -8.82125  -33.97159 1.000 13.49623 ? 157 PHE A CB    1 
ATOM   1222 C  CG    . PHE A 1 157 ? 29.72108  -7.76322  -32.91062 1.000 12.00897 ? 157 PHE A CG    1 
ATOM   1223 C  CD1   . PHE A 1 157 ? 29.48006  -6.44423  -33.25665 1.000 11.38827 ? 157 PHE A CD1   1 
ATOM   1224 C  CD2   . PHE A 1 157 ? 29.82511  -8.09018  -31.56861 1.000 10.77253 ? 157 PHE A CD2   1 
ATOM   1225 C  CE1   . PHE A 1 157 ? 29.34907  -5.46921  -32.28468 1.000 9.99902  ? 157 PHE A CE1   1 
ATOM   1226 C  CE2   . PHE A 1 157 ? 29.69412  -7.12015  -30.59164 1.000 10.98181 ? 157 PHE A CE2   1 
ATOM   1227 C  CZ    . PHE A 1 157 ? 29.45610  -5.80716  -30.95067 1.000 9.68919  ? 157 PHE A CZ    1 
ATOM   1228 N  N     . THR A 1 158 ? 32.49609  -10.57821 -33.33759 1.000 16.20312 ? 158 THR A N     1 
ATOM   1229 C  CA    . THR A 1 158 ? 33.51811  -11.02518 -32.39660 1.000 18.23439 ? 158 THR A CA    1 
ATOM   1230 C  C     . THR A 1 158 ? 34.91510  -10.68518 -32.90064 1.000 19.55442 ? 158 THR A C     1 
ATOM   1231 O  O     . THR A 1 158 ? 35.79111  -10.30815 -32.11467 1.000 22.82696 ? 158 THR A O     1 
ATOM   1232 C  CB    . THR A 1 158 ? 33.38313  -12.53017 -32.15255 1.000 21.09494 ? 158 THR A CB    1 
ATOM   1233 O  OG1   . THR A 1 158 ? 32.07814  -12.81516 -31.63452 1.000 17.97476 ? 158 THR A OG1   1 
ATOM   1234 C  CG2   . THR A 1 158 ? 34.43115  -13.01013 -31.15756 1.000 19.13955 ? 158 THR A CG2   1 
ATOM   1235 N  N     . LYS A 1 159 ? 35.14007  -10.80722 -34.21164 1.000 18.78051 ? 159 LYS A N     1 
ATOM   1236 C  CA    . LYS A 1 159 ? 36.42806  -10.42723 -34.78068 1.000 18.05386 ? 159 LYS A CA    1 
ATOM   1237 C  C     . LYS A 1 159 ? 36.67605  -8.92922  -34.65573 1.000 20.63051 ? 159 LYS A C     1 
ATOM   1238 O  O     . LYS A 1 159 ? 37.83305  -8.49621  -34.59877 1.000 20.08634 ? 159 LYS A O     1 
ATOM   1239 C  CB    . LYS A 1 159 ? 36.49903  -10.85627 -36.24767 1.000 18.13755 ? 159 LYS A CB    1 
ATOM   1240 C  CG    . LYS A 1 159 ? 36.38104  -12.35728 -36.46862 1.000 18.42222 ? 159 LYS A CG    1 
ATOM   1241 C  CD    . LYS A 1 159 ? 35.73901  -12.67132 -37.81560 0.000 18.88341 ? 159 LYS A CD    1 
ATOM   1242 C  CE    . LYS A 1 159 ? 36.59498  -12.20135 -38.98163 0.000 18.71890 ? 159 LYS A CE    1 
ATOM   1243 N  NZ    . LYS A 1 159 ? 37.71498  -13.13935 -39.26863 0.000 18.49984 ? 159 LYS A NZ    1 
ATOM   1244 N  N     . LEU A 1 160 ? 35.61104  -8.12623  -34.60773 1.000 18.58507 ? 160 LEU A N     1 
ATOM   1245 C  CA    . LEU A 1 160 ? 35.76603  -6.67922  -34.50278 1.000 16.27146 ? 160 LEU A CA    1 
ATOM   1246 C  C     . LEU A 1 160 ? 36.12906  -6.25918  -33.08380 1.000 18.46623 ? 160 LEU A C     1 
ATOM   1247 O  O     . LEU A 1 160 ? 37.07806  -5.49416  -32.88084 1.000 20.05514 ? 160 LEU A O     1 
ATOM   1248 C  CB    . LEU A 1 160 ? 34.48402  -5.97925  -34.95777 1.000 17.91474 ? 160 LEU A CB    1 
ATOM   1249 C  CG    . LEU A 1 160 ? 34.46601  -4.45524  -34.80882 1.000 19.26150 ? 160 LEU A CG    1 
ATOM   1250 C  CD1   . LEU A 1 160 ? 35.56799  -3.81826  -35.64186 1.000 19.93615 ? 160 LEU A CD1   1 
ATOM   1251 C  CD2   . LEU A 1 160 ? 33.10600  -3.89226  -35.18981 1.000 17.65224 ? 160 LEU A CD2   1 
ATOM   1252 N  N     . VAL A 1 161 ? 35.38408  -6.75015  -32.08977 1.000 17.26220 ? 161 VAL A N     1 
ATOM   1253 C  CA    . VAL A 1 161 ? 35.66611  -6.39111  -30.70479 1.000 16.95019 ? 161 VAL A CA    1 
ATOM   1254 C  C     . VAL A 1 161 ? 37.01713  -6.92208  -30.24780 1.000 17.73317 ? 161 VAL A C     1 
ATOM   1255 O  O     . VAL A 1 161 ? 37.61014  -6.37105  -29.31283 1.000 19.00943 ? 161 VAL A O     1 
ATOM   1256 C  CB    . VAL A 1 161 ? 34.54213  -6.89009  -29.77775 1.000 14.07622 ? 161 VAL A CB    1 
ATOM   1257 C  CG1   . VAL A 1 161 ? 33.21912  -6.24111  -30.15574 1.000 14.26725 ? 161 VAL A CG1   1 
ATOM   1258 C  CG2   . VAL A 1 161 ? 34.43315  -8.40509  -29.83170 1.000 16.78310 ? 161 VAL A CG2   1 
ATOM   1259 N  N     . ASP A 1 162 ? 37.52912  -7.97810  -30.88478 1.000 19.89009 ? 162 ASP A N     1 
ATOM   1260 C  CA    . ASP A 1 162 ? 38.86213  -8.46308  -30.54379 1.000 17.37160 ? 162 ASP A CA    1 
ATOM   1261 C  C     . ASP A 1 162 ? 39.94811  -7.55209  -31.09884 1.000 18.50002 ? 162 ASP A C     1 
ATOM   1262 O  O     . ASP A 1 162 ? 41.01712  -7.42706  -30.49287 1.000 21.46347 ? 162 ASP A O     1 
ATOM   1263 C  CB    . ASP A 1 162 ? 39.05513  -9.89309  -31.05075 1.000 17.75860 ? 162 ASP A CB    1 
ATOM   1264 C  CG    . ASP A 1 162 ? 38.21716  -10.90108 -30.28770 1.000 22.39371 ? 162 ASP A CG    1 
ATOM   1265 O  OD1   . ASP A 1 162 ? 37.43717  -10.48405 -29.40370 1.000 22.65762 ? 162 ASP A OD1   1 
ATOM   1266 O  OD2   . ASP A 1 162 ? 38.34016  -12.11008 -30.57067 1.000 28.99858 ? 162 ASP A OD2   1 
ATOM   1267 N  N     . ARG A 1 163 ? 39.70103  -6.91322  -32.24536 1.000 20.92584 ? 163 ARG A N     1 
ATOM   1268 C  CA    . ARG A 1 163 ? 40.66397  -5.94808  -32.76444 1.000 21.32487 ? 163 ARG A CA    1 
ATOM   1269 C  C     . ARG A 1 163 ? 40.65961  -4.66221  -31.94966 1.000 19.42438 ? 163 ARG A C     1 
ATOM   1270 O  O     . ARG A 1 163 ? 41.70797  -4.02613  -31.79227 1.000 22.09536 ? 163 ARG A O     1 
ATOM   1271 C  CB    . ARG A 1 163 ? 40.37451  -5.64024  -34.23435 1.000 24.20989 ? 163 ARG A CB    1 
ATOM   1272 C  CG    . ARG A 1 163 ? 40.65944  -6.78979  -35.18706 1.000 28.75696 ? 163 ARG A CG    1 
ATOM   1273 C  CD    . ARG A 1 163 ? 40.64766  -6.31651  -36.63318 1.000 30.27526 ? 163 ARG A CD    1 
ATOM   1274 N  NE    . ARG A 1 163 ? 39.36537  -5.73460  -37.01132 1.000 30.52398 ? 163 ARG A NE    1 
ATOM   1275 C  CZ    . ARG A 1 163 ? 38.39745  -6.39451  -37.63252 1.000 31.84987 ? 163 ARG A CZ    1 
ATOM   1276 N  NH1   . ARG A 1 163 ? 38.53386  -7.66663  -37.96912 1.000 35.72054 ? 163 ARG A NH1   1 
ATOM   1277 N  NH2   . ARG A 1 163 ? 37.26488  -5.76174  -37.92519 1.000 28.86127 ? 163 ARG A NH2   1 
ATOM   1278 N  N     . VAL A 1 164 ? 39.49808  -4.26510  -31.42693 1.000 18.36041 ? 164 VAL A N     1 
ATOM   1279 C  CA    . VAL A 1 164 ? 39.42309  -3.04608  -30.62997 1.000 16.15755 ? 164 VAL A CA    1 
ATOM   1280 C  C     . VAL A 1 164 ? 40.07712  -3.25703  -29.26897 1.000 16.72016 ? 164 VAL A C     1 
ATOM   1281 O  O     . VAL A 1 164 ? 40.79112  -2.38201  -28.76502 1.000 18.63759 ? 164 VAL A O     1 
ATOM   1282 C  CB    . VAL A 1 164 ? 37.95909  -2.59008  -30.49095 1.000 17.75583 ? 164 VAL A CB    1 
ATOM   1283 C  CG1   . VAL A 1 164 ? 37.87409  -1.30206  -29.68399 1.000 18.64715 ? 164 VAL A CG1   1 
ATOM   1284 C  CG2   . VAL A 1 164 ? 37.32806  -2.40713  -31.86294 1.000 17.36725 ? 164 VAL A CG2   1 
ATOM   1285 N  N     . GLY A 1 165 ? 39.84914  -4.41001  -28.65893 1.000 15.54634 ? 165 GLY A N     1 
ATOM   1286 C  CA    . GLY A 1 165 ? 40.43817  -4.74297  -27.38194 1.000 16.86387 ? 165 GLY A CA    1 
ATOM   1287 C  C     . GLY A 1 165 ? 39.41519  -4.81094  -26.26591 1.000 15.08749 ? 165 GLY A C     1 
ATOM   1288 O  O     . GLY A 1 165 ? 38.20419  -4.90196  -26.48689 1.000 13.51487 ? 165 GLY A O     1 
ATOM   1289 N  N     . ASP A 1 166 ? 39.92522  -4.76490  -25.03793 1.000 11.49336 ? 166 ASP A N     1 
ATOM   1290 C  CA    . ASP A 1 166 ? 39.06824  -4.84387  -23.86891 1.000 12.04667 ? 166 ASP A CA    1 
ATOM   1291 C  C     . ASP A 1 166 ? 38.18524  -3.60088  -23.76392 1.000 11.84738 ? 166 ASP A C     1 
ATOM   1292 O  O     . ASP A 1 166 ? 38.57422  -2.51289  -24.19697 1.000 14.60357 ? 166 ASP A O     1 
ATOM   1293 C  CB    . ASP A 1 166 ? 39.90527  -4.98583  -22.59892 1.000 11.42034 ? 166 ASP A CB    1 
ATOM   1294 C  CG    . ASP A 1 166 ? 40.62528  -6.31682  -22.51989 1.000 14.17284 ? 166 ASP A CG    1 
ATOM   1295 O  OD1   . ASP A 1 166 ? 40.04228  -7.33584  -22.94485 1.000 14.57168 ? 166 ASP A OD1   1 
ATOM   1296 O  OD2   . ASP A 1 166 ? 41.77529  -6.34380  -22.03192 1.000 18.31060 ? 166 ASP A OD2   1 
ATOM   1297 N  N     . PRO A 1 167 ? 36.98825  -3.74087  -23.20289 1.000 10.38146 ? 167 PRO A N     1 
ATOM   1298 C  CA    . PRO A 1 167 ? 36.15125  -2.56887  -22.93491 1.000 9.27870  ? 167 PRO A CA    1 
ATOM   1299 C  C     . PRO A 1 167 ? 36.79126  -1.68383  -21.88195 1.000 8.64238  ? 167 PRO A C     1 
ATOM   1300 O  O     . PRO A 1 167 ? 37.70028  -2.12580  -21.16196 1.000 8.89335  ? 167 PRO A O     1 
ATOM   1301 C  CB    . PRO A 1 167 ? 34.83626  -3.18086  -22.42287 1.000 8.71106  ? 167 PRO A CB    1 
ATOM   1302 C  CG    . PRO A 1 167 ? 34.86026  -4.60188  -22.88582 1.000 11.34149 ? 167 PRO A CG    1 
ATOM   1303 C  CD    . PRO A 1 167 ? 36.30127  -4.99987  -22.87384 1.000 9.57506  ? 167 PRO A CD    1 
ATOM   1304 N  N     . PRO A 1 168 ? 36.36325  -0.42683  -21.76998 1.000 11.45221 ? 168 PRO A N     1 
ATOM   1305 C  CA    . PRO A 1 168 ? 36.89027  0.43220   -20.70302 1.000 10.07857 ? 168 PRO A CA    1 
ATOM   1306 C  C     . PRO A 1 168 ? 36.61030  -0.16076  -19.33000 1.000 10.51728 ? 168 PRO A C     1 
ATOM   1307 O  O     . PRO A 1 168 ? 35.57631  -0.79176  -19.10195 1.000 10.01970 ? 168 PRO A O     1 
ATOM   1308 C  CB    . PRO A 1 168 ? 36.14325  1.75419   -20.91204 1.000 8.51073  ? 168 PRO A CB    1 
ATOM   1309 C  CG    . PRO A 1 168 ? 35.77122  1.74615   -22.35504 1.000 9.62642  ? 168 PRO A CG    1 
ATOM   1310 C  CD    . PRO A 1 168 ? 35.48123  0.31113   -22.68999 1.000 10.91747 ? 168 PRO A CD    1 
ATOM   1311 N  N     . ALA A 1 169 ? 37.55432  0.04128   -18.41502 1.000 10.68177 ? 169 ALA A N     1 
ATOM   1312 C  CA    . ALA A 1 169 ? 37.40335  -0.46768  -17.06400 1.000 10.54972 ? 169 ALA A CA    1 
ATOM   1313 C  C     . ALA A 1 169 ? 36.25236  0.24533   -16.35500 1.000 9.74283  ? 169 ALA A C     1 
ATOM   1314 O  O     . ALA A 1 169 ? 35.91835  1.38432   -16.68903 1.000 8.41196  ? 169 ALA A O     1 
ATOM   1315 C  CB    . ALA A 1 169 ? 38.69837  -0.28065  -16.27704 1.000 14.41150 ? 169 ALA A CB    1 
ATOM   1316 N  N     . PRO A 1 170 ? 35.61739  -0.41064  -15.38297 1.000 10.48469 ? 170 PRO A N     1 
ATOM   1317 C  CA    . PRO A 1 170 ? 34.54340  0.25437   -14.63696 1.000 9.09307  ? 170 PRO A CA    1 
ATOM   1318 C  C     . PRO A 1 170 ? 35.07541  1.42940   -13.83201 1.000 10.96168 ? 170 PRO A C     1 
ATOM   1319 O  O     . PRO A 1 170 ? 36.17042  1.37442   -13.26503 1.000 8.72793  ? 170 PRO A O     1 
ATOM   1320 C  CB    . PRO A 1 170 ? 33.99943  -0.85361  -13.72692 1.000 10.32178 ? 170 PRO A CB    1 
ATOM   1321 C  CG    . PRO A 1 170 ? 35.11044  -1.84760  -13.62991 1.000 10.23023 ? 170 PRO A CG    1 
ATOM   1322 C  CD    . PRO A 1 170 ? 35.79841  -1.80963  -14.95993 1.000 8.36051  ? 170 PRO A CD    1 
ATOM   1323 N  N     . ALA A 1 171 ? 34.28740  2.50139   -13.79503 1.000 9.47879  ? 171 ALA A N     1 
ATOM   1324 C  CA    . ALA A 1 171 ? 34.67841  3.69542   -13.06807 1.000 9.77134  ? 171 ALA A CA    1 
ATOM   1325 C  C     . ALA A 1 171 ? 34.70444  3.41946   -11.56506 1.000 10.87851 ? 171 ALA A C     1 
ATOM   1326 O  O     . ALA A 1 171 ? 33.99146  2.54047   -11.07602 1.000 12.63532 ? 171 ALA A O     1 
ATOM   1327 C  CB    . ALA A 1 171 ? 33.71639  4.84140   -13.37309 1.000 12.18302 ? 171 ALA A CB    1 
ATOM   1328 N  N     . PRO A 1 172 ? 35.52545  4.14949   -10.81210 1.000 11.92931 ? 172 PRO A N     1 
ATOM   1329 C  CA    . PRO A 1 172 ? 35.55748  3.95554   -9.36010  1.000 12.77692 ? 172 PRO A CA    1 
ATOM   1330 C  C     . PRO A 1 172 ? 34.24849  4.37955   -8.71008  1.000 13.24798 ? 172 PRO A C     1 
ATOM   1331 O  O     . PRO A 1 172 ? 33.41647  5.07252   -9.30109  1.000 12.54947 ? 172 PRO A O     1 
ATOM   1332 C  CB    . PRO A 1 172 ? 36.71948  4.84356   -8.90315  1.000 13.65229 ? 172 PRO A CB    1 
ATOM   1333 C  CG    . PRO A 1 172 ? 36.86045  5.86553   -9.98218  1.000 13.11837 ? 172 PRO A CG    1 
ATOM   1334 C  CD    . PRO A 1 172 ? 36.50843  5.15549   -11.25415 1.000 11.01601 ? 172 PRO A CD    1 
ATOM   1335 N  N     . ASP A 1 173 ? 34.07452  3.94058   -7.46707  1.000 15.08866 ? 173 ASP A N     1 
ATOM   1336 C  CA    . ASP A 1 173 ? 32.86353  4.25360   -6.73005  1.000 16.23644 ? 173 ASP A CA    1 
ATOM   1337 C  C     . ASP A 1 173 ? 32.85353  5.72561   -6.31709  1.000 15.87784 ? 173 ASP A C     1 
ATOM   1338 O  O     . ASP A 1 173 ? 33.91053  6.33962   -6.14513  1.000 14.76730 ? 173 ASP A O     1 
ATOM   1339 C  CB    . ASP A 1 173 ? 32.74357  3.36463   -5.49502  1.000 16.50182 ? 173 ASP A CB    1 
ATOM   1340 C  CG    . ASP A 1 173 ? 32.29457  1.95762   -5.83497  1.000 17.92690 ? 173 ASP A CG    1 
ATOM   1341 O  OD1   . ASP A 1 173 ? 33.11657  1.17661   -6.35996  1.000 24.25361 ? 173 ASP A OD1   1 
ATOM   1342 O  OD2   . ASP A 1 173 ? 31.11558  1.63162   -5.58093  1.000 24.40527 ? 173 ASP A OD2   1 
ATOM   1343 N  N     . PRO A 1 174 ? 31.67053  6.31560   -6.16009  1.000 16.35042 ? 174 PRO A N     1 
ATOM   1344 C  CA    . PRO A 1 174 ? 31.58353  7.71362   -5.71813  1.000 15.31009 ? 174 PRO A CA    1 
ATOM   1345 C  C     . PRO A 1 174 ? 32.10956  7.86866   -4.30314  1.000 17.01348 ? 174 PRO A C     1 
ATOM   1346 O  O     . PRO A 1 174 ? 32.27458  6.87169   -3.58212  1.000 15.03354 ? 174 PRO A O     1 
ATOM   1347 C  CB    . PRO A 1 174 ? 30.07752  8.01160   -5.79310  1.000 16.05544 ? 174 PRO A CB    1 
ATOM   1348 C  CG    . PRO A 1 174 ? 29.42054  6.67660   -5.70605  1.000 15.46537 ? 174 PRO A CG    1 
ATOM   1349 C  CD    . PRO A 1 174 ? 30.34153  5.73659   -6.42004  1.000 12.36555 ? 174 PRO A CD    1 
ATOM   1350 N  N     . PRO A 1 175 ? 32.39656  9.09668   -3.86619  1.000 14.99820 ? 175 PRO A N     1 
ATOM   1351 C  CA    . PRO A 1 175 ? 32.91558  9.28972   -2.50820  1.000 16.57842 ? 175 PRO A CA    1 
ATOM   1352 C  C     . PRO A 1 175 ? 31.89361  8.88975   -1.45317  1.000 16.72637 ? 175 PRO A C     1 
ATOM   1353 O  O     . PRO A 1 175 ? 30.70261  8.72473   -1.72814  1.000 15.28827 ? 175 PRO A O     1 
ATOM   1354 C  CB    . PRO A 1 175 ? 33.21857  10.79173  -2.45126  1.000 17.60784 ? 175 PRO A CB    1 
ATOM   1355 C  CG    . PRO A 1 175 ? 32.34655  11.39369  -3.50225  1.000 16.00637 ? 175 PRO A CG    1 
ATOM   1356 C  CD    . PRO A 1 175 ? 32.28953  10.37166  -4.59822  1.000 16.67290 ? 175 PRO A CD    1 
ATOM   1357 N  N     . ALA A 1 176 ? 32.38564  8.73279   -0.22118  1.000 14.85039 ? 176 ALA A N     1 
ATOM   1358 C  CA    . ALA A 1 176 ? 31.52066  8.31582   0.87786   1.000 15.31401 ? 176 ALA A CA    1 
ATOM   1359 C  C     . ALA A 1 176 ? 30.47666  9.37382   1.20985   1.000 14.97003 ? 176 ALA A C     1 
ATOM   1360 O  O     . ALA A 1 176 ? 29.39168  9.03782   1.69888   1.000 13.80285 ? 176 ALA A O     1 
ATOM   1361 C  CB    . ALA A 1 176 ? 32.36069  7.99286   2.11285   1.000 12.90517 ? 176 ALA A CB    1 
ATOM   1362 N  N     . ALA A 1 177 ? 30.78265  10.64381  0.96080   1.000 14.29619 ? 177 ALA A N     1 
ATOM   1363 C  CA    . ALA A 1 177 ? 29.85164  11.74081  1.17779   1.000 13.58074 ? 177 ALA A CA    1 
ATOM   1364 C  C     . ALA A 1 177 ? 29.69761  12.53377  -0.11123  1.000 15.43824 ? 177 ALA A C     1 
ATOM   1365 O  O     . ALA A 1 177 ? 30.68259  12.80476  -0.80626  1.000 16.49157 ? 177 ALA A O     1 
ATOM   1366 C  CB    . ALA A 1 177 ? 30.32566  12.66185  2.30775   1.000 14.28002 ? 177 ALA A CB    1 
ATOM   1367 N  N     . MET A 1 178 ? 28.45960  12.90275  -0.42922  1.000 12.20019 ? 178 MET A N     1 
ATOM   1368 C  CA    . MET A 1 178 ? 28.17057  13.63271  -1.65023  1.000 14.61354 ? 178 MET A CA    1 
ATOM   1369 C  C     . MET A 1 178 ? 27.60356  15.00972  -1.32726  1.000 14.33803 ? 178 MET A C     1 
ATOM   1370 O  O     . MET A 1 178 ? 27.00559  15.20375  -0.26326  1.000 15.52214 ? 178 MET A O     1 
ATOM   1371 C  CB    . MET A 1 178 ? 27.17156  12.86868  -2.53019  1.000 14.23507 ? 178 MET A CB    1 
ATOM   1372 C  CG    . MET A 1 178 ? 27.48856  11.39368  -2.70115  1.000 17.62486 ? 178 MET A CG    1 
ATOM   1373 S  SD    . MET A 1 178 ? 26.99553  10.77062  -4.31912  1.000 25.75283 ? 178 MET A SD    1 
ATOM   1374 C  CE    . MET A 1 178 ? 25.67852  11.91060  -4.73213  1.000 14.72491 ? 178 MET A CE    1 
ATOM   1375 N  N     . PRO A 1 179 ? 27.78454  15.98569  -2.21330  1.000 16.12883 ? 179 PRO A N     1 
ATOM   1376 C  CA    . PRO A 1 179 ? 27.17353  17.30269  -2.00632  1.000 15.32246 ? 179 PRO A CA    1 
ATOM   1377 C  C     . PRO A 1 179 ? 25.66053  17.20168  -2.02229  1.000 13.60786 ? 179 PRO A C     1 
ATOM   1378 O  O     . PRO A 1 179 ? 25.06451  16.81765  -3.04127  1.000 16.60049 ? 179 PRO A O     1 
ATOM   1379 C  CB    . PRO A 1 179 ? 27.69150  18.12666  -3.19536  1.000 12.86530 ? 179 PRO A CB    1 
ATOM   1380 C  CG    . PRO A 1 179 ? 28.92250  17.41466  -3.64636  1.000 13.68893 ? 179 PRO A CG    1 
ATOM   1381 C  CD    . PRO A 1 179 ? 28.65651  15.96266  -3.40032  1.000 14.96781 ? 179 PRO A CD    1 
ATOM   1382 N  N     . PRO A 1 180 ? 25.00155  17.53471  -0.91829  1.000 12.56445 ? 180 PRO A N     1 
ATOM   1383 C  CA    . PRO A 1 180 ? 23.54756  17.38070  -0.84325  1.000 14.20295 ? 180 PRO A CA    1 
ATOM   1384 C  C     . PRO A 1 180 ? 22.84353  18.47567  -1.62227  1.000 13.26880 ? 180 PRO A C     1 
ATOM   1385 O  O     . PRO A 1 180 ? 23.44352  19.51567  -1.93031  1.000 14.27926 ? 180 PRO A O     1 
ATOM   1386 C  CB    . PRO A 1 180 ? 23.26459  17.49774  0.66175   1.000 14.56760 ? 180 PRO A CB    1 
ATOM   1387 C  CG    . PRO A 1 180 ? 24.34659  18.39477  1.15770   1.000 14.46897 ? 180 PRO A CG    1 
ATOM   1388 C  CD    . PRO A 1 180 ? 25.56858  18.06775  0.33369   1.000 16.33116 ? 180 PRO A CD    1 
ATOM   1389 N  N     . PRO A 1 181 ? 21.57352  18.27765  -1.96924  1.000 12.66227 ? 181 PRO A N     1 
ATOM   1390 C  CA    . PRO A 1 181 ? 20.81050  19.36063  -2.59725  1.000 10.70094 ? 181 PRO A CA    1 
ATOM   1391 C  C     . PRO A 1 181 ? 20.55852  20.49165  -1.61328  1.000 13.10285 ? 181 PRO A C     1 
ATOM   1392 O  O     . PRO A 1 181 ? 20.47654  20.28569  -0.39927  1.000 14.65406 ? 181 PRO A O     1 
ATOM   1393 C  CB    . PRO A 1 181 ? 19.50150  18.67860  -3.01420  1.000 12.84148 ? 181 PRO A CB    1 
ATOM   1394 C  CG    . PRO A 1 181 ? 19.38053  17.50763  -2.09817  1.000 15.98702 ? 181 PRO A CG    1 
ATOM   1395 C  CD    . PRO A 1 181 ? 20.78454  17.03865  -1.85318  1.000 12.91515 ? 181 PRO A CD    1 
ATOM   1396 N  N     . ALA A 1 182 ? 20.44449  21.70264  -2.15532  1.000 11.84252 ? 182 ALA A N     1 
ATOM   1397 C  CA    . ALA A 1 182 ? 20.23550  22.87566  -1.32035  1.000 13.25909 ? 182 ALA A CA    1 
ATOM   1398 C  C     . ALA A 1 182 ? 18.89552  22.79067  -0.59632  1.000 15.40661 ? 182 ALA A C     1 
ATOM   1399 O  O     . ALA A 1 182 ? 17.92951  22.20465  -1.09228  1.000 15.03288 ? 182 ALA A O     1 
ATOM   1400 C  CB    . ALA A 1 182 ? 20.29947  24.15064  -2.16039  1.000 14.09024 ? 182 ALA A CB    1 
ATOM   1401 N  N     . GLU A 1 183 ? 18.84754  23.38671  0.58967   1.000 16.25227 ? 183 GLU A N     1 
ATOM   1402 C  CA    . GLU A 1 183 ? 17.66456  23.31272  1.43269   1.000 18.60079 ? 183 GLU A CA    1 
ATOM   1403 C  C     . GLU A 1 183 ? 16.65154  24.38670  1.04468   1.000 17.72574 ? 183 GLU A C     1 
ATOM   1404 O  O     . GLU A 1 183 ? 16.98252  25.40069  0.42465   1.000 19.03764 ? 183 GLU A O     1 
ATOM   1405 C  CB    . GLU A 1 183 ? 18.04859  23.46177  2.90568   1.000 18.28029 ? 183 GLU A CB    1 
ATOM   1406 C  CG    . GLU A 1 183 ? 19.05661  22.43179  3.39069   1.000 20.67477 ? 183 GLU A CG    1 
ATOM   1407 C  CD    . GLU A 1 183 ? 19.56163  22.72384  4.79067   0.000 19.64238 ? 183 GLU A CD    1 
ATOM   1408 O  OE1   . GLU A 1 183 ? 19.27864  23.82385  5.30965   0.000 19.55808 ? 183 GLU A OE1   1 
ATOM   1409 O  OE2   . GLU A 1 183 ? 20.24165  21.85186  5.37268   0.000 19.79317 ? 183 GLU A OE2   1 
ATOM   1410 N  N     . ASP A 1 184 ? 15.39455  24.13971  1.41972   1.000 19.91945 ? 184 ASP A N     1 
ATOM   1411 C  CA    . ASP A 1 184 ? 14.29554  25.08969  1.23071   1.000 20.86355 ? 184 ASP A CA    1 
ATOM   1412 C  C     . ASP A 1 184 ? 14.08051  25.44064  -0.23929  1.000 19.76074 ? 184 ASP A C     1 
ATOM   1413 O  O     . ASP A 1 184 ? 13.64149  26.54663  -0.56632  1.000 16.86207 ? 184 ASP A O     1 
ATOM   1414 C  CB    . ASP A 1 184 ? 14.51255  26.35872  2.05967   1.000 19.63468 ? 184 ASP A CB    1 
ATOM   1415 C  CG    . ASP A 1 184 ? 14.44258  26.09776  3.55168   1.000 27.36564 ? 184 ASP A CG    1 
ATOM   1416 O  OD1   . ASP A 1 184 ? 13.58160  25.29877  3.97772   1.000 30.20959 ? 184 ASP A OD1   1 
ATOM   1417 O  OD2   . ASP A 1 184 ? 15.24959  26.68879  4.29864   1.000 27.28473 ? 184 ASP A OD2   1 
ATOM   1418 N  N     . MET A 1 185 ? 14.38649  24.50562  -1.14027  1.000 18.48680 ? 185 MET A N     1 
ATOM   1419 C  CA    . MET A 1 185 ? 14.04846  24.70857  -2.54527  1.000 15.46448 ? 185 MET A CA    1 
ATOM   1420 C  C     . MET A 1 185 ? 12.63546  24.20056  -2.80923  1.000 16.75879 ? 185 MET A C     1 
ATOM   1421 O  O     . MET A 1 185 ? 12.29548  23.09157  -2.38118  1.000 15.15366 ? 185 MET A O     1 
ATOM   1422 C  CB    . MET A 1 185 ? 15.03745  23.99255  -3.45327  1.000 16.34148 ? 185 MET A CB    1 
ATOM   1423 C  CG    . MET A 1 185 ? 16.43944  24.58757  -3.43932  1.000 14.88367 ? 185 MET A CG    1 
ATOM   1424 S  SD    . MET A 1 185 ? 16.49042  26.28355  -4.05737  1.000 18.87813 ? 185 MET A SD    1 
ATOM   1425 C  CE    . MET A 1 185 ? 18.23442  26.65757  -3.89342  1.000 12.06021 ? 185 MET A CE    1 
ATOM   1426 N  N     . PRO A 1 186 ? 11.78944  24.97453  -3.49923  1.000 16.15683 ? 186 PRO A N     1 
ATOM   1427 C  CA    . PRO A 1 186 ? 10.38544  24.57351  -3.67319  1.000 12.76394 ? 186 PRO A CA    1 
ATOM   1428 C  C     . PRO A 1 186 ? 10.21243  23.30349  -4.49015  1.000 13.05627 ? 186 PRO A C     1 
ATOM   1429 O  O     . PRO A 1 186 ? 9.44745   22.41249  -4.10410  1.000 13.99791 ? 186 PRO A O     1 
ATOM   1430 C  CB    . PRO A 1 186 ? 9.75941   25.78348  -4.38121  1.000 16.76483 ? 186 PRO A CB    1 
ATOM   1431 C  CG    . PRO A 1 186 ? 10.90540  26.49347  -5.02426  1.000 14.86679 ? 186 PRO A CG    1 
ATOM   1432 C  CD    . PRO A 1 186 ? 12.07642  26.28151  -4.11328  1.000 14.62107 ? 186 PRO A CD    1 
ATOM   1433 N  N     . SER A 1 187 ? 10.91141  23.20546  -5.62116  1.000 12.90176 ? 187 SER A N     1 
ATOM   1434 C  CA    . SER A 1 187 ? 10.80840  22.01143  -6.45212  1.000 14.57739 ? 187 SER A CA    1 
ATOM   1435 C  C     . SER A 1 187 ? 11.50742  20.80445  -5.84110  1.000 14.93996 ? 187 SER A C     1 
ATOM   1436 O  O     . SER A 1 187 ? 11.35142  19.69244  -6.35806  1.000 15.14230 ? 187 SER A O     1 
ATOM   1437 C  CB    . SER A 1 187 ? 11.37437  22.28739  -7.84714  1.000 14.90176 ? 187 SER A CB    1 
ATOM   1438 O  OG    . SER A 1 187 ? 10.59635  23.25337  -8.53015  1.000 17.45703 ? 187 SER A OG    1 
ATOM   1439 N  N     . ALA A 1 188 ? 12.26944  20.99149  -4.76212  1.000 12.81876 ? 188 ALA A N     1 
ATOM   1440 C  CA    . ALA A 1 188 ? 12.93547  19.89852  -4.06810  1.000 13.92835 ? 188 ALA A CA    1 
ATOM   1441 C  C     . ALA A 1 188 ? 12.21250  19.50255  -2.78507  1.000 11.87996 ? 188 ALA A C     1 
ATOM   1442 O  O     . ALA A 1 188 ? 12.82752  18.90958  -1.89307  1.000 12.86467 ? 188 ALA A O     1 
ATOM   1443 C  CB    . ALA A 1 188 ? 14.38747  20.27154  -3.76314  1.000 13.56639 ? 188 ALA A CB    1 
ATOM   1444 N  N     . ALA A 1 189 ? 10.92750  19.81955  -2.67606  1.000 11.71356 ? 189 ALA A N     1 
ATOM   1445 C  CA    . ALA A 1 189 ? 10.17253  19.47658  -1.47803  1.000 12.06710 ? 189 ALA A CA    1 
ATOM   1446 C  C     . ALA A 1 189 ? 10.02754  17.96358  -1.37098  1.000 14.29065 ? 189 ALA A C     1 
ATOM   1447 O  O     . ALA A 1 189 ? 9.68352   17.30755  -2.36095  1.000 15.26768 ? 189 ALA A O     1 
ATOM   1448 C  CB    . ALA A 1 189 ? 8.79852   20.14156  -1.50402  1.000 15.75979 ? 189 ALA A CB    1 
ATOM   1449 N  N     . PRO A 1 190 ? 10.28257  17.37362  -0.19997  1.000 15.45485 ? 190 PRO A N     1 
ATOM   1450 C  CA    . PRO A 1 190 ? 10.20858  15.90762  -0.08992  1.000 14.50366 ? 190 PRO A CA    1 
ATOM   1451 C  C     . PRO A 1 190 ? 8.82058   15.34560  -0.34088  1.000 15.81248 ? 190 PRO A C     1 
ATOM   1452 O  O     . PRO A 1 190 ? 8.69858   14.19059  -0.76684  1.000 13.33563 ? 190 PRO A O     1 
ATOM   1453 C  CB    . PRO A 1 190 ? 10.67062  15.64167  1.35108   1.000 16.29662 ? 190 PRO A CB    1 
ATOM   1454 C  CG    . PRO A 1 190 ? 11.43661  16.86668  1.74502   1.000 13.84945 ? 190 PRO A CG    1 
ATOM   1455 C  CD    . PRO A 1 190 ? 10.76259  18.00166  1.04200   1.000 15.08332 ? 190 PRO A CD    1 
ATOM   1456 N  N     . ALA A 1 191 ? 7.76758   16.12860  -0.09288  1.000 17.78640 ? 191 ALA A N     1 
ATOM   1457 C  CA    . ALA A 1 191 ? 6.41158   15.62158  -0.27383  1.000 16.37271 ? 191 ALA A CA    1 
ATOM   1458 C  C     . ALA A 1 191 ? 6.08155   15.38754  -1.74282  1.000 15.96279 ? 191 ALA A C     1 
ATOM   1459 O  O     . ALA A 1 191 ? 5.27255   14.50752  -2.05978  1.000 18.02483 ? 191 ALA A O     1 
ATOM   1460 C  CB    . ALA A 1 191 ? 5.40159   16.58459  0.34916   1.000 15.31317 ? 191 ALA A CB    1 
ATOM   1461 N  N     . ALA A 1 192 ? 6.68853   16.15251  -2.64786  1.000 13.43821 ? 192 ALA A N     1 
ATOM   1462 C  CA    . ALA A 1 192 ? 6.43350   16.02147  -4.07485  1.000 17.91016 ? 192 ALA A CA    1 
ATOM   1463 C  C     . ALA A 1 192 ? 7.58749   15.38145  -4.83185  1.000 14.57532 ? 192 ALA A C     1 
ATOM   1464 O  O     . ALA A 1 192 ? 7.53046   15.29542  -6.06385  1.000 13.96967 ? 192 ALA A O     1 
ATOM   1465 C  CB    . ALA A 1 192 ? 6.11447   17.39345  -4.68288  1.000 19.42853 ? 192 ALA A CB    1 
ATOM   1466 N  N     . THR A 1 193 ? 8.63251   14.92748  -4.13386  1.000 14.83970 ? 193 THR A N     1 
ATOM   1467 C  CA    . THR A 1 193 ? 9.79550   14.32647  -4.77687  1.000 13.84262 ? 193 THR A CA    1 
ATOM   1468 C  C     . THR A 1 193 ? 10.10552  12.94349  -4.21483  1.000 11.74286 ? 193 THR A C     1 
ATOM   1469 O  O     . THR A 1 193 ? 11.21352  12.43450  -4.41484  1.000 11.86283 ? 193 THR A O     1 
ATOM   1470 C  CB    . THR A 1 193 ? 11.02449  15.23149  -4.64092  1.000 12.08959 ? 193 THR A CB    1 
ATOM   1471 O  OG1   . THR A 1 193 ? 11.27852  15.48653  -3.25393  1.000 13.32748 ? 193 THR A OG1   1 
ATOM   1472 C  CG2   . THR A 1 193 ? 10.79947  16.55146  -5.36095  1.000 14.76440 ? 193 THR A CG2   1 
ATOM   1473 N  N     . GLY A 1 194 ? 9.15454   12.32351  -3.51679  1.000 11.90614 ? 194 GLY A N     1 
ATOM   1474 C  CA    . GLY A 1 194 ? 9.38556   11.00452  -2.96976  1.000 10.84087 ? 194 GLY A CA    1 
ATOM   1475 C  C     . GLY A 1 194 ? 9.12755   9.89949   -3.97472  1.000 12.85323 ? 194 GLY A C     1 
ATOM   1476 O  O     . GLY A 1 194 ? 8.48253   10.08946  -5.00571  1.000 12.09129 ? 194 GLY A O     1 
ATOM   1477 N  N     . VAL A 1 195 ? 9.65056   8.71951   -3.65969  1.000 10.93477 ? 195 VAL A N     1 
ATOM   1478 C  CA    . VAL A 1 195 ? 9.47356   7.54348   -4.50765  1.000 10.32056 ? 195 VAL A CA    1 
ATOM   1479 C  C     . VAL A 1 195 ? 8.07356   6.98347   -4.28861  1.000 14.04332 ? 195 VAL A C     1 
ATOM   1480 O  O     . VAL A 1 195 ? 7.71859   6.62651   -3.15559  1.000 13.99381 ? 195 VAL A O     1 
ATOM   1481 C  CB    . VAL A 1 195 ? 10.54757  6.48150   -4.22664  1.000 12.93918 ? 195 VAL A CB    1 
ATOM   1482 C  CG1   . VAL A 1 195 ? 10.30056  5.24447   -5.07360  1.000 13.38586 ? 195 VAL A CG1   1 
ATOM   1483 C  CG2   . VAL A 1 195 ? 11.93556  7.04550   -4.48869  1.000 13.20661 ? 195 VAL A CG2   1 
ATOM   1484 N  N     . PRO A 1 196 ? 7.24954   6.89044   -5.32659  1.000 11.93829 ? 196 PRO A N     1 
ATOM   1485 C  CA    . PRO A 1 196 ? 5.88255   6.39543   -5.15254  1.000 13.93604 ? 196 PRO A CA    1 
ATOM   1486 C  C     . PRO A 1 196 ? 5.84056   4.87343   -5.09450  1.000 13.60736 ? 196 PRO A C     1 
ATOM   1487 O  O     . PRO A 1 196 ? 6.81256   4.17743   -5.38950  1.000 15.40736 ? 196 PRO A O     1 
ATOM   1488 C  CB    . PRO A 1 196 ? 5.16452   6.92039   -6.39854  1.000 14.88084 ? 196 PRO A CB    1 
ATOM   1489 C  CG    . PRO A 1 196 ? 6.23450   6.94936   -7.43657  1.000 11.96769 ? 196 PRO A CG    1 
ATOM   1490 C  CD    . PRO A 1 196 ? 7.51351   7.30940   -6.71361  1.000 12.65494 ? 196 PRO A CD    1 
ATOM   1491 N  N     . THR A 1 197 ? 4.67758   4.36544   -4.70146  1.000 17.04428 ? 197 THR A N     1 
ATOM   1492 C  CA    . THR A 1 197 ? 4.41359   2.93643   -4.66041  1.000 17.73102 ? 197 THR A CA    1 
ATOM   1493 C  C     . THR A 1 197 ? 3.55257   2.52739   -5.85138  1.000 16.10785 ? 197 THR A C     1 
ATOM   1494 O  O     . THR A 1 197 ? 3.03954   3.36336   -6.59839  1.000 17.79965 ? 197 THR A O     1 
ATOM   1495 C  CB    . THR A 1 197 ? 3.72862   2.55147   -3.34438  1.000 17.73082 ? 197 THR A CB    1 
ATOM   1496 O  OG1   . THR A 1 197 ? 2.52762   3.31746   -3.18538  1.000 18.40608 ? 197 THR A OG1   1 
ATOM   1497 C  CG2   . THR A 1 197 ? 4.65164   2.81651   -2.16541  1.000 17.02460 ? 197 THR A CG2   1 
ATOM   1498 N  N     . TRP A 1 198 ? 3.39557   1.21238   -6.02633  1.000 14.95786 ? 198 TRP A N     1 
ATOM   1499 C  CA    . TRP A 1 198 ? 2.62255   0.71234   -7.15830  1.000 19.99160 ? 198 TRP A CA    1 
ATOM   1500 C  C     . TRP A 1 198 ? 1.12856   0.96134   -6.99728  1.000 19.14367 ? 198 TRP A C     1 
ATOM   1501 O  O     . TRP A 1 198 ? 0.39053   0.87630   -7.98526  1.000 20.65814 ? 198 TRP A O     1 
ATOM   1502 C  CB    . TRP A 1 198 ? 2.88856   -0.78066  -7.37126  1.000 19.43161 ? 198 TRP A CB    1 
ATOM   1503 C  CG    . TRP A 1 198 ? 2.41159   -1.66363  -6.25723  1.000 17.29157 ? 198 TRP A CG    1 
ATOM   1504 C  CD1   . TRP A 1 198 ? 3.14062   -2.10359  -5.19123  1.000 17.17909 ? 198 TRP A CD1   1 
ATOM   1505 C  CD2   . TRP A 1 198 ? 1.10260   -2.22964  -6.10818  1.000 19.99525 ? 198 TRP A CD2   1 
ATOM   1506 N  NE1   . TRP A 1 198 ? 2.36564   -2.90157  -4.38419  1.000 19.48126 ? 198 TRP A NE1   1 
ATOM   1507 C  CE2   . TRP A 1 198 ? 1.11063   -2.99460  -4.92616  1.000 21.00558 ? 198 TRP A CE2   1 
ATOM   1508 C  CE3   . TRP A 1 198 ? -0.07542  -2.15867  -6.85816  1.000 19.26002 ? 198 TRP A CE3   1 
ATOM   1509 C  CZ2   . TRP A 1 198 ? -0.01335  -3.68359  -4.47511  1.000 20.38392 ? 198 TRP A CZ2   1 
ATOM   1510 C  CZ3   . TRP A 1 198 ? -1.19040  -2.84366  -6.40911  1.000 20.26341 ? 198 TRP A CZ3   1 
ATOM   1511 C  CH2   . TRP A 1 198 ? -1.15137  -3.59463  -5.22909  1.000 22.52549 ? 198 TRP A CH2   1 
ATOM   1512 N  N     . GLN A 1 199 ? 0.66358   1.26537   -5.78328  1.000 17.30301 ? 199 GLN A N     1 
ATOM   1513 C  CA    . GLN A 1 199 ? -0.74142  1.60637   -5.59526  1.000 19.04727 ? 199 GLN A CA    1 
ATOM   1514 C  C     . GLN A 1 199 ? -1.02644  3.05735   -5.95830  1.000 21.23067 ? 199 GLN A C     1 
ATOM   1515 O  O     . GLN A 1 199 ? -2.13645  3.37733   -6.39828  1.000 25.47366 ? 199 GLN A O     1 
ATOM   1516 C  CB    . GLN A 1 199 ? -1.16939  1.34641   -4.14924  1.000 20.44333 ? 199 GLN A CB    1 
ATOM   1517 C  CG    . GLN A 1 199 ? -0.99637  -0.08858  -3.67520  1.000 18.56980 ? 199 GLN A CG    1 
ATOM   1518 C  CD    . GLN A 1 199 ? 0.38965   -0.36055  -3.12322  1.000 21.64831 ? 199 GLN A CD    1 
ATOM   1519 O  OE1   . GLN A 1 199 ? 1.35563   0.31445   -3.47626  1.000 21.06810 ? 199 GLN A OE1   1 
ATOM   1520 N  NE2   . GLN A 1 199 ? 0.49167   -1.35352  -2.24619  1.000 27.18475 ? 199 GLN A NE2   1 
ATOM   1521 N  N     . GLU A 1 200 ? -0.04344  3.94337   -5.78234  1.000 19.01928 ? 200 GLU A N     1 
ATOM   1522 C  CA    . GLU A 1 200 ? -0.24446  5.35835   -6.07238  1.000 20.23718 ? 200 GLU A CA    1 
ATOM   1523 C  C     . GLU A 1 200 ? -0.24149  5.64931   -7.56639  1.000 19.61067 ? 200 GLU A C     1 
ATOM   1524 O  O     . GLU A 1 200 ? -0.95251  6.55429   -8.01840  1.000 23.84855 ? 200 GLU A O     1 
ATOM   1525 C  CB    . GLU A 1 200 ? 0.83455   6.19338   -5.38143  1.000 19.38038 ? 200 GLU A CB    1 
ATOM   1526 C  CG    . GLU A 1 200 ? 0.83158   6.08043   -3.86943  1.000 19.67025 ? 200 GLU A CG    1 
ATOM   1527 C  CD    . GLU A 1 200 ? 1.93959   6.88746   -3.22747  1.000 20.38485 ? 200 GLU A CD    1 
ATOM   1528 O  OE1   . GLU A 1 200 ? 2.92857   7.20544   -3.92151  1.000 20.27320 ? 200 GLU A OE1   1 
ATOM   1529 O  OE2   . GLU A 1 200 ? 1.81861   7.20949   -2.02848  1.000 27.21809 ? 200 GLU A OE2   1 
ATOM   1530 N  N     . VAL A 1 201 ? 0.54550   4.90329   -8.34539  1.000 20.98257 ? 201 VAL A N     1 
ATOM   1531 C  CA    . VAL A 1 201 ? 0.65346   5.18025   -9.77140  1.000 22.21136 ? 201 VAL A CA    1 
ATOM   1532 C  C     . VAL A 1 201 ? -0.61155  4.79222   -10.52536 1.000 24.00089 ? 201 VAL A C     1 
ATOM   1533 O  O     . VAL A 1 201 ? -0.83358  5.27418   -11.64237 1.000 25.06917 ? 201 VAL A O     1 
ATOM   1534 C  CB    . VAL A 1 201 ? 1.88146   4.46724   -10.36540 1.000 19.24533 ? 201 VAL A CB    1 
ATOM   1535 C  CG1   . VAL A 1 201 ? 3.16046   5.03827   -9.77544  1.000 18.63256 ? 201 VAL A CG1   1 
ATOM   1536 C  CG2   . VAL A 1 201 ? 1.79847   2.97225   -10.11735 1.000 20.93808 ? 201 VAL A CG2   1 
ATOM   1537 N  N     . GLY A 1 202 ? -1.44853  3.93323   -9.95031  1.000 22.35412 ? 202 GLY A N     1 
ATOM   1538 C  CA    . GLY A 1 202 ? -2.71754  3.56320   -10.55328 1.000 27.03105 ? 202 GLY A CA    1 
ATOM   1539 C  C     . GLY A 1 202 ? -2.92953  2.07819   -10.75223 1.000 26.59263 ? 202 GLY A C     1 
ATOM   1540 O  O     . GLY A 1 202 ? -4.03054  1.68017   -11.16119 1.000 23.84604 ? 202 GLY A O     1 
ATOM   1541 N  N     . PHE A 1 203 ? -1.93452  1.23421   -10.49022 1.000 22.24562 ? 203 PHE A N     1 
ATOM   1542 C  CA    . PHE A 1 203 ? -2.11751  -0.19980  -10.65917 1.000 23.18403 ? 203 PHE A CA    1 
ATOM   1543 C  C     . PHE A 1 203 ? -3.07049  -0.74677  -9.60414  1.000 27.07281 ? 203 PHE A C     1 
ATOM   1544 O  O     . PHE A 1 203 ? -3.02046  -0.35974  -8.43415  1.000 25.73909 ? 203 PHE A O     1 
ATOM   1545 C  CB    . PHE A 1 203 ? -0.77551  -0.92679  -10.58518 1.000 22.76506 ? 203 PHE A CB    1 
ATOM   1546 C  CG    . PHE A 1 203 ? 0.04547   -0.81282  -11.83620 1.000 20.86830 ? 203 PHE A CG    1 
ATOM   1547 C  CD1   . PHE A 1 203 ? -0.32955  -1.48286  -12.98917 1.000 20.11728 ? 203 PHE A CD1   1 
ATOM   1548 C  CD2   . PHE A 1 203 ? 1.19446   -0.04281  -11.86025 1.000 18.88192 ? 203 PHE A CD2   1 
ATOM   1549 C  CE1   . PHE A 1 203 ? 0.42342   -1.38288  -14.14219 1.000 19.31946 ? 203 PHE A CE1   1 
ATOM   1550 C  CE2   . PHE A 1 203 ? 1.95343   0.06116   -13.01127 1.000 19.50806 ? 203 PHE A CE2   1 
ATOM   1551 C  CZ    . PHE A 1 203 ? 1.56642   -0.61088  -14.15324 1.000 17.18811 ? 203 PHE A CZ    1 
ATOM   1552 N  N     . LYS A 1 204 ? -3.94649  -1.65779  -10.03009 1.000 25.39539 ? 204 LYS A N     1 
ATOM   1553 C  CA    . LYS A 1 204 ? -4.94247  -2.25478  -9.15405  1.000 25.95935 ? 204 LYS A CA    1 
ATOM   1554 C  C     . LYS A 1 204 ? -4.62145  -3.68976  -8.76102  1.000 24.49018 ? 204 LYS A C     1 
ATOM   1555 O  O     . LYS A 1 204 ? -5.29442  -4.23874  -7.88098  1.000 28.46509 ? 204 LYS A O     1 
ATOM   1556 C  CB    . LYS A 1 204 ? -6.32448  -2.20681  -9.82202  1.000 28.22108 ? 204 LYS A CB    1 
ATOM   1557 C  CG    . LYS A 1 204 ? -6.68250  -0.83883  -10.38606 1.000 28.81808 ? 204 LYS A CG    1 
ATOM   1558 C  CD    . LYS A 1 204 ? -8.04052  -0.84486  -11.06903 0.000 28.51074 ? 204 LYS A CD    1 
ATOM   1559 C  CE    . LYS A 1 204 ? -8.35954  0.51812   -11.66306 0.000 28.59223 ? 204 LYS A CE    1 
ATOM   1560 N  NZ    . LYS A 1 204 ? -9.71255  0.56009   -12.28104 0.000 27.90870 ? 204 LYS A NZ    1 
ATOM   1561 N  N     . GLU A 1 205 ? -3.61845  -4.30677  -9.38302  1.000 25.49485 ? 205 GLU A N     1 
ATOM   1562 C  CA    A GLU A 1 205 ? -3.21844  -5.67276  -9.09298  0.602 25.20800 ? 205 GLU A CA    1 
ATOM   1563 C  CA    B GLU A 1 205 ? -3.22644  -5.66576  -9.06798  0.398 25.19488 ? 205 GLU A CA    1 
ATOM   1564 C  C     . GLU A 1 205 ? -1.79842  -5.69473  -8.53301  1.000 20.86327 ? 205 GLU A C     1 
ATOM   1565 O  O     . GLU A 1 205 ? -0.93044  -4.97774  -9.03805  1.000 20.76275 ? 205 GLU A O     1 
ATOM   1566 C  CB    A GLU A 1 205 ? -3.28546  -6.53580  -10.36496 0.602 26.15115 ? 205 GLU A CB    1 
ATOM   1567 C  CB    B GLU A 1 205 ? -3.33246  -6.57380  -10.30296 0.398 26.13495 ? 205 GLU A CB    1 
ATOM   1568 C  CG    A GLU A 1 205 ? -3.46844  -8.02679  -10.12891 0.602 27.74956 ? 205 GLU A CG    1 
ATOM   1569 C  CG    B GLU A 1 205 ? -2.62349  -6.04083  -11.53499 0.398 25.41110 ? 205 GLU A CG    1 
ATOM   1570 C  CD    A GLU A 1 205 ? -4.91044  -8.46981  -10.29086 0.602 25.80318 ? 205 GLU A CD    1 
ATOM   1571 C  CD    B GLU A 1 205 ? -2.47450  -7.09086  -12.61696 0.398 26.20756 ? 205 GLU A CD    1 
ATOM   1572 O  OE1   A GLU A 1 205 ? -5.81143  -7.78980  -9.75587  0.602 30.12986 ? 205 GLU A OE1   1 
ATOM   1573 O  OE1   B GLU A 1 205 ? -2.68648  -8.28385  -12.31692 0.398 27.61459 ? 205 GLU A OE1   1 
ATOM   1574 O  OE2   A GLU A 1 205 ? -5.14445  -9.49483  -10.96583 0.602 24.65009 ? 205 GLU A OE2   1 
ATOM   1575 O  OE2   B GLU A 1 205 ? -2.14553  -6.72489  -13.76498 0.398 24.38253 ? 205 GLU A OE2   1 
ATOM   1576 N  N     . PRO A 1 206 ? -1.53040  -6.50170  -7.50300  1.000 21.14345 ? 206 PRO A N     1 
ATOM   1577 C  CA    . PRO A 1 206 ? -0.18338  -6.51967  -6.93402  1.000 21.42003 ? 206 PRO A CA    1 
ATOM   1578 C  C     . PRO A 1 206 ? 0.78360   -7.25969  -7.83902  1.000 18.29837 ? 206 PRO A C     1 
ATOM   1579 O  O     . PRO A 1 206 ? 0.37459   -8.11272  -8.64499  1.000 16.51754 ? 206 PRO A O     1 
ATOM   1580 C  CB    . PRO A 1 206 ? -0.37935  -7.26163  -5.59900  1.000 23.81825 ? 206 PRO A CB    1 
ATOM   1581 C  CG    . PRO A 1 206 ? -1.55535  -8.13665  -5.83795  1.000 21.96030 ? 206 PRO A CG    1 
ATOM   1582 C  CD    . PRO A 1 206 ? -2.46137  -7.35468  -6.74795  1.000 26.38016 ? 206 PRO A CD    1 
ATOM   1583 N  N     . PRO A 1 207 ? 2.07860   -6.96068  -7.74606  1.000 17.29810 ? 207 PRO A N     1 
ATOM   1584 C  CA    . PRO A 1 207 ? 3.06259   -7.70069  -8.54106  1.000 13.94617 ? 207 PRO A CA    1 
ATOM   1585 C  C     . PRO A 1 207 ? 3.28961   -9.09268  -7.97702  1.000 14.23874 ? 207 PRO A C     1 
ATOM   1586 O  O     . PRO A 1 207 ? 3.23364   -9.31564  -6.76501  1.000 16.16586 ? 207 PRO A O     1 
ATOM   1587 C  CB    . PRO A 1 207 ? 4.32659   -6.84168  -8.42811  1.000 13.30526 ? 207 PRO A CB    1 
ATOM   1588 C  CG    . PRO A 1 207 ? 4.17561   -6.14264  -7.11913  1.000 14.87820 ? 207 PRO A CG    1 
ATOM   1589 C  CD    . PRO A 1 207 ? 2.70161   -5.88865  -6.94910  1.000 16.83743 ? 207 PRO A CD    1 
ATOM   1590 N  N     . LEU A 1 208 ? 3.54860   -10.03770 -8.88000  1.000 9.95773  ? 208 LEU A N     1 
ATOM   1591 C  CA    . LEU A 1 208 ? 3.73662   -11.43369 -8.51096  1.000 11.50186 ? 208 LEU A CA    1 
ATOM   1592 C  C     . LEU A 1 208 ? 5.13962   -11.95269 -8.79197  1.000 10.29733 ? 208 LEU A C     1 
ATOM   1593 O  O     . LEU A 1 208 ? 5.40863   -13.13168 -8.53294  1.000 11.83402 ? 208 LEU A O     1 
ATOM   1594 C  CB    . LEU A 1 208 ? 2.71261   -12.31672 -9.23691  1.000 10.80832 ? 208 LEU A CB    1 
ATOM   1595 C  CG    . LEU A 1 208 ? 1.23862   -11.99872 -8.97089  1.000 14.11190 ? 208 LEU A CG    1 
ATOM   1596 C  CD1   . LEU A 1 208 ? 0.32961   -12.96175 -9.72384  1.000 12.17048 ? 208 LEU A CD1   1 
ATOM   1597 C  CD2   . LEU A 1 208 ? 0.94265   -12.03268 -7.47888  1.000 13.21731 ? 208 LEU A CD2   1 
ATOM   1598 N  N     . THR A 1 209 ? 6.03760   -11.11769 -9.30802  1.000 11.25751 ? 209 THR A N     1 
ATOM   1599 C  CA    . THR A 1 209 ? 7.38260   -11.57069 -9.62003  1.000 8.44911  ? 209 THR A CA    1 
ATOM   1600 C  C     . THR A 1 209 ? 8.17463   -11.83165 -8.34104  1.000 8.81128  ? 209 THR A C     1 
ATOM   1601 O  O     . THR A 1 209 ? 7.86165   -11.31662 -7.26405  1.000 12.90856 ? 209 THR A O     1 
ATOM   1602 C  CB    . THR A 1 209 ? 8.10757   -10.54071 -10.48908 1.000 10.67953 ? 209 THR A CB    1 
ATOM   1603 O  OG1   . THR A 1 209 ? 9.39357   -11.04971 -10.86709 1.000 10.74073 ? 209 THR A OG1   1 
ATOM   1604 C  CG2   . THR A 1 209 ? 8.28658   -9.23369  -9.73012  1.000 9.91572  ? 209 THR A CG2   1 
ATOM   1605 N  N     . VAL A 1 210 ? 9.21663   -12.65164 -8.47304  1.000 9.04910  ? 210 VAL A N     1 
ATOM   1606 C  CA    . VAL A 1 210 ? 10.07566  -13.01960 -7.35604  1.000 9.65893  ? 210 VAL A CA    1 
ATOM   1607 C  C     . VAL A 1 210 ? 11.44165  -12.35259 -7.45009  1.000 10.28269 ? 210 VAL A C     1 
ATOM   1608 O  O     . VAL A 1 210 ? 12.34667  -12.68756 -6.67810  1.000 10.85659 ? 210 VAL A O     1 
ATOM   1609 C  CB    . VAL A 1 210 ? 10.22167  -14.54560 -7.24500  1.000 8.63926  ? 210 VAL A CB    1 
ATOM   1610 C  CG1   . VAL A 1 210 ? 8.85968   -15.19760 -7.06395  1.000 8.16889  ? 210 VAL A CG1   1 
ATOM   1611 C  CG2   . VAL A 1 210 ? 10.92765  -15.10363 -8.47200  1.000 11.57226 ? 210 VAL A CG2   1 
ATOM   1612 N  N     . PHE A 1 211 ? 11.61662  -11.41562 -8.37812  1.000 8.80221  ? 211 PHE A N     1 
ATOM   1613 C  CA    . PHE A 1 211 ? 12.88561  -10.73262 -8.59017  1.000 11.20245 ? 211 PHE A CA    1 
ATOM   1614 C  C     . PHE A 1 211 ? 12.74361  -9.28361  -8.14721  1.000 11.52683 ? 211 PHE A C     1 
ATOM   1615 O  O     . PHE A 1 211 ? 11.90859  -8.54663  -8.68322  1.000 10.75962 ? 211 PHE A O     1 
ATOM   1616 C  CB    . PHE A 1 211 ? 13.30758  -10.81466 -10.05818 1.000 11.28120 ? 211 PHE A CB    1 
ATOM   1617 C  CG    . PHE A 1 211 ? 13.47058  -12.21967 -10.56114 1.000 11.42783 ? 211 PHE A CG    1 
ATOM   1618 C  CD1   . PHE A 1 211 ? 14.11561  -13.17264 -9.79112  1.000 11.66549 ? 211 PHE A CD1   1 
ATOM   1619 C  CD2   . PHE A 1 211 ? 12.96556  -12.59171 -11.79512 1.000 12.17539 ? 211 PHE A CD2   1 
ATOM   1620 C  CE1   . PHE A 1 211 ? 14.26561  -14.46866 -10.24609 1.000 11.66449 ? 211 PHE A CE1   1 
ATOM   1621 C  CE2   . PHE A 1 211 ? 13.11056  -13.88773 -12.25708 1.000 10.78588 ? 211 PHE A CE2   1 
ATOM   1622 C  CZ    . PHE A 1 211 ? 13.76158  -14.82670 -11.48107 1.000 11.14694 ? 211 PHE A CZ    1 
ATOM   1623 N  N     . LYS A 1 212 ? 13.55463  -8.88157  -7.17324  1.000 10.56307 ? 212 LYS A N     1 
ATOM   1624 C  CA    . LYS A 1 212 ? 13.50263  -7.53755  -6.61628  1.000 11.60893 ? 212 LYS A CA    1 
ATOM   1625 C  C     . LYS A 1 212 ? 14.54061  -6.65557  -7.29633  1.000 9.09465  ? 212 LYS A C     1 
ATOM   1626 O  O     . LYS A 1 212 ? 15.67561  -7.07956  -7.52934  1.000 11.55065 ? 212 LYS A O     1 
ATOM   1627 C  CB    . LYS A 1 212 ? 13.73966  -7.56251  -5.10329  1.000 12.14361 ? 212 LYS A CB    1 
ATOM   1628 C  CG    . LYS A 1 212 ? 12.92969  -8.62349  -4.36624  1.000 15.59127 ? 212 LYS A CG    1 
ATOM   1629 C  CD    . LYS A 1 212 ? 11.44868  -8.54451  -4.71421  1.000 16.28448 ? 212 LYS A CD    1 
ATOM   1630 C  CE    . LYS A 1 212 ? 10.73669  -7.45949  -3.92623  0.000 13.12858 ? 212 LYS A CE    1 
ATOM   1631 N  NZ    . LYS A 1 212 ? 10.47272  -7.88045  -2.52321  0.000 13.39057 ? 212 LYS A NZ    1 
ATOM   1632 N  N     . GLY A 1 213 ? 14.14359  -5.42358  -7.61436  1.000 8.87002  ? 213 GLY A N     1 
ATOM   1633 C  CA    . GLY A 1 213 ? 15.02657  -4.51259  -8.30641  1.000 9.81222  ? 213 GLY A CA    1 
ATOM   1634 C  C     . GLY A 1 213 ? 16.01158  -3.82256  -7.38245  1.000 7.80575  ? 213 GLY A C     1 
ATOM   1635 O  O     . GLY A 1 213 ? 15.95761  -3.94052  -6.15844  1.000 10.41857 ? 213 GLY A O     1 
ATOM   1636 N  N     . GLY A 1 214 ? 16.93457  -3.08757  -7.99749  1.000 7.25732  ? 214 GLY A N     1 
ATOM   1637 C  CA    . GLY A 1 214 ? 17.90958  -2.32654  -7.24453  1.000 8.90700  ? 214 GLY A CA    1 
ATOM   1638 C  C     . GLY A 1 214 ? 19.34757  -2.72053  -7.50655  1.000 8.61891  ? 214 GLY A C     1 
ATOM   1639 O  O     . GLY A 1 214 ? 19.63057  -3.85854  -7.89352  1.000 8.09317  ? 214 GLY A O     1 
ATOM   1640 N  N     . GLU A 1 215 ? 20.26757  -1.77652  -7.29560  1.000 9.26200  ? 215 GLU A N     1 
ATOM   1641 C  CA    . GLU A 1 215 ? 21.68657  -2.06251  -7.47962  1.000 8.08428  ? 215 GLU A CA    1 
ATOM   1642 C  C     . GLU A 1 215 ? 22.17860  -3.09548  -6.47260  1.000 7.70759  ? 215 GLU A C     1 
ATOM   1643 O  O     . GLU A 1 215 ? 23.03060  -3.93148  -6.79759  1.000 7.27353  ? 215 GLU A O     1 
ATOM   1644 C  CB    . GLU A 1 215 ? 22.49656  -0.77050  -7.36168  1.000 7.56968  ? 215 GLU A CB    1 
ATOM   1645 C  CG    . GLU A 1 215 ? 24.00056  -0.96150  -7.43970  1.000 7.53432  ? 215 GLU A CG    1 
ATOM   1646 C  CD    . GLU A 1 215 ? 24.76756  0.30352   -7.10676  1.000 8.87856  ? 215 GLU A CD    1 
ATOM   1647 O  OE1   . GLU A 1 215 ? 24.13056  1.29953   -6.70678  1.000 8.94224  ? 215 GLU A OE1   1 
ATOM   1648 O  OE2   . GLU A 1 215 ? 26.00856  0.30053   -7.24578  1.000 8.28485  ? 215 GLU A OE2   1 
ATOM   1649 N  N     . THR A 1 216 ? 21.65062  -3.05545  -5.24659  1.000 8.50601  ? 216 THR A N     1 
ATOM   1650 C  CA    . THR A 1 216 ? 22.09865  -3.98741  -4.21557  1.000 11.15483 ? 216 THR A CA    1 
ATOM   1651 C  C     . THR A 1 216 ? 21.74066  -5.42443  -4.57552  1.000 10.26820 ? 216 THR A C     1 
ATOM   1652 O  O     . THR A 1 216 ? 22.56167  -6.33542  -4.41551  1.000 9.10845  ? 216 THR A O     1 
ATOM   1653 C  CB    . THR A 1 216 ? 21.49168  -3.60938  -2.86357  1.000 12.67855 ? 216 THR A CB    1 
ATOM   1654 O  OG1   . THR A 1 216 ? 21.77767  -2.23537  -2.57662  1.000 14.31822 ? 216 THR A OG1   1 
ATOM   1655 C  CG2   . THR A 1 216 ? 22.07071  -4.48134  -1.75856  1.000 13.79379 ? 216 THR A CG2   1 
ATOM   1656 N  N     . GLU A 1 217 ? 20.51665  -5.64745  -5.05949  1.000 10.19083 ? 217 GLU A N     1 
ATOM   1657 C  CA    . GLU A 1 217 ? 20.12065  -6.98947  -5.47244  1.000 10.39230 ? 217 GLU A CA    1 
ATOM   1658 C  C     . GLU A 1 217 ? 20.88263  -7.44450  -6.70944  1.000 8.51186  ? 217 GLU A C     1 
ATOM   1659 O  O     . GLU A 1 217 ? 21.13763  -8.64350  -6.87141  1.000 11.23323 ? 217 GLU A O     1 
ATOM   1660 C  CB    . GLU A 1 217 ? 18.61365  -7.03949  -5.72441  1.000 8.96961  ? 217 GLU A CB    1 
ATOM   1661 C  CG    . GLU A 1 217 ? 17.77167  -6.95545  -4.46139  1.000 12.38536 ? 217 GLU A CG    1 
ATOM   1662 C  CD    . GLU A 1 217 ? 17.87170  -8.20543  -3.60635  1.000 13.69854 ? 217 GLU A CD    1 
ATOM   1663 O  OE1   . GLU A 1 217 ? 18.18970  -9.28144  -4.15633  1.000 14.19663 ? 217 GLU A OE1   1 
ATOM   1664 O  OE2   . GLU A 1 217 ? 17.63372  -8.11139  -2.38435  1.000 20.58061 ? 217 GLU A OE2   1 
ATOM   1665 N  N     . ALA A 1 218 ? 21.25260  -6.51052  -7.58848  1.000 8.24148  ? 218 ALA A N     1 
ATOM   1666 C  CA    . ALA A 1 218 ? 22.04658  -6.86755  -8.75848  1.000 10.01243 ? 218 ALA A CA    1 
ATOM   1667 C  C     . ALA A 1 218 ? 23.43859  -7.33353  -8.35050  1.000 10.25993 ? 218 ALA A C     1 
ATOM   1668 O  O     . ALA A 1 218 ? 23.92959  -8.35854  -8.83848  1.000 9.23714  ? 218 ALA A O     1 
ATOM   1669 C  CB    . ALA A 1 218 ? 22.13455  -5.68058  -9.71752  1.000 9.74130  ? 218 ALA A CB    1 
ATOM   1670 N  N     . LEU A 1 219 ? 24.09160  -6.58650  -7.45654  1.000 9.66597  ? 219 LEU A N     1 
ATOM   1671 C  CA    . LEU A 1 219 ? 25.41262  -6.98147  -6.97955  1.000 10.22271 ? 219 LEU A CA    1 
ATOM   1672 C  C     . LEU A 1 219 ? 25.35864  -8.28445  -6.19251  1.000 10.26663 ? 219 LEU A C     1 
ATOM   1673 O  O     . LEU A 1 219 ? 26.32065  -9.06144  -6.21751  1.000 11.32541 ? 219 LEU A O     1 
ATOM   1674 C  CB    . LEU A 1 219 ? 26.01663  -5.86744  -6.12360  1.000 11.32116 ? 219 LEU A CB    1 
ATOM   1675 C  CG    . LEU A 1 219 ? 26.28860  -4.53546  -6.82764  1.000 7.92291  ? 219 LEU A CG    1 
ATOM   1676 C  CD1   . LEU A 1 219 ? 26.71261  -3.47143  -5.82469  1.000 7.65454  ? 219 LEU A CD1   1 
ATOM   1677 C  CD2   . LEU A 1 219 ? 27.34758  -4.70748  -7.90466  1.000 10.21973 ? 219 LEU A CD2   1 
ATOM   1678 N  N     . ALA A 1 220 ? 24.25066  -8.54043  -5.49248  1.000 9.77060  ? 220 ALA A N     1 
ATOM   1679 C  CA    . ALA A 1 220 ? 24.11169  -9.79741  -4.76444  1.000 10.53598 ? 220 ALA A CA    1 
ATOM   1680 C  C     . ALA A 1 220 ? 23.95568  -10.97144 -5.72140  1.000 10.07301 ? 220 ALA A C     1 
ATOM   1681 O  O     . ALA A 1 220 ? 24.46869  -12.06543 -5.45938  1.000 11.26060 ? 220 ALA A O     1 
ATOM   1682 C  CB    . ALA A 1 220 ? 22.92271  -9.72039  -3.80642  1.000 8.67923  ? 220 ALA A CB    1 
ATOM   1683 N  N     . ARG A 1 221 ? 23.25391  -10.76335 -6.83734  1.000 9.47721  ? 221 ARG A N     1 
ATOM   1684 C  CA    . ARG A 1 221 ? 23.11982  -11.82297 -7.82922  1.000 11.63640 ? 221 ARG A CA    1 
ATOM   1685 C  C     . ARG A 1 221 ? 24.41398  -12.02592 -8.60521  1.000 10.09434 ? 221 ARG A C     1 
ATOM   1686 O  O     . ARG A 1 221 ? 24.68264  -13.13444 -9.08243  1.000 9.19308  ? 221 ARG A O     1 
ATOM   1687 C  CB    . ARG A 1 221 ? 21.96891  -11.50516 -8.78256  1.000 9.87873  ? 221 ARG A CB    1 
ATOM   1688 C  CG    . ARG A 1 221 ? 21.48961  -12.69798 -9.58752  1.000 12.73996 ? 221 ARG A CG    1 
ATOM   1689 C  CD    . ARG A 1 221 ? 19.98128  -12.82228 -9.50683  1.000 10.37220 ? 221 ARG A CD    1 
ATOM   1690 N  NE    . ARG A 1 221 ? 19.53431  -14.18967 -9.73843  1.000 12.48028 ? 221 ARG A NE    1 
ATOM   1691 C  CZ    . ARG A 1 221 ? 18.30028  -14.61917 -9.51465  1.000 14.78352 ? 221 ARG A CZ    1 
ATOM   1692 N  NH1   . ARG A 1 221 ? 17.35936  -13.80939 -9.05723  1.000 18.28325 ? 221 ARG A NH1   1 
ATOM   1693 N  NH2   . ARG A 1 221 ? 18.00315  -15.89338 -9.75344  1.000 21.14012 ? 221 ARG A NH2   1 
ATOM   1694 N  N     . LEU A 1 222 ? 25.22361  -10.97353 -8.73943  1.000 9.88480  ? 222 LEU A N     1 
ATOM   1695 C  CA    . LEU A 1 222 ? 26.50560  -11.10154 -9.42345  1.000 9.30686  ? 222 LEU A CA    1 
ATOM   1696 C  C     . LEU A 1 222 ? 27.46662  -11.97150 -8.62144  1.000 10.48781 ? 222 LEU A C     1 
ATOM   1697 O  O     . LEU A 1 222 ? 28.09062  -12.88952 -9.16543  1.000 12.51275 ? 222 LEU A O     1 
ATOM   1698 C  CB    . LEU A 1 222 ? 27.10658  -9.71654  -9.66750  1.000 10.84376 ? 222 LEU A CB    1 
ATOM   1699 C  CG    . LEU A 1 222 ? 28.37356  -9.64955  -10.52253 1.000 12.06154 ? 222 LEU A CG    1 
ATOM   1700 C  CD1   . LEU A 1 222 ? 28.07154  -10.04660 -11.95851 1.000 10.93953 ? 222 LEU A CD1   1 
ATOM   1701 C  CD2   . LEU A 1 222 ? 28.98955  -8.26055  -10.46259 1.000 13.92163 ? 222 LEU A CD2   1 
ATOM   1702 N  N     . GLU A 1 223 ? 27.59165  -11.69946 -7.31945  1.000 9.65737  ? 223 GLU A N     1 
ATOM   1703 C  CA    . GLU A 1 223 ? 28.49167  -12.48543 -6.48245  1.000 12.52068 ? 223 GLU A CA    1 
ATOM   1704 C  C     . GLU A 1 223 ? 28.01469  -13.92743 -6.35440  1.000 12.46324 ? 223 GLU A C     1 
ATOM   1705 O  O     . GLU A 1 223 ? 28.83169  -14.85442 -6.31539  1.000 10.63744 ? 223 GLU A O     1 
ATOM   1706 C  CB    . GLU A 1 223 ? 28.62370  -11.84039 -5.10247  1.000 11.24646 ? 223 GLU A CB    1 
ATOM   1707 C  CG    . GLU A 1 223 ? 29.13368  -10.40438 -5.11953  1.000 13.72092 ? 223 GLU A CG    1 
ATOM   1708 C  CD    . GLU A 1 223 ? 30.61968  -10.30338 -5.40956  1.000 12.32948 ? 223 GLU A CD    1 
ATOM   1709 O  OE1   . GLU A 1 223 ? 31.28968  -11.35338 -5.50454  1.000 16.64277 ? 223 GLU A OE1   1 
ATOM   1710 O  OE2   . GLU A 1 223 ? 31.12167  -9.16638  -5.54061  1.000 9.70033  ? 223 GLU A OE2   1 
ATOM   1711 N  N     . ALA A 1 224 ? 26.69669  -14.13544 -6.29036  1.000 12.16897 ? 224 ALA A N     1 
ATOM   1712 C  CA    . ALA A 1 224 ? 26.16770  -15.48944 -6.16431  1.000 13.67913 ? 224 ALA A CA    1 
ATOM   1713 C  C     . ALA A 1 224 ? 26.49568  -16.33747 -7.38629  1.000 14.92795 ? 224 ALA A C     1 
ATOM   1714 O  O     . ALA A 1 224 ? 26.66870  -17.55547 -7.26826  1.000 15.42947 ? 224 ALA A O     1 
ATOM   1715 C  CB    . ALA A 1 224 ? 24.65671  -15.44444 -5.93628  1.000 15.06609 ? 224 ALA A CB    1 
ATOM   1716 N  N     . ALA A 1 225 ? 26.58665  -15.71651 -8.56331  1.000 12.72261 ? 225 ALA A N     1 
ATOM   1717 C  CA    . ALA A 1 225 ? 26.94363  -16.45554 -9.76630  1.000 11.26283 ? 225 ALA A CA    1 
ATOM   1718 C  C     . ALA A 1 225 ? 28.43763  -16.74653 -9.83632  1.000 13.26398 ? 225 ALA A C     1 
ATOM   1719 O  O     . ALA A 1 225 ? 28.83763  -17.77555 -10.39230 1.000 14.77105 ? 225 ALA A O     1 
ATOM   1720 C  CB    . ALA A 1 225 ? 26.50060  -15.68458 -11.01031 1.000 10.46832 ? 225 ALA A CB    1 
ATOM   1721 N  N     . PHE A 1 226 ? 29.26864  -15.86751 -9.27936  1.000 13.23296 ? 226 PHE A N     1 
ATOM   1722 C  CA    . PHE A 1 226 ? 30.71564  -16.02250 -9.31139  1.000 12.26265 ? 226 PHE A CA    1 
ATOM   1723 C  C     . PHE A 1 226 ? 31.26067  -16.78546 -8.10838  1.000 14.61065 ? 226 PHE A C     1 
ATOM   1724 O  O     . PHE A 1 226 ? 32.48268  -16.88044 -7.95440  1.000 11.41362 ? 226 PHE A O     1 
ATOM   1725 C  CB    . PHE A 1 226 ? 31.39263  -14.65250 -9.40645  1.000 10.43391 ? 226 PHE A CB    1 
ATOM   1726 C  CG    . PHE A 1 226 ? 31.38559  -14.06654 -10.79046 1.000 10.76477 ? 226 PHE A CG    1 
ATOM   1727 C  CD1   . PHE A 1 226 ? 30.28358  -13.37256 -11.25846 1.000 11.43710 ? 226 PHE A CD1   1 
ATOM   1728 C  CD2   . PHE A 1 226 ? 32.48458  -14.20756 -11.62148 1.000 9.84331  ? 226 PHE A CD2   1 
ATOM   1729 C  CE1   . PHE A 1 226 ? 30.27555  -12.83160 -12.53048 1.000 10.99934 ? 226 PHE A CE1   1 
ATOM   1730 C  CE2   . PHE A 1 226 ? 32.48355  -13.66859 -12.89350 1.000 8.70323  ? 226 PHE A CE2   1 
ATOM   1731 C  CZ    . PHE A 1 226 ? 31.37753  -12.98062 -13.34750 1.000 10.36752 ? 226 PHE A CZ    1 
ATOM   1732 N  N     . GLN A 1 227 ? 30.38969  -17.32944 -7.25434  1.000 16.26558 ? 227 GLN A N     1 
ATOM   1733 C  CA    . GLN A 1 227 ? 30.86372  -18.14340 -6.14133  1.000 16.41068 ? 227 GLN A CA    1 
ATOM   1734 C  C     . GLN A 1 227 ? 31.39272  -19.49541 -6.60330  1.000 15.44679 ? 227 GLN A C     1 
ATOM   1735 O  O     . GLN A 1 227 ? 32.08075  -20.17338 -5.83429  1.000 14.71454 ? 227 GLN A O     1 
ATOM   1736 C  CB    . GLN A 1 227 ? 29.74875  -18.33838 -5.11230  1.000 16.12808 ? 227 GLN A CB    1 
ATOM   1737 C  CG    . GLN A 1 227 ? 29.54676  -17.14635 -4.19433  1.000 19.92407 ? 227 GLN A CG    1 
ATOM   1738 C  CD    . GLN A 1 227 ? 28.43478  -17.36433 -3.18830  1.000 20.96884 ? 227 GLN A CD    1 
ATOM   1739 O  OE1   . GLN A 1 227 ? 28.28579  -16.59930 -2.23532  1.000 16.27291 ? 227 GLN A OE1   1 
ATOM   1740 N  NE2   . GLN A 1 227 ? 27.64478  -18.41134 -3.39825  1.000 22.01587 ? 227 GLN A NE2   1 
ATOM   1741 N  N     . ASP A 1 228 ? 31.08470  -19.89745 -7.83728  1.000 14.43293 ? 228 ASP A N     1 
ATOM   1742 C  CA    . ASP A 1 228 ? 31.60670  -21.12247 -8.44025  1.000 15.88036 ? 228 ASP A CA    1 
ATOM   1743 C  C     . ASP A 1 228 ? 32.30167  -20.73450 -9.73928  1.000 13.14288 ? 228 ASP A C     1 
ATOM   1744 O  O     . ASP A 1 228 ? 31.65965  -20.65654 -10.79827 1.000 11.20517 ? 228 ASP A O     1 
ATOM   1745 C  CB    . ASP A 1 228 ? 30.49270  -22.13748 -8.68720  1.000 14.11461 ? 228 ASP A CB    1 
ATOM   1746 C  CG    . ASP A 1 228 ? 31.01670  -23.47449 -9.17717  1.000 17.17842 ? 228 ASP A CG    1 
ATOM   1747 O  OD1   . ASP A 1 228 ? 32.24870  -23.67848 -9.16119  1.000 19.52430 ? 228 ASP A OD1   1 
ATOM   1748 O  OD2   . ASP A 1 228 ? 30.19270  -24.32351 -9.57813  1.000 20.21922 ? 228 ASP A OD2   1 
ATOM   1749 N  N     . PRO A 1 229 ? 33.61267  -20.47549 -9.70632  1.000 14.05039 ? 229 PRO A N     1 
ATOM   1750 C  CA    . PRO A 1 229 ? 34.31064  -20.07452 -10.93834 1.000 12.75685 ? 229 PRO A CA    1 
ATOM   1751 C  C     . PRO A 1 229 ? 34.33362  -21.15455 -12.00531 1.000 12.74157 ? 229 PRO A C     1 
ATOM   1752 O  O     . PRO A 1 229 ? 34.52460  -20.83159 -13.18432 1.000 12.90024 ? 229 PRO A O     1 
ATOM   1753 C  CB    . PRO A 1 229 ? 35.72565  -19.73849 -10.44738 1.000 14.38921 ? 229 PRO A CB    1 
ATOM   1754 C  CG    . PRO A 1 229 ? 35.87668  -20.50845 -9.17636  1.000 14.65299 ? 229 PRO A CG    1 
ATOM   1755 C  CD    . PRO A 1 229 ? 34.51469  -20.52145 -8.54433  1.000 14.62274 ? 229 PRO A CD    1 
ATOM   1756 N  N     . LYS A 1 230 ? 34.14864  -22.42454 -11.63327 1.000 13.94592 ? 230 LYS A N     1 
ATOM   1757 C  CA    . LYS A 1 230 ? 34.06263  -23.47857 -12.64023 1.000 14.36122 ? 230 LYS A CA    1 
ATOM   1758 C  C     . LYS A 1 230 ? 32.79061  -23.34861 -13.46821 1.000 12.68285 ? 230 LYS A C     1 
ATOM   1759 O  O     . LYS A 1 230 ? 32.80559  -23.59065 -14.68120 1.000 11.04467 ? 230 LYS A O     1 
ATOM   1760 C  CB    . LYS A 1 230 ? 34.12765  -24.85455 -11.97519 1.000 17.70616 ? 230 LYS A CB    1 
ATOM   1761 C  CG    . LYS A 1 230 ? 35.46666  -25.55855 -12.12920 1.000 18.97840 ? 230 LYS A CG    1 
ATOM   1762 C  CD    . LYS A 1 230 ? 36.46867  -25.10051 -11.08424 1.000 24.18009 ? 230 LYS A CD    1 
ATOM   1763 C  CE    . LYS A 1 230 ? 36.37271  -25.94547 -9.82421  0.359 17.99025 ? 230 LYS A CE    1 
ATOM   1764 N  NZ    . LYS A 1 230 ? 36.71971  -27.36948 -10.09517 0.309 18.18321 ? 230 LYS A NZ    1 
ATOM   1765 N  N     . TRP A 1 231 ? 31.68162  -22.96560 -12.83220 1.000 10.18756 ? 231 TRP A N     1 
ATOM   1766 C  CA    . TRP A 1 231 ? 30.41860  -22.83863 -13.55418 1.000 10.79206 ? 231 TRP A CA    1 
ATOM   1767 C  C     . TRP A 1 231 ? 30.44357  -21.64966 -14.50721 1.000 10.61330 ? 231 TRP A C     1 
ATOM   1768 O  O     . TRP A 1 231 ? 29.87555  -21.71470 -15.60320 1.000 11.32754 ? 231 TRP A O     1 
ATOM   1769 C  CB    . TRP A 1 231 ? 29.26262  -22.71061 -12.56216 1.000 11.07555 ? 231 TRP A CB    1 
ATOM   1770 C  CG    . TRP A 1 231 ? 27.91961  -22.56964 -13.21213 1.000 8.40992  ? 231 TRP A CG    1 
ATOM   1771 C  CD1   . TRP A 1 231 ? 27.09861  -23.57966 -13.62408 1.000 9.37636  ? 231 TRP A CD1   1 
ATOM   1772 C  CD2   . TRP A 1 231 ? 27.23759  -21.34765 -13.51815 1.000 8.62534  ? 231 TRP A CD2   1 
ATOM   1773 N  NE1   . TRP A 1 231 ? 25.94959  -23.06168 -14.17108 1.000 10.29845 ? 231 TRP A NE1   1 
ATOM   1774 C  CE2   . TRP A 1 231 ? 26.01058  -21.69468 -14.11812 1.000 9.21590  ? 231 TRP A CE2   1 
ATOM   1775 C  CE3   . TRP A 1 231 ? 27.54659  -19.99565 -13.34520 1.000 9.00464  ? 231 TRP A CE3   1 
ATOM   1776 C  CZ2   . TRP A 1 231 ? 25.09257  -20.73770 -14.54713 1.000 9.47519  ? 231 TRP A CZ2   1 
ATOM   1777 C  CZ3   . TRP A 1 231 ? 26.63357  -19.04667 -13.77121 1.000 9.76184  ? 231 TRP A CZ3   1 
ATOM   1778 C  CH2   . TRP A 1 231 ? 25.42156  -19.42269 -14.36417 1.000 7.93984  ? 231 TRP A CH2   1 
ATOM   1779 N  N     . VAL A 1 232 ? 31.09957  -20.55764 -14.11026 1.000 10.13286 ? 232 VAL A N     1 
ATOM   1780 C  CA    . VAL A 1 232 ? 31.16755  -19.37667 -14.96630 1.000 10.32770 ? 232 VAL A CA    1 
ATOM   1781 C  C     . VAL A 1 232 ? 32.04852  -19.64270 -16.18031 1.000 8.75315  ? 232 VAL A C     1 
ATOM   1782 O  O     . VAL A 1 232 ? 31.73350  -19.21873 -17.29931 1.000 7.09742  ? 232 VAL A O     1 
ATOM   1783 C  CB    . VAL A 1 232 ? 31.66655  -18.16564 -14.15734 1.000 9.62215  ? 232 VAL A CB    1 
ATOM   1784 C  CG1   . VAL A 1 232 ? 31.82653  -16.94866 -15.05839 1.000 8.74511  ? 232 VAL A CG1   1 
ATOM   1785 C  CG2   . VAL A 1 232 ? 30.71258  -17.86161 -13.01633 1.000 10.23837 ? 232 VAL A CG2   1 
ATOM   1786 N  N     . ALA A 1 233 ? 33.16153  -20.35268 -15.98531 1.000 12.60662 ? 233 ALA A N     1 
ATOM   1787 C  CA    . ALA A 1 233 ? 34.09951  -20.58271 -17.08032 1.000 14.10373 ? 233 ALA A CA    1 
ATOM   1788 C  C     . ALA A 1 233 ? 33.51550  -21.53074 -18.12128 1.000 11.09341 ? 233 ALA A C     1 
ATOM   1789 O  O     . ALA A 1 233 ? 33.61047  -21.27878 -19.32829 1.000 11.16208 ? 233 ALA A O     1 
ATOM   1790 C  CB    . ALA A 1 233 ? 35.41953  -21.12768 -16.53333 1.000 11.00466 ? 233 ALA A CB    1 
ATOM   1791 N  N     . GLY A 1 234 ? 32.90751  -22.62674 -17.67524 1.000 13.52029 ? 234 GLY A N     1 
ATOM   1792 C  CA    . GLY A 1 234 ? 32.38150  -23.61977 -18.59119 1.000 11.85411 ? 234 GLY A CA    1 
ATOM   1793 C  C     . GLY A 1 234 ? 30.94349  -23.37479 -19.00017 1.000 11.71530 ? 234 GLY A C     1 
ATOM   1794 O  O     . GLY A 1 234 ? 30.24849  -24.30081 -19.42813 1.000 14.26738 ? 234 GLY A O     1 
ATOM   1795 N  N     . PHE A 1 235 ? 30.48949  -22.13079 -18.87420 1.000 11.01881 ? 235 PHE A N     1 
ATOM   1796 C  CA    . PHE A 1 235 ? 29.11248  -21.79881 -19.21318 1.000 10.41464 ? 235 PHE A CA    1 
ATOM   1797 C  C     . PHE A 1 235 ? 28.89144  -21.91286 -20.71717 1.000 11.07850 ? 235 PHE A C     1 
ATOM   1798 O  O     . PHE A 1 235 ? 29.61242  -21.30088 -21.51121 1.000 9.59315  ? 235 PHE A O     1 
ATOM   1799 C  CB    . PHE A 1 235 ? 28.77547  -20.38780 -18.73122 1.000 8.15057  ? 235 PHE A CB    1 
ATOM   1800 C  CG    . PHE A 1 235 ? 27.40746  -19.91482 -19.14220 1.000 9.06757  ? 235 PHE A CG    1 
ATOM   1801 C  CD1   . PHE A 1 235 ? 26.29048  -20.25381 -18.39717 1.000 10.47327 ? 235 PHE A CD1   1 
ATOM   1802 C  CD2   . PHE A 1 235 ? 27.24143  -19.12386 -20.26922 1.000 8.53855  ? 235 PHE A CD2   1 
ATOM   1803 C  CE1   . PHE A 1 235 ? 25.03147  -19.81883 -18.77315 1.000 9.84138  ? 235 PHE A CE1   1 
ATOM   1804 C  CE2   . PHE A 1 235 ? 25.98542  -18.68688 -20.64821 1.000 7.38302  ? 235 PHE A CE2   1 
ATOM   1805 C  CZ    . PHE A 1 235 ? 24.88044  -19.03487 -19.89917 1.000 7.04950  ? 235 PHE A CZ    1 
ATOM   1806 N  N     . GLN A 1 236 ? 27.89244  -22.70288 -21.10513 1.000 9.65742  ? 236 GLN A N     1 
ATOM   1807 C  CA    . GLN A 1 236 ? 27.47341  -22.82092 -22.49712 1.000 10.03706 ? 236 GLN A CA    1 
ATOM   1808 C  C     . GLN A 1 236 ? 25.97541  -22.57094 -22.56509 1.000 10.38662 ? 236 GLN A C     1 
ATOM   1809 O  O     . GLN A 1 236 ? 25.19043  -23.32893 -21.98605 1.000 10.28874 ? 236 GLN A O     1 
ATOM   1810 C  CB    . GLN A 1 236 ? 27.82641  -24.19394 -23.07708 1.000 13.25845 ? 236 GLN A CB    1 
ATOM   1811 C  CG    . GLN A 1 236 ? 29.31642  -24.49693 -23.07310 1.000 13.77407 ? 236 GLN A CG    1 
ATOM   1812 C  CD    . GLN A 1 236 ? 29.70940  -25.50996 -24.12908 1.000 14.70428 ? 236 GLN A CD    1 
ATOM   1813 O  OE1   . GLN A 1 236 ? 30.31942  -26.53494 -23.82706 1.000 21.12457 ? 236 GLN A OE1   1 
ATOM   1814 N  NE2   . GLN A 1 236 ? 29.36937  -25.22300 -25.38008 1.000 17.02982 ? 236 GLN A NE2   1 
ATOM   1815 N  N     . LYS A 1 237 ? 25.58539  -21.50896 -23.27111 1.000 8.03659  ? 237 LYS A N     1 
ATOM   1816 C  CA    . LYS A 1 237 ? 24.18438  -21.08897 -23.28410 1.000 9.22537  ? 237 LYS A CA    1 
ATOM   1817 C  C     . LYS A 1 237 ? 23.24138  -22.13600 -23.86805 1.000 9.71905  ? 237 LYS A C     1 
ATOM   1818 O  O     . LYS A 1 237 ? 22.20440  -22.41299 -23.23902 1.000 8.19194  ? 237 LYS A O     1 
ATOM   1819 C  CB    . LYS A 1 237 ? 24.06136  -19.75000 -24.01914 1.000 7.82176  ? 237 LYS A CB    1 
ATOM   1820 C  CG    . LYS A 1 237 ? 22.69136  -19.10600 -23.91613 1.000 9.59422  ? 237 LYS A CG    1 
ATOM   1821 C  CD    . LYS A 1 237 ? 22.34038  -18.79496 -22.47213 1.000 7.06214  ? 237 LYS A CD    1 
ATOM   1822 C  CE    . LYS A 1 237 ? 21.03238  -18.03097 -22.37512 1.000 6.08617  ? 237 LYS A CE    1 
ATOM   1823 N  NZ    . LYS A 1 237 ? 21.10635  -16.71399 -23.06417 1.000 5.53476  ? 237 LYS A NZ    1 
ATOM   1824 N  N     . PRO A 1 238 ? 23.50636  -22.74403 -25.03303 1.000 11.50417 ? 238 PRO A N     1 
ATOM   1825 C  CA    . PRO A 1 238 ? 22.54836  -23.72306 -25.57398 1.000 10.42362 ? 238 PRO A CA    1 
ATOM   1826 C  C     . PRO A 1 238 ? 22.41038  -24.98903 -24.74394 1.000 11.50304 ? 238 PRO A C     1 
ATOM   1827 O  O     . PRO A 1 238 ? 21.52338  -25.80105 -25.03690 1.000 8.76488  ? 238 PRO A O     1 
ATOM   1828 C  CB    . PRO A 1 238 ? 23.11533  -24.04309 -26.96599 1.000 11.25158 ? 238 PRO A CB    1 
ATOM   1829 C  CG    . PRO A 1 238 ? 24.00631  -22.89710 -27.29204 1.000 12.06009 ? 238 PRO A CG    1 
ATOM   1830 C  CD    . PRO A 1 238 ? 24.60434  -22.49405 -25.98506 1.000 10.62629 ? 238 PRO A CD    1 
ATOM   1831 N  N     . ASP A 1 239 ? 23.24841  -25.19099 -23.72895 1.000 10.72191 ? 239 ASP A N     1 
ATOM   1832 C  CA    . ASP A 1 239 ? 23.19043  -26.38197 -22.89292 1.000 11.37738 ? 239 ASP A CA    1 
ATOM   1833 C  C     . ASP A 1 239 ? 22.50046  -26.14194 -21.55691 1.000 10.10603 ? 239 ASP A C     1 
ATOM   1834 O  O     . ASP A 1 239 ? 22.46849  -27.05091 -20.72188 1.000 10.05056 ? 239 ASP A O     1 
ATOM   1835 C  CB    . ASP A 1 239 ? 24.60244  -26.92495 -22.65093 1.000 12.68541 ? 239 ASP A CB    1 
ATOM   1836 C  CG    . ASP A 1 239 ? 25.26942  -27.40198 -23.92493 1.000 14.26668 ? 239 ASP A CG    1 
ATOM   1837 O  OD1   . ASP A 1 239 ? 24.60840  -27.39402 -24.98392 1.000 15.03744 ? 239 ASP A OD1   1 
ATOM   1838 O  OD2   . ASP A 1 239 ? 26.45742  -27.78297 -23.86694 1.000 18.69260 ? 239 ASP A OD2   1 
ATOM   1839 N  N     . THR A 1 240 ? 21.94946  -24.95293 -21.33293 1.000 9.47123  ? 240 THR A N     1 
ATOM   1840 C  CA    . THR A 1 240 ? 21.27848  -24.66190 -20.07693 1.000 8.01207  ? 240 THR A CA    1 
ATOM   1841 C  C     . THR A 1 240 ? 19.86949  -25.25191 -20.06688 1.000 7.51577  ? 240 THR A C     1 
ATOM   1842 O  O     . THR A 1 240 ? 19.30447  -25.60595 -21.10586 1.000 8.35612  ? 240 THR A O     1 
ATOM   1843 C  CB    . THR A 1 240 ? 21.22347  -23.15289 -19.82897 1.000 8.34233  ? 240 THR A CB    1 
ATOM   1844 O  OG1   . THR A 1 240 ? 20.62944  -22.50193 -20.95798 1.000 10.99824 ? 240 THR A OG1   1 
ATOM   1845 C  CG2   . THR A 1 240 ? 22.62347  -22.59788 -19.60902 1.000 9.15404  ? 240 THR A CG2   1 
ATOM   1846 N  N     . ASP A 1 241 ? 19.30251  -25.35088 -18.86387 1.000 6.39410  ? 241 ASP A N     1 
ATOM   1847 C  CA    . ASP A 1 241 ? 18.00952  -25.99088 -18.66682 1.000 6.97924  ? 241 ASP A CA    1 
ATOM   1848 C  C     . ASP A 1 241 ? 16.91051  -24.94289 -18.66783 1.000 6.93125  ? 241 ASP A C     1 
ATOM   1849 O  O     . ASP A 1 241 ? 16.88552  -24.08786 -17.76885 1.000 7.47063  ? 241 ASP A O     1 
ATOM   1850 C  CB    . ASP A 1 241 ? 17.99855  -26.76484 -17.35080 1.000 8.09645  ? 241 ASP A CB    1 
ATOM   1851 C  CG    . ASP A 1 241 ? 16.85656  -27.76385 -17.26374 1.000 8.13961  ? 241 ASP A CG    1 
ATOM   1852 O  OD1   . ASP A 1 241 ? 15.82555  -27.56988 -17.94072 1.000 7.04782  ? 241 ASP A OD1   1 
ATOM   1853 O  OD2   . ASP A 1 241 ? 16.99159  -28.74983 -16.50871 1.000 9.70519  ? 241 ASP A OD2   1 
ATOM   1854 N  N     . PRO A 1 242 ? 15.98849  -24.96293 -19.63681 1.000 6.26381  ? 242 PRO A N     1 
ATOM   1855 C  CA    . PRO A 1 242 ? 14.87948  -23.99894 -19.61181 1.000 6.56266  ? 242 PRO A CA    1 
ATOM   1856 C  C     . PRO A 1 242 ? 13.79851  -24.32991 -18.59678 1.000 6.47616  ? 242 PRO A C     1 
ATOM   1857 O  O     . PRO A 1 242 ? 13.06651  -23.41991 -18.18379 1.000 6.58505  ? 242 PRO A O     1 
ATOM   1858 C  CB    . PRO A 1 242 ? 14.32746  -24.06498 -21.04080 1.000 6.15426  ? 242 PRO A CB    1 
ATOM   1859 C  CG    . PRO A 1 242 ? 14.63946  -25.45699 -21.48176 1.000 7.82849  ? 242 PRO A CG    1 
ATOM   1860 C  CD    . PRO A 1 242 ? 15.95447  -25.81796 -20.83678 1.000 6.40655  ? 242 PRO A CD    1 
ATOM   1861 N  N     . SER A 1 243 ? 13.67853  -25.58990 -18.17974 1.000 8.31738  ? 243 SER A N     1 
ATOM   1862 C  CA    . SER A 1 243 ? 12.64055  -25.99088 -17.23971 1.000 7.85690  ? 243 SER A CA    1 
ATOM   1863 C  C     . SER A 1 243 ? 13.03258  -25.76883 -15.78572 1.000 9.46288  ? 243 SER A C     1 
ATOM   1864 O  O     . SER A 1 243 ? 12.20060  -25.99281 -14.89970 1.000 8.88184  ? 243 SER A O     1 
ATOM   1865 C  CB    . SER A 1 243 ? 12.28156  -27.46389 -17.45065 1.000 10.04841 ? 243 SER A CB    1 
ATOM   1866 O  OG    . SER A 1 243 ? 13.39257  -28.30287 -17.18465 1.000 11.15876 ? 243 SER A OG    1 
ATOM   1867 N  N     . ALA A 1 244 ? 14.26558  -25.34782 -15.51776 1.000 7.76715  ? 244 ALA A N     1 
ATOM   1868 C  CA    . ALA A 1 244 ? 14.69861  -25.10177 -14.14778 1.000 8.51497  ? 244 ALA A CA    1 
ATOM   1869 C  C     . ALA A 1 244 ? 14.07861  -23.80976 -13.63080 1.000 8.70891  ? 244 ALA A C     1 
ATOM   1870 O  O     . ALA A 1 244 ? 14.31259  -22.73378 -14.18984 1.000 9.05532  ? 244 ALA A O     1 
ATOM   1871 C  CB    . ALA A 1 244 ? 16.22161  -25.03276 -14.08081 1.000 8.50181  ? 244 ALA A CB    1 
ATOM   1872 N  N     . TRP A 1 245 ? 13.28663  -23.91374 -12.56578 1.000 8.67740  ? 245 TRP A N     1 
ATOM   1873 C  CA    . TRP A 1 245 ? 12.64564  -22.75272 -11.96280 1.000 10.14748 ? 245 TRP A CA    1 
ATOM   1874 C  C     . TRP A 1 245 ? 13.00567  -22.53967 -10.49982 1.000 10.50419 ? 245 TRP A C     1 
ATOM   1875 O  O     . TRP A 1 245 ? 13.07967  -21.38766 -10.06685 1.000 9.32142  ? 245 TRP A O     1 
ATOM   1876 C  CB    . TRP A 1 245 ? 11.11763  -22.85674 -12.09177 1.000 8.55867  ? 245 TRP A CB    1 
ATOM   1877 C  CG    . TRP A 1 245 ? 10.52766  -24.00172 -11.33472 1.000 13.05879 ? 245 TRP A CG    1 
ATOM   1878 C  CD1   . TRP A 1 245 ? 10.34366  -25.27473 -11.78568 1.000 10.68901 ? 245 TRP A CD1   1 
ATOM   1879 C  CD2   . TRP A 1 245 ? 10.03969  -23.97768 -9.98871  1.000 12.08834 ? 245 TRP A CD2   1 
ATOM   1880 N  NE1   . TRP A 1 245 ? 9.77169   -26.04671 -10.80364 1.000 11.74477 ? 245 TRP A NE1   1 
ATOM   1881 C  CE2   . TRP A 1 245 ? 9.57470   -25.27368 -9.68966  1.000 13.06107 ? 245 TRP A CE2   1 
ATOM   1882 C  CE3   . TRP A 1 245 ? 9.95070   -22.98665 -9.00674  1.000 10.69588 ? 245 TRP A CE3   1 
ATOM   1883 C  CZ2   . TRP A 1 245 ? 9.02973   -25.60464 -8.45164  1.000 12.93137 ? 245 TRP A CZ2   1 
ATOM   1884 C  CZ3   . TRP A 1 245 ? 9.40973   -23.31562 -7.77772  1.000 13.02695 ? 245 TRP A CZ3   1 
ATOM   1885 C  CH2   . TRP A 1 245 ? 8.95675   -24.61362 -7.51167  1.000 16.36944 ? 245 TRP A CH2   1 
ATOM   1886 N  N     . GLU A 1 246 ? 13.21969  -23.60965 -9.72779  1.000 11.53562 ? 246 GLU A N     1 
ATOM   1887 C  CA    . GLU A 1 246 ? 13.68772  -23.44460 -8.35480  1.000 11.46979 ? 246 GLU A CA    1 
ATOM   1888 C  C     . GLU A 1 246 ? 15.03071  -22.72859 -8.32085  1.000 12.56160 ? 246 GLU A C     1 
ATOM   1889 O  O     . GLU A 1 246 ? 15.25072  -21.83457 -7.49589  1.000 12.84755 ? 246 GLU A O     1 
ATOM   1890 C  CB    . GLU A 1 246 ? 13.79274  -24.80458 -7.66377  1.000 13.17360 ? 246 GLU A CB    1 
ATOM   1891 C  CG    . GLU A 1 246 ? 12.49675  -25.59359 -7.61771  1.000 14.89198 ? 246 GLU A CG    1 
ATOM   1892 C  CD    . GLU A 1 246 ? 12.64278  -26.90157 -6.86368  1.000 16.64360 ? 246 GLU A CD    1 
ATOM   1893 O  OE1   . GLU A 1 246 ? 13.66279  -27.07554 -6.16469  1.000 18.91034 ? 246 GLU A OE1   1 
ATOM   1894 O  OE2   . GLU A 1 246 ? 11.73978  -27.75658 -6.97163  1.000 21.65172 ? 246 GLU A OE2   1 
ATOM   1895 N  N     . LYS A 1 247 ? 15.93870  -23.11561 -9.21086  1.000 9.78325  ? 247 LYS A N     1 
ATOM   1896 C  CA    . LYS A 1 247 ? 17.21269  -22.42761 -9.40691  1.000 12.44695 ? 247 LYS A CA    1 
ATOM   1897 C  C     . LYS A 1 247 ? 17.39966  -22.26365 -10.90792 1.000 10.38887 ? 247 LYS A C     1 
ATOM   1898 O  O     . LYS A 1 247 ? 17.74865  -23.23567 -11.59990 1.000 11.95240 ? 247 LYS A O     1 
ATOM   1899 C  CB    . LYS A 1 247 ? 18.37071  -23.20258 -8.79091  1.000 13.92266 ? 247 LYS A CB    1 
ATOM   1900 C  CG    . LYS A 1 247 ? 19.72370  -22.52357 -8.93296  1.000 13.62807 ? 247 LYS A CG    1 
ATOM   1901 C  CD    . LYS A 1 247 ? 19.88771  -21.39354 -7.93100  0.000 12.40909 ? 247 LYS A CD    1 
ATOM   1902 C  CE    . LYS A 1 247 ? 19.85675  -21.91750 -6.50398  0.000 12.89922 ? 247 LYS A CE    1 
ATOM   1903 N  NZ    . LYS A 1 247 ? 20.20476  -20.86647 -5.51002  0.000 13.39680 ? 247 LYS A NZ    1 
ATOM   1904 N  N     . PRO A 1 248 ? 17.15263  -21.07067 -11.44995 1.000 9.11529  ? 248 PRO A N     1 
ATOM   1905 C  CA    . PRO A 1 248 ? 17.27960  -20.88071 -12.89996 1.000 10.13609 ? 248 PRO A CA    1 
ATOM   1906 C  C     . PRO A 1 248 ? 18.68059  -21.21872 -13.38698 1.000 9.38669  ? 248 PRO A C     1 
ATOM   1907 O  O     . PRO A 1 248 ? 19.67461  -21.01769 -12.68500 1.000 7.07312  ? 248 PRO A O     1 
ATOM   1908 C  CB    . PRO A 1 248 ? 16.95959  -19.39472 -13.09300 1.000 11.52491 ? 248 PRO A CB    1 
ATOM   1909 C  CG    . PRO A 1 248 ? 16.12261  -19.03469 -11.90599 1.000 11.98501 ? 248 PRO A CG    1 
ATOM   1910 C  CD    . PRO A 1 248 ? 16.66664  -19.85765 -10.77198 1.000 9.81799  ? 248 PRO A CD    1 
ATOM   1911 N  N     . ALA A 1 249 ? 18.74557  -21.74775 -14.61196 1.000 8.91546  ? 249 ALA A N     1 
ATOM   1912 C  CA    . ALA A 1 249 ? 19.99757  -22.27476 -15.13897 1.000 8.24345  ? 249 ALA A CA    1 
ATOM   1913 C  C     . ALA A 1 249 ? 20.97855  -21.18076 -15.54303 1.000 6.71254  ? 249 ALA A C     1 
ATOM   1914 O  O     . ALA A 1 249 ? 22.16655  -21.47076 -15.72404 1.000 6.08526  ? 249 ALA A O     1 
ATOM   1915 C  CB    . ALA A 1 249 ? 19.72155  -23.18680 -16.33394 1.000 6.68503  ? 249 ALA A CB    1 
ATOM   1916 N  N     . THR A 1 250 ? 20.51854  -19.94477 -15.69206 1.000 5.84650  ? 250 THR A N     1 
ATOM   1917 C  CA    . THR A 1 250 ? 21.37552  -18.83378 -16.08111 1.000 5.74889  ? 250 THR A CA    1 
ATOM   1918 C  C     . THR A 1 250 ? 21.43453  -17.81174 -14.94314 1.000 5.75142  ? 250 THR A C     1 
ATOM   1919 O  O     . THR A 1 250 ? 20.96956  -18.06471 -13.82812 1.000 9.01885  ? 250 THR A O     1 
ATOM   1920 C  CB    . THR A 1 250 ? 20.88749  -18.21582 -17.39412 1.000 5.61224  ? 250 THR A CB    1 
ATOM   1921 O  OG1   . THR A 1 250 ? 19.51149  -17.83683 -17.26510 1.000 5.55540  ? 250 THR A OG1   1 
ATOM   1922 C  CG2   . THR A 1 250 ? 21.02947  -19.21286 -18.53609 1.000 5.66473  ? 250 THR A CG2   1 
ATOM   1923 N  N     . THR A 1 251 ? 22.01352  -16.64475 -15.23519 1.000 5.77194  ? 251 THR A N     1 
ATOM   1924 C  CA    . THR A 1 251 ? 22.29753  -15.67071 -14.18522 1.000 5.72339  ? 251 THR A CA    1 
ATOM   1925 C  C     . THR A 1 251 ? 21.06854  -14.86471 -13.78322 1.000 6.01687  ? 251 THR A C     1 
ATOM   1926 O  O     . THR A 1 251 ? 20.98856  -14.40468 -12.63723 1.000 6.41035  ? 251 THR A O     1 
ATOM   1927 C  CB    . THR A 1 251 ? 23.40852  -14.71772 -14.63227 1.000 5.69300  ? 251 THR A CB    1 
ATOM   1928 O  OG1   . THR A 1 251 ? 22.93549  -13.89475 -15.70729 1.000 5.56226  ? 251 THR A OG1   1 
ATOM   1929 C  CG2   . THR A 1 251 ? 24.62751  -15.50172 -15.09828 1.000 5.75804  ? 251 THR A CG2   1 
ATOM   1930 N  N     . VAL A 1 252 ? 20.10952  -14.69275 -14.69621 1.000 5.58289  ? 252 VAL A N     1 
ATOM   1931 C  CA    . VAL A 1 252 ? 18.92651  -13.86275 -14.47821 1.000 6.25444  ? 252 VAL A CA    1 
ATOM   1932 C  C     . VAL A 1 252 ? 19.36951  -12.45773 -14.08326 1.000 5.67821  ? 252 VAL A C     1 
ATOM   1933 O  O     . VAL A 1 252 ? 18.83753  -11.86071 -13.14126 1.000 6.89103  ? 252 VAL A O     1 
ATOM   1934 C  CB    . VAL A 1 252 ? 17.98154  -14.47772 -13.42517 1.000 7.83478  ? 252 VAL A CB    1 
ATOM   1935 C  CG1   . VAL A 1 252 ? 16.57953  -13.88874 -13.54816 1.000 9.24817  ? 252 VAL A CG1   1 
ATOM   1936 C  CG2   . VAL A 1 252 ? 17.92655  -15.98873 -13.57812 1.000 9.68949  ? 252 VAL A CG2   1 
ATOM   1937 N  N     . LEU A 1 253 ? 20.35849  -11.92675 -14.79829 1.000 5.55031  ? 253 LEU A N     1 
ATOM   1938 C  CA    . LEU A 1 253 ? 20.82448  -10.56274 -14.60035 1.000 5.59547  ? 253 LEU A CA    1 
ATOM   1939 C  C     . LEU A 1 253 ? 20.27346  -9.59677  -15.63836 1.000 5.53727  ? 253 LEU A C     1 
ATOM   1940 O  O     . LEU A 1 253 ? 20.65345  -8.42277  -15.63341 1.000 5.59332  ? 253 LEU A O     1 
ATOM   1941 C  CB    . LEU A 1 253 ? 22.35648  -10.51673 -14.62138 1.000 5.66899  ? 253 LEU A CB    1 
ATOM   1942 C  CG    . LEU A 1 253 ? 23.08851  -11.09268 -13.40838 1.000 6.10610  ? 253 LEU A CG    1 
ATOM   1943 C  CD1   . LEU A 1 253 ? 24.58351  -11.17768 -13.67641 1.000 6.69427  ? 253 LEU A CD1   1 
ATOM   1944 C  CD2   . LEU A 1 253 ? 22.81353  -10.24865 -12.17540 1.000 6.91143  ? 253 LEU A CD2   1 
ATOM   1945 N  N     . SER A 1 254 ? 19.38944  -10.05881 -16.52233 1.000 5.46130  ? 254 SER A N     1 
ATOM   1946 C  CA    . SER A 1 254 ? 18.85441  -9.23284  -17.60134 1.000 5.73461  ? 254 SER A CA    1 
ATOM   1947 C  C     . SER A 1 254 ? 17.99941  -8.06484  -17.11036 1.000 5.54737  ? 254 SER A C     1 
ATOM   1948 O  O     . SER A 1 254 ? 18.10739  -6.96785  -17.67440 1.000 5.79837  ? 254 SER A O     1 
ATOM   1949 C  CB    . SER A 1 254 ? 18.05940  -10.09188 -18.59630 1.000 5.43051  ? 254 SER A CB    1 
ATOM   1950 O  OG    . SER A 1 254 ? 17.16142  -10.97787 -17.95026 1.000 5.72167  ? 254 SER A OG    1 
ATOM   1951 N  N     . PRO A 1 255 ? 17.14144  -8.22581  -16.09034 1.000 5.83607  ? 255 PRO A N     1 
ATOM   1952 C  CA    . PRO A 1 255 ? 16.39144  -7.05180  -15.61436 1.000 7.11539  ? 255 PRO A CA    1 
ATOM   1953 C  C     . PRO A 1 255 ? 17.27944  -5.99378  -14.98741 1.000 6.55127  ? 255 PRO A C     1 
ATOM   1954 O  O     . PRO A 1 255 ? 16.92143  -4.80878  -15.00344 1.000 6.02204  ? 255 PRO A O     1 
ATOM   1955 C  CB    . PRO A 1 255 ? 15.41146  -7.64278  -14.59032 1.000 6.25774  ? 255 PRO A CB    1 
ATOM   1956 C  CG    . PRO A 1 255 ? 15.35147  -9.09279  -14.90627 1.000 7.85694  ? 255 PRO A CG    1 
ATOM   1957 C  CD    . PRO A 1 255 ? 16.72446  -9.44379  -15.37029 1.000 5.62311  ? 255 PRO A CD    1 
ATOM   1958 N  N     . TYR A 1 256 ? 18.43246  -6.38375  -14.44342 1.000 6.08280  ? 256 TYR A N     1 
ATOM   1959 C  CA    . TYR A 1 256 ? 19.34046  -5.41173  -13.84947 1.000 6.60899  ? 256 TYR A CA    1 
ATOM   1960 C  C     . TYR A 1 256 ? 20.23343  -4.75875  -14.89551 1.000 6.38894  ? 256 TYR A C     1 
ATOM   1961 O  O     . TYR A 1 256 ? 20.63543  -3.60274  -14.72555 1.000 7.30742  ? 256 TYR A O     1 
ATOM   1962 C  CB    . TYR A 1 256 ? 20.18149  -6.08369  -12.76347 1.000 6.04256  ? 256 TYR A CB    1 
ATOM   1963 C  CG    . TYR A 1 256 ? 19.35152  -6.85566  -11.76243 1.000 7.80798  ? 256 TYR A CG    1 
ATOM   1964 C  CD1   . TYR A 1 256 ? 18.74553  -6.21364  -10.69043 1.000 7.88788  ? 256 TYR A CD1   1 
ATOM   1965 C  CD2   . TYR A 1 256 ? 19.16352  -8.22567  -11.89738 1.000 6.72921  ? 256 TYR A CD2   1 
ATOM   1966 C  CE1   . TYR A 1 256 ? 17.97956  -6.91461  -9.77640  1.000 7.37221  ? 256 TYR A CE1   1 
ATOM   1967 C  CE2   . TYR A 1 256 ? 18.40055  -8.93465  -10.98834 1.000 9.08816  ? 256 TYR A CE2   1 
ATOM   1968 C  CZ    . TYR A 1 256 ? 17.81157  -8.27462  -9.93035  1.000 9.25962  ? 256 TYR A CZ    1 
ATOM   1969 O  OH    . TYR A 1 256 ? 17.04959  -8.97660  -9.02331  1.000 7.95430  ? 256 TYR A OH    1 
ATOM   1970 N  N     . LEU A 1 257 ? 20.54842  -5.47478  -15.97749 1.000 6.46105  ? 257 LEU A N     1 
ATOM   1971 C  CA    . LEU A 1 257 ? 21.29339  -4.87281  -17.07653 1.000 5.77257  ? 257 LEU A CA    1 
ATOM   1972 C  C     . LEU A 1 257 ? 20.41236  -3.96984  -17.92854 1.000 6.36867  ? 257 LEU A C     1 
ATOM   1973 O  O     . LEU A 1 257 ? 20.91634  -3.02686  -18.54758 1.000 6.83174  ? 257 LEU A O     1 
ATOM   1974 C  CB    . LEU A 1 257 ? 21.92538  -5.96283  -17.94251 1.000 6.79856  ? 257 LEU A CB    1 
ATOM   1975 C  CG    . LEU A 1 257 ? 23.07340  -6.74980  -17.30751 1.000 6.21398  ? 257 LEU A CG    1 
ATOM   1976 C  CD1   . LEU A 1 257 ? 23.42239  -7.96582  -18.14648 1.000 5.53356  ? 257 LEU A CD1   1 
ATOM   1977 C  CD2   . LEU A 1 257 ? 24.29239  -5.85979  -17.12456 1.000 5.74210  ? 257 LEU A CD2   1 
ATOM   1978 N  N     . LYS A 1 258 ? 19.10536  -4.23985  -17.96950 1.000 5.81914  ? 258 LYS A N     1 
ATOM   1979 C  CA    . LYS A 1 258 ? 18.18634  -3.39088  -18.72151 1.000 5.91930  ? 258 LYS A CA    1 
ATOM   1980 C  C     . LYS A 1 258 ? 18.06734  -2.01486  -18.07955 1.000 6.13140  ? 258 LYS A C     1 
ATOM   1981 O  O     . LYS A 1 258 ? 18.34132  -0.99088  -18.71558 1.000 6.46769  ? 258 LYS A O     1 
ATOM   1982 C  CB    . LYS A 1 258 ? 16.81634  -4.07290  -18.82546 1.000 6.54608  ? 258 LYS A CB    1 
ATOM   1983 C  CG    . LYS A 1 258 ? 15.72932  -3.25893  -19.52546 1.000 7.53652  ? 258 LYS A CG    1 
ATOM   1984 C  CD    . LYS A 1 258 ? 14.83734  -2.53390  -18.52146 1.000 7.60638  ? 258 LYS A CD    1 
ATOM   1985 C  CE    . LYS A 1 258 ? 13.60032  -1.94793  -19.17945 1.000 7.25804  ? 258 LYS A CE    1 
ATOM   1986 N  NZ    . LYS A 1 258 ? 13.93529  -1.11597  -20.36849 1.000 11.48026 ? 258 LYS A NZ    1 
ATOM   1987 N  N     . PHE A 1 259 ? 17.65737  -1.96983  -16.80954 1.000 6.21947  ? 259 PHE A N     1 
ATOM   1988 C  CA    . PHE A 1 259 ? 17.51938  -0.70781  -16.09057 1.000 6.69148  ? 259 PHE A CA    1 
ATOM   1989 C  C     . PHE A 1 259 ? 18.85538  -0.10879  -15.67762 1.000 6.54323  ? 259 PHE A C     1 
ATOM   1990 O  O     . PHE A 1 259 ? 18.86938  0.99523   -15.12165 1.000 6.97865  ? 259 PHE A O     1 
ATOM   1991 C  CB    . PHE A 1 259 ? 16.64340  -0.89578  -14.84855 1.000 7.80734  ? 259 PHE A CB    1 
ATOM   1992 C  CG    . PHE A 1 259 ? 15.18240  -1.05580  -15.15351 1.000 7.80608  ? 259 PHE A CG    1 
ATOM   1993 C  CD1   . PHE A 1 259 ? 14.41838  0.03418   -15.53753 1.000 8.88772  ? 259 PHE A CD1   1 
ATOM   1994 C  CD2   . PHE A 1 259 ? 14.56741  -2.29180  -15.04246 1.000 9.25076  ? 259 PHE A CD2   1 
ATOM   1995 C  CE1   . PHE A 1 259 ? 13.07238  -0.10684  -15.81550 1.000 8.11374  ? 259 PHE A CE1   1 
ATOM   1996 C  CE2   . PHE A 1 259 ? 13.22041  -2.43982  -15.31943 1.000 7.70773  ? 259 PHE A CE2   1 
ATOM   1997 C  CZ    . PHE A 1 259 ? 12.47339  -1.34484  -15.70645 1.000 8.78890  ? 259 PHE A CZ    1 
ATOM   1998 N  N     . GLY A 1 260 ? 19.96738  -0.79378  -15.92862 1.000 6.37909  ? 260 GLY A N     1 
ATOM   1999 C  CA    . GLY A 1 260 ? 21.25938  -0.27876  -15.53067 1.000 6.83562  ? 260 GLY A CA    1 
ATOM   2000 C  C     . GLY A 1 260 ? 21.59142  -0.46072  -14.07067 1.000 6.57089  ? 260 GLY A C     1 
ATOM   2001 O  O     . GLY A 1 260 ? 22.50242  0.20331   -13.56871 1.000 6.72762  ? 260 GLY A O     1 
ATOM   2002 N  N     . CYS A 1 261 ? 20.87344  -1.33670  -13.36363 1.000 7.53493  ? 261 CYS A N     1 
ATOM   2003 C  CA    . CYS A 1 261 ? 21.21047  -1.62065  -11.97262 1.000 7.08692  ? 261 CYS A CA    1 
ATOM   2004 C  C     . CYS A 1 261 ? 22.55948  -2.31364  -11.84463 1.000 6.96182  ? 261 CYS A C     1 
ATOM   2005 O  O     . CYS A 1 261 ? 23.17950  -2.24460  -10.77865 1.000 8.00328  ? 261 CYS A O     1 
ATOM   2006 C  CB    . CYS A 1 261 ? 20.12049  -2.47864  -11.32858 1.000 7.40043  ? 261 CYS A CB    1 
ATOM   2007 S  SG    . CYS A 1 261 ? 18.46348  -1.76066  -11.40356 1.000 6.78014  ? 261 CYS A SG    1 
ATOM   2008 N  N     . LEU A 1 262 ? 23.02146  -2.97267  -12.90462 1.000 6.71353  ? 262 LEU A N     1 
ATOM   2009 C  CA    . LEU A 1 262 ? 24.32047  -3.62666  -12.93463 1.000 6.30329  ? 262 LEU A CA    1 
ATOM   2010 C  C     . LEU A 1 262 ? 25.08644  -3.13369  -14.15166 1.000 6.25097  ? 262 LEU A C     1 
ATOM   2011 O  O     . LEU A 1 262 ? 24.55441  -3.13573  -15.26565 1.000 6.98128  ? 262 LEU A O     1 
ATOM   2012 C  CB    . LEU A 1 262 ? 24.17748  -5.15066  -12.98158 1.000 6.44975  ? 262 LEU A CB    1 
ATOM   2013 C  CG    . LEU A 1 262 ? 25.47848  -5.93766  -13.14358 1.000 6.11044  ? 262 LEU A CG    1 
ATOM   2014 C  CD1   . LEU A 1 262 ? 26.36850  -5.75961  -11.92361 1.000 7.80617  ? 262 LEU A CD1   1 
ATOM   2015 C  CD2   . LEU A 1 262 ? 25.19149  -7.40967  -13.40153 1.000 6.27340  ? 262 LEU A CD2   1 
ATOM   2016 N  N     . SER A 1 263 ? 26.32944  -2.71367  -13.93570 1.000 6.37307  ? 263 SER A N     1 
ATOM   2017 C  CA    . SER A 1 263 ? 27.16341  -2.25470  -15.03673 1.000 6.36887  ? 263 SER A CA    1 
ATOM   2018 C  C     . SER A 1 263 ? 27.58840  -3.43272  -15.90270 1.000 6.19928  ? 263 SER A C     1 
ATOM   2019 O  O     . SER A 1 263 ? 28.03042  -4.46670  -15.39068 1.000 7.29637  ? 263 SER A O     1 
ATOM   2020 C  CB    . SER A 1 263 ? 28.39142  -1.52167  -14.49978 1.000 7.04787  ? 263 SER A CB    1 
ATOM   2021 O  OG    . SER A 1 263 ? 29.28939  -1.20070  -15.54781 1.000 6.68354  ? 263 SER A OG    1 
ATOM   2022 N  N     . ALA A 1 264 ? 27.44737  -3.27776  -17.22171 1.000 6.12939  ? 264 ALA A N     1 
ATOM   2023 C  CA    . ALA A 1 264 ? 27.92036  -4.30779  -18.13669 1.000 6.02660  ? 264 ALA A CA    1 
ATOM   2024 C  C     . ALA A 1 264 ? 29.44036  -4.39478  -18.13971 1.000 6.14126  ? 264 ALA A C     1 
