data_8Z8K
# 
_entry.id   8Z8K 
# 
_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   8Z8K         pdb_00008z8k 10.2210/pdb8z8k/pdb 
WWPDB D_1300047201 ?            ?                   
# 
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                        8Z8K 
_pdbx_database_status.recvd_initial_deposition_date   2024-04-22 
_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 300 ns after illumination of the dark-adapted form' 8Z44 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 
PDB 'The same protein 300 us after illumination of the dark-adapted form' 8Z45 unspecified 
PDB 'The same protein 1 ms after illumination of the dark-adapted form'   8Z4K unspecified 
PDB 'The same protein 7 ms after illumination of the dark-adapted form'   8Z4M unspecified 
PDB 'The same protein 33 ms after illumination of the dark-adapted form'  8Z4P unspecified 
PDB 'The same protein 66 ms after illumination of the dark-adapted form'  8Z4U unspecified 
PDB 'The same protein 100 ms after illumination of the dark-adapted form' 8Z6I unspecified 
PDB 'The same protein 133 ms after illumination of the dark-adapted form' 8Z6J unspecified 
PDB 'The same protein 166 ms after illumination of the dark-adapted form' 8Z6K unspecified 
PDB .                                                                     8Z8F 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    96 ? ? ? ? 
# 
_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 ?   ?   ?   A . n 
A 1 494 LYS 494 494 ?   ?   ?   A . n 
A 1 495 GLY 495 495 ?   ?   ?   A . n 
A 1 496 GLU 496 496 ?   ?   ?   A . n 
A 1 497 LYS 497 497 ?   ?   ?   A . n 
A 1 498 LEU 498 498 ?   ?   ?   A . n 
A 1 499 ALA 499 499 ?   ?   ?   A . n 
A 1 500 ALA 500 500 ?   ?   ?   A . n 
A 1 501 ALA 501 501 ?   ?   ?   A . n 
A 1 502 LEU 502 502 ?   ?   ?   A . n 
A 1 503 GLU 503 503 ?   ?   ?   A . n 
A 1 504 HIS 504 504 ?   ?   ?   A . n 
A 1 505 HIS 505 505 ?   ?   ?   A . n 
A 1 506 HIS 506 506 ?   ?   ?   A . n 
A 1 507 HIS 507 507 ?   ?   ?   A . n 
A 1 508 HIS 508 508 ?   ?   ?   A . n 
A 1 509 HIS 509 509 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        FAD 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   FAD 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 FAD 1  601 602 FAD FAD A . 
C 3 CL  1  602 1   CL  CL  A . 
D 4 HOH 1  701 60  HOH HOH A . 
D 4 HOH 2  702 1   HOH HOH A . 
D 4 HOH 3  703 38  HOH HOH A . 
D 4 HOH 4  704 44  HOH HOH A . 
D 4 HOH 5  705 42  HOH HOH A . 
D 4 HOH 6  706 52  HOH HOH A . 
D 4 HOH 7  707 48  HOH HOH A . 
D 4 HOH 8  708 34  HOH HOH A . 
D 4 HOH 9  709 14  HOH HOH A . 
D 4 HOH 10 710 47  HOH HOH A . 
D 4 HOH 11 711 32  HOH HOH A . 
D 4 HOH 12 712 12  HOH HOH A . 
D 4 HOH 13 713 36  HOH HOH A . 
D 4 HOH 14 714 88  HOH HOH A . 
D 4 HOH 15 715 6   HOH HOH A . 
D 4 HOH 16 716 13  HOH HOH A . 
D 4 HOH 17 717 3   HOH HOH A . 
D 4 HOH 18 718 40  HOH HOH A . 
D 4 HOH 19 719 54  HOH HOH A . 
D 4 HOH 20 720 26  HOH HOH A . 
D 4 HOH 21 721 64  HOH HOH A . 
D 4 HOH 22 722 16  HOH HOH A . 
D 4 HOH 23 723 68  HOH HOH A . 
D 4 HOH 24 724 94  HOH HOH A . 
D 4 HOH 25 725 51  HOH HOH A . 
D 4 HOH 26 726 95  HOH HOH A . 
D 4 HOH 27 727 33  HOH HOH A . 
D 4 HOH 28 728 59  HOH HOH A . 
D 4 HOH 29 729 29  HOH HOH A . 
D 4 HOH 30 730 27  HOH HOH A . 
D 4 HOH 31 731 89  HOH HOH A . 
D 4 HOH 32 732 55  HOH HOH A . 
D 4 HOH 33 733 65  HOH HOH A . 
D 4 HOH 34 734 53  HOH HOH A . 
D 4 HOH 35 735 49  HOH HOH A . 
D 4 HOH 36 736 69  HOH HOH A . 
D 4 HOH 37 737 24  HOH HOH A . 
D 4 HOH 38 738 75  HOH HOH A . 
D 4 HOH 39 739 77  HOH HOH A . 
D 4 HOH 40 740 20  HOH HOH A . 
D 4 HOH 41 741 96  HOH HOH A . 
D 4 HOH 42 742 2   HOH HOH A . 
D 4 HOH 43 743 56  HOH HOH A . 
D 4 HOH 44 744 87  HOH HOH A . 
D 4 HOH 45 745 43  HOH HOH A . 
D 4 HOH 46 746 39  HOH HOH A . 
D 4 HOH 47 747 37  HOH HOH A . 
D 4 HOH 48 748 7   HOH HOH A . 
D 4 HOH 49 749 31  HOH HOH A . 
D 4 HOH 50 750 85  HOH HOH A . 
D 4 HOH 51 751 82  HOH HOH A . 
D 4 HOH 52 752 8   HOH HOH A . 
D 4 HOH 53 753 21  HOH HOH A . 
D 4 HOH 54 754 74  HOH HOH A . 
D 4 HOH 55 755 45  HOH HOH A . 
D 4 HOH 56 756 11  HOH HOH A . 
D 4 HOH 57 757 78  HOH HOH A . 
D 4 HOH 58 758 58  HOH HOH A . 
D 4 HOH 59 759 80  HOH HOH A . 
D 4 HOH 60 760 46  HOH HOH A . 
D 4 HOH 61 761 90  HOH HOH A . 
D 4 HOH 62 762 17  HOH HOH A . 
D 4 HOH 63 763 84  HOH HOH A . 
D 4 HOH 64 764 93  HOH HOH A . 
D 4 HOH 65 765 91  HOH HOH A . 
D 4 HOH 66 766 79  HOH HOH A . 
D 4 HOH 67 767 62  HOH HOH A . 
D 4 HOH 68 768 66  HOH HOH A . 
D 4 HOH 69 769 15  HOH HOH A . 
D 4 HOH 70 770 25  HOH HOH A . 
D 4 HOH 71 771 83  HOH HOH A . 
D 4 HOH 72 772 18  HOH HOH A . 
D 4 HOH 73 773 4   HOH HOH A . 
D 4 HOH 74 774 70  HOH HOH A . 
D 4 HOH 75 775 72  HOH HOH A . 
D 4 HOH 76 776 67  HOH HOH A . 
D 4 HOH 77 777 92  HOH HOH A . 
D 4 HOH 78 778 10  HOH HOH A . 
D 4 HOH 79 779 73  HOH HOH A . 
D 4 HOH 80 780 50  HOH HOH A . 
D 4 HOH 81 781 41  HOH HOH A . 
D 4 HOH 82 782 23  HOH HOH A . 
D 4 HOH 83 783 76  HOH HOH A . 
D 4 HOH 84 784 63  HOH HOH A . 
D 4 HOH 85 785 5   HOH HOH A . 
D 4 HOH 86 786 61  HOH HOH A . 
D 4 HOH 87 787 30  HOH HOH A . 
D 4 HOH 88 788 57  HOH HOH A . 
D 4 HOH 89 789 35  HOH HOH A . 
D 4 HOH 90 790 71  HOH HOH A . 
D 4 HOH 91 791 81  HOH HOH A . 
D 4 HOH 92 792 28  HOH HOH A . 
D 4 HOH 93 793 86  HOH HOH A . 
D 4 HOH 94 794 22  HOH HOH A . 
D 4 HOH 95 795 9   HOH HOH A . 
D 4 HOH 96 796 19  HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A GLY 3   ? N   ? A GLY 3   N   
2  1 Y 1 A GLY 3   ? CA  ? A GLY 3   CA  
3  1 Y 0 A LYS 28  ? CD  ? A LYS 28  CD  
4  1 Y 0 A LYS 28  ? CE  ? A LYS 28  CE  
5  1 Y 0 A LYS 28  ? NZ  ? A LYS 28  NZ  
6  1 Y 0 A LEU 44  ? CG  ? A LEU 44  CG  
7  1 Y 0 A LEU 44  ? CD1 ? A LEU 44  CD1 
8  1 Y 0 A LEU 44  ? CD2 ? A LEU 44  CD2 
9  1 Y 0 A GLN 45  ? CG  ? A GLN 45  CG  
10 1 Y 0 A GLN 45  ? CD  ? A GLN 45  CD  
11 1 Y 0 A GLN 45  ? OE1 ? A GLN 45  OE1 
12 1 Y 0 A GLN 45  ? NE2 ? A GLN 45  NE2 
13 1 Y 0 A GLN 46  ? CG  ? A GLN 46  CG  
14 1 Y 0 A GLN 46  ? CD  ? A GLN 46  CD  
15 1 Y 0 A GLN 46  ? OE1 ? A GLN 46  OE1 
16 1 Y 0 A GLN 46  ? NE2 ? A GLN 46  NE2 
17 1 Y 1 A LYS 50  ? CG  ? A LYS 50  CG  
18 1 Y 1 A LYS 50  ? CD  ? A LYS 50  CD  
19 1 Y 1 A LYS 50  ? CE  ? A LYS 50  CE  
20 1 Y 1 A LYS 50  ? NZ  ? A LYS 50  NZ  
21 1 Y 0 A LYS 83  ? CD  ? A LYS 83  CD  
22 1 Y 0 A LYS 83  ? CE  ? A LYS 83  CE  
23 1 Y 0 A LYS 83  ? NZ  ? A LYS 83  NZ  
24 1 Y 0 A ARG 119 ? CG  ? A ARG 119 CG  
25 1 Y 0 A ARG 119 ? CD  ? A ARG 119 CD  
26 1 Y 0 A ARG 119 ? NE  ? A ARG 119 NE  
27 1 Y 0 A ARG 119 ? CZ  ? A ARG 119 CZ  
28 1 Y 0 A ARG 119 ? NH1 ? A ARG 119 NH1 
29 1 Y 0 A ARG 119 ? NH2 ? A ARG 119 NH2 
30 1 Y 0 A ILE 132 ? CD1 ? A ILE 132 CD1 
31 1 Y 0 A GLN 155 ? OE1 ? A GLN 155 OE1 
32 1 Y 0 A GLN 155 ? NE2 ? A GLN 155 NE2 
33 1 Y 0 A LYS 159 ? CD  ? A LYS 159 CD  
34 1 Y 0 A LYS 159 ? CE  ? A LYS 159 CE  
35 1 Y 0 A LYS 159 ? NZ  ? A LYS 159 NZ  
36 1 Y 0 A GLU 183 ? CD  ? A GLU 183 CD  
37 1 Y 0 A GLU 183 ? OE1 ? A GLU 183 OE1 
38 1 Y 0 A GLU 183 ? OE2 ? A GLU 183 OE2 
39 1 Y 0 A LYS 204 ? CD  ? A LYS 204 CD  
40 1 Y 0 A LYS 204 ? CE  ? A LYS 204 CE  
41 1 Y 0 A LYS 204 ? NZ  ? A LYS 204 NZ  
42 1 Y 0 A LYS 212 ? CE  ? A LYS 212 CE  
43 1 Y 0 A LYS 212 ? NZ  ? A LYS 212 NZ  
44 1 Y 0 A LYS 230 ? CE  ? A LYS 230 CE  
45 1 Y 0 A LYS 230 ? NZ  ? A LYS 230 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 ? NH1 ? A ARG 277 NH1 
55 1 Y 0 A ARG 277 ? NH2 ? A ARG 277 NH2 
56 1 Y 0 A ARG 310 ? CG  ? A ARG 310 CG  
57 1 Y 0 A ARG 310 ? CD  ? A ARG 310 CD  
58 1 Y 0 A ARG 310 ? NE  ? A ARG 310 NE  
59 1 Y 0 A ARG 310 ? CZ  ? A ARG 310 CZ  
60 1 Y 0 A ARG 310 ? NH1 ? A ARG 310 NH1 
61 1 Y 0 A ARG 310 ? NH2 ? A ARG 310 NH2 
62 1 Y 0 A LYS 423 ? CG  ? A LYS 423 CG  
63 1 Y 0 A LYS 423 ? CD  ? A LYS 423 CD  
64 1 Y 0 A LYS 423 ? CE  ? A LYS 423 CE  
65 1 Y 0 A LYS 423 ? NZ  ? A LYS 423 NZ  
66 1 Y 0 A GLU 427 ? OE1 ? A GLU 427 OE1 
67 1 Y 0 A GLU 427 ? OE2 ? A GLU 427 OE2 
68 1 Y 0 A ARG 429 ? CD  ? A ARG 429 CD  
69 1 Y 0 A ARG 429 ? NE  ? A ARG 429 NE  
70 1 Y 0 A ARG 429 ? CZ  ? A ARG 429 CZ  
71 1 Y 0 A ARG 429 ? NH1 ? A ARG 429 NH1 
72 1 Y 0 A ARG 429 ? NH2 ? A ARG 429 NH2 
73 1 Y 0 A LYS 439 ? CD  ? A LYS 439 CD  
74 1 Y 0 A LYS 439 ? CE  ? A LYS 439 CE  
75 1 Y 0 A LYS 439 ? NZ  ? A LYS 439 NZ  
76 1 Y 0 A LYS 444 ? CE  ? A LYS 444 CE  
77 1 Y 0 A LYS 444 ? NZ  ? A LYS 444 NZ  
78 1 Y 0 A GLU 455 ? CG  ? A GLU 455 CG  
79 1 Y 0 A GLU 455 ? CD  ? A GLU 455 CD  
80 1 Y 0 A GLU 455 ? OE1 ? A GLU 455 OE1 
81 1 Y 0 A GLU 455 ? OE2 ? A GLU 455 OE2 
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 ? CD  ? A LYS 459 CD  
86 1 Y 0 A LYS 459 ? CE  ? A LYS 459 CE  
87 1 Y 0 A LYS 459 ? NZ  ? A LYS 459 NZ  
88 1 Y 0 A LYS 480 ? CG  ? A LYS 480 CG  
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 491 ? CG  ? A ARG 491 CG  
93 1 Y 1 A ARG 491 ? CD  ? A ARG 491 CD  
94 1 Y 1 A ARG 491 ? NE  ? A ARG 491 NE  
95 1 Y 1 A ARG 491 ? CZ  ? A ARG 491 CZ  
96 1 Y 1 A ARG 491 ? NH1 ? A ARG 491 NH1 
97 1 Y 1 A ARG 491 ? NH2 ? A ARG 491 NH2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX    ? ? ? 1.20.1_4487 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? CrystFEL  ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? pointless ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? REFMAC    ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8Z8K 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     50.740 
_cell.length_a_esd                 ? 
_cell.length_b                     65.450 
_cell.length_b_esd                 ? 
_cell.length_c                     152.950 
_cell.length_c_esd                 ? 
_cell.volume                       507936.702 
_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                         8Z8K 
_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                   8Z8K 
_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             2.20 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          44.01 
_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         2021-11-05 
_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                          25.83 
_reflns.entry_id                                       8Z8K 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.8 
_reflns.d_resolution_low                               33.02 
_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                                     48171 
_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                           99.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                1138 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          8.71 
_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                                   0.999 
_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                                    1.80 
_reflns_shell.d_res_low                                     1.84 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.00 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2360 
_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                               67.2 
_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                                  0.385 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          100 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               27.78 
_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                                 8Z8K 
_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                            2.20 
_refine.ls_d_res_low                             27.71 
_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                     26607 
_refine.ls_number_reflns_R_free                  832 
_refine.ls_number_reflns_R_work                  25775 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.87 
_refine.ls_percent_reflns_R_free                 3.13 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2129 
_refine.ls_R_factor_R_free                       0.2380 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2120 
_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                 28.9713 
_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                            0.2998 
_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                       2.20 
_refine_hist.d_res_low                        27.71 
_refine_hist.number_atoms_solvent             96 
_refine_hist.number_atoms_total               4047 
_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        3897 
_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' ? 0.0029  ? 4143 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.5405  ? 5672 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0390  ? 592  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0047  ? 733  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 12.8178 ? 1494 ? 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' 2.20 2.34  . . 140 4214 100.00 . . . . 0.3996 . . . . . . . . . . . 0.3962 
'X-RAY DIFFRACTION' 2.34 2.52  . . 125 4269 100.00 . . . . 0.3512 . . . . . . . . . . . 0.3904 
'X-RAY DIFFRACTION' 2.52 2.77  . . 153 4206 100.00 . . . . 0.3036 . . . . . . . . . . . 0.2954 
'X-RAY DIFFRACTION' 2.77 3.17  . . 142 4292 99.98  . . . . 0.2455 . . . . . . . . . . . 0.2744 
'X-RAY DIFFRACTION' 3.17 3.99  . . 138 4281 99.71  . . . . 0.1688 . . . . . . . . . . . 0.1871 
'X-RAY DIFFRACTION' 3.99 27.71 . . 134 4513 99.57  . . . . 0.1302 . . . . . . . . . . . 0.1578 
# 
_struct.entry_id                     8Z8K 
_struct.title                        'SFX structure of CraCRY 233 ms 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        8Z8K 
_struct_keywords.text            'photoreceptor, FLAVOPROTEIN, time-resolved crystallography, 233 ms 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              8Z8K 
_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 8Z8K LYS A 497 ? UNP A8J8W0 ? ? 'expression tag' 497 1  
1 8Z8K LEU A 498 ? UNP A8J8W0 ? ? 'expression tag' 498 2  
1 8Z8K ALA A 499 ? UNP A8J8W0 ? ? 'expression tag' 499 3  
1 8Z8K ALA A 500 ? UNP A8J8W0 ? ? 'expression tag' 500 4  
1 8Z8K ALA A 501 ? UNP A8J8W0 ? ? 'expression tag' 501 5  
1 8Z8K LEU A 502 ? UNP A8J8W0 ? ? 'expression tag' 502 6  
1 8Z8K GLU A 503 ? UNP A8J8W0 ? ? 'expression tag' 503 7  
1 8Z8K HIS A 504 ? UNP A8J8W0 ? ? 'expression tag' 504 8  
1 8Z8K HIS A 505 ? UNP A8J8W0 ? ? 'expression tag' 505 9  
1 8Z8K HIS A 506 ? UNP A8J8W0 ? ? 'expression tag' 506 10 
1 8Z8K HIS A 507 ? UNP A8J8W0 ? ? 'expression tag' 507 11 
1 8Z8K HIS A 508 ? UNP A8J8W0 ? ? 'expression tag' 508 12 
1 8Z8K 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         -18   ? 
1 'SSA (A^2)'  20440 ? 
# 
_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   homology 
_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 HIS A 42  ? GLN A 46  ? HIS A 42  GLN A 46  5 ? 5  
HELX_P HELX_P3  AA3 SER A 52  ? ALA A 72  ? SER A 52  ALA A 72  1 ? 21 
HELX_P HELX_P4  AA4 LYS A 83  ? TRP A 95  ? LYS A 83  TRP A 95  1 ? 13 
HELX_P HELX_P5  AA5 GLU A 107 ? GLY A 125 ? GLU A 107 GLY A 125 1 ? 19 
HELX_P HELX_P6  AA6 ASP A 138 ? ASN A 146 ? ASP A 138 ASN A 146 1 ? 9  
HELX_P HELX_P7  AA7 THR A 153 ? GLY A 165 ? THR A 153 GLY A 165 1 ? 13 
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 ? HIS A 278 ? SER A 263 HIS A 278 1 ? 16 
HELX_P HELX_P13 AB4 SER A 287 ? SER A 303 ? SER A 287 SER A 303 1 ? 17 
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 ? TRP A 352 ? PHE A 339 TRP A 352 1 ? 14 
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 VAL A 418 ? LYS A 423 ? VAL A 418 LYS A 423 1 ? 6  
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 GLU A 448 ? ALA A 452 ? GLU A 448 ALA A 452 5 ? 5  
HELX_P HELX_P23 AC5 PRO A 453 ? GLY A 461 ? PRO A 453 GLY A 461 1 ? 9  
HELX_P HELX_P24 AC6 ASP A 474 ? ARG A 492 ? ASP A 474 ARG A 492 1 ? 19 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          PRO 
_struct_mon_prot_cis.label_seq_id           284 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           PRO 
_struct_mon_prot_cis.auth_seq_id            284 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    285 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     285 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       0.84 
# 
_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   ? TRP A 10  ? ASN A 6   TRP A 10  
AA1 4 GLN A 99  ? PHE A 102 ? GLN A 99  PHE A 102 
AA1 5 GLU A 127 ? VAL A 129 ? GLU A 127 VAL A 129 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O LEU A 78  ? O LEU A 78  N PRO A 35  ? N PRO A 35  
AA1 2 3 O TYR A 34  ? O TYR A 34  N SER A 7   ? N SER A 7   
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                   8Z8K 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 LYS A 13  ? ? -103.10 -163.70 
2  1 SER A 75  ? ? -120.31 -163.70 
3  1 SER A 133 ? ? -157.18 -13.04  
4  1 SER A 243 ? ? -96.45  39.68   
5  1 ALA A 249 ? ? -62.80  8.65    
6  1 ALA A 280 ? ? -85.47  30.29   
7  1 ARG A 336 ? ? -147.09 43.69   
8  1 THR A 368 ? ? -97.22  -118.13 
9  1 ASP A 371 ? ? -127.72 -58.89  
10 1 GLN A 390 ? ? -62.36  98.59   
11 1 PHE A 407 ? ? 64.10   -53.53  
# 
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 20.4360614004 8.86587605443  -17.7983111145 0.189403300002 ? -0.0205166298307  ? -0.0027421261655 
? 0.20345716677  ? -0.000894634482117 ? 0.209964652456 ? 0.482654375142 ? -0.349950901073 ? -0.123945879029   ? 1.4540606231   ? 
0.548691211214   ? 0.939927907573  ? 0.011328671986    ? 0.0476433917975 ? 0.0361915601003  ? -0.0942677600727 ? -0.029909362591   
? 0.0229012096411 ? -0.0497352916027 ? -0.0559543316216 ? 0.00766552355954 ? 
2 'X-RAY DIFFRACTION' ? refined 12.2065949827 -15.1237151976 -22.47034527   0.167554093779 ? -0.00025427530623 ? 0.00537901243253 
? 0.180410348254 ? -0.0115865863821   ? 0.172156583941 ? 0.16576630948  ? 0.0629977752901 ? -0.00174530522482 ? 0.279747429539 ? 
-0.0296677247389 ? 0.0355319737302 ? -0.00309979879697 ? 0.0175511380165 ? -0.0106078785201 ? -0.010026531845  ? -0.00174544731213 
? 0.0335334347942 ? 0.0139478009465  ? -0.0270002189484 ? 0.00819533707651 ? 
# 
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 159 A 164 ? ? 
;chain 'A' and (resid 3 through 164 )
;
2 'X-RAY DIFFRACTION' 2 A 160 A 165 ? A 487 A 492 ? ? 
;chain 'A' and (resid 165 through 492 )
;
# 
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 SER 493 ? A SER 493 
7  1 Y 1 A LYS 494 ? A LYS 494 
8  1 Y 1 A GLY 495 ? A GLY 495 
9  1 Y 1 A GLU 496 ? A GLU 496 
10 1 Y 1 A LYS 497 ? A LYS 497 
11 1 Y 1 A LEU 498 ? A LEU 498 
12 1 Y 1 A ALA 499 ? A ALA 499 
13 1 Y 1 A ALA 500 ? A ALA 500 
14 1 Y 1 A ALA 501 ? A ALA 501 
15 1 Y 1 A LEU 502 ? A LEU 502 
16 1 Y 1 A GLU 503 ? A GLU 503 
17 1 Y 1 A HIS 504 ? A HIS 504 
18 1 Y 1 A HIS 505 ? A HIS 505 
19 1 Y 1 A HIS 506 ? A HIS 506 
20 1 Y 1 A HIS 507 ? A HIS 507 
21 1 Y 1 A HIS 508 ? A HIS 508 
22 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               0.76 
_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                    8Z8K 
_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]   0.019708 
_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]   0.015279 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.006538 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C  ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
CL ? ? 9.50761 7.44341 ? ? 1.04373  23.83732 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N  ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O  ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
P  ? ? 9.51135 5.44231 ? ? 1.42069  35.72801 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S  ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    C  C     . GLY A 1 3   ? 29.75787  30.07748  -8.80385  1.000 48.82910 ? 3   GLY A C     1 
ATOM   2    O  O     . GLY A 1 3   ? 30.74686  30.62647  -8.31884  1.000 51.71311 ? 3   GLY A O     1 
ATOM   3    N  N     . VAL A 1 4   ? 28.98086  29.24247  -8.11487  1.000 48.33327 ? 4   VAL A N     1 
ATOM   4    C  CA    . VAL A 1 4   ? 29.45585  27.93947  -7.66487  1.000 42.30556 ? 4   VAL A CA    1 
ATOM   5    C  C     . VAL A 1 4   ? 28.95886  26.87048  -8.62688  1.000 37.69859 ? 4   VAL A C     1 
ATOM   6    O  O     . VAL A 1 4   ? 28.25888  27.17148  -9.59989  1.000 36.96636 ? 4   VAL A O     1 
ATOM   7    C  CB    . VAL A 1 4   ? 29.00183  27.64547  -6.22387  1.000 38.14042 ? 4   VAL A CB    1 
ATOM   8    C  CG1   . VAL A 1 4   ? 29.52281  28.71746  -5.27686  1.000 31.57101 ? 4   VAL A CG1   1 
ATOM   9    C  CG2   . VAL A 1 4   ? 27.48583  27.55347  -6.15390  1.000 31.56746 ? 4   VAL A CG2   1 
ATOM   10   N  N     . LYS A 1 5   ? 29.31486  25.61547  -8.36188  1.000 34.04864 ? 5   LYS A N     1 
ATOM   11   C  CA    . LYS A 1 5   ? 28.94487  24.49648  -9.22089  1.000 27.76811 ? 5   LYS A CA    1 
ATOM   12   C  C     . LYS A 1 5   ? 27.78986  23.73448  -8.57991  1.000 24.96511 ? 5   LYS A C     1 
ATOM   13   O  O     . LYS A 1 5   ? 27.95084  23.12347  -7.51791  1.000 24.78950 ? 5   LYS A O     1 
ATOM   14   C  CB    . LYS A 1 5   ? 30.13587  23.57248  -9.46487  1.000 23.59270 ? 5   LYS A CB    1 
ATOM   15   C  CG    . LYS A 1 5   ? 29.77788  22.31548  -10.24188 1.000 23.87686 ? 5   LYS A CG    1 
ATOM   16   C  CD    . LYS A 1 5   ? 31.01688  21.55448  -10.67787 1.000 20.10473 ? 5   LYS A CD    1 
ATOM   17   C  CE    . LYS A 1 5   ? 30.64589  20.30848  -11.46688 1.000 21.53460 ? 5   LYS A CE    1 
ATOM   18   N  NZ    . LYS A 1 5   ? 29.97888  19.28848  -10.61289 1.000 21.96889 ? 5   LYS A NZ    1 
ATOM   19   N  N     . ASN A 1 6   ? 26.62887  23.77648  -9.22692  1.000 25.14644 ? 6   ASN A N     1 
ATOM   20   C  CA    . ASN A 1 6   ? 25.46386  22.98948  -8.84194  1.000 24.41603 ? 6   ASN A CA    1 
ATOM   21   C  C     . ASN A 1 6   ? 25.07687  22.12449  -10.03095 1.000 21.63406 ? 6   ASN A C     1 
ATOM   22   O  O     . ASN A 1 6   ? 24.75189  22.64749  -11.10196 1.000 20.43405 ? 6   ASN A O     1 
ATOM   23   C  CB    . ASN A 1 6   ? 24.30385  23.89248  -8.41696  1.000 25.23416 ? 6   ASN A CB    1 
ATOM   24   C  CG    . ASN A 1 6   ? 24.64584  24.75748  -7.21995  1.000 29.37955 ? 6   ASN A CG    1 
ATOM   25   O  OD1   . ASN A 1 6   ? 25.17082  24.27147  -6.21694  1.000 29.96300 ? 6   ASN A OD1   1 
ATOM   26   N  ND2   . ASN A 1 6   ? 24.35884  26.05048  -7.32195  1.000 28.56389 ? 6   ASN A ND2   1 
ATOM   27   N  N     . SER A 1 7   ? 25.11987  20.80749  -9.84796  1.000 22.24922 ? 7   SER A N     1 
ATOM   28   C  CA    . SER A 1 7   ? 24.96788  19.86649  -10.94596 1.000 24.55771 ? 7   SER A CA    1 
ATOM   29   C  C     . SER A 1 7   ? 23.74788  18.97849  -10.73899 1.000 20.69172 ? 7   SER A C     1 
ATOM   30   O  O     . SER A 1 7   ? 23.23386  18.83049  -9.62599  1.000 17.64145 ? 7   SER A O     1 
ATOM   31   C  CB    . SER A 1 7   ? 26.22089  18.99649  -11.10095 1.000 21.18567 ? 7   SER A CB    1 
ATOM   32   O  OG    . SER A 1 7   ? 26.50387  18.29749  -9.90195  1.000 17.59175 ? 7   SER A OG    1 
ATOM   33   N  N     . ILE A 1 8   ? 23.29390  18.38250  -11.83899 1.000 23.22401 ? 8   ILE A N     1 
ATOM   34   C  CA    . ILE A 1 8   ? 22.17589  17.44850  -11.84701 1.000 21.30875 ? 8   ILE A CA    1 
ATOM   35   C  C     . ILE A 1 8   ? 22.64990  16.14750  -12.47601 1.000 20.22122 ? 8   ILE A C     1 
ATOM   36   O  O     . ILE A 1 8   ? 23.26292  16.16150  -13.55000 1.000 22.50571 ? 8   ILE A O     1 
ATOM   37   C  CB    . ILE A 1 8   ? 20.96691  18.00850  -12.61903 1.000 20.87200 ? 8   ILE A CB    1 
ATOM   38   C  CG1   . ILE A 1 8   ? 20.48790  19.32150  -12.00103 1.000 20.09154 ? 8   ILE A CG1   1 
ATOM   39   C  CG2   . ILE A 1 8   ? 19.83391  16.99051  -12.65305 1.000 19.00307 ? 8   ILE A CG2   1 
ATOM   40   C  CD1   . ILE A 1 8   ? 19.27791  19.90151  -12.69805 1.000 24.63315 ? 8   ILE A CD1   1 
ATOM   41   N  N     . ILE A 1 9   ? 22.36989  15.03250  -11.81202 1.000 16.47578 ? 9   ILE A N     1 
ATOM   42   C  CA    . ILE A 1 9   ? 22.65789  13.70450  -12.33902 1.000 16.05162 ? 9   ILE A CA    1 
ATOM   43   C  C     . ILE A 1 9   ? 21.31490  13.07150  -12.69004 1.000 18.59142 ? 9   ILE A C     1 
ATOM   44   O  O     . ILE A 1 9   ? 20.58288  12.59050  -11.81806 1.000 20.29976 ? 9   ILE A O     1 
ATOM   45   C  CB    . ILE A 1 9   ? 23.46588  12.85350  -11.34901 1.000 16.00400 ? 9   ILE A CB    1 
ATOM   46   C  CG1   . ILE A 1 9   ? 23.47188  11.37950  -11.76802 1.000 19.85248 ? 9   ILE A CG1   1 
ATOM   47   C  CG2   . ILE A 1 9   ? 22.96986  13.05049  -9.91702  1.000 22.39718 ? 9   ILE A CG2   1 
ATOM   48   C  CD1   . ILE A 1 9   ? 24.18590  11.12150  -13.07801 1.000 21.97828 ? 9   ILE A CD1   1 
ATOM   49   N  N     . TRP A 1 10  ? 20.99892  13.06851  -13.98105 1.000 24.50619 ? 10  TRP A N     1 
ATOM   50   C  CA    . TRP A 1 10  ? 19.70393  12.55151  -14.47707 1.000 20.39892 ? 10  TRP A CA    1 
ATOM   51   C  C     . TRP A 1 10  ? 19.71292  11.02851  -14.57308 1.000 19.47480 ? 10  TRP A C     1 
ATOM   52   O  O     . TRP A 1 10  ? 20.60393  10.43651  -15.18506 1.000 17.67505 ? 10  TRP A O     1 
ATOM   53   C  CB    . TRP A 1 10  ? 19.34395  13.20852  -15.81407 1.000 19.07270 ? 10  TRP A CB    1 
ATOM   54   C  CG    . TRP A 1 10  ? 17.93195  12.96652  -16.27410 1.000 21.50788 ? 10  TRP A CG    1 
ATOM   55   C  CD1   . TRP A 1 10  ? 16.90094  12.46952  -15.53811 1.000 26.47963 ? 10  TRP A CD1   1 
ATOM   56   C  CD2   . TRP A 1 10  ? 17.39497  13.21753  -17.58910 1.000 24.75683 ? 10  TRP A CD2   1 
ATOM   57   N  NE1   . TRP A 1 10  ? 15.76895  12.38853  -16.29713 1.000 20.52777 ? 10  TRP A NE1   1 
ATOM   58   C  CE2   . TRP A 1 10  ? 16.03697  12.83953  -17.55713 1.000 19.99021 ? 10  TRP A CE2   1 
ATOM   59   C  CE3   . TRP A 1 10  ? 17.92499  13.71553  -18.78209 1.000 23.25492 ? 10  TRP A CE3   1 
ATOM   60   C  CZ2   . TRP A 1 10  ? 15.20699  12.94554  -18.66714 1.000 20.06450 ? 10  TRP A CZ2   1 
ATOM   61   C  CZ3   . TRP A 1 10  ? 17.10001  13.83254  -19.87711 1.000 23.46013 ? 10  TRP A CZ3   1 
ATOM   62   C  CH2   . TRP A 1 10  ? 15.76501  13.44554  -19.82113 1.000 27.15912 ? 10  TRP A CH2   1 
ATOM   63   N  N     . PHE A 1 11  ? 18.71591  10.43551  -13.95509 1.000 19.06423 ? 11  PHE A N     1 
ATOM   64   C  CA    . PHE A 1 11  ? 18.59091  8.98351   -13.98510 1.000 19.91491 ? 11  PHE A CA    1 
ATOM   65   C  C     . PHE A 1 11  ? 17.45993  8.60652   -14.93312 1.000 19.91119 ? 11  PHE A C     1 
ATOM   66   O  O     . PHE A 1 11  ? 16.29192  8.90652   -14.66614 1.000 26.21317 ? 11  PHE A O     1 
ATOM   67   C  CB    . PHE A 1 11  ? 18.33889  8.42251   -12.58711 1.000 20.46646 ? 11  PHE A CB    1 
ATOM   68   C  CG    . PHE A 1 11  ? 19.53788  8.47550   -11.68309 1.000 18.76812 ? 11  PHE A CG    1 
ATOM   69   C  CD1   . PHE A 1 11  ? 20.57588  7.56850   -11.83307 1.000 15.61636 ? 11  PHE A CD1   1 
ATOM   70   C  CD2   . PHE A 1 11  ? 19.62286  9.42250   -10.67508 1.000 16.89378 ? 11  PHE A CD2   1 
ATOM   71   C  CE1   . PHE A 1 11  ? 21.67786  7.61050   -11.00206 1.000 15.63852 ? 11  PHE A CE1   1 
ATOM   72   C  CE2   . PHE A 1 11  ? 20.72385  9.46850   -9.83907  1.000 15.80753 ? 11  PHE A CE2   1 
ATOM   73   C  CZ    . PHE A 1 11  ? 21.75185  8.56149   -10.00405 1.000 15.74685 ? 11  PHE A CZ    1 
ATOM   74   N  N     . ARG A 1 12  ? 17.81412  7.96753   -16.04687 1.000 22.10819 ? 12  ARG A N     1 
ATOM   75   C  CA    . ARG A 1 12  ? 16.84984  7.29886   -16.91402 1.000 20.85526 ? 12  ARG A CA    1 
ATOM   76   C  C     . ARG A 1 12  ? 17.12174  5.79982   -16.88181 1.000 24.87510 ? 12  ARG A C     1 
ATOM   77   O  O     . ARG A 1 12  ? 16.30095  5.02965   -16.37792 1.000 30.92009 ? 12  ARG A O     1 
ATOM   78   C  CB    . ARG A 1 12  ? 16.91569  7.84291   -18.34429 1.000 24.87273 ? 12  ARG A CB    1 
ATOM   79   C  CG    . ARG A 1 12  ? 16.81204  9.35743   -18.46114 1.000 22.22034 ? 12  ARG A CG    1 
ATOM   80   C  CD    . ARG A 1 12  ? 18.18662  10.01108  -18.48348 1.000 19.79825 ? 12  ARG A CD    1 
ATOM   81   N  NE    . ARG A 1 12  ? 19.02029  9.49207   -19.56122 1.000 21.18982 ? 12  ARG A NE    1 
ATOM   82   C  CZ    . ARG A 1 12  ? 19.04844  9.98539   -20.79166 1.000 27.15198 ? 12  ARG A CZ    1 
ATOM   83   N  NH1   . ARG A 1 12  ? 18.30113  11.02041  -21.13906 1.000 31.03977 ? 12  ARG A NH1   1 
ATOM   84   N  NH2   . ARG A 1 12  ? 19.84713  9.42661   -21.69659 1.000 33.24329 ? 12  ARG A NH2   1 
ATOM   85   N  N     . LYS A 1 13  ? 18.25696  5.36753   -17.41112 1.000 27.83362 ? 13  LYS A N     1 
ATOM   86   C  CA    . LYS A 1 13  ? 18.82395  4.06452   -17.13211 1.000 23.85991 ? 13  LYS A CA    1 
ATOM   87   C  C     . LYS A 1 13  ? 19.97894  4.25952   -16.14810 1.000 19.47920 ? 13  LYS A C     1 
ATOM   88   O  O     . LYS A 1 13  ? 20.09993  5.31852   -15.52009 1.000 18.35750 ? 13  LYS A O     1 
ATOM   89   C  CB    . LYS A 1 13  ? 19.25797  3.38953   -18.43811 1.000 25.08915 ? 13  LYS A CB    1 
ATOM   90   C  CG    . LYS A 1 13  ? 18.12298  3.11053   -19.40713 1.000 16.66284 ? 13  LYS A CG    1 
ATOM   91   C  CD    . LYS A 1 13  ? 18.64800  2.46254   -20.67612 1.000 26.56480 ? 13  LYS A CD    1 
ATOM   92   C  CE    . LYS A 1 13  ? 17.52002  2.09154   -21.62314 1.000 33.98859 ? 13  LYS A CE    1 
ATOM   93   N  NZ    . LYS A 1 13  ? 18.03203  1.41755   -22.85014 1.000 27.12599 ? 13  LYS A NZ    1 
ATOM   94   N  N     . GLY A 1 14  ? 20.83893  3.25452   -16.01709 1.000 28.40360 ? 14  GLY A N     1 
ATOM   95   C  CA    . GLY A 1 14  ? 21.97192  3.37151   -15.11207 1.000 27.45118 ? 14  GLY A CA    1 
ATOM   96   C  C     . GLY A 1 14  ? 21.57390  3.63751   -13.67707 1.000 27.24249 ? 14  GLY A C     1 
ATOM   97   O  O     . GLY A 1 14  ? 22.23189  4.42550   -12.98506 1.000 25.84904 ? 14  GLY A O     1 
ATOM   98   N  N     . LEU A 1 15  ? 20.49689  3.00351   -13.21609 1.000 22.73252 ? 15  LEU A N     1 
ATOM   99   C  CA    . LEU A 1 15  ? 20.03187  3.17450   -11.84610 1.000 19.79707 ? 15  LEU A CA    1 
ATOM   100  C  C     . LEU A 1 15  ? 20.99685  2.50650   -10.87509 1.000 19.86286 ? 15  LEU A C     1 
ATOM   101  O  O     . LEU A 1 15  ? 20.65684  1.50150   -10.24209 1.000 19.67522 ? 15  LEU A O     1 
ATOM   102  C  CB    . LEU A 1 15  ? 18.62286  2.59751   -11.69112 1.000 27.01977 ? 15  LEU A CB    1 
ATOM   103  C  CG    . LEU A 1 15  ? 17.61788  3.03051   -12.76114 1.000 18.76812 ? 15  LEU A CG    1 
ATOM   104  C  CD1   . LEU A 1 15  ? 16.32588  2.24251   -12.63416 1.000 20.08921 ? 15  LEU A CD1   1 
ATOM   105  C  CD2   . LEU A 1 15  ? 17.34888  4.52551   -12.67413 1.000 23.49799 ? 15  LEU A CD2   1 
ATOM   106  N  N     . ARG A 1 16  ? 22.20150  3.05777   -10.75291 1.000 16.80723 ? 16  ARG A N     1 
ATOM   107  C  CA    . ARG A 1 16  ? 23.24237  2.44072   -9.94555  1.000 18.26146 ? 16  ARG A CA    1 
ATOM   108  C  C     . ARG A 1 16  ? 24.23864  3.50790   -9.52225  1.000 21.79813 ? 16  ARG A C     1 
ATOM   109  O  O     . ARG A 1 16  ? 24.31369  4.58722   -10.11550 1.000 21.23343 ? 16  ARG A O     1 
ATOM   110  C  CB    . ARG A 1 16  ? 23.95296  1.32064   -10.71308 1.000 18.09169 ? 16  ARG A CB    1 
ATOM   111  C  CG    . ARG A 1 16  ? 24.70113  1.80415   -11.94831 1.000 23.90314 ? 16  ARG A CG    1 
ATOM   112  C  CD    . ARG A 1 16  ? 25.32670  0.64955   -12.71560 1.000 20.59140 ? 16  ARG A CD    1 
ATOM   113  N  NE    . ARG A 1 16  ? 26.17931  1.11704   -13.80188 1.000 24.10389 ? 16  ARG A NE    1 
ATOM   114  C  CZ    . ARG A 1 16  ? 25.76597  1.32000   -15.04524 1.000 19.85144 ? 16  ARG A CZ    1 
ATOM   115  N  NH1   . ARG A 1 16  ? 24.51202  1.09589   -15.40206 1.000 19.09745 ? 16  ARG A NH1   1 
ATOM   116  N  NH2   . ARG A 1 16  ? 26.63265  1.75936   -15.95326 1.000 22.65189 ? 16  ARG A NH2   1 
ATOM   117  N  N     . LEU A 1 17  ? 25.00182  3.18848   -8.48002  1.000 20.54562 ? 17  LEU A N     1 
ATOM   118  C  CA    . LEU A 1 17  ? 26.09981  4.03648   -8.03600  1.000 23.08018 ? 17  LEU A CA    1 
ATOM   119  C  C     . LEU A 1 17  ? 27.45982  3.51248   -8.46698  1.000 19.90581 ? 17  LEU A C     1 
ATOM   120  O  O     . LEU A 1 17  ? 28.38882  4.30648   -8.64797  1.000 21.94950 ? 17  LEU A O     1 
ATOM   121  C  CB    . LEU A 1 17  ? 26.07479  4.19247   -6.51100  1.000 22.18228 ? 17  LEU A CB    1 
ATOM   122  C  CG    . LEU A 1 17  ? 25.29578  5.38347   -5.93901  1.000 21.33272 ? 17  LEU A CG    1 
ATOM   123  C  CD1   . LEU A 1 17  ? 23.82879  5.34248   -6.34103  1.000 16.61421 ? 17  LEU A CD1   1 
ATOM   124  C  CD2   . LEU A 1 17  ? 25.43576  5.43847   -4.42401  1.000 22.70624 ? 17  LEU A CD2   1 
ATOM   125  N  N     . HIS A 1 18  ? 27.59782  2.20048   -8.63799  1.000 22.56212 ? 18  HIS A N     1 
ATOM   126  C  CA    . HIS A 1 18  ? 28.83582  1.62548   -9.13797  1.000 24.29196 ? 18  HIS A CA    1 
ATOM   127  C  C     . HIS A 1 18  ? 28.92985  1.82448   -10.64497 1.000 20.84403 ? 18  HIS A C     1 
ATOM   128  O  O     . HIS A 1 18  ? 27.93586  1.69049   -11.36398 1.000 21.92357 ? 18  HIS A O     1 
ATOM   129  C  CB    . HIS A 1 18  ? 28.90782  0.13548   -8.79997  1.000 22.78785 ? 18  HIS A CB    1 
ATOM   130  C  CG    . HIS A 1 18  ? 28.01883  -0.72052  -9.64799  1.000 24.85603 ? 18  HIS A CG    1 
ATOM   131  N  ND1   . HIS A 1 18  ? 26.66082  -0.82352  -9.43901  1.000 20.70126 ? 18  HIS A ND1   1 
ATOM   132  C  CD2   . HIS A 1 18  ? 28.29584  -1.51252  -10.71199 1.000 23.67343 ? 18  HIS A CD2   1 
ATOM   133  C  CE1   . HIS A 1 18  ? 26.13984  -1.64151  -10.33502 1.000 18.68650 ? 18  HIS A CE1   1 
ATOM   134  N  NE2   . HIS A 1 18  ? 27.10985  -2.07251  -11.12001 1.000 17.96835 ? 18  HIS A NE2   1 
ATOM   135  N  N     . ASP A 1 19  ? 30.13186  2.15148   -11.11495 1.000 28.09627 ? 19  ASP A N     1 
ATOM   136  C  CA    . ASP A 1 19  ? 30.40088  2.37449   -12.53494 1.000 19.60799 ? 19  ASP A CA    1 
ATOM   137  C  C     . ASP A 1 19  ? 29.39289  3.35749   -13.13295 1.000 18.48787 ? 19  ASP A C     1 
ATOM   138  O  O     . ASP A 1 19  ? 28.57990  3.02050   -13.99597 1.000 26.01928 ? 19  ASP A O     1 
ATOM   139  C  CB    . ASP A 1 19  ? 30.40489  1.04949   -13.30395 1.000 20.69740 ? 19  ASP A CB    1 
ATOM   140  C  CG    . ASP A 1 19  ? 30.84691  1.21049   -14.74694 1.000 26.79868 ? 19  ASP A CG    1 
ATOM   141  O  OD1   . ASP A 1 19  ? 31.41392  2.27149   -15.08293 1.000 25.84628 ? 19  ASP A OD1   1 
ATOM   142  O  OD2   . ASP A 1 19  ? 30.61992  0.27750   -15.54595 1.000 24.97768 ? 19  ASP A OD2   1 
ATOM   143  N  N     . ASN A 1 20  ? 29.45288  4.59249   -12.64395 1.000 26.10320 ? 20  ASN A N     1 
ATOM   144  C  CA    . ASN A 1 20  ? 28.57389  5.67049   -13.09496 1.000 24.39382 ? 20  ASN A CA    1 
ATOM   145  C  C     . ASN A 1 20  ? 29.44090  6.89049   -13.37394 1.000 21.94926 ? 20  ASN A C     1 
ATOM   146  O  O     . ASN A 1 20  ? 29.60089  7.76649   -12.51294 1.000 18.34204 ? 20  ASN A O     1 
ATOM   147  C  CB    . ASN A 1 20  ? 27.48688  5.97049   -12.06097 1.000 23.67734 ? 20  ASN A CB    1 
ATOM   148  C  CG    . ASN A 1 20  ? 26.28989  6.68450   -12.66199 1.000 20.43435 ? 20  ASN A CG    1 
ATOM   149  O  OD1   . ASN A 1 20  ? 26.43290  7.52050   -13.55499 1.000 27.82456 ? 20  ASN A OD1   1 
ATOM   150  N  ND2   . ASN A 1 20  ? 25.09988  6.35350   -12.17601 1.000 17.64312 ? 20  ASN A ND2   1 
ATOM   151  N  N     . PRO A 1 21  ? 30.02592  6.97450   -14.57093 1.000 24.13432 ? 21  PRO A N     1 
ATOM   152  C  CA    . PRO A 1 21  ? 30.87792  8.13150   -14.89192 1.000 19.82140 ? 21  PRO A CA    1 
ATOM   153  C  C     . PRO A 1 21  ? 30.12493  9.44750   -14.92292 1.000 20.63182 ? 21  PRO A C     1 
ATOM   154  O  O     . PRO A 1 21  ? 30.75193  10.50449  -14.77991 1.000 25.49171 ? 21  PRO A O     1 
ATOM   155  C  CB    . PRO A 1 21  ? 31.44594  7.77550   -16.27291 1.000 23.33747 ? 21  PRO A CB    1 
ATOM   156  C  CG    . PRO A 1 21  ? 30.46095  6.81350   -16.84993 1.000 23.01956 ? 21  PRO A CG    1 
ATOM   157  C  CD    . PRO A 1 21  ? 29.93893  6.02050   -15.68894 1.000 27.28008 ? 21  PRO A CD    1 
ATOM   158  N  N     . ALA A 1 22  ? 28.80393  9.42050   -15.10494 1.000 21.61467 ? 22  ALA A N     1 
ATOM   159  C  CA    . ALA A 1 22  ? 28.01893  10.64750  -15.06095 1.000 22.15204 ? 22  ALA A CA    1 
ATOM   160  C  C     . ALA A 1 22  ? 27.82291  11.14650  -13.63495 1.000 21.51060 ? 22  ALA A C     1 
ATOM   161  O  O     . ALA A 1 22  ? 27.72291  12.35950  -13.41695 1.000 25.58948 ? 22  ALA A O     1 
ATOM   162  C  CB    . ALA A 1 22  ? 26.66394  10.42851  -15.73397 1.000 19.62403 ? 22  ALA A CB    1 
ATOM   163  N  N     . LEU A 1 23  ? 27.76889  10.23749  -12.65896 1.000 19.79395 ? 23  LEU A N     1 
ATOM   164  C  CA    . LEU A 1 23  ? 27.60987  10.65449  -11.26996 1.000 21.07993 ? 23  LEU A CA    1 
ATOM   165  C  C     . LEU A 1 23  ? 28.90387  11.23848  -10.71593 1.000 18.49694 ? 23  LEU A C     1 
ATOM   166  O  O     . LEU A 1 23  ? 28.87686  12.22448  -9.97093  1.000 20.04136 ? 23  LEU A O     1 
ATOM   167  C  CB    . LEU A 1 23  ? 27.14586  9.47349   -10.41697 1.000 21.15770 ? 23  LEU A CB    1 
ATOM   168  C  CG    . LEU A 1 23  ? 26.97884  9.73148   -8.91797  1.000 16.43663 ? 23  LEU A CG    1 
ATOM   169  C  CD1   . LEU A 1 23  ? 25.95583  10.82948  -8.67198  1.000 24.92113 ? 23  LEU A CD1   1 
ATOM   170  C  CD2   . LEU A 1 23  ? 26.58682  8.45448   -8.18598  1.000 18.71539 ? 23  LEU A CD2   1 
ATOM   171  N  N     . LEU A 1 24  ? 30.04587  10.64548  -11.07392 1.000 21.14873 ? 24  LEU A N     1 
ATOM   172  C  CA    . LEU A 1 24  ? 31.32686  11.13048  -10.57090 1.000 22.96821 ? 24  LEU A CA    1 
ATOM   173  C  C     . LEU A 1 24  ? 31.65287  12.52248  -11.09689 1.000 23.40451 ? 24  LEU A C     1 
ATOM   174  O  O     . LEU A 1 24  ? 32.30486  13.30848  -10.39987 1.000 28.35556 ? 24  LEU A O     1 
ATOM   175  C  CB    . LEU A 1 24  ? 32.43887  10.14948  -10.93988 1.000 20.06290 ? 24  LEU A CB    1 
ATOM   176  C  CG    . LEU A 1 24  ? 32.30786  8.74048   -10.36189 1.000 18.31810 ? 24  LEU A CG    1 
ATOM   177  C  CD1   . LEU A 1 24  ? 33.33286  7.80648   -10.98388 1.000 24.55579 ? 24  LEU A CD1   1 
ATOM   178  C  CD2   . LEU A 1 24  ? 32.45883  8.77247   -8.85089  1.000 19.85521 ? 24  LEU A CD2   1 
ATOM   179  N  N     . GLU A 1 25  ? 31.21689  12.84349  -12.31589 1.000 23.37688 ? 25  GLU A N     1 