ATOM   2025 O  O     . ALA A 1 264 ? 29.99837  -5.48078  -18.34069 1.000 6.10610  ? 264 ALA A O     1 
ATOM   2026 C  CB    . ALA A 1 264 ? 27.40133  -4.03884  -19.54968 1.000 5.98502  ? 264 ALA A CB    1 
ATOM   2027 N  N     . ARG A 1 265 ? 30.12357  -3.26892  -17.91880 1.000 6.31117  ? 265 ARG A N     1 
ATOM   2028 C  CA    . ARG A 1 265 ? 31.58066  -3.28906  -17.86474 1.000 7.41306  ? 265 ARG A CA    1 
ATOM   2029 C  C     . ARG A 1 265 ? 32.08287  -3.96580  -16.59762 1.000 6.51119  ? 265 ARG A C     1 
ATOM   2030 O  O     . ARG A 1 265 ? 33.12056  -4.63714  -16.62589 1.000 9.24074  ? 265 ARG A O     1 
ATOM   2031 C  CB    . ARG A 1 265 ? 32.13064  -1.86689  -17.96615 1.000 8.48388  ? 265 ARG A CB    1 
ATOM   2032 C  CG    . ARG A 1 265 ? 31.81507  -1.17704  -19.28390 1.000 7.28698  ? 265 ARG A CG    1 
ATOM   2033 C  CD    . ARG A 1 265 ? 32.27022  0.27200   -19.27223 1.000 8.67972  ? 265 ARG A CD    1 
ATOM   2034 N  NE    . ARG A 1 265 ? 31.96967  0.94857   -20.52841 1.000 9.68706  ? 265 ARG A NE    1 
ATOM   2035 C  CZ    . ARG A 1 265 ? 32.18578  2.23670   -20.75546 1.000 10.05732 ? 265 ARG A CZ    1 
ATOM   2036 N  NH1   . ARG A 1 265 ? 32.70114  3.02525   -19.82636 1.000 8.92882  ? 265 ARG A NH1   1 
ATOM   2037 N  NH2   . ARG A 1 265 ? 31.87494  2.74754   -21.94395 1.000 10.92362 ? 265 ARG A NH2   1 
ATOM   2038 N  N     . LEU A 1 266 ? 31.36841  -3.80268  -15.48177 1.000 6.51713  ? 266 LEU A N     1 
ATOM   2039 C  CA    . LEU A 1 266 ? 31.73644  -4.52564  -14.26776 1.000 6.59771  ? 266 LEU A CA    1 
ATOM   2040 C  C     . LEU A 1 266 ? 31.49545  -6.02065  -14.42871 1.000 7.40859  ? 266 LEU A C     1 
ATOM   2041 O  O     . LEU A 1 266 ? 32.29447  -6.83863  -13.95770 1.000 6.99694  ? 266 LEU A O     1 
ATOM   2042 C  CB    . LEU A 1 266 ? 30.95747  -3.97861  -13.07076 1.000 7.62535  ? 266 LEU A CB    1 
ATOM   2043 C  CG    . LEU A 1 266 ? 31.22850  -4.67057  -11.73174 1.000 9.53394  ? 266 LEU A CG    1 
ATOM   2044 C  CD1   . LEU A 1 266 ? 32.69551  -4.54555  -11.34778 1.000 8.16817  ? 266 LEU A CD1   1 
ATOM   2045 C  CD2   . LEU A 1 266 ? 30.33152  -4.10654  -10.63874 1.000 10.70253 ? 266 LEU A CD2   1 
ATOM   2046 N  N     . PHE A 1 267 ? 30.39444  -6.39368  -15.08367 1.000 7.13087  ? 267 PHE A N     1 
ATOM   2047 C  CA    . PHE A 1 267 ? 30.16145  -7.79469  -15.41963 1.000 7.10712  ? 267 PHE A CA    1 
ATOM   2048 C  C     . PHE A 1 267 ? 31.30043  -8.33871  -16.27363 1.000 6.98867  ? 267 PHE A C     1 
ATOM   2049 O  O     . PHE A 1 267 ? 31.82845  -9.42469  -16.00961 1.000 6.44409  ? 267 PHE A O     1 
ATOM   2050 C  CB    . PHE A 1 267 ? 28.81843  -7.93372  -16.14359 1.000 5.96386  ? 267 PHE A CB    1 
ATOM   2051 C  CG    . PHE A 1 267 ? 28.27644  -9.34073  -16.18754 1.000 5.87992  ? 267 PHE A CG    1 
ATOM   2052 C  CD1   . PHE A 1 267 ? 28.95746  -10.39370 -15.59652 1.000 6.89432  ? 267 PHE A CD1   1 
ATOM   2053 C  CD2   . PHE A 1 267 ? 27.07543  -9.60576  -16.82651 1.000 7.82289  ? 267 PHE A CD2   1 
ATOM   2054 C  CE1   . PHE A 1 267 ? 28.45247  -11.68071 -15.64547 1.000 5.98456  ? 267 PHE A CE1   1 
ATOM   2055 C  CE2   . PHE A 1 267 ? 26.56544  -10.88976 -16.87746 1.000 7.74670  ? 267 PHE A CE2   1 
ATOM   2056 C  CZ    . PHE A 1 267 ? 27.25546  -11.92874 -16.28444 1.000 7.79533  ? 267 PHE A CZ    1 
ATOM   2057 N  N     . HIS A 1 268 ? 31.70440  -7.58273  -17.29667 1.000 7.36329  ? 268 HIS A N     1 
ATOM   2058 C  CA    . HIS A 1 268 ? 32.78939  -8.02975  -18.16168 1.000 6.59046  ? 268 HIS A CA    1 
ATOM   2059 C  C     . HIS A 1 268 ? 34.12341  -8.05172  -17.42770 1.000 7.83678  ? 268 HIS A C     1 
ATOM   2060 O  O     . HIS A 1 268 ? 34.97141  -8.90572  -17.71270 1.000 8.18147  ? 268 HIS A O     1 
ATOM   2061 C  CB    . HIS A 1 268 ? 32.87536  -7.13279  -19.39870 1.000 7.93447  ? 268 HIS A CB    1 
ATOM   2062 C  CG    . HIS A 1 268 ? 33.76134  -7.67481  -20.47571 1.000 8.31741  ? 268 HIS A CG    1 
ATOM   2063 N  ND1   . HIS A 1 268 ? 35.12834  -7.50480  -20.47274 1.000 9.36946  ? 268 HIS A ND1   1 
ATOM   2064 C  CD2   . HIS A 1 268 ? 33.47232  -8.38585  -21.59268 1.000 7.30591  ? 268 HIS A CD2   1 
ATOM   2065 C  CE1   . HIS A 1 268 ? 35.64532  -8.08783  -21.54073 1.000 7.97047  ? 268 HIS A CE1   1 
ATOM   2066 N  NE2   . HIS A 1 268 ? 34.66131  -8.62786  -22.23670 1.000 9.60706  ? 268 HIS A NE2   1 
ATOM   2067 N  N     . ALA A 1 269 ? 34.32942  -7.13069  -16.48274 1.000 8.42538  ? 269 ALA A N     1 
ATOM   2068 C  CA    . ALA A 1 269 ? 35.58343  -7.10766  -15.73576 1.000 7.81681  ? 269 ALA A CA    1 
ATOM   2069 C  C     . ALA A 1 269 ? 35.70746  -8.32163  -14.82373 1.000 8.62258  ? 269 ALA A C     1 
ATOM   2070 O  O     . ALA A 1 269 ? 36.80447  -8.86561  -14.65274 1.000 7.54902  ? 269 ALA A O     1 
ATOM   2071 C  CB    . ALA A 1 269 ? 35.69044  -5.81463  -14.92780 1.000 9.42228  ? 269 ALA A CB    1 
ATOM   2072 N  N     . ARG A 1 270 ? 34.59574  -8.76016  -14.22773 1.000 8.68238  ? 270 ARG A N     1 
ATOM   2073 C  CA    . ARG A 1 270 ? 34.63540  -9.94397  -13.37574 1.000 8.75848  ? 270 ARG A CA    1 
ATOM   2074 C  C     . ARG A 1 270 ? 34.81239  -11.21774 -14.19248 1.000 9.06258  ? 270 ARG A C     1 
ATOM   2075 O  O     . ARG A 1 270 ? 35.36824  -12.20180 -13.69045 1.000 10.10485 ? 270 ARG A O     1 
ATOM   2076 C  CB    . ARG A 1 270 ? 33.36308  -10.03030 -12.53186 1.000 7.81572  ? 270 ARG A CB    1 
ATOM   2077 C  CG    . ARG A 1 270 ? 33.15055  -8.85900  -11.58333 1.000 12.21269 ? 270 ARG A CG    1 
ATOM   2078 C  CD    . ARG A 1 270 ? 34.16482  -8.85983  -10.44949 1.000 13.49761 ? 270 ARG A CD    1 
ATOM   2079 N  NE    . ARG A 1 270 ? 34.09911  -10.08283 -9.65819  1.000 13.41986 ? 270 ARG A NE    1 
ATOM   2080 C  CZ    . ARG A 1 270 ? 33.26699  -10.27727 -8.64403  1.000 11.86014 ? 270 ARG A CZ    1 
ATOM   2081 N  NH1   . ARG A 1 270 ? 32.40266  -9.34802  -8.27065  1.000 16.28696 ? 270 ARG A NH1   1 
ATOM   2082 N  NH2   . ARG A 1 270 ? 33.30071  -11.43507 -7.98994  1.000 13.94663 ? 270 ARG A NH2   1 
ATOM   2083 N  N     . LEU A 1 271 ? 34.34747  -11.22066 -15.44461 1.000 6.66069  ? 271 LEU A N     1 
ATOM   2084 C  CA    . LEU A 1 271 ? 34.49046  -12.40568 -16.28658 1.000 7.93897  ? 271 LEU A CA    1 
ATOM   2085 C  C     . LEU A 1 271 ? 35.94146  -12.62468 -16.69460 1.000 8.95840  ? 271 LEU A C     1 
ATOM   2086 O  O     . LEU A 1 271 ? 36.40946  -13.76868 -16.74858 1.000 10.03779 ? 271 LEU A O     1 
ATOM   2087 C  CB    . LEU A 1 271 ? 33.60044  -12.28173 -17.52456 1.000 6.57666  ? 271 LEU A CB    1 
ATOM   2088 C  CG    . LEU A 1 271 ? 32.08644  -12.33973 -17.31353 1.000 6.78814  ? 271 LEU A CG    1 
ATOM   2089 C  CD1   . LEU A 1 271 ? 31.35841  -11.93478 -18.58453 1.000 8.63500  ? 271 LEU A CD1   1 
ATOM   2090 C  CD2   . LEU A 1 271 ? 31.65446  -13.72872 -16.87148 1.000 7.85307  ? 271 LEU A CD2   1 
ATOM   2091 N  N     . LEU A 1 272 ? 36.66944  -11.54468 -16.98665 1.000 8.88540  ? 272 LEU A N     1 
ATOM   2092 C  CA    . LEU A 1 272 ? 38.06343  -11.68669 -17.39368 1.000 10.56434 ? 272 LEU A CA    1 
ATOM   2093 C  C     . LEU A 1 272 ? 38.94346  -12.16264 -16.24568 1.000 10.86080 ? 272 LEU A C     1 
ATOM   2094 O  O     . LEU A 1 272 ? 39.93346  -12.86564 -16.47968 1.000 10.61152 ? 272 LEU A O     1 
ATOM   2095 C  CB    . LEU A 1 272 ? 38.59141  -10.36470 -17.95273 1.000 7.68861  ? 272 LEU A CB    1 
ATOM   2096 C  CG    . LEU A 1 272 ? 38.01138  -9.89974  -19.28973 1.000 10.52573 ? 272 LEU A CG    1 
ATOM   2097 C  CD1   . LEU A 1 272 ? 38.70336  -8.62775  -19.75878 1.000 12.11321 ? 272 LEU A CD1   1 
ATOM   2098 C  CD2   . LEU A 1 272 ? 38.12837  -10.99377 -20.34070 1.000 13.33083 ? 272 LEU A CD2   1 
ATOM   2099 N  N     . GLU A 1 273 ? 38.60649  -11.79061 -15.00768 1.000 12.52774 ? 273 GLU A N     1 
ATOM   2100 C  CA    . GLU A 1 273 ? 39.37851  -12.26257 -13.86269 1.000 11.69178 ? 273 GLU A CA    1 
ATOM   2101 C  C     . GLU A 1 273 ? 39.28653  -13.77657 -13.72564 1.000 10.64910 ? 273 GLU A C     1 
ATOM   2102 O  O     . GLU A 1 273 ? 40.27654  -14.43955 -13.39664 1.000 10.99930 ? 273 GLU A O     1 
ATOM   2103 C  CB    . GLU A 1 273 ? 38.89454  -11.57653 -12.58370 1.000 12.85958 ? 273 GLU A CB    1 
ATOM   2104 C  CG    . GLU A 1 273 ? 39.08852  -10.06953 -12.57275 1.000 17.08214 ? 273 GLU A CG    1 
ATOM   2105 C  CD    . GLU A 1 273 ? 38.60355  -9.43050  -11.28576 1.000 17.68507 ? 273 GLU A CD    1 
ATOM   2106 O  OE1   . GLU A 1 273 ? 37.98257  -10.13948 -10.46472 1.000 17.25046 ? 273 GLU A OE1   1 
ATOM   2107 O  OE2   . GLU A 1 273 ? 38.84554  -8.22049  -11.09280 1.000 22.92021 ? 273 GLU A OE2   1 
ATOM   2108 N  N     . VAL A 1 274 ? 38.10453  -14.33958 -13.97760 1.000 12.03285 ? 274 VAL A N     1 
ATOM   2109 C  CA    . VAL A 1 274 ? 37.94354  -15.78658 -13.89955 1.000 14.60317 ? 274 VAL A CA    1 
ATOM   2110 C  C     . VAL A 1 274 ? 38.56152  -16.47261 -15.11354 1.000 11.43733 ? 274 VAL A C     1 
ATOM   2111 O  O     . VAL A 1 274 ? 39.10653  -17.57461 -14.99652 1.000 13.16650 ? 274 VAL A O     1 
ATOM   2112 C  CB    . VAL A 1 274 ? 36.45355  -16.14459 -13.75051 1.000 12.56897 ? 274 VAL A CB    1 
ATOM   2113 C  CG1   . VAL A 1 274 ? 36.27656  -17.64158 -13.55346 1.000 13.02230 ? 274 VAL A CG1   1 
ATOM   2114 C  CG2   . VAL A 1 274 ? 35.83457  -15.37056 -12.59452 1.000 12.80270 ? 274 VAL A CG2   1 
ATOM   2115 N  N     . TYR A 1 275 ? 38.50449  -15.83565 -16.28656 1.000 10.43491 ? 275 TYR A N     1 
ATOM   2116 C  CA    . TYR A 1 275 ? 39.00247  -16.47368 -17.50155 1.000 10.36604 ? 275 TYR A CA    1 
ATOM   2117 C  C     . TYR A 1 275 ? 40.52147  -16.59267 -17.50658 1.000 11.50057 ? 275 TYR A C     1 
ATOM   2118 O  O     . TYR A 1 275 ? 41.06247  -17.53668 -18.09356 1.000 10.02342 ? 275 TYR A O     1 
ATOM   2119 C  CB    . TYR A 1 275 ? 38.52944  -15.70172 -18.73456 1.000 9.53379  ? 275 TYR A CB    1 
ATOM   2120 C  CG    . TYR A 1 275 ? 37.06443  -15.89874 -19.06653 1.000 10.73132 ? 275 TYR A CG    1 
ATOM   2121 C  CD1   . TYR A 1 275 ? 36.29445  -16.83473 -18.38648 1.000 9.78713  ? 275 TYR A CD1   1 
ATOM   2122 C  CD2   . TYR A 1 275 ? 36.45541  -15.15478 -20.06854 1.000 9.44044  ? 275 TYR A CD2   1 
ATOM   2123 C  CE1   . TYR A 1 275 ? 34.95745  -17.01875 -18.69245 1.000 9.72578  ? 275 TYR A CE1   1 
ATOM   2124 C  CE2   . TYR A 1 275 ? 35.12040  -15.33180 -20.38050 1.000 9.28614  ? 275 TYR A CE2   1 
ATOM   2125 C  CZ    . TYR A 1 275 ? 34.37742  -16.26478 -19.68946 1.000 8.72872  ? 275 TYR A CZ    1 
ATOM   2126 O  OH    . TYR A 1 275 ? 33.04842  -16.44080 -20.00043 1.000 8.32748  ? 275 TYR A OH    1 
ATOM   2127 N  N     . ARG A 1 276 ? 41.22328  -15.65482 -16.86817 1.000 12.06849 ? 276 ARG A N     1 
ATOM   2128 C  CA    . ARG A 1 276 ? 42.67839  -15.71701 -16.81355 1.000 13.53156 ? 276 ARG A CA    1 
ATOM   2129 C  C     . ARG A 1 276 ? 43.18449  -16.77659 -15.84557 1.000 13.77381 ? 276 ARG A C     1 
ATOM   2130 O  O     . ARG A 1 276 ? 44.37235  -17.11295 -15.88858 1.000 16.18956 ? 276 ARG A O     1 
ATOM   2131 C  CB    . ARG A 1 276 ? 43.24976  -14.34830 -16.43542 1.000 14.39492 ? 276 ARG A CB    1 
ATOM   2132 C  CG    . ARG A 1 276 ? 42.95775  -13.26102 -17.45867 1.000 17.42563 ? 276 ARG A CG    1 
ATOM   2133 C  CD    . ARG A 1 276 ? 43.51968  -11.91569 -17.02906 0.000 16.85290 ? 276 ARG A CD    1 
ATOM   2134 N  NE    . ARG A 1 276 ? 42.99508  -10.82361 -17.84029 0.000 17.76350 ? 276 ARG A NE    1 
ATOM   2135 C  CZ    . ARG A 1 276 ? 43.35810  -9.55470  -17.71402 0.000 18.82975 ? 276 ARG A CZ    1 
ATOM   2136 N  NH1   . ARG A 1 276 ? 44.26561  -9.18014  -16.82721 0.000 20.07093 ? 276 ARG A NH1   1 
ATOM   2137 N  NH2   . ARG A 1 276 ? 42.79584  -8.63846  -18.49658 0.000 19.21083 ? 276 ARG A NH2   1 
ATOM   2138 N  N     . ARG A 1 277 ? 42.32158  -17.30668 -14.97994 1.000 12.76803 ? 277 ARG A N     1 
ATOM   2139 C  CA    . ARG A 1 277 ? 42.68438  -18.39699 -14.08853 1.000 13.81159 ? 277 ARG A CA    1 
ATOM   2140 C  C     . ARG A 1 277 ? 42.11590  -19.73705 -14.52705 1.000 12.99537 ? 277 ARG A C     1 
ATOM   2141 O  O     . ARG A 1 277 ? 42.42264  -20.75642 -13.89932 1.000 10.98437 ? 277 ARG A O     1 
ATOM   2142 C  CB    . ARG A 1 277 ? 42.22346  -18.08916 -12.65562 1.000 13.24780 ? 277 ARG A CB    1 
ATOM   2143 C  CG    . ARG A 1 277 ? 42.87540  -16.84696 -12.06813 1.000 13.83503 ? 277 ARG A CG    1 
ATOM   2144 C  CD    . ARG A 1 277 ? 42.44642  -16.59686 -10.63041 1.000 13.87897 ? 277 ARG A CD    1 
ATOM   2145 N  NE    . ARG A 1 277 ? 43.17176  -15.47403 -10.04729 0.000 13.89524 ? 277 ARG A NE    1 
ATOM   2146 C  CZ    . ARG A 1 277 ? 43.00247  -15.02950 -8.80964  0.000 13.98114 ? 277 ARG A CZ    1 
ATOM   2147 N  NH1   . ARG A 1 277 ? 42.12883  -15.58788 -7.98772  0.000 13.99218 ? 277 ARG A NH1   1 
ATOM   2148 N  NH2   . ARG A 1 277 ? 43.72859  -13.99870 -8.38605  0.000 13.98583 ? 277 ARG A NH2   1 
ATOM   2149 N  N     . HIS A 1 278 ? 41.29754  -19.76061 -15.57750 1.000 15.15702 ? 278 HIS A N     1 
ATOM   2150 C  CA    . HIS A 1 278 ? 40.74153  -20.99163 -16.13445 1.000 13.46169 ? 278 HIS A CA    1 
ATOM   2151 C  C     . HIS A 1 278 ? 40.98550  -20.96267 -17.63746 1.000 14.61895 ? 278 HIS A C     1 
ATOM   2152 O  O     . HIS A 1 278 ? 40.16048  -20.44470 -18.40346 1.000 12.48157 ? 278 HIS A O     1 
ATOM   2153 C  CB    . HIS A 1 278 ? 39.25654  -21.12763 -15.80742 1.000 11.17593 ? 278 HIS A CB    1 
ATOM   2154 C  CG    . HIS A 1 278 ? 38.96357  -21.17259 -14.33941 1.000 13.52309 ? 278 HIS A CG    1 
ATOM   2155 N  ND1   . HIS A 1 278 ? 38.85960  -22.35457 -13.63837 1.000 16.52394 ? 278 HIS A ND1   1 
ATOM   2156 C  CD2   . HIS A 1 278 ? 38.75759  -20.18256 -13.43943 1.000 12.53715 ? 278 HIS A CD2   1 
ATOM   2157 C  CE1   . HIS A 1 278 ? 38.60062  -22.09053 -12.37037 1.000 17.45065 ? 278 HIS A CE1   1 
ATOM   2158 N  NE2   . HIS A 1 278 ? 38.53362  -20.77953 -12.22341 1.000 15.76361 ? 278 HIS A NE2   1 
ATOM   2159 N  N     . PRO A 1 279 ? 42.11450  -21.51268 -18.09746 1.000 11.67693 ? 279 PRO A N     1 
ATOM   2160 C  CA    . PRO A 1 279 ? 42.46147  -21.39472 -19.52348 1.000 13.06983 ? 279 PRO A CA    1 
ATOM   2161 C  C     . PRO A 1 279 ? 41.51645  -22.13175 -20.45543 1.000 11.21723 ? 279 PRO A C     1 
ATOM   2162 O  O     . PRO A 1 279 ? 41.46142  -21.78879 -21.64344 1.000 10.20324 ? 279 PRO A O     1 
ATOM   2163 C  CB    . PRO A 1 279 ? 43.87847  -21.98171 -19.58849 1.000 11.59117 ? 279 PRO A CB    1 
ATOM   2164 C  CG    . PRO A 1 279 ? 43.96050  -22.89567 -18.40946 1.000 14.66457 ? 279 PRO A CG    1 
ATOM   2165 C  CD    . PRO A 1 279 ? 43.13652  -22.24864 -17.33446 1.000 11.48240 ? 279 PRO A CD    1 
ATOM   2166 N  N     . ALA A 1 280 ? 40.77747  -23.12774 -19.96839 1.000 13.25744 ? 280 ALA A N     1 
ATOM   2167 C  CA    . ALA A 1 280 ? 39.83346  -23.86878 -20.79235 1.000 12.87287 ? 280 ALA A CA    1 
ATOM   2168 C  C     . ALA A 1 280 ? 38.43145  -23.27379 -20.75833 1.000 10.39308 ? 280 ALA A C     1 
ATOM   2169 O  O     . ALA A 1 280 ? 37.45546  -23.99280 -21.00529 1.000 9.77044  ? 280 ALA A O     1 
ATOM   2170 C  CB    . ALA A 1 280 ? 39.79648  -25.33676 -20.36130 1.000 10.81681 ? 280 ALA A CB    1 
ATOM   2171 N  N     . HIS A 1 281 ? 38.30745  -21.98078 -20.46637 1.000 11.87944 ? 281 HIS A N     1 
ATOM   2172 C  CA    . HIS A 1 281 ? 36.99845  -21.35079 -20.39936 1.000 9.93533  ? 281 HIS A CA    1 
ATOM   2173 C  C     . HIS A 1 281 ? 36.34242  -21.32283 -21.77535 1.000 9.21937  ? 281 HIS A C     1 
ATOM   2174 O  O     . HIS A 1 281 ? 37.01340  -21.32686 -22.81136 1.000 10.05933 ? 281 HIS A O     1 
ATOM   2175 C  CB    . HIS A 1 281 ? 37.11445  -19.93077 -19.84641 1.000 10.89234 ? 281 HIS A CB    1 
ATOM   2176 C  CG    . HIS A 1 281 ? 37.89742  -19.00079 -20.72045 1.000 10.86971 ? 281 HIS A CG    1 
ATOM   2177 N  ND1   . HIS A 1 281 ? 37.34439  -18.35583 -21.80546 1.000 11.34507 ? 281 HIS A ND1   1 
ATOM   2178 C  CD2   . HIS A 1 281 ? 39.19042  -18.60478 -20.66549 1.000 11.64028 ? 281 HIS A CD2   1 
ATOM   2179 C  CE1   . HIS A 1 281 ? 38.26338  -17.60284 -22.38350 1.000 10.87468 ? 281 HIS A CE1   1 
ATOM   2180 N  NE2   . HIS A 1 281 ? 39.39239  -17.73681 -21.71252 1.000 10.71874 ? 281 HIS A NE2   1 
ATOM   2181 N  N     . SER A 1 282 ? 35.01242  -21.29584 -21.77632 1.000 9.90815  ? 282 SER A N     1 
ATOM   2182 C  CA    . SER A 1 282 ? 34.26439  -21.29589 -23.02431 1.000 10.78949 ? 282 SER A CA    1 
ATOM   2183 C  C     . SER A 1 282 ? 34.47436  -19.98791 -23.77835 1.000 9.57575  ? 282 SER A C     1 
ATOM   2184 O  O     . SER A 1 282 ? 34.74037  -18.93689 -23.18939 1.000 10.02886 ? 282 SER A O     1 
ATOM   2185 C  CB    . SER A 1 282 ? 32.77540  -21.51789 -22.75427 1.000 11.82063 ? 282 SER A CB    1 
ATOM   2186 O  OG    . SER A 1 282 ? 32.26941  -20.56087 -21.84029 1.000 10.13034 ? 282 SER A OG    1 
ATOM   2187 N  N     . GLN A 1 283 ? 34.35834  -20.06595 -25.09734 1.000 8.88987  ? 283 GLN A N     1 
ATOM   2188 C  CA    . GLN A 1 283 ? 34.52931  -18.93697 -25.99338 1.000 9.47049  ? 283 GLN A CA    1 
ATOM   2189 C  C     . GLN A 1 283 ? 33.18529  -18.50100 -26.56737 1.000 12.29212 ? 283 GLN A C     1 
ATOM   2190 O  O     . GLN A 1 283 ? 32.20830  -19.25601 -26.52432 1.000 10.83232 ? 283 GLN A O     1 
ATOM   2191 C  CB    . GLN A 1 283 ? 35.48829  -19.30300 -27.13739 1.000 12.67666 ? 283 GLN A CB    1 
ATOM   2192 C  CG    . GLN A 1 283 ? 36.83230  -19.84898 -26.67740 1.000 13.81193 ? 283 GLN A CG    1 
ATOM   2193 C  CD    . GLN A 1 283 ? 37.65831  -18.82795 -25.91645 1.000 13.45303 ? 283 GLN A CD    1 
ATOM   2194 O  OE1   . GLN A 1 283 ? 37.46930  -17.61995 -26.06448 1.000 15.06237 ? 283 GLN A OE1   1 
ATOM   2195 N  NE2   . GLN A 1 283 ? 38.58433  -19.31092 -25.09546 1.000 15.23340 ? 283 GLN A NE2   1 
ATOM   2196 N  N     . PRO A 1 284 ? 33.09127  -17.28102 -27.09240 1.000 11.98693 ? 284 PRO A N     1 
ATOM   2197 C  CA    . PRO A 1 284 ? 31.85226  -16.84805 -27.74939 1.000 10.25545 ? 284 PRO A CA    1 
ATOM   2198 C  C     . PRO A 1 284 ? 31.52024  -17.74809 -28.92635 1.000 11.73955 ? 284 PRO A C     1 
ATOM   2199 O  O     . PRO A 1 284 ? 32.41423  -18.39010 -29.49835 1.000 11.83523 ? 284 PRO A O     1 
ATOM   2200 C  CB    . PRO A 1 284 ? 32.17824  -15.41906 -28.21144 1.000 10.35103 ? 284 PRO A CB    1 
ATOM   2201 C  CG    . PRO A 1 284 ? 33.23625  -14.96102 -27.27648 1.000 10.87679 ? 284 PRO A CG    1 
ATOM   2202 C  CD    . PRO A 1 284 ? 34.06227  -16.17801 -26.97646 1.000 10.18497 ? 284 PRO A CD    1 
ATOM   2203 N  N     . PRO A 1 285 ? 30.24523  -17.81511 -29.32833 1.000 10.60868 ? 285 PRO A N     1 
ATOM   2204 C  CA    . PRO A 1 285 ? 29.08824  -17.08010 -28.79932 1.000 11.79339 ? 285 PRO A CA    1 
ATOM   2205 C  C     . PRO A 1 285 ? 28.39627  -17.77607 -27.62929 1.000 10.37670 ? 285 PRO A C     1 
ATOM   2206 O  O     . PRO A 1 285 ? 27.38627  -17.28507 -27.12928 1.000 10.54773 ? 285 PRO A O     1 
ATOM   2207 C  CB    . PRO A 1 285 ? 28.17021  -16.99615 -30.02131 1.000 11.51929 ? 285 PRO A CB    1 
ATOM   2208 C  CG    . PRO A 1 285 ? 28.40620  -18.30917 -30.71727 1.000 8.56062  ? 285 PRO A CG    1 
ATOM   2209 C  CD    . PRO A 1 285 ? 29.87721  -18.61615 -30.51129 1.000 10.27180 ? 285 PRO A CD    1 
ATOM   2210 N  N     . VAL A 1 286 ? 28.90928  -18.91805 -27.16126 1.000 10.26335 ? 286 VAL A N     1 
ATOM   2211 C  CA    . VAL A 1 286 ? 28.23131  -19.67503 -26.11023 1.000 10.51473 ? 286 VAL A CA    1 
ATOM   2212 C  C     . VAL A 1 286 ? 28.70034  -19.31298 -24.70825 1.000 9.57927  ? 286 VAL A C     1 
ATOM   2213 O  O     . VAL A 1 286 ? 28.06136  -19.72496 -23.72822 1.000 9.37059  ? 286 VAL A O     1 
ATOM   2214 C  CB    . VAL A 1 286 ? 28.41132  -21.19203 -26.31918 1.000 9.80573  ? 286 VAL A CB    1 
ATOM   2215 C  CG1   . VAL A 1 286 ? 27.81030  -21.62108 -27.64816 1.000 9.91446  ? 286 VAL A CG1   1 
ATOM   2216 C  CG2   . VAL A 1 286 ? 29.88333  -21.56702 -26.24720 1.000 10.65363 ? 286 VAL A CG2   1 
ATOM   2217 N  N     . SER A 1 287 ? 29.78834  -18.55797 -24.57629 1.000 9.00997  ? 287 SER A N     1 
ATOM   2218 C  CA    . SER A 1 287 ? 30.31436  -18.22393 -23.26331 1.000 9.45817  ? 287 SER A CA    1 
ATOM   2219 C  C     . SER A 1 287 ? 29.44337  -17.16491 -22.58733 1.000 6.97069  ? 287 SER A C     1 
ATOM   2220 O  O     . SER A 1 287 ? 28.58235  -16.53394 -23.20633 1.000 6.08855  ? 287 SER A O     1 
ATOM   2221 C  CB    . SER A 1 287 ? 31.75436  -17.72592 -23.37536 1.000 7.06747  ? 287 SER A CB    1 
ATOM   2222 O  OG    . SER A 1 287 ? 31.82033  -16.53494 -24.13740 1.000 6.57572  ? 287 SER A OG    1 
ATOM   2223 N  N     . LEU A 1 288 ? 29.68039  -16.97787 -21.28534 1.000 6.42814  ? 288 LEU A N     1 
ATOM   2224 C  CA    . LEU A 1 288 ? 28.98840  -15.91885 -20.55836 1.000 6.73971  ? 288 LEU A CA    1 
ATOM   2225 C  C     . LEU A 1 288 ? 29.38938  -14.54787 -21.08341 1.000 5.97014  ? 288 LEU A C     1 
ATOM   2226 O  O     . LEU A 1 288 ? 28.55537  -13.63888 -21.17142 1.000 5.83774  ? 288 LEU A O     1 
ATOM   2227 C  CB    . LEU A 1 288 ? 29.27743  -16.02581 -19.06136 1.000 8.89168  ? 288 LEU A CB    1 
ATOM   2228 C  CG    . LEU A 1 288 ? 28.06945  -16.29879 -18.16333 1.000 6.52483  ? 288 LEU A CG    1 
ATOM   2229 C  CD1   . LEU A 1 288 ? 28.44948  -16.16974 -16.69734 1.000 10.43086 ? 288 LEU A CD1   1 
ATOM   2230 C  CD2   . LEU A 1 288 ? 26.91644  -15.36981 -18.50933 1.000 5.75950  ? 288 LEU A CD2   1 
ATOM   2231 N  N     . ARG A 1 289 ? 30.66773  -14.37891 -21.43263 1.000 6.12704  ? 289 ARG A N     1 
ATOM   2232 C  CA    . ARG A 1 289 ? 31.09887  -13.14880 -22.08739 1.000 6.14700  ? 289 ARG A CA    1 
ATOM   2233 C  C     . ARG A 1 289 ? 30.41393  -12.98368 -23.43705 1.000 6.11780  ? 289 ARG A C     1 
ATOM   2234 O  O     . ARG A 1 289 ? 30.07776  -11.86375 -23.84097 1.000 6.06997  ? 289 ARG A O     1 
ATOM   2235 C  CB    . ARG A 1 289 ? 32.61966  -13.14663 -22.25033 1.000 8.28063  ? 289 ARG A CB    1 
ATOM   2236 C  CG    . ARG A 1 289 ? 33.15493  -12.00242 -23.09886 1.000 6.60174  ? 289 ARG A CG    1 
ATOM   2237 C  CD    . ARG A 1 289 ? 34.66719  -12.06232 -23.23088 1.000 7.24103  ? 289 ARG A CD    1 
ATOM   2238 N  NE    . ARG A 1 289 ? 35.17617  -11.01213 -24.10503 1.000 8.19817  ? 289 ARG A NE    1 
ATOM   2239 C  CZ    . ARG A 1 289 ? 35.42518  -11.16812 -25.39822 1.000 7.80327  ? 289 ARG A CZ    1 
ATOM   2240 N  NH1   . ARG A 1 289 ? 35.23814  -12.32938 -26.00325 1.000 11.28959 ? 289 ARG A NH1   1 
ATOM   2241 N  NH2   . ARG A 1 289 ? 35.87396  -10.13305 -26.10221 1.000 9.33700  ? 289 ARG A NH2   1 
ATOM   2242 N  N     . GLY A 1 290 ? 30.19131  -14.09295 -24.14544 1.000 6.18371  ? 290 GLY A N     1 
ATOM   2243 C  CA    . GLY A 1 290 ? 29.49628  -14.02200 -25.41842 1.000 6.19747  ? 290 GLY A CA    1 
ATOM   2244 C  C     . GLY A 1 290 ? 28.06428  -13.54500 -25.28741 1.000 6.00659  ? 290 GLY A C     1 
ATOM   2245 O  O     . GLY A 1 290 ? 27.52626  -12.92504 -26.20842 1.000 6.55769  ? 290 GLY A O     1 
ATOM   2246 N  N     . GLN A 1 291 ? 27.42731  -13.82097 -24.14639 1.000 5.86546  ? 291 GLN A N     1 
ATOM   2247 C  CA    . GLN A 1 291 ? 26.06231  -13.34998 -23.93637 1.000 5.71549  ? 291 GLN A CA    1 
ATOM   2248 C  C     . GLN A 1 291 ? 26.01530  -11.83098 -23.83742 1.000 5.67574  ? 291 GLN A C     1 
ATOM   2249 O  O     . GLN A 1 291 ? 25.08528  -11.19800 -24.34942 1.000 5.64189  ? 291 GLN A O     1 
ATOM   2250 C  CB    . GLN A 1 291 ? 25.46934  -13.99695 -22.68534 1.000 5.69935  ? 291 GLN A CB    1 
ATOM   2251 C  CG    . GLN A 1 291 ? 25.53335  -15.51695 -22.68830 1.000 5.69920  ? 291 GLN A CG    1 
ATOM   2252 C  CD    . GLN A 1 291 ? 24.96733  -16.12499 -23.95826 1.000 5.76189  ? 291 GLN A CD    1 
ATOM   2253 O  OE1   . GLN A 1 291 ? 25.63732  -16.90300 -24.63926 1.000 9.20365  ? 291 GLN A OE1   1 
ATOM   2254 N  NE2   . GLN A 1 291 ? 23.72832  -15.77601 -24.28125 1.000 6.04180  ? 291 GLN A NE2   1 
ATOM   2255 N  N     . LEU A 1 292 ? 27.01231  -11.22695 -23.18346 1.000 5.71388  ? 292 LEU A N     1 
ATOM   2256 C  CA    . LEU A 1 292 ? 27.11130  -9.77095  -23.17450 1.000 5.72988  ? 292 LEU A CA    1 
ATOM   2257 C  C     . LEU A 1 292 ? 27.40226  -9.22599  -24.56553 1.000 5.84986  ? 292 LEU A C     1 
ATOM   2258 O  O     . LEU A 1 292 ? 27.00225  -8.10100  -24.88555 1.000 5.87443  ? 292 LEU A O     1 
ATOM   2259 C  CB    . LEU A 1 292 ? 28.19231  -9.31691  -22.19454 1.000 5.78815  ? 292 LEU A CB    1 
ATOM   2260 C  CG    . LEU A 1 292 ? 27.90935  -9.52687  -20.70753 1.000 5.72406  ? 292 LEU A CG    1 
ATOM   2261 C  CD1   . LEU A 1 292 ? 29.07436  -9.02583  -19.86757 1.000 6.81671  ? 292 LEU A CD1   1 
ATOM   2262 C  CD2   . LEU A 1 292 ? 26.61935  -8.82986  -20.30952 1.000 5.63519  ? 292 LEU A CD2   1 
ATOM   2263 N  N     . LEU A 1 293 ? 28.09425  -10.00301 -25.40252 1.000 5.96679  ? 293 LEU A N     1 
ATOM   2264 C  CA    . LEU A 1 293 ? 28.35722  -9.55805  -26.76554 1.000 6.13038  ? 293 LEU A CA    1 
ATOM   2265 C  C     . LEU A 1 293 ? 27.09420  -9.61208  -27.61551 1.000 6.11462  ? 293 LEU A C     1 
ATOM   2266 O  O     . LEU A 1 293 ? 26.88618  -8.75111  -28.47653 1.000 6.77344  ? 293 LEU A O     1 
ATOM   2267 C  CB    . LEU A 1 293 ? 29.47121  -10.40006 -27.38653 1.000 6.31170  ? 293 LEU A CB    1 
ATOM   2268 C  CG    . LEU A 1 293 ? 30.84823  -10.26603 -26.73257 1.000 6.39776  ? 293 LEU A CG    1 
ATOM   2269 C  CD1   . LEU A 1 293 ? 31.88222  -11.10004 -27.47056 1.000 6.62808  ? 293 LEU A CD1   1 
ATOM   2270 C  CD2   . LEU A 1 293 ? 31.27522  -8.80702  -26.67462 1.000 9.68327  ? 293 LEU A CD2   1 
ATOM   2271 N  N     . TRP A 1 294 ? 26.24021  -10.61708 -27.39146 1.000 6.00964  ? 294 TRP A N     1 
ATOM   2272 C  CA    . TRP A 1 294 ? 24.93320  -10.63311 -28.04343 1.000 6.45151  ? 294 TRP A CA    1 
ATOM   2273 C  C     . TRP A 1 294 ? 24.14320  -9.37611  -27.70645 1.000 5.93220  ? 294 TRP A C     1 
ATOM   2274 O  O     . TRP A 1 294 ? 23.48518  -8.79214  -28.57646 1.000 6.03044  ? 294 TRP A O     1 
ATOM   2275 C  CB    . TRP A 1 294 ? 24.14522  -11.87811 -27.63038 1.000 6.62062  ? 294 TRP A CB    1 
ATOM   2276 C  CG    . TRP A 1 294 ? 24.58322  -13.14112 -28.30435 1.000 7.27705  ? 294 TRP A CG    1 
ATOM   2277 C  CD1   . TRP A 1 294 ? 25.24624  -14.18810 -27.73333 1.000 8.12839  ? 294 TRP A CD1   1 
ATOM   2278 C  CD2   . TRP A 1 294 ? 24.38219  -13.49517 -29.67833 1.000 9.23774  ? 294 TRP A CD2   1 
ATOM   2279 N  NE1   . TRP A 1 294 ? 25.47322  -15.17013 -28.66630 1.000 9.52554  ? 294 TRP A NE1   1 
ATOM   2280 C  CE2   . TRP A 1 294 ? 24.95219  -14.76917 -29.86831 1.000 10.00120 ? 294 TRP A CE2   1 
ATOM   2281 C  CE3   . TRP A 1 294 ? 23.77616  -12.85820 -30.76534 1.000 8.09249  ? 294 TRP A CE3   1 
ATOM   2282 C  CZ2   . TRP A 1 294 ? 24.93417  -15.41920 -31.10129 1.000 13.32876 ? 294 TRP A CZ2   1 
ATOM   2283 C  CZ3   . TRP A 1 294 ? 23.76014  -13.50424 -31.98832 1.000 11.17502 ? 294 TRP A CZ3   1 
ATOM   2284 C  CH2   . TRP A 1 294 ? 24.33515  -14.77124 -32.14529 1.000 11.31791 ? 294 TRP A CH2   1 
ATOM   2285 N  N     . ARG A 1 295 ? 24.19510  -8.94750  -26.44408 1.000 5.80685  ? 295 ARG A N     1 
ATOM   2286 C  CA    . ARG A 1 295 ? 23.57459  -7.68505  -26.06128 1.000 5.79413  ? 295 ARG A CA    1 
ATOM   2287 C  C     . ARG A 1 295 ? 24.24713  -6.51248  -26.76240 1.000 5.95944  ? 295 ARG A C     1 
ATOM   2288 O  O     . ARG A 1 295 ? 23.57022  -5.60975  -27.26763 1.000 6.05156  ? 295 ARG A O     1 
ATOM   2289 C  CB    . ARG A 1 295 ? 23.63865  -7.51887  -24.54322 1.000 5.68129  ? 295 ARG A CB    1 
ATOM   2290 C  CG    . ARG A 1 295 ? 23.14251  -6.18295  -24.02697 1.000 5.71508  ? 295 ARG A CG    1 
ATOM   2291 C  CD    . ARG A 1 295 ? 23.22312  -6.13370  -22.50900 1.000 5.72641  ? 295 ARG A CD    1 
ATOM   2292 N  NE    . ARG A 1 295 ? 22.82297  -4.83681  -21.97663 1.000 5.72910  ? 295 ARG A NE    1 
ATOM   2293 C  CZ    . ARG A 1 295 ? 23.65905  -3.83505  -21.74182 1.000 6.07688  ? 295 ARG A CZ    1 
ATOM   2294 N  NH1   . ARG A 1 295 ? 24.95443  -3.94352  -21.98721 1.000 5.88251  ? 295 ARG A NH1   1 
ATOM   2295 N  NH2   . ARG A 1 295 ? 23.18371  -2.69524  -21.24675 1.000 7.23790  ? 295 ARG A NH2   1 
ATOM   2296 N  N     . GLU A 1 296 ? 25.58119  -6.51707  -26.81257 1.000 6.03296  ? 296 GLU A N     1 
ATOM   2297 C  CA    . GLU A 1 296 ? 26.30717  -5.44608  -27.48462 1.000 6.22396  ? 296 GLU A CA    1 
ATOM   2298 C  C     . GLU A 1 296 ? 26.11514  -5.49713  -28.99561 1.000 6.85185  ? 296 GLU A C     1 
ATOM   2299 O  O     . GLU A 1 296 ? 26.10312  -4.45115  -29.65464 1.000 7.23976  ? 296 GLU A O     1 
ATOM   2300 C  CB    . GLU A 1 296 ? 27.79418  -5.52606  -27.13365 1.000 6.28470  ? 296 GLU A CB    1 
ATOM   2301 C  CG    . GLU A 1 296 ? 28.60716  -4.30207  -27.53570 1.000 8.63359  ? 296 GLU A CG    1 
ATOM   2302 C  CD    . GLU A 1 296 ? 28.42817  -3.13904  -26.57873 1.000 6.47329  ? 296 GLU A CD    1 
ATOM   2303 O  OE1   . GLU A 1 296 ? 27.92520  -3.36101  -25.45671 1.000 6.30742  ? 296 GLU A OE1   1 
ATOM   2304 O  OE2   . GLU A 1 296 ? 28.79216  -2.00405  -26.94677 1.000 6.66069  ? 296 GLU A OE2   1 
ATOM   2305 N  N     . PHE A 1 297 ? 25.96114  -6.69815  -29.55957 1.000 6.39982  ? 297 PHE A N     1 
ATOM   2306 C  CA    . PHE A 1 297 ? 25.79911  -6.82520  -31.00456 1.000 7.56395  ? 297 PHE A CA    1 
ATOM   2307 C  C     . PHE A 1 297 ? 24.44209  -6.30322  -31.46055 1.000 7.51479  ? 297 PHE A C     1 
ATOM   2308 O  O     . PHE A 1 297 ? 24.34707  -5.61025  -32.48057 1.000 6.88767  ? 297 PHE A O     1 
ATOM   2309 C  CB    . PHE A 1 297 ? 25.98811  -8.28421  -31.42152 1.000 7.93409  ? 297 PHE A CB    1 
ATOM   2310 C  CG    . PHE A 1 297 ? 25.56608  -8.57725  -32.83151 1.000 9.14760  ? 297 PHE A CG    1 
ATOM   2311 C  CD1   . PHE A 1 297 ? 26.21206  -7.98228  -33.90154 1.000 9.50009  ? 297 PHE A CD1   1 
ATOM   2312 C  CD2   . PHE A 1 297 ? 24.53409  -9.46527  -33.08646 1.000 8.88407  ? 297 PHE A CD2   1 
ATOM   2313 C  CE1   . PHE A 1 297 ? 25.82703  -8.25932  -35.19952 1.000 13.51650 ? 297 PHE A CE1   1 
ATOM   2314 C  CE2   . PHE A 1 297 ? 24.14406  -9.74631  -34.38244 1.000 10.11536 ? 297 PHE A CE2   1 
ATOM   2315 C  CZ    . PHE A 1 297 ? 24.79203  -9.14134  -35.44047 1.000 11.12839 ? 297 PHE A CZ    1 
ATOM   2316 N  N     . PHE A 1 298 ? 23.37911  -6.62021  -30.71652 1.000 6.56050  ? 298 PHE A N     1 
ATOM   2317 C  CA    . PHE A 1 298 ? 22.05210  -6.14623  -31.09251 1.000 6.51296  ? 298 PHE A CA    1 
ATOM   2318 C  C     . PHE A 1 298 ? 21.89609  -4.65222  -30.84255 1.000 6.92242  ? 298 PHE A C     1 
ATOM   2319 O  O     . PHE A 1 298 ? 21.13207  -3.98425  -31.54855 1.000 7.00151  ? 298 PHE A O     1 
ATOM   2320 C  CB    . PHE A 1 298 ? 20.98212  -6.93321  -30.34046 1.000 6.31431  ? 298 PHE A CB    1 
ATOM   2321 C  CG    . PHE A 1 298 ? 20.90513  -8.37923  -30.73941 1.000 6.29790  ? 298 PHE A CG    1 
ATOM   2322 C  CD1   . PHE A 1 298 ? 21.27910  -8.78126  -32.01041 1.000 7.77732  ? 298 PHE A CD1   1 
ATOM   2323 C  CD2   . PHE A 1 298 ? 20.45715  -9.33720  -29.84438 1.000 6.32142  ? 298 PHE A CD2   1 
ATOM   2324 C  CE1   . PHE A 1 298 ? 21.20710  -10.11027 -32.38437 1.000 8.27852  ? 298 PHE A CE1   1 
ATOM   2325 C  CE2   . PHE A 1 298 ? 20.38516  -10.66821 -30.21133 1.000 6.13003  ? 298 PHE A CE2   1 
ATOM   2326 C  CZ    . PHE A 1 298 ? 20.76013  -11.05425 -31.48233 1.000 7.16485  ? 298 PHE A CZ    1 
ATOM   2327 N  N     . TYR A 1 299 ? 22.60511  -4.11119  -29.84858 1.000 6.49760  ? 299 TYR A N     1 
ATOM   2328 C  CA    . TYR A 1 299 ? 22.59410  -2.66818  -29.63562 1.000 8.00273  ? 299 TYR A CA    1 
ATOM   2329 C  C     . TYR A 1 299 ? 23.31307  -1.93921  -30.76366 1.000 7.46881  ? 299 TYR A C     1 
ATOM   2330 O  O     . TYR A 1 299 ? 22.90906  -0.83922  -31.15668 1.000 8.11454  ? 299 TYR A O     1 
ATOM   2331 C  CB    . TYR A 1 299 ? 23.23313  -2.32813  -28.28965 1.000 6.49080  ? 299 TYR A CB    1 
ATOM   2332 C  CG    . TYR A 1 299 ? 22.24415  -2.09411  -27.17063 1.000 6.94714  ? 299 TYR A CG    1 
ATOM   2333 C  CD1   . TYR A 1 299 ? 21.74318  -3.15309  -26.42459 1.000 7.58174  ? 299 TYR A CD1   1 
ATOM   2334 C  CD2   . TYR A 1 299 ? 21.81715  -0.81110  -26.85366 1.000 8.96707  ? 299 TYR A CD2   1 
ATOM   2335 C  CE1   . TYR A 1 299 ? 20.84120  -2.94106  -25.39858 1.000 9.43348  ? 299 TYR A CE1   1 
ATOM   2336 C  CE2   . TYR A 1 299 ? 20.91617  -0.58808  -25.83065 1.000 10.44896 ? 299 TYR A CE2   1 
ATOM   2337 C  CZ    . TYR A 1 299 ? 20.43119  -1.65706  -25.10661 1.000 8.05368  ? 299 TYR A CZ    1 
ATOM   2338 O  OH    . TYR A 1 299 ? 19.53521  -1.44104  -24.08659 1.000 7.29861  ? 299 TYR A OH    1 
ATOM   2339 N  N     . THR A 1 300 ? 24.38107  -2.53822  -31.29466 1.000 7.23121  ? 300 THR A N     1 
ATOM   2340 C  CA    . THR A 1 300 ? 25.13504  -1.89524  -32.36570 1.000 8.77188  ? 300 THR A CA    1 
ATOM   2341 C  C     . THR A 1 300 ? 24.33301  -1.85629  -33.66068 1.000 10.02914 ? 300 THR A C     1 
ATOM   2342 O  O     . THR A 1 300 ? 24.33199  -0.84231  -34.36771 1.000 9.01430  ? 300 THR A O     1 
ATOM   2343 C  CB    . THR A 1 300 ? 26.46504  -2.62124  -32.57971 1.000 8.18432  ? 300 THR A CB    1 
ATOM   2344 O  OG1   . THR A 1 300 ? 27.16307  -2.71819  -31.33172 1.000 8.21726  ? 300 THR A OG1   1 
ATOM   2345 C  CG2   . THR A 1 300 ? 27.33101  -1.86826  -33.57875 1.000 10.29507 ? 300 THR A CG2   1 
ATOM   2346 N  N     . VAL A 1 301 ? 23.63701  -2.94830  -33.98364 1.000 11.13348 ? 301 VAL A N     1 
ATOM   2347 C  CA    . VAL A 1 301 ? 22.85099  -2.99035  -35.21262 1.000 10.41389 ? 301 VAL A CA    1 
ATOM   2348 C  C     . VAL A 1 301 ? 21.58199  -2.15935  -35.06562 1.000 10.17605 ? 301 VAL A C     1 
ATOM   2349 O  O     . VAL A 1 301 ? 21.21396  -1.40038  -35.96963 1.000 12.08708 ? 301 VAL A O     1 
ATOM   2350 C  CB    . VAL A 1 301 ? 22.52999  -4.44736  -35.59257 1.000 10.62628 ? 301 VAL A CB    1 
ATOM   2351 C  CG1   . VAL A 1 301 ? 21.73797  -4.49741  -36.88955 1.000 8.87166  ? 301 VAL A CG1   1 
ATOM   2352 C  CG2   . VAL A 1 301 ? 23.80900  -5.25835  -35.70857 1.000 10.99637 ? 301 VAL A CG2   1 
ATOM   2353 N  N     . GLY A 1 302 ? 20.90001  -2.28032  -33.92460 1.000 10.15748 ? 302 GLY A N     1 
ATOM   2354 C  CA    . GLY A 1 302 ? 19.62401  -1.60333  -33.76059 1.000 10.78469 ? 302 GLY A CA    1 
ATOM   2355 C  C     . GLY A 1 302 ? 19.74400  -0.09133  -33.74864 1.000 11.33996 ? 302 GLY A C     1 
ATOM   2356 O  O     . GLY A 1 302 ? 18.88998  0.61065   -34.29664 1.000 13.71508 ? 302 GLY A O     1 
ATOM   2357 N  N     . SER A 1 303 ? 20.80201  0.43370   -33.12668 1.000 11.51459 ? 303 SER A N     1 
ATOM   2358 C  CA    . SER A 1 303 ? 20.97900  1.87970   -33.05373 1.000 13.77066 ? 303 SER A CA    1 
ATOM   2359 C  C     . SER A 1 303 ? 21.30896  2.49467   -34.40675 1.000 13.64893 ? 303 SER A C     1 
ATOM   2360 O  O     . SER A 1 303 ? 21.14995  3.70866   -34.57479 1.000 15.74213 ? 303 SER A O     1 
ATOM   2361 C  CB    . SER A 1 303 ? 22.07301  2.22774   -32.04276 1.000 14.50264 ? 303 SER A CB    1 
ATOM   2362 O  OG    . SER A 1 303 ? 23.30801  1.63174   -32.40177 1.000 17.17784 ? 303 SER A OG    1 
ATOM   2363 N  N     . THR A 1 304 ? 21.75995  1.69264   -35.37074 1.000 12.42544 ? 304 THR A N     1 
ATOM   2364 C  CA    . THR A 1 304 ? 22.11192  2.18060   -36.69776 1.000 12.04695 ? 304 THR A CA    1 
ATOM   2365 C  C     . THR A 1 304 ? 21.16490  1.67456   -37.77772 1.000 13.97740 ? 304 THR A C     1 
ATOM   2366 O  O     . THR A 1 304 ? 21.40887  1.91653   -38.96474 1.000 14.92736 ? 304 THR A O     1 
ATOM   2367 C  CB    . THR A 1 304 ? 23.55191  1.79160   -37.04178 1.000 13.70656 ? 304 THR A CB    1 
ATOM   2368 O  OG1   . THR A 1 304 ? 23.68792  0.36561   -36.98874 1.000 14.69183 ? 304 THR A OG1   1 
ATOM   2369 C  CG2   . THR A 1 304 ? 24.52493  2.42464   -36.05682 1.000 15.97596 ? 304 THR A CG2   1 
ATOM   2370 N  N     . THR A 1 305 ? 20.09291  0.98057   -37.39868 1.000 12.88437 ? 305 THR A N     1 
ATOM   2371 C  CA    . THR A 1 305 ? 19.12490  0.46353   -38.35564 1.000 16.67783 ? 305 THR A CA    1 
ATOM   2372 C  C     . THR A 1 305 ? 17.78789  1.15453   -38.14464 1.000 14.17465 ? 305 THR A C     1 
ATOM   2373 O  O     . THR A 1 305 ? 17.18592  1.00555   -37.07062 1.000 16.06977 ? 305 THR A O     1 
ATOM   2374 C  CB    . THR A 1 305 ? 18.96991  -1.04947  -38.20959 1.000 13.97112 ? 305 THR A CB    1 
ATOM   2375 O  OG1   . THR A 1 305 ? 20.24591  -1.68046  -38.36260 1.000 11.21181 ? 305 THR A OG1   1 
ATOM   2376 C  CG2   . THR A 1 305 ? 18.01689  -1.59051  -39.26156 1.000 13.96011 ? 305 THR A CG2   1 
ATOM   2377 N  N     . PRO A 1 306 ? 17.28787  1.91149   -39.11765 1.000 15.14514 ? 306 PRO A N     1 
ATOM   2378 C  CA    . PRO A 1 306 ? 15.99887  2.58549   -38.93564 1.000 18.50567 ? 306 PRO A CA    1 
ATOM   2379 C  C     . PRO A 1 306 ? 14.84787  1.59348   -38.93759 1.000 16.48492 ? 306 PRO A C     1 
ATOM   2380 O  O     . PRO A 1 306 ? 14.86587  0.58446   -39.64656 1.000 18.93166 ? 306 PRO A O     1 
ATOM   2381 C  CB    . PRO A 1 306 ? 15.92083  3.53045   -40.13967 1.000 18.20725 ? 306 PRO A CB    1 
ATOM   2382 C  CG    . PRO A 1 306 ? 16.76282  2.87143   -41.17967 1.000 19.68153 ? 306 PRO A CG    1 
ATOM   2383 C  CD    . PRO A 1 306 ? 17.88384  2.19646   -40.43467 1.000 16.47703 ? 306 PRO A CD    1 
ATOM   2384 N  N     . ASN A 1 307 ? 13.83589  1.89949   -38.12258 1.000 16.59526 ? 307 ASN A N     1 
ATOM   2385 C  CA    . ASN A 1 307 ? 12.65490  1.04649   -37.96652 1.000 18.55365 ? 307 ASN A CA    1 
ATOM   2386 C  C     . ASN A 1 307 ? 13.05192  -0.37049  -37.55649 1.000 15.94695 ? 307 ASN A C     1 
ATOM   2387 O  O     . ASN A 1 307 ? 12.48192  -1.35751  -38.02545 1.000 17.13274 ? 307 ASN A O     1 
ATOM   2388 C  CB    . ASN A 1 307 ? 11.80987  1.03044   -39.24251 1.000 18.21031 ? 307 ASN A CB    1 
ATOM   2389 C  CG    . ASN A 1 307 ? 11.50885  2.42443   -39.75654 1.000 17.37469 ? 307 ASN A CG    1 
ATOM   2390 O  OD1   . ASN A 1 307 ? 10.53085  3.05143   -39.35254 1.000 19.08069 ? 307 ASN A OD1   1 
ATOM   2391 N  ND2   . ASN A 1 307 ? 12.35483  2.91741   -40.65357 1.000 20.99730 ? 307 ASN A ND2   1 
ATOM   2392 N  N     . PHE A 1 308 ? 14.04294  -0.46546  -36.66651 1.000 15.77612 ? 308 PHE A N     1 
ATOM   2393 C  CA    . PHE A 1 308 ? 14.55796  -1.75944  -36.23748 1.000 14.07195 ? 308 PHE A CA    1 
ATOM   2394 C  C     . PHE A 1 308 ? 13.52998  -2.57143  -35.45843 1.000 14.62983 ? 308 PHE A C     1 
ATOM   2395 O  O     . PHE A 1 308 ? 13.65799  -3.79742  -35.38040 1.000 12.51610 ? 308 PHE A O     1 
ATOM   2396 C  CB    . PHE A 1 308 ? 15.81797  -1.55541  -35.39251 1.000 12.37346 ? 308 PHE A CB    1 
ATOM   2397 C  CG    . PHE A 1 308 ? 16.48999  -2.83339  -34.97849 1.000 10.05976 ? 308 PHE A CG    1 
ATOM   2398 C  CD1   . PHE A 1 308 ? 17.26998  -3.54341  -35.87548 1.000 10.65642 ? 308 PHE A CD1   1 
ATOM   2399 C  CD2   . PHE A 1 308 ? 16.35202  -3.31735  -33.68747 1.000 9.25457  ? 308 PHE A CD2   1 
ATOM   2400 C  CE1   . PHE A 1 308 ? 17.89300  -4.71739  -35.49646 1.000 8.64734  ? 308 PHE A CE1   1 
ATOM   2401 C  CE2   . PHE A 1 308 ? 16.97204  -4.49133  -33.30145 1.000 9.10394  ? 308 PHE A CE2   1 
ATOM   2402 C  CZ    . PHE A 1 308 ? 17.74303  -5.19236  -34.20844 1.000 9.00237  ? 308 PHE A CZ    1 
ATOM   2403 N  N     . HIS A 1 309 ? 12.51499  -1.92342  -34.89043 1.000 17.25409 ? 309 HIS A N     1 
ATOM   2404 C  CA    . HIS A 1 309 ? 11.51101  -2.59840  -34.08039 1.000 16.33182 ? 309 HIS A CA    1 
ATOM   2405 C  C     . HIS A 1 309 ? 10.23200  -2.90443  -34.85035 1.000 15.09755 ? 309 HIS A C     1 
ATOM   2406 O  O     . HIS A 1 309 ? 9.22201   -3.25742  -34.23532 1.000 14.01548 ? 309 HIS A O     1 
ATOM   2407 C  CB    . HIS A 1 309 ? 11.18300  -1.76200  -32.84200 1.000 15.89279 ? 309 HIS A CB    1 
ATOM   2408 C  CG    . HIS A 1 309 ? 10.59100  -0.42600  -33.14600 1.000 18.88292 ? 309 HIS A CG    1 
ATOM   2409 N  ND1   . HIS A 1 309 ? 11.12400  0.46600   -34.05000 1.000 15.24796 ? 309 HIS A ND1   1 
ATOM   2410 C  CD2   . HIS A 1 309 ? 9.50100   0.16700   -32.64700 1.000 20.91474 ? 309 HIS A CD2   1 
ATOM   2411 C  CE1   . HIS A 1 309 ? 10.37200  1.55400   -34.09100 1.000 17.24650 ? 309 HIS A CE1   1 
ATOM   2412 N  NE2   . HIS A 1 309 ? 9.37900   1.39300   -33.24700 1.000 21.02568 ? 309 HIS A NE2   1 
ATOM   2413 N  N     . ARG A 1 310 ? 10.24975  -2.77865  -36.17642 1.000 13.69579 ? 310 ARG A N     1 
ATOM   2414 C  CA    . ARG A 1 310 ? 9.08506   -3.06852  -37.00026 1.000 16.90613 ? 310 ARG A CA    1 
ATOM   2415 C  C     . ARG A 1 310 ? 9.52980   -3.83469  -38.23928 1.000 16.30485 ? 310 ARG A C     1 
ATOM   2416 O  O     . ARG A 1 310 ? 10.72052  -4.08407  -38.44915 1.000 17.27012 ? 310 ARG A O     1 
ATOM   2417 C  CB    . ARG A 1 310 ? 8.33435   -1.78622  -37.38081 1.000 15.41815 ? 310 ARG A CB    1 
ATOM   2418 C  CG    . ARG A 1 310 ? 7.51227   -1.19206  -36.24839 1.000 20.26262 ? 310 ARG A CG    1 
ATOM   2419 C  CD    . ARG A 1 310 ? 6.53361   -0.14882  -36.76104 0.000 17.73568 ? 310 ARG A CD    1 
ATOM   2420 N  NE    . ARG A 1 310 ? 5.61169   0.28812   -35.71943 0.000 17.80179 ? 310 ARG A NE    1 
ATOM   2421 C  CZ    . ARG A 1 310 ? 5.80230   1.34778   -34.94572 0.000 17.81374 ? 310 ARG A CZ    1 
ATOM   2422 N  NH1   . ARG A 1 310 ? 6.87248   2.11472   -35.07543 0.000 17.99557 ? 310 ARG A NH1   1 
ATOM   2423 N  NH2   . ARG A 1 310 ? 4.89599   1.64591   -34.01896 0.000 17.73784 ? 310 ARG A NH2   1 
ATOM   2424 N  N     . MET A 1 311 ? 8.55392   -4.21458  -39.06528 1.000 18.95231 ? 311 MET A N     1 
ATOM   2425 C  CA    . MET A 1 311 ? 8.80690   -4.96161  -40.29326 1.000 21.24601 ? 311 MET A CA    1 
ATOM   2426 C  C     . MET A 1 311 ? 8.89486   -4.03965  -41.50529 1.000 19.40818 ? 311 MET A C     1 
ATOM   2427 O  O     . MET A 1 311 ? 9.91985   -4.00866  -42.19231 1.000 22.57175 ? 311 MET A O     1 
ATOM   2428 C  CB    . MET A 1 311 ? 7.71090   -6.01663  -40.49921 1.000 21.08837 ? 311 MET A CB    1 
ATOM   2429 C  CG    . MET A 1 311 ? 7.98088   -6.98166  -41.64318 1.000 21.11205 ? 311 MET A CG    1 
ATOM   2430 S  SD    . MET A 1 311 ? 6.57289   -8.04968  -42.00612 1.000 25.22996 ? 311 MET A SD    1 
ATOM   2431 C  CE    . MET A 1 311 ? 5.36786   -6.84471  -42.55713 1.000 24.31987 ? 311 MET A CE    1 
ATOM   2432 N  N     . ALA A 1 312 ? 7.83185   -3.28666  -41.77929 1.000 20.68321 ? 312 ALA A N     1 
ATOM   2433 C  CA    . ALA A 1 312 ? 7.83682   -2.36270  -42.90632 1.000 20.14662 ? 312 ALA A CA    1 
ATOM   2434 C  C     . ALA A 1 312 ? 8.81482   -1.22368  -42.65137 1.000 24.12058 ? 312 ALA A C     1 
ATOM   2435 O  O     . ALA A 1 312 ? 8.78984   -0.59365  -41.58939 1.000 25.15068 ? 312 ALA A O     1 
ATOM   2436 C  CB    . ALA A 1 312 ? 6.43181   -1.81272  -43.14631 1.000 24.23243 ? 312 ALA A CB    1 
ATOM   2437 N  N     . GLY A 1 313 ? 9.68079   -0.95970  -43.63040 1.000 24.57080 ? 313 GLY A N     1 
ATOM   2438 C  CA    . GLY A 1 313 ? 10.71279  0.04131   -43.49345 1.000 21.03017 ? 313 GLY A CA    1 
ATOM   2439 C  C     . GLY A 1 313 ? 11.99681  -0.45266  -42.86247 1.000 22.87993 ? 313 GLY A C     1 
ATOM   2440 O  O     . GLY A 1 313 ? 13.00580  0.26334   -42.90951 1.000 23.33188 ? 313 GLY A O     1 
ATOM   2441 N  N     . ASN A 1 314 ? 11.99383  -1.64465  -42.27743 1.000 21.47993 ? 314 ASN A N     1 
ATOM   2442 C  CA    . ASN A 1 314 ? 13.19885  -2.20062  -41.67844 1.000 20.25312 ? 314 ASN A CA    1 
ATOM   2443 C  C     . ASN A 1 314 ? 14.08683  -2.78364  -42.77144 1.000 17.03172 ? 314 ASN A C     1 
ATOM   2444 O  O     . ASN A 1 314 ? 13.67982  -3.74267  -43.43740 1.000 18.20076 ? 314 ASN A O     1 
ATOM   2445 C  CB    . ASN A 1 314 ? 12.83888  -3.27559  -40.66140 1.000 20.02703 ? 314 ASN A CB    1 
ATOM   2446 C  CG    . ASN A 1 314 ? 13.98590  -3.60355  -39.72341 1.000 17.21556 ? 314 ASN A CG    1 
ATOM   2447 O  OD1   . ASN A 1 314 ? 15.15189  -3.38255  -40.04644 1.000 18.07943 ? 314 ASN A OD1   1 
ATOM   2448 N  ND2   . ASN A 1 314 ? 13.65593  -4.13452  -38.55239 1.000 18.05647 ? 314 ASN A ND2   1 
ATOM   2449 N  N     . PRO A 1 315 ? 15.29282  -2.24864  -42.98948 1.000 20.60832 ? 315 PRO A N     1 
ATOM   2450 C  CA    . PRO A 1 315 ? 16.13380  -2.76067  -44.08248 1.000 19.78301 ? 315 PRO A CA    1 
ATOM   2451 C  C     . PRO A 1 315 ? 16.72082  -4.13465  -43.81645 1.000 19.90268 ? 315 PRO A C     1 
ATOM   2452 O  O     . PRO A 1 315 ? 17.18180  -4.78168  -44.76444 1.000 23.03127 ? 315 PRO A O     1 
ATOM   2453 C  CB    . PRO A 1 315 ? 17.23379  -1.69766  -44.20354 1.000 23.08584 ? 315 PRO A CB    1 
ATOM   2454 C  CG    . PRO A 1 315 ? 17.32481  -1.10962  -42.83756 1.000 21.44297 ? 315 PRO A CG    1 
ATOM   2455 C  CD    . PRO A 1 315 ? 15.92382  -1.11961  -42.28353 1.000 20.27076 ? 315 PRO A CD    1 
ATOM   2456 N  N     . VAL A 1 316 ? 16.72485  -4.60562  -42.56644 1.000 18.51610 ? 316 VAL A N     1 
ATOM   2457 C  CA    . VAL A 1 316 ? 17.29286  -5.91360  -42.24841 1.000 18.42239 ? 316 VAL A CA    1 
ATOM   2458 C  C     . VAL A 1 316 ? 16.23088  -6.97760  -42.01436 1.000 17.26496 ? 316 VAL A C     1 
ATOM   2459 O  O     . VAL A 1 316 ? 16.56789  -8.17260  -41.97833 1.000 18.09417 ? 316 VAL A O     1 
ATOM   2460 C  CB    . VAL A 1 316 ? 18.22689  -5.83656  -41.02143 1.000 22.09138 ? 316 VAL A CB    1 
ATOM   2461 C  CG1   . VAL A 1 316 ? 19.22488  -4.69756  -41.18349 1.000 20.61487 ? 316 VAL A CG1   1 
ATOM   2462 C  CG2   . VAL A 1 316 ? 17.42191  -5.67753  -39.74142 1.000 20.26515 ? 316 VAL A CG2   1 
ATOM   2463 N  N     . CYS A 1 317 ? 14.96788  -6.59361  -41.86034 1.000 18.52205 ? 317 CYS A N     1 
ATOM   2464 C  CA    . CYS A 1 317 ? 13.89689  -7.54661  -41.61729 1.000 18.32645 ? 317 CYS A CA    1 
ATOM   2465 C  C     . CYS A 1 317 ? 13.27287  -7.99866  -42.93126 1.000 17.78363 ? 317 CYS A C     1 
ATOM   2466 O  O     . CYS A 1 317 ? 13.19284  -7.23869  -43.90028 1.000 20.27828 ? 317 CYS A O     1 
ATOM   2467 C  CB    . CYS A 1 317 ? 12.82390  -6.93859  -40.71229 1.000 17.04753 ? 317 CYS A CB    1 
ATOM   2468 S  SG    . CYS A 1 317 ? 11.45192  -8.04959  -40.32722 1.000 17.70241 ? 317 CYS A SG    1 
ATOM   2469 N  N     . LYS A 1 318 ? 12.88987  -9.24366  -42.97322 1.000 19.76702 ? 318 LYS A N     1 
ATOM   2470 C  CA    . LYS A 1 318 ? 12.22785  -9.81370  -44.16819 1.000 19.12095 ? 318 LYS A CA    1 
ATOM   2471 C  C     . LYS A 1 318 ? 10.73185  -9.50571  -44.17316 1.000 19.43452 ? 318 LYS A C     1 
ATOM   2472 O  O     . LYS A 1 318 ? 10.12587  -9.51969  -43.11715 1.000 19.85910 ? 318 LYS A O     1 
ATOM   2473 C  CB    . LYS A 1 318 ? 12.47886  -11.31070 -44.20415 1.000 20.46888 ? 318 LYS A CB    1 
ATOM   2474 C  CG    . LYS A 1 318 ? 13.78385  -11.71671 -44.86716 1.000 26.32360 ? 318 LYS A CG    1 
ATOM   2475 C  CD    . LYS A 1 318 ? 13.55683  -12.50075 -46.12313 1.000 26.15705 ? 318 LYS A CD    1 
ATOM   2476 C  CE    . LYS A 1 318 ? 12.35284  -13.40876 -46.00708 1.000 27.67014 ? 318 LYS A CE    1 
ATOM   2477 N  NZ    . LYS A 1 318 ? 11.80082  -13.71980 -47.34106 1.000 32.84585 ? 318 LYS A NZ    1 
ATOM   2478 N  N     . GLN A 1 319 ? 10.20182  -9.21775  -45.35416 1.000 21.68828 ? 319 GLN A N     1 
ATOM   2479 C  CA    . GLN A 1 319 ? 8.78682   -8.90577  -45.55314 1.000 22.58063 ? 319 GLN A CA    1 
ATOM   2480 C  C     . GLN A 1 319 ? 8.03782   -10.21678 -45.75309 1.000 20.88565 ? 319 GLN A C     1 
ATOM   2481 O  O     . GLN A 1 319 ? 7.84580   -10.68582 -46.87507 1.000 25.38801 ? 319 GLN A O     1 
ATOM   2482 C  CB    . GLN A 1 319 ? 8.60178   -7.96381  -46.73617 1.000 25.50936 ? 319 GLN A CB    1 
ATOM   2483 C  CG    . GLN A 1 319 ? 9.29878   -6.62380  -46.58122 1.000 23.00181 ? 319 GLN A CG    1 
ATOM   2484 C  CD    . GLN A 1 319 ? 8.72379   -5.79377  -45.45123 1.000 23.36198 ? 319 GLN A CD    1 
ATOM   2485 O  OE1   . GLN A 1 319 ? 9.28982   -5.73473  -44.36025 1.000 22.76764 ? 319 GLN A OE1   1 
ATOM   2486 N  NE2   . GLN A 1 319 ? 7.59578   -5.14378  -45.70923 1.000 28.66216 ? 319 GLN A NE2   1 
ATOM   2487 N  N     . ILE A 1 320 ? 7.60785   -10.81475 -44.64606 1.000 21.47502 ? 320 ILE A N     1 
ATOM   2488 C  CA    . ILE A 1 320 ? 6.88386   -12.08076 -44.65800 1.000 21.59527 ? 320 ILE A CA    1 
ATOM   2489 C  C     . ILE A 1 320 ? 5.39786   -11.79277 -44.51498 1.000 21.85109 ? 320 ILE A C     1 
ATOM   2490 O  O     . ILE A 1 320 ? 4.99687   -10.87975 -43.78100 1.000 19.30959 ? 320 ILE A O     1 
ATOM   2491 C  CB    . ILE A 1 320 ? 7.38789   -13.01672 -43.54199 1.000 22.56401 ? 320 ILE A CB    1 
ATOM   2492 C  CG1   . ILE A 1 320 ? 8.90289   -13.19971 -43.65501 1.000 24.16150 ? 320 ILE A CG1   1 
ATOM   2493 C  CG2   . ILE A 1 320 ? 6.68990   -14.36673 -43.60893 1.000 22.26456 ? 320 ILE A CG2   1 
ATOM   2494 C  CD1   . ILE A 1 320 ? 9.48892   -14.13268 -42.62000 1.000 23.23770 ? 320 ILE A CD1   1 
ATOM   2495 N  N     . ASP A 1 321 ? 4.57300   -12.56800 -45.22100 1.000 25.35213 ? 321 ASP A N     1 
ATOM   2496 C  CA    . ASP A 1 321 ? 3.11000   -12.32000 -45.25600 1.000 22.35967 ? 321 ASP A CA    1 
ATOM   2497 C  C     . ASP A 1 321 ? 2.43300   -12.93300 -44.02400 1.000 24.92879 ? 321 ASP A C     1 
ATOM   2498 O  O     . ASP A 1 321 ? 1.46700   -13.66300 -44.21000 1.000 25.63168 ? 321 ASP A O     1 
ATOM   2499 C  CB    . ASP A 1 321 ? 2.51400   -12.90200 -46.55200 1.000 27.20392 ? 321 ASP A CB    1 
ATOM   2500 C  CG    . ASP A 1 321 ? 2.51400   -11.96900 -47.77100 1.000 34.53251 ? 321 ASP A CG    1 
ATOM   2501 O  OD1   . ASP A 1 321 ? 3.61900   -11.58300 -48.21400 1.000 42.95573 ? 321 ASP A OD1   1 
ATOM   2502 O  OD2   . ASP A 1 321 ? 1.41300   -11.62900 -48.28400 1.000 38.75357 ? 321 ASP A OD2   1 
ATOM   2503 N  N     . TRP A 1 322 ? 2.87600   -12.61900 -42.80200 1.000 19.16667 ? 322 TRP A N     1 
ATOM   2504 C  CA    . TRP A 1 322 ? 2.29493   -13.16770 -41.57787 1.000 18.71902 ? 322 TRP A CA    1 
ATOM   2505 C  C     . TRP A 1 322 ? 0.76993   -13.09171 -41.54584 1.000 18.73593 ? 322 TRP A C     1 
ATOM   2506 O  O     . TRP A 1 322 ? 0.16791   -12.22174 -42.18386 1.000 21.07403 ? 322 TRP A O     1 
ATOM   2507 C  CB    . TRP A 1 322 ? 2.85095   -12.44066 -40.35491 1.000 17.79969 ? 322 TRP A CB    1 
ATOM   2508 C  CG    . TRP A 1 322 ? 4.34096   -12.47464 -40.24694 1.000 15.03734 ? 322 TRP A CG    1 
ATOM   2509 C  CD1   . TRP A 1 322 ? 5.20294   -11.44164 -40.47199 1.000 16.49832 ? 322 TRP A CD1   1 
ATOM   2510 C  CD2   . TRP A 1 322 ? 5.14897   -13.59963 -39.88492 1.000 16.63028 ? 322 TRP A CD2   1 
ATOM   2511 N  NE1   . TRP A 1 322 ? 6.49795   -11.85363 -40.27000 1.000 15.79007 ? 322 TRP A NE1   1 
ATOM   2512 C  CE2   . TRP A 1 322 ? 6.49197   -13.17562 -39.91096 1.000 14.94020 ? 322 TRP A CE2   1 
ATOM   2513 C  CE3   . TRP A 1 322 ? 4.86699   -14.92662 -39.54188 1.000 15.93671 ? 322 TRP A CE3   1 
ATOM   2514 C  CZ2   . TRP A 1 322 ? 7.55098   -14.02860 -39.60796 1.000 13.30572 ? 322 TRP A CZ2   1 
ATOM   2515 C  CZ3   . TRP A 1 322 ? 5.92000   -15.77260 -39.24087 1.000 14.72667 ? 322 TRP A CZ3   1 
ATOM   2516 C  CH2   . TRP A 1 322 ? 7.24500   -15.31959 -39.27591 1.000 14.96142 ? 322 TRP A CH2   1 
ATOM   2517 N  N     . ASP A 1 323 ? 0.14096   -13.98769 -40.78880 1.000 22.01285 ? 323 ASP A N     1 
ATOM   2518 C  CA    . ASP A 1 323 ? -1.31204  -14.02770 -40.70977 1.000 26.69968 ? 323 ASP A CA    1 
ATOM   2519 C  C     . ASP A 1 323 ? -1.83603  -13.02368 -39.68879 1.000 27.10226 ? 323 ASP A C     1 
ATOM   2520 O  O     . ASP A 1 323 ? -1.17101  -12.69464 -38.70282 1.000 23.84027 ? 323 ASP A O     1 
ATOM   2521 C  CB    . ASP A 1 323 ? -1.79702  -15.43170 -40.34072 1.000 23.46855 ? 323 ASP A CB    1 
ATOM   2522 C  CG    . ASP A 1 323 ? -1.70104  -16.40473 -41.49769 1.000 21.59408 ? 323 ASP A CG    1 
ATOM   2523 O  OD1   . ASP A 1 323 ? -1.49807  -15.94876 -42.64171 1.000 20.64431 ? 323 ASP A OD1   1 
ATOM   2524 O  OD2   . ASP A 1 323 ? -1.82602  -17.62472 -41.26465 1.000 19.11299 ? 323 ASP A OD2   1 
ATOM   2525 N  N     . ASP A 1 324 ? -3.04904  -12.53869 -39.93978 1.000 25.10970 ? 324 ASP A N     1 
ATOM   2526 C  CA    . ASP A 1 324 ? -3.75902  -11.64167 -39.03379 1.000 24.95414 ? 324 ASP A CA    1 
ATOM   2527 C  C     . ASP A 1 324 ? -4.89700  -12.44166 -38.40574 1.000 25.26401 ? 324 ASP A C     1 
ATOM   2528 O  O     . ASP A 1 324 ? -6.06001  -12.32368 -38.79472 1.000 22.16703 ? 324 ASP A O     1 
ATOM   2529 C  CB    . ASP A 1 324 ? -4.27005  -10.39670 -39.77482 1.000 26.73021 ? 324 ASP A CB    1 
ATOM   2530 C  CG    . ASP A 1 324 ? -4.89004  -9.37267  -38.84284 1.000 28.19724 ? 324 ASP A CG    1 
ATOM   2531 O  OD1   . ASP A 1 324 ? -4.78601  -9.53964  -37.60883 1.000 28.58292 ? 324 ASP A OD1   1 
ATOM   2532 O  OD2   . ASP A 1 324 ? -5.48706  -8.39569  -39.34585 1.000 27.21385 ? 324 ASP A OD2   1 
ATOM   2533 N  N     . ASN A 1 325 ? -4.54698  -13.26863 -37.42273 1.000 25.08305 ? 325 ASN A N     1 
ATOM   2534 C  CA    . ASN A 1 325 ? -5.50496  -14.14362 -36.74768 1.000 23.38794 ? 325 ASN A CA    1 
ATOM   2535 C  C     . ASN A 1 325 ? -5.62793  -13.72257 -35.29069 1.000 23.30375 ? 325 ASN A C     1 
ATOM   2536 O  O     . ASN A 1 325 ? -4.76291  -14.06654 -34.46570 1.000 23.94168 ? 325 ASN A O     1 
ATOM   2537 C  CB    . ASN A 1 325 ? -5.06895  -15.60462 -36.85064 1.000 21.14890 ? 325 ASN A CB    1 
ATOM   2538 C  CG    . ASN A 1 325 ? -6.22393  -16.57662 -36.67859 1.000 21.15865 ? 325 ASN A CG    1 
ATOM   2539 O  OD1   . ASN A 1 325 ? -6.41895  -17.47365 -37.49856 1.000 27.94809 ? 325 ASN A OD1   1 
ATOM   2540 N  ND2   . ASN A 1 325 ? -6.99491  -16.40159 -35.61258 1.000 22.56494 ? 325 ASN A ND2   1 
ATOM   2541 N  N     . PRO A 1 326 ? -6.67593  -12.97957 -34.92269 1.000 22.26909 ? 326 PRO A N     1 
ATOM   2542 C  CA    . PRO A 1 326 ? -6.82390  -12.56953 -33.51670 1.000 26.18228 ? 326 PRO A CA    1 
ATOM   2543 C  C     . PRO A 1 326 ? -7.12087  -13.72350 -32.57466 1.000 21.62690 ? 326 PRO A C     1 
ATOM   2544 O  O     . PRO A 1 326 ? -6.82785  -13.61146 -31.37767 1.000 19.31787 ? 326 PRO A O     1 
ATOM   2545 C  CB    . PRO A 1 326 ? -7.99291  -11.57354 -33.55771 1.000 26.50689 ? 326 PRO A CB    1 
ATOM   2546 C  CG    . PRO A 1 326 ? -8.11994  -11.17358 -35.00071 1.000 24.91385 ? 326 PRO A CG    1 
ATOM   2547 C  CD    . PRO A 1 326 ? -7.70095  -12.37360 -35.78569 1.000 22.07640 ? 326 PRO A CD    1 
ATOM   2548 N  N     . GLU A 1 327 ? -7.69187  -14.82352 -33.06861 1.000 22.27075 ? 327 GLU A N     1 
ATOM   2549 C  CA    . GLU A 1 327 ? -8.02084  -15.94250 -32.19057 1.000 23.41234 ? 327 GLU A CA    1 
ATOM   2550 C  C     . GLU A 1 327 ? -6.76783  -16.69047 -31.75058 1.000 18.28155 ? 327 GLU A C     1 
ATOM   2551 O  O     . GLU A 1 327 ? -6.64180  -17.06244 -30.57857 1.000 14.70529 ? 327 GLU A O     1 
ATOM   2552 C  CB    . GLU A 1 327 ? -8.99885  -16.89053 -32.88652 1.000 20.53015 ? 327 GLU A CB    1 
ATOM   2553 C  CG    . GLU A 1 327 ? -10.42386 -16.35854 -32.99951 1.000 22.73179 ? 327 GLU A CG    1 
ATOM   2554 C  CD    . GLU A 1 327 ? -10.56089 -15.23557 -34.00954 1.000 24.97765 ? 327 GLU A CD    1 
ATOM   2555 O  OE1   . GLU A 1 327 ? -9.64591  -15.06359 -34.84256 1.000 26.98974 ? 327 GLU A OE1   1 
ATOM   2556 O  OE2   . GLU A 1 327 ? -11.58389 -14.52058 -33.96954 1.000 30.75212 ? 327 GLU A OE2   1 
ATOM   2557 N  N     . PHE A 1 328 ? -5.83285  -16.92550 -32.67559 1.000 18.59744 ? 328 PHE A N     1 
ATOM   2558 C  CA    . PHE A 1 328 ? -4.58083  -17.57547 -32.30560 1.000 16.19038 ? 328 PHE A CA    1 
ATOM   2559 C  C     . PHE A 1 328 ? -3.73582  -16.69144 -31.39864 1.000 15.17004 ? 328 PHE A C     1 
ATOM   2560 O  O     . PHE A 1 328 ? -2.97980  -17.20241 -30.56464 1.000 13.60617 ? 328 PHE A O     1 
ATOM   2561 C  CB    . PHE A 1 328 ? -3.78786  -17.95551 -33.55760 1.000 16.95352 ? 328 PHE A CB    1 
ATOM   2562 C  CG    . PHE A 1 328 ? -4.36286  -19.12053 -34.31155 1.000 16.03723 ? 328 PHE A CG    1 
ATOM   2563 C  CD1   . PHE A 1 328 ? -5.29285  -19.95852 -33.71951 1.000 16.71985 ? 328 PHE A CD1   1 
ATOM   2564 C  CD2   . PHE A 1 328 ? -3.96489  -19.38357 -35.61255 1.000 18.69743 ? 328 PHE A CD2   1 
ATOM   2565 C  CE1   . PHE A 1 328 ? -5.81985  -21.03255 -34.41246 1.000 16.20224 ? 328 PHE A CE1   1 
ATOM   2566 C  CE2   . PHE A 1 328 ? -4.48790  -20.45559 -36.31051 1.000 17.55784 ? 328 PHE A CE2   1 
ATOM   2567 C  CZ    . PHE A 1 328 ? -5.41688  -21.28158 -35.70947 1.000 17.50911 ? 328 PHE A CZ    1 
ATOM   2568 N  N     . LEU A 1 329 ? -3.84884  -15.36945 -31.54468 1.000 13.55887 ? 329 LEU A N     1 
ATOM   2569 C  CA    . LEU A 1 329 ? -3.08682  -14.46541 -30.69072 1.000 15.14406 ? 329 LEU A CA    1 
ATOM   2570 C  C     . LEU A 1 329 ? -3.63279  -14.45637 -29.26871 1.000 14.09409 ? 329 LEU A C     1 
ATOM   2571 O  O     . LEU A 1 329 ? -2.86277  -14.45734 -28.30273 1.000 14.49035 ? 329 LEU A O     1 
ATOM   2572 C  CB    . LEU A 1 329 ? -3.09885  -13.05443 -31.27676 1.000 15.25998 ? 329 LEU A CB    1 
ATOM   2573 C  CG    . LEU A 1 329 ? -2.38584  -11.98040 -30.45281 1.000 16.02883 ? 329 LEU A CG    1 
ATOM   2574 C  CD1   . LEU A 1 329 ? -0.88284  -12.22239 -30.42784 1.000 13.11869 ? 329 LEU A CD1   1 
ATOM   2575 C  CD2   . LEU A 1 329 ? -2.70686  -10.59342 -30.98585 1.000 20.30102 ? 329 LEU A CD2   1 
ATOM   2576 N  N     . ALA A 1 330 ? -4.96079  -14.44538 -29.12168 1.000 15.11082 ? 330 ALA A N     1 
ATOM   2577 C  CA    . ALA A 1 330 ? -5.55676  -14.43735 -27.78967 1.000 14.44973 ? 330 ALA A CA    1 
ATOM   2578 C  C     . ALA A 1 330 ? -5.28474  -15.74132 -27.05364 1.000 13.93092 ? 330 ALA A C     1 
ATOM   2579 O  O     . ALA A 1 330 ? -5.00871  -15.73428 -25.84864 1.000 11.78583 ? 330 ALA A O     1 
ATOM   2580 C  CB    . ALA A 1 330 ? -7.05877  -14.17636 -27.88665 1.000 17.28218 ? 330 ALA A CB    1 
ATOM   2581 N  N     . ALA A 1 331 ? -5.35574  -16.87334 -27.76060 1.000 12.82446 ? 331 ALA A N     1 
ATOM   2582 C  CA    . ALA A 1 331 ? -5.05672  -18.15332 -27.13057 1.000 12.06120 ? 331 ALA A CA    1 
ATOM   2583 C  C     . ALA A 1 331 ? -3.59971  -18.22130 -26.69460 1.000 10.47932 ? 331 ALA A C     1 
ATOM   2584 O  O     . ALA A 1 331 ? -3.28768  -18.74926 -25.62059 1.000 11.32619 ? 331 ALA A O     1 
ATOM   2585 C  CB    . ALA A 1 331 ? -5.38673  -19.30035 -28.08453 1.000 12.94266 ? 331 ALA A CB    1 
ATOM   2586 N  N     . TRP A 1 332 ? -2.69173  -17.68631 -27.51463 1.000 11.32365 ? 332 TRP A N     1 
ATOM   2587 C  CA    . TRP A 1 332 ? -1.28072  -17.66629 -27.14866 1.000 10.20708 ? 332 TRP A CA    1 
ATOM   2588 C  C     . TRP A 1 332 ? -1.00371  -16.66226 -26.03870 1.000 11.08192 ? 332 TRP A C     1 
ATOM   2589 O  O     . TRP A 1 332 ? -0.14669  -16.90822 -25.18071 1.000 9.61349  ? 332 TRP A O     1 
ATOM   2590 C  CB    . TRP A 1 332 ? -0.43275  -17.35632 -28.38269 1.000 10.96329 ? 332 TRP A CB    1 
ATOM   2591 C  CG    . TRP A 1 332 ? 1.04325   -17.33530 -28.13072 1.000 10.06395 ? 332 TRP A CG    1 
ATOM   2592 C  CD1   . TRP A 1 332 ? 1.88926   -18.40630 -28.13371 1.000 9.32016  ? 332 TRP A CD1   1 
ATOM   2593 C  CD2   . TRP A 1 332 ? 1.85125   -16.18629 -27.85377 1.000 7.87640  ? 332 TRP A CD2   1 
ATOM   2594 N  NE1   . TRP A 1 332 ? 3.17326   -17.99528 -27.86875 1.000 8.47977  ? 332 TRP A NE1   1 
ATOM   2595 C  CE2   . TRP A 1 332 ? 3.17726   -16.63627 -27.69379 1.000 8.49752  ? 332 TRP A CE2   1 
ATOM   2596 C  CE3   . TRP A 1 332 ? 1.58124   -14.82029 -27.72281 1.000 9.60361  ? 332 TRP A CE3   1 
ATOM   2597 C  CZ2   . TRP A 1 332 ? 4.22925   -15.77026 -27.40784 1.000 8.11062  ? 332 TRP A CZ2   1 
ATOM   2598 C  CZ3   . TRP A 1 332 ? 2.62824   -13.96227 -27.43986 1.000 10.71123 ? 332 TRP A CZ3   1 
ATOM   2599 C  CH2   . TRP A 1 332 ? 3.93625   -14.44025 -27.28487 1.000 10.95198 ? 332 TRP A CH2   1 
ATOM   2600 N  N     . ARG A 1 333 ? -1.71899  -15.53500 -26.03105 1.000 11.30418 ? 333 ARG A N     1 
ATOM   2601 C  CA    . ARG A 1 333 ? -1.49529  -14.52034 -25.00601 1.000 11.03052 ? 333 ARG A CA    1 
ATOM   2602 C  C     . ARG A 1 333 ? -2.08016  -14.94520 -23.66319 1.000 10.48982 ? 333 ARG A C     1 
ATOM   2603 O  O     . ARG A 1 333 ? -1.46368  -14.72421 -22.61410 1.000 12.13334 ? 333 ARG A O     1 
ATOM   2604 C  CB    . ARG A 1 333 ? -2.09198  -13.18644 -25.45614 1.000 12.37920 ? 333 ARG A CB    1 
ATOM   2605 C  CG    . ARG A 1 333 ? -1.88604  -12.04260 -24.47790 1.000 16.20396 ? 333 ARG A CG    1 
ATOM   2606 C  CD    . ARG A 1 333 ? -2.51145  -10.74816 -24.98554 1.000 16.85932 ? 333 ARG A CD    1 
ATOM   2607 N  NE    . ARG A 1 333 ? -3.95669  -10.85641 -25.15010 1.000 20.82788 ? 333 ARG A NE    1 
ATOM   2608 C  CZ    . ARG A 1 333 ? -4.57305  -10.97892 -26.31809 1.000 16.72546 ? 333 ARG A CZ    1 
ATOM   2609 N  NH1   . ARG A 1 333 ? -3.89947  -10.99971 -27.45642 1.000 19.41092 ? 333 ARG A NH1   1 
ATOM   2610 N  NH2   . ARG A 1 333 ? -5.89881  -11.07990 -26.34468 1.000 18.97632 ? 333 ARG A NH2   1 
ATOM   2611 N  N     . GLU A 1 334 ? -3.26267  -15.55720 -23.67368 1.000 10.90530 ? 334 GLU A N     1 
ATOM   2612 C  CA    . GLU A 1 334 ? -3.94064  -15.97017 -22.45166 1.000 12.10426 ? 334 GLU A CA    1 
ATOM   2613 C  C     . GLU A 1 334 ? -3.52862  -17.35715 -21.97462 1.000 11.86979 ? 334 GLU A C     1 
ATOM   2614 O  O     . GLU A 1 334 ? -4.09459  -17.84713 -20.99160 1.000 11.51601 ? 334 GLU A O     1 
ATOM   2615 C  CB    . GLU A 1 334 ? -5.45864  -15.92919 -22.65563 1.000 10.89966 ? 334 GLU A CB    1 
ATOM   2616 C  CG    . GLU A 1 334 ? -5.99366  -14.55920 -23.03466 1.000 12.85595 ? 334 GLU A CG    1 
ATOM   2617 C  CD    . GLU A 1 334 ? -7.43567  -14.60423 -23.49663 1.000 12.96598 ? 334 GLU A CD    1 
ATOM   2618 O  OE1   . GLU A 1 334 ? -8.07666  -15.66523 -23.34858 1.000 17.60913 ? 334 GLU A OE1   1 
ATOM   2619 O  OE2   . GLU A 1 334 ? -7.92669  -13.58025 -24.01565 1.000 17.24947 ? 334 GLU A OE2   1 
ATOM   2620 N  N     . ALA A 1 335 ? -2.56963  -17.99717 -22.64763 1.000 8.74190  ? 335 ALA A N     1 
ATOM   2621 C  CA    . ALA A 1 335 ? -2.05861  -19.31415 -22.25760 1.000 9.41427  ? 335 ALA A CA    1 
ATOM   2622 C  C     . ALA A 1 335 ? -3.17660  -20.35816 -22.21854 1.000 9.36019  ? 335 ALA A C     1 
ATOM   2623 O  O     . ALA A 1 335 ? -3.38757  -21.04413 -21.21752 1.000 10.69641 ? 335 ALA A O     1 
ATOM   2624 C  CB    . ALA A 1 335 ? -1.31958  -19.24510 -20.91861 1.000 11.06104 ? 335 ALA A CB    1 
ATOM   2625 N  N     . ARG A 1 336 ? -3.89592  -20.47450 -23.33055 1.000 8.66327  ? 336 ARG A N     1 
ATOM   2626 C  CA    . ARG A 1 336 ? -4.92953  -21.48736 -23.50769 1.000 10.43216 ? 336 ARG A CA    1 
ATOM   2627 C  C     . ARG A 1 336 ? -4.79829  -22.14173 -24.87479 1.000 11.17579 ? 336 ARG A C     1 
ATOM   2628 O  O     . ARG A 1 336 ? -5.78850  -22.39590 -25.56713 1.000 8.74661  ? 336 ARG A O     1 
ATOM   2629 C  CB    . ARG A 1 336 ? -6.32213  -20.89253 -23.31405 1.000 10.55707 ? 336 ARG A CB    1 
ATOM   2630 C  CG    . ARG A 1 336 ? -6.57623  -19.61896 -24.09811 1.000 13.82385 ? 336 ARG A CG    1 
ATOM   2631 C  CD    . ARG A 1 336 ? -7.98695  -19.10878 -23.85783 1.000 11.15730 ? 336 ARG A CD    1 
ATOM   2632 N  NE    . ARG A 1 336 ? -8.24434  -17.86059 -24.56452 1.000 11.96076 ? 336 ARG A NE    1 
ATOM   2633 C  CZ    . ARG A 1 336 ? -8.72634  -17.78374 -25.79707 1.000 13.85163 ? 336 ARG A CZ    1 
ATOM   2634 N  NH1   . ARG A 1 336 ? -9.01303  -18.86956 -26.49606 1.000 13.14601 ? 336 ARG A NH1   1 
ATOM   2635 N  NH2   . ARG A 1 336 ? -8.92607  -16.58714 -26.34193 1.000 17.85204 ? 336 ARG A NH2   1 
ATOM   2636 N  N     . THR A 1 337 ? -3.55965  -22.42425 -25.28047 1.000 8.53267  ? 337 THR A N     1 
ATOM   2637 C  CA    . THR A 1 337 ? -3.29967  -23.04729 -26.57046 1.000 9.87844  ? 337 THR A CA    1 
ATOM   2638 C  C     . THR A 1 337 ? -3.55966  -24.54729 -26.56541 1.000 9.68287  ? 337 THR A C     1 
ATOM   2639 O  O     . THR A 1 337 ? -3.68768  -25.14433 -27.64039 1.000 9.80979  ? 337 THR A O     1 
ATOM   2640 C  CB    . THR A 1 337 ? -1.85168  -22.79429 -26.99650 1.000 8.06105  ? 337 THR A CB    1 
ATOM   2641 O  OG1   . THR A 1 337 ? -0.96366  -23.37626 -26.03450 1.000 7.85769  ? 337 THR A OG1   1 
ATOM   2642 C  CG2   . THR A 1 337 ? -1.57769  -21.30429 -27.09255 1.000 9.96473  ? 337 THR A CG2   1 
ATOM   2643 N  N     . GLY A 1 338 ? -3.63963  -25.16726 -25.38939 1.000 9.18928  ? 338 GLY A N     1 
ATOM   2644 C  CA    . GLY A 1 338 ? -3.79661  -26.59926 -25.28634 1.000 10.61104 ? 338 GLY A CA    1 
ATOM   2645 C  C     . GLY A 1 338 ? -2.50361  -27.37024 -25.13234 1.000 9.88483  ? 338 GLY A C     1 
ATOM   2646 O  O     . GLY A 1 338 ? -2.54859  -28.56723 -24.82231 1.000 10.92689 ? 338 GLY A O     1 
ATOM   2647 N  N     . PHE A 1 339 ? -1.35562  -26.72624 -25.34639 1.000 8.25576  ? 339 PHE A N     1 
ATOM   2648 C  CA    . PHE A 1 339 ? -0.06261  -27.36022 -25.14339 1.000 8.11166  ? 339 PHE A CA    1 
ATOM   2649 C  C     . PHE A 1 339 ? 0.48142   -26.93818 -23.78942 1.000 8.01246  ? 339 PHE A C     1 
ATOM   2650 O  O     . PHE A 1 339 ? 0.82841   -25.76017 -23.61446 1.000 7.75125  ? 339 PHE A O     1 
ATOM   2651 C  CB    . PHE A 1 339 ? 0.91137   -26.97225 -26.25443 1.000 7.99428  ? 339 PHE A CB    1 
ATOM   2652 C  CG    . PHE A 1 339 ? 0.48334   -27.42229 -27.62140 1.000 9.04257  ? 339 PHE A CG    1 
ATOM   2653 C  CD1   . PHE A 1 339 ? 0.84234   -28.67330 -28.09537 1.000 9.82740  ? 339 PHE A CD1   1 
ATOM   2654 C  CD2   . PHE A 1 339 ? -0.27468  -26.59632 -28.43341 1.000 8.36520  ? 339 PHE A CD2   1 
ATOM   2655 C  CE1   . PHE A 1 339 ? 0.45232   -29.09235 -29.35335 1.000 9.78213  ? 339 PHE A CE1   1 
ATOM   2656 C  CE2   . PHE A 1 339 ? -0.66770  -27.00736 -29.69139 1.000 9.81197  ? 339 PHE A CE2   1 
ATOM   2657 C  CZ    . PHE A 1 339 ? -0.30370  -28.25838 -30.15236 1.000 10.87477 ? 339 PHE A CZ    1 
ATOM   2658 N  N     . PRO A 1 340 ? 0.57145   -27.84215 -22.80939 1.000 7.95515  ? 340 PRO A N     1 
ATOM   2659 C  CA    . PRO A 1 340 ? 1.00047   -27.42510 -21.46342 1.000 7.79069  ? 340 PRO A CA    1 
ATOM   2660 C  C     . PRO A 1 340 ? 2.38447   -26.80409 -21.42346 1.000 8.31256  ? 340 PRO A C     1 
ATOM   2661 O  O     . PRO A 1 340 ? 2.62148   -25.90406 -20.60850 1.000 7.33162  ? 340 PRO A O     1 
ATOM   2662 C  CB    . PRO A 1 340 ? 0.94550   -28.73308 -20.66337 1.000 8.11193  ? 340 PRO A CB    1 
ATOM   2663 C  CG    . PRO A 1 340 ? -0.04051  -29.58311 -21.39833 1.000 8.30180  ? 340 PRO A CG    1 
ATOM   2664 C  CD    . PRO A 1 340 ? 0.16146   -29.25515 -22.84834 1.000 8.99887  ? 340 PRO A CD    1 
ATOM   2665 N  N     . TRP A 1 341 ? 3.30745   -27.25611 -22.27547 1.000 7.48321  ? 341 TRP A N     1 
ATOM   2666 C  CA    . TRP A 1 341 ? 4.64645   -26.67510 -22.27852 1.000 8.00171  ? 341 TRP A CA    1 
ATOM   2667 C  C     . TRP A 1 341 ? 4.61243   -25.21311 -22.70456 1.000 7.76489  ? 341 TRP A C     1 
ATOM   2668 O  O     . TRP A 1 341 ? 5.35143   -24.38209 -22.16360 1.000 7.38354  ? 341 TRP A O     1 
ATOM   2669 C  CB    . TRP A 1 341 ? 5.56644   -27.48212 -23.19351 1.000 8.05984  ? 341 TRP A CB    1 
ATOM   2670 C  CG    . TRP A 1 341 ? 6.93243   -26.89111 -23.34256 1.000 7.43098  ? 341 TRP A CG    1 
ATOM   2671 C  CD1   . TRP A 1 341 ? 7.44240   -26.27314 -24.44759 1.000 7.43501  ? 341 TRP A CD1   1 
ATOM   2672 C  CD2   . TRP A 1 341 ? 7.96545   -26.85507 -22.35058 1.000 8.14118  ? 341 TRP A CD2   1 
ATOM   2673 N  NE1   . TRP A 1 341 ? 8.72840   -25.86012 -24.20563 1.000 8.27121  ? 341 TRP A NE1   1 
ATOM   2674 C  CE2   . TRP A 1 341 ? 9.07443   -26.20408 -22.92562 1.000 7.48002  ? 341 TRP A CE2   1 
ATOM   2675 C  CE3   . TRP A 1 341 ? 8.06148   -27.31303 -21.03257 1.000 8.49673  ? 341 TRP A CE3   1 
ATOM   2676 C  CZ2   . TRP A 1 341 ? 10.26345  -25.99905 -22.22965 1.000 8.49434  ? 341 TRP A CZ2   1 
ATOM   2677 C  CZ3   . TRP A 1 341 ? 9.24249   -27.10800 -20.34360 1.000 8.83261  ? 341 TRP A CZ3   1 
ATOM   2678 C  CH2   . TRP A 1 341 ? 10.32748  -26.45701 -20.94264 1.000 8.31678  ? 341 TRP A CH2   1 
ATOM   2679 N  N     . ILE A 1 342 ? 3.75541   -24.87815 -23.66955 1.000 7.12906  ? 342 ILE A N     1 
ATOM   2680 C  CA    . ILE A 1 342 ? 3.64239   -23.49416 -24.11259 1.000 7.73619  ? 342 ILE A CA    1 
ATOM   2681 C  C     . ILE A 1 342 ? 2.86540   -22.66314 -23.09960 1.000 6.98469  ? 342 ILE A C     1 
ATOM   2682 O  O     . ILE A 1 342 ? 3.26340   -21.54212 -22.76564 1.000 6.81964  ? 342 ILE A O     1 
ATOM   2683 C  CB    . ILE A 1 342 ? 2.99636   -23.43821 -25.50958 1.000 7.89791  ? 342 ILE A CB    1 
ATOM   2684 C  CG1   . ILE A 1 342 ? 3.90834   -24.09723 -26.54658 1.000 8.24350  ? 342 ILE A CG1   1 
ATOM   2685 C  CG2   . ILE A 1 342 ? 2.68134   -22.00022 -25.90262 1.000 8.26031  ? 342 ILE A CG2   1 
ATOM   2686 C  CD1   . ILE A 1 342 ? 5.27133   -23.45023 -26.66163 1.000 8.61218  ? 342 ILE A CD1   1 
ATOM   2687 N  N     . ASP A 1 343 ? 1.75442   -23.20013 -22.58856 1.000 7.18264  ? 343 ASP A N     1 
ATOM   2688 C  CA    . ASP A 1 343 ? 0.92443   -22.44511 -21.65556 1.000 8.03584  ? 343 ASP A CA    1 
ATOM   2689 C  C     . ASP A 1 343 ? 1.62446   -22.22706 -20.31859 1.000 7.85685  ? 343 ASP A C     1 
ATOM   2690 O  O     . ASP A 1 343 ? 1.30746   -21.26804 -19.60561 1.000 8.98931  ? 343 ASP A O     1 
ATOM   2691 C  CB    . ASP A 1 343 ? -0.41256  -23.15711 -21.44651 1.000 7.51480  ? 343 ASP A CB    1 
ATOM   2692 C  CG    . ASP A 1 343 ? -1.25259  -23.20616 -22.70750 1.000 7.70030  ? 343 ASP A CG    1 
ATOM   2693 O  OD1   . ASP A 1 343 ? -1.09161  -22.31718 -23.56853 1.000 7.62979  ? 343 ASP A OD1   1 
ATOM   2694 O  OD2   . ASP A 1 343 ? -2.07758  -24.13417 -22.83645 1.000 9.25087  ? 343 ASP A OD2   1 
ATOM   2695 N  N     . ALA A 1 344 ? 2.56747   -23.09904 -19.95758 1.000 7.02114  ? 344 ALA A N     1 
ATOM   2696 C  CA    . ALA A 1 344 ? 3.30450   -22.90400 -18.71260 1.000 7.40902  ? 344 ALA A CA    1 
ATOM   2697 C  C     . ALA A 1 344 ? 4.29548   -21.75300 -18.83266 1.000 6.67948  ? 344 ALA A C     1 
ATOM   2698 O  O     . ALA A 1 344 ? 4.47050   -20.97597 -17.88668 1.000 6.62986  ? 344 ALA A O     1 
ATOM   2699 C  CB    . ALA A 1 344 ? 4.02151   -24.19298 -18.31458 1.000 7.07350  ? 344 ALA A CB    1 
ATOM   2700 N  N     . ILE A 1 345 ? 4.95146   -21.62903 -19.98667 1.000 8.06563  ? 345 ILE A N     1 
ATOM   2701 C  CA    . ILE A 1 345 ? 5.89945   -20.53802 -20.18973 1.000 6.49456  ? 345 ILE A CA    1 
ATOM   2702 C  C     . ILE A 1 345 ? 5.17043   -19.20203 -20.26175 1.000 7.50969  ? 345 ILE A C     1 
ATOM   2703 O  O     . ILE A 1 345 ? 5.65044   -18.18801 -19.73979 1.000 6.26907  ? 345 ILE A O     1 
ATOM   2704 C  CB    . ILE A 1 345 ? 6.74242   -20.79406 -21.45174 1.000 7.13044  ? 345 ILE A CB    1 
ATOM   2705 C  CG1   . ILE A 1 345 ? 7.48743   -22.12505 -21.33471 1.000 8.54100  ? 345 ILE A CG1   1 
ATOM   2706 C  CG2   . ILE A 1 345 ? 7.72641   -19.66006 -21.67679 1.000 8.13736  ? 345 ILE A CG2   1 
ATOM   2707 C  CD1   . ILE A 1 345 ? 8.28141   -22.49108 -22.56972 1.000 7.24661  ? 345 ILE A CD1   1 
ATOM   2708 N  N     . MET A 1 346 ? 3.99942   -19.17606 -20.90473 1.000 7.42957  ? 346 MET A N     1 
ATOM   2709 C  CA    . MET A 1 346 ? 3.22141   -17.94407 -20.96775 1.000 7.57123  ? 346 MET A CA    1 
ATOM   2710 C  C     . MET A 1 346 ? 2.66043   -17.56403 -19.60375 1.000 8.49094  ? 346 MET A C     1 
ATOM   2711 O  O     . MET A 1 346 ? 2.48343   -16.37502 -19.31778 1.000 11.56893 ? 346 MET A O     1 
ATOM   2712 C  CB    . MET A 1 346 ? 2.09439   -18.08411 -21.99072 1.000 9.54121  ? 346 MET A CB    1 
ATOM   2713 C  CG    . MET A 1 346 ? 2.58036   -18.33415 -23.40972 1.000 8.67033  ? 346 MET A CG    1 
ATOM   2714 S  SD    . MET A 1 346 ? 3.71834   -17.06016 -23.98779 1.000 8.29934  ? 346 MET A SD    1 
ATOM   2715 C  CE    . MET A 1 346 ? 2.64733   -15.62417 -23.98581 1.000 10.63370 ? 346 MET A CE    1 
ATOM   2716 N  N     . THR A 1 347 ? 2.37246   -18.55301 -18.75471 1.000 7.92897  ? 347 THR A N     1 
ATOM   2717 C  CA    . THR A 1 347 ? 1.97849   -18.24997 -17.38271 1.000 8.20014  ? 347 THR A CA    1 
ATOM   2718 C  C     . THR A 1 347 ? 3.15550   -17.69494 -16.59176 1.000 7.92038  ? 347 THR A C     1 
ATOM   2719 O  O     . THR A 1 347 ? 2.98751   -16.78891 -15.76678 1.000 7.14682  ? 347 THR A O     1 
ATOM   2720 C  CB    . THR A 1 347 ? 1.40951   -19.49995 -16.70866 1.000 8.73106  ? 347 THR A CB    1 
ATOM   2721 O  OG1   . THR A 1 347 ? 0.28550   -19.97599 -17.45863 1.000 7.25371  ? 347 THR A OG1   1 
ATOM   2722 C  CG2   . THR A 1 347 ? 0.96154   -19.18891 -15.28866 1.000 11.08505 ? 347 THR A CG2   1 
ATOM   2723 N  N     . GLN A 1 348 ? 4.36050   -18.21894 -16.83877 1.000 6.69371  ? 348 GLN A N     1 
ATOM   2724 C  CA    . GLN A 1 348 ? 5.55351   -17.66591 -16.20881 1.000 7.81019  ? 348 GLN A CA    1 
ATOM   2725 C  C     . GLN A 1 348 ? 5.83549   -16.24992 -16.69586 1.000 6.82464  ? 348 GLN A C     1 
ATOM   2726 O  O     . GLN A 1 348 ? 6.39549   -15.43889 -15.94989 1.000 6.28655  ? 348 GLN A O     1 
ATOM   2727 C  CB    . GLN A 1 348 ? 6.75551   -18.57191 -16.47981 1.000 7.65128  ? 348 GLN A CB    1 
ATOM   2728 C  CG    . GLN A 1 348 ? 8.01952   -18.18987 -15.72584 1.000 6.17452  ? 348 GLN A CG    1 
ATOM   2729 C  CD    . GLN A 1 348 ? 9.21352   -19.03588 -16.12484 1.000 6.24068  ? 348 GLN A CD    1 
ATOM   2730 O  OE1   . GLN A 1 348 ? 9.28250   -19.54491 -17.24383 1.000 6.73801  ? 348 GLN A OE1   1 
ATOM   2731 N  NE2   . GLN A 1 348 ? 10.16154  -19.19184 -15.20786 1.000 7.52388  ? 348 GLN A NE2   1 
ATOM   2732 N  N     . LEU A 1 349 ? 5.45546   -15.93596 -17.93686 1.000 7.05487  ? 349 LEU A N     1 
ATOM   2733 C  CA    . LEU A 1 349 ? 5.64244   -14.58497 -18.45690 1.000 8.41512  ? 349 LEU A CA    1 
ATOM   2734 C  C     . LEU A 1 349 ? 4.83244   -13.56996 -17.65992 1.000 7.94084  ? 349 LEU A C     1 
ATOM   2735 O  O     . LEU A 1 349 ? 5.34944   -12.51994 -17.26296 1.000 6.70344  ? 349 LEU A O     1 
ATOM   2736 C  CB    . LEU A 1 349 ? 5.25540   -14.53602 -19.93590 1.000 6.26938  ? 349 LEU A CB    1 
ATOM   2737 C  CG    . LEU A 1 349 ? 5.16438   -13.14304 -20.56294 1.000 6.44098  ? 349 LEU A CG    1 
ATOM   2738 C  CD1   . LEU A 1 349 ? 6.53637   -12.49403 -20.65498 1.000 6.86530  ? 349 LEU A CD1   1 
ATOM   2739 C  CD2   . LEU A 1 349 ? 4.50135   -13.20209 -21.93092 1.000 11.73542 ? 349 LEU A CD2   1 
ATOM   2740 N  N     . VAL A 1 350 ? 3.55545   -13.86896 -17.41388 1.000 7.06247  ? 350 VAL A N     1 
ATOM   2741 C  CA    . VAL A 1 350 ? 2.69446   -12.91694 -16.72089 1.000 9.15329  ? 350 VAL A CA    1 
ATOM   2742 C  C     . VAL A 1 350 ? 2.86149   -12.97390 -15.20789 1.000 8.25346  ? 350 VAL A C     1 
ATOM   2743 O  O     . VAL A 1 350 ? 2.42450   -12.04888 -14.51191 1.000 11.66823 ? 350 VAL A O     1 
ATOM   2744 C  CB    . VAL A 1 350 ? 1.21845   -13.14497 -17.09085 1.000 9.24616  ? 350 VAL A CB    1 
ATOM   2745 C  CG1   . VAL A 1 350 ? 1.02942   -13.04401 -18.59485 1.000 9.58286  ? 350 VAL A CG1   1 
ATOM   2746 C  CG2   . VAL A 1 350 ? 0.74047   -14.49496 -16.57580 1.000 9.50743  ? 350 VAL A CG2   1 
ATOM   2747 N  N     . THR A 1 351 ? 3.48151   -14.02688 -14.67587 1.000 6.95468  ? 351 THR A N     1 
ATOM   2748 C  CA    . THR A 1 351 ? 3.66954   -14.14683 -13.23487 1.000 7.52526  ? 351 THR A CA    1 
ATOM   2749 C  C     . THR A 1 351 ? 5.03055   -13.62081 -12.79092 1.000 8.72984  ? 351 THR A C     1 
ATOM   2750 O  O     . THR A 1 351 ? 5.11156   -12.77378 -11.89695 1.000 8.18839  ? 351 THR A O     1 
ATOM   2751 C  CB    . THR A 1 351 ? 3.50256   -15.60682 -12.79783 1.000 8.72981  ? 351 THR A CB    1 
ATOM   2752 O  OG1   . THR A 1 351 ? 2.18856   -16.06384 -13.13978 1.000 8.80061  ? 351 THR A OG1   1 
ATOM   2753 C  CG2   . THR A 1 351 ? 3.70160   -15.73777 -11.29483 1.000 11.67075 ? 351 THR A CG2   1 
ATOM   2754 N  N     . TRP A 1 352 ? 6.10654   -14.10982 -13.40693 1.000 7.01739  ? 352 TRP A N     1 
ATOM   2755 C  CA    . TRP A 1 352 ? 7.45154   -13.69080 -13.03297 1.000 8.70678  ? 352 TRP A CA    1 
ATOM   2756 C  C     . TRP A 1 352 ? 7.97152   -12.53382 -13.87201 1.000 6.40612  ? 352 TRP A C     1 
ATOM   2757 O  O     . TRP A 1 352 ? 8.79652   -11.75080 -13.38706 1.000 8.60097  ? 352 TRP A O     1 
ATOM   2758 C  CB    . TRP A 1 352 ? 8.42655   -14.86679 -13.15095 1.000 8.27398  ? 352 TRP A CB    1 
ATOM   2759 C  CG    . TRP A 1 352 ? 8.25458   -15.91876 -12.09892 1.000 9.12885  ? 352 TRP A CG    1 
ATOM   2760 C  CD1   . TRP A 1 352 ? 7.21160   -16.04974 -11.22989 1.000 9.89488  ? 352 TRP A CD1   1 
ATOM   2761 C  CD2   . TRP A 1 352 ? 9.16259   -16.98574 -11.80090 1.000 10.63524 ? 352 TRP A CD2   1 
ATOM   2762 N  NE1   . TRP A 1 352 ? 7.41163   -17.13472 -10.41086 1.000 12.43848 ? 352 TRP A NE1   1 
ATOM   2763 C  CE2   . TRP A 1 352 ? 8.60262   -17.72672 -10.74187 1.000 12.17334 ? 352 TRP A CE2   1 
ATOM   2764 C  CE3   . TRP A 1 352 ? 10.39459  -17.38675 -12.32692 1.000 9.80732  ? 352 TRP A CE3   1 
ATOM   2765 C  CZ2   . TRP A 1 352 ? 9.23064   -18.84570 -10.19785 1.000 11.04895 ? 352 TRP A CZ2   1 
ATOM   2766 C  CZ3   . TRP A 1 352 ? 11.01661  -18.49873 -11.78690 1.000 9.64285  ? 352 TRP A CZ3   1 
ATOM   2767 C  CH2   . TRP A 1 352 ? 10.43464  -19.21470 -10.73386 1.000 12.48975 ? 352 TRP A CH2   1 
ATOM   2768 N  N     . GLY A 1 353 ? 7.51449   -12.40486 -15.11501 1.000 6.58870  ? 353 GLY A N     1 
ATOM   2769 C  CA    . GLY A 1 353 ? 8.09446   -11.43588 -16.01905 1.000 6.98711  ? 353 GLY A CA    1 
ATOM   2770 C  C     . GLY A 1 353 ? 9.45145   -11.81889 -16.56007 1.000 7.61025  ? 353 GLY A C     1 
ATOM   2771 O  O     . GLY A 1 353 ? 10.14543  -10.96090 -17.11711 1.000 6.96834  ? 353 GLY A O     1 
ATOM   2772 N  N     . TRP A 1 354 ? 9.85447   -13.07788 -16.40704 1.000 5.87973  ? 354 TRP A N     1 
ATOM   2773 C  CA    . TRP A 1 354 ? 11.13746  -13.55288 -16.89905 1.000 5.86179  ? 354 TRP A CA    1 
ATOM   2774 C  C     . TRP A 1 354 ? 11.01746  -15.03489 -17.21400 1.000 6.68713  ? 354 TRP A C     1 
ATOM   2775 O  O     . TRP A 1 354 ? 10.42849  -15.79488 -16.43997 1.000 6.17044  ? 354 TRP A O     1 
ATOM   2776 C  CB    . TRP A 1 354 ? 12.25848  -13.31984 -15.87708 1.000 6.30249  ? 354 TRP A CB    1 
ATOM   2777 C  CG    . TRP A 1 354 ? 13.61347  -13.75485 -16.36010 1.000 6.28181  ? 354 TRP A CG    1 
ATOM   2778 C  CD1   . TRP A 1 354 ? 14.56145  -12.97386 -16.95314 1.000 6.19232  ? 354 TRP A CD1   1 
ATOM   2779 C  CD2   . TRP A 1 354 ? 14.16848  -15.07584 -16.29307 1.000 5.91096  ? 354 TRP A CD2   1 
ATOM   2780 N  NE1   . TRP A 1 354 ? 15.67145  -13.72286 -17.25814 1.000 5.43786  ? 354 TRP A NE1   1 
ATOM   2781 C  CE2   . TRP A 1 354 ? 15.45547  -15.01585 -16.86410 1.000 6.55997  ? 354 TRP A CE2   1 
ATOM   2782 C  CE3   . TRP A 1 354 ? 13.70350  -16.30183 -15.80602 1.000 7.27203  ? 354 TRP A CE3   1 
ATOM   2783 C  CZ2   . TRP A 1 354 ? 16.28248  -16.13484 -16.96208 1.000 6.28790  ? 354 TRP A CZ2   1 
ATOM   2784 C  CZ3   . TRP A 1 354 ? 14.52451  -17.41083 -15.90600 1.000 6.63798  ? 354 TRP A CZ3   1 
ATOM   2785 C  CH2   . TRP A 1 354 ? 15.79950  -17.31983 -16.47903 1.000 7.30074  ? 354 TRP A CH2   1 
ATOM   2786 N  N     . MET A 1 355 ? 11.57244  -15.43492 -18.35500 1.000 6.33617  ? 355 MET A N     1 
ATOM   2787 C  CA    . MET A 1 355 ? 11.66645  -16.83593 -18.73096 1.000 6.36302  ? 355 MET A CA    1 
ATOM   2788 C  C     . MET A 1 355 ? 13.07144  -17.11894 -19.23998 1.000 5.78406  ? 355 MET A C     1 
ATOM   2789 O  O     . MET A 1 355 ? 13.81742  -16.20694 -19.60703 1.000 5.48774  ? 355 MET A O     1 
ATOM   2790 C  CB    . MET A 1 355 ? 10.63743  -17.21798 -19.80593 1.000 6.34388  ? 355 MET A CB    1 
ATOM   2791 C  CG    . MET A 1 355 ? 9.22943   -16.73098 -19.52791 1.000 5.94716  ? 355 MET A CG    1 
ATOM   2792 S  SD    . MET A 1 355 ? 8.80840   -15.29901 -20.53395 1.000 6.39745  ? 355 MET A SD    1 
ATOM   2793 C  CE    . MET A 1 355 ? 8.42437   -16.08906 -22.09392 1.000 8.02291  ? 355 MET A CE    1 
ATOM   2794 N  N     . HIS A 1 356 ? 13.42745  -18.39894 -19.25295 1.000 5.61457  ? 356 HIS A N     1 
ATOM   2795 C  CA    . HIS A 1 356 ? 14.71344  -18.81094 -19.79197 1.000 5.58742  ? 356 HIS A CA    1 
ATOM   2796 C  C     . HIS A 1 356 ? 14.75541  -18.56799 -21.29797 1.000 5.85469  ? 356 HIS A C     1 
ATOM   2797 O  O     . HIS A 1 356 ? 13.72339  -18.55402 -21.97495 1.000 6.21780  ? 356 HIS A O     1 
ATOM   2798 C  CB    . HIS A 1 356 ? 14.97246  -20.28393 -19.47993 1.000 5.70196  ? 356 HIS A CB    1 
ATOM   2799 C  CG    . HIS A 1 356 ? 16.30145  -20.77994 -19.95294 1.000 5.72574  ? 356 HIS A CG    1 
ATOM   2800 N  ND1   . HIS A 1 356 ? 16.47143  -21.39797 -21.17293 1.000 5.79919  ? 356 HIS A ND1   1 
ATOM   2801 C  CD2   . HIS A 1 356 ? 17.52446  -20.75191 -19.37197 1.000 5.98568  ? 356 HIS A CD2   1 
ATOM   2802 C  CE1   . HIS A 1 356 ? 17.74143  -21.72797 -21.32394 1.000 5.93537  ? 356 HIS A CE1   1 
ATOM   2803 N  NE2   . HIS A 1 356 ? 18.40245  -21.34793 -20.24497 1.000 6.57662  ? 356 HIS A NE2   1 
ATOM   2804 N  N     . HIS A 1 357 ? 15.97039  -18.36799 -21.81701 1.000 5.54709  ? 357 HIS A N     1 
ATOM   2805 C  CA    . HIS A 1 357 ? 16.14236  -18.04904 -23.23202 1.000 5.57597  ? 357 HIS A CA    1 
ATOM   2806 C  C     . HIS A 1 357 ? 15.50135  -19.10807 -24.12297 1.000 5.93202  ? 357 HIS A C     1 
ATOM   2807 O  O     . HIS A 1 357 ? 14.73033  -18.78610 -25.03397 1.000 5.76911  ? 357 HIS A O     1 
ATOM   2808 C  CB    . HIS A 1 357 ? 17.62935  -17.90003 -23.55406 1.000 5.57311  ? 357 HIS A CB    1 
ATOM   2809 C  CG    . HIS A 1 357 ? 17.91232  -17.60008 -24.99307 1.000 5.64949  ? 357 HIS A CG    1 
ATOM   2810 N  ND1   . HIS A 1 357 ? 17.49630  -16.44010 -25.60710 1.000 5.63332  ? 357 HIS A ND1   1 
ATOM   2811 C  CD2   . HIS A 1 357 ? 18.57531  -18.30910 -25.93706 1.000 6.86977  ? 357 HIS A CD2   1 
ATOM   2812 C  CE1   . HIS A 1 357 ? 17.88827  -16.44713 -26.86911 1.000 6.39972  ? 357 HIS A CE1   1 
ATOM   2813 N  NE2   . HIS A 1 357 ? 18.54428  -17.57013 -27.09509 1.000 6.01528  ? 357 HIS A NE2   1 
ATOM   2814 N  N     . LEU A 1 358 ? 15.80537  -20.38306 -23.86894 1.000 5.80387  ? 358 LEU A N     1 
ATOM   2815 C  CA    . LEU A 1 358 ? 15.20236  -21.45709 -24.64890 1.000 6.87816  ? 358 LEU A CA    1 
ATOM   2816 C  C     . LEU A 1 358 ? 13.71037  -21.60309 -24.37786 1.000 6.00374  ? 358 LEU A C     1 
ATOM   2817 O  O     . LEU A 1 358 ? 12.98635  -22.12212 -25.23383 1.000 7.28599  ? 358 LEU A O     1 
ATOM   2818 C  CB    . LEU A 1 358 ? 15.91937  -22.77807 -24.37087 1.000 6.10431  ? 358 LEU A CB    1 
ATOM   2819 C  CG    . LEU A 1 358 ? 17.39637  -22.81607 -24.76790 1.000 6.72304  ? 358 LEU A CG    1 
ATOM   2820 C  CD1   . LEU A 1 358 ? 17.97938  -24.20406 -24.55487 1.000 6.33728  ? 358 LEU A CD1   1 
ATOM   2821 C  CD2   . LEU A 1 358 ? 17.58033  -22.36811 -26.21192 1.000 6.68569  ? 358 LEU A CD2   1 
ATOM   2822 N  N     . ALA A 1 359 ? 13.23639  -21.16506 -23.20986 1.000 5.90707  ? 359 ALA A N     1 
ATOM   2823 C  CA    . ALA A 1 359 ? 11.79739  -21.12606 -22.97483 1.000 5.95721  ? 359 ALA A CA    1 
ATOM   2824 C  C     . ALA A 1 359 ? 11.13636  -20.05709 -23.83285 1.000 6.24836  ? 359 ALA A C     1 
ATOM   2825 O  O     . ALA A 1 359 ? 10.05035  -20.27412 -24.38182 1.000 6.68708  ? 359 ALA A O     1 
ATOM   2826 C  CB    . ALA A 1 359 ? 11.50942  -20.88802 -21.49284 1.000 5.90455  ? 359 ALA A CB    1 
ATOM   2827 N  N     . ARG A 1 360 ? 11.78024  -18.89477 -23.96268 1.000 5.82871  ? 360 ARG A N     1 
ATOM   2828 C  CA    . ARG A 1 360 ? 11.30131  -17.87429 -24.88531 1.000 6.02398  ? 360 ARG A CA    1 
ATOM   2829 C  C     . ARG A 1 360 ? 11.45056  -18.30623 -26.33801 1.000 5.99468  ? 360 ARG A C     1 
ATOM   2830 O  O     . ARG A 1 360 ? 10.73628  -17.78803 -27.20130 1.000 6.10201  ? 360 ARG A O     1 
ATOM   2831 C  CB    . ARG A 1 360 ? 12.04469  -16.55977 -24.64056 1.000 6.54811  ? 360 ARG A CB    1 
ATOM   2832 C  CG    . ARG A 1 360 ? 11.90719  -16.03462 -23.21681 1.000 7.27167  ? 360 ARG A CG    1 
ATOM   2833 C  CD    . ARG A 1 360 ? 13.22808  -15.49363 -22.69591 1.000 8.61013  ? 360 ARG A CD    1 
ATOM   2834 N  NE    . ARG A 1 360 ? 13.33891  -14.04541 -22.82102 1.000 7.96410  ? 360 ARG A NE    1 
ATOM   2835 C  CZ    . ARG A 1 360 ? 13.37942  -13.20582 -21.79490 1.000 6.88931  ? 360 ARG A CZ    1 
ATOM   2836 N  NH1   . ARG A 1 360 ? 13.34014  -13.63843 -20.54521 1.000 6.68015  ? 360 ARG A NH1   1 
ATOM   2837 N  NH2   . ARG A 1 360 ? 13.46956  -11.89987 -22.02786 1.000 5.49987  ? 360 ARG A NH2   1 
ATOM   2838 N  N     . HIS A 1 361 ? 12.36030  -19.24217 -26.62390 1.000 6.93707  ? 361 HIS A N     1 
ATOM   2839 C  CA    . HIS A 1 361 ? 12.45327  -19.80421 -27.96789 1.000 6.85714  ? 361 HIS A CA    1 
ATOM   2840 C  C     . HIS A 1 361 ? 11.19427  -20.58323 -28.32584 1.000 8.24325  ? 361 HIS A C     1 
ATOM   2841 O  O     . HIS A 1 361 ? 10.71525  -20.51727 -29.46383 1.000 6.86846  ? 361 HIS A O     1 
ATOM   2842 C  CB    . HIS A 1 361 ? 13.67828  -20.71220 -28.07989 1.000 7.56864  ? 361 HIS A CB    1 
ATOM   2843 C  CG    . HIS A 1 361 ? 14.89026  -20.03721 -28.63893 1.000 8.28619  ? 361 HIS A CG    1 
ATOM   2844 N  ND1   . HIS A 1 361 ? 15.73325  -20.65323 -29.53893 1.000 7.59446  ? 361 HIS A ND1   1 
ATOM   2845 C  CD2   . HIS A 1 361 ? 15.40926  -18.80620 -28.41898 1.000 8.47982  ? 361 HIS A CD2   1 
ATOM   2846 C  CE1   . HIS A 1 361 ? 16.71524  -19.82823 -29.85398 1.000 9.00247  ? 361 HIS A CE1   1 
ATOM   2847 N  NE2   . HIS A 1 361 ? 16.54224  -18.70121 -29.18901 1.000 9.19943  ? 361 HIS A NE2   1 
ATOM   2848 N  N     . SER A 1 362 ? 10.64630  -21.33120 -27.36480 1.000 7.32309  ? 362 SER A N     1 
ATOM   2849 C  CA    . SER A 1 362 ? 9.50030   -22.18822 -27.64775 1.000 8.74508  ? 362 SER A CA    1 
ATOM   2850 C  C     . SER A 1 362 ? 8.26129   -21.36724 -27.98375 1.000 7.07289  ? 362 SER A C     1 
ATOM   2851 O  O     . SER A 1 362 ? 7.60427   -21.60428 -29.00373 1.000 7.67980  ? 362 SER A O     1 
ATOM   2852 C  CB    . SER A 1 362 ? 9.22933   -23.10719 -26.45772 1.000 7.30687  ? 362 SER A CB    1 
ATOM   2853 O  OG    . SER A 1 362 ? 10.36135  -23.90717 -26.16072 1.000 8.35880  ? 362 SER A OG    1 
ATOM   2854 N  N     . VAL A 1 363 ? 7.92730   -20.39222 -27.13477 1.000 6.49012  ? 363 VAL A N     1 
ATOM   2855 C  CA    . VAL A 1 363 ? 6.70529   -19.62123 -27.33877 1.000 7.20864  ? 363 VAL A CA    1 
ATOM   2856 C  C     . VAL A 1 363 ? 6.83325   -18.68827 -28.53780 1.000 7.92326  ? 363 VAL A C     1 
ATOM   2857 O  O     . VAL A 1 363 ? 5.84024   -18.40530 -29.21879 1.000 8.39925  ? 363 VAL A O     1 
ATOM   2858 C  CB    . VAL A 1 363 ? 6.34131   -18.85020 -26.05779 1.000 6.45027  ? 363 VAL A CB    1 
ATOM   2859 C  CG1   . VAL A 1 363 ? 5.89134   -19.81617 -24.97575 1.000 7.05126  ? 363 VAL A CG1   1 
ATOM   2860 C  CG2   . VAL A 1 363 ? 7.52631   -18.02517 -25.57884 1.000 6.23988  ? 363 VAL A CG2   1 
ATOM   2861 N  N     . ALA A 1 364 ? 8.04324   -18.19627 -28.81984 1.000 7.05699  ? 364 ALA A N     1 
ATOM   2862 C  CA    . ALA A 1 364 ? 8.22621   -17.32030 -29.97387 1.000 6.76228  ? 364 ALA A CA    1 
ATOM   2863 C  C     . ALA A 1 364 ? 8.18319   -18.11034 -31.27485 1.000 6.90139  ? 364 ALA A C     1 
ATOM   2864 O  O     . ALA A 1 364 ? 7.66217   -17.62238 -32.28485 1.000 8.25509  ? 364 ALA A O     1 
ATOM   2865 C  CB    . ALA A 1 364 ? 9.54121   -16.55229 -29.85493 1.000 6.48750  ? 364 ALA A CB    1 
ATOM   2866 N  N     . CYS A 1 365 ? 8.73320   -19.32634 -31.27382 1.000 6.92304  ? 365 CYS A N     1 
ATOM   2867 C  CA    . CYS A 1 365 ? 8.64918   -20.16537 -32.46280 1.000 8.34557  ? 365 CYS A CA    1 
ATOM   2868 C  C     . CYS A 1 365 ? 7.22818   -20.67539 -32.67375 1.000 7.51755  ? 365 CYS A C     1 
ATOM   2869 O  O     . CYS A 1 365 ? 6.77616   -20.81443 -33.81574 1.000 9.40902  ? 365 CYS A O     1 
ATOM   2870 C  CB    . CYS A 1 365 ? 9.63319   -21.33236 -32.35378 1.000 8.80236  ? 365 CYS A CB    1 
ATOM   2871 S  SG    . CYS A 1 365 ? 9.62817   -22.46341 -33.77175 1.000 13.14343 ? 365 CYS A SG    1 
ATOM   2872 N  N     . PHE A 1 366 ? 6.51021   -20.95636 -31.58273 1.000 7.30999  ? 366 PHE A N     1 
ATOM   2873 C  CA    . PHE A 1 366 ? 5.14821   -21.46838 -31.70068 1.000 9.24467  ? 366 PHE A CA    1 
ATOM   2874 C  C     . PHE A 1 366 ? 4.21919   -20.43041 -32.31970 1.000 7.78578  ? 366 PHE A C     1 
ATOM   2875 O  O     . PHE A 1 366 ? 3.39217   -20.75744 -33.17867 1.000 7.97328  ? 366 PHE A O     1 
ATOM   2876 C  CB    . PHE A 1 366 ? 4.63424   -21.90234 -30.32766 1.000 10.65823 ? 366 PHE A CB    1 
ATOM   2877 C  CG    . PHE A 1 366 ? 3.27225   -22.54135 -30.35761 1.000 10.47770 ? 366 PHE A CG    1 
ATOM   2878 C  CD1   . PHE A 1 366 ? 3.13625   -23.89936 -30.59357 1.000 8.74065  ? 366 PHE A CD1   1 
ATOM   2879 C  CD2   . PHE A 1 366 ? 2.12924   -21.78736 -30.14261 1.000 9.46622  ? 366 PHE A CD2   1 
ATOM   2880 C  CE1   . PHE A 1 366 ? 1.88826   -24.49237 -30.62152 1.000 9.28034  ? 366 PHE A CE1   1 
ATOM   2881 C  CE2   . PHE A 1 366 ? 0.87725   -22.37337 -30.16957 1.000 7.94453  ? 366 PHE A CE2   1 
ATOM   2882 C  CZ    . PHE A 1 366 ? 0.75725   -23.72837 -30.40852 1.000 10.47566 ? 366 PHE A CZ    1 
ATOM   2883 N  N     . LEU A 1 367 ? 4.34319   -19.17139 -31.89574 1.000 7.86343  ? 367 LEU A N     1 
ATOM   2884 C  CA    . LEU A 1 367 ? 3.46117   -18.12841 -32.40575 1.000 9.09868  ? 367 LEU A CA    1 
ATOM   2885 C  C     . LEU A 1 367 ? 3.78013   -17.78246 -33.85577 1.000 11.04083 ? 367 LEU A C     1 
ATOM   2886 O  O     . LEU A 1 367 ? 2.86912   -17.56649 -34.66275 1.000 10.11549 ? 367 LEU A O     1 
ATOM   2887 C  CB    . LEU A 1 367 ? 3.56318   -16.88239 -31.52679 1.000 8.60085  ? 367 LEU A CB    1 
ATOM   2888 C  CG    . LEU A 1 367 ? 2.76916   -15.66941 -32.01281 1.000 7.64788  ? 367 LEU A CG    1 
ATOM   2889 C  CD1   . LEU A 1 367 ? 1.31217   -15.76641 -31.58578 1.000 10.48228 ? 367 LEU A CD1   1 
ATOM   2890 C  CD2   . LEU A 1 367 ? 3.40216   -14.38239 -31.52086 1.000 10.24461 ? 367 LEU A CD2   1 
ATOM   2891 N  N     . THR A 1 368 ? 5.06513   -17.72646 -34.20680 1.000 8.41725  ? 368 THR A N     1 
ATOM   2892 C  CA    . THR A 1 368 ? 5.46709   -17.26549 -35.53082 1.000 9.30968  ? 368 THR A CA    1 
ATOM   2893 C  C     . THR A 1 368 ? 5.62208   -18.41852 -36.51579 1.000 10.98931 ? 368 THR A C     1 
ATOM   2894 O  O     . THR A 1 368 ? 4.64608   -19.10154 -36.84174 1.000 13.74874 ? 368 THR A O     1 
ATOM   2895 C  CB    . THR A 1 368 ? 6.77109   -16.46848 -35.44287 1.000 9.91867  ? 368 THR A CB    1 
ATOM   2896 O  OG1   . THR A 1 368 ? 7.80011   -17.29145 -34.87787 1.000 7.84208  ? 368 THR A OG1   1 
ATOM   2897 C  CG2   . THR A 1 368 ? 6.58110   -15.23245 -34.57290 1.000 11.82756 ? 368 THR A CG2   1 
ATOM   2898 N  N     . ARG A 1 369 ? 6.84177   -18.64450 -36.99310 1.000 8.64044  ? 369 ARG A N     1 
ATOM   2899 C  CA    . ARG A 1 369 ? 7.13048   -19.59401 -38.07048 1.000 11.22005 ? 369 ARG A CA    1 
ATOM   2900 C  C     . ARG A 1 369 ? 6.89343   -21.05735 -37.69069 1.000 12.60467 ? 369 ARG A C     1 
ATOM   2901 O  O     . ARG A 1 369 ? 7.28485   -21.92064 -38.48785 1.000 13.91458 ? 369 ARG A O     1 
ATOM   2902 C  CB    . ARG A 1 369 ? 8.57704   -19.42068 -38.53162 1.000 11.65285 ? 369 ARG A CB    1 
ATOM   2903 C  CG    . ARG A 1 369 ? 9.59401   -19.72585 -37.44790 1.000 10.21978 ? 369 ARG A CG    1 
ATOM   2904 C  CD    . ARG A 1 369 ? 11.00707  -19.75471 -37.99795 1.000 14.06075 ? 369 ARG A CD    1 
ATOM   2905 N  NE    . ARG A 1 369 ? 11.98014  -20.08107 -36.96263 1.000 11.09118 ? 369 ARG A NE    1 
ATOM   2906 C  CZ    . ARG A 1 369 ? 12.34043  -21.31473 -36.63743 1.000 12.05998 ? 369 ARG A CZ    1 
ATOM   2907 N  NH1   . ARG A 1 369 ? 11.83092  -22.36866 -37.25370 1.000 12.70920 ? 369 ARG A NH1   1 
ATOM   2908 N  NH2   . ARG A 1 369 ? 13.23375  -21.49591 -35.66911 1.000 11.29952 ? 369 ARG A NH2   1 
ATOM   2909 N  N     . GLY A 1 370 ? 6.28611   -21.39852 -36.55771 1.000 14.48651 ? 370 GLY A N     1 
ATOM   2910 C  CA    . GLY A 1 370 ? 6.17212   -22.78851 -36.16967 1.000 11.24672 ? 370 GLY A CA    1 
ATOM   2911 C  C     . GLY A 1 370 ? 4.77813   -23.37252 -36.26362 1.000 12.44355 ? 370 GLY A C     1 
ATOM   2912 O  O     . GLY A 1 370 ? 4.61513   -24.50954 -36.71558 1.000 12.06326 ? 370 GLY A O     1 
ATOM   2913 N  N     . ASP A 1 371 ? 3.76113   -22.61752 -35.84362 1.000 13.66391 ? 371 ASP A N     1 
ATOM   2914 C  CA    . ASP A 1 371 ? 2.42114   -23.18252 -35.73857 1.000 11.24323 ? 371 ASP A CA    1 
ATOM   2915 C  C     . ASP A 1 371 ? 1.32512   -22.19154 -36.11558 1.000 12.11315 ? 371 ASP A C     1 
ATOM   2916 O  O     . ASP A 1 371 ? 0.51510   -22.46958 -37.00556 1.000 12.71394 ? 371 ASP A O     1 
ATOM   2917 C  CB    . ASP A 1 371 ? 2.19317   -23.70748 -34.31955 1.000 11.23686 ? 371 ASP A CB    1 
ATOM   2918 C  CG    . ASP A 1 371 ? 2.97019   -24.97947 -34.04153 1.000 11.79924 ? 371 ASP A CG    1 
ATOM   2919 O  OD1   . ASP A 1 371 ? 2.52419   -26.05748 -34.48549 1.000 13.49142 ? 371 ASP A OD1   1 
ATOM   2920 O  OD2   . ASP A 1 371 ? 4.03920   -24.89744 -33.40056 1.000 10.99481 ? 371 ASP A OD2   1 
ATOM   2921 N  N     . LEU A 1 372 ? 1.28413   -21.04052 -35.44361 1.000 12.00889 ? 372 LEU A N     1 
ATOM   2922 C  CA    . LEU A 1 372 ? 0.19511   -20.08954 -35.62862 1.000 12.46627 ? 372 LEU A CA    1 
ATOM   2923 C  C     . LEU A 1 372 ? 0.43908   -19.10257 -36.76166 1.000 12.56510 ? 372 LEU A C     1 
ATOM   2924 O  O     . LEU A 1 372 ? -0.52893  -18.54659 -37.29565 1.000 10.98174 ? 372 LEU A O     1 
ATOM   2925 C  CB    . LEU A 1 372 ? -0.05586  -19.32250 -34.32664 1.000 12.88004 ? 372 LEU A CB    1 
ATOM   2926 C  CG    . LEU A 1 372 ? -0.32283  -20.19346 -33.09561 1.000 10.76237 ? 372 LEU A CG    1 
ATOM   2927 C  CD1   . LEU A 1 372 ? -0.60081  -19.33343 -31.87263 1.000 9.86354  ? 372 LEU A CD1   1 
ATOM   2928 C  CD2   . LEU A 1 372 ? -1.47183  -21.15648 -33.35555 1.000 12.18509 ? 372 LEU A CD2   1 
ATOM   2929 N  N     . TYR A 1 373 ? 1.69907   -18.87057 -37.13069 1.000 11.58353 ? 373 TYR A N     1 
ATOM   2930 C  CA    . TYR A 1 373 ? 2.06904   -17.98460 -38.23672 1.000 13.93346 ? 373 TYR A CA    1 
ATOM   2931 C  C     . TYR A 1 373 ? 1.56204   -16.55960 -38.02676 1.000 13.46483 ? 373 TYR A C     1 
ATOM   2932 O  O     . TYR A 1 373 ? 1.20301   -15.86863 -38.98277 1.000 15.44990 ? 373 TYR A O     1 
ATOM   2933 C  CB    . TYR A 1 373 ? 1.58202   -18.53665 -39.57970 1.000 15.29083 ? 373 TYR A CB    1 
ATOM   2934 C  CG    . TYR A 1 373 ? 2.54699   -18.28867 -40.71572 1.000 18.55383 ? 373 TYR A CG    1 
ATOM   2935 C  CD1   . TYR A 1 373 ? 3.65100   -19.10967 -40.90372 1.000 15.70428 ? 373 TYR A CD1   1 
ATOM   2936 C  CD2   . TYR A 1 373 ? 2.35897   -17.23270 -41.59875 1.000 16.72686 ? 373 TYR A CD2   1 
ATOM   2937 C  CE1   . TYR A 1 373 ? 4.53897   -18.88869 -41.93775 1.000 17.34538 ? 373 TYR A CE1   1 
ATOM   2938 C  CE2   . TYR A 1 373 ? 3.24194   -17.00373 -42.63678 1.000 18.88686 ? 373 TYR A CE2   1 
ATOM   2939 C  CZ    . TYR A 1 373 ? 4.32995   -17.83472 -42.80178 1.000 17.37861 ? 373 TYR A CZ    1 
ATOM   2940 O  OH    . TYR A 1 373 ? 5.21092   -17.61175 -43.83280 1.000 21.26427 ? 373 TYR A OH    1 
ATOM   2941 N  N     . VAL A 1 374 ? 1.53306   -16.10856 -36.77977 1.000 12.06278 ? 374 VAL A N     1 
ATOM   2942 C  CA    . VAL A 1 374 ? 1.17606   -14.73355 -36.45280 1.000 12.40211 ? 374 VAL A CA    1 
ATOM   2943 C  C     . VAL A 1 374 ? 2.44905   -13.89654 -36.45686 1.000 10.94918 ? 374 VAL A C     1 
ATOM   2944 O  O     . VAL A 1 374 ? 3.54106   -14.39453 -36.16486 1.000 11.71145 ? 374 VAL A O     1 
ATOM   2945 C  CB    . VAL A 1 374 ? 0.44108   -14.66052 -35.09679 1.000 11.95664 ? 374 VAL A CB    1 
ATOM   2946 C  CG1   . VAL A 1 374 ? -0.05892  -13.25051 -34.81982 1.000 10.75676 ? 374 VAL A CG1   1 
ATOM   2947 C  CG2   . VAL A 1 374 ? -0.71491  -15.65053 -35.06874 1.000 13.92885 ? 374 VAL A CG2   1 
ATOM   2948 N  N     . SER A 1 375 ? 2.31203   -12.61856 -36.80389 1.000 11.42638 ? 375 SER A N     1 
ATOM   2949 C  CA    . SER A 1 375 ? 3.47002   -11.74155 -36.91094 1.000 12.57816 ? 375 SER A CA    1 
ATOM   2950 C  C     . SER A 1 375 ? 4.20005   -11.63050 -35.57796 1.000 11.18630 ? 375 SER A C     1 
ATOM   2951 O  O     . SER A 1 375 ? 3.58207   -11.59248 -34.51095 1.000 10.10890 ? 375 SER A O     1 
ATOM   2952 C  CB    . SER A 1 375 ? 3.04200   -10.35257 -37.38498 1.000 12.34985 ? 375 SER A CB    1 
ATOM   2953 O  OG    . SER A 1 375 ? 4.14999   -9.46856  -37.42803 1.000 9.28760  ? 375 SER A OG    1 
ATOM   2954 N  N     . TRP A 1 376 ? 5.53205   -11.58050 -35.64899 1.000 12.34504 ? 376 TRP A N     1 
ATOM   2955 C  CA    . TRP A 1 376 ? 6.33607   -11.41745 -34.44501 1.000 12.66782 ? 376 TRP A CA    1 
ATOM   2956 C  C     . TRP A 1 376 ? 6.12107   -10.05943 -33.79005 1.000 9.74166  ? 376 TRP A C     1 
ATOM   2957 O  O     . TRP A 1 376 ? 6.46710   -9.89140  -32.61706 1.000 11.29699 ? 376 TRP A O     1 
ATOM   2958 C  CB    . TRP A 1 376 ? 7.81907   -11.61445 -34.76604 1.000 8.86843  ? 376 TRP A CB    1 
ATOM   2959 C  CG    . TRP A 1 376 ? 8.34604   -10.65448 -35.78608 1.000 8.37277  ? 376 TRP A CG    1 
ATOM   2960 C  CD1   . TRP A 1 376 ? 8.39901   -10.83952 -37.13607 1.000 9.05456  ? 376 TRP A CD1   1 
ATOM   2961 C  CD2   . TRP A 1 376 ? 8.89703   -9.35547  -35.53913 1.000 9.07827  ? 376 TRP A CD2   1 
ATOM   2962 N  NE1   . TRP A 1 376 ? 8.94799   -9.73753  -37.74612 1.000 11.22071 ? 376 TRP A NE1   1 
ATOM   2963 C  CE2   . TRP A 1 376 ? 9.26200   -8.81150  -36.78615 1.000 10.81010 ? 376 TRP A CE2   1 
ATOM   2964 C  CE3   . TRP A 1 376 ? 9.11705   -8.59943  -34.38316 1.000 9.52082  ? 376 TRP A CE3   1 
ATOM   2965 C  CZ2   . TRP A 1 376 ? 9.83399   -7.54750  -36.90920 1.000 10.07776 ? 376 TRP A CZ2   1 
ATOM   2966 C  CZ3   . TRP A 1 376 ? 9.68404   -7.34443  -34.50721 1.000 8.33490  ? 376 TRP A CZ3   1 
ATOM   2967 C  CH2   . TRP A 1 376 ? 10.03701  -6.83146  -35.76123 1.000 9.18471  ? 376 TRP A CH2   1 
ATOM   2968 N  N     . GLU A 1 377 ? 5.56305   -9.09146  -34.52107 1.000 10.39534 ? 377 GLU A N     1 
ATOM   2969 C  CA    . GLU A 1 377 ? 5.25405   -7.79645  -33.92510 1.000 10.86521 ? 377 GLU A CA    1 
ATOM   2970 C  C     . GLU A 1 377 ? 4.15508   -7.91642  -32.87707 1.000 13.44036 ? 377 GLU A C     1 
ATOM   2971 O  O     . GLU A 1 377 ? 4.20509   -7.24639  -31.83909 1.000 14.04632 ? 377 GLU A O     1 
ATOM   2972 C  CB    . GLU A 1 377 ? 4.84702   -6.80048  -35.00812 1.000 13.58739 ? 377 GLU A CB    1 
ATOM   2973 C  CG    . GLU A 1 377 ? 5.99900   -6.25950  -35.83316 1.000 11.11466 ? 377 GLU A CG    1 
ATOM   2974 C  CD    . GLU A 1 377 ? 5.53397   -5.28953  -36.89918 1.000 14.62115 ? 377 GLU A CD    1 
ATOM   2975 O  OE1   . GLU A 1 377 ? 4.63796   -5.65656  -37.68715 1.000 18.41944 ? 377 GLU A OE1   1 
ATOM   2976 O  OE2   . GLU A 1 377 ? 6.05396   -4.15553  -36.94223 1.000 17.89163 ? 377 GLU A OE2   1 
ATOM   2977 N  N     . ARG A 1 378 ? 3.14912   -8.75701  -33.13372 1.000 13.23349 ? 378 ARG A N     1 
ATOM   2978 C  CA    . ARG A 1 378 ? 2.06067   -8.91975  -32.17461 1.000 14.60855 ? 378 ARG A CA    1 
ATOM   2979 C  C     . ARG A 1 378 ? 2.54215   -9.60256  -30.90078 1.000 12.87011 ? 378 ARG A C     1 
ATOM   2980 O  O     . ARG A 1 378 ? 2.16049   -9.20450  -29.79382 1.000 12.97584 ? 378 ARG A O     1 
ATOM   2981 C  CB    . ARG A 1 378 ? 0.91326   -9.70700  -32.80859 1.000 12.28111 ? 378 ARG A CB    1 
ATOM   2982 C  CG    . ARG A 1 378 ? -0.30286  -8.86791  -33.19409 1.000 16.71564 ? 378 ARG A CG    1 
ATOM   2983 C  CD    . ARG A 1 378 ? -0.02564  -7.94443  -34.37305 1.000 19.80748 ? 378 ARG A CD    1 
ATOM   2984 N  NE    . ARG A 1 378 ? 0.62465   -6.70213  -33.97311 1.000 14.91894 ? 378 ARG A NE    1 
ATOM   2985 C  CZ    . ARG A 1 378 ? 1.02230   -5.76017  -34.81712 1.000 18.43725 ? 378 ARG A CZ    1 
ATOM   2986 N  NH1   . ARG A 1 378 ? 0.84784   -5.88355  -36.12254 1.000 27.75744 ? 378 ARG A NH1   1 
ATOM   2987 N  NH2   . ARG A 1 378 ? 1.61150   -4.66778  -34.33973 1.000 15.92062 ? 378 ARG A NH2   1 
ATOM   2988 N  N     . GLY A 1 379 ? 3.37714   -10.63437 -31.03497 1.000 13.26318 ? 379 GLY A N     1 
ATOM   2989 C  CA    . GLY A 1 379 ? 3.93817   -11.27333 -29.85897 1.000 12.98480 ? 379 GLY A CA    1 
ATOM   2990 C  C     . GLY A 1 379 ? 4.95218   -10.40630 -29.14401 1.000 10.16573 ? 379 GLY A C     1 
ATOM   2991 O  O     . GLY A 1 379 ? 5.10720   -10.50527 -27.92301 1.000 11.25918 ? 379 GLY A O     1 
ATOM   2992 N  N     . MET A 1 380 ? 5.65815   -9.55232  -29.88806 1.000 8.61059  ? 380 MET A N     1 
ATOM   2993 C  CA    . MET A 1 380 ? 6.58116   -8.61229  -29.26210 1.000 10.46183 ? 380 MET A CA    1 
ATOM   2994 C  C     . MET A 1 380 ? 5.84217   -7.61627  -28.38012 1.000 10.90042 ? 380 MET A C     1 
ATOM   2995 O  O     . MET A 1 380 ? 6.36219   -7.20324  -27.33614 1.000 10.65766 ? 380 MET A O     1 
ATOM   2996 C  CB    . MET A 1 380 ? 7.39013   -7.88232  -30.33414 1.000 11.37597 ? 380 MET A CB    1 
ATOM   2997 C  CG    . MET A 1 380 ? 8.52214   -7.02929  -29.79319 1.000 11.13033 ? 380 MET A CG    1 
ATOM   2998 S  SD    . MET A 1 380 ? 9.38810   -6.12833  -31.09124 1.000 15.36086 ? 380 MET A SD    1 
ATOM   2999 C  CE    . MET A 1 380 ? 8.09008   -5.03635  -31.66224 1.000 11.74051 ? 380 MET A CE    1 
ATOM   3000 N  N     . GLU A 1 381 ? 4.62916   -7.22429  -28.77910 1.000 10.78768 ? 381 GLU A N     1 
ATOM   3001 C  CA    . GLU A 1 381 ? 3.81417   -6.35428  -27.93811 1.000 13.00500 ? 381 GLU A CA    1 
ATOM   3002 C  C     . GLU A 1 381 ? 3.40520   -7.05024  -26.64808 1.000 10.82698 ? 381 GLU A C     1 
ATOM   3003 O  O     . GLU A 1 381 ? 3.22422   -6.39021  -25.61810 1.000 13.34339 ? 381 GLU A O     1 
ATOM   3004 C  CB    . GLU A 1 381 ? 2.57815   -5.88931  -28.71210 1.000 13.35107 ? 381 GLU A CB    1 
ATOM   3005 C  CG    . GLU A 1 381 ? 2.89812   -5.04334  -29.93613 1.000 13.61269 ? 381 GLU A CG    1 
ATOM   3006 C  CD    . GLU A 1 381 ? 1.71910   -4.90138  -30.88011 1.000 14.67140 ? 381 GLU A CD    1 
ATOM   3007 O  OE1   . GLU A 1 381 ? 0.69511   -5.58438  -30.66607 1.000 16.60768 ? 381 GLU A OE1   1 
ATOM   3008 O  OE2   . GLU A 1 381 ? 1.81907   -4.10841  -31.83914 1.000 11.63649 ? 381 GLU A OE2   1 
ATOM   3009 N  N     . VAL A 1 382 ? 3.26221   -8.37724  -26.68004 1.000 9.56164  ? 382 VAL A N     1 
ATOM   3010 C  CA    . VAL A 1 382 ? 2.92224   -9.11821  -25.47001 1.000 11.48530 ? 382 VAL A CA    1 
ATOM   3011 C  C     . VAL A 1 382 ? 4.13126   -9.21917  -24.54803 1.000 9.51466  ? 382 VAL A C     1 
ATOM   3012 O  O     . VAL A 1 382 ? 4.00929   -9.08513  -23.32403 1.000 9.74566  ? 382 VAL A O     1 
ATOM   3013 C  CB    . VAL A 1 382 ? 2.36825   -10.50822 -25.83596 1.000 10.41988 ? 382 VAL A CB    1 
ATOM   3014 C  CG1   . VAL A 1 382 ? 2.01828   -11.29219 -24.58093 1.000 10.77247 ? 382 VAL A CG1   1 
ATOM   3015 C  CG2   . VAL A 1 382 ? 1.15423   -10.36926 -26.74294 1.000 13.15472 ? 382 VAL A CG2   1 
ATOM   3016 N  N     . PHE A 1 383 ? 5.31725   -9.45318  -25.11805 1.000 7.94909  ? 383 PHE A N     1 
ATOM   3017 C  CA    . PHE A 1 383 ? 6.52327   -9.55014  -24.30207 1.000 8.16863  ? 383 PHE A CA    1 
ATOM   3018 C  C     . PHE A 1 383 ? 6.89727   -8.20312  -23.69612 1.000 8.50933  ? 383 PHE A C     1 
ATOM   3019 O  O     . PHE A 1 383 ? 7.25830   -8.12808  -22.51613 1.000 7.74738  ? 383 PHE A O     1 
ATOM   3020 C  CB    . PHE A 1 383 ? 7.68426   -10.09616 -25.13308 1.000 7.01379  ? 383 PHE A CB    1 
ATOM   3021 C  CG    . PHE A 1 383 ? 7.77327   -11.59516 -25.14104 1.000 6.64058  ? 383 PHE A CG    1 
ATOM   3022 C  CD1   . PHE A 1 383 ? 6.70628   -12.37116 -24.72199 1.000 7.18736  ? 383 PHE A CD1   1 
ATOM   3023 C  CD2   . PHE A 1 383 ? 8.93427   -12.22816 -25.55104 1.000 6.94160  ? 383 PHE A CD2   1 
ATOM   3024 C  CE1   . PHE A 1 383 ? 6.79030   -13.75015 -24.72695 1.000 7.23274  ? 383 PHE A CE1   1 
ATOM   3025 C  CE2   . PHE A 1 383 ? 9.02428   -13.60616 -25.55600 1.000 7.50780  ? 383 PHE A CE2   1 
ATOM   3026 C  CZ    . PHE A 1 383 ? 7.95029   -14.36816 -25.14496 1.000 6.79683  ? 383 PHE A CZ    1 
ATOM   3027 N  N     . GLU A 1 384 ? 6.82425   -7.12915  -24.48615 1.000 10.07143 ? 384 GLU A N     1 
ATOM   3028 C  CA    . GLU A 1 384 ? 7.17825   -5.80913  -23.97320 1.000 11.63749 ? 384 GLU A CA    1 
ATOM   3029 C  C     . GLU A 1 384 ? 6.26827   -5.39110  -22.82419 1.000 11.53684 ? 384 GLU A C     1 
ATOM   3030 O  O     . GLU A 1 384 ? 6.68328   -4.61907  -21.95023 1.000 14.18371 ? 384 GLU A O     1 
ATOM   3031 C  CB    . GLU A 1 384 ? 7.14000   -4.78200  -25.11400 1.000 14.82334 ? 384 GLU A CB    1 
ATOM   3032 C  CG    . GLU A 1 384 ? 6.80600   -3.36100  -24.71000 1.000 14.48307 ? 384 GLU A CG    1 
ATOM   3033 C  CD    . GLU A 1 384 ? 6.85400   -2.35700  -25.84600 1.000 18.04102 ? 384 GLU A CD    1 
ATOM   3034 O  OE1   . GLU A 1 384 ? 6.99600   -2.78600  -27.00500 1.000 20.91205 ? 384 GLU A OE1   1 
ATOM   3035 O  OE2   . GLU A 1 384 ? 6.74700   -1.15100  -25.56800 1.000 20.88247 ? 384 GLU A OE2   1 
ATOM   3036 N  N     . GLU A 1 385 ? 5.04128   -5.91311  -22.78615 1.000 10.00991 ? 385 GLU A N     1 
ATOM   3037 C  CA    . GLU A 1 385 ? 4.12530   -5.56408  -21.70714 1.000 10.57377 ? 385 GLU A CA    1 
ATOM   3038 C  C     . GLU A 1 385 ? 4.54133   -6.21404  -20.39113 1.000 9.82108  ? 385 GLU A C     1 
ATOM   3039 O  O     . GLU A 1 385 ? 4.56635   -5.55701  -19.34715 1.000 11.41371 ? 385 GLU A O     1 
ATOM   3040 C  CB    . GLU A 1 385 ? 2.69729   -5.96911  -22.07910 1.000 12.78082 ? 385 GLU A CB    1 
ATOM   3041 C  CG    . GLU A 1 385 ? 1.67131   -5.69108  -20.98809 1.000 12.87501 ? 385 GLU A CG    1 
ATOM   3042 C  CD    . GLU A 1 385 ? 0.26431   -6.09511  -21.38905 1.000 14.88083 ? 385 GLU A CD    1 
ATOM   3043 O  OE1   . GLU A 1 385 ? 0.07529   -6.54014  -22.54103 1.000 18.94523 ? 385 GLU A OE1   1 
ATOM   3044 O  OE2   . GLU A 1 385 ? -0.65368  -5.96609  -20.55103 1.000 18.51968 ? 385 GLU A OE2   1 
ATOM   3045 N  N     . HIS A 1 386 ? 4.88834   -7.50204  -20.42510 1.000 8.92202  ? 386 HIS A N     1 
ATOM   3046 C  CA    . HIS A 1 386 ? 5.06237   -8.27800  -19.20208 1.000 8.85904  ? 386 HIS A CA    1 
ATOM   3047 C  C     . HIS A 1 386 ? 6.51538   -8.50498  -18.80411 1.000 7.56844  ? 386 HIS A C     1 
ATOM   3048 O  O     . HIS A 1 386 ? 6.78941   -8.68894  -17.61411 1.000 9.79207  ? 386 HIS A O     1 
ATOM   3049 C  CB    . HIS A 1 386 ? 4.36838   -9.63901  -19.33803 1.000 8.42253  ? 386 HIS A CB    1 
ATOM   3050 C  CG    . HIS A 1 386 ? 2.89137   -9.54403  -19.56300 1.000 9.77731  ? 386 HIS A CG    1 
ATOM   3051 N  ND1   . HIS A 1 386 ? 2.00239   -9.23901  -18.55499 1.000 10.37626 ? 386 HIS A ND1   1 
ATOM   3052 C  CD2   . HIS A 1 386 ? 2.14735   -9.71407  -20.68198 1.000 9.78009  ? 386 HIS A CD2   1 
ATOM   3053 C  CE1   . HIS A 1 386 ? 0.77438   -9.22403  -19.04196 1.000 11.43134 ? 386 HIS A CE1   1 
ATOM   3054 N  NE2   . HIS A 1 386 ? 0.83536   -9.50907  -20.33095 1.000 10.09566 ? 386 HIS A NE2   1 
ATOM   3055 N  N     . LEU A 1 387 ? 7.45036   -8.50700  -19.75112 1.000 6.33232  ? 387 LEU A N     1 
ATOM   3056 C  CA    . LEU A 1 387 ? 8.84237   -8.78998  -19.41715 1.000 8.08566  ? 387 LEU A CA    1 
ATOM   3057 C  C     . LEU A 1 387 ? 9.43538   -7.66495  -18.57719 1.000 7.59149  ? 387 LEU A C     1 
ATOM   3058 O  O     . LEU A 1 387 ? 9.39836   -6.49596  -18.97023 1.000 7.96511  ? 387 LEU A O     1 
ATOM   3059 C  CB    . LEU A 1 387 ? 9.67134   -8.98801  -20.68516 1.000 7.28824  ? 387 LEU A CB    1 
ATOM   3060 C  CG    . LEU A 1 387 ? 9.58234   -10.35503 -21.36211 1.000 5.86913  ? 387 LEU A CG    1 
ATOM   3061 C  CD1   . LEU A 1 387 ? 10.40231  -10.36706 -22.63813 1.000 6.85628  ? 387 LEU A CD1   1 
ATOM   3062 C  CD2   . LEU A 1 387 ? 10.04937  -11.45000 -20.41609 1.000 7.67798  ? 387 LEU A CD2   1 
ATOM   3063 N  N     . ILE A 1 388 ? 9.98441   -8.02391  -17.41519 1.000 7.02246  ? 388 ILE A N     1 
ATOM   3064 C  CA    . ILE A 1 388 ? 10.64442  -7.03288  -16.57124 1.000 10.13289 ? 388 ILE A CA    1 
ATOM   3065 C  C     . ILE A 1 388 ? 12.02340  -6.66288  -17.10328 1.000 7.64741  ? 388 ILE A C     1 
ATOM   3066 O  O     . ILE A 1 388 ? 12.57240  -5.62487  -16.71132 1.000 7.46280  ? 388 ILE A O     1 
ATOM   3067 C  CB    . ILE A 1 388 ? 10.75645  -7.52783  -15.12022 1.000 8.87688  ? 388 ILE A CB    1 
ATOM   3068 C  CG1   . ILE A 1 388 ? 11.64846  -8.76882  -15.04321 1.000 10.82911 ? 388 ILE A CG1   1 
ATOM   3069 C  CG2   . ILE A 1 388 ? 9.37746   -7.82383  -14.55219 1.000 9.03635  ? 388 ILE A CG2   1 
ATOM   3070 C  CD1   . ILE A 1 388 ? 11.83750  -9.29878  -13.63619 1.000 9.94756  ? 388 ILE A CD1   1 
ATOM   3071 N  N     . ASP A 1 389 ? 12.59839  -7.48290  -17.98226 1.000 6.46020  ? 389 ASP A N     1 
ATOM   3072 C  CA    . ASP A 1 389 ? 13.87337  -7.18891  -18.62030 1.000 7.26956  ? 389 ASP A CA    1 
ATOM   3073 C  C     . ASP A 1 389 ? 13.70234  -6.70096  -20.05431 1.000 5.77024  ? 389 ASP A C     1 
ATOM   3074 O  O     . ASP A 1 389 ? 14.64532  -6.78898  -20.84833 1.000 5.69740  ? 389 ASP A O     1 
ATOM   3075 C  CB    . ASP A 1 389 ? 14.78138  -8.41991  -18.58328 1.000 6.77255  ? 389 ASP A CB    1 
ATOM   3076 C  CG    . ASP A 1 389 ? 14.17238  -9.62293  -19.28723 1.000 6.34609  ? 389 ASP A CG    1 
ATOM   3077 O  OD1   . ASP A 1 389 ? 13.00837  -9.54095  -19.73221 1.000 9.63325  ? 389 ASP A OD1   1 
ATOM   3078 O  OD2   . ASP A 1 389 ? 14.86538  -10.65593 -19.39522 1.000 5.45123  ? 389 ASP A OD2   1 
ATOM   3079 N  N     . GLN A 1 390 ? 12.51833  -6.19398  -20.39730 1.000 7.37401  ? 390 GLN A N     1 
ATOM   3080 C  CA    . GLN A 1 390 ? 12.20930  -5.77602  -21.75931 1.000 6.77306  ? 390 GLN A CA    1 
ATOM   3081 C  C     . GLN A 1 390 ? 13.19528  -4.73203  -22.26536 1.000 8.54746  ? 390 GLN A C     1 
ATOM   3082 O  O     . GLN A 1 390 ? 13.21128  -3.59402  -21.78640 1.000 9.22580  ? 390 GLN A O     1 
ATOM   3083 C  CB    . GLN A 1 390 ? 10.77929  -5.23604  -21.83629 1.000 10.03077 ? 390 GLN A CB    1 
ATOM   3084 C  CG    . GLN A 1 390 ? 10.43826  -4.55608  -23.15231 1.000 11.36928 ? 390 GLN A CG    1 
ATOM   3085 C  CD    . GLN A 1 390 ? 10.47225  -3.04208  -23.05535 1.000 13.18954 ? 390 GLN A CD    1 
ATOM   3086 O  OE1   . GLN A 1 390 ? 10.60522  -2.34710  -24.06238 1.000 15.41996 ? 390 GLN A OE1   1 
ATOM   3087 N  NE2   . GLN A 1 390 ? 10.34227  -2.52404  -21.83937 1.000 10.66280 ? 390 GLN A NE2   1 
ATOM   3088 N  N     . ASP A 1 391 ? 14.02626  -5.11605  -23.22937 1.000 7.37156  ? 391 ASP A N     1 
ATOM   3089 C  CA    . ASP A 1 391 ? 14.98324  -4.21906  -23.85941 1.000 8.44360  ? 391 ASP A CA    1 
ATOM   3090 C  C     . ASP A 1 391 ? 14.55121  -3.98911  -25.30041 1.000 8.68956  ? 391 ASP A C     1 
ATOM   3091 O  O     . ASP A 1 391 ? 14.24920  -4.94614  -26.01938 1.000 7.17491  ? 391 ASP A O     1 
ATOM   3092 C  CB    . ASP A 1 391 ? 16.39724  -4.79905  -23.79843 1.000 7.32952  ? 391 ASP A CB    1 
ATOM   3093 C  CG    . ASP A 1 391 ? 17.46423  -3.78605  -24.16548 1.000 10.21564 ? 391 ASP A CG    1 
ATOM   3094 O  OD1   . ASP A 1 391 ? 17.41420  -3.23809  -25.28650 1.000 10.07441 ? 391 ASP A OD1   1 
ATOM   3095 O  OD2   . ASP A 1 391 ? 18.35224  -3.53302  -23.32351 1.000 13.72227 ? 391 ASP A OD2   1 
ATOM   3096 N  N     . HIS A 1 392 ? 14.52419  -2.71912  -25.71245 1.000 7.92804  ? 392 HIS A N     1 
ATOM   3097 C  CA    . HIS A 1 392 ? 13.99216  -2.36417  -27.02545 1.000 9.55176  ? 392 HIS A CA    1 
ATOM   3098 C  C     . HIS A 1 392 ? 14.71614  -3.10720  -28.14244 1.000 7.66228  ? 392 HIS A C     1 
ATOM   3099 O  O     . HIS A 1 392 ? 14.08100  -3.71900  -29.01000 1.000 7.41424  ? 392 HIS A O     1 
ATOM   3100 C  CB    . HIS A 1 392 ? 14.08800  -0.85000  -27.23100 1.000 8.86833  ? 392 HIS A CB    1 
ATOM   3101 C  CG    . HIS A 1 392 ? 13.60400  -0.38500  -28.56900 1.000 11.48072 ? 392 HIS A CG    1 
ATOM   3102 N  ND1   . HIS A 1 392 ? 12.29200  -0.03700  -28.80700 1.000 12.84287 ? 392 HIS A ND1   1 
ATOM   3103 C  CD2   . HIS A 1 392 ? 14.25800  -0.21100  -29.74200 1.000 12.60125 ? 392 HIS A CD2   1 
ATOM   3104 C  CE1   . HIS A 1 392 ? 12.15800  0.33200   -30.06900 1.000 14.57579 ? 392 HIS A CE1   1 
ATOM   3105 N  NE2   . HIS A 1 392 ? 13.33600  0.23500   -30.65700 1.000 12.93548 ? 392 HIS A NE2   1 
ATOM   3106 N  N     . TYR A 1 393 ? 16.04914  -3.07019  -28.13347 1.000 6.95229  ? 393 TYR A N     1 
ATOM   3107 C  CA    . TYR A 1 393 ? 16.81812  -3.67521  -29.21647 1.000 7.28315  ? 393 TYR A CA    1 
ATOM   3108 C  C     . TYR A 1 393 ? 16.91914  -5.19121  -29.08643 1.000 7.51688  ? 393 TYR A C     1 
ATOM   3109 O  O     . TYR A 1 393 ? 16.98112  -5.88824  -30.10541 1.000 7.05151  ? 393 TYR A O     1 
ATOM   3110 C  CB    . TYR A 1 393 ? 18.21612  -3.05820  -29.26952 1.000 7.53904  ? 393 TYR A CB    1 
ATOM   3111 C  CG    . TYR A 1 393 ? 18.23409  -1.61922  -29.73756 1.000 8.18700  ? 393 TYR A CG    1 
ATOM   3112 C  CD1   . TYR A 1 393 ? 17.40207  -1.19125  -30.76356 1.000 10.30031 ? 393 TYR A CD1   1 
ATOM   3113 C  CD2   . TYR A 1 393 ? 19.08110  -0.68719  -29.15061 1.000 10.20278 ? 393 TYR A CD2   1 
ATOM   3114 C  CE1   . TYR A 1 393 ? 17.41505  0.12273   -31.19660 1.000 9.23897  ? 393 TYR A CE1   1 
ATOM   3115 C  CE2   . TYR A 1 393 ? 19.10108  0.62980   -29.57565 1.000 11.13695 ? 393 TYR A CE2   1 
ATOM   3116 C  CZ    . TYR A 1 393 ? 18.26605  1.02876   -30.59864 1.000 10.80729 ? 393 TYR A CZ    1 
ATOM   3117 O  OH    . TYR A 1 393 ? 18.28104  2.33674   -31.02568 1.000 9.97893  ? 393 TYR A OH    1 
ATOM   3118 N  N     . LEU A 1 394 ? 16.93517  -5.71917  -27.86041 1.000 6.45584  ? 394 LEU A N     1 
ATOM   3119 C  CA    . LEU A 1 394 ? 17.10918  -7.15716  -27.67237 1.000 7.28839  ? 394 LEU A CA    1 
ATOM   3120 C  C     . LEU A 1 394 ? 15.81418  -7.92118  -27.92432 1.000 7.02616  ? 394 LEU A C     1 
ATOM   3121 O  O     . LEU A 1 394 ? 15.83518  -9.00820  -28.51329 1.000 7.33127  ? 394 LEU A O     1 
ATOM   3122 C  CB    . LEU A 1 394 ? 17.62821  -7.43912  -26.26137 1.000 5.78979  ? 394 LEU A CB    1 
ATOM   3123 C  CG    . LEU A 1 394 ? 18.86922  -6.65009  -25.83442 1.000 6.69906  ? 394 LEU A CG    1 
ATOM   3124 C  CD1   . LEU A 1 394 ? 19.32425  -7.05705  -24.43942 1.000 7.77765  ? 394 LEU A CD1   1 
ATOM   3125 C  CD2   . LEU A 1 394 ? 19.99520  -6.82211  -26.84244 1.000 5.85348  ? 394 LEU A CD2   1 
ATOM   3126 N  N     . ASN A 1 395 ? 14.68319  -7.37018  -27.47831 1.000 6.02818  ? 395 ASN A N     1 
ATOM   3127 C  CA    . ASN A 1 395 ? 13.38519  -8.00219  -27.69827 1.000 7.28846  ? 395 ASN A CA    1 
ATOM   3128 C  C     . ASN A 1 395 ? 13.05516  -8.08724  -29.18226 1.000 8.97998  ? 395 ASN A C     1 
ATOM   3129 O  O     . ASN A 1 395 ? 12.32515  -8.98726  -29.60721 1.000 10.26311 ? 395 ASN A O     1 
ATOM   3130 C  CB    . ASN A 1 395 ? 12.32000  -7.19500  -26.95600 1.000 8.39957  ? 395 ASN A CB    1 
ATOM   3131 C  CG    . ASN A 1 395 ? 11.11900  -8.00500  -26.51700 1.000 9.30966  ? 395 ASN A CG    1 
ATOM   3132 O  OD1   . ASN A 1 395 ? 10.11300  -8.05300  -27.21800 1.000 14.56263 ? 395 ASN A OD1   1 
ATOM   3133 N  ND2   . ASN A 1 395 ? 11.24400  -8.65200  -25.35800 1.000 11.00751 ? 395 ASN A ND2   1 
ATOM   3134 N  N     . ALA A 1 396 ? 13.59013  -7.16526  -29.98530 1.000 8.90794  ? 396 ALA A N     1 
ATOM   3135 C  CA    . ALA A 1 396 ? 13.27010  -7.12931  -31.40829 1.000 8.87628  ? 396 ALA A CA    1 
ATOM   3136 C  C     . ALA A 1 396 ? 14.14809  -8.08832  -32.20628 1.000 7.45875  ? 396 ALA A C     1 
ATOM   3137 O  O     . ALA A 1 396 ? 13.64108  -8.89135  -32.99824 1.000 8.90360  ? 396 ALA A O     1 
ATOM   3138 C  CB    . ALA A 1 396 ? 13.41108  -5.70232  -31.94234 1.000 9.19577  ? 396 ALA A CB    1 
ATOM   3139 N  N     . ALA A 1 397 ? 15.46810  -8.01331  -32.01231 1.000 7.84621  ? 397 ALA A N     1 
ATOM   3140 C  CA    . ALA A 1 397 ? 16.37909  -8.84232  -32.79630 1.000 8.67970  ? 397 ALA A CA    1 
ATOM   3141 C  C     . ALA A 1 397 ? 16.16810  -10.32532 -32.52825 1.000 7.85247  ? 397 ALA A C     1 
ATOM   3142 O  O     . ALA A 1 397 ? 16.38809  -11.15534 -33.41723 1.000 9.54958  ? 397 ALA A O     1 
ATOM   3143 C  CB    . ALA A 1 397 ? 17.82609  -8.44830  -32.50735 1.000 8.38281  ? 397 ALA A CB    1 
ATOM   3144 N  N     . ASN A 1 398 ? 15.74113  -10.67728 -31.31523 1.000 8.40562  ? 398 ASN A N     1 
ATOM   3145 C  CA    . ASN A 1 398 ? 15.48215  -12.07528 -30.99919 1.000 7.91864  ? 398 ASN A CA    1 
ATOM   3146 C  C     . ASN A 1 398 ? 14.11514  -12.53230 -31.49114 1.000 7.04837  ? 398 ASN A C     1 
ATOM   3147 O  O     . ASN A 1 398 ? 13.94715  -13.70931 -31.82710 1.000 6.47937  ? 398 ASN A O     1 
ATOM   3148 C  CB    . ASN A 1 398 ? 15.60218  -12.30023 -29.49518 1.000 6.70115  ? 398 ASN A CB    1 
ATOM   3149 C  CG    . ASN A 1 398 ? 17.03619  -12.26220 -29.01021 1.000 5.93204  ? 398 ASN A CG    1 
ATOM   3150 O  OD1   . ASN A 1 398 ? 17.74120  -13.27120 -29.04020 1.000 5.93022  ? 398 ASN A OD1   1 
ATOM   3151 N  ND2   . ASN A 1 398 ? 17.47719  -11.09619 -28.55526 1.000 6.80980  ? 398 ASN A ND2   1 
ATOM   3152 N  N     . TRP A 1 399 ? 13.12914  -11.63131 -31.52615 1.000 8.72968  ? 399 TRP A N     1 
ATOM   3153 C  CA    . TRP A 1 399 ? 11.86112  -11.97334 -32.16111 1.000 7.37983  ? 399 TRP A CA    1 
ATOM   3154 C  C     . TRP A 1 399 ? 12.02309  -12.11938 -33.66711 1.000 9.00153  ? 399 TRP A C     1 
ATOM   3155 O  O     . TRP A 1 399 ? 11.34109  -12.94341 -34.28707 1.000 7.87801  ? 399 TRP A O     1 
ATOM   3156 C  CB    . TRP A 1 399 ? 10.79712  -10.92134 -31.83812 1.000 8.96633  ? 399 TRP A CB    1 
ATOM   3157 C  CG    . TRP A 1 399 ? 9.93615   -11.26731 -30.65409 1.000 9.06234  ? 399 TRP A CG    1 
ATOM   3158 C  CD1   . TRP A 1 399 ? 9.98617   -10.70827 -29.41011 1.000 9.24623  ? 399 TRP A CD1   1 
ATOM   3159 C  CD2   . TRP A 1 399 ? 8.89616   -12.25232 -30.60704 1.000 10.02337 ? 399 TRP A CD2   1 
ATOM   3160 N  NE1   . TRP A 1 399 ? 9.04219   -11.28125 -28.59307 1.000 7.55839  ? 399 TRP A NE1   1 
ATOM   3161 C  CE2   . TRP A 1 399 ? 8.36119   -12.23328 -29.30303 1.000 7.90174  ? 399 TRP A CE2   1 
ATOM   3162 C  CE3   . TRP A 1 399 ? 8.36415   -13.14835 -31.54100 1.000 9.99295  ? 399 TRP A CE3   1 
ATOM   3163 C  CZ2   . TRP A 1 399 ? 7.32220   -13.07428 -28.90998 1.000 8.93470  ? 399 TRP A CZ2   1 
ATOM   3164 C  CZ3   . TRP A 1 399 ? 7.33316   -13.98235 -31.14796 1.000 8.58439  ? 399 TRP A CZ3   1 
ATOM   3165 C  CH2   . TRP A 1 399 ? 6.82319   -13.93931 -29.84395 1.000 8.48909  ? 399 TRP A CH2   1 
ATOM   3166 N  N     . MET A 1 400 ? 12.91807  -11.33340 -34.27216 1.000 8.87268  ? 400 MET A N     1 
ATOM   3167 C  CA    . MET A 1 400 ? 13.23305  -11.52944 -35.68316 1.000 10.80555 ? 400 MET A CA    1 
ATOM   3168 C  C     . MET A 1 400 ? 14.11005  -12.75744 -35.88714 1.000 8.78773  ? 400 MET A C     1 
ATOM   3169 O  O     . MET A 1 400 ? 14.07603  -13.37147 -36.96012 1.000 9.92618  ? 400 MET A O     1 
ATOM   3170 C  CB    . MET A 1 400 ? 13.91102  -10.28345 -36.25221 1.000 8.36274  ? 400 MET A CB    1 
ATOM   3171 C  CG    . MET A 1 400 ? 13.02801  -9.04846  -36.25823 1.000 12.43057 ? 400 MET A CG    1 
ATOM   3172 S  SD    . MET A 1 400 ? 13.78999  -7.63147  -37.07229 1.000 13.28238 ? 400 MET A SD    1 
ATOM   3173 C  CE    . MET A 1 400 ? 15.17901  -7.31743  -35.98732 1.000 10.23827 ? 400 MET A CE    1 
ATOM   3174 N  N     . TRP A 1 401 ? 14.90108  -13.12740 -34.87614 1.000 7.69705  ? 401 TRP A N     1 
ATOM   3175 C  CA    . TRP A 1 401 ? 15.68008  -14.35839 -34.94912 1.000 9.68339  ? 401 TRP A CA    1 
ATOM   3176 C  C     . TRP A 1 401 ? 14.76609  -15.57840 -34.94507 1.000 8.49385  ? 401 TRP A C     1 
ATOM   3177 O  O     . TRP A 1 401 ? 14.91408  -16.48043 -35.77604 1.000 8.90114  ? 401 TRP A O     1 
ATOM   3178 C  CB    . TRP A 1 401 ? 16.67011  -14.41935 -33.78214 1.000 9.69025  ? 401 TRP A CB    1 
ATOM   3179 C  CG    . TRP A 1 401 ? 17.64512  -15.56735 -33.84013 1.000 9.97989  ? 401 TRP A CG    1 
ATOM   3180 C  CD1   . TRP A 1 401 ? 17.35713  -16.89734 -33.73008 1.000 10.99308 ? 401 TRP A CD1   1 
ATOM   3181 C  CD2   . TRP A 1 401 ? 19.06711  -15.47734 -33.99516 1.000 13.90464 ? 401 TRP A CD2   1 
ATOM   3182 N  NE1   . TRP A 1 401 ? 18.50913  -17.64134 -33.82308 1.000 12.03087 ? 401 TRP A NE1   1 
ATOM   3183 C  CE2   . TRP A 1 401 ? 19.57312  -16.79333 -33.98413 1.000 14.65346 ? 401 TRP A CE2   1 
ATOM   3184 C  CE3   . TRP A 1 401 ? 19.96110  -14.41334 -34.14721 1.000 12.36790 ? 401 TRP A CE3   1 
ATOM   3185 C  CZ2   . TRP A 1 401 ? 20.93112  -17.07233 -34.11915 1.000 13.37869 ? 401 TRP A CZ2   1 
ATOM   3186 C  CZ3   . TRP A 1 401 ? 21.31010  -14.69333 -34.28223 1.000 14.95120 ? 401 TRP A CZ3   1 
ATOM   3187 C  CH2   . TRP A 1 401 ? 21.78111  -16.01133 -34.26620 1.000 15.74971 ? 401 TRP A CH2   1 
ATOM   3188 N  N     . LEU A 1 402 ? 13.80811  -15.61638 -34.01504 1.000 8.58124  ? 402 LEU A N     1 
ATOM   3189 C  CA    . LEU A 1 402 ? 12.94513  -16.78638 -33.88899 1.000 7.80358  ? 402 LEU A CA    1 
ATOM   3190 C  C     . LEU A 1 402 ? 11.92810  -16.86743 -35.01997 1.000 9.68391  ? 402 LEU A C     1 
ATOM   3191 O  O     . LEU A 1 402 ? 11.47710  -17.96544 -35.36292 1.000 8.44414  ? 402 LEU A O     1 
ATOM   3192 C  CB    . LEU A 1 402 ? 12.23515  -16.77335 -32.53398 1.000 8.72455  ? 402 LEU A CB    1 
ATOM   3193 C  CG    . LEU A 1 402 ? 12.92918  -17.51531 -31.38897 1.000 7.45045  ? 402 LEU A CG    1 
ATOM   3194 C  CD1   . LEU A 1 402 ? 13.01419  -19.00332 -31.69492 1.000 8.94021  ? 402 LEU A CD1   1 
ATOM   3195 C  CD2   . LEU A 1 402 ? 14.31219  -16.94629 -31.12001 1.000 7.89444  ? 402 LEU A CD2   1 
ATOM   3196 N  N     . SER A 1 403 ? 11.55208  -15.73245 -35.60499 1.000 8.49401  ? 403 SER A N     1 
ATOM   3197 C  CA    . SER A 1 403 ? 10.63506  -15.71649 -36.73697 1.000 8.48361  ? 403 SER A CA    1 
ATOM   3198 C  C     . SER A 1 403 ? 11.34703  -15.88152 -38.07298 1.000 10.07817 ? 403 SER A C     1 
ATOM   3199 O  O     . SER A 1 403 ? 10.69101  -15.82056 -39.11797 1.000 10.44805 ? 403 SER A O     1 
ATOM   3200 C  CB    . SER A 1 403 ? 9.82005   -14.41950 -36.74300 1.000 10.26945 ? 403 SER A CB    1 
ATOM   3201 O  OG    . SER A 1 403 ? 10.65803  -13.28549 -36.88305 1.000 8.48720  ? 403 SER A OG    1 
ATOM   3202 N  N     . ALA A 1 404 ? 12.66703  -16.08851 -38.05801 1.000 9.44138  ? 404 ALA A N     1 
ATOM   3203 C  CA    . ALA A 1 404 ? 13.47001  -16.26054 -39.27002 1.000 11.52385 ? 404 ALA A CA    1 
ATOM   3204 C  C     . ALA A 1 404 ? 13.33298  -15.07357 -40.22005 1.000 12.55524 ? 404 ALA A C     1 
ATOM   3205 O  O     . ALA A 1 404 ? 13.37895  -15.23261 -41.44205 1.000 14.09114 ? 404 ALA A O     1 
ATOM   3206 C  CB    . ALA A 1 404 ? 13.12100  -17.56757 -39.99197 1.000 10.83986 ? 404 ALA A CB    1 
ATOM   3207 N  N     . SER A 1 405 ? 13.16698  -13.87356 -39.66708 1.000 11.05009 ? 405 SER A N     1 
ATOM   3208 C  CA    . SER A 1 405 ? 13.09195  -12.66058 -40.46912 1.000 13.66563 ? 405 SER A CA    1 
ATOM   3209 C  C     . SER A 1 405 ? 14.42695  -11.93958 -40.59117 1.000 11.32060 ? 405 SER A C     1 
ATOM   3210 O  O     . SER A 1 405 ? 14.61392  -11.17660 -41.54420 1.000 13.64195 ? 405 SER A O     1 
ATOM   3211 C  CB    . SER A 1 405 ? 12.05296  -11.69657 -39.88113 1.000 13.70501 ? 405 SER A CB    1 
ATOM   3212 O  OG    . SER A 1 405 ? 10.76796  -12.29058 -39.84908 1.000 11.87041 ? 405 SER A OG    1 
ATOM   3213 N  N     . ALA A 1 406 ? 15.34997  -12.16154 -39.65918 1.000 12.64358 ? 406 ALA A N     1 
ATOM   3214 C  CA    . ALA A 1 406 ? 16.66096  -11.53353 -39.70323 1.000 13.00924 ? 406 ALA A CA    1 
ATOM   3215 C  C     . ALA A 1 406 ? 17.64298  -12.39350 -38.92322 1.000 14.36702 ? 406 ALA A C     1 
ATOM   3216 O  O     . ALA A 1 406 ? 17.24901  -13.15548 -38.03619 1.000 15.42157 ? 406 ALA A O     1 
ATOM   3217 C  CB    . ALA A 1 406 ? 16.62696  -10.11051 -39.13427 1.000 13.62339 ? 406 ALA A CB    1 
ATOM   3218 N  N     . PHE A 1 407 ? 18.92398  -12.27250 -39.28225 1.000 15.35079 ? 407 PHE A N     1 
ATOM   3219 C  CA    . PHE A 1 407 ? 20.02000  -12.98947 -38.63426 1.000 14.29933 ? 407 PHE A CA    1 
ATOM   3220 C  C     . PHE A 1 407 ? 19.88200  -14.50148 -38.78221 1.000 16.42609 ? 407 PHE A C     1 
ATOM   3221 O  O     . PHE A 1 407 ? 20.78800  -15.16249 -39.30121 1.000 23.10196 ? 407 PHE A O     1 
ATOM   3222 C  CB    . PHE A 1 407 ? 20.11702  -12.60843 -37.15427 1.000 15.26088 ? 407 PHE A CB    1 
ATOM   3223 C  CG    . PHE A 1 407 ? 20.09802  -11.12642 -36.90731 1.000 14.14539 ? 407 PHE A CG    1 
ATOM   3224 C  CD1   . PHE A 1 407 ? 21.11500  -10.31743 -37.38836 1.000 12.89825 ? 407 PHE A CD1   1 
ATOM   3225 C  CD2   . PHE A 1 407 ? 19.06803  -10.54341 -36.18731 1.000 13.85309 ? 407 PHE A CD2   1 
ATOM   3226 C  CE1   . PHE A 1 407 ? 21.09999  -8.95342  -37.16140 1.000 13.21231 ? 407 PHE A CE1   1 
ATOM   3227 C  CE2   . PHE A 1 407 ? 19.04902  -9.18140  -35.95635 1.000 12.57367 ? 407 PHE A CE2   1 
ATOM   3228 C  CZ    . PHE A 1 407 ? 20.06601  -8.38541  -36.44440 1.000 13.83499 ? 407 PHE A CZ    1 
ATOM   3229 N  N     . PHE A 1 408 ? 18.76502  -15.05947 -38.32317 1.000 14.40603 ? 408 PHE A N     1 
ATOM   3230 C  CA    . PHE A 1 408 ? 18.51703  -16.49048 -38.41212 1.000 14.85940 ? 408 PHE A CA    1 
ATOM   3231 C  C     . PHE A 1 408 ? 17.72300  -16.80452 -39.67309 1.000 16.47294 ? 408 PHE A C     1 
ATOM   3232 O  O     . PHE A 1 408 ? 16.81899  -16.05554 -40.05409 1.000 15.98318 ? 408 PHE A O     1 
ATOM   3233 C  CB    . PHE A 1 408 ? 17.76206  -16.97345 -37.17209 1.000 14.24898 ? 408 PHE A CB    1 
ATOM   3234 C  CG    . PHE A 1 408 ? 17.59307  -18.46344 -37.10004 1.000 15.37300 ? 408 PHE A CG    1 
ATOM   3235 C  CD1   . PHE A 1 408 ? 18.67808  -19.28743 -36.84404 1.000 16.61591 ? 408 PHE A CD1   1 
ATOM   3236 C  CD2   . PHE A 1 408 ? 16.34507  -19.03746 -37.26499 1.000 13.84682 ? 408 PHE A CD2   1 
ATOM   3237 C  CE1   . PHE A 1 408 ? 18.52110  -20.65943 -36.76899 1.000 13.93917 ? 408 PHE A CE1   1 
ATOM   3238 C  CE2   . PHE A 1 408 ? 16.18308  -20.40546 -37.18795 1.000 17.41646 ? 408 PHE A CE2   1 
ATOM   3239 C  CZ    . PHE A 1 408 ? 17.27210  -21.21744 -36.94095 1.000 15.38131 ? 408 PHE A CZ    1 
ATOM   3240 N  N     . SER A 1 409 ? 18.06700  -17.92054 -40.32106 1.000 13.05283 ? 409 SER A N     1 
ATOM   3241 C  CA    . SER A 1 409 ? 17.44797  -18.27158 -41.59204 1.000 15.62000 ? 409 SER A CA    1 
ATOM   3242 C  C     . SER A 1 409 ? 17.07898  -19.74259 -41.72499 1.000 15.13559 ? 409 SER A C     1 
ATOM   3243 O  O     . SER A 1 409 ? 16.62096  -20.14362 -42.79997 1.000 14.95459 ? 409 SER A O     1 
ATOM   3244 C  CB    . SER A 1 409 ? 18.37195  -17.87861 -42.75607 1.000 14.39855 ? 409 SER A CB    1 
ATOM   3245 O  OG    . SER A 1 409 ? 19.64795  -18.47960 -42.61508 1.000 18.13475 ? 409 SER A OG    1 
ATOM   3246 N  N     . GLN A 1 410 ? 17.25401  -20.55856 -40.68497 1.000 15.74424 ? 410 GLN A N     1 
ATOM   3247 C  CA    . GLN A 1 410 ? 16.95902  -21.98856 -40.77292 1.000 15.06104 ? 410 GLN A CA    1 
ATOM   3248 C  C     . GLN A 1 410 ? 15.53103  -22.22656 -40.28988 1.000 13.32999 ? 410 GLN A C     1 
ATOM   3249 O  O     . GLN A 1 410 ? 15.27706  -22.63753 -39.15586 1.000 14.86172 ? 410 GLN A O     1 
ATOM   3250 C  CB    . GLN A 1 410 ? 17.97404  -22.79453 -39.97191 1.000 15.03972 ? 410 GLN A CB    1 
ATOM   3251 C  CG    . GLN A 1 410 ? 17.86805  -24.29154 -40.18087 1.000 14.69014 ? 410 GLN A CG    1 
ATOM   3252 C  CD    . GLN A 1 410 ? 18.03002  -24.68558 -41.63386 1.000 12.45583 ? 410 GLN A CD    1 
ATOM   3253 O  OE1   . GLN A 1 410 ? 17.15502  -25.32560 -42.21682 1.000 16.81592 ? 410 GLN A OE1   1 
ATOM   3254 N  NE2   . GLN A 1 410 ? 19.15401  -24.30459 -42.22889 1.000 14.78768 ? 410 GLN A NE2   1 
ATOM   3255 N  N     . TYR A 1 411 ? 14.57701  -21.96259 -41.18487 1.000 15.57997 ? 411 TYR A N     1 
ATOM   3256 C  CA    . TYR A 1 411 ? 13.16802  -22.14759 -40.86083 1.000 14.75339 ? 411 TYR A CA    1 
ATOM   3257 C  C     . TYR A 1 411 ? 12.74603  -23.61060 -40.85378 1.000 15.00518 ? 411 TYR A C     1 
ATOM   3258 O  O     . TYR A 1 411 ? 11.64204  -23.91459 -40.38875 1.000 16.53508 ? 411 TYR A O     1 
ATOM   3259 C  CB    . TYR A 1 411 ? 12.28899  -21.36163 -41.83884 1.000 15.64624 ? 411 TYR A CB    1 
ATOM   3260 C  CG    . TYR A 1 411 ? 12.50797  -21.70767 -43.29483 1.000 16.68194 ? 411 TYR A CG    1 
ATOM   3261 C  CD1   . TYR A 1 411 ? 11.80296  -22.74170 -43.89779 1.000 17.56449 ? 411 TYR A CD1   1 
ATOM   3262 C  CD2   . TYR A 1 411 ? 13.41394  -20.99369 -44.06787 1.000 17.48249 ? 411 TYR A CD2   1 
ATOM   3263 C  CE1   . TYR A 1 411 ? 12.00094  -23.05873 -45.22878 1.000 18.32701 ? 411 TYR A CE1   1 
ATOM   3264 C  CE2   . TYR A 1 411 ? 13.61692  -21.30373 -45.39887 1.000 19.85560 ? 411 TYR A CE2   1 
ATOM   3265 C  CZ    . TYR A 1 411 ? 12.90791  -22.33675 -45.97282 1.000 17.94912 ? 411 TYR A CZ    1 
ATOM   3266 O  OH    . TYR A 1 411 ? 13.10989  -22.64679 -47.29782 1.000 18.20718 ? 411 TYR A OH    1 
ATOM   3267 N  N     . PHE A 1 412 ? 13.58503  -24.51861 -41.35677 1.000 15.56394 ? 412 PHE A N     1 
ATOM   3268 C  CA    . PHE A 1 412 ? 13.27204  -25.93961 -41.27072 1.000 15.30198 ? 412 PHE A CA    1 
ATOM   3269 C  C     . PHE A 1 412 ? 13.41608  -26.47356 -39.85171 1.000 12.56016 ? 412 PHE A C     1 
ATOM   3270 O  O     . PHE A 1 412 ? 12.89109  -27.55156 -39.55266 1.000 11.97464 ? 412 PHE A O     1 
ATOM   3271 C  CB    . PHE A 1 412 ? 14.16203  -26.73863 -42.22371 1.000 12.55191 ? 412 PHE A CB    1 
ATOM   3272 C  CG    . PHE A 1 412 ? 13.81700  -26.55467 -43.67571 1.000 17.71142 ? 412 PHE A CG    1 
ATOM   3273 C  CD1   . PHE A 1 412 ? 12.69899  -27.16670 -44.21667 1.000 18.34864 ? 412 PHE A CD1   1 
ATOM   3274 C  CD2   . PHE A 1 412 ? 14.61597  -25.78069 -44.50075 1.000 19.78973 ? 412 PHE A CD2   1 
ATOM   3275 C  CE1   . PHE A 1 412 ? 12.37896  -27.00474 -45.55167 1.000 19.84423 ? 412 PHE A CE1   1 
ATOM   3276 C  CE2   . PHE A 1 412 ? 14.30294  -25.61574 -45.83875 1.000 17.03632 ? 412 PHE A CE2   1 
ATOM   3277 C  CZ    . PHE A 1 412 ? 13.18194  -26.22876 -46.36371 1.000 19.97082 ? 412 PHE A CZ    1 
ATOM   3278 N  N     A ARG A 1 413 ? 14.10746  -25.74795 -38.97498 0.557 13.55174 ? 413 ARG A N     1 
ATOM   3279 N  N     B ARG A 1 413 ? 14.11594  -25.75181 -38.97880 0.443 13.63321 ? 413 ARG A N     1 
ATOM   3280 C  CA    A ARG A 1 413 ? 14.26439  -26.14398 -37.57638 0.557 14.10885 ? 413 ARG A CA    1 
ATOM   3281 C  CA    B ARG A 1 413 ? 14.26268  -26.13830 -37.57689 0.443 14.09590 ? 413 ARG A CA    1 
ATOM   3282 C  C     A ARG A 1 413 ? 13.07622  -25.59887 -36.79348 0.557 13.93749 ? 413 ARG A C     1 
ATOM   3283 C  C     B ARG A 1 413 ? 13.06486  -25.59312 -36.80989 0.443 13.89642 ? 413 ARG A C     1 
ATOM   3284 O  O     A ARG A 1 413 ? 13.01912  -24.40873 -36.47529 0.557 12.38367 ? 413 ARG A O     1 
ATOM   3285 O  O     B ARG A 1 413 ? 12.98913  -24.39680 -36.51983 0.443 12.10098 ? 413 ARG A O     1 
ATOM   3286 C  CB    A ARG A 1 413 ? 15.58643  -25.63250 -37.01562 0.557 13.84665 ? 413 ARG A CB    1 
ATOM   3287 C  CB    B ARG A 1 413 ? 15.57620  -25.61642 -37.00591 0.443 13.84384 ? 413 ARG A CB    1 
ATOM   3288 C  CG    A ARG A 1 413 ? 15.83747  -26.01349 -35.56487 0.557 13.32473 ? 413 ARG A CG    1 
ATOM   3289 C  CG    B ARG A 1 413 ? 15.74047  -25.85817 -35.51399 0.443 13.33854 ? 413 ARG A CG    1 
ATOM   3290 C  CD    A ARG A 1 413 ? 15.97243  -27.51903 -35.40039 0.557 13.71961 ? 413 ARG A CD    1 
ATOM   3291 C  CD    B ARG A 1 413 ? 15.85187  -27.34050 -35.19889 0.443 13.75508 ? 413 ARG A CD    1 
ATOM   3292 N  NE    A ARG A 1 413 ? 16.23556  -27.89484 -34.01626 0.557 14.40234 ? 413 ARG A NE    1 
ATOM   3293 N  NE    B ARG A 1 413 ? 15.78484  -27.59913 -33.76546 0.443 15.04832 ? 413 ARG A NE    1 
ATOM   3294 C  CZ    A ARG A 1 413 ? 15.29658  -28.20436 -33.13262 0.557 15.36455 ? 413 ARG A CZ    1 
ATOM   3295 C  CZ    B ARG A 1 413 ? 16.81530  -27.50356 -32.93637 0.443 14.73189 ? 413 ARG A CZ    1 
ATOM   3296 N  NH1   A ARG A 1 413 ? 14.01391  -28.20119 -33.45716 0.557 15.03225 ? 413 ARG A NH1   1 
ATOM   3297 N  NH1   B ARG A 1 413 ? 18.01510  -27.14498 -33.36287 0.443 15.74856 ? 413 ARG A NH1   1 
ATOM   3298 N  NH2   A ARG A 1 413 ? 15.65344  -28.52636 -31.89227 0.557 14.99181 ? 413 ARG A NH2   1 
ATOM   3299 N  NH2   B ARG A 1 413 ? 16.63728  -27.77436 -31.64643 0.443 15.43418 ? 413 ARG A NH2   1 
ATOM   3300 N  N     . VAL A 1 414 ? 12.12315  -26.47247 -36.48068 1.000 13.64269 ? 414 VAL A N     1 
ATOM   3301 C  CA    . VAL A 1 414 ? 10.90516  -26.10146 -35.76967 1.000 13.82543 ? 414 VAL A CA    1 
ATOM   3302 C  C     . VAL A 1 414 ? 10.87619  -26.85142 -34.44564 1.000 14.36437 ? 414 VAL A C     1 
ATOM   3303 O  O     . VAL A 1 414 ? 10.92820  -28.08742 -34.42461 1.000 15.67123 ? 414 VAL A O     1 
ATOM   3304 C  CB    . VAL A 1 414 ? 9.64514   -26.40249 -36.59563 1.000 14.29445 ? 414 VAL A CB    1 
ATOM   3305 C  CG1   . VAL A 1 414 ? 8.39516   -26.14248 -35.76961 1.000 13.31521 ? 414 VAL A CG1   1 
ATOM   3306 C  CG2   . VAL A 1 414 ? 9.63311   -25.56453 -37.86465 1.000 14.77498 ? 414 VAL A CG2   1 
ATOM   3307 N  N     . TYR A 1 415 ? 10.79521  -26.10538 -33.34766 1.000 14.02912 ? 415 TYR A N     1 
ATOM   3308 C  CA    . TYR A 1 415 ? 10.68424  -26.72035 -32.03264 1.000 12.16431 ? 415 TYR A CA    1 
ATOM   3309 C  C     . TYR A 1 415 ? 9.31825   -27.37435 -31.86959 1.000 12.36398 ? 415 TYR A C     1 
ATOM   3310 O  O     . TYR A 1 415 ? 8.30224   -26.85137 -32.33359 1.000 12.20707 ? 415 TYR A O     1 
ATOM   3311 C  CB    . TYR A 1 415 ? 10.89826  -25.67431 -30.93768 1.000 12.35538 ? 415 TYR A CB    1 
ATOM   3312 C  CG    . TYR A 1 415 ? 12.26925  -25.03930 -30.94573 1.000 13.36735 ? 415 TYR A CG    1 
ATOM   3313 C  CD1   . TYR A 1 415 ? 13.39925  -25.78230 -31.25673 1.000 13.68428 ? 415 TYR A CD1   1 
ATOM   3314 C  CD2   . TYR A 1 415 ? 12.43325  -23.69329 -30.64477 1.000 11.55940 ? 415 TYR A CD2   1 
ATOM   3315 C  CE1   . TYR A 1 415 ? 14.65425  -25.20529 -31.26577 1.000 11.95130 ? 415 TYR A CE1   1 
ATOM   3316 C  CE2   . TYR A 1 415 ? 13.68424  -23.10728 -30.65081 1.000 15.09163 ? 415 TYR A CE2   1 
ATOM   3317 C  CZ    . TYR A 1 415 ? 14.79124  -23.86728 -30.96181 1.000 14.56886 ? 415 TYR A CZ    1 
ATOM   3318 O  OH    . TYR A 1 415 ? 16.03924  -23.28727 -30.96886 1.000 18.68034 ? 415 TYR A OH    1 
ATOM   3319 N  N     . SER A 1 416 ? 9.30028   -28.52833 -31.20756 1.000 11.33956 ? 416 SER A N     1 
ATOM   3320 C  CA    . SER A 1 416 ? 8.05429   -29.23933 -30.95551 1.000 12.15398 ? 416 SER A CA    1 
ATOM   3321 C  C     . SER A 1 416 ? 7.50331   -28.83630 -29.59551 1.000 10.10976 ? 416 SER A C     1 
ATOM   3322 O  O     . SER A 1 416 ? 8.20133   -29.00026 -28.58652 1.000 9.76845  ? 416 SER A O     1 
ATOM   3323 C  CB    . SER A 1 416 ? 8.27230   -30.74133 -31.00447 1.000 11.67671 ? 416 SER A CB    1 
ATOM   3324 O  OG    . SER A 1 416 ? 7.08231   -31.43833 -30.67542 1.000 11.33823 ? 416 SER A OG    1 
ATOM   3325 N  N     . PRO A 1 417 ? 6.27431   -28.31730 -29.51350 1.000 10.08817 ? 417 PRO A N     1 
ATOM   3326 C  CA    . PRO A 1 417 ? 5.70833   -27.95427 -28.20550 1.000 10.82448 ? 417 PRO A CA    1 
ATOM   3327 C  C     . PRO A 1 417 ? 5.36836   -29.14724 -27.32746 1.000 12.53255 ? 417 PRO A C     1 
ATOM   3328 O  O     . PRO A 1 417 ? 4.89038   -28.95021 -26.20445 1.000 12.25918 ? 417 PRO A O     1 
ATOM   3329 C  CB    . PRO A 1 417 ? 4.44332   -27.16929 -28.58350 1.000 10.36285 ? 417 PRO A CB    1 
ATOM   3330 C  CG    . PRO A 1 417 ? 4.05730   -27.71133 -29.91747 1.000 11.44286 ? 417 PRO A CG    1 
ATOM   3331 C  CD    . PRO A 1 417 ? 5.34928   -28.02034 -30.62149 1.000 11.68669 ? 417 PRO A CD    1 
ATOM   3332 N  N     . VAL A 1 418 ? 5.59736   -30.37226 -27.79942 1.000 12.71788 ? 418 VAL A N     1 
ATOM   3333 C  CA    . VAL A 1 418 ? 5.31039   -31.56424 -27.02238 1.000 14.46185 ? 418 VAL A CA    1 
ATOM   3334 C  C     . VAL A 1 418 ? 6.57840   -32.27921 -26.56139 1.000 14.06185 ? 418 VAL A C     1 
ATOM   3335 O  O     . VAL A 1 418 ? 6.59243   -32.83618 -25.45737 1.000 19.12881 ? 418 VAL A O     1 
ATOM   3336 C  CB    . VAL A 1 418 ? 4.40438   -32.52427 -27.82333 1.000 15.51558 ? 418 VAL A CB    1 
ATOM   3337 C  CG1   . VAL A 1 418 ? 3.97241   -33.70124 -26.96429 1.000 18.14699 ? 418 VAL A CG1   1 
ATOM   3338 C  CG2   . VAL A 1 418 ? 3.19136   -31.78129 -28.37033 1.000 14.24568 ? 418 VAL A CG2   1 
ATOM   3339 N  N     . VAL A 1 419 ? 7.64439   -32.26323 -27.35841 1.000 15.00039 ? 419 VAL A N     1 
ATOM   3340 C  CA    . VAL A 1 419 ? 8.84540   -33.03021 -27.05241 1.000 13.84231 ? 419 VAL A CA    1 
ATOM   3341 C  C     . VAL A 1 419 ? 9.99740   -32.16418 -26.55346 1.000 11.67953 ? 419 VAL A C     1 
ATOM   3342 O  O     . VAL A 1 419 ? 10.88242  -32.68716 -25.85747 1.000 13.88490 ? 419 VAL A O     1 
ATOM   3343 C  CB    . VAL A 1 419 ? 9.29438   -33.85924 -28.27440 1.000 11.76651 ? 419 VAL A CB    1 
ATOM   3344 C  CG1   . VAL A 1 419 ? 10.25840  -34.96322 -27.85938 1.000 15.13144 ? 419 VAL A CG1   1 
ATOM   3345 C  CG2   . VAL A 1 419 ? 8.08637   -34.44027 -28.99335 1.000 14.20413 ? 419 VAL A CG2   1 
ATOM   3346 N  N     . PHE A 1 420 ? 10.01739  -30.86619 -26.87350 1.000 11.73842 ? 420 PHE A N     1 
ATOM   3347 C  CA    . PHE A 1 420 ? 11.15339  -30.02517 -26.50355 1.000 10.67472 ? 420 PHE A CA    1 
ATOM   3348 C  C     . PHE A 1 420 ? 11.33342  -29.97113 -24.99156 1.000 10.30429 ? 420 PHE A C     1 
ATOM   3349 O  O     . PHE A 1 420 ? 12.44943  -30.12810 -24.48158 1.000 12.81904 ? 420 PHE A O     1 
ATOM   3350 C  CB    . PHE A 1 420 ? 10.97536  -28.61919 -27.07559 1.000 11.46443 ? 420 PHE A CB    1 
ATOM   3351 C  CG    . PHE A 1 420 ? 12.15336  -27.71418 -26.84264 1.000 10.95861 ? 420 PHE A CG    1 
ATOM   3352 C  CD1   . PHE A 1 420 ? 13.24334  -27.74319 -27.69766 1.000 14.28080 ? 420 PHE A CD1   1 
ATOM   3353 C  CD2   . PHE A 1 420 ? 12.17038  -26.83314 -25.77467 1.000 11.31496 ? 420 PHE A CD2   1 
ATOM   3354 C  CE1   . PHE A 1 420 ? 14.32834  -26.91218 -27.48971 1.000 14.83423 ? 420 PHE A CE1   1 
ATOM   3355 C  CE2   . PHE A 1 420 ? 13.25137  -26.00013 -25.56072 1.000 10.76095 ? 420 PHE A CE2   1 
ATOM   3356 C  CZ    . PHE A 1 420 ? 14.33236  -26.03915 -26.41974 1.000 13.25867 ? 420 PHE A CZ    1 
ATOM   3357 N  N     . GLY A 1 421 ? 10.24343  -29.74911 -24.25454 1.000 10.35067 ? 421 GLY A N     1 
ATOM   3358 C  CA    . GLY A 1 421 ? 10.33146  -29.70007 -22.80654 1.000 11.45965 ? 421 GLY A CA    1 
ATOM   3359 C  C     . GLY A 1 421 ? 10.48449  -31.05605 -22.15151 1.000 11.31402 ? 421 GLY A C     1 
ATOM   3360 O  O     . GLY A 1 421 ? 10.94051  -31.13101 -21.00651 1.000 9.93709  ? 421 GLY A O     1 
ATOM   3361 N  N     . LYS A 1 422 ? 10.11848  -32.13007 -22.85447 1.000 12.40910 ? 422 LYS A N     1 
ATOM   3362 C  CA    . LYS A 1 422 ? 10.20450  -33.46505 -22.27043 1.000 12.41563 ? 422 LYS A CA    1 
ATOM   3363 C  C     . LYS A 1 422 ? 11.65151  -33.91504 -22.10144 1.000 13.62221 ? 422 LYS A C     1 
ATOM   3364 O  O     . LYS A 1 422 ? 11.94654  -34.73401 -21.22243 1.000 13.23702 ? 422 LYS A O     1 
ATOM   3365 C  CB    . LYS A 1 422 ? 9.42449   -34.46009 -23.13438 1.000 15.33323 ? 422 LYS A CB    1 
ATOM   3366 C  CG    . LYS A 1 422 ? 9.35552   -35.87007 -22.56934 1.000 18.16484 ? 422 LYS A CG    1 
ATOM   3367 C  CD    . LYS A 1 422 ? 8.43151   -36.75710 -23.39029 1.000 20.63360 ? 422 LYS A CD    1 
ATOM   3368 C  CE    . LYS A 1 422 ? 6.98550   -36.29911 -23.28527 1.000 15.64956 ? 422 LYS A CE    1 
ATOM   3369 N  NZ    . LYS A 1 422 ? 6.06049   -37.18514 -24.04523 1.000 15.30131 ? 422 LYS A NZ    1 
ATOM   3370 N  N     . LYS A 1 423 ? 12.56649  -33.38805 -22.91948 1.000 13.04419 ? 423 LYS A N     1 
ATOM   3371 C  CA    . LYS A 1 423 ? 13.95649  -33.82604 -22.84850 1.000 14.03165 ? 423 LYS A CA    1 
ATOM   3372 C  C     . LYS A 1 423 ? 14.64852  -33.32200 -21.58753 1.000 12.82988 ? 423 LYS A C     1 
ATOM   3373 O  O     . LYS A 1 423 ? 15.59753  -33.95498 -21.11053 1.000 15.86313 ? 423 LYS A O     1 
ATOM   3374 C  CB    . LYS A 1 423 ? 14.71246  -33.36807 -24.09553 1.000 14.35506 ? 423 LYS A CB    1 
ATOM   3375 C  CG    . LYS A 1 423 ? 14.16244  -33.94512 -25.38850 0.000 14.81733 ? 423 LYS A CG    1 
ATOM   3376 C  CD    . LYS A 1 423 ? 14.88441  -33.38815 -26.60153 0.000 15.66144 ? 423 LYS A CD    1 
ATOM   3377 C  CE    . LYS A 1 423 ? 14.31439  -33.96119 -27.88950 0.000 16.40612 ? 423 LYS A CE    1 
ATOM   3378 N  NZ    . LYS A 1 423 ? 14.96636  -33.38822 -29.09853 0.000 17.76264 ? 423 LYS A NZ    1 
ATOM   3379 N  N     . TYR A 1 424 ? 14.19652  -32.19798 -21.03455 1.000 10.49226 ? 424 TYR A N     1 
ATOM   3380 C  CA    . TYR A 1 424 ? 14.76354  -31.65194 -19.80758 1.000 11.70051 ? 424 TYR A CA    1 
ATOM   3381 C  C     . TYR A 1 424 ? 13.99757  -32.07191 -18.56155 1.000 12.28367 ? 424 TYR A C     1 
ATOM   3382 O  O     . TYR A 1 424 ? 14.61259  -32.37288 -17.53355 1.000 10.55165 ? 424 TYR A O     1 
ATOM   3383 C  CB    . TYR A 1 424 ? 14.80053  -30.12194 -19.87363 1.000 11.56370 ? 424 TYR A CB    1 
ATOM   3384 C  CG    . TYR A 1 424 ? 15.62950  -29.55897 -21.00466 1.000 9.80783  ? 424 TYR A CG    1 
ATOM   3385 C  CD1   . TYR A 1 424 ? 16.99350  -29.34996 -20.85370 1.000 9.67334  ? 424 TYR A CD1   1 
ATOM   3386 C  CD2   . TYR A 1 424 ? 15.04447  -29.22301 -22.21766 1.000 10.03573 ? 424 TYR A CD2   1 
ATOM   3387 C  CE1   . TYR A 1 424 ? 17.75347  -28.82998 -21.88473 1.000 7.81300  ? 424 TYR A CE1   1 
ATOM   3388 C  CE2   . TYR A 1 424 ? 15.79544  -28.70204 -23.25369 1.000 10.05725 ? 424 TYR A CE2   1 
ATOM   3389 C  CZ    . TYR A 1 424 ? 17.14945  -28.50702 -23.08172 1.000 7.21774  ? 424 TYR A CZ    1 
ATOM   3390 O  OH    . TYR A 1 424 ? 17.89942  -27.98805 -24.11076 1.000 8.52600  ? 424 TYR A OH    1 
ATOM   3391 N  N     . ASP A 1 425 ? 12.66757  -32.09692 -18.63152 1.000 10.08888 ? 425 ASP A N     1 
ATOM   3392 C  CA    . ASP A 1 425 ? 11.80460  -32.34190 -17.47749 1.000 13.11389 ? 425 ASP A CA    1 
ATOM   3393 C  C     . ASP A 1 425 ? 10.76060  -33.37692 -17.87344 1.000 11.34678 ? 425 ASP A C     1 
ATOM   3394 O  O     . ASP A 1 425 ? 9.63158   -33.02794 -18.24443 1.000 13.38682 ? 425 ASP A O     1 
ATOM   3395 C  CB    . ASP A 1 425 ? 11.15460  -31.04189 -17.00052 1.000 12.03278 ? 425 ASP A CB    1 
ATOM   3396 C  CG    . ASP A 1 425 ? 10.43762  -31.19285 -15.67450 1.000 12.95287 ? 425 ASP A CG    1 
ATOM   3397 O  OD1   . ASP A 1 425 ? 10.49365  -32.28883 -15.07847 1.000 12.50456 ? 425 ASP A OD1   1 
ATOM   3398 O  OD2   . ASP A 1 425 ? 9.81863   -30.20584 -15.22652 1.000 14.74324 ? 425 ASP A OD2   1 
ATOM   3399 N  N     . PRO A 1 426 ? 11.10461  -34.66691 -17.80441 1.000 12.27162 ? 426 PRO A N     1 
ATOM   3400 C  CA    . PRO A 1 426 ? 10.14861  -35.70193 -18.22636 1.000 11.22886 ? 426 PRO A CA    1 
ATOM   3401 C  C     . PRO A 1 426 ? 8.94063   -35.82891 -17.31633 1.000 14.66404 ? 426 PRO A C     1 
ATOM   3402 O  O     . PRO A 1 426 ? 7.88962   -36.29394 -17.77429 1.000 12.76737 ? 426 PRO A O     1 
ATOM   3403 C  CB    . PRO A 1 426 ? 10.99162  -36.98392 -18.21134 1.000 10.59099 ? 426 PRO A CB    1 
ATOM   3404 C  CG    . PRO A 1 426 ? 12.06464  -36.70689 -17.21037 1.000 13.52469 ? 426 PRO A CG    1 
ATOM   3405 C  CD    . PRO A 1 426 ? 12.37762  -35.24189 -17.33842 1.000 12.36041 ? 426 PRO A CD    1 
ATOM   3406 N  N     . GLU A 1 427 ? 9.05065   -35.43687 -16.04934 1.000 13.43491 ? 427 GLU A N     1 
ATOM   3407 C  CA    . GLU A 1 427 ? 7.92867   -35.50186 -15.12432 1.000 15.58954 ? 427 GLU A CA    1 
ATOM   3408 C  C     . GLU A 1 427 ? 7.05566   -34.25586 -15.15434 1.000 13.89212 ? 427 GLU A C     1 
ATOM   3409 O  O     . GLU A 1 427 ? 6.00667   -34.23785 -14.50331 1.000 14.88044 ? 427 GLU A O     1 
ATOM   3410 C  CB    . GLU A 1 427 ? 8.43570   -35.73781 -13.69932 1.000 15.60610 ? 427 GLU A CB    1 
ATOM   3411 C  CG    . GLU A 1 427 ? 9.02672   -37.11780 -13.48729 1.000 16.47161 ? 427 GLU A CG    1 
ATOM   3412 C  CD    . GLU A 1 427 ? 8.00272   -38.21681 -13.68424 1.000 21.27298 ? 427 GLU A CD    1 
ATOM   3413 O  OE1   . GLU A 1 427 ? 6.90173   -38.11280 -13.10422 1.000 24.73998 ? 427 GLU A OE1   1 
ATOM   3414 O  OE2   . GLU A 1 427 ? 8.29171   -39.17583 -14.42921 1.000 21.60291 ? 427 GLU A OE2   1 
ATOM   3415 N  N     . GLY A 1 428 ? 7.45664   -33.22488 -15.89138 1.000 10.53078 ? 428 GLY A N     1 
ATOM   3416 C  CA    . GLY A 1 428 ? 6.66462   -32.01189 -15.97940 1.000 14.68068 ? 428 GLY A CA    1 
ATOM   3417 C  C     . GLY A 1 428 ? 6.60165   -31.20785 -14.69842 1.000 13.98320 ? 428 GLY A C     1 
ATOM   3418 O  O     . GLY A 1 428 ? 5.55065   -30.63685 -14.38341 1.000 12.91407 ? 428 GLY A O     1 
ATOM   3419 N  N     . ARG A 1 429 ? 7.70431   -31.14985 -13.94607 1.000 12.56728 ? 429 ARG A N     1 
ATOM   3420 C  CA    . ARG A 1 429 ? 7.71907   -30.35222 -12.72389 1.000 12.62596 ? 429 ARG A CA    1 
ATOM   3421 C  C     . ARG A 1 429 ? 7.53188   -28.87150 -13.02369 1.000 12.85578 ? 429 ARG A C     1 
ATOM   3422 O  O     . ARG A 1 429 ? 6.91548   -28.14979 -12.23105 1.000 14.15769 ? 429 ARG A O     1 
ATOM   3423 C  CB    . ARG A 1 429 ? 9.02521   -30.57833 -11.96192 1.000 13.45273 ? 429 ARG A CB    1 
ATOM   3424 C  CG    . ARG A 1 429 ? 9.34412   -32.03978 -11.69615 1.000 14.28877 ? 429 ARG A CG    1 
ATOM   3425 C  CD    . ARG A 1 429 ? 8.19994   -32.73442 -10.97653 1.000 19.51566 ? 429 ARG A CD    1 
ATOM   3426 N  NE    . ARG A 1 429 ? 8.47802   -34.14709 -10.74693 0.000 17.25033 ? 429 ARG A NE    1 
ATOM   3427 C  CZ    . ARG A 1 429 ? 7.60761   -35.00952 -10.24006 0.000 17.81381 ? 429 ARG A CZ    1 
ATOM   3428 N  NH1   . ARG A 1 429 ? 6.38459   -34.63770 -9.89920  0.000 17.70397 ? 429 ARG A NH1   1 
ATOM   3429 N  NH2   . ARG A 1 429 ? 7.97270   -36.27745 -10.07308 0.000 18.42902 ? 429 ARG A NH2   1 
ATOM   3430 N  N     . PHE A 1 430 ? 8.05463   -28.40282 -14.15953 1.000 10.90035 ? 430 PHE A N     1 
ATOM   3431 C  CA    . PHE A 1 430 ? 7.85062   -27.01484 -14.55857 1.000 12.48336 ? 430 PHE A CA    1 
ATOM   3432 C  C     . PHE A 1 430 ? 6.39461   -26.74686 -14.92155 1.000 12.30850 ? 430 PHE A C     1 
ATOM   3433 O  O     . PHE A 1 430 ? 5.90260   -25.63086 -14.71757 1.000 15.07873 ? 430 PHE A O     1 
ATOM   3434 C  CB    . PHE A 1 430 ? 8.77059   -26.67687 -15.73260 1.000 10.40397 ? 430 PHE A CB    1 
ATOM   3435 C  CG    . PHE A 1 430 ? 8.63957   -25.26388 -16.22964 1.000 11.01299 ? 430 PHE A CG    1 
ATOM   3436 C  CD1   . PHE A 1 430 ? 9.31857   -24.23086 -15.60569 1.000 10.43593 ? 430 PHE A CD1   1 
ATOM   3437 C  CD2   . PHE A 1 430 ? 7.85254   -24.97092 -17.33263 1.000 10.55276 ? 430 PHE A CD2   1 
ATOM   3438 C  CE1   . PHE A 1 430 ? 9.20655   -22.92987 -16.06473 1.000 9.25803  ? 430 PHE A CE1   1 
ATOM   3439 C  CE2   . PHE A 1 430 ? 7.73552   -23.67294 -17.79567 1.000 11.10577 ? 430 PHE A CE2   1 
ATOM   3440 C  CZ    . PHE A 1 430 ? 8.41453   -22.65091 -17.16072 1.000 8.54908  ? 430 PHE A CZ    1 
ATOM   3441 N  N     . ILE A 1 431 ? 5.69360   -27.75088 -15.44750 1.000 13.46213 ? 431 ILE A N     1 
ATOM   3442 C  CA    . ILE A 1 431 ? 4.30259   -27.56191 -15.84848 1.000 13.00921 ? 431 ILE A CA    1 
ATOM   3443 C  C     . ILE A 1 431 ? 3.38062   -27.56788 -14.63446 1.000 13.19919 ? 431 ILE A C     1 
ATOM   3444 O  O     . ILE A 1 431 ? 2.48361   -26.72388 -14.52147 1.000 13.46797 ? 431 ILE A O     1 
ATOM   3445 C  CB    . ILE A 1 431 ? 3.89658   -28.63494 -16.87344 1.000 11.53093 ? 431 ILE A CB    1 
ATOM   3446 C  CG1   . ILE A 1 431 ? 4.77155   -28.53497 -18.12346 1.000 12.89126 ? 431 ILE A CG1   1 
ATOM   3447 C  CG2   . ILE A 1 431 ? 2.42457   -28.50096 -17.23541 1.000 14.08531 ? 431 ILE A CG2   1 
ATOM   3448 C  CD1   . ILE A 1 431 ? 4.40354   -29.52401 -19.20742 1.000 10.32620 ? 431 ILE A CD1   1 
ATOM   3449 N  N     . ARG A 1 432 ? 3.58905   -28.50566 -13.70589 1.000 11.36635 ? 432 ARG A N     1 
ATOM   3450 C  CA    . ARG A 1 432 ? 2.72540   -28.59246 -12.53181 1.000 12.91125 ? 432 ARG A CA    1 
ATOM   3451 C  C     . ARG A 1 432 ? 2.83782   -27.35339 -11.65250 1.000 12.36788 ? 432 ARG A C     1 
ATOM   3452 O  O     . ARG A 1 432 ? 1.89710   -27.02624 -10.92023 1.000 12.61542 ? 432 ARG A O     1 
ATOM   3453 C  CB    . ARG A 1 432 ? 3.06404   -29.84448 -11.72215 1.000 15.21110 ? 432 ARG A CB    1 
ATOM   3454 C  CG    . ARG A 1 432 ? 3.03344   -31.13404 -12.52454 1.000 14.10827 ? 432 ARG A CG    1 
ATOM   3455 C  CD    . ARG A 1 432 ? 3.51545   -32.30909 -11.69140 1.000 15.37579 ? 432 ARG A CD    1 
ATOM   3456 N  NE    . ARG A 1 432 ? 3.84123   -33.46581 -12.51681 1.000 17.17623 ? 432 ARG A NE    1 
ATOM   3457 C  CZ    . ARG A 1 432 ? 2.97821   -34.41348 -12.85550 1.000 17.51624 ? 432 ARG A CZ    1 
ATOM   3458 N  NH1   . ARG A 1 432 ? 1.71659   -34.37355 -12.45884 1.000 20.33867 ? 432 ARG A NH1   1 
ATOM   3459 N  NH2   . ARG A 1 432 ? 3.39161   -35.42714 -13.61099 1.000 17.36793 ? 432 ARG A NH2   1 
ATOM   3460 N  N     . LYS A 1 433 ? 3.97367   -26.65578 -11.70550 1.000 10.82379 ? 433 LYS A N     1 
ATOM   3461 C  CA    . LYS A 1 433 ? 4.14768   -25.45376 -10.89654 1.000 13.54956 ? 433 LYS A CA    1 
ATOM   3462 C  C     . LYS A 1 433 ? 3.29766   -24.30578 -11.42956 1.000 12.94711 ? 433 LYS A C     1 
ATOM   3463 O  O     . LYS A 1 433 ? 2.47367   -23.73676 -10.70456 1.000 14.65385 ? 433 LYS A O     1 
ATOM   3464 C  CB    . LYS A 1 433 ? 5.62668   -25.06374 -10.85658 1.000 12.09241 ? 433 LYS A CB    1 
ATOM   3465 C  CG    . LYS A 1 433 ? 5.89468   -23.63573 -10.39863 1.000 14.33903 ? 433 LYS A CG    1 
ATOM   3466 C  CD    . LYS A 1 433 ? 5.47571   -23.40769 -8.95563  1.000 16.68547 ? 433 LYS A CD    1 
ATOM   3467 C  CE    . LYS A 1 433 ? 5.71470   -21.96267 -8.54368  1.000 16.85052 ? 433 LYS A CE    1 
ATOM   3468 N  NZ    . LYS A 1 433 ? 5.28673   -21.69963 -7.14268  1.000 17.68798 ? 433 LYS A NZ    1 
ATOM   3469 N  N     . PHE A 1 434 ? 3.48363   -23.95282 -12.70057 1.000 13.10383 ? 434 PHE A N     1 
ATOM   3470 C  CA    . PHE A 1 434 ? 2.79061   -22.81784 -13.29459 1.000 11.42258 ? 434 PHE A CA    1 
ATOM   3471 C  C     . PHE A 1 434 ? 1.41660   -23.17287 -13.84755 1.000 10.11839 ? 434 PHE A C     1 
ATOM   3472 O  O     . PHE A 1 434 ? 0.63459   -22.26488 -14.14756 1.000 13.26450 ? 434 PHE A O     1 
ATOM   3473 C  CB    . PHE A 1 434 ? 3.65258   -22.20187 -14.40063 1.000 12.72940 ? 434 PHE A CB    1 
ATOM   3474 C  CG    . PHE A 1 434 ? 4.94859   -21.62384 -13.90367 1.000 9.73139  ? 434 PHE A CG    1 
ATOM   3475 C  CD1   . PHE A 1 434 ? 5.01059   -20.31583 -13.45272 1.000 7.36836  ? 434 PHE A CD1   1 
ATOM   3476 C  CD2   . PHE A 1 434 ? 6.10059   -22.38983 -13.88268 1.000 11.07013 ? 434 PHE A CD2   1 
ATOM   3477 C  CE1   . PHE A 1 434 ? 6.19959   -19.78280 -12.99076 1.000 11.04137 ? 434 PHE A CE1   1 
ATOM   3478 C  CE2   . PHE A 1 434 ? 7.29260   -21.86181 -13.42072 1.000 9.98715  ? 434 PHE A CE2   1 
ATOM   3479 C  CZ    . PHE A 1 434 ? 7.34260   -20.55579 -12.97576 1.000 10.05139 ? 434 PHE A CZ    1 
ATOM   3480 N  N     . LEU A 1 435 ? 1.10561   -24.45887 -13.99451 1.000 12.09337 ? 435 LEU A N     1 
ATOM   3481 C  CA    . LEU A 1 435 ? -0.22640  -24.92190 -14.38347 1.000 13.12189 ? 435 LEU A CA    1 
ATOM   3482 C  C     . LEU A 1 435 ? -0.67037  -25.95787 -13.36042 1.000 12.46198 ? 435 LEU A C     1 
ATOM   3483 O  O     . LEU A 1 435 ? -0.61636  -27.16788 -13.61839 1.000 11.70394 ? 435 LEU A O     1 
ATOM   3484 C  CB    . LEU A 1 435 ? -0.22842  -25.49594 -15.80145 1.000 9.67899  ? 435 LEU A CB    1 
ATOM   3485 C  CG    . LEU A 1 435 ? 0.00255   -24.51197 -16.95048 1.000 11.88525 ? 435 LEU A CG    1 
ATOM   3486 C  CD1   . LEU A 1 435 ? 0.03152   -25.24201 -18.28446 1.000 8.31354  ? 435 LEU A CD1   1 
ATOM   3487 C  CD2   . LEU A 1 435 ? -1.06746  -23.43098 -16.95649 1.000 10.01644 ? 435 LEU A CD2   1 
ATOM   3488 N  N     . PRO A 1 436 ? -1.11935  -25.51484 -12.18043 1.000 14.12013 ? 436 PRO A N     1 
ATOM   3489 C  CA    . PRO A 1 436 ? -1.48632  -26.47281 -11.12439 1.000 13.90187 ? 436 PRO A CA    1 
ATOM   3490 C  C     . PRO A 1 436 ? -2.69832  -27.32483 -11.45434 1.000 13.43014 ? 436 PRO A C     1 
ATOM   3491 O  O     . PRO A 1 436 ? -2.96229  -28.29181 -10.72631 1.000 11.70222 ? 436 PRO A O     1 
ATOM   3492 C  CB    . PRO A 1 436 ? -1.75730  -25.57077 -9.91341  1.000 16.72309 ? 436 PRO A CB    1 
ATOM   3493 C  CG    . PRO A 1 436 ? -2.14232  -24.25679 -10.50844 1.000 16.04766 ? 436 PRO A CG    1 
ATOM   3494 C  CD    . PRO A 1 436 ? -1.32135  -24.11883 -11.75947 1.000 13.70839 ? 436 PRO A CD    1 
ATOM   3495 N  N     . VAL A 1 437 ? -3.44234  -27.00687 -12.51633 1.000 12.96296 ? 437 VAL A N     1 
ATOM   3496 C  CA    . VAL A 1 437 ? -4.57534  -27.83389 -12.91228 1.000 15.61528 ? 437 VAL A CA    1 
ATOM   3497 C  C     . VAL A 1 437 ? -4.11934  -29.21890 -13.35625 1.000 14.76366 ? 437 VAL A C     1 
ATOM   3498 O  O     . VAL A 1 437 ? -4.89233  -30.18090 -13.28521 1.000 15.01343 ? 437 VAL A O     1 
ATOM   3499 C  CB    . VAL A 1 437 ? -5.38537  -27.11993 -14.02029 1.000 14.28687 ? 437 VAL A CB    1 
ATOM   3500 C  CG1   . VAL A 1 437 ? -4.56740  -27.00396 -15.30031 1.000 15.32485 ? 437 VAL A CG1   1 
ATOM   3501 C  CG2   . VAL A 1 437 ? -6.70737  -27.83294 -14.27524 1.000 14.34913 ? 437 VAL A CG2   1 
ATOM   3502 N  N     . LEU A 1 438 ? -2.86635  -29.34990 -13.79428 1.000 14.29711 ? 438 LEU A N     1 
ATOM   3503 C  CA    . LEU A 1 438 ? -2.31235  -30.61291 -14.26125 1.000 13.92619 ? 438 LEU A CA    1 
ATOM   3504 C  C     . LEU A 1 438 ? -1.40232  -31.27187 -13.23025 1.000 14.05249 ? 438 LEU A C     1 
ATOM   3505 O  O     . LEU A 1 438 ? -0.58632  -32.12688 -13.59124 1.000 16.27483 ? 438 LEU A O     1 
ATOM   3506 C  CB    . LEU A 1 438 ? -1.54638  -30.39594 -15.56827 1.000 11.34078 ? 438 LEU A CB    1 
ATOM   3507 C  CG    . LEU A 1 438 ? -2.35041  -30.01099 -16.80927 1.000 8.87620  ? 438 LEU A CG    1 
ATOM   3508 C  CD1   . LEU A 1 438 ? -1.45344  -29.33401 -17.82931 1.000 11.07834 ? 438 LEU A CD1   1 
ATOM   3509 C  CD2   . LEU A 1 438 ? -3.00241  -31.24101 -17.41321 1.000 10.56078 ? 438 LEU A CD2   1 
ATOM   3510 N  N     . LYS A 1 439 ? -1.52530  -30.89783 -11.95326 1.000 15.37850 ? 439 LYS A N     1 
ATOM   3511 C  CA    . LYS A 1 439 ? -0.59427  -31.40080 -10.94926 1.000 16.71223 ? 439 LYS A CA    1 
ATOM   3512 C  C     . LYS A 1 439 ? -0.81426  -32.87479 -10.62921 1.000 15.81005 ? 439 LYS A C     1 
ATOM   3513 O  O     . LYS A 1 439 ? 0.11176   -33.53277 -10.14421 1.000 18.70398 ? 439 LYS A O     1 
ATOM   3514 C  CB    . LYS A 1 439 ? -0.68325  -30.55976 -9.67228  1.000 15.43943 ? 439 LYS A CB    1 
ATOM   3515 C  CG    . LYS A 1 439 ? -1.62723  -31.08673 -8.59425  1.000 17.94139 ? 439 LYS A CG    1 
ATOM   3516 C  CD    . LYS A 1 439 ? -3.09024  -30.92876 -8.97422  0.000 16.57205 ? 439 LYS A CD    1 
ATOM   3517 C  CE    . LYS A 1 439 ? -3.96521  -30.82272 -7.73421  0.000 17.14844 ? 439 LYS A CE    1 
ATOM   3518 N  NZ    . LYS A 1 439 ? -3.61718  -31.84869 -6.71318  0.000 17.93729 ? 439 LYS A NZ    1 
ATOM   3519 N  N     . ASP A 1 440 ? -2.00526  -33.40781 -10.89417 1.000 14.95812 ? 440 ASP A N     1 
ATOM   3520 C  CA    . ASP A 1 440 ? -2.29324  -34.81980 -10.68012 1.000 16.27095 ? 440 ASP A CA    1 
ATOM   3521 C  C     . ASP A 1 440 ? -2.22826  -35.63584 -11.96310 1.000 14.26716 ? 440 ASP A C     1 
ATOM   3522 O  O     . ASP A 1 440 ? -2.50625  -36.83784 -11.92906 1.000 15.38264 ? 440 ASP A O     1 
ATOM   3523 C  CB    . ASP A 1 440 ? -3.67023  -34.98779 -10.03009 1.000 20.18282 ? 440 ASP A CB    1 
ATOM   3524 C  CG    . ASP A 1 440 ? -3.70920  -34.47175 -8.60510  1.000 19.84635 ? 440 ASP A CG    1 
ATOM   3525 O  OD1   . ASP A 1 440 ? -2.66318  -34.52172 -7.92412  1.000 17.42442 ? 440 ASP A OD1   1 
ATOM   3526 O  OD2   . ASP A 1 440 ? -4.78619  -34.01774 -8.16609  1.000 23.62536 ? 440 ASP A OD2   1 
ATOM   3527 N  N     . MET A 1 441 ? -1.87329  -35.01987 -13.08112 1.000 15.82860 ? 441 MET A N     1 
ATOM   3528 C  CA    . MET A 1 441 ? -1.78131  -35.73591 -14.34710 1.000 14.07535 ? 441 MET A CA    1 
ATOM   3529 C  C     . MET A 1 441 ? -0.51431  -36.58390 -14.37111 1.000 13.09523 ? 441 MET A C     1 
ATOM   3530 O  O     . MET A 1 441 ? 0.56770   -36.07588 -14.05914 1.000 12.44400 ? 441 MET A O     1 
ATOM   3531 C  CB    . MET A 1 441 ? -1.77934  -34.75494 -15.51513 1.000 15.52262 ? 441 MET A CB    1 
ATOM   3532 C  CG    . MET A 1 441 ? -1.74637  -35.40598 -16.89012 1.000 14.73584 ? 441 MET A CG    1 
ATOM   3533 S  SD    . MET A 1 441 ? -3.24537  -36.33301 -17.26406 1.000 16.07658 ? 441 MET A SD    1 
ATOM   3534 C  CE    . MET A 1 441 ? -4.49037  -35.06101 -17.07007 1.000 18.84242 ? 441 MET A CE    1 
ATOM   3535 N  N     . PRO A 1 442 ? -0.60730  -37.86791 -14.71606 1.000 16.45543 ? 442 PRO A N     1 
ATOM   3536 C  CA    . PRO A 1 442 ? 0.60070   -38.69590 -14.79907 1.000 17.50526 ? 442 PRO A CA    1 
ATOM   3537 C  C     . PRO A 1 442 ? 1.56968   -38.16393 -15.84310 1.000 14.64752 ? 442 PRO A C     1 
ATOM   3538 O  O     . PRO A 1 442 ? 1.17965   -37.49396 -16.80211 1.000 16.29695 ? 442 PRO A O     1 
ATOM   3539 C  CB    . PRO A 1 442 ? 0.05971   -40.07692 -15.18701 1.000 15.77768 ? 442 PRO A CB    1 
ATOM   3540 C  CG    . PRO A 1 442 ? -1.36029  -40.06892 -14.72198 1.000 17.10789 ? 442 PRO A CG    1 
ATOM   3541 C  CD    . PRO A 1 442 ? -1.83430  -38.65893 -14.91101 1.000 17.27546 ? 442 PRO A CD    1 
ATOM   3542 N  N     . ALA A 1 443 ? 2.85268   -38.47691 -15.64612 1.000 16.26984 ? 443 ALA A N     1 
ATOM   3543 C  CA    . ALA A 1 443 ? 3.89866   -37.95793 -16.52116 1.000 15.81156 ? 443 ALA A CA    1 
ATOM   3544 C  C     . ALA A 1 443 ? 3.79063   -38.48697 -17.94514 1.000 16.65770 ? 443 ALA A C     1 
ATOM   3545 O  O     . ALA A 1 443 ? 4.36161   -37.88400 -18.86017 1.000 18.81808 ? 443 ALA A O     1 
ATOM   3546 C  CB    . ALA A 1 443 ? 5.27668   -38.29190 -15.94918 1.000 16.81564 ? 443 ALA A CB    1 
ATOM   3547 N  N     . LYS A 1 444 ? 3.07664   -39.59499 -18.15409 1.000 14.02811 ? 444 LYS A N     1 
ATOM   3548 C  CA    . LYS A 1 444 ? 2.94361   -40.14803 -19.49707 1.000 17.33614 ? 444 LYS A CA    1 
ATOM   3549 C  C     . LYS A 1 444 ? 2.15959   -39.21806 -20.41508 1.000 17.93315 ? 444 LYS A C     1 
ATOM   3550 O  O     . LYS A 1 444 ? 2.40556   -39.19410 -21.62609 1.000 17.03621 ? 444 LYS A O     1 
ATOM   3551 C  CB    . LYS A 1 444 ? 2.28063   -41.52403 -19.42902 1.000 21.43411 ? 444 LYS A CB    1 
ATOM   3552 C  CG    . LYS A 1 444 ? 2.19260   -42.25607 -20.75899 1.000 18.49169 ? 444 LYS A CG    1 
ATOM   3553 C  CD    . LYS A 1 444 ? 1.64862   -43.66307 -20.56794 1.000 17.90231 ? 444 LYS A CD    1 
ATOM   3554 C  CE    . LYS A 1 444 ? 1.45560   -44.37411 -21.89691 0.000 20.26213 ? 444 LYS A CE    1 
ATOM   3555 N  NZ    . LYS A 1 444 ? 0.93061   -45.75511 -21.70986 0.000 20.86799 ? 444 LYS A NZ    1 
ATOM   3556 N  N     . TYR A 1 445 ? 1.22459   -38.44005 -19.86309 1.000 16.65132 ? 445 TYR A N     1 
ATOM   3557 C  CA    . TYR A 1 445 ? 0.38457   -37.55008 -20.65810 1.000 16.18307 ? 445 TYR A CA    1 
ATOM   3558 C  C     . TYR A 1 445 ? 0.46657   -36.10207 -20.18614 1.000 14.69362 ? 445 TYR A C     1 
ATOM   3559 O  O     . TYR A 1 445 ? -0.43444  -35.31008 -20.47515 1.000 14.33973 ? 445 TYR A O     1 
ATOM   3560 C  CB    . TYR A 1 445 ? -1.06843  -38.02509 -20.63305 1.000 18.49280 ? 445 TYR A CB    1 
ATOM   3561 C  CG    . TYR A 1 445 ? -1.22942  -39.52710 -20.66400 1.000 17.23371 ? 445 TYR A CG    1 
ATOM   3562 C  CD1   . TYR A 1 445 ? -1.18443  -40.22613 -21.86098 1.000 16.55243 ? 445 TYR A CD1   1 
ATOM   3563 C  CD2   . TYR A 1 445 ? -1.43638  -40.24406 -19.49298 1.000 17.86242 ? 445 TYR A CD2   1 
ATOM   3564 C  CE1   . TYR A 1 445 ? -1.33442  -41.59913 -21.89194 1.000 15.83071 ? 445 TYR A CE1   1 
ATOM   3565 C  CE2   . TYR A 1 445 ? -1.58637  -41.61606 -19.51293 1.000 18.76942 ? 445 TYR A CE2   1 
ATOM   3566 C  CZ    . TYR A 1 445 ? -1.53539  -42.28910 -20.71491 1.000 19.19462 ? 445 TYR A CZ    1 
ATOM   3567 O  OH    . TYR A 1 445 ? -1.68438  -43.65610 -20.74087 1.000 24.85215 ? 445 TYR A OH    1 
ATOM   3568 N  N     . ILE A 1 446 ? 1.52858   -35.73704 -19.46217 1.000 12.78614 ? 446 ILE A N     1 
ATOM   3569 C  CA    . ILE A 1 446 ? 1.62458   -34.37702 -18.94222 1.000 14.89195 ? 446 ILE A CA    1 
ATOM   3570 C  C     . ILE A 1 446 ? 1.87955   -33.38005 -20.06825 1.000 13.73949 ? 446 ILE A C     1 
ATOM   3571 O  O     . ILE A 1 446 ? 1.44754   -32.22305 -19.99128 1.000 15.30149 ? 446 ILE A O     1 
ATOM   3572 C  CB    . ILE A 1 446 ? 2.70760   -34.30098 -17.84624 1.000 16.76927 ? 446 ILE A CB    1 
ATOM   3573 C  CG1   . ILE A 1 446 ? 2.71061   -32.92396 -17.17528 1.000 12.99836 ? 446 ILE A CG1   1 
ATOM   3574 C  CG2   . ILE A 1 446 ? 4.08059   -34.63698 -18.40926 1.000 12.50827 ? 446 ILE A CG2   1 
ATOM   3575 C  CD1   . ILE A 1 446 ? 1.49062   -32.65694 -16.32327 1.000 15.14576 ? 446 ILE A CD1   1 
ATOM   3576 N  N     . TYR A 1 447 ? 2.56153   -33.80308 -21.13426 1.000 11.59683 ? 447 TYR A N     1 
ATOM   3577 C  CA    . TYR A 1 447 ? 2.79150   -32.93711 -22.28329 1.000 15.06758 ? 447 TYR A CA    1 
ATOM   3578 C  C     . TYR A 1 447 ? 1.71648   -33.07115 -23.35326 1.000 14.39600 ? 447 TYR A C     1 
ATOM   3579 O  O     . TYR A 1 447 ? 1.60645   -32.19118 -24.21428 1.000 10.41254 ? 447 TYR A O     1 
ATOM   3580 C  CB    . TYR A 1 447 ? 4.16249   -33.22312 -22.90331 1.000 14.76456 ? 447 TYR A CB    1 
ATOM   3581 C  CG    . TYR A 1 447 ? 5.32350   -32.75309 -22.05735 1.000 12.69641 ? 447 TYR A CG    1 
ATOM   3582 C  CD1   . TYR A 1 447 ? 5.78149   -31.44408 -22.13739 1.000 13.40405 ? 447 TYR A CD1   1 
ATOM   3583 C  CD2   . TYR A 1 447 ? 5.96353   -33.61705 -21.18133 1.000 13.68968 ? 447 TYR A CD2   1 
ATOM   3584 C  CE1   . TYR A 1 447 ? 6.84350   -31.01005 -21.36643 1.000 10.59249 ? 447 TYR A CE1   1 
ATOM   3585 C  CE2   . TYR A 1 447 ? 7.02454   -33.19302 -20.40537 1.000 13.32789 ? 447 TYR A CE2   1 
ATOM   3586 C  CZ    . TYR A 1 447 ? 7.46053   -31.88902 -20.50242 1.000 12.78358 ? 447 TYR A CZ    1 
ATOM   3587 O  OH    . TYR A 1 447 ? 8.51854   -31.46299 -19.73145 1.000 12.80499 ? 447 TYR A OH    1 
ATOM   3588 N  N     . GLU A 1 448 ? 0.93249   -34.14716 -23.32321 1.000 15.27696 ? 448 GLU A N     1 
ATOM   3589 C  CA    . GLU A 1 448 ? -0.18253  -34.34320 -24.24918 1.000 16.49134 ? 448 GLU A CA    1 
ATOM   3590 C  C     . GLU A 1 448 ? -1.37551  -34.85618 -23.45714 1.000 16.92086 ? 448 GLU A C     1 
ATOM   3591 O  O     . GLU A 1 448 ? -1.68250  -36.05418 -23.46510 1.000 19.41759 ? 448 GLU A O     1 
ATOM   3592 C  CB    . GLU A 1 448 ? 0.19445   -35.30823 -25.37716 1.000 18.91120 ? 448 GLU A CB    1 
ATOM   3593 C  CG    . GLU A 1 448 ? 1.59846   -35.88321 -25.26917 1.000 21.95870 ? 448 GLU A CG    1 
ATOM   3594 C  CD    . GLU A 1 448 ? 2.00344   -36.67225 -26.49916 1.000 22.66222 ? 448 GLU A CD    1 
ATOM   3595 O  OE1   . GLU A 1 448 ? 1.15042   -36.86628 -27.39113 1.000 30.31769 ? 448 GLU A OE1   1 
ATOM   3596 O  OE2   . GLU A 1 448 ? 3.17544   -37.09724 -26.57317 1.000 25.04411 ? 448 GLU A OE2   1 
ATOM   3597 N  N     . PRO A 1 449 ? -2.07950  -33.96417 -22.75415 1.000 16.13486 ? 449 PRO A N     1 
ATOM   3598 C  CA    . PRO A 1 449 ? -3.19048  -34.42215 -21.90511 1.000 17.12244 ? 449 PRO A CA    1 
ATOM   3599 C  C     . PRO A 1 449 ? -4.37049  -34.97118 -22.68707 1.000 15.14770 ? 449 PRO A C     1 
ATOM   3600 O  O     . PRO A 1 449 ? -5.12148  -35.79217 -22.14603 1.000 15.29892 ? 449 PRO A O     1 
ATOM   3601 C  CB    . PRO A 1 449 ? -3.57147  -33.16113 -21.11714 1.000 17.24191 ? 449 PRO A CB    1 
ATOM   3602 C  CG    . PRO A 1 449 ? -3.12450  -32.03115 -21.98219 1.000 12.18923 ? 449 PRO A CG    1 
ATOM   3603 C  CD    . PRO A 1 449 ? -1.87651  -32.50716 -22.67020 1.000 12.72584 ? 449 PRO A CD    1 
ATOM   3604 N  N     . TRP A 1 450 ? -4.56152  -34.54822 -23.93908 1.000 16.75063 ? 450 TRP A N     1 
ATOM   3605 C  CA    . TRP A 1 450 ? -5.67054  -35.06625 -24.73304 1.000 15.48309 ? 450 TRP A CA    1 
ATOM   3606 C  C     . TRP A 1 450 ? -5.49153  -36.53726 -25.08200 1.000 17.61524 ? 450 TRP A C     1 
ATOM   3607 O  O     . TRP A 1 450 ? -6.48453  -37.22128 -25.35396 1.000 15.86137 ? 450 TRP A O     1 
ATOM   3608 C  CB    . TRP A 1 450 ? -5.84157  -34.24029 -26.00906 1.000 17.57301 ? 450 TRP A CB    1 
ATOM   3609 C  CG    . TRP A 1 450 ? -4.66959  -34.31231 -26.93909 1.000 19.28763 ? 450 TRP A CG    1 
ATOM   3610 C  CD1   . TRP A 1 450 ? -4.51260  -35.16234 -27.99606 1.000 17.62304 ? 450 TRP A CD1   1 
ATOM   3611 C  CD2   . TRP A 1 450 ? -3.48959  -33.50130 -26.89714 1.000 15.04847 ? 450 TRP A CD2   1 
ATOM   3612 N  NE1   . TRP A 1 450 ? -3.30862  -34.93035 -28.61310 1.000 17.59174 ? 450 TRP A NE1   1 
ATOM   3613 C  CE2   . TRP A 1 450 ? -2.66061  -33.91633 -27.95814 1.000 16.90294 ? 450 TRP A CE2   1 
ATOM   3614 C  CE3   . TRP A 1 450 ? -3.05359  -32.46627 -26.06518 1.000 17.27485 ? 450 TRP A CE3   1 
ATOM   3615 C  CZ2   . TRP A 1 450 ? -1.42162  -33.33233 -28.20919 1.000 14.07503 ? 450 TRP A CZ2   1 
ATOM   3616 C  CZ3   . TRP A 1 450 ? -1.82159  -31.88627 -26.31622 1.000 16.33103 ? 450 TRP A CZ3   1 
ATOM   3617 C  CH2   . TRP A 1 450 ? -1.02061  -32.32030 -27.37922 1.000 15.61929 ? 450 TRP A CH2   1 
ATOM   3618 N  N     . THR A 1 451 ? -4.25553  -37.03725 -25.08101 1.000 15.37275 ? 451 THR A N     1 
ATOM   3619 C  CA    . THR A 1 451 ? -3.99852  -38.44726 -25.34498 1.000 17.41336 ? 451 THR A CA    1 
ATOM   3620 C  C     . THR A 1 451 ? -4.30449  -39.34022 -24.14994 1.000 17.34625 ? 451 THR A C     1 
ATOM   3621 O  O     . THR A 1 451 ? -4.39248  -40.56123 -24.31790 1.000 15.61565 ? 451 THR A O     1 
ATOM   3622 C  CB    . THR A 1 451 ? -2.54053  -38.65126 -25.76600 1.000 16.45830 ? 451 THR A CB    1 
ATOM   3623 O  OG1   . THR A 1 451 ? -1.67251  -38.23122 -24.70503 1.000 15.92316 ? 451 THR A OG1   1 
ATOM   3624 C  CG2   . THR A 1 451 ? -2.22856  -37.84230 -27.01703 1.000 19.31264 ? 451 THR A CG2   1 
ATOM   3625 N  N     . ALA A 1 452 ? -4.46247  -38.76819 -22.96096 1.000 17.01429 ? 452 ALA A N     1 
ATOM   3626 C  CA    . ALA A 1 452 ? -4.76944  -39.57116 -21.78793 1.000 17.53046 ? 452 ALA A CA    1 
ATOM   3627 C  C     . ALA A 1 452 ? -6.19044  -40.12017 -21.88588 1.000 17.02532 ? 452 ALA A C     1 
ATOM   3628 O  O     . ALA A 1 452 ? -7.08445  -39.44319 -22.40488 1.000 17.21485 ? 452 ALA A O     1 
ATOM   3629 C  CB    . ALA A 1 452 ? -4.61842  -38.74112 -20.51495 1.000 16.41786 ? 452 ALA A CB    1 
ATOM   3630 N  N     . PRO A 1 453 ? -6.42842  -41.34116 -21.40884 1.000 18.69046 ? 453 PRO A N     1 