ATOM   180  C  CA    . GLU A 1 25  ? 31.43590  14.18649  -12.84389 1.000 25.23084 ? 25  GLU A CA    1 
ATOM   181  C  C     . GLU A 1 25  ? 30.56489  15.20849  -12.12389 1.000 24.19793 ? 25  GLU A C     1 
ATOM   182  O  O     . GLU A 1 25  ? 31.02389  16.31248  -11.80888 1.000 27.64616 ? 25  GLU A O     1 
ATOM   183  C  CB    . GLU A 1 25  ? 31.16193  14.21249  -14.34789 1.000 21.28476 ? 25  GLU A CB    1 
ATOM   184  C  CG    . GLU A 1 25  ? 31.26094  15.59549  -14.97488 1.000 21.51014 ? 25  GLU A CG    1 
ATOM   185  C  CD    . GLU A 1 25  ? 32.67994  16.12849  -15.00086 1.000 26.34072 ? 25  GLU A CD    1 
ATOM   186  O  OE1   . GLU A 1 25  ? 33.61994  15.31449  -15.12085 1.000 20.23252 ? 25  GLU A OE1   1 
ATOM   187  O  OE2   . GLU A 1 25  ? 32.85594  17.36149  -14.89985 1.000 29.37297 ? 25  GLU A OE2   1 
ATOM   188  N  N     . ALA A 1 26  ? 29.30689  14.85349  -11.84892 1.000 24.89419 ? 26  ALA A N     1 
ATOM   189  C  CA    . ALA A 1 26  ? 28.39388  15.77249  -11.18093 1.000 22.10695 ? 26  ALA A CA    1 
ATOM   190  C  C     . ALA A 1 26  ? 28.77586  16.02448  -9.72892  1.000 23.06033 ? 26  ALA A C     1 
ATOM   191  O  O     . ALA A 1 26  ? 28.36185  17.04048  -9.16192  1.000 22.23497 ? 26  ALA A O     1 
ATOM   192  C  CB    . ALA A 1 26  ? 26.96288  15.23849  -11.25695 1.000 24.29641 ? 26  ALA A CB    1 
ATOM   193  N  N     . CYS A 1 27  ? 29.54585  15.12848  -9.11391  1.000 25.82547 ? 27  CYS A N     1 
ATOM   194  C  CA    . CYS A 1 27  ? 30.00483  15.31647  -7.74490  1.000 29.24342 ? 27  CYS A CA    1 
ATOM   195  C  C     . CYS A 1 27  ? 31.35783  16.01047  -7.65988  1.000 20.57003 ? 27  CYS A C     1 
ATOM   196  O  O     . CYS A 1 27  ? 31.76481  16.40646  -6.56287  1.000 21.40560 ? 27  CYS A O     1 
ATOM   197  C  CB    . CYS A 1 27  ? 30.08381  13.96747  -7.02091  1.000 24.57433 ? 27  CYS A CB    1 
ATOM   198  S  SG    . CYS A 1 27  ? 28.50281  13.11447  -6.84093  1.000 33.85890 ? 27  CYS A SG    1 
ATOM   199  N  N     . LYS A 1 28  ? 32.05284  16.16947  -8.78287  1.000 24.38324 ? 28  LYS A N     1 
ATOM   200  C  CA    . LYS A 1 28  ? 33.39485  16.73647  -8.79285  1.000 27.02358 ? 28  LYS A CA    1 
ATOM   201  C  C     . LYS A 1 28  ? 33.31185  18.25147  -8.64084  1.000 26.68398 ? 28  LYS A C     1 
ATOM   202  O  O     . LYS A 1 28  ? 32.69986  18.92947  -9.47285  1.000 26.57608 ? 28  LYS A O     1 
ATOM   203  C  CB    . LYS A 1 28  ? 34.10887  16.35447  -10.08884 1.000 26.95481 ? 28  LYS A CB    1 
ATOM   204  C  CG    . LYS A 1 28  ? 35.61286  16.16147  -9.96981  1.000 31.74826 ? 28  LYS A CG    1 
ATOM   205  C  CD    . LYS A 1 28  ? 36.36687  17.46947  -10.12380 0.000 31.29438 ? 28  LYS A CD    1 
ATOM   206  C  CE    . LYS A 1 28  ? 37.84387  17.22347  -10.39178 0.000 33.74894 ? 28  LYS A CE    1 
ATOM   207  N  NZ    . LYS A 1 28  ? 38.46885  16.37146  -9.34277  0.000 35.07089 ? 28  LYS A NZ    1 
ATOM   208  N  N     . ASP A 1 29  ? 33.91883  18.77646  -7.57483  1.000 29.09200 ? 29  ASP A N     1 
ATOM   209  C  CA    . ASP A 1 29  ? 33.96783  20.21146  -7.28882  1.000 26.79872 ? 29  ASP A CA    1 
ATOM   210  C  C     . ASP A 1 29  ? 32.57983  20.83146  -7.15284  1.000 21.83361 ? 29  ASP A C     1 
ATOM   211  O  O     . ASP A 1 29  ? 32.41783  22.04147  -7.34084  1.000 21.56713 ? 29  ASP A O     1 
ATOM   212  C  CB    . ASP A 1 29  ? 34.77085  20.96546  -8.35581  1.000 25.65084 ? 29  ASP A CB    1 
ATOM   213  C  CG    . ASP A 1 29  ? 36.19385  20.46446  -8.47679  1.000 25.14804 ? 29  ASP A CG    1 
ATOM   214  O  OD1   . ASP A 1 29  ? 36.60183  19.62046  -7.65179  1.000 33.99747 ? 29  ASP A OD1   1 
ATOM   215  O  OD2   . ASP A 1 29  ? 36.90486  20.91246  -9.40078  1.000 27.05321 ? 29  ASP A OD2   1 
ATOM   216  N  N     . ALA A 1 30  ? 31.57182  20.03246  -6.82086  1.000 21.00600 ? 30  ALA A N     1 
ATOM   217  C  CA    . ALA A 1 30  ? 30.20182  20.51647  -6.75888  1.000 23.50413 ? 30  ALA A CA    1 
ATOM   218  C  C     . ALA A 1 30  ? 29.84480  20.97846  -5.35189  1.000 19.84124 ? 30  ALA A C     1 
ATOM   219  O  O     . ALA A 1 30  ? 30.38379  20.48746  -4.35688  1.000 26.46768 ? 30  ALA A O     1 
ATOM   220  C  CB    . ALA A 1 30  ? 29.22383  19.43147  -7.20990  1.000 19.76138 ? 30  ALA A CB    1 
ATOM   221  N  N     . LYS A 1 31  ? 28.92380  21.93846  -5.28290  1.000 21.25062 ? 31  LYS A N     1 
ATOM   222  C  CA    . LYS A 1 31  ? 28.38778  22.43446  -4.02090  1.000 23.51718 ? 31  LYS A CA    1 
ATOM   223  C  C     . LYS A 1 31  ? 27.05078  21.80046  -3.66692  1.000 24.12314 ? 31  LYS A C     1 
ATOM   224  O  O     . LYS A 1 31  ? 26.80076  21.50546  -2.49393  1.000 23.82603 ? 31  LYS A O     1 
ATOM   225  C  CB    . LYS A 1 31  ? 28.23379  23.95846  -4.07590  1.000 23.87929 ? 31  LYS A CB    1 
ATOM   226  C  CG    . LYS A 1 31  ? 27.88177  24.61046  -2.74590  1.000 26.32318 ? 31  LYS A CG    1 
ATOM   227  C  CD    . LYS A 1 31  ? 29.04175  24.55345  -1.76188  1.000 26.68352 ? 31  LYS A CD    1 
ATOM   228  C  CE    . LYS A 1 31  ? 28.72473  25.33645  -0.49389  1.000 31.35123 ? 31  LYS A CE    1 
ATOM   229  N  NZ    . LYS A 1 31  ? 29.85372  25.34544  0.48013   1.000 22.65152 ? 31  LYS A NZ    1 
ATOM   230  N  N     . HIS A 1 32  ? 26.18679  21.58147  -4.65694  1.000 20.25470 ? 32  HIS A N     1 
ATOM   231  C  CA    . HIS A 1 32  ? 24.90779  20.90947  -4.45396  1.000 27.13264 ? 32  HIS A CA    1 
ATOM   232  C  C     . HIS A 1 32  ? 24.62580  20.03547  -5.66597  1.000 24.90862 ? 32  HIS A C     1 
ATOM   233  O  O     . HIS A 1 32  ? 24.59082  20.53348  -6.79497  1.000 22.79704 ? 32  HIS A O     1 
ATOM   234  C  CB    . HIS A 1 32  ? 23.77179  21.91547  -4.24197  1.000 27.58100 ? 32  HIS A CB    1 
ATOM   235  C  CG    . HIS A 1 32  ? 23.92777  22.75747  -3.01397  1.000 32.52261 ? 32  HIS A CG    1 
ATOM   236  N  ND1   . HIS A 1 32  ? 24.54477  23.99046  -3.02996  1.000 27.15747 ? 32  HIS A ND1   1 
ATOM   237  C  CD2   . HIS A 1 32  ? 23.55075  22.54246  -1.73198  1.000 28.42163 ? 32  HIS A CD2   1 
ATOM   238  C  CE1   . HIS A 1 32  ? 24.53775  24.49946  -1.81095  1.000 29.28579 ? 32  HIS A CE1   1 
ATOM   239  N  NE2   . HIS A 1 32  ? 23.94174  23.64046  -1.00397  1.000 28.75405 ? 32  HIS A NE2   1 
ATOM   240  N  N     . VAL A 1 33  ? 24.42980  18.73947  -5.43298  1.000 20.88985 ? 33  VAL A N     1 
ATOM   241  C  CA    . VAL A 1 33  ? 24.12081  17.77948  -6.48598  1.000 25.11792 ? 33  VAL A CA    1 
ATOM   242  C  C     . VAL A 1 33  ? 22.65681  17.38548  -6.36301  1.000 25.08108 ? 33  VAL A C     1 
ATOM   243  O  O     . VAL A 1 33  ? 22.14079  17.21148  -5.25202  1.000 26.46049 ? 33  VAL A O     1 
ATOM   244  C  CB    . VAL A 1 33  ? 25.03681  16.54048  -6.40797  1.000 22.63231 ? 33  VAL A CB    1 
ATOM   245  C  CG1   . VAL A 1 33  ? 24.75783  15.59348  -7.56498  1.000 27.93131 ? 33  VAL A CG1   1 
ATOM   246  C  CG2   . VAL A 1 33  ? 26.49681  16.96147  -6.40295  1.000 24.49028 ? 33  VAL A CG2   1 
ATOM   247  N  N     . TYR A 1 34  ? 21.98583  17.24948  -7.50502  1.000 20.36821 ? 34  TYR A N     1 
ATOM   248  C  CA    . TYR A 1 34  ? 20.55883  16.92649  -7.54604  1.000 24.17612 ? 34  TYR A CA    1 
ATOM   249  C  C     . TYR A 1 34  ? 20.33284  15.62249  -8.29905  1.000 21.34852 ? 34  TYR A C     1 
ATOM   250  O  O     . TYR A 1 34  ? 20.39186  15.60149  -9.54205  1.000 18.90227 ? 34  TYR A O     1 
ATOM   251  C  CB    . TYR A 1 34  ? 19.76884  18.05949  -8.19905  1.000 25.39304 ? 34  TYR A CB    1 
ATOM   252  C  CG    . TYR A 1 34  ? 19.87083  19.38149  -7.47404  1.000 26.71747 ? 34  TYR A CG    1 
ATOM   253  C  CD1   . TYR A 1 34  ? 18.97482  19.71349  -6.46606  1.000 28.77192 ? 34  TYR A CD1   1 
ATOM   254  C  CD2   . TYR A 1 34  ? 20.85984  20.30049  -7.80002  1.000 24.31010 ? 34  TYR A CD2   1 
ATOM   255  C  CE1   . TYR A 1 34  ? 19.06381  20.92148  -5.80105  1.000 24.97844 ? 34  TYR A CE1   1 
ATOM   256  C  CE2   . TYR A 1 34  ? 20.95583  21.51149  -7.14102  1.000 28.96579 ? 34  TYR A CE2   1 
ATOM   257  C  CZ    . TYR A 1 34  ? 20.05481  21.81648  -6.14203  1.000 27.56054 ? 34  TYR A CZ    1 
ATOM   258  O  OH    . TYR A 1 34  ? 20.14781  23.02048  -5.48303  1.000 33.60472 ? 34  TYR A OH    1 
ATOM   259  N  N     . PRO A 1 35  ? 20.07582  14.51249  -7.60206  1.000 22.75206 ? 35  PRO A N     1 
ATOM   260  C  CA    . PRO A 1 35  ? 19.70983  13.26049  -8.28107  1.000 20.87777 ? 35  PRO A CA    1 
ATOM   261  C  C     . PRO A 1 35  ? 18.23284  13.25750  -8.62609  1.000 21.78551 ? 35  PRO A C     1 
ATOM   262  O  O     . PRO A 1 35  ? 17.36782  13.24549  -7.73810  1.000 19.66870 ? 35  PRO A O     1 
ATOM   263  C  CB    . PRO A 1 35  ? 20.06581  12.18449  -7.24107  1.000 17.62784 ? 35  PRO A CB    1 
ATOM   264  C  CG    . PRO A 1 35  ? 20.57880  12.92548  -6.01106  1.000 26.27956 ? 35  PRO A CG    1 
ATOM   265  C  CD    . PRO A 1 35  ? 20.14080  14.34248  -6.14406  1.000 26.22362 ? 35  PRO A CD    1 
ATOM   266  N  N     . VAL A 1 36  ? 17.92686  13.27150  -9.92009  1.000 21.23332 ? 36  VAL A N     1 
ATOM   267  C  CA    . VAL A 1 36  ? 16.57086  13.47050  -10.40911 1.000 17.58290 ? 36  VAL A CA    1 
ATOM   268  C  C     . VAL A 1 36  ? 16.15688  12.28251  -11.26613 1.000 22.84656 ? 36  VAL A C     1 
ATOM   269  O  O     . VAL A 1 36  ? 16.92789  11.81151  -12.11012 1.000 21.27687 ? 36  VAL A O     1 
ATOM   270  C  CB    . VAL A 1 36  ? 16.45088  14.78451  -11.20911 1.000 18.55296 ? 36  VAL A CB    1 
ATOM   271  C  CG1   . VAL A 1 36  ? 15.04689  14.94651  -11.76813 1.000 16.92272 ? 36  VAL A CG1   1 
ATOM   272  C  CG2   . VAL A 1 36  ? 16.81987  15.97350  -10.33410 1.000 18.45977 ? 36  VAL A CG2   1 
ATOM   273  N  N     . PHE A 1 37  ? 14.93387  11.80151  -11.04115 1.000 20.57879 ? 37  PHE A N     1 
ATOM   274  C  CA    . PHE A 1 37  ? 14.28888  10.81651  -11.90416 1.000 21.87350 ? 37  PHE A CA    1 
ATOM   275  C  C     . PHE A 1 37  ? 12.94689  11.38452  -12.33918 1.000 23.42297 ? 37  PHE A C     1 
ATOM   276  O  O     . PHE A 1 37  ? 12.06188  11.59352  -11.50319 1.000 23.59901 ? 37  PHE A O     1 
ATOM   277  C  CB    . PHE A 1 37  ? 14.10087  9.47651   -11.18317 1.000 22.24443 ? 37  PHE A CB    1 
ATOM   278  C  CG    . PHE A 1 37  ? 13.57188  8.37552   -12.06818 1.000 20.95219 ? 37  PHE A CG    1 
ATOM   279  C  CD1   . PHE A 1 37  ? 12.20788  8.21252   -12.26120 1.000 21.58920 ? 37  PHE A CD1   1 
ATOM   280  C  CD2   . PHE A 1 37  ? 14.44089  7.50152   -12.70017 1.000 23.24497 ? 37  PHE A CD2   1 
ATOM   281  C  CE1   . PHE A 1 37  ? 11.72489  7.20452   -13.07421 1.000 24.64313 ? 37  PHE A CE1   1 
ATOM   282  C  CE2   . PHE A 1 37  ? 13.96190  6.49252   -13.51418 1.000 20.68041 ? 37  PHE A CE2   1 
ATOM   283  C  CZ    . PHE A 1 37  ? 12.60290  6.34452   -13.70120 1.000 21.05603 ? 37  PHE A CZ    1 
ATOM   284  N  N     . VAL A 1 38  ? 12.79791  11.63652  -13.63518 1.000 19.20575 ? 38  VAL A N     1 
ATOM   285  C  CA    . VAL A 1 38  ? 11.56692  12.21753  -14.16320 1.000 22.79517 ? 38  VAL A CA    1 
ATOM   286  C  C     . VAL A 1 38  ? 10.55692  11.09953  -14.39121 1.000 24.16519 ? 38  VAL A C     1 
ATOM   287  O  O     . VAL A 1 38  ? 10.79393  10.18653  -15.18921 1.000 27.77335 ? 38  VAL A O     1 
ATOM   288  C  CB    . VAL A 1 38  ? 11.83294  12.99953  -15.45719 1.000 21.84762 ? 38  VAL A CB    1 
ATOM   289  C  CG1   . VAL A 1 38  ? 10.55795  13.67454  -15.93621 1.000 32.54840 ? 38  VAL A CG1   1 
ATOM   290  C  CG2   . VAL A 1 38  ? 12.93094  14.02653  -15.24017 1.000 21.97832 ? 38  VAL A CG2   1 
ATOM   291  N  N     . LEU A 1 39  ? 9.42891   11.17053  -13.68923 1.000 28.43099 ? 39  LEU A N     1 
ATOM   292  C  CA    . LEU A 1 39  ? 8.39091   10.14953  -13.74425 1.000 32.82684 ? 39  LEU A CA    1 
ATOM   293  C  C     . LEU A 1 39  ? 7.09992   10.76854  -14.25827 1.000 37.44517 ? 39  LEU A C     1 
ATOM   294  O  O     . LEU A 1 39  ? 6.68291   11.83053  -13.78427 1.000 32.51841 ? 39  LEU A O     1 
ATOM   295  C  CB    . LEU A 1 39  ? 8.17189   9.51953   -12.36426 1.000 31.31582 ? 39  LEU A CB    1 
ATOM   296  C  CG    . LEU A 1 39  ? 7.13088   8.40353   -12.25028 1.000 29.74283 ? 39  LEU A CG    1 
ATOM   297  C  CD1   . LEU A 1 39  ? 7.70587   7.22052   -11.48827 1.000 36.06893 ? 39  LEU A CD1   1 
ATOM   298  C  CD2   . LEU A 1 39  ? 5.86787   8.91053   -11.57329 1.000 36.41327 ? 39  LEU A CD2   1 
ATOM   299  N  N     A ASP A 1 40  ? 6.46993   10.10554  -15.22928 0.516 37.19439 ? 40  ASP A N     1 
ATOM   300  N  N     B ASP A 1 40  ? 6.46993   10.09854  -15.22428 0.484 37.19279 ? 40  ASP A N     1 
ATOM   301  C  CA    A ASP A 1 40  ? 5.22994   10.60154  -15.81030 0.516 39.82078 ? 40  ASP A CA    1 
ATOM   302  C  CA    B ASP A 1 40  ? 5.22894   10.58154  -15.81330 0.484 39.82768 ? 40  ASP A CA    1 
ATOM   303  C  C     A ASP A 1 40  ? 4.04993   9.99754   -15.05932 0.516 43.87986 ? 40  ASP A C     1 
ATOM   304  C  C     B ASP A 1 40  ? 4.05493   9.98854   -15.04532 0.484 43.87017 ? 40  ASP A C     1 
ATOM   305  O  O     A ASP A 1 40  ? 3.84893   8.77454   -15.12833 0.516 42.10437 ? 40  ASP A O     1 
ATOM   306  O  O     B ASP A 1 40  ? 3.86293   8.76354   -15.08333 0.484 42.10539 ? 40  ASP A O     1 
ATOM   307  C  CB    A ASP A 1 40  ? 5.15296   10.25855  -17.29030 0.516 41.59152 ? 40  ASP A CB    1 
ATOM   308  C  CB    B ASP A 1 40  ? 5.14996   10.19555  -17.28330 0.484 41.58533 ? 40  ASP A CB    1 
ATOM   309  C  CG    A ASP A 1 40  ? 3.98298   10.92955  -17.98332 0.516 43.77939 ? 40  ASP A CG    1 
ATOM   310  C  CG    B ASP A 1 40  ? 6.48397   10.32455  -17.99328 0.484 39.73297 ? 40  ASP A CG    1 
ATOM   311  O  OD1   A ASP A 1 40  ? 3.94698   12.17755  -18.01531 0.516 40.73885 ? 40  ASP A OD1   1 
ATOM   312  O  OD1   B ASP A 1 40  ? 7.30397   11.16855  -17.57526 0.484 38.40726 ? 40  ASP A OD1   1 
ATOM   313  O  OD2   A ASP A 1 40  ? 3.10198   10.21056  -18.49833 0.516 44.30889 ? 40  ASP A OD2   1 
ATOM   314  O  OD2   B ASP A 1 40  ? 6.71399   9.57755   -18.96728 0.484 41.56495 ? 40  ASP A OD2   1 
ATOM   315  N  N     . PRO A 1 41  ? 3.25092   10.79554  -14.34433 1.000 44.78425 ? 41  PRO A N     1 
ATOM   316  C  CA    . PRO A 1 41  ? 2.12591   10.22654  -13.58335 1.000 42.17646 ? 41  PRO A CA    1 
ATOM   317  C  C     . PRO A 1 41  ? 0.96292   9.76955   -14.44737 1.000 51.60538 ? 41  PRO A C     1 
ATOM   318  O  O     . PRO A 1 41  ? 0.02291   9.16655   -13.91338 1.000 56.80435 ? 41  PRO A O     1 
ATOM   319  C  CB    . PRO A 1 41  ? 1.70990   11.38354  -12.66735 1.000 40.12515 ? 41  PRO A CB    1 
ATOM   320  C  CG    . PRO A 1 41  ? 2.10091   12.60854  -13.42834 1.000 46.75573 ? 41  PRO A CG    1 
ATOM   321  C  CD    . PRO A 1 41  ? 3.35592   12.25554  -14.18532 1.000 41.90061 ? 41  PRO A CD    1 
ATOM   322  N  N     . HIS A 1 42  ? 0.98794   10.03655  -15.75236 1.000 49.46918 ? 42  HIS A N     1 
ATOM   323  C  CA    . HIS A 1 42  ? -0.06405  9.60956   -16.66638 1.000 52.06087 ? 42  HIS A CA    1 
ATOM   324  C  C     . HIS A 1 42  ? 0.43397   8.55256   -17.64638 1.000 55.38833 ? 42  HIS A C     1 
ATOM   325  O  O     . HIS A 1 42  ? -0.09002  8.42756   -18.75539 1.000 56.33365 ? 42  HIS A O     1 
ATOM   326  C  CB    . HIS A 1 42  ? -0.63803  10.81156  -17.41639 1.000 55.70696 ? 42  HIS A CB    1 
ATOM   327  C  CG    . HIS A 1 42  ? -1.07204  11.93056  -16.52239 1.000 57.80834 ? 42  HIS A CG    1 
ATOM   328  N  ND1   . HIS A 1 42  ? -0.18705  12.84755  -15.99637 1.000 55.16215 ? 42  HIS A ND1   1 
ATOM   329  C  CD2   . HIS A 1 42  ? -2.29505  12.27956  -16.05941 1.000 58.03840 ? 42  HIS A CD2   1 
ATOM   330  C  CE1   . HIS A 1 42  ? -0.84706  13.71355  -15.24938 1.000 51.14727 ? 42  HIS A CE1   1 
ATOM   331  N  NE2   . HIS A 1 42  ? -2.12806  13.39256  -15.27140 1.000 60.25513 ? 42  HIS A NE2   1 
ATOM   332  N  N     . PHE A 1 43  ? 1.44896   7.78356   -17.24337 1.000 49.30434 ? 43  PHE A N     1 
ATOM   333  C  CA    . PHE A 1 43  ? 2.00297   6.75956   -18.12236 1.000 49.58107 ? 43  PHE A CA    1 
ATOM   334  C  C     . PHE A 1 43  ? 0.99897   5.64456   -18.38738 1.000 55.16249 ? 43  PHE A C     1 
ATOM   335  O  O     . PHE A 1 43  ? 1.07799   4.97256   -19.42138 1.000 54.60012 ? 43  PHE A O     1 
ATOM   336  C  CB    . PHE A 1 43  ? 3.28596   6.18855   -17.51534 1.000 46.96608 ? 43  PHE A CB    1 
ATOM   337  C  CG    . PHE A 1 43  ? 4.19497   5.53456   -18.51733 1.000 43.76430 ? 43  PHE A CG    1 
ATOM   338  C  CD1   . PHE A 1 43  ? 4.02898   4.20156   -18.86134 1.000 44.25384 ? 43  PHE A CD1   1 
ATOM   339  C  CD2   . PHE A 1 43  ? 5.22198   6.25056   -19.10931 1.000 41.15408 ? 43  PHE A CD2   1 
ATOM   340  C  CE1   . PHE A 1 43  ? 4.86599   3.60056   -19.78233 1.000 48.25722 ? 43  PHE A CE1   1 
ATOM   341  C  CE2   . PHE A 1 43  ? 6.06200   5.65356   -20.03030 1.000 42.15454 ? 43  PHE A CE2   1 
ATOM   342  C  CZ    . PHE A 1 43  ? 5.88400   4.32656   -20.36631 1.000 39.38135 ? 43  PHE A CZ    1 
ATOM   343  N  N     . LEU A 1 44  ? 0.05396   5.43356   -17.47440 1.000 54.39937 ? 44  LEU A N     1 
ATOM   344  C  CA    . LEU A 1 44  ? -0.95904  4.40456   -17.64941 1.000 54.04147 ? 44  LEU A CA    1 
ATOM   345  C  C     . LEU A 1 44  ? -2.16403  4.88457   -18.44543 1.000 63.64448 ? 44  LEU A C     1 
ATOM   346  O  O     . LEU A 1 44  ? -2.97302  4.05457   -18.87445 1.000 63.91534 ? 44  LEU A O     1 
ATOM   347  C  CB    . LEU A 1 44  ? -1.41506  3.88056   -16.28242 1.000 48.88273 ? 44  LEU A CB    1 
ATOM   348  C  CG    . LEU A 1 44  ? -0.28208  3.33555   -15.41041 0.000 45.91546 ? 44  LEU A CG    1 
ATOM   349  C  CD1   . LEU A 1 44  ? -0.82610  2.70555   -14.14042 0.000 38.83982 ? 44  LEU A CD1   1 
ATOM   350  C  CD2   . LEU A 1 44  ? 0.56793   2.33955   -16.18640 0.000 44.50471 ? 44  LEU A CD2   1 
ATOM   351  N  N     . GLN A 1 45  ? -2.30402  6.19357   -18.65343 1.000 77.73374 ? 45  GLN A N     1 
ATOM   352  C  CA    . GLN A 1 45  ? -3.35001  6.74557   -19.50144 1.000 80.15229 ? 45  GLN A CA    1 
ATOM   353  C  C     . GLN A 1 45  ? -2.89099  6.94258   -20.94244 1.000 80.31153 ? 45  GLN A C     1 
ATOM   354  O  O     . GLN A 1 45  ? -3.49697  7.73158   -21.67444 1.000 84.89954 ? 45  GLN A O     1 
ATOM   355  C  CB    . GLN A 1 45  ? -3.85801  8.07157   -18.92745 1.000 75.05158 ? 45  GLN A CB    1 
ATOM   356  C  CG    . GLN A 1 45  ? -4.64003  7.93757   -17.62946 0.000 77.01696 ? 45  GLN A CG    1 
ATOM   357  C  CD    . GLN A 1 45  ? -3.87305  8.45556   -16.43044 0.000 73.38975 ? 45  GLN A CD    1 
ATOM   358  O  OE1   . GLN A 1 45  ? -4.07606  9.58756   -15.99144 0.000 72.85349 ? 45  GLN A OE1   1 
ATOM   359  N  NE2   . GLN A 1 45  ? -2.98606  7.62756   -15.89143 0.000 69.23958 ? 45  GLN A NE2   1 
ATOM   360  N  N     . GLN A 1 46  ? -1.83498  6.24958   -21.36042 1.000 69.16452 ? 46  GLN A N     1 
ATOM   361  C  CA    . GLN A 1 46  ? -1.35896  6.33858   -22.73641 1.000 66.60257 ? 46  GLN A CA    1 
ATOM   362  C  C     . GLN A 1 46  ? -1.38095  4.96658   -23.40042 1.000 64.26989 ? 46  GLN A C     1 
ATOM   363  O  O     . GLN A 1 46  ? -1.50693  4.86059   -24.62042 1.000 67.31560 ? 46  GLN A O     1 
ATOM   364  C  CB    . GLN A 1 46  ? 0.05404   6.92358   -22.79039 1.000 60.11189 ? 46  GLN A CB    1 
ATOM   365  C  CG    . GLN A 1 46  ? 1.15103   5.94158   -22.41038 0.000 56.79520 ? 46  GLN A CG    1 
ATOM   366  C  CD    . GLN A 1 46  ? 2.54204   6.52857   -22.56235 0.000 52.06434 ? 46  GLN A CD    1 
ATOM   367  O  OE1   . GLN A 1 46  ? 3.45903   6.18157   -21.81834 0.000 49.15280 ? 46  GLN A OE1   1 
ATOM   368  N  NE2   . GLN A 1 46  ? 2.70605   7.41858   -23.53335 0.000 52.94196 ? 46  GLN A NE2   1 
ATOM   369  N  N     . LYS A 1 50  ? -0.52800  -1.38843  -21.30143 1.000 48.52018 ? 50  LYS A N     1 
ATOM   370  C  CA    . LYS A 1 50  ? 0.63602   -1.67242  -22.13241 1.000 40.16882 ? 50  LYS A CA    1 
ATOM   371  C  C     . LYS A 1 50  ? 1.83800   -2.05843  -21.27740 1.000 38.24318 ? 50  LYS A C     1 