ATOM   3631 C  CA    . PRO A 1 453 ? -7.79341  -41.87717 -21.40579 1.000 21.56617 ? 453 PRO A CA    1 
ATOM   3632 C  C     . PRO A 1 453 ? -8.71240  -41.03915 -20.52880 1.000 19.62195 ? 453 PRO A C     1 
ATOM   3633 O  O     . PRO A 1 453 ? -8.27739  -40.33212 -19.61883 1.000 18.19251 ? 453 PRO A O     1 
ATOM   3634 C  CB    . PRO A 1 453 ? -7.62139  -43.29415 -20.84075 1.000 20.00469 ? 453 PRO A CB    1 
ATOM   3635 C  CG    . PRO A 1 453 ? -6.17939  -43.62715 -21.07377 1.000 20.68806 ? 453 PRO A CG    1 
ATOM   3636 C  CD    . PRO A 1 453 ? -5.44440  -42.32814 -20.93383 1.000 18.59504 ? 453 PRO A CD    1 
ATOM   3637 N  N     . LEU A 1 454 ? -10.01241 -41.12917 -20.82177 1.000 21.50552 ? 454 LEU A N     1 
ATOM   3638 C  CA    . LEU A 1 454 ? -10.99040 -40.34315 -20.07677 1.000 18.49407 ? 454 LEU A CA    1 
ATOM   3639 C  C     . LEU A 1 454 ? -11.02136 -40.73211 -18.60376 1.000 21.40032 ? 454 LEU A C     1 
ATOM   3640 O  O     . LEU A 1 454 ? -11.30435 -39.88809 -17.74578 1.000 23.19358 ? 454 LEU A O     1 
ATOM   3641 C  CB    . LEU A 1 454 ? -12.37741 -40.50418 -20.70074 1.000 24.08734 ? 454 LEU A CB    1 
ATOM   3642 C  CG    . LEU A 1 454 ? -13.47140 -39.57218 -20.17574 1.000 20.97408 ? 454 LEU A CG    1 
ATOM   3643 C  CD1   . LEU A 1 454 ? -13.10142 -38.11818 -20.42279 1.000 23.84229 ? 454 LEU A CD1   1 
ATOM   3644 C  CD2   . LEU A 1 454 ? -14.81042 -39.90121 -20.81470 1.000 26.14220 ? 454 LEU A CD2   1 
ATOM   3645 N  N     . GLU A 1 455 ? -10.72735 -41.99710 -18.29073 1.000 21.09170 ? 455 GLU A N     1 
ATOM   3646 C  CA    . GLU A 1 455 ? -10.67831 -42.41906 -16.89571 1.000 18.14969 ? 455 GLU A CA    1 
ATOM   3647 C  C     . GLU A 1 455 ? -9.52430  -41.76202 -16.14876 1.000 19.36582 ? 455 GLU A C     1 
ATOM   3648 O  O     . GLU A 1 455 ? -9.64628  -41.47699 -14.95276 1.000 19.27276 ? 455 GLU A O     1 
ATOM   3649 C  CB    . GLU A 1 455 ? -10.56530 -43.94105 -16.80867 1.000 19.74733 ? 455 GLU A CB    1 
ATOM   3650 C  CG    . GLU A 1 455 ? -11.75231 -44.69008 -17.39362 0.000 20.78741 ? 455 GLU A CG    1 
ATOM   3651 C  CD    . GLU A 1 455 ? -11.58229 -46.19508 -17.31958 0.000 20.57039 ? 455 GLU A CD    1 
ATOM   3652 O  OE1   . GLU A 1 455 ? -10.46028 -46.65406 -17.01859 0.000 20.03642 ? 455 GLU A OE1   1 
ATOM   3653 O  OE2   . GLU A 1 455 ? -12.57029 -46.91909 -17.56154 0.000 20.98804 ? 455 GLU A OE2   1 
ATOM   3654 N  N     . VAL A 1 456 ? -8.40532  -41.51404 -16.83079 1.000 22.09024 ? 456 VAL A N     1 
ATOM   3655 C  CA    . VAL A 1 456 ? -7.26531  -40.87501 -16.18383 1.000 20.44190 ? 456 VAL A CA    1 
ATOM   3656 C  C     . VAL A 1 456 ? -7.48532  -39.37200 -16.06287 1.000 19.49418 ? 456 VAL A C     1 
ATOM   3657 O  O     . VAL A 1 456 ? -7.11030  -38.75897 -15.05690 1.000 18.37218 ? 456 VAL A O     1 
ATOM   3658 C  CB    . VAL A 1 456 ? -5.97032  -41.20202 -16.94985 1.000 20.08369 ? 456 VAL A CB    1 
ATOM   3659 C  CG1   . VAL A 1 456 ? -4.76631  -40.57799 -16.25789 1.000 23.34212 ? 456 VAL A CG1   1 
ATOM   3660 C  CG2   . VAL A 1 456 ? -5.79831  -42.70802 -17.07581 1.000 18.59289 ? 456 VAL A CG2   1 
ATOM   3661 N  N     . GLN A 1 457 ? -8.09535  -38.75704 -17.07988 1.000 15.23023 ? 457 GLN A N     1 
ATOM   3662 C  CA    . GLN A 1 457 ? -8.39536  -37.33104 -17.01292 1.000 17.50548 ? 457 GLN A CA    1 
ATOM   3663 C  C     . GLN A 1 457 ? -9.34533  -37.02301 -15.86191 1.000 19.02856 ? 457 GLN A C     1 
ATOM   3664 O  O     . GLN A 1 457 ? -9.19133  -36.00799 -15.17294 1.000 19.00783 ? 457 GLN A O     1 
ATOM   3665 C  CB    . GLN A 1 457 ? -8.99139  -36.85309 -18.33792 1.000 16.54954 ? 457 GLN A CB    1 
ATOM   3666 C  CG    . GLN A 1 457 ? -8.08241  -37.04512 -19.54193 1.000 16.56824 ? 457 GLN A CG    1 
ATOM   3667 C  CD    . GLN A 1 457 ? -8.71744  -36.56616 -20.83593 1.000 15.92198 ? 457 GLN A CD    1 
ATOM   3668 O  OE1   . GLN A 1 457 ? -8.16646  -36.76019 -21.91894 1.000 16.55765 ? 457 GLN A OE1   1 
ATOM   3669 N  NE2   . GLN A 1 457 ? -9.88044  -35.93617 -20.72693 1.000 17.10842 ? 457 GLN A NE2   1 
ATOM   3670 N  N     . ARG A 1 458 ? -10.33558 -37.88979 -15.63596 1.000 21.80007 ? 458 ARG A N     1 
ATOM   3671 C  CA    . ARG A 1 458 ? -11.25891 -37.67717 -14.52557 1.000 18.79017 ? 458 ARG A CA    1 
ATOM   3672 C  C     . ARG A 1 458 ? -10.59803 -37.98560 -13.18820 1.000 18.85077 ? 458 ARG A C     1 
ATOM   3673 O  O     . ARG A 1 458 ? -10.87832 -37.32084 -12.18379 1.000 20.37447 ? 458 ARG A O     1 
ATOM   3674 C  CB    . ARG A 1 458 ? -12.51367 -38.52982 -14.71025 1.000 19.92850 ? 458 ARG A CB    1 
ATOM   3675 C  CG    . ARG A 1 458 ? -13.41968 -38.07032 -15.83835 1.000 18.54376 ? 458 ARG A CG    1 
ATOM   3676 C  CD    . ARG A 1 458 ? -14.72218 -38.85037 -15.83986 0.000 19.71844 ? 458 ARG A CD    1 
ATOM   3677 N  NE    . ARG A 1 458 ? -15.36818 -38.82195 -14.53304 0.000 19.41103 ? 458 ARG A NE    1 
ATOM   3678 C  CZ    . ARG A 1 458 ? -16.16334 -37.84845 -14.11093 0.000 19.42070 ? 458 ARG A CZ    1 
ATOM   3679 N  NH1   . ARG A 1 458 ? -16.43371 -36.79881 -14.86968 0.000 19.77306 ? 458 ARG A NH1   1 
ATOM   3680 N  NH2   . ARG A 1 458 ? -16.69905 -37.92902 -12.89617 0.000 19.34104 ? 458 ARG A NH2   1 
ATOM   3681 N  N     . LYS A 1 459 ? -9.71926  -38.98993 -13.15284 1.000 22.31058 ? 459 LYS A N     1 
ATOM   3682 C  CA    . LYS A 1 459 ? -9.05523  -39.35089 -11.90684 1.000 19.56356 ? 459 LYS A CA    1 
ATOM   3683 C  C     . LYS A 1 459 ? -8.05223  -38.29487 -11.46389 1.000 20.06046 ? 459 LYS A C     1 
ATOM   3684 O  O     . LYS A 1 459 ? -7.71821  -38.23283 -10.27590 1.000 23.02708 ? 459 LYS A O     1 
ATOM   3685 C  CB    . LYS A 1 459 ? -8.36622  -40.70789 -12.05981 1.000 22.57685 ? 459 LYS A CB    1 
ATOM   3686 C  CG    . LYS A 1 459 ? -8.14619  -41.44585 -10.75180 0.000 22.10566 ? 459 LYS A CG    1 
ATOM   3687 C  CD    . LYS A 1 459 ? -7.85718  -42.92385 -10.98076 0.000 23.14742 ? 459 LYS A CD    1 
ATOM   3688 C  CE    . LYS A 1 459 ? -9.01019  -43.62688 -11.69171 0.000 23.29101 ? 459 LYS A CE    1 
ATOM   3689 N  NZ    . LYS A 1 459 ? -8.82922  -43.67893 -13.17171 0.000 22.29205 ? 459 LYS A NZ    1 
ATOM   3690 N  N     . ALA A 1 460 ? -7.56926  -37.46489 -12.38493 1.000 17.60335 ? 460 ALA A N     1 
ATOM   3691 C  CA    . ALA A 1 460 ? -6.65326  -36.38088 -12.06698 1.000 18.84132 ? 460 ALA A CA    1 
ATOM   3692 C  C     . ALA A 1 460 ? -7.35826  -35.04188 -11.90301 1.000 19.75311 ? 460 ALA A C     1 
ATOM   3693 O  O     . ALA A 1 460 ? -6.69327  -34.03386 -11.64105 1.000 16.57317 ? 460 ALA A O     1 
ATOM   3694 C  CB    . ALA A 1 460 ? -5.57228  -36.26590 -13.14601 1.000 15.66102 ? 460 ALA A CB    1 
ATOM   3695 N  N     . GLY A 1 461 ? -8.68027  -35.00689 -12.04998 1.000 18.65943 ? 461 GLY A N     1 
ATOM   3696 C  CA    . GLY A 1 461 ? -9.41628  -33.76389 -11.91900 1.000 20.14586 ? 461 GLY A CA    1 
ATOM   3697 C  C     . GLY A 1 461 ? -9.17431  -32.77493 -13.03604 1.000 19.90488 ? 461 GLY A C     1 
ATOM   3698 O  O     . GLY A 1 461 ? -9.34531  -31.56892 -12.83407 1.000 18.87220 ? 461 GLY A O     1 
ATOM   3699 N  N     . CYS A 1 462 ? -8.78033  -33.25296 -14.21703 1.000 21.83907 ? 462 CYS A N     1 
ATOM   3700 C  CA    . CYS A 1 462 ? -8.48036  -32.38399 -15.36006 1.000 18.62606 ? 462 CYS A CA    1 
ATOM   3701 C  C     . CYS A 1 462 ? -8.98138  -33.07703 -16.62603 1.000 17.62513 ? 462 CYS A C     1 
ATOM   3702 O  O     . CYS A 1 462 ? -8.24739  -33.83805 -17.26303 1.000 16.44158 ? 462 CYS A O     1 
ATOM   3703 C  CB    . CYS A 1 462 ? -6.99236  -32.07198 -15.43711 1.000 17.08940 ? 462 CYS A CB    1 
ATOM   3704 S  SG    . CYS A 1 462 ? -6.51440  -31.09402 -16.87815 1.000 17.57675 ? 462 CYS A SG    1 
ATOM   3705 N  N     . VAL A 1 463 ? -10.23239 -32.80905 -16.98201 1.000 19.50306 ? 463 VAL A N     1 
ATOM   3706 C  CA    . VAL A 1 463 ? -10.82841 -33.34210 -18.20199 1.000 18.00426 ? 463 VAL A CA    1 
ATOM   3707 C  C     . VAL A 1 463 ? -10.52044 -32.38113 -19.34202 1.000 16.36673 ? 463 VAL A C     1 
ATOM   3708 O  O     . VAL A 1 463 ? -10.82045 -31.18613 -19.25605 1.000 16.89596 ? 463 VAL A O     1 
ATOM   3709 C  CB    . VAL A 1 463 ? -12.34241 -33.54410 -18.04195 1.000 18.68785 ? 463 VAL A CB    1 
ATOM   3710 C  CG1   . VAL A 1 463 ? -12.95743 -34.01115 -19.35392 1.000 21.97108 ? 463 VAL A CG1   1 
ATOM   3711 C  CG2   . VAL A 1 463 ? -12.63038 -34.53807 -16.92991 1.000 20.62262 ? 463 VAL A CG2   1 
ATOM   3712 N  N     . VAL A 1 464 ? -9.91646  -32.90116 -20.41002 1.000 16.46594 ? 464 VAL A N     1 
ATOM   3713 C  CA    . VAL A 1 464 ? -9.57949  -32.07519 -21.56405 1.000 15.19007 ? 464 VAL A CA    1 
ATOM   3714 C  C     . VAL A 1 464 ? -10.86751 -31.59222 -22.21904 1.000 17.37119 ? 464 VAL A C     1 
ATOM   3715 O  O     . VAL A 1 464 ? -11.71751 -32.39624 -22.61900 1.000 18.83610 ? 464 VAL A O     1 
ATOM   3716 C  CB    . VAL A 1 464 ? -8.70251  -32.84921 -22.55705 1.000 17.49291 ? 464 VAL A CB    1 
ATOM   3717 C  CG1   . VAL A 1 464 ? -8.42554  -32.00025 -23.78908 1.000 15.87270 ? 464 VAL A CG1   1 
ATOM   3718 C  CG2   . VAL A 1 464 ? -7.40349  -33.27318 -21.89306 1.000 15.35965 ? 464 VAL A CG2   1 
ATOM   3719 N  N     . GLY A 1 465 ? -11.01652 -30.27422 -22.33007 1.000 20.74522 ? 465 GLY A N     1 
ATOM   3720 C  CA    . GLY A 1 465 ? -12.21954 -29.66825 -22.85807 1.000 17.36776 ? 465 GLY A CA    1 
ATOM   3721 C  C     . GLY A 1 465 ? -13.11152 -29.03122 -21.81507 1.000 15.99169 ? 465 GLY A C     1 
ATOM   3722 O  O     . GLY A 1 465 ? -14.03154 -28.28624 -22.18107 1.000 14.77793 ? 465 GLY A O     1 
ATOM   3723 N  N     . ARG A 1 466 ? -12.87233 -29.30095 -20.53258 1.000 16.13320 ? 466 ARG A N     1 
ATOM   3724 C  CA    . ARG A 1 466 ? -13.63463 -28.71377 -19.43829 1.000 17.93674 ? 466 ARG A CA    1 
ATOM   3725 C  C     . ARG A 1 466 ? -12.74721 -27.98520 -18.44193 1.000 18.61328 ? 466 ARG A C     1 
ATOM   3726 O  O     . ARG A 1 466 ? -13.04166 -26.84025 -18.07768 1.000 18.00532 ? 466 ARG A O     1 
ATOM   3727 C  CB    . ARG A 1 466 ? -14.44582 -29.80109 -18.71574 1.000 18.45655 ? 466 ARG A CB    1 
ATOM   3728 C  CG    . ARG A 1 466 ? -15.35611 -29.26717 -17.62301 1.000 19.89004 ? 466 ARG A CG    1 
ATOM   3729 C  CD    . ARG A 1 466 ? -15.77773 -30.36957 -16.66783 1.000 24.34351 ? 466 ARG A CD    1 
ATOM   3730 N  NE    . ARG A 1 466 ? -14.63645 -30.92587 -15.95119 1.000 23.06956 ? 466 ARG A NE    1 
ATOM   3731 C  CZ    . ARG A 1 466 ? -14.72517 -31.83440 -14.98966 1.000 28.83747 ? 466 ARG A CZ    1 
ATOM   3732 N  NH1   . ARG A 1 466 ? -15.89403 -32.31524 -14.59839 1.000 28.29003 ? 466 ARG A NH1   1 
ATOM   3733 N  NH2   . ARG A 1 466 ? -13.61324 -32.26970 -14.40411 1.000 30.18834 ? 466 ARG A NH2   1 
ATOM   3734 N  N     . ASP A 1 467 ? -11.66644 -28.61910 -17.98711 1.000 17.04290 ? 467 ASP A N     1 
ATOM   3735 C  CA    . ASP A 1 467 ? -10.73443 -27.99806 -17.05415 1.000 15.92807 ? 467 ASP A CA    1 
ATOM   3736 C  C     . ASP A 1 467 ? -9.49145  -27.44307 -17.73119 1.000 16.26886 ? 467 ASP A C     1 
ATOM   3737 O  O     . ASP A 1 467 ? -8.95345  -26.43005 -17.27523 1.000 12.29243 ? 467 ASP A O     1 
ATOM   3738 C  CB    . ASP A 1 467 ? -10.30940 -29.00402 -15.97813 1.000 16.07458 ? 467 ASP A CB    1 
ATOM   3739 C  CG    . ASP A 1 467 ? -11.49038 -29.56701 -15.21109 1.000 16.36955 ? 467 ASP A CG    1 
ATOM   3740 O  OD1   . ASP A 1 467 ? -12.37538 -28.77601 -14.82109 1.000 11.38691 ? 467 ASP A OD1   1 
ATOM   3741 O  OD2   . ASP A 1 467 ? -11.54136 -30.79800 -15.00705 1.000 19.14007 ? 467 ASP A OD2   1 
ATOM   3742 N  N     . TYR A 1 468 ? -9.02247  -28.08410 -18.80118 1.000 13.69181 ? 468 TYR A N     1 
ATOM   3743 C  CA    . TYR A 1 468 ? -7.89549  -27.59711 -19.58022 1.000 14.79817 ? 468 TYR A CA    1 
ATOM   3744 C  C     . TYR A 1 468 ? -8.27352  -27.66616 -21.05421 1.000 13.75951 ? 468 TYR A C     1 
ATOM   3745 O  O     . TYR A 1 468 ? -8.82152  -28.68818 -21.50517 1.000 14.06739 ? 468 TYR A O     1 
ATOM   3746 C  CB    . TYR A 1 468 ? -6.62647  -28.41510 -19.30322 1.000 14.06900 ? 468 TYR A CB    1 
ATOM   3747 C  CG    . TYR A 1 468 ? -5.39649  -27.88711 -20.00227 1.000 12.35566 ? 468 TYR A CG    1 
ATOM   3748 C  CD1   . TYR A 1 468 ? -4.72749  -26.76809 -19.52031 1.000 10.26588 ? 468 TYR A CD1   1 
ATOM   3749 C  CD2   . TYR A 1 468 ? -4.90351  -28.50614 -21.14126 1.000 11.30057 ? 468 TYR A CD2   1 
ATOM   3750 C  CE1   . TYR A 1 468 ? -3.60351  -26.28110 -20.15835 1.000 10.73352 ? 468 TYR A CE1   1 
ATOM   3751 C  CE2   . TYR A 1 468 ? -3.78053  -28.02615 -21.78430 1.000 10.35841 ? 468 TYR A CE2   1 
ATOM   3752 C  CZ    . TYR A 1 468 ? -3.13453  -26.91413 -21.28834 1.000 8.44102  ? 468 TYR A CZ    1 
ATOM   3753 O  OH    . TYR A 1 468 ? -2.01555  -26.43414 -21.92738 1.000 8.49836  ? 468 TYR A OH    1 
ATOM   3754 N  N     . PRO A 1 469 ? -8.01354  -26.61918 -21.83325 1.000 12.97147 ? 469 PRO A N     1 
ATOM   3755 C  CA    . PRO A 1 469 ? -8.48157  -26.59423 -23.22224 1.000 13.92072 ? 469 PRO A CA    1 
ATOM   3756 C  C     . PRO A 1 469 ? -7.74658  -27.59825 -24.09822 1.000 13.56925 ? 469 PRO A C     1 
ATOM   3757 O  O     . PRO A 1 469 ? -6.62157  -28.01623 -23.82024 1.000 11.01341 ? 469 PRO A O     1 
ATOM   3758 C  CB    . PRO A 1 469 ? -8.19359  -25.15724 -23.66829 1.000 12.85162 ? 469 PRO A CB    1 
ATOM   3759 C  CG    . PRO A 1 469 ? -7.07358  -24.71421 -22.78833 1.000 13.37141 ? 469 PRO A CG    1 
ATOM   3760 C  CD    . PRO A 1 469 ? -7.31254  -25.37817 -21.46230 1.000 12.89067 ? 469 PRO A CD    1 
ATOM   3761 N  N     . ALA A 1 470 ? -8.42060  -27.98429 -25.17920 1.000 13.11622 ? 470 ALA A N     1 
ATOM   3762 C  CA    . ALA A 1 470 ? -7.83062  -28.86231 -26.17018 1.000 12.22229 ? 470 ALA A CA    1 
ATOM   3763 C  C     . ALA A 1 470 ? -6.80264  -28.09733 -27.00123 1.000 11.36370 ? 470 ALA A C     1 
ATOM   3764 O  O     . ALA A 1 470 ? -6.84665  -26.86733 -27.07527 1.000 9.55445  ? 470 ALA A O     1 
ATOM   3765 C  CB    . ALA A 1 470 ? -8.91963  -29.44435 -27.07114 1.000 12.65911 ? 470 ALA A CB    1 
ATOM   3766 N  N     . PRO A 1 471 ? -5.85565  -28.80134 -27.62223 1.000 11.16394 ? 471 PRO A N     1 
ATOM   3767 C  CA    . PRO A 1 471 ? -4.87767  -28.11536 -28.47727 1.000 10.65215 ? 471 PRO A CA    1 
ATOM   3768 C  C     . PRO A 1 471 ? -5.56470  -27.39740 -29.63028 1.000 11.30928 ? 471 PRO A C     1 
ATOM   3769 O  O     . PRO A 1 471 ? -6.40971  -27.96543 -30.32624 1.000 11.74038 ? 471 PRO A O     1 
ATOM   3770 C  CB    . PRO A 1 471 ? -3.97367  -29.25337 -28.96925 1.000 11.43792 ? 471 PRO A CB    1 
ATOM   3771 C  CG    . PRO A 1 471 ? -4.77866  -30.49737 -28.77820 1.000 13.87363 ? 471 PRO A CG    1 
ATOM   3772 C  CD    . PRO A 1 471 ? -5.59463  -30.24934 -27.55019 1.000 14.41580 ? 471 PRO A CD    1 
ATOM   3773 N  N     . ILE A 1 472 ? -5.19571  -26.12840 -29.82332 1.000 11.80707 ? 472 ILE A N     1 
ATOM   3774 C  CA    . ILE A 1 472 ? -5.84474  -25.32144 -30.85133 1.000 12.28038 ? 472 ILE A CA    1 
ATOM   3775 C  C     . ILE A 1 472 ? -5.45677  -25.79548 -32.24433 1.000 13.67917 ? 472 ILE A C     1 
ATOM   3776 O  O     . ILE A 1 472 ? -6.22079  -25.62051 -33.20132 1.000 15.49592 ? 472 ILE A O     1 
ATOM   3777 C  CB    . ILE A 1 472 ? -5.51375  -23.83043 -30.65139 1.000 12.13475 ? 472 ILE A CB    1 
ATOM   3778 C  CG1   . ILE A 1 472 ? -3.99875  -23.62042 -30.59342 1.000 10.28842 ? 472 ILE A CG1   1 
ATOM   3779 C  CG2   . ILE A 1 472 ? -6.18273  -23.30040 -29.39139 1.000 10.36681 ? 472 ILE A CG2   1 
ATOM   3780 C  CD1   . ILE A 1 472 ? -3.58976  -22.17341 -30.44148 1.000 13.07180 ? 472 ILE A CD1   1 
ATOM   3781 N  N     . VAL A 1 473 ? -4.27677  -26.39847 -32.39033 1.000 13.84538 ? 473 VAL A N     1 
ATOM   3782 C  CA    . VAL A 1 473 ? -3.79679  -26.87551 -33.67933 1.000 13.30812 ? 473 VAL A CA    1 
ATOM   3783 C  C     . VAL A 1 473 ? -3.10078  -28.21550 -33.49230 1.000 13.83242 ? 473 VAL A C     1 
ATOM   3784 O  O     . VAL A 1 473 ? -2.56075  -28.51446 -32.42331 1.000 16.01037 ? 473 VAL A O     1 
ATOM   3785 C  CB    . VAL A 1 473 ? -2.83581  -25.86752 -34.35338 1.000 14.15156 ? 473 VAL A CB    1 
ATOM   3786 C  CG1   . VAL A 1 473 ? -3.58583  -24.62854 -34.81840 1.000 14.68777 ? 473 VAL A CG1   1 
ATOM   3787 C  CG2   . VAL A 1 473 ? -1.70980  -25.49148 -33.39942 1.000 14.28555 ? 473 VAL A CG2   1 
ATOM   3788 N  N     . ASP A 1 474 ? -3.12479  -29.02853 -34.54528 1.000 15.37851 ? 474 ASP A N     1 
ATOM   3789 C  CA    . ASP A 1 474 ? -2.27878  -30.21153 -34.61626 1.000 16.44902 ? 474 ASP A CA    1 
ATOM   3790 C  C     . ASP A 1 474 ? -0.90080  -29.78153 -35.10330 1.000 15.54508 ? 474 ASP A C     1 
ATOM   3791 O  O     . ASP A 1 474 ? -0.77882  -29.17656 -36.17332 1.000 15.44601 ? 474 ASP A O     1 
ATOM   3792 C  CB    . ASP A 1 474 ? -2.88680  -31.25756 -35.54922 1.000 15.42555 ? 474 ASP A CB    1 
ATOM   3793 C  CG    . ASP A 1 474 ? -2.06879  -32.53455 -35.61120 1.000 19.48988 ? 474 ASP A CG    1 
ATOM   3794 O  OD1   . ASP A 1 474 ? -1.19677  -32.73152 -34.73821 1.000 26.06894 ? 474 ASP A OD1   1 
ATOM   3795 O  OD2   . ASP A 1 474 ? -2.29580  -33.34158 -36.53717 1.000 19.86402 ? 474 ASP A OD2   1 
ATOM   3796 N  N     . HIS A 1 475 ? 0.13422   -30.08650 -34.31632 1.000 16.67997 ? 475 HIS A N     1 
ATOM   3797 C  CA    . HIS A 1 475 ? 1.46421   -29.56350 -34.61436 1.000 14.12790 ? 475 HIS A CA    1 
ATOM   3798 C  C     . HIS A 1 475 ? 1.97219   -30.05453 -35.96436 1.000 14.07987 ? 475 HIS A C     1 
ATOM   3799 O  O     . HIS A 1 475 ? 2.60016   -29.29555 -36.70939 1.000 14.65133 ? 475 HIS A O     1 
ATOM   3800 C  CB    . HIS A 1 475 ? 2.44324   -29.94446 -33.50537 1.000 13.66389 ? 475 HIS A CB    1 
ATOM   3801 C  CG    . HIS A 1 475 ? 3.82723   -29.41845 -33.72341 1.000 13.25708 ? 475 HIS A CG    1 
ATOM   3802 N  ND1   . HIS A 1 475 ? 4.08921   -28.08346 -33.94446 1.000 13.60248 ? 475 HIS A ND1   1 
ATOM   3803 C  CD2   . HIS A 1 475 ? 5.02623   -30.04844 -33.76442 1.000 12.34629 ? 475 HIS A CD2   1 
ATOM   3804 C  CE1   . HIS A 1 475 ? 5.38921   -27.91245 -34.10649 1.000 12.58600 ? 475 HIS A CE1   1 
ATOM   3805 N  NE2   . HIS A 1 475 ? 5.98122   -29.08944 -34.00147 1.000 12.88715 ? 475 HIS A NE2   1 
ATOM   3806 N  N     . ALA A 1 476 ? 1.71019   -31.32055 -36.29631 1.000 14.87323 ? 476 ALA A N     1 
ATOM   3807 C  CA    . ALA A 1 476 ? 2.18717   -31.86058 -37.56731 1.000 13.52856 ? 476 ALA A CA    1 
ATOM   3808 C  C     . ALA A 1 476 ? 1.55214   -31.13662 -38.74831 1.000 14.62291 ? 476 ALA A C     1 
ATOM   3809 O  O     . ALA A 1 476 ? 2.23911   -30.79465 -39.71934 1.000 14.75042 ? 476 ALA A O     1 
ATOM   3810 C  CB    . ALA A 1 476 ? 1.90418   -33.36058 -37.64025 1.000 16.13016 ? 476 ALA A CB    1 
ATOM   3811 N  N     . VAL A 1 477 ? 0.24314   -30.88963 -38.68129 1.000 15.93360 ? 477 VAL A N     1 
ATOM   3812 C  CA    . VAL A 1 477 ? -0.43889  -30.18167 -39.76130 1.000 14.89652 ? 477 VAL A CA    1 
ATOM   3813 C  C     . VAL A 1 477 ? -0.01691  -28.71767 -39.79335 1.000 15.41891 ? 477 VAL A C     1 
ATOM   3814 O  O     . VAL A 1 477 ? 0.16707   -28.13270 -40.86838 1.000 14.76178 ? 477 VAL A O     1 
ATOM   3815 C  CB    . VAL A 1 477 ? -1.96389  -30.33067 -39.61026 1.000 15.90528 ? 477 VAL A CB    1 
ATOM   3816 C  CG1   . VAL A 1 477 ? -2.69092  -29.47171 -40.63528 0.399 16.08385 ? 477 VAL A CG1   1 
ATOM   3817 C  CG2   . VAL A 1 477 ? -2.36988  -31.79068 -39.74421 1.000 14.76749 ? 477 VAL A CG2   1 
ATOM   3818 N  N     . ALA A 1 478 ? 0.15111   -28.10363 -38.62038 1.000 17.09122 ? 478 ALA A N     1 
ATOM   3819 C  CA    . ALA A 1 478 ? 0.46810   -26.68162 -38.56543 1.000 15.02503 ? 478 ALA A CA    1 
ATOM   3820 C  C     . ALA A 1 478 ? 1.92510   -26.40662 -38.92247 1.000 16.15460 ? 478 ALA A C     1 
ATOM   3821 O  O     . ALA A 1 478 ? 2.21807   -25.43464 -39.62650 1.000 15.82521 ? 478 ALA A O     1 
ATOM   3822 C  CB    . ALA A 1 478 ? 0.14613   -26.12558 -37.17844 1.000 14.42333 ? 478 ALA A CB    1 
ATOM   3823 N  N     . SER A 1 479 ? 2.85111   -27.24660 -38.45046 1.000 14.54842 ? 479 SER A N     1 
ATOM   3824 C  CA    . SER A 1 479 ? 4.26510   -27.00260 -38.71850 1.000 14.65019 ? 479 SER A CA    1 
ATOM   3825 C  C     . SER A 1 479 ? 4.59107   -27.18664 -40.19550 1.000 17.25893 ? 479 SER A C     1 
ATOM   3826 O  O     . SER A 1 479 ? 5.31906   -26.37665 -40.77954 1.000 16.59962 ? 479 SER A O     1 
ATOM   3827 C  CB    . SER A 1 479 ? 5.13613   -27.91857 -37.85849 1.000 14.14316 ? 479 SER A CB    1 
ATOM   3828 O  OG    . SER A 1 479 ? 4.86413   -29.28358 -38.12744 1.000 16.98940 ? 479 SER A OG    1 
ATOM   3829 N  N     . LYS A 1 480 ? 4.06207   -28.24366 -40.81646 1.000 17.26482 ? 480 LYS A N     1 
ATOM   3830 C  CA    . LYS A 1 480 ? 4.31204   -28.46070 -42.23645 1.000 19.55295 ? 480 LYS A CA    1 
ATOM   3831 C  C     . LYS A 1 480 ? 3.69701   -27.35574 -43.08647 1.000 17.58787 ? 480 LYS A C     1 
ATOM   3832 O  O     . LYS A 1 480 ? 4.21899   -27.03676 -44.16150 1.000 17.22108 ? 480 LYS A O     1 
ATOM   3833 C  CB    . LYS A 1 480 ? 3.77704   -29.82972 -42.66040 1.000 15.22438 ? 480 LYS A CB    1 
ATOM   3834 C  CG    . LYS A 1 480 ? 4.09502   -30.20276 -44.09940 1.000 18.58921 ? 480 LYS A CG    1 
ATOM   3835 C  CD    . LYS A 1 480 ? 3.99302   -31.70177 -44.31635 0.000 17.81284 ? 480 LYS A CD    1 
ATOM   3836 C  CE    . LYS A 1 480 ? 5.01805   -32.44674 -43.47535 0.000 17.82928 ? 480 LYS A CE    1 
ATOM   3837 N  NZ    . LYS A 1 480 ? 5.05605   -33.89975 -43.79330 0.000 18.03571 ? 480 LYS A NZ    1 
ATOM   3838 N  N     . ALA A 1 481 ? 2.60102   -26.75373 -42.62147 1.000 20.99639 ? 481 ALA A N     1 
ATOM   3839 C  CA    . ALA A 1 481 ? 2.01400   -25.63276 -43.34649 1.000 16.82998 ? 481 ALA A CA    1 
ATOM   3840 C  C     . ALA A 1 481 ? 2.84999   -24.37075 -43.17955 1.000 15.87650 ? 481 ALA A C     1 
ATOM   3841 O  O     . ALA A 1 481 ? 2.98696   -23.58077 -44.12057 1.000 15.42180 ? 481 ALA A O     1 
ATOM   3842 C  CB    . ALA A 1 481 ? 0.57900   -25.39575 -42.87747 1.000 13.04706 ? 481 ALA A CB    1 
ATOM   3843 N  N     . CYS A 1 482 ? 3.42101   -24.16570 -41.98957 1.000 17.72624 ? 482 CYS A N     1 
ATOM   3844 C  CA    . CYS A 1 482 ? 4.22301   -22.96969 -41.75262 1.000 15.18271 ? 482 CYS A CA    1 
ATOM   3845 C  C     . CYS A 1 482 ? 5.55599   -23.03770 -42.48664 1.000 16.74284 ? 482 CYS A C     1 
ATOM   3846 O  O     . CYS A 1 482 ? 6.04197   -22.02071 -42.99469 1.000 16.35833 ? 482 CYS A O     1 
ATOM   3847 C  CB    . CYS A 1 482 ? 4.44704   -22.77464 -40.25263 1.000 15.05136 ? 482 CYS A CB    1 
ATOM   3848 S  SG    . CYS A 1 482 ? 2.96205   -22.33663 -39.31761 1.000 16.31246 ? 482 CYS A SG    1 
ATOM   3849 N  N     . ILE A 1 483 ? 6.16300   -24.22470 -42.55362 1.000 15.67031 ? 483 ILE A N     1 
ATOM   3850 C  CA    . ILE A 1 483 ? 7.46199   -24.35971 -43.20764 1.000 16.57844 ? 483 ILE A CA    1 
ATOM   3851 C  C     . ILE A 1 483 ? 7.34295   -24.08976 -44.70265 1.000 17.91898 ? 483 ILE A C     1 
ATOM   3852 O  O     . ILE A 1 483 ? 8.18994   -23.40977 -45.29369 1.000 16.72386 ? 483 ILE A O     1 
ATOM   3853 C  CB    . ILE A 1 483 ? 8.05901   -25.75170 -42.92762 1.000 16.70008 ? 483 ILE A CB    1 
ATOM   3854 C  CG1   . ILE A 1 483 ? 8.40904   -25.89765 -41.44462 1.000 19.02820 ? 483 ILE A CG1   1 
ATOM   3855 C  CG2   . ILE A 1 483 ? 9.28899   -25.99471 -43.78863 1.000 18.77520 ? 483 ILE A CG2   1 
ATOM   3856 C  CD1   . ILE A 1 483 ? 8.99906   -27.24563 -41.08859 1.000 16.84621 ? 483 ILE A CD1   1 
ATOM   3857 N  N     . ALA A 1 484 ? 6.28795   -24.60978 -45.33661 1.000 18.65802 ? 484 ALA A N     1 
ATOM   3858 C  CA    . ALA A 1 484 ? 6.12391   -24.42083 -46.77461 1.000 18.16980 ? 484 ALA A CA    1 
ATOM   3859 C  C     . ALA A 1 484 ? 5.85789   -22.95984 -47.11765 1.000 21.84199 ? 484 ALA A C     1 
ATOM   3860 O  O     . ALA A 1 484 ? 6.36187   -22.45287 -48.12668 1.000 21.13011 ? 484 ALA A O     1 
ATOM   3861 C  CB    . ALA A 1 484 ? 4.99391   -25.30985 -47.29356 1.000 21.79341 ? 484 ALA A CB    1 
ATOM   3862 N  N     . ARG A 1 485 ? 5.06754   -22.26811 -46.29166 1.000 19.46376 ? 485 ARG A N     1 
ATOM   3863 C  CA    . ARG A 1 485 ? 4.79891   -20.85498 -46.53694 1.000 17.98178 ? 485 ARG A CA    1 
ATOM   3864 C  C     . ARG A 1 485 ? 6.04081   -20.00079 -46.31927 1.000 20.63216 ? 485 ARG A C     1 
ATOM   3865 O  O     . ARG A 1 485 ? 6.22753   -18.99477 -47.01344 1.000 22.94422 ? 485 ARG A O     1 
ATOM   3866 C  CB    . ARG A 1 485 ? 3.65758   -20.37238 -45.64195 1.000 19.41056 ? 485 ARG A CB    1 
ATOM   3867 C  CG    . ARG A 1 485 ? 2.32411   -21.04617 -45.92193 1.000 21.73370 ? 485 ARG A CG    1 
ATOM   3868 C  CD    . ARG A 1 485 ? 1.26629   -20.62377 -44.91455 1.000 15.69231 ? 485 ARG A CD    1 
ATOM   3869 N  NE    . ARG A 1 485 ? 0.92893   -19.21072 -45.03302 1.000 17.34260 ? 485 ARG A NE    1 
ATOM   3870 C  CZ    . ARG A 1 485 ? 0.07546   -18.57575 -44.24162 1.000 16.14948 ? 485 ARG A CZ    1 
ATOM   3871 N  NH1   . ARG A 1 485 ? -0.54130  -19.19754 -43.25020 1.000 19.35538 ? 485 ARG A NH1   1 
ATOM   3872 N  NH2   . ARG A 1 485 ? -0.16505  -17.28446 -44.45003 1.000 17.22790 ? 485 ARG A NH2   1 
ATOM   3873 N  N     . MET A 1 486 ? 6.89391   -20.37678 -45.36275 1.000 17.22845 ? 486 MET A N     1 
ATOM   3874 C  CA    . MET A 1 486 ? 8.15591   -19.66576 -45.18180 1.000 19.67143 ? 486 MET A CA    1 
ATOM   3875 C  C     . MET A 1 486 ? 9.08689   -19.87479 -46.36782 1.000 19.63170 ? 486 MET A C     1 
ATOM   3876 O  O     . MET A 1 486 ? 9.85287   -18.96980 -46.71886 1.000 20.77566 ? 486 MET A O     1 
ATOM   3877 C  CB    . MET A 1 486 ? 8.83594   -20.11472 -43.88880 1.000 19.52337 ? 486 MET A CB    1 
ATOM   3878 C  CG    . MET A 1 486 ? 8.12496   -19.67469 -42.61780 1.000 20.03062 ? 486 MET A CG    1 
ATOM   3879 S  SD    . MET A 1 486 ? 8.27596   -17.90768 -42.29886 1.000 19.53212 ? 486 MET A SD    1 
ATOM   3880 C  CE    . MET A 1 486 ? 10.04496  -17.76265 -42.05990 1.000 17.81632 ? 486 MET A CE    1 
ATOM   3881 N  N     . ALA A 1 487 ? 9.03888   -21.05381 -46.99278 1.000 19.97967 ? 487 ALA A N     1 
ATOM   3882 C  CA    . ALA A 1 487 ? 9.85386   -21.29584 -48.17979 1.000 22.51251 ? 487 ALA A CA    1 
ATOM   3883 C  C     . ALA A 1 487 ? 9.40983   -20.41488 -49.33881 1.000 24.67715 ? 487 ALA A C     1 
ATOM   3884 O  O     . ALA A 1 487 ? 10.24681  -19.88690 -50.08184 1.000 25.44639 ? 487 ALA A O     1 
ATOM   3885 C  CB    . ALA A 1 487 ? 9.79086   -22.77285 -48.57074 1.000 20.79349 ? 487 ALA A CB    1 
ATOM   3886 N  N     . ALA A 1 488 ? 8.09682   -20.24590 -49.51278 1.000 25.43021 ? 488 ALA A N     1 
ATOM   3887 C  CA    . ALA A 1 488 ? 7.60279   -19.32393 -50.52880 1.000 27.51617 ? 488 ALA A CA    1 
ATOM   3888 C  C     . ALA A 1 488 ? 7.96879   -17.88392 -50.19885 1.000 27.46611 ? 488 ALA A C     1 
ATOM   3889 O  O     . ALA A 1 488 ? 8.19076   -17.07694 -51.10788 1.000 27.91407 ? 488 ALA A O     1 
ATOM   3890 C  CB    . ALA A 1 488 ? 6.08879   -19.46795 -50.68376 1.000 23.77303 ? 488 ALA A CB    1 
ATOM   3891 N  N     . ALA A 1 489 ? 8.03981   -17.54688 -48.90886 1.000 25.53736 ? 489 ALA A N     1 
ATOM   3892 C  CA    . ALA A 1 489 ? 8.47781   -16.21186 -48.51791 1.000 27.13199 ? 489 ALA A CA    1 
ATOM   3893 C  C     . ALA A 1 489 ? 9.95480   -16.00586 -48.83295 1.000 27.04888 ? 489 ALA A C     1 
ATOM   3894 O  O     . ALA A 1 489 ? 10.35379  -14.92887 -49.29099 1.000 31.80364 ? 489 ALA A O     1 
ATOM   3895 C  CB    . ALA A 1 489 ? 8.20684   -15.98382 -47.03191 1.000 22.75667 ? 489 ALA A CB    1 
ATOM   3896 N  N     . TYR A 1 490 ? 10.78082  -17.02785 -48.60094 1.000 26.44860 ? 490 TYR A N     1 
ATOM   3897 C  CA    . TYR A 1 490 ? 12.20281  -16.94184 -48.90397 1.000 26.89345 ? 490 TYR A CA    1 
ATOM   3898 C  C     . TYR A 1 490 ? 12.50278  -17.05289 -50.39297 1.000 29.27898 ? 490 TYR A C     1 
ATOM   3899 O  O     . TYR A 1 490 ? 13.64177  -16.79289 -50.79700 1.000 35.15148 ? 490 TYR A O     1 
ATOM   3900 C  CB    . TYR A 1 490 ? 12.97383  -18.02182 -48.13795 1.000 24.28623 ? 490 TYR A CB    1 
ATOM   3901 C  CG    . TYR A 1 490 ? 13.47686  -17.55577 -46.78898 1.000 22.02613 ? 490 TYR A CG    1 
ATOM   3902 C  CD1   . TYR A 1 490 ? 12.64488  -17.55174 -45.67696 1.000 20.72671 ? 490 TYR A CD1   1 
ATOM   3903 C  CD2   . TYR A 1 490 ? 14.78486  -17.11476 -46.63002 1.000 19.38335 ? 490 TYR A CD2   1 
ATOM   3904 C  CE1   . TYR A 1 490 ? 13.10190  -17.12370 -44.44498 1.000 21.61760 ? 490 TYR A CE1   1 
ATOM   3905 C  CE2   . TYR A 1 490 ? 15.24988  -16.68571 -45.40304 1.000 17.81906 ? 490 TYR A CE2   1 
ATOM   3906 C  CZ    . TYR A 1 490 ? 14.40490  -16.69169 -44.31402 1.000 16.57285 ? 490 TYR A CZ    1 
ATOM   3907 O  OH    . TYR A 1 490 ? 14.86493  -16.26565 -43.09005 1.000 15.24445 ? 490 TYR A OH    1 
ATOM   3908 N  N     . ARG A 1 491 ? 11.51970  -17.42006 -51.21494 1.000 31.13702 ? 491 ARG A N     1 
ATOM   3909 C  CA    . ARG A 1 491 ? 11.70252  -17.43028 -52.65999 1.000 32.86105 ? 491 ARG A CA    1 
ATOM   3910 C  C     . ARG A 1 491 ? 11.28048  -16.12542 -53.32063 1.000 30.37763 ? 491 ARG A C     1 
ATOM   3911 O  O     . ARG A 1 491 ? 11.76143  -15.81909 -54.41746 1.000 33.30113 ? 491 ARG A O     1 
ATOM   3912 C  CB    . ARG A 1 491 ? 10.92962  -18.59505 -53.28924 1.000 34.91202 ? 491 ARG A CB    1 
ATOM   3913 C  CG    . ARG A 1 491 ? 11.67173  -19.92358 -53.23984 1.000 39.52492 ? 491 ARG A CG    1 
ATOM   3914 C  CD    . ARG A 1 491 ? 10.99965  -20.98486 -54.10326 1.000 35.35219 ? 491 ARG A CD    1 
ATOM   3915 N  NE    . ARG A 1 491 ? 9.95717   -21.71220 -53.38839 1.000 32.34886 ? 491 ARG A NE    1 
ATOM   3916 C  CZ    . ARG A 1 491 ? 8.66625   -21.41195 -53.42960 1.000 34.60414 ? 491 ARG A CZ    1 
ATOM   3917 N  NH1   . ARG A 1 491 ? 8.21596   -20.39022 -54.13873 1.000 37.89554 ? 491 ARG A NH1   1 
ATOM   3918 N  NH2   . ARG A 1 491 ? 7.80496   -22.15716 -52.74291 1.000 38.18076 ? 491 ARG A NH2   1 
ATOM   3919 N  N     . ARG A 1 492 ? 10.39856  -15.35355 -52.68533 1.000 29.73005 ? 492 ARG A N     1 
ATOM   3920 C  CA    . ARG A 1 492 ? 10.01342  -14.04750 -53.20343 1.000 32.70467 ? 492 ARG A CA    1 
ATOM   3921 C  C     . ARG A 1 492 ? 10.98039  -12.94498 -52.79333 1.000 37.00768 ? 492 ARG A C     1 
ATOM   3922 O  O     . ARG A 1 492 ? 10.87994  -11.82851 -53.31413 1.000 35.98999 ? 492 ARG A O     1 
ATOM   3923 C  CB    . ARG A 1 492 ? 8.59903   -13.69280 -52.73668 1.000 33.12656 ? 492 ARG A CB    1 
ATOM   3924 N  N     . SER A 1 493 ? 11.90672  -13.23294 -51.87608 1.000 34.46229 ? 493 SER A N     1 
ATOM   3925 C  CA    . SER A 1 493 ? 12.91872  -12.22992 -51.47013 1.000 35.38765 ? 493 SER A CA    1 
ATOM   3926 C  C     . SER A 1 493 ? 13.85269  -11.93795 -52.64516 1.000 36.48620 ? 493 SER A C     1 
ATOM   3927 O  O     . SER A 1 493 ? 14.22568  -10.78295 -52.78220 1.000 38.37645 ? 493 SER A O     1 
ATOM   3928 C  CB    . SER A 1 493 ? 13.66075  -12.65087 -50.21613 1.000 31.94560 ? 493 SER A CB    1 
ATOM   3929 O  OG    . SER A 1 493 ? 13.20177  -13.89586 -49.73008 1.000 35.99579 ? 493 SER A OG    1 
ATOM   3930 N  N     . LYS A 1 494 ? 14.19368  -12.95097 -53.45013 1.000 38.42794 ? 494 LYS A N     1 
ATOM   3931 C  CA    . LYS A 1 494 ? 15.07166  -12.80499 -54.61016 1.000 36.19802 ? 494 LYS A CA    1 
ATOM   3932 C  C     . LYS A 1 494 ? 16.41066  -12.17397 -54.23920 1.000 35.85691 ? 494 LYS A C     1 
ATOM   3933 O  O     . LYS A 1 494 ? 17.44565  -12.51198 -54.81222 1.000 36.68217 ? 494 LYS A O     1 
ATOM   3934 C  CB    . LYS A 1 494 ? 14.38463  -11.97903 -55.70117 1.000 34.12542 ? 494 LYS A CB    1 
HETATM 3935 P  PA    . FAD B 2 .   ? 22.34242  -15.01787 -19.33324 1.000 3.12525  ? 601 FAD A PA    1 
HETATM 3936 O  O1A   . FAD B 2 .   ? 22.76745  -14.84082 -17.93326 1.000 4.28560  ? 601 FAD A O1A   1 
HETATM 3937 O  O2A   . FAD B 2 .   ? 22.57342  -16.33789 -19.96221 1.000 3.93348  ? 601 FAD A O2A   1 
HETATM 3938 O  O5B   . FAD B 2 .   ? 22.99539  -13.89389 -20.25529 1.000 4.23463  ? 601 FAD A O5B   1 
HETATM 3939 C  C5B   . FAD B 2 .   ? 23.69740  -12.83187 -19.60534 1.000 5.65409  ? 601 FAD A C5B   1 
HETATM 3940 C  C4B   . FAD B 2 .   ? 23.24137  -11.51089 -20.17137 1.000 4.78657  ? 601 FAD A C4B   1 
HETATM 3941 O  O4B   . FAD B 2 .   ? 23.55034  -11.45593 -21.57938 1.000 5.04298  ? 601 FAD A O4B   1 
HETATM 3942 C  C3B   . FAD B 2 .   ? 21.73737  -11.24290 -20.07934 1.000 5.75247  ? 601 FAD A C3B   1 
HETATM 3943 O  O3B   . FAD B 2 .   ? 21.41540  -10.66686 -18.82336 1.000 3.78483  ? 601 FAD A O3B   1 
HETATM 3944 C  C2B   . FAD B 2 .   ? 21.50934  -10.28093 -21.25137 1.000 5.03230  ? 601 FAD A C2B   1 
HETATM 3945 O  O2B   . FAD B 2 .   ? 21.80334  -8.94692  -20.90542 1.000 6.20034  ? 601 FAD A O2B   1 
HETATM 3946 C  C1B   . FAD B 2 .   ? 22.49632  -10.81896 -22.29137 1.000 4.94574  ? 601 FAD A C1B   1 
HETATM 3947 N  N9A   . FAD B 2 .   ? 21.91031  -11.77999 -23.22533 1.000 4.71483  ? 601 FAD A N9A   1 
HETATM 3948 C  C8A   . FAD B 2 .   ? 21.74433  -13.12699 -23.05029 1.000 5.14152  ? 601 FAD A C8A   1 
HETATM 3949 N  N7A   . FAD B 2 .   ? 21.18731  -13.72902 -24.06926 1.000 4.84750  ? 601 FAD A N7A   1 
HETATM 3950 C  C5A   . FAD B 2 .   ? 20.96628  -12.70705 -24.97828 1.000 6.09393  ? 601 FAD A C5A   1 
HETATM 3951 C  C6A   . FAD B 2 .   ? 20.39825  -12.70009 -26.26327 1.000 5.17068  ? 601 FAD A C6A   1 
HETATM 3952 N  N6A   . FAD B 2 .   ? 19.92925  -13.78612 -26.87023 1.000 6.11219  ? 601 FAD A N6A   1 
HETATM 3953 N  N1A   . FAD B 2 .   ? 20.32123  -11.51011 -26.90031 1.000 6.41350  ? 601 FAD A N1A   1 
HETATM 3954 C  C2A   . FAD B 2 .   ? 20.79324  -10.42409 -26.28335 1.000 5.24071  ? 601 FAD A C2A   1 
HETATM 3955 N  N3A   . FAD B 2 .   ? 21.34926  -10.31105 -25.08536 1.000 5.09150  ? 601 FAD A N3A   1 
HETATM 3956 C  C4A   . FAD B 2 .   ? 21.40828  -11.50003 -24.47033 1.000 5.77130  ? 601 FAD A C4A   1 
HETATM 3957 N  N1    . FAD B 2 .   ? 16.78600  -10.25300 -23.48000 1.000 5.07569  ? 601 FAD A N1    1 
HETATM 3958 C  C2    . FAD B 2 .   ? 16.57400  -9.11800  -22.79700 1.000 6.37112  ? 601 FAD A C2    1 
HETATM 3959 O  O2    . FAD B 2 .   ? 17.35100  -8.74000  -21.94100 1.000 5.97344  ? 601 FAD A O2    1 
HETATM 3960 N  N3    . FAD B 2 .   ? 15.50200  -8.32000  -23.05000 1.000 6.39909  ? 601 FAD A N3    1 
HETATM 3961 C  C4    . FAD B 2 .   ? 14.54000  -8.64700  -23.96300 1.000 6.53595  ? 601 FAD A C4    1 
HETATM 3962 O  O4    . FAD B 2 .   ? 13.61100  -7.85900  -24.16300 1.000 6.15225  ? 601 FAD A O4    1 
HETATM 3963 C  C4X   . FAD B 2 .   ? 14.66800  -9.91500  -24.61900 1.000 6.11724  ? 601 FAD A C4X   1 
HETATM 3964 N  N5    . FAD B 2 .   ? 13.70100  -10.33300 -25.41200 1.000 6.22832  ? 601 FAD A N5    1 
HETATM 3965 C  C5X   . FAD B 2 .   ? 13.75900  -11.63400 -25.85100 1.000 6.13666  ? 601 FAD A C5X   1 
HETATM 3966 C  C6    . FAD B 2 .   ? 12.66900  -12.18900 -26.55900 1.000 7.02636  ? 601 FAD A C6    1 
HETATM 3967 C  C7    . FAD B 2 .   ? 12.77000  -13.41000 -27.19400 1.000 6.08055  ? 601 FAD A C7    1 
HETATM 3968 C  C7M   . FAD B 2 .   ? 11.58000  -13.96500 -27.93900 1.000 7.91117  ? 601 FAD A C7M   1 
HETATM 3969 C  C8    . FAD B 2 .   ? 13.99600  -14.13600 -27.12400 1.000 6.56821  ? 601 FAD A C8    1 
HETATM 3970 C  C8M   . FAD B 2 .   ? 14.16000  -15.46600 -27.81700 1.000 7.40659  ? 601 FAD A C8M   1 
HETATM 3971 C  C9    . FAD B 2 .   ? 15.08500  -13.56300 -26.51000 1.000 6.22836  ? 601 FAD A C9    1 
HETATM 3972 C  C9A   . FAD B 2 .   ? 15.00000  -12.32100 -25.85600 1.000 5.69077  ? 601 FAD A C9A   1 
HETATM 3973 N  N10   . FAD B 2 .   ? 16.01300  -11.86500 -24.98400 1.000 5.20248  ? 601 FAD A N10   1 
HETATM 3974 C  C10   . FAD B 2 .   ? 15.84900  -10.67000 -24.30900 1.000 5.72511  ? 601 FAD A C10   1 
HETATM 3975 C  "C1'" . FAD B 2 .   ? 17.25729  -12.63507 -24.78521 1.000 5.44936  ? 601 FAD A "C1'" 1 
HETATM 3976 C  "C2'" . FAD B 2 .   ? 17.22232  -13.69904 -23.70717 1.000 5.02394  ? 601 FAD A "C2'" 1 
HETATM 3977 O  "O2'" . FAD B 2 .   ? 15.93832  -14.31905 -23.66413 1.000 7.23518  ? 601 FAD A "O2'" 1 
HETATM 3978 C  "C3'" . FAD B 2 .   ? 17.54134  -13.12500 -22.32320 1.000 5.82709  ? 601 FAD A "C3'" 1 
HETATM 3979 O  "O3'" . FAD B 2 .   ? 18.59333  -12.16999 -22.41825 1.000 5.06278  ? 601 FAD A "O3'" 1 
HETATM 3980 C  "C4'" . FAD B 2 .   ? 17.89937  -14.18296 -21.27717 1.000 5.03005  ? 601 FAD A "C4'" 1 
HETATM 3981 O  "O4'" . FAD B 2 .   ? 16.95938  -15.25197 -21.29412 1.000 4.72786  ? 601 FAD A "O4'" 1 
HETATM 3982 C  "C5'" . FAD B 2 .   ? 17.93540  -13.57392 -19.89119 1.000 5.46888  ? 601 FAD A "C5'" 1 
HETATM 3983 O  "O5'" . FAD B 2 .   ? 18.39142  -14.52789 -18.92617 1.000 5.28316  ? 601 FAD A "O5'" 1 
HETATM 3984 P  P     . FAD B 2 .   ? 19.80744  -14.29886 -18.24221 1.000 5.57199  ? 601 FAD A P     1 
HETATM 3985 O  O1P   . FAD B 2 .   ? 19.94543  -12.87784 -17.86026 1.000 5.66185  ? 601 FAD A O1P   1 
HETATM 3986 O  O2P   . FAD B 2 .   ? 19.96447  -15.27382 -17.14718 1.000 5.27617  ? 601 FAD A O2P   1 
HETATM 3987 O  O3P   . FAD B 2 .   ? 20.81342  -14.61988 -19.41022 1.000 5.58978  ? 601 FAD A O3P   1 
HETATM 3988 CL CL    . CL  C 3 .   ? 12.26030  -30.29529 -30.75257 1.000 21.04057 ? 602 CL  A CL    1 
HETATM 3989 O  O     . HOH D 4 .   ? 43.60634  -7.54773  -20.33192 1.000 24.07091 ? 701 HOH A O     1 
HETATM 3990 O  O     . HOH D 4 .   ? 16.59294  -14.32859 -41.54114 1.000 15.80253 ? 702 HOH A O     1 
HETATM 3991 O  O     . HOH D 4 .   ? 19.38667  -10.30648 -5.83832  1.000 16.29525 ? 703 HOH A O     1 
HETATM 3992 O  O     . HOH D 4 .   ? 23.72551  15.06562  -3.72018  1.000 12.19456 ? 704 HOH A O     1 
HETATM 3993 O  O     . HOH D 4 .   ? 41.54539  -16.80078 -21.47260 1.000 13.30790 ? 705 HOH A O     1 
HETATM 3994 O  O     . HOH D 4 .   ? 1.95745   -9.03491  -15.44799 1.000 15.53052 ? 706 HOH A O     1 
HETATM 3995 O  O     . HOH D 4 .   ? 21.02501  12.86585  -28.38206 1.000 25.37292 ? 707 HOH A O     1 
HETATM 3996 O  O     . HOH D 4 .   ? 11.52981  -4.89272  -44.51732 1.000 27.68618 ? 708 HOH A O     1 
HETATM 3997 O  O     . HOH D 4 .   ? 11.99264  -27.99878 -13.58463 1.000 15.27841 ? 709 HOH A O     1 
HETATM 3998 O  O     . HOH D 4 .   ? 26.47508  4.38790   -28.09192 1.000 16.92694 ? 710 HOH A O     1 
HETATM 3999 O  O     . HOH D 4 .   ? 1.08253   -11.44583 -12.58490 1.000 16.69236 ? 711 HOH A O     1 
HETATM 4000 O  O     . HOH D 4 .   ? 36.81632  3.53030   -17.37411 1.000 11.86015 ? 712 HOH A O     1 
HETATM 4001 O  O     . HOH D 4 .   ? 34.12357  -24.97768 -16.18619 1.000 15.16529 ? 713 HOH A O     1 
HETATM 4002 O  O     . HOH D 4 .   ? 10.40376  -12.49587 -49.35407 1.000 32.28148 ? 714 HOH A O     1 
HETATM 4003 O  O     . HOH D 4 .   ? 16.75388  -10.31163 -43.14927 1.000 18.05834 ? 715 HOH A O     1 
HETATM 4004 O  O     . HOH D 4 .   ? 7.47841   16.37635  -8.25888  1.000 16.46115 ? 716 HOH A O     1 
HETATM 4005 O  O     . HOH D 4 .   ? 3.14842   -29.32518 -24.47440 1.000 10.89044 ? 717 HOH A O     1 
HETATM 4006 O  O     . HOH D 4 .   ? 33.53343  12.56854  -8.67032  1.000 19.77072 ? 718 HOH A O     1 
HETATM 4007 O  O     . HOH D 4 .   ? 14.97565  -3.40546  -3.90544  1.000 19.75551 ? 719 HOH A O     1 
HETATM 4008 O  O     . HOH D 4 .   ? 34.34123  -7.24796  -25.40073 1.000 11.09853 ? 720 HOH A O     1 
HETATM 4009 O  O     A HOH D 4 .   ? 7.93655   -5.96869  -9.59021  0.617 6.42172  ? 721 HOH A O     1 
HETATM 4010 O  O     B HOH D 4 .   ? 10.09859  -6.82463  -8.26423  0.383 8.61232  ? 721 HOH A O     1 
HETATM 4011 O  O     . HOH D 4 .   ? 8.98993   -10.68162 -40.68209 1.000 16.91332 ? 722 HOH A O     1 
HETATM 4012 O  O     . HOH D 4 .   ? 6.04829   -33.28238 -32.08934 1.000 14.08176 ? 723 HOH A O     1 
HETATM 4013 O  O     . HOH D 4 .   ? -4.55529  -32.52387 -12.35214 1.000 15.56131 ? 724 HOH A O     1 
HETATM 4014 O  O     . HOH D 4 .   ? 4.17984   -17.66087 -47.72478 1.000 24.10239 ? 725 HOH A O     1 
HETATM 4015 O  O     . HOH D 4 .   ? 26.40825  -5.15597  -23.69063 1.000 6.35560  ? 726 HOH A O     1 
HETATM 4016 O  O     . HOH D 4 .   ? 21.73539  24.97753  -5.97444  1.000 15.76583 ? 727 HOH A O     1 
HETATM 4017 O  O     . HOH D 4 .   ? 0.73850   -39.06120 -24.54706 1.000 19.27960 ? 728 HOH A O     1 
HETATM 4018 O  O     . HOH D 4 .   ? 19.77065  -24.72067 -12.11789 1.000 16.23813 ? 729 HOH A O     1 
HETATM 4019 O  O     . HOH D 4 .   ? 7.69161   1.71347   -4.22344  1.000 13.71538 ? 730 HOH A O     1 
HETATM 4020 O  O     . HOH D 4 .   ? 32.97932  3.05828   -17.27502 1.000 10.62351 ? 731 HOH A O     1 
HETATM 4021 O  O     . HOH D 4 .   ? 6.88444   22.36946  -4.43205  1.000 15.51689 ? 732 HOH A O     1 
HETATM 4022 O  O     . HOH D 4 .   ? 22.12829  -16.43808 -26.21520 1.000 10.11796 ? 733 HOH A O     1 
HETATM 4023 O  O     . HOH D 4 .   ? 21.99959  2.00056   -5.05775  1.000 9.88471  ? 734 HOH A O     1 
HETATM 4024 O  O     . HOH D 4 .   ? -4.67357  -30.01523 -24.38322 1.000 11.08665 ? 735 HOH A O     1 
HETATM 4025 O  O     . HOH D 4 .   ? 32.99557  13.92576  -1.31135  1.000 17.42090 ? 736 HOH A O     1 
HETATM 4026 O  O     . HOH D 4 .   ? 13.48955  13.53758  -2.33592  1.000 13.37938 ? 737 HOH A O     1 
HETATM 4027 O  O     . HOH D 4 .   ? 37.89427  -8.40589  -24.00877 1.000 14.84046 ? 738 HOH A O     1 
HETATM 4028 O  O     . HOH D 4 .   ? 17.72164  -11.08855 -7.61526  1.000 13.17248 ? 739 HOH A O     1 
HETATM 4029 O  O     . HOH D 4 .   ? 31.71844  -18.70581 -19.96333 1.000 7.14102  ? 740 HOH A O     1 
HETATM 4030 O  O     . HOH D 4 .   ? 5.35583   -14.40984 -46.92590 1.000 33.44333 ? 741 HOH A O     1 
HETATM 4031 O  O     . HOH D 4 .   ? 5.04594   -8.15862  -39.53308 1.000 20.22641 ? 742 HOH A O     1 
HETATM 4032 O  O     . HOH D 4 .   ? 26.71430  7.11025   -16.65301 1.000 8.87547  ? 743 HOH A O     1 
HETATM 4033 O  O     . HOH D 4 .   ? 15.01463  -29.44279 -14.84465 1.000 16.33872 ? 744 HOH A O     1 
HETATM 4034 O  O     . HOH D 4 .   ? 31.38870  -14.00639 -5.85547  1.000 13.12678 ? 745 HOH A O     1 
HETATM 4035 O  O     . HOH D 4 .   ? 35.03135  -3.66274  -18.22986 1.000 10.20044 ? 746 HOH A O     1 
HETATM 4036 O  O     . HOH D 4 .   ? 25.71419  4.52905   -22.80991 1.000 8.42270  ? 747 HOH A O     1 
HETATM 4037 O  O     . HOH D 4 .   ? 11.33359  24.11472  3.06080   1.000 24.06187 ? 748 HOH A O     1 
HETATM 4038 O  O     . HOH D 4 .   ? -8.48666  -22.36531 -25.84537 1.000 12.81771 ? 749 HOH A O     1 
HETATM 4039 O  O     . HOH D 4 .   ? 18.11142  -17.47593 -20.25208 1.000 5.60019  ? 750 HOH A O     1 
HETATM 4040 O  O     . HOH D 4 .   ? 6.85922   -24.55839 -32.51863 1.000 7.04741  ? 751 HOH A O     1 
HETATM 4041 O  O     . HOH D 4 .   ? 11.48077  -9.12182  -47.75219 1.000 22.71632 ? 752 HOH A O     1 
HETATM 4042 O  O     . HOH D 4 .   ? -6.38685  -11.07643 -30.49475 1.000 22.14807 ? 753 HOH A O     1 
HETATM 4043 O  O     . HOH D 4 .   ? 32.65749  15.95867  -4.31940  1.000 19.51825 ? 754 HOH A O     1 
HETATM 4044 O  O     . HOH D 4 .   ? 38.98744  -7.43862  -15.43782 1.000 20.07694 ? 755 HOH A O     1 
HETATM 4045 O  O     . HOH D 4 .   ? 14.21122  -0.67305  -23.24851 1.000 8.56229  ? 756 HOH A O     1 
HETATM 4046 O  O     . HOH D 4 .   ? 8.18167   -3.40049  -3.19930  1.000 23.19064 ? 757 HOH A O     1 
HETATM 4047 O  O     . HOH D 4 .   ? 12.28421  10.22704  -19.84679 1.000 20.97066 ? 758 HOH A O     1 
HETATM 4048 O  O     . HOH D 4 .   ? 32.40050  1.18451   -9.32195  1.000 14.08607 ? 759 HOH A O     1 
HETATM 4049 O  O     . HOH D 4 .   ? 27.27964  15.34083  2.45473   1.000 20.45818 ? 760 HOH A O     1 
HETATM 4050 O  O     . HOH D 4 .   ? 23.13432  1.58019   -17.63976 1.000 8.23792  ? 761 HOH A O     1 
HETATM 4051 O  O     . HOH D 4 .   ? 6.15057   11.94052  -2.43272  1.000 15.86541 ? 762 HOH A O     1 
HETATM 4052 O  O     . HOH D 4 .   ? 5.89112   -4.00730  -29.19423 1.000 19.44010 ? 763 HOH A O     1 
HETATM 4053 O  O     . HOH D 4 .   ? 7.72541   -29.29816 -25.25650 1.000 11.16515 ? 764 HOH A O     1 
HETATM 4054 O  O     . HOH D 4 .   ? 31.82438  24.44259  -6.61364  1.000 16.95217 ? 765 HOH A O     1 
HETATM 4055 O  O     . HOH D 4 .   ? 8.39420   -29.93746 -35.05650 1.000 15.51503 ? 766 HOH A O     1 
HETATM 4056 O  O     . HOH D 4 .   ? 30.82245  5.31647   -10.27804 1.000 9.88587  ? 767 HOH A O     1 
HETATM 4057 O  O     . HOH D 4 .   ? 4.50620   9.53696   -20.47561 1.000 37.69380 ? 768 HOH A O     1 
HETATM 4058 O  O     . HOH D 4 .   ? 14.52966  -1.31943  -2.83849  1.000 16.34851 ? 769 HOH A O     1 
HETATM 4059 O  O     . HOH D 4 .   ? 19.98992  -10.62455 -41.25833 1.000 16.26082 ? 770 HOH A O     1 
HETATM 4060 O  O     . HOH D 4 .   ? 28.25455  -23.75974 -16.60810 1.000 12.64739 ? 771 HOH A O     1 
HETATM 4061 O  O     . HOH D 4 .   ? -0.43057  -5.02292  -15.18006 1.000 17.73999 ? 772 HOH A O     1 
HETATM 4062 O  O     . HOH D 4 .   ? 12.94122  28.68527  -12.34037 1.000 18.58794 ? 773 HOH A O     1 
HETATM 4063 O  O     . HOH D 4 .   ? 5.03746   -9.97689  -15.67203 1.000 10.80221 ? 774 HOH A O     1 
HETATM 4064 O  O     . HOH D 4 .   ? 10.45931  27.79836  -8.63129  1.000 22.83286 ? 775 HOH A O     1 
HETATM 4065 O  O     . HOH D 4 .   ? 19.14622  -17.65121 -29.84810 1.000 13.14072 ? 776 HOH A O     1 
HETATM 4066 O  O     . HOH D 4 .   ? 21.60523  5.51009   -20.46985 1.000 12.26107 ? 777 HOH A O     1 
HETATM 4067 O  O     . HOH D 4 .   ? 20.07230  -4.81395  -21.31350 1.000 6.18458  ? 778 HOH A O     1 
HETATM 4068 O  O     . HOH D 4 .   ? 25.89934  -1.05780  -18.07774 1.000 5.14059  ? 779 HOH A O     1 
HETATM 4069 O  O     . HOH D 4 .   ? 15.97453  -21.69483 -16.51591 1.000 7.12440  ? 780 HOH A O     1 
HETATM 4070 O  O     . HOH D 4 .   ? 13.91030  10.20417  -15.81283 1.000 8.52256  ? 781 HOH A O     1 
HETATM 4071 O  O     . HOH D 4 .   ? 22.57315  2.94095   -25.27579 1.000 11.66310 ? 782 HOH A O     1 
HETATM 4072 O  O     . HOH D 4 .   ? 7.64827   -24.26731 -30.05165 1.000 11.66823 ? 783 HOH A O     1 
HETATM 4073 O  O     . HOH D 4 .   ? 38.16721  -7.75397  -26.72780 1.000 15.22515 ? 784 HOH A O     1 
HETATM 4074 O  O     . HOH D 4 .   ? 36.45221  -13.21803 -28.44060 1.000 20.75032 ? 785 HOH A O     1 
HETATM 4075 O  O     . HOH D 4 .   ? -0.06276  -7.69722  -25.15899 1.000 18.78423 ? 786 HOH A O     1 
HETATM 4076 O  O     A HOH D 4 .   ? 20.48527  7.26115   -18.33988 0.518 5.92673  ? 787 HOH A O     1 
HETATM 4077 O  O     B HOH D 4 .   ? 21.88730  8.36622   -16.19294 0.482 5.45168  ? 787 HOH A O     1 
HETATM 4078 O  O     . HOH D 4 .   ? 18.87753  0.59744   -8.39664  1.000 8.51813  ? 788 HOH A O     1 
HETATM 4079 O  O     . HOH D 4 .   ? 34.32714  2.72903   -25.84403 1.000 10.62540 ? 789 HOH A O     1 
HETATM 4080 O  O     . HOH D 4 .   ? 12.71855  -20.50482 -15.12187 1.000 10.71214 ? 790 HOH A O     1 
HETATM 4081 O  O     . HOH D 4 .   ? 35.96449  0.70552   -10.05501 1.000 19.13577 ? 791 HOH A O     1 
HETATM 4082 O  O     . HOH D 4 .   ? 19.38333  -7.12093  -20.69542 1.000 5.36109  ? 792 HOH A O     1 
HETATM 4083 O  O     . HOH D 4 .   ? 39.83753  -23.98167 -17.37734 1.000 12.93139 ? 793 HOH A O     1 
HETATM 4084 O  O     . HOH D 4 .   ? 17.19216  -0.38812  -26.20758 1.000 12.20289 ? 794 HOH A O     1 
HETATM 4085 O  O     . HOH D 4 .   ? 36.87336  -5.86374  -18.83483 1.000 14.30481 ? 795 HOH A O     1 
HETATM 4086 O  O     . HOH D 4 .   ? -7.03983  -26.91560 -35.67426 1.000 17.16865 ? 796 HOH A O     1 
HETATM 4087 O  O     . HOH D 4 .   ? 11.86949  -20.61392 -18.18385 1.000 7.32428  ? 797 HOH A O     1 
HETATM 4088 O  O     . HOH D 4 .   ? 14.27293  16.59473  -30.48903 1.000 26.63907 ? 798 HOH A O     1 
HETATM 4089 O  O     . HOH D 4 .   ? -1.79265  -10.60811 -21.06287 1.000 24.26310 ? 799 HOH A O     1 
HETATM 4090 O  O     . HOH D 4 .   ? 27.25305  21.61906  -23.09546 1.000 14.75002 ? 800 HOH A O     1 
HETATM 4091 O  O     . HOH D 4 .   ? 19.66962  -17.92064 -11.09710 1.000 15.11487 ? 801 HOH A O     1 
HETATM 4092 O  O     . HOH D 4 .   ? 35.81358  -12.25750 -10.69961 1.000 14.73968 ? 802 HOH A O     1 
HETATM 4093 O  O     . HOH D 4 .   ? 15.01703  27.37799  -22.01837 1.000 17.48226 ? 803 HOH A O     1 
HETATM 4094 O  O     . HOH D 4 .   ? 17.44726  -1.08897  -21.54256 1.000 10.58224 ? 804 HOH A O     1 
HETATM 4095 O  O     . HOH D 4 .   ? 23.29635  7.16628   -14.50694 1.000 5.57319  ? 805 HOH A O     1 
HETATM 4096 O  O     . HOH D 4 .   ? 5.24290   -3.16262  -39.64524 1.000 19.91045 ? 806 HOH A O     1 
HETATM 4097 O  O     . HOH D 4 .   ? 23.06360  -15.51560 -10.78624 1.000 12.47912 ? 807 HOH A O     1 
HETATM 4098 O  O     . HOH D 4 .   ? 33.18725  20.22837  -14.18154 1.000 21.68990 ? 808 HOH A O     1 
HETATM 4099 O  O     . HOH D 4 .   ? 15.41068  -10.55551 -5.52123  1.000 14.21010 ? 809 HOH A O     1 
HETATM 4100 O  O     . HOH D 4 .   ? 16.00487  26.50776  -29.81237 1.000 24.00604 ? 810 HOH A O     1 
HETATM 4101 O  O     . HOH D 4 .   ? 28.28860  0.68561   -5.20684  1.000 23.93145 ? 811 HOH A O     1 
HETATM 4102 O  O     . HOH D 4 .   ? 30.14512  14.38109  -22.77630 1.000 14.35407 ? 812 HOH A O     1 
HETATM 4103 O  O     . HOH D 4 .   ? 23.71602  21.64799  -24.43638 1.000 17.45268 ? 813 HOH A O     1 
HETATM 4104 O  O     . HOH D 4 .   ? 6.40374   -28.73969 -9.31149  1.000 21.31393 ? 814 HOH A O     1 
HETATM 4105 O  O     . HOH D 4 .   ? 25.19716  3.13198   -25.05885 1.000 11.32603 ? 815 HOH A O     1 
HETATM 4106 O  O     . HOH D 4 .   ? 32.26217  8.16811   -22.45716 1.000 6.94252  ? 816 HOH A O     1 
HETATM 4107 O  O     . HOH D 4 .   ? 5.95902   -3.24344  -34.05325 1.000 15.04648 ? 817 HOH A O     1 
HETATM 4108 O  O     . HOH D 4 .   ? -2.74210  -12.30479 -43.07279 1.000 26.14125 ? 818 HOH A O     1 
HETATM 4109 O  O     . HOH D 4 .   ? 15.79116  -21.74237 -34.02690 1.000 19.92838 ? 819 HOH A O     1 
HETATM 4110 O  O     . HOH D 4 .   ? 14.08045  29.48261  -1.29742  1.000 22.78560 ? 820 HOH A O     1 
HETATM 4111 O  O     . HOH D 4 .   ? 13.39769  -26.49268 -10.77571 1.000 13.76479 ? 821 HOH A O     1 
HETATM 4112 O  O     . HOH D 4 .   ? 24.95876  -12.86934 -2.53336  1.000 17.41337 ? 822 HOH A O     1 
HETATM 4113 O  O     . HOH D 4 .   ? 24.45565  -0.90537  -3.29472  1.000 11.28781 ? 823 HOH A O     1 
HETATM 4114 O  O     . HOH D 4 .   ? 25.72027  28.49444  -10.12163 1.000 21.84485 ? 824 HOH A O     1 
HETATM 4115 O  O     . HOH D 4 .   ? 10.35816  -0.31818  -26.36643 1.000 21.31204 ? 825 HOH A O     1 
HETATM 4116 O  O     . HOH D 4 .   ? 42.98721  -4.43389  -25.26900 1.000 17.71740 ? 826 HOH A O     1 
HETATM 4117 O  O     . HOH D 4 .   ? 12.80598  28.60392  -23.82636 1.000 25.81554 ? 827 HOH A O     1 
HETATM 4118 O  O     . HOH D 4 .   ? 10.71111  -2.63127  -29.41237 1.000 21.80603 ? 828 HOH A O     1 
HETATM 4119 O  O     . HOH D 4 .   ? 8.00657   -29.23993 -17.62551 1.000 19.19441 ? 829 HOH A O     1 
HETATM 4120 O  O     . HOH D 4 .   ? -5.91968  -11.16919 -22.70376 1.000 22.67337 ? 830 HOH A O     1 
HETATM 4121 O  O     . HOH D 4 .   ? 8.59032   -25.89724 -28.11662 1.000 9.52447  ? 831 HOH A O     1 
HETATM 4122 O  O     . HOH D 4 .   ? 21.39556  -26.37180 -16.71888 1.000 7.91014  ? 832 HOH A O     1 
HETATM 4123 O  O     A HOH D 4 .   ? 31.62854  23.72681  0.80339   0.571 16.48426 ? 833 HOH A O     1 
HETATM 4124 O  O     B HOH D 4 .   ? 5.95556   9.50048   -3.56664  0.429 13.48359 ? 833 HOH A O     1 
HETATM 4125 O  O     . HOH D 4 .   ? 11.64862  8.39760   -1.21273  1.000 13.60950 ? 834 HOH A O     1 
HETATM 4126 O  O     . HOH D 4 .   ? 34.94819  -17.26412 -31.05244 1.000 27.81291 ? 835 HOH A O     1 
HETATM 4127 O  O     . HOH D 4 .   ? 26.26950  -24.58683 -19.12404 1.000 17.27177 ? 836 HOH A O     1 
HETATM 4128 O  O     . HOH D 4 .   ? 15.57397  1.90162   -34.46261 1.000 24.91842 ? 837 HOH A O     1 
HETATM 4129 O  O     . HOH D 4 .   ? -9.45177  -18.37644 -29.78847 1.000 24.83189 ? 838 HOH A O     1 
HETATM 4130 O  O     . HOH D 4 .   ? 35.41864  -13.80343 -8.40156  1.000 15.25419 ? 839 HOH A O     1 
HETATM 4131 O  O     . HOH D 4 .   ? 8.44040   19.16438  -7.60498  1.000 18.15243 ? 840 HOH A O     1 
HETATM 4132 O  O     . HOH D 4 .   ? 40.70719  -9.59799  -28.14280 1.000 23.09237 ? 841 HOH A O     1 
HETATM 4133 O  O     . HOH D 4 .   ? 26.76272  -8.97334  -3.03352  1.000 20.05186 ? 842 HOH A O     1 
HETATM 4134 O  O     . HOH D 4 .   ? 14.36792  4.19757   -35.91566 1.000 14.29596 ? 843 HOH A O     1 
HETATM 4135 O  O     . HOH D 4 .   ? 9.96917   -4.04620  -27.14031 1.000 14.00645 ? 844 HOH A O     1 
HETATM 4136 O  O     . HOH D 4 .   ? -8.74482  -23.74856 -33.96332 1.000 20.34831 ? 845 HOH A O     1 
HETATM 4137 O  O     . HOH D 4 .   ? 12.70428  8.64312   -17.11876 1.000 16.98048 ? 846 HOH A O     1 
HETATM 4138 O  O     . HOH D 4 .   ? 1.60784   -17.14588 -47.44374 1.000 18.06232 ? 847 HOH A O     1 
HETATM 4139 O  O     . HOH D 4 .   ? 35.10351  9.37564   -5.94125  1.000 20.40858 ? 848 HOH A O     1 
HETATM 4140 O  O     . HOH D 4 .   ? 24.48505  -14.02137 -36.56332 1.000 15.41435 ? 849 HOH A O     1 
HETATM 4141 O  O     . HOH D 4 .   ? 17.50671  -4.18837  -1.62047  1.000 22.26204 ? 850 HOH A O     1 
HETATM 4142 O  O     . HOH D 4 .   ? 34.47946  15.05363  -6.08041  1.000 24.31246 ? 851 HOH A O     1 
HETATM 4143 O  O     . HOH D 4 .   ? -0.89401  -9.53361  -37.77992 1.000 24.78990 ? 852 HOH A O     1 
HETATM 4144 O  O     . HOH D 4 .   ? 35.71032  -15.09591 -24.25652 1.000 17.11204 ? 853 HOH A O     1 
HETATM 4145 O  O     . HOH D 4 .   ? 10.91153  26.73567  1.29173   1.000 25.10076 ? 854 HOH A O     1 
HETATM 4146 O  O     . HOH D 4 .   ? -2.98949  -20.33100 -17.06955 1.000 26.44503 ? 855 HOH A O     1 
HETATM 4147 O  O     . HOH D 4 .   ? 16.77590  -20.57472 -46.11596 1.000 21.14968 ? 856 HOH A O     1 
HETATM 4148 O  O     . HOH D 4 .   ? 24.42428  -18.80710 -27.49317 1.000 14.47519 ? 857 HOH A O     1 
HETATM 4149 O  O     . HOH D 4 .   ? 9.83432   0.43406   -18.26845 1.000 20.17946 ? 858 HOH A O     1 
HETATM 4150 O  O     . HOH D 4 .   ? -4.95386  -28.08763 -37.20227 1.000 23.74805 ? 859 HOH A O     1 
HETATM 4151 O  O     . HOH D 4 .   ? 33.99231  9.93135   -15.19425 1.000 21.57375 ? 860 HOH A O     1 
HETATM 4152 O  O     . HOH D 4 .   ? 28.88089  -8.60850  -41.74858 1.000 16.06754 ? 861 HOH A O     1 
HETATM 4153 O  O     . HOH D 4 .   ? 16.26270  -26.39064 -10.11177 1.000 19.06566 ? 862 HOH A O     1 
HETATM 4154 O  O     . HOH D 4 .   ? -0.72070  -31.60441 -31.31625 1.000 18.69022 ? 863 HOH A O     1 
HETATM 4155 O  O     . HOH D 4 .   ? 14.94726  4.90907   -19.40869 1.000 13.88156 ? 864 HOH A O     1 
HETATM 4156 O  O     . HOH D 4 .   ? 4.82566   -0.49850  -2.71731  1.000 21.78489 ? 865 HOH A O     1 
HETATM 4157 O  O     . HOH D 4 .   ? 8.46114   -29.93955 -38.05650 1.000 19.95030 ? 866 HOH A O     1 
HETATM 4158 O  O     . HOH D 4 .   ? 38.76936  -4.36271  -18.24791 1.000 21.19557 ? 867 HOH A O     1 
HETATM 4159 O  O     . HOH D 4 .   ? 22.07040  27.45658  -4.28452  1.000 17.46935 ? 868 HOH A O     1 
HETATM 4160 O  O     . HOH D 4 .   ? 25.88769  -4.76734  -2.82863  1.000 16.94621 ? 869 HOH A O     1 
HETATM 4161 O  O     . HOH D 4 .   ? 11.83266  4.60962   -0.56862  1.000 18.13633 ? 870 HOH A O     1 
HETATM 4162 O  O     . HOH D 4 .   ? 37.88132  -14.25688 -23.64859 1.000 21.07482 ? 871 HOH A O     1 
HETATM 4163 O  O     . HOH D 4 .   ? 7.91522   11.14703  -19.02073 1.000 23.60367 ? 872 HOH A O     1 
HETATM 4164 O  O     . HOH D 4 .   ? 32.35251  -1.10450  -9.69688  1.000 13.86462 ? 873 HOH A O     1 
HETATM 4165 O  O     . HOH D 4 .   ? 24.03055  -25.48679 -17.01296 1.000 15.51141 ? 874 HOH A O     1 
HETATM 4166 O  O     . HOH D 4 .   ? 34.38531  5.71930   -17.00113 1.000 24.72471 ? 875 HOH A O     1 
HETATM 4167 O  O     . HOH D 4 .   ? 9.53967   6.99364   0.75436   1.000 19.50428 ? 876 HOH A O     1 
HETATM 4168 O  O     . HOH D 4 .   ? 34.69151  -1.66950  -10.33191 1.000 20.37134 ? 877 HOH A O     1 
HETATM 4169 O  O     . HOH D 4 .   ? 4.51377   -26.88565 -7.33951  1.000 17.54895 ? 878 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    N N   . GLY A 3   ? 0.35274 0.25282 0.37466 -0.03336 0.01860  -0.03886 3   GLY A N   
2    C CA  . GLY A 3   ? 0.35297 0.25874 0.38150 -0.03956 0.01698  -0.04303 3   GLY A CA  
3    C C   . GLY A 3   ? 0.35636 0.27566 0.38479 -0.03942 0.01063  -0.04415 3   GLY A C   
4    O O   . GLY A 3   ? 0.33454 0.26080 0.36770 -0.04378 0.00760  -0.04866 3   GLY A O   
5    N N   . VAL A 4   ? 0.36062 0.28399 0.38381 -0.03425 0.00849  -0.03996 4   VAL A N   
6    C CA  . VAL A 4   ? 0.29823 0.23302 0.32042 -0.03346 0.00303  -0.04021 4   VAL A CA  
7    C C   . VAL A 4   ? 0.29527 0.23320 0.31496 -0.02900 0.00284  -0.03366 4   VAL A C   
8    O O   . VAL A 4   ? 0.28707 0.21884 0.30457 -0.02596 0.00619  -0.02939 4   VAL A O   
9    C CB  . VAL A 4   ? 0.27687 0.21356 0.29358 -0.03242 -0.00020 -0.04426 4   VAL A CB  
10   C CG1 . VAL A 4   ? 0.24713 0.17977 0.26544 -0.03689 0.00019  -0.05127 4   VAL A CG1 
11   C CG2 . VAL A 4   ? 0.30674 0.23873 0.31723 -0.02723 0.00161  -0.04118 4   VAL A CG2 
12   N N   . LYS A 5   ? 0.25125 0.19864 0.27108 -0.02845 -0.00117 -0.03292 5   LYS A N   
13   C CA  . LYS A 5   ? 0.18698 0.13786 0.20472 -0.02485 -0.00160 -0.02750 5   LYS A CA  
14   C C   . LYS A 5   ? 0.21225 0.16545 0.22378 -0.02116 -0.00398 -0.02684 5   LYS A C   
15   O O   . LYS A 5   ? 0.19188 0.15054 0.20181 -0.02157 -0.00757 -0.02935 5   LYS A O   
16   C CB  . LYS A 5   ? 0.20943 0.16842 0.23166 -0.02644 -0.00375 -0.02691 5   LYS A CB  
17   C CG  . LYS A 5   ? 0.20596 0.16855 0.22557 -0.02295 -0.00439 -0.02208 5   LYS A CG  
18   C CD  . LYS A 5   ? 0.17075 0.14118 0.19480 -0.02414 -0.00642 -0.02188 5   LYS A CD  
19   C CE  . LYS A 5   ? 0.14904 0.12222 0.16988 -0.02079 -0.00691 -0.01767 5   LYS A CE  
20   N NZ  . LYS A 5   ? 0.15839 0.13857 0.18352 -0.02142 -0.00847 -0.01740 5   LYS A NZ  
21   N N   . ASN A 6   ? 0.16274 0.11195 0.17084 -0.01751 -0.00190 -0.02338 6   ASN A N   
22   C CA  . ASN A 6   ? 0.15468 0.10666 0.15804 -0.01402 -0.00348 -0.02211 6   ASN A CA  
23   C C   . ASN A 6   ? 0.14911 0.10408 0.15193 -0.01152 -0.00355 -0.01722 6   ASN A C   
24   O O   . ASN A 6   ? 0.13428 0.08525 0.13723 -0.00991 -0.00105 -0.01405 6   ASN A O   
25   C CB  . ASN A 6   ? 0.18181 0.12771 0.18242 -0.01171 -0.00120 -0.02286 6   ASN A CB  
26   C CG  . ASN A 6   ? 0.19047 0.13313 0.19057 -0.01415 -0.00108 -0.02833 6   ASN A CG  
27   O OD1 . ASN A 6   ? 0.21190 0.15911 0.21141 -0.01647 -0.00405 -0.03167 6   ASN A OD1 
28   N ND2 . ASN A 6   ? 0.20944 0.14398 0.20940 -0.01345 0.00230  -0.02936 6   ASN A ND2 
29   N N   . SER A 7   ? 0.15064 0.11220 0.15239 -0.01115 -0.00634 -0.01665 7   SER A N   
30   C CA  . SER A 7   ? 0.15344 0.11812 0.15484 -0.00950 -0.00660 -0.01284 7   SER A CA  
31   C C   . SER A 7   ? 0.11067 0.07820 0.10852 -0.00684 -0.00775 -0.01170 7   SER A C   
32   O O   . SER A 7   ? 0.10739 0.07586 0.10309 -0.00661 -0.00871 -0.01382 7   SER A O   
33   C CB  . SER A 7   ? 0.14573 0.11539 0.14983 -0.01145 -0.00831 -0.01296 7   SER A CB  
34   O OG  . SER A 7   ? 0.14034 0.11420 0.14342 -0.01207 -0.01127 -0.01533 7   SER A OG  
35   N N   . ILE A 8   ? 0.10385 0.07278 0.10102 -0.00501 -0.00744 -0.00848 8   ILE A N   
36   C CA  . ILE A 8   ? 0.10046 0.07294 0.09540 -0.00307 -0.00846 -0.00742 8   ILE A CA  
37   C C   . ILE A 8   ? 0.09601 0.07230 0.09097 -0.00356 -0.00961 -0.00587 8   ILE A C   
38   O O   . ILE A 8   ? 0.09949 0.07506 0.09528 -0.00367 -0.00880 -0.00407 8   ILE A O   
39   C CB  . ILE A 8   ? 0.12960 0.10059 0.12387 -0.00013 -0.00722 -0.00547 8   ILE A CB  
40   C CG1 . ILE A 8   ? 0.12691 0.09387 0.12123 0.00091  -0.00574 -0.00712 8   ILE A CG1 
41   C CG2 . ILE A 8   ? 0.10626 0.08220 0.09952 0.00126  -0.00839 -0.00459 8   ILE A CG2 
42   C CD1 . ILE A 8   ? 0.17220 0.13850 0.16648 0.00453  -0.00474 -0.00516 8   ILE A CD1 
43   N N   . ILE A 9   ? 0.09973 0.07941 0.09339 -0.00380 -0.01108 -0.00654 9   ILE A N   
44   C CA  . ILE A 9   ? 0.11052 0.09312 0.10385 -0.00395 -0.01185 -0.00522 9   ILE A CA  
45   C C   . ILE A 9   ? 0.09640 0.08085 0.08819 -0.00261 -0.01177 -0.00437 9   ILE A C   
46   O O   . ILE A 9   ? 0.08909 0.07474 0.07971 -0.00246 -0.01194 -0.00532 9   ILE A O   
47   C CB  . ILE A 9   ? 0.09477 0.07928 0.08789 -0.00507 -0.01336 -0.00628 9   ILE A CB  
48   C CG1 . ILE A 9   ? 0.09804 0.08459 0.09023 -0.00479 -0.01367 -0.00495 9   ILE A CG1 
49   C CG2 . ILE A 9   ? 0.09325 0.07758 0.08413 -0.00511 -0.01405 -0.00816 9   ILE A CG2 
50   C CD1 . ILE A 9   ? 0.10604 0.09270 0.09982 -0.00489 -0.01292 -0.00360 9   ILE A CD1 
51   N N   . TRP A 10  ? 0.09937 0.08430 0.09115 -0.00173 -0.01142 -0.00272 10  TRP A N   
52   C CA  . TRP A 10  ? 0.08732 0.07493 0.07856 -0.00054 -0.01170 -0.00224 10  TRP A CA  
53   C C   . TRP A 10  ? 0.09134 0.08136 0.08185 -0.00168 -0.01225 -0.00234 10  TRP A C   
54   O O   . TRP A 10  ? 0.08721 0.07689 0.07714 -0.00215 -0.01224 -0.00161 10  TRP A O   
55   C CB  . TRP A 10  ? 0.09599 0.08302 0.08692 0.00132  -0.01149 -0.00050 10  TRP A CB  
56   C CG  . TRP A 10  ? 0.10461 0.09566 0.09564 0.00271  -0.01242 -0.00023 10  TRP A CG  
57   C CD1 . TRP A 10  ? 0.10938 0.10409 0.10184 0.00242  -0.01276 -0.00161 10  TRP A CD1 
58   C CD2 . TRP A 10  ? 0.11870 0.11103 0.10849 0.00452  -0.01319 0.00139  10  TRP A CD2 
59   N NE1 . TRP A 10  ? 0.11535 0.11427 0.10865 0.00371  -0.01386 -0.00128 10  TRP A NE1 
60   C CE2 . TRP A 10  ? 0.10157 0.09925 0.09287 0.00520  -0.01448 0.00056  10  TRP A CE2 
61   C CE3 . TRP A 10  ? 0.10003 0.08959 0.08733 0.00565  -0.01282 0.00351  10  TRP A CE3 
62   C CZ2 . TRP A 10  ? 0.12658 0.12763 0.11712 0.00709  -0.01610 0.00153  10  TRP A CZ2 
63   C CZ3 . TRP A 10  ? 0.12036 0.11237 0.10569 0.00777  -0.01416 0.00487  10  TRP A CZ3 
64   C CH2 . TRP A 10  ? 0.15622 0.15428 0.14323 0.00854  -0.01613 0.00376  10  TRP A CH2 
65   N N   . PHE A 11  ? 0.09400 0.08595 0.08444 -0.00218 -0.01226 -0.00330 11  PHE A N   
66   C CA  . PHE A 11  ? 0.08710 0.08038 0.07690 -0.00347 -0.01226 -0.00352 11  PHE A CA  
67   C C   . PHE A 11  ? 0.08561 0.08222 0.07626 -0.00332 -0.01261 -0.00373 11  PHE A C   
68   O O   . PHE A 11  ? 0.09954 0.09878 0.09187 -0.00240 -0.01269 -0.00413 11  PHE A O   
69   C CB  . PHE A 11  ? 0.08360 0.07657 0.07252 -0.00434 -0.01161 -0.00425 11  PHE A CB  
70   C CG  . PHE A 11  ? 0.08856 0.07906 0.07600 -0.00449 -0.01198 -0.00414 11  PHE A CG  
71   C CD1 . PHE A 11  ? 0.08444 0.07385 0.07122 -0.00494 -0.01226 -0.00351 11  PHE A CD1 
72   C CD2 . PHE A 11  ? 0.11242 0.10193 0.09929 -0.00403 -0.01218 -0.00490 11  PHE A CD2 
73   C CE1 . PHE A 11  ? 0.09559 0.08390 0.08164 -0.00470 -0.01313 -0.00341 11  PHE A CE1 
74   C CE2 . PHE A 11  ? 0.09906 0.08728 0.08468 -0.00425 -0.01313 -0.00520 11  PHE A CE2 
75   C CZ  . PHE A 11  ? 0.10611 0.09420 0.09157 -0.00446 -0.01382 -0.00434 11  PHE A CZ  
76   N N   . ARG A 12  ? 0.08307 0.07989 0.07275 -0.00413 -0.01288 -0.00370 12  ARG A N   
77   C CA  . ARG A 12  ? 0.10647 0.10684 0.09667 -0.00466 -0.01355 -0.00463 12  ARG A CA  
78   C C   . ARG A 12  ? 0.08404 0.08328 0.07344 -0.00689 -0.01271 -0.00568 12  ARG A C   
79   O O   . ARG A 12  ? 0.08475 0.08533 0.07551 -0.00846 -0.01197 -0.00688 12  ARG A O   
80   C CB  . ARG A 12  ? 0.10395 0.10519 0.09261 -0.00322 -0.01474 -0.00379 12  ARG A CB  
81   C CG  . ARG A 12  ? 0.10777 0.10844 0.09664 -0.00068 -0.01509 -0.00217 12  ARG A CG  
82   C CD  . ARG A 12  ? 0.11049 0.10634 0.09795 -0.00040 -0.01397 -0.00079 12  ARG A CD  
83   N NE  . ARG A 12  ? 0.11205 0.10650 0.09694 -0.00093 -0.01360 -0.00030 12  ARG A NE  
84   C CZ  . ARG A 12  ? 0.13993 0.13386 0.12206 0.00047  -0.01377 0.00110  12  ARG A CZ  
85   N NH1 . ARG A 12  ? 0.12641 0.12098 0.10808 0.00280  -0.01455 0.00247  12  ARG A NH1 
86   N NH2 . ARG A 12  ? 0.12660 0.11905 0.10598 -0.00018 -0.01292 0.00126  12  ARG A NH2 
87   N N   . LYS A 13  ? 0.09785 0.09424 0.08525 -0.00701 -0.01238 -0.00523 13  LYS A N   
88   C CA  . LYS A 13  ? 0.08646 0.07996 0.07301 -0.00840 -0.01110 -0.00571 13  LYS A CA  
89   C C   . LYS A 13  ? 0.09746 0.08805 0.08394 -0.00749 -0.01064 -0.00434 13  LYS A C   
90   O O   . LYS A 13  ? 0.10191 0.09298 0.08912 -0.00655 -0.01122 -0.00369 13  LYS A O   
91   C CB  . LYS A 13  ? 0.12759 0.12023 0.11224 -0.00887 -0.01088 -0.00648 13  LYS A CB  
92   C CG  . LYS A 13  ? 0.11200 0.10814 0.09631 -0.00995 -0.01192 -0.00836 13  LYS A CG  
93   C CD  . LYS A 13  ? 0.13019 0.12496 0.11140 -0.01037 -0.01163 -0.00941 13  LYS A CD  
94   C CE  . LYS A 13  ? 0.16989 0.16893 0.15025 -0.01138 -0.01339 -0.01162 13  LYS A CE  
95   N NZ  . LYS A 13  ? 0.16033 0.15781 0.13640 -0.01173 -0.01313 -0.01294 13  LYS A NZ  
96   N N   . GLY A 14  ? 0.09496 0.08273 0.08073 -0.00765 -0.00971 -0.00410 14  GLY A N   
97   C CA  . GLY A 14  ? 0.08605 0.07221 0.07225 -0.00653 -0.00983 -0.00291 14  GLY A CA  
98   C C   . GLY A 14  ? 0.09668 0.08276 0.08239 -0.00639 -0.01021 -0.00254 14  GLY A C   
99   O O   . GLY A 14  ? 0.08562 0.07209 0.07175 -0.00549 -0.01124 -0.00209 14  GLY A O   
100  N N   . LEU A 15  ? 0.08784 0.07337 0.07252 -0.00750 -0.00919 -0.00295 15  LEU A N   
101  C CA  . LEU A 15  ? 0.08916 0.07430 0.07248 -0.00742 -0.00890 -0.00257 15  LEU A CA  
102  C C   . LEU A 15  ? 0.09210 0.07419 0.07309 -0.00629 -0.00894 -0.00112 15  LEU A C   
103  O O   . LEU A 15  ? 0.09584 0.07498 0.07458 -0.00666 -0.00736 -0.00036 15  LEU A O   
104  C CB  . LEU A 15  ? 0.09665 0.08225 0.08009 -0.00921 -0.00714 -0.00342 15  LEU A CB  
105  C CG  . LEU A 15  ? 0.08826 0.07813 0.07456 -0.01002 -0.00761 -0.00495 15  LEU A CG  
106  C CD1 . LEU A 15  ? 0.08998 0.08117 0.07769 -0.01223 -0.00583 -0.00620 15  LEU A CD1 
107  C CD2 . LEU A 15  ? 0.08803 0.08043 0.07534 -0.00857 -0.00879 -0.00492 15  LEU A CD2 
108  N N   . ARG A 16  ? 0.09114 0.07398 0.07276 -0.00486 -0.01072 -0.00068 16  ARG A N   
109  C CA  . ARG A 16  ? 0.10071 0.08192 0.08073 -0.00326 -0.01153 0.00067  16  ARG A CA  
110  C C   . ARG A 16  ? 0.09758 0.08144 0.07908 -0.00234 -0.01396 0.00024  16  ARG A C   
111  O O   . ARG A 16  ? 0.08965 0.07557 0.07378 -0.00303 -0.01441 -0.00091 16  ARG A O   
112  C CB  . ARG A 16  ? 0.10735 0.08656 0.08842 -0.00253 -0.01070 0.00148  16  ARG A CB  
113  C CG  . ARG A 16  ? 0.11727 0.09866 0.10213 -0.00249 -0.01109 0.00069  16  ARG A CG  
114  C CD  . ARG A 16  ? 0.09606 0.07519 0.08176 -0.00173 -0.00964 0.00112  16  ARG A CD  
115  N NE  . ARG A 16  ? 0.09129 0.07253 0.08026 -0.00159 -0.00955 0.00044  16  ARG A NE  
116  C CZ  . ARG A 16  ? 0.09007 0.07152 0.07901 -0.00292 -0.00843 -0.00068 16  ARG A CZ  
117  N NH1 . ARG A 16  ? 0.10551 0.08611 0.09223 -0.00454 -0.00780 -0.00158 16  ARG A NH1 
118  N NH2 . ARG A 16  ? 0.09667 0.07955 0.08787 -0.00261 -0.00792 -0.00093 16  ARG A NH2 
119  N N   . LEU A 17  ? 0.10245 0.08614 0.08217 -0.00076 -0.01552 0.00115  17  LEU A N   
120  C CA  . LEU A 17  ? 0.11969 0.10657 0.10148 -0.00010 -0.01821 0.00031  17  LEU A CA  
121  C C   . LEU A 17  ? 0.10968 0.09841 0.09552 0.00129  -0.01924 0.00095  17  LEU A C   
122  O O   . LEU A 17  ? 0.10810 0.10029 0.09834 0.00093  -0.02065 -0.00028 17  LEU A O   
123  C CB  . LEU A 17  ? 0.12385 0.11064 0.10091 0.00084  -0.02000 0.00040  17  LEU A CB  
124  C CG  . LEU A 17  ? 0.12763 0.11460 0.10248 -0.00048 -0.01994 -0.00146 17  LEU A CG  
125  C CD1 . LEU A 17  ? 0.12358 0.10834 0.09698 -0.00166 -0.01689 -0.00134 17  LEU A CD1 
126  C CD2 . LEU A 17  ? 0.17361 0.16054 0.14297 0.00063  -0.02191 -0.00161 17  LEU A CD2 
127  N N   . HIS A 18  ? 0.09745 0.08381 0.08236 0.00283  -0.01821 0.00273  18  HIS A N   
128  C CA  . HIS A 18  ? 0.12107 0.10916 0.11034 0.00459  -0.01867 0.00335  18  HIS A CA  
129  C C   . HIS A 18  ? 0.11002 0.09842 0.10329 0.00322  -0.01648 0.00238  18  HIS A C   
130  O O   . HIS A 18  ? 0.11184 0.09761 0.10318 0.00163  -0.01434 0.00199  18  HIS A O   
131  C CB  . HIS A 18  ? 0.12138 0.10571 0.10785 0.00711  -0.01786 0.00572  18  HIS A CB  
132  C CG  . HIS A 18  ? 0.10625 0.08531 0.09053 0.00596  -0.01430 0.00606  18  HIS A CG  
133  N ND1 . HIS A 18  ? 0.12265 0.09795 0.10200 0.00453  -0.01273 0.00640  18  HIS A ND1 
134  C CD2 . HIS A 18  ? 0.10847 0.08561 0.09499 0.00576  -0.01191 0.00572  18  HIS A CD2 
135  C CE1 . HIS A 18  ? 0.10648 0.07813 0.08569 0.00327  -0.00979 0.00609  18  HIS A CE1 
136  N NE2 . HIS A 18  ? 0.10501 0.07744 0.08803 0.00403  -0.00933 0.00560  18  HIS A NE2 
137  N N   . ASP A 19  ? 0.09185 0.08386 0.09071 0.00385  -0.01701 0.00192  19  ASP A N   
138  C CA  . ASP A 19  ? 0.11054 0.10286 0.11280 0.00283  -0.01461 0.00119  19  ASP A CA  
139  C C   . ASP A 19  ? 0.09434 0.08566 0.09477 0.00031  -0.01360 0.00017  19  ASP A C   
140  O O   . ASP A 19  ? 0.08674 0.07558 0.08507 -0.00051 -0.01154 0.00005  19  ASP A O   
141  C CB  . ASP A 19  ? 0.11653 0.10527 0.11775 0.00403  -0.01208 0.00198  19  ASP A CB  
142  C CG  . ASP A 19  ? 0.11299 0.10235 0.11740 0.00348  -0.00956 0.00116  19  ASP A CG  
143  O OD1 . ASP A 19  ? 0.11162 0.10455 0.11998 0.00257  -0.00973 0.00045  19  ASP A OD1 
144  O OD2 . ASP A 19  ? 0.12092 0.10679 0.12355 0.00380  -0.00710 0.00109  19  ASP A OD2 
145  N N   . ASN A 20  ? 0.08567 0.07899 0.08684 -0.00075 -0.01525 -0.00070 20  ASN A N   
146  C CA  . ASN A 20  ? 0.09901 0.09134 0.09884 -0.00252 -0.01447 -0.00143 20  ASN A CA  
147  C C   . ASN A 20  ? 0.09587 0.09048 0.10028 -0.00359 -0.01450 -0.00233 20  ASN A C   
148  O O   . ASN A 20  ? 0.08363 0.07951 0.08899 -0.00432 -0.01617 -0.00345 20  ASN A O   
149  C CB  . ASN A 20  ? 0.09942 0.09065 0.09531 -0.00286 -0.01562 -0.00176 20  ASN A CB  
150  C CG  . ASN A 20  ? 0.11943 0.10915 0.11337 -0.00386 -0.01436 -0.00202 20  ASN A CG  
151  O OD1 . ASN A 20  ? 0.15428 0.14285 0.14514 -0.00395 -0.01408 -0.00194 20  ASN A OD1 
152  N ND2 . ASN A 20  ? 0.09868 0.08855 0.09461 -0.00449 -0.01346 -0.00219 20  ASN A ND2 
153  N N   . PRO A 21  ? 0.08382 0.07866 0.09100 -0.00391 -0.01234 -0.00204 21  PRO A N   
154  C CA  . PRO A 21  ? 0.13438 0.13078 0.14617 -0.00534 -0.01156 -0.00277 21  PRO A CA  
155  C C   . PRO A 21  ? 0.11383 0.10777 0.12360 -0.00665 -0.01120 -0.00310 21  PRO A C   
156  O O   . PRO A 21  ? 0.10754 0.10211 0.12083 -0.00812 -0.01110 -0.00414 21  PRO A O   
157  C CB  . PRO A 21  ? 0.13635 0.13244 0.14981 -0.00521 -0.00845 -0.00199 21  PRO A CB  
158  C CG  . PRO A 21  ? 0.13478 0.12806 0.14281 -0.00415 -0.00770 -0.00118 21  PRO A CG  
159  C CD  . PRO A 21  ? 0.09813 0.09146 0.10413 -0.00315 -0.01014 -0.00125 21  PRO A CD  
160  N N   . ALA A 22  ? 0.12911 0.12034 0.13378 -0.00614 -0.01092 -0.00238 22  ALA A N   
161  C CA  . ALA A 22  ? 0.11063 0.09959 0.11357 -0.00666 -0.01067 -0.00251 22  ALA A CA  
162  C C   . ALA A 22  ? 0.12323 0.11270 0.12625 -0.00706 -0.01273 -0.00410 22  ALA A C   
163  O O   . ALA A 22  ? 0.11491 0.10282 0.11890 -0.00797 -0.01239 -0.00502 22  ALA A O   
164  C CB  . ALA A 22  ? 0.10538 0.09266 0.10373 -0.00567 -0.01019 -0.00146 22  ALA A CB  
165  N N   . LEU A 23  ? 0.10907 0.10009 0.11050 -0.00633 -0.01461 -0.00445 23  LEU A N   
166  C CA  . LEU A 23  ? 0.11633 0.10782 0.11659 -0.00656 -0.01657 -0.00603 23  LEU A CA  
167  C C   . LEU A 23  ? 0.11717 0.11117 0.12181 -0.00774 -0.01801 -0.00779 23  LEU A C   
168  O O   . LEU A 23  ? 0.10956 0.10310 0.11417 -0.00881 -0.01890 -0.00982 23  LEU A O   
169  C CB  . LEU A 23  ? 0.10206 0.09402 0.09855 -0.00531 -0.01783 -0.00545 23  LEU A CB  
170  C CG  . LEU A 23  ? 0.11279 0.10535 0.10668 -0.00519 -0.01994 -0.00684 23  LEU A CG  
171  C CD1 . LEU A 23  ? 0.12715 0.11757 0.11899 -0.00587 -0.01921 -0.00826 23  LEU A CD1 
172  C CD2 . LEU A 23  ? 0.11924 0.11139 0.10882 -0.00373 -0.02051 -0.00547 23  LEU A CD2 
173  N N   . LEU A 24  ? 0.08897 0.08592 0.09782 -0.00762 -0.01817 -0.00737 24  LEU A N   
174  C CA  . LEU A 24  ? 0.10896 0.10981 0.12339 -0.00885 -0.01978 -0.00932 24  LEU A CA  
175  C C   . LEU A 24  ? 0.12382 0.12312 0.14194 -0.01137 -0.01787 -0.01070 24  LEU A C   
176  O O   . LEU A 24  ? 0.14365 0.14422 0.16419 -0.01315 -0.01932 -0.01337 24  LEU A O   
177  C CB  . LEU A 24  ? 0.08566 0.09049 0.10478 -0.00780 -0.01990 -0.00841 24  LEU A CB  
178  C CG  . LEU A 24  ? 0.11285 0.11848 0.12877 -0.00504 -0.02151 -0.00683 24  LEU A CG  
179  C CD1 . LEU A 24  ? 0.11412 0.12325 0.13545 -0.00368 -0.02104 -0.00597 24  LEU A CD1 
180  C CD2 . LEU A 24  ? 0.11226 0.11964 0.12525 -0.00428 -0.02523 -0.00787 24  LEU A CD2 
181  N N   . GLU A 25  ? 0.12609 0.12225 0.14424 -0.01158 -0.01450 -0.00898 25  GLU A N   
182  C CA  . GLU A 25  ? 0.12542 0.11865 0.14621 -0.01372 -0.01199 -0.00962 25  GLU A CA  
183  C C   . GLU A 25  ? 0.16345 0.15268 0.18076 -0.01415 -0.01232 -0.01089 25  GLU A C   
184  O O   . GLU A 25  ? 0.12227 0.10967 0.14246 -0.01636 -0.01146 -0.01286 25  GLU A O   
185  C CB  . GLU A 25  ? 0.17510 0.16519 0.19469 -0.01318 -0.00836 -0.00690 25  GLU A CB  
186  C CG  . GLU A 25  ? 0.18331 0.16893 0.20440 -0.01496 -0.00509 -0.00667 25  GLU A CG  
187  C CD  . GLU A 25  ? 0.15367 0.14181 0.18263 -0.01792 -0.00396 -0.00858 25  GLU A CD  
188  O OE1 . GLU A 25  ? 0.16479 0.15853 0.19836 -0.01801 -0.00479 -0.00911 25  GLU A OE1 
189  O OE2 . GLU A 25  ? 0.19409 0.17865 0.22511 -0.02016 -0.00209 -0.00968 25  GLU A OE2 
190  N N   . ALA A 26  ? 0.15757 0.14527 0.16908 -0.01215 -0.01322 -0.01001 26  ALA A N   
191  C CA  . ALA A 26  ? 0.12970 0.11386 0.13805 -0.01208 -0.01319 -0.01124 26  ALA A CA  
192  C C   . ALA A 26  ? 0.14497 0.13078 0.15377 -0.01343 -0.01567 -0.01469 26  ALA A C   
193  O O   . ALA A 26  ? 0.13737 0.11973 0.14509 -0.01424 -0.01504 -0.01667 26  ALA A O   
194  C CB  . ALA A 26  ? 0.09663 0.07993 0.09968 -0.00971 -0.01333 -0.00961 26  ALA A CB  
195  N N   . CYS A 27  ? 0.14306 0.13392 0.15318 -0.01349 -0.01850 -0.01553 27  CYS A N   
196  C CA  . CYS A 27  ? 0.15831 0.15147 0.16775 -0.01443 -0.02156 -0.01880 27  CYS A CA  
197  C C   . CYS A 27  ? 0.16476 0.16090 0.18101 -0.01734 -0.02251 -0.02178 27  CYS A C   
198  O O   . CYS A 27  ? 0.15198 0.14915 0.16782 -0.01884 -0.02475 -0.02539 27  CYS A O   
199  C CB  . CYS A 27  ? 0.13486 0.13189 0.14097 -0.01233 -0.02456 -0.01785 27  CYS A CB  
200  S SG  . CYS A 27  ? 0.15437 0.14810 0.15236 -0.00975 -0.02356 -0.01546 27  CYS A SG  
201  N N   . LYS A 28  ? 0.18816 0.18595 0.21070 -0.01836 -0.02075 -0.02067 28  LYS A N   
202  C CA  . LYS A 28  ? 0.20243 0.20408 0.23289 -0.02148 -0.02138 -0.02365 28  LYS A CA  
203  C C   . LYS A 28  ? 0.17466 0.17108 0.20637 -0.02459 -0.01918 -0.02642 28  LYS A C   
204  O O   . LYS A 28  ? 0.17435 0.16418 0.20448 -0.02452 -0.01521 -0.02447 28  LYS A O   
205  C CB  . LYS A 28  ? 0.18422 0.18859 0.22121 -0.02180 -0.01908 -0.02162 28  LYS A CB  
206  C CG  . LYS A 28  ? 0.24062 0.24972 0.28730 -0.02538 -0.01915 -0.02478 28  LYS A CG  
207  C CD  . LYS A 28  ? 0.22946 0.24018 0.28253 -0.02592 -0.01551 -0.02269 28  LYS A CD  
208  C CE  . LYS A 28  ? 0.24063 0.25635 0.30447 -0.03003 -0.01502 -0.02613 28  LYS A CE  
209  N NZ  . LYS A 28  ? 0.24065 0.25791 0.31098 -0.03072 -0.01067 -0.02415 28  LYS A NZ  
210  N N   . ASP A 29  ? 0.20557 0.20475 0.23991 -0.02721 -0.02183 -0.03103 29  ASP A N   
211  C CA  . ASP A 29  ? 0.22531 0.21923 0.26107 -0.03063 -0.01987 -0.03460 29  ASP A CA  
212  C C   . ASP A 29  ? 0.25459 0.23998 0.28257 -0.02882 -0.01754 -0.03352 29  ASP A C   
213  O O   . ASP A 29  ? 0.27590 0.25426 0.30462 -0.03047 -0.01393 -0.03428 29  ASP A O   
214  C CB  . ASP A 29  ? 0.28267 0.27488 0.32656 -0.03386 -0.01572 -0.03448 29  ASP A CB  
215  C CG  . ASP A 29  ? 0.29773 0.29898 0.35126 -0.03666 -0.01789 -0.03715 29  ASP A CG  
216  O OD1 . ASP A 29  ? 0.34950 0.35637 0.40447 -0.03806 -0.02247 -0.04150 29  ASP A OD1 
217  O OD2 . ASP A 29  ? 0.33841 0.34155 0.39808 -0.03734 -0.01505 -0.03500 29  ASP A OD2 
218  N N   . ALA A 30  ? 0.18955 0.17544 0.21038 -0.02534 -0.01934 -0.03169 30  ALA A N   
219  C CA  . ALA A 30  ? 0.18561 0.16490 0.19992 -0.02311 -0.01713 -0.03032 30  ALA A CA  
220  C C   . ALA A 30  ? 0.18522 0.16273 0.19505 -0.02378 -0.01868 -0.03462 30  ALA A C   
221  O O   . ALA A 30  ? 0.19857 0.18109 0.20608 -0.02381 -0.02260 -0.03678 30  ALA A O   
222  C CB  . ALA A 30  ? 0.16979 0.15064 0.17949 -0.01934 -0.01752 -0.02609 30  ALA A CB  
223  N N   . LYS A 31  ? 0.22311 0.19318 0.23130 -0.02403 -0.01549 -0.03578 31  LYS A N   
224  C CA  . LYS A 31  ? 0.19948 0.16673 0.20250 -0.02422 -0.01610 -0.03983 31  LYS A CA  
225  C C   . LYS A 31  ? 0.19501 0.16240 0.19090 -0.02037 -0.01626 -0.03756 31  LYS A C   
226  O O   . LYS A 31  ? 0.18039 0.15020 0.17101 -0.01996 -0.01876 -0.03975 31  LYS A O   
227  C CB  . LYS A 31  ? 0.21769 0.17623 0.22207 -0.02570 -0.01207 -0.04198 31  LYS A CB  
228  C CG  . LYS A 31  ? 0.27947 0.23587 0.28251 -0.02874 -0.01305 -0.04858 31  LYS A CG  
229  C CD  . LYS A 31  ? 0.28379 0.23985 0.27848 -0.02641 -0.01418 -0.05032 31  LYS A CD  
230  C CE  . LYS A 31  ? 0.32850 0.28144 0.32096 -0.02942 -0.01472 -0.05729 31  LYS A CE  
231  N NZ  . LYS A 31  ? 0.39759 0.35705 0.39366 -0.03344 -0.01912 -0.06134 31  LYS A NZ  
232  N N   . HIS A 32  ? 0.18852 0.15357 0.18411 -0.01761 -0.01358 -0.03320 32  HIS A N   
233  C CA  . HIS A 32  ? 0.16923 0.13504 0.15967 -0.01429 -0.01328 -0.03092 32  HIS A CA  
234  C C   . HIS A 32  ? 0.14715 0.11559 0.13936 -0.01240 -0.01292 -0.02591 32  HIS A C   
235  O O   . HIS A 32  ? 0.14633 0.11279 0.14235 -0.01249 -0.01113 -0.02377 32  HIS A O   
236  C CB  . HIS A 32  ? 0.19352 0.15329 0.18165 -0.01260 -0.00998 -0.03180 32  HIS A CB  
237  C CG  . HIS A 32  ? 0.19092 0.14717 0.17647 -0.01435 -0.00980 -0.03717 32  HIS A CG  
238  N ND1 . HIS A 32  ? 0.23755 0.18651 0.22443 -0.01477 -0.00659 -0.03930 32  HIS A ND1 
239  C CD2 . HIS A 32  ? 0.20478 0.16339 0.18589 -0.01567 -0.01240 -0.04095 32  HIS A CD2 
240  C CE1 . HIS A 32  ? 0.23188 0.17883 0.21553 -0.01661 -0.00710 -0.04463 32  HIS A CE1 
241  N NE2 . HIS A 32  ? 0.24958 0.20261 0.22941 -0.01718 -0.01081 -0.04574 32  HIS A NE2 
242  N N   . VAL A 33  ? 0.13753 0.10996 0.12648 -0.01079 -0.01442 -0.02415 33  VAL A N   
243  C CA  . VAL A 33  ? 0.13549 0.11037 0.12545 -0.00919 -0.01416 -0.02004 33  VAL A CA  
244  C C   . VAL A 33  ? 0.11074 0.08538 0.09738 -0.00682 -0.01274 -0.01871 33  VAL A C   
245  O O   . VAL A 33  ? 0.12355 0.09845 0.10602 -0.00644 -0.01296 -0.02031 33  VAL A O   
246  C CB  . VAL A 33  ? 0.13247 0.11229 0.12264 -0.00965 -0.01689 -0.01908 33  VAL A CB  
247  C CG1 . VAL A 33  ? 0.10064 0.08213 0.09151 -0.00819 -0.01623 -0.01535 33  VAL A CG1 
248  C CG2 . VAL A 33  ? 0.12033 0.10173 0.11519 -0.01198 -0.01831 -0.02070 33  VAL A CG2 
249  N N   . TYR A 34  ? 0.10548 0.07994 0.09396 -0.00525 -0.01123 -0.01588 34  TYR A N   
250  C CA  . TYR A 34  ? 0.10731 0.08270 0.09439 -0.00311 -0.00991 -0.01469 34  TYR A CA  
251  C C   . TYR A 34  ? 0.09931 0.07847 0.08683 -0.00272 -0.01067 -0.01197 34  TYR A C   
252  O O   . TYR A 34  ? 0.09705 0.07658 0.08678 -0.00199 -0.01033 -0.00988 34  TYR A O   
253  C CB  . TYR A 34  ? 0.10670 0.07900 0.09574 -0.00123 -0.00775 -0.01411 34  TYR A CB  
254  C CG  . TYR A 34  ? 0.12996 0.09747 0.11836 -0.00137 -0.00628 -0.01706 34  TYR A CG  
255  C CD1 . TYR A 34  ? 0.11751 0.08097 0.10752 -0.00315 -0.00603 -0.01838 34  TYR A CD1 
256  C CD2 . TYR A 34  ? 0.14130 0.10812 0.12774 0.00008  -0.00473 -0.01880 34  TYR A CD2 
257  C CE1 . TYR A 34  ? 0.13307 0.09143 0.12249 -0.00363 -0.00447 -0.02157 34  TYR A CE1 
258  C CE2 . TYR A 34  ? 0.14358 0.10538 0.12908 -0.00000 -0.00307 -0.02191 34  TYR A CE2 
259  C CZ  . TYR A 34  ? 0.15755 0.11488 0.14441 -0.00194 -0.00304 -0.02339 34  TYR A CZ  
260  O OH  . TYR A 34  ? 0.14630 0.09795 0.13221 -0.00237 -0.00118 -0.02695 34  TYR A OH  
261  N N   . PRO A 35  ? 0.11903 0.10056 0.10399 -0.00319 -0.01155 -0.01195 35  PRO A N   
262  C CA  . PRO A 35  ? 0.11081 0.09508 0.09611 -0.00295 -0.01166 -0.00977 35  PRO A CA  
263  C C   . PRO A 35  ? 0.10744 0.09323 0.09386 -0.00164 -0.01008 -0.00920 35  PRO A C   
264  O O   . PRO A 35  ? 0.09821 0.08440 0.08321 -0.00122 -0.00879 -0.01026 35  PRO A O   
265  C CB  . PRO A 35  ? 0.11791 0.10294 0.09960 -0.00361 -0.01247 -0.00997 35  PRO A CB  
266  C CG  . PRO A 35  ? 0.11347 0.09713 0.09338 -0.00425 -0.01384 -0.01203 35  PRO A CG  
267  C CD  . PRO A 35  ? 0.12636 0.10770 0.10754 -0.00401 -0.01259 -0.01384 35  PRO A CD  
268  N N   . VAL A 36  ? 0.10248 0.08956 0.09146 -0.00091 -0.01017 -0.00764 36  VAL A N   
269  C CA  . VAL A 36  ? 0.09530 0.08479 0.08637 0.00071  -0.00931 -0.00721 36  VAL A CA  
270  C C   . VAL A 36  ? 0.08998 0.08307 0.08205 0.00017  -0.00998 -0.00608 36  VAL A C   
271  O O   . VAL A 36  ? 0.08661 0.07926 0.07834 -0.00043 -0.01098 -0.00503 36  VAL A O   
272  C CB  . VAL A 36  ? 0.09749 0.08499 0.09028 0.00270  -0.00902 -0.00649 36  VAL A CB  
273  C CG1 . VAL A 36  ? 0.15289 0.14407 0.14823 0.00495  -0.00887 -0.00565 36  VAL A CG1 
274  C CG2 . VAL A 36  ? 0.12529 0.10862 0.11735 0.00303  -0.00785 -0.00821 36  VAL A CG2 
275  N N   . PHE A 37  ? 0.10287 0.09952 0.09637 0.00019  -0.00918 -0.00662 37  PHE A N   
276  C CA  . PHE A 37  ? 0.10874 0.10950 0.10420 -0.00040 -0.00978 -0.00625 37  PHE A CA  
277  C C   . PHE A 37  ? 0.11627 0.12148 0.11560 0.00157  -0.00972 -0.00652 37  PHE A C   
278  O O   . PHE A 37  ? 0.12290 0.12940 0.12386 0.00227  -0.00809 -0.00755 37  PHE A O   
279  C CB  . PHE A 37  ? 0.09625 0.09777 0.09086 -0.00276 -0.00871 -0.00688 37  PHE A CB  
280  C CG  . PHE A 37  ? 0.11478 0.11986 0.11143 -0.00409 -0.00922 -0.00710 37  PHE A CG  
281  C CD1 . PHE A 37  ? 0.12072 0.13123 0.12151 -0.00425 -0.00873 -0.00820 37  PHE A CD1 
282  C CD2 . PHE A 37  ? 0.11172 0.11501 0.10655 -0.00529 -0.01011 -0.00659 37  PHE A CD2 
283  C CE1 . PHE A 37  ? 0.14009 0.15427 0.14302 -0.00595 -0.00946 -0.00905 37  PHE A CE1 
284  C CE2 . PHE A 37  ? 0.11788 0.12396 0.11414 -0.00679 -0.01050 -0.00738 37  PHE A CE2 
285  C CZ  . PHE A 37  ? 0.08850 0.10008 0.08875 -0.00731 -0.01034 -0.00875 37  PHE A CZ  
286  N N   . VAL A 38  ? 0.13180 0.13957 0.13244 0.00275  -0.01148 -0.00560 38  VAL A N   
287  C CA  . VAL A 38  ? 0.15329 0.16606 0.15782 0.00533  -0.01216 -0.00553 38  VAL A CA  
288  C C   . VAL A 38  ? 0.13509 0.15471 0.14330 0.00365  -0.01251 -0.00703 38  VAL A C   
289  O O   . VAL A 38  ? 0.13296 0.15399 0.14030 0.00173  -0.01382 -0.00731 38  VAL A O   
290  C CB  . VAL A 38  ? 0.16310 0.17514 0.16638 0.00788  -0.01411 -0.00351 38  VAL A CB  
291  C CG1 . VAL A 38  ? 0.18240 0.20028 0.18967 0.01120  -0.01535 -0.00315 38  VAL A CG1 
292  C CG2 . VAL A 38  ? 0.13101 0.13580 0.13138 0.00899  -0.01308 -0.00222 38  VAL A CG2 
293  N N   . LEU A 39  ? 0.17371 0.19753 0.18631 0.00418  -0.01102 -0.00829 39  LEU A N   
294  C CA  . LEU A 39  ? 0.18914 0.22007 0.20666 0.00218  -0.01076 -0.01010 39  LEU A CA  
295  C C   . LEU A 39  ? 0.23798 0.27677 0.26168 0.00527  -0.01227 -0.01039 39  LEU A C   
296  O O   . LEU A 39  ? 0.23454 0.27308 0.25995 0.00863  -0.01135 -0.00981 39  LEU A O   
297  C CB  . LEU A 39  ? 0.19533 0.22529 0.21343 -0.00014 -0.00711 -0.01140 39  LEU A CB  
298  C CG  . LEU A 39  ? 0.23522 0.27114 0.25821 -0.00333 -0.00579 -0.01335 39  LEU A CG  