ATOM   372  O  O     . LYS A 1 50  ? 2.78601   -2.67243  -21.76338 1.000 41.57089 ? 50  LYS A O     1 
ATOM   373  C  CB    . LYS A 1 50  ? 0.98003   -0.46342  -23.00440 1.000 52.03901 ? 50  LYS A CB    1 
ATOM   374  N  N     . VAL A 1 51  ? 1.79098   -1.69243  -19.99839 1.000 39.42958 ? 51  VAL A N     1 
ATOM   375  C  CA    . VAL A 1 51  ? 2.85997   -1.97544  -19.04838 1.000 34.20341 ? 51  VAL A CA    1 
ATOM   376  C  C     . VAL A 1 51  ? 2.26995   -2.76044  -17.88639 1.000 32.55515 ? 51  VAL A C     1 
ATOM   377  O  O     . VAL A 1 51  ? 1.21794   -2.39044  -17.35241 1.000 32.98052 ? 51  VAL A O     1 
ATOM   378  C  CB    . VAL A 1 51  ? 3.53596   -0.68344  -18.55236 1.000 39.06719 ? 51  VAL A CB    1 
ATOM   379  C  CG1   . VAL A 1 51  ? 4.63795   -1.00545  -17.55435 1.000 36.79322 ? 51  VAL A CG1   1 
ATOM   380  C  CG2   . VAL A 1 51  ? 4.08998   0.10756   -19.72635 1.000 38.07052 ? 51  VAL A CG2   1 
ATOM   381  N  N     . SER A 1 52  ? 2.94194   -3.84145  -17.50438 1.000 28.94008 ? 52  SER A N     1 
ATOM   382  C  CA    A SER A 1 52  ? 2.48892   -4.66345  -16.39539 0.537 29.72862 ? 52  SER A CA    1 
ATOM   383  C  CA    B SER A 1 52  ? 2.48492   -4.66145  -16.39539 0.463 29.24282 ? 52  SER A CA    1 
ATOM   384  C  C     . SER A 1 52  ? 2.94190   -4.06745  -15.06539 1.000 29.27137 ? 52  SER A C     1 
ATOM   385  O  O     . SER A 1 52  ? 3.80890   -3.19146  -15.00437 1.000 29.83937 ? 52  SER A O     1 
ATOM   386  C  CB    A SER A 1 52  ? 3.00792   -6.09345  -16.53939 0.537 27.61924 ? 52  SER A CB    1 
ATOM   387  C  CB    B SER A 1 52  ? 2.99792   -6.09345  -16.53839 0.463 27.81252 ? 52  SER A CB    1 
ATOM   388  O  OG    A SER A 1 52  ? 2.65490   -6.88045  -15.41540 0.537 30.60516 ? 52  SER A OG    1 
ATOM   389  O  OG    B SER A 1 52  ? 4.41392   -6.12845  -16.51537 0.463 29.47923 ? 52  SER A OG    1 
ATOM   390  N  N     . VAL A 1 53  ? 2.33889   -4.56246  -13.98240 1.000 29.33821 ? 53  VAL A N     1 
ATOM   391  C  CA    . VAL A 1 53  ? 2.71787   -4.10446  -12.65239 1.000 27.95100 ? 53  VAL A CA    1 
ATOM   392  C  C     . VAL A 1 53  ? 4.01986   -4.74547  -12.18837 1.000 28.85250 ? 53  VAL A C     1 
ATOM   393  O  O     . VAL A 1 53  ? 4.64485   -4.24747  -11.24436 1.000 31.68641 ? 53  VAL A O     1 
ATOM   394  C  CB    . VAL A 1 53  ? 1.58585   -4.37846  -11.64641 1.000 27.27875 ? 53  VAL A CB    1 
ATOM   395  C  CG1   . VAL A 1 53  ? 1.55284   -5.85147  -11.26141 1.000 32.38012 ? 53  VAL A CG1   1 
ATOM   396  C  CG2   . VAL A 1 53  ? 1.72383   -3.48747  -10.41440 1.000 27.69721 ? 53  VAL A CG2   1 
ATOM   397  N  N     . ASN A 1 54  ? 4.45687   -5.82746  -12.83537 1.000 26.34855 ? 54  ASN A N     1 
ATOM   398  C  CA    . ASN A 1 54  ? 5.70986   -6.46547  -12.44835 1.000 26.61654 ? 54  ASN A CA    1 
ATOM   399  C  C     . ASN A 1 54  ? 6.90987   -5.60447  -12.82333 1.000 29.31488 ? 54  ASN A C     1 
ATOM   400  O  O     . ASN A 1 54  ? 7.81586   -5.39647  -12.00632 1.000 28.94566 ? 54  ASN A O     1 
ATOM   401  C  CB    . ASN A 1 54  ? 5.81987   -7.84747  -13.09435 1.000 26.07586 ? 54  ASN A CB    1 
ATOM   402  C  CG    . ASN A 1 54  ? 5.20085   -8.93947  -12.24537 1.000 25.61336 ? 54  ASN A CG    1 
ATOM   403  O  OD1   . ASN A 1 54  ? 5.22583   -8.87547  -11.01737 1.000 25.79488 ? 54  ASN A OD1   1 
ATOM   404  N  ND2   . ASN A 1 54  ? 4.64586   -9.95446  -12.89738 1.000 26.40843 ? 54  ASN A ND2   1 
ATOM   405  N  N     . ARG A 1 55  ? 6.93571   -5.09403  -14.05727 1.000 30.76342 ? 55  ARG A N     1 
ATOM   406  C  CA    . ARG A 1 55  ? 8.08743   -4.31640  -14.50338 1.000 31.50462 ? 55  ARG A CA    1 
ATOM   407  C  C     . ARG A 1 55  ? 8.11226   -2.93565  -13.85787 1.000 29.78888 ? 55  ARG A C     1 
ATOM   408  O  O     . ARG A 1 55  ? 9.18594   -2.42365  -13.52011 1.000 34.17058 ? 55  ARG A O     1 
ATOM   409  C  CB    . ARG A 1 55  ? 8.09150   -4.19807  -16.02910 1.000 23.06955 ? 55  ARG A CB    1 
ATOM   410  C  CG    . ARG A 1 55  ? 9.30664   -3.45602  -16.56895 1.000 24.37954 ? 55  ARG A CG    1 
ATOM   411  C  CD    . ARG A 1 55  ? 9.52270   -3.66691  -18.06086 1.000 21.46995 ? 55  ARG A CD    1 
ATOM   412  N  NE    . ARG A 1 55  ? 8.72302   -2.76574  -18.88162 1.000 22.35863 ? 55  ARG A NE    1 
ATOM   413  C  CZ    . ARG A 1 55  ? 7.64958   -3.13050  -19.56828 1.000 23.08668 ? 55  ARG A CZ    1 
ATOM   414  N  NH1   . ARG A 1 55  ? 7.21554   -4.38027  -19.56005 1.000 28.28562 ? 55  ARG A NH1   1 
ATOM   415  N  NH2   . ARG A 1 55  ? 6.99806   -2.21950  -20.28536 1.000 26.56035 ? 55  ARG A NH2   1 
ATOM   416  N  N     . TYR A 1 56  ? 6.94289   -2.31847  -13.67132 1.000 28.76409 ? 56  TYR A N     1 
ATOM   417  C  CA    . TYR A 1 56  ? 6.90888   -0.97847  -13.09531 1.000 29.35749 ? 56  TYR A CA    1 
ATOM   418  C  C     . TYR A 1 56  ? 7.25886   -1.00347  -11.61231 1.000 28.49497 ? 56  TYR A C     1 
ATOM   419  O  O     . TYR A 1 56  ? 7.96485   -0.11448  -11.12129 1.000 26.16081 ? 56  TYR A O     1 
ATOM   420  C  CB    . TYR A 1 56  ? 5.53788   -0.34146  -13.31633 1.000 34.58284 ? 56  TYR A CB    1 
ATOM   421  C  CG    . TYR A 1 56  ? 5.56589   1.17053   -13.28933 1.000 29.65719 ? 56  TYR A CG    1 
ATOM   422  C  CD1   . TYR A 1 56  ? 5.38487   1.86753   -12.10233 1.000 35.44538 ? 56  TYR A CD1   1 
ATOM   423  C  CD2   . TYR A 1 56  ? 5.77991   1.89954   -14.45232 1.000 22.50947 ? 56  TYR A CD2   1 
ATOM   424  C  CE1   . TYR A 1 56  ? 5.41387   3.25053   -12.07532 1.000 34.28934 ? 56  TYR A CE1   1 
ATOM   425  C  CE2   . TYR A 1 56  ? 5.81091   3.28154   -14.43532 1.000 30.43345 ? 56  TYR A CE2   1 
ATOM   426  C  CZ    . TYR A 1 56  ? 5.62689   3.95153   -13.24432 1.000 39.86764 ? 56  TYR A CZ    1 
ATOM   427  O  OH    . TYR A 1 56  ? 5.65589   5.32753   -13.22331 1.000 46.88200 ? 56  TYR A OH    1 
ATOM   428  N  N     . ASN A 1 57  ? 6.77384   -2.01048  -10.87832 1.000 28.09610 ? 57  ASN A N     1 
ATOM   429  C  CA    . ASN A 1 57  ? 7.15882   -2.14148  -9.47731  1.000 26.13120 ? 57  ASN A CA    1 
ATOM   430  C  C     . ASN A 1 57  ? 8.61982   -2.55148  -9.34129  1.000 25.61617 ? 57  ASN A C     1 
ATOM   431  O  O     . ASN A 1 57  ? 9.25280   -2.25649  -8.32128  1.000 29.38480 ? 57  ASN A O     1 
ATOM   432  C  CB    . ASN A 1 57  ? 6.25281   -3.14548  -8.76833  1.000 25.26257 ? 57  ASN A CB    1 
ATOM   433  C  CG    . ASN A 1 57  ? 6.50479   -3.20449  -7.27333  1.000 35.80156 ? 57  ASN A CG    1 
ATOM   434  O  OD1   . ASN A 1 57  ? 7.25278   -4.05549  -6.79232  1.000 47.96903 ? 57  ASN A OD1   1 
ATOM   435  N  ND2   . ASN A 1 57  ? 5.88278   -2.29649  -6.53133  1.000 35.91314 ? 57  ASN A ND2   1 
ATOM   436  N  N     . PHE A 1 58  ? 9.16583   -3.23048  -10.35229 1.000 24.97793 ? 58  PHE A N     1 
ATOM   437  C  CA    . PHE A 1 58  ? 10.59883  -3.49948  -10.37627 1.000 24.57768 ? 58  PHE A CA    1 
ATOM   438  C  C     . PHE A 1 58  ? 11.38884  -2.20249  -10.49425 1.000 27.88278 ? 58  PHE A C     1 
ATOM   439  O  O     . PHE A 1 58  ? 12.47283  -2.06749  -9.91323  1.000 26.77127 ? 58  PHE A O     1 
ATOM   440  C  CB    . PHE A 1 58  ? 10.93085  -4.44348  -11.53526 1.000 23.43014 ? 58  PHE A CB    1 
ATOM   441  C  CG    . PHE A 1 58  ? 12.30185  -5.05548  -11.45625 1.000 22.06008 ? 58  PHE A CG    1 
ATOM   442  C  CD1   . PHE A 1 58  ? 13.41286  -4.37448  -11.92723 1.000 22.01699 ? 58  PHE A CD1   1 
ATOM   443  C  CD2   . PHE A 1 58  ? 12.47884  -6.32249  -10.92525 1.000 20.41484 ? 58  PHE A CD2   1 
ATOM   444  C  CE1   . PHE A 1 58  ? 14.67185  -4.93949  -11.85921 1.000 20.35789 ? 58  PHE A CE1   1 
ATOM   445  C  CE2   . PHE A 1 58  ? 13.73383  -6.89349  -10.85523 1.000 20.10814 ? 58  PHE A CE2   1 
ATOM   446  C  CZ    . PHE A 1 58  ? 14.83284  -6.20149  -11.32521 1.000 21.75024 ? 58  PHE A CZ    1 
ATOM   447  N  N     . LEU A 1 59  ? 10.85785  -1.23448  -11.24425 1.000 24.67467 ? 59  LEU A N     1 
ATOM   448  C  CA    . LEU A 1 59  ? 11.49585  0.07452   -11.33524 1.000 23.25779 ? 59  LEU A CA    1 
ATOM   449  C  C     . LEU A 1 59  ? 11.41784  0.81751   -10.00824 1.000 28.45519 ? 59  LEU A C     1 
ATOM   450  O  O     . LEU A 1 59  ? 12.40283  1.42551   -9.57222  1.000 25.71228 ? 59  LEU A O     1 
ATOM   451  C  CB    . LEU A 1 59  ? 10.84287  0.89452   -12.44725 1.000 25.56553 ? 59  LEU A CB    1 
ATOM   452  C  CG    . LEU A 1 59  ? 11.27388  2.35552   -12.58724 1.000 19.65658 ? 59  LEU A CG    1 
ATOM   453  C  CD1   . LEU A 1 59  ? 12.68189  2.45352   -13.15121 1.000 17.74335 ? 59  LEU A CD1   1 
ATOM   454  C  CD2   . LEU A 1 59  ? 10.28689  3.12653   -13.45125 1.000 21.24943 ? 59  LEU A CD2   1 
ATOM   455  N  N     . LEU A 1 60  ? 10.25483  0.77751   -9.35226  1.000 28.72421 ? 60  LEU A N     1 
ATOM   456  C  CA    . LEU A 1 60  ? 10.09381  1.46751   -8.07726  1.000 23.32912 ? 60  LEU A CA    1 
ATOM   457  C  C     . LEU A 1 60  ? 10.99479  0.86750   -7.00524  1.000 26.15417 ? 60  LEU A C     1 
ATOM   458  O  O     . LEU A 1 60  ? 11.64178  1.59950   -6.24723  1.000 24.87343 ? 60  LEU A O     1 
ATOM   459  C  CB    . LEU A 1 60  ? 8.62880   1.42051   -7.63928  1.000 20.63975 ? 60  LEU A CB    1 
ATOM   460  C  CG    . LEU A 1 60  ? 7.61582   2.03851   -8.60529  1.000 21.31141 ? 60  LEU A CG    1 
ATOM   461  C  CD1   . LEU A 1 60  ? 6.19881   1.87352   -8.07831  1.000 23.84649 ? 60  LEU A CD1   1 
ATOM   462  C  CD2   . LEU A 1 60  ? 7.93282   3.50651   -8.85228  1.000 25.64944 ? 60  LEU A CD2   1 
ATOM   463  N  N     . GLU A 1 61  ? 11.04679  -0.46550  -6.92225  1.000 22.92994 ? 61  GLU A N     1 
ATOM   464  C  CA    . GLU A 1 61  ? 11.95877  -1.10950  -5.98224  1.000 22.49660 ? 61  GLU A CA    1 
ATOM   465  C  C     . GLU A 1 61  ? 13.40678  -0.74750  -6.28121  1.000 22.14329 ? 61  GLU A C     1 
ATOM   466  O  O     . GLU A 1 61  ? 14.22276  -0.63851  -5.36020  1.000 26.30164 ? 61  GLU A O     1 
ATOM   467  C  CB    . GLU A 1 61  ? 11.77077  -2.62550  -6.01525  1.000 26.64013 ? 61  GLU A CB    1 
ATOM   468  C  CG    . GLU A 1 61  ? 10.47376  -3.10850  -5.38727  1.000 26.62507 ? 61  GLU A CG    1 
ATOM   469  C  CD    . GLU A 1 61  ? 10.31876  -4.61450  -5.46327  1.000 30.44273 ? 61  GLU A CD    1 
ATOM   470  O  OE1   . GLU A 1 61  ? 11.04977  -5.24850  -6.25427  1.000 21.92034 ? 61  GLU A OE1   1 
ATOM   471  O  OE2   . GLU A 1 61  ? 9.46874   -5.16450  -4.73129  1.000 35.75087 ? 61  GLU A OE2   1 
ATOM   472  N  N     . SER A 1 62  ? 13.74280  -0.55550  -7.55921  1.000 24.91168 ? 62  SER A N     1 
ATOM   473  C  CA    . SER A 1 62  ? 15.08180  -0.09450  -7.90819  1.000 22.37464 ? 62  SER A CA    1 
ATOM   474  C  C     . SER A 1 62  ? 15.28180  1.36650   -7.52618  1.000 23.62963 ? 62  SER A C     1 
ATOM   475  O  O     . SER A 1 62  ? 16.39679  1.76349   -7.16916  1.000 21.38414 ? 62  SER A O     1 
ATOM   476  C  CB    . SER A 1 62  ? 15.33382  -0.29550  -9.40218  1.000 26.57122 ? 62  SER A CB    1 
ATOM   477  O  OG    . SER A 1 62  ? 15.16783  -1.65449  -9.77019  1.000 24.40654 ? 62  SER A OG    1 
ATOM   478  N  N     . LEU A 1 63  ? 14.22180  2.17650   -7.59519  1.000 20.33950 ? 63  LEU A N     1 
ATOM   479  C  CA    . LEU A 1 63  ? 14.33680  3.57650   -7.19818  1.000 21.13556 ? 63  LEU A CA    1 
ATOM   480  C  C     . LEU A 1 63  ? 14.52778  3.71049   -5.69218  1.000 25.23764 ? 63  LEU A C     1 
ATOM   481  O  O     . LEU A 1 63  ? 15.25377  4.59849   -5.23017  1.000 26.76660 ? 63  LEU A O     1 
ATOM   482  C  CB    . LEU A 1 63  ? 13.10581  4.35850   -7.65820  1.000 24.31553 ? 63  LEU A CB    1 
ATOM   483  C  CG    . LEU A 1 63  ? 12.94583  4.56451   -9.16620  1.000 17.92162 ? 63  LEU A CG    1 
ATOM   484  C  CD1   . LEU A 1 63  ? 11.70384  5.39051   -9.46922  1.000 24.79689 ? 63  LEU A CD1   1 
ATOM   485  C  CD2   . LEU A 1 63  ? 14.18484  5.21851   -9.75718  1.000 22.66662 ? 63  LEU A CD2   1 
ATOM   486  N  N     . GLU A 1 64  ? 13.88376  2.84049   -4.90919  1.000 25.83498 ? 64  GLU A N     1 
ATOM   487  C  CA    . GLU A 1 64  ? 14.08674  2.85548   -3.46619  1.000 26.55234 ? 64  GLU A CA    1 
ATOM   488  C  C     . GLU A 1 64  ? 15.49173  2.41548   -3.07917  1.000 21.50524 ? 64  GLU A C     1 
ATOM   489  O  O     . GLU A 1 64  ? 15.97272  2.79348   -2.00616  1.000 23.86143 ? 64  GLU A O     1 
ATOM   490  C  CB    . GLU A 1 64  ? 13.05173  1.96648   -2.77421  1.000 25.11858 ? 64  GLU A CB    1 
ATOM   491  C  CG    . GLU A 1 64  ? 11.61673  2.43249   -2.95423  1.000 31.37209 ? 64  GLU A CG    1 
ATOM   492  C  CD    . GLU A 1 64  ? 10.63772  1.66749   -2.08525  1.000 30.11589 ? 64  GLU A CD    1 
ATOM   493  O  OE1   . GLU A 1 64  ? 11.08470  0.80948   -1.29424  1.000 32.31086 ? 64  GLU A OE1   1 
ATOM   494  O  OE2   . GLU A 1 64  ? 9.42072   1.92649   -2.19127  1.000 25.99892 ? 64  GLU A OE2   1 
ATOM   495  N  N     . ASP A 1 65  ? 16.15674  1.62548   -3.92616  1.000 20.78133 ? 65  ASP A N     1 
ATOM   496  C  CA    . ASP A 1 65  ? 17.54574  1.26648   -3.66314  1.000 21.89262 ? 65  ASP A CA    1 
ATOM   497  C  C     . ASP A 1 65  ? 18.45874  2.47648   -3.81713  1.000 23.45134 ? 65  ASP A C     1 
ATOM   498  O  O     . ASP A 1 65  ? 19.40473  2.65247   -3.04111  1.000 22.51851 ? 65  ASP A O     1 
ATOM   499  C  CB    . ASP A 1 65  ? 17.97675  0.13548   -4.59714  1.000 22.77546 ? 65  ASP A CB    1 
ATOM   500  C  CG    . ASP A 1 65  ? 19.22874  -0.58052  -4.12012  1.000 18.91130 ? 65  ASP A CG    1 
ATOM   501  O  OD1   . ASP A 1 65  ? 20.25874  0.08647   -3.88511  1.000 18.71291 ? 65  ASP A OD1   1 
ATOM   502  O  OD2   . ASP A 1 65  ? 19.17774  -1.81952  -3.97613  1.000 19.10623 ? 65  ASP A OD2   1 
ATOM   503  N  N     . LEU A 1 66  ? 18.18876  3.32348   -4.81413  1.000 22.57365 ? 66  LEU A N     1 
ATOM   504  C  CA    . LEU A 1 66  ? 18.95377  4.55448   -4.96511  1.000 20.25690 ? 66  LEU A CA    1 
ATOM   505  C  C     . LEU A 1 66  ? 18.68875  5.51048   -3.80711  1.000 26.29863 ? 66  LEU A C     1 
ATOM   506  O  O     . LEU A 1 66  ? 19.61974  6.13047   -3.28209  1.000 19.11160 ? 66  LEU A O     1 
ATOM   507  C  CB    . LEU A 1 66  ? 18.61779  5.22249   -6.29611  1.000 18.14754 ? 66  LEU A CB    1 
ATOM   508  C  CG    . LEU A 1 66  ? 18.78480  4.37749   -7.56111  1.000 18.32420 ? 66  LEU A CG    1 
ATOM   509  C  CD1   . LEU A 1 66  ? 18.33083  5.15650   -8.78312  1.000 16.35438 ? 66  LEU A CD1   1 
ATOM   510  C  CD2   . LEU A 1 66  ? 20.22681  3.91949   -7.71709  1.000 21.28976 ? 66  LEU A CD2   1 
ATOM   511  N  N     . GLN A 1 67  ? 17.42374  5.63548   -3.39513  1.000 28.80179 ? 67  GLN A N     1 
ATOM   512  C  CA    . GLN A 1 67  ? 17.08373  6.55847   -2.31913  1.000 26.47416 ? 67  GLN A CA    1 
ATOM   513  C  C     . GLN A 1 67  ? 17.74071  6.14647   -1.00712  1.000 21.72590 ? 67  GLN A C     1 
ATOM   514  O  O     . GLN A 1 67  ? 18.17970  7.00147   -0.22911  1.000 23.99290 ? 67  GLN A O     1 
ATOM   515  C  CB    . GLN A 1 67  ? 15.56573  6.64448   -2.16115  1.000 23.08189 ? 67  GLN A CB    1 
ATOM   516  C  CG    . GLN A 1 67  ? 15.10571  7.61847   -1.08816  1.000 19.85377 ? 67  GLN A CG    1 
ATOM   517  C  CD    . GLN A 1 67  ? 15.57272  9.03747   -1.34715  1.000 24.37427 ? 67  GLN A CD    1 
ATOM   518  O  OE1   . GLN A 1 67  ? 14.96873  9.76948   -2.13215  1.000 25.85063 ? 67  GLN A OE1   1 
ATOM   519  N  NE2   . GLN A 1 67  ? 16.65271  9.43447   -0.68613  1.000 18.60791 ? 67  GLN A NE2   1 
ATOM   520  N  N     . ARG A 1 68  ? 17.82206  4.84015   -0.74424  1.000 23.40555 ? 68  ARG A N     1 
ATOM   521  C  CA    . ARG A 1 68  ? 18.52037  4.37863   0.45045   1.000 25.25879 ? 68  ARG A CA    1 
ATOM   522  C  C     . ARG A 1 68  ? 20.02513  4.58343   0.33474   1.000 23.98723 ? 68  ARG A C     1 
ATOM   523  O  O     . ARG A 1 68  ? 20.69186  4.84887   1.34142   1.000 20.79291 ? 68  ARG A O     1 
ATOM   524  C  CB    . ARG A 1 68  ? 18.20391  2.90704   0.71431   1.000 24.60218 ? 68  ARG A CB    1 
ATOM   525  C  CG    . ARG A 1 68  ? 16.79574  2.65522   1.22457   1.000 26.69927 ? 68  ARG A CG    1 
ATOM   526  C  CD    . ARG A 1 68  ? 16.57599  1.18008   1.50939   1.000 30.03403 ? 68  ARG A CD    1 
ATOM   527  N  NE    . ARG A 1 68  ? 16.66883  0.37304   0.29877   1.000 27.92648 ? 68  ARG A NE    1 
ATOM   528  C  CZ    . ARG A 1 68  ? 15.62816  0.00309   -0.43478  1.000 25.00232 ? 68  ARG A CZ    1 
ATOM   529  N  NH1   . ARG A 1 68  ? 14.39358  0.34415   -0.10397  1.000 25.93356 ? 68  ARG A NH1   1 
ATOM   530  N  NH2   . ARG A 1 68  ? 15.83088  -0.72995  -1.52584  1.000 27.73188 ? 68  ARG A NH2   1 
ATOM   531  N  N     . SER A 1 69  ? 20.57570  4.46846   -0.87609  1.000 26.69686 ? 69  SER A N     1 
ATOM   532  C  CA    . SER A 1 69  ? 22.00771  4.68046   -1.05706  1.000 23.98160 ? 69  SER A CA    1 
ATOM   533  C  C     . SER A 1 69  ? 22.36271  6.16046   -0.97205  1.000 25.86957 ? 69  SER A C     1 
ATOM   534  O  O     . SER A 1 69  ? 23.43370  6.51846   -0.47003  1.000 32.02042 ? 69  SER A O     1 
ATOM   535  C  CB    . SER A 1 69  ? 22.46173  4.09347   -2.39306  1.000 18.01188 ? 69  SER A CB    1 
ATOM   536  O  OG    . SER A 1 69  ? 22.25672  2.69247   -2.42807  1.000 18.23650 ? 69  SER A OG    1 
ATOM   537  N  N     . PHE A 1 70  ? 21.47772  7.03446   -1.45806  1.000 24.28460 ? 70  PHE A N     1 
ATOM   538  C  CA    . PHE A 1 70  ? 21.73272  8.46746   -1.35405  1.000 24.84730 ? 70  PHE A CA    1 
ATOM   539  C  C     . PHE A 1 70  ? 21.52370  8.96546   0.07194   1.000 26.43919 ? 70  PHE A C     1 
ATOM   540  O  O     . PHE A 1 70  ? 22.24869  9.85246   0.53596   1.000 27.38676 ? 70  PHE A O     1 
ATOM   541  C  CB    . PHE A 1 70  ? 20.84173  9.23847   -2.33006  1.000 22.77897 ? 70  PHE A CB    1 
ATOM   542  C  CG    . PHE A 1 70  ? 21.33776  9.22047   -3.74906  1.000 25.59013 ? 70  PHE A CG    1 
ATOM   543  C  CD1   . PHE A 1 70  ? 22.51476  9.86347   -4.09404  1.000 24.08898 ? 70  PHE A CD1   1 
ATOM   544  C  CD2   . PHE A 1 70  ? 20.62077  8.57448   -4.74207  1.000 22.88095 ? 70  PHE A CD2   1 
ATOM   545  C  CE1   . PHE A 1 70  ? 22.97278  9.85248   -5.39903  1.000 22.26499 ? 70  PHE A CE1   1 
ATOM   546  C  CE2   . PHE A 1 70  ? 21.07279  8.55848   -6.04806  1.000 20.92656 ? 70  PHE A CE2   1 
ATOM   547  C  CZ    . PHE A 1 70  ? 22.24980  9.19948   -6.37704  1.000 20.74569 ? 70  PHE A CZ    1 
ATOM   548  N  N     . GLN A 1 71  ? 20.53768  8.40846   0.78193   1.000 25.16929 ? 71  GLN A N     1 
ATOM   549  C  CA    . GLN A 1 71  ? 20.31666  8.81245   2.16693   1.000 28.31141 ? 71  GLN A CA    1 
ATOM   550  C  C     . GLN A 1 71  ? 21.46065  8.37445   3.06894   1.000 29.70933 ? 71  GLN A C     1 
ATOM   551  O  O     . GLN A 1 71  ? 21.78664  9.07244   4.03695   1.000 27.59527 ? 71  GLN A O     1 
ATOM   552  C  CB    . GLN A 1 71  ? 18.99066  8.24945   2.67990   1.000 27.96698 ? 71  GLN A CB    1 
ATOM   553  C  CG    . GLN A 1 71  ? 17.78566  9.11046   2.34389   1.000 29.81550 ? 71  GLN A CG    1 
ATOM   554  C  CD    . GLN A 1 71  ? 16.47665  8.48746   2.78887   1.000 34.26557 ? 71  GLN A CD    1 
ATOM   555  O  OE1   . GLN A 1 71  ? 16.39665  7.28146   3.02186   1.000 31.62384 ? 71  GLN A OE1   1 
ATOM   556  N  NE2   . GLN A 1 71  ? 15.44165  9.31146   2.90985   1.000 31.28402 ? 71  GLN A NE2   1 
ATOM   557  N  N     . ALA A 1 72  ? 22.08265  7.23145   2.77195   1.000 25.95309 ? 72  ALA A N     1 
ATOM   558  C  CA    . ALA A 1 72  ? 23.22264  6.76844   3.55196   1.000 28.03145 ? 72  ALA A CA    1 
ATOM   559  C  C     . ALA A 1 72  ? 24.49465  7.55444   3.26099   1.000 30.59379 ? 72  ALA A C     1 
ATOM   560  O  O     . ALA A 1 72  ? 25.50863  7.32444   3.92800   1.000 35.76119 ? 72  ALA A O     1 
ATOM   561  C  CB    . ALA A 1 72  ? 23.46464  5.27944   3.29396   1.000 33.08145 ? 72  ALA A CB    1 
ATOM   562  N  N     . ARG A 1 73  ? 24.46666  8.46907   2.29034   1.000 23.89557 ? 73  ARG A N     1 
ATOM   563  C  CA    . ARG A 1 73  ? 25.63060  9.27211   1.93528   1.000 32.19712 ? 73  ARG A CA    1 
ATOM   564  C  C     . ARG A 1 73  ? 25.35785  10.76572  2.07309   1.000 27.90320 ? 73  ARG A C     1 
ATOM   565  O  O     . ARG A 1 73  ? 26.10380  11.58209  1.52383   1.000 27.81331 ? 73  ARG A O     1 
ATOM   566  C  CB    . ARG A 1 73  ? 26.09104  8.94064   0.51466   1.000 29.30676 ? 73  ARG A CB    1 
ATOM   567  C  CG    . ARG A 1 73  ? 26.46236  7.47920   0.31981   1.000 28.69149 ? 73  ARG A CG    1 
ATOM   568  C  CD    . ARG A 1 73  ? 26.71835  7.15921   -1.14164  1.000 19.22433 ? 73  ARG A CD    1 
ATOM   569  N  NE    . ARG A 1 73  ? 26.98123  5.74073   -1.35203  1.000 18.68547 ? 73  ARG A NE    1 
ATOM   570  C  CZ    . ARG A 1 73  ? 28.19155  5.20066   -1.39479  1.000 28.76260 ? 73  ARG A CZ    1 
ATOM   571  N  NH1   . ARG A 1 73  ? 29.28232  5.93514   -1.24672  1.000 28.79147 ? 73  ARG A NH1   1 
ATOM   572  N  NH2   . ARG A 1 73  ? 28.31084  3.89101   -1.59363  1.000 22.47004 ? 73  ARG A NH2   1 
ATOM   573  N  N     . GLY A 1 74  ? 24.30266  11.13944  2.79200   1.000 28.35650 ? 74  GLY A N     1 
ATOM   574  C  CA    . GLY A 1 74  ? 24.00066  12.53444  3.03600   1.000 27.17731 ? 74  GLY A CA    1 
ATOM   575  C  C     . GLY A 1 74  ? 23.19768  13.22745  1.95999   1.000 26.92749 ? 74  GLY A C     1 
ATOM   576  O  O     . GLY A 1 74  ? 23.06168  14.45545  2.00899   1.000 28.99969 ? 74  GLY A O     1 
ATOM   577  N  N     . SER A 1 75  ? 22.65869  12.48745  0.99097   1.000 24.34437 ? 75  SER A N     1 
ATOM   578  C  CA    . SER A 1 75  ? 21.87871  13.09746  -0.07903  1.000 25.80619 ? 75  SER A CA    1 
ATOM   579  C  C     . SER A 1 75  ? 20.45971  12.54346  -0.09806  1.000 28.64156 ? 75  SER A C     1 
ATOM   580  O  O     . SER A 1 75  ? 20.01269  11.93446  0.87893   1.000 28.78335 ? 75  SER A O     1 
ATOM   581  C  CB    . SER A 1 75  ? 22.55673  12.87446  -1.43103  1.000 22.73333 ? 75  SER A CB    1 
ATOM   582  O  OG    . SER A 1 75  ? 21.85274  13.53647  -2.46703  1.000 26.76681 ? 75  SER A OG    1 
ATOM   583  N  N     . ARG A 1 76  ? 19.74764  12.75156  -1.20453  1.000 20.82625 ? 76  ARG A N     1 
ATOM   584  C  CA    . ARG A 1 76  ? 18.35766  12.32786  -1.31252  1.000 24.30768 ? 76  ARG A CA    1 
ATOM   585  C  C     . ARG A 1 76  ? 17.95306  12.33311  -2.77790  1.000 23.56278 ? 76  ARG A C     1 
ATOM   586  O  O     . ARG A 1 76  ? 18.25005  13.28900  -3.50038  1.000 30.91867 ? 76  ARG A O     1 
ATOM   587  C  CB    . ARG A 1 76  ? 17.44000  13.24688  -0.49739  1.000 25.47980 ? 76  ARG A CB    1 
ATOM   588  C  CG    . ARG A 1 76  ? 15.95787  12.94623  -0.63834  1.000 24.35752 ? 76  ARG A CG    1 
ATOM   589  C  CD    . ARG A 1 76  ? 15.14116  13.79093  0.32522   1.000 19.06779 ? 76  ARG A CD    1 
ATOM   590  N  NE    . ARG A 1 76  ? 15.46978  15.20702  0.21701   1.000 19.52360 ? 76  ARG A NE    1 
ATOM   591  C  CZ    . ARG A 1 76  ? 14.78200  16.08495  -0.50016  1.000 25.03259 ? 76  ARG A CZ    1 
ATOM   592  N  NH1   . ARG A 1 76  ? 13.70400  15.72952  -1.17952  1.000 21.19748 ? 76  ARG A NH1   1 
ATOM   593  N  NH2   . ARG A 1 76  ? 15.18423  17.35234  -0.53370  1.000 22.11834 ? 76  ARG A NH2   1 
ATOM   594  N  N     . LEU A 1 77  ? 17.28075  11.26948  -3.20811  1.000 19.19472 ? 77  LEU A N     1 
ATOM   595  C  CA    . LEU A 1 77  ? 16.80477  11.16948  -4.58012  1.000 17.20368 ? 77  LEU A CA    1 
ATOM   596  C  C     . LEU A 1 77  ? 15.54878  12.01149  -4.77014  1.000 24.93436 ? 77  LEU A C     1 
ATOM   597  O  O     . LEU A 1 77  ? 14.66876  12.04648  -3.90515  1.000 22.13131 ? 77  LEU A O     1 
ATOM   598  C  CB    . LEU A 1 77  ? 16.51777  9.71249   -4.94113  1.000 22.78333 ? 77  LEU A CB    1 
ATOM   599  C  CG    . LEU A 1 77  ? 15.99080  9.42449   -6.34714  1.000 23.79652 ? 77  LEU A CG    1 
ATOM   600  C  CD1   . LEU A 1 77  ? 17.01681  9.83049   -7.39612  1.000 24.25270 ? 77  LEU A CD1   1 
ATOM   601  C  CD2   . LEU A 1 77  ? 15.62579  7.95349   -6.48715  1.000 19.91410 ? 77  LEU A CD2   1 
ATOM   602  N  N     . LEU A 1 78  ? 15.46879  12.69149  -5.91313  1.000 23.47770 ? 78  LEU A N     1 
ATOM   603  C  CA    . LEU A 1 78  ? 14.33980  13.55049  -6.25415  1.000 22.04905 ? 78  LEU A CA    1 
ATOM   604  C  C     . LEU A 1 78  ? 13.56282  12.92750  -7.40616  1.000 23.57527 ? 78  LEU A C     1 
ATOM   605  O  O     . LEU A 1 78  ? 14.11283  12.74350  -8.49715  1.000 21.09175 ? 78  LEU A O     1 
ATOM   606  C  CB    . LEU A 1 78  ? 14.81681  14.95449  -6.63014  1.000 17.43642 ? 78  LEU A CB    1 
ATOM   607  C  CG    . LEU A 1 78  ? 15.53079  15.71249  -5.51212  1.000 17.91545 ? 78  LEU A CG    1 
ATOM   608  C  CD1   . LEU A 1 78  ? 16.15780  16.98649  -6.04111  1.000 22.54096 ? 78  LEU A CD1   1 
ATOM   609  C  CD2   . LEU A 1 78  ? 14.55078  16.01349  -4.39814  1.000 18.56278 ? 78  LEU A CD2   1 
ATOM   610  N  N     . VAL A 1 79  ? 12.29081  12.60750  -7.16518  1.000 23.61136 ? 79  VAL A N     1 
ATOM   611  C  CA    . VAL A 1 79  ? 11.43683  12.04851  -8.20720  1.000 23.13995 ? 79  VAL A CA    1 
ATOM   612  C  C     . VAL A 1 79  ? 10.47884  13.12551  -8.70421  1.000 22.05584 ? 79  VAL A C     1 
ATOM   613  O  O     . VAL A 1 79  ? 9.38883   13.30851  -8.14622  1.000 23.87244 ? 79  VAL A O     1 
ATOM   614  C  CB    . VAL A 1 79  ? 10.65382  10.81751  -7.70721  1.000 24.89006 ? 79  VAL A CB    1 
ATOM   615  C  CG1   . VAL A 1 79  ? 9.81984   10.23151  -8.84323  1.000 25.58005 ? 79  VAL A CG1   1 
ATOM   616  C  CG2   . VAL A 1 79  ? 11.58781  9.77550   -7.12620  1.000 23.31734 ? 79  VAL A CG2   1 
ATOM   617  N  N     . LEU A 1 80  ? 10.86286  13.82451  -9.77120  1.000 22.99075 ? 80  LEU A N     1 
ATOM   618  C  CA    . LEU A 1 80  ? 10.03887  14.90152  -10.30221 1.000 24.39150 ? 80  LEU A CA    1 
ATOM   619  C  C     . LEU A 1 80  ? 8.96888   14.36352  -11.24323 1.000 27.32020 ? 80  LEU A C     1 
ATOM   620  O  O     . LEU A 1 80  ? 9.22689   13.47352  -12.05723 1.000 25.58845 ? 80  LEU A O     1 
ATOM   621  C  CB    . LEU A 1 80  ? 10.91388  15.91952  -11.03019 1.000 22.70205 ? 80  LEU A CB    1 
ATOM   622  C  CG    . LEU A 1 80  ? 11.86287  16.73351  -10.14817 1.000 18.31708 ? 80  LEU A CG    1 
ATOM   623  C  CD1   . LEU A 1 80  ? 12.75988  17.63951  -10.98116 1.000 18.35226 ? 80  LEU A CD1   1 
ATOM   624  C  CD2   . LEU A 1 80  ? 11.07485  17.55251  -9.13718  1.000 24.47818 ? 80  LEU A CD2   1 
ATOM   625  N  N     . ARG A 1 81  ? 7.76648   14.92009  -11.13300 1.000 24.97833 ? 81  ARG A N     1 
ATOM   626  C  CA    . ARG A 1 81  ? 6.64970   14.53108  -11.98014 1.000 30.89015 ? 81  ARG A CA    1 
ATOM   627  C  C     . ARG A 1 81  ? 6.56684   15.43128  -13.20745 1.000 26.93875 ? 81  ARG A C     1 
ATOM   628  O  O     . ARG A 1 81  ? 6.95236   16.60288  -13.17225 1.000 27.22812 ? 81  ARG A O     1 
ATOM   629  C  CB    . ARG A 1 81  ? 5.33062   14.58910  -11.20512 1.000 29.27020 ? 81  ARG A CB    1 
ATOM   630  C  CG    . ARG A 1 81  ? 4.97524   13.31315  -10.44808 1.000 35.76225 ? 81  ARG A CG    1 
ATOM   631  C  CD    . ARG A 1 81  ? 5.85631   13.09890  -9.22553  1.000 30.58624 ? 81  ARG A CD    1 
ATOM   632  N  NE    . ARG A 1 81  ? 5.42979   11.94120  -8.44764  1.000 29.51269 ? 81  ARG A NE    1 
ATOM   633  C  CZ    . ARG A 1 81  ? 5.99139   11.55207  -7.31087  1.000 32.08962 ? 81  ARG A CZ    1 
ATOM   634  N  NH1   . ARG A 1 81  ? 7.01570   12.20515  -6.78651  1.000 22.56408 ? 81  ARG A NH1   1 
ATOM   635  N  NH2   . ARG A 1 81  ? 5.51185   10.48167  -6.68320  1.000 21.22541 ? 81  ARG A NH2   1 
ATOM   636  N  N     . GLY A 1 82  ? 6.05693   14.87054  -14.29427 1.000 31.01333 ? 82  GLY A N     1 
ATOM   637  C  CA    . GLY A 1 82  ? 5.88995   15.58854  -15.53727 1.000 34.66211 ? 82  GLY A CA    1 
ATOM   638  C  C     . GLY A 1 82  ? 6.79996   15.07454  -16.63626 1.000 37.23159 ? 82  GLY A C     1 
ATOM   639  O  O     . GLY A 1 82  ? 7.35596   13.97454  -16.57125 1.000 38.27032 ? 82  GLY A O     1 
ATOM   640  N  N     . LYS A 1 83  ? 6.94698   15.90755  -17.68425 1.000 36.03111 ? 83  LYS A N     1 
ATOM   641  C  CA    . LYS A 1 83  ? 7.80700   15.56955  -18.80624 1.000 34.13761 ? 83  LYS A CA    1 
ATOM   642  C  C     . LYS A 1 83  ? 9.13300   16.31755  -18.71622 1.000 28.20824 ? 83  LYS A C     1 
ATOM   643  O  O     . LYS A 1 83  ? 9.18499   17.44455  -18.21421 1.000 34.35477 ? 83  LYS A O     1 
ATOM   644  C  CB    . LYS A 1 83  ? 7.12402   15.90056  -20.13725 1.000 39.06295 ? 83  LYS A CB    1 
ATOM   645  C  CG    . LYS A 1 83  ? 6.19602   14.80756  -20.64227 1.000 38.51828 ? 83  LYS A CG    1 
ATOM   646  C  CD    . LYS A 1 83  ? 5.63305   15.14557  -22.01328 0.000 41.10439 ? 83  LYS A CD    1 
ATOM   647  C  CE    . LYS A 1 83  ? 4.82305   13.98857  -22.57629 0.000 43.84954 ? 83  LYS A CE    1 
ATOM   648  N  NZ    . LYS A 1 83  ? 4.20807   14.32658  -23.89030 0.000 45.51144 ? 83  LYS A NZ    1 
ATOM   649  N  N     . PRO A 1 84  ? 10.22100  15.70655  -19.19320 1.000 29.75406 ? 84  PRO A N     1 
ATOM   650  C  CA    . PRO A 1 84  ? 11.53500  16.36454  -19.08518 1.000 34.19581 ? 84  PRO A CA    1 
ATOM   651  C  C     . PRO A 1 84  ? 11.62202  17.68655  -19.82918 1.000 23.65524 ? 84  PRO A C     1 
ATOM   652  O  O     . PRO A 1 84  ? 12.36301  18.57854  -19.39916 1.000 21.38232 ? 84  PRO A O     1 
ATOM   653  C  CB    . PRO A 1 84  ? 12.49601  15.32255  -19.67317 1.000 27.58602 ? 84  PRO A CB    1 
ATOM   654  C  CG    . PRO A 1 84  ? 11.77901  14.01855  -19.52619 1.000 24.52490 ? 84  PRO A CG    1 
ATOM   655  C  CD    . PRO A 1 84  ? 10.33001  14.33755  -19.72421 1.000 29.38872 ? 84  PRO A CD    1 
ATOM   656  N  N     . GLU A 1 85  ? 10.88403  17.84355  -20.93119 1.000 31.46929 ? 85  GLU A N     1 
ATOM   657  C  CA    . GLU A 1 85  ? 10.92805  19.09356  -21.68018 1.000 28.93547 ? 85  GLU A CA    1 
ATOM   658  C  C     . GLU A 1 85  ? 10.24604  20.23855  -20.94319 1.000 33.39271 ? 85  GLU A C     1 
ATOM   659  O  O     . GLU A 1 85  ? 10.46005  21.40255  -21.29918 1.000 33.11888 ? 85  GLU A O     1 
ATOM   660  C  CB    . GLU A 1 85  ? 10.28107  18.91356  -23.05619 1.000 25.91816 ? 85  GLU A CB    1 
ATOM   661  C  CG    . GLU A 1 85  ? 11.00408  17.93856  -23.97718 1.000 37.52092 ? 85  GLU A CG    1 
ATOM   662  C  CD    . GLU A 1 85  ? 10.65107  16.48956  -23.69719 1.000 27.98314 ? 85  GLU A CD    1 
ATOM   663  O  OE1   . GLU A 1 85  ? 9.74806   16.24256  -22.87021 1.000 30.32680 ? 85  GLU A OE1   1 
ATOM   664  O  OE2   . GLU A 1 85  ? 11.27608  15.59656  -24.30719 1.000 21.54391 ? 85  GLU A OE2   1 
ATOM   665  N  N     . GLU A 1 86  ? 9.43602   19.93655  -19.92620 1.000 33.31491 ? 86  GLU A N     1 
ATOM   666  C  CA    . GLU A 1 86  ? 8.70001   20.95355  -19.19121 1.000 29.56366 ? 86  GLU A CA    1 
ATOM   667  C  C     . GLU A 1 86  ? 9.18999   21.15554  -17.76520 1.000 28.72359 ? 86  GLU A C     1 
ATOM   668  O  O     . GLU A 1 86  ? 8.86698   22.18254  -17.16120 1.000 36.20219 ? 86  GLU A O     1 
ATOM   669  C  CB    . GLU A 1 86  ? 7.20501   20.60155  -19.15123 1.000 30.04128 ? 86  GLU A CB    1 
ATOM   670  C  CG    . GLU A 1 86  ? 6.63203   20.19456  -20.49824 1.000 35.93812 ? 86  GLU A CG    1 
ATOM   671  C  CD    . GLU A 1 86  ? 5.22903   19.62956  -20.38927 1.000 36.47164 ? 86  GLU A CD    1 
ATOM   672  O  OE1   . GLU A 1 86  ? 4.57501   19.86056  -19.35027 1.000 44.81148 ? 86  GLU A OE1   1 
ATOM   673  O  OE2   . GLU A 1 86  ? 4.78304   18.95057  -21.33728 1.000 33.22170 ? 86  GLU A OE2   1 
ATOM   674  N  N     . VAL A 1 87  ? 9.95498   20.21554  -17.21819 1.000 28.09129 ? 87  VAL A N     1 
ATOM   675  C  CA    . VAL A 1 87  ? 10.40396  20.28254  -15.83418 1.000 31.58920 ? 87  VAL A CA    1 
ATOM   676  C  C     . VAL A 1 87  ? 11.81196  20.85453  -15.72316 1.000 31.21109 ? 87  VAL A C     1 
ATOM   677  O  O     . VAL A 1 87  ? 12.08195  21.67053  -14.84015 1.000 25.82084 ? 87  VAL A O     1 
ATOM   678  C  CB    . VAL A 1 87  ? 10.31895  18.88553  -15.18219 1.000 26.73978 ? 87  VAL A CB    1 
ATOM   679  C  CG1   . VAL A 1 87  ? 10.89893  18.91553  -13.78118 1.000 19.00537 ? 87  VAL A CG1   1 
ATOM   680  C  CG2   . VAL A 1 87  ? 8.87795   18.40154  -15.15221 1.000 32.86403 ? 87  VAL A CG2   1 
ATOM   681  N  N     . PHE A 1 88  ? 12.71397  20.44353  -16.61315 1.000 26.88356 ? 88  PHE A N     1 
ATOM   682  C  CA    . PHE A 1 88  ? 14.10497  20.88053  -16.51513 1.000 27.99305 ? 88  PHE A CA    1 
ATOM   683  C  C     . PHE A 1 88  ? 14.29098  22.39153  -16.63912 1.000 31.50922 ? 88  PHE A C     1 
ATOM   684  O  O     . PHE A 1 88  ? 15.07396  22.94753  -15.84810 1.000 31.57060 ? 88  PHE A O     1 
ATOM   685  C  CB    . PHE A 1 88  ? 14.95299  20.13753  -17.55512 1.000 28.37929 ? 88  PHE A CB    1 
ATOM   686  C  CG    . PHE A 1 88  ? 15.32898  18.74353  -17.14111 1.000 29.67645 ? 88  PHE A CG    1 
ATOM   687  C  CD1   . PHE A 1 88  ? 15.67096  18.46653  -15.82711 1.000 19.89427 ? 88  PHE A CD1   1 
ATOM   688  C  CD2   . PHE A 1 88  ? 15.33599  17.70853  -18.06112 1.000 24.22223 ? 88  PHE A CD2   1 
ATOM   689  C  CE1   . PHE A 1 88  ? 16.01695  17.18652  -15.44011 1.000 26.38606 ? 88  PHE A CE1   1 
ATOM   690  C  CE2   . PHE A 1 88  ? 15.67998  16.42653  -17.68112 1.000 24.63140 ? 88  PHE A CE2   1 
ATOM   691  C  CZ    . PHE A 1 88  ? 16.02096  16.16453  -16.36811 1.000 25.99132 ? 88  PHE A CZ    1 
ATOM   692  N  N     . PRO A 1 89  ? 13.64499  23.10554  -17.57212 1.000 34.10522 ? 89  PRO A N     1 
ATOM   693  C  CA    . PRO A 1 89  ? 13.81199  24.56954  -17.59212 1.000 29.26303 ? 89  PRO A CA    1 
ATOM   694  C  C     . PRO A 1 89  ? 13.40598  25.24453  -16.29412 1.000 34.16330 ? 89  PRO A C     1 
ATOM   695  O  O     . PRO A 1 89  ? 13.94797  26.30553  -15.96211 1.000 27.26446 ? 89  PRO A O     1 
ATOM   696  C  CB    . PRO A 1 89  ? 12.91801  25.00754  -18.76013 1.000 21.35093 ? 89  PRO A CB    1 
ATOM   697  C  CG    . PRO A 1 89  ? 12.86602  23.82654  -19.64813 1.000 31.91770 ? 89  PRO A CG    1 
ATOM   698  C  CD    . PRO A 1 89  ? 12.86401  22.63854  -18.73314 1.000 37.66158 ? 89  PRO A CD    1 
ATOM   699  N  N     . ARG A 1 90  ? 12.46978  24.65614  -15.54640 1.000 35.34304 ? 90  ARG A N     1 
ATOM   700  C  CA    . ARG A 1 90  ? 12.08057  25.22935  -14.26252 1.000 32.83755 ? 90  ARG A CA    1 
ATOM   701  C  C     . ARG A 1 90  ? 13.17201  25.03388  -13.21706 1.000 33.97057 ? 90  ARG A C     1 
ATOM   702  O  O     . ARG A 1 90  ? 13.49626  25.96215  -12.46576 1.000 33.13110 ? 90  ARG A O     1 
ATOM   703  C  CB    . ARG A 1 90  ? 10.76931  24.60467  -13.78593 1.000 35.48954 ? 90  ARG A CB    1 
ATOM   704  C  CG    . ARG A 1 90  ? 10.35484  25.02763  -12.38552 1.000 35.23521 ? 90  ARG A CG    1 
ATOM   705  C  CD    . ARG A 1 90  ? 9.92186   23.83076  -11.55778 1.000 31.31319 ? 90  ARG A CD    1 
ATOM   706  N  NE    . ARG A 1 90  ? 8.88561   23.04735  -12.21977 1.000 27.39097 ? 90  ARG A NE    1 
ATOM   707  C  CZ    . ARG A 1 90  ? 8.36790   21.92855  -11.73108 1.000 32.40203 ? 90  ARG A CZ    1 
ATOM   708  N  NH1   . ARG A 1 90  ? 8.76565   21.43229  -10.57112 1.000 30.95108 ? 90  ARG A NH1   1 
ATOM   709  N  NH2   . ARG A 1 90  ? 7.42825   21.29101  -12.42385 1.000 39.20421 ? 90  ARG A NH2   1 
ATOM   710  N  N     . VAL A 1 91  ? 13.74893  23.82952  -13.15112 1.000 36.49413 ? 91  VAL A N     1 
ATOM   711  C  CA    . VAL A 1 91  ? 14.76491  23.53551  -12.14211 1.000 35.33496 ? 91  VAL A CA    1 
ATOM   712  C  C     . VAL A 1 91  ? 16.14992  24.01951  -12.53608 1.000 35.29043 ? 91  VAL A C     1 
ATOM   713  O  O     . VAL A 1 91  ? 17.05690  24.01751  -11.69307 1.000 32.86834 ? 91  VAL A O     1 
ATOM   714  C  CB    . VAL A 1 91  ? 14.82490  22.02551  -11.84311 1.000 34.19132 ? 91  VAL A CB    1 
ATOM   715  C  CG1   . VAL A 1 91  ? 13.45489  21.51451  -11.41913 1.000 36.59087 ? 91  VAL A CG1   1 
ATOM   716  C  CG2   . VAL A 1 91  ? 15.33792  21.25952  -13.05111 1.000 31.62790 ? 91  VAL A CG2   1 
ATOM   717  N  N     . PHE A 1 92  ? 16.34694  24.42952  -13.79108 1.000 38.24134 ? 92  PHE A N     1 
ATOM   718  C  CA    . PHE A 1 92  ? 17.63594  24.98652  -14.18606 1.000 34.70390 ? 92  PHE A CA    1 
ATOM   719  C  C     . PHE A 1 92  ? 17.87494  26.34051  -13.53005 1.000 32.40608 ? 92  PHE A C     1 
ATOM   720  O  O     . PHE A 1 92  ? 18.99793  26.64551  -13.11203 1.000 29.88573 ? 92  PHE A O     1 
ATOM   721  C  CB    . PHE A 1 92  ? 17.71597  25.10652  -15.70806 1.000 34.15164 ? 92  PHE A CB    1 
ATOM   722  C  CG    . PHE A 1 92  ? 18.02597  23.81152  -16.40206 1.000 25.83608 ? 92  PHE A CG    1 
ATOM   723  C  CD1   . PHE A 1 92  ? 18.78396  22.83852  -15.77305 1.000 29.16144 ? 92  PHE A CD1   1 
ATOM   724  C  CD2   . PHE A 1 92  ? 17.56199  23.56853  -17.68406 1.000 33.21990 ? 92  PHE A CD2   1 
ATOM   725  C  CE1   . PHE A 1 92  ? 19.07297  21.64552  -16.41005 1.000 32.72836 ? 92  PHE A CE1   1 
ATOM   726  C  CE2   . PHE A 1 92  ? 17.84600  22.37853  -18.32606 1.000 34.15415 ? 92  PHE A CE2   1 
ATOM   727  C  CZ    . PHE A 1 92  ? 18.60199  21.41553  -17.68806 1.000 33.35821 ? 92  PHE A CZ    1 
ATOM   728  N  N     . ARG A 1 93  ? 16.83025  27.16101  -13.42474 1.000 35.70334 ? 93  ARG A N     1 
ATOM   729  C  CA    . ARG A 1 93  ? 16.94263  28.47233  -12.79942 1.000 32.42390 ? 93  ARG A CA    1 
ATOM   730  C  C     . ARG A 1 93  ? 16.65168  28.43799  -11.30605 1.000 29.05781 ? 93  ARG A C     1 
ATOM   731  O  O     . ARG A 1 93  ? 17.19514  29.25893  -10.55804 1.000 35.15532 ? 93  ARG A O     1 
ATOM   732  C  CB    . ARG A 1 93  ? 15.99532  29.46912  -13.47687 1.000 26.07241 ? 93  ARG A CB    1 
ATOM   733  C  CG    . ARG A 1 93  ? 16.46065  29.97771  -14.83782 1.000 26.54771 ? 93  ARG A CG    1 
ATOM   734  C  CD    . ARG A 1 93  ? 16.17667  28.98431  -15.95421 1.000 29.50670 ? 93  ARG A CD    1 
ATOM   735  N  NE    . ARG A 1 93  ? 16.49390  29.53453  -17.26678 1.000 32.16415 ? 93  ARG A NE    1 
ATOM   736  C  CZ    . ARG A 1 93  ? 16.38011  28.86685  -18.40689 1.000 36.14792 ? 93  ARG A CZ    1 
ATOM   737  N  NH1   . ARG A 1 93  ? 15.96638  27.61044  -18.43409 1.000 32.91924 ? 93  ARG A NH1   1 
ATOM   738  N  NH2   . ARG A 1 93  ? 16.68964  29.47482  -19.54856 1.000 35.94195 ? 93  ARG A NH2   1 
ATOM   739  N  N     . GLU A 1 94  ? 15.80590  27.50851  -10.85608 1.000 31.43887 ? 94  GLU A N     1 
ATOM   740  C  CA    . GLU A 1 94  ? 15.48288  27.42350  -9.43608  1.000 32.47975 ? 94  GLU A CA    1 
ATOM   741  C  C     . GLU A 1 94  ? 16.66886  26.91850  -8.62407  1.000 32.76087 ? 94  GLU A C     1 
ATOM   742  O  O     . GLU A 1 94  ? 16.88085  27.35749  -7.48806  1.000 31.47939 ? 94  GLU A O     1 
ATOM   743  C  CB    . GLU A 1 94  ? 14.26787  26.51750  -9.23210  1.000 30.78735 ? 94  GLU A CB    1 
ATOM   744  C  CG    . GLU A 1 94  ? 13.91585  26.25850  -7.77911  1.000 28.40246 ? 94  GLU A CG    1 
ATOM   745  C  CD    . GLU A 1 94  ? 12.80084  25.24550  -7.62113  1.000 28.61432 ? 94  GLU A CD    1 
ATOM   746  O  OE1   . GLU A 1 94  ? 11.95786  25.13651  -8.53714  1.000 25.82430 ? 94  GLU A OE1   1 
ATOM   747  O  OE2   . GLU A 1 94  ? 12.77183  24.55050  -6.58313  1.000 30.63365 ? 94  GLU A OE2   1 
ATOM   748  N  N     . TRP A 1 95  ? 17.45787  26.00650  -9.19006  1.000 29.41202 ? 95  TRP A N     1 
ATOM   749  C  CA    . TRP A 1 95  ? 18.57686  25.39649  -8.48604  1.000 30.70357 ? 95  TRP A CA    1 
ATOM   750  C  C     . TRP A 1 95  ? 19.92486  25.98649  -8.88002  1.000 29.23860 ? 95  TRP A C     1 
ATOM   751  O  O     . TRP A 1 95  ? 20.94185  25.61849  -8.28300  1.000 37.43395 ? 95  TRP A O     1 
ATOM   752  C  CB    . TRP A 1 95  ? 18.58486  23.88250  -8.72805  1.000 28.04274 ? 95  TRP A CB    1 
ATOM   753  C  CG    . TRP A 1 95  ? 17.32785  23.19650  -8.27707  1.000 27.05921 ? 95  TRP A CG    1 
ATOM   754  C  CD1   . TRP A 1 95  ? 16.36684  23.70349  -7.45108  1.000 29.41809 ? 95  TRP A CD1   1 
ATOM   755  C  CD2   . TRP A 1 95  ? 16.89085  21.88050  -8.63808  1.000 29.15356 ? 95  TRP A CD2   1 
ATOM   756  N  NE1   . TRP A 1 95  ? 15.36283  22.78350  -7.27110  1.000 32.20142 ? 95  TRP A NE1   1 