299  C CD1 . LEU A 39  ? 0.22558 0.25822 0.24514 -0.00700 -0.00602 -0.01351 39  LEU A CD1 
300  C CD2 . LEU A 39  ? 0.19656 0.23287 0.22140 -0.00414 -0.00159 -0.01433 39  LEU A CD2 
301  N N   . ASP A 40  ? 0.29163 0.33750 0.31879 0.00428  -0.01468 -0.01147 40  ASP A N   
302  C CA  . ASP A 40  ? 0.31890 0.37402 0.35274 0.00725  -0.01678 -0.01195 40  ASP A CA  
303  C C   . ASP A 40  ? 0.36966 0.43240 0.41136 0.00481  -0.01466 -0.01474 40  ASP A C   
304  O O   . ASP A 40  ? 0.39370 0.45990 0.43733 0.00063  -0.01489 -0.01683 40  ASP A O   
305  C CB  . ASP A 40  ? 0.36336 0.42267 0.39618 0.00782  -0.02125 -0.01175 40  ASP A CB  
306  C CG  . ASP A 40  ? 0.42405 0.49279 0.46279 0.01209  -0.02432 -0.01158 40  ASP A CG  
307  O OD1 . ASP A 40  ? 0.42167 0.48816 0.45961 0.01707  -0.02456 -0.00907 40  ASP A OD1 
308  O OD2 . ASP A 40  ? 0.45505 0.53350 0.49948 0.01054  -0.02654 -0.01403 40  ASP A OD2 
309  N N   . PRO A 41  ? 0.40760 0.47289 0.45415 0.00706  -0.01215 -0.01504 41  PRO A N   
310  C CA  . PRO A 41  ? 0.43133 0.50379 0.48569 0.00445  -0.00922 -0.01770 41  PRO A CA  
311  C C   . PRO A 41  ? 0.46139 0.54666 0.52496 0.00430  -0.01220 -0.01977 41  PRO A C   
312  O O   . PRO A 41  ? 0.50678 0.59932 0.57843 0.00197  -0.00970 -0.02224 41  PRO A O   
313  C CB  . PRO A 41  ? 0.45841 0.52961 0.51474 0.00786  -0.00578 -0.01730 41  PRO A CB  
314  C CG  . PRO A 41  ? 0.39972 0.46782 0.45319 0.01330  -0.00852 -0.01484 41  PRO A CG  
315  C CD  . PRO A 41  ? 0.37027 0.43153 0.41545 0.01201  -0.01136 -0.01314 41  PRO A CD  
316  N N   . HIS A 42  ? 0.46827 0.55684 0.53088 0.00664  -0.01738 -0.01894 42  HIS A N   
317  C CA  . HIS A 42  ? 0.50240 0.60371 0.57294 0.00647  -0.02124 -0.02118 42  HIS A CA  
318  C C   . HIS A 42  ? 0.47369 0.57461 0.54004 0.00244  -0.02427 -0.02255 42  HIS A C   
319  O O   . HIS A 42  ? 0.46312 0.57229 0.53193 0.00342  -0.02914 -0.02365 42  HIS A O   
320  C CB  . HIS A 42  ? 0.48954 0.59656 0.56269 0.01340  -0.02520 -0.01920 42  HIS A CB  
321  C CG  . HIS A 42  ? 0.50967 0.61472 0.58542 0.01805  -0.02204 -0.01756 42  HIS A CG  
322  N ND1 . HIS A 42  ? 0.53694 0.65089 0.62336 0.01887  -0.01961 -0.01954 42  HIS A ND1 
323  C CD2 . HIS A 42  ? 0.51220 0.60715 0.58143 0.02195  -0.02058 -0.01447 42  HIS A CD2 
324  C CE1 . HIS A 42  ? 0.59179 0.70087 0.67763 0.02335  -0.01675 -0.01772 42  HIS A CE1 
325  N NE2 . HIS A 42  ? 0.58592 0.68330 0.66136 0.02514  -0.01737 -0.01475 42  HIS A NE2 
326  N N   . PHE A 43  ? 0.48691 0.57823 0.54664 -0.00189 -0.02146 -0.02259 43  PHE A N   
327  C CA  . PHE A 43  ? 0.47081 0.55996 0.52566 -0.00542 -0.02370 -0.02383 43  PHE A CA  
328  C C   . PHE A 43  ? 0.48174 0.57975 0.54426 -0.01054 -0.02398 -0.02829 43  PHE A C   
329  O O   . PHE A 43  ? 0.48713 0.58890 0.54876 -0.01219 -0.02776 -0.03033 43  PHE A O   
330  C CB  . PHE A 43  ? 0.47860 0.55480 0.52465 -0.00783 -0.02048 -0.02232 43  PHE A CB  
331  C CG  . PHE A 43  ? 0.49014 0.56182 0.52905 -0.00926 -0.02289 -0.02235 43  PHE A CG  
332  C CD1 . PHE A 43  ? 0.47003 0.53738 0.50205 -0.00539 -0.02540 -0.01950 43  PHE A CD1 
333  C CD2 . PHE A 43  ? 0.45544 0.52670 0.49446 -0.01453 -0.02213 -0.02529 43  PHE A CD2 
334  C CE1 . PHE A 43  ? 0.51557 0.57879 0.54089 -0.00663 -0.02706 -0.01960 43  PHE A CE1 
335  C CE2 . PHE A 43  ? 0.46480 0.53160 0.49710 -0.01565 -0.02395 -0.02560 43  PHE A CE2 
336  C CZ  . PHE A 43  ? 0.50836 0.57142 0.53378 -0.01164 -0.02639 -0.02276 43  PHE A CZ  
337  N N   . LEU A 44  ? 0.47427 0.57549 0.54416 -0.01337 -0.01976 -0.03007 44  LEU A N   
338  C CA  . LEU A 44  ? 0.46164 0.57182 0.54038 -0.01865 -0.01941 -0.03456 44  LEU A CA  
339  C C   . LEU A 44  ? 0.49900 0.62473 0.58818 -0.01629 -0.02374 -0.03673 44  LEU A C   
340  O O   . LEU A 44  ? 0.51276 0.64791 0.61011 -0.02066 -0.02472 -0.04105 44  LEU A O   
341  C CB  . LEU A 44  ? 0.43414 0.54176 0.51692 -0.02268 -0.01260 -0.03543 44  LEU A CB  
342  C CG  . LEU A 44  ? 0.36664 0.45944 0.43941 -0.02373 -0.00806 -0.03259 44  LEU A CG  
343  C CD1 . LEU A 44  ? 0.29031 0.38148 0.36689 -0.02769 -0.00139 -0.03347 44  LEU A CD1 
344  C CD2 . LEU A 44  ? 0.34247 0.42711 0.40697 -0.02633 -0.00949 -0.03263 44  LEU A CD2 
345  N N   . GLN A 45  ? 0.51600 0.64463 0.60534 -0.00949 -0.02638 -0.03391 45  GLN A N   
346  C CA  . GLN A 45  ? 0.48670 0.63022 0.58601 -0.00582 -0.03069 -0.03522 45  GLN A CA  
347  C C   . GLN A 45  ? 0.49650 0.64286 0.59046 -0.00206 -0.03787 -0.03420 45  GLN A C   
348  O O   . GLN A 45  ? 0.50317 0.65284 0.59715 0.00476  -0.04109 -0.03137 45  GLN A O   
349  C CB  . GLN A 45  ? 0.51294 0.65768 0.61656 -0.00022 -0.02821 -0.03266 45  GLN A CB  
350  C CG  . GLN A 45  ? 0.51440 0.67566 0.63161 0.00303  -0.03082 -0.03450 45  GLN A CG  
351  C CD  . GLN A 45  ? 0.52263 0.68331 0.64239 0.00980  -0.02862 -0.03147 45  GLN A CD  
352  O OE1 . GLN A 45  ? 0.52783 0.67557 0.63877 0.01181  -0.02538 -0.02823 45  GLN A OE1 
353  N NE2 . GLN A 45  ? 0.51764 0.69260 0.64989 0.01339  -0.03040 -0.03278 45  GLN A NE2 
354  N N   . GLN A 46  ? 0.44392 0.58831 0.53255 -0.00628 -0.04019 -0.03638 46  GLN A N   
355  C CA  . GLN A 46  ? 0.48315 0.62989 0.56536 -0.00315 -0.04676 -0.03570 46  GLN A CA  
356  C C   . GLN A 46  ? 0.46868 0.62685 0.55610 -0.00763 -0.05111 -0.04126 46  GLN A C   
357  O O   . GLN A 46  ? 0.49063 0.64418 0.57449 -0.01375 -0.04992 -0.04432 46  GLN A O   
358  C CB  . GLN A 46  ? 0.46440 0.59601 0.53216 -0.00295 -0.04576 -0.03259 46  GLN A CB  
359  C CG  . GLN A 46  ? 0.48945 0.61130 0.55349 -0.00968 -0.04098 -0.03441 46  GLN A CG  
360  C CD  . GLN A 46  ? 0.46603 0.57350 0.51735 -0.00852 -0.03947 -0.03085 46  GLN A CD  
361  O OE1 . GLN A 46  ? 0.45461 0.55365 0.50163 -0.01297 -0.03627 -0.03181 46  GLN A OE1 
362  N NE2 . GLN A 46  ? 0.47522 0.57977 0.52088 -0.00244 -0.04155 -0.02664 46  GLN A NE2 
363  N N   . LYS A 50  ? 0.23975 0.34454 0.30664 -0.04561 -0.02731 -0.05488 50  LYS A N   
364  C CA  . LYS A 50  ? 0.23662 0.33325 0.29285 -0.03948 -0.02852 -0.04948 50  LYS A CA  
365  C C   . LYS A 50  ? 0.22217 0.30430 0.27234 -0.04015 -0.02253 -0.04611 50  LYS A C   
366  O O   . LYS A 50  ? 0.22740 0.30021 0.26879 -0.04009 -0.02220 -0.04524 50  LYS A O   
367  C CB  . LYS A 50  ? 0.27589 0.37918 0.33481 -0.03303 -0.03104 -0.04586 50  LYS A CB  
368  C CG  . LYS A 50  ? 0.30833 0.42734 0.37939 -0.03285 -0.03382 -0.04862 50  LYS A CG  
369  C CD  . LYS A 50  ? 0.33631 0.46599 0.40745 -0.03046 -0.04134 -0.05068 50  LYS A CD  
370  C CE  . LYS A 50  ? 0.36632 0.49157 0.42731 -0.02345 -0.04473 -0.04579 50  LYS A CE  
371  N NZ  . LYS A 50  ? 0.36079 0.47893 0.41067 -0.02453 -0.04653 -0.04647 50  LYS A NZ  
372  N N   . VAL A 51  ? 0.23231 0.31315 0.28704 -0.04056 -0.01804 -0.04437 51  VAL A N   
373  C CA  . VAL A 51  ? 0.23072 0.29854 0.27935 -0.04072 -0.01283 -0.04097 51  VAL A CA  
374  C C   . VAL A 51  ? 0.20470 0.27161 0.25952 -0.04568 -0.00715 -0.04253 51  VAL A C   
375  O O   . VAL A 51  ? 0.23411 0.30969 0.29757 -0.04610 -0.00622 -0.04350 51  VAL A O   
376  C CB  . VAL A 51  ? 0.24552 0.31003 0.29006 -0.03477 -0.01281 -0.03584 51  VAL A CB  
377  C CG1 . VAL A 51  ? 0.24085 0.29216 0.27583 -0.03372 -0.01044 -0.03253 51  VAL A CG1 
378  C CG2 . VAL A 51  ? 0.25632 0.32788 0.30043 -0.02973 -0.01842 -0.03487 51  VAL A CG2 
379  N N   . SER A 52  ? 0.17301 0.22928 0.22348 -0.04924 -0.00301 -0.04262 52  SER A N   
380  C CA  A SER A 52  ? 0.13483 0.18785 0.18948 -0.05382 0.00322  -0.04329 52  SER A CA  
381  C CA  B SER A 52  ? 0.13477 0.18785 0.18946 -0.05381 0.00321  -0.04330 52  SER A CA  
382  C C   . SER A 52  ? 0.11408 0.16013 0.16443 -0.05066 0.00709  -0.03824 52  SER A C   
383  O O   . SER A 52  ? 0.11219 0.15310 0.15511 -0.04582 0.00538  -0.03450 52  SER A O   
384  C CB  A SER A 52  ? 0.11653 0.16015 0.16804 -0.05880 0.00636  -0.04538 52  SER A CB  
385  C CB  B SER A 52  ? 0.11653 0.16028 0.16817 -0.05884 0.00636  -0.04542 52  SER A CB  
386  O OG  A SER A 52  ? 0.12122 0.15976 0.17553 -0.06294 0.01308  -0.04519 52  SER A OG  
387  O OG  B SER A 52  ? 0.11730 0.14898 0.15848 -0.05591 0.00692  -0.04181 52  SER A OG  
388  N N   . VAL A 53  ? 0.11812 0.16407 0.17315 -0.05373 0.01254  -0.03840 53  VAL A N   
389  C CA  . VAL A 53  ? 0.12592 0.16527 0.17618 -0.05109 0.01653  -0.03397 53  VAL A CA  
390  C C   . VAL A 53  ? 0.11502 0.14000 0.15463 -0.05037 0.01877  -0.03059 53  VAL A C   
391  O O   . VAL A 53  ? 0.11832 0.13734 0.15161 -0.04699 0.02033  -0.02658 53  VAL A O   
392  C CB  . VAL A 53  ? 0.14343 0.18609 0.20091 -0.05477 0.02240  -0.03504 53  VAL A CB  
393  C CG1 . VAL A 53  ? 0.16769 0.20268 0.22518 -0.06089 0.02782  -0.03639 53  VAL A CG1 
394  C CG2 . VAL A 53  ? 0.15251 0.19163 0.20569 -0.05111 0.02552  -0.03100 53  VAL A CG2 
395  N N   . ASN A 54  ? 0.11895 0.13844 0.15643 -0.05326 0.01880  -0.03229 54  ASN A N   
396  C CA  . ASN A 54  ? 0.12313 0.12929 0.15122 -0.05209 0.02090  -0.02905 54  ASN A CA  
397  C C   . ASN A 54  ? 0.11808 0.12229 0.13940 -0.04643 0.01625  -0.02630 54  ASN A C   
398  O O   . ASN A 54  ? 0.11892 0.11549 0.13332 -0.04328 0.01742  -0.02226 54  ASN A O   
399  C CB  . ASN A 54  ? 0.12966 0.13017 0.15795 -0.05676 0.02276  -0.03201 54  ASN A CB  
400  C CG  . ASN A 54  ? 0.13724 0.13455 0.16977 -0.06240 0.02929  -0.03334 54  ASN A CG  
401  O OD1 . ASN A 54  ? 0.14080 0.14214 0.17736 -0.06321 0.03222  -0.03262 54  ASN A OD1 
402  N ND2 . ASN A 54  ? 0.14469 0.13424 0.17633 -0.06644 0.03209  -0.03537 54  ASN A ND2 
403  N N   . ARG A 55  ? 0.11352 0.12465 0.13666 -0.04512 0.01101  -0.02843 55  ARG A N   
404  C CA  . ARG A 55  ? 0.10945 0.11852 0.12656 -0.04019 0.00719  -0.02591 55  ARG A CA  
405  C C   . ARG A 55  ? 0.10421 0.11729 0.12122 -0.03594 0.00561  -0.02326 55  ARG A C   
406  O O   . ARG A 55  ? 0.11138 0.11947 0.12259 -0.03231 0.00482  -0.02006 55  ARG A O   
407  C CB  . ARG A 55  ? 0.11206 0.12592 0.12978 -0.04020 0.00267  -0.02879 55  ARG A CB  
408  C CG  . ARG A 55  ? 0.10730 0.11866 0.11890 -0.03548 -0.00058 -0.02618 55  ARG A CG  
409  C CD  . ARG A 55  ? 0.13916 0.15280 0.14928 -0.03574 -0.00399 -0.02878 55  ARG A CD  
410  N NE  . ARG A 55  ? 0.13403 0.15855 0.14858 -0.03535 -0.00798 -0.03096 55  ARG A NE  
411  C CZ  . ARG A 55  ? 0.15071 0.18185 0.17034 -0.03906 -0.00907 -0.03538 55  ARG A CZ  
412  N NH1 . ARG A 55  ? 0.12368 0.15113 0.14482 -0.04402 -0.00602 -0.03841 55  ARG A NH1 
413  N NH2 . ARG A 55  ? 0.17815 0.21985 0.20155 -0.03771 -0.01337 -0.03686 55  ARG A NH2 
414  N N   . TYR A 56  ? 0.10198 0.12416 0.12576 -0.03635 0.00522  -0.02481 56  TYR A N   
415  C CA  . TYR A 56  ? 0.09790 0.12342 0.12175 -0.03220 0.00405  -0.02265 56  TYR A CA  
416  C C   . TYR A 56  ? 0.10016 0.11877 0.11962 -0.03137 0.00810  -0.01970 56  TYR A C   
417  O O   . TYR A 56  ? 0.11772 0.13419 0.13303 -0.02757 0.00699  -0.01726 56  TYR A O   
418  C CB  . TYR A 56  ? 0.10153 0.13859 0.13432 -0.03249 0.00301  -0.02507 56  TYR A CB  
419  C CG  . TYR A 56  ? 0.15233 0.19365 0.18534 -0.02739 0.00009  -0.02343 56  TYR A CG  
420  C CD1 . TYR A 56  ? 0.16209 0.20202 0.19440 -0.02520 0.00263  -0.02153 56  TYR A CD1 
421  C CD2 . TYR A 56  ? 0.15621 0.20218 0.18946 -0.02471 -0.00493 -0.02375 56  TYR A CD2 
422  C CE1 . TYR A 56  ? 0.15902 0.20180 0.19153 -0.02063 0.00037  -0.02028 56  TYR A CE1 
423  C CE2 . TYR A 56  ? 0.18518 0.23381 0.21841 -0.01994 -0.00713 -0.02196 56  TYR A CE2 
424  C CZ  . TYR A 56  ? 0.21210 0.25897 0.24529 -0.01800 -0.00441 -0.02036 56  TYR A CZ  
425  O OH  . TYR A 56  ? 0.17799 0.22655 0.21120 -0.01336 -0.00620 -0.01884 56  TYR A OH  
426  N N   . ASN A 57  ? 0.10542 0.12017 0.12532 -0.03497 0.01291  -0.01995 57  ASN A N   
427  C CA  . ASN A 57  ? 0.10933 0.11652 0.12325 -0.03400 0.01675  -0.01680 57  ASN A CA  
428  C C   . ASN A 57  ? 0.11103 0.10876 0.11633 -0.03187 0.01578  -0.01394 57  ASN A C   
429  O O   . ASN A 57  ? 0.11244 0.10549 0.11172 -0.02915 0.01641  -0.01107 57  ASN A O   
430  C CB  . ASN A 57  ? 0.11886 0.12389 0.13514 -0.03839 0.02269  -0.01745 57  ASN A CB  
431  C CG  . ASN A 57  ? 0.14214 0.13969 0.15138 -0.03713 0.02689  -0.01398 57  ASN A CG  
432  O OD1 . ASN A 57  ? 0.12051 0.12118 0.12987 -0.03531 0.02794  -0.01341 57  ASN A OD1 
433  N ND2 . ASN A 57  ? 0.16701 0.15437 0.16961 -0.03784 0.02939  -0.01163 57  ASN A ND2 
434  N N   . PHE A 58  ? 0.11142 0.10662 0.11616 -0.03298 0.01420  -0.01491 58  PHE A N   
435  C CA  . PHE A 58  ? 0.11234 0.10000 0.11024 -0.03042 0.01288  -0.01242 58  PHE A CA  
436  C C   . PHE A 58  ? 0.10657 0.09681 0.10242 -0.02612 0.00874  -0.01108 58  PHE A C   
437  O O   . PHE A 58  ? 0.10739 0.09265 0.09778 -0.02340 0.00828  -0.00839 58  PHE A O   
438  C CB  . PHE A 58  ? 0.11399 0.09922 0.11241 -0.03240 0.01222  -0.01434 58  PHE A CB  
439  C CG  . PHE A 58  ? 0.14259 0.11919 0.13481 -0.03021 0.01228  -0.01185 58  PHE A CG  
440  C CD1 . PHE A 58  ? 0.11511 0.09238 0.10504 -0.02670 0.00857  -0.01082 58  PHE A CD1 
441  C CD2 . PHE A 58  ? 0.12520 0.09300 0.11431 -0.03155 0.01632  -0.01046 58  PHE A CD2 
442  C CE1 . PHE A 58  ? 0.11648 0.08694 0.10196 -0.02454 0.00867  -0.00871 58  PHE A CE1 
443  C CE2 . PHE A 58  ? 0.12925 0.08959 0.11328 -0.02893 0.01627  -0.00804 58  PHE A CE2 
444  C CZ  . PHE A 58  ? 0.13096 0.09321 0.11361 -0.02541 0.01233  -0.00731 58  PHE A CZ  
445  N N   . LEU A 59  ? 0.10548 0.10353 0.10579 -0.02546 0.00570  -0.01293 59  LEU A N   
446  C CA  . LEU A 59  ? 0.12072 0.12073 0.11949 -0.02165 0.00242  -0.01167 59  LEU A CA  
447  C C   . LEU A 59  ? 0.10876 0.10828 0.10580 -0.01987 0.00379  -0.01016 59  LEU A C   
448  O O   . LEU A 59  ? 0.12369 0.12037 0.11665 -0.01717 0.00237  -0.00842 59  LEU A O   
449  C CB  . LEU A 59  ? 0.10368 0.11153 0.10720 -0.02108 -0.00073 -0.01362 59  LEU A CB  
450  C CG  . LEU A 59  ? 0.13130 0.14138 0.13420 -0.01729 -0.00345 -0.01239 59  LEU A CG  
451  C CD1 . LEU A 59  ? 0.12647 0.13145 0.12448 -0.01539 -0.00512 -0.01063 59  LEU A CD1 
452  C CD2 . LEU A 59  ? 0.12231 0.14027 0.13004 -0.01651 -0.00608 -0.01398 59  LEU A CD2 
453  N N   . LEU A 60  ? 0.11670 0.11912 0.11693 -0.02153 0.00672  -0.01110 60  LEU A N   
454  C CA  . LEU A 60  ? 0.14252 0.14424 0.14052 -0.01993 0.00859  -0.01002 60  LEU A CA  
455  C C   . LEU A 60  ? 0.11602 0.10951 0.10614 -0.01933 0.01035  -0.00746 60  LEU A C   
456  O O   . LEU A 60  ? 0.10647 0.09803 0.09214 -0.01682 0.00958  -0.00627 60  LEU A O   
457  C CB  . LEU A 60  ? 0.10236 0.10910 0.10589 -0.02205 0.01208  -0.01169 60  LEU A CB  
458  C CG  . LEU A 60  ? 0.10584 0.12227 0.11777 -0.02173 0.01005  -0.01412 60  LEU A CG  
459  C CD1 . LEU A 60  ? 0.11708 0.13905 0.13563 -0.02421 0.01394  -0.01595 60  LEU A CD1 
460  C CD2 . LEU A 60  ? 0.12645 0.14470 0.13765 -0.01754 0.00730  -0.01352 60  LEU A CD2 
461  N N   . GLU A 61  ? 0.12596 0.11438 0.11410 -0.02150 0.01263  -0.00664 61  GLU A N   
462  C CA  . GLU A 61  ? 0.12373 0.10415 0.10401 -0.02028 0.01398  -0.00371 61  GLU A CA  
463  C C   . GLU A 61  ? 0.11361 0.09188 0.09045 -0.01727 0.00987  -0.00240 61  GLU A C   
464  O O   . GLU A 61  ? 0.11723 0.09126 0.08789 -0.01509 0.00948  -0.00020 61  GLU A O   
465  C CB  . GLU A 61  ? 0.13117 0.10587 0.11043 -0.02307 0.01772  -0.00294 61  GLU A CB  
466  C CG  . GLU A 61  ? 0.13405 0.10977 0.11613 -0.02641 0.02279  -0.00386 61  GLU A CG  
467  C CD  . GLU A 61  ? 0.13653 0.10581 0.11811 -0.02967 0.02689  -0.00333 61  GLU A CD  
468  O OE1 . GLU A 61  ? 0.13531 0.09931 0.11434 -0.02902 0.02563  -0.00235 61  GLU A OE1 
469  O OE2 . GLU A 61  ? 0.17378 0.14305 0.15779 -0.03295 0.03176  -0.00397 61  GLU A OE2 
470  N N   . SER A 62  ? 0.10805 0.08950 0.08878 -0.01711 0.00683  -0.00378 62  SER A N   
471  C CA  . SER A 62  ? 0.13156 0.11188 0.11018 -0.01447 0.00334  -0.00279 62  SER A CA  
472  C C   . SER A 62  ? 0.12568 0.10876 0.10358 -0.01225 0.00122  -0.00289 62  SER A C   
473  O O   . SER A 62  ? 0.10993 0.09101 0.08457 -0.01020 -0.00077 -0.00172 62  SER A O   
474  C CB  . SER A 62  ? 0.10318 0.08572 0.08551 -0.01504 0.00137  -0.00421 62  SER A CB  
475  O OG  . SER A 62  ? 0.10666 0.08583 0.08921 -0.01718 0.00338  -0.00458 62  SER A OG  
476  N N   . LEU A 63  ? 0.10769 0.09546 0.08902 -0.01261 0.00165  -0.00448 63  LEU A N   
477  C CA  . LEU A 63  ? 0.12598 0.11540 0.10660 -0.01057 0.00023  -0.00485 63  LEU A CA  
478  C C   . LEU A 63  ? 0.12486 0.11105 0.09978 -0.00988 0.00190  -0.00402 63  LEU A C   
479  O O   . LEU A 63  ? 0.15598 0.14126 0.12793 -0.00814 0.00010  -0.00406 63  LEU A O   
480  C CB  . LEU A 63  ? 0.14771 0.14280 0.13384 -0.01059 0.00041  -0.00664 63  LEU A CB  
481  C CG  . LEU A 63  ? 0.14296 0.14184 0.13379 -0.01066 -0.00185 -0.00743 63  LEU A CG  
482  C CD1 . LEU A 63  ? 0.16384 0.16854 0.15974 -0.00975 -0.00201 -0.00877 63  LEU A CD1 
483  C CD2 . LEU A 63  ? 0.13312 0.12986 0.12212 -0.00910 -0.00467 -0.00654 63  LEU A CD2 
484  N N   . GLU A 64  ? 0.14109 0.12534 0.11410 -0.01138 0.00548  -0.00339 64  GLU A N   
485  C CA  . GLU A 64  ? 0.16417 0.14455 0.13006 -0.01055 0.00729  -0.00217 64  GLU A CA  
486  C C   . GLU A 64  ? 0.15254 0.12832 0.11240 -0.00885 0.00500  -0.00004 64  GLU A C   
487  O O   . GLU A 64  ? 0.14336 0.11723 0.09709 -0.00721 0.00423  0.00050  64  GLU A O   
488  C CB  . GLU A 64  ? 0.16583 0.14448 0.13083 -0.01269 0.01229  -0.00156 64  GLU A CB  
489  C CG  . GLU A 64  ? 0.20644 0.19071 0.17795 -0.01420 0.01484  -0.00385 64  GLU A CG  
490  C CD  . GLU A 64  ? 0.24672 0.22941 0.21775 -0.01670 0.02041  -0.00336 64  GLU A CD  
491  O OE1 . GLU A 64  ? 0.28238 0.25866 0.24762 -0.01732 0.02238  -0.00096 64  GLU A OE1 
492  O OE2 . GLU A 64  ? 0.27154 0.25932 0.24822 -0.01794 0.02306  -0.00525 64  GLU A OE2 
493  N N   . ASP A 65  ? 0.15315 0.12745 0.11470 -0.00908 0.00381  0.00098  65  ASP A N   
494  C CA  . ASP A 65  ? 0.16757 0.13861 0.12492 -0.00697 0.00132  0.00294  65  ASP A CA  
495  C C   . ASP A 65  ? 0.13516 0.10934 0.09362 -0.00529 -0.00282 0.00174  65  ASP A C   
496  O O   . ASP A 65  ? 0.15472 0.12776 0.10869 -0.00341 -0.00499 0.00257  65  ASP A O   
497  C CB  . ASP A 65  ? 0.14767 0.11642 0.10741 -0.00750 0.00156  0.00395  65  ASP A CB  
498  C CG  . ASP A 65  ? 0.15335 0.11819 0.10876 -0.00494 -0.00008 0.00650  65  ASP A CG  
499  O OD1 . ASP A 65  ? 0.16961 0.12971 0.11877 -0.00400 0.00173  0.00891  65  ASP A OD1 
500  O OD2 . ASP A 65  ? 0.18665 0.15323 0.14492 -0.00367 -0.00302 0.00626  65  ASP A OD2 
501  N N   . LEU A 66  ? 0.12921 0.10736 0.09362 -0.00599 -0.00395 -0.00022 66  LEU A N   
502  C CA  . LEU A 66  ? 0.13046 0.11091 0.09629 -0.00487 -0.00707 -0.00148 66  LEU A CA  
503  C C   . LEU A 66  ? 0.13528 0.11588 0.09757 -0.00432 -0.00700 -0.00276 66  LEU A C   
504  O O   . LEU A 66  ? 0.11400 0.09485 0.07459 -0.00335 -0.00957 -0.00355 66  LEU A O   
505  C CB  . LEU A 66  ? 0.12905 0.11268 0.10112 -0.00554 -0.00766 -0.00279 66  LEU A CB  
506  C CG  . LEU A 66  ? 0.13430 0.11801 0.10946 -0.00605 -0.00802 -0.00212 66  LEU A CG  
507  C CD1 . LEU A 66  ? 0.11437 0.10121 0.09416 -0.00644 -0.00856 -0.00331 66  LEU A CD1 
508  C CD2 . LEU A 66  ? 0.14068 0.12314 0.11509 -0.00481 -0.01008 -0.00109 66  LEU A CD2 
509  N N   . GLN A 67  ? 0.12496 0.10563 0.08640 -0.00508 -0.00390 -0.00334 67  GLN A N   
510  C CA  . GLN A 67  ? 0.14105 0.12149 0.09880 -0.00449 -0.00317 -0.00489 67  GLN A CA  
511  C C   . GLN A 67  ? 0.15861 0.13598 0.10807 -0.00338 -0.00414 -0.00393 67  GLN A C   
512  O O   . GLN A 67  ? 0.13883 0.11628 0.08521 -0.00259 -0.00609 -0.00564 67  GLN A O   
513  C CB  . GLN A 67  ? 0.13760 0.11905 0.09656 -0.00543 0.00097  -0.00553 67  GLN A CB  
514  C CG  . GLN A 67  ? 0.15102 0.13242 0.10708 -0.00468 0.00237  -0.00759 67  GLN A CG  
515  C CD  . GLN A 67  ? 0.13841 0.12166 0.09866 -0.00384 0.00032  -0.00981 67  GLN A CD  
516  O OE1 . GLN A 67  ? 0.17518 0.15701 0.13277 -0.00322 -0.00232 -0.01085 67  GLN A OE1 
517  N NE2 . GLN A 67  ? 0.16697 0.15339 0.13394 -0.00382 0.00155  -0.01055 67  GLN A NE2 
518  N N   . ARG A 68  ? 0.15810 0.13250 0.10355 -0.00324 -0.00287 -0.00126 68  ARG A N   
519  C CA  . ARG A 68  ? 0.17091 0.14234 0.10772 -0.00154 -0.00416 0.00028  68  ARG A CA  
520  C C   . ARG A 68  ? 0.18283 0.15582 0.12045 -0.00006 -0.00920 0.00028  68  ARG A C   
521  O O   . ARG A 68  ? 0.18113 0.15385 0.11275 0.00146  -0.01179 0.00014  68  ARG A O   
522  C CB  . ARG A 68  ? 0.18294 0.14987 0.11526 -0.00146 -0.00109 0.00367  68  ARG A CB  
523  C CG  . ARG A 68  ? 0.25398 0.21959 0.18589 -0.00335 0.00443  0.00363  68  ARG A CG  
524  C CD  . ARG A 68  ? 0.28024 0.24025 0.20724 -0.00354 0.00795  0.00714  68  ARG A CD  
525  N NE  . ARG A 68  ? 0.27088 0.22978 0.20284 -0.00407 0.00743  0.00851  68  ARG A NE  
526  C CZ  . ARG A 68  ? 0.26598 0.22582 0.20484 -0.00674 0.01011  0.00768  68  ARG A CZ  
527  N NH1 . ARG A 68  ? 0.26969 0.23243 0.21237 -0.00903 0.01331  0.00568  68  ARG A NH1 
528  N NH2 . ARG A 68  ? 0.24747 0.20566 0.18971 -0.00707 0.00951  0.00863  68  ARG A NH2 
529  N N   . SER A 69  ? 0.18186 0.15690 0.12686 -0.00051 -0.01061 0.00028  69  SER A N   
530  C CA  . SER A 69  ? 0.18149 0.15875 0.12875 0.00069  -0.01486 0.00012  69  SER A CA  
531  C C   . SER A 69  ? 0.17593 0.15628 0.12548 0.00010  -0.01728 -0.00320 69  SER A C   
532  O O   . SER A 69  ? 0.17424 0.15639 0.12247 0.00101  -0.02085 -0.00406 69  SER A O   
533  C CB  . SER A 69  ? 0.15765 0.13567 0.11166 0.00033  -0.01482 0.00111  69  SER A CB  
534  O OG  . SER A 69  ? 0.17923 0.15361 0.13107 0.00079  -0.01258 0.00386  69  SER A OG  
535  N N   . PHE A 70  ? 0.14616 0.12719 0.09941 -0.00136 -0.01539 -0.00516 70  PHE A N   
536  C CA  . PHE A 70  ? 0.16491 0.14748 0.12012 -0.00197 -0.01696 -0.00830 70  PHE A CA  
537  C C   . PHE A 70  ? 0.16250 0.14386 0.11045 -0.00159 -0.01731 -0.01017 70  PHE A C   
538  O O   . PHE A 70  ? 0.17783 0.16034 0.12539 -0.00188 -0.02002 -0.01278 70  PHE A O   
539  C CB  . PHE A 70  ? 0.15380 0.13673 0.11443 -0.00295 -0.01465 -0.00940 70  PHE A CB  
540  C CG  . PHE A 70  ? 0.14491 0.12933 0.11225 -0.00336 -0.01523 -0.00848 70  PHE A CG  
541  C CD1 . PHE A 70  ? 0.13951 0.12522 0.11037 -0.00369 -0.01762 -0.00937 70  PHE A CD1 
542  C CD2 . PHE A 70  ? 0.15179 0.13650 0.12188 -0.00363 -0.01322 -0.00698 70  PHE A CD2 
543  C CE1 . PHE A 70  ? 0.16307 0.14978 0.13933 -0.00403 -0.01757 -0.00841 70  PHE A CE1 
544  C CE2 . PHE A 70  ? 0.13904 0.12490 0.11405 -0.00391 -0.01370 -0.00629 70  PHE A CE2 
545  C CZ  . PHE A 70  ? 0.10885 0.09543 0.08659 -0.00399 -0.01567 -0.00683 70  PHE A CZ  
546  N N   . GLN A 71  ? 0.17163 0.15063 0.11369 -0.00118 -0.01436 -0.00914 71  GLN A N   
547  C CA  . GLN A 71  ? 0.20164 0.17905 0.13546 -0.00070 -0.01421 -0.01089 71  GLN A CA  
548  C C   . GLN A 71  ? 0.18801 0.16575 0.11551 0.00070  -0.01822 -0.01024 71  GLN A C   
549  O O   . GLN A 71  ? 0.15596 0.13399 0.07839 0.00082  -0.02031 -0.01302 71  GLN A O   
550  C CB  . GLN A 71  ? 0.19215 0.16692 0.12124 -0.00064 -0.00939 -0.00962 71  GLN A CB  
551  C CG  . GLN A 71  ? 0.22307 0.19856 0.15770 -0.00164 -0.00572 -0.01129 71  GLN A CG  
552  C CD  . GLN A 71  ? 0.28938 0.26317 0.22019 -0.00179 -0.00067 -0.01039 71  GLN A CD  
553  O OE1 . GLN A 71  ? 0.29546 0.26668 0.21918 -0.00135 0.00053  -0.00807 71  GLN A OE1 
554  N NE2 . GLN A 71  ? 0.29688 0.27211 0.23257 -0.00225 0.00253  -0.01209 71  GLN A NE2 
555  N N   . ALA A 72  ? 0.17283 0.15061 0.10050 0.00194  -0.01944 -0.00676 72  ALA A N   
556  C CA  . ALA A 72  ? 0.17657 0.15550 0.09924 0.00396  -0.02378 -0.00577 72  ALA A CA  
557  C C   . ALA A 72  ? 0.21041 0.19419 0.13888 0.00340  -0.02857 -0.00874 72  ALA A C   
558  O O   . ALA A 72  ? 0.17909 0.16532 0.10382 0.00481  -0.03292 -0.00924 72  ALA A O   
559  C CB  . ALA A 72  ? 0.19000 0.16731 0.11243 0.00580  -0.02347 -0.00116 72  ALA A CB  
560  N N   . ARG A 73  ? 0.19382 0.17917 0.13133 0.00137  -0.02784 -0.01069 73  ARG A N   
561  C CA  . ARG A 73  ? 0.19344 0.18289 0.13746 0.00021  -0.03137 -0.01360 73  ARG A CA  
562  C C   . ARG A 73  ? 0.20207 0.19079 0.14691 -0.00198 -0.03064 -0.01806 73  ARG A C   
563  O O   . ARG A 73  ? 0.17780 0.16858 0.12962 -0.00372 -0.03192 -0.02050 73  ARG A O   
564  C CB  . ARG A 73  ? 0.17955 0.17069 0.13309 -0.00027 -0.03085 -0.01201 73  ARG A CB  
565  C CG  . ARG A 73  ? 0.20983 0.20127 0.16320 0.00197  -0.03142 -0.00803 73  ARG A CG  
566  C CD  . ARG A 73  ? 0.20394 0.19611 0.16567 0.00139  -0.02992 -0.00671 73  ARG A CD  
567  N NE  . ARG A 73  ? 0.23524 0.22692 0.19672 0.00362  -0.03004 -0.00323 73  ARG A NE  
568  C CZ  . ARG A 73  ? 0.26146 0.25677 0.22645 0.00526  -0.03308 -0.00255 73  ARG A CZ  
569  N NH1 . ARG A 73  ? 0.24515 0.24561 0.21477 0.00451  -0.03641 -0.00528 73  ARG A NH1 
570  N NH2 . ARG A 73  ? 0.27283 0.26659 0.23718 0.00768  -0.03256 0.00079  73  ARG A NH2 
571  N N   . GLY A 74  ? 0.17340 0.15878 0.11130 -0.00192 -0.02811 -0.01916 74  GLY A N   
572  C CA  . GLY A 74  ? 0.19559 0.17939 0.13337 -0.00358 -0.02701 -0.02353 74  GLY A CA  
573  C C   . GLY A 74  ? 0.22996 0.21184 0.17459 -0.00459 -0.02325 -0.02377 74  GLY A C   
574  O O   . GLY A 74  ? 0.21681 0.19689 0.16266 -0.00578 -0.02227 -0.02730 74  GLY A O   
575  N N   . SER A 75  ? 0.17000 0.15202 0.11884 -0.00400 -0.02117 -0.02024 75  SER A N   
576  C CA  . SER A 75  ? 0.19881 0.17979 0.15402 -0.00448 -0.01822 -0.02002 75  SER A CA  
577  C C   . SER A 75  ? 0.18620 0.16592 0.13945 -0.00354 -0.01435 -0.01823 75  SER A C   
578  O O   . SER A 75  ? 0.17989 0.15862 0.12642 -0.00289 -0.01323 -0.01770 75  SER A O   
579  C CB  . SER A 75  ? 0.18297 0.16598 0.14553 -0.00487 -0.01934 -0.01800 75  SER A CB  
580  O OG  . SER A 75  ? 0.19611 0.17809 0.16386 -0.00503 -0.01689 -0.01763 75  SER A OG  
581  N N   . ARG A 76  ? 0.18598 0.16603 0.14524 -0.00349 -0.01226 -0.01725 76  ARG A N   
582  C CA  . ARG A 76  ? 0.16553 0.14572 0.12500 -0.00286 -0.00874 -0.01606 76  ARG A CA  
583  C C   . ARG A 76  ? 0.17839 0.16041 0.14507 -0.00278 -0.00820 -0.01439 76  ARG A C   
584  O O   . ARG A 76  ? 0.16665 0.14840 0.13753 -0.00275 -0.00903 -0.01502 76  ARG A O   
585  C CB  . ARG A 76  ? 0.22672 0.20519 0.18401 -0.00231 -0.00604 -0.01872 76  ARG A CB  
586  C CG  . ARG A 76  ? 0.20909 0.18883 0.16811 -0.00162 -0.00215 -0.01786 76  ARG A CG  
587  C CD  . ARG A 76  ? 0.21278 0.19070 0.16843 -0.00085 0.00086  -0.02060 76  ARG A CD  
588  N NE  . ARG A 76  ? 0.25135 0.22710 0.20906 -0.00036 0.00037  -0.02335 76  ARG A NE  
589  C CZ  . ARG A 76  ? 0.21234 0.18826 0.17582 0.00100  0.00229  -0.02383 76  ARG A CZ  
590  N NH1 . ARG A 76  ? 0.19499 0.17438 0.16333 0.00203  0.00437  -0.02205 76  ARG A NH1 
591  N NH2 . ARG A 76  ? 0.24112 0.21367 0.20572 0.00140  0.00210  -0.02620 76  ARG A NH2 
592  N N   . LEU A 77  ? 0.15641 0.14004 0.12411 -0.00286 -0.00671 -0.01232 77  LEU A N   
593  C CA  . LEU A 77  ? 0.15241 0.13836 0.12616 -0.00283 -0.00648 -0.01103 77  LEU A CA  
594  C C   . LEU A 77  ? 0.13093 0.11841 0.10810 -0.00182 -0.00421 -0.01201 77  LEU A C   
595  O O   . LEU A 77  ? 0.12482 0.11279 0.10049 -0.00163 -0.00162 -0.01278 77  LEU A O   
596  C CB  . LEU A 77  ? 0.11480 0.10186 0.08854 -0.00370 -0.00593 -0.00901 77  LEU A CB  
597  C CG  . LEU A 77  ? 0.12267 0.11249 0.10189 -0.00398 -0.00593 -0.00813 77  LEU A CG  
598  C CD1 . LEU A 77  ? 0.11326 0.10286 0.09480 -0.00365 -0.00832 -0.00769 77  LEU A CD1 
599  C CD2 . LEU A 77  ? 0.17496 0.16509 0.15377 -0.00533 -0.00488 -0.00684 77  LEU A CD2 
600  N N   . LEU A 78  ? 0.12381 0.11208 0.10555 -0.00091 -0.00499 -0.01180 78  LEU A N   
601  C CA  . LEU A 78  ? 0.12602 0.11596 0.11162 0.00085  -0.00334 -0.01238 78  LEU A CA  
602  C C   . LEU A 78  ? 0.13390 0.12840 0.12411 0.00105  -0.00367 -0.01086 78  LEU A C   
603  O O   . LEU A 78  ? 0.13952 0.13431 0.13090 0.00081  -0.00564 -0.00951 78  LEU A O   
604  C CB  . LEU A 78  ? 0.13004 0.11689 0.11686 0.00221  -0.00387 -0.01304 78  LEU A CB  
605  C CG  . LEU A 78  ? 0.14366 0.12601 0.12652 0.00156  -0.00386 -0.01530 78  LEU A CG  
606  C CD1 . LEU A 78  ? 0.15058 0.12925 0.13555 0.00253  -0.00384 -0.01591 78  LEU A CD1 
607  C CD2 . LEU A 78  ? 0.15912 0.14099 0.13874 0.00193  -0.00143 -0.01737 78  LEU A CD2 
608  N N   . VAL A 79  ? 0.13529 0.13363 0.12818 0.00136  -0.00165 -0.01136 79  VAL A N   
609  C CA  . VAL A 79  ? 0.12817 0.13200 0.12617 0.00138  -0.00220 -0.01063 79  VAL A CA  
610  C C   . VAL A 79  ? 0.15185 0.15880 0.15476 0.00439  -0.00194 -0.01091 79  VAL A C   
611  O O   . VAL A 79  ? 0.15651 0.16647 0.16233 0.00532  0.00042  -0.01210 79  VAL A O   
612  C CB  . VAL A 79  ? 0.14565 0.15250 0.14447 -0.00083 -0.00013 -0.01107 79  VAL A CB  
613  C CG1 . VAL A 79  ? 0.13294 0.14600 0.13753 -0.00139 -0.00110 -0.01100 79  VAL A CG1 
614  C CG2 . VAL A 79  ? 0.13786 0.14049 0.13109 -0.00310 -0.00014 -0.01032 79  VAL A CG2 
615  N N   . LEU A 80  ? 0.15128 0.15738 0.15509 0.00620  -0.00411 -0.00964 80  LEU A N   
616  C CA  . LEU A 80  ? 0.15094 0.15901 0.15873 0.00982  -0.00410 -0.00928 80  LEU A CA  
617  C C   . LEU A 80  ? 0.19777 0.21397 0.21105 0.01063  -0.00540 -0.00891 80  LEU A C   
618  O O   . LEU A 80  ? 0.17782 0.19642 0.19088 0.00883  -0.00744 -0.00833 80  LEU A O   
619  C CB  . LEU A 80  ? 0.18586 0.18875 0.19159 0.01154  -0.00551 -0.00766 80  LEU A CB  
620  C CG  . LEU A 80  ? 0.18575 0.18110 0.18716 0.01049  -0.00452 -0.00849 80  LEU A CG  
621  C CD1 . LEU A 80  ? 0.19313 0.18353 0.19371 0.01203  -0.00523 -0.00686 80  LEU A CD1 
622  C CD2 . LEU A 80  ? 0.19935 0.19298 0.20057 0.01131  -0.00178 -0.01075 80  LEU A CD2 
623  N N   . ARG A 81  ? 0.18191 0.20271 0.20042 0.01335  -0.00422 -0.00958 81  ARG A N   
624  C CA  . ARG A 81  ? 0.18150 0.21151 0.20649 0.01446  -0.00581 -0.00963 81  ARG A CA  
625  C C   . ARG A 81  ? 0.17303 0.20386 0.19894 0.01860  -0.00871 -0.00745 81  ARG A C   
626  O O   . ARG A 81  ? 0.24045 0.26554 0.26442 0.02168  -0.00800 -0.00622 81  ARG A O   
627  C CB  . ARG A 81  ? 0.16150 0.19738 0.19282 0.01550  -0.00296 -0.01149 81  ARG A CB  
628  C CG  . ARG A 81  ? 0.18757 0.22684 0.22035 0.01116  -0.00067 -0.01338 81  ARG A CG  
629  C CD  . ARG A 81  ? 0.16297 0.19413 0.18849 0.00851  0.00202  -0.01378 81  ARG A CD  
630  N NE  . ARG A 81  ? 0.15350 0.18699 0.17982 0.00482  0.00486  -0.01506 81  ARG A NE  
631  C CZ  . ARG A 81  ? 0.15672 0.18437 0.17687 0.00261  0.00754  -0.01531 81  ARG A CZ  
632  N NH1 . ARG A 81  ? 0.18013 0.20016 0.19329 0.00347  0.00734  -0.01488 81  ARG A NH1 
633  N NH2 . ARG A 81  ? 0.14560 0.17510 0.16650 -0.00057 0.01049  -0.01602 81  ARG A NH2 
634  N N   . GLY A 82  ? 0.21216 0.24974 0.24058 0.01863  -0.01187 -0.00700 82  GLY A N   
635  C CA  . GLY A 82  ? 0.24100 0.28011 0.26952 0.02287  -0.01495 -0.00464 82  GLY A CA  
636  C C   . GLY A 82  ? 0.23171 0.26867 0.25472 0.02140  -0.01779 -0.00319 82  GLY A C   
637  O O   . GLY A 82  ? 0.21577 0.25184 0.23638 0.01696  -0.01771 -0.00443 82  GLY A O   
638  N N   . LYS A 83  ? 0.22597 0.26159 0.24657 0.02536  -0.02000 -0.00040 83  LYS A N   
639  C CA  . LYS A 83  ? 0.23584 0.26888 0.25037 0.02451  -0.02224 0.00124  83  LYS A CA  
640  C C   . LYS A 83  ? 0.22441 0.24634 0.23280 0.02461  -0.02018 0.00339  83  LYS A C   
641  O O   . LYS A 83  ? 0.24238 0.25910 0.25112 0.02708  -0.01804 0.00440  83  LYS A O   
642  C CB  . LYS A 83  ? 0.24001 0.27895 0.25482 0.02880  -0.02607 0.00315  83  LYS A CB  
643  C CG  . LYS A 83  ? 0.26022 0.31159 0.28173 0.02827  -0.02885 0.00056  83  LYS A CG  
644  C CD  . LYS A 83  ? 0.26611 0.32389 0.28725 0.03283  -0.03341 0.00242  83  LYS A CD  
645  C CE  . LYS A 83  ? 0.26202 0.33334 0.29072 0.03170  -0.03658 -0.00085 83  LYS A CE  
646  N NZ  . LYS A 83  ? 0.25414 0.33288 0.28236 0.03642  -0.04181 0.00076  83  LYS A NZ  
647  N N   . PRO A 84  ? 0.20141 0.21958 0.20457 0.02177  -0.02050 0.00384  84  PRO A N   
648  C CA  . PRO A 84  ? 0.24488 0.25331 0.24342 0.02122  -0.01826 0.00548  84  PRO A CA  
649  C C   . PRO A 84  ? 0.22355 0.22696 0.21970 0.02572  -0.01787 0.00892  84  PRO A C   
650  O O   . PRO A 84  ? 0.21575 0.21164 0.21118 0.02603  -0.01516 0.00955  84  PRO A O   
651  C CB  . PRO A 84  ? 0.18750 0.19501 0.18183 0.01792  -0.01898 0.00533  84  PRO A CB  
652  C CG  . PRO A 84  ? 0.19455 0.20957 0.19175 0.01538  -0.02055 0.00258  84  PRO A CG  
653  C CD  . PRO A 84  ? 0.20309 0.22558 0.20501 0.01846  -0.02239 0.00231  84  PRO A CD  
654  N N   . GLU A 85  ? 0.20156 0.20863 0.19616 0.02925  -0.02049 0.01114  85  GLU A N   
655  C CA  . GLU A 85  ? 0.26287 0.26427 0.25414 0.03400  -0.01997 0.01513  85  GLU A CA  
656  C C   . GLU A 85  ? 0.23980 0.23957 0.23543 0.03783  -0.01839 0.01556  85  GLU A C   
657  O O   . GLU A 85  ? 0.23005 0.22213 0.22312 0.04121  -0.01658 0.01864  85  GLU A O   
658  C CB  . GLU A 85  ? 0.31095 0.31743 0.29885 0.03743  -0.02366 0.01751  85  GLU A CB  
659  C CG  . GLU A 85  ? 0.33129 0.33885 0.31390 0.03408  -0.02502 0.01699  85  GLU A CG  
660  C CD  . GLU A 85  ? 0.28732 0.30445 0.27373 0.03069  -0.02758 0.01294  85  GLU A CD  
661  O OE1 . GLU A 85  ? 0.34534 0.36865 0.33874 0.03082  -0.02818 0.01070  85  GLU A OE1 
662  O OE2 . GLU A 85  ? 0.33212 0.35022 0.31461 0.02781  -0.02857 0.01188  85  GLU A OE2 
663  N N   . GLU A 86  ? 0.25179 0.25808 0.25388 0.03740  -0.01857 0.01254  86  GLU A N   
664  C CA  . GLU A 86  ? 0.24021 0.24533 0.24680 0.04106  -0.01665 0.01244  86  GLU A CA  
665  C C   . GLU A 86  ? 0.19932 0.19837 0.20688 0.03783  -0.01283 0.00970  86  GLU A C   
666  O O   . GLU A 86  ? 0.25309 0.24719 0.26222 0.04063  -0.01028 0.00984  86  GLU A O   
667  C CB  . GLU A 86  ? 0.25962 0.27655 0.27337 0.04329  -0.01888 0.01084  86  GLU A CB  
668  C CG  . GLU A 86  ? 0.27431 0.29888 0.28792 0.04705  -0.02337 0.01309  86  GLU A CG  
669  C CD  . GLU A 86  ? 0.27888 0.31662 0.30104 0.04836  -0.02574 0.01075  86  GLU A CD  
670  O OE1 . GLU A 86  ? 0.25873 0.29918 0.28659 0.04600  -0.02335 0.00750  86  GLU A OE1 
671  O OE2 . GLU A 86  ? 0.31959 0.36528 0.34276 0.05170  -0.02997 0.01208  86  GLU A OE2 
672  N N   . VAL A 87  ? 0.19466 0.19382 0.20100 0.03228  -0.01245 0.00717  87  VAL A N   
673  C CA  . VAL A 87  ? 0.22410 0.21888 0.23090 0.02926  -0.00951 0.00431  87  VAL A CA  
674  C C   . VAL A 87  ? 0.19913 0.18405 0.20143 0.02710  -0.00768 0.00487  87  VAL A C   
675  O O   . VAL A 87  ? 0.21142 0.19023 0.21374 0.02681  -0.00506 0.00343  87  VAL A O   
676  C CB  . VAL A 87  ? 0.25038 0.25119 0.25862 0.02490  -0.01009 0.00137  87  VAL A CB  
677  C CG1 . VAL A 87  ? 0.23391 0.22980 0.24080 0.02178  -0.00751 -0.00123 87  VAL A CG1 
678  C CG2 . VAL A 87  ? 0.22802 0.23838 0.24207 0.02656  -0.01096 0.00022  87  VAL A CG2 
679  N N   . PHE A 88  ? 0.18493 0.16836 0.18362 0.02543  -0.00885 0.00665  88  PHE A N   
680  C CA  . PHE A 88  ? 0.17805 0.15354 0.17366 0.02265  -0.00702 0.00680  88  PHE A CA  
681  C C   . PHE A 88  ? 0.18074 0.14735 0.17536 0.02525  -0.00441 0.00865  88  PHE A C   
682  O O   . PHE A 88  ? 0.18792 0.14827 0.18249 0.02286  -0.00209 0.00682  88  PHE A O   
683  C CB  . PHE A 88  ? 0.15229 0.12868 0.14467 0.02062  -0.00838 0.00837  88  PHE A CB  
684  C CG  . PHE A 88  ? 0.17083 0.15219 0.16370 0.01663  -0.00968 0.00592  88  PHE A CG  
685  C CD1 . PHE A 88  ? 0.17102 0.15007 0.16436 0.01315  -0.00856 0.00349  88  PHE A CD1 
686  C CD2 . PHE A 88  ? 0.20660 0.19474 0.19931 0.01646  -0.01207 0.00599  88  PHE A CD2 
687  C CE1 . PHE A 88  ? 0.16805 0.15098 0.16145 0.01009  -0.00964 0.00175  88  PHE A CE1 
688  C CE2 . PHE A 88  ? 0.17094 0.16239 0.16397 0.01291  -0.01275 0.00388  88  PHE A CE2 
689  C CZ  . PHE A 88  ? 0.15787 0.14647 0.15113 0.00999  -0.01145 0.00206  88  PHE A CZ  
690  N N   . PRO A 89  ? 0.16868 0.13413 0.16238 0.03010  -0.00465 0.01216  89  PRO A N   
691  C CA  . PRO A 89  ? 0.21395 0.16963 0.20674 0.03285  -0.00153 0.01402  89  PRO A CA  
692  C C   . PRO A 89  ? 0.20536 0.15812 0.20148 0.03335  0.00076  0.01094  89  PRO A C   
693  O O   . PRO A 89  ? 0.21186 0.15504 0.20726 0.03352  0.00401  0.01094  89  PRO A O   
694  C CB  . PRO A 89  ? 0.20599 0.16309 0.19733 0.03892  -0.00300 0.01848  89  PRO A CB  
695  C CG  . PRO A 89  ? 0.16786 0.13303 0.15729 0.03781  -0.00657 0.01923  89  PRO A CG  
696  C CD  . PRO A 89  ? 0.22083 0.19299 0.21358 0.03329  -0.00778 0.01480  89  PRO A CD  
697  N N   . ARG A 90  ? 0.20636 0.16667 0.20592 0.03338  -0.00042 0.00815  90  ARG A N   
698  C CA  . ARG A 90  ? 0.19420 0.15193 0.19619 0.03363  0.00209  0.00481  90  ARG A CA  
699  C C   . ARG A 90  ? 0.21265 0.16690 0.21310 0.02795  0.00327  0.00096  90  ARG A C   
700  O O   . ARG A 90  ? 0.20306 0.14941 0.20298 0.02721  0.00606  -0.00103 90  ARG A O   
701  C CB  . ARG A 90  ? 0.23794 0.20525 0.24417 0.03565  0.00091  0.00331  90  ARG A CB  
702  C CG  . ARG A 90  ? 0.21864 0.18410 0.22683 0.03560  0.00383  -0.00052 90  ARG A CG  
703  C CD  . ARG A 90  ? 0.30161 0.27740 0.31414 0.03647  0.00306  -0.00216 90  ARG A CD  
704  N NE  . ARG A 90  ? 0.31091 0.29291 0.32244 0.03172  0.00096  -0.00341 90  ARG A NE  
705  C CZ  . ARG A 90  ? 0.34786 0.33920 0.36290 0.03132  -0.00001 -0.00441 90  ARG A CZ  
706  N NH1 . ARG A 90  ? 0.47669 0.47375 0.49726 0.03528  0.00064  -0.00448 90  ARG A NH1 
707  N NH2 . ARG A 90  ? 0.37978 0.37480 0.39321 0.02686  -0.00144 -0.00539 90  ARG A NH2 
708  N N   . VAL A 91  ? 0.21048 0.17053 0.21018 0.02399  0.00106  -0.00025 91  VAL A N   
709  C CA  . VAL A 91  ? 0.21347 0.17160 0.21173 0.01912  0.00148  -0.00374 91  VAL A CA  
710  C C   . VAL A 91  ? 0.18359 0.13480 0.18016 0.01640  0.00236  -0.00331 91  VAL A C   
711  O O   . VAL A 91  ? 0.18150 0.13015 0.17748 0.01272  0.00286  -0.00649 91  VAL A O   
712  C CB  . VAL A 91  ? 0.17862 0.14467 0.17659 0.01632  -0.00098 -0.00472 91  VAL A CB  
713  C CG1 . VAL A 91  ? 0.18197 0.15475 0.18230 0.01834  -0.00117 -0.00550 91  VAL A CG1 
714  C CG2 . VAL A 91  ? 0.18287 0.15166 0.17997 0.01556  -0.00309 -0.00187 91  VAL A CG2 
715  N N   . PHE A 92  ? 0.18748 0.13591 0.18325 0.01807  0.00260  0.00050  92  PHE A N   
716  C CA  . PHE A 92  ? 0.18805 0.12947 0.18280 0.01542  0.00433  0.00105  92  PHE A CA  
717  C C   . PHE A 92  ? 0.19387 0.12609 0.18924 0.01537  0.00769  -0.00088 92  PHE A C   
718  O O   . PHE A 92  ? 0.17654 0.10514 0.17246 0.01113  0.00871  -0.00394 92  PHE A O   
719  C CB  . PHE A 92  ? 0.18545 0.12537 0.17822 0.01758  0.00442  0.00592  92  PHE A CB  
720  C CG  . PHE A 92  ? 0.19468 0.14181 0.18630 0.01609  0.00169  0.00705  92  PHE A CG  
721  C CD1 . PHE A 92  ? 0.18496 0.13769 0.17770 0.01243  -0.00014 0.00403  92  PHE A CD1 
722  C CD2 . PHE A 92  ? 0.19884 0.14667 0.18771 0.01857  0.00105  0.01113  92  PHE A CD2 
723  C CE1 . PHE A 92  ? 0.19532 0.15372 0.18705 0.01120  -0.00222 0.00492  92  PHE A CE1 
724  C CE2 . PHE A 92  ? 0.18704 0.14092 0.17450 0.01709  -0.00119 0.01166  92  PHE A CE2 
725  C CZ  . PHE A 92  ? 0.18652 0.14544 0.17572 0.01337  -0.00265 0.00848  92  PHE A CZ  
726  N N   . ARG A 93  ? 0.19228 0.12076 0.18790 0.02011  0.00940  0.00062  93  ARG A N   
727  C CA  . ARG A 93  ? 0.21554 0.13415 0.21161 0.02046  0.01309  -0.00129 93  ARG A CA  
728  C C   . ARG A 93  ? 0.19715 0.11687 0.19401 0.01858  0.01334  -0.00684 93  ARG A C   
729  O O   . ARG A 93  ? 0.19902 0.11139 0.19582 0.01604  0.01576  -0.01031 93  ARG A O   
730  C CB  . ARG A 93  ? 0.21027 0.12413 0.20629 0.02690  0.01501  0.00246  93  ARG A CB  
731  C CG  . ARG A 93  ? 0.25509 0.16281 0.24884 0.02877  0.01638  0.00782  93  ARG A CG  
732  C CD  . ARG A 93  ? 0.23869 0.15485 0.23074 0.03024  0.01283  0.01169  93  ARG A CD  
733  N NE  . ARG A 93  ? 0.26062 0.17056 0.24920 0.03272  0.01433  0.01711  93  ARG A NE  
734  C CZ  . ARG A 93  ? 0.23585 0.15092 0.22151 0.03429  0.01184  0.02088  93  ARG A CZ  
735  N NH1 . ARG A 93  ? 0.22382 0.15020 0.21023 0.03340  0.00775  0.01967  93  ARG A NH1 
736  N NH2 . ARG A 93  ? 0.22762 0.13578 0.20901 0.03672  0.01376  0.02593  93  ARG A NH2 
737  N N   . GLU A 94  ? 0.21855 0.14708 0.21586 0.01959  0.01110  -0.00791 94  GLU A N   
738  C CA  . GLU A 94  ? 0.18888 0.11831 0.18585 0.01823  0.01173  -0.01284 94  GLU A CA  
739  C C   . GLU A 94  ? 0.17756 0.10772 0.17283 0.01237  0.01032  -0.01659 94  GLU A C   
740  O O   . GLU A 94  ? 0.16959 0.09521 0.16365 0.01020  0.01176  -0.02106 94  GLU A O   
741  C CB  . GLU A 94  ? 0.20398 0.14259 0.20204 0.02076  0.01027  -0.01257 94  GLU A CB  
742  C CG  . GLU A 94  ? 0.20989 0.15045 0.20647 0.01895  0.01091  -0.01729 94  GLU A CG  
743  C CD  . GLU A 94  ? 0.19828 0.14799 0.19638 0.02086  0.01003  -0.01678 94  GLU A CD  
744  O OE1 . GLU A 94  ? 0.18558 0.13868 0.18713 0.02510  0.01007  -0.01387 94  GLU A OE1 
745  O OE2 . GLU A 94  ? 0.20932 0.16295 0.20521 0.01811  0.00932  -0.01925 94  GLU A OE2 
746  N N   . TRP A 95  ? 0.16391 0.09988 0.15901 0.00994  0.00742  -0.01503 95  TRP A N   
747  C CA  . TRP A 95  ? 0.19194 0.13023 0.18593 0.00508  0.00548  -0.01811 95  TRP A CA  
748  C C   . TRP A 95  ? 0.19769 0.13094 0.19302 0.00162  0.00612  -0.01862 95  TRP A C   
749  O O   . TRP A 95  ? 0.19081 0.12648 0.18619 -0.00237 0.00428  -0.02133 95  TRP A O   
750  C CB  . TRP A 95  ? 0.18299 0.13014 0.17653 0.00445  0.00230  -0.01633 95  TRP A CB  
751  C CG  . TRP A 95  ? 0.16130 0.11384 0.15400 0.00678  0.00190  -0.01639 95  TRP A CG  
752  C CD1 . TRP A 95  ? 0.17265 0.12376 0.16470 0.00868  0.00389  -0.01866 95  TRP A CD1 
753  C CD2 . TRP A 95  ? 0.14886 0.10890 0.14169 0.00721  -0.00012 -0.01431 95  TRP A CD2 
754  N NE1 . TRP A 95  ? 0.16484 0.12258 0.15701 0.01016  0.00335  -0.01797 95  TRP A NE1 
755  C CE2 . TRP A 95  ? 0.15810 0.12122 0.15080 0.00912  0.00085  -0.01538 95  TRP A CE2 
756  C CE3 . TRP A 95  ? 0.15089 0.11505 0.14407 0.00603  -0.00230 -0.01188 95  TRP A CE3 
757  C CZ2 . TRP A 95  ? 0.14905 0.11918 0.14234 0.00949  -0.00028 -0.01412 95  TRP A CZ2 
758  C CZ3 . TRP A 95  ? 0.16549 0.13609 0.15874 0.00656  -0.00356 -0.01079 95  TRP A CZ3 
759  C CH2 . TRP A 95  ? 0.15785 0.13138 0.15135 0.00808  -0.00255 -0.01191 95  TRP A CH2 
760  N N   . GLY A 96  ? 0.19948 0.12594 0.19606 0.00311  0.00879  -0.01601 96  GLY A N   
761  C CA  . GLY A 96  ? 0.23056 0.15191 0.22893 -0.00041 0.01021  -0.01622 96  GLY A CA  
762  C C   . GLY A 96  ? 0.20711 0.13472 0.20657 -0.00287 0.00784  -0.01446 96  GLY A C   
763  O O   . GLY A 96  ? 0.20568 0.13402 0.20727 -0.00725 0.00725  -0.01705 96  GLY A O   
764  N N   . VAL A 97  ? 0.18949 0.12196 0.18780 -0.00001 0.00645  -0.01030 97  VAL A N   
765  C CA  . VAL A 97  ? 0.18028 0.11897 0.17917 -0.00187 0.00427  -0.00884 97  VAL A CA  
766  C C   . VAL A 97  ? 0.14387 0.07815 0.14435 -0.00368 0.00663  -0.00674 97  VAL A C   
767  O O   . VAL A 97  ? 0.14372 0.07142 0.14313 -0.00147 0.00950  -0.00365 97  VAL A O   
768  C CB  . VAL A 97  ? 0.15852 0.10326 0.15546 0.00147  0.00229  -0.00564 97  VAL A CB  
769  C CG1 . VAL A 97  ? 0.13978 0.09077 0.13703 -0.00056 0.00008  -0.00497 97  VAL A CG1 
770  C CG2 . VAL A 97  ? 0.15841 0.10648 0.15438 0.00342  0.00110  -0.00746 97  VAL A CG2 
771  N N   . THR A 98  ? 0.14660 0.08449 0.14970 -0.00754 0.00564  -0.00826 98  THR A N   
772  C CA  . THR A 98  ? 0.13661 0.07172 0.14191 -0.00971 0.00813  -0.00645 98  THR A CA  
773  C C   . THR A 98  ? 0.16136 0.10294 0.16664 -0.00980 0.00665  -0.00417 98  THR A C   
774  O O   . THR A 98  ? 0.17519 0.11479 0.18173 -0.01112 0.00915  -0.00215 98  THR A O   
775  C CB  . THR A 98  ? 0.16271 0.09606 0.17289 -0.01473 0.00915  -0.01075 98  THR A CB  
776  O OG1 . THR A 98  ? 0.16338 0.10497 0.17550 -0.01688 0.00523  -0.01421 98  THR A OG1 
777  C CG2 . THR A 98  ? 0.20099 0.12661 0.21098 -0.01503 0.01120  -0.01348 98  THR A CG2 
778  N N   . GLN A 99  ? 0.15581 0.10448 0.15958 -0.00852 0.00316  -0.00449 99  GLN A N   
779  C CA  . GLN A 99  ? 0.15241 0.10672 0.15612 -0.00863 0.00189  -0.00283 99  GLN A CA  
780  C C   . GLN A 99  ? 0.13789 0.09710 0.13831 -0.00593 -0.00094 -0.00209 99  GLN A C   
781  O O   . GLN A 99  ? 0.14299 0.10454 0.14310 -0.00580 -0.00293 -0.00443 99  GLN A O   
782  C CB  . GLN A 99  ? 0.14036 0.09925 0.14871 -0.01221 0.00065  -0.00570 99  GLN A CB  
783  C CG  . GLN A 99  ? 0.16989 0.13408 0.17867 -0.01211 -0.00018 -0.00414 99  GLN A CG  
784  C CD  . GLN A 99  ? 0.18625 0.15617 0.19981 -0.01463 -0.00219 -0.00696 99  GLN A CD  
785  O OE1 . GLN A 99  ? 0.14673 0.12042 0.15964 -0.01434 -0.00538 -0.00891 99  GLN A OE1 
786  N NE2 . GLN A 99  ? 0.17271 0.14347 0.19112 -0.01693 -0.00023 -0.00705 99  GLN A NE2 
787  N N   . LEU A 100 ? 0.12795 0.08858 0.12576 -0.00401 -0.00090 0.00097  100 LEU A N   
788  C CA  . LEU A 100 ? 0.14139 0.10700 0.13678 -0.00209 -0.00336 0.00146  100 LEU A CA  
789  C C   . LEU A 100 ? 0.13535 0.10501 0.13092 -0.00326 -0.00410 0.00180  100 LEU A C   
790  O O   . LEU A 100 ? 0.14398 0.11216 0.13913 -0.00359 -0.00227 0.00358  100 LEU A O   
791  C CB  . LEU A 100 ? 0.12859 0.09293 0.12063 0.00141  -0.00314 0.00425  100 LEU A CB  
792  C CG  . LEU A 100 ? 0.11883 0.08886 0.10904 0.00297  -0.00558 0.00456  100 LEU A CG  
793  C CD1 . LEU A 100 ? 0.10744 0.08089 0.09917 0.00241  -0.00721 0.00188  100 LEU A CD1 
794  C CD2 . LEU A 100 ? 0.12534 0.09497 0.11289 0.00655  -0.00579 0.00717  100 LEU A CD2 
795  N N   . CYS A 101 ? 0.10478 0.07895 0.10069 -0.00375 -0.00634 0.00018  101 CYS A N   
796  C CA  . CYS A 101 ? 0.11500 0.09252 0.11132 -0.00460 -0.00694 0.00024  101 CYS A CA  
797  C C   . CYS A 101 ? 0.11039 0.09102 0.10418 -0.00342 -0.00861 0.00034  101 CYS A C   
798  O O   . CYS A 101 ? 0.11842 0.10022 0.11179 -0.00302 -0.00984 -0.00078 101 CYS A O   
799  C CB  . CYS A 101 ? 0.13386 0.11344 0.13383 -0.00662 -0.00784 -0.00190 101 CYS A CB  
800  S SG  . CYS A 101 ? 0.19871 0.17578 0.20332 -0.00899 -0.00603 -0.00303 101 CYS A SG  
801  N N   . PHE A 102 ? 0.12381 0.10557 0.11590 -0.00310 -0.00831 0.00142  102 PHE A N   
802  C CA  . PHE A 102 ? 0.10882 0.09336 0.09905 -0.00269 -0.00964 0.00102  102 PHE A CA  
803  C C   . PHE A 102 ? 0.10780 0.09285 0.09697 -0.00313 -0.00887 0.00137  102 PHE A C   
804  O O   . PHE A 102 ? 0.10841 0.09180 0.09712 -0.00313 -0.00718 0.00247  102 PHE A O   
805  C CB  . PHE A 102 ? 0.11465 0.10008 0.10279 -0.00102 -0.01039 0.00165  102 PHE A CB  
806  C CG  . PHE A 102 ? 0.10584 0.08927 0.09166 0.00051  -0.00951 0.00372  102 PHE A CG  
807  C CD1 . PHE A 102 ? 0.12624 0.11046 0.10882 0.00093  -0.00949 0.00456  102 PHE A CD1 
808  C CD2 . PHE A 102 ? 0.12933 0.10951 0.11554 0.00168  -0.00856 0.00486  102 PHE A CD2 
809  C CE1 . PHE A 102 ? 0.14150 0.12360 0.12066 0.00269  -0.00871 0.00683  102 PHE A CE1 
810  C CE2 . PHE A 102 ? 0.13376 0.11122 0.11702 0.00350  -0.00750 0.00736  102 PHE A CE2 
811  C CZ  . PHE A 102 ? 0.16490 0.14347 0.14432 0.00412  -0.00767 0.00852  102 PHE A CZ  
812  N N   . GLU A 103 ? 0.09352 0.08034 0.08215 -0.00355 -0.00968 0.00039  103 GLU A N   
813  C CA  . GLU A 103 ? 0.10959 0.09636 0.09719 -0.00392 -0.00873 0.00025  103 GLU A CA  
814  C C   . GLU A 103 ? 0.10965 0.09617 0.09341 -0.00328 -0.00825 0.00088  103 GLU A C   
815  O O   . GLU A 103 ? 0.14278 0.13059 0.12470 -0.00258 -0.00958 0.00094  103 GLU A O   
816  C CB  . GLU A 103 ? 0.09665 0.08427 0.08421 -0.00449 -0.00941 -0.00095 103 GLU A CB  
817  C CG  . GLU A 103 ? 0.08751 0.07421 0.07458 -0.00473 -0.00809 -0.00137 103 GLU A CG  
818  C CD  . GLU A 103 ? 0.10018 0.08639 0.08702 -0.00523 -0.00833 -0.00229 103 GLU A CD  
819  O OE1 . GLU A 103 ? 0.08702 0.07389 0.07242 -0.00595 -0.00900 -0.00308 103 GLU A OE1 
820  O OE2 . GLU A 103 ? 0.12251 0.10770 0.11089 -0.00481 -0.00772 -0.00213 103 GLU A OE2 
821  N N   . HIS A 104 ? 0.10888 0.09409 0.09137 -0.00336 -0.00637 0.00129  104 HIS A N   
822  C CA  . HIS A 104 ? 0.13336 0.11800 0.11084 -0.00264 -0.00584 0.00189  104 HIS A CA  
823  C C   . HIS A 104 ? 0.15065 0.13713 0.12556 -0.00310 -0.00730 0.00002  104 HIS A C   
824  O O   . HIS A 104 ? 0.12292 0.10939 0.09928 -0.00418 -0.00702 -0.00159 104 HIS A O   
825  C CB  . HIS A 104 ? 0.15347 0.13602 0.12991 -0.00276 -0.00282 0.00255  104 HIS A CB  
826  C CG  . HIS A 104 ? 0.15446 0.13594 0.12431 -0.00190 -0.00202 0.00322  104 HIS A CG  
827  N ND1 . HIS A 104 ? 0.19390 0.17389 0.16012 -0.00049 -0.00184 0.00555  104 HIS A ND1 
828  C CD2 . HIS A 104 ? 0.14819 0.12953 0.11373 -0.00210 -0.00136 0.00184  104 HIS A CD2 
829  C CE1 . HIS A 104 ? 0.19727 0.17665 0.15677 0.00030  -0.00139 0.00579  104 HIS A CE1 
830  N NE2 . HIS A 104 ? 0.20454 0.18485 0.16352 -0.00084 -0.00111 0.00326  104 HIS A NE2 
831  N N   . ASP A 105 ? 0.17606 0.16410 0.14731 -0.00223 -0.00888 0.00019  105 ASP A N   
832  C CA  . ASP A 105 ? 0.16953 0.16017 0.13873 -0.00303 -0.01059 -0.00206 105 ASP A CA  
833  C C   . ASP A 105 ? 0.17105 0.16178 0.13386 -0.00212 -0.01082 -0.00191 105 ASP A C   
834  O O   . ASP A 105 ? 0.20879 0.19853 0.16869 -0.00018 -0.01066 0.00059  105 ASP A O   
835  C CB  . ASP A 105 ? 0.18231 0.17676 0.15421 -0.00292 -0.01315 -0.00263 105 ASP A CB  
836  C CG  . ASP A 105 ? 0.19748 0.19488 0.16965 -0.00480 -0.01443 -0.00562 105 ASP A CG  
837  O OD1 . ASP A 105 ? 0.22236 0.21802 0.19237 -0.00623 -0.01329 -0.00736 105 ASP A OD1 
838  O OD2 . ASP A 105 ? 0.17267 0.17403 0.14758 -0.00497 -0.01625 -0.00642 105 ASP A OD2 
839  N N   . THR A 106 ? 0.20975 0.20116 0.16984 -0.00350 -0.01104 -0.00462 106 THR A N   
840  C CA  . THR A 106 ? 0.22946 0.22088 0.18233 -0.00284 -0.01131 -0.00510 106 THR A CA  
841  C C   . THR A 106 ? 0.20217 0.19849 0.15313 -0.00347 -0.01489 -0.00771 106 THR A C   
842  O O   . THR A 106 ? 0.20847 0.20528 0.15300 -0.00342 -0.01558 -0.00916 106 THR A O   
843  C CB  . THR A 106 ? 0.21455 0.20217 0.16478 -0.00393 -0.00804 -0.00657 106 THR A CB  
844  O OG1 . THR A 106 ? 0.21718 0.20452 0.17100 -0.00616 -0.00770 -0.00956 106 THR A OG1 
845  C CG2 . THR A 106 ? 0.20763 0.19166 0.15986 -0.00308 -0.00456 -0.00394 106 THR A CG2 
846  N N   . GLU A 107 ? 0.22460 0.22491 0.18102 -0.00415 -0.01713 -0.00860 107 GLU A N   
847  C CA  . GLU A 107 ? 0.24015 0.24643 0.19635 -0.00492 -0.02065 -0.01128 107 GLU A CA  
848  C C   . GLU A 107 ? 0.25941 0.26915 0.21155 -0.00161 -0.02360 -0.00908 107 GLU A C   
849  O O   . GLU A 107 ? 0.23939 0.24682 0.19101 0.00115  -0.02280 -0.00520 107 GLU A O   
850  C CB  . GLU A 107 ? 0.21924 0.22904 0.18314 -0.00657 -0.02156 -0.01266 107 GLU A CB  
851  C CG  . GLU A 107 ? 0.21276 0.21900 0.17980 -0.00968 -0.01886 -0.01473 107 GLU A CG  
852  C CD  . GLU A 107 ? 0.20986 0.21996 0.18289 -0.01204 -0.01968 -0.01698 107 GLU A CD  
853  O OE1 . GLU A 107 ? 0.22136 0.23785 0.19694 -0.01135 -0.02245 -0.01731 107 GLU A OE1 
854  O OE2 . GLU A 107 ? 0.22686 0.23355 0.20216 -0.01444 -0.01731 -0.01829 107 GLU A OE2 
855  N N   . PRO A 108 ? 0.27514 0.29025 0.22419 -0.00176 -0.02706 -0.01153 108 PRO A N   
856  C CA  . PRO A 108 ? 0.24668 0.26525 0.19099 0.00211  -0.03028 -0.00906 108 PRO A CA  
857  C C   . PRO A 108 ? 0.26526 0.28679 0.21523 0.00493  -0.03173 -0.00613 108 PRO A C   
858  O O   . PRO A 108 ? 0.29720 0.31631 0.24370 0.00873  -0.03160 -0.00192 108 PRO A O   
859  C CB  . PRO A 108 ? 0.31266 0.33807 0.25457 0.00069  -0.03434 -0.01337 108 PRO A CB  
860  C CG  . PRO A 108 ? 0.32411 0.34611 0.26559 -0.00371 -0.03180 -0.01757 108 PRO A CG  
861  C CD  . PRO A 108 ? 0.23426 0.25187 0.18299 -0.00534 -0.02805 -0.01669 108 PRO A CD  
862  N N   . TYR A 109 ? 0.27642 0.30263 0.23487 0.00320  -0.03267 -0.00825 109 TYR A N   
863  C CA  . TYR A 109 ? 0.26954 0.29826 0.23364 0.00591  -0.03346 -0.00581 109 TYR A CA  
864  C C   . TYR A 109 ? 0.25818 0.27925 0.22312 0.00682  -0.02960 -0.00248 109 TYR A C   
865  O O   . TYR A 109 ? 0.26056 0.28095 0.22679 0.01011  -0.02969 0.00058  109 TYR A O   
866  C CB  . TYR A 109 ? 0.30587 0.34120 0.27884 0.00347  -0.03457 -0.00910 109 TYR A CB  
867  C CG  . TYR A 109 ? 0.29181 0.32855 0.27114 0.00577  -0.03410 -0.00702 109 TYR A CG  
868  C CD1 . TYR A 109 ? 0.31066 0.35250 0.29115 0.01015  -0.03701 -0.00504 109 TYR A CD1 
869  C CD2 . TYR A 109 ? 0.30249 0.33530 0.28626 0.00386  -0.03074 -0.00706 109 TYR A CD2 
870  C CE1 . TYR A 109 ? 0.34264 0.38524 0.32893 0.01244  -0.03614 -0.00340 109 TYR A CE1 
871  C CE2 . TYR A 109 ? 0.32866 0.36235 0.31748 0.00588  -0.03004 -0.00559 109 TYR A CE2 
872  C CZ  . TYR A 109 ? 0.34109 0.37949 0.33136 0.01011  -0.03253 -0.00388 109 TYR A CZ  
873  O OH  . TYR A 109 ? 0.42559 0.46439 0.42093 0.01230  -0.03140 -0.00267 109 TYR A OH  
874  N N   . ALA A 110 ? 0.23662 0.25203 0.20112 0.00402  -0.02627 -0.00322 110 ALA A N   
875  C CA  . ALA A 110 ? 0.22540 0.23461 0.19146 0.00442  -0.02302 -0.00071 110 ALA A CA  
876  C C   . ALA A 110 ? 0.21832 0.22277 0.17888 0.00732  -0.02180 0.00308  110 ALA A C   
877  O O   . ALA A 110 ? 0.23832 0.23970 0.20072 0.00908  -0.02051 0.00567  110 ALA A O   
878  C CB  . ALA A 110 ? 0.22710 0.23245 0.19428 0.00112  -0.02022 -0.00242 110 ALA A CB  
879  N N   . LYS A 111 ? 0.21855 0.22182 0.17199 0.00773  -0.02183 0.00336  111 LYS A N   
880  C CA  . LYS A 111 ? 0.26876 0.26667 0.21619 0.01025  -0.01986 0.00723  111 LYS A CA  
881  C C   . LYS A 111 ? 0.26329 0.26226 0.20957 0.01449  -0.02188 0.01051  111 LYS A C   
882  O O   . LYS A 111 ? 0.25699 0.25042 0.20261 0.01636  -0.01946 0.01400  111 LYS A O   
883  C CB  . LYS A 111 ? 0.26400 0.26074 0.20305 0.00996  -0.01941 0.00667  111 LYS A CB  
884  C CG  . LYS A 111 ? 0.31003 0.30474 0.25004 0.00633  -0.01677 0.00366  111 LYS A CG  
885  C CD  . LYS A 111 ? 0.37537 0.36865 0.30656 0.00622  -0.01599 0.00276  111 LYS A CD  
886  C CE  . LYS A 111 ? 0.27873 0.26953 0.21134 0.00306  -0.01294 -0.00023 111 LYS A CE  
887  N NZ  . LYS A 111 ? 0.34299 0.33207 0.26669 0.00292  -0.01175 -0.00161 111 LYS A NZ  
888  N N   . VAL A 112 ? 0.22661 0.23268 0.17308 0.01609  -0.02622 0.00935  112 VAL A N   
889  C CA  . VAL A 112 ? 0.23598 0.24386 0.18228 0.02077  -0.02845 0.01248  112 VAL A CA  
890  C C   . VAL A 112 ? 0.21032 0.21704 0.16469 0.02116  -0.02706 0.01308  112 VAL A C   
891  O O   . VAL A 112 ? 0.21619 0.21904 0.17003 0.02467  -0.02609 0.01667  112 VAL A O   
892  C CB  . VAL A 112 ? 0.24097 0.25845 0.18700 0.02229  -0.03386 0.01052  112 VAL A CB  
893  C CG1 . VAL A 112 ? 0.27677 0.29655 0.22273 0.02798  -0.03639 0.01413  112 VAL A CG1 
894  C CG2 . VAL A 112 ? 0.30443 0.32276 0.24162 0.02150  -0.03526 0.00923  112 VAL A CG2 
895  N N   . ARG A 113 ? 0.23890 0.24828 0.20023 0.01763  -0.02666 0.00958  113 ARG A N   
896  C CA  . ARG A 113 ? 0.24214 0.25029 0.21026 0.01770  -0.02514 0.00968  113 ARG A CA  
897  C C   . ARG A 113 ? 0.22793 0.22727 0.19510 0.01706  -0.02108 0.01171  113 ARG A C   
898  O O   . ARG A 113 ? 0.24291 0.23864 0.21178 0.01924  -0.01976 0.01375  113 ARG A O   
899  C CB  . ARG A 113 ? 0.23244 0.24510 0.20686 0.01400  -0.02541 0.00565  113 ARG A CB  
900  C CG  . ARG A 113 ? 0.24154 0.25224 0.22169 0.01351  -0.02336 0.00535  113 ARG A CG  
901  C CD  . ARG A 113 ? 0.20091 0.21338 0.18487 0.00937  -0.02254 0.00202  113 ARG A CD  
902  N NE  . ARG A 113 ? 0.20668 0.21502 0.18744 0.00656  -0.02095 0.00144  113 ARG A NE  
903  C CZ  . ARG A 113 ? 0.21988 0.22835 0.20244 0.00324  -0.02004 -0.00092 113 ARG A CZ  
904  N NH1 . ARG A 113 ? 0.21259 0.22477 0.19967 0.00184  -0.02028 -0.00293 113 ARG A NH1 
905  N NH2 . ARG A 113 ? 0.17663 0.18121 0.15642 0.00146  -0.01852 -0.00112 113 ARG A NH2 
906  N N   . ASP A 114 ? 0.21346 0.20939 0.17841 0.01401  -0.01895 0.01090  114 ASP A N   
907  C CA  . ASP A 114 ? 0.23560 0.22451 0.20102 0.01286  -0.01525 0.01225  114 ASP A CA  
908  C C   . ASP A 114 ? 0.24859 0.23167 0.20905 0.01570  -0.01342 0.01631  114 ASP A C   
909  O O   . ASP A 114 ? 0.24562 0.22306 0.20793 0.01557  -0.01062 0.01770  114 ASP A O   
910  C CB  . ASP A 114 ? 0.21907 0.20680 0.18407 0.00934  -0.01350 0.01042  114 ASP A CB  
911  C CG  . ASP A 114 ? 0.21006 0.20167 0.17983 0.00661  -0.01453 0.00695  114 ASP A CG  
912  O OD1 . ASP A 114 ? 0.21839 0.21365 0.19181 0.00707  -0.01628 0.00587  114 ASP A OD1 
913  O OD2 . ASP A 114 ? 0.17562 0.16637 0.14545 0.00419  -0.01327 0.00545  114 ASP A OD2 
914  N N   . ALA A 115 ? 0.24946 0.23349 0.20329 0.01819  -0.01487 0.01820  115 ALA A N   
915  C CA  . ALA A 115 ? 0.24580 0.22353 0.19373 0.02130  -0.01286 0.02270  115 ALA A CA  
916  C C   . ALA A 115 ? 0.27716 0.25299 0.22756 0.02491  -0.01321 0.02503  115 ALA A C   
917  O O   . ALA A 115 ? 0.34059 0.30865 0.28980 0.02599  -0.00981 0.02802  115 ALA A O   
918  C CB  . ALA A 115 ? 0.26385 0.24345 0.20297 0.02359  -0.01482 0.02421  115 ALA A CB  
919  N N   . ALA A 116 ? 0.23213 0.21478 0.18637 0.02674  -0.01691 0.02357  116 ALA A N   
920  C CA  . ALA A 116 ? 0.26211 0.24335 0.21920 0.03066  -0.01711 0.02558  116 ALA A CA  
921  C C   . ALA A 116 ? 0.22218 0.19858 0.18529 0.02843  -0.01389 0.02425  116 ALA A C   
922  O O   . ALA A 116 ? 0.22983 0.20016 0.19335 0.03100  -0.01182 0.02662  116 ALA A O   
923  C CB  . ALA A 116 ? 0.28074 0.27173 0.24162 0.03299  -0.02169 0.02391  116 ALA A CB  
924  N N   . VAL A 117 ? 0.20904 0.18761 0.17639 0.02380  -0.01341 0.02046  117 VAL A N   
925  C CA  . VAL A 117 ? 0.22909 0.20394 0.20158 0.02160  -0.01098 0.01872  117 VAL A CA  
926  C C   . VAL A 117 ? 0.23341 0.19954 0.20409 0.02007  -0.00698 0.02041  117 VAL A C   
927  O O   . VAL A 117 ? 0.23005 0.19065 0.20321 0.02010  -0.00464 0.02054  117 VAL A O   
928  C CB  . VAL A 117 ? 0.23876 0.21871 0.21549 0.01758  -0.01196 0.01455  117 VAL A CB  
929  C CG1 . VAL A 117 ? 0.24007 0.21642 0.22096 0.01539  -0.00984 0.01267  117 VAL A CG1 
930  C CG2 . VAL A 117 ? 0.24125 0.22943 0.22057 0.01869  -0.01519 0.01280  117 VAL A CG2 
931  N N   . ARG A 118 ? 0.21827 0.18304 0.18489 0.01849  -0.00584 0.02143  118 ARG A N   
932  C CA  . ARG A 118 ? 0.26070 0.21766 0.22604 0.01693  -0.00158 0.02321  118 ARG A CA  
933  C C   . ARG A 118 ? 0.25421 0.20386 0.21607 0.02069  0.00051  0.02740  118 ARG A C   
934  O O   . ARG A 118 ? 0.30366 0.24587 0.26706 0.01944  0.00432  0.02819  118 ARG A O   
935  C CB  . ARG A 118 ? 0.27279 0.23012 0.23404 0.01512  -0.00043 0.02374  118 ARG A CB  
936  C CG  . ARG A 118 ? 0.27072 0.23357 0.23553 0.01145  -0.00158 0.01990  118 ARG A CG  
937  C CD  . ARG A 118 ? 0.29951 0.26159 0.26050 0.00996  0.00048  0.02048  118 ARG A CD  
938  N NE  . ARG A 118 ? 0.32961 0.29644 0.29389 0.00704  -0.00046 0.01705  118 ARG A NE  
939  C CZ  . ARG A 118 ? 0.33866 0.31037 0.30070 0.00716  -0.00304 0.01542  118 ARG A CZ  
940  N NH1 . ARG A 118 ? 0.37842 0.35218 0.33524 0.00981  -0.00547 0.01650  118 ARG A NH1 
941  N NH2 . ARG A 118 ? 0.31107 0.28568 0.27631 0.00462  -0.00325 0.01257  118 ARG A NH2 
942  N N   . ARG A 119 ? 0.29401 0.24562 0.25126 0.02536  -0.00195 0.03009  119 ARG A N   
943  C CA  . ARG A 119 ? 0.25529 0.19993 0.20896 0.02996  -0.00032 0.03456  119 ARG A CA  
944  C C   . ARG A 119 ? 0.26714 0.20872 0.22674 0.03080  0.00064  0.03340  119 ARG A C   
945  O O   . ARG A 119 ? 0.28186 0.21404 0.24106 0.03151  0.00454  0.03554  119 ARG A O   
946  C CB  . ARG A 119 ? 0.32851 0.27794 0.27665 0.03522  -0.00426 0.03726  119 ARG A CB  
947  C CG  . ARG A 119 ? 0.31418 0.25679 0.25768 0.04110  -0.00312 0.04260  119 ARG A CG  
948  C CD  . ARG A 119 ? 0.33166 0.28198 0.27221 0.04660  -0.00845 0.04419  119 ARG A CD  
949  N NE  . ARG A 119 ? 0.34810 0.30647 0.28498 0.04490  -0.01187 0.04238  119 ARG A NE  
950  C CZ  . ARG A 119 ? 0.37338 0.32959 0.30082 0.04593  -0.01158 0.04526  119 ARG A CZ  
951  N NH1 . ARG A 119 ? 0.38413 0.33031 0.30449 0.04870  -0.00787 0.05060  119 ARG A NH1 
952  N NH2 . ARG A 119 ? 0.38120 0.34495 0.30584 0.04404  -0.01473 0.04266  119 ARG A NH2 
953  N N   . LEU A 120 ? 0.28230 0.23132 0.24733 0.03058  -0.00248 0.02983  120 LEU A N   
954  C CA  . LEU A 120 ? 0.24249 0.18918 0.21289 0.03129  -0.00147 0.02810  120 LEU A CA  
955  C C   . LEU A 120 ? 0.20228 0.14340 0.17614 0.02630  0.00196  0.02531  120 LEU A C   
956  O O   . LEU A 120 ? 0.20807 0.14248 0.18406 0.02683  0.00459  0.02502  120 LEU A O   
957  C CB  . LEU A 120 ? 0.22399 0.18049 0.19907 0.03182  -0.00519 0.02482  120 LEU A CB  
958  C CG  . LEU A 120 ? 0.21525 0.17918 0.18875 0.03648  -0.00915 0.02669  120 LEU A CG  
959  C CD1 . LEU A 120 ? 0.19124 0.16566 0.17010 0.03513  -0.01231 0.02270  120 LEU A CD1 
960  C CD2 . LEU A 120 ? 0.27239 0.23216 0.24517 0.04275  -0.00857 0.03032  120 LEU A CD2 
961  N N   . ALA A 121 ? 0.20977 0.15366 0.18441 0.02155  0.00192  0.02307  121 ALA A N   
962  C CA  . ALA A 121 ? 0.22912 0.16910 0.20751 0.01683  0.00459  0.02027  121 ALA A CA  
963  C C   . ALA A 121 ? 0.22955 0.15986 0.20605 0.01607  0.00916  0.02296  121 ALA A C   
964  O O   . ALA A 121 ? 0.20254 0.12727 0.18253 0.01347  0.01191  0.02107  121 ALA A O   
965  C CB  . ALA A 121 ? 0.19715 0.14352 0.17738 0.01265  0.00303  0.01739  121 ALA A CB  
966  N N   . ALA A 122 ? 0.26504 0.19307 0.23581 0.01810  0.01021  0.02721  122 ALA A N   
967  C CA  . ALA A 122 ? 0.24607 0.16418 0.21443 0.01748  0.01528  0.03034  122 ALA A CA  
968  C C   . ALA A 122 ? 0.26404 0.17326 0.23174 0.02093  0.01764  0.03262  122 ALA A C   
969  O O   . ALA A 122 ? 0.27129 0.17153 0.24065 0.01868  0.02225  0.03276  122 ALA A O   
970  C CB  . ALA A 122 ? 0.22288 0.14055 0.18387 0.01926  0.01597  0.03458  122 ALA A CB  
971  N N   . GLU A 123 ? 0.23900 0.15058 0.20478 0.02640  0.01471  0.03428  123 GLU A N   
972  C CA  . GLU A 123 ? 0.26972 0.17312 0.23534 0.03045  0.01685  0.03639  123 GLU A CA  
973  C C   . GLU A 123 ? 0.24839 0.14967 0.22074 0.02763  0.01804  0.03148  123 GLU A C   
974  O O   . GLU A 123 ? 0.27038 0.16221 0.24319 0.02938  0.02142  0.03240  123 GLU A O   
975  C CB  . GLU A 123 ? 0.29237 0.20070 0.25535 0.03733  0.01295  0.03910  123 GLU A CB  
976  C CG  . GLU A 123 ? 0.28428 0.19405 0.23934 0.04091  0.01147  0.04415  123 GLU A CG  
977  C CD  . GLU A 123 ? 0.27994 0.19729 0.23363 0.04727  0.00649  0.04589  123 GLU A CD  
978  O OE1 . GLU A 123 ? 0.28923 0.21138 0.24892 0.04859  0.00447  0.04301  123 GLU A OE1 
979  O OE2 . GLU A 123 ? 0.27717 0.19607 0.22383 0.05093  0.00462  0.04998  123 GLU A OE2 
980  N N   . ALA A 124 ? 0.23366 0.14298 0.21062 0.02347  0.01548  0.02631  124 ALA A N   
981  C CA  . ALA A 124 ? 0.24460 0.15265 0.22690 0.02044  0.01623  0.02123  124 ALA A CA  
982  C C   . ALA A 124 ? 0.21452 0.11969 0.19991 0.01390  0.01869  0.01813  124 ALA A C   
983  O O   . ALA A 124 ? 0.23073 0.13500 0.22016 0.01081  0.01908  0.01347  124 ALA A O   
984  C CB  . ALA A 124 ? 0.23702 0.15568 0.22201 0.02044  0.01183  0.01759  124 ALA A CB  
985  N N   . GLY A 125 ? 0.24777 0.15196 0.23148 0.01174  0.02033  0.02039  125 GLY A N   
986  C CA  . GLY A 125 ? 0.23210 0.13488 0.21999 0.00557  0.02266  0.01744  125 GLY A CA  
987  C C   . GLY A 125 ? 0.21837 0.13134 0.21021 0.00187  0.01896  0.01292  125 GLY A C   
988  O O   . GLY A 125 ? 0.23134 0.14444 0.22812 -0.00294 0.01975  0.00895  125 GLY A O   
989  N N   . VAL A 126 ? 0.23189 0.15340 0.22175 0.00400  0.01491  0.01339  126 VAL A N   
990  C CA  . VAL A 126 ? 0.17120 0.10177 0.16403 0.00125  0.01143  0.00967  126 VAL A CA  
991  C C   . VAL A 126 ? 0.17652 0.11094 0.16888 -0.00050 0.01153  0.01099  126 VAL A C   
992  O O   . VAL A 126 ? 0.18801 0.12263 0.17570 0.00216  0.01165  0.01466  126 VAL A O   
993  C CB  . VAL A 126 ? 0.17987 0.11684 0.17132 0.00429  0.00751  0.00896  126 VAL A CB  
994  C CG1 . VAL A 126 ? 0.15238 0.09751 0.14605 0.00161  0.00442  0.00573  126 VAL A CG1 
995  C CG2 . VAL A 126 ? 0.17427 0.10756 0.16651 0.00619  0.00796  0.00744  126 VAL A CG2 
996  N N   . GLU A 127 ? 0.15732 0.09500 0.15442 -0.00477 0.01143  0.00787  127 GLU A N   
997  C CA  . GLU A 127 ? 0.17126 0.11330 0.16893 -0.00635 0.01162  0.00858  127 GLU A CA  
998  C C   . GLU A 127 ? 0.18404 0.13372 0.17964 -0.00466 0.00763  0.00823  127 GLU A C   
999  O O   . GLU A 127 ? 0.16476 0.11830 0.16145 -0.00445 0.00455  0.00574  127 GLU A O   
1000 C CB  . GLU A 127 ? 0.20270 0.14678 0.20725 -0.01108 0.01249  0.00518  127 GLU A CB  
1001 C CG  . GLU A 127 ? 0.22742 0.17667 0.23385 -0.01255 0.01287  0.00551  127 GLU A CG  
1002 C CD  . GLU A 127 ? 0.24123 0.19476 0.25564 -0.01670 0.01260  0.00171  127 GLU A CD  
1003 O OE1 . GLU A 127 ? 0.28915 0.24182 0.30703 -0.01868 0.01171  -0.00147 127 GLU A OE1 
1004 O OE2 . GLU A 127 ? 0.26322 0.22131 0.28053 -0.01786 0.01318  0.00170  127 GLU A OE2 
1005 N N   . VAL A 128 ? 0.19510 0.14647 0.18736 -0.00360 0.00805  0.01062  128 VAL A N   
1006 C CA  . VAL A 128 ? 0.17951 0.13719 0.16954 -0.00227 0.00483  0.01027  128 VAL A CA  
1007 C C   . VAL A 128 ? 0.16157 0.12306 0.15425 -0.00466 0.00534  0.00909  128 VAL A C   
1008 O O   . VAL A 128 ? 0.18215 0.14150 0.17427 -0.00544 0.00852  0.01072  128 VAL A O   
1009 C CB  . VAL A 128 ? 0.18457 0.14146 0.16794 0.00127  0.00443  0.01351  128 VAL A CB  
1010 C CG1 . VAL A 128 ? 0.21258 0.17593 0.19425 0.00188  0.00129  0.01242  128 VAL A CG1 
1011 C CG2 . VAL A 128 ? 0.19041 0.14414 0.17208 0.00427  0.00383  0.01482  128 VAL A CG2 
1012 N N   . VAL A 129 ? 0.14154 0.10840 0.13698 -0.00557 0.00251  0.00645  129 VAL A N   
1013 C CA  . VAL A 129 ? 0.15877 0.12971 0.15705 -0.00708 0.00254  0.00530  129 VAL A CA  
1014 C C   . VAL A 129 ? 0.15728 0.13194 0.15245 -0.00559 -0.00003 0.00501  129 VAL A C   
1015 O O   . VAL A 129 ? 0.14842 0.12516 0.14361 -0.00512 -0.00275 0.00365  129 VAL A O   
1016 C CB  . VAL A 129 ? 0.13009 0.10377 0.13503 -0.00953 0.00158  0.00241  129 VAL A CB  
1017 C CG1 . VAL A 129 ? 0.20747 0.18581 0.21578 -0.01032 0.00148  0.00156  129 VAL A CG1 
1018 C CG2 . VAL A 129 ? 0.18477 0.15467 0.19339 -0.01168 0.00423  0.00205  129 VAL A CG2 
1019 N N   . THR A 130 ? 0.15270 0.12783 0.14502 -0.00503 0.00120  0.00611  130 THR A N   
1020 C CA  . THR A 130 ? 0.13121 0.10902 0.12023 -0.00396 -0.00070 0.00560  130 THR A CA  
1021 C C   . THR A 130 ? 0.13127 0.11111 0.12233 -0.00482 0.00042  0.00465  130 THR A C   
1022 O O   . THR A 130 ? 0.13696 0.11576 0.12510 -0.00450 0.00265  0.00551  130 THR A O   
1023 C CB  . THR A 130 ? 0.14039 0.11668 0.12284 -0.00207 -0.00061 0.00743  130 THR A CB  
1024 O OG1 . THR A 130 ? 0.10873 0.08216 0.08865 -0.00205 0.00272  0.00924  130 THR A OG1 
1025 C CG2 . THR A 130 ? 0.13744 0.11210 0.11855 -0.00052 -0.00180 0.00857  130 THR A CG2 
1026 N N   . PRO A 131 ? 0.11529 0.09789 0.11095 -0.00559 -0.00099 0.00294  131 PRO A N   
1027 C CA  . PRO A 131 ? 0.12594 0.11053 0.12389 -0.00571 -0.00007 0.00217  131 PRO A CA  
1028 C C   . PRO A 131 ? 0.14807 0.13277 0.14179 -0.00478 -0.00094 0.00167  131 PRO A C   
1029 O O   . PRO A 131 ? 0.14139 0.12594 0.13185 -0.00440 -0.00294 0.00147  131 PRO A O   
1030 C CB  . PRO A 131 ? 0.12585 0.11339 0.12967 -0.00631 -0.00196 0.00080  131 PRO A CB  
1031 C CG  . PRO A 131 ? 0.13552 0.12251 0.13757 -0.00625 -0.00453 0.00042  131 PRO A CG  
1032 C CD  . PRO A 131 ? 0.13286 0.11670 0.13151 -0.00608 -0.00340 0.00171  131 PRO A CD  
1033 N N   . ILE A 132 ? 0.10945 0.09447 0.10378 -0.00454 0.00088  0.00122  132 ILE A N   
1034 C CA  . ILE A 132 ? 0.12269 0.10698 0.11322 -0.00400 0.00075  0.00028  132 ILE A CA  
1035 C C   . ILE A 132 ? 0.11238 0.09786 0.10641 -0.00360 -0.00047 -0.00062 132 ILE A C   
1036 O O   . ILE A 132 ? 0.10251 0.08949 0.10144 -0.00310 0.00047  -0.00066 132 ILE A O   
1037 C CB  . ILE A 132 ? 0.15103 0.13380 0.13879 -0.00373 0.00403  0.00022  132 ILE A CB  
1038 C CG1 . ILE A 132 ? 0.14487 0.12587 0.12744 -0.00372 0.00507  0.00162  132 ILE A CG1 
1039 C CG2 . ILE A 132 ? 0.12241 0.10399 0.10672 -0.00348 0.00406  -0.00145 132 ILE A CG2 
1040 C CD1 . ILE A 132 ? 0.13969 0.11891 0.11906 -0.00348 0.00893  0.00193  132 ILE A CD1 
1041 N N   . SER A 133 ? 0.09928 0.08421 0.09096 -0.00368 -0.00244 -0.00121 133 SER A N   
1042 C CA  . SER A 133 ? 0.10821 0.09309 0.10181 -0.00307 -0.00331 -0.00156 133 SER A CA  
1043 C C   . SER A 133 ? 0.09423 0.07696 0.08405 -0.00355 -0.00361 -0.00248 133 SER A C   
1044 O O   . SER A 133 ? 0.11625 0.09769 0.10678 -0.00298 -0.00379 -0.00244 133 SER A O   
1045 C CB  . SER A 133 ? 0.10294 0.08981 0.09949 -0.00295 -0.00566 -0.00103 133 SER A CB  
1046 O OG  . SER A 133 ? 0.08582 0.07274 0.08011 -0.00378 -0.00708 -0.00103 133 SER A OG  
1047 N N   . HIS A 134 ? 0.09260 0.07495 0.07854 -0.00457 -0.00368 -0.00329 134 HIS A N   
1048 C CA  . HIS A 134 ? 0.09474 0.07565 0.07805 -0.00565 -0.00385 -0.00476 134 HIS A CA  
1049 C C   . HIS A 134 ? 0.09868 0.07657 0.08043 -0.00568 -0.00152 -0.00615 134 HIS A C   
1050 O O   . HIS A 134 ? 0.10081 0.07607 0.08211 -0.00626 -0.00087 -0.00712 134 HIS A O   
1051 C CB  . HIS A 134 ? 0.09465 0.07752 0.07521 -0.00666 -0.00528 -0.00548 134 HIS A CB  
1052 C CG  . HIS A 134 ? 0.09873 0.08125 0.07764 -0.00835 -0.00556 -0.00754 134 HIS A CG  
1053 N ND1 . HIS A 134 ? 0.09587 0.07764 0.07638 -0.00921 -0.00570 -0.00774 134 HIS A ND1 
1054 C CD2 . HIS A 134 ? 0.10022 0.08308 0.07605 -0.00959 -0.00561 -0.00969 134 HIS A CD2 
1055 C CE1 . HIS A 134 ? 0.10036 0.08197 0.07964 -0.01121 -0.00551 -0.00998 134 HIS A CE1 
1056 N NE2 . HIS A 134 ? 0.10110 0.08370 0.07768 -0.01152 -0.00575 -0.01143 134 HIS A NE2 
1057 N N   . THR A 135 ? 0.10268 0.08035 0.08337 -0.00510 0.00019  -0.00631 135 THR A N   
1058 C CA  . THR A 135 ? 0.11032 0.08491 0.08942 -0.00486 0.00294  -0.00786 135 THR A CA  
1059 C C   . THR A 135 ? 0.10514 0.07952 0.08878 -0.00286 0.00485  -0.00668 135 THR A C   
1060 O O   . THR A 135 ? 0.10135 0.07859 0.08916 -0.00204 0.00388  -0.00491 135 THR A O   
1061 C CB  . THR A 135 ? 0.10968 0.08416 0.08359 -0.00547 0.00393  -0.00914 135 THR A CB  
1062 O OG1 . THR A 135 ? 0.11492 0.09144 0.08934 -0.00461 0.00426  -0.00716 135 THR A OG1 
1063 C CG2 . THR A 135 ? 0.11071 0.08644 0.08074 -0.00721 0.00152  -0.01067 135 THR A CG2 
1064 N N   . LEU A 136 ? 0.11694 0.08811 0.10014 -0.00209 0.00763  -0.00797 136 LEU A N   
1065 C CA  . LEU A 136 ? 0.10981 0.08134 0.09817 0.00026  0.00960  -0.00701 136 LEU A CA  
1066 C C   . LEU A 136 ? 0.10887 0.08363 0.09933 0.00061  0.01108  -0.00626 136 LEU A C   
1067 O O   . LEU A 136 ? 0.10715 0.08555 0.10353 0.00152  0.01040  -0.00472 136 LEU A O   
1068 C CB  . LEU A 136 ? 0.11587 0.08261 0.10305 0.00126  0.01278  -0.00875 136 LEU A CB  
1069 C CG  . LEU A 136 ? 0.11798 0.08051 0.10482 0.00152  0.01231  -0.00889 136 LEU A CG  
1070 C CD1 . LEU A 136 ? 0.13655 0.09330 0.12193 0.00245  0.01612  -0.01090 136 LEU A CD1 
1071 C CD2 . LEU A 136 ? 0.11455 0.07920 0.10658 0.00377  0.01032  -0.00610 136 LEU A CD2 
1072 N N   . TYR A 137 ? 0.11287 0.08629 0.09833 -0.00026 0.01323  -0.00742 137 TYR A N   
1073 C CA  . TYR A 137 ? 0.11376 0.08907 0.10000 -0.00012 0.01559  -0.00653 137 TYR A CA  
1074 C C   . TYR A 137 ? 0.11348 0.08949 0.09483 -0.00159 0.01395  -0.00562 137 TYR A C   
1075 O O   . TYR A 137 ? 0.11266 0.08829 0.09018 -0.00256 0.01098  -0.00604 137 TYR A O   
1076 C CB  . TYR A 137 ? 0.12212 0.09476 0.10548 0.00056  0.02016  -0.00820 137 TYR A CB  
1077 C CG  . TYR A 137 ? 0.12219 0.09346 0.11017 0.00257  0.02238  -0.00917 137 TYR A CG  
1078 C CD1 . TYR A 137 ? 0.14293 0.10973 0.12779 0.00268  0.02238  -0.01112 137 TYR A CD1 
1079 C CD2 . TYR A 137 ? 0.12304 0.09746 0.11893 0.00442  0.02469  -0.00819 137 TYR A CD2 
1080 C CE1 . TYR A 137 ? 0.14040 0.10494 0.12922 0.00500  0.02472  -0.01170 137 TYR A CE1 
1081 C CE2 . TYR A 137 ? 0.12418 0.09762 0.12469 0.00696  0.02665  -0.00884 137 TYR A CE2 
1082 C CZ  . TYR A 137 ? 0.13717 0.10518 0.13376 0.00745  0.02673  -0.01042 137 TYR A CZ  
1083 O OH  . TYR A 137 ? 0.17282 0.13888 0.17376 0.01044  0.02895  -0.01077 137 TYR A OH  
1084 N N   . ASP A 138 ? 0.12121 0.09824 0.10311 -0.00160 0.01621  -0.00424 138 ASP A N   
1085 C CA  . ASP A 138 ? 0.13973 0.11598 0.11540 -0.00234 0.01586  -0.00308 138 ASP A CA  
1086 C C   . ASP A 138 ? 0.14473 0.11810 0.11141 -0.00235 0.01727  -0.00478 138 ASP A C   
1087 O O   . ASP A 138 ? 0.15829 0.13001 0.12291 -0.00188 0.02143  -0.00537 138 ASP A O   
1088 C CB  . ASP A 138 ? 0.15178 0.12884 0.13049 -0.00246 0.01875  -0.00098 138 ASP A CB  
1089 C CG  . ASP A 138 ? 0.19282 0.16803 0.16471 -0.00273 0.01874  0.00094  138 ASP A CG  
1090 O OD1 . ASP A 138 ? 0.17001 0.14451 0.13568 -0.00258 0.01567  0.00069  138 ASP A OD1 
1091 O OD2 . ASP A 138 ? 0.20585 0.18037 0.17890 -0.00302 0.02193  0.00281  138 ASP A OD2 
1092 N N   . THR A 139 ? 0.13006 0.10321 0.09158 -0.00299 0.01387  -0.00591 139 THR A N   
1093 C CA  . THR A 139 ? 0.16999 0.14103 0.12304 -0.00333 0.01444  -0.00832 139 THR A CA  
1094 C C   . THR A 139 ? 0.16303 0.13280 0.10871 -0.00268 0.01678  -0.00697 139 THR A C   
1095 O O   . THR A 139 ? 0.18647 0.15395 0.12523 -0.00264 0.01902  -0.00898 139 THR A O   
1096 C CB  . THR A 139 ? 0.16814 0.14056 0.11836 -0.00443 0.00991  -0.00989 139 THR A CB  
1097 O OG1 . THR A 139 ? 0.21990 0.19494 0.17069 -0.00407 0.00688  -0.00734 139 THR A OG1 
1098 C CG2 . THR A 139 ? 0.15823 0.13041 0.11403 -0.00529 0.00881  -0.01158 139 THR A CG2 
1099 N N   . ASP A 140 ? 0.18747 0.15804 0.13390 -0.00214 0.01659  -0.00361 140 ASP A N   
1100 C CA  . ASP A 140 ? 0.17697 0.14535 0.11633 -0.00134 0.01962  -0.00158 140 ASP A CA  
1101 C C   . ASP A 140 ? 0.19136 0.15810 0.13345 -0.00124 0.02562  -0.00132 140 ASP A C   
1102 O O   . ASP A 140 ? 0.18476 0.14887 0.11948 -0.00071 0.02932  -0.00060 140 ASP A O   
1103 C CB  . ASP A 140 ? 0.19207 0.16074 0.13157 -0.00074 0.01805  0.00212  140 ASP A CB  
1104 C CG  . ASP A 140 ? 0.23214 0.20284 0.16845 -0.00029 0.01250  0.00201  140 ASP A CG  
1105 O OD1 . ASP A 140 ? 0.27342 0.24507 0.20446 -0.00049 0.01026  -0.00068 140 ASP A OD1 
1106 O OD2 . ASP A 140 ? 0.22232 0.19384 0.16179 0.00019  0.01050  0.00432  140 ASP A OD2 
1107 N N   . MET A 141 ? 0.18722 0.15581 0.13969 -0.00157 0.02669  -0.00185 141 MET A N   
1108 C CA  . MET A 141 ? 0.17927 0.14758 0.13605 -0.00131 0.03230  -0.00202 141 MET A CA  
1109 C C   . MET A 141 ? 0.18403 0.15021 0.13668 -0.00074 0.03487  -0.00526 141 MET A C   
1110 O O   . MET A 141 ? 0.20129 0.16574 0.15145 -0.00027 0.04028  -0.00551 141 MET A O   
1111 C CB  . MET A 141 ? 0.20702 0.17905 0.17671 -0.00151 0.03189  -0.00163 141 MET A CB  
1112 C CG  . MET A 141 ? 0.21426 0.18767 0.19082 -0.00102 0.03724  -0.00211 141 MET A CG  
1113 S SD  . MET A 141 ? 0.25309 0.22691 0.23394 0.00059  0.03769  -0.00528 141 MET A SD  
1114 C CE  . MET A 141 ? 0.13486 0.11222 0.12398 0.00064  0.03151  -0.00482 141 MET A CE  
1115 N N   . LEU A 142 ? 0.18118 0.14703 0.13302 -0.00089 0.03154  -0.00790 142 LEU A N   
1116 C CA  . LEU A 142 ? 0.19667 0.15946 0.14405 -0.00059 0.03399  -0.01145 142 LEU A CA  
1117 C C   . LEU A 142 ? 0.19779 0.15770 0.13236 -0.00079 0.03548  -0.01248 142 LEU A C   
1118 O O   . LEU A 142 ? 0.22615 0.18312 0.15629 -0.00034 0.03988  -0.01484 142 LEU A O   
1119 C CB  . LEU A 142 ? 0.15578 0.11808 0.10461 -0.00121 0.03015  -0.01397 142 LEU A CB  
1120 C CG  . LEU A 142 ? 0.17817 0.14257 0.13803 -0.00062 0.02859  -0.01301 142 LEU A CG  
1121 C CD1 . LEU A 142 ? 0.14218 0.10472 0.10172 -0.00137 0.02569  -0.01534 142 LEU A CD1 
1122 C CD2 . LEU A 142 ? 0.19272 0.15743 0.15974 0.00117  0.03322  -0.01288 142 LEU A CD2 
1123 N N   . VAL A 143 ? 0.20087 0.16157 0.12905 -0.00118 0.03188  -0.01079 143 VAL A N   
1124 C CA  . VAL A 143 ? 0.21138 0.16979 0.12652 -0.00090 0.03272  -0.01124 143 VAL A CA  
1125 C C   . VAL A 143 ? 0.22352 0.17979 0.13590 0.00004  0.03894  -0.00874 143 VAL A C   
1126 O O   . VAL A 143 ? 0.23885 0.19203 0.14194 0.00046  0.04267  -0.01032 143 VAL A O   
1127 C CB  . VAL A 143 ? 0.20493 0.16537 0.11487 -0.00090 0.02693  -0.00955 143 VAL A CB  
1128 C CG1 . VAL A 143 ? 0.19417 0.15266 0.08998 -0.00002 0.02738  -0.00941 143 VAL A CG1 
1129 C CG2 . VAL A 143 ? 0.22057 0.18344 0.13336 -0.00219 0.02148  -0.01253 143 VAL A CG2 
1130 N N   . ALA A 144 ? 0.21914 0.17689 0.13949 0.00014  0.04047  -0.00506 144 ALA A N   
1131 C CA  . ALA A 144 ? 0.21492 0.17072 0.13402 0.00054  0.04697  -0.00258 144 ALA A CA  
1132 C C   . ALA A 144 ? 0.22651 0.18190 0.15033 0.00077  0.05292  -0.00506 144 ALA A C   
1133 O O   . ALA A 144 ? 0.24031 0.19301 0.15837 0.00121  0.05899  -0.00478 144 ALA A O   
1134 C CB  . ALA A 144 ? 0.21985 0.17742 0.14753 0.00002  0.04706  0.00137  144 ALA A CB  
1135 N N   . ARG A 145 ? 0.22713 0.18502 0.16128 0.00077  0.05153  -0.00730 145 ARG A N   
1136 C CA  . ARG A 145 ? 0.26651 0.22429 0.20620 0.00164  0.05691  -0.00960 145 ARG A CA  
1137 C C   . ARG A 145 ? 0.24880 0.20218 0.17797 0.00215  0.05921  -0.01351 145 ARG A C   
1138 O O   . ARG A 145 ? 0.26481 0.21683 0.19521 0.00314  0.06534  -0.01521 145 ARG A O   
1139 C CB  . ARG A 145 ? 0.22047 0.18179 0.17337 0.00210  0.05429  -0.01050 145 ARG A CB  
1140 C CG  . ARG A 145 ? 0.24676 0.21298 0.21132 0.00162  0.05295  -0.00742 145 ARG A CG  
1141 C CD  . ARG A 145 ? 0.31324 0.28180 0.28539 0.00191  0.05948  -0.00649 145 ARG A CD  
1142 N NE  . ARG A 145 ? 0.39086 0.36367 0.37594 0.00334  0.06002  -0.00778 145 ARG A NE  
1143 C CZ  . ARG A 145 ? 0.31091 0.28928 0.30800 0.00312  0.05729  -0.00648 145 ARG A CZ  
1144 N NH1 . ARG A 145 ? 0.28478 0.26471 0.28308 0.00122  0.05425  -0.00417 145 ARG A NH1 
1145 N NH2 . ARG A 145 ? 0.30102 0.28342 0.30895 0.00504  0.05754  -0.00762 145 ARG A NH2 
1146 N N   . ASN A 146 ? 0.22342 0.17486 0.14269 0.00145  0.05453  -0.01529 146 ASN A N   
1147 C CA  . ASN A 146 ? 0.24294 0.19023 0.15153 0.00142  0.05599  -0.01972 146 ASN A CA  
1148 C C   . ASN A 146 ? 0.22324 0.16784 0.11695 0.00153  0.05801  -0.01906 146 ASN A C   
1149 O O   . ASN A 146 ? 0.25766 0.19969 0.13986 0.00109  0.05658  -0.02256 146 ASN A O   
1150 C CB  . ASN A 146 ? 0.25720 0.20440 0.16441 0.00018  0.04970  -0.02285 146 ASN A CB  
1151 C CG  . ASN A 146 ? 0.24932 0.19202 0.14990 -0.00020 0.05181  -0.02848 146 ASN A CG  
1152 O OD1 . ASN A 146 ? 0.21866 0.15863 0.12108 0.00097  0.05786  -0.03025 146 ASN A OD1 
1153 N ND2 . ASN A 146 ? 0.27924 0.22130 0.17250 -0.00191 0.04696  -0.03161 146 ASN A ND2 
1154 N N   . GLY A 147 ? 0.27270 0.21771 0.16613 0.00206  0.06130  -0.01466 147 GLY A N   
1155 C CA  . GLY A 147 ? 0.27423 0.21597 0.15304 0.00260  0.06398  -0.01317 147 GLY A CA  
1156 C C   . GLY A 147 ? 0.25957 0.20185 0.12951 0.00270  0.05774  -0.01060 147 GLY A C   
1157 O O   . GLY A 147 ? 0.26993 0.20931 0.12619 0.00362  0.05928  -0.00905 147 GLY A O   
1158 N N   . GLY A 148 ? 0.26490 0.21082 0.14188 0.00208  0.05090  -0.00998 148 GLY A N   
1159 C CA  . GLY A 148 ? 0.25278 0.20000 0.12316 0.00258  0.04486  -0.00746 148 GLY A CA  
1160 C C   . GLY A 148 ? 0.29301 0.24254 0.15945 0.00186  0.03784  -0.01138 148 GLY A C   
1161 O O   . GLY A 148 ? 0.32945 0.28124 0.19170 0.00250  0.03228  -0.00955 148 GLY A O   
1162 N N   . ALA A 149 ? 0.30861 0.25765 0.17671 0.00055  0.03810  -0.01676 149 ALA A N   
1163 C CA  . ALA A 149 ? 0.27655 0.22764 0.14201 -0.00087 0.03203  -0.02114 149 ALA A CA  
1164 C C   . ALA A 149 ? 0.26559 0.21742 0.14357 -0.00244 0.03135  -0.02390 149 ALA A C   
1165 O O   . ALA A 149 ? 0.28914 0.23891 0.17440 -0.00214 0.03631  -0.02410 149 ALA A O   
1166 C CB  . ALA A 149 ? 0.31863 0.26699 0.17017 -0.00125 0.03298  -0.02589 149 ALA A CB  
1167 N N   . ALA A 150 ? 0.21411 0.16906 0.09462 -0.00394 0.02526  -0.02588 150 ALA A N   
1168 C CA  . ALA A 150 ? 0.23632 0.19133 0.12750 -0.00545 0.02453  -0.02819 150 ALA A CA  
1169 C C   . ALA A 150 ? 0.26389 0.21470 0.15129 -0.00693 0.02696  -0.03426 150 ALA A C   
1170 O O   . ALA A 150 ? 0.22397 0.17404 0.10059 -0.00788 0.02580  -0.03792 150 ALA A O   
1171 C CB  . ALA A 150 ? 0.21021 0.16986 0.10579 -0.00673 0.01787  -0.02799 150 ALA A CB  
1172 N N   . PRO A 151 ? 0.23978 0.18759 0.13556 -0.00698 0.03033  -0.03551 151 PRO A N   
1173 C CA  . PRO A 151 ? 0.23556 0.17829 0.12834 -0.00835 0.03293  -0.04138 151 PRO A CA  
1174 C C   . PRO A 151 ? 0.24731 0.19109 0.13816 -0.01150 0.02775  -0.04560 151 PRO A C   
1175 O O   . PRO A 151 ? 0.25799 0.20587 0.15489 -0.01247 0.02307  -0.04382 151 PRO A O   
1176 C CB  . PRO A 151 ? 0.27506 0.21506 0.17919 -0.00705 0.03677  -0.04038 151 PRO A CB  
1177 C CG  . PRO A 151 ? 0.24805 0.19179 0.15895 -0.00479 0.03756  -0.03444 151 PRO A CG  
1178 C CD  . PRO A 151 ? 0.25536 0.20403 0.16328 -0.00548 0.03216  -0.03160 151 PRO A CD  
1179 N N   . LEU A 152 ? 0.28155 0.22169 0.16402 -0.01332 0.02887  -0.05159 152 LEU A N   
1180 C CA  . LEU A 152 ? 0.28708 0.22841 0.16748 -0.01695 0.02429  -0.05663 152 LEU A CA  
1181 C C   . LEU A 152 ? 0.27074 0.20584 0.15607 -0.01913 0.02705  -0.06123 152 LEU A C   
1182 O O   . LEU A 152 ? 0.26178 0.19771 0.14816 -0.02267 0.02364  -0.06513 152 LEU A O   
1183 C CB  . LEU A 152 ? 0.30022 0.24268 0.16675 -0.01808 0.02235  -0.06083 152 LEU A CB  
1184 C CG  . LEU A 152 ? 0.29856 0.24678 0.15840 -0.01583 0.01899  -0.05632 152 LEU A CG  
1185 C CD1 . LEU A 152 ? 0.36453 0.31403 0.20999 -0.01685 0.01635  -0.06083 152 LEU A CD1 
1186 C CD2 . LEU A 152 ? 0.24703 0.20214 0.11489 -0.01578 0.01318  -0.05215 152 LEU A CD2 
1187 N N   . THR A 153 ? 0.28067 0.20957 0.16944 -0.01707 0.03327  -0.06083 153 THR A N   
1188 C CA  . THR A 153 ? 0.30927 0.23104 0.20291 -0.01832 0.03652  -0.06438 153 THR A CA  
1189 C C   . THR A 153 ? 0.27178 0.19272 0.17732 -0.01554 0.03838  -0.05906 153 THR A C   
1190 O O   . THR A 153 ? 0.29111 0.21500 0.20007 -0.01221 0.03972  -0.05403 153 THR A O   
1191 C CB  . THR A 153 ? 0.28325 0.19734 0.16989 -0.01791 0.04265  -0.06946 153 THR A CB  
1192 O OG1 . THR A 153 ? 0.31999 0.23328 0.20831 -0.01363 0.04771  -0.06563 153 THR A OG1 
1193 C CG2 . THR A 153 ? 0.29763 0.21290 0.17098 -0.02035 0.04065  -0.07472 153 THR A CG2 
1194 N N   . MET A 154 ? 0.25042 0.16730 0.16212 -0.01704 0.03847  -0.06027 154 MET A N   
1195 C CA  . MET A 154 ? 0.24806 0.16396 0.17017 -0.01422 0.03977  -0.05529 154 MET A CA  
1196 C C   . MET A 154 ? 0.26532 0.17668 0.18986 -0.01007 0.04592  -0.05425 154 MET A C   
1197 O O   . MET A 154 ? 0.28233 0.19643 0.21453 -0.00664 0.04645  -0.04909 154 MET A O   
1198 C CB  . MET A 154 ? 0.24307 0.15432 0.16972 -0.01665 0.03919  -0.05683 154 MET A CB  
1199 C CG  . MET A 154 ? 0.23997 0.15051 0.17619 -0.01367 0.03966  -0.05133 154 MET A CG  
1200 S SD  . MET A 154 ? 0.32417 0.24527 0.26525 -0.01276 0.03388  -0.04500 154 MET A SD  
1201 C CE  . MET A 154 ? 0.19867 0.12003 0.14756 -0.00709 0.03668  -0.03944 154 MET A CE  
1202 N N   . GLN A 155 ? 0.26643 0.17126 0.18487 -0.01031 0.05058  -0.05936 155 GLN A N   
1203 C CA  . GLN A 155 ? 0.28874 0.18953 0.20980 -0.00611 0.05695  -0.05873 155 GLN A CA  
1204 C C   . GLN A 155 ? 0.27370 0.18128 0.19518 -0.00336 0.05767  -0.05470 155 GLN A C   
1205 O O   . GLN A 155 ? 0.28591 0.19494 0.21553 0.00050  0.06040  -0.05091 155 GLN A O   
1206 C CB  . GLN A 155 ? 0.25166 0.14397 0.16483 -0.00721 0.06197  -0.06563 155 GLN A CB  
1207 C CG  . GLN A 155 ? 0.35016 0.23419 0.26871 -0.00367 0.06845  -0.06630 155 GLN A CG  