ATOM   757  C  CE2   . TRP A 1 95  ? 15.66084  21.65550  -7.99010  1.000 28.03994 ? 95  TRP A CE2   1 
ATOM   758  C  CE3   . TRP A 1 95  ? 17.42286  20.86950  -9.44508  1.000 28.78714 ? 95  TRP A CE3   1 
ATOM   759  C  CZ2   . TRP A 1 95  ? 14.95384  20.46250  -8.12411  1.000 27.96681 ? 95  TRP A CZ2   1 
ATOM   760  C  CZ3   . TRP A 1 95  ? 16.71986  19.68650  -9.57609  1.000 26.15210 ? 95  TRP A CZ3   1 
ATOM   761  C  CH2   . TRP A 1 95  ? 15.49785  19.49350  -8.91911  1.000 26.47005 ? 95  TRP A CH2   1 
ATOM   762  N  N     . GLY A 1 96  ? 19.95988  26.89050  -9.85701  1.000 25.51501 ? 96  GLY A N     1 
ATOM   763  C  CA    . GLY A 1 96  ? 21.20889  27.47550  -10.30499 1.000 30.24096 ? 96  GLY A CA    1 
ATOM   764  C  C     . GLY A 1 96  ? 22.17189  26.44250  -10.85298 1.000 30.14773 ? 96  GLY A C     1 
ATOM   765  O  O     . GLY A 1 96  ? 23.29089  26.29749  -10.35297 1.000 34.17402 ? 96  GLY A O     1 
ATOM   766  N  N     . VAL A 1 97  ? 21.74791  25.72350  -11.88199 1.000 28.26272 ? 97  VAL A N     1 
ATOM   767  C  CA    . VAL A 1 97  ? 22.49092  24.58550  -12.40798 1.000 27.57373 ? 97  VAL A CA    1 
ATOM   768  C  C     . VAL A 1 97  ? 23.49493  25.06350  -13.44597 1.000 28.99531 ? 97  VAL A C     1 
ATOM   769  O  O     . VAL A 1 97  ? 23.19495  25.93451  -14.27297 1.000 27.84971 ? 97  VAL A O     1 
ATOM   770  C  CB    . VAL A 1 97  ? 21.52792  23.54151  -13.00300 1.000 28.77014 ? 97  VAL A CB    1 
ATOM   771  C  CG1   . VAL A 1 97  ? 22.27593  22.26651  -13.36200 1.000 28.90942 ? 97  VAL A CG1   1 
ATOM   772  C  CG2   . VAL A 1 97  ? 20.39791  23.25450  -12.02702 1.000 26.15372 ? 97  VAL A CG2   1 
ATOM   773  N  N     . THR A 1 98  ? 24.69893  24.49050  -13.40095 1.000 24.65386 ? 98  THR A N     1 
ATOM   774  C  CA    . THR A 1 98  ? 25.73295  24.76450  -14.38593 1.000 26.17622 ? 98  THR A CA    1 
ATOM   775  C  C     . THR A 1 98  ? 26.21095  23.52450  -15.12693 1.000 24.50000 ? 98  THR A C     1 
ATOM   776  O  O     . THR A 1 98  ? 26.97897  23.66051  -16.08592 1.000 28.08210 ? 98  THR A O     1 
ATOM   777  C  CB    . THR A 1 98  ? 26.94494  25.44450  -13.72591 1.000 25.35779 ? 98  THR A CB    1 
ATOM   778  O  OG1   . THR A 1 98  ? 27.45992  24.60449  -12.68591 1.000 26.93081 ? 98  THR A OG1   1 
ATOM   779  C  CG2   . THR A 1 98  ? 26.54993  26.79250  -13.13891 1.000 25.91154 ? 98  THR A CG2   1 
ATOM   780  N  N     . GLN A 1 99  ? 25.78795  22.32950  -14.71894 1.000 21.64081 ? 99  GLN A N     1 
ATOM   781  C  CA    . GLN A 1 99  ? 26.20995  21.09951  -15.37694 1.000 23.66083 ? 99  GLN A CA    1 
ATOM   782  C  C     . GLN A 1 99  ? 25.10095  20.06451  -15.26296 1.000 27.56825 ? 99  GLN A C     1 
ATOM   783  O  O     . GLN A 1 99  ? 24.52693  19.88350  -14.18497 1.000 20.46130 ? 99  GLN A O     1 
ATOM   784  C  CB    . GLN A 1 99  ? 27.50594  20.55850  -14.76192 1.000 20.53895 ? 99  GLN A CB    1 
ATOM   785  C  CG    . GLN A 1 99  ? 28.07695  19.34950  -15.48692 1.000 23.60619 ? 99  GLN A CG    1 
ATOM   786  C  CD    . GLN A 1 99  ? 29.29694  18.77350  -14.79290 1.000 26.75978 ? 99  GLN A CD    1 
ATOM   787  O  OE1   . GLN A 1 99  ? 29.20092  18.23549  -13.68990 1.000 24.21822 ? 99  GLN A OE1   1 
ATOM   788  N  NE2   . GLN A 1 99  ? 30.45295  18.88550  -15.43788 1.000 24.14870 ? 99  GLN A NE2   1 
ATOM   789  N  N     . LEU A 1 100 ? 24.80297  19.39351  -16.37397 1.000 23.52769 ? 100 LEU A N     1 
ATOM   790  C  CA    . LEU A 1 100 ? 23.80197  18.33451  -16.42099 1.000 24.86675 ? 100 LEU A CA    1 
ATOM   791  C  C     . LEU A 1 100 ? 24.45597  17.07251  -16.96098 1.000 27.19178 ? 100 LEU A C     1 
ATOM   792  O  O     . LEU A 1 100 ? 24.98399  17.07252  -18.07797 1.000 26.97163 ? 100 LEU A O     1 
ATOM   793  C  CB    . LEU A 1 100 ? 22.60898  18.73652  -17.29000 1.000 27.32925 ? 100 LEU A CB    1 
ATOM   794  C  CG    . LEU A 1 100 ? 21.57298  17.64252  -17.56102 1.000 27.98369 ? 100 LEU A CG    1 
ATOM   795  C  CD1   . LEU A 1 100 ? 20.94796  17.14952  -16.26403 1.000 17.02033 ? 100 LEU A CD1   1 
ATOM   796  C  CD2   . LEU A 1 100 ? 20.50300  18.14153  -18.52004 1.000 28.04332 ? 100 LEU A CD2   1 
ATOM   797  N  N     . CYS A 1 101 ? 24.42096  16.00251  -16.16999 1.000 25.23576 ? 101 CYS A N     1 
ATOM   798  C  CA    . CYS A 1 101 ? 25.03696  14.73351  -16.52998 1.000 25.73106 ? 101 CYS A CA    1 
ATOM   799  C  C     . CYS A 1 101 ? 23.97496  13.64351  -16.56100 1.000 22.32674 ? 101 CYS A C     1 
ATOM   800  O  O     . CYS A 1 101 ? 23.17694  13.52351  -15.62601 1.000 19.13781 ? 101 CYS A O     1 
ATOM   801  C  CB    . CYS A 1 101 ? 26.14694  14.35851  -15.54297 1.000 25.15641 ? 101 CYS A CB    1 
ATOM   802  S  SG    . CYS A 1 101 ? 27.52095  15.53250  -15.45994 1.000 26.46461 ? 101 CYS A SG    1 
ATOM   803  N  N     . PHE A 1 102 ? 23.96697  12.85752  -17.63500 1.000 23.05689 ? 102 PHE A N     1 
ATOM   804  C  CA    . PHE A 1 102 ? 23.08897  11.70152  -17.73202 1.000 26.04719 ? 102 PHE A CA    1 
ATOM   805  C  C     . PHE A 1 102 ? 23.72399  10.67652  -18.66102 1.000 28.68267 ? 102 PHE A C     1 
ATOM   806  O  O     . PHE A 1 102 ? 24.45600  11.02552  -19.59100 1.000 25.37719 ? 102 PHE A O     1 
ATOM   807  C  CB    . PHE A 1 102 ? 21.68398  12.08152  -18.22204 1.000 23.72127 ? 102 PHE A CB    1 
ATOM   808  C  CG    . PHE A 1 102 ? 21.66700  12.84953  -19.51504 1.000 24.31284 ? 102 PHE A CG    1 
ATOM   809  C  CD1   . PHE A 1 102 ? 21.58502  12.18953  -20.73004 1.000 28.62593 ? 102 PHE A CD1   1 
ATOM   810  C  CD2   . PHE A 1 102 ? 21.71101  14.23453  -19.51303 1.000 22.04652 ? 102 PHE A CD2   1 
ATOM   811  C  CE1   . PHE A 1 102 ? 21.56004  12.89354  -21.91904 1.000 24.52980 ? 102 PHE A CE1   1 
ATOM   812  C  CE2   . PHE A 1 102 ? 21.68802  14.94553  -20.69803 1.000 20.77853 ? 102 PHE A CE2   1 
ATOM   813  C  CZ    . PHE A 1 102 ? 21.61104  14.27454  -21.90203 1.000 28.39497 ? 102 PHE A CZ    1 
ATOM   814  N  N     . GLU A 1 103 ? 23.43798  9.40552   -18.39102 1.000 29.21580 ? 103 GLU A N     1 
ATOM   815  C  CA    . GLU A 1 103 ? 24.01999  8.32052   -19.16802 1.000 23.96173 ? 103 GLU A CA    1 
ATOM   816  C  C     . GLU A 1 103 ? 23.48401  8.33553   -20.59403 1.000 22.34365 ? 103 GLU A C     1 
ATOM   817  O  O     . GLU A 1 103 ? 22.30002  8.59653   -20.82704 1.000 22.50169 ? 103 GLU A O     1 
ATOM   818  C  CB    . GLU A 1 103 ? 23.71998  6.97752   -18.50303 1.000 17.58465 ? 103 GLU A CB    1 
ATOM   819  C  CG    . GLU A 1 103 ? 24.54098  5.81652   -19.03202 1.000 18.23636 ? 103 GLU A CG    1 
ATOM   820  C  CD    . GLU A 1 103 ? 24.15897  4.49752   -18.39103 1.000 23.39738 ? 103 GLU A CD    1 
ATOM   821  O  OE1   . GLU A 1 103 ? 22.97797  4.10552   -18.49305 1.000 22.00834 ? 103 GLU A OE1   1 
ATOM   822  O  OE2   . GLU A 1 103 ? 25.03596  3.85652   -17.77402 1.000 23.15666 ? 103 GLU A OE2   1 
ATOM   823  N  N     . HIS A 1 104 ? 24.36603  8.05353   -21.55001 1.000 22.03078 ? 104 HIS A N     1 
ATOM   824  C  CA    . HIS A 1 104 ? 23.98505  8.08954   -22.95502 1.000 17.59710 ? 104 HIS A CA    1 
ATOM   825  C  C     . HIS A 1 104 ? 23.02405  6.95454   -23.28304 1.000 24.10216 ? 104 HIS A C     1 
ATOM   826  O  O     . HIS A 1 104 ? 23.13704  5.84554   -22.75204 1.000 24.53355 ? 104 HIS A O     1 
ATOM   827  C  CB    . HIS A 1 104 ? 25.22606  8.00254   -23.84300 1.000 21.77466 ? 104 HIS A CB    1 
ATOM   828  C  CG    . HIS A 1 104 ? 24.92908  8.08654   -25.30801 1.000 22.79950 ? 104 HIS A CG    1 
ATOM   829  N  ND1   . HIS A 1 104 ? 24.42209  9.22355   -25.90101 1.000 19.92246 ? 104 HIS A ND1   1 
ATOM   830  C  CD2   . HIS A 1 104 ? 25.06610  7.17555   -26.29901 1.000 26.51085 ? 104 HIS A CD2   1 
ATOM   831  C  CE1   . HIS A 1 104 ? 24.26111  9.00955   -27.19401 1.000 26.07207 ? 104 HIS A CE1   1 
ATOM   832  N  NE2   . HIS A 1 104 ? 24.64411  7.77355   -27.46201 1.000 28.31811 ? 104 HIS A NE2   1 
ATOM   833  N  N     . ASP A 1 105 ? 22.07006  7.23954   -24.16605 1.000 22.54138 ? 105 ASP A N     1 
ATOM   834  C  CA    . ASP A 1 105 ? 21.07707  6.26755   -24.59507 1.000 22.30252 ? 105 ASP A CA    1 
ATOM   835  C  C     . ASP A 1 105 ? 20.97409  6.30155   -26.11207 1.000 24.05174 ? 105 ASP A C     1 
ATOM   836  O  O     . ASP A 1 105 ? 21.03510  7.37255   -26.72407 1.000 27.24747 ? 105 ASP A O     1 
ATOM   837  C  CB    . ASP A 1 105 ? 19.71106  6.55555   -23.95809 1.000 21.69265 ? 105 ASP A CB    1 
ATOM   838  C  CG    . ASP A 1 105 ? 18.78506  5.35255   -23.98611 1.000 30.70352 ? 105 ASP A CG    1 
ATOM   839  O  OD1   . ASP A 1 105 ? 18.88007  4.54055   -24.93211 1.000 34.42436 ? 105 ASP A OD1   1 
ATOM   840  O  OD2   . ASP A 1 105 ? 17.95904  5.21955   -23.05912 1.000 29.19664 ? 105 ASP A OD2   1 
ATOM   841  N  N     . THR A 1 106 ? 20.81510  5.12356   -26.71608 1.000 32.88584 ? 106 THR A N     1 
ATOM   842  C  CA    . THR A 1 106 ? 20.79312  4.97956   -28.16708 1.000 26.76120 ? 106 THR A CA    1 
ATOM   843  C  C     . THR A 1 106 ? 19.43813  4.48656   -28.67110 1.000 29.78981 ? 106 THR A C     1 
ATOM   844  O  O     . THR A 1 106 ? 19.35314  3.86557   -29.73211 1.000 31.18868 ? 106 THR A O     1 
ATOM   845  C  CB    . THR A 1 106 ? 21.90513  4.04056   -28.63107 1.000 22.95211 ? 106 THR A CB    1 
ATOM   846  O  OG1   . THR A 1 106 ? 21.73511  2.75556   -28.01707 1.000 27.43861 ? 106 THR A OG1   1 
ATOM   847  C  CG2   . THR A 1 106 ? 23.26612  4.60256   -28.25104 1.000 30.31251 ? 106 THR A CG2   1 
ATOM   848  N  N     . GLU A 1 107 ? 18.37412  4.75856   -27.92312 1.000 31.23253 ? 107 GLU A N     1 
ATOM   849  C  CA    . GLU A 1 107 ? 17.03812  4.35357   -28.33114 1.000 30.81707 ? 107 GLU A CA    1 
ATOM   850  C  C     . GLU A 1 107 ? 16.37314  5.44857   -29.15515 1.000 32.93507 ? 107 GLU A C     1 
ATOM   851  O  O     . GLU A 1 107 ? 16.75214  6.62157   -29.06914 1.000 37.82349 ? 107 GLU A O     1 
ATOM   852  C  CB    . GLU A 1 107 ? 16.19310  4.02257   -27.10215 1.000 30.73413 ? 107 GLU A CB    1 
ATOM   853  C  CG    . GLU A 1 107 ? 16.59209  2.72356   -26.41615 1.000 30.97298 ? 107 GLU A CG    1 
ATOM   854  C  CD    . GLU A 1 107 ? 15.62907  2.32056   -25.31717 1.000 24.13602 ? 107 GLU A CD    1 
ATOM   855  O  OE1   . GLU A 1 107 ? 14.74007  3.12956   -24.97818 1.000 30.67535 ? 107 GLU A OE1   1 
ATOM   856  O  OE2   . GLU A 1 107 ? 15.76106  1.19456   -24.79517 1.000 22.74715 ? 107 GLU A OE2   1 
ATOM   857  N  N     . PRO A 1 108 ? 15.38415  5.09158   -29.98416 1.000 32.72364 ? 108 PRO A N     1 
ATOM   858  C  CA    . PRO A 1 108 ? 14.74616  6.11558   -30.83517 1.000 32.35128 ? 108 PRO A CA    1 
ATOM   859  C  C     . PRO A 1 108 ? 14.13515  7.26758   -30.05517 1.000 31.68508 ? 108 PRO A C     1 
ATOM   860  O  O     . PRO A 1 108 ? 14.42516  8.43458   -30.35217 1.000 34.06487 ? 108 PRO A O     1 
ATOM   861  C  CB    . PRO A 1 108 ? 13.68617  5.31159   -31.60119 1.000 35.06857 ? 108 PRO A CB    1 
ATOM   862  C  CG    . PRO A 1 108 ? 14.21617  3.92058   -31.62418 1.000 34.44556 ? 108 PRO A CG    1 
ATOM   863  C  CD    . PRO A 1 108 ? 14.91515  3.73358   -30.31017 1.000 33.27810 ? 108 PRO A CD    1 
ATOM   864  N  N     . TYR A 1 109 ? 13.28814  6.97558   -29.06419 1.000 35.16673 ? 109 TYR A N     1 
ATOM   865  C  CA    . TYR A 1 109 ? 12.68813  8.04858   -28.27819 1.000 36.22384 ? 109 TYR A CA    1 
ATOM   866  C  C     . TYR A 1 109 ? 13.73012  8.80057   -27.46317 1.000 32.99032 ? 109 TYR A C     1 
ATOM   867  O  O     . TYR A 1 109 ? 13.59012  10.00857  -27.24417 1.000 37.69237 ? 109 TYR A O     1 
ATOM   868  C  CB    . TYR A 1 109 ? 11.59911  7.49057   -27.36021 1.000 41.39770 ? 109 TYR A CB    1 
ATOM   869  C  CG    . TYR A 1 109 ? 11.12210  8.47557   -26.31522 1.000 36.35237 ? 109 TYR A CG    1 
ATOM   870  C  CD1   . TYR A 1 109 ? 10.33311  9.56357   -26.66622 1.000 44.71979 ? 109 TYR A CD1   1 
ATOM   871  C  CD2   . TYR A 1 109 ? 11.46208  8.31857   -24.97721 1.000 40.14755 ? 109 TYR A CD2   1 
ATOM   872  C  CE1   . TYR A 1 109 ? 9.89709   10.46857  -25.71523 1.000 45.07316 ? 109 TYR A CE1   1 
ATOM   873  C  CE2   . TYR A 1 109 ? 11.03006  9.21656   -24.01921 1.000 40.74916 ? 109 TYR A CE2   1 
ATOM   874  C  CZ    . TYR A 1 109 ? 10.24907  10.28957  -24.39322 1.000 43.91718 ? 109 TYR A CZ    1 
ATOM   875  O  OH    . TYR A 1 109 ? 9.81706   11.18656  -23.44323 1.000 38.44495 ? 109 TYR A OH    1 
ATOM   876  N  N     . ALA A 1 110 ? 14.78211  8.11157   -27.01516 1.000 31.35621 ? 110 ALA A N     1 
ATOM   877  C  CA    . ALA A 1 110 ? 15.79910  8.76656   -26.19914 1.000 34.96767 ? 110 ALA A CA    1 
ATOM   878  C  C     . ALA A 1 110 ? 16.60411  9.77256   -27.01213 1.000 29.50604 ? 110 ALA A C     1 
ATOM   879  O  O     . ALA A 1 110 ? 16.97011  10.83756  -26.50212 1.000 30.74397 ? 110 ALA A O     1 
ATOM   880  C  CB    . ALA A 1 110 ? 16.72109  7.72056   -25.57313 1.000 32.45404 ? 110 ALA A CB    1 
ATOM   881  N  N     . LYS A 1 111 ? 16.89013  9.45757   -28.27812 1.000 34.12554 ? 111 LYS A N     1 
ATOM   882  C  CA    . LYS A 1 111 ? 17.65814  10.37957  -29.11011 1.000 36.51807 ? 111 LYS A CA    1 
ATOM   883  C  C     . LYS A 1 111 ? 16.88615  11.66657  -29.36912 1.000 31.98242 ? 111 LYS A C     1 
ATOM   884  O  O     . LYS A 1 111 ? 17.47815  12.74957  -29.43610 1.000 35.37771 ? 111 LYS A O     1 
ATOM   885  C  CB    . LYS A 1 111 ? 18.04416  9.70657   -30.42611 1.000 35.28134 ? 111 LYS A CB    1 
ATOM   886  C  CG    . LYS A 1 111 ? 19.11716  8.64057   -30.28109 1.000 34.15135 ? 111 LYS A CG    1 
ATOM   887  C  CD    . LYS A 1 111 ? 19.39018  7.93858   -31.60009 1.000 29.78110 ? 111 LYS A CD    1 
ATOM   888  C  CE    . LYS A 1 111 ? 20.41617  6.83057   -31.42508 1.000 24.87469 ? 111 LYS A CE    1 
ATOM   889  N  NZ    . LYS A 1 111 ? 20.60319  6.03658   -32.67008 1.000 21.33077 ? 111 LYS A NZ    1 
ATOM   890  N  N     . VAL A 1 112 ? 15.56415  11.57257  -29.51714 1.000 34.76379 ? 112 VAL A N     1 
ATOM   891  C  CA    . VAL A 1 112 ? 14.75016  12.77058  -29.69214 1.000 28.45469 ? 112 VAL A CA    1 
ATOM   892  C  C     . VAL A 1 112 ? 14.54514  13.47657  -28.35815 1.000 29.49416 ? 112 VAL A C     1 
ATOM   893  O  O     . VAL A 1 112 ? 14.55714  14.71157  -28.28914 1.000 30.33568 ? 112 VAL A O     1 
ATOM   894  C  CB    . VAL A 1 112 ? 13.41017  12.41058  -30.36017 1.000 33.47023 ? 112 VAL A CB    1 
ATOM   895  C  CG1   . VAL A 1 112 ? 12.55417  13.65358  -30.55018 1.000 22.98105 ? 112 VAL A CG1   1 
ATOM   896  C  CG2   . VAL A 1 112 ? 13.65219  11.71559  -31.69317 1.000 24.29956 ? 112 VAL A CG2   1 
ATOM   897  N  N     . ARG A 1 113 ? 14.36353  12.70890  -27.28055 1.000 31.38001 ? 113 ARG A N     1 
ATOM   898  C  CA    . ARG A 1 113 ? 14.16533  13.30409  -25.96196 1.000 30.96070 ? 113 ARG A CA    1 
ATOM   899  C  C     . ARG A 1 113 ? 15.41343  14.04407  -25.49637 1.000 28.49806 ? 113 ARG A C     1 
ATOM   900  O  O     . ARG A 1 113 ? 15.32809  15.17102  -24.99547 1.000 27.01077 ? 113 ARG A O     1 
ATOM   901  C  CB    . ARG A 1 113 ? 13.77676  12.22313  -24.95262 1.000 31.07010 ? 113 ARG A CB    1 
ATOM   902  C  CG    . ARG A 1 113 ? 13.68534  12.71380  -23.51688 1.000 31.77224 ? 113 ARG A CG    1 
ATOM   903  C  CD    . ARG A 1 113 ? 13.64818  11.54882  -22.54049 1.000 30.95956 ? 113 ARG A CD    1 
ATOM   904  N  NE    . ARG A 1 113 ? 14.82765  10.70033  -22.66692 1.000 32.77239 ? 113 ARG A NE    1 
ATOM   905  C  CZ    . ARG A 1 113 ? 15.07185  9.63627   -21.91415 1.000 25.29843 ? 113 ARG A CZ    1 
ATOM   906  N  NH1   . ARG A 1 113 ? 14.23628  9.25665   -20.96132 1.000 28.50443 ? 113 ARG A NH1   1 
ATOM   907  N  NH2   . ARG A 1 113 ? 16.18301  8.93587   -22.12205 1.000 27.36337 ? 113 ARG A NH2   1 
ATOM   908  N  N     . ASP A 1 114 ? 16.58510  13.42256  -25.65011 1.000 28.46432 ? 114 ASP A N     1 
ATOM   909  C  CA    . ASP A 1 114 ? 17.81909  14.05756  -25.20109 1.000 28.89490 ? 114 ASP A CA    1 
ATOM   910  C  C     . ASP A 1 114 ? 18.16011  15.27356  -26.05508 1.000 32.89037 ? 114 ASP A C     1 
ATOM   911  O  O     . ASP A 1 114 ? 18.63210  16.28956  -25.53107 1.000 32.98659 ? 114 ASP A O     1 
ATOM   912  C  CB    . ASP A 1 114 ? 18.96709  13.04755  -25.21608 1.000 34.09736 ? 114 ASP A CB    1 
ATOM   913  C  CG    . ASP A 1 114 ? 18.74307  11.89655  -24.25209 1.000 30.63216 ? 114 ASP A CG    1 
ATOM   914  O  OD1   . ASP A 1 114 ? 17.72206  11.91155  -23.53210 1.000 26.40869 ? 114 ASP A OD1   1 
ATOM   915  O  OD2   . ASP A 1 114 ? 19.58607  10.97555  -24.21708 1.000 26.61366 ? 114 ASP A OD2   1 
ATOM   916  N  N     . ALA A 1 115 ? 17.92513  15.19156  -27.36809 1.000 31.80956 ? 115 ALA A N     1 
ATOM   917  C  CA    . ALA A 1 115 ? 18.18914  16.33357  -28.23808 1.000 29.94820 ? 115 ALA A CA    1 
ATOM   918  C  C     . ALA A 1 115 ? 17.32914  17.53257  -27.86209 1.000 29.92254 ? 115 ALA A C     1 
ATOM   919  O  O     . ALA A 1 115 ? 17.73014  18.67957  -28.09108 1.000 41.87638 ? 115 ALA A O     1 
ATOM   920  C  CB    . ALA A 1 115 ? 17.95716  15.95057  -29.70008 1.000 28.84186 ? 115 ALA A CB    1 
ATOM   921  N  N     . ALA A 1 116 ? 16.14913  17.28957  -27.29011 1.000 28.58827 ? 116 ALA A N     1 
ATOM   922  C  CA    . ALA A 1 116 ? 15.33112  18.39157  -26.79812 1.000 32.54871 ? 116 ALA A CA    1 
ATOM   923  C  C     . ALA A 1 116 ? 15.91111  18.97256  -25.51511 1.000 32.68931 ? 116 ALA A C     1 
ATOM   924  O  O     . ALA A 1 116 ? 15.87510  20.19056  -25.30710 1.000 31.41062 ? 116 ALA A O     1 
ATOM   925  C  CB    . ALA A 1 116 ? 13.89412  17.92057  -26.57714 1.000 31.15909 ? 116 ALA A CB    1 
ATOM   926  N  N     . VAL A 1 117 ? 16.45509  18.11656  -24.64610 1.000 29.86231 ? 117 VAL A N     1 
ATOM   927  C  CA    . VAL A 1 117 ? 17.04607  18.59655  -23.40109 1.000 36.42740 ? 117 VAL A CA    1 
ATOM   928  C  C     . VAL A 1 117 ? 18.34708  19.34155  -23.67807 1.000 34.09488 ? 117 VAL A C     1 
ATOM   929  O  O     . VAL A 1 117 ? 18.67307  20.32255  -22.99806 1.000 36.37441 ? 117 VAL A O     1 
ATOM   930  C  CB    . VAL A 1 117 ? 17.25806  17.42355  -22.42609 1.000 31.41618 ? 117 VAL A CB    1 
ATOM   931  C  CG1   . VAL A 1 117 ? 17.84604  17.91554  -21.11308 1.000 25.41429 ? 117 VAL A CG1   1 
ATOM   932  C  CG2   . VAL A 1 117 ? 15.94705  16.69255  -22.18311 1.000 31.35434 ? 117 VAL A CG2   1 
ATOM   933  N  N     . ARG A 1 118 ? 19.10838  18.90041  -24.68382 1.000 30.62059 ? 118 ARG A N     1 
ATOM   934  C  CA    . ARG A 1 118 ? 20.35325  19.58316  -25.02585 1.000 37.65362 ? 118 ARG A CA    1 
ATOM   935  C  C     . ARG A 1 118 ? 20.09439  21.01770  -25.46866 1.000 36.63962 ? 118 ARG A C     1 
ATOM   936  O  O     . ARG A 1 118 ? 20.86146  21.92768  -25.13239 1.000 33.25230 ? 118 ARG A O     1 
ATOM   937  C  CB    . ARG A 1 118 ? 21.09321  18.81408  -26.12027 1.000 38.50921 ? 118 ARG A CB    1 
ATOM   938  C  CG    . ARG A 1 118 ? 21.57988  17.43874  -25.70169 1.000 32.61702 ? 118 ARG A CG    1 
ATOM   939  C  CD    . ARG A 1 118 ? 22.22822  16.71338  -26.86898 1.000 47.43127 ? 118 ARG A CD    1 
ATOM   940  N  NE    . ARG A 1 118 ? 22.62925  15.35696  -26.51679 1.000 36.67186 ? 118 ARG A NE    1 
ATOM   941  C  CZ    . ARG A 1 118 ? 23.80834  15.03493  -26.00363 1.000 35.46092 ? 118 ARG A CZ    1 
ATOM   942  N  NH1   . ARG A 1 118 ? 24.73120  15.95193  -25.76363 1.000 37.83596 ? 118 ARG A NH1   1 
ATOM   943  N  NH2   . ARG A 1 118 ? 24.06823  13.76096  -25.72472 1.000 40.24224 ? 118 ARG A NH2   1 
ATOM   944  N  N     . ARG A 1 119 ? 19.01792  21.23979  -26.22613 1.000 36.55624 ? 119 ARG A N     1 
ATOM   945  C  CA    . ARG A 1 119 ? 18.67755  22.59029  -26.65535 1.000 32.81171 ? 119 ARG A CA    1 
ATOM   946  C  C     . ARG A 1 119 ? 18.14334  23.44360  -25.51283 1.000 30.70262 ? 119 ARG A C     1 
ATOM   947  O  O     . ARG A 1 119 ? 18.18902  24.67462  -25.60318 1.000 38.48655 ? 119 ARG A O     1 
ATOM   948  C  CB    . ARG A 1 119 ? 17.65989  22.53819  -27.79658 1.000 38.73789 ? 119 ARG A CB    1 