1208 C CD  . GLN A 155 ? 0.34269 0.22940 0.26537 0.00138  0.07300  -0.06307 155 GLN A CD  
1209 O OE1 . GLN A 155 ? 0.32118 0.20514 0.23871 0.00241  0.07791  -0.06619 155 GLN A OE1 
1210 N NE2 . GLN A 155 ? 0.30864 0.20162 0.24134 0.00438  0.07109  -0.05669 155 GLN A NE2 
1211 N N   . SER A 156 ? 0.29821 0.21016 0.21119 -0.00528 0.05520  -0.05535 156 SER A N   
1212 C CA  . SER A 156 ? 0.29239 0.20999 0.20513 -0.00309 0.05620  -0.05127 156 SER A CA  
1213 C C   . SER A 156 ? 0.27003 0.19455 0.19197 -0.00211 0.05209  -0.04505 156 SER A C   
1214 O O   . SER A 156 ? 0.28690 0.21523 0.21357 0.00031  0.05409  -0.04115 156 SER A O   
1215 C CB  . SER A 156 ? 0.30184 0.22125 0.20174 -0.00509 0.05467  -0.05330 156 SER A CB  
1216 O OG  . SER A 156 ? 0.30236 0.22652 0.20170 -0.00320 0.05574  -0.04877 156 SER A OG  
1217 N N   . PHE A 157 ? 0.27258 0.19883 0.19728 -0.00417 0.04662  -0.04432 157 PHE A N   
1218 C CA  . PHE A 157 ? 0.22973 0.16207 0.16251 -0.00333 0.04275  -0.03889 157 PHE A CA  
1219 C C   . PHE A 157 ? 0.24556 0.17726 0.18927 -0.00018 0.04501  -0.03608 157 PHE A C   
1220 O O   . PHE A 157 ? 0.22387 0.16088 0.17438 0.00160  0.04408  -0.03172 157 PHE A O   
1221 C CB  . PHE A 157 ? 0.21537 0.14964 0.14779 -0.00632 0.03681  -0.03920 157 PHE A CB  
1222 C CG  . PHE A 157 ? 0.19227 0.13268 0.13133 -0.00570 0.03272  -0.03410 157 PHE A CG  
1223 C CD1 . PHE A 157 ? 0.18355 0.12936 0.11979 -0.00583 0.03018  -0.03157 157 PHE A CD1 
1224 C CD2 . PHE A 157 ? 0.17388 0.11408 0.12135 -0.00485 0.03160  -0.03184 157 PHE A CD2 
1225 C CE1 . PHE A 157 ? 0.16233 0.11307 0.10452 -0.00535 0.02676  -0.02733 157 PHE A CE1 
1226 C CE2 . PHE A 157 ? 0.17294 0.11855 0.12577 -0.00439 0.02793  -0.02765 157 PHE A CE2 
1227 C CZ  . PHE A 157 ? 0.15563 0.10645 0.10607 -0.00476 0.02559  -0.02562 157 PHE A CZ  
1228 N N   . THR A 158 ? 0.24832 0.17349 0.19384 0.00062  0.04791  -0.03860 158 THR A N   
1229 C CA  . THR A 158 ? 0.27098 0.19541 0.22643 0.00439  0.05002  -0.03583 158 THR A CA  
1230 C C   . THR A 158 ? 0.28562 0.21258 0.24478 0.00772  0.05470  -0.03459 158 THR A C   
1231 O O   . THR A 158 ? 0.32235 0.25397 0.29099 0.01059  0.05450  -0.03079 158 THR A O   
1232 C CB  . THR A 158 ? 0.31012 0.22570 0.26569 0.00478  0.05260  -0.03874 158 THR A CB  
1233 O OG1 . THR A 158 ? 0.27209 0.18571 0.22515 0.00121  0.04861  -0.03981 158 THR A OG1 
1234 C CG2 . THR A 158 ? 0.28231 0.19711 0.24780 0.00945  0.05443  -0.03536 158 THR A CG2 
1235 N N   . LYS A 159 ? 0.27913 0.20347 0.23097 0.00729  0.05899  -0.03796 159 LYS A N   
1236 C CA  . LYS A 159 ? 0.26797 0.19498 0.22302 0.01007  0.06414  -0.03693 159 LYS A CA  
1237 C C   . LYS A 159 ? 0.29690 0.23214 0.25483 0.00965  0.06188  -0.03270 159 LYS A C   
1238 O O   . LYS A 159 ? 0.28605 0.22556 0.25158 0.01203  0.06502  -0.03045 159 LYS A O   
1239 C CB  . LYS A 159 ? 0.27421 0.19603 0.21891 0.00937  0.06939  -0.04163 159 LYS A CB  
1240 C CG  . LYS A 159 ? 0.28178 0.19450 0.22368 0.00978  0.07271  -0.04649 159 LYS A CG  
1241 C CD  . LYS A 159 ? 0.29399 0.20160 0.22189 0.00687  0.07456  -0.05211 159 LYS A CD  
1242 C CE  . LYS A 159 ? 0.29317 0.20187 0.21618 0.00824  0.08025  -0.05275 159 LYS A CE  
1243 N NZ  . LYS A 159 ? 0.29074 0.19452 0.21765 0.01181  0.08791  -0.05502 159 LYS A NZ  
1244 N N   . LEU A 160 ? 0.27200 0.20959 0.22457 0.00664  0.05666  -0.03168 160 LEU A N   
1245 C CA  . LEU A 160 ? 0.23983 0.18397 0.19444 0.00613  0.05469  -0.02773 160 LEU A CA  
1246 C C   . LEU A 160 ? 0.26194 0.21128 0.22841 0.00734  0.05134  -0.02389 160 LEU A C   
1247 O O   . LEU A 160 ? 0.27794 0.23236 0.25170 0.00856  0.05282  -0.02121 160 LEU A O   
1248 C CB  . LEU A 160 ? 0.26380 0.20839 0.20850 0.00311  0.05032  -0.02792 160 LEU A CB  
1249 C CG  . LEU A 160 ? 0.27860 0.22868 0.22457 0.00257  0.04798  -0.02367 160 LEU A CG  
1250 C CD1 . LEU A 160 ? 0.28690 0.23799 0.23260 0.00369  0.05371  -0.02232 160 LEU A CD1 
1251 C CD2 . LEU A 160 ? 0.26126 0.21162 0.19782 0.00029  0.04322  -0.02386 160 LEU A CD2 
1252 N N   . VAL A 161 ? 0.24643 0.19464 0.21482 0.00683  0.04693  -0.02376 161 VAL A N   
1253 C CA  . VAL A 161 ? 0.23768 0.19049 0.21586 0.00804  0.04343  -0.02030 161 VAL A CA  
1254 C C   . VAL A 161 ? 0.24377 0.19807 0.23194 0.01181  0.04658  -0.01938 161 VAL A C   
1255 O O   . VAL A 161 ? 0.25503 0.21516 0.25209 0.01313  0.04440  -0.01645 161 VAL A O   
1256 C CB  . VAL A 161 ? 0.20249 0.15294 0.17940 0.00672  0.03874  -0.02042 161 VAL A CB  
1257 C CG1 . VAL A 161 ? 0.20741 0.15835 0.17633 0.00325  0.03515  -0.02113 161 VAL A CG1 
1258 C CG2 . VAL A 161 ? 0.23978 0.18292 0.21498 0.00757  0.04121  -0.02329 161 VAL A CG2 
1259 N N   . ASP A 162 ? 0.27305 0.22248 0.26020 0.01372  0.05159  -0.02200 162 ASP A N   
1260 C CA  . ASP A 162 ? 0.23708 0.18859 0.23437 0.01791  0.05492  -0.02110 162 ASP A CA  
1261 C C   . ASP A 162 ? 0.24748 0.20544 0.25000 0.01850  0.05839  -0.02007 162 ASP A C   
1262 O O   . ASP A 162 ? 0.27923 0.24314 0.29314 0.02127  0.05890  -0.01819 162 ASP A O   
1263 C CB  . ASP A 162 ? 0.24547 0.18906 0.24022 0.02005  0.05969  -0.02434 162 ASP A CB  
1264 C CG  . ASP A 162 ? 0.30711 0.24417 0.29958 0.02000  0.05698  -0.02485 162 ASP A CG  
1265 O OD1 . ASP A 162 ? 0.30986 0.24885 0.30217 0.01818  0.05146  -0.02275 162 ASP A OD1 
1266 O OD2 . ASP A 162 ? 0.39382 0.32336 0.38463 0.02175  0.06081  -0.02738 162 ASP A OD2 
1267 N N   . ARG A 163 ? 0.28120 0.23825 0.27564 0.01596  0.06086  -0.02125 163 ARG A N   
1268 C CA  . ARG A 163 ? 0.28291 0.24554 0.28180 0.01594  0.06456  -0.01989 163 ARG A CA  
1269 C C   . ARG A 163 ? 0.25454 0.22412 0.25938 0.01431  0.06003  -0.01646 163 ARG A C   
1270 O O   . ARG A 163 ? 0.28301 0.25901 0.29751 0.01497  0.06205  -0.01494 163 ARG A O   
1271 C CB  . ARG A 163 ? 0.32474 0.28340 0.31173 0.01391  0.06877  -0.02174 163 ARG A CB  
1272 C CG  . ARG A 163 ? 0.38618 0.33858 0.36787 0.01556  0.07474  -0.02563 163 ARG A CG  
1273 C CD  . ARG A 163 ? 0.40990 0.35980 0.38063 0.01395  0.07959  -0.02698 163 ARG A CD  
1274 N NE  . ARG A 163 ? 0.41788 0.36553 0.37636 0.01073  0.07514  -0.02688 163 ARG A NE  
1275 C CZ  . ARG A 163 ? 0.44066 0.38228 0.38721 0.00939  0.07403  -0.03038 163 ARG A CZ  
1276 N NH1 . ARG A 163 ? 0.49228 0.42829 0.43664 0.01062  0.07738  -0.03450 163 ARG A NH1 
1277 N NH2 . ARG A 163 ? 0.40613 0.34744 0.34303 0.00678  0.06944  -0.02993 163 ARG A NH2 
1278 N N   . VAL A 164 ? 0.24315 0.21167 0.24280 0.01205  0.05416  -0.01550 164 VAL A N   
1279 C CA  . VAL A 164 ? 0.21171 0.18591 0.21629 0.01048  0.04994  -0.01261 164 VAL A CA  
1280 C C   . VAL A 164 ? 0.21304 0.19253 0.22972 0.01267  0.04691  -0.01120 164 VAL A C   
1281 O O   . VAL A 164 ? 0.23217 0.21836 0.25761 0.01238  0.04610  -0.00954 164 VAL A O   
1282 C CB  . VAL A 164 ? 0.23587 0.20739 0.23138 0.00782  0.04487  -0.01218 164 VAL A CB  
1283 C CG1 . VAL A 164 ? 0.24390 0.22047 0.24414 0.00632  0.04099  -0.00943 164 VAL A CG1 
1284 C CG2 . VAL A 164 ? 0.23655 0.20355 0.21978 0.00615  0.04730  -0.01355 164 VAL A CG2 
1285 N N   . GLY A 165 ? 0.19904 0.17549 0.21616 0.01486  0.04521  -0.01189 165 GLY A N   
1286 C CA  . GLY A 165 ? 0.21097 0.19174 0.23804 0.01765  0.04218  -0.01032 165 GLY A CA  
1287 C C   . GLY A 165 ? 0.19002 0.16916 0.21407 0.01685  0.03607  -0.00908 165 GLY A C   
1288 O O   . GLY A 165 ? 0.17495 0.14885 0.18971 0.01448  0.03458  -0.00990 165 GLY A O   
1289 N N   . ASP A 166 ? 0.14008 0.12431 0.17230 0.01892  0.03249  -0.00718 166 ASP A N   
1290 C CA  . ASP A 166 ? 0.14839 0.13130 0.17802 0.01855  0.02706  -0.00576 166 ASP A CA  
1291 C C   . ASP A 166 ? 0.14683 0.13120 0.17212 0.01452  0.02392  -0.00533 166 ASP A C   
1292 O O   . ASP A 166 ? 0.17950 0.16810 0.20727 0.01271  0.02485  -0.00526 166 ASP A O   
1293 C CB  . ASP A 166 ? 0.13549 0.12417 0.17426 0.02194  0.02380  -0.00377 166 ASP A CB  
1294 C CG  . ASP A 166 ? 0.16986 0.15624 0.21241 0.02679  0.02619  -0.00359 166 ASP A CG  
1295 O OD1 . ASP A 166 ? 0.17999 0.15778 0.21589 0.02726  0.02870  -0.00461 166 ASP A OD1 
1296 O OD2 . ASP A 166 ? 0.21665 0.20990 0.26916 0.03019  0.02555  -0.00257 166 ASP A OD2 
1297 N N   . PRO A 167 ? 0.13161 0.11224 0.15060 0.01311  0.02059  -0.00500 167 PRO A N   
1298 C CA  . PRO A 167 ? 0.11809 0.10050 0.13396 0.00995  0.01733  -0.00441 167 PRO A CA  
1299 C C   . PRO A 167 ? 0.10528 0.09452 0.12858 0.01030  0.01404  -0.00290 167 PRO A C   
1300 O O   . PRO A 167 ? 0.10504 0.09770 0.13516 0.01316  0.01313  -0.00214 167 PRO A O   
1301 C CB  . PRO A 167 ? 0.11485 0.09213 0.12400 0.00904  0.01492  -0.00452 167 PRO A CB  
1302 C CG  . PRO A 167 ? 0.15097 0.12228 0.15767 0.01062  0.01806  -0.00585 167 PRO A CG  
1303 C CD  . PRO A 167 ? 0.12516 0.09914 0.13951 0.01417  0.02038  -0.00533 167 PRO A CD  
1304 N N   . PRO A 168 ? 0.14047 0.13191 0.16275 0.00759  0.01213  -0.00257 168 PRO A N   
1305 C CA  . PRO A 168 ? 0.11890 0.11635 0.14769 0.00743  0.00877  -0.00176 168 PRO A CA  
1306 C C   . PRO A 168 ? 0.12451 0.12199 0.15311 0.00925  0.00464  -0.00082 168 PRO A C   
1307 O O   . PRO A 168 ? 0.12216 0.11446 0.14409 0.00919  0.00383  -0.00055 168 PRO A O   
1308 C CB  . PRO A 168 ? 0.10039 0.09743 0.12554 0.00414  0.00793  -0.00174 168 PRO A CB  
1309 C CG  . PRO A 168 ? 0.11780 0.11078 0.13719 0.00307  0.01184  -0.00225 168 PRO A CG  
1310 C CD  . PRO A 168 ? 0.13691 0.12557 0.15234 0.00479  0.01322  -0.00303 168 PRO A CD  
1311 N N   . ALA A 169 ? 0.12209 0.12568 0.15809 0.01083  0.00211  -0.00035 169 ALA A N   
1312 C CA  . ALA A 169 ? 0.12054 0.12451 0.15579 0.01298  -0.00198 0.00087  169 ALA A CA  
1313 C C   . ALA A 169 ? 0.11296 0.11506 0.14217 0.01049  -0.00497 0.00098  169 ALA A C   
1314 O O   . ALA A 169 ? 0.09599 0.09897 0.12466 0.00746  -0.00481 0.00010  169 ALA A O   
1315 C CB  . ALA A 169 ? 0.16362 0.17580 0.20815 0.01518  -0.00463 0.00104  169 ALA A CB  
1316 N N   . PRO A 170 ? 0.12496 0.12400 0.14941 0.01187  -0.00727 0.00220  170 PRO A N   
1317 C CA  . PRO A 170 ? 0.10957 0.10724 0.12868 0.00971  -0.00976 0.00220  170 PRO A CA  
1318 C C   . PRO A 170 ? 0.12979 0.13365 0.15306 0.00879  -0.01310 0.00147  170 PRO A C   
1319 O O   . PRO A 170 ? 0.09773 0.10704 0.12685 0.01077  -0.01522 0.00155  170 PRO A O   
1320 C CB  . PRO A 170 ? 0.12833 0.12159 0.14226 0.01187  -0.01083 0.00391  170 PRO A CB  
1321 C CG  . PRO A 170 ? 0.12539 0.11973 0.14358 0.01587  -0.01051 0.00511  170 PRO A CG  
1322 C CD  . PRO A 170 ? 0.09954 0.09535 0.12277 0.01552  -0.00707 0.00378  170 PRO A CD  
1323 N N   . ALA A 171 ? 0.11219 0.11531 0.13265 0.00580  -0.01361 0.00054  171 ALA A N   
1324 C CA  . ALA A 171 ? 0.11324 0.12104 0.13699 0.00434  -0.01637 -0.00072 171 ALA A CA  
1325 C C   . ALA A 171 ? 0.12743 0.13686 0.14904 0.00613  -0.02048 -0.00023 171 ALA A C   
1326 O O   . ALA A 171 ? 0.15313 0.15833 0.16863 0.00771  -0.02071 0.00133  171 ALA A O   
1327 C CB  . ALA A 171 ? 0.14576 0.15098 0.16616 0.00122  -0.01553 -0.00163 171 ALA A CB  
1328 N N   . PRO A 172 ? 0.13718 0.15260 0.16347 0.00580  -0.02367 -0.00164 172 PRO A N   
1329 C CA  . PRO A 172 ? 0.14840 0.16560 0.17147 0.00760  -0.02797 -0.00134 172 PRO A CA  
1330 C C   . PRO A 172 ? 0.15876 0.17117 0.17343 0.00604  -0.02835 -0.00151 172 PRO A C   
1331 O O   . PRO A 172 ? 0.15158 0.16075 0.16449 0.00339  -0.02600 -0.00233 172 PRO A O   
1332 C CB  . PRO A 172 ? 0.15418 0.17956 0.18498 0.00664  -0.03114 -0.00378 172 PRO A CB  
1333 C CG  . PRO A 172 ? 0.14557 0.17129 0.18159 0.00301  -0.02794 -0.00557 172 PRO A CG  
1334 C CD  . PRO A 172 ? 0.12092 0.14191 0.15573 0.00366  -0.02339 -0.00374 172 PRO A CD  
1335 N N   . ASP A 173 ? 0.18396 0.19605 0.19328 0.00806  -0.03126 -0.00057 173 ASP A N   
1336 C CA  . ASP A 173 ? 0.20264 0.21042 0.20385 0.00692  -0.03131 -0.00069 173 ASP A CA  
1337 C C   . ASP A 173 ? 0.19683 0.20724 0.19922 0.00402  -0.03295 -0.00388 173 ASP A C   
1338 O O   . ASP A 173 ? 0.17882 0.19506 0.18721 0.00338  -0.03543 -0.00592 173 ASP A O   
1339 C CB  . ASP A 173 ? 0.20880 0.21505 0.20314 0.01002  -0.03352 0.00144  173 ASP A CB  
1340 C CG  . ASP A 173 ? 0.22990 0.23044 0.22080 0.01219  -0.03067 0.00465  173 ASP A CG  
1341 O OD1 . ASP A 173 ? 0.30818 0.30984 0.30350 0.01450  -0.03029 0.00596  173 ASP A OD1 
1342 O OD2 . ASP A 173 ? 0.31609 0.31094 0.30026 0.01148  -0.02851 0.00568  173 ASP A OD2 
1343 N N   . PRO A 174 ? 0.20592 0.21214 0.20318 0.00217  -0.03140 -0.00460 174 PRO A N   
1344 C CA  . PRO A 174 ? 0.19219 0.19961 0.18991 -0.00038 -0.03251 -0.00775 174 PRO A CA  
1345 C C   . PRO A 174 ? 0.21357 0.22439 0.20847 0.00048  -0.03685 -0.00925 174 PRO A C   
1346 O O   . PRO A 174 ? 0.18980 0.20098 0.18043 0.00342  -0.03877 -0.00720 174 PRO A O   
1347 C CB  . PRO A 174 ? 0.20537 0.20720 0.19747 -0.00143 -0.02965 -0.00750 174 PRO A CB  
1348 C CG  . PRO A 174 ? 0.20064 0.19926 0.18772 0.00063  -0.02834 -0.00452 174 PRO A CG  
1349 C CD  . PRO A 174 ? 0.15930 0.15966 0.15087 0.00225  -0.02831 -0.00280 174 PRO A CD  
1350 N N   . PRO A 175 ? 0.18670 0.19974 0.18343 -0.00194 -0.03850 -0.01287 175 PRO A N   
1351 C CA  . PRO A 175 ? 0.20654 0.22330 0.20007 -0.00135 -0.04310 -0.01496 175 PRO A CA  
1352 C C   . PRO A 175 ? 0.21363 0.22594 0.19595 0.00028  -0.04314 -0.01379 175 PRO A C   
1353 O O   . PRO A 175 ? 0.19872 0.20534 0.17682 0.00013  -0.03940 -0.01220 175 PRO A O   
1354 C CB  . PRO A 175 ? 0.21762 0.23597 0.21543 -0.00514 -0.04361 -0.01960 175 PRO A CB  
1355 C CG  . PRO A 175 ? 0.19874 0.21151 0.19792 -0.00708 -0.03867 -0.01916 175 PRO A CG  
1356 C CD  . PRO A 175 ? 0.20669 0.21857 0.20823 -0.00532 -0.03620 -0.01529 175 PRO A CD  
1357 N N   . ALA A 176 ? 0.19043 0.20586 0.16796 0.00187  -0.04748 -0.01464 176 ALA A N   
1358 C CA  . ALA A 176 ? 0.20159 0.21279 0.16748 0.00363  -0.04743 -0.01334 176 ALA A CA  
1359 C C   . ALA A 176 ? 0.20011 0.20705 0.16163 0.00099  -0.04496 -0.01624 176 ALA A C   
1360 O O   . ALA A 176 ? 0.18973 0.19162 0.14310 0.00185  -0.04239 -0.01468 176 ALA A O   
1361 C CB  . ALA A 176 ? 0.17116 0.18696 0.13221 0.00614  -0.05303 -0.01370 176 ALA A CB  
1362 N N   . ALA A 177 ? 0.18916 0.19780 0.15622 -0.00219 -0.04530 -0.02046 177 ALA A N   
1363 C CA  . ALA A 177 ? 0.18257 0.18678 0.14665 -0.00449 -0.04264 -0.02341 177 ALA A CA  
1364 C C   . ALA A 177 ? 0.20380 0.20639 0.17640 -0.00693 -0.03930 -0.02411 177 ALA A C   
1365 O O   . ALA A 177 ? 0.21309 0.21937 0.19414 -0.00829 -0.04038 -0.02495 177 ALA A O   
1366 C CB  . ALA A 177 ? 0.19182 0.19817 0.15258 -0.00601 -0.04616 -0.02845 177 ALA A CB  
1367 N N   . MET A 178 ? 0.16531 0.16256 0.13568 -0.00729 -0.03512 -0.02361 178 MET A N   
1368 C CA  . MET A 178 ? 0.19443 0.18943 0.17139 -0.00890 -0.03187 -0.02360 178 MET A CA  
1369 C C   . MET A 178 ? 0.19261 0.18376 0.16841 -0.01068 -0.03008 -0.02722 178 MET A C   
1370 O O   . MET A 178 ? 0.21060 0.19979 0.17938 -0.01024 -0.03008 -0.02900 178 MET A O   
1371 C CB  . MET A 178 ? 0.19059 0.18305 0.16723 -0.00737 -0.02849 -0.01960 178 MET A CB  
1372 C CG  . MET A 178 ? 0.23306 0.22758 0.20902 -0.00537 -0.02949 -0.01608 178 MET A CG  
1373 S SD  . MET A 178 ? 0.33496 0.32810 0.31543 -0.00501 -0.02618 -0.01272 178 MET A SD  
1374 C CE  . MET A 178 ? 0.19659 0.18594 0.17695 -0.00603 -0.02281 -0.01385 178 MET A CE  
1375 N N   . PRO A 179 ? 0.21375 0.20315 0.19592 -0.01257 -0.02819 -0.02832 179 PRO A N   
1376 C CA  . PRO A 179 ? 0.20549 0.18992 0.18677 -0.01386 -0.02580 -0.03137 179 PRO A CA  
1377 C C   . PRO A 179 ? 0.18655 0.16713 0.16336 -0.01172 -0.02249 -0.02950 179 PRO A C   
1378 O O   . PRO A 179 ? 0.22386 0.20385 0.20303 -0.01043 -0.02036 -0.02602 179 PRO A O   
1379 C CB  . PRO A 179 ? 0.17222 0.15512 0.16148 -0.01576 -0.02392 -0.03135 179 PRO A CB  
1380 C CG  . PRO A 179 ? 0.17901 0.16759 0.17351 -0.01639 -0.02637 -0.03015 179 PRO A CG  
1381 C CD  . PRO A 179 ? 0.19562 0.18718 0.18591 -0.01360 -0.02794 -0.02693 179 PRO A CD  
1382 N N   . PRO A 180 ? 0.17619 0.15452 0.14668 -0.01131 -0.02196 -0.03195 180 PRO A N   
1383 C CA  . PRO A 180 ? 0.19900 0.17471 0.16594 -0.00923 -0.01860 -0.03035 180 PRO A CA  
1384 C C   . PRO A 180 ? 0.18721 0.15872 0.15823 -0.00900 -0.01514 -0.03062 180 PRO A C   
1385 O O   . PRO A 180 ? 0.19958 0.16862 0.17435 -0.01070 -0.01495 -0.03281 180 PRO A O   
1386 C CB  . PRO A 180 ? 0.20672 0.18133 0.16545 -0.00908 -0.01902 -0.03346 180 PRO A CB  
1387 C CG  . PRO A 180 ? 0.20530 0.17979 0.16467 -0.01154 -0.02160 -0.03805 180 PRO A CG  
1388 C CD  . PRO A 180 ? 0.22523 0.20376 0.19152 -0.01281 -0.02438 -0.03664 180 PRO A CD  
1389 N N   . PRO A 181 ? 0.17990 0.15057 0.15064 -0.00686 -0.01229 -0.02837 181 PRO A N   
1390 C CA  . PRO A 181 ? 0.15525 0.12202 0.12933 -0.00581 -0.00915 -0.02853 181 PRO A CA  
1391 C C   . PRO A 181 ? 0.18820 0.15043 0.15922 -0.00611 -0.00750 -0.03292 181 PRO A C   
1392 O O   . PRO A 181 ? 0.20974 0.17226 0.17478 -0.00641 -0.00797 -0.03541 181 PRO A O   
1393 C CB  . PRO A 181 ? 0.18154 0.15040 0.15598 -0.00334 -0.00721 -0.02540 181 PRO A CB  
1394 C CG  . PRO A 181 ? 0.22211 0.19395 0.19138 -0.00347 -0.00815 -0.02508 181 PRO A CG  
1395 C CD  . PRO A 181 ? 0.18307 0.15653 0.15112 -0.00530 -0.01175 -0.02549 181 PRO A CD  
1396 N N   . ALA A 182 ? 0.17265 0.13003 0.14729 -0.00592 -0.00530 -0.03385 182 ALA A N   
1397 C CA  . ALA A 182 ? 0.19323 0.14507 0.16548 -0.00626 -0.00323 -0.03835 182 ALA A CA  
1398 C C   . ALA A 182 ? 0.22182 0.17337 0.19019 -0.00360 -0.00048 -0.03889 182 ALA A C   
1399 O O   . ALA A 182 ? 0.21551 0.17004 0.18563 -0.00112 0.00080  -0.03543 182 ALA A O   
1400 C CB  . ALA A 182 ? 0.20418 0.14984 0.18134 -0.00612 -0.00076 -0.03847 182 ALA A CB  
1401 N N   . GLU A 183 ? 0.23536 0.18356 0.19860 -0.00432 0.00056  -0.04360 183 GLU A N   
1402 C CA  . GLU A 183 ? 0.26668 0.21455 0.22552 -0.00207 0.00363  -0.04470 183 GLU A CA  
1403 C C   . GLU A 183 ? 0.25588 0.19905 0.21857 0.00078  0.00804  -0.04502 183 GLU A C   
1404 O O   . GLU A 183 ? 0.27286 0.21095 0.23954 0.00063  0.00887  -0.04561 183 GLU A O   
1405 C CB  . GLU A 183 ? 0.26599 0.21216 0.21642 -0.00386 0.00298  -0.04979 183 GLU A CB  
1406 C CG  . GLU A 183 ? 0.29620 0.24713 0.24221 -0.00601 -0.00173 -0.04943 183 GLU A CG  
1407 C CD  . GLU A 183 ? 0.28658 0.23583 0.22391 -0.00777 -0.00315 -0.05481 183 GLU A CD  
1408 O OE1 . GLU A 183 ? 0.28803 0.23176 0.22333 -0.00801 -0.00051 -0.05944 183 GLU A OE1 
1409 O OE2 . GLU A 183 ? 0.28885 0.24214 0.22106 -0.00871 -0.00694 -0.05444 183 GLU A OE2 
1410 N N   . ASP A 184 ? 0.28343 0.22831 0.24511 0.00357  0.01115  -0.04444 184 ASP A N   
1411 C CA  . ASP A 184 ? 0.29537 0.23675 0.26061 0.00706  0.01557  -0.04492 184 ASP A CA  
1412 C C   . ASP A 184 ? 0.27876 0.22010 0.25196 0.00929  0.01549  -0.04076 184 ASP A C   
1413 O O   . ASP A 184 ? 0.24277 0.17879 0.21912 0.01184  0.01833  -0.04126 184 ASP A O   
1414 C CB  . ASP A 184 ? 0.28371 0.21694 0.24538 0.00645  0.01800  -0.05057 184 ASP A CB  
1415 C CG  . ASP A 184 ? 0.38461 0.31775 0.33742 0.00518  0.01885  -0.05486 184 ASP A CG  
1416 O OD1 . ASP A 184 ? 0.41976 0.35754 0.37053 0.00674  0.02048  -0.05342 184 ASP A OD1 
1417 O OD2 . ASP A 184 ? 0.38685 0.31531 0.33454 0.00248  0.01797  -0.05979 184 ASP A OD2 
1418 N N   . MET A 185 ? 0.25989 0.20669 0.23584 0.00860  0.01236  -0.03657 185 MET A N   
1419 C CA  . MET A 185 ? 0.21919 0.16684 0.20155 0.01110  0.01220  -0.03233 185 MET A CA  
1420 C C   . MET A 185 ? 0.23233 0.18614 0.21828 0.01460  0.01367  -0.02992 185 MET A C   
1421 O O   . MET A 185 ? 0.21052 0.17028 0.19497 0.01361  0.01309  -0.02953 185 MET A O   
1422 C CB  . MET A 185 ? 0.22897 0.17941 0.21252 0.00874  0.00844  -0.02934 185 MET A CB  
1423 C CG  . MET A 185 ? 0.21265 0.15784 0.19502 0.00541  0.00713  -0.03133 185 MET A CG  
1424 S SD  . MET A 185 ? 0.26540 0.20096 0.25092 0.00698  0.01024  -0.03172 185 MET A SD  
1425 C CE  . MET A 185 ? 0.18066 0.11223 0.16534 0.00156  0.00844  -0.03468 185 MET A CE  
1426 N N   . PRO A 186 ? 0.22341 0.17612 0.21435 0.01875  0.01562  -0.02825 186 PRO A N   
1427 C CA  . PRO A 186 ? 0.17660 0.13627 0.17211 0.02220  0.01700  -0.02660 186 PRO A CA  
1428 C C   . PRO A 186 ? 0.17659 0.14475 0.17474 0.02137  0.01390  -0.02312 186 PRO A C   
1429 O O   . PRO A 186 ? 0.18592 0.16072 0.18522 0.02111  0.01454  -0.02323 186 PRO A O   
1430 C CB  . PRO A 186 ? 0.22689 0.18291 0.22719 0.02713  0.01891  -0.02518 186 PRO A CB  
1431 C CG  . PRO A 186 ? 0.20599 0.15428 0.20461 0.02581  0.01766  -0.02426 186 PRO A CG  
1432 C CD  . PRO A 186 ? 0.20596 0.15084 0.19873 0.02059  0.01684  -0.02783 186 PRO A CD  
1433 N N   . SER A 187 ? 0.17449 0.14220 0.17352 0.02076  0.01091  -0.02018 187 SER A N   
1434 C CA  . SER A 187 ? 0.19260 0.16767 0.19360 0.01980  0.00799  -0.01730 187 SER A CA  
1435 C C   . SER A 187 ? 0.19790 0.17503 0.19472 0.01543  0.00651  -0.01823 187 SER A C   
1436 O O   . SER A 187 ? 0.19809 0.18099 0.19626 0.01433  0.00468  -0.01639 187 SER A O   
1437 C CB  . SER A 187 ? 0.19687 0.17027 0.19906 0.02061  0.00563  -0.01397 187 SER A CB  
1438 O OG  . SER A 187 ? 0.22836 0.20068 0.23425 0.02539  0.00666  -0.01216 187 SER A OG  
1439 N N   . ALA A 188 ? 0.17432 0.14679 0.16595 0.01306  0.00717  -0.02110 188 ALA A N   
1440 C CA  . ALA A 188 ? 0.18939 0.16346 0.17637 0.00961  0.00571  -0.02181 188 ALA A CA  
1441 C C   . ALA A 188 ? 0.16400 0.13957 0.14781 0.00942  0.00835  -0.02396 188 ALA A C   
1442 O O   . ALA A 188 ? 0.17873 0.15339 0.15668 0.00703  0.00770  -0.02516 188 ALA A O   
1443 C CB  . ALA A 188 ? 0.18783 0.15676 0.17087 0.00702  0.00391  -0.02340 188 ALA A CB  
1444 N N   . ALA A 189 ? 0.15987 0.13784 0.14735 0.01210  0.01140  -0.02434 189 ALA A N   
1445 C CA  . ALA A 189 ? 0.16480 0.14419 0.14950 0.01196  0.01477  -0.02635 189 ALA A CA  
1446 C C   . ALA A 189 ? 0.19165 0.17605 0.17528 0.00966  0.01421  -0.02458 189 ALA A C   
1447 O O   . ALA A 189 ? 0.20056 0.19003 0.18951 0.00965  0.01272  -0.02208 189 ALA A O   
1448 C CB  . ALA A 189 ? 0.20879 0.19065 0.19937 0.01559  0.01841  -0.02702 189 ALA A CB  
1449 N N   . PRO A 190 ? 0.20936 0.19209 0.18577 0.00772  0.01541  -0.02579 190 PRO A N   
1450 C CA  . PRO A 190 ? 0.19673 0.18279 0.17155 0.00555  0.01525  -0.02371 190 PRO A CA  
1451 C C   . PRO A 190 ? 0.20907 0.20136 0.19037 0.00607  0.01832  -0.02282 190 PRO A C   
1452 O O   . PRO A 190 ? 0.17596 0.17165 0.15909 0.00425  0.01763  -0.02078 190 PRO A O   
1453 C CB  . PRO A 190 ? 0.22417 0.20615 0.18888 0.00423  0.01652  -0.02529 190 PRO A CB  
1454 C CG  . PRO A 190 ? 0.19615 0.17290 0.15717 0.00482  0.01528  -0.02820 190 PRO A CG  
1455 C CD  . PRO A 190 ? 0.20917 0.18625 0.17768 0.00734  0.01665  -0.02905 190 PRO A CD  
1456 N N   . ALA A 191 ? 0.23211 0.22617 0.21752 0.00844  0.02183  -0.02454 191 ALA A N   
1457 C CA  . ALA A 191 ? 0.20934 0.21058 0.20217 0.00884  0.02490  -0.02412 191 ALA A CA  
1458 C C   . ALA A 191 ? 0.19911 0.20649 0.20092 0.00943  0.02174  -0.02212 191 ALA A C   
1459 O O   . ALA A 191 ? 0.22120 0.23509 0.22857 0.00816  0.02273  -0.02142 191 ALA A O   
1460 C CB  . ALA A 191 ? 0.19470 0.19675 0.19039 0.01174  0.02949  -0.02660 191 ALA A CB  
1461 N N   . ALA A 192 ? 0.16737 0.17274 0.17048 0.01118  0.01809  -0.02131 192 ALA A N   
1462 C CA  . ALA A 192 ? 0.21992 0.23055 0.23003 0.01216  0.01483  -0.01934 192 ALA A CA  
1463 C C   . ALA A 192 ? 0.17959 0.18793 0.18628 0.00985  0.01069  -0.01743 192 ALA A C   
1464 O O   . ALA A 192 ? 0.16938 0.18112 0.18028 0.01059  0.00776  -0.01582 192 ALA A O   
1465 C CB  . ALA A 192 ? 0.23782 0.24805 0.25233 0.01657  0.01428  -0.01927 192 ALA A CB  
1466 N N   . THR A 193 ? 0.18727 0.19024 0.18633 0.00734  0.01033  -0.01757 193 THR A N   
1467 C CA  . THR A 193 ? 0.17632 0.17715 0.17248 0.00541  0.00674  -0.01589 193 THR A CA  
1468 C C   . THR A 193 ? 0.15125 0.15172 0.14321 0.00232  0.00725  -0.01530 193 THR A C   
1469 O O   . THR A 193 ? 0.15497 0.15257 0.14319 0.00089  0.00478  -0.01419 193 THR A O   
1470 C CB  . THR A 193 ? 0.15778 0.15214 0.14943 0.00581  0.00501  -0.01637 193 THR A CB  
1471 O OG1 . THR A 193 ? 0.17680 0.16713 0.16245 0.00524  0.00697  -0.01847 193 THR A OG1 
1472 C CG2 . THR A 193 ? 0.19066 0.18404 0.18628 0.00882  0.00468  -0.01634 193 THR A CG2 
1473 N N   . GLY A 194 ? 0.15222 0.15530 0.14487 0.00140  0.01072  -0.01587 194 GLY A N   
1474 C CA  . GLY A 194 ? 0.14065 0.14233 0.12892 -0.00135 0.01183  -0.01488 194 GLY A CA  
1475 C C   . GLY A 194 ? 0.16329 0.16882 0.15626 -0.00327 0.01073  -0.01359 194 GLY A C   
1476 O O   . GLY A 194 ? 0.14944 0.16036 0.14962 -0.00260 0.00953  -0.01381 194 GLY A O   
1477 N N   . VAL A 195 ? 0.14154 0.14400 0.12993 -0.00554 0.01108  -0.01229 195 VAL A N   
1478 C CA  . VAL A 195 ? 0.13185 0.13656 0.12373 -0.00783 0.01057  -0.01141 195 VAL A CA  
1479 C C   . VAL A 195 ? 0.17564 0.18509 0.17285 -0.00963 0.01458  -0.01239 195 VAL A C   
1480 O O   . VAL A 195 ? 0.17696 0.18414 0.17060 -0.01059 0.01869  -0.01231 195 VAL A O   
1481 C CB  . VAL A 195 ? 0.16916 0.16807 0.15440 -0.00926 0.00993  -0.00956 195 VAL A CB  
1482 C CG1 . VAL A 195 ? 0.17317 0.17349 0.16195 -0.01179 0.01008  -0.00908 195 VAL A CG1 
1483 C CG2 . VAL A 195 ? 0.17485 0.17049 0.15645 -0.00762 0.00593  -0.00890 195 VAL A CG2 
1484 N N   . PRO A 196 ? 0.14388 0.16018 0.14955 -0.01021 0.01364  -0.01341 196 PRO A N   
1485 C CA  . PRO A 196 ? 0.16493 0.18717 0.17740 -0.01223 0.01737  -0.01484 196 PRO A CA  
1486 C C   . PRO A 196 ? 0.16179 0.18186 0.17337 -0.01635 0.01962  -0.01434 196 PRO A C   
1487 O O   . PRO A 196 ? 0.18804 0.20272 0.19465 -0.01729 0.01779  -0.01292 196 PRO A O   
1488 C CB  . PRO A 196 ? 0.17093 0.20181 0.19266 -0.01095 0.01428  -0.01620 196 PRO A CB  
1489 C CG  . PRO A 196 ? 0.13601 0.16408 0.15463 -0.01019 0.00940  -0.01503 196 PRO A CG  
1490 C CD  . PRO A 196 ? 0.15065 0.17009 0.16009 -0.00889 0.00905  -0.01343 196 PRO A CD  
1491 N N   . THR A 197 ? 0.20213 0.22636 0.21911 -0.01882 0.02405  -0.01561 197 THR A N   
1492 C CA  . THR A 197 ? 0.21119 0.23364 0.22887 -0.02325 0.02714  -0.01552 197 THR A CA  
1493 C C   . THR A 197 ? 0.18415 0.21535 0.21253 -0.02573 0.02555  -0.01806 197 THR A C   
1494 O O   . THR A 197 ? 0.20055 0.23993 0.23583 -0.02365 0.02234  -0.01963 197 THR A O   
1495 C CB  . THR A 197 ? 0.21244 0.23282 0.22843 -0.02503 0.03399  -0.01522 197 THR A CB  
1496 O OG1 . THR A 197 ? 0.21529 0.24433 0.23972 -0.02421 0.03613  -0.01744 197 THR A OG1 
1497 C CG2 . THR A 197 ? 0.21062 0.22187 0.21436 -0.02273 0.03513  -0.01275 197 THR A CG2 
1498 N N   . TRP A 198 ? 0.16987 0.19908 0.19938 -0.03018 0.02779  -0.01851 198 TRP A N   
1499 C CA  . TRP A 198 ? 0.22766 0.26501 0.26692 -0.03321 0.02608  -0.02153 198 TRP A CA  
1500 C C   . TRP A 198 ? 0.20956 0.25770 0.26011 -0.03462 0.02885  -0.02425 198 TRP A C   
1501 O O   . TRP A 198 ? 0.22238 0.28013 0.28241 -0.03610 0.02616  -0.02719 198 TRP A O   
1502 C CB  . TRP A 198 ? 0.22322 0.25453 0.26056 -0.03792 0.02812  -0.02169 198 TRP A CB  
1503 C CG  . TRP A 198 ? 0.19807 0.22455 0.23438 -0.04152 0.03543  -0.02098 198 TRP A CG  
1504 C CD1 . TRP A 198 ? 0.20387 0.21911 0.22975 -0.04101 0.03905  -0.01750 198 TRP A CD1 
1505 C CD2 . TRP A 198 ? 0.22703 0.25972 0.27298 -0.04621 0.04018  -0.02369 198 TRP A CD2 
1506 N NE1 . TRP A 198 ? 0.23319 0.24633 0.26068 -0.04493 0.04610  -0.01750 198 TRP A NE1 
1507 C CE2 . TRP A 198 ? 0.24471 0.26848 0.28493 -0.04845 0.04718  -0.02141 198 TRP A CE2 
1508 C CE3 . TRP A 198 ? 0.20911 0.25447 0.26821 -0.04868 0.03914  -0.02784 198 TRP A CE3 
1509 C CZ2 . TRP A 198 ? 0.23356 0.26005 0.28089 -0.05344 0.05380  -0.02311 198 TRP A CZ2 
1510 C CZ3 . TRP A 198 ? 0.21787 0.26702 0.28503 -0.05373 0.04526  -0.02994 198 TRP A CZ3 
1511 C CH2 . TRP A 198 ? 0.25169 0.29115 0.31302 -0.05624 0.05283  -0.02756 198 TRP A CH2 
1512 N N   . GLN A 199 ? 0.18677 0.23403 0.23664 -0.03409 0.03410  -0.02352 199 GLN A N   
1513 C CA  . GLN A 199 ? 0.20139 0.25958 0.26275 -0.03486 0.03706  -0.02612 199 GLN A CA  
1514 C C   . GLN A 199 ? 0.22498 0.29091 0.29078 -0.02943 0.03307  -0.02673 199 GLN A C   
1515 O O   . GLN A 199 ? 0.27077 0.34864 0.34848 -0.02930 0.03253  -0.02933 199 GLN A O   
1516 C CB  . GLN A 199 ? 0.22134 0.27536 0.28006 -0.03643 0.04508  -0.02516 199 GLN A CB  
1517 C CG  . GLN A 199 ? 0.20196 0.24749 0.25612 -0.04163 0.05016  -0.02405 199 GLN A CG  
1518 C CD  . GLN A 199 ? 0.25066 0.28228 0.28961 -0.03989 0.04971  -0.02013 199 GLN A CD  
1519 O OE1 . GLN A 199 ? 0.24611 0.27512 0.27926 -0.03588 0.04414  -0.01887 199 GLN A OE1 
1520 N NE2 . GLN A 199 ? 0.32585 0.34858 0.35846 -0.04282 0.05569  -0.01808 199 GLN A NE2 
1521 N N   . GLU A 200 ? 0.20216 0.26152 0.25896 -0.02489 0.03031  -0.02440 200 GLU A N   
1522 C CA  . GLU A 200 ? 0.21476 0.27940 0.27476 -0.01955 0.02712  -0.02464 200 GLU A CA  
1523 C C   . GLU A 200 ? 0.20295 0.27419 0.26798 -0.01794 0.02031  -0.02541 200 GLU A C   
1524 O O   . GLU A 200 ? 0.25123 0.33112 0.32379 -0.01444 0.01813  -0.02637 200 GLU A O   
1525 C CB  . GLU A 200 ? 0.21096 0.26575 0.25965 -0.01585 0.02672  -0.02226 200 GLU A CB  
1526 C CG  . GLU A 200 ? 0.21886 0.26734 0.26118 -0.01657 0.03298  -0.02157 200 GLU A CG  
1527 C CD  . GLU A 200 ? 0.23469 0.27405 0.26579 -0.01325 0.03182  -0.01984 200 GLU A CD  
1528 O OE1 . GLU A 200 ? 0.23571 0.27172 0.26286 -0.01159 0.02662  -0.01872 200 GLU A OE1 
1529 O OE2 . GLU A 200 ? 0.32406 0.35977 0.35033 -0.01245 0.03625  -0.01983 200 GLU A OE2 
1530 N N   . VAL A 201 ? 0.22318 0.29029 0.28377 -0.02009 0.01703  -0.02489 201 VAL A N   
1531 C CA  . VAL A 201 ? 0.23615 0.30839 0.29939 -0.01842 0.01064  -0.02542 201 VAL A CA  
1532 C C   . VAL A 201 ? 0.25042 0.33563 0.32587 -0.02056 0.00932  -0.02872 201 VAL A C   
1533 O O   . VAL A 201 ? 0.26038 0.35260 0.33954 -0.01805 0.00390  -0.02936 201 VAL A O   
1534 C CB  . VAL A 201 ? 0.20423 0.26809 0.25891 -0.02013 0.00806  -0.02418 201 VAL A CB  
1535 C CG1 . VAL A 201 ? 0.20359 0.25674 0.24762 -0.01729 0.00811  -0.02112 201 VAL A CG1 
1536 C CG2 . VAL A 201 ? 0.22667 0.28754 0.28134 -0.02598 0.01152  -0.02539 201 VAL A CG2 
1537 N N   . GLY A 202 ? 0.22627 0.31504 0.30805 -0.02519 0.01411  -0.03086 202 GLY A N   
1538 C CA  . GLY A 202 ? 0.27662 0.37889 0.37154 -0.02777 0.01325  -0.03458 202 GLY A CA  
1539 C C   . GLY A 202 ? 0.27027 0.37230 0.36783 -0.03493 0.01532  -0.03716 202 GLY A C   
1540 O O   . GLY A 202 ? 0.22765 0.34132 0.33708 -0.03806 0.01515  -0.04089 202 GLY A O   
1541 N N   . PHE A 203 ? 0.22274 0.31220 0.31029 -0.03765 0.01730  -0.03553 203 PHE A N   
1542 C CA  . PHE A 203 ? 0.23452 0.32216 0.32421 -0.04444 0.01988  -0.03793 203 PHE A CA  
1543 C C   . PHE A 203 ? 0.28085 0.37049 0.37730 -0.04868 0.02750  -0.03917 203 PHE A C   
1544 O O   . PHE A 203 ? 0.26684 0.35167 0.35946 -0.04686 0.03229  -0.03666 203 PHE A O   
1545 C CB  . PHE A 203 ? 0.23835 0.31124 0.31538 -0.04543 0.02046  -0.03537 203 PHE A CB  
1546 C CG  . PHE A 203 ? 0.21633 0.28799 0.28858 -0.04347 0.01382  -0.03539 203 PHE A CG  
1547 C CD1 . PHE A 203 ? 0.20317 0.28069 0.28051 -0.04696 0.01062  -0.03923 203 PHE A CD1 
1548 C CD2 . PHE A 203 ? 0.19672 0.26138 0.25933 -0.03841 0.01101  -0.03184 203 PHE A CD2 
1549 C CE1 . PHE A 203 ? 0.19533 0.27139 0.26733 -0.04510 0.00494  -0.03928 203 PHE A CE1 
1550 C CE2 . PHE A 203 ? 0.20656 0.26993 0.26473 -0.03672 0.00561  -0.03174 203 PHE A CE2 
1551 C CZ  . PHE A 203 ? 0.17393 0.24280 0.23634 -0.03992 0.00269  -0.03535 203 PHE A CZ  
1552 N N   . LYS A 204 ? 0.29280 0.31561 0.35649 0.02471  0.04120  -0.03346 204 LYS A N   
1553 C CA  . LYS A 204 ? 0.29704 0.32647 0.36283 0.02376  0.04521  -0.03495 204 LYS A CA  
1554 C C   . LYS A 204 ? 0.28101 0.31231 0.33720 0.02046  0.04523  -0.03250 204 LYS A C   
1555 O O   . LYS A 204 ? 0.32957 0.36628 0.38569 0.01908  0.04888  -0.03366 204 LYS A O   
1556 C CB  . LYS A 204 ? 0.32036 0.35365 0.39826 0.02549  0.04455  -0.03317 204 LYS A CB  
1557 C CG  . LYS A 204 ? 0.32505 0.35620 0.41371 0.02894  0.04362  -0.03448 204 LYS A CG  
1558 C CD  . LYS A 204 ? 0.31566 0.35100 0.41662 0.03057  0.04244  -0.03220 204 LYS A CD  
1559 C CE  . LYS A 204 ? 0.31379 0.34667 0.42591 0.03409  0.04102  -0.03291 204 LYS A CE  
1560 N NZ  . LYS A 204 ? 0.29929 0.33675 0.42437 0.03581  0.03975  -0.03064 204 LYS A NZ  
1561 N N   . GLU A 205 ? 0.29773 0.32476 0.34620 0.01915  0.04139  -0.02912 205 GLU A N   
1562 C CA  A GLU A 205 ? 0.29667 0.32458 0.33655 0.01621  0.04089  -0.02650 205 GLU A CA  
1563 C CA  B GLU A 205 ? 0.29647 0.32446 0.33636 0.01621  0.04099  -0.02657 205 GLU A CA  
1564 C C   . GLU A 205 ? 0.24631 0.27060 0.27579 0.01487  0.04072  -0.02749 205 GLU A C   
1565 O O   . GLU A 205 ? 0.24708 0.26653 0.27528 0.01600  0.03854  -0.02787 205 GLU A O   
1566 C CB  A GLU A 205 ? 0.30903 0.33527 0.34932 0.01574  0.03634  -0.02155 205 GLU A CB  
1567 C CB  B GLU A 205 ? 0.30871 0.33529 0.34902 0.01565  0.03656  -0.02161 205 GLU A CB  
1568 C CG  A GLU A 205 ? 0.32994 0.35863 0.36579 0.01298  0.03627  -0.01874 205 GLU A CG  
1569 C CG  B GLU A 205 ? 0.30138 0.32238 0.34175 0.01708  0.03228  -0.01988 205 GLU A CG  
1570 C CD  A GLU A 205 ? 0.30082 0.33477 0.34481 0.01281  0.03708  -0.01752 205 GLU A CD  
1571 C CD  B GLU A 205 ? 0.31288 0.33224 0.35065 0.01586  0.02823  -0.01550 205 GLU A CD  
1572 O OE1 A GLU A 205 ? 0.35185 0.38999 0.40296 0.01404  0.04041  -0.02023 205 GLU A OE1 
1573 O OE1 B GLU A 205 ? 0.33100 0.35257 0.36566 0.01375  0.02863  -0.01392 205 GLU A OE1 
1574 O OE2 A GLU A 205 ? 0.28631 0.32028 0.33000 0.01143  0.03439  -0.01400 205 GLU A OE2 
1575 O OE2 B GLU A 205 ? 0.29061 0.30642 0.32939 0.01688  0.02469  -0.01368 205 GLU A OE2 
1576 N N   . PRO A 206 ? 0.25151 0.27817 0.27368 0.01235  0.04280  -0.02764 206 PRO A N   
1577 C CA  . PRO A 206 ? 0.25917 0.28284 0.27185 0.01101  0.04235  -0.02841 206 PRO A CA  
1578 C C   . PRO A 206 ? 0.22268 0.24195 0.23063 0.01038  0.03788  -0.02431 206 PRO A C   
1579 O O   . PRO A 206 ? 0.19945 0.21882 0.20933 0.01008  0.03570  -0.02075 206 PRO A O   
1580 C CB  . PRO A 206 ? 0.28985 0.31821 0.29692 0.00834  0.04574  -0.02904 206 PRO A CB  
1581 C CG  . PRO A 206 ? 0.26337 0.29576 0.27526 0.00771  0.04630  -0.02637 206 PRO A CG  
1582 C CD  . PRO A 206 ? 0.31572 0.34826 0.33834 0.01052  0.04579  -0.02713 206 PRO A CD  
1583 N N   . PRO A 207 ? 0.21327 0.22872 0.21525 0.01012  0.03646  -0.02488 207 PRO A N   
1584 C CA  . PRO A 207 ? 0.17358 0.18523 0.17109 0.00949  0.03265  -0.02126 207 PRO A CA  
1585 C C   . PRO A 207 ? 0.17873 0.19206 0.17023 0.00699  0.03256  -0.01862 207 PRO A C   
1586 O O   . PRO A 207 ? 0.20338 0.21983 0.19101 0.00534  0.03512  -0.01980 207 PRO A O   
1587 C CB  . PRO A 207 ? 0.16793 0.17585 0.16176 0.00991  0.03178  -0.02319 207 PRO A CB  
1588 C CG  . PRO A 207 ? 0.18741 0.19790 0.17999 0.00944  0.03539  -0.02750 207 PRO A CG  
1589 C CD  . PRO A 207 ? 0.20854 0.22300 0.20820 0.01040  0.03827  -0.02911 207 PRO A CD  
1590 N N   . LEU A 208 ? 0.12548 0.13665 0.11622 0.00664  0.02954  -0.01497 208 LEU A N   
1591 C CA  . LEU A 208 ? 0.14624 0.15826 0.13251 0.00445  0.02898  -0.01197 208 LEU A CA  
1592 C C   . LEU A 208 ? 0.13413 0.14224 0.11488 0.00395  0.02620  -0.01009 208 LEU A C   
1593 O O   . LEU A 208 ? 0.15467 0.16285 0.13212 0.00230  0.02536  -0.00739 208 LEU A O   
1594 C CB  . LEU A 208 ? 0.13554 0.14878 0.12634 0.00414  0.02807  -0.00938 208 LEU A CB  
1595 C CG  . LEU A 208 ? 0.17368 0.19158 0.17093 0.00443  0.03074  -0.01066 208 LEU A CG  
1596 C CD1 . LEU A 208 ? 0.14731 0.16629 0.14882 0.00377  0.02929  -0.00780 208 LEU A CD1 
1597 C CD2 . LEU A 208 ? 0.16179 0.18409 0.15632 0.00282  0.03459  -0.01222 208 LEU A CD2 
1598 N N   . THR A 209 ? 0.14760 0.15237 0.12777 0.00531  0.02479  -0.01133 209 THR A N   
1599 C CA  . THR A 209 ? 0.11459 0.11605 0.09038 0.00497  0.02233  -0.00968 209 THR A CA  
1600 C C   . THR A 209 ? 0.12074 0.12345 0.09060 0.00329  0.02305  -0.00984 209 THR A C   
1601 O O   . THR A 209 ? 0.17216 0.17772 0.14058 0.00256  0.02549  -0.01211 209 THR A O   
1602 C CB  . THR A 209 ? 0.14355 0.14159 0.12063 0.00665  0.02088  -0.01091 209 THR A CB  
1603 O OG1 . THR A 209 ? 0.14646 0.14170 0.11994 0.00633  0.01868  -0.00923 209 THR A OG1 
1604 C CG2 . THR A 209 ? 0.13372 0.13229 0.11074 0.00710  0.02269  -0.01444 209 THR A CG2 
1605 N N   . VAL A 210 ? 0.12556 0.12623 0.09203 0.00262  0.02085  -0.00743 210 VAL A N   
1606 C CA  . VAL A 210 ? 0.13477 0.13648 0.09574 0.00095  0.02070  -0.00674 210 VAL A CA  
1607 C C   . VAL A 210 ? 0.14414 0.14352 0.10303 0.00151  0.01916  -0.00783 210 VAL A C   
1608 O O   . VAL A 210 ? 0.15264 0.15255 0.10730 0.00022  0.01825  -0.00687 210 VAL A O   
1609 C CB  . VAL A 210 ? 0.12242 0.12407 0.08176 -0.00041 0.01929  -0.00277 210 VAL A CB  
1610 C CG1 . VAL A 210 ? 0.11488 0.11911 0.07639 -0.00134 0.02090  -0.00161 210 VAL A CG1 
1611 C CG2 . VAL A 210 ? 0.16029 0.15801 0.12139 0.00075  0.01664  -0.00101 210 VAL A CG2 
1612 N N   . PHE A 211 ? 0.12517 0.12212 0.08715 0.00324  0.01871  -0.00954 211 PHE A N   
1613 C CA  . PHE A 211 ? 0.15671 0.15140 0.11753 0.00371  0.01731  -0.01047 211 PHE A CA  
1614 C C   . PHE A 211 ? 0.16044 0.15549 0.12204 0.00410  0.01892  -0.01433 211 PHE A C   
1615 O O   . PHE A 211 ? 0.14947 0.14400 0.11535 0.00543  0.01998  -0.01588 211 PHE A O   
1616 C CB  . PHE A 211 ? 0.15788 0.14927 0.12148 0.00513  0.01548  -0.00912 211 PHE A CB  
1617 C CG  . PHE A 211 ? 0.16011 0.15073 0.12337 0.00486  0.01403  -0.00597 211 PHE A CG  
1618 C CD1 . PHE A 211 ? 0.16387 0.15534 0.12403 0.00360  0.01321  -0.00405 211 PHE A CD1 
1619 C CD2 . PHE A 211 ? 0.16916 0.15813 0.13532 0.00578  0.01335  -0.00494 211 PHE A CD2 
1620 C CE1 . PHE A 211 ? 0.16409 0.15440 0.12470 0.00347  0.01189  -0.00129 211 PHE A CE1 
1621 C CE2 . PHE A 211 ? 0.15195 0.13990 0.11796 0.00547  0.01212  -0.00257 211 PHE A CE2 
1622 C CZ  . PHE A 211 ? 0.15718 0.14561 0.12074 0.00442  0.01148  -0.00081 211 PHE A CZ  
1623 N N   . LYS A 212 ? 0.14923 0.14511 0.10701 0.00290  0.01894  -0.01589 212 LYS A N   
1624 C CA  . LYS A 212 ? 0.16231 0.15837 0.12040 0.00296  0.02050  -0.02005 212 LYS A CA  
1625 C C   . LYS A 212 ? 0.13103 0.12376 0.09076 0.00378  0.01885  -0.02088 212 LYS A C   
1626 O O   . LYS A 212 ? 0.16307 0.15477 0.12103 0.00333  0.01669  -0.01887 212 LYS A O   
1627 C CB  . LYS A 212 ? 0.16992 0.16908 0.12239 0.00078  0.02152  -0.02170 212 LYS A CB  
1628 C CG  . LYS A 212 ? 0.21329 0.21603 0.16308 -0.00060 0.02284  -0.01989 212 LYS A CG  
1629 C CD  . LYS A 212 ? 0.22015 0.22402 0.17456 0.00054  0.02528  -0.02069 212 LYS A CD  
1630 C CE  . LYS A 212 ? 0.17928 0.18522 0.13432 0.00050  0.02855  -0.02551 212 LYS A CE  
1631 N NZ  . LYS A 212 ? 0.18305 0.19338 0.13234 -0.00197 0.03057  -0.02621 212 LYS A NZ  
1632 N N   . GLY A 213 ? 0.12740 0.11854 0.09108 0.00498  0.01993  -0.02373 213 GLY A N   
1633 C CA  . GLY A 213 ? 0.13971 0.12755 0.10555 0.00563  0.01850  -0.02431 213 GLY A CA  
1634 C C   . GLY A 213 ? 0.11529 0.10317 0.07812 0.00417  0.01825  -0.02700 213 GLY A C   
1635 O O   . GLY A 213 ? 0.14887 0.13940 0.10759 0.00264  0.01928  -0.02888 213 GLY A O   
1636 N N   . GLY A 214 ? 0.10864 0.09367 0.07343 0.00444  0.01677  -0.02711 214 GLY A N   
1637 C CA  . GLY A 214 ? 0.13030 0.11502 0.09310 0.00298  0.01621  -0.02975 214 GLY A CA  
1638 C C   . GLY A 214 ? 0.12731 0.11170 0.08847 0.00206  0.01364  -0.02730 214 GLY A C   
1639 O O   . GLY A 214 ? 0.12074 0.10608 0.08069 0.00220  0.01248  -0.02372 214 GLY A O   
1640 N N   . GLU A 215 ? 0.13573 0.11879 0.09740 0.00112  0.01277  -0.02935 215 GLU A N   
1641 C CA  . GLU A 215 ? 0.12103 0.10427 0.08186 0.00013  0.01038  -0.02726 215 GLU A CA  
1642 C C   . GLU A 215 ? 0.11680 0.10360 0.07245 -0.00147 0.00921  -0.02600 215 GLU A C   
1643 O O   . GLU A 215 ? 0.11108 0.09874 0.06654 -0.00158 0.00737  -0.02271 215 GLU A O   
1644 C CB  . GLU A 215 ? 0.11452 0.09580 0.07729 -0.00086 0.00972  -0.02999 215 GLU A CB  
1645 C CG  . GLU A 215 ? 0.11392 0.09596 0.07638 -0.00214 0.00728  -0.02819 215 GLU A CG  
1646 C CD  . GLU A 215 ? 0.13093 0.11146 0.09495 -0.00363 0.00657  -0.03127 215 GLU A CD  
1647 O OE1 . GLU A 215 ? 0.13205 0.11079 0.09693 -0.00371 0.00800  -0.03516 215 GLU A OE1 
1648 O OE2 . GLU A 215 ? 0.12293 0.10406 0.08779 -0.00472 0.00460  -0.02992 215 GLU A OE2 
1649 N N   . THR A 216 ? 0.12752 0.11656 0.07910 -0.00276 0.01029  -0.02851 216 THR A N   
1650 C CA  . THR A 216 ? 0.16168 0.15429 0.10787 -0.00461 0.00896  -0.02700 216 THR A CA  
1651 C C   . THR A 216 ? 0.15021 0.14398 0.09596 -0.00375 0.00866  -0.02259 216 THR A C   
1652 O O   . THR A 216 ? 0.13550 0.13078 0.07980 -0.00442 0.00646  -0.01938 216 THR A O   
1653 C CB  . THR A 216 ? 0.18180 0.17675 0.12318 -0.00636 0.01058  -0.03074 216 THR A CB  
1654 O OG1 . THR A 216 ? 0.20279 0.19612 0.14512 -0.00708 0.01101  -0.03542 216 THR A OG1 
1655 C CG2 . THR A 216 ? 0.19669 0.19548 0.13193 -0.00871 0.00874  -0.02887 216 THR A CG2 
1656 N N   . GLU A 217 ? 0.14889 0.14194 0.09638 -0.00227 0.01072  -0.02237 217 GLU A N   
1657 C CA  . GLU A 217 ? 0.15119 0.14491 0.09876 -0.00154 0.01044  -0.01842 217 GLU A CA  
1658 C C   . GLU A 217 ? 0.12689 0.11849 0.07803 -0.00019 0.00875  -0.01548 217 GLU A C   
1659 O O   . GLU A 217 ? 0.16126 0.15351 0.11204 -0.00007 0.00758  -0.01213 217 GLU A O   
1660 C CB  . GLU A 217 ? 0.13267 0.12632 0.08181 -0.00044 0.01296  -0.01914 217 GLU A CB  
1661 C CG  . GLU A 217 ? 0.17618 0.17287 0.12154 -0.00187 0.01503  -0.02139 217 GLU A CG  
1662 C CD  . GLU A 217 ? 0.19338 0.19312 0.13398 -0.00360 0.01419  -0.01834 217 GLU A CD  
1663 O OE1 . GLU A 217 ? 0.19956 0.19868 0.14118 -0.00311 0.01249  -0.01432 217 GLU A OE1 
1664 O OE2 . GLU A 217 ? 0.28113 0.28386 0.21698 -0.00554 0.01524  -0.01996 217 GLU A OE2 
1665 N N   . ALA A 218 ? 0.12313 0.11217 0.07784 0.00076  0.00872  -0.01670 218 ALA A N   
1666 C CA  . ALA A 218 ? 0.14510 0.13252 0.10280 0.00179  0.00745  -0.01421 218 ALA A CA  
1667 C C   . ALA A 218 ? 0.14803 0.13701 0.10479 0.00075  0.00524  -0.01262 218 ALA A C   
1668 O O   . ALA A 218 ? 0.13464 0.12383 0.09250 0.00136  0.00421  -0.00972 218 ALA A O   
1669 C CB  . ALA A 218 ? 0.14136 0.12601 0.10276 0.00266  0.00796  -0.01566 218 ALA A CB  
1670 N N   . LEU A 219 ? 0.14067 0.13080 0.09580 -0.00084 0.00442  -0.01463 219 LEU A N   
1671 C CA  . LEU A 219 ? 0.14724 0.13937 0.10180 -0.00201 0.00197  -0.01306 219 LEU A CA  
1672 C C   . LEU A 219 ? 0.14797 0.14267 0.09945 -0.00266 0.00083  -0.01030 219 LEU A C   
1673 O O   . LEU A 219 ? 0.16055 0.15645 0.11331 -0.00270 -0.00124 -0.00750 219 LEU A O   
1674 C CB  . LEU A 219 ? 0.16137 0.15431 0.11447 -0.00391 0.00118  -0.01610 219 LEU A CB  
1675 C CG  . LEU A 219 ? 0.11801 0.10825 0.07478 -0.00362 0.00184  -0.01853 219 LEU A CG  
1676 C CD1 . LEU A 219 ? 0.11501 0.10588 0.06995 -0.00575 0.00117  -0.02211 219 LEU A CD1 
1677 C CD2 . LEU A 219 ? 0.14585 0.13543 0.10702 -0.00283 0.00077  -0.01609 219 LEU A CD2 
1678 N N   . ALA A 220 ? 0.14256 0.13822 0.09046 -0.00320 0.00217  -0.01088 220 ALA A N   
1679 C CA  . ALA A 220 ? 0.15247 0.15040 0.09745 -0.00401 0.00115  -0.00777 220 ALA A CA  
1680 C C   . ALA A 220 ? 0.14601 0.14247 0.09425 -0.00223 0.00103  -0.00443 220 ALA A C   
1681 O O   . ALA A 220 ? 0.16065 0.15823 0.10897 -0.00247 -0.00083 -0.00106 220 ALA A O   
1682 C CB  . ALA A 220 ? 0.12994 0.12952 0.07032 -0.00523 0.00304  -0.00934 220 ALA A CB  
1683 N N   . ARG A 221 ? 0.13835 0.13225 0.08949 -0.00051 0.00286  -0.00533 221 ARG A N   
1684 C CA  . ARG A 221 ? 0.16525 0.15755 0.11933 0.00103  0.00279  -0.00276 221 ARG A CA  
1685 C C   . ARG A 221 ? 0.14478 0.13629 0.10247 0.00193  0.00134  -0.00153 221 ARG A C   
1686 O O   . ARG A 221 ? 0.13284 0.12378 0.09268 0.00283  0.00064  0.00091  221 ARG A O   
1687 C CB  . ARG A 221 ? 0.14316 0.13332 0.09886 0.00231  0.00492  -0.00412 221 ARG A CB  
1688 C CG  . ARG A 221 ? 0.17923 0.16808 0.13675 0.00339  0.00502  -0.00184 221 ARG A CG  
1689 C CD  . ARG A 221 ? 0.14948 0.13843 0.10618 0.00334  0.00670  -0.00233 221 ARG A CD  
1690 N NE  . ARG A 221 ? 0.17610 0.16460 0.13350 0.00351  0.00636  0.00025  221 ARG A NE  
1691 C CZ  . ARG A 221 ? 0.20524 0.19437 0.16210 0.00309  0.00747  0.00065  221 ARG A CZ  
1692 N NH1 . ARG A 221 ? 0.24946 0.23997 0.20525 0.00266  0.00921  -0.00143 221 ARG A NH1 
1693 N NH2 . ARG A 221 ? 0.28565 0.27402 0.24356 0.00308  0.00692  0.00308  221 ARG A NH2 
1694 N N   . LEU A 222 ? 0.14175 0.13326 0.10056 0.00167  0.00102  -0.00330 222 LEU A N   
1695 C CA  . LEU A 222 ? 0.13320 0.12463 0.09579 0.00233  -0.00012 -0.00222 222 LEU A CA  
1696 C C   . LEU A 222 ? 0.14725 0.14113 0.11011 0.00165  -0.00259 0.00033  222 LEU A C   
1697 O O   . LEU A 222 ? 0.17178 0.16553 0.13812 0.00278  -0.00332 0.00248  222 LEU A O   
1698 C CB  . LEU A 222 ? 0.15238 0.14342 0.11622 0.00184  0.00008  -0.00458 222 LEU A CB  
1699 C CG  . LEU A 222 ? 0.16632 0.15744 0.13452 0.00242  -0.00050 -0.00377 222 LEU A CG  
1700 C CD1 . LEU A 222 ? 0.15205 0.14103 0.12257 0.00415  0.00111  -0.00315 222 LEU A CD1 
1701 C CD2 . LEU A 222 ? 0.18956 0.18069 0.15871 0.00131  -0.00066 -0.00589 222 LEU A CD2 
1702 N N   . GLU A 223 ? 0.13713 0.13334 0.09646 -0.00024 -0.00395 0.00009  223 GLU A N   
1703 C CA  . GLU A 223 ? 0.17248 0.17135 0.13190 -0.00112 -0.00678 0.00295  223 GLU A CA  
1704 C C   . GLU A 223 ? 0.17184 0.17050 0.13121 -0.00053 -0.00723 0.00628  223 GLU A C   
1705 O O   . GLU A 223 ? 0.14737 0.14688 0.10993 -0.00002 -0.00927 0.00930  223 GLU A O   
1706 C CB  . GLU A 223 ? 0.15706 0.15861 0.11164 -0.00365 -0.00817 0.00182  223 GLU A CB  
1707 C CG  . GLU A 223 ? 0.18832 0.18987 0.14314 -0.00454 -0.00799 -0.00167 223 GLU A CG  
1708 C CD  . GLU A 223 ? 0.16869 0.17156 0.12822 -0.00450 -0.01015 -0.00062 223 GLU A CD  
1709 O OE1 . GLU A 223 ? 0.22186 0.22597 0.18452 -0.00372 -0.01189 0.00276  223 GLU A OE1 
1710 O OE2 . GLU A 223 ? 0.13507 0.13777 0.09573 -0.00526 -0.01008 -0.00319 223 GLU A OE2 
1711 N N   . ALA A 224 ? 0.16947 0.16699 0.12591 -0.00058 -0.00538 0.00585  224 ALA A N   
1712 C CA  . ALA A 224 ? 0.18870 0.18579 0.14526 -0.00028 -0.00574 0.00904  224 ALA A CA  
1713 C C   . ALA A 224 ? 0.20347 0.19811 0.16561 0.00194  -0.00558 0.01029  224 ALA A C   
1714 O O   . ALA A 224 ? 0.20923 0.20360 0.17342 0.00234  -0.00692 0.01344  224 ALA A O   
1715 C CB  . ALA A 224 ? 0.20765 0.20424 0.16055 -0.00086 -0.00351 0.00800  224 ALA A CB  
1716 N N   . ALA A 225 ? 0.17533 0.16813 0.13995 0.00331  -0.00392 0.00786  225 ALA A N   
1717 C CA  . ALA A 225 ? 0.15594 0.14667 0.12532 0.00524  -0.00346 0.00847  225 ALA A CA  
1718 C C   . ALA A 225 ? 0.17934 0.17141 0.15322 0.00588  -0.00521 0.00980  225 ALA A C   
1719 O O   . ALA A 225 ? 0.19736 0.18838 0.17549 0.00730  -0.00549 0.01125  225 ALA A O   
1720 C CB  . ALA A 225 ? 0.14640 0.13507 0.11627 0.00619  -0.00110 0.00566  225 ALA A CB  
1721 N N   . PHE A 226 ? 0.17828 0.17272 0.15179 0.00484  -0.00640 0.00918  226 PHE A N   
1722 C CA  . PHE A 226 ? 0.16373 0.16010 0.14210 0.00529  -0.00816 0.01038  226 PHE A CA  
1723 C C   . PHE A 226 ? 0.19253 0.19138 0.17122 0.00439  -0.01140 0.01379  226 PHE A C   
1724 O O   . PHE A 226 ? 0.14986 0.15096 0.13285 0.00457  -0.01338 0.01509  226 PHE A O   
1725 C CB  . PHE A 226 ? 0.14007 0.13780 0.11858 0.00445  -0.00797 0.00803  226 PHE A CB  
1726 C CG  . PHE A 226 ? 0.14421 0.13998 0.12482 0.00561  -0.00535 0.00576  226 PHE A CG  
1727 C CD1 . PHE A 226 ? 0.15464 0.14810 0.13182 0.00550  -0.00320 0.00360  226 PHE A CD1 
1728 C CD2 . PHE A 226 ? 0.13043 0.12696 0.11661 0.00673  -0.00503 0.00594  226 PHE A CD2 
1729 C CE1 . PHE A 226 ? 0.14912 0.14092 0.12789 0.00634  -0.00111 0.00202  226 PHE A CE1 
1730 C CE2 . PHE A 226 ? 0.11606 0.11111 0.10351 0.00747  -0.00255 0.00410  226 PHE A CE2 
1731 C CZ  . PHE A 226 ? 0.13928 0.13188 0.12276 0.00720  -0.00075 0.00231  226 PHE A CZ  
1732 N N   . GLN A 227 ? 0.21492 0.21370 0.18939 0.00331  -0.01207 0.01551  227 GLN A N   
1733 C CA  . GLN A 227 ? 0.21597 0.21702 0.19054 0.00232  -0.01535 0.01945  227 GLN A CA  
1734 C C   . GLN A 227 ? 0.20191 0.20180 0.18320 0.00429  -0.01644 0.02248  227 GLN A C   
1735 O O   . GLN A 227 ? 0.19124 0.19309 0.17475 0.00390  -0.01960 0.02614  227 GLN A O   
1736 C CB  . GLN A 227 ? 0.21449 0.21597 0.18234 0.00035  -0.01547 0.02061  227 GLN A CB  
1737 C CG  . GLN A 227 ? 0.26390 0.26780 0.22532 -0.00206 -0.01550 0.01833  227 GLN A CG  
1738 C CD  . GLN A 227 ? 0.27907 0.28385 0.23380 -0.00407 -0.01512 0.01927  227 GLN A CD  
1739 O OE1 . GLN A 227 ? 0.22069 0.22789 0.16972 -0.00633 -0.01539 0.01781  227 GLN A OE1 
1740 N NE2 . GLN A 227 ? 0.29271 0.29561 0.24817 -0.00341 -0.01434 0.02152  227 GLN A NE2 
1741 N N   . ASP A 228 ? 0.18900 0.18572 0.17367 0.00635  -0.01398 0.02098  228 ASP A N   
1742 C CA  . ASP A 228 ? 0.20551 0.20065 0.19722 0.00848  -0.01443 0.02283  228 ASP A CA  
1743 C C   . ASP A 228 ? 0.16945 0.16402 0.16590 0.01033  -0.01228 0.01982  228 ASP A C   
1744 O O   . ASP A 228 ? 0.14604 0.13793 0.14178 0.01122  -0.00940 0.01718  228 ASP A O   
1745 C CB  . ASP A 228 ? 0.18454 0.17624 0.17551 0.00892  -0.01339 0.02375  228 ASP A CB  
1746 C CG  . ASP A 228 ? 0.22150 0.21121 0.21999 0.01099  -0.01410 0.02566  228 ASP A CG  
1747 O OD1 . ASP A 228 ? 0.24864 0.24009 0.25310 0.01210  -0.01569 0.02683  228 ASP A OD1 
1748 O OD2 . ASP A 228 ? 0.26098 0.24737 0.25989 0.01152  -0.01307 0.02587  228 ASP A OD2 
1749 N N   . PRO A 229 ? 0.17840 0.17576 0.17969 0.01079  -0.01359 0.02021  229 PRO A N   
1750 C CA  . PRO A 229 ? 0.16053 0.15787 0.16630 0.01231  -0.01122 0.01742  229 PRO A CA  
1751 C C   . PRO A 229 ? 0.15948 0.15413 0.17051 0.01469  -0.00938 0.01686  229 PRO A C   
1752 O O   . PRO A 229 ? 0.16120 0.15514 0.17380 0.01569  -0.00654 0.01394  229 PRO A O   
1753 C CB  . PRO A 229 ? 0.17821 0.17971 0.18880 0.01207  -0.01356 0.01871  229 PRO A CB  
1754 C CG  . PRO A 229 ? 0.18091 0.18388 0.19196 0.01135  -0.01741 0.02290  229 PRO A CG  
1755 C CD  . PRO A 229 ? 0.18389 0.18491 0.18679 0.00972  -0.01735 0.02332  229 PRO A CD  
1756 N N   . LYS A 230 ? 0.17436 0.16744 0.18809 0.01548  -0.01090 0.01952  230 LYS A N   
1757 C CA  . LYS A 230 ? 0.17907 0.16898 0.19761 0.01764  -0.00903 0.01847  230 LYS A CA  
1758 C C   . LYS A 230 ? 0.16078 0.14724 0.17387 0.01733  -0.00619 0.01563  230 LYS A C   
1759 O O   . LYS A 230 ? 0.13994 0.12455 0.15515 0.01869  -0.00355 0.01282  230 LYS A O   
1760 C CB  . LYS A 230 ? 0.22035 0.20897 0.24343 0.01840  -0.01162 0.02226  230 LYS A CB  
1761 C CG  . LYS A 230 ? 0.23262 0.22265 0.26582 0.02059  -0.01269 0.02347  230 LYS A CG  
1762 C CD  . LYS A 230 ? 0.29626 0.29101 0.33146 0.01972  -0.01609 0.02646  230 LYS A CD  
1763 C CE  . LYS A 230 ? 0.21759 0.21246 0.25350 0.01897  -0.02023 0.03174  230 LYS A CE  
1764 N NZ  . LYS A 230 ? 0.21784 0.21022 0.26282 0.02141  -0.02091 0.03362  230 LYS A NZ  
1765 N N   . TRP A 231 ? 0.13169 0.11757 0.13782 0.01548  -0.00668 0.01626  231 TRP A N   
1766 C CA  . TRP A 231 ? 0.14186 0.12486 0.14333 0.01511  -0.00435 0.01391  231 TRP A CA  
1767 C C   . TRP A 231 ? 0.14023 0.12378 0.13925 0.01502  -0.00188 0.01045  231 TRP A C   
1768 O O   . TRP A 231 ? 0.15039 0.13168 0.14832 0.01553  0.00036  0.00805  231 TRP A O   
1769 C CB  . TRP A 231 ? 0.14750 0.13036 0.14297 0.01317  -0.00540 0.01557  231 TRP A CB  
1770 C CG  . TRP A 231 ? 0.11594 0.09635 0.10725 0.01272  -0.00331 0.01348  231 TRP A CG  
1771 C CD1 . TRP A 231 ? 0.12896 0.10627 0.12103 0.01304  -0.00280 0.01363  231 TRP A CD1 
1772 C CD2 . TRP A 231 ? 0.12016 0.10106 0.10651 0.01183  -0.00170 0.01105  231 TRP A CD2 
1773 N NE1 . TRP A 231 ? 0.14242 0.11866 0.13021 0.01233  -0.00107 0.01149  231 TRP A NE1 
1774 C CE2 . TRP A 231 ? 0.12913 0.10750 0.11354 0.01170  -0.00038 0.00999  231 TRP A CE2 
1775 C CE3 . TRP A 231 ? 0.12506 0.10817 0.10891 0.01110  -0.00138 0.00971  231 TRP A CE3 
1776 C CZ2 . TRP A 231 ? 0.13380 0.11205 0.11416 0.01103  0.00113  0.00789  231 TRP A CZ2 
1777 C CZ3 . TRP A 231 ? 0.13616 0.11869 0.11605 0.01049  0.00026  0.00753  231 TRP A CZ3 
1778 C CH2 . TRP A 231 ? 0.11438 0.09462 0.09268 0.01053  0.00144  0.00676  231 TRP A CH2 
1779 N N   . VAL A 232 ? 0.13346 0.11997 0.13157 0.01421  -0.00242 0.01027  232 VAL A N   
1780 C CA  . VAL A 232 ? 0.13644 0.12338 0.13259 0.01393  -0.00028 0.00748  232 VAL A CA  
1781 C C   . VAL A 232 ? 0.11484 0.10183 0.11591 0.01550  0.00167  0.00582  232 VAL A C   
1782 O O   . VAL A 232 ? 0.09488 0.08070 0.09409 0.01559  0.00408  0.00346  232 VAL A O   
1783 C CB  . VAL A 232 ? 0.12711 0.11698 0.12151 0.01246  -0.00153 0.00773  232 VAL A CB  
1784 C CG1 . VAL A 232 ? 0.11630 0.10639 0.10958 0.01213  0.00055  0.00523  232 VAL A CG1 
1785 C CG2 . VAL A 232 ? 0.13675 0.12664 0.12563 0.01082  -0.00287 0.00866  232 VAL A CG2 
1786 N N   . ALA A 233 ? 0.16097 0.14952 0.16851 0.01670  0.00070  0.00707  233 ALA A N   
1787 C CA  . ALA A 233 ? 0.17791 0.16717 0.19080 0.01823  0.00288  0.00525  233 ALA A CA  
1788 C C   . ALA A 233 ? 0.14081 0.12668 0.15400 0.01943  0.00503  0.00331  233 ALA A C   
1789 O O   . ALA A 233 ? 0.14195 0.12752 0.15463 0.01975  0.00786  0.00058  233 ALA A O   
1790 C CB  . ALA A 233 ? 0.13510 0.12718 0.15584 0.01936  0.00115  0.00716  233 ALA A CB  
1791 N N   . GLY A 234 ? 0.17218 0.15550 0.18603 0.01990  0.00367  0.00470  234 GLY A N   
1792 C CA  . GLY A 234 ? 0.15194 0.13180 0.16666 0.02093  0.00539  0.00275  234 GLY A CA  
1793 C C   . GLY A 234 ? 0.15341 0.13065 0.16107 0.01963  0.00620  0.00150  234 GLY A C   
1794 O O   . GLY A 234 ? 0.18679 0.16084 0.19447 0.01998  0.00666  0.00060  234 GLY A O   
1795 N N   . PHE A 235 ? 0.14599 0.12455 0.14812 0.01813  0.00628  0.00140  235 PHE A N   
1796 C CA  . PHE A 235 ? 0.14102 0.11758 0.13710 0.01696  0.00683  0.00048  235 PHE A CA  
1797 C C   . PHE A 235 ? 0.15035 0.12533 0.14525 0.01729  0.00935  -0.00262 235 PHE A C   
1798 O O   . PHE A 235 ? 0.13090 0.10746 0.12613 0.01746  0.01112  -0.00421 235 PHE A O   
1799 C CB  . PHE A 235 ? 0.11326 0.09163 0.10479 0.01550  0.00639  0.00097  235 PHE A CB  
1800 C CG  . PHE A 235 ? 0.12718 0.10394 0.11341 0.01449  0.00702  0.00001  235 PHE A CG  
1801 C CD1 . PHE A 235 ? 0.14609 0.12177 0.13008 0.01375  0.00583  0.00129  235 PHE A CD1 
1802 C CD2 . PHE A 235 ? 0.12134 0.09797 0.10511 0.01418  0.00874  -0.00191 235 PHE A CD2 
1803 C CE1 . PHE A 235 ? 0.13974 0.11437 0.11981 0.01291  0.00636  0.00046  235 PHE A CE1 
1804 C CE2 . PHE A 235 ? 0.10853 0.08389 0.08810 0.01332  0.00895  -0.00246 235 PHE A CE2 
1805 C CZ  . PHE A 235 ? 0.10512 0.07956 0.08317 0.01278  0.00777  -0.00138 235 PHE A CZ  
1806 N N   . GLN A 236 ? 0.13384 0.10587 0.12722 0.01714  0.00946  -0.00343 236 GLN A N   
1807 C CA  . GLN A 236 ? 0.13997 0.11042 0.13098 0.01699  0.01146  -0.00642 236 GLN A CA  
1808 C C   . GLN A 236 ? 0.14660 0.11557 0.13247 0.01559  0.01074  -0.00625 236 GLN A C   
1809 O O   . GLN A 236 ? 0.14582 0.11301 0.13209 0.01531  0.00939  -0.00510 236 GLN A O   
1810 C CB  . GLN A 236 ? 0.18010 0.14828 0.17538 0.01826  0.01240  -0.00831 236 GLN A CB  
1811 C CG  . GLN A 236 ? 0.18397 0.15385 0.18553 0.01993  0.01333  -0.00869 236 GLN A CG  
1812 C CD  . GLN A 236 ? 0.19526 0.16331 0.20012 0.02113  0.01553  -0.01210 236 GLN A CD  
1813 O OE1 . GLN A 236 ? 0.27473 0.24172 0.28619 0.02272  0.01524  -0.01199 236 GLN A OE1 
1814 N NE2 . GLN A 236 ? 0.22633 0.19404 0.22669 0.02033  0.01772  -0.01520 236 GLN A NE2 
1815 N N   . LYS A 237 ? 0.11799 0.08785 0.09951 0.01466  0.01158  -0.00716 237 LYS A N   
1816 C CA  . LYS A 237 ? 0.13469 0.10379 0.11204 0.01342  0.01073  -0.00671 237 LYS A CA  
1817 C C   . LYS A 237 ? 0.14205 0.10850 0.11873 0.01304  0.01055  -0.00798 237 LYS A C   
1818 O O   . LYS A 237 ? 0.12315 0.08879 0.09932 0.01238  0.00919  -0.00666 237 LYS A O   
1819 C CB  . LYS A 237 ? 0.11768 0.08816 0.09136 0.01263  0.01150  -0.00720 237 LYS A CB  
1820 C CG  . LYS A 237 ? 0.14129 0.11153 0.11172 0.01158  0.01044  -0.00638 237 LYS A CG  
1821 C CD  . LYS A 237 ? 0.10865 0.07974 0.07994 0.01149  0.00916  -0.00440 237 LYS A CD  
1822 C CE  . LYS A 237 ? 0.09702 0.06832 0.06590 0.01064  0.00851  -0.00387 237 LYS A CE  
1823 N NZ  . LYS A 237 ? 0.09039 0.06249 0.05742 0.01032  0.00899  -0.00413 237 LYS A NZ  
1824 N N   . PRO A 238 ? 0.16511 0.13027 0.14172 0.01325  0.01192  -0.01064 238 PRO A N   
1825 C CA  . PRO A 238 ? 0.15259 0.11507 0.12839 0.01259  0.01151  -0.01211 238 PRO A CA  
1826 C C   . PRO A 238 ? 0.16557 0.12581 0.14568 0.01310  0.01039  -0.01116 238 PRO A C   
1827 O O   . PRO A 238 ? 0.13176 0.08962 0.11165 0.01233  0.00976  -0.01203 238 PRO A O   
1828 C CB  . PRO A 238 ? 0.16362 0.12551 0.13838 0.01271  0.01354  -0.01560 238 PRO A CB  
1829 C CG  . PRO A 238 ? 0.17337 0.13814 0.14672 0.01289  0.01493  -0.01544 238 PRO A CG  
1830 C CD  . PRO A 238 ? 0.15358 0.11987 0.13030 0.01377  0.01405  -0.01269 238 PRO A CD  
1831 N N   . ASP A 239 ? 0.15411 0.11503 0.13824 0.01421  0.00993  -0.00919 239 ASP A N   
1832 C CA  . ASP A 239 ? 0.16165 0.12047 0.15017 0.01464  0.00862  -0.00758 239 ASP A CA  
1833 C C   . ASP A 239 ? 0.14546 0.10532 0.13320 0.01375  0.00675  -0.00396 239 ASP A C   
1834 O O   . ASP A 239 ? 0.14410 0.10262 0.13516 0.01384  0.00546  -0.00180 239 ASP A O   
1835 C CB  . ASP A 239 ? 0.17630 0.13520 0.17049 0.01646  0.00906  -0.00749 239 ASP A CB  
1836 C CG  . ASP A 239 ? 0.19616 0.15386 0.19205 0.01744  0.01129  -0.01145 239 ASP A CG  
1837 O OD1 . ASP A 239 ? 0.20758 0.16412 0.19966 0.01649  0.01229  -0.01424 239 ASP A OD1 
1838 O OD2 . ASP A 239 ? 0.25032 0.20848 0.25143 0.01911  0.01205  -0.01185 239 ASP A OD2 
1839 N N   . THR A 240 ? 0.13802 0.10023 0.12161 0.01283  0.00666  -0.00323 240 THR A N   
1840 C CA  . THR A 240 ? 0.11944 0.08302 0.10196 0.01190  0.00535  -0.00033 240 THR A CA  
1841 C C   . THR A 240 ? 0.11393 0.07600 0.09564 0.01059  0.00471  0.00006  240 THR A C   
1842 O O   . THR A 240 ? 0.12539 0.08568 0.10643 0.01021  0.00510  -0.00209 240 THR A O   
1843 C CB  . THR A 240 ? 0.12378 0.09030 0.10289 0.01152  0.00569  -0.00014 240 THR A CB  
1844 O OG1 . THR A 240 ? 0.15842 0.12482 0.13464 0.01112  0.00656  -0.00221 240 THR A OG1 
1845 C CG2 . THR A 240 ? 0.13303 0.10130 0.11348 0.01250  0.00600  -0.00001 240 THR A CG2 
1846 N N   . ASP A 241 ? 0.09940 0.06248 0.08106 0.00969  0.00372  0.00285  241 ASP A N   
1847 C CA  . ASP A 241 ? 0.10713 0.06920 0.08885 0.00829  0.00313  0.00378  241 ASP A CA  
1848 C C   . ASP A 241 ? 0.10683 0.07128 0.08524 0.00730  0.00355  0.00345  241 ASP A C   
1849 O O   . ASP A 241 ? 0.11332 0.08047 0.09006 0.00709  0.00370  0.00471  241 ASP A O   
1850 C CB  . ASP A 241 ? 0.12061 0.08268 0.10433 0.00765  0.00198  0.00730  241 ASP A CB  
1851 C CG  . ASP A 241 ? 0.12128 0.08153 0.10646 0.00618  0.00137  0.00838  241 ASP A CG  
1852 O OD1 . ASP A 241 ? 0.10790 0.06812 0.09176 0.00534  0.00177  0.00674  241 ASP A OD1 
1853 O OD2 . ASP A 241 ? 0.14064 0.09955 0.12857 0.00575  0.00032  0.01112  241 ASP A OD2 
1854 N N   . PRO A 242 ? 0.09891 0.06255 0.07654 0.00667  0.00365  0.00172  242 PRO A N   
1855 C CA  . PRO A 242 ? 0.10256 0.06862 0.07816 0.00587  0.00385  0.00170  242 PRO A CA  
1856 C C   . PRO A 242 ? 0.10070 0.06812 0.07724 0.00451  0.00356  0.00388  242 PRO A C   
1857 O O   . PRO A 242 ? 0.10153 0.07171 0.07696 0.00412  0.00406  0.00418  242 PRO A O   
1858 C CB  . PRO A 242 ? 0.09807 0.06284 0.07292 0.00553  0.00364  -0.00061 242 PRO A CB  
1859 C CG  . PRO A 242 ? 0.11970 0.08111 0.09663 0.00542  0.00324  -0.00145 242 PRO A CG  
1860 C CD  . PRO A 242 ? 0.10138 0.06202 0.08002 0.00666  0.00355  -0.00053 242 PRO A CD  
1861 N N   . SER A 243 ? 0.12385 0.08947 0.10270 0.00375  0.00289  0.00541  243 SER A N   
1862 C CA  . SER A 243 ? 0.11722 0.08427 0.09703 0.00214  0.00276  0.00777  243 SER A CA  
1863 C C   . SER A 243 ? 0.13715 0.10646 0.11594 0.00189  0.00305  0.01038  243 SER A C   
1864 O O   . SER A 243 ? 0.12911 0.10030 0.10806 0.00038  0.00330  0.01245  243 SER A O   
1865 C CB  . SER A 243 ? 0.14499 0.10888 0.12793 0.00109  0.00179  0.00855  243 SER A CB  
1866 O OG  . SER A 243 ? 0.15932 0.12057 0.14409 0.00187  0.00119  0.00958  243 SER A OG  
1867 N N   . ALA A 244 ? 0.11598 0.08546 0.09367 0.00313  0.00302  0.01034  244 ALA A N   
1868 C CA  . ALA A 244 ? 0.12517 0.09702 0.10134 0.00269  0.00298  0.01269  244 ALA A CA  
1869 C C   . ALA A 244 ? 0.12736 0.10289 0.10065 0.00227  0.00427  0.01184  244 ALA A C   
1870 O O   . ALA A 244 ? 0.13193 0.10804 0.10408 0.00333  0.00487  0.00949  244 ALA A O   
1871 C CB  . ALA A 244 ? 0.12516 0.09627 0.10160 0.00409  0.00229  0.01277  244 ALA A CB  
1872 N N   . TRP A 245 ? 0.12644 0.10446 0.09880 0.00066  0.00482  0.01372  245 TRP A N   
1873 C CA  . TRP A 245 ? 0.14461 0.12627 0.11468 0.00023  0.00639  0.01264  245 TRP A CA  
1874 C C   . TRP A 245 ? 0.14921 0.13367 0.11622 -0.00086 0.00671  0.01436  245 TRP A C   
1875 O O   . TRP A 245 ? 0.13423 0.12104 0.09889 -0.00065 0.00778  0.01260  245 TRP A O   
1876 C CB  . TRP A 245 ? 0.12346 0.10660 0.09513 -0.00086 0.00743  0.01251  245 TRP A CB  
1877 C CG  . TRP A 245 ? 0.17998 0.16365 0.15255 -0.00284 0.00730  0.01561  245 TRP A CG  
1878 C CD1 . TRP A 245 ? 0.14998 0.13076 0.12539 -0.00350 0.00607  0.01719  245 TRP A CD1 
1879 C CD2 . TRP A 245 ? 0.16715 0.15444 0.13772 -0.00464 0.00854  0.01755  245 TRP A CD2 
1880 N NE1 . TRP A 245 ? 0.16279 0.14501 0.13845 -0.00562 0.00631  0.02037  245 TRP A NE1 
1881 C CE2 . TRP A 245 ? 0.17913 0.16558 0.15155 -0.00642 0.00790  0.02074  245 TRP A CE2 
1882 C CE3 . TRP A 245 ? 0.14932 0.14047 0.11661 -0.00507 0.01022  0.01674  245 TRP A CE3 
1883 C CZ2 . TRP A 245 ? 0.17694 0.16659 0.14779 -0.00871 0.00892  0.02354  245 TRP A CZ2 
1884 C CZ3 . TRP A 245 ? 0.17838 0.17281 0.14377 -0.00729 0.01138  0.01905  245 TRP A CZ3 
1885 C CH2 . TRP A 245 ? 0.22037 0.21418 0.18742 -0.00914 0.01074  0.02262  245 TRP A CH2 
1886 N N   . GLU A 246 ? 0.16238 0.14661 0.12932 -0.00215 0.00570  0.01775  246 GLU A N   
1887 C CA  . GLU A 246 ? 0.16181 0.14881 0.12518 -0.00340 0.00557  0.01969  246 GLU A CA  
1888 C C   . GLU A 246 ? 0.17619 0.16304 0.13806 -0.00212 0.00462  0.01848  246 GLU A C   
1889 O O   . GLU A 246 ? 0.18004 0.16975 0.13836 -0.00270 0.00524  0.01760  246 GLU A O   
1890 C CB  . GLU A 246 ? 0.18341 0.16968 0.14745 -0.00496 0.00410  0.02419  246 GLU A CB  
1891 C CG  . GLU A 246 ? 0.20451 0.19098 0.17033 -0.00663 0.00494  0.02585  246 GLU A CG  
1892 C CD  . GLU A 246 ? 0.22674 0.21236 0.19328 -0.00839 0.00337  0.03078  246 GLU A CD  
1893 O OE1 . GLU A 246 ? 0.25595 0.24177 0.22080 -0.00853 0.00173  0.03312  246 GLU A OE1 
1894 O OE2 . GLU A 246 ? 0.28960 0.27436 0.25870 -0.00973 0.00358  0.03253  246 GLU A OE2 
1895 N N   . LYS A 247 ? 0.14111 0.12477 0.10584 -0.00047 0.00322  0.01823  247 LYS A N   
1896 C CA  . LYS A 247 ? 0.17501 0.15850 0.13942 0.00089  0.00247  0.01683  247 LYS A CA  
1897 C C   . LYS A 247 ? 0.14894 0.12961 0.11619 0.00278  0.00280  0.01420  247 LYS A C   
1898 O O   . LYS A 247 ? 0.16862 0.14643 0.13908 0.00357  0.00193  0.01488  247 LYS A O   
1899 C CB  . LYS A 247 ? 0.19352 0.17668 0.15880 0.00079  0.00023  0.01996  247 LYS A CB  
1900 C CG  . LYS A 247 ? 0.18957 0.17309 0.15514 0.00203  -0.00066 0.01872  247 LYS A CG  
1901 C CD  . LYS A 247 ? 0.17446 0.16150 0.13553 0.00087  -0.00039 0.01786  247 LYS A CD  
1902 C CE  . LYS A 247 ? 0.18084 0.17036 0.13891 -0.00126 -0.00164 0.02140  247 LYS A CE  
1903 N NZ  . LYS A 247 ? 0.18756 0.18053 0.14092 -0.00254 -0.00166 0.02029  247 LYS A NZ  
1904 N N   . PRO A 248 ? 0.13293 0.11427 0.09913 0.00345  0.00408  0.01119  248 PRO A N   
1905 C CA  . PRO A 248 ? 0.14598 0.12496 0.11418 0.00492  0.00438  0.00898  248 PRO A CA  
1906 C C   . PRO A 248 ? 0.13640 0.11375 0.10650 0.00615  0.00339  0.00903  248 PRO A C   
1907 O O   . PRO A 248 ? 0.10680 0.08542 0.07652 0.00619  0.00257  0.00995  248 PRO A O   
1908 C CB  . PRO A 248 ? 0.16363 0.14409 0.13017 0.00522  0.00561  0.00647  248 PRO A CB  
1909 C CG  . PRO A 248 ? 0.16923 0.15249 0.13365 0.00388  0.00647  0.00690  248 PRO A CG  
1910 C CD  . PRO A 248 ? 0.14186 0.12606 0.10512 0.00279  0.00538  0.00967  248 PRO A CD  
1911 N N   . ALA A 249 ? 0.13056 0.10531 0.10288 0.00709  0.00350  0.00790  249 ALA A N   
1912 C CA  . ALA A 249 ? 0.12169 0.09487 0.09665 0.00834  0.00293  0.00777  249 ALA A CA  
1913 C C   . ALA A 249 ? 0.10210 0.07638 0.07656 0.00922  0.00345  0.00607  249 ALA A C   
1914 O O   . ALA A 249 ? 0.09344 0.06744 0.07033 0.01017  0.00305  0.00619  249 ALA A O   
1915 C CB  . ALA A 249 ? 0.10225 0.07236 0.07939 0.00889  0.00321  0.00653  249 ALA A CB  
1916 N N   . THR A 250 ? 0.09155 0.06706 0.06353 0.00892  0.00433  0.00459  250 THR A N   
1917 C CA  . THR A 250 ? 0.09014 0.06652 0.06177 0.00947  0.00481  0.00316  250 THR A CA  
1918 C C   . THR A 250 ? 0.09006 0.06880 0.05966 0.00867  0.00460  0.00336  250 THR A C   
1919 O O   . THR A 250 ? 0.13148 0.11145 0.09974 0.00772  0.00411  0.00467  250 THR A O   
1920 C CB  . THR A 250 ? 0.08902 0.06433 0.05989 0.00979  0.00589  0.00121  250 THR A CB  
1921 O OG1 . THR A 250 ? 0.08873 0.06432 0.05804 0.00911  0.00616  0.00102  250 THR A OG1 
1922 C CG2 . THR A 250 ? 0.08991 0.06307 0.06226 0.01041  0.00615  0.00051  250 THR A CG2 
1923 N N   . THR A 251 ? 0.09022 0.06960 0.05949 0.00888  0.00504  0.00196  251 THR A N   
1924 C CA  . THR A 251 ? 0.08946 0.07084 0.05716 0.00808  0.00473  0.00168  251 THR A CA  
1925 C C   . THR A 251 ? 0.09372 0.07563 0.05927 0.00743  0.00564  0.00055  251 THR A C   
1926 O O   . THR A 251 ? 0.09873 0.08241 0.06242 0.00648  0.00552  0.00033  251 THR A O   
1927 C CB  . THR A 251 ? 0.08860 0.07030 0.05740 0.00839  0.00482  0.00059  251 THR A CB  
1928 O OG1 . THR A 251 ? 0.08742 0.06782 0.05610 0.00876  0.00598  -0.00085 251 THR A OG1 
1929 C CG2 . THR A 251 ? 0.08847 0.07009 0.06022 0.00919  0.00428  0.00147  251 THR A CG2 
1930 N N   . VAL A 252 ? 0.08853 0.06914 0.05445 0.00788  0.00652  -0.00025 252 VAL A N   
1931 C CA  . VAL A 252 ? 0.09710 0.07827 0.06227 0.00760  0.00746  -0.00142 252 VAL A CA  
1932 C C   . VAL A 252 ? 0.08973 0.07152 0.05450 0.00743  0.00778  -0.00305 252 VAL A C   
1933 O O   . VAL A 252 ? 0.10501 0.08814 0.06868 0.00683  0.00840  -0.00414 252 VAL A O   
1934 C CB  . VAL A 252 ? 0.11700 0.09970 0.08099 0.00671  0.00775  -0.00063 252 VAL A CB  
1935 C CG1 . VAL A 252 ? 0.13454 0.11774 0.09911 0.00675  0.00894  -0.00178 252 VAL A CG1 
1936 C CG2 . VAL A 252 ? 0.14053 0.12243 0.10519 0.00659  0.00700  0.00142  252 VAL A CG2 
1937 N N   . LEU A 253 ? 0.08808 0.06893 0.05387 0.00785  0.00748  -0.00338 253 LEU A N   
1938 C CA  . LEU A 253 ? 0.08855 0.06945 0.05461 0.00760  0.00767  -0.00488 253 LEU A CA  
1939 C C   . LEU A 253 ? 0.08787 0.06714 0.05538 0.00818  0.00827  -0.00560 253 LEU A C   
1940 O O   . LEU A 253 ? 0.08847 0.06720 0.05686 0.00801  0.00839  -0.00668 253 LEU A O   
1941 C CB  . LEU A 253 ? 0.08912 0.07041 0.05587 0.00738  0.00684  -0.00448 253 LEU A CB  
1942 C CG  . LEU A 253 ? 0.09434 0.07762 0.06005 0.00659  0.00574  -0.00376 253 LEU A CG  
1943 C CD1 . LEU A 253 ? 0.10095 0.08479 0.06862 0.00665  0.00483  -0.00307 253 LEU A CD1 
1944 C CD2 . LEU A 253 ? 0.10479 0.08936 0.06845 0.00546  0.00580  -0.00537 253 LEU A CD2 
1945 N N   . SER A 254 ? 0.08705 0.06547 0.05499 0.00874  0.00845  -0.00489 254 SER A N   
1946 C CA  . SER A 254 ? 0.09053 0.06756 0.05980 0.00921  0.00858  -0.00495 254 SER A CA  
1947 C C   . SER A 254 ? 0.08766 0.06467 0.05844 0.00937  0.00909  -0.00627 254 SER A C   
1948 O O   . SER A 254 ? 0.09074 0.06642 0.06315 0.00957  0.00900  -0.00646 254 SER A O   
1949 C CB  . SER A 254 ? 0.08691 0.06340 0.05602 0.00952  0.00832  -0.00390 254 SER A CB  
1950 O OG  . SER A 254 ? 0.09035 0.06786 0.05919 0.00939  0.00843  -0.00376 254 SER A OG  
1951 N N   . PRO A 255 ? 0.09089 0.06931 0.06154 0.00927  0.00976  -0.00720 255 PRO A N   
1952 C CA  . PRO A 255 ? 0.10639 0.08485 0.07912 0.00958  0.01060  -0.00900 255 PRO A CA  
1953 C C   . PRO A 255 ? 0.09942 0.07732 0.07218 0.00913  0.01077  -0.01075 255 PRO A C   
1954 O O   . PRO A 255 ? 0.09222 0.06899 0.06759 0.00955  0.01121  -0.01216 255 PRO A O   
1955 C CB  . PRO A 255 ? 0.09499 0.07571 0.06706 0.00932  0.01164  -0.00970 255 PRO A CB  
1956 C CG  . PRO A 255 ? 0.11559 0.09683 0.08610 0.00903  0.01100  -0.00765 255 PRO A CG  
1957 C CD  . PRO A 255 ? 0.08818 0.06826 0.05722 0.00883  0.00996  -0.00664 255 PRO A CD  
1958 N N   . TYR A 256 ? 0.09403 0.07264 0.06445 0.00826  0.01027  -0.01066 256 TYR A N   
1959 C CA  . TYR A 256 ? 0.10080 0.07905 0.07126 0.00754  0.01014  -0.01236 256 TYR A CA  
1960 C C   . TYR A 256 ? 0.09805 0.07434 0.07036 0.00761  0.00941  -0.01144 256 TYR A C   
1961 O O   . TYR A 256 ? 0.10954 0.08464 0.08346 0.00721  0.00941  -0.01287 256 TYR A O   
1962 C CB  . TYR A 256 ? 0.09395 0.07428 0.06136 0.00638  0.00959  -0.01244 256 TYR A CB  
1963 C CG  . TYR A 256 ? 0.11638 0.09890 0.08139 0.00599  0.01028  -0.01267 256 TYR A CG  
1964 C CD1 . TYR A 256 ? 0.11733 0.10099 0.08138 0.00540  0.01149  -0.01532 256 TYR A CD1 
1965 C CD2 . TYR A 256 ? 0.10281 0.08623 0.06664 0.00608  0.00987  -0.01033 256 TYR A CD2 
1966 C CE1 . TYR A 256 ? 0.11081 0.09689 0.07241 0.00479  0.01240  -0.01538 256 TYR A CE1 
1967 C CE2 . TYR A 256 ? 0.13269 0.11815 0.09446 0.00546  0.01051  -0.01012 256 TYR A CE2 
1968 C CZ  . TYR A 256 ? 0.13479 0.12178 0.09526 0.00475  0.01184  -0.01253 256 TYR A CZ  
1969 O OH  . TYR A 256 ? 0.11821 0.10764 0.07638 0.00389  0.01275  -0.01219 256 TYR A OH  
1970 N N   . LEU A 257 ? 0.09913 0.07510 0.07127 0.00796  0.00892  -0.00918 257 LEU A N   
1971 C CA  . LEU A 257 ? 0.09042 0.06488 0.06404 0.00787  0.00857  -0.00808 257 LEU A CA  
1972 C C   . LEU A 257 ? 0.09787 0.07037 0.07374 0.00847  0.00864  -0.00764 257 LEU A C   
1973 O O   . LEU A 257 ? 0.10368 0.07462 0.08128 0.00813  0.00839  -0.00706 257 LEU A O   
1974 C CB  . LEU A 257 ? 0.10361 0.07867 0.07604 0.00796  0.00834  -0.00621 257 LEU A CB  
1975 C CG  . LEU A 257 ? 0.09591 0.07273 0.06747 0.00749  0.00799  -0.00613 257 LEU A CG  
1976 C CD1 . LEU A 257 ? 0.08734 0.06456 0.05835 0.00796  0.00807  -0.00469 257 LEU A CD1 
1977 C CD2 . LEU A 257 ? 0.08938 0.06637 0.06242 0.00661  0.00768  -0.00659 257 LEU A CD2 
1978 N N   . LYS A 258 ? 0.09072 0.06339 0.06699 0.00927  0.00886  -0.00764 258 LYS A N   
1979 C CA  . LYS A 258 ? 0.09156 0.06266 0.07068 0.00995  0.00861  -0.00697 258 LYS A CA  
1980 C C   . LYS A 258 ? 0.09366 0.06336 0.07595 0.01007  0.00898  -0.00891 258 LYS A C   
1981 O O   . LYS A 258 ? 0.09781 0.06538 0.08255 0.00998  0.00845  -0.00809 258 LYS A O   
1982 C CB  . LYS A 258 ? 0.09904 0.07122 0.07846 0.01073  0.00866  -0.00659 258 LYS A CB  
1983 C CG  . LYS A 258 ? 0.11073 0.08180 0.09383 0.01158  0.00811  -0.00573 258 LYS A CG  
1984 C CD  . LYS A 258 ? 0.11034 0.08172 0.09694 0.01237  0.00911  -0.00807 258 LYS A CD  
1985 C CE  . LYS A 258 ? 0.10457 0.07545 0.09575 0.01349  0.00844  -0.00701 258 LYS A CE  
1986 N NZ  . LYS A 258 ? 0.15831 0.12678 0.15111 0.01344  0.00691  -0.00457 258 LYS A NZ  
1987 N N   . PHE A 259 ? 0.09440 0.06522 0.07669 0.01016  0.00996  -0.01155 259 PHE A N   
1988 C CA  . PHE A 259 ? 0.09984 0.06932 0.08508 0.01025  0.01060  -0.01422 259 PHE A CA  
1989 C C   . PHE A 259 ? 0.09850 0.06705 0.08306 0.00898  0.01028  -0.01536 259 PHE A C   
1990 O O   . PHE A 259 ? 0.10370 0.07069 0.09076 0.00883  0.01069  -0.01784 259 PHE A O   
1991 C CB  . PHE A 259 ? 0.11344 0.08488 0.09833 0.01053  0.01210  -0.01706 259 PHE A CB  
1992 C CG  . PHE A 259 ? 0.11224 0.08443 0.09992 0.01186  0.01264  -0.01659 259 PHE A CG  
1993 C CD1 . PHE A 259 ? 0.12471 0.09508 0.11790 0.01306  0.01272  -0.01706 259 PHE A CD1 
1994 C CD2 . PHE A 259 ? 0.13044 0.10519 0.11586 0.01187  0.01294  -0.01557 259 PHE A CD2 
1995 C CE1 . PHE A 259 ? 0.11342 0.08491 0.10995 0.01433  0.01303  -0.01649 259 PHE A CE1 
1996 C CE2 . PHE A 259 ? 0.10953 0.08532 0.09801 0.01293  0.01333  -0.01510 259 PHE A CE2 
1997 C CZ  . PHE A 259 ? 0.12181 0.09619 0.11594 0.01419  0.01336  -0.01557 259 PHE A CZ  
1998 N N   . GLY A 260 ? 0.09704 0.06655 0.07879 0.00807  0.00958  -0.01380 260 GLY A N   
1999 C CA  . GLY A 260 ? 0.10299 0.07217 0.08456 0.00675  0.00911  -0.01471 260 GLY A CA  
2000 C C   . GLY A 260 ? 0.09982 0.07090 0.07895 0.00580  0.00935  -0.01746 260 GLY A C   
2001 O O   . GLY A 260 ? 0.10181 0.07249 0.08132 0.00456  0.00886  -0.01896 260 GLY A O   
2002 N N   . CYS A 261 ? 0.11218 0.08544 0.08867 0.00612  0.00999  -0.01805 261 CYS A N   
2003 C CA  . CYS A 261 ? 0.10684 0.08237 0.08006 0.00491  0.01007  -0.02015 261 CYS A CA  
2004 C C   . CYS A 261 ? 0.10541 0.08258 0.07653 0.00380  0.00861  -0.01854 261 CYS A C   
2005 O O   . CYS A 261 ? 0.11879 0.09754 0.08776 0.00240  0.00801  -0.02011 261 CYS A O   
2006 C CB  . CYS A 261 ? 0.11087 0.08859 0.08171 0.00531  0.01115  -0.02046 261 CYS A CB  
2007 S SG  . CYS A 261 ? 0.10223 0.07892 0.07646 0.00676  0.01304  -0.02242 261 CYS A SG  
2008 N N   . LEU A 262 ? 0.10207 0.07909 0.07393 0.00437  0.00802  -0.01555 262 LEU A N   
2009 C CA  . LEU A 262 ? 0.09655 0.07518 0.06776 0.00366  0.00681  -0.01392 262 LEU A CA  
2010 C C   . LEU A 262 ? 0.09541 0.07255 0.06955 0.00374  0.00663  -0.01247 262 LEU A C   
2011 O O   . LEU A 262 ? 0.10480 0.08044 0.08001 0.00471  0.00724  -0.01108 262 LEU A O   
2012 C CB  . LEU A 262 ? 0.09847 0.07884 0.06774 0.00427  0.00659  -0.01178 262 LEU A CB  
2013 C CG  . LEU A 262 ? 0.09349 0.07545 0.06323 0.00398  0.00543  -0.00989 262 LEU A CG  
2014 C CD1 . LEU A 262 ? 0.11460 0.09866 0.08335 0.00247  0.00406  -0.01080 262 LEU A CD1 
2015 C CD2 . LEU A 262 ? 0.09560 0.07835 0.06441 0.00489  0.00541  -0.00783 262 LEU A CD2 
2016 N N   . SER A 263 ? 0.09631 0.07417 0.07167 0.00253  0.00574  -0.01269 263 SER A N   
2017 C CA  . SER A 263 ? 0.09559 0.07259 0.07381 0.00228  0.00576  -0.01118 263 SER A CA  
2018 C C   . SER A 263 ? 0.09303 0.07147 0.07105 0.00308  0.00600  -0.00870 263 SER A C   
2019 O O   . SER A 263 ? 0.10649 0.08721 0.08353 0.00320  0.00539  -0.00818 263 SER A O   
2020 C CB  . SER A 263 ? 0.10331 0.08111 0.08336 0.00058  0.00474  -0.01216 263 SER A CB  
2021 O OG  . SER A 263 ? 0.09778 0.07541 0.08075 0.00015  0.00494  -0.01038 263 SER A OG  
2022 N N   . ALA A 264 ? 0.09227 0.06935 0.07127 0.00357  0.00687  -0.00718 264 ALA A N   
2023 C CA  . ALA A 264 ? 0.09058 0.06896 0.06944 0.00418  0.00742  -0.00538 264 ALA A CA  
2024 C C   . ALA A 264 ? 0.09048 0.07112 0.07173 0.00336  0.00720  -0.00486 264 ALA A C   
2025 O O   . ALA A 264 ? 0.08927 0.07184 0.07089 0.00398  0.00740  -0.00405 264 ALA A O   
2026 C CB  . ALA A 264 ? 0.09071 0.06735 0.06935 0.00453  0.00838  -0.00402 264 ALA A CB  
2027 N N   . ARG A 265 ? 0.09195 0.07241 0.07544 0.00199  0.00677  -0.00537 265 ARG A N   
2028 C CA  . ARG A 265 ? 0.10404 0.08710 0.09052 0.00103  0.00643  -0.00487 265 ARG A CA  
2029 C C   . ARG A 265 ? 0.09178 0.07738 0.07823 0.00090  0.00484  -0.00555 265 ARG A C   
2030 O O   . ARG A 265 ? 0.12461 0.11304 0.11345 0.00096  0.00454  -0.00460 265 ARG A O   
2031 C CB  . ARG A 265 ? 0.11706 0.09908 0.10621 -0.00068 0.00624  -0.00516 265 ARG A CB  
2032 C CG  . ARG A 265 ? 0.10249 0.08229 0.09209 -0.00085 0.00758  -0.00368 265 ARG A CG  
2033 C CD  . ARG A 265 ? 0.11966 0.09787 0.11226 -0.00266 0.00718  -0.00382 265 ARG A CD  
2034 N NE  . ARG A 265 ? 0.13299 0.10904 0.12603 -0.00300 0.00822  -0.00179 265 ARG A NE  
2035 C CZ  . ARG A 265 ? 0.13748 0.11137 0.13328 -0.00451 0.00798  -0.00123 265 ARG A CZ  
2036 N NH1 . ARG A 265 ? 0.12247 0.09584 0.12095 -0.00585 0.00683  -0.00301 265 ARG A NH1 
2037 N NH2 . ARG A 265 ? 0.14904 0.12114 0.14487 -0.00485 0.00877  0.00124  265 ARG A NH2 
2038 N N   . LEU A 266 ? 0.09294 0.07782 0.07686 0.00068  0.00383  -0.00711 266 LEU A N   
2039 C CA  . LEU A 266 ? 0.09344 0.08087 0.07637 0.00038  0.00216  -0.00734 266 LEU A CA  
2040 C C   . LEU A 266 ? 0.10368 0.09216 0.08565 0.00194  0.00235  -0.00573 266 LEU A C   
2041 O O   . LEU A 266 ? 0.09711 0.08823 0.08050 0.00199  0.00109  -0.00464 266 LEU A O   
2042 C CB  . LEU A 266 ? 0.10781 0.09437 0.08755 -0.00045 0.00141  -0.00957 266 LEU A CB  
2043 C CG  . LEU A 266 ? 0.13179 0.12112 0.10934 -0.00117 -0.00046 -0.00965 266 LEU A CG  
2044 C CD1 . LEU A 266 ? 0.11255 0.10475 0.09305 -0.00254 -0.00237 -0.00913 266 LEU A CD1 
2045 C CD2 . LEU A 266 ? 0.14816 0.13668 0.12181 -0.00208 -0.00057 -0.01223 266 LEU A CD2 
2046 N N   . PHE A 267 ? 0.10152 0.08792 0.08150 0.00318  0.00371  -0.00551 267 PHE A N   
2047 C CA  . PHE A 267 ? 0.10121 0.08806 0.08076 0.00458  0.00405  -0.00415 267 PHE A CA  
2048 C C   . PHE A 267 ? 0.09799 0.08639 0.08116 0.00513  0.00460  -0.00297 267 PHE A C   
2049 O O   . PHE A 267 ? 0.08997 0.08010 0.07478 0.00584  0.00391  -0.00195 267 PHE A O   
2050 C CB  . PHE A 267 ? 0.08836 0.07267 0.06557 0.00551  0.00539  -0.00430 267 PHE A CB  
2051 C CG  . PHE A 267 ? 0.08766 0.07198 0.06377 0.00664  0.00546  -0.00336 267 PHE A CG  
2052 C CD1 . PHE A 267 ? 0.09948 0.08565 0.07683 0.00692  0.00438  -0.00227 267 PHE A CD1 
2053 C CD2 . PHE A 267 ? 0.11353 0.09592 0.08779 0.00735  0.00640  -0.00342 267 PHE A CD2 
2054 C CE1 . PHE A 267 ? 0.08828 0.07397 0.06513 0.00788  0.00437  -0.00131 267 PHE A CE1 
2055 C CE2 . PHE A 267 ? 0.11288 0.09504 0.08642 0.00816  0.00639  -0.00266 267 PHE A CE2 
2056 C CZ  . PHE A 267 ? 0.11257 0.09618 0.08744 0.00843  0.00544  -0.00163 267 PHE A CZ  
2057 N N   . HIS A 268 ? 0.10236 0.09028 0.08714 0.00477  0.00590  -0.00303 268 HIS A N   
2058 C CA  . HIS A 268 ? 0.09077 0.08058 0.07905 0.00516  0.00696  -0.00221 268 HIS A CA  
2059 C C   . HIS A 268 ? 0.10412 0.09720 0.09645 0.00451  0.00556  -0.00181 268 HIS A C   
2060 O O   . HIS A 268 ? 0.10655 0.10188 0.10242 0.00537  0.00591  -0.00106 268 HIS A O   
2061 C CB  . HIS A 268 ? 0.10805 0.09685 0.09658 0.00452  0.00876  -0.00211 268 HIS A CB  
2062 C CG  . HIS A 268 ? 0.11140 0.10210 0.10253 0.00496  0.01060  -0.00153 268 HIS A CG  
2063 N ND1 . HIS A 268 ? 0.12214 0.11594 0.11791 0.00433  0.01081  -0.00116 268 HIS A ND1 
2064 C CD2 . HIS A 268 ? 0.09920 0.08937 0.08902 0.00588  0.01248  -0.00152 268 HIS A CD2 
2065 C CE1 . HIS A 268 ? 0.10341 0.09863 0.10080 0.00497  0.01302  -0.00100 268 HIS A CE1 
2066 N NE2 . HIS A 268 ? 0.12619 0.11914 0.11970 0.00587  0.01406  -0.00135 268 HIS A NE2 
2067 N N   . ALA A 269 ? 0.11147 0.10496 0.10370 0.00299  0.00392  -0.00245 269 ALA A N   
2068 C CA  . ALA A 269 ? 0.10136 0.09825 0.09740 0.00208  0.00212  -0.00202 269 ALA A CA  
2069 C C   . ALA A 269 ? 0.11089 0.10962 0.10711 0.00292  0.00025  -0.00099 269 ALA A C   
2070 O O   . ALA A 269 ? 0.09471 0.09661 0.09551 0.00315  -0.00076 0.00017  269 ALA A O   
2071 C CB  . ALA A 269 ? 0.12203 0.11862 0.11735 -0.00001 0.00068  -0.00333 269 ALA A CB  
2072 N N   . ARG A 270 ? 0.11376 0.11069 0.10544 0.00333  -0.00027 -0.00117 270 ARG A N   
2073 C CA  . ARG A 270 ? 0.11426 0.11267 0.10585 0.00396  -0.00209 0.00032  270 ARG A CA  
2074 C C   . ARG A 270 ? 0.11710 0.11549 0.11174 0.00600  -0.00096 0.00159  270 ARG A C   
2075 O O   . ARG A 270 ? 0.12872 0.12900 0.12622 0.00669  -0.00256 0.00328  270 ARG A O   
2076 C CB  . ARG A 270 ? 0.10481 0.10149 0.09067 0.00357  -0.00264 -0.00015 270 ARG A CB  
2077 C CG  . ARG A 270 ? 0.16152 0.15829 0.14421 0.00157  -0.00366 -0.00192 270 ARG A CG  
2078 C CD  . ARG A 270 ? 0.17629 0.17650 0.16005 0.00007  -0.00660 -0.00120 270 ARG A CD  
2079 N NE  . ARG A 270 ? 0.17513 0.17692 0.15784 0.00043  -0.00841 0.00107  270 ARG A NE  
2080 C CZ  . ARG A 270 ? 0.15716 0.15887 0.13460 -0.00046 -0.00923 0.00104  270 ARG A CZ  
2081 N NH1 . ARG A 270 ? 0.21522 0.21546 0.18815 -0.00157 -0.00820 -0.00157 270 ARG A NH1 
2082 N NH2 . ARG A 270 ? 0.18324 0.18645 0.16022 -0.00026 -0.01101 0.00375  270 ARG A NH2 
2083 N N   . LEU A 271 ? 0.08756 0.08380 0.08172 0.00694  0.00167  0.00077  271 LEU A N   
2084 C CA  . LEU A 271 ? 0.10297 0.09894 0.09973 0.00877  0.00304  0.00129  271 LEU A CA  
2085 C C   . LEU A 271 ? 0.11267 0.11177 0.11595 0.00928  0.00342  0.00174  271 LEU A C   
2086 O O   . LEU A 271 ? 0.12469 0.12476 0.13194 0.01078  0.00326  0.00258  271 LEU A O   
2087 C CB  . LEU A 271 ? 0.08764 0.08077 0.08147 0.00925  0.00562  0.00009  271 LEU A CB  
2088 C CG  . LEU A 271 ? 0.09306 0.08326 0.08160 0.00920  0.00551  -0.00026 271 LEU A CG  
2089 C CD1 . LEU A 271 ? 0.11800 0.10599 0.10411 0.00930  0.00765  -0.00127 271 LEU A CD1 
2090 C CD2 . LEU A 271 ? 0.10676 0.09631 0.09531 0.01026  0.00465  0.00071  271 LEU A CD2 
2091 N N   . LEU A 272 ? 0.11061 0.11134 0.11566 0.00806  0.00399  0.00122  272 LEU A N   
2092 C CA  . LEU A 272 ? 0.12845 0.13271 0.14024 0.00840  0.00462  0.00162  272 LEU A CA  
2093 C C   . LEU A 272 ? 0.12962 0.13713 0.14591 0.00842  0.00155  0.00320  272 LEU A C   
2094 O O   . LEU A 272 ? 0.12334 0.13364 0.14621 0.00964  0.00177  0.00393  272 LEU A O   
2095 C CB  . LEU A 272 ? 0.09141 0.09668 0.10405 0.00672  0.00590  0.00096  272 LEU A CB  
2096 C CG  . LEU A 272 ? 0.12918 0.13210 0.13866 0.00660  0.00901  0.00001  272 LEU A CG  
2097 C CD1 . LEU A 272 ? 0.14821 0.15250 0.15953 0.00473  0.00999  0.00001  272 LEU A CD1 
2098 C CD2 . LEU A 272 ? 0.16408 0.16725 0.17519 0.00840  0.01157  -0.00044 272 LEU A CD2 
2099 N N   . GLU A 273 ? 0.15187 0.15928 0.16485 0.00706  -0.00134 0.00374  273 GLU A N   
2100 C CA  . GLU A 273 ? 0.13907 0.14970 0.15547 0.00680  -0.00474 0.00561  273 GLU A CA  
2101 C C   . GLU A 273 ? 0.12516 0.13555 0.14390 0.00889  -0.00542 0.00733  273 GLU A C   
2102 O O   . GLU A 273 ? 0.12641 0.13991 0.15160 0.00968  -0.00715 0.00911  273 GLU A O   
2103 C CB  . GLU A 273 ? 0.15576 0.16614 0.16670 0.00467  -0.00746 0.00551  273 GLU A CB  
2104 C CG  . GLU A 273 ? 0.20965 0.22016 0.21924 0.00250  -0.00724 0.00369  273 GLU A CG  
2105 C CD  . GLU A 273 ? 0.21921 0.22941 0.22334 0.00041  -0.00970 0.00295  273 GLU A CD  
2106 O OE1 . GLU A 273 ? 0.21505 0.22487 0.21551 0.00059  -0.01119 0.00393  273 GLU A OE1 
2107 O OE2 . GLU A 273 ? 0.28566 0.29601 0.28920 -0.00154 -0.01005 0.00131  273 GLU A OE2 
2108 N N   . VAL A 274 ? 0.14545 0.15214 0.15960 0.00977  -0.00421 0.00694  274 VAL A N   
2109 C CA  . VAL A 274 ? 0.17751 0.18331 0.19403 0.01164  -0.00475 0.00851  274 VAL A CA  
2110 C C   . VAL A 274 ? 0.13528 0.14130 0.15799 0.01377  -0.00209 0.00767  274 VAL A C   
2111 O O   . VAL A 274 ? 0.15491 0.16184 0.18351 0.01545  -0.00297 0.00910  274 VAL A O   
2112 C CB  . VAL A 274 ? 0.15529 0.15719 0.16508 0.01160  -0.00435 0.00831  274 VAL A CB  
2113 C CG1 . VAL A 274 ? 0.16056 0.16127 0.17295 0.01321  -0.00529 0.01024  274 VAL A CG1 
2114 C CG2 . VAL A 274 ? 0.16028 0.16230 0.16386 0.00943  -0.00633 0.00856  274 VAL A CG2 
2115 N N   . TYR A 275 ? 0.12318 0.12846 0.14484 0.01369  0.00121  0.00536  275 TYR A N   
2116 C CA  . TYR A 275 ? 0.12064 0.12616 0.14707 0.01549  0.00426  0.00404  275 TYR A CA  
2117 C C   . TYR A 275 ? 0.13050 0.14060 0.16587 0.01617  0.00407  0.00469  275 TYR A C   
2118 O O   . TYR A 275 ? 0.10953 0.12036 0.15095 0.01821  0.00565  0.00419  275 TYR A O   
2119 C CB  . TYR A 275 ? 0.11207 0.11599 0.13418 0.01480  0.00769  0.00172  275 TYR A CB  
2120 C CG  . TYR A 275 ? 0.13105 0.13058 0.14611 0.01479  0.00845  0.00084  275 TYR A CG  
2121 C CD1 . TYR A 275 ? 0.12037 0.11763 0.13387 0.01550  0.00666  0.00185  275 TYR A CD1 
2122 C CD2 . TYR A 275 ? 0.11685 0.11470 0.12714 0.01394  0.01081  -0.00073 275 TYR A CD2 
2123 C CE1 . TYR A 275 ? 0.12274 0.11636 0.13044 0.01536  0.00733  0.00107  275 TYR A CE1 
2124 C CE2 . TYR A 275 ? 0.11804 0.11229 0.12250 0.01389  0.01123  -0.00140 275 TYR A CE2 
2125 C CZ  . TYR A 275 ? 0.11202 0.10426 0.11537 0.01461  0.00955  -0.00062 275 TYR A CZ  
2126 O OH  . TYR A 275 ? 0.10975 0.09877 0.10789 0.01444  0.00995  -0.00126 275 TYR A OH  
2127 N N   . ARG A 276 ? 0.13616 0.14946 0.17293 0.01449  0.00219  0.00562  276 ARG A N   
2128 C CA  . ARG A 276 ? 0.15002 0.16824 0.19588 0.01494  0.00170  0.00645  276 ARG A CA  
2129 C C   . ARG A 276 ? 0.15054 0.17053 0.20227 0.01628  -0.00175 0.00905  276 ARG A C   
2130 O O   . ARG A 276 ? 0.17675 0.20079 0.23758 0.01733  -0.00206 0.00985  276 ARG A O   
2131 C CB  . ARG A 276 ? 0.16010 0.18113 0.20571 0.01240  0.00053  0.00659  276 ARG A CB  
2132 C CG  . ARG A 276 ? 0.20027 0.21998 0.24184 0.01105  0.00388  0.00454  276 ARG A CG  
2133 C CD  . ARG A 276 ? 0.19214 0.21415 0.23404 0.00842  0.00249  0.00474  276 ARG A CD  
2134 N NE  . ARG A 276 ? 0.20614 0.22579 0.24301 0.00692  0.00504  0.00329  276 ARG A NE  
2135 C CZ  . ARG A 276 ? 0.21933 0.23997 0.25614 0.00453  0.00455  0.00314  276 ARG A CZ  
2136 N NH1 . ARG A 276 ? 0.23240 0.25655 0.27366 0.00318  0.00167  0.00404  276 ARG A NH1 
2137 N NH2 . ARG A 276 ? 0.22652 0.24448 0.25892 0.00335  0.00679  0.00219  276 ARG A NH2 
2138 N N   . ARG A 277 ? 0.14025 0.15752 0.18735 0.01621  -0.00435 0.01062  277 ARG A N   
2139 C CA  . ARG A 277 ? 0.15142 0.16981 0.20356 0.01742  -0.00776 0.01365  277 ARG A CA  
2140 C C   . ARG A 277 ? 0.14182 0.15659 0.19536 0.01982  -0.00648 0.01362  277 ARG A C   
2141 O O   . ARG A 277 ? 0.11447 0.12967 0.17322 0.02112  -0.00912 0.01632  277 ARG A O   
2142 C CB  . ARG A 277 ? 0.14620 0.16469 0.19247 0.01527  -0.01203 0.01601  277 ARG A CB  
2143 C CG  . ARG A 277 ? 0.15264 0.17481 0.19821 0.01276  -0.01394 0.01601  277 ARG A CG  
2144 C CD  . ARG A 277 ? 0.15514 0.17765 0.19455 0.01050  -0.01807 0.01796  277 ARG A CD  
2145 N NE  . ARG A 277 ? 0.15411 0.18027 0.19358 0.00803  -0.02017 0.01770  277 ARG A NE  
2146 C CZ  . ARG A 277 ? 0.15656 0.18389 0.19077 0.00556  -0.02372 0.01873  277 ARG A CZ  
2147 N NH1 . ARG A 277 ? 0.15933 0.18478 0.18752 0.00513  -0.02546 0.02034  277 ARG A NH1 
2148 N NH2 . ARG A 277 ? 0.15531 0.18587 0.19022 0.00327  -0.02548 0.01802  277 ARG A NH2 
2149 N N   . HIS A 278 ? 0.17186 0.18301 0.22103 0.02030  -0.00274 0.01076  278 HIS A N   
2150 C CA  . HIS A 278 ? 0.15122 0.15865 0.20161 0.02238  -0.00118 0.01003  278 HIS A CA  
2151 C C   . HIS A 278 ? 0.16531 0.17249 0.21765 0.02351  0.00360  0.00635  278 HIS A C   
2152 O O   . HIS A 278 ? 0.14140 0.14614 0.18671 0.02258  0.00614  0.00403  278 HIS A O   
2153 C CB  . HIS A 278 ? 0.12672 0.12968 0.16824 0.02137  -0.00182 0.01029  278 HIS A CB  
2154 C CG  . HIS A 278 ? 0.15720 0.16063 0.19598 0.02001  -0.00611 0.01379  278 HIS A CG  
2155 N ND1 . HIS A 278 ? 0.19459 0.19684 0.23640 0.02096  -0.00869 0.01677  278 HIS A ND1 
2156 C CD2 . HIS A 278 ? 0.14608 0.15107 0.17921 0.01762  -0.00820 0.01474  278 HIS A CD2 
2157 C CE1 . HIS A 278 ? 0.20735 0.21074 0.24496 0.01906  -0.01217 0.01963  278 HIS A CE1 
2158 N NE2 . HIS A 278 ? 0.18721 0.19229 0.21944 0.01704  -0.01185 0.01817  278 HIS A NE2 
2159 N N   . PRO A 279 ? 0.12394 0.13387 0.18586 0.02547  0.00495  0.00575  279 PRO A N   
2160 C CA  . PRO A 279 ? 0.14081 0.15140 0.20438 0.02623  0.00986  0.00206  279 PRO A CA  
2161 C C   . PRO A 279 ? 0.12025 0.12609 0.17986 0.02717  0.01269  -0.00073 279 PRO A C   
2162 O O   . PRO A 279 ? 0.10828 0.11410 0.16530 0.02687  0.01665  -0.00389 279 PRO A O   
2163 C CB  . PRO A 279 ? 0.11656 0.13139 0.19247 0.02836  0.01027  0.00232  279 PRO A CB  
2164 C CG  . PRO A 279 ? 0.15408 0.16833 0.23477 0.02953  0.00579  0.00588  279 PRO A CG  
2165 C CD  . PRO A 279 ? 0.11716 0.13005 0.18907 0.02704  0.00207  0.00850  279 PRO A CD  
2166 N N   . ALA A 280 ? 0.14760 0.14956 0.20656 0.02806  0.01072  0.00040  280 ALA A N   
2167 C CA  . ALA A 280 ? 0.14550 0.14277 0.20084 0.02871  0.01298  -0.00225 280 ALA A CA  
2168 C C   . ALA A 280 ? 0.11885 0.11291 0.16314 0.02655  0.01247  -0.00227 280 ALA A C   
2169 O O   . ALA A 280 ? 0.11342 0.10328 0.15454 0.02679  0.01272  -0.00319 280 ALA A O   
2170 C CB  . ALA A 280 ? 0.11826 0.11279 0.17993 0.03084  0.01130  -0.00110 280 ALA A CB  
2171 N N   . HIS A 281 ? 0.13883 0.13476 0.17777 0.02447  0.01176  -0.00137 281 HIS A N   
2172 C CA  . HIS A 281 ? 0.11830 0.11149 0.14771 0.02259  0.01128  -0.00136 281 HIS A CA  
2173 C C   . HIS A 281 ? 0.11154 0.10244 0.13631 0.02239  0.01472  -0.00468 281 HIS A C   
2174 O O   . HIS A 281 ? 0.12084 0.11326 0.14811 0.02299  0.01786  -0.00709 281 HIS A O   
2175 C CB  . HIS A 281 ? 0.13081 0.12646 0.15659 0.02056  0.01002  -0.00009 281 HIS A CB  
2176 C CG  . HIS A 281 ? 0.12924 0.12776 0.15600 0.01996  0.01267  -0.00171 281 HIS A CG  
2177 N ND1 . HIS A 281 ? 0.13754 0.13482 0.15871 0.01895  0.01538  -0.00376 281 HIS A ND1 
2178 C CD2 . HIS A 281 ? 0.13554 0.13834 0.16840 0.02004  0.01293  -0.00130 281 HIS A CD2 
2179 C CE1 . HIS A 281 ? 0.12972 0.13025 0.15322 0.01836  0.01733  -0.00442 281 HIS A CE1 
2180 N NE2 . HIS A 281 ? 0.12418 0.12815 0.15493 0.01901  0.01600  -0.00309 281 HIS A NE2 
2181 N N   . SER A 282 ? 0.12368 0.11122 0.14157 0.02139  0.01411  -0.00475 282 SER A N   
2182 C CA  . SER A 282 ? 0.13724 0.12256 0.15015 0.02094  0.01672  -0.00757 282 SER A CA  
2183 C C   . SER A 282 ? 0.12241 0.10986 0.13156 0.01949  0.01864  -0.00845 282 SER A C   
2184 O O   . SER A 282 ? 0.12773 0.11721 0.13611 0.01840  0.01741  -0.00672 282 SER A O   
2185 C CB  . SER A 282 ? 0.15345 0.13514 0.16054 0.02008  0.01519  -0.00701 282 SER A CB  
2186 O OG  . SER A 282 ? 0.13311 0.11545 0.13635 0.01866  0.01305  -0.00476 282 SER A OG  
2187 N N   . GLN A 283 ? 0.11471 0.10163 0.12143 0.01931  0.02162  -0.01115 283 GLN A N   
2188 C CA  . GLN A 283 ? 0.12272 0.11148 0.12563 0.01779  0.02370  -0.01184 283 GLN A CA  
2189 C C   . GLN A 283 ? 0.16205 0.14813 0.15687 0.01630  0.02351  -0.01217 283 GLN A C   
2190 O O   . GLN A 283 ? 0.14532 0.12833 0.13794 0.01659  0.02252  -0.01272 283 GLN A O   
2191 C CB  . GLN A 283 ? 0.16159 0.15252 0.16754 0.01843  0.02748  -0.01457 283 GLN A CB  
2192 C CG  . GLN A 283 ? 0.17189 0.16574 0.18716 0.02022  0.02792  -0.01452 283 GLN A CG  
2193 C CD  . GLN A 283 ? 0.16515 0.16254 0.18347 0.01949  0.02654  -0.01194 283 GLN A CD  
2194 O OE1 . GLN A 283 ? 0.18677 0.18492 0.20062 0.01756  0.02649  -0.01093 283 GLN A OE1 
2195 N NE2 . GLN A 283 ? 0.18431 0.18385 0.21064 0.02095  0.02522  -0.01079 283 GLN A NE2 
2196 N N   . PRO A 284 ? 0.15918 0.14637 0.14990 0.01463  0.02421  -0.01158 284 PRO A N   
2197 C CA  . PRO A 284 ? 0.14036 0.12533 0.12397 0.01325  0.02394  -0.01167 284 PRO A CA  
2198 C C   . PRO A 284 ? 0.16044 0.14413 0.14148 0.01335  0.02596  -0.01447 284 PRO A C   
2199 O O   . PRO A 284 ? 0.16013 0.14526 0.14429 0.01416  0.02851  -0.01666 284 PRO A O   
2200 C CB  . PRO A 284 ? 0.14167 0.12858 0.12303 0.01158  0.02474  -0.01040 284 PRO A CB  
2201 C CG  . PRO A 284 ? 0.14570 0.13505 0.13252 0.01191  0.02408  -0.00903 284 PRO A CG  
2202 C CD  . PRO A 284 ? 0.13457 0.12499 0.12742 0.01379  0.02475  -0.01029 284 PRO A CD  
2203 N N   . PRO A 285 ? 0.14879 0.12995 0.12435 0.01248  0.02494  -0.01470 285 PRO A N   
2204 C CA  . PRO A 285 ? 0.16545 0.14508 0.13756 0.01158  0.02229  -0.01248 285 PRO A CA  
2205 C C   . PRO A 285 ? 0.14753 0.12511 0.12162 0.01253  0.01988  -0.01168 285 PRO A C   
2206 O O   . PRO A 285 ? 0.15085 0.12734 0.12258 0.01192  0.01794  -0.01016 285 PRO A O   
2207 C CB  . PRO A 285 ? 0.16441 0.14293 0.13034 0.01018  0.02273  -0.01345 285 PRO A CB  
2208 C CG  . PRO A 285 ? 0.12701 0.10478 0.09347 0.01083  0.02456  -0.01670 285 PRO A CG  
2209 C CD  . PRO A 285 ? 0.14601 0.12598 0.11829 0.01215  0.02666  -0.01763 285 PRO A CD  
2210 N N   . VAL A 286 ? 0.14470 0.12183 0.12343 0.01399  0.02000  -0.01254 286 VAL A N   
2211 C CA  . VAL A 286 ? 0.14801 0.12313 0.12837 0.01463  0.01776  -0.01146 286 VAL A CA  
2212 C C   . VAL A 286 ? 0.13460 0.11112 0.11824 0.01507  0.01600  -0.00899 286 VAL A C   
2213 O O   . VAL A 286 ? 0.13224 0.10755 0.11625 0.01517  0.01402  -0.00755 286 VAL A O   
2214 C CB  . VAL A 286 ? 0.13851 0.11177 0.12229 0.01587  0.01840  -0.01337 286 VAL A CB  
2215 C CG1 . VAL A 286 ? 0.14175 0.11335 0.12161 0.01515  0.01988  -0.01623 286 VAL A CG1 
2216 C CG2 . VAL A 286 ? 0.14657 0.12175 0.13648 0.01735  0.01984  -0.01403 286 VAL A CG2 
2217 N N   . SER A 287 ? 0.12575 0.10498 0.11161 0.01509  0.01663  -0.00844 287 SER A N   
2218 C CA  . SER A 287 ? 0.12990 0.11072 0.11875 0.01527  0.01478  -0.00632 287 SER A CA  
2219 C C   . SER A 287 ? 0.09982 0.08035 0.08468 0.01400  0.01316  -0.00489 287 SER A C   
2220 O O   . SER A 287 ? 0.09042 0.06987 0.07104 0.01310  0.01358  -0.00532 287 SER A O   
2221 C CB  . SER A 287 ? 0.09721 0.08123 0.09009 0.01549  0.01587  -0.00633 287 SER A CB  
2222 O OG  . SER A 287 ? 0.09166 0.07669 0.08150 0.01421  0.01724  -0.00668 287 SER A OG  
2223 N N   . LEU A 288 ? 0.09206 0.07367 0.07851 0.01391  0.01125  -0.00322 288 LEU A N   
2224 C CA  . LEU A 288 ? 0.09708 0.07872 0.08027 0.01274  0.01002  -0.00238 288 LEU A CA  
2225 C C   . LEU A 288 ? 0.08729 0.07001 0.06954 0.01183  0.01094  -0.00278 288 LEU A C   
2226 O O   . LEU A 288 ? 0.08702 0.06874 0.06605 0.01098  0.01080  -0.00281 288 LEU A O   
2227 C CB  . LEU A 288 ? 0.12341 0.10635 0.10808 0.01258  0.00788  -0.00078 288 LEU A CB  
2228 C CG  . LEU A 288 ? 0.09483 0.07654 0.07654 0.01210  0.00656  0.00007  288 LEU A CG  
2229 C CD1 . LEU A 288 ? 0.14353 0.12712 0.12568 0.01147  0.00455  0.00160  288 LEU A CD1 
2230 C CD2 . LEU A 288 ? 0.08688 0.06739 0.06457 0.01132  0.00720  -0.00081 288 LEU A CD2 
2231 N N   . ARG A 289 ? 0.08745 0.07227 0.07308 0.01197  0.01189  -0.00296 289 ARG A N   
2232 C CA  . ARG A 289 ? 0.08758 0.07335 0.07263 0.01092  0.01303  -0.00314 289 ARG A CA  
2233 C C   . ARG A 289 ? 0.08893 0.07316 0.07036 0.01056  0.01470  -0.00390 289 ARG A C   
2234 O O   . ARG A 289 ? 0.08926 0.07300 0.06837 0.00945  0.01487  -0.00346 289 ARG A O   
2235 C CB  . ARG A 289 ? 0.11197 0.10074 0.10192 0.01109  0.01397  -0.00315 289 ARG A CB  
2236 C CG  . ARG A 289 ? 0.09038 0.08033 0.08013 0.00983  0.01557  -0.00317 289 ARG A CG  
2237 C CD  . ARG A 289 ? 0.09545 0.08891 0.09076 0.00995  0.01667  -0.00317 289 ARG A CD  
2238 N NE  . ARG A 289 ? 0.10721 0.10195 0.10234 0.00850  0.01846  -0.00297 289 ARG A NE  
2239 C CZ  . ARG A 289 ? 0.10222 0.09773 0.09654 0.00834  0.02128  -0.00370 289 ARG A CZ  
2240 N NH1 . ARG A 289 ? 0.14671 0.14175 0.14049 0.00963  0.02273  -0.00519 289 ARG A NH1 
2241 N NH2 . ARG A 289 ? 0.12134 0.11812 0.11530 0.00669  0.02271  -0.00298 289 ARG A NH2 
2242 N N   . GLY A 290 ? 0.09021 0.07357 0.07117 0.01138  0.01577  -0.00499 290 GLY A N   
2243 C CA  . GLY A 290 ? 0.09218 0.07424 0.06905 0.01080  0.01705  -0.00580 290 GLY A CA  
2244 C C   . GLY A 290 ? 0.09177 0.07171 0.06474 0.01018  0.01556  -0.00509 290 GLY A C   
2245 O O   . GLY A 290 ? 0.10005 0.07938 0.06973 0.00926  0.01598  -0.00489 290 GLY A O   
2246 N N   . GLN A 291 ? 0.09011 0.06918 0.06357 0.01062  0.01379  -0.00456 291 GLN A N   
2247 C CA  . GLN A 291 ? 0.08966 0.06719 0.06031 0.01015  0.01258  -0.00402 291 GLN A CA  
2248 C C   . GLN A 291 ? 0.08925 0.06703 0.05937 0.00928  0.01225  -0.00316 291 GLN A C   
2249 O O   . GLN A 291 ? 0.08993 0.06659 0.05785 0.00877  0.01191  -0.00272 291 GLN A O   
2250 C CB  . GLN A 291 ? 0.08936 0.06640 0.06079 0.01064  0.01115  -0.00366 291 GLN A CB  
2251 C CG  . GLN A 291 ? 0.08914 0.06551 0.06189 0.01146  0.01122  -0.00415 291 GLN A CG  
2252 C CD  . GLN A 291 ? 0.09110 0.06602 0.06181 0.01138  0.01209  -0.00537 291 GLN A CD  
2253 O OE1 . GLN A 291 ? 0.13432 0.10917 0.10620 0.01188  0.01331  -0.00661 291 GLN A OE1 
2254 N NE2 . GLN A 291 ? 0.09592 0.06985 0.06379 0.01071  0.01145  -0.00518 291 GLN A NE2 
2255 N N   . LEU A 292 ? 0.08846 0.06763 0.06101 0.00906  0.01217  -0.00287 292 LEU A N   
2256 C CA  . LEU A 292 ? 0.08866 0.06775 0.06130 0.00811  0.01198  -0.00226 292 LEU A CA  
2257 C C   . LEU A 292 ? 0.09055 0.06968 0.06204 0.00731  0.01327  -0.00169 292 LEU A C   
2258 O O   . LEU A 292 ? 0.09145 0.06958 0.06216 0.00650  0.01293  -0.00075 292 LEU A O   
2259 C CB  . LEU A 292 ? 0.08786 0.06857 0.06349 0.00779  0.01149  -0.00226 292 LEU A CB  
2260 C CG  . LEU A 292 ? 0.08686 0.06777 0.06286 0.00804  0.00996  -0.00258 292 LEU A CG  
2261 C CD1 . LEU A 292 ? 0.09917 0.08198 0.07786 0.00738  0.00925  -0.00260 292 LEU A CD1 
2262 C CD2 . LEU A 292 ? 0.08697 0.06617 0.06097 0.00783  0.00932  -0.00286 292 LEU A CD2 
2263 N N   . LEU A 293 ? 0.09165 0.07195 0.06311 0.00747  0.01482  -0.00221 293 LEU A N   
2264 C CA  . LEU A 293 ? 0.09422 0.07496 0.06375 0.00643  0.01631  -0.00168 293 LEU A CA  
2265 C C   . LEU A 293 ? 0.09599 0.07501 0.06132 0.00609  0.01582  -0.00133 293 LEU A C   
2266 O O   . LEU A 293 ? 0.10513 0.08386 0.06837 0.00490  0.01592  0.00007  293 LEU A O   
2267 C CB  . LEU A 293 ? 0.09539 0.07824 0.06619 0.00669  0.01849  -0.00283 293 LEU A CB  
2268 C CG  . LEU A 293 ? 0.09404 0.07930 0.06975 0.00687  0.01902  -0.00286 293 LEU A CG  
2269 C CD1 . LEU A 293 ? 0.09555 0.08314 0.07314 0.00729  0.02152  -0.00415 293 LEU A CD1 
2270 C CD2 . LEU A 293 ? 0.13515 0.12092 0.11185 0.00540  0.01879  -0.00131 293 LEU A CD2 
2271 N N   . TRP A 294 ? 0.09538 0.07332 0.05963 0.00696  0.01508  -0.00234 294 TRP A N   
2272 C CA  . TRP A 294 ? 0.10259 0.07908 0.06346 0.00656  0.01409  -0.00192 294 TRP A CA  
2273 C C   . TRP A 294 ? 0.09625 0.07169 0.05746 0.00619  0.01251  -0.00021 294 TRP A C   
2274 O O   . TRP A 294 ? 0.09843 0.07328 0.05742 0.00536  0.01187  0.00114  294 TRP A O   
2275 C CB  . TRP A 294 ? 0.10511 0.08065 0.06579 0.00747  0.01336  -0.00319 294 TRP A CB  
2276 C CG  . TRP A 294 ? 0.11363 0.08939 0.07347 0.00771  0.01474  -0.00504 294 TRP A CG  
2277 C CD1 . TRP A 294 ? 0.12339 0.09937 0.08608 0.00880  0.01540  -0.00635 294 TRP A CD1 
2278 C CD2 . TRP A 294 ? 0.13975 0.11546 0.09578 0.00680  0.01560  -0.00592 294 TRP A CD2 
2279 N NE1 . TRP A 294 ? 0.14155 0.11736 0.10301 0.00882  0.01682  -0.00828 294 TRP A NE1 
2280 C CE2 . TRP A 294 ? 0.14910 0.12483 0.10607 0.00749  0.01705  -0.00826 294 TRP A CE2 
2281 C CE3 . TRP A 294 ? 0.12662 0.10232 0.07853 0.00538  0.01516  -0.00490 294 TRP A CE3 
2282 C CZ2 . TRP A 294 ? 0.19237 0.16807 0.14599 0.00676  0.01835  -0.01018 294 TRP A CZ2 
2283 C CZ3 . TRP A 294 ? 0.16687 0.14283 0.11489 0.00446  0.01621  -0.00641 294 TRP A CZ3 
2284 C CH2 . TRP A 294 ? 0.16845 0.14439 0.11719 0.00513  0.01793  -0.00930 294 TRP A CH2 
2285 N N   . ARG A 295 ? 0.09376 0.06901 0.05786 0.00678  0.01181  -0.00029 295 ARG A N   
2286 C CA  . ARG A 295 ? 0.09357 0.06774 0.05884 0.00655  0.01065  0.00081  295 ARG A CA  
2287 C C   . ARG A 295 ? 0.09557 0.06970 0.06116 0.00540  0.01107  0.00235  295 ARG A C   
2288 O O   . ARG A 295 ? 0.09724 0.07015 0.06254 0.00490  0.01016  0.00396  295 ARG A O   
2289 C CB  . ARG A 295 ? 0.09126 0.06548 0.05912 0.00719  0.01016  -0.00017 295 ARG A CB  
2290 C CG  . ARG A 295 ? 0.09148 0.06450 0.06117 0.00703  0.00933  0.00021  295 ARG A CG  
2291 C CD  . ARG A 295 ? 0.09094 0.06435 0.06230 0.00744  0.00906  -0.00129 295 ARG A CD  
2292 N NE  . ARG A 295 ? 0.09072 0.06286 0.06410 0.00729  0.00857  -0.00161 295 ARG A NE  
2293 C CZ  . ARG A 295 ? 0.09463 0.06635 0.06992 0.00653  0.00860  -0.00175 295 ARG A CZ  
2294 N NH1 . ARG A 295 ? 0.09169 0.06457 0.06725 0.00578  0.00909  -0.00136 295 ARG A NH1 
2295 N NH2 . ARG A 295 ? 0.10915 0.07927 0.08659 0.00649  0.00818  -0.00243 295 ARG A NH2 
2296 N N   . GLU A 296 ? 0.09566 0.07123 0.06233 0.00492  0.01239  0.00210  296 GLU A N   
2297 C CA  . GLU A 296 ? 0.09782 0.07363 0.06503 0.00355  0.01300  0.00375  296 GLU A CA  
2298 C C   . GLU A 296 ? 0.10692 0.08302 0.07040 0.00249  0.01365  0.00520  296 GLU A C   
2299 O O   . GLU A 296 ? 0.11217 0.08764 0.07526 0.00122  0.01335  0.00747  296 GLU A O   
2300 C CB  . GLU A 296 ? 0.09704 0.07490 0.06685 0.00323  0.01434  0.00306  296 GLU A CB  
2301 C CG  . GLU A 296 ? 0.12611 0.10428 0.09764 0.00163  0.01486  0.00476  296 GLU A CG  
2302 C CD  . GLU A 296 ? 0.09835 0.07468 0.07293 0.00142  0.01333  0.00499  296 GLU A CD  
2303 O OE1 . GLU A 296 ? 0.09620 0.07178 0.07167 0.00251  0.01224  0.00339  296 GLU A OE1 
2304 O OE2 . GLU A 296 ? 0.10047 0.07606 0.07655 0.00003  0.01331  0.00668  296 GLU A OE2 
2305 N N   . PHE A 297 ? 0.10187 0.07883 0.06246 0.00283  0.01444  0.00394  297 PHE A N   
2306 C CA  . PHE A 297 ? 0.11789 0.09543 0.07407 0.00157  0.01512  0.00488  297 PHE A CA  
2307 C C   . PHE A 297 ? 0.11853 0.09439 0.07260 0.00116  0.01291  0.00679  297 PHE A C   
2308 O O   . PHE A 297 ? 0.11139 0.08734 0.06296 -0.00038 0.01263  0.00918  297 PHE A O   
2309 C CB  . PHE A 297 ? 0.12294 0.10161 0.07691 0.00205  0.01658  0.00238  297 PHE A CB  
2310 C CG  . PHE A 297 ? 0.13998 0.11909 0.08850 0.00072  0.01697  0.00266  297 PHE A CG  
2311 C CD1 . PHE A 297 ? 0.14482 0.12547 0.09067 -0.00113 0.01843  0.00415  297 PHE A CD1 
2312 C CD2 . PHE A 297 ? 0.13784 0.11601 0.08370 0.00105  0.01587  0.00143  297 PHE A CD2 
2313 C CE1 . PHE A 297 ? 0.19741 0.17875 0.13741 -0.00265 0.01874  0.00437  297 PHE A CE1 
2314 C CE2 . PHE A 297 ? 0.15508 0.13379 0.09547 -0.00044 0.01601  0.00146  297 PHE A CE2 
2315 C CZ  . PHE A 297 ? 0.16844 0.14880 0.10559 -0.00231 0.01743  0.00290  297 PHE A CZ  
2316 N N   . PHE A 298 ? 0.10647 0.08104 0.06176 0.00243  0.01126  0.00602  298 PHE A N   
2317 C CA  . PHE A 298 ? 0.10658 0.07991 0.06097 0.00225  0.00905  0.00781  298 PHE A CA  
2318 C C   . PHE A 298 ? 0.11116 0.08312 0.06873 0.00203  0.00787  0.01019  298 PHE A C   
2319 O O   . PHE A 298 ? 0.11266 0.08386 0.06951 0.00136  0.00620  0.01273  298 PHE A O   
2320 C CB  . PHE A 298 ? 0.10389 0.07666 0.05936 0.00361  0.00792  0.00622  298 PHE A CB  
2321 C CG  . PHE A 298 ? 0.10443 0.07794 0.05692 0.00363  0.00859  0.00420  298 PHE A CG  
2322 C CD1 . PHE A 298 ? 0.12433 0.09876 0.07242 0.00231  0.00947  0.00413  298 PHE A CD1 
2323 C CD2 . PHE A 298 ? 0.10430 0.07752 0.05837 0.00482  0.00841  0.00230  298 PHE A CD2 
2324 C CE1 . PHE A 298 ? 0.13139 0.10615 0.07701 0.00231  0.01017  0.00177  298 PHE A CE1 
2325 C CE2 . PHE A 298 ? 0.10252 0.07594 0.05445 0.00480  0.00893  0.00043  298 PHE A CE2 
2326 C CZ  . PHE A 298 ? 0.11678 0.09081 0.06464 0.00361  0.00981  -0.00006 298 PHE A CZ  
2327 N N   . TYR A 299 ? 0.10467 0.07621 0.06600 0.00252  0.00854  0.00944  299 TYR A N   
2328 C CA  . TYR A 299 ? 0.12317 0.09304 0.08786 0.00216  0.00763  0.01133  299 TYR A CA  
2329 C C   . TYR A 299 ? 0.11683 0.08698 0.07997 0.00023  0.00810  0.01416  299 TYR A C   
2330 O O   . TYR A 299 ? 0.12507 0.09359 0.08966 -0.00043 0.00669  0.01698  299 TYR A O   
2331 C CB  . TYR A 299 ? 0.10283 0.07231 0.07148 0.00286  0.00822  0.00938  299 TYR A CB  
2332 C CG  . TYR A 299 ? 0.10808 0.07620 0.07969 0.00430  0.00711  0.00797  299 TYR A CG  
2333 C CD1 . TYR A 299 ? 0.11605 0.08508 0.08695 0.00547  0.00725  0.00576  299 TYR A CD1 
2334 C CD2 . TYR A 299 ? 0.13312 0.09908 0.10851 0.00442  0.00609  0.00881  299 TYR A CD2 
2335 C CE1 . TYR A 299 ? 0.13892 0.10720 0.11231 0.00659  0.00662  0.00443  299 TYR A CE1 
2336 C CE2 . TYR A 299 ? 0.15124 0.11626 0.12951 0.00576  0.00551  0.00707  299 TYR A CE2 
2337 C CZ  . TYR A 299 ? 0.12085 0.08728 0.09787 0.00678  0.00589  0.00488  299 TYR A CZ  
2338 O OH  . TYR A 299 ? 0.11056 0.07653 0.09022 0.00793  0.00567  0.00312  299 TYR A OH  
2339 N N   . THR A 300 ? 0.11398 0.08627 0.07450 -0.00071 0.01016  0.01356  300 THR A N   
2340 C CA  . THR A 300 ? 0.13380 0.10695 0.09255 -0.00282 0.01107  0.01623  300 THR A CA  
2341 C C   . THR A 300 ? 0.15126 0.12447 0.10533 -0.00403 0.00990  0.01886  300 THR A C   
2342 O O   . THR A 300 ? 0.13874 0.11127 0.09249 -0.00561 0.00906  0.02247  300 THR A O   
2343 C CB  . THR A 300 ? 0.12581 0.10179 0.08337 -0.00340 0.01394  0.01450  300 THR A CB  
2344 O OG1 . THR A 300 ? 0.12466 0.10083 0.08673 -0.00226 0.01452  0.01225  300 THR A OG1 
2345 C CG2 . THR A 300 ? 0.15253 0.12980 0.10883 -0.00577 0.01528  0.01727  300 THR A CG2 
2346 N N   . VAL A 301 ? 0.16619 0.14019 0.11663 -0.00347 0.00960  0.01727  301 VAL A N   
2347 C CA  . VAL A 301 ? 0.15859 0.13298 0.10411 -0.00483 0.00817  0.01954  301 VAL A CA  
2348 C C   . VAL A 301 ? 0.15540 0.12762 0.10363 -0.00426 0.00489  0.02216  301 VAL A C   
2349 O O   . VAL A 301 ? 0.18024 0.15216 0.12685 -0.00576 0.00321  0.02601  301 VAL A O   
2350 C CB  . VAL A 301 ? 0.16229 0.13811 0.10336 -0.00458 0.00883  0.01660  301 VAL A CB  
2351 C CG1 . VAL A 301 ? 0.14173 0.11823 0.07712 -0.00634 0.00714  0.01878  301 VAL A CG1 
2352 C CG2 . VAL A 301 ? 0.16680 0.14466 0.10635 -0.00483 0.01223  0.01380  301 VAL A CG2 
2353 N N   . GLY A 302 ? 0.15414 0.12501 0.10678 -0.00213 0.00397  0.02024  302 GLY A N   
2354 C CA  . GLY A 302 ? 0.16153 0.13075 0.11748 -0.00130 0.00113  0.02219  302 GLY A CA  
2355 C C   . GLY A 302 ? 0.16785 0.13501 0.12801 -0.00171 0.00006  0.02544  302 GLY A C   
2356 O O   . GLY A 302 ? 0.19786 0.16403 0.15922 -0.00200 -0.00247 0.02880  302 GLY A O   
2357 N N   . SER A 303 ? 0.16940 0.13582 0.13228 -0.00179 0.00177  0.02459  303 SER A N   
2358 C CA  . SER A 303 ? 0.19725 0.16125 0.16471 -0.00229 0.00083  0.02737  303 SER A CA  
2359 C C   . SER A 303 ? 0.19665 0.16094 0.16101 -0.00478 0.00020  0.03205  303 SER A C   
2360 O O   . SER A 303 ? 0.22268 0.18463 0.19083 -0.00531 -0.00140 0.03546  303 SER A O   
2361 C CB  . SER A 303 ? 0.20558 0.16892 0.17654 -0.00207 0.00273  0.02502  303 SER A CB  
2362 O OG  . SER A 303 ? 0.23985 0.20564 0.20719 -0.00341 0.00512  0.02420  303 SER A OG  
2363 N N   . THR A 304 ? 0.18247 0.14953 0.14012 -0.00639 0.00146  0.03230  304 THR A N   
2364 C CA  . THR A 304 ? 0.17876 0.14675 0.13221 -0.00914 0.00120  0.03667  304 THR A CA  
2365 C C   . THR A 304 ? 0.20464 0.17406 0.15238 -0.01004 -0.00078 0.03859  304 THR A C   
2366 O O   . THR A 304 ? 0.21790 0.18869 0.16058 -0.01262 -0.00100 0.04211  304 THR A O   
2367 C CB  . THR A 304 ? 0.20008 0.17062 0.15009 -0.01081 0.00469  0.03550  304 THR A CB  
2368 O OG1 . THR A 304 ? 0.21307 0.18600 0.15915 -0.01003 0.00656  0.03125  304 THR A OG1 
2369 C CG2 . THR A 304 ? 0.22724 0.19658 0.18320 -0.01037 0.00617  0.03427  304 THR A CG2 
2370 N N   . THR A 305 ? 0.19064 0.15999 0.13891 -0.00823 -0.00227 0.03643  305 THR A N   
2371 C CA  . THR A 305 ? 0.23985 0.21066 0.18317 -0.00912 -0.00452 0.03795  305 THR A CA  
2372 C C   . THR A 305 ? 0.20699 0.17595 0.15564 -0.00781 -0.00830 0.04058  305 THR A C   
2373 O O   . THR A 305 ? 0.22955 0.19737 0.18366 -0.00530 -0.00856 0.03787  305 THR A O   
2374 C CB  . THR A 305 ? 0.20622 0.17888 0.14574 -0.00838 -0.00316 0.03320  305 THR A CB  
2375 O OG1 . THR A 305 ? 0.17197 0.14630 0.10772 -0.00928 0.00049  0.03057  305 THR A OG1 
2376 C CG2 . THR A 305 ? 0.20739 0.18165 0.14138 -0.00972 -0.00558 0.03455  305 THR A CG2 
2377 N N   . PRO A 306 ? 0.21968 0.18849 0.16728 -0.00941 -0.01124 0.04587  306 PRO A N   
2378 C CA  . PRO A 306 ? 0.26070 0.22792 0.21452 -0.00795 -0.01500 0.04857  306 PRO A CA  
2379 C C   . PRO A 306 ? 0.23489 0.20391 0.18755 -0.00698 -0.01669 0.04654  306 PRO A C   
2380 O O   . PRO A 306 ? 0.26753 0.23903 0.21275 -0.00852 -0.01637 0.04527  306 PRO A O   
2381 C CB  . PRO A 306 ? 0.25763 0.22471 0.20946 -0.01041 -0.01776 0.05525  306 PRO A CB  
2382 C CG  . PRO A 306 ? 0.27873 0.24867 0.22040 -0.01345 -0.01587 0.05534  306 PRO A CG  
2383 C CD  . PRO A 306 ? 0.23829 0.20862 0.17914 -0.01271 -0.01128 0.04986  306 PRO A CD  
2384 N N   . ASN A 307 ? 0.23411 0.20187 0.19457 -0.00446 -0.01837 0.04604  307 ASN A N   
2385 C CA  . ASN A 307 ? 0.25810 0.22758 0.21928 -0.00335 -0.02000 0.04418  307 ASN A CA  
2386 C C   . ASN A 307 ? 0.22614 0.19712 0.18265 -0.00319 -0.01704 0.03871  307 ASN A C   
2387 O O   . ASN A 307 ? 0.24185 0.21489 0.19422 -0.00395 -0.01804 0.03758  307 ASN A O   
2388 C CB  . ASN A 307 ? 0.25430 0.22571 0.21189 -0.00525 -0.02401 0.04851  307 ASN A CB  
2389 C CG  . ASN A 307 ? 0.24278 0.21266 0.20472 -0.00566 -0.02720 0.05470  307 ASN A CG  
2390 O OD1 . ASN A 307 ? 0.26190 0.23083 0.23224 -0.00369 -0.02966 0.05634  307 ASN A OD1 
2391 N ND2 . ASN A 307 ? 0.29049 0.26020 0.24711 -0.00826 -0.02709 0.05826  307 ASN A ND2 
2392 N N   . PHE A 308 ? 0.22401 0.19387 0.18154 -0.00227 -0.01356 0.03538  308 PHE A N   
2393 C CA  . PHE A 308 ? 0.20328 0.17429 0.15710 -0.00204 -0.01074 0.03057  308 PHE A CA  
2394 C C   . PHE A 308 ? 0.20911 0.18074 0.16601 -0.00027 -0.01126 0.02767  308 PHE A C   
2395 O O   . PHE A 308 ? 0.18318 0.15594 0.13643 -0.00046 -0.00990 0.02443  308 PHE A O   
2396 C CB  . PHE A 308 ? 0.18167 0.15146 0.13700 -0.00138 -0.00741 0.02825  308 PHE A CB  
2397 C CG  . PHE A 308 ? 0.15309 0.12401 0.10513 -0.00114 -0.00459 0.02381  308 PHE A CG  
2398 C CD1 . PHE A 308 ? 0.16237 0.13484 0.10768 -0.00294 -0.00307 0.02312  308 PHE A CD1 
2399 C CD2 . PHE A 308 ? 0.14176 0.11224 0.09764 0.00086  -0.00341 0.02038  308 PHE A CD2 
2400 C CE1 . PHE A 308 ? 0.13733 0.11060 0.08063 -0.00249 -0.00053 0.01907  308 PHE A CE1 
2401 C CE2 . PHE A 308 ? 0.14039 0.11172 0.09380 0.00111  -0.00114 0.01681  308 PHE A CE2 
2402 C CZ  . PHE A 308 ? 0.14064 0.11322 0.08818 -0.00044 0.00025  0.01614  308 PHE A CZ  
2403 N N   . HIS A 309 ? 0.24024 0.21120 0.20414 0.00140  -0.01310 0.02877  309 HIS A N   
2404 C CA  . HIS A 309 ? 0.22701 0.19890 0.19463 0.00303  -0.01334 0.02622  309 HIS A CA  
2405 C C   . HIS A 309 ? 0.21075 0.18454 0.17834 0.00239  -0.01675 0.02827  309 HIS A C   
2406 O O   . HIS A 309 ? 0.19518 0.17000 0.16734 0.00371  -0.01741 0.02696  309 HIS A O   
2407 C CB  . HIS A 309 ? 0.21917 0.18965 0.19503 0.00538  -0.01267 0.02534  309 HIS A CB  
2408 C CG  . HIS A 309 ? 0.25551 0.22484 0.23712 0.00593  -0.01516 0.02916  309 HIS A CG  
2409 N ND1 . HIS A 309 ? 0.21042 0.17845 0.19048 0.00454  -0.01643 0.03307  309 HIS A ND1 
2410 C CD2 . HIS A 309 ? 0.27863 0.24790 0.26813 0.00778  -0.01655 0.02972  309 HIS A CD2 
2411 C CE1 . HIS A 309 ? 0.23379 0.20070 0.22080 0.00558  -0.01879 0.03609  309 HIS A CE1 
2412 N NE2 . HIS A 309 ? 0.27938 0.24707 0.27243 0.00767  -0.01883 0.03394  309 HIS A NE2 
2413 N N   . ARG A 310 ? 0.19443 0.16901 0.15694 0.00022  -0.01897 0.03151  310 ARG A N   
2414 C CA  . ARG A 310 ? 0.23462 0.21129 0.19645 -0.00079 -0.02266 0.03369  310 ARG A CA  
2415 C C   . ARG A 310 ? 0.22985 0.20788 0.18179 -0.00372 -0.02306 0.03382  310 ARG A C   
2416 O O   . ARG A 310 ? 0.24414 0.22155 0.19049 -0.00474 -0.02027 0.03230  310 ARG A O   
2417 C CB  . ARG A 310 ? 0.21394 0.19036 0.18151 -0.00038 -0.02620 0.03877  310 ARG A CB  
2418 C CG  . ARG A 310 ? 0.27198 0.24776 0.25014 0.00258  -0.02629 0.03819  310 ARG A CG  
2419 C CD  . ARG A 310 ? 0.23777 0.21385 0.22226 0.00302  -0.03042 0.04319  310 ARG A CD  
2420 N NE  . ARG A 310 ? 0.23508 0.21116 0.23015 0.00594  -0.03036 0.04207  310 ARG A NE  
2421 C CZ  . ARG A 310 ? 0.23372 0.20728 0.23584 0.00798  -0.02904 0.04196  310 ARG A CZ  
2422 N NH1 . ARG A 310 ? 0.23762 0.20830 0.23783 0.00739  -0.02792 0.04320  310 ARG A NH1 
2423 N NH2 . ARG A 310 ? 0.22948 0.20351 0.24097 0.01056  -0.02871 0.04038  310 ARG A NH2 
2424 N N   . MET A 311 ? 0.26334 0.24347 0.21329 -0.00515 -0.02653 0.03545  311 MET A N   
2425 C CA  . MET A 311 ? 0.29511 0.27680 0.23534 -0.00819 -0.02729 0.03528  311 MET A CA  
2426 C C   . MET A 311 ? 0.27292 0.25529 0.20921 -0.01044 -0.03006 0.04069  311 MET A C   
2427 O O   . MET A 311 ? 0.31543 0.29775 0.24445 -0.01240 -0.02830 0.04097  311 MET A O   
2428 C CB  . MET A 311 ? 0.29264 0.27636 0.23226 -0.00889 -0.02958 0.03353  311 MET A CB  
2429 C CG  . MET A 311 ? 0.29589 0.28099 0.22528 -0.01202 -0.02988 0.03190  311 MET A CG  
2430 S SD  . MET A 311 ? 0.34730 0.33480 0.27652 -0.01332 -0.03356 0.03055  311 MET A SD  
2431 C CE  . MET A 311 ? 0.33343 0.32295 0.26767 -0.01361 -0.03940 0.03734  311 MET A CE  
2432 N N   . ALA A 312 ? 0.28714 0.27034 0.22839 -0.01023 -0.03440 0.04519  312 ALA A N   
2433 C CA  . ALA A 312 ? 0.28118 0.26500 0.21930 -0.01240 -0.03760 0.05115  312 ALA A CA  
2434 C C   . ALA A 312 ? 0.33163 0.31285 0.27199 -0.01173 -0.03554 0.05347  312 ALA A C   
2435 O O   . ALA A 312 ? 0.34248 0.32151 0.29161 -0.00889 -0.03433 0.05293  312 ALA A O   
2436 C CB  . ALA A 312 ? 0.33027 0.31554 0.27491 -0.01193 -0.04296 0.05560  312 ALA A CB  
2437 N N   . GLY A 313 ? 0.33989 0.32147 0.27222 -0.01454 -0.03505 0.05591  313 GLY A N   
2438 C CA  . GLY A 313 ? 0.29536 0.27471 0.22898 -0.01449 -0.03292 0.05810  313 GLY A CA  
2439 C C   . GLY A 313 ? 0.31990 0.29821 0.25123 -0.01392 -0.02741 0.05304  313 GLY A C   
2440 O O   . GLY A 313 ? 0.32621 0.30323 0.25707 -0.01456 -0.02539 0.05467  313 GLY A O   
2441 N N   . ASN A 314 ? 0.30231 0.28118 0.23265 -0.01281 -0.02510 0.04722  314 ASN A N   
2442 C CA  . ASN A 314 ? 0.28761 0.26575 0.21617 -0.01219 -0.02017 0.04250  314 ASN A CA  
2443 C C   . ASN A 314 ? 0.24962 0.22971 0.16780 -0.01523 -0.01821 0.04169  314 ASN A C   
2444 O O   . ASN A 314 ? 0.26581 0.24782 0.17792 -0.01674 -0.01904 0.03985  314 ASN A O   
2445 C CB  . ASN A 314 ? 0.28378 0.26174 0.21542 -0.00996 -0.01868 0.03705  314 ASN A CB  
2446 C CG  . ASN A 314 ? 0.24816 0.22488 0.18107 -0.00855 -0.01417 0.03293  314 ASN A CG  
2447 O OD1 . ASN A 314 ? 0.26025 0.23699 0.18970 -0.00971 -0.01169 0.03307  314 ASN A OD1 
2448 N ND2 . ASN A 314 ? 0.25736 0.23331 0.19539 -0.00615 -0.01318 0.02942  314 ASN A ND2 
2449 N N   . PRO A 315 ? 0.29574 0.27556 0.21173 -0.01632 -0.01549 0.04277  315 PRO A N   
2450 C CA  . PRO A 315 ? 0.28779 0.26997 0.19391 -0.01935 -0.01328 0.04200  315 PRO A CA  
2451 C C   . PRO A 315 ? 0.29008 0.27306 0.19307 -0.01880 -0.00948 0.03536  315 PRO A C   
2452 O O   . PRO A 315 ? 0.33175 0.31692 0.22641 -0.02119 -0.00784 0.03372  315 PRO A O   
2453 C CB  . PRO A 315 ? 0.32959 0.31121 0.23636 -0.02034 -0.01131 0.04522  315 PRO A CB  
2454 C CG  . PRO A 315 ? 0.30641 0.28508 0.22325 -0.01718 -0.01071 0.04450  315 PRO A CG  
2455 C CD  . PRO A 315 ? 0.29004 0.26756 0.21260 -0.01504 -0.01433 0.04475  315 PRO A CD  
2456 N N   . VAL A 316 ? 0.27094 0.25226 0.18033 -0.01579 -0.00800 0.03150  316 VAL A N   
2457 C CA  . VAL A 316 ? 0.27025 0.25200 0.17772 -0.01506 -0.00461 0.02555  316 VAL A CA  
2458 C C   . VAL A 316 ? 0.25551 0.23711 0.16337 -0.01420 -0.00641 0.02256  316 VAL A C   
2459 O O   . VAL A 316 ? 0.26675 0.24864 0.17211 -0.01407 -0.00412 0.01780  316 VAL A O   
2460 C CB  . VAL A 316 ? 0.31512 0.29541 0.22884 -0.01263 -0.00140 0.02321  316 VAL A CB  
2461 C CG1 . VAL A 316 ? 0.29616 0.27649 0.21062 -0.01355 0.00006  0.02640  316 VAL A CG1 
2462 C CG2 . VAL A 316 ? 0.28998 0.26823 0.21177 -0.00981 -0.00310 0.02284  316 VAL A CG2 
2463 N N   . CYS A 317 ? 0.27036 0.25156 0.18183 -0.01365 -0.01038 0.02518  317 CYS A N   
2464 C CA  . CYS A 317 ? 0.26746 0.24878 0.18007 -0.01301 -0.01226 0.02271  317 CYS A CA  
2465 C C   . CYS A 317 ? 0.26244 0.24580 0.16746 -0.01597 -0.01488 0.02338  317 CYS A C   
2466 O O   . CYS A 317 ? 0.29498 0.27963 0.19586 -0.01816 -0.01694 0.02760  317 CYS A O   
2467 C CB  . CYS A 317 ? 0.24871 0.22905 0.16996 -0.01080 -0.01499 0.02486  317 CYS A CB  
2468 S SG  . CYS A 317 ? 0.25594 0.23684 0.17983 -0.01008 -0.01724 0.02224  317 CYS A SG  
2469 N N   . LYS A 318 ? 0.28817 0.27178 0.19110 -0.01625 -0.01476 0.01923  318 LYS A N   
2470 C CA  . LYS A 318 ? 0.28179 0.26731 0.17741 -0.01922 -0.01742 0.01900  318 LYS A CA  
2471 C C   . LYS A 318 ? 0.28417 0.27051 0.18374 -0.01924 -0.02258 0.02226  318 LYS A C   
2472 O O   . LYS A 318 ? 0.28718 0.27247 0.19491 -0.01673 -0.02314 0.02192  318 LYS A O   
2473 C CB  . LYS A 318 ? 0.30012 0.28522 0.19238 -0.01957 -0.01504 0.01275  318 LYS A CB  
2474 C CG  . LYS A 318 ? 0.37648 0.36207 0.26163 -0.02098 -0.01085 0.00969  318 LYS A CG  
2475 C CD  . LYS A 318 ? 0.37692 0.36416 0.25277 -0.02427 -0.01166 0.00723  318 LYS A CD  
2476 C CE  . LYS A 318 ? 0.39573 0.38250 0.27310 -0.02447 -0.01477 0.00505  318 LYS A CE  
2477 N NZ  . LYS A 318 ? 0.46356 0.45250 0.33194 -0.02826 -0.01753 0.00484  318 LYS A NZ  
2478 N N   . GLN A 319 ? 0.31394 0.30242 0.20770 -0.02213 -0.02614 0.02542  319 GLN A N   
2479 C CA  . GLN A 319 ? 0.32363 0.31356 0.22077 -0.02256 -0.03157 0.02900  319 GLN A CA  
2480 C C   . GLN A 319 ? 0.30263 0.29340 0.19754 -0.02375 -0.03294 0.02486  319 GLN A C   
2481 O O   . GLN A 319 ? 0.36182 0.35442 0.24839 -0.02702 -0.03480 0.02426  319 GLN A O   
2482 C CB  . GLN A 319 ? 0.36177 0.35374 0.25373 -0.02531 -0.03515 0.03486  319 GLN A CB  
2483 C CG  . GLN A 319 ? 0.32948 0.32035 0.22413 -0.02439 -0.03412 0.03943  319 GLN A CG  
2484 C CD  . GLN A 319 ? 0.33057 0.31975 0.23732 -0.02090 -0.03530 0.04188  319 GLN A CD  
2485 O OE1 . GLN A 319 ? 0.32195 0.30892 0.23420 -0.01818 -0.03173 0.03939  319 GLN A OE1 
2486 N NE2 . GLN A 319 ? 0.39585 0.38624 0.30694 -0.02099 -0.04034 0.04669  319 GLN A NE2 
2487 N N   . ILE A 320 ? 0.30805 0.29750 0.21040 -0.02128 -0.03202 0.02196  320 ILE A N   
2488 C CA  . ILE A 320 ? 0.30962 0.29941 0.21150 -0.02217 -0.03313 0.01799  320 ILE A CA  
2489 C C   . ILE A 320 ? 0.31003 0.30171 0.21849 -0.02197 -0.03808 0.02125  320 ILE A C   
2490 O O   . ILE A 320 ? 0.27507 0.26673 0.19187 -0.01956 -0.03892 0.02467  320 ILE A O   
2491 C CB  . ILE A 320 ? 0.32143 0.30867 0.22724 -0.01986 -0.02888 0.01287  320 ILE A CB  
2492 C CG1 . ILE A 320 ? 0.34390 0.32961 0.24452 -0.01975 -0.02404 0.01006  320 ILE A CG1 
2493 C CG2 . ILE A 320 ? 0.31784 0.30504 0.22308 -0.02108 -0.02996 0.00879  320 ILE A CG2 
2494 C CD1 . ILE A 320 ? 0.33178 0.31504 0.23611 -0.01757 -0.02009 0.00537  320 ILE A CD1 
2495 N N   . ASP A 321 ? 0.35492 0.34836 0.25999 -0.02455 -0.04134 0.02001  321 ASP A N   
2496 C CA  . ASP A 321 ? 0.31414 0.31016 0.22527 -0.02484 -0.04661 0.02336  321 ASP A CA  
2497 C C   . ASP A 321 ? 0.34371 0.33907 0.26440 -0.02246 -0.04569 0.02095  321 ASP A C   
2498 O O   . ASP A 321 ? 0.35163 0.34861 0.27365 -0.02395 -0.04857 0.01982  321 ASP A O   
2499 C CB  . ASP A 321 ? 0.37729 0.37580 0.28054 -0.02898 -0.05079 0.02305  321 ASP A CB  
2500 C CG  . ASP A 321 ? 0.47151 0.47239 0.36818 -0.03154 -0.05440 0.02825  321 ASP A CG  
2501 O OD1 . ASP A 321 ? 0.58084 0.58075 0.47054 -0.03221 -0.05164 0.02853  321 ASP A OD1 
2502 O OD2 . ASP A 321 ? 0.52331 0.52720 0.42195 -0.03299 -0.06004 0.03225  321 ASP A OD2 
2503 N N   . TRP A 322 ? 0.26921 0.26256 0.19647 -0.01910 -0.04202 0.02040  322 TRP A N   
2504 C CA  . TRP A 322 ? 0.26083 0.25376 0.19665 -0.01698 -0.04074 0.01832  322 TRP A CA  
2505 C C   . TRP A 322 ? 0.25761 0.25371 0.20056 -0.01728 -0.04518 0.02076  322 TRP A C   
2506 O O   . TRP A 322 ? 0.28601 0.28449 0.23022 -0.01792 -0.04917 0.02524  322 TRP A O   
2507 C CB  . TRP A 322 ? 0.24770 0.23887 0.18975 -0.01348 -0.03714 0.01889  322 TRP A CB  
2508 C CG  . TRP A 322 ? 0.21544 0.20383 0.15208 -0.01294 -0.03280 0.01669  322 TRP A CG  
2509 C CD1 . TRP A 322 ? 0.23495 0.22255 0.16937 -0.01241 -0.03165 0.01905  322 TRP A CD1 
2510 C CD2 . TRP A 322 ? 0.23741 0.22357 0.17090 -0.01289 -0.02910 0.01183  322 TRP A CD2 
2511 N NE1 . TRP A 322 ? 0.22814 0.21353 0.15828 -0.01207 -0.02740 0.01587  322 TRP A NE1 
2512 C CE2 . TRP A 322 ? 0.21785 0.20231 0.14749 -0.01223 -0.02582 0.01143  322 TRP A CE2 
2513 C CE3 . TRP A 322 ? 0.22868 0.21406 0.16279 -0.01337 -0.02835 0.00794  322 TRP A CE3 
2514 C CZ2 . TRP A 322 ? 0.19884 0.18114 0.12558 -0.01185 -0.02189 0.00728  322 TRP A CZ2 
2515 C CZ3 . TRP A 322 ? 0.21521 0.19800 0.14634 -0.01297 -0.02451 0.00393  322 TRP A CZ3 
2516 C CH2 . TRP A 322 ? 0.21980 0.20121 0.14745 -0.01212 -0.02135 0.00362  322 TRP A CH2 
2517 N N   . ASP A 323 ? 0.29729 0.29360 0.24549 -0.01682 -0.04455 0.01810  323 ASP A N   
2518 C CA  . ASP A 323 ? 0.35302 0.35274 0.30870 -0.01721 -0.04844 0.02004  323 ASP A CA  
2519 C C   . ASP A 323 ? 0.35409 0.35508 0.32059 -0.01392 -0.04790 0.02295  323 ASP A C   
2520 O O   . ASP A 323 ? 0.31265 0.31150 0.28167 -0.01133 -0.04379 0.02197  323 ASP A O   
2521 C CB  . ASP A 323 ? 0.31169 0.31126 0.26876 -0.01841 -0.04793 0.01606  323 ASP A CB  
2522 C CG  . ASP A 323 ? 0.29110 0.29028 0.23910 -0.02212 -0.04991 0.01338  323 ASP A CG  
2523 O OD1 . ASP A 323 ? 0.28110 0.28119 0.22210 -0.02405 -0.05245 0.01514  323 ASP A OD1 
2524 O OD2 . ASP A 323 ? 0.26017 0.25808 0.20795 -0.02325 -0.04892 0.00947  323 ASP A OD2 
2525 N N   . ASP A 324 ? 0.32542 0.33010 0.29854 -0.01410 -0.05218 0.02643  324 ASP A N   
2526 C CA  . ASP A 324 ? 0.31898 0.32550 0.30366 -0.01106 -0.05202 0.02893  324 ASP A CA  
2527 C C   . ASP A 324 ? 0.31941 0.32875 0.31175 -0.01122 -0.05253 0.02746  324 ASP A C   
2528 O O   . ASP A 324 ? 0.27697 0.29024 0.27504 -0.01206 -0.05677 0.02996  324 ASP A O   
2529 C CB  . ASP A 324 ? 0.33966 0.34842 0.32755 -0.01084 -0.05645 0.03441  324 ASP A CB  
2530 C CG  . ASP A 324 ? 0.35365 0.36381 0.35391 -0.00734 -0.05582 0.03665  324 ASP A CG  
2531 O OD1 . ASP A 324 ? 0.35725 0.36647 0.36230 -0.00513 -0.05149 0.03382  324 ASP A OD1 
2532 O OD2 . ASP A 324 ? 0.33883 0.35106 0.34411 -0.00684 -0.05970 0.04124  324 ASP A OD2 
2533 N N   . ASN A 325 ? 0.31764 0.32510 0.31030 -0.01051 -0.04823 0.02360  325 ASN A N   
2534 C CA  . ASN A 325 ? 0.29320 0.30297 0.29246 -0.01094 -0.04802 0.02199  325 ASN A CA  
2535 C C   . ASN A 325 ? 0.28921 0.29939 0.29684 -0.00776 -0.04397 0.02159  325 ASN A C   
2536 O O   . ASN A 325 ? 0.29923 0.30635 0.30410 -0.00673 -0.03954 0.01893  325 ASN A O   
2537 C CB  . ASN A 325 ? 0.26793 0.27521 0.26042 -0.01330 -0.04667 0.01791  325 ASN A CB  
2538 C CG  . ASN A 325 ? 0.26528 0.27538 0.26326 -0.01512 -0.04846 0.01702  325 ASN A CG  
2539 O OD1 . ASN A 325 ? 0.35288 0.36283 0.34619 -0.01822 -0.05106 0.01551  325 ASN A OD1 
2540 N ND2 . ASN A 325 ? 0.27887 0.29166 0.28684 -0.01336 -0.04696 0.01779  325 ASN A ND2 
2541 N N   . PRO A 326 ? 0.27136 0.28541 0.28935 -0.00616 -0.04528 0.02408  326 PRO A N   
2542 C CA  . PRO A 326 ? 0.31809 0.33284 0.34387 -0.00325 -0.04107 0.02322  326 PRO A CA  
2543 C C   . PRO A 326 ? 0.25950 0.27494 0.28729 -0.00398 -0.03818 0.02035  326 PRO A C   
2544 O O   . PRO A 326 ? 0.22967 0.24441 0.25991 -0.00209 -0.03378 0.01879  326 PRO A O   
2545 C CB  . PRO A 326 ? 0.31702 0.33626 0.35386 -0.00168 -0.04374 0.02652  326 PRO A CB  
2546 C CG  . PRO A 326 ? 0.29781 0.31758 0.33123 -0.00329 -0.04924 0.02982  326 PRO A CG  
2547 C CD  . PRO A 326 ? 0.26590 0.28390 0.28901 -0.00676 -0.05060 0.02789  326 PRO A CD  
2548 N N   . GLU A 327 ? 0.26757 0.28432 0.29430 -0.00685 -0.04059 0.01967  327 GLU A N   
2549 C CA  . GLU A 327 ? 0.28102 0.29834 0.31020 -0.00781 -0.03805 0.01739  327 GLU A CA  
2550 C C   . GLU A 327 ? 0.22049 0.23272 0.24140 -0.00803 -0.03437 0.01443  327 GLU A C   
2551 O O   . GLU A 327 ? 0.17457 0.18645 0.19772 -0.00719 -0.03051 0.01306  327 GLU A O   
2552 C CB  . GLU A 327 ? 0.24306 0.26303 0.27397 -0.01102 -0.04198 0.01755  327 GLU A CB  
2553 C CG  . GLU A 327 ? 0.26529 0.29137 0.30705 -0.01080 -0.04510 0.02036  327 GLU A CG  
2554 C CD  . GLU A 327 ? 0.29323 0.32058 0.33523 -0.01010 -0.04926 0.02354  327 GLU A CD  
2555 O OE1 . GLU A 327 ? 0.32308 0.34682 0.35559 -0.01075 -0.05046 0.02355  327 GLU A OE1 
2556 O OE2 . GLU A 327 ? 0.36145 0.39355 0.41344 -0.00892 -0.05130 0.02620  327 GLU A OE2 
2557 N N   . PHE A 328 ? 0.22887 0.23739 0.24035 -0.00921 -0.03551 0.01349  328 PHE A N   
2558 C CA  . PHE A 328 ? 0.20234 0.20614 0.20668 -0.00914 -0.03208 0.01076  328 PHE A CA  
2559 C C   . PHE A 328 ? 0.18990 0.19216 0.19434 -0.00617 -0.02827 0.01083  328 PHE A C   
2560 O O   . PHE A 328 ? 0.17169 0.17141 0.17387 -0.00560 -0.02478 0.00895  328 PHE A O   
2561 C CB  . PHE A 328 ? 0.21626 0.21693 0.21097 -0.01101 -0.03394 0.00953  328 PHE A CB  
2562 C CG  . PHE A 328 ? 0.20516 0.20609 0.19809 -0.01427 -0.03684 0.00808  328 PHE A CG  
2563 C CD1 . PHE A 328 ? 0.21111 0.21391 0.21026 -0.01540 -0.03695 0.00761  328 PHE A CD1 
2564 C CD2 . PHE A 328 ? 0.24206 0.24141 0.22695 -0.01642 -0.03937 0.00706  328 PHE A CD2 
2565 C CE1 . PHE A 328 ? 0.20501 0.20779 0.20282 -0.01860 -0.03975 0.00611  328 PHE A CE1 
2566 C CE2 . PHE A 328 ? 0.22823 0.22764 0.21124 -0.01961 -0.04208 0.00524  328 PHE A CE2 
2567 C CZ  . PHE A 328 ? 0.22487 0.22584 0.21456 -0.02069 -0.04238 0.00474  328 PHE A CZ  
2568 N N   . LEU A 329 ? 0.16808 0.17176 0.17533 -0.00434 -0.02907 0.01306  329 LEU A N   
2569 C CA  . LEU A 329 ? 0.18849 0.19066 0.19625 -0.00166 -0.02564 0.01292  329 LEU A CA  
2570 C C   . LEU A 329 ? 0.17206 0.17645 0.18701 -0.00022 -0.02248 0.01226  329 LEU A C   
2571 O O   . LEU A 329 ? 0.17830 0.18078 0.19149 0.00094  -0.01880 0.01074  329 LEU A O   
2572 C CB  . LEU A 329 ? 0.18923 0.19197 0.19861 -0.00024 -0.02757 0.01554  329 LEU A CB  
2573 C CG  . LEU A 329 ? 0.19904 0.20019 0.20980 0.00246  -0.02440 0.01541  329 LEU A CG  
2574 C CD1 . LEU A 329 ? 0.16647 0.16334 0.16863 0.00232  -0.02204 0.01363  329 LEU A CD1 
2575 C CD2 . LEU A 329 ? 0.25143 0.25356 0.26636 0.00383  -0.02674 0.01840  329 LEU A CD2 
2576 N N   . ALA A 330 ? 0.18076 0.18954 0.20384 -0.00042 -0.02385 0.01341  330 ALA A N   
2577 C CA  . ALA A 330 ? 0.16914 0.18070 0.19919 0.00073  -0.02057 0.01272  330 ALA A CA  
2578 C C   . ALA A 330 ? 0.16397 0.17429 0.19104 -0.00080 -0.01808 0.01083  330 ALA A C   
2579 O O   . ALA A 330 ? 0.13653 0.14685 0.16443 0.00022  -0.01425 0.00974  330 ALA A O   
2580 C CB  . ALA A 330 ? 0.19988 0.21688 0.23988 0.00072  -0.02264 0.01443  330 ALA A CB  
2581 N N   . ALA A 331 ? 0.15152 0.16067 0.17508 -0.00338 -0.02031 0.01044  331 ALA A N   
2582 C CA  . ALA A 331 ? 0.14331 0.15064 0.16433 -0.00489 -0.01828 0.00890  331 ALA A CA  
2583 C C   . ALA A 331 ? 0.12715 0.12993 0.14109 -0.00388 -0.01551 0.00745  331 ALA A C   
2584 O O   . ALA A 331 ? 0.13817 0.14026 0.15191 -0.00382 -0.01249 0.00673  331 ALA A O   
2585 C CB  . ALA A 331 ? 0.15550 0.16192 0.17434 -0.00784 -0.02147 0.00845  331 ALA A CB  
2586 N N   . TRP A 332 ? 0.14070 0.14062 0.14892 -0.00321 -0.01656 0.00724  332 TRP A N   
2587 C CA  . TRP A 332 ? 0.12987 0.12590 0.13205 -0.00218 -0.01405 0.00596  332 TRP A CA  
2588 C C   . TRP A 332 ? 0.13982 0.13678 0.14446 0.00016  -0.01105 0.00614  332 TRP A C   
2589 O O   . TRP A 332 ? 0.12278 0.11782 0.12467 0.00072  -0.00831 0.00512  332 TRP A O   
2590 C CB  . TRP A 332 ? 0.14251 0.13579 0.13825 -0.00236 -0.01587 0.00574  332 TRP A CB  
2591 C CG  . TRP A 332 ? 0.13425 0.12388 0.12425 -0.00139 -0.01347 0.00445  332 TRP A CG  
2592 C CD1 . TRP A 332 ? 0.12739 0.11386 0.11287 -0.00224 -0.01242 0.00267  332 TRP A CD1 
2593 C CD2 . TRP A 332 ? 0.10720 0.09603 0.09604 0.00058  -0.01194 0.00484  332 TRP A CD2 
2594 N NE1 . TRP A 332 ? 0.11876 0.10291 0.10052 -0.00085 -0.01035 0.00205  332 TRP A NE1 
2595 C CE2 . TRP A 332 ? 0.11793 0.10347 0.10146 0.00075  -0.01004 0.00334  332 TRP A CE2 
2596 C CE3 . TRP A 332 ? 0.12736 0.11783 0.11970 0.00222  -0.01204 0.00628  332 TRP A CE3 
2597 C CZ2 . TRP A 332 ? 0.11419 0.09836 0.09563 0.00229  -0.00834 0.00329  332 TRP A CZ2 
2598 C CZ3 . TRP A 332 ? 0.14276 0.13138 0.13284 0.00372  -0.01030 0.00610  332 TRP A CZ3 
2599 C CH2 . TRP A 332 ? 0.14864 0.13429 0.13320 0.00365  -0.00851 0.00464  332 TRP A CH2 
2600 N N   . ARG A 333 ? 0.13987 0.13973 0.14990 0.00152  -0.01162 0.00736  333 ARG A N   
2601 C CA  . ARG A 333 ? 0.13529 0.13588 0.14794 0.00373  -0.00874 0.00702  333 ARG A CA  
2602 C C   . ARG A 333 ? 0.12615 0.12948 0.14294 0.00366  -0.00578 0.00632  333 ARG A C   
2603 O O   . ARG A 333 ? 0.14770 0.15034 0.16297 0.00458  -0.00269 0.00522  333 ARG A O   
2604 C CB  . ARG A 333 ? 0.14998 0.15251 0.16786 0.00531  -0.01031 0.00842  333 ARG A CB  
2605 C CG  . ARG A 333 ? 0.19722 0.20015 0.21831 0.00765  -0.00743 0.00765  333 ARG A CG  
2606 C CD  . ARG A 333 ? 0.20294 0.20739 0.23024 0.00929  -0.00925 0.00919  333 ARG A CD  
2607 N NE  . ARG A 333 ? 0.24907 0.25799 0.28431 0.00906  -0.01088 0.01039  333 ARG A NE  
2608 C CZ  . ARG A 333 ? 0.19626 0.20636 0.23287 0.00800  -0.01501 0.01257  333 ARG A CZ  
2609 N NH1 . ARG A 333 ? 0.23343 0.24059 0.26351 0.00700  -0.01781 0.01373  333 ARG A NH1 
2610 N NH2 . ARG A 333 ? 0.22055 0.23520 0.26526 0.00781  -0.01636 0.01360  333 ARG A NH2 
2611 N N   . GLU A 334 ? 0.12861 0.13527 0.15047 0.00236  -0.00670 0.00701  334 GLU A N   
2612 C CA  . GLU A 334 ? 0.14125 0.15119 0.16747 0.00196  -0.00384 0.00667  334 GLU A CA  
2613 C C   . GLU A 334 ? 0.14029 0.14837 0.16234 -0.00004 -0.00278 0.00635  334 GLU A C   
2614 O O   . GLU A 334 ? 0.13388 0.14468 0.15899 -0.00089 -0.00055 0.00650  334 GLU A O   
2615 C CB  . GLU A 334 ? 0.12144 0.13643 0.15627 0.00145  -0.00520 0.00780  334 GLU A CB  
2616 C CG  . GLU A 334 ? 0.14350 0.16075 0.18421 0.00362  -0.00628 0.00844  334 GLU A CG  
2617 C CD  . GLU A 334 ? 0.14041 0.16253 0.18970 0.00298  -0.00863 0.00992  334 GLU A CD  
2618 O OE1 . GLU A 334 ? 0.19792 0.22211 0.24903 0.00080  -0.00880 0.01020  334 GLU A OE1 
2619 O OE2 . GLU A 334 ? 0.19230 0.21617 0.24693 0.00459  -0.01047 0.01098  334 GLU A OE2 
2620 N N   . ALA A 335 ? 0.10435 0.10796 0.11985 -0.00084 -0.00425 0.00597  335 ALA A N   
2621 C CA  . ALA A 335 ? 0.11492 0.11600 0.12679 -0.00249 -0.00347 0.00570  335 ALA A CA  
2622 C C   . ALA A 335 ? 0.11199 0.11535 0.12830 -0.00482 -0.00435 0.00653  335 ALA A C   
2623 O O   . ALA A 335 ? 0.12810 0.13253 0.14579 -0.00588 -0.00227 0.00706  335 ALA A O   
2624 C CB  . ALA A 335 ? 0.13668 0.13727 0.14631 -0.00170 -0.00002 0.00537  335 ALA A CB  
2625 N N   . ARG A 336 ? 0.10214 0.10638 0.12065 -0.00585 -0.00760 0.00682  336 ARG A N   
2626 C CA  . ARG A 336 ? 0.12253 0.12863 0.14522 -0.00838 -0.00912 0.00746  336 ARG A CA  
2627 C C   . ARG A 336 ? 0.13406 0.13716 0.15341 -0.01003 -0.01281 0.00669  336 ARG A C   
2628 O O   . ARG A 336 ? 0.10127 0.10668 0.12438 -0.01168 -0.01563 0.00715  336 ARG A O   
2629 C CB  . ARG A 336 ? 0.11925 0.13144 0.15043 -0.00826 -0.00930 0.00863  336 ARG A CB  
2630 C CG  . ARG A 336 ? 0.15939 0.17329 0.19256 -0.00642 -0.01130 0.00896  336 ARG A CG  
2631 C CD  . ARG A 336 ? 0.12029 0.14045 0.16318 -0.00618 -0.01143 0.01014  336 ARG A CD  
2632 N NE  . ARG A 336 ? 0.12900 0.15071 0.17474 -0.00423 -0.01350 0.01085  336 ARG A NE  
2633 C CZ  . ARG A 336 ? 0.15232 0.17475 0.19923 -0.00511 -0.01793 0.01193  336 ARG A CZ  
2634 N NH1 . ARG A 336 ? 0.14416 0.16589 0.18943 -0.00794 -0.02074 0.01194  336 ARG A NH1 
2635 N NH2 . ARG A 336 ? 0.20157 0.22537 0.25136 -0.00321 -0.01973 0.01307  336 ARG A NH2 
2636 N N   . THR A 337 ? 0.10462 0.10272 0.11686 -0.00969 -0.01280 0.00533  337 THR A N   
2637 C CA  . THR A 337 ? 0.12409 0.11908 0.13217 -0.01124 -0.01578 0.00398  337 THR A CA  
2638 C C   . THR A 337 ? 0.12204 0.11500 0.13087 -0.01387 -0.01645 0.00323  337 THR A C   
2639 O O   . THR A 337 ? 0.12490 0.11611 0.13172 -0.01571 -0.01923 0.00186  337 THR A O   
2640 C CB  . THR A 337 ? 0.10497 0.09566 0.10566 -0.00986 -0.01506 0.00255  337 THR A CB  
2641 O OG1 . THR A 337 ? 0.10392 0.09181 0.10282 -0.00928 -0.01221 0.00212  337 THR A OG1 
2642 C CG2 . THR A 337 ? 0.12877 0.12106 0.12879 -0.00753 -0.01468 0.00338  337 THR A CG2 
2643 N N   . GLY A 338 ? 0.11483 0.10791 0.12641 -0.01426 -0.01404 0.00411  338 GLY A N   
2644 C CA  . GLY A 338 ? 0.13333 0.12387 0.14597 -0.01670 -0.01450 0.00374  338 GLY A CA  
2645 C C   . GLY A 338 ? 0.12768 0.11248 0.13541 -0.01632 -0.01325 0.00248  338 GLY A C   
2646 O O   . GLY A 338 ? 0.14120 0.12348 0.15049 -0.01808 -0.01320 0.00254  338 GLY A O   
2647 N N   . PHE A 339 ? 0.10952 0.09220 0.11197 -0.01410 -0.01232 0.00145  339 PHE A N   
2648 C CA  . PHE A 339 ? 0.11063 0.08839 0.10919 -0.01336 -0.01095 0.00037  339 PHE A CA  
2649 C C   . PHE A 339 ? 0.10899 0.08773 0.10771 -0.01164 -0.00801 0.00221  339 PHE A C   
2650 O O   . PHE A 339 ? 0.10560 0.08627 0.10264 -0.00965 -0.00694 0.00245  339 PHE A O   
2651 C CB  . PHE A 339 ? 0.11197 0.08707 0.10471 -0.01224 -0.01167 -0.00201 339 PHE A CB  
2652 C CG  . PHE A 339 ? 0.12610 0.10010 0.11737 -0.01417 -0.01453 -0.00416 339 PHE A CG  
2653 C CD1 . PHE A 339 ? 0.13794 0.10746 0.12800 -0.01562 -0.01515 -0.00651 339 PHE A CD1 
2654 C CD2 . PHE A 339 ? 0.11643 0.09381 0.10760 -0.01460 -0.01672 -0.00389 339 PHE A CD2 
2655 C CE1 . PHE A 339 ? 0.13833 0.10686 0.12649 -0.01765 -0.01776 -0.00896 339 PHE A CE1 
2656 C CE2 . PHE A 339 ? 0.13566 0.11233 0.12483 -0.01668 -0.01963 -0.00581 339 PHE A CE2 
2657 C CZ  . PHE A 339 ? 0.15120 0.12346 0.13853 -0.01830 -0.02007 -0.00856 339 PHE A CZ  
2658 N N   . PRO A 340 ? 0.10805 0.08554 0.10867 -0.01249 -0.00677 0.00363  340 PRO A N   
2659 C CA  . PRO A 340 ? 0.10551 0.08461 0.10589 -0.01124 -0.00415 0.00558  340 PRO A CA  
2660 C C   . PRO A 340 ? 0.11437 0.09145 0.11002 -0.00886 -0.00309 0.00468  340 PRO A C   
2661 O O   . PRO A 340 ? 0.10139 0.08095 0.09622 -0.00749 -0.00132 0.00558  340 PRO A O   
2662 C CB  . PRO A 340 ? 0.10946 0.08661 0.11215 -0.01303 -0.00373 0.00738  340 PRO A CB  
2663 C CG  . PRO A 340 ? 0.11088 0.08746 0.11709 -0.01548 -0.00585 0.00682  340 PRO A CG  
2664 C CD  . PRO A 340 ? 0.12117 0.09612 0.12462 -0.01492 -0.00786 0.00379  340 PRO A CD  
2665 N N   . TRP A 341 ? 0.10627 0.07907 0.09899 -0.00840 -0.00400 0.00272  341 TRP A N   
2666 C CA  . TRP A 341 ? 0.11467 0.08590 0.10345 -0.00623 -0.00294 0.00189  341 TRP A CA  
2667 C C   . TRP A 341 ? 0.11139 0.08536 0.09827 -0.00482 -0.00281 0.00129  341 TRP A C   
2668 O O   . TRP A 341 ? 0.10692 0.08164 0.09198 -0.00316 -0.00139 0.00164  341 TRP A O   
2669 C CB  . TRP A 341 ? 0.11769 0.08419 0.10436 -0.00610 -0.00370 -0.00040 341 TRP A CB  
2670 C CG  . TRP A 341 ? 0.11132 0.07659 0.09443 -0.00399 -0.00262 -0.00142 341 TRP A CG  
2671 C CD1 . TRP A 341 ? 0.11267 0.07747 0.09236 -0.00319 -0.00291 -0.00356 341 TRP A CD1 
2672 C CD2 . TRP A 341 ? 0.12063 0.08533 0.10337 -0.00262 -0.00115 -0.00014 341 TRP A CD2 
2673 N NE1 . TRP A 341 ? 0.12421 0.08820 0.10186 -0.00139 -0.00152 -0.00377 341 TRP A NE1 
2674 C CE2 . TRP A 341 ? 0.11357 0.07749 0.09315 -0.00097 -0.00057 -0.00175 341 TRP A CE2 
2675 C CE3 . TRP A 341 ? 0.12439 0.08939 0.10906 -0.00284 -0.00041 0.00241  341 TRP A CE3 
2676 C CZ2 . TRP A 341 ? 0.12680 0.09031 0.10564 0.00054  0.00061  -0.00105 341 TRP A CZ2 
2677 C CZ3 . TRP A 341 ? 0.12922 0.09376 0.11263 -0.00137 0.00057  0.00321  341 TRP A CZ3 
2678 C CH2 . TRP A 341 ? 0.12379 0.08762 0.10458 0.00034  0.00102  0.00141  341 TRP A CH2 
2679 N N   . ILE A 342 ? 0.10263 0.07808 0.09016 -0.00556 -0.00451 0.00053  342 ILE A N   
2680 C CA  . ILE A 342 ? 0.10986 0.08778 0.09630 -0.00431 -0.00474 0.00044  342 ILE A CA  
2681 C C   . ILE A 342 ? 0.09775 0.07988 0.08776 -0.00374 -0.00349 0.00214  342 ILE A C   
2682 O O   . ILE A 342 ? 0.09556 0.07890 0.08466 -0.00206 -0.00232 0.00228  342 ILE A O   
2683 C CB  . ILE A 342 ? 0.11200 0.09020 0.09788 -0.00543 -0.00735 -0.00058 342 ILE A CB  
2684 C CG1 . ILE A 342 ? 0.11922 0.09341 0.10058 -0.00584 -0.00806 -0.00289 342 ILE A CG1 
2685 C CG2 . ILE A 342 ? 0.11560 0.09670 0.10155 -0.00429 -0.00795 0.00013  342 ILE A CG2 
2686 C CD1 . ILE A 342 ? 0.12578 0.09843 0.10302 -0.00397 -0.00658 -0.00360 342 ILE A CD1 
2687 N N   . ASP A 343 ? 0.09804 0.08248 0.09239 -0.00521 -0.00354 0.00327  343 ASP A N   
2688 C CA  . ASP A 343 ? 0.10605 0.09500 0.10427 -0.00477 -0.00201 0.00453  343 ASP A CA  
2689 C C   . ASP A 343 ? 0.10421 0.09340 0.10092 -0.00383 0.00075  0.00512  343 ASP A C   
2690 O O   . ASP A 343 ? 0.11694 0.10936 0.11525 -0.00283 0.00244  0.00533  343 ASP A O   
2691 C CB  . ASP A 343 ? 0.09679 0.08848 0.10025 -0.00683 -0.00254 0.00562  343 ASP A CB  
2692 C CG  . ASP A 343 ? 0.09819 0.09065 0.10373 -0.00788 -0.00555 0.00514  343 ASP A CG  
2693 O OD1 . ASP A 343 ? 0.09781 0.09032 0.10176 -0.00671 -0.00690 0.00447  343 ASP A OD1 
2694 O OD2 . ASP A 343 ? 0.11654 0.10963 0.12531 -0.01006 -0.00674 0.00560  343 ASP A OD2 
2695 N N   . ALA A 344 ? 0.09567 0.08158 0.08952 -0.00416 0.00117  0.00533  344 ALA A N   
2696 C CA  . ALA A 344 ? 0.10111 0.08735 0.09304 -0.00345 0.00333  0.00612  344 ALA A CA  
2697 C C   . ALA A 344 ? 0.09317 0.07875 0.08187 -0.00136 0.00388  0.00490  344 ALA A C   
2698 O O   . ALA A 344 ? 0.09203 0.07969 0.08018 -0.00057 0.00568  0.00501  344 ALA A O   
2699 C CB  . ALA A 344 ? 0.09841 0.08137 0.08898 -0.00440 0.00318  0.00716  344 ALA A CB  
2700 N N   . ILE A 345 ? 0.11240 0.09520 0.09886 -0.00062 0.00243  0.00362  345 ILE A N   
2701 C CA  . ILE A 345 ? 0.09364 0.07580 0.07733 0.00113  0.00288  0.00267  345 ILE A CA  
2702 C C   . ILE A 345 ? 0.10480 0.08993 0.09060 0.00202  0.00314  0.00244  345 ILE A C   
2703 O O   . ILE A 345 ? 0.08912 0.07496 0.07411 0.00328  0.00439  0.00204  345 ILE A O   
2704 C CB  . ILE A 345 ? 0.10378 0.08257 0.08457 0.00141  0.00151  0.00145  345 ILE A CB  
2705 C CG1 . ILE A 345 ? 0.12303 0.09872 0.10277 0.00082  0.00145  0.00140  345 ILE A CG1 
2706 C CG2 . ILE A 345 ? 0.11754 0.09588 0.09577 0.00299  0.00205  0.00075  345 ILE A CG2 
2707 C CD1 . ILE A 345 ? 0.10852 0.08108 0.08573 0.00103  0.00054  -0.00033 345 ILE A CD1 
2708 N N   . MET A 346 ? 0.10214 0.08901 0.09115 0.00137  0.00182  0.00269  346 MET A N   
2709 C CA  . MET A 346 ? 0.10185 0.09166 0.09416 0.00236  0.00190  0.00271  346 MET A CA  
2710 C C   . MET A 346 ? 0.11138 0.10455 0.10668 0.00262  0.00437  0.00287  346 MET A C   
2711 O O   . MET A 346 ? 0.14916 0.14404 0.14637 0.00400  0.00537  0.00228  346 MET A O   
2712 C CB  . MET A 346 ? 0.12526 0.11648 0.12078 0.00148  -0.00047 0.00321  346 MET A CB  
2713 C CG  . MET A 346 ? 0.11639 0.10473 0.10831 0.00102  -0.00292 0.00279  346 MET A CG  
2714 S SD  . MET A 346 ? 0.11357 0.10003 0.10173 0.00277  -0.00292 0.00239  346 MET A SD  
2715 C CE  . MET A 346 ? 0.14012 0.13006 0.13386 0.00399  -0.00345 0.00342  346 MET A CE  
2716 N N   . THR A 347 ? 0.10378 0.09791 0.09958 0.00122  0.00548  0.00362  347 THR A N   
2717 C CA  . THR A 347 ? 0.10558 0.10303 0.10296 0.00118  0.00822  0.00368  347 THR A CA  
2718 C C   . THR A 347 ? 0.10385 0.10007 0.09701 0.00216  0.00978  0.00288  347 THR A C   
2719 O O   . THR A 347 ? 0.09296 0.09160 0.08699 0.00291  0.01184  0.00189  347 THR A O   
2720 C CB  . THR A 347 ? 0.11147 0.11025 0.11002 -0.00094 0.00889  0.00518  347 THR A CB  
2721 O OG1 . THR A 347 ? 0.09084 0.09096 0.09381 -0.00203 0.00728  0.00579  347 THR A OG1 
2722 C CG2 . THR A 347 ? 0.13958 0.14237 0.13924 -0.00129 0.01199  0.00528  347 THR A CG2 
2723 N N   . GLN A 348 ? 0.09097 0.08354 0.07983 0.00214  0.00881  0.00310  348 GLN A N   
2724 C CA  . GLN A 348 ? 0.10672 0.09816 0.09187 0.00303  0.00981  0.00241  348 GLN A CA  
2725 C C   . GLN A 348 ? 0.09426 0.08537 0.07968 0.00475  0.00975  0.00089  348 GLN A C   
2726 O O   . GLN A 348 ? 0.08778 0.07933 0.07175 0.00544  0.01111  -0.00013 348 GLN A O   
2727 C CB  . GLN A 348 ? 0.10707 0.09491 0.08873 0.00275  0.00862  0.00306  348 GLN A CB  
2728 C CG  . GLN A 348 ? 0.08977 0.07684 0.06799 0.00336  0.00939  0.00277  348 GLN A CG  
2729 C CD  . GLN A 348 ? 0.09247 0.07618 0.06847 0.00341  0.00813  0.00335  348 GLN A CD  
2730 O OE1 . GLN A 348 ? 0.09938 0.08082 0.07582 0.00349  0.00680  0.00311  348 GLN A OE1 
2731 N NE2 . GLN A 348 ? 0.10951 0.09310 0.08326 0.00332  0.00853  0.00402  348 GLN A NE2 
2732 N N   . LEU A 349 ? 0.09684 0.08714 0.08407 0.00527  0.00803  0.00084  349 LEU A N   
2733 C CA  . LEU A 349 ? 0.11394 0.10381 0.10199 0.00677  0.00772  -0.00003 349 LEU A CA  
2734 C C   . LEU A 349 ? 0.10561 0.09853 0.09758 0.00759  0.00952  -0.00099 349 LEU A C   
2735 O O   . LEU A 349 ? 0.09020 0.08271 0.08179 0.00865  0.01054  -0.00225 349 LEU A O   
2736 C CB  . LEU A 349 ? 0.08673 0.07559 0.07589 0.00681  0.00527  0.00063  349 LEU A CB  
2737 C CG  . LEU A 349 ? 0.08828 0.07705 0.07941 0.00817  0.00454  0.00050  349 LEU A CG  
2738 C CD1 . LEU A 349 ? 0.09576 0.08189 0.08321 0.00889  0.00485  -0.00007 349 LEU A CD1 
2739 C CD2 . LEU A 349 ? 0.15487 0.14361 0.14741 0.00779  0.00185  0.00168  349 LEU A CD2 
2740 N N   . VAL A 350 ? 0.09202 0.08809 0.08822 0.00705  0.01004  -0.00062 350 VAL A N   
2741 C CA  . VAL A 350 ? 0.11585 0.11519 0.11674 0.00797  0.01202  -0.00183 350 VAL A CA  
2742 C C   . VAL A 350 ? 0.10442 0.10572 0.10345 0.00742  0.01507  -0.00302 350 VAL A C   
2743 O O   . VAL A 350 ? 0.14597 0.14956 0.14781 0.00830  0.01724  -0.00484 350 VAL A O   
2744 C CB  . VAL A 350 ? 0.11388 0.11648 0.12095 0.00767  0.01146  -0.00098 350 VAL A CB  
2745 C CG1 . VAL A 350 ? 0.11823 0.11919 0.12669 0.00798  0.00810  0.00030  350 VAL A CG1 
2746 C CG2 . VAL A 350 ? 0.11674 0.12112 0.12338 0.00564  0.01210  0.00012  350 VAL A CG2 
2747 N N   . THR A 351 ? 0.08977 0.09027 0.08420 0.00594  0.01526  -0.00207 351 THR A N   
2748 C CA  . THR A 351 ? 0.09718 0.09975 0.08899 0.00503  0.01783  -0.00272 351 THR A CA  
2749 C C   . THR A 351 ? 0.11483 0.11514 0.10173 0.00548  0.01799  -0.00382 351 THR A C   
2750 O O   . THR A 351 ? 0.10765 0.10951 0.09396 0.00580  0.02005  -0.00589 351 THR A O   
2751 C CB  . THR A 351 ? 0.11276 0.11609 0.10284 0.00293  0.01780  -0.00049 351 THR A CB  
2752 O OG1 . THR A 351 ? 0.11115 0.11697 0.10627 0.00226  0.01777  0.00043  351 THR A OG1 
2753 C CG2 . THR A 351 ? 0.15032 0.15609 0.13703 0.00168  0.02029  -0.00068 351 THR A CG2 
2754 N N   . TRP A 352 ? 0.09541 0.09220 0.07901 0.00545  0.01590  -0.00268 352 TRP A N   
2755 C CA  . TRP A 352 ? 0.11883 0.11371 0.09828 0.00574  0.01578  -0.00345 352 TRP A CA  
2756 C C   . TRP A 352 ? 0.09013 0.08271 0.07056 0.00734  0.01487  -0.00474 352 TRP A C   
2757 O O   . TRP A 352 ? 0.11880 0.11071 0.09729 0.00769  0.01541  -0.00617 352 TRP A O   
2758 C CB  . TRP A 352 ? 0.11526 0.10789 0.09122 0.00488  0.01421  -0.00148 352 TRP A CB  
2759 C CG  . TRP A 352 ? 0.12609 0.12052 0.10025 0.00315  0.01496  0.00015  352 TRP A CG  
2760 C CD1 . TRP A 352 ? 0.13424 0.13223 0.10949 0.00206  0.01690  0.00025  352 TRP A CD1 
2761 C CD2 . TRP A 352 ? 0.14666 0.13952 0.11790 0.00224  0.01379  0.00218  352 TRP A CD2 
2762 N NE1 . TRP A 352 ? 0.16709 0.16577 0.13975 0.00031  0.01693  0.00249  352 TRP A NE1 
2763 C CE2 . TRP A 352 ? 0.16557 0.16098 0.13598 0.00047  0.01487  0.00380  352 TRP A CE2 
2764 C CE3 . TRP A 352 ? 0.13775 0.12746 0.10743 0.00277  0.01199  0.00288  352 TRP A CE3 
2765 C CZ2 . TRP A 352 ? 0.15237 0.14694 0.12050 -0.00078 0.01387  0.00643  352 TRP A CZ2 
2766 C CZ3 . TRP A 352 ? 0.13647 0.12545 0.10446 0.00177  0.01113  0.00514  352 TRP A CZ3 
2767 C CH2 . TRP A 352 ? 0.17203 0.16326 0.13927 0.00001  0.01190  0.00706  352 TRP A CH2 
2768 N N   . GLY A 353 ? 0.09188 0.08330 0.07516 0.00809  0.01337  -0.00411 353 GLY A N   
2769 C CA  . GLY A 353 ? 0.09759 0.08660 0.08129 0.00928  0.01220  -0.00457 353 GLY A CA  
2770 C C   . GLY A 353 ? 0.10774 0.09387 0.08754 0.00908  0.01088  -0.00384 353 GLY A C   
2771 O O   . GLY A 353 ? 0.10032 0.08463 0.07982 0.00981  0.01029  -0.00424 353 GLY A O   
2772 N N   . TRP A 354 ? 0.08680 0.07252 0.06408 0.00812  0.01047  -0.00272 354 TRP A N   
2773 C CA  . TRP A 354 ? 0.08835 0.07163 0.06274 0.00807  0.00943  -0.00217 354 TRP A CA  
2774 C C   . TRP A 354 ? 0.09924 0.08180 0.07304 0.00723  0.00860  -0.00085 354 TRP A C   
2775 O O   . TRP A 354 ? 0.09208 0.07607 0.06630 0.00634  0.00913  -0.00011 354 TRP A O   
2776 C CB  . TRP A 354 ? 0.09472 0.07810 0.06664 0.00792  0.01012  -0.00270 354 TRP A CB  
2777 C CG  . TRP A 354 ? 0.09579 0.07713 0.06576 0.00803  0.00914  -0.00215 354 TRP A CG  
2778 C CD1 . TRP A 354 ? 0.09525 0.07523 0.06480 0.00863  0.00881  -0.00272 354 TRP A CD1 
2779 C CD2 . TRP A 354 ? 0.09173 0.07227 0.06060 0.00754  0.00850  -0.00089 354 TRP A CD2 
2780 N NE1 . TRP A 354 ? 0.08651 0.06530 0.05480 0.00859  0.00820  -0.00207 354 TRP A NE1 
2781 C CE2 . TRP A 354 ? 0.10074 0.07970 0.06881 0.00806  0.00795  -0.00102 354 TRP A CE2 
2782 C CE3 . TRP A 354 ? 0.10879 0.08975 0.07776 0.00670  0.00836  0.00043  354 TRP A CE3 
2783 C CZ2 . TRP A 354 ? 0.09776 0.07561 0.06555 0.00801  0.00733  -0.00013 354 TRP A CZ2 
2784 C CZ3 . TRP A 354 ? 0.10141 0.08082 0.06998 0.00658  0.00752  0.00153  354 TRP A CZ3 
2785 C CH2 . TRP A 354 ? 0.11044 0.08834 0.07862 0.00736  0.00705  0.00112  354 TRP A CH2 
2786 N N   . MET A 355 ? 0.09585 0.07615 0.06874 0.00741  0.00741  -0.00065 355 MET A N   
2787 C CA  . MET A 355 ? 0.09682 0.07571 0.06923 0.00672  0.00663  0.00008  355 MET A CA  
2788 C C   . MET A 355 ? 0.09084 0.06755 0.06137 0.00719  0.00631  -0.00022 355 MET A C   
2789 O O   . MET A 355 ? 0.08750 0.06387 0.05713 0.00788  0.00648  -0.00086 355 MET A O   
2790 C CB  . MET A 355 ? 0.09622 0.07482 0.07000 0.00624  0.00554  0.00012  355 MET A CB  
2791 C CG  . MET A 355 ? 0.08937 0.07054 0.06606 0.00601  0.00574  0.00036  355 MET A CG  
2792 S SD  . MET A 355 ? 0.09449 0.07608 0.07250 0.00694  0.00495  -0.00007 355 MET A SD  
2793 C CE  . MET A 355 ? 0.11578 0.09598 0.09307 0.00604  0.00279  0.00022  355 MET A CE  
2794 N N   . HIS A 356 ? 0.08918 0.06446 0.05968 0.00680  0.00591  0.00026  356 HIS A N   
2795 C CA  . HIS A 356 ? 0.08976 0.06312 0.05941 0.00737  0.00578  -0.00023 356 HIS A CA  
2796 C C   . HIS A 356 ? 0.09388 0.06605 0.06252 0.00754  0.00548  -0.00149 356 HIS A C   
2797 O O   . HIS A 356 ? 0.09841 0.07069 0.06715 0.00696  0.00482  -0.00170 356 HIS A O   
2798 C CB  . HIS A 356 ? 0.09134 0.06318 0.06213 0.00703  0.00539  0.00052  356 HIS A CB  
2799 C CG  . HIS A 356 ? 0.09217 0.06223 0.06316 0.00784  0.00545  -0.00013 356 HIS A CG  
2800 N ND1 . HIS A 356 ? 0.09378 0.06177 0.06480 0.00796  0.00539  -0.00166 356 HIS A ND1 
2801 C CD2 . HIS A 356 ? 0.09520 0.06553 0.06669 0.00856  0.00562  0.00039  356 HIS A CD2 
2802 C CE1 . HIS A 356 ? 0.09554 0.06261 0.06737 0.00886  0.00584  -0.00219 356 HIS A CE1 
2803 N NE2 . HIS A 356 ? 0.10298 0.07151 0.07540 0.00927  0.00584  -0.00079 356 HIS A NE2 
2804 N N   . HIS A 357 ? 0.09059 0.06194 0.05823 0.00818  0.00592  -0.00223 357 HIS A N   
2805 C CA  . HIS A 357 ? 0.09177 0.06239 0.05770 0.00812  0.00591  -0.00333 357 HIS A CA  
2806 C C   . HIS A 357 ? 0.09691 0.06608 0.06240 0.00735  0.00525  -0.00424 357 HIS A C   
2807 O O   . HIS A 357 ? 0.09522 0.06461 0.05936 0.00666  0.00448  -0.00452 357 HIS A O   
2808 C CB  . HIS A 357 ? 0.09204 0.06229 0.05742 0.00879  0.00687  -0.00401 357 HIS A CB  
2809 C CG  . HIS A 357 ? 0.09392 0.06374 0.05699 0.00849  0.00722  -0.00508 357 HIS A CG  
2810 N ND1 . HIS A 357 ? 0.09398 0.06461 0.05545 0.00807  0.00685  -0.00452 357 HIS A ND1 
2811 C CD2 . HIS A 357 ? 0.11006 0.07885 0.07211 0.00844  0.00798  -0.00666 357 HIS A CD2 
2812 C CE1 . HIS A 357 ? 0.10464 0.07491 0.06361 0.00758  0.00725  -0.00539 357 HIS A CE1 
2813 N NE2 . HIS A 357 ? 0.10006 0.06932 0.05918 0.00778  0.00812  -0.00696 357 HIS A NE2 
2814 N N   . LEU A 358 ? 0.09536 0.06296 0.06220 0.00737  0.00533  -0.00465 358 LEU A N   
2815 C CA  . LEU A 358 ? 0.10957 0.07541 0.07636 0.00650  0.00468  -0.00587 358 LEU A CA  
2816 C C   . LEU A 358 ? 0.09790 0.06449 0.06573 0.00540  0.00348  -0.00489 358 LEU A C   
2817 O O   . LEU A 358 ? 0.11460 0.08035 0.08188 0.00434  0.00254  -0.00592 358 LEU A O   
2818 C CB  . LEU A 358 ? 0.09980 0.06338 0.06875 0.00691  0.00506  -0.00648 358 LEU A CB  
2819 C CG  . LEU A 358 ? 0.10785 0.07082 0.07677 0.00806  0.00636  -0.00781 358 LEU A CG  
2820 C CD1 . LEU A 358 ? 0.10271 0.06322 0.07486 0.00861  0.00656  -0.00848 358 LEU A CD1 
2821 C CD2 . LEU A 358 ? 0.10846 0.07151 0.07405 0.00769  0.00700  -0.00992 358 LEU A CD2 
2822 N N   . ALA A 359 ? 0.09555 0.06396 0.06493 0.00550  0.00355  -0.00310 359 ALA A N   
2823 C CA  . ALA A 359 ? 0.09520 0.06510 0.06605 0.00452  0.00275  -0.00221 359 ALA A CA  
2824 C C   . ALA A 359 ? 0.09872 0.07010 0.06858 0.00440  0.00203  -0.00245 359 ALA A C   
2825 O O   . ALA A 359 ? 0.10383 0.07576 0.07449 0.00338  0.00079  -0.00246 359 ALA A O   
2826 C CB  . ALA A 359 ? 0.09332 0.06518 0.06585 0.00462  0.00346  -0.00051 359 ALA A CB  
2827 N N   . ARG A 360 ? 0.09365 0.06570 0.06211 0.00534  0.00260  -0.00242 360 ARG A N   
2828 C CA  . ARG A 360 ? 0.09610 0.06912 0.06366 0.00525  0.00171  -0.00226 360 ARG A CA  
2829 C C   . ARG A 360 ? 0.09714 0.06882 0.06181 0.00439  0.00079  -0.00340 360 ARG A C   
2830 O O   . ARG A 360 ? 0.09845 0.07103 0.06236 0.00374  -0.00064 -0.00295 360 ARG A O   
2831 C CB  . ARG A 360 ? 0.10271 0.07633 0.06976 0.00631  0.00257  -0.00184 360 ARG A CB  
2832 C CG  . ARG A 360 ? 0.11063 0.08567 0.07999 0.00700  0.00355  -0.00124 360 ARG A CG  
2833 C CD  . ARG A 360 ? 0.12808 0.10268 0.09639 0.00778  0.00471  -0.00151 360 ARG A CD  
2834 N NE  . ARG A 360 ? 0.11960 0.09474 0.08825 0.00834  0.00481  -0.00128 360 ARG A NE  
2835 C CZ  . ARG A 360 ? 0.10519 0.08129 0.07528 0.00887  0.00560  -0.00137 360 ARG A CZ  
2836 N NH1 . ARG A 360 ? 0.10204 0.07909 0.07269 0.00881  0.00640  -0.00157 360 ARG A NH1 
2837 N NH2 . ARG A 360 ? 0.08735 0.06340 0.05822 0.00934  0.00556  -0.00126 360 ARG A NH2 
2838 N N   . HIS A 361 ? 0.11026 0.07993 0.07339 0.00434  0.00155  -0.00489 361 HIS A N   
2839 C CA  . HIS A 361 ? 0.11067 0.07907 0.07081 0.00332  0.00098  -0.00662 361 HIS A CA  
2840 C C   . HIS A 361 ? 0.12799 0.09626 0.08895 0.00185  -0.00078 -0.00696 361 HIS A C   
2841 O O   . HIS A 361 ? 0.11132 0.07988 0.06977 0.00063  -0.00218 -0.00760 361 HIS A O   
2842 C CB  . HIS A 361 ? 0.12063 0.08689 0.08005 0.00380  0.00251  -0.00854 361 HIS A CB  
2843 C CG  . HIS A 361 ? 0.13046 0.09699 0.08739 0.00443  0.00391  -0.00912 361 HIS A CG  
2844 N ND1 . HIS A 361 ? 0.12284 0.08811 0.07760 0.00424  0.00507  -0.01151 361 HIS A ND1 
2845 C CD2 . HIS A 361 ? 0.13255 0.10052 0.08913 0.00514  0.00450  -0.00773 361 HIS A CD2 
2846 C CE1 . HIS A 361 ? 0.14088 0.10716 0.09401 0.00475  0.00639  -0.01135 361 HIS A CE1 
2847 N NE2 . HIS A 361 ? 0.14251 0.11028 0.09676 0.00524  0.00593  -0.00897 361 HIS A NE2 
2848 N N   . SER A 362 ? 0.11526 0.08330 0.07968 0.00173  -0.00086 -0.00641 362 SER A N   
2849 C CA  . SER A 362 ? 0.13286 0.10069 0.09872 0.00013  -0.00248 -0.00676 362 SER A CA  
2850 C C   . SER A 362 ? 0.11045 0.08109 0.07720 -0.00058 -0.00427 -0.00536 362 SER A C   
2851 O O   . SER A 362 ? 0.11853 0.08934 0.08393 -0.00206 -0.00615 -0.00609 362 SER A O   
2852 C CB  . SER A 362 ? 0.11360 0.08076 0.08327 0.00004  -0.00199 -0.00593 362 SER A CB  
2853 O OG  . SER A 362 ? 0.12784 0.09233 0.09743 0.00076  -0.00071 -0.00689 362 SER A OG  
2854 N N   . VAL A 363 ? 0.10147 0.07442 0.07070 0.00045  -0.00378 -0.00344 363 VAL A N   
2855 C CA  . VAL A 363 ? 0.10884 0.08464 0.08041 0.00008  -0.00539 -0.00200 363 VAL A CA  
2856 C C   . VAL A 363 ? 0.11875 0.09500 0.08730 0.00001  -0.00673 -0.00172 363 VAL A C   
2857 O O   . VAL A 363 ? 0.12388 0.10188 0.09337 -0.00092 -0.00900 -0.00084 363 VAL A O   
2858 C CB  . VAL A 363 ? 0.09719 0.07525 0.07264 0.00132  -0.00409 -0.00051 363 VAL A CB  
2859 C CG1 . VAL A 363 ? 0.10370 0.08210 0.08211 0.00075  -0.00319 -0.00026 363 VAL A CG1 
2860 C CG2 . VAL A 363 ? 0.09537 0.07268 0.06904 0.00291  -0.00229 -0.00054 363 VAL A CG2 
2861 N N   . ALA A 364 ? 0.10939 0.08429 0.07445 0.00084  -0.00551 -0.00219 364 ALA A N   
2862 C CA  . ALA A 364 ? 0.10661 0.08194 0.06839 0.00049  -0.00668 -0.00155 364 ALA A CA  
2863 C C   . ALA A 364 ? 0.11012 0.08454 0.06756 -0.00140 -0.00808 -0.00310 364 ALA A C   
2864 O O   . ALA A 364 ? 0.12751 0.10319 0.08295 -0.00252 -0.01027 -0.00211 364 ALA A O   
2865 C CB  . ALA A 364 ? 0.10413 0.07855 0.06381 0.00171  -0.00476 -0.00148 364 ALA A CB  
2866 N N   . CYS A 365 ? 0.11162 0.08383 0.06760 -0.00184 -0.00693 -0.00557 365 CYS A N   
2867 C CA  . CYS A 365 ? 0.13132 0.10247 0.08330 -0.00375 -0.00807 -0.00777 365 CYS A CA  
2868 C C   . CYS A 365 ? 0.11973 0.09200 0.07390 -0.00541 -0.01079 -0.00750 365 CYS A C   
2869 O O   . CYS A 365 ? 0.14464 0.11743 0.09543 -0.00731 -0.01293 -0.00820 365 CYS A O   
2870 C CB  . CYS A 365 ? 0.13845 0.10664 0.08936 -0.00353 -0.00593 -0.01076 365 CYS A CB  
2871 S SG  . CYS A 365 ? 0.19567 0.16203 0.14170 -0.00585 -0.00675 -0.01456 365 CYS A SG  
2872 N N   . PHE A 366 ? 0.11503 0.08797 0.07475 -0.00493 -0.01076 -0.00644 366 PHE A N   
2873 C CA  . PHE A 366 ? 0.13804 0.11241 0.10081 -0.00659 -0.01319 -0.00606 366 PHE A CA  
2874 C C   . PHE A 366 ? 0.11825 0.09590 0.08167 -0.00709 -0.01587 -0.00376 366 PHE A C   
2875 O O   . PHE A 366 ? 0.12052 0.09923 0.08320 -0.00912 -0.01869 -0.00400 366 PHE A O   
2876 C CB  . PHE A 366 ? 0.15380 0.12867 0.12250 -0.00597 -0.01213 -0.00508 366 PHE A CB  
2877 C CG  . PHE A 366 ? 0.14969 0.12613 0.12229 -0.00782 -0.01429 -0.00471 366 PHE A CG  
2878 C CD1 . PHE A 366 ? 0.12852 0.10259 0.10100 -0.00960 -0.01486 -0.00676 366 PHE A CD1 
2879 C CD2 . PHE A 366 ? 0.13410 0.11440 0.11117 -0.00778 -0.01573 -0.00237 366 PHE A CD2 
2880 C CE1 . PHE A 366 ? 0.13354 0.10912 0.10995 -0.01155 -0.01694 -0.00637 366 PHE A CE1 
2881 C CE2 . PHE A 366 ? 0.11278 0.09500 0.09408 -0.00957 -0.01771 -0.00194 366 PHE A CE2 
2882 C CZ  . PHE A 366 ? 0.14577 0.12566 0.12660 -0.01158 -0.01837 -0.00388 366 PHE A CZ  
2883 N N   . LEU A 367 ? 0.11814 0.09737 0.08326 -0.00531 -0.01522 -0.00151 367 LEU A N   
2884 C CA  . LEU A 367 ? 0.13217 0.11438 0.09916 -0.00546 -0.01783 0.00106  367 LEU A CA  
2885 C C   . LEU A 367 ? 0.15891 0.14094 0.11965 -0.00685 -0.01980 0.00122  367 LEU A C   
2886 O O   . LEU A 367 ? 0.14641 0.13061 0.10732 -0.00831 -0.02315 0.00264  367 LEU A O   
2887 C CB  . LEU A 367 ? 0.12416 0.10755 0.09509 -0.00310 -0.01638 0.00311  367 LEU A CB  
2888 C CG  . LEU A 367 ? 0.11025 0.09631 0.08403 -0.00278 -0.01892 0.00599  367 LEU A CG  
2889 C CD1 . LEU A 367 ? 0.14267 0.13194 0.12367 -0.00295 -0.02050 0.00712  367 LEU A CD1 
2890 C CD2 . LEU A 367 ? 0.14286 0.12853 0.11786 -0.00063 -0.01724 0.00731  367 LEU A CD2 
2891 N N   . THR A 368 ? 0.12826 0.10807 0.08348 -0.00656 -0.01782 -0.00009 368 THR A N   
2892 C CA  . THR A 368 ? 0.14163 0.12163 0.09046 -0.00790 -0.01917 0.00034  368 THR A CA  
2893 C C   . THR A 368 ? 0.16527 0.14401 0.10826 -0.01030 -0.01978 -0.00285 368 THR A C   
2894 O O   . THR A 368 ? 0.19964 0.17921 0.14354 -0.01206 -0.02225 -0.00352 368 THR A O   
2895 C CB  . THR A 368 ? 0.15063 0.12942 0.09681 -0.00648 -0.01655 0.00077  368 THR A CB  
2896 O OG1 . THR A 368 ? 0.12546 0.10180 0.07071 -0.00567 -0.01326 -0.00217 368 THR A OG1 
2897 C CG2 . THR A 368 ? 0.17260 0.15246 0.12433 -0.00436 -0.01624 0.00369  368 THR A CG2 
2898 N N   . ARG A 369 ? 0.13805 0.11489 0.07536 -0.01046 -0.01745 -0.00505 369 ARG A N   
2899 C CA  . ARG A 369 ? 0.17324 0.14893 0.10414 -0.01274 -0.01759 -0.00852 369 ARG A CA  
2900 C C   . ARG A 369 ? 0.19079 0.16426 0.12387 -0.01325 -0.01705 -0.01203 369 ARG A C   
2901 O O   . ARG A 369 ? 0.20955 0.18140 0.13775 -0.01486 -0.01653 -0.01570 369 ARG A O   
2902 C CB  . ARG A 369 ? 0.18095 0.15544 0.10636 -0.01238 -0.01448 -0.01010 369 ARG A CB  
2903 C CG  . ARG A 369 ? 0.16235 0.13467 0.09128 -0.00991 -0.01075 -0.01147 369 ARG A CG  
2904 C CD  . ARG A 369 ? 0.21294 0.18435 0.13695 -0.00978 -0.00764 -0.01364 369 ARG A CD  
2905 N NE  . ARG A 369 ? 0.17461 0.14422 0.10259 -0.00744 -0.00445 -0.01478 369 ARG A NE  
2906 C CZ  . ARG A 369 ? 0.18711 0.15431 0.11681 -0.00700 -0.00286 -0.01812 369 ARG A CZ  
2907 N NH1 . ARG A 369 ? 0.19636 0.16231 0.12422 -0.00875 -0.00390 -0.02113 369 ARG A NH1 
2908 N NH2 . ARG A 369 ? 0.17659 0.14254 0.11021 -0.00483 -0.00037 -0.01840 369 ARG A NH2 
2909 N N   . GLY A 370 ? 0.21240 0.18564 0.15239 -0.01215 -0.01706 -0.01123 370 GLY A N   
2910 C CA  . GLY A 370 ? 0.17145 0.14218 0.11370 -0.01268 -0.01639 -0.01420 370 GLY A CA  
2911 C C   . GLY A 370 ? 0.18520 0.15704 0.13056 -0.01468 -0.01956 -0.01403 370 GLY A C   
2912 O O   . GLY A 370 ? 0.18149 0.15134 0.12552 -0.01654 -0.02019 -0.01723 370 GLY A O   
2913 N N   . ASP A 371 ? 0.19803 0.17308 0.14805 -0.01435 -0.02155 -0.01049 371 ASP A N   
2914 C CA  . ASP A 371 ? 0.16534 0.14191 0.11994 -0.01605 -0.02428 -0.01005 371 ASP A CA  
2915 C C   . ASP A 371 ? 0.17418 0.15509 0.13097 -0.01662 -0.02770 -0.00661 371 ASP A C   
2916 O O   . ASP A 371 ? 0.18172 0.16416 0.13719 -0.01914 -0.03117 -0.00690 371 ASP A O   
2917 C CB  . ASP A 371 ? 0.16318 0.13905 0.12472 -0.01477 -0.02238 -0.00948 371 ASP A CB  
2918 C CG  . ASP A 371 ? 0.17204 0.14358 0.13270 -0.01490 -0.02015 -0.01273 371 ASP A CG  
2919 O OD1 . ASP A 371 ? 0.19400 0.16397 0.15464 -0.01713 -0.02159 -0.01507 371 ASP A OD1 
2920 O OD2 . ASP A 371 ? 0.16262 0.13226 0.12288 -0.01281 -0.01710 -0.01295 371 ASP A OD2 
2921 N N   . LEU A 372 ? 0.17096 0.15386 0.13146 -0.01432 -0.02690 -0.00342 372 LEU A N   
2922 C CA  . LEU A 372 ? 0.17402 0.16100 0.13864 -0.01436 -0.02996 0.00005  372 LEU A CA  
2923 C C   . LEU A 372 ? 0.17665 0.16474 0.13602 -0.01485 -0.03207 0.00184  372 LEU A C   
2924 O O   . LEU A 372 ? 0.15476 0.14612 0.11638 -0.01576 -0.03575 0.00449  372 LEU A O   
2925 C CB  . LEU A 372 ? 0.17628 0.16486 0.14824 -0.01163 -0.02800 0.00236  372 LEU A CB  
2926 C CG  . LEU A 372 ? 0.14792 0.13595 0.12505 -0.01121 -0.02574 0.00127  372 LEU A CG  
2927 C CD1 . LEU A 372 ? 0.13367 0.12383 0.11727 -0.00875 -0.02375 0.00336  372 LEU A CD1 
2928 C CD2 . LEU A 372 ? 0.16438 0.15391 0.14469 -0.01373 -0.02835 0.00072  372 LEU A CD2 
2929 N N   . TYR A 373 ? 0.16719 0.15289 0.12004 -0.01435 -0.02989 0.00073  373 TYR A N   
2930 C CA  . TYR A 373 ? 0.19864 0.18520 0.14556 -0.01515 -0.03150 0.00250  373 TYR A CA  
2931 C C   . TYR A 373 ? 0.19019 0.17934 0.14207 -0.01354 -0.03310 0.00710  373 TYR A C   
2932 O O   . TYR A 373 ? 0.21543 0.20657 0.16502 -0.01478 -0.03639 0.00982  373 TYR A O   
2933 C CB  . TYR A 373 ? 0.21743 0.20503 0.15853 -0.01860 -0.03508 0.00145  373 TYR A CB  
2934 C CG  . TYR A 373 ? 0.26227 0.24903 0.19366 -0.01999 -0.03468 0.00071  373 TYR A CG  
2935 C CD1 . TYR A 373 ? 0.22911 0.21281 0.15478 -0.02037 -0.03132 -0.00361 373 TYR A CD1 
2936 C CD2 . TYR A 373 ? 0.23937 0.22855 0.16762 -0.02097 -0.03758 0.00446  373 TYR A CD2 
2937 C CE1 . TYR A 373 ? 0.25292 0.23631 0.16981 -0.02173 -0.03050 -0.00450 373 TYR A CE1 
2938 C CE2 . TYR A 373 ? 0.26996 0.25871 0.18894 -0.02254 -0.03700 0.00401  373 TYR A CE2 
2939 C CZ  . TYR A 373 ? 0.25369 0.23971 0.16691 -0.02294 -0.03328 -0.00064 373 TYR A CZ  
2940 O OH  . TYR A 373 ? 0.30593 0.29198 0.21003 -0.02459 -0.03227 -0.00130 373 TYR A OH  
2941 N N   . VAL A 374 ? 0.17016 0.15928 0.12889 -0.01085 -0.03082 0.00798  374 VAL A N   
2942 C CA  . VAL A 374 ? 0.17205 0.16299 0.13618 -0.00892 -0.03161 0.01171  374 VAL A CA  
2943 C C   . VAL A 374 ? 0.15565 0.14442 0.11595 -0.00759 -0.02914 0.01224  374 VAL A C   
2944 O O   . VAL A 374 ? 0.16748 0.15365 0.12386 -0.00724 -0.02584 0.00956  374 VAL A O   
2945 C CB  . VAL A 374 ? 0.16282 0.15513 0.13634 -0.00686 -0.03022 0.01194  374 VAL A CB  
2946 C CG1 . VAL A 374 ? 0.14480 0.13910 0.12481 -0.00486 -0.03121 0.01540  374 VAL A CG1 
2947 C CG2 . VAL A 374 ? 0.18589 0.18030 0.16304 -0.00849 -0.03221 0.01111  374 VAL A CG2 
2948 N N   . SER A 375 ? 0.16078 0.15065 0.12272 -0.00691 -0.03087 0.01589  375 SER A N   
2949 C CA  . SER A 375 ? 0.17714 0.16508 0.13569 -0.00603 -0.02893 0.01686  375 SER A CA  
2950 C C   . SER A 375 ? 0.15907 0.14507 0.12089 -0.00356 -0.02470 0.01500  375 SER A C   
2951 O O   . SER A 375 ? 0.14283 0.12963 0.11163 -0.00191 -0.02388 0.01469  375 SER A O   
2952 C CB  . SER A 375 ? 0.17280 0.16210 0.13434 -0.00559 -0.03180 0.02153  375 SER A CB  
2953 O OG  . SER A 375 ? 0.13554 0.12282 0.09452 -0.00483 -0.02987 0.02264  375 SER A OG  
2954 N N   . TRP A 376 ? 0.17622 0.15997 0.13286 -0.00346 -0.02201 0.01375  376 TRP A N   
2955 C CA  . TRP A 376 ? 0.18003 0.16208 0.13920 -0.00136 -0.01833 0.01220  376 TRP A CA  
2956 C C   . TRP A 376 ? 0.14082 0.12311 0.10621 0.00065  -0.01831 0.01460  376 TRP A C   
2957 O O   . TRP A 376 ? 0.15965 0.14110 0.12849 0.00241  -0.01568 0.01325  376 TRP A O   
2958 C CB  . TRP A 376 ? 0.13472 0.11475 0.08749 -0.00182 -0.01575 0.01058  376 TRP A CB  
2959 C CG  . TRP A 376 ? 0.12977 0.10982 0.07854 -0.00278 -0.01671 0.01319  376 TRP A CG  
2960 C CD1 . TRP A 376 ? 0.14036 0.12114 0.08254 -0.00517 -0.01845 0.01390  376 TRP A CD1 
2961 C CD2 . TRP A 376 ? 0.13824 0.11753 0.08917 -0.00163 -0.01598 0.01552  376 TRP A CD2 
2962 N NE1 . TRP A 376 ? 0.16855 0.14926 0.10852 -0.00563 -0.01882 0.01692  376 TRP A NE1 
2963 C CE2 . TRP A 376 ? 0.16184 0.14145 0.10745 -0.00345 -0.01737 0.01799  376 TRP A CE2 
2964 C CE3 . TRP A 376 ? 0.14224 0.12057 0.09894 0.00057  -0.01430 0.01565  376 TRP A CE3 
2965 C CZ2 . TRP A 376 ? 0.15254 0.13138 0.09898 -0.00311 -0.01718 0.02091  376 TRP A CZ2 
2966 C CZ3 . TRP A 376 ? 0.12724 0.10464 0.08481 0.00096  -0.01416 0.01809  376 TRP A CZ3 
2967 C CH2 . TRP A 376 ? 0.13956 0.11712 0.09229 -0.00085 -0.01561 0.02084  376 TRP A CH2 
2968 N N   . GLU A 377 ? 0.14821 0.13158 0.11519 0.00035  -0.02126 0.01810  377 GLU A N   
2969 C CA  . GLU A 377 ? 0.15183 0.13517 0.12583 0.00238  -0.02142 0.02026  377 GLU A CA  
2970 C C   . GLU A 377 ? 0.18118 0.16625 0.16324 0.00399  -0.02119 0.01935  377 GLU A C   
2971 O O   . GLU A 377 ? 0.18727 0.17180 0.17463 0.00602  -0.01919 0.01874  377 GLU A O   
2972 C CB  . GLU A 377 ? 0.18593 0.16999 0.16034 0.00162  -0.02505 0.02465  377 GLU A CB  
2973 C CG  . GLU A 377 ? 0.15735 0.13967 0.12529 0.00039  -0.02472 0.02626  377 GLU A CG  
2974 C CD  . GLU A 377 ? 0.20136 0.18449 0.16970 -0.00059 -0.02863 0.03123  377 GLU A CD  
2975 O OE1 . GLU A 377 ? 0.24905 0.23445 0.21636 -0.00208 -0.03210 0.03281  377 GLU A OE1 
2976 O OE2 . GLU A 377 ? 0.24279 0.22430 0.21271 0.00001  -0.02845 0.03373  377 GLU A OE2 
2977 N N   . ARG A 378 ? 0.17745 0.16478 0.16058 0.00294  -0.02314 0.01911  378 ARG A N   
2978 C CA  . ARG A 378 ? 0.19150 0.18105 0.18250 0.00422  -0.02275 0.01835  378 ARG A CA  
2979 C C   . ARG A 378 ? 0.16982 0.15842 0.16077 0.00505  -0.01877 0.01492  378 ARG A C   
2980 O O   . ARG A 378 ? 0.16884 0.15834 0.16585 0.00680  -0.01691 0.01418  378 ARG A O   
2981 C CB  . ARG A 378 ? 0.16073 0.15308 0.15281 0.00253  -0.02594 0.01901  378 ARG A CB  
2982 C CG  . ARG A 378 ? 0.21345 0.20872 0.21294 0.00309  -0.02947 0.02239  378 ARG A CG  
2983 C CD  . ARG A 378 ? 0.25382 0.24837 0.25040 0.00241  -0.03256 0.02600  378 ARG A CD  
2984 N NE  . ARG A 378 ? 0.19186 0.18420 0.19079 0.00442  -0.03091 0.02710  378 ARG A NE  
2985 C CZ  . ARG A 378 ? 0.23748 0.22861 0.23443 0.00405  -0.03293 0.03044  378 ARG A CZ  
2986 N NH1 . ARG A 378 ? 0.35683 0.34899 0.34883 0.00172  -0.03669 0.03317  378 ARG A NH1 
2987 N NH2 . ARG A 378 ? 0.20541 0.19424 0.20525 0.00586  -0.03120 0.03110  378 ARG A NH2 
2988 N N   . GLY A 379 ? 0.17760 0.16449 0.16185 0.00378  -0.01743 0.01281  379 GLY A N   
2989 C CA  . GLY A 379 ? 0.17453 0.16036 0.15848 0.00448  -0.01399 0.01011  379 GLY A CA  
2990 C C   . GLY A 379 ? 0.13946 0.12348 0.12330 0.00607  -0.01144 0.00965  379 GLY A C   
2991 O O   . GLY A 379 ? 0.15258 0.13661 0.13861 0.00712  -0.00889 0.00804  379 GLY A O   
2992 N N   . MET A 380 ? 0.12115 0.10372 0.10229 0.00603  -0.01214 0.01112  380 MET A N   
2993 C CA  . MET A 380 ? 0.14498 0.12583 0.12669 0.00736  -0.01005 0.01085  380 MET A CA  
2994 C C   . MET A 380 ? 0.14769 0.12952 0.13696 0.00921  -0.00963 0.01120  380 MET A C   
2995 O O   . MET A 380 ? 0.14442 0.12538 0.13515 0.01036  -0.00716 0.00959  380 MET A O   
2996 C CB  . MET A 380 ? 0.15839 0.13771 0.13614 0.00663  -0.01110 0.01281  380 MET A CB  
2997 C CG  . MET A 380 ? 0.15597 0.13330 0.13363 0.00755  -0.00895 0.01240  380 MET A CG  
2998 S SD  . MET A 380 ? 0.21141 0.18728 0.18496 0.00636  -0.01019 0.01528  380 MET A SD  
2999 C CE  . MET A 380 ? 0.16332 0.14013 0.14263 0.00680  -0.01373 0.01906  380 MET A CE  
3000 N N   . GLU A 381 ? 0.14392 0.12770 0.13826 0.00948  -0.01203 0.01311  381 GLU A N   
3001 C CA  . GLU A 381 ? 0.16884 0.15389 0.17139 0.01141  -0.01140 0.01305  381 GLU A CA  
3002 C C   . GLU A 381 ? 0.13989 0.12667 0.14481 0.01193  -0.00872 0.01028  381 GLU A C   
3003 O O   . GLU A 381 ? 0.17005 0.15725 0.17969 0.01349  -0.00662 0.00888  381 GLU A O   
3004 C CB  . GLU A 381 ? 0.17066 0.15785 0.17877 0.01158  -0.01481 0.01592  381 GLU A CB  
3005 C CG  . GLU A 381 ? 0.17507 0.16074 0.18141 0.01103  -0.01770 0.01934  381 GLU A CG  
3006 C CD  . GLU A 381 ? 0.18638 0.17454 0.19653 0.01054  -0.02183 0.02259  381 GLU A CD  
3007 O OE1 . GLU A 381 ? 0.20874 0.19987 0.22241 0.01040  -0.02247 0.02195  381 GLU A OE1 
3008 O OE2 . GLU A 381 ? 0.14838 0.13567 0.15809 0.01013  -0.02457 0.02601  381 GLU A OE2 
3009 N N   . VAL A 382 ? 0.12465 0.11238 0.12627 0.01051  -0.00868 0.00941  382 VAL A N   
3010 C CA  . VAL A 382 ? 0.14791 0.13726 0.15121 0.01063  -0.00618 0.00727  382 VAL A CA  
3011 C C   . VAL A 382 ? 0.12499 0.11230 0.12422 0.01090  -0.00325 0.00524  382 VAL A C   
3012 O O   . VAL A 382 ? 0.12677 0.11514 0.12838 0.01168  -0.00077 0.00360  382 VAL A O   
3013 C CB  . VAL A 382 ? 0.13454 0.12522 0.13616 0.00885  -0.00737 0.00731  382 VAL A CB  
3014 C CG1 . VAL A 382 ? 0.13786 0.13021 0.14123 0.00871  -0.00481 0.00563  382 VAL A CG1 
3015 C CG2 . VAL A 382 ? 0.16694 0.16004 0.17285 0.00840  -0.01063 0.00939  382 VAL A CG2 
3016 N N   . PHE A 383 ? 0.10810 0.09277 0.10116 0.01017  -0.00349 0.00529  383 PHE A N   
3017 C CA  . PHE A 383 ? 0.11260 0.09557 0.10220 0.01038  -0.00110 0.00363  383 PHE A CA  
3018 C C   . PHE A 383 ? 0.11632 0.09853 0.10847 0.01176  0.00014  0.00310  383 PHE A C   
3019 O O   . PHE A 383 ? 0.10658 0.08894 0.09885 0.01221  0.00240  0.00127  383 PHE A O   
3020 C CB  . PHE A 383 ? 0.10081 0.08153 0.08416 0.00935  -0.00159 0.00379  383 PHE A CB  
3021 C CG  . PHE A 383 ? 0.09711 0.07777 0.07744 0.00819  -0.00142 0.00294  383 PHE A CG  
3022 C CD1 . PHE A 383 ? 0.10251 0.08505 0.08553 0.00773  -0.00158 0.00277  383 PHE A CD1 
3023 C CD2 . PHE A 383 ? 0.10322 0.08193 0.07861 0.00756  -0.00099 0.00228  383 PHE A CD2 
3024 C CE1 . PHE A 383 ? 0.10402 0.08604 0.08476 0.00657  -0.00153 0.00210  383 PHE A CE1 
3025 C CE2 . PHE A 383 ? 0.11122 0.08944 0.08460 0.00664  -0.00083 0.00136  383 PHE A CE2 
3026 C CZ  . PHE A 383 ? 0.10086 0.08051 0.07688 0.00610  -0.00121 0.00134  383 PHE A CZ  