ATOM   949  C  CG    . ARG A 1 119 ? 18.25941  22.12351  -29.13223 0.000 35.19228 ? 119 ARG A CG    1 
ATOM   950  C  CD    . ARG A 1 119 ? 17.21580  22.09306  -30.23876 0.000 34.56182 ? 119 ARG A CD    1 
ATOM   951  N  NE    . ARG A 1 119 ? 16.60578  20.77720  -30.39025 0.000 33.84382 ? 119 ARG A NE    1 
ATOM   952  C  CZ    . ARG A 1 119 ? 15.47615  20.39967  -29.80758 0.000 33.23517 ? 119 ARG A CZ    1 
ATOM   953  N  NH1   . ARG A 1 119 ? 14.80161  21.21470  -29.01331 0.000 33.13284 ? 119 ARG A NH1   1 
ATOM   954  N  NH2   . ARG A 1 119 ? 15.00999  19.17400  -30.02995 0.000 32.69160 ? 119 ARG A NH2   1 
ATOM   955  N  N     . LEU A 1 120 ? 17.64310  22.82255  -24.44306 1.000 37.10781 ? 120 LEU A N     1 
ATOM   956  C  CA    . LEU A 1 120 ? 17.17608  23.58555  -23.29107 1.000 34.15932 ? 120 LEU A CA    1 
ATOM   957  C  C     . LEU A 1 120 ? 18.33007  23.96954  -22.37105 1.000 30.83681 ? 120 LEU A C     1 
ATOM   958  O  O     . LEU A 1 120 ? 18.33806  25.07054  -21.81005 1.000 37.31589 ? 120 LEU A O     1 
ATOM   959  C  CB    . LEU A 1 120 ? 16.12407  22.78755  -22.52309 1.000 31.86876 ? 120 LEU A CB    1 
ATOM   960  C  CG    . LEU A 1 120 ? 14.83208  22.48155  -23.28411 1.000 35.30450 ? 120 LEU A CG    1 
ATOM   961  C  CD1   . LEU A 1 120 ? 13.89706  21.62355  -22.44613 1.000 41.36463 ? 120 LEU A CD1   1 
ATOM   962  C  CD2   . LEU A 1 120 ? 14.14609  23.76956  -23.71211 1.000 37.62775 ? 120 LEU A CD2   1 
ATOM   963  N  N     . ALA A 1 121 ? 19.30806  23.07654  -22.20404 1.000 31.28937 ? 121 ALA A N     1 
ATOM   964  C  CA    . ALA A 1 121 ? 20.45805  23.39354  -21.36402 1.000 29.78035 ? 121 ALA A CA    1 
ATOM   965  C  C     . ALA A 1 121 ? 21.35806  24.43554  -22.01500 1.000 32.92097 ? 121 ALA A C     1 
ATOM   966  O  O     . ALA A 1 121 ? 22.05405  25.17653  -21.31199 1.000 33.48825 ? 121 ALA A O     1 
ATOM   967  C  CB    . ALA A 1 121 ? 21.25004  22.12453  -21.05201 1.000 23.38960 ? 121 ALA A CB    1 
ATOM   968  N  N     . ALA A 1 122 ? 21.36108  24.50554  -23.34900 1.000 26.07433 ? 122 ALA A N     1 
ATOM   969  C  CA    . ALA A 1 122 ? 22.15109  25.52554  -24.02999 1.000 36.67059 ? 122 ALA A CA    1 
ATOM   970  C  C     . ALA A 1 122 ? 21.56109  26.91254  -23.81399 1.000 35.33619 ? 122 ALA A C     1 
ATOM   971  O  O     . ALA A 1 122 ? 22.30109  27.89054  -23.65398 1.000 34.36177 ? 122 ALA A O     1 
ATOM   972  C  CB    . ALA A 1 122 ? 22.24712  25.20755  -25.52199 1.000 30.33340 ? 122 ALA A CB    1 
ATOM   973  N  N     . GLU A 1 123 ? 20.23009  27.01855  -23.81001 1.000 38.81525 ? 123 GLU A N     1 
ATOM   974  C  CA    . GLU A 1 123 ? 19.59009  28.30355  -23.55102 1.000 36.59637 ? 123 GLU A CA    1 
ATOM   975  C  C     . GLU A 1 123 ? 19.80607  28.75654  -22.11401 1.000 32.93898 ? 123 GLU A C     1 
ATOM   976  O  O     . GLU A 1 123 ? 19.87607  29.96254  -21.84801 1.000 31.50792 ? 123 GLU A O     1 
ATOM   977  C  CB    . GLU A 1 123 ? 18.09610  28.21355  -23.86204 1.000 36.90499 ? 123 GLU A CB    1 
ATOM   978  C  CG    . GLU A 1 123 ? 17.78312  27.85156  -25.30704 1.000 41.55257 ? 123 GLU A CG    1 
ATOM   979  C  CD    . GLU A 1 123 ? 16.32312  27.49956  -25.51907 1.000 44.75640 ? 123 GLU A CD    1 
ATOM   980  O  OE1   . GLU A 1 123 ? 15.57211  27.44456  -24.52308 1.000 38.22542 ? 123 GLU A OE1   1 
ATOM   981  O  OE2   . GLU A 1 123 ? 15.92714  27.27456  -26.68208 1.000 42.48425 ? 123 GLU A OE2   1 
ATOM   982  N  N     . ALA A 1 124 ? 19.91706  27.81254  -21.18101 1.000 38.28345 ? 124 ALA A N     1 
ATOM   983  C  CA    . ALA A 1 124 ? 20.13103  28.11653  -19.77401 1.000 33.66162 ? 124 ALA A CA    1 
ATOM   984  C  C     . ALA A 1 124 ? 21.60303  28.24753  -19.40499 1.000 36.52810 ? 124 ALA A C     1 
ATOM   985  O  O     . ALA A 1 124 ? 21.91001  28.76252  -18.32398 1.000 39.79085 ? 124 ALA A O     1 
ATOM   986  C  CB    . ALA A 1 124 ? 19.48802  27.03653  -18.89902 1.000 31.30706 ? 124 ALA A CB    1 
ATOM   987  N  N     . GLY A 1 125 ? 22.51004  27.79953  -20.26597 1.000 37.93502 ? 125 GLY A N     1 
ATOM   988  C  CA    . GLY A 1 125 ? 23.92604  27.86253  -19.95895 1.000 33.69055 ? 125 GLY A CA    1 
ATOM   989  C  C     . GLY A 1 125 ? 24.42502  26.71352  -19.11095 1.000 36.94211 ? 125 GLY A C     1 
ATOM   990  O  O     . GLY A 1 125 ? 25.29601  26.91152  -18.25393 1.000 39.58285 ? 125 GLY A O     1 
ATOM   991  N  N     . VAL A 1 126 ? 23.89802  25.51252  -19.32996 1.000 31.81706 ? 126 VAL A N     1 
ATOM   992  C  CA    . VAL A 1 126 ? 24.23601  24.33252  -18.54296 1.000 26.29081 ? 126 VAL A CA    1 
ATOM   993  C  C     . VAL A 1 126 ? 25.08502  23.40652  -19.40195 1.000 25.25882 ? 126 VAL A C     1 
ATOM   994  O  O     . VAL A 1 126 ? 24.70204  23.07153  -20.52996 1.000 36.27178 ? 126 VAL A O     1 
ATOM   995  C  CB    . VAL A 1 126 ? 22.97100  23.61652  -18.03998 1.000 31.63007 ? 126 VAL A CB    1 
ATOM   996  C  CG1   . VAL A 1 126 ? 23.33599  22.35752  -17.27698 1.000 29.20551 ? 126 VAL A CG1   1 
ATOM   997  C  CG2   . VAL A 1 126 ? 22.14299  24.55152  -17.17099 1.000 29.91897 ? 126 VAL A CG2   1 
ATOM   998  N  N     . GLU A 1 127 ? 26.23401  22.99652  -18.87093 1.000 26.33479 ? 127 GLU A N     1 
ATOM   999  C  CA    . GLU A 1 127 ? 27.12402  22.08852  -19.58292 1.000 26.28139 ? 127 GLU A CA    1 
ATOM   1000 C  C     . GLU A 1 127 ? 26.57402  20.66852  -19.52694 1.000 20.01138 ? 127 GLU A C     1 
ATOM   1001 O  O     . GLU A 1 127 ? 26.22600  20.16952  -18.45294 1.000 19.58988 ? 127 GLU A O     1 
ATOM   1002 C  CB    . GLU A 1 127 ? 28.52701  22.13751  -18.97990 1.000 25.43186 ? 127 GLU A CB    1 
ATOM   1003 C  CG    . GLU A 1 127 ? 29.49602  21.13451  -19.58089 1.000 34.27962 ? 127 GLU A CG    1 
ATOM   1004 C  CD    . GLU A 1 127 ? 30.84401  21.14151  -18.88687 1.000 41.77938 ? 127 GLU A CD    1 
ATOM   1005 O  OE1   . GLU A 1 127 ? 31.05800  22.00151  -18.00686 1.000 33.90072 ? 127 GLU A OE1   1 
ATOM   1006 O  OE2   . GLU A 1 127 ? 31.68901  20.28351  -19.21986 1.000 53.69957 ? 127 GLU A OE2   1 
ATOM   1007 N  N     . VAL A 1 128 ? 26.50003  20.01652  -20.68494 1.000 24.52449 ? 128 VAL A N     1 
ATOM   1008 C  CA    . VAL A 1 128 ? 25.95003  18.67052  -20.79695 1.000 20.48055 ? 128 VAL A CA    1 
ATOM   1009 C  C     . VAL A 1 128 ? 27.09703  17.68252  -20.94794 1.000 23.26580 ? 128 VAL A C     1 
ATOM   1010 O  O     . VAL A 1 128 ? 27.93505  17.82253  -21.84793 1.000 23.46177 ? 128 VAL A O     1 
ATOM   1011 C  CB    . VAL A 1 128 ? 24.97405  18.56553  -21.98097 1.000 20.65873 ? 128 VAL A CB    1 
ATOM   1012 C  CG1   . VAL A 1 128 ? 24.39105  17.16353  -22.06198 1.000 32.32659 ? 128 VAL A CG1   1 
ATOM   1013 C  CG2   . VAL A 1 128 ? 23.86805  19.59953  -21.84698 1.000 23.62823 ? 128 VAL A CG2   1 
ATOM   1014 N  N     . VAL A 1 129 ? 27.13902  16.68552  -20.06694 1.000 27.27108 ? 129 VAL A N     1 
ATOM   1015 C  CA    . VAL A 1 129 ? 28.14702  15.62952  -20.09793 1.000 21.78877 ? 129 VAL A CA    1 
ATOM   1016 C  C     . VAL A 1 129 ? 27.41902  14.29652  -20.19495 1.000 23.81652 ? 129 VAL A C     1 
ATOM   1017 O  O     . VAL A 1 129 ? 26.64400  13.94052  -19.29896 1.000 19.85666 ? 129 VAL A O     1 
ATOM   1018 C  CB    . VAL A 1 129 ? 29.05600  15.66851  -18.85992 1.000 24.01035 ? 129 VAL A CB    1 
ATOM   1019 C  CG1   . VAL A 1 129 ? 30.15000  14.61851  -18.97290 1.000 24.23596 ? 129 VAL A CG1   1 
ATOM   1020 C  CG2   . VAL A 1 129 ? 29.65500  17.05651  -18.68090 1.000 30.88583 ? 129 VAL A CG2   1 
ATOM   1021 N  N     . THR A 1 130 ? 27.66803  13.56052  -21.27894 1.000 23.28388 ? 130 THR A N     1 
ATOM   1022 C  CA    . THR A 1 130 ? 26.96303  12.31153  -21.56896 1.000 20.51857 ? 130 THR A CA    1 
ATOM   1023 C  C     . THR A 1 130 ? 27.96703  11.19152  -21.80895 1.000 20.28095 ? 130 THR A C     1 
ATOM   1024 O  O     . THR A 1 130 ? 28.39305  10.95753  -22.94794 1.000 18.73016 ? 130 THR A O     1 
ATOM   1025 C  CB    . THR A 1 130 ? 26.04105  12.46953  -22.77497 1.000 21.00019 ? 130 THR A CB    1 
ATOM   1026 O  OG1   . THR A 1 130 ? 26.81307  12.84753  -23.92096 1.000 26.83686 ? 130 THR A OG1   1 
ATOM   1027 C  CG2   . THR A 1 130 ? 24.99305  13.53453  -22.50399 1.000 23.04548 ? 130 THR A CG2   1 
ATOM   1028 N  N     . PRO A 1 131 ? 28.36302  10.47452  -20.76195 1.000 19.89869 ? 131 PRO A N     1 
ATOM   1029 C  CA    . PRO A 1 131 ? 29.26102  9.33252   -20.93494 1.000 20.03815 ? 131 PRO A CA    1 
ATOM   1030 C  C     . PRO A 1 131 ? 28.50302  8.04752   -21.24495 1.000 18.67439 ? 131 PRO A C     1 
ATOM   1031 O  O     . PRO A 1 131 ? 27.31102  7.90452   -20.96297 1.000 19.30703 ? 131 PRO A O     1 
ATOM   1032 C  CB    . PRO A 1 131 ? 29.95600  9.23851   -19.56993 1.000 17.21849 ? 131 PRO A CB    1 
ATOM   1033 C  CG    . PRO A 1 131 ? 28.91498  9.71051   -18.61494 1.000 16.85551 ? 131 PRO A CG    1 
ATOM   1034 C  CD    . PRO A 1 131 ? 28.11200  10.76752  -19.33995 1.000 17.97593 ? 131 PRO A CD    1 
ATOM   1035 N  N     . ILE A 1 132 ? 29.22803  7.10552   -21.83794 1.000 20.29302 ? 132 ILE A N     1 
ATOM   1036 C  CA    . ILE A 1 132 ? 28.68303  5.79452   -22.16996 1.000 20.23047 ? 132 ILE A CA    1 
ATOM   1037 C  C     . ILE A 1 132 ? 29.01201  4.83252   -21.03696 1.000 18.71318 ? 132 ILE A C     1 
ATOM   1038 O  O     . ILE A 1 132 ? 30.16000  4.76652   -20.57994 1.000 17.57292 ? 132 ILE A O     1 
ATOM   1039 C  CB    . ILE A 1 132 ? 29.24505  5.28653   -23.50995 1.000 19.37903 ? 132 ILE A CB    1 
ATOM   1040 C  CG1   . ILE A 1 132 ? 28.76407  6.16053   -24.67395 1.000 17.69011 ? 132 ILE A CG1   1 
ATOM   1041 C  CG2   . ILE A 1 132 ? 28.84805  3.83653   -23.74196 1.000 17.22966 ? 132 ILE A CG2   1 
ATOM   1042 C  CD1   . ILE A 1 132 ? 29.68208  7.31953   -25.00894 0.000 20.50242 ? 132 ILE A CD1   1 
ATOM   1043 N  N     . SER A 1 133 ? 28.00500  4.08852   -20.57597 1.000 17.73366 ? 133 SER A N     1 
ATOM   1044 C  CA    . SER A 1 133 ? 28.20698  3.12752   -19.49797 1.000 23.14422 ? 133 SER A CA    1 
ATOM   1045 C  C     . SER A 1 133 ? 27.14198  2.03652   -19.50699 1.000 20.28498 ? 133 SER A C     1 
ATOM   1046 O  O     . SER A 1 133 ? 27.28997  1.01552   -18.82800 1.000 18.99910 ? 133 SER A O     1 
ATOM   1047 C  CB    . SER A 1 133 ? 28.23197  3.84451   -18.14597 1.000 24.07631 ? 133 SER A CB    1 
ATOM   1048 O  OG    . SER A 1 133 ? 27.52797  5.07251   -18.20398 1.000 22.21502 ? 133 SER A OG    1 
ATOM   1049 N  N     . HIS A 1 134 ? 26.06600  2.23852   -20.27301 1.000 21.51215 ? 134 HIS A N     1 
ATOM   1050 C  CA    . HIS A 1 134 ? 25.05200  1.19553   -20.40003 1.000 16.72817 ? 134 HIS A CA    1 
ATOM   1051 C  C     . HIS A 1 134 ? 25.54901  0.03453   -21.25203 1.000 21.58828 ? 134 HIS A C     1 
ATOM   1052 O  O     . HIS A 1 134 ? 25.09400  -1.10147  -21.07704 1.000 17.91709 ? 134 HIS A O     1 
ATOM   1053 C  CB    . HIS A 1 134 ? 23.76701  1.77653   -20.99405 1.000 20.50273 ? 134 HIS A CB    1 
ATOM   1054 C  CG    . HIS A 1 134 ? 22.67801  0.76653   -21.18807 1.000 16.17046 ? 134 HIS A CG    1 
ATOM   1055 N  ND1   . HIS A 1 134 ? 21.96799  0.22453   -20.13808 1.000 21.86705 ? 134 HIS A ND1   1 
ATOM   1056 C  CD2   . HIS A 1 134 ? 22.17602  0.20154   -22.31208 1.000 20.11112 ? 134 HIS A CD2   1 
ATOM   1057 C  CE1   . HIS A 1 134 ? 21.07600  -0.63047  -20.60610 1.000 16.32238 ? 134 HIS A CE1   1 
ATOM   1058 N  NE2   . HIS A 1 134 ? 21.18202  -0.66446  -21.92209 1.000 16.51591 ? 134 HIS A NE2   1 
ATOM   1059 N  N     . THR A 1 135 ? 26.47302  0.29753   -22.16901 1.000 18.03760 ? 135 THR A N     1 
ATOM   1060 C  CA    . THR A 1 135 ? 27.04003  -0.71947  -23.04001 1.000 19.79195 ? 135 THR A CA    1 
ATOM   1061 C  C     . THR A 1 135 ? 28.50303  -0.95647  -22.68698 1.000 20.88132 ? 135 THR A C     1 
ATOM   1062 O  O     . THR A 1 135 ? 29.10802  -0.22448  -21.89797 1.000 20.86054 ? 135 THR A O     1 
ATOM   1063 C  CB    . THR A 1 135 ? 26.90706  -0.31146  -24.51301 1.000 17.05056 ? 135 THR A CB    1 
ATOM   1064 O  OG1   . THR A 1 135 ? 27.60806  0.91754   -24.73799 1.000 17.54114 ? 135 THR A OG1   1 
ATOM   1065 C  CG2   . THR A 1 135 ? 25.44406  -0.12946  -24.88503 1.000 17.53608 ? 135 THR A CG2   1 
ATOM   1066 N  N     . LEU A 1 136 ? 29.07203  -2.00247  -23.28698 1.000 24.49073 ? 136 LEU A N     1 
ATOM   1067 C  CA    . LEU A 1 136 ? 30.47703  -2.31748  -23.04896 1.000 18.70553 ? 136 LEU A CA    1 
ATOM   1068 C  C     . LEU A 1 136 ? 31.38904  -1.34047  -23.77894 1.000 21.03963 ? 136 LEU A C     1 
ATOM   1069 O  O     . LEU A 1 136 ? 32.33503  -0.80048  -23.19292 1.000 21.79859 ? 136 LEU A O     1 
ATOM   1070 C  CB    . LEU A 1 136 ? 30.77303  -3.75547  -23.47796 1.000 25.23917 ? 136 LEU A CB    1 
ATOM   1071 C  CG    . LEU A 1 136 ? 30.20602  -4.86748  -22.59597 1.000 22.39268 ? 136 LEU A CG    1 
ATOM   1072 C  CD1   . LEU A 1 136 ? 30.49802  -6.23147  -23.19897 1.000 24.88365 ? 136 LEU A CD1   1 
ATOM   1073 C  CD2   . LEU A 1 136 ? 30.78000  -4.77148  -21.19296 1.000 19.49993 ? 136 LEU A CD2   1 
ATOM   1074 N  N     . TYR A 1 137 ? 31.12406  -1.10147  -25.05694 1.000 23.97302 ? 137 TYR A N     1 
ATOM   1075 C  CA    . TYR A 1 137 ? 31.93008  -0.21247  -25.87993 1.000 26.28395 ? 137 TYR A CA    1 
ATOM   1076 C  C     . TYR A 1 137 ? 31.10509  0.99754   -26.30194 1.000 24.86061 ? 137 TYR A C     1 
ATOM   1077 O  O     . TYR A 1 137 ? 29.91008  1.10154   -26.01396 1.000 26.02539 ? 137 TYR A O     1 
ATOM   1078 C  CB    . TYR A 1 137 ? 32.46409  -0.94046  -27.11692 1.000 26.70402 ? 137 TYR A CB    1 
ATOM   1079 C  CG    . TYR A 1 137 ? 33.37909  -2.10747  -26.82591 1.000 26.00076 ? 137 TYR A CG    1 
ATOM   1080 C  CD1   . TYR A 1 137 ? 34.71908  -1.90547  -26.52789 1.000 26.39835 ? 137 TYR A CD1   1 
ATOM   1081 C  CD2   . TYR A 1 137 ? 32.90709  -3.41147  -26.87093 1.000 27.62773 ? 137 TYR A CD2   1 
ATOM   1082 C  CE1   . TYR A 1 137 ? 35.56208  -2.96947  -26.27188 1.000 25.25418 ? 137 TYR A CE1   1 
ATOM   1083 C  CE2   . TYR A 1 137 ? 33.74208  -4.48147  -26.61492 1.000 26.37947 ? 137 TYR A CE2   1 
ATOM   1084 C  CZ    . TYR A 1 137 ? 35.06808  -4.25447  -26.31590 1.000 29.40073 ? 137 TYR A CZ    1 
ATOM   1085 O  OH    . TYR A 1 137 ? 35.90507  -5.31747  -26.06089 1.000 30.17601 ? 137 TYR A OH    1 
ATOM   1086 N  N     . ASP A 1 138 ? 31.76810  1.92154   -26.99092 1.000 18.81169 ? 138 ASP A N     1 
ATOM   1087 C  CA    . ASP A 1 138 ? 31.08611  3.00154   -27.69193 1.000 27.11582 ? 138 ASP A CA    1 
ATOM   1088 C  C     . ASP A 1 138 ? 30.56513  2.43855   -29.00794 1.000 29.88343 ? 138 ASP A C     1 
ATOM   1089 O  O     . ASP A 1 138 ? 31.34614  2.16255   -29.92493 1.000 31.48364 ? 138 ASP A O     1 
ATOM   1090 C  CB    . ASP A 1 138 ? 32.03812  4.17354   -27.91791 1.000 27.87983 ? 138 ASP A CB    1 
ATOM   1091 C  CG    . ASP A 1 138 ? 31.34713  5.38654   -28.51492 1.000 26.96571 ? 138 ASP A CG    1 
ATOM   1092 O  OD1   . ASP A 1 138 ? 30.10613  5.36355   -28.65894 1.000 31.97079 ? 138 ASP A OD1   1 
ATOM   1093 O  OD2   . ASP A 1 138 ? 32.04913  6.36754   -28.83990 1.000 21.87476 ? 138 ASP A OD2   1 
ATOM   1094 N  N     . THR A 1 139 ? 29.24513  2.24855   -29.09796 1.000 29.73820 ? 139 THR A N     1 
ATOM   1095 C  CA    . THR A 1 139 ? 28.66915  1.58955   -30.26797 1.000 25.20437 ? 139 THR A CA    1 
ATOM   1096 C  C     . THR A 1 139 ? 28.94117  2.36456   -31.54897 1.000 34.76826 ? 139 THR A C     1 
ATOM   1097 O  O     . THR A 1 139 ? 29.12818  1.75756   -32.61096 1.000 31.18833 ? 139 THR A O     1 
ATOM   1098 C  CB    . THR A 1 139 ? 27.16514  1.39256   -30.07600 1.000 29.17821 ? 139 THR A CB    1 
ATOM   1099 O  OG1   . THR A 1 139 ? 26.56114  2.63656   -29.69800 1.000 39.87349 ? 139 THR A OG1   1 
ATOM   1100 C  CG2   . THR A 1 139 ? 26.89713  0.35155   -28.99900 1.000 25.94940 ? 139 THR A CG2   1 
ATOM   1101 N  N     . ASP A 1 140 ? 28.97117  3.69756   -31.47696 1.000 34.67029 ? 140 ASP A N     1 
ATOM   1102 C  CA    . ASP A 1 140 ? 29.31519  4.48456   -32.65595 1.000 32.62316 ? 140 ASP A CA    1 
ATOM   1103 C  C     . ASP A 1 140 ? 30.77919  4.30656   -33.03893 1.000 34.50360 ? 140 ASP A C     1 
ATOM   1104 O  O     . ASP A 1 140 ? 31.12421  4.40556   -34.22092 1.000 31.79180 ? 140 ASP A O     1 
ATOM   1105 C  CB    . ASP A 1 140 ? 28.99819  5.96056   -32.41495 1.000 34.56883 ? 140 ASP A CB    1 
ATOM   1106 C  CG    . ASP A 1 140 ? 27.51019  6.21756   -32.26697 1.000 39.79848 ? 140 ASP A CG    1 
ATOM   1107 O  OD1   . ASP A 1 140 ? 26.71219  5.43157   -32.81699 1.000 41.43385 ? 140 ASP A OD1   1 
ATOM   1108 O  OD2   . ASP A 1 140 ? 27.13918  7.20856   -31.60398 1.000 35.34897 ? 140 ASP A OD2   1 
ATOM   1109 N  N     . MET A 1 141 ? 31.64718  4.04055   -32.05992 1.000 33.41544 ? 141 MET A N     1 
ATOM   1110 C  CA    . MET A 1 141 ? 33.05018  3.77855   -32.36490 1.000 33.51914 ? 141 MET A CA    1 
ATOM   1111 C  C     . MET A 1 141 ? 33.21319  2.46156   -33.11290 1.000 33.63830 ? 141 MET A C     1 
ATOM   1112 O  O     . MET A 1 141 ? 34.05621  2.35056   -34.01089 1.000 35.62614 ? 141 MET A O     1 
ATOM   1113 C  CB    . MET A 1 141 ? 33.87216  3.77955   -31.07389 1.000 30.01712 ? 141 MET A CB    1 
ATOM   1114 C  CG    . MET A 1 141 ? 35.30116  3.27355   -31.21587 1.000 36.80686 ? 141 MET A CG    1 
ATOM   1115 S  SD    . MET A 1 141 ? 35.47216  1.51054   -30.86587 1.000 35.67996 ? 141 MET A SD    1 
ATOM   1116 C  CE    . MET A 1 141 ? 34.88013  1.44254   -29.17688 1.000 28.25785 ? 141 MET A CE    1 
ATOM   1117 N  N     . LEU A 1 142 ? 32.40818  1.45456   -32.76292 1.000 29.53654 ? 142 LEU A N     1 
ATOM   1118 C  CA    . LEU A 1 142 ? 32.50119  0.16056   -33.43192 1.000 32.98257 ? 142 LEU A CA    1 
ATOM   1119 C  C     . LEU A 1 142 ? 32.11922  0.26556   -34.90292 1.000 34.46600 ? 142 LEU A C     1 
ATOM   1120 O  O     . LEU A 1 142 ? 32.71823  -0.40243  -35.75492 1.000 34.94655 ? 142 LEU A O     1 
ATOM   1121 C  CB    . LEU A 1 142 ? 31.61218  -0.85844  -32.71794 1.000 35.70392 ? 142 LEU A CB    1 
ATOM   1122 C  CG    . LEU A 1 142 ? 31.91416  -1.10745  -31.23893 1.000 25.31308 ? 142 LEU A CG    1 
ATOM   1123 C  CD1   . LEU A 1 142 ? 30.82815  -1.96245  -30.60595 1.000 31.89788 ? 142 LEU A CD1   1 
ATOM   1124 C  CD2   . LEU A 1 142 ? 33.27615  -1.76145  -31.07591 1.000 30.58301 ? 142 LEU A CD2   1 
ATOM   1125 N  N     . VAL A 1 143 ? 31.12522  1.09857   -35.22094 1.000 34.79816 ? 143 VAL A N     1 
ATOM   1126 C  CA    . VAL A 1 143 ? 30.69324  1.24357   -36.60794 1.000 31.34142 ? 143 VAL A CA    1 
ATOM   1127 C  C     . VAL A 1 143 ? 31.75426  1.96257   -37.43092 1.000 35.74341 ? 143 VAL A C     1 
ATOM   1128 O  O     . VAL A 1 143 ? 31.94227  1.65858   -38.61692 1.000 33.39699 ? 143 VAL A O     1 
ATOM   1129 C  CB    . VAL A 1 143 ? 29.33825  1.97358   -36.66496 1.000 31.46211 ? 143 VAL A CB    1 
ATOM   1130 C  CG1   . VAL A 1 143 ? 28.81827  2.02258   -38.09097 1.000 38.14027 ? 143 VAL A CG1   1 
ATOM   1131 C  CG2   . VAL A 1 143 ? 28.33123  1.29457   -35.75198 1.000 33.30407 ? 143 VAL A CG2   1 
ATOM   1132 N  N     . ALA A 1 144 ? 32.47125  2.91257   -36.82591 1.000 31.04237 ? 144 ALA A N     1 
ATOM   1133 C  CA    . ALA A 1 144 ? 33.50126  3.64057   -37.55889 1.000 34.01736 ? 144 ALA A CA    1 
ATOM   1134 C  C     . ALA A 1 144 ? 34.71126  2.75857   -37.84088 1.000 33.38805 ? 144 ALA A C     1 
ATOM   1135 O  O     . ALA A 1 144 ? 35.29628  2.82857   -38.92787 1.000 38.47856 ? 144 ALA A O     1 
ATOM   1136 C  CB    . ALA A 1 144 ? 33.91725  4.88757   -36.77888 1.000 33.30540 ? 144 ALA A CB    1 
ATOM   1137 N  N     . ARG A 1 145 ? 35.10203  1.92556   -36.87286 1.000 30.53634 ? 145 ARG A N     1 
ATOM   1138 C  CA    . ARG A 1 145 ? 36.25766  1.05585   -37.06328 1.000 36.63513 ? 145 ARG A CA    1 
ATOM   1139 C  C     . ARG A 1 145 ? 35.97793  -0.03675  -38.08618 1.000 36.43528 ? 145 ARG A C     1 
ATOM   1140 O  O     . ARG A 1 145 ? 36.90951  -0.53769  -38.72621 1.000 34.65109 ? 145 ARG A O     1 