3027 N N   . GLU A 384 ? 0.13576 0.11703 0.12988 0.01229  -0.00144 0.00472  384 GLU A N   
3028 C CA  . GLU A 384 ? 0.15501 0.13502 0.15214 0.01354  -0.00043 0.00417  384 GLU A CA  
3029 C C   . GLU A 384 ? 0.15111 0.13303 0.15421 0.01483  0.00126  0.00239  384 GLU A C   
3030 O O   . GLU A 384 ? 0.18445 0.16550 0.18897 0.01565  0.00311  0.00051  384 GLU A O   
3031 C CB  . GLU A 384 ? 0.19527 0.17386 0.19409 0.01373  -0.00280 0.00684  384 GLU A CB  
3032 C CG  . GLU A 384 ? 0.18904 0.16684 0.19441 0.01534  -0.00255 0.00680  384 GLU A CG  
3033 C CD  . GLU A 384 ? 0.23413 0.21017 0.24118 0.01537  -0.00512 0.01006  384 GLU A CD  
3034 O OE1 . GLU A 384 ? 0.27189 0.24794 0.27474 0.01400  -0.00723 0.01250  384 GLU A OE1 
3035 O OE2 . GLU A 384 ? 0.26878 0.24339 0.28127 0.01666  -0.00499 0.01015  384 GLU A OE2 
3036 N N   . GLU A 385 ? 0.12966 0.11440 0.13627 0.01489  0.00082  0.00269  385 GLU A N   
3037 C CA  . GLU A 385 ? 0.13400 0.12119 0.14656 0.01605  0.00283  0.00085  385 GLU A CA  
3038 C C   . GLU A 385 ? 0.12526 0.11332 0.13457 0.01551  0.00583  -0.00174 385 GLU A C   
3039 O O   . GLU A 385 ? 0.14460 0.13309 0.15598 0.01634  0.00818  -0.00409 385 GLU A O   
3040 C CB  . GLU A 385 ? 0.15915 0.14961 0.17686 0.01609  0.00147  0.00215  385 GLU A CB  
3041 C CG  . GLU A 385 ? 0.15702 0.15075 0.18142 0.01723  0.00391  0.00017  385 GLU A CG  
3042 C CD  . GLU A 385 ? 0.17923 0.17665 0.20952 0.01718  0.00247  0.00164  385 GLU A CD  
3043 O OE1 . GLU A 385 ? 0.23121 0.22843 0.26019 0.01621  -0.00077 0.00421  385 GLU A OE1 
3044 O OE2 . GLU A 385 ? 0.22222 0.22298 0.25846 0.01799  0.00462  0.00011  385 GLU A OE2 
3045 N N   . HIS A 386 ? 0.11553 0.10378 0.11968 0.01402  0.00569  -0.00134 386 HIS A N   
3046 C CA  . HIS A 386 ? 0.11511 0.10474 0.11675 0.01328  0.00809  -0.00300 386 HIS A CA  
3047 C C   . HIS A 386 ? 0.10157 0.08890 0.09710 0.01267  0.00880  -0.00374 386 HIS A C   
3048 O O   . HIS A 386 ? 0.12995 0.11827 0.12383 0.01233  0.01086  -0.00530 386 HIS A O   
3049 C CB  . HIS A 386 ? 0.10909 0.10066 0.11027 0.01198  0.00753  -0.00192 386 HIS A CB  
3050 C CG  . HIS A 386 ? 0.12306 0.11771 0.13073 0.01233  0.00698  -0.00126 386 HIS A CG  
3051 N ND1 . HIS A 386 ? 0.12792 0.12588 0.14045 0.01291  0.00935  -0.00267 386 HIS A ND1 
3052 C CD2 . HIS A 386 ? 0.12201 0.11729 0.13230 0.01210  0.00430  0.00063  386 HIS A CD2 
3053 C CE1 . HIS A 386 ? 0.13839 0.13898 0.15697 0.01317  0.00820  -0.00160 386 HIS A CE1 
3054 N NE2 . HIS A 386 ? 0.12244 0.12144 0.13971 0.01264  0.00492  0.00052  386 HIS A NE2 
3055 N N   . LEU A 387 ? 0.08792 0.07256 0.08012 0.01241  0.00717  -0.00260 387 LEU A N   
3056 C CA  . LEU A 387 ? 0.11238 0.09526 0.09958 0.01186  0.00776  -0.00316 387 LEU A CA  
3057 C C   . LEU A 387 ? 0.10614 0.08839 0.09391 0.01250  0.00918  -0.00496 387 LEU A C   
3058 O O   . LEU A 387 ? 0.11033 0.09136 0.10095 0.01337  0.00874  -0.00501 387 LEU A O   
3059 C CB  . LEU A 387 ? 0.10409 0.08467 0.08816 0.01144  0.00601  -0.00172 387 LEU A CB  
3060 C CG  . LEU A 387 ? 0.08699 0.06753 0.06849 0.01042  0.00495  -0.00076 387 LEU A CG  
3061 C CD1 . LEU A 387 ? 0.10120 0.07972 0.07959 0.01003  0.00365  0.00016  387 LEU A CD1 
3062 C CD2 . LEU A 387 ? 0.11057 0.09146 0.08970 0.00979  0.00615  -0.00145 387 LEU A CD2 
3063 N N   . ILE A 388 ? 0.09957 0.08257 0.08468 0.01193  0.01070  -0.00633 388 ILE A N   
3064 C CA  . ILE A 388 ? 0.13923 0.12164 0.12413 0.01218  0.01191  -0.00837 388 ILE A CA  
3065 C C   . ILE A 388 ? 0.10941 0.08926 0.09189 0.01198  0.01089  -0.00787 388 ILE A C   
3066 O O   . ILE A 388 ? 0.10720 0.08596 0.09040 0.01218  0.01138  -0.00934 388 ILE A O   
3067 C CB  . ILE A 388 ? 0.12347 0.10799 0.10582 0.01132  0.01367  -0.00990 388 ILE A CB  
3068 C CG1 . ILE A 388 ? 0.14979 0.13409 0.12758 0.01022  0.01290  -0.00842 388 ILE A CG1 
3069 C CG2 . ILE A 388 ? 0.12361 0.11113 0.10860 0.01135  0.01512  -0.01045 388 ILE A CG2 
3070 C CD1 . ILE A 388 ? 0.13891 0.12530 0.11375 0.00912  0.01416  -0.00918 388 ILE A CD1 
3071 N N   . ASP A 389 ? 0.09555 0.07447 0.07544 0.01149  0.00963  -0.00604 389 ASP A N   
3072 C CA  . ASP A 389 ? 0.10709 0.08404 0.08508 0.01125  0.00889  -0.00541 389 ASP A CA  
3073 C C   . ASP A 389 ? 0.08819 0.06367 0.06738 0.01152  0.00753  -0.00370 389 ASP A C   
3074 O O   . ASP A 389 ? 0.08839 0.06268 0.06541 0.01107  0.00695  -0.00271 389 ASP A O   
3075 C CB  . ASP A 389 ? 0.10194 0.07906 0.07633 0.01052  0.00872  -0.00481 389 ASP A CB  
3076 C CG  . ASP A 389 ? 0.09669 0.07410 0.07034 0.01031  0.00803  -0.00356 389 ASP A CG  
3077 O OD1 . ASP A 389 ? 0.13747 0.11538 0.11317 0.01056  0.00758  -0.00310 389 ASP A OD1 
3078 O OD2 . ASP A 389 ? 0.08619 0.06331 0.05762 0.00988  0.00785  -0.00311 389 ASP A OD2 
3079 N N   . GLN A 390 ? 0.10722 0.08303 0.08992 0.01219  0.00702  -0.00323 390 GLN A N   
3080 C CA  . GLN A 390 ? 0.09961 0.07438 0.08336 0.01227  0.00531  -0.00110 390 GLN A CA  
3081 C C   . GLN A 390 ? 0.12286 0.09547 0.10643 0.01211  0.00495  -0.00037 390 GLN A C   
3082 O O   . GLN A 390 ? 0.13071 0.10232 0.11751 0.01270  0.00536  -0.00120 390 GLN A O   
3083 C CB  . GLN A 390 ? 0.13885 0.11459 0.12768 0.01319  0.00470  -0.00069 390 GLN A CB  
3084 C CG  . GLN A 390 ? 0.15557 0.13024 0.14617 0.01329  0.00255  0.00190  390 GLN A CG  
3085 C CD  . GLN A 390 ? 0.17771 0.15066 0.17277 0.01421  0.00246  0.00201  390 GLN A CD  
3086 O OE1 . GLN A 390 ? 0.20622 0.17765 0.20201 0.01404  0.00078  0.00444  390 GLN A OE1 
3087 N NE2 . GLN A 390 ? 0.14466 0.11778 0.14270 0.01506  0.00428  -0.00062 390 GLN A NE2 
3088 N N   . ASP A 391 ? 0.10939 0.08130 0.08939 0.01123  0.00433  0.00102  391 ASP A N   
3089 C CA  . ASP A 391 ? 0.12368 0.09389 0.10325 0.01074  0.00404  0.00219  391 ASP A CA  
3090 C C   . ASP A 391 ? 0.12710 0.09689 0.10618 0.01026  0.00228  0.00499  391 ASP A C   
3091 O O   . ASP A 391 ? 0.10857 0.07933 0.08472 0.00970  0.00161  0.00565  391 ASP A O   
3092 C CB  . ASP A 391 ? 0.11075 0.08105 0.08669 0.00993  0.00504  0.00156  391 ASP A CB  
3093 C CG  . ASP A 391 ? 0.14765 0.11657 0.12393 0.00930  0.00515  0.00241  391 ASP A CG  
3094 O OD1 . ASP A 391 ? 0.14620 0.11427 0.12231 0.00876  0.00419  0.00471  391 ASP A OD1 
3095 O OD2 . ASP A 391 ? 0.19195 0.16076 0.16867 0.00915  0.00608  0.00095  391 ASP A OD2 
3096 N N   . HIS A 392 ? 0.11703 0.08527 0.09893 0.01034  0.00140  0.00666  392 HIS A N   
3097 C CA  . HIS A 392 ? 0.13772 0.10568 0.11952 0.00981  -0.00068 0.00987  392 HIS A CA  
3098 C C   . HIS A 392 ? 0.11561 0.08415 0.09137 0.00824  -0.00082 0.01108  392 HIS A C   
3099 O O   . HIS A 392 ? 0.11290 0.08251 0.08630 0.00763  -0.00219 0.01229  392 HIS A O   
3100 C CB  . HIS A 392 ? 0.12843 0.09421 0.11432 0.00999  -0.00153 0.01177  392 HIS A CB  
3101 C CG  . HIS A 392 ? 0.16164 0.12709 0.14748 0.00927  -0.00398 0.01574  392 HIS A CG  
3102 N ND1 . HIS A 392 ? 0.17731 0.14314 0.16752 0.01019  -0.00602 0.01737  392 HIS A ND1 
3103 C CD2 . HIS A 392 ? 0.17726 0.14236 0.15917 0.00759  -0.00478 0.01860  392 HIS A CD2 
3104 C CE1 . HIS A 392 ? 0.19980 0.16539 0.18862 0.00906  -0.00832 0.02129  392 HIS A CE1 
3105 N NE2 . HIS A 392 ? 0.18096 0.14613 0.16440 0.00738  -0.00750 0.02208  392 HIS A NE2 
3106 N N   . TYR A 393 ? 0.10758 0.07565 0.08093 0.00748  0.00065  0.01056  393 TYR A N   
3107 C CA  . TYR A 393 ? 0.11330 0.08211 0.08131 0.00600  0.00100  0.01145  393 TYR A CA  
3108 C C   . TYR A 393 ? 0.11690 0.08710 0.08161 0.00602  0.00200  0.00913  393 TYR A C   
3109 O O   . TYR A 393 ? 0.11215 0.08312 0.07265 0.00497  0.00180  0.00954  393 TYR A O   
3110 C CB  . TYR A 393 ? 0.11691 0.08509 0.08445 0.00517  0.00238  0.01180  393 TYR A CB  
3111 C CG  . TYR A 393 ? 0.12483 0.09136 0.09488 0.00459  0.00126  0.01476  393 TYR A CG  
3112 C CD1 . TYR A 393 ? 0.15181 0.11809 0.12147 0.00401  -0.00089 0.01797  393 TYR A CD1 
3113 C CD2 . TYR A 393 ? 0.14980 0.11498 0.12288 0.00449  0.00212  0.01453  393 TYR A CD2 
3114 C CE1 . TYR A 393 ? 0.13803 0.10256 0.11045 0.00346  -0.00215 0.02117  393 TYR A CE1 
3115 C CE2 . TYR A 393 ? 0.16133 0.12457 0.13725 0.00387  0.00102  0.01737  393 TYR A CE2 
3116 C CZ  . TYR A 393 ? 0.15737 0.12020 0.13306 0.00341  -0.00111 0.02084  393 TYR A CZ  
3117 O OH  . TYR A 393 ? 0.14651 0.10718 0.12546 0.00278  -0.00242 0.02414  393 TYR A OH  
3118 N N   . LEU A 394 ? 0.10278 0.07324 0.06927 0.00707  0.00304  0.00671  394 LEU A N   
3119 C CA  . LEU A 394 ? 0.11383 0.08522 0.07788 0.00710  0.00391  0.00480  394 LEU A CA  
3120 C C   . LEU A 394 ? 0.11041 0.08241 0.07415 0.00716  0.00260  0.00477  394 LEU A C   
3121 O O   . LEU A 394 ? 0.11517 0.08757 0.07581 0.00653  0.00265  0.00404  394 LEU A O   
3122 C CB  . LEU A 394 ? 0.09416 0.06575 0.06008 0.00795  0.00521  0.00280  394 LEU A CB  
3123 C CG  . LEU A 394 ? 0.10546 0.07668 0.07240 0.00781  0.00622  0.00262  394 LEU A CG  
3124 C CD1 . LEU A 394 ? 0.11851 0.09030 0.08671 0.00841  0.00708  0.00073  394 LEU A CD1 
3125 C CD2 . LEU A 394 ? 0.09552 0.06708 0.05980 0.00683  0.00706  0.00323  394 LEU A CD2 
3126 N N   . ASN A 395 ? 0.09651 0.06866 0.06388 0.00789  0.00150  0.00537  395 ASN A N   
3127 C CA  . ASN A 395 ? 0.11193 0.08506 0.07995 0.00786  0.00010  0.00556  395 ASN A CA  
3128 C C   . ASN A 395 ? 0.13429 0.10766 0.09925 0.00659  -0.00172 0.00736  395 ASN A C   
3129 O O   . ASN A 395 ? 0.15071 0.12490 0.11434 0.00598  -0.00277 0.00703  395 ASN A O   
3130 C CB  . ASN A 395 ? 0.12404 0.09763 0.09748 0.00899  -0.00049 0.00593  395 ASN A CB  
3131 C CG  . ASN A 395 ? 0.13437 0.10954 0.10981 0.00925  -0.00092 0.00520  395 ASN A CG  
3132 O OD1 . ASN A 395 ? 0.20020 0.17631 0.17680 0.00893  -0.00283 0.00656  395 ASN A OD1 
3133 N ND2 . ASN A 395 ? 0.15556 0.13124 0.13144 0.00965  0.00075  0.00327  395 ASN A ND2 
3134 N N   . ALA A 396 ? 0.13405 0.10677 0.09764 0.00594  -0.00219 0.00932  396 ALA A N   
3135 C CA  . ALA A 396 ? 0.13465 0.10785 0.09475 0.00444  -0.00409 0.01144  396 ALA A CA  
3136 C C   . ALA A 396 ? 0.11867 0.09212 0.07261 0.00306  -0.00290 0.01010  396 ALA A C   
3137 O O   . ALA A 396 ? 0.13782 0.11204 0.08844 0.00193  -0.00402 0.00974  396 ALA A O   
3138 C CB  . ALA A 396 ? 0.13852 0.11098 0.09989 0.00414  -0.00523 0.01464  396 ALA A CB  
3139 N N   . ALA A 397 ? 0.12417 0.09711 0.07684 0.00308  -0.00059 0.00913  397 ALA A N   
3140 C CA  . ALA A 397 ? 0.13629 0.10968 0.08382 0.00192  0.00095  0.00767  397 ALA A CA  
3141 C C   . ALA A 397 ? 0.12609 0.09953 0.07274 0.00221  0.00155  0.00469  397 ALA A C   
3142 O O   . ALA A 397 ? 0.14892 0.12269 0.09123 0.00105  0.00200  0.00332  397 ALA A O   
3143 C CB  . ALA A 397 ? 0.13250 0.10571 0.08030 0.00209  0.00337  0.00724  397 ALA A CB  
3144 N N   . ASN A 398 ? 0.13187 0.10494 0.08257 0.00360  0.00163  0.00362  398 ASN A N   
3145 C CA  . ASN A 398 ? 0.12584 0.09869 0.07634 0.00378  0.00199  0.00127  398 ASN A CA  
3146 C C   . ASN A 398 ? 0.11481 0.08812 0.06488 0.00297  -0.00028 0.00159  398 ASN A C   
3147 O O   . ASN A 398 ? 0.10835 0.08133 0.05651 0.00230  -0.00029 -0.00030 398 ASN A O   
3148 C CB  . ASN A 398 ? 0.10915 0.08170 0.06376 0.00525  0.00297  0.00038  398 ASN A CB  
3149 C CG  . ASN A 398 ? 0.09941 0.07171 0.05427 0.00585  0.00505  -0.00050 398 ASN A CG  
3150 O OD1 . ASN A 398 ? 0.09979 0.07179 0.05374 0.00593  0.00629  -0.00223 398 ASN A OD1 
3151 N ND2 . ASN A 398 ? 0.10988 0.08231 0.06655 0.00628  0.00537  0.00065  398 ASN A ND2 
3152 N N   . TRP A 399 ? 0.13510 0.10912 0.08747 0.00304  -0.00228 0.00387  399 TRP A N   
3153 C CA  . TRP A 399 ? 0.11779 0.09275 0.06986 0.00204  -0.00481 0.00455  399 TRP A CA  
3154 C C   . TRP A 399 ? 0.14020 0.11548 0.08633 0.00007  -0.00587 0.00491  399 TRP A C   
3155 O O   . TRP A 399 ? 0.12653 0.10228 0.07052 -0.00122 -0.00737 0.00401  399 TRP A O   
3156 C CB  . TRP A 399 ? 0.13594 0.11187 0.09287 0.00279  -0.00672 0.00706  399 TRP A CB  
3157 C CG  . TRP A 399 ? 0.13519 0.11178 0.09736 0.00393  -0.00653 0.00623  399 TRP A CG  
3158 C CD1 . TRP A 399 ? 0.13608 0.11263 0.10261 0.00553  -0.00510 0.00600  399 TRP A CD1 
3159 C CD2 . TRP A 399 ? 0.14660 0.12421 0.11004 0.00332  -0.00771 0.00547  399 TRP A CD2 
3160 N NE1 . TRP A 399 ? 0.11310 0.09083 0.08325 0.00593  -0.00509 0.00524  399 TRP A NE1 
3161 C CE2 . TRP A 399 ? 0.11774 0.09611 0.08638 0.00460  -0.00671 0.00505  399 TRP A CE2 
3162 C CE3 . TRP A 399 ? 0.14701 0.12505 0.10762 0.00161  -0.00949 0.00498  399 TRP A CE3 
3163 C CZ2 . TRP A 399 ? 0.12947 0.10914 0.10087 0.00422  -0.00732 0.00450  399 TRP A CZ2 
3164 C CZ3 . TRP A 399 ? 0.12784 0.10688 0.09145 0.00125  -0.01035 0.00430  399 TRP A CZ3 
3165 C CH2 . TRP A 399 ? 0.12450 0.10442 0.09362 0.00255  -0.00921 0.00423  399 TRP A CH2 
3166 N N   . MET A 400 ? 0.13957 0.11475 0.08280 -0.00043 -0.00510 0.00617  400 MET A N   
3167 C CA  . MET A 400 ? 0.16605 0.14184 0.10268 -0.00255 -0.00550 0.00623  400 MET A CA  
3168 C C   . MET A 400 ? 0.14189 0.11705 0.07495 -0.00296 -0.00297 0.00244  400 MET A C   
3169 O O   . MET A 400 ? 0.15795 0.13358 0.08562 -0.00479 -0.00332 0.00111  400 MET A O   
3170 C CB  . MET A 400 ? 0.13560 0.11170 0.07045 -0.00315 -0.00530 0.00912  400 MET A CB  
3171 C CG  . MET A 400 ? 0.18581 0.16224 0.12425 -0.00289 -0.00814 0.01312  400 MET A CG  
3172 S SD  . MET A 400 ? 0.19736 0.17381 0.13350 -0.00407 -0.00827 0.01706  400 MET A SD  
3173 C CE  . MET A 400 ? 0.15822 0.13331 0.09748 -0.00244 -0.00450 0.01535  400 MET A CE  
3174 N N   . TRP A 401 ? 0.12739 0.10155 0.06351 -0.00132 -0.00049 0.00059  401 TRP A N   
3175 C CA  . TRP A 401 ? 0.15340 0.12678 0.08774 -0.00131 0.00179  -0.00300 401 TRP A CA  
3176 C C   . TRP A 401 ? 0.13851 0.11115 0.07306 -0.00176 0.00053  -0.00507 401 TRP A C   
3177 O O   . TRP A 401 ? 0.14510 0.11736 0.07574 -0.00301 0.00101  -0.00768 401 TRP A O   
3178 C CB  . TRP A 401 ? 0.15236 0.12503 0.09080 0.00060  0.00415  -0.00384 401 TRP A CB  
3179 C CG  . TRP A 401 ? 0.15650 0.12845 0.09424 0.00092  0.00660  -0.00715 401 TRP A CG  
3180 C CD1 . TRP A 401 ? 0.16958 0.14022 0.10789 0.00102  0.00666  -0.00978 401 TRP A CD1 
3181 C CD2 . TRP A 401 ? 0.20619 0.17866 0.14346 0.00128  0.00936  -0.00814 401 TRP A CD2 
3182 N NE1 . TRP A 401 ? 0.18287 0.15299 0.12126 0.00159  0.00926  -0.01241 401 TRP A NE1 
3183 C CE2 . TRP A 401 ? 0.21581 0.18730 0.15366 0.00179  0.01101  -0.01149 401 TRP A CE2 
3184 C CE3 . TRP A 401 ? 0.18642 0.16014 0.12337 0.00118  0.01059  -0.00648 401 TRP A CE3 
3185 C CZ2 . TRP A 401 ? 0.19929 0.17131 0.13773 0.00239  0.01391  -0.01329 401 TRP A CZ2 
3186 C CZ3 . TRP A 401 ? 0.21881 0.19325 0.15602 0.00153  0.01348  -0.00819 401 TRP A CZ3 
3187 C CH2 . TRP A 401 ? 0.22886 0.20260 0.16696 0.00223  0.01514  -0.01160 401 TRP A CH2 
3188 N N   . LEU A 402 ? 0.13811 0.11060 0.07733 -0.00088 -0.00097 -0.00408 402 LEU A N   
3189 C CA  . LEU A 402 ? 0.12814 0.09993 0.06843 -0.00138 -0.00209 -0.00581 402 LEU A CA  
3190 C C   . LEU A 402 ? 0.15274 0.12552 0.08968 -0.00348 -0.00487 -0.00544 402 LEU A C   
3191 O O   . LEU A 402 ? 0.13766 0.10970 0.07348 -0.00462 -0.00558 -0.00773 402 LEU A O   
3192 C CB  . LEU A 402 ? 0.13778 0.10964 0.08408 -0.00002 -0.00259 -0.00468 402 LEU A CB  
3193 C CG  . LEU A 402 ? 0.12110 0.09159 0.07039 0.00138  -0.00047 -0.00611 402 LEU A CG  
3194 C CD1 . LEU A 402 ? 0.14088 0.10961 0.08920 0.00065  -0.00008 -0.00896 402 LEU A CD1 
3195 C CD2 . LEU A 402 ? 0.12691 0.09724 0.07580 0.00251  0.00177  -0.00608 402 LEU A CD2 
3196 N N   . SER A 403 ? 0.13759 0.11199 0.07315 -0.00413 -0.00667 -0.00249 403 SER A N   
3197 C CA  . SER A 403 ? 0.13817 0.11393 0.07024 -0.00631 -0.00973 -0.00160 403 SER A CA  
3198 C C   . SER A 403 ? 0.16091 0.13687 0.08515 -0.00833 -0.00909 -0.00297 403 SER A C   
3199 O O   . SER A 403 ? 0.16653 0.14385 0.08660 -0.01051 -0.01173 -0.00215 403 SER A O   
3200 C CB  . SER A 403 ? 0.15927 0.13677 0.09415 -0.00607 -0.01238 0.00268  403 SER A CB  
3201 O OG  . SER A 403 ? 0.13706 0.11460 0.07082 -0.00555 -0.01127 0.00482  403 SER A OG  
3202 N N   . ALA A 404 ? 0.15383 0.12882 0.07608 -0.00773 -0.00565 -0.00504 404 ALA A N   
3203 C CA  . ALA A 404 ? 0.18246 0.15796 0.09743 -0.00955 -0.00418 -0.00680 404 ALA A CA  
3204 C C   . ALA A 404 ? 0.19629 0.17386 0.10690 -0.01124 -0.00598 -0.00303 404 ALA A C   
3205 O O   . ALA A 404 ? 0.21773 0.19646 0.12122 -0.01372 -0.00646 -0.00376 404 ALA A O   
3206 C CB  . ALA A 404 ? 0.17533 0.15016 0.08637 -0.01135 -0.00459 -0.01083 404 ALA A CB  
3207 N N   . SER A 405 ? 0.17569 0.15367 0.09049 -0.01001 -0.00700 0.00102  405 SER A N   
3208 C CA  . SER A 405 ? 0.20929 0.18883 0.12111 -0.01139 -0.00877 0.00524  405 SER A CA  
3209 C C   . SER A 405 ? 0.18011 0.15976 0.09026 -0.01124 -0.00577 0.00614  405 SER A C   
3210 O O   . SER A 405 ? 0.21061 0.19164 0.11608 -0.01314 -0.00654 0.00900  405 SER A O   
3211 C CB  . SER A 405 ? 0.20761 0.18741 0.12571 -0.01021 -0.01192 0.00933  405 SER A CB  
3212 O OG  . SER A 405 ? 0.18355 0.16391 0.10356 -0.01058 -0.01486 0.00892  405 SER A OG  
3213 N N   . ALA A 406 ? 0.19601 0.17444 0.10994 -0.00922 -0.00253 0.00403  406 ALA A N   
3214 C CA  . ALA A 406 ? 0.20077 0.17954 0.11399 -0.00909 0.00041  0.00465  406 ALA A CA  
3215 C C   . ALA A 406 ? 0.21737 0.19518 0.13334 -0.00735 0.00393  0.00070  406 ALA A C   
3216 O O   . ALA A 406 ? 0.22980 0.20628 0.14987 -0.00577 0.00372  -0.00131 406 ALA A O   
3217 C CB  . ALA A 406 ? 0.20709 0.18551 0.12503 -0.00810 -0.00068 0.00892  406 ALA A CB  
3218 N N   . PHE A 407 ? 0.23021 0.20895 0.14410 -0.00776 0.00712  -0.00017 407 PHE A N   
3219 C CA  . PHE A 407 ? 0.21602 0.19432 0.13297 -0.00613 0.01051  -0.00352 407 PHE A CA  
3220 C C   . PHE A 407 ? 0.24365 0.22107 0.15940 -0.00597 0.01138  -0.00808 407 PHE A C   
3221 O O   . PHE A 407 ? 0.32872 0.30679 0.24225 -0.00632 0.01441  -0.01128 407 PHE A O   
3222 C CB  . PHE A 407 ? 0.22613 0.20319 0.15052 -0.00371 0.01026  -0.00245 407 PHE A CB  
3223 C CG  . PHE A 407 ? 0.21125 0.18854 0.13767 -0.00375 0.00907  0.00167  407 PHE A CG  
3224 C CD1 . PHE A 407 ? 0.19550 0.17406 0.12051 -0.00474 0.01085  0.00324  407 PHE A CD1 
3225 C CD2 . PHE A 407 ? 0.20664 0.18285 0.13687 -0.00283 0.00633  0.00387  407 PHE A CD2 
3226 C CE1 . PHE A 407 ? 0.19877 0.17708 0.12616 -0.00488 0.00966  0.00703  407 PHE A CE1 
3227 C CE2 . PHE A 407 ? 0.18966 0.16567 0.12240 -0.00275 0.00530  0.00731  407 PHE A CE2 
3228 C CZ  . PHE A 407 ? 0.20584 0.18266 0.13717 -0.00381 0.00684  0.00895  407 PHE A CZ  
3229 N N   . PHE A 408 ? 0.21789 0.19384 0.13563 -0.00546 0.00889  -0.00852 408 PHE A N   
3230 C CA  . PHE A 408 ? 0.22424 0.19884 0.14151 -0.00543 0.00930  -0.01262 408 PHE A CA  
3231 C C   . PHE A 408 ? 0.24670 0.22194 0.15727 -0.00806 0.00753  -0.01352 408 PHE A C   
3232 O O   . PHE A 408 ? 0.24084 0.21705 0.14940 -0.00934 0.00447  -0.01027 408 PHE A O   
3233 C CB  . PHE A 408 ? 0.21508 0.18786 0.13846 -0.00369 0.00765  -0.01249 408 PHE A CB  
3234 C CG  . PHE A 408 ? 0.22966 0.20056 0.15388 -0.00350 0.00813  -0.01642 408 PHE A CG  
3235 C CD1 . PHE A 408 ? 0.24501 0.21492 0.17139 -0.00224 0.01114  -0.01951 408 PHE A CD1 
3236 C CD2 . PHE A 408 ? 0.21080 0.18088 0.13443 -0.00457 0.00545  -0.01690 408 PHE A CD2 
3237 C CE1 . PHE A 408 ? 0.21134 0.17905 0.13924 -0.00199 0.01147  -0.02302 408 PHE A CE1 
3238 C CE2 . PHE A 408 ? 0.25630 0.22428 0.18116 -0.00455 0.00580  -0.02045 408 PHE A CE2 
3239 C CZ  . PHE A 408 ? 0.23028 0.19685 0.15729 -0.00322 0.00882  -0.02351 408 PHE A CZ  
3240 N N   . SER A 409 ? 0.20463 0.17935 0.11196 -0.00888 0.00937  -0.01805 409 SER A N   
3241 C CA  . SER A 409 ? 0.23933 0.21483 0.13932 -0.01172 0.00798  -0.01960 409 SER A CA  
3242 C C   . SER A 409 ? 0.23394 0.20733 0.13381 -0.01206 0.00805  -0.02454 409 SER A C   
3243 O O   . SER A 409 ? 0.23361 0.20755 0.12705 -0.01462 0.00704  -0.02664 409 SER A O   
3244 C CB  . SER A 409 ? 0.22541 0.20327 0.11839 -0.01361 0.01060  -0.02029 409 SER A CB  
3245 O OG  . SER A 409 ? 0.27221 0.24979 0.16704 -0.01227 0.01506  -0.02403 409 SER A OG  
3246 N N   . GLN A 410 ? 0.24022 0.21116 0.14683 -0.00976 0.00903  -0.02639 410 GLN A N   
3247 C CA  . GLN A 410 ? 0.23216 0.20056 0.13953 -0.01002 0.00918  -0.03103 410 GLN A CA  
3248 C C   . GLN A 410 ? 0.20969 0.17701 0.11978 -0.01046 0.00518  -0.02935 410 GLN A C   
3249 O O   . GLN A 410 ? 0.22745 0.19298 0.14425 -0.00866 0.00470  -0.02866 410 GLN A O   
3250 C CB  . GLN A 410 ? 0.23054 0.19686 0.14404 -0.00743 0.01237  -0.03369 410 GLN A CB  
3251 C CG  . GLN A 410 ? 0.22678 0.19009 0.14128 -0.00766 0.01306  -0.03889 410 GLN A CG  
3252 C CD  . GLN A 410 ? 0.20085 0.16481 0.10761 -0.01014 0.01443  -0.04334 410 GLN A CD  
3253 O OE1 . GLN A 410 ? 0.25753 0.22032 0.16108 -0.01222 0.01241  -0.04571 410 GLN A OE1 
3254 N NE2 . GLN A 410 ? 0.23072 0.19679 0.13435 -0.01012 0.01794  -0.04461 410 GLN A NE2 
3255 N N   . TYR A 411 ? 0.23948 0.20825 0.14423 -0.01308 0.00220  -0.02851 411 TYR A N   
3256 C CA  . TYR A 411 ? 0.22826 0.19669 0.13561 -0.01382 -0.00174 -0.02686 411 TYR A CA  
3257 C C   . TYR A 411 ? 0.23187 0.19748 0.14077 -0.01451 -0.00207 -0.03125 411 TYR A C   
3258 O O   . TYR A 411 ? 0.25018 0.21528 0.16280 -0.01489 -0.00494 -0.03005 411 TYR A O   
3259 C CB  . TYR A 411 ? 0.24052 0.21175 0.14221 -0.01644 -0.00523 -0.02417 411 TYR A CB  
3260 C CG  . TYR A 411 ? 0.25638 0.22849 0.14897 -0.01942 -0.00490 -0.02748 411 TYR A CG  
3261 C CD1 . TYR A 411 ? 0.26881 0.23989 0.15867 -0.02168 -0.00666 -0.03122 411 TYR A CD1 
3262 C CD2 . TYR A 411 ? 0.26787 0.24198 0.15441 -0.02020 -0.00277 -0.02693 411 TYR A CD2 
3263 C CE1 . TYR A 411 ? 0.28115 0.25316 0.16203 -0.02463 -0.00628 -0.03467 411 TYR A CE1 
3264 C CE2 . TYR A 411 ? 0.30053 0.27583 0.17805 -0.02316 -0.00221 -0.03006 411 TYR A CE2 
3265 C CZ  . TYR A 411 ? 0.27775 0.25200 0.15224 -0.02536 -0.00396 -0.03408 411 TYR A CZ  
3266 O OH  . TYR A 411 ? 0.28378 0.25933 0.14868 -0.02853 -0.00332 -0.03761 411 TYR A OH  
3267 N N   . PHE A 412 ? 0.24031 0.20410 0.14694 -0.01472 0.00086  -0.03633 412 PHE A N   
3268 C CA  . PHE A 412 ? 0.23728 0.19767 0.14646 -0.01513 0.00077  -0.04068 412 PHE A CA  
3269 C C   . PHE A 412 ? 0.20038 0.15818 0.11867 -0.01239 0.00155  -0.03973 412 PHE A C   
3270 O O   . PHE A 412 ? 0.19271 0.14765 0.11462 -0.01275 0.00059  -0.04182 412 PHE A O   
3271 C CB  . PHE A 412 ? 0.20441 0.16346 0.10904 -0.01598 0.00396  -0.04676 412 PHE A CB  
3272 C CG  . PHE A 412 ? 0.27228 0.23346 0.16721 -0.01946 0.00279  -0.04872 412 PHE A CG  
3273 C CD1 . PHE A 412 ? 0.28143 0.24190 0.17384 -0.02223 -0.00056 -0.05060 412 PHE A CD1 
3274 C CD2 . PHE A 412 ? 0.29987 0.26397 0.18808 -0.02020 0.00497  -0.04857 412 PHE A CD2 
3275 C CE1 . PHE A 412 ? 0.30279 0.26546 0.18574 -0.02570 -0.00195 -0.05233 412 PHE A CE1 
3276 C CE2 . PHE A 412 ? 0.26747 0.23380 0.14604 -0.02370 0.00383  -0.05011 412 PHE A CE2 
3277 C CZ  . PHE A 412 ? 0.30581 0.27145 0.18154 -0.02646 0.00025  -0.05202 412 PHE A CZ  
3278 N N   A ARG A 413 ? 0.21141 0.17015 0.13334 -0.00989 0.00313  -0.03652 413 ARG A N   
3279 N N   B ARG A 413 ? 0.21245 0.17119 0.13436 -0.00988 0.00315  -0.03655 413 ARG A N   
3280 C CA  A ARG A 413 ? 0.21644 0.17327 0.14636 -0.00746 0.00366  -0.03500 413 ARG A CA  
3281 C CA  B ARG A 413 ? 0.21628 0.17312 0.14619 -0.00746 0.00365  -0.03499 413 ARG A CA  
3282 C C   A ARG A 413 ? 0.21280 0.17095 0.14580 -0.00759 0.00054  -0.03055 413 ARG A C   
3283 C C   B ARG A 413 ? 0.21230 0.17048 0.14522 -0.00763 0.00051  -0.03055 413 ARG A C   
3284 O O   A ARG A 413 ? 0.19230 0.15303 0.12519 -0.00690 0.00003  -0.02676 413 ARG A O   
3285 O O   B ARG A 413 ? 0.18877 0.14956 0.12145 -0.00700 -0.00005 -0.02677 413 ARG A O   
3286 C CB  A ARG A 413 ? 0.21215 0.16966 0.14430 -0.00496 0.00669  -0.03393 413 ARG A CB  
3287 C CB  B ARG A 413 ? 0.21210 0.16964 0.14427 -0.00495 0.00665  -0.03386 413 ARG A CB  
3288 C CG  A ARG A 413 ? 0.20353 0.15940 0.14335 -0.00260 0.00709  -0.03214 413 ARG A CG  
3289 C CG  B ARG A 413 ? 0.20362 0.15985 0.14334 -0.00264 0.00681  -0.03154 413 ARG A CG  
3290 C CD  A ARG A 413 ? 0.20851 0.16051 0.15226 -0.00226 0.00777  -0.03562 413 ARG A CD  
3291 C CD  B ARG A 413 ? 0.20868 0.16108 0.15286 -0.00215 0.00739  -0.03458 413 ARG A CD  
3292 N NE  A ARG A 413 ? 0.21528 0.16584 0.16610 -0.00021 0.00792  -0.03336 413 ARG A NE  
3293 N NE  B ARG A 413 ? 0.22319 0.17451 0.17406 -0.00050 0.00684  -0.03165 413 ARG A NE  
3294 C CZ  A ARG A 413 ? 0.22653 0.17622 0.18104 -0.00049 0.00575  -0.03089 413 ARG A CZ  
3295 C CZ  B ARG A 413 ? 0.21788 0.16923 0.17264 0.00176  0.00857  -0.03040 413 ARG A CZ  
3296 N NH1 A ARG A 413 ? 0.22278 0.17292 0.17545 -0.00257 0.00325  -0.03043 413 ARG A NH1 
3297 N NH1 B ARG A 413 ? 0.23081 0.18329 0.18428 0.00282  0.01110  -0.03180 413 ARG A NH1 
3298 N NH2 A ARG A 413 ? 0.22025 0.16890 0.18047 0.00123  0.00606  -0.02869 413 ARG A NH2 
3299 N NH2 B ARG A 413 ? 0.22528 0.17581 0.18534 0.00281  0.00769  -0.02756 413 ARG A NH2 
3300 N N   . VAL A 414 ? 0.20859 0.16499 0.14477 -0.00852 -0.00142 -0.03112 414 VAL A N   
3301 C CA  . VAL A 414 ? 0.20924 0.16715 0.14891 -0.00886 -0.00417 -0.02736 414 VAL A CA  
3302 C C   . VAL A 414 ? 0.21445 0.17020 0.16113 -0.00742 -0.00359 -0.02646 414 VAL A C   
3303 O O   . VAL A 414 ? 0.23136 0.18385 0.18023 -0.00785 -0.00327 -0.02922 414 VAL A O   
3304 C CB  . VAL A 414 ? 0.21574 0.17432 0.15306 -0.01174 -0.00743 -0.02821 414 VAL A CB  
3305 C CG1 . VAL A 414 ? 0.20107 0.16138 0.14348 -0.01192 -0.00993 -0.02452 414 VAL A CG1 
3306 C CG2 . VAL A 414 ? 0.22340 0.18459 0.15339 -0.01335 -0.00842 -0.02826 414 VAL A CG2 
3307 N N   . TYR A 415 ? 0.20847 0.16597 0.15861 -0.00585 -0.00348 -0.02260 415 TYR A N   
3308 C CA  . TYR A 415 ? 0.18330 0.13941 0.13948 -0.00481 -0.00312 -0.02108 415 TYR A CA  
3309 C C   . TYR A 415 ? 0.18495 0.14085 0.14398 -0.00669 -0.00550 -0.02056 415 TYR A C   
3310 O O   . TYR A 415 ? 0.18256 0.14095 0.14031 -0.00813 -0.00767 -0.01952 415 TYR A O   
3311 C CB  . TYR A 415 ? 0.18423 0.14271 0.14250 -0.00299 -0.00238 -0.01739 415 TYR A CB  
3312 C CG  . TYR A 415 ? 0.19756 0.15633 0.15401 -0.00122 -0.00011 -0.01760 415 TYR A CG  
3313 C CD1 . TYR A 415 ? 0.20247 0.15883 0.15864 -0.00048 0.00180  -0.02040 415 TYR A CD1 
3314 C CD2 . TYR A 415 ? 0.17405 0.13551 0.12965 -0.00029 0.00014  -0.01508 415 TYR A CD2 
3315 C CE1 . TYR A 415 ? 0.18062 0.13772 0.13576 0.00105  0.00391  -0.02052 415 TYR A CE1 
3316 C CE2 . TYR A 415 ? 0.21909 0.18092 0.17339 0.00109  0.00211  -0.01519 415 TYR A CE2 
3317 C CZ  . TYR A 415 ? 0.21320 0.17307 0.16729 0.00171  0.00398  -0.01782 415 TYR A CZ  
3318 O OH  . TYR A 415 ? 0.26522 0.22591 0.21864 0.00300  0.00598  -0.01786 415 TYR A OH  
3319 N N   . SER A 416 ? 0.17149 0.12450 0.13487 -0.00672 -0.00522 -0.02106 416 SER A N   
3320 C CA  . SER A 416 ? 0.18075 0.13343 0.14762 -0.00865 -0.00727 -0.02039 416 SER A CA  
3321 C C   . SER A 416 ? 0.15262 0.10765 0.12386 -0.00795 -0.00726 -0.01617 416 SER A C   
3322 O O   . SER A 416 ? 0.14782 0.10187 0.12146 -0.00637 -0.00563 -0.01472 416 SER A O   
3323 C CB  . SER A 416 ? 0.17539 0.12338 0.14490 -0.00937 -0.00706 -0.02311 416 SER A CB  
3324 O OG  . SER A 416 ? 0.16990 0.11753 0.14337 -0.01140 -0.00901 -0.02210 416 SER A OG  
3325 N N   . PRO A 417 ? 0.15080 0.10917 0.12333 -0.00913 -0.00901 -0.01415 417 PRO A N   
3326 C CA  . PRO A 417 ? 0.15785 0.11880 0.13463 -0.00857 -0.00857 -0.01054 417 PRO A CA  
3327 C C   . PRO A 417 ? 0.17856 0.13753 0.16008 -0.00954 -0.00847 -0.00958 417 PRO A C   
3328 O O   . PRO A 417 ? 0.17326 0.13451 0.15803 -0.00940 -0.00788 -0.00660 417 PRO A O   
3329 C CB  . PRO A 417 ? 0.15043 0.11548 0.12783 -0.00970 -0.01055 -0.00926 417 PRO A CB  
3330 C CG  . PRO A 417 ? 0.16534 0.12912 0.14032 -0.01180 -0.01275 -0.01199 417 PRO A CG  
3331 C CD  . PRO A 417 ? 0.17115 0.13144 0.14145 -0.01105 -0.01147 -0.01508 417 PRO A CD  
3332 N N   . VAL A 418 ? 0.18212 0.13690 0.16420 -0.01061 -0.00894 -0.01202 418 VAL A N   
3333 C CA  . VAL A 418 ? 0.20341 0.15570 0.19036 -0.01169 -0.00904 -0.01091 418 VAL A CA  
3334 C C   . VAL A 418 ? 0.19942 0.14759 0.18728 -0.01010 -0.00744 -0.01133 418 VAL A C   
3335 O O   . VAL A 418 ? 0.26261 0.20992 0.25428 -0.01011 -0.00698 -0.00858 418 VAL A O   
3336 C CB  . VAL A 418 ? 0.21686 0.16726 0.20540 -0.01449 -0.01122 -0.01309 418 VAL A CB  
3337 C CG1 . VAL A 418 ? 0.24907 0.19710 0.24334 -0.01591 -0.01146 -0.01131 418 VAL A CG1 
3338 C CG2 . VAL A 418 ? 0.19951 0.15438 0.18738 -0.01601 -0.01318 -0.01260 418 VAL A CG2 
3339 N N   . VAL A 419 ? 0.21311 0.15905 0.19779 -0.00879 -0.00657 -0.01448 419 VAL A N   
3340 C CA  . VAL A 419 ? 0.19915 0.14111 0.18568 -0.00723 -0.00519 -0.01530 419 VAL A CA  
3341 C C   . VAL A 419 ? 0.17176 0.11545 0.15656 -0.00460 -0.00337 -0.01399 419 VAL A C   
3342 O O   . VAL A 419 ? 0.19946 0.14101 0.18710 -0.00321 -0.00247 -0.01296 419 VAL A O   
3343 C CB  . VAL A 419 ? 0.17460 0.11241 0.16006 -0.00766 -0.00517 -0.02034 419 VAL A CB  
3344 C CG1 . VAL A 419 ? 0.21733 0.15038 0.20721 -0.00637 -0.00414 -0.02101 419 VAL A CG1 
3345 C CG2 . VAL A 419 ? 0.20568 0.14262 0.19139 -0.01060 -0.00729 -0.02223 419 VAL A CG2 
3346 N N   . PHE A 420 ? 0.17265 0.12007 0.15329 -0.00396 -0.00300 -0.01382 420 PHE A N   
3347 C CA  . PHE A 420 ? 0.15923 0.10812 0.13824 -0.00169 -0.00134 -0.01297 420 PHE A CA  
3348 C C   . PHE A 420 ? 0.15318 0.10314 0.13519 -0.00085 -0.00092 -0.00909 420 PHE A C   
3349 O O   . PHE A 420 ? 0.18498 0.13387 0.16821 0.00077  0.00008  -0.00851 420 PHE A O   
3350 C CB  . PHE A 420 ? 0.16949 0.12206 0.14405 -0.00151 -0.00130 -0.01304 420 PHE A CB  
3351 C CG  . PHE A 420 ? 0.16322 0.11715 0.13601 0.00054  0.00034  -0.01253 420 PHE A CG  
3352 C CD1 . PHE A 420 ? 0.20646 0.15908 0.17706 0.00144  0.00161  -0.01530 420 PHE A CD1 
3353 C CD2 . PHE A 420 ? 0.16660 0.12330 0.14001 0.00141  0.00072  -0.00949 420 PHE A CD2 
3354 C CE1 . PHE A 420 ? 0.21333 0.16747 0.18283 0.00313  0.00309  -0.01471 420 PHE A CE1 
3355 C CE2 . PHE A 420 ? 0.15965 0.11754 0.13167 0.00306  0.00203  -0.00914 420 PHE A CE2 
3356 C CZ  . PHE A 420 ? 0.19228 0.14894 0.16255 0.00389  0.00314  -0.01159 420 PHE A CZ  
3357 N N   . GLY A 421 ? 0.15254 0.10493 0.13581 -0.00206 -0.00168 -0.00638 421 GLY A N   
3358 C CA  . GLY A 421 ? 0.16543 0.11923 0.15075 -0.00168 -0.00119 -0.00275 421 GLY A CA  
3359 C C   . GLY A 421 ? 0.16331 0.11381 0.15277 -0.00225 -0.00162 -0.00124 421 GLY A C   
3360 O O   . GLY A 421 ? 0.14525 0.09633 0.13599 -0.00169 -0.00125 0.00174  421 GLY A O   
3361 N N   . LYS A 422 ? 0.17765 0.12460 0.16925 -0.00347 -0.00256 -0.00316 422 LYS A N   
3362 C CA  . LYS A 422 ? 0.17740 0.12064 0.17370 -0.00415 -0.00316 -0.00157 422 LYS A CA  
3363 C C   . LYS A 422 ? 0.19310 0.13341 0.19107 -0.00201 -0.00252 -0.00186 422 LYS A C   
3364 O O   . LYS A 422 ? 0.18759 0.12588 0.18948 -0.00201 -0.00299 0.00102  422 LYS A O   
3365 C CB  . LYS A 422 ? 0.21474 0.15468 0.21317 -0.00612 -0.00440 -0.00404 422 LYS A CB  
3366 C CG  . LYS A 422 ? 0.25017 0.18585 0.25417 -0.00717 -0.00524 -0.00226 422 LYS A CG  
3367 C CD  . LYS A 422 ? 0.28170 0.21444 0.28784 -0.00955 -0.00660 -0.00478 422 LYS A CD  
3368 C CE  . LYS A 422 ? 0.21742 0.15429 0.22291 -0.01189 -0.00745 -0.00326 422 LYS A CE  
3369 N NZ  . LYS A 422 ? 0.21306 0.14731 0.22101 -0.01452 -0.00910 -0.00553 422 LYS A NZ  
3370 N N   . LYS A 423 ? 0.18664 0.12694 0.18204 -0.00024 -0.00148 -0.00501 423 LYS A N   
3371 C CA  . LYS A 423 ? 0.19915 0.13701 0.19698 0.00189  -0.00074 -0.00563 423 LYS A CA  
3372 C C   . LYS A 423 ? 0.18294 0.12336 0.18118 0.00312  -0.00056 -0.00163 423 LYS A C   
3373 O O   . LYS A 423 ? 0.22076 0.15914 0.22283 0.00444  -0.00069 -0.00037 423 LYS A O   
3374 C CB  . LYS A 423 ? 0.20426 0.14202 0.19915 0.00319  0.00063  -0.01017 423 LYS A CB  
3375 C CG  . LYS A 423 ? 0.21132 0.14640 0.20527 0.00186  0.00044  -0.01458 423 LYS A CG  
3376 C CD  . LYS A 423 ? 0.22311 0.15888 0.21307 0.00284  0.00201  -0.01882 423 LYS A CD  
3377 C CE  . LYS A 423 ? 0.23396 0.16731 0.22209 0.00117  0.00172  -0.02340 423 LYS A CE  
3378 N NZ  . LYS A 423 ? 0.25237 0.18688 0.23565 0.00172  0.00337  -0.02740 423 LYS A NZ  
3379 N N   . TYR A 424 ? 0.15305 0.09793 0.14768 0.00268  -0.00036 0.00032  424 TYR A N   
3380 C CA  . TYR A 424 ? 0.16757 0.11520 0.16180 0.00345  -0.00026 0.00382  424 TYR A CA  
3381 C C   . TYR A 424 ? 0.17418 0.12274 0.16980 0.00174  -0.00116 0.00814  424 TYR A C   
3382 O O   . TYR A 424 ? 0.15165 0.10035 0.14891 0.00209  -0.00170 0.01142  424 TYR A O   
3383 C CB  . TYR A 424 ? 0.16599 0.11788 0.15550 0.00399  0.00070  0.00314  424 TYR A CB  
3384 C CG  . TYR A 424 ? 0.14445 0.09612 0.13209 0.00548  0.00172  -0.00043 424 TYR A CG  
3385 C CD1 . TYR A 424 ? 0.14239 0.09429 0.13087 0.00730  0.00234  -0.00051 424 TYR A CD1 
3386 C CD2 . TYR A 424 ? 0.14822 0.09983 0.13326 0.00487  0.00201  -0.00349 424 TYR A CD2 
3387 C CE1 . TYR A 424 ? 0.11930 0.07139 0.10616 0.00846  0.00357  -0.00364 424 TYR A CE1 
3388 C CE2 . TYR A 424 ? 0.14921 0.10092 0.13200 0.00593  0.00307  -0.00647 424 TYR A CE2 
3389 C CZ  . TYR A 424 ? 0.11284 0.06481 0.09659 0.00770  0.00403  -0.00657 424 TYR A CZ  
3390 O OH  . TYR A 424 ? 0.12997 0.08239 0.11159 0.00856  0.00536  -0.00941 424 TYR A OH  
3391 N N   . ASP A 425 ? 0.14624 0.09578 0.14131 -0.00024 -0.00137 0.00836  425 ASP A N   
3392 C CA  . ASP A 425 ? 0.18366 0.13507 0.17953 -0.00217 -0.00174 0.01234  425 ASP A CA  
3393 C C   . ASP A 425 ? 0.16107 0.10989 0.16017 -0.00421 -0.00261 0.01219  425 ASP A C   
3394 O O   . ASP A 425 ? 0.18653 0.13739 0.18472 -0.00560 -0.00249 0.01120  425 ASP A O   
3395 C CB  . ASP A 425 ? 0.16947 0.12620 0.16152 -0.00259 -0.00070 0.01287  425 ASP A CB  
3396 C CG  . ASP A 425 ? 0.18013 0.13959 0.17243 -0.00447 -0.00053 0.01690  425 ASP A CG  
3397 O OD1 . ASP A 425 ? 0.17423 0.13150 0.16938 -0.00554 -0.00143 0.01988  425 ASP A OD1 
3398 O OD2 . ASP A 425 ? 0.20220 0.16602 0.19195 -0.00491 0.00059  0.01711  425 ASP A OD2 
3399 N N   . PRO A 426 ? 0.17284 0.11712 0.17631 -0.00448 -0.00364 0.01322  426 PRO A N   
3400 C CA  . PRO A 426 ? 0.15947 0.10072 0.16646 -0.00660 -0.00459 0.01281  426 PRO A CA  
3401 C C   . PRO A 426 ? 0.20178 0.14583 0.20956 -0.00926 -0.00474 0.01662  426 PRO A C   
3402 O O   . PRO A 426 ? 0.17733 0.12064 0.18713 -0.01129 -0.00532 0.01579  426 PRO A O   
3403 C CB  . PRO A 426 ? 0.15162 0.08715 0.16364 -0.00589 -0.00557 0.01336  426 PRO A CB  
3404 C CG  . PRO A 426 ? 0.18844 0.12540 0.20004 -0.00427 -0.00547 0.01662  426 PRO A CG  
3405 C CD  . PRO A 426 ? 0.17399 0.11562 0.18003 -0.00287 -0.00413 0.01487  426 PRO A CD  
3406 N N   . GLU A 427 ? 0.18558 0.13308 0.19181 -0.00950 -0.00420 0.02066  427 GLU A N   
3407 C CA  . GLU A 427 ? 0.21163 0.16250 0.21821 -0.01213 -0.00384 0.02427  427 GLU A CA  
3408 C C   . GLU A 427 ? 0.18935 0.14593 0.19255 -0.01244 -0.00237 0.02289  427 GLU A C   
3409 O O   . GLU A 427 ? 0.20051 0.16051 0.20437 -0.01461 -0.00169 0.02521  427 GLU A O   
3410 C CB  . GLU A 427 ? 0.21158 0.16363 0.21774 -0.01260 -0.00390 0.02941  427 GLU A CB  
3411 C CG  . GLU A 427 ? 0.22277 0.16937 0.23371 -0.01288 -0.00566 0.03211  427 GLU A CG  
3412 C CD  . GLU A 427 ? 0.28294 0.22674 0.29860 -0.01556 -0.00649 0.03323  427 GLU A CD  
3413 O OE1 . GLU A 427 ? 0.32576 0.27327 0.34097 -0.01810 -0.00574 0.03559  427 GLU A OE1 
3414 O OE2 . GLU A 427 ? 0.28758 0.22556 0.30767 -0.01518 -0.00776 0.03152  427 GLU A OE2 
3415 N N   . GLY A 428 ? 0.14743 0.10518 0.14751 -0.01037 -0.00182 0.01929  428 GLY A N   
3416 C CA  . GLY A 428 ? 0.19913 0.16187 0.19679 -0.01039 -0.00062 0.01796  428 GLY A CA  
3417 C C   . GLY A 428 ? 0.18955 0.15713 0.18461 -0.01052 0.00097  0.02044  428 GLY A C   
3418 O O   . GLY A 428 ? 0.17455 0.14647 0.16965 -0.01161 0.00214  0.02071  428 GLY A O   
3419 N N   . ARG A 429 ? 0.17246 0.13960 0.16544 -0.00949 0.00104  0.02211  429 ARG A N   
3420 C CA  . ARG A 429 ? 0.17275 0.14452 0.16246 -0.00978 0.00250  0.02403  429 ARG A CA  
3421 C C   . ARG A 429 ? 0.17540 0.15064 0.16241 -0.00838 0.00389  0.02092  429 ARG A C   
3422 O O   . ARG A 429 ? 0.19089 0.17067 0.17637 -0.00912 0.00557  0.02148  429 ARG A O   
3423 C CB  . ARG A 429 ? 0.18421 0.15471 0.17222 -0.00897 0.00178  0.02627  429 ARG A CB  
3424 C CG  . ARG A 429 ? 0.19499 0.16150 0.18642 -0.01000 0.00009  0.02961  429 ARG A CG  
3425 C CD  . ARG A 429 ? 0.26010 0.22816 0.25324 -0.01303 0.00043  0.03308  429 ARG A CD  
3426 N NE  . ARG A 429 ? 0.23156 0.19533 0.22854 -0.01413 -0.00138 0.03657  429 ARG A NE  
3427 C CZ  . ARG A 429 ? 0.23784 0.20163 0.23738 -0.01693 -0.00152 0.04004  429 ARG A CZ  
3428 N NH1 . ARG A 429 ? 0.23519 0.20350 0.23398 -0.01896 0.00021  0.04041  429 ARG A NH1 
3429 N NH2 . ARG A 429 ? 0.24583 0.20506 0.24933 -0.01771 -0.00340 0.04327  429 ARG A NH2 
3430 N N   . PHE A 430 ? 0.15148 0.12466 0.13803 -0.00643 0.00332  0.01763  430 PHE A N   
3431 C CA  . PHE A 430 ? 0.17126 0.14720 0.15586 -0.00515 0.00434  0.01495  430 PHE A CA  
3432 C C   . PHE A 430 ? 0.16741 0.14599 0.15426 -0.00623 0.00482  0.01418  430 PHE A C   
3433 O O   . PHE A 430 ? 0.20151 0.18375 0.18766 -0.00574 0.00612  0.01317  430 PHE A O   
3434 C CB  . PHE A 430 ? 0.14624 0.11926 0.12981 -0.00314 0.00351  0.01212  430 PHE A CB  
3435 C CG  . PHE A 430 ? 0.15378 0.12907 0.13559 -0.00187 0.00425  0.00975  430 PHE A CG  
3436 C CD1 . PHE A 430 ? 0.14672 0.12388 0.12592 -0.00076 0.00524  0.00950  430 PHE A CD1 
3437 C CD2 . PHE A 430 ? 0.14753 0.12295 0.13048 -0.00190 0.00371  0.00788  430 PHE A CD2 
3438 C CE1 . PHE A 430 ? 0.13160 0.11038 0.10978 0.00039  0.00583  0.00747  430 PHE A CE1 
3439 C CE2 . PHE A 430 ? 0.15430 0.13158 0.13609 -0.00074 0.00413  0.00621  430 PHE A CE2 
3440 C CZ  . PHE A 430 ? 0.12215 0.10092 0.10176 0.00046  0.00526  0.00600  430 PHE A CZ  
3441 N N   . ILE A 431 ? 0.18154 0.15836 0.17160 -0.00771 0.00372  0.01460  431 ILE A N   
3442 C CA  . ILE A 431 ? 0.17394 0.15349 0.16686 -0.00887 0.00381  0.01400  431 ILE A CA  
3443 C C   . ILE A 431 ? 0.17437 0.15837 0.16877 -0.01063 0.00556  0.01647  431 ILE A C   
3444 O O   . ILE A 431 ? 0.17591 0.16423 0.17159 -0.01063 0.00682  0.01572  431 ILE A O   
3445 C CB  . ILE A 431 ? 0.15540 0.13151 0.15121 -0.01009 0.00183  0.01328  431 ILE A CB  
3446 C CG1 . ILE A 431 ? 0.17458 0.14689 0.16834 -0.00844 0.00053  0.01031  431 ILE A CG1 
3447 C CG2 . ILE A 431 ? 0.18550 0.16486 0.18482 -0.01159 0.00160  0.01301  431 ILE A CG2 
3448 C CD1 . ILE A 431 ? 0.14251 0.11141 0.13843 -0.00969 -0.00135 0.00881  431 ILE A CD1 
3449 N N   . ARG A 432 ? 0.15142 0.13460 0.14585 -0.01217 0.00575  0.01955  432 ARG A N   
3450 C CA  . ARG A 432 ? 0.16918 0.15683 0.16455 -0.01424 0.00762  0.02216  432 ARG A CA  
3451 C C   . ARG A 432 ? 0.16191 0.15404 0.15397 -0.01329 0.00998  0.02151  432 ARG A C   
3452 O O   . ARG A 432 ? 0.16306 0.16010 0.15617 -0.01456 0.01214  0.02219  432 ARG A O   
3453 C CB  . ARG A 432 ? 0.19897 0.18449 0.19449 -0.01617 0.00707  0.02607  432 ARG A CB  
3454 C CG  . ARG A 432 ? 0.18549 0.16586 0.18471 -0.01712 0.00476  0.02657  432 ARG A CG  
3455 C CD  . ARG A 432 ? 0.20226 0.18000 0.20195 -0.01870 0.00401  0.03073  432 ARG A CD  
3456 N NE  . ARG A 432 ? 0.22599 0.19756 0.22907 -0.01884 0.00168  0.03049  432 ARG A NE  
3457 C CZ  . ARG A 432 ? 0.22932 0.19925 0.23697 -0.02108 0.00078  0.03132  432 ARG A CZ  
3458 N NH1 . ARG A 432 ? 0.26290 0.23721 0.27266 -0.02343 0.00198  0.03275  432 ARG A NH1 
3459 N NH2 . ARG A 432 ? 0.22850 0.19234 0.23906 -0.02101 -0.00128 0.03051  432 ARG A NH2 
3460 N N   . LYS A 433 ? 0.14411 0.13474 0.13240 -0.01117 0.00975  0.01999  433 LYS A N   
3461 C CA  . LYS A 433 ? 0.17844 0.17284 0.16354 -0.01031 0.01184  0.01890  433 LYS A CA  
3462 C C   . LYS A 433 ? 0.16910 0.16645 0.15638 -0.00915 0.01298  0.01594  433 LYS A C   
3463 O O   . LYS A 433 ? 0.18886 0.19094 0.17698 -0.00977 0.01536  0.01567  433 LYS A O   
3464 C CB  . LYS A 433 ? 0.16219 0.15398 0.14328 -0.00854 0.01096  0.01816  433 LYS A CB  
3465 C CG  . LYS A 433 ? 0.19066 0.18531 0.16885 -0.00722 0.01263  0.01586  433 LYS A CG  
3466 C CD  . LYS A 433 ? 0.21959 0.21887 0.19551 -0.00889 0.01500  0.01705  433 LYS A CD  
3467 C CE  . LYS A 433 ? 0.22170 0.22348 0.19506 -0.00758 0.01673  0.01407  433 LYS A CE  
3468 N NZ  . LYS A 433 ? 0.23162 0.23818 0.20226 -0.00932 0.01937  0.01458  433 LYS A NZ  
3469 N N   . PHE A 434 ? 0.17157 0.16633 0.15998 -0.00746 0.01135  0.01376  434 PHE A N   
3470 C CA  . PHE A 434 ? 0.14874 0.14584 0.13942 -0.00614 0.01189  0.01134  434 PHE A CA  
3471 C C   . PHE A 434 ? 0.12979 0.12889 0.12577 -0.00731 0.01145  0.01161  434 PHE A C   
3472 O O   . PHE A 434 ? 0.16764 0.16972 0.16663 -0.00644 0.01206  0.01015  434 PHE A O   
3473 C CB  . PHE A 434 ? 0.16697 0.16069 0.15600 -0.00402 0.01022  0.00927  434 PHE A CB  
3474 C CG  . PHE A 434 ? 0.13088 0.12334 0.11552 -0.00275 0.01072  0.00868  434 PHE A CG  
3475 C CD1 . PHE A 434 ? 0.10048 0.09529 0.08419 -0.00156 0.01231  0.00701  434 PHE A CD1 
3476 C CD2 . PHE A 434 ? 0.14987 0.13883 0.13191 -0.00277 0.00954  0.00970  434 PHE A CD2 
3477 C CE1 . PHE A 434 ? 0.14864 0.14238 0.12850 -0.00066 0.01258  0.00637  434 PHE A CE1 
3478 C CE2 . PHE A 434 ? 0.13756 0.12579 0.11611 -0.00173 0.00979  0.00928  434 PHE A CE2 
3479 C CZ  . PHE A 434 ? 0.13800 0.12864 0.11526 -0.00079 0.01124  0.00761  434 PHE A CZ  
3480 N N   . LEU A 435 ? 0.15476 0.15226 0.15247 -0.00926 0.01026  0.01348  435 LEU A N   
3481 C CA  . LEU A 435 ? 0.16526 0.16499 0.16832 -0.01090 0.00980  0.01405  435 LEU A CA  
3482 C C   . LEU A 435 ? 0.15601 0.15723 0.16026 -0.01356 0.01098  0.01704  435 LEU A C   
3483 O O   . LEU A 435 ? 0.14715 0.14513 0.15241 -0.01519 0.00932  0.01862  435 LEU A O   
3484 C CB  . LEU A 435 ? 0.12251 0.11837 0.12687 -0.01100 0.00670  0.01310  435 LEU A CB  
3485 C CG  . LEU A 435 ? 0.15104 0.14600 0.15454 -0.00888 0.00530  0.01058  435 LEU A CG  
3486 C CD1 . LEU A 435 ? 0.10695 0.09818 0.11075 -0.00953 0.00234  0.00966  435 LEU A CD1 
3487 C CD2 . LEU A 435 ? 0.12436 0.12439 0.13183 -0.00822 0.00620  0.00991  435 LEU A CD2 
3488 N N   . PRO A 436 ? 0.17541 0.18151 0.17958 -0.01421 0.01395  0.01786  436 PRO A N   
3489 C CA  . PRO A 436 ? 0.17194 0.17980 0.17647 -0.01703 0.01530  0.02116  436 PRO A CA  
3490 C C   . PRO A 436 ? 0.16347 0.17280 0.17402 -0.01942 0.01471  0.02263  436 PRO A C   
3491 O O   . PRO A 436 ? 0.14117 0.15106 0.15240 -0.02207 0.01533  0.02581  436 PRO A O   
3492 C CB  . PRO A 436 ? 0.20638 0.21986 0.20917 -0.01700 0.01894  0.02080  436 PRO A CB  
3493 C CG  . PRO A 436 ? 0.19634 0.21197 0.20143 -0.01455 0.01952  0.01728  436 PRO A CG  
3494 C CD  . PRO A 436 ? 0.16895 0.17916 0.17275 -0.01251 0.01634  0.01570  436 PRO A CD  
3495 N N   . VAL A 437 ? 0.15581 0.16589 0.17084 -0.01878 0.01335  0.02070  437 VAL A N   
3496 C CA  . VAL A 437 ? 0.18694 0.19835 0.20802 -0.02121 0.01233  0.02195  437 VAL A CA  
3497 C C   . VAL A 437 ? 0.17827 0.18372 0.19897 -0.02286 0.00962  0.02349  437 VAL A C   
3498 O O   . VAL A 437 ? 0.17983 0.18582 0.20480 -0.02566 0.00915  0.02553  437 VAL A O   
3499 C CB  . VAL A 437 ? 0.16788 0.18138 0.19358 -0.02003 0.01090  0.01952  437 VAL A CB  
3500 C CG1 . VAL A 437 ? 0.18383 0.19182 0.20663 -0.01822 0.00767  0.01735  437 VAL A CG1 
3501 C CG2 . VAL A 437 ? 0.16533 0.18178 0.19810 -0.02273 0.01016  0.02083  437 VAL A CG2 
3502 N N   . LEU A 438 ? 0.17578 0.17554 0.19191 -0.02122 0.00794  0.02250  438 LEU A N   
3503 C CA  . LEU A 438 ? 0.17318 0.16676 0.18920 -0.02230 0.00550  0.02335  438 LEU A CA  
3504 C C   . LEU A 438 ? 0.17666 0.16778 0.18950 -0.02287 0.00619  0.02630  438 LEU A C   
3505 O O   . LEU A 438 ? 0.20699 0.19230 0.21908 -0.02276 0.00426  0.02660  438 LEU A O   
3506 C CB  . LEU A 438 ? 0.14272 0.13165 0.15653 -0.02014 0.00311  0.02006  438 LEU A CB  
3507 C CG  . LEU A 438 ? 0.11018 0.10025 0.12682 -0.02002 0.00135  0.01749  438 LEU A CG  
3508 C CD1 . LEU A 438 ? 0.14041 0.12752 0.15299 -0.01742 0.00003  0.01443  438 LEU A CD1 
3509 C CD2 . LEU A 438 ? 0.13093 0.11860 0.15173 -0.02272 -0.00086 0.01783  438 LEU A CD2 
3510 N N   . LYS A 439 ? 0.19257 0.18810 0.20364 -0.02350 0.00887  0.02846  439 LYS A N   
3511 C CA  . LYS A 439 ? 0.21135 0.20499 0.21865 -0.02399 0.00923  0.03148  439 LYS A CA  
3512 C C   . LYS A 439 ? 0.19982 0.19074 0.21016 -0.02696 0.00811  0.03539  439 LYS A C   
3513 O O   . LYS A 439 ? 0.23838 0.22568 0.24661 -0.02711 0.00716  0.03792  439 LYS A O   
3514 C CB  . LYS A 439 ? 0.19446 0.19389 0.19827 -0.02416 0.01240  0.03248  439 LYS A CB  
3515 C CG  . LYS A 439 ? 0.22404 0.22803 0.22962 -0.02754 0.01454  0.03616  439 LYS A CG  
3516 C CD  . LYS A 439 ? 0.20325 0.21165 0.21476 -0.02875 0.01568  0.03512  439 LYS A CD  
3517 C CE  . LYS A 439 ? 0.20809 0.22343 0.22004 -0.03125 0.01930  0.03747  439 LYS A CE  
3518 N NZ  . LYS A 439 ? 0.21926 0.23354 0.22874 -0.03406 0.01943  0.04245  439 LYS A NZ  
3519 N N   . ASP A 440 ? 0.18671 0.17921 0.20242 -0.02935 0.00801  0.03609  440 ASP A N   
3520 C CA  . ASP A 440 ? 0.20308 0.19264 0.22251 -0.03240 0.00678  0.03973  440 ASP A CA  
3521 C C   . ASP A 440 ? 0.17855 0.16188 0.20166 -0.03237 0.00361  0.03767  440 ASP A C   
3522 O O   . ASP A 440 ? 0.19242 0.17256 0.21949 -0.03492 0.00231  0.04016  440 ASP A O   
3523 C CB  . ASP A 440 ? 0.24930 0.24485 0.27270 -0.03566 0.00887  0.04224  440 ASP A CB  
3524 C CG  . ASP A 440 ? 0.24440 0.24573 0.26394 -0.03648 0.01221  0.04489  440 ASP A CG  
3525 O OD1 . ASP A 440 ? 0.21608 0.21547 0.23050 -0.03579 0.01214  0.04672  440 ASP A OD1 
3526 O OD2 . ASP A 440 ? 0.28930 0.29734 0.31102 -0.03788 0.01491  0.04505  440 ASP A OD2 
3527 N N   . MET A 441 ? 0.19937 0.18088 0.22117 -0.02976 0.00240  0.03318  441 MET A N   
3528 C CA  . MET A 441 ? 0.17819 0.15403 0.20257 -0.02978 -0.00043 0.03058  441 MET A CA  
3529 C C   . MET A 441 ? 0.16856 0.13738 0.19162 -0.02885 -0.00188 0.03122  441 MET A C   
3530 O O   . MET A 441 ? 0.16200 0.13014 0.18068 -0.02641 -0.00130 0.03103  441 MET A O   
3531 C CB  . MET A 441 ? 0.19683 0.17345 0.21951 -0.02744 -0.00115 0.02583  441 MET A CB  
3532 C CG  . MET A 441 ? 0.18800 0.15945 0.21244 -0.02770 -0.00396 0.02260  441 MET A CG  
3533 S SD  . MET A 441 ? 0.20234 0.17465 0.23384 -0.03170 -0.00551 0.02330  441 MET A SD  
3534 C CE  . MET A 441 ? 0.23378 0.21527 0.26688 -0.03177 -0.00387 0.02333  441 MET A CE  
3535 N N   . PRO A 442 ? 0.21145 0.17504 0.23875 -0.03072 -0.00379 0.03195  442 PRO A N   
3536 C CA  . PRO A 442 ? 0.22710 0.18375 0.25428 -0.02955 -0.00519 0.03227  442 PRO A CA  
3537 C C   . PRO A 442 ? 0.19296 0.14676 0.21682 -0.02622 -0.00585 0.02737  442 PRO A C   
3538 O O   . PRO A 442 ? 0.21370 0.16916 0.23634 -0.02551 -0.00607 0.02345  442 PRO A O   
3539 C CB  . PRO A 442 ? 0.20480 0.15659 0.23810 -0.03236 -0.00711 0.03292  442 PRO A CB  
3540 C CG  . PRO A 442 ? 0.21883 0.17601 0.25518 -0.03561 -0.00623 0.03539  442 PRO A CG  
3541 C CD  . PRO A 442 ? 0.21979 0.18372 0.25287 -0.03419 -0.00465 0.03296  442 PRO A CD  
3542 N N   . ALA A 443 ? 0.21530 0.16497 0.23791 -0.02426 -0.00621 0.02788  443 ALA A N   
3543 C CA  . ALA A 443 ? 0.21131 0.15871 0.23074 -0.02106 -0.00642 0.02360  443 ALA A CA  
3544 C C   . ALA A 443 ? 0.22290 0.16579 0.24423 -0.02116 -0.00792 0.01884  443 ALA A C   
3545 O O   . ALA A 443 ? 0.25151 0.19386 0.26963 -0.01900 -0.00783 0.01470  443 ALA A O   
3546 C CB  . ALA A 443 ? 0.22528 0.16944 0.24419 -0.01913 -0.00656 0.02549  443 ALA A CB  
3547 N N   . LYS A 444 ? 0.18900 0.12872 0.21529 -0.02381 -0.00927 0.01929  444 LYS A N   
3548 C CA  . LYS A 444 ? 0.23183 0.16717 0.25969 -0.02426 -0.01079 0.01439  444 LYS A CA  
3549 C C   . LYS A 444 ? 0.23895 0.17854 0.26389 -0.02453 -0.01095 0.01093  444 LYS A C   
3550 O O   . LYS A 444 ? 0.22899 0.16617 0.25215 -0.02384 -0.01181 0.00613  444 LYS A O   
3551 C CB  . LYS A 444 ? 0.28302 0.21414 0.31723 -0.02740 -0.01232 0.01584  444 LYS A CB  
3552 C CG  . LYS A 444 ? 0.24689 0.17267 0.28304 -0.02816 -0.01400 0.01051  444 LYS A CG  
3553 C CD  . LYS A 444 ? 0.23875 0.15964 0.28182 -0.03124 -0.01552 0.01223  444 LYS A CD  
3554 C CE  . LYS A 444 ? 0.26975 0.18550 0.31462 -0.03240 -0.01724 0.00640  444 LYS A CE  
3555 N NZ  . LYS A 444 ? 0.27674 0.18725 0.32890 -0.03553 -0.01881 0.00792  444 LYS A NZ  
3556 N N   . TYR A 445 ? 0.22071 0.16676 0.24520 -0.02554 -0.01013 0.01330  445 TYR A N   
3557 C CA  . TYR A 445 ? 0.21386 0.16433 0.23670 -0.02585 -0.01056 0.01073  445 TYR A CA  
3558 C C   . TYR A 445 ? 0.19431 0.15075 0.21324 -0.02377 -0.00873 0.01168  445 TYR A C   
3559 O O   . TYR A 445 ? 0.18818 0.14951 0.20716 -0.02423 -0.00882 0.01110  445 TYR A O   
3560 C CB  . TYR A 445 ? 0.24066 0.19347 0.26851 -0.02935 -0.01163 0.01206  445 TYR A CB  
3561 C CG  . TYR A 445 ? 0.22492 0.17209 0.25780 -0.03191 -0.01310 0.01262  445 TYR A CG  
3562 C CD1 . TYR A 445 ? 0.21770 0.15982 0.25140 -0.03275 -0.01518 0.00826  445 TYR A CD1 
3563 C CD2 . TYR A 445 ? 0.23170 0.17855 0.26844 -0.03366 -0.01240 0.01750  445 TYR A CD2 
3564 C CE1 . TYR A 445 ? 0.20873 0.14523 0.24754 -0.03511 -0.01655 0.00847  445 TYR A CE1 
3565 C CE2 . TYR A 445 ? 0.24331 0.18462 0.28522 -0.03608 -0.01387 0.01831  445 TYR A CE2 
3566 C CZ  . TYR A 445 ? 0.25004 0.18600 0.29327 -0.03673 -0.01594 0.01365  445 TYR A CZ  
3567 O OH  . TYR A 445 ? 0.32181 0.25179 0.37067 -0.03915 -0.01742 0.01414  445 TYR A OH  
3568 N N   . ILE A 446 ? 0.17124 0.12735 0.18722 -0.02152 -0.00721 0.01310  446 ILE A N   
3569 C CA  . ILE A 446 ? 0.19730 0.15875 0.20977 -0.01972 -0.00544 0.01383  446 ILE A CA  
3570 C C   . ILE A 446 ? 0.18365 0.14589 0.19250 -0.01778 -0.00586 0.00995  446 ILE A C   
3571 O O   . ILE A 446 ? 0.20228 0.16937 0.20974 -0.01698 -0.00503 0.00991  446 ILE A O   
3572 C CB  . ILE A 446 ? 0.22201 0.18288 0.23227 -0.01818 -0.00402 0.01641  446 ILE A CB  
3573 C CG1 . ILE A 446 ? 0.17350 0.13999 0.18039 -0.01675 -0.00207 0.01712  446 ILE A CG1 
3574 C CG2 . ILE A 446 ? 0.17041 0.12594 0.17891 -0.01606 -0.00467 0.01426  446 ILE A CG2 
3575 C CD1 . ILE A 446 ? 0.19813 0.17019 0.20715 -0.01869 -0.00074 0.01966  446 ILE A CD1 
3576 N N   . TYR A 447 ? 0.15855 0.11611 0.16596 -0.01707 -0.00707 0.00665  447 TYR A N   
3577 C CA  . TYR A 447 ? 0.20356 0.16179 0.20715 -0.01567 -0.00758 0.00317  447 TYR A CA  
3578 C C   . TYR A 447 ? 0.19438 0.15340 0.19920 -0.01769 -0.00964 0.00106  447 TYR A C   
3579 O O   . TYR A 447 ? 0.14423 0.10529 0.14610 -0.01697 -0.01029 -0.00090 447 TYR A O   
3580 C CB  . TYR A 447 ? 0.20227 0.15572 0.20300 -0.01384 -0.00743 0.00046  447 TYR A CB  
3581 C CG  . TYR A 447 ? 0.17666 0.13030 0.17545 -0.01144 -0.00568 0.00208  447 TYR A CG  
3582 C CD1 . TYR A 447 ? 0.18591 0.14258 0.18081 -0.00947 -0.00467 0.00154  447 TYR A CD1 
3583 C CD2 . TYR A 447 ? 0.18942 0.14019 0.19053 -0.01127 -0.00528 0.00432  447 TYR A CD2 
3584 C CE1 . TYR A 447 ? 0.15075 0.10771 0.14401 -0.00751 -0.00328 0.00287  447 TYR A CE1 
3585 C CE2 . TYR A 447 ? 0.18523 0.13651 0.18465 -0.00926 -0.00406 0.00593  447 TYR A CE2 
3586 C CZ  . TYR A 447 ? 0.17862 0.13306 0.17404 -0.00744 -0.00305 0.00504  447 TYR A CZ  
3587 O OH  . TYR A 447 ? 0.17920 0.13426 0.17307 -0.00567 -0.00203 0.00650  447 TYR A OH  
3588 N N   . GLU A 448 ? 0.20459 0.16207 0.21379 -0.02036 -0.01088 0.00161  448 GLU A N   
3589 C CA  . GLU A 448 ? 0.21898 0.17761 0.23000 -0.02273 -0.01316 -0.00012 448 GLU A CA  
3590 C C   . GLU A 448 ? 0.22157 0.18282 0.23853 -0.02535 -0.01336 0.00306  448 GLU A C   
3591 O O   . GLU A 448 ? 0.25310 0.21094 0.27374 -0.02768 -0.01444 0.00315  448 GLU A O   
3592 C CB  . GLU A 448 ? 0.25187 0.20475 0.26191 -0.02373 -0.01487 -0.00413 448 GLU A CB  
3593 C CG  . GLU A 448 ? 0.29287 0.24018 0.30128 -0.02186 -0.01360 -0.00538 448 GLU A CG  
3594 C CD  . GLU A 448 ? 0.30400 0.24607 0.31099 -0.02253 -0.01485 -0.01026 448 GLU A CD  
3595 O OE1 . GLU A 448 ? 0.40079 0.34331 0.40783 -0.02485 -0.01696 -0.01253 448 GLU A OE1 
3596 O OE2 . GLU A 448 ? 0.33598 0.27367 0.34192 -0.02078 -0.01371 -0.01196 448 GLU A OE2 
3597 N N   . PRO A 449 ? 0.20909 0.17649 0.22747 -0.02510 -0.01217 0.00566  449 PRO A N   
3598 C CA  . PRO A 449 ? 0.21860 0.18920 0.24278 -0.02761 -0.01178 0.00889  449 PRO A CA  
3599 C C   . PRO A 449 ? 0.19185 0.16330 0.22040 -0.03065 -0.01439 0.00783  449 PRO A C   
3600 O O   . PRO A 449 ? 0.19184 0.16380 0.22565 -0.03335 -0.01449 0.01007  449 PRO A O   
3601 C CB  . PRO A 449 ? 0.21791 0.19517 0.24204 -0.02614 -0.00960 0.01092  449 PRO A CB  
3602 C CG  . PRO A 449 ? 0.15514 0.13314 0.17486 -0.02363 -0.01016 0.00827  449 PRO A CG  
3603 C CD  . PRO A 449 ? 0.16558 0.13721 0.18073 -0.02253 -0.01091 0.00570  449 PRO A CD  
3604 N N   . TRP A 450 ? 0.21271 0.18450 0.23923 -0.03053 -0.01664 0.00467  450 TRP A N   
3605 C CA  . TRP A 450 ? 0.19503 0.16779 0.22546 -0.03363 -0.01958 0.00351  450 TRP A CA  
3606 C C   . TRP A 450 ? 0.22372 0.18998 0.25561 -0.03603 -0.02107 0.00184  450 TRP A C   
3607 O O   . TRP A 450 ? 0.19969 0.16653 0.23644 -0.03927 -0.02311 0.00182  450 TRP A O   
3608 C CB  . TRP A 450 ? 0.22199 0.19665 0.24905 -0.03301 -0.02191 0.00071  450 TRP A CB  
3609 C CG  . TRP A 450 ? 0.24777 0.21710 0.26797 -0.03160 -0.02246 -0.00298 450 TRP A CG  
3610 C CD1 . TRP A 450 ? 0.22886 0.19355 0.24719 -0.03340 -0.02471 -0.00667 450 TRP A CD1 
3611 C CD2 . TRP A 450 ? 0.19634 0.16464 0.21079 -0.02823 -0.02051 -0.00356 450 TRP A CD2 
3612 N NE1 . TRP A 450 ? 0.23186 0.19296 0.24359 -0.03128 -0.02402 -0.00955 450 TRP A NE1 
3613 C CE2 . TRP A 450 ? 0.22317 0.18645 0.23261 -0.02812 -0.02152 -0.00753 450 TRP A CE2 
3614 C CE3 . TRP A 450 ? 0.22401 0.19520 0.23715 -0.02544 -0.01795 -0.00132 450 TRP A CE3 
3615 C CZ2 . TRP A 450 ? 0.18993 0.15135 0.19351 -0.02533 -0.01998 -0.00898 450 TRP A CZ2 
3616 C CZ3 . TRP A 450 ? 0.21472 0.18375 0.22204 -0.02274 -0.01673 -0.00277 450 TRP A CZ3 
3617 C CH2 . TRP A 450 ? 0.20878 0.17312 0.21155 -0.02270 -0.01771 -0.00641 450 TRP A CH2 
3618 N N   . THR A 451 ? 0.19853 0.15864 0.22693 -0.03452 -0.02012 0.00038  451 THR A N   
3619 C CA  . THR A 451 ? 0.22594 0.17927 0.25642 -0.03644 -0.02126 -0.00132 451 THR A CA  
3620 C C   . THR A 451 ? 0.22349 0.17576 0.25983 -0.03820 -0.02023 0.00281  451 THR A C   
3621 O O   . THR A 451 ? 0.20211 0.14921 0.24201 -0.04049 -0.02154 0.00200  451 THR A O   
3622 C CB  . THR A 451 ? 0.21749 0.16483 0.24302 -0.03394 -0.02045 -0.00439 451 THR A CB  
3623 O OG1 . THR A 451 ? 0.21104 0.15881 0.23516 -0.03118 -0.01772 -0.00141 451 THR A OG1 
3624 C CG2 . THR A 451 ? 0.25539 0.20365 0.27475 -0.03265 -0.02141 -0.00847 451 THR A CG2 
3625 N N   . ALA A 452 ? 0.21740 0.17433 0.25473 -0.03734 -0.01790 0.00713  452 ALA A N   
3626 C CA  . ALA A 452 ? 0.22242 0.17897 0.26469 -0.03928 -0.01680 0.01155  452 ALA A CA  
3627 C C   . ALA A 452 ? 0.21297 0.17215 0.26177 -0.04327 -0.01838 0.01262  452 ALA A C   
3628 O O   . ALA A 452 ? 0.21328 0.17781 0.26300 -0.04391 -0.01939 0.01157  452 ALA A O   
3629 C CB  . ALA A 452 ? 0.20711 0.16875 0.24794 -0.03759 -0.01376 0.01556  452 ALA A CB  
3630 N N   . PRO A 453 ? 0.23356 0.18915 0.28744 -0.04607 -0.01880 0.01489  453 PRO A N   
3631 C CA  . PRO A 453 ? 0.26674 0.22519 0.32748 -0.05016 -0.02015 0.01636  453 PRO A CA  
3632 C C   . PRO A 453 ? 0.23833 0.20585 0.30137 -0.05057 -0.01799 0.02013  453 PRO A C   
3633 O O   . PRO A 453 ? 0.22022 0.19079 0.28023 -0.04832 -0.01513 0.02257  453 PRO A O   
3634 C CB  . PRO A 453 ? 0.24752 0.19979 0.31278 -0.05259 -0.02042 0.01890  453 PRO A CB  
3635 C CG  . PRO A 453 ? 0.26011 0.20484 0.32110 -0.04978 -0.02037 0.01671  453 PRO A CG  
3636 C CD  . PRO A 453 ? 0.23466 0.18303 0.28883 -0.04570 -0.01839 0.01614  453 PRO A CD  
3637 N N   . LEU A 454 ? 0.25877 0.23080 0.32754 -0.05359 -0.01939 0.02036  454 LEU A N   
3638 C CA  . LEU A 454 ? 0.21646 0.19763 0.28860 -0.05405 -0.01726 0.02346  454 LEU A CA  
3639 C C   . LEU A 454 ? 0.25206 0.23477 0.32629 -0.05527 -0.01407 0.02875  454 LEU A C   
3640 O O   . LEU A 454 ? 0.27264 0.26209 0.34652 -0.05422 -0.01101 0.03108  454 LEU A O   
3641 C CB  . LEU A 454 ? 0.28354 0.26910 0.36257 -0.05734 -0.01966 0.02281  454 LEU A CB  
3642 C CG  . LEU A 454 ? 0.23924 0.23498 0.32270 -0.05747 -0.01776 0.02507  454 LEU A CG  
3643 C CD1 . LEU A 454 ? 0.27605 0.27541 0.35444 -0.05322 -0.01680 0.02315  454 LEU A CD1 
3644 C CD2 . LEU A 454 ? 0.30078 0.30044 0.39207 -0.06105 -0.02059 0.02463  454 LEU A CD2 
3645 N N   . GLU A 455 ? 0.24950 0.22603 0.32586 -0.05756 -0.01472 0.03070  455 GLU A N   
3646 C CA  . GLU A 455 ? 0.21145 0.18903 0.28913 -0.05894 -0.01197 0.03624  455 GLU A CA  
3647 C C   . GLU A 455 ? 0.22938 0.20657 0.29987 -0.05528 -0.00946 0.03734  455 GLU A C   
3648 O O   . GLU A 455 ? 0.22685 0.20873 0.29670 -0.05564 -0.00641 0.04140  455 GLU A O   
3649 C CB  . GLU A 455 ? 0.23272 0.20296 0.31463 -0.06213 -0.01372 0.03823  455 GLU A CB  
3650 C CG  . GLU A 455 ? 0.24315 0.21381 0.33287 -0.06642 -0.01613 0.03770  455 GLU A CG  
3651 C CD  . GLU A 455 ? 0.24162 0.20417 0.33579 -0.06951 -0.01793 0.03947  455 GLU A CD  
3652 O OE1 . GLU A 455 ? 0.23813 0.19396 0.32920 -0.06782 -0.01777 0.04033  455 GLU A OE1 
3653 O OE2 . GLU A 455 ? 0.24443 0.20731 0.34571 -0.07364 -0.01960 0.04006  455 GLU A OE2 
3654 N N   . VAL A 456 ? 0.26747 0.23941 0.33245 -0.05195 -0.01064 0.03370  456 VAL A N   
3655 C CA  . VAL A 456 ? 0.24891 0.22045 0.30734 -0.04852 -0.00858 0.03451  456 VAL A CA  
3656 C C   . VAL A 456 ? 0.23556 0.21452 0.29061 -0.04602 -0.00649 0.03322  456 VAL A C   
3657 O O   . VAL A 456 ? 0.22142 0.20366 0.27298 -0.04463 -0.00373 0.03549  456 VAL A O   
3658 C CB  . VAL A 456 ? 0.24837 0.21174 0.30298 -0.04597 -0.01044 0.03116  456 VAL A CB  
3659 C CG1 . VAL A 456 ? 0.29178 0.25489 0.34023 -0.04260 -0.00852 0.03223  456 VAL A CG1 
3660 C CG2 . VAL A 456 ? 0.23057 0.18630 0.28958 -0.04837 -0.01246 0.03214  456 VAL A CG2 
3661 N N   . GLN A 457 ? 0.18031 0.16192 0.23645 -0.04550 -0.00791 0.02959  457 GLN A N   
3662 C CA  . GLN A 457 ? 0.20747 0.19598 0.26168 -0.04317 -0.00615 0.02846  457 GLN A CA  
3663 C C   . GLN A 457 ? 0.22295 0.21922 0.28083 -0.04482 -0.00302 0.03207  457 GLN A C   
3664 O O   . GLN A 457 ? 0.22214 0.22302 0.27706 -0.04273 -0.00018 0.03249  457 GLN A O   
3665 C CB  . GLN A 457 ? 0.19435 0.18432 0.25014 -0.04284 -0.00878 0.02460  457 GLN A CB  
3666 C CG  . GLN A 457 ? 0.19835 0.18145 0.24971 -0.04128 -0.01155 0.02057  457 GLN A CG  
3667 C CD  . GLN A 457 ? 0.18920 0.17426 0.24151 -0.04138 -0.01435 0.01716  457 GLN A CD  
3668 O OE1 . GLN A 457 ? 0.19999 0.18021 0.24891 -0.04078 -0.01674 0.01366  457 GLN A OE1 
3669 N NE2 . GLN A 457 ? 0.20019 0.19264 0.25721 -0.04219 -0.01407 0.01822  457 GLN A NE2 
3670 N N   . ARG A 458 ? 0.25531 0.25321 0.31978 -0.04870 -0.00334 0.03454  458 ARG A N   
3671 C CA  . ARG A 458 ? 0.21336 0.21898 0.28160 -0.05062 0.00000  0.03807  458 ARG A CA  
3672 C C   . ARG A 458 ? 0.21567 0.22052 0.28006 -0.05103 0.00279  0.04208  458 ARG A C   
3673 O O   . ARG A 458 ? 0.23315 0.24446 0.29653 -0.05085 0.00643  0.04388  458 ARG A O   
3674 C CB  . ARG A 458 ? 0.22418 0.23201 0.30100 -0.05492 -0.00122 0.03968  458 ARG A CB  
3675 C CG  . ARG A 458 ? 0.20395 0.21516 0.28548 -0.05493 -0.00363 0.03640  458 ARG A CG  
3676 C CD  . ARG A 458 ? 0.21462 0.22932 0.30527 -0.05944 -0.00443 0.03845  458 ARG A CD  
3677 N NE  . ARG A 458 ? 0.20734 0.22885 0.30134 -0.06136 -0.00025 0.04266  458 ARG A NE  
3678 C CZ  . ARG A 458 ? 0.20338 0.23398 0.30053 -0.06057 0.00266  0.04278  458 ARG A CZ  
3679 N NH1 . ARG A 458 ? 0.20645 0.24042 0.30441 -0.05779 0.00162  0.03933  458 ARG A NH1 
3680 N NH2 . ARG A 458 ? 0.19954 0.23607 0.29926 -0.06264 0.00677  0.04651  458 ARG A NH2 
3681 N N   . LYS A 459 ? 0.26276 0.25986 0.32508 -0.05162 0.00111  0.04350  459 LYS A N   
3682 C CA  . LYS A 459 ? 0.22949 0.22559 0.28825 -0.05219 0.00313  0.04785  459 LYS A CA  
3683 C C   . LYS A 459 ? 0.23802 0.23513 0.28905 -0.04839 0.00495  0.04666  459 LYS A C   
3684 O O   . LYS A 459 ? 0.27603 0.27528 0.32361 -0.04886 0.00736  0.05012  459 LYS A O   
3685 C CB  . LYS A 459 ? 0.27032 0.25751 0.32998 -0.05357 0.00043  0.04969  459 LYS A CB  
3686 C CG  . LYS A 459 ? 0.26464 0.25145 0.32383 -0.05600 0.00191  0.05585  459 LYS A CG  
3687 C CD  . LYS A 459 ? 0.27927 0.25773 0.34249 -0.05825 -0.00103 0.05806  459 LYS A CD  
3688 C CE  . LYS A 459 ? 0.27852 0.25671 0.34972 -0.06164 -0.00276 0.05726  459 LYS A CE  
3689 N NZ  . LYS A 459 ? 0.26724 0.24031 0.33944 -0.05995 -0.00595 0.05128  459 LYS A NZ  
3690 N N   . ALA A 460 ? 0.20834 0.20406 0.25645 -0.04490 0.00377  0.04197  460 ALA A N   
3691 C CA  . ALA A 460 ? 0.22593 0.22268 0.26727 -0.04132 0.00533  0.04042  460 ALA A CA  
3692 C C   . ALA A 460 ? 0.23481 0.23943 0.27629 -0.03996 0.00790  0.03853  460 ALA A C   
3693 O O   . ALA A 460 ? 0.19584 0.20171 0.23216 -0.03707 0.00934  0.03691  460 ALA A O   
3694 C CB  . ALA A 460 ? 0.18899 0.17917 0.22688 -0.03826 0.00265  0.03663  460 ALA A CB  
3695 N N   . GLY A 461 ? 0.21707 0.22699 0.26491 -0.04195 0.00848  0.03863  461 GLY A N   
3696 C CA  . GLY A 461 ? 0.23284 0.25033 0.28228 -0.04054 0.01092  0.03679  461 GLY A CA  
3697 C C   . GLY A 461 ? 0.23049 0.24706 0.27875 -0.03710 0.00909  0.03236  461 GLY A C   
3698 O O   . GLY A 461 ? 0.21602 0.23737 0.26367 -0.03486 0.01117  0.03064  461 GLY A O   
3699 N N   . CYS A 462 ? 0.25711 0.26763 0.30505 -0.03671 0.00530  0.03043  462 CYS A N   
3700 C CA  . CYS A 462 ? 0.21746 0.22669 0.26355 -0.03376 0.00327  0.02653  462 CYS A CA  
3701 C C   . CYS A 462 ? 0.20445 0.21088 0.25435 -0.03541 -0.00062 0.02504  462 CYS A C   
3702 O O   . CYS A 462 ? 0.19261 0.19220 0.23989 -0.03560 -0.00303 0.02397  462 CYS A O   
3703 C CB  . CYS A 462 ? 0.20232 0.20623 0.24077 -0.03087 0.00304  0.02513  462 CYS A CB  
3704 S SG  . CYS A 462 ? 0.21017 0.21196 0.24570 -0.02763 0.00054  0.02077  462 CYS A SG  
3705 N N   . VAL A 463 ? 0.22427 0.23619 0.28057 -0.03664 -0.00121 0.02481  463 VAL A N   
3706 C CA  . VAL A 463 ? 0.20456 0.21489 0.26463 -0.03841 -0.00515 0.02323  463 VAL A CA  
3707 C C   . VAL A 463 ? 0.18506 0.19476 0.24205 -0.03561 -0.00738 0.01989  463 VAL A C   
3708 O O   . VAL A 463 ? 0.18979 0.20453 0.24765 -0.03342 -0.00615 0.01943  463 VAL A O   
3709 C CB  . VAL A 463 ? 0.20801 0.22499 0.27706 -0.04133 -0.00505 0.02492  463 VAL A CB  
3710 C CG1 . VAL A 463 ? 0.24881 0.26448 0.32152 -0.04323 -0.00957 0.02306  463 VAL A CG1 
3711 C CG2 . VAL A 463 ? 0.23139 0.24891 0.30327 -0.04448 -0.00279 0.02860  463 VAL A CG2 
3712 N N   . VAL A 464 ? 0.18957 0.19303 0.24303 -0.03575 -0.01058 0.01754  464 VAL A N   
3713 C CA  . VAL A 464 ? 0.17493 0.17751 0.22471 -0.03353 -0.01287 0.01458  464 VAL A CA  
3714 C C   . VAL A 464 ? 0.19855 0.20706 0.25442 -0.03455 -0.01508 0.01441  464 VAL A C   
3715 O O   . VAL A 464 ? 0.21522 0.22440 0.27607 -0.03772 -0.01739 0.01462  464 VAL A O   
3716 C CB  . VAL A 464 ? 0.20833 0.20326 0.25307 -0.03392 -0.01553 0.01191  464 VAL A CB  
3717 C CG1 . VAL A 464 ? 0.18927 0.18391 0.22991 -0.03210 -0.01788 0.00910  464 VAL A CG1 
3718 C CG2 . VAL A 464 ? 0.18481 0.17427 0.22451 -0.03257 -0.01339 0.01227  464 VAL A CG2 
3719 N N   . GLY A 465 ? 0.23982 0.25262 0.29579 -0.03189 -0.01454 0.01411  465 GLY A N   
3720 C CA  . GLY A 465 ? 0.19277 0.21182 0.25531 -0.03232 -0.01653 0.01438  465 GLY A CA  
3721 C C   . GLY A 465 ? 0.17048 0.19707 0.24007 -0.03176 -0.01326 0.01648  465 GLY A C   
3722 O O   . GLY A 465 ? 0.15121 0.18350 0.22678 -0.03123 -0.01449 0.01672  465 GLY A O   
3723 N N   . ARG A 466 ? 0.17228 0.19926 0.24146 -0.03190 -0.00914 0.01801  466 ARG A N   
3724 C CA  . ARG A 466 ? 0.19078 0.22497 0.26576 -0.03144 -0.00526 0.01963  466 ARG A CA  
3725 C C   . ARG A 466 ? 0.20135 0.23499 0.27088 -0.02866 -0.00117 0.01947  466 ARG A C   
3726 O O   . ARG A 466 ? 0.19125 0.22965 0.26322 -0.02631 0.00101  0.01897  466 ARG A O   
3727 C CB  . ARG A 466 ? 0.19460 0.23140 0.27526 -0.03522 -0.00390 0.02205  466 ARG A CB  
3728 C CG  . ARG A 466 ? 0.20777 0.25289 0.29507 -0.03520 0.00035  0.02361  466 ARG A CG  
3729 C CD  . ARG A 466 ? 0.26278 0.30930 0.35287 -0.03886 0.00270  0.02640  466 ARG A CD  
3730 N NE  . ARG A 466 ? 0.25128 0.29201 0.33325 -0.03898 0.00445  0.02733  466 ARG A NE  
3731 C CZ  . ARG A 466 ? 0.32414 0.36503 0.40652 -0.04185 0.00672  0.03022  466 ARG A CZ  
3732 N NH1 . ARG A 466 ? 0.31266 0.35923 0.40301 -0.04502 0.00789  0.03239  466 ARG A NH1 
3733 N NH2 . ARG A 466 ? 0.34557 0.38099 0.42046 -0.04163 0.00777  0.03121  466 ARG A NH2 
3734 N N   . ASP A 467 ? 0.18569 0.21363 0.24824 -0.02890 -0.00017 0.01980  467 ASP A N   
3735 C CA  . ASP A 467 ? 0.17378 0.20088 0.23053 -0.02657 0.00326  0.01966  467 ASP A CA  
3736 C C   . ASP A 467 ? 0.18240 0.20396 0.23178 -0.02374 0.00168  0.01750  467 ASP A C   
3737 O O   . ASP A 467 ? 0.13278 0.15519 0.17909 -0.02109 0.00385  0.01663  467 ASP A O   
3738 C CB  . ASP A 467 ? 0.17723 0.20227 0.23126 -0.02867 0.00547  0.02199  467 ASP A CB  
3739 C CG  . ASP A 467 ? 0.17678 0.20750 0.23768 -0.03178 0.00751  0.02452  467 ASP A CG  
3740 O OD1 . ASP A 467 ? 0.10959 0.14737 0.17568 -0.03120 0.00985  0.02437  467 ASP A OD1 
3741 O OD2 . ASP A 467 ? 0.21250 0.24066 0.27408 -0.03481 0.00683  0.02666  467 ASP A OD2 
3742 N N   . TYR A 468 ? 0.15254 0.16856 0.19912 -0.02438 -0.00189 0.01646  468 TYR A N   
3743 C CA  . TYR A 468 ? 0.17038 0.18153 0.21035 -0.02198 -0.00345 0.01434  468 TYR A CA  
3744 C C   . TYR A 468 ? 0.15724 0.16727 0.19828 -0.02261 -0.00765 0.01282  468 TYR A C   
3745 O O   . TYR A 468 ? 0.16055 0.16957 0.20438 -0.02542 -0.00985 0.01301  468 TYR A O   
3746 C CB  . TYR A 468 ? 0.16538 0.17008 0.19910 -0.02207 -0.00306 0.01437  468 TYR A CB  
3747 C CG  . TYR A 468 ? 0.14738 0.14758 0.17450 -0.01955 -0.00406 0.01221  468 TYR A CG  
3748 C CD1 . TYR A 468 ? 0.12169 0.12288 0.14549 -0.01679 -0.00196 0.01179  468 TYR A CD1 
3749 C CD2 . TYR A 468 ? 0.13665 0.13176 0.16096 -0.02008 -0.00695 0.01042  468 TYR A CD2 
3750 C CE1 . TYR A 468 ? 0.13076 0.12812 0.14895 -0.01470 -0.00279 0.01001  468 TYR A CE1 
3751 C CE2 . TYR A 468 ? 0.12789 0.11938 0.14630 -0.01793 -0.00752 0.00847  468 TYR A CE2 
3752 C CZ  . TYR A 468 ? 0.10416 0.09687 0.11969 -0.01527 -0.00546 0.00847  468 TYR A CZ  
3753 O OH  . TYR A 468 ? 0.10784 0.09718 0.11788 -0.01333 -0.00596 0.00673  468 TYR A OH  
3754 N N   . PRO A 469 ? 0.14793 0.15813 0.18680 -0.02033 -0.00900 0.01139  469 PRO A N   
3755 C CA  . PRO A 469 ? 0.15967 0.16979 0.19947 -0.02118 -0.01316 0.01032  469 PRO A CA  
3756 C C   . PRO A 469 ? 0.15917 0.16286 0.19354 -0.02262 -0.01556 0.00856  469 PRO A C   
3757 O O   . PRO A 469 ? 0.13023 0.12898 0.15925 -0.02192 -0.01415 0.00784  469 PRO A O   
3758 C CB  . PRO A 469 ? 0.14628 0.15776 0.18426 -0.01817 -0.01348 0.00972  469 PRO A CB  
3759 C CG  . PRO A 469 ? 0.15526 0.16445 0.18834 -0.01587 -0.01003 0.00948  469 PRO A CG  
3760 C CD  . PRO A 469 ? 0.14783 0.15851 0.18344 -0.01708 -0.00688 0.01088  469 PRO A CD  
3761 N N   . ALA A 470 ? 0.15274 0.15675 0.18887 -0.02471 -0.01930 0.00773  470 ALA A N   
3762 C CA  . ALA A 470 ? 0.14501 0.14330 0.17609 -0.02621 -0.02177 0.00536  470 ALA A CA  
3763 C C   . ALA A 470 ? 0.13753 0.13307 0.16118 -0.02396 -0.02243 0.00356  470 ALA A C   
3764 O O   . ALA A 470 ? 0.11359 0.11226 0.13717 -0.02181 -0.02222 0.00437  470 ALA A O   
3765 C CB  . ALA A 470 ? 0.14866 0.14864 0.18368 -0.02940 -0.02571 0.00483  470 ALA A CB  
3766 N N   . PRO A 471 ? 0.13893 0.12863 0.15661 -0.02442 -0.02304 0.00109  471 PRO A N   
3767 C CA  . PRO A 471 ? 0.13560 0.12301 0.14613 -0.02261 -0.02352 -0.00066 471 PRO A CA  
3768 C C   . PRO A 471 ? 0.14293 0.13362 0.15315 -0.02328 -0.02705 -0.00074 471 PRO A C   
3769 O O   . PRO A 471 ? 0.14737 0.13907 0.15965 -0.02603 -0.03022 -0.00138 471 PRO A O   
3770 C CB  . PRO A 471 ? 0.14927 0.13029 0.15503 -0.02367 -0.02365 -0.00363 471 PRO A CB  
3771 C CG  . PRO A 471 ? 0.17871 0.15895 0.18947 -0.02669 -0.02479 -0.00368 471 PRO A CG  
3772 C CD  . PRO A 471 ? 0.18179 0.16661 0.19933 -0.02654 -0.02308 -0.00024 471 PRO A CD  
3773 N N   . ILE A 472 ? 0.14949 0.14186 0.15727 -0.02087 -0.02670 0.00012  472 ILE A N   
3774 C CA  . ILE A 472 ? 0.15431 0.15009 0.16220 -0.02129 -0.03019 0.00086  472 ILE A CA  
3775 C C   . ILE A 472 ? 0.17536 0.16810 0.17628 -0.02326 -0.03306 -0.00173 472 ILE A C   
3776 O O   . ILE A 472 ? 0.19740 0.19277 0.19860 -0.02506 -0.03694 -0.00141 472 ILE A O   
3777 C CB  . ILE A 472 ? 0.15188 0.14978 0.15940 -0.01819 -0.02899 0.00268  472 ILE A CB  
3778 C CG1 . ILE A 472 ? 0.13243 0.12581 0.13267 -0.01629 -0.02638 0.00127  472 ILE A CG1 
3779 C CG2 . ILE A 472 ? 0.12554 0.12753 0.14083 -0.01663 -0.02663 0.00491  472 ILE A CG2 
3780 C CD1 . ILE A 472 ? 0.16740 0.16225 0.16702 -0.01348 -0.02528 0.00287  472 ILE A CD1 
3781 N N   . VAL A 473 ? 0.18132 0.16874 0.17600 -0.02303 -0.03125 -0.00439 473 VAL A N   
3782 C CA  . VAL A 473 ? 0.17793 0.16228 0.16544 -0.02482 -0.03324 -0.00750 473 VAL A CA  
3783 C C   . VAL A 473 ? 0.18701 0.16583 0.17273 -0.02569 -0.03143 -0.01069 473 VAL A C   
3784 O O   . VAL A 473 ? 0.21455 0.19133 0.20245 -0.02408 -0.02823 -0.01018 473 VAL A O   
3785 C CB  . VAL A 473 ? 0.19116 0.17496 0.17158 -0.02308 -0.03276 -0.00763 473 VAL A CB  
3786 C CG1 . VAL A 473 ? 0.19578 0.18456 0.17772 -0.02277 -0.03552 -0.00454 473 VAL A CG1 
3787 C CG2 . VAL A 473 ? 0.19383 0.17549 0.17346 -0.01995 -0.02848 -0.00721 473 VAL A CG2 
3788 N N   . ASP A 474 ? 0.20868 0.18508 0.19055 -0.02833 -0.03364 -0.01403 474 ASP A N   
3789 C CA  . ASP A 474 ? 0.22509 0.19558 0.20431 -0.02889 -0.03194 -0.01780 474 ASP A CA  
3790 C C   . ASP A 474 ? 0.21697 0.18497 0.18870 -0.02693 -0.02976 -0.01974 474 ASP A C   
3791 O O   . ASP A 474 ? 0.21723 0.18664 0.18302 -0.02754 -0.03135 -0.02059 474 ASP A O   
3792 C CB  . ASP A 474 ? 0.21296 0.18180 0.19134 -0.03264 -0.03506 -0.02115 474 ASP A CB  
3793 C CG  . ASP A 474 ? 0.26714 0.22947 0.24391 -0.03318 -0.03327 -0.02537 474 ASP A CG  
3794 O OD1 . ASP A 474 ? 0.35096 0.31041 0.32913 -0.03075 -0.02984 -0.02491 474 ASP A OD1 
3795 O OD2 . ASP A 474 ? 0.27344 0.23353 0.24776 -0.03606 -0.03540 -0.02923 474 ASP A OD2 
3796 N N   . HIS A 475 ? 0.23235 0.19692 0.20450 -0.02470 -0.02619 -0.02019 475 HIS A N   
3797 C CA  . HIS A 475 ? 0.20252 0.16547 0.16880 -0.02251 -0.02377 -0.02145 475 HIS A CA  
3798 C C   . HIS A 475 ? 0.20507 0.16544 0.16446 -0.02420 -0.02442 -0.02610 475 HIS A C   
3799 O O   . HIS A 475 ? 0.21403 0.17542 0.16723 -0.02360 -0.02398 -0.02668 475 HIS A O   
3800 C CB  . HIS A 475 ? 0.19683 0.15666 0.16567 -0.02007 -0.02021 -0.02112 475 HIS A CB  
3801 C CG  . HIS A 475 ? 0.19376 0.15230 0.15766 -0.01779 -0.01762 -0.02225 475 HIS A CG  
3802 N ND1 . HIS A 475 ? 0.19815 0.15989 0.15880 -0.01644 -0.01739 -0.02030 475 HIS A ND1 
3803 C CD2 . HIS A 475 ? 0.18412 0.13862 0.14637 -0.01666 -0.01517 -0.02506 475 HIS A CD2 
3804 C CE1 . HIS A 475 ? 0.18712 0.14700 0.14409 -0.01475 -0.01485 -0.02182 475 HIS A CE1 
3805 N NE2 . HIS A 475 ? 0.19199 0.14768 0.14998 -0.01477 -0.01342 -0.02476 475 HIS A NE2 
3806 N N   . ALA A 476 ? 0.21593 0.17294 0.17625 -0.02646 -0.02537 -0.02955 476 ALA A N   
3807 C CA  . ALA A 476 ? 0.20199 0.15638 0.15565 -0.02822 -0.02571 -0.03473 476 ALA A CA  
3808 C C   . ALA A 476 ? 0.21646 0.17484 0.16431 -0.03047 -0.02901 -0.03463 476 ALA A C   
3809 O O   . ALA A 476 ? 0.22063 0.17902 0.16080 -0.03074 -0.02843 -0.03694 476 ALA A O   
3810 C CB  . ALA A 476 ? 0.23544 0.18529 0.19214 -0.03039 -0.02635 -0.03852 476 ALA A CB  
3811 N N   . VAL A 477 ? 0.23059 0.19266 0.18216 -0.03218 -0.03253 -0.03176 477 VAL A N   
3812 C CA  . VAL A 477 ? 0.21762 0.18388 0.16449 -0.03436 -0.03627 -0.03094 477 VAL A CA  
3813 C C   . VAL A 477 ? 0.22408 0.19373 0.16804 -0.03205 -0.03554 -0.02723 477 VAL A C   
3814 O O   . VAL A 477 ? 0.21760 0.18900 0.15428 -0.03319 -0.03698 -0.02761 477 VAL A O   
3815 C CB  . VAL A 477 ? 0.22720 0.19680 0.18032 -0.03664 -0.04031 -0.02861 477 VAL A CB  
3816 C CG1 . VAL A 477 ? 0.22910 0.20366 0.17835 -0.03858 -0.04457 -0.02676 477 VAL A CG1 
3817 C CG2 . VAL A 477 ? 0.21324 0.17924 0.16861 -0.03950 -0.04138 -0.03261 477 VAL A CG2 
3818 N N   . ALA A 478 ? 0.24313 0.21371 0.19255 -0.02895 -0.03332 -0.02358 478 ALA A N   
3819 C CA  . ALA A 478 ? 0.21647 0.19009 0.16431 -0.02677 -0.03278 -0.01994 478 ALA A CA  
3820 C C   . ALA A 478 ? 0.23380 0.20506 0.17494 -0.02526 -0.02953 -0.02185 478 ALA A C   
3821 O O   . ALA A 478 ? 0.23065 0.20403 0.16661 -0.02521 -0.03014 -0.02041 478 ALA A O   
3822 C CB  . ALA A 478 ? 0.20559 0.18098 0.16145 -0.02414 -0.03137 -0.01596 478 ALA A CB  
3823 N N   . SER A 479 ? 0.21472 0.18176 0.15629 -0.02407 -0.02610 -0.02484 479 SER A N   
3824 C CA  . SER A 479 ? 0.21836 0.18356 0.15472 -0.02246 -0.02275 -0.02664 479 SER A CA  
3825 C C   . SER A 479 ? 0.25443 0.21934 0.18199 -0.02489 -0.02348 -0.03029 479 SER A C   
3826 O O   . SER A 479 ? 0.24754 0.21378 0.16939 -0.02442 -0.02236 -0.02979 479 SER A O   
3827 C CB  . SER A 479 ? 0.21217 0.17312 0.15208 -0.02060 -0.01923 -0.02886 479 SER A CB  
3828 O OG  . SER A 479 ? 0.24902 0.20664 0.18986 -0.02255 -0.01985 -0.03284 479 SER A OG  
3829 N N   . LYS A 480 ? 0.25551 0.21877 0.18171 -0.02770 -0.02531 -0.03406 480 LYS A N   
3830 C CA  . LYS A 480 ? 0.28751 0.25070 0.20471 -0.03039 -0.02604 -0.03801 480 LYS A CA  
3831 C C   . LYS A 480 ? 0.26270 0.23072 0.17483 -0.03215 -0.02956 -0.03464 480 LYS A C   
3832 O O   . LYS A 480 ? 0.26061 0.22961 0.16410 -0.03359 -0.02931 -0.03621 480 LYS A O   
3833 C CB  . LYS A 480 ? 0.23359 0.19390 0.15097 -0.03323 -0.02758 -0.04290 480 LYS A CB  
3834 C CG  . LYS A 480 ? 0.27961 0.23940 0.18730 -0.03619 -0.02789 -0.04809 480 LYS A CG  
3835 C CD  . LYS A 480 ? 0.27094 0.22615 0.17971 -0.03807 -0.02770 -0.05424 480 LYS A CD  
3836 C CE  . LYS A 480 ? 0.27104 0.22134 0.18505 -0.03503 -0.02312 -0.05664 480 LYS A CE  
3837 N NZ  . LYS A 480 ? 0.27504 0.22028 0.18996 -0.03673 -0.02261 -0.06312 480 LYS A NZ  
3838 N N   . ALA A 481 ? 0.30298 0.27422 0.22057 -0.03208 -0.03278 -0.02985 481 ALA A N   
3839 C CA  . ALA A 481 ? 0.24983 0.22567 0.16397 -0.03336 -0.03635 -0.02590 481 ALA A CA  
3840 C C   . ALA A 481 ? 0.23790 0.21502 0.15031 -0.03078 -0.03413 -0.02242 481 ALA A C   
3841 O O   . ALA A 481 ? 0.23354 0.21309 0.13933 -0.03208 -0.03560 -0.02075 481 ALA A O   
3842 C CB  . ALA A 481 ? 0.19830 0.17731 0.12012 -0.03383 -0.04036 -0.02199 481 ALA A CB  
3843 N N   . CYS A 482 ? 0.25991 0.23547 0.17813 -0.02735 -0.03071 -0.02116 482 CYS A N   
3844 C CA  . CYS A 482 ? 0.22766 0.20424 0.14498 -0.02495 -0.02860 -0.01801 482 CYS A CA  
3845 C C   . CYS A 482 ? 0.25061 0.22560 0.15994 -0.02519 -0.02540 -0.02108 482 CYS A C   
3846 O O   . CYS A 482 ? 0.24661 0.22344 0.15149 -0.02511 -0.02515 -0.01867 482 CYS A O   
3847 C CB  . CYS A 482 ? 0.22363 0.19912 0.14914 -0.02151 -0.02598 -0.01617 482 CYS A CB  
3848 S SG  . CYS A 482 ? 0.23541 0.21385 0.17054 -0.02078 -0.02894 -0.01181 482 CYS A SG  
3849 N N   . ILE A 483 ? 0.23864 0.21026 0.14650 -0.02551 -0.02284 -0.02637 483 ILE A N   
3850 C CA  . ILE A 483 ? 0.25281 0.22312 0.15398 -0.02554 -0.01926 -0.02980 483 ILE A CA  
3851 C C   . ILE A 483 ? 0.27229 0.24496 0.16359 -0.02894 -0.02122 -0.03068 483 ILE A C   
3852 O O   . ILE A 483 ? 0.25868 0.23269 0.14406 -0.02904 -0.01933 -0.03010 483 ILE A O   
3853 C CB  . ILE A 483 ? 0.25515 0.22119 0.15819 -0.02498 -0.01623 -0.03546 483 ILE A CB  
3854 C CG1 . ILE A 483 ? 0.28236 0.24634 0.19428 -0.02153 -0.01397 -0.03393 483 ILE A CG1 
3855 C CG2 . ILE A 483 ? 0.28408 0.24920 0.18009 -0.02543 -0.01264 -0.03982 483 ILE A CG2 
3856 C CD1 . ILE A 483 ? 0.25519 0.21479 0.17010 -0.02074 -0.01129 -0.03871 483 ILE A CD1 
3857 N N   . ALA A 484 ? 0.28207 0.25554 0.17131 -0.03199 -0.02512 -0.03192 484 ALA A N   
3858 C CA  . ALA A 484 ? 0.27844 0.25435 0.15758 -0.03566 -0.02737 -0.03286 484 ALA A CA  
3859 C C   . ALA A 484 ? 0.32434 0.30436 0.20120 -0.03593 -0.02997 -0.02642 484 ALA A C   
3860 O O   . ALA A 484 ? 0.31763 0.29955 0.18567 -0.03778 -0.02968 -0.02613 484 ALA A O   
3861 C CB  . ALA A 484 ? 0.32464 0.30058 0.20283 -0.03899 -0.03145 -0.03549 484 ALA A CB  
3862 N N   . ARG A 485 ? 0.29105 0.27251 0.17597 -0.03414 -0.03242 -0.02119 485 ARG A N   
3863 C CA  . ARG A 485 ? 0.27134 0.25624 0.15564 -0.03402 -0.03493 -0.01489 485 ARG A CA  
3864 C C   . ARG A 485 ? 0.30554 0.28995 0.18844 -0.03177 -0.03090 -0.01322 485 ARG A C   
3865 O O   . ARG A 485 ? 0.33567 0.32246 0.21364 -0.03280 -0.03207 -0.00954 485 ARG A O   
3866 C CB  . ARG A 485 ? 0.28557 0.27198 0.17996 -0.03236 -0.03807 -0.01035 485 ARG A CB  
3867 C CG  . ARG A 485 ? 0.31384 0.30171 0.21023 -0.03486 -0.04268 -0.01100 485 ARG A CG  
3868 C CD  . ARG A 485 ? 0.23306 0.22258 0.14060 -0.03287 -0.04489 -0.00691 485 ARG A CD  
3869 N NE  . ARG A 485 ? 0.25227 0.24497 0.16170 -0.03200 -0.04738 -0.00076 485 ARG A NE  
3870 C CZ  . ARG A 485 ? 0.23329 0.22794 0.15238 -0.03000 -0.04912 0.00326  485 ARG A CZ  
3871 N NH1 . ARG A 485 ? 0.27129 0.26545 0.19868 -0.02879 -0.04852 0.00205  485 ARG A NH1 
3872 N NH2 . ARG A 485 ? 0.24558 0.24273 0.16627 -0.02923 -0.05139 0.00865  485 ARG A NH2 
3873 N N   . MET A 486 ? 0.26192 0.24338 0.14930 -0.02885 -0.02638 -0.01559 486 MET A N   
3874 C CA  . MET A 486 ? 0.29343 0.27449 0.17950 -0.02695 -0.02242 -0.01458 486 MET A CA  
3875 C C   . MET A 486 ? 0.29620 0.27769 0.17203 -0.02925 -0.02012 -0.01777 486 MET A C   
3876 O O   . MET A 486 ? 0.31144 0.29432 0.18362 -0.02919 -0.01853 -0.01532 486 MET A O   
3877 C CB  . MET A 486 ? 0.29014 0.26821 0.18345 -0.02352 -0.01847 -0.01652 486 MET A CB  
3878 C CG  . MET A 486 ? 0.29335 0.27142 0.19630 -0.02101 -0.01982 -0.01291 486 MET A CG  
3879 S SD  . MET A 486 ? 0.28552 0.26567 0.19094 -0.01928 -0.02033 -0.00659 486 MET A SD  
3880 C CE  . MET A 486 ? 0.26504 0.24349 0.16841 -0.01754 -0.01482 -0.00846 486 MET A CE  
3881 N N   . ALA A 487 ? 0.30253 0.28286 0.17375 -0.03139 -0.01976 -0.02336 487 ALA A N   
3882 C CA  . ALA A 487 ? 0.33777 0.31886 0.19874 -0.03387 -0.01742 -0.02701 487 ALA A CA  
3883 C C   . ALA A 487 ? 0.36561 0.35099 0.22101 -0.03623 -0.02066 -0.02277 487 ALA A C   
3884 O O   . ALA A 487 ? 0.37606 0.36348 0.22731 -0.03639 -0.01821 -0.02191 487 ALA A O   
3885 C CB  . ALA A 487 ? 0.31710 0.29612 0.17684 -0.03501 -0.01639 -0.03398 487 ALA A CB  
3886 N N   . ALA A 488 ? 0.37434 0.36132 0.23057 -0.03793 -0.02618 -0.01982 488 ALA A N   
3887 C CA  . ALA A 488 ? 0.40061 0.39164 0.25324 -0.03976 -0.02965 -0.01486 488 ALA A CA  
3888 C C   . ALA A 488 ? 0.39904 0.39124 0.25330 -0.03832 -0.02962 -0.00845 488 ALA A C   
3889 O O   . ALA A 488 ? 0.40511 0.40004 0.25546 -0.03937 -0.03007 -0.00505 488 ALA A O   
3890 C CB  . ALA A 488 ? 0.35196 0.34457 0.20674 -0.04159 -0.03573 -0.01292 488 ALA A CB  
3891 N N   . ALA A 489 ? 0.37338 0.36333 0.23360 -0.03591 -0.02906 -0.00671 489 ALA A N   
3892 C CA  . ALA A 489 ? 0.39226 0.38287 0.25577 -0.03392 -0.02839 -0.00110 489 ALA A CA  
3893 C C   . ALA A 489 ? 0.39300 0.38332 0.25141 -0.03377 -0.02321 -0.00266 489 ALA A C   
3894 O O   . ALA A 489 ? 0.45307 0.44528 0.31005 -0.03396 -0.02310 0.00178  489 ALA A O   
3895 C CB  . ALA A 489 ? 0.33347 0.32217 0.20901 -0.02989 -0.02786 0.00042  489 ALA A CB  
3896 N N   . TYR A 490 ? 0.38639 0.37455 0.24399 -0.03298 -0.01868 -0.00885 490 TYR A N   
3897 C CA  . TYR A 490 ? 0.39273 0.38120 0.24790 -0.03224 -0.01334 -0.01081 490 TYR A CA  
3898 C C   . TYR A 490 ? 0.42418 0.41563 0.27266 -0.03448 -0.01259 -0.01205 490 TYR A C   
3899 O O   . TYR A 490 ? 0.49896 0.49147 0.34516 -0.03420 -0.00857 -0.01266 490 TYR A O   
3900 C CB  . TYR A 490 ? 0.35988 0.34511 0.21778 -0.03031 -0.00886 -0.01692 490 TYR A CB  
3901 C CG  . TYR A 490 ? 0.32872 0.31220 0.19597 -0.02644 -0.00684 -0.01486 490 TYR A CG  
3902 C CD1 . TYR A 490 ? 0.30984 0.29179 0.18588 -0.02417 -0.00922 -0.01300 490 TYR A CD1 
3903 C CD2 . TYR A 490 ? 0.29510 0.27882 0.16256 -0.02516 -0.00250 -0.01482 490 TYR A CD2 
3904 C CE1 . TYR A 490 ? 0.31890 0.29949 0.20298 -0.02082 -0.00738 -0.01133 490 TYR A CE1 
3905 C CE2 . TYR A 490 ? 0.27293 0.25525 0.14886 -0.02180 -0.00093 -0.01304 490 TYR A CE2 
3906 C CZ  . TYR A 490 ? 0.25505 0.23574 0.13890 -0.01969 -0.00340 -0.01138 490 TYR A CZ  
3907 O OH  . TYR A 490 ? 0.23607 0.21554 0.12761 -0.01662 -0.00185 -0.00985 490 TYR A OH  
3908 N N   . ARG A 491 ? 0.44829 0.44120 0.29357 -0.03677 -0.01635 -0.01238 491 ARG A N   
3909 C CA  . ARG A 491 ? 0.47154 0.46731 0.30972 -0.03919 -0.01616 -0.01299 491 ARG A CA  
3910 C C   . ARG A 491 ? 0.43981 0.43858 0.27581 -0.04071 -0.01967 -0.00585 491 ARG A C   
3911 O O   . ARG A 491 ? 0.47801 0.47915 0.30813 -0.04244 -0.01852 -0.00518 491 ARG A O   
3912 C CB  . ARG A 491 ? 0.49850 0.49418 0.33383 -0.04109 -0.01818 -0.01768 491 ARG A CB  
3913 C CG  . ARG A 491 ? 0.55779 0.55111 0.39287 -0.04024 -0.01366 -0.02552 491 ARG A CG  
3914 C CD  . ARG A 491 ? 0.50620 0.49964 0.33738 -0.04253 -0.01554 -0.03008 491 ARG A CD  
3915 N NE  . ARG A 491 ? 0.46737 0.45849 0.30325 -0.04247 -0.01875 -0.03169 491 ARG A NE  
3916 C CZ  . ARG A 491 ? 0.49517 0.48767 0.33196 -0.04405 -0.02439 -0.02805 491 ARG A CZ  
3917 N NH1 . ARG A 491 ? 0.53675 0.53275 0.37036 -0.04565 -0.02769 -0.02240 491 ARG A NH1 
3918 N NH2 . ARG A 491 ? 0.53961 0.52996 0.38113 -0.04404 -0.02683 -0.02998 491 ARG A NH2 
3919 N N   . ARG A 492 ? 0.43001 0.42867 0.27093 -0.04008 -0.02390 -0.00045 492 ARG A N   
3920 C CA  . ARG A 492 ? 0.46701 0.46806 0.30755 -0.04108 -0.02729 0.00676  492 ARG A CA  
3921 C C   . ARG A 492 ? 0.52095 0.52159 0.36357 -0.03953 -0.02457 0.01060  492 ARG A C   
3922 O O   . ARG A 492 ? 0.50767 0.51004 0.34974 -0.04042 -0.02662 0.01643  492 ARG A O   
3923 C CB  . ARG A 492 ? 0.47044 0.47169 0.31653 -0.04089 -0.03321 0.01093  492 ARG A CB  
3924 N N   . SER A 493 ? 0.48859 0.48692 0.33390 -0.03734 -0.02011 0.00753  493 SER A N   
3925 C CA  . SER A 493 ? 0.49975 0.49770 0.34713 -0.03599 -0.01721 0.01076  493 SER A CA  
3926 C C   . SER A 493 ? 0.51489 0.51532 0.35610 -0.03779 -0.01434 0.01089  493 SER A C   
3927 O O   . SER A 493 ? 0.53833 0.53957 0.38023 -0.03797 -0.01442 0.01607  493 SER A O   
3928 C CB  . SER A 493 ? 0.45566 0.45073 0.30740 -0.03337 -0.01331 0.00735  493 SER A CB  
3929 O OG  . SER A 493 ? 0.50720 0.50039 0.36008 -0.03278 -0.01337 0.00206  493 SER A OG  
3930 N N   . LYS A 494 ? 0.54098 0.54245 0.37666 -0.03910 -0.01195 0.00538  494 LYS A N   
3931 C CA  . LYS A 494 ? 0.51401 0.51802 0.34333 -0.04095 -0.00898 0.00484  494 LYS A CA  
3932 C C   . LYS A 494 ? 0.50902 0.51303 0.34035 -0.03965 -0.00435 0.00592  494 LYS A C   
3933 O O   . LYS A 494 ? 0.52017 0.52557 0.34801 -0.04017 0.00010  0.00267  494 LYS A O   
3934 C CB  . LYS A 494 ? 0.48834 0.49496 0.31331 -0.04370 -0.01321 0.01034  494 LYS A CB  
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