ATOM   1141 C  CB    . ARG A 1 145 ? 36.67292  0.43612   -35.72833 1.000 37.97774 ? 145 ARG A CB    1 
ATOM   1142 C  CG    . ARG A 1 145 ? 37.03677  1.45145   -34.65571 1.000 40.93730 ? 145 ARG A CG    1 
ATOM   1143 C  CD    . ARG A 1 145 ? 38.41612  2.04390   -34.88715 1.000 46.51828 ? 145 ARG A CD    1 
ATOM   1144 N  NE    . ARG A 1 145 ? 39.47213  1.08711   -34.57968 1.000 51.19061 ? 145 ARG A NE    1 
ATOM   1145 C  CZ    . ARG A 1 145 ? 39.99555  0.91422   -33.37361 1.000 42.83879 ? 145 ARG A CZ    1 
ATOM   1146 N  NH1   . ARG A 1 145 ? 39.58569  1.62290   -32.33438 1.000 37.79784 ? 145 ARG A NH1   1 
ATOM   1147 N  NH2   . ARG A 1 145 ? 40.95352  0.00700   -33.20564 1.000 33.77004 ? 145 ARG A NH2   1 
ATOM   1148 N  N     . ASN A 1 146 ? 34.71427  -0.41543  -38.25689 1.000 35.68238 ? 146 ASN A N     1 
ATOM   1149 C  CA    . ASN A 1 146 ? 34.34228  -1.47842  -39.18090 1.000 38.50936 ? 146 ASN A CA    1 
ATOM   1150 C  C     . ASN A 1 146 ? 34.15930  -0.98542  -40.61090 1.000 39.13207 ? 146 ASN A C     1 
ATOM   1151 O  O     . ASN A 1 146 ? 33.88231  -1.79942  -41.49890 1.000 38.44898 ? 146 ASN A O     1 
ATOM   1152 C  CB    . ASN A 1 146 ? 33.06227  -2.16542  -38.69392 1.000 31.96294 ? 146 ASN A CB    1 
ATOM   1153 C  CG    . ASN A 1 146 ? 32.90627  -3.56842  -39.24793 1.000 34.87607 ? 146 ASN A CG    1 
ATOM   1154 O  OD1   . ASN A 1 146 ? 33.60327  -4.49342  -38.82892 1.000 35.36888 ? 146 ASN A OD1   1 
ATOM   1155 N  ND2   . ASN A 1 146 ? 31.98529  -3.73542  -40.18894 1.000 41.20674 ? 146 ASN A ND2   1 
ATOM   1156 N  N     . GLY A 1 147 ? 34.30831  0.31558   -40.85989 1.000 35.24637 ? 147 GLY A N     1 
ATOM   1157 C  CA    . GLY A 1 147 ? 34.22633  0.86359   -42.19889 1.000 34.01674 ? 147 GLY A CA    1 
ATOM   1158 C  C     . GLY A 1 147 ? 33.06333  1.79959   -42.44490 1.000 32.31744 ? 147 GLY A C     1 
ATOM   1159 O  O     . GLY A 1 147 ? 32.90135  2.26659   -43.57891 1.000 35.96657 ? 147 GLY A O     1 
ATOM   1160 N  N     . GLY A 1 148 ? 32.25332  2.09659   -41.43192 1.000 29.84057 ? 148 GLY A N     1 
ATOM   1161 C  CA    . GLY A 1 148 ? 31.09532  2.95459   -41.57393 1.000 33.36358 ? 148 GLY A CA    1 
ATOM   1162 C  C     . GLY A 1 148 ? 29.77232  2.23259   -41.45095 1.000 34.39666 ? 148 GLY A C     1 
ATOM   1163 O  O     . GLY A 1 148 ? 28.74032  2.88859   -41.24497 1.000 32.56180 ? 148 GLY A O     1 
ATOM   1164 N  N     . ALA A 1 149 ? 29.76732  0.90859   -41.57196 1.000 30.33294 ? 149 ALA A N     1 
ATOM   1165 C  CA    . ALA A 1 149 ? 28.56331  0.10559   -41.43298 1.000 30.54195 ? 149 ALA A CA    1 
ATOM   1166 C  C     . ALA A 1 149 ? 28.71929  -0.85841  -40.26598 1.000 34.56669 ? 149 ALA A C     1 
ATOM   1167 O  O     . ALA A 1 149 ? 29.83129  -1.27141  -39.92396 1.000 37.69126 ? 149 ALA A O     1 
ATOM   1168 C  CB    . ALA A 1 149 ? 28.25933  -0.67340  -42.71799 1.000 38.89918 ? 149 ALA A CB    1 
ATOM   1169 N  N     . ALA A 1 150 ? 27.59328  -1.21241  -39.65600 1.000 35.10376 ? 150 ALA A N     1 
ATOM   1170 C  CA    . ALA A 1 150 ? 27.61527  -2.13141  -38.53200 1.000 23.76767 ? 150 ALA A CA    1 
ATOM   1171 C  C     . ALA A 1 150 ? 27.65127  -3.57841  -39.02101 1.000 35.34770 ? 150 ALA A C     1 
ATOM   1172 O  O     . ALA A 1 150 ? 27.10429  -3.89841  -40.08002 1.000 24.42535 ? 150 ALA A O     1 
ATOM   1173 C  CB    . ALA A 1 150 ? 26.39325  -1.91642  -37.64502 1.000 30.18343 ? 150 ALA A CB    1 
ATOM   1174 N  N     . PRO A 1 151 ? 28.30126  -4.46742  -38.27200 1.000 37.07459 ? 151 PRO A N     1 
ATOM   1175 C  CA    . PRO A 1 151 ? 28.30226  -5.88442  -38.65100 1.000 23.58776 ? 151 PRO A CA    1 
ATOM   1176 C  C     . PRO A 1 151 ? 26.91026  -6.48341  -38.53903 1.000 27.75422 ? 151 PRO A C     1 
ATOM   1177 O  O     . PRO A 1 151 ? 26.08725  -6.05841  -37.72504 1.000 27.16502 ? 151 PRO A O     1 
ATOM   1178 C  CB    . PRO A 1 151 ? 29.26524  -6.52442  -37.64299 1.000 27.30309 ? 151 PRO A CB    1 
ATOM   1179 C  CG    . PRO A 1 151 ? 30.07624  -5.38742  -37.10098 1.000 23.08868 ? 151 PRO A CG    1 
ATOM   1180 C  CD    . PRO A 1 151 ? 29.15824  -4.20742  -37.10399 1.000 26.61155 ? 151 PRO A CD    1 
ATOM   1181 N  N     . LEU A 1 152 ? 26.65027  -7.48741  -39.37704 1.000 29.80637 ? 152 LEU A N     1 
ATOM   1182 C  CA    . LEU A 1 152 ? 25.36027  -8.16141  -39.39306 1.000 26.84619 ? 152 LEU A CA    1 
ATOM   1183 C  C     . LEU A 1 152 ? 25.41526  -9.59541  -38.88806 1.000 31.62174 ? 152 LEU A C     1 
ATOM   1184 O  O     . LEU A 1 152 ? 24.36226  -10.23241 -38.77208 1.000 33.35579 ? 152 LEU A O     1 
ATOM   1185 C  CB    . LEU A 1 152 ? 24.76929  -8.15040  -40.81107 1.000 25.03744 ? 152 LEU A CB    1 
ATOM   1186 C  CG    . LEU A 1 152 ? 24.40030  -6.77840  -41.37807 1.000 31.56636 ? 152 LEU A CG    1 
ATOM   1187 C  CD1   . LEU A 1 152 ? 23.77032  -6.91639  -42.75608 1.000 26.66675 ? 152 LEU A CD1   1 
ATOM   1188 C  CD2   . LEU A 1 152 ? 23.46829  -6.03740  -40.42908 1.000 24.72470 ? 152 LEU A CD2   1 
ATOM   1189 N  N     . THR A 1 153 ? 26.60125  -10.12041 -38.58705 1.000 26.22898 ? 153 THR A N     1 
ATOM   1190 C  CA    . THR A 1 153 ? 26.74824  -11.47041 -38.06805 1.000 28.38716 ? 153 THR A CA    1 
ATOM   1191 C  C     . THR A 1 153 ? 27.53622  -11.43742 -36.76704 1.000 26.74926 ? 153 THR A C     1 
ATOM   1192 O  O     . THR A 1 153 ? 28.36422  -10.54942 -36.54402 1.000 26.77643 ? 153 THR A O     1 
ATOM   1193 C  CB    . THR A 1 153 ? 27.46026  -12.39741 -39.06604 1.000 28.64517 ? 153 THR A CB    1 
ATOM   1194 O  OG1   . THR A 1 153 ? 28.85126  -12.06041 -39.12802 1.000 28.66983 ? 153 THR A OG1   1 
ATOM   1195 C  CG2   . THR A 1 153 ? 26.84828  -12.26641 -40.45605 1.000 31.92400 ? 153 THR A CG2   1 
ATOM   1196 N  N     A MET A 1 154 ? 27.26521  -12.42342 -35.90804 0.535 28.80569 ? 154 MET A N     1 
ATOM   1197 N  N     B MET A 1 154 ? 27.26421  -12.41642 -35.90004 0.465 28.28760 ? 154 MET A N     1 
ATOM   1198 C  CA    A MET A 1 154 ? 28.01019  -12.55343 -34.66103 0.535 28.14721 ? 154 MET A CA    1 
ATOM   1199 C  CA    B MET A 1 154 ? 28.02519  -12.52843 -34.66103 0.465 28.35403 ? 154 MET A CA    1 
ATOM   1200 C  C     A MET A 1 154 ? 29.46119  -12.93943 -34.91601 0.535 26.66637 ? 154 MET A C     1 
ATOM   1201 C  C     B MET A 1 154 ? 29.47319  -12.91643 -34.93101 0.465 26.64493 ? 154 MET A C     1 
ATOM   1202 O  O     A MET A 1 154 ? 30.35318  -12.52744 -34.16600 0.535 26.74356 ? 154 MET A O     1 
ATOM   1203 O  O     B MET A 1 154 ? 30.37618  -12.47644 -34.20900 0.465 26.46707 ? 154 MET A O     1 
ATOM   1204 C  CB    A MET A 1 154 ? 27.33117  -13.58543 -33.76005 0.535 26.88648 ? 154 MET A CB    1 
ATOM   1205 C  CB    B MET A 1 154 ? 27.36117  -13.54143 -33.72605 0.465 26.70226 ? 154 MET A CB    1 
ATOM   1206 C  CG    A MET A 1 154 ? 27.94915  -13.73244 -32.38204 0.535 25.07070 ? 154 MET A CG    1 
ATOM   1207 C  CG    B MET A 1 154 ? 28.16915  -13.87744 -32.48004 0.465 24.92690 ? 154 MET A CG    1 
ATOM   1208 S  SD    A MET A 1 154 ? 27.76514  -12.25444 -31.36904 0.535 23.47196 ? 154 MET A SD    1 
ATOM   1209 S  SD    B MET A 1 154 ? 28.61814  -12.42644 -31.50802 0.465 23.74605 ? 154 MET A SD    1 
ATOM   1210 C  CE    A MET A 1 154 ? 28.21211  -12.90545 -29.76403 0.535 20.83509 ? 154 MET A CE    1 
ATOM   1211 C  CE    B MET A 1 154 ? 27.00413  -11.83744 -31.00605 0.465 23.60292 ? 154 MET A CE    1 
ATOM   1212 N  N     . GLN A 1 155 ? 29.71321  -13.72443 -35.96801 1.000 27.47942 ? 155 GLN A N     1 
ATOM   1213 C  CA    . GLN A 1 155 ? 31.07821  -14.11943 -36.30199 1.000 26.72000 ? 155 GLN A CA    1 
ATOM   1214 C  C     . GLN A 1 155 ? 31.93622  -12.91043 -36.65497 1.000 27.57344 ? 155 GLN A C     1 
ATOM   1215 O  O     . GLN A 1 155 ? 33.11621  -12.84843 -36.28996 1.000 29.18047 ? 155 GLN A O     1 
ATOM   1216 C  CB    . GLN A 1 155 ? 31.05223  -15.12642 -37.45400 1.000 29.02082 ? 155 GLN A CB    1 
ATOM   1217 C  CG    . GLN A 1 155 ? 32.20124  -15.00542 -38.44698 1.000 37.29038 ? 155 GLN A CG    1 
ATOM   1218 C  CD    . GLN A 1 155 ? 33.49423  -15.60543 -37.93296 1.000 36.30289 ? 155 GLN A CD    1 
ATOM   1219 O  OE1   . GLN A 1 155 ? 34.58324  -15.17543 -38.31194 0.000 34.69702 ? 155 GLN A OE1   1 
ATOM   1220 N  NE2   . GLN A 1 155 ? 33.38022  -16.61143 -37.07497 0.000 34.42159 ? 155 GLN A NE2   1 
ATOM   1221 N  N     . SER A 1 156 ? 31.36023  -11.93143 -37.35298 1.000 26.90019 ? 156 SER A N     1 
ATOM   1222 C  CA    . SER A 1 156 ? 32.10824  -10.72843 -37.70096 1.000 25.12786 ? 156 SER A CA    1 
ATOM   1223 C  C     . SER A 1 156 ? 32.15922  -9.73143  -36.54896 1.000 29.01916 ? 156 SER A C     1 
ATOM   1224 O  O     . SER A 1 156 ? 33.11722  -8.95743  -36.44894 1.000 26.50988 ? 156 SER A O     1 
ATOM   1225 C  CB    . SER A 1 156 ? 31.49626  -10.06942 -38.93697 1.000 27.58067 ? 156 SER A CB    1 
ATOM   1226 O  OG    . SER A 1 156 ? 30.12826  -9.76342  -38.72399 1.000 24.13544 ? 156 SER A OG    1 
ATOM   1227 N  N     . PHE A 1 157 ? 31.14721  -9.73343  -35.67697 1.000 25.03344 ? 157 PHE A N     1 
ATOM   1228 C  CA    . PHE A 1 157 ? 31.12519  -8.79344  -34.56097 1.000 26.22053 ? 157 PHE A CA    1 
ATOM   1229 C  C     . PHE A 1 157 ? 32.07218  -9.22244  -33.44696 1.000 27.02111 ? 157 PHE A C     1 
ATOM   1230 O  O     . PHE A 1 157 ? 32.72017  -8.37544  -32.82195 1.000 29.35157 ? 157 PHE A O     1 
ATOM   1231 C  CB    . PHE A 1 157 ? 29.69919  -8.65043  -34.02499 1.000 24.00257 ? 157 PHE A CB    1 
ATOM   1232 C  CG    . PHE A 1 157 ? 29.56717  -7.65244  -32.90999 1.000 23.63404 ? 157 PHE A CG    1 
ATOM   1233 C  CD1   . PHE A 1 157 ? 29.42318  -6.30144  -33.18499 1.000 26.75216 ? 157 PHE A CD1   1 
ATOM   1234 C  CD2   . PHE A 1 157 ? 29.58215  -8.06344  -31.58699 1.000 27.79200 ? 157 PHE A CD2   1 
ATOM   1235 C  CE1   . PHE A 1 157 ? 29.30116  -5.38044  -32.16199 1.000 23.39571 ? 157 PHE A CE1   1 
ATOM   1236 C  CE2   . PHE A 1 157 ? 29.46114  -7.14745  -30.55999 1.000 20.43878 ? 157 PHE A CE2   1 
ATOM   1237 C  CZ    . PHE A 1 157 ? 29.31914  -5.80545  -30.84799 1.000 23.71116 ? 157 PHE A CZ    1 
ATOM   1238 N  N     . THR A 1 158 ? 32.15717  -10.52844 -33.18096 1.000 27.48677 ? 158 THR A N     1 
ATOM   1239 C  CA    . THR A 1 158 ? 33.06515  -11.01645 -32.14795 1.000 26.30362 ? 158 THR A CA    1 
ATOM   1240 C  C     . THR A 1 158 ? 34.51616  -10.73345 -32.51593 1.000 26.45344 ? 158 THR A C     1 
ATOM   1241 O  O     . THR A 1 158 ? 35.33915  -10.42045 -31.64691 1.000 32.66061 ? 158 THR A O     1 
ATOM   1242 C  CB    . THR A 1 158 ? 32.85015  -12.51545 -31.92396 1.000 25.71384 ? 158 THR A CB    1 
ATOM   1243 O  OG1   . THR A 1 158 ? 31.49414  -12.75145 -31.52498 1.000 22.76941 ? 158 THR A OG1   1 
ATOM   1244 C  CG2   . THR A 1 158 ? 33.78813  -13.03845 -30.84395 1.000 25.20284 ? 158 THR A CG2   1 
ATOM   1245 N  N     . LYS A 1 159 ? 34.84518  -10.83044 -33.80092 1.000 27.55134 ? 159 LYS A N     1 
ATOM   1246 C  CA    . LYS A 1 159 ? 36.19119  -10.52645 -34.26690 1.000 30.01667 ? 159 LYS A CA    1 
ATOM   1247 C  C     . LYS A 1 159 ? 36.47219  -9.03145  -34.30889 1.000 25.68712 ? 159 LYS A C     1 
ATOM   1248 O  O     . LYS A 1 159 ? 37.63719  -8.64045  -34.43787 1.000 27.38639 ? 159 LYS A O     1 
ATOM   1249 C  CB    . LYS A 1 159 ? 36.42521  -11.13344 -35.65590 1.000 30.35360 ? 159 LYS A CB    1 
ATOM   1250 C  CG    . LYS A 1 159 ? 36.84720  -12.60544 -35.66090 1.000 38.61746 ? 159 LYS A CG    1 
ATOM   1251 C  CD    . LYS A 1 159 ? 35.84119  -13.49944 -34.94792 0.000 32.68561 ? 159 LYS A CD    1 
ATOM   1252 C  CE    . LYS A 1 159 ? 36.02719  -14.96444 -35.29992 0.000 34.91892 ? 159 LYS A CE    1 
ATOM   1253 N  NZ    . LYS A 1 159 ? 34.99718  -15.82144 -34.64494 0.000 33.53498 ? 159 LYS A NZ    1 
ATOM   1254 N  N     . LEU A 1 160 ? 35.44119  -8.19044  -34.20790 1.000 28.63964 ? 160 LEU A N     1 
ATOM   1255 C  CA    . LEU A 1 160 ? 35.66619  -6.75044  -34.18190 1.000 26.01688 ? 160 LEU A CA    1 
ATOM   1256 C  C     . LEU A 1 160 ? 35.96417  -6.25645  -32.77089 1.000 30.18165 ? 160 LEU A C     1 
ATOM   1257 O  O     . LEU A 1 160 ? 36.82917  -5.39445  -32.58487 1.000 35.81332 ? 160 LEU A O     1 
ATOM   1258 C  CB    . LEU A 1 160 ? 34.45720  -6.01744  -34.75891 1.000 30.31957 ? 160 LEU A CB    1 
ATOM   1259 C  CG    . LEU A 1 160 ? 34.54221  -4.49144  -34.82690 1.000 35.16219 ? 160 LEU A CG    1 
ATOM   1260 C  CD1   . LEU A 1 160 ? 35.66522  -4.04144  -35.75789 1.000 35.64520 ? 160 LEU A CD1   1 
ATOM   1261 C  CD2   . LEU A 1 160 ? 33.21221  -3.90744  -35.26392 1.000 31.06168 ? 160 LEU A CD2   1 
ATOM   1262 N  N     . VAL A 1 161 ? 35.27315  -6.80045  -31.76590 1.000 28.49517 ? 161 VAL A N     1 
ATOM   1263 C  CA    . VAL A 1 161 ? 35.52513  -6.39046  -30.38890 1.000 29.10201 ? 161 VAL A CA    1 
ATOM   1264 C  C     . VAL A 1 161 ? 36.86213  -6.93446  -29.90088 1.000 30.46019 ? 161 VAL A C     1 
ATOM   1265 O  O     . VAL A 1 161 ? 37.50111  -6.33447  -29.02987 1.000 26.01713 ? 161 VAL A O     1 
ATOM   1266 C  CB    . VAL A 1 161 ? 34.36112  -6.82646  -29.47792 1.000 32.10108 ? 161 VAL A CB    1 
ATOM   1267 C  CG1   . VAL A 1 161 ? 33.05713  -6.20846  -29.95793 1.000 32.63834 ? 161 VAL A CG1   1 
ATOM   1268 C  CG2   . VAL A 1 161 ? 34.24912  -8.34246  -29.42792 1.000 31.23541 ? 161 VAL A CG2   1 
ATOM   1269 N  N     . ASP A 1 162 ? 37.30913  -8.07146  -30.44187 1.000 34.86700 ? 162 ASP A N     1 
ATOM   1270 C  CA    . ASP A 1 162 ? 38.64513  -8.56046  -30.11686 1.000 30.00728 ? 162 ASP A CA    1 
ATOM   1271 C  C     . ASP A 1 162 ? 39.72114  -7.68646  -30.74584 1.000 30.87323 ? 162 ASP A C     1 
ATOM   1272 O  O     . ASP A 1 162 ? 40.82813  -7.57947  -30.20682 1.000 25.26112 ? 162 ASP A O     1 
ATOM   1273 C  CB    . ASP A 1 162 ? 38.80413  -10.01146 -30.57186 1.000 30.76038 ? 162 ASP A CB    1 
ATOM   1274 C  CG    . ASP A 1 162 ? 37.95712  -10.97246 -29.76188 1.000 30.53750 ? 162 ASP A CG    1 
ATOM   1275 O  OD1   . ASP A 1 162 ? 37.77010  -10.72647 -28.55188 1.000 28.66553 ? 162 ASP A OD1   1 
ATOM   1276 O  OD2   . ASP A 1 162 ? 37.47912  -11.97546 -30.33589 1.000 24.73591 ? 162 ASP A OD2   1 
ATOM   1277 N  N     . ARG A 1 163 ? 39.41110  -7.05003  -31.87670 1.000 33.16858 ? 163 ARG A N     1 
ATOM   1278 C  CA    . ARG A 1 163 ? 40.37484  -6.16108  -32.51420 1.000 29.12757 ? 163 ARG A CA    1 
ATOM   1279 C  C     . ARG A 1 163 ? 40.51019  -4.85436  -31.74242 1.000 30.20523 ? 163 ARG A C     1 
ATOM   1280 O  O     . ARG A 1 163 ? 41.60775  -4.29327  -31.64828 1.000 27.50287 ? 163 ARG A O     1 
ATOM   1281 C  CB    . ARG A 1 163 ? 39.95781  -5.89617  -33.95983 1.000 31.02634 ? 163 ARG A CB    1 
ATOM   1282 C  CG    . ARG A 1 163 ? 41.11702  -5.74409  -34.92646 1.000 34.11988 ? 163 ARG A CG    1 
ATOM   1283 C  CD    . ARG A 1 163 ? 40.61614  -5.59702  -36.35269 1.000 41.15487 ? 163 ARG A CD    1 
ATOM   1284 N  NE    . ARG A 1 163 ? 39.66647  -6.64628  -36.70444 1.000 38.52464 ? 163 ARG A NE    1 
ATOM   1285 C  CZ    . ARG A 1 163 ? 40.00236  -7.81973  -37.22254 1.000 42.97532 ? 163 ARG A CZ    1 
ATOM   1286 N  NH1   . ARG A 1 163 ? 41.26487  -8.13327  -37.46343 0.161 41.89295 ? 163 ARG A NH1   1 
ATOM   1287 N  NH2   . ARG A 1 163 ? 39.04736  -8.70093  -37.50614 0.352 40.93491 ? 163 ARG A NH2   1 
ATOM   1288 N  N     . VAL A 1 164 ? 39.40615  -4.35646  -31.18083 1.000 33.78785 ? 164 VAL A N     1 
ATOM   1289 C  CA    . VAL A 1 164 ? 39.46314  -3.13147  -30.38882 1.000 24.88161 ? 164 VAL A CA    1 
ATOM   1290 C  C     . VAL A 1 164 ? 40.12312  -3.39847  -29.04182 1.000 23.69171 ? 164 VAL A C     1 
ATOM   1291 O  O     . VAL A 1 164 ? 40.93311  -2.59747  -28.56280 1.000 27.31052 ? 164 VAL A O     1 
ATOM   1292 C  CB    . VAL A 1 164 ? 38.05314  -2.53646  -30.22384 1.000 28.49491 ? 164 VAL A CB    1 
ATOM   1293 C  CG1   . VAL A 1 164 ? 38.10613  -1.25947  -29.39984 1.000 28.13705 ? 164 VAL A CG1   1 
ATOM   1294 C  CG2   . VAL A 1 164 ? 37.42716  -2.27046  -31.58385 1.000 30.50249 ? 164 VAL A CG2   1 
ATOM   1295 N  N     . GLY A 1 165 ? 39.79311  -4.51747  -28.41482 1.000 24.25879 ? 165 GLY A N     1 
ATOM   1296 C  CA    . GLY A 1 165 ? 40.38509  -4.90448  -27.15482 1.000 30.93062 ? 165 GLY A CA    1 
ATOM   1297 C  C     . GLY A 1 165 ? 39.38207  -4.92148  -26.01783 1.000 29.50119 ? 165 GLY A C     1 
ATOM   1298 O  O     . GLY A 1 165 ? 38.17107  -5.06448  -26.20985 1.000 30.43875 ? 165 GLY A O     1 
ATOM   1299 N  N     . ASP A 1 166 ? 39.90705  -4.77149  -24.80782 1.000 30.20588 ? 166 ASP A N     1 
ATOM   1300 C  CA    . ASP A 1 166 ? 39.05803  -4.78749  -23.62784 1.000 24.52112 ? 166 ASP A CA    1 
ATOM   1301 C  C     . ASP A 1 166 ? 38.27603  -3.47949  -23.52384 1.000 27.31376 ? 166 ASP A C     1 
ATOM   1302 O  O     . ASP A 1 166 ? 38.80004  -2.41249  -23.85983 1.000 24.34885 ? 166 ASP A O     1 
ATOM   1303 C  CB    . ASP A 1 166 ? 39.89301  -4.99449  -22.36482 1.000 27.84453 ? 166 ASP A CB    1 
ATOM   1304 C  CG    . ASP A 1 166 ? 40.61801  -6.32450  -22.35882 1.000 27.57205 ? 166 ASP A CG    1 
ATOM   1305 O  OD1   . ASP A 1 166 ? 40.15802  -7.25649  -23.05183 1.000 34.80410 ? 166 ASP A OD1   1 
ATOM   1306 O  OD2   . ASP A 1 166 ? 41.64500  -6.43850  -21.65680 1.000 22.33132 ? 166 ASP A OD2   1 
ATOM   1307 N  N     . PRO A 1 167 ? 37.02903  -3.52749  -23.06686 1.000 30.43719 ? 167 PRO A N     1 
ATOM   1308 C  CA    . PRO A 1 167 ? 36.25403  -2.29849  -22.87787 1.000 24.90511 ? 167 PRO A CA    1 
ATOM   1309 C  C     . PRO A 1 167 ? 36.81601  -1.47949  -21.73186 1.000 30.17689 ? 167 PRO A C     1 
ATOM   1310 O  O     . PRO A 1 167 ? 37.65100  -1.97550  -20.95985 1.000 24.32714 ? 167 PRO A O     1 
ATOM   1311 C  CB    . PRO A 1 167 ? 34.84402  -2.81848  -22.55989 1.000 24.88543 ? 167 PRO A CB    1 
ATOM   1312 C  CG    . PRO A 1 167 ? 35.07201  -4.16449  -21.97290 1.000 29.12041 ? 167 PRO A CG    1 
ATOM   1313 C  CD    . PRO A 1 167 ? 36.25902  -4.72949  -22.69988 1.000 27.22603 ? 167 PRO A CD    1 
ATOM   1314 N  N     . PRO A 1 168 ? 36.40401  -0.21849  -21.59786 1.000 23.30980 ? 168 PRO A N     1 
ATOM   1315 C  CA    . PRO A 1 168 ? 36.88800  0.59450   -20.47485 1.000 24.62900 ? 168 PRO A CA    1 
ATOM   1316 C  C     . PRO A 1 168 ? 36.56297  -0.05250  -19.13686 1.000 26.08835 ? 168 PRO A C     1 
ATOM   1317 O  O     . PRO A 1 168 ? 35.50897  -0.66650  -18.96088 1.000 31.39222 ? 168 PRO A O     1 
ATOM   1318 C  CB    . PRO A 1 168 ? 36.14500  1.92251   -20.65486 1.000 29.39823 ? 168 PRO A CB    1 
ATOM   1319 C  CG    . PRO A 1 168 ? 35.86102  1.98951   -22.11586 1.000 19.85797 ? 168 PRO A CG    1 
ATOM   1320 C  CD    . PRO A 1 168 ? 35.59403  0.57351   -22.53987 1.000 24.56232 ? 168 PRO A CD    1 
ATOM   1321 N  N     . ALA A 1 169 ? 37.49296  0.08049   -18.19584 1.000 28.60694 ? 169 ALA A N     1 
ATOM   1322 C  CA    . ALA A 1 169 ? 37.29794  -0.48451  -16.87285 1.000 23.87787 ? 169 ALA A CA    1 
ATOM   1323 C  C     . ALA A 1 169 ? 36.10793  0.18649   -16.18786 1.000 21.67553 ? 169 ALA A C     1 
ATOM   1324 O  O     . ALA A 1 169 ? 35.76794  1.33149   -16.50286 1.000 25.96369 ? 169 ALA A O     1 
ATOM   1325 C  CB    . ALA A 1 169 ? 38.55993  -0.31251  -16.02883 1.000 33.14998 ? 169 ALA A CB    1 
ATOM   1326 N  N     . PRO A 1 170 ? 35.44391  -0.50751  -15.26288 1.000 22.20987 ? 170 PRO A N     1 
ATOM   1327 C  CA    . PRO A 1 170 ? 34.32490  0.11649   -14.54689 1.000 27.49534 ? 170 PRO A CA    1 
ATOM   1328 C  C     . PRO A 1 170 ? 34.78889  1.32148   -13.74088 1.000 20.83357 ? 170 PRO A C     1 
ATOM   1329 O  O     . PRO A 1 170 ? 35.89089  1.33948   -13.18786 1.000 24.22213 ? 170 PRO A O     1 
ATOM   1330 C  CB    . PRO A 1 170 ? 33.80789  -1.00851  -13.64090 1.000 25.03504 ? 170 PRO A CB    1 
ATOM   1331 C  CG    . PRO A 1 170 ? 34.94288  -1.97952  -13.54289 1.000 26.41407 ? 170 PRO A CG    1 
ATOM   1332 C  CD    . PRO A 1 170 ? 35.63691  -1.91151  -14.86588 1.000 22.94030 ? 170 PRO A CD    1 
ATOM   1333 N  N     . ALA A 1 171 ? 33.93089  2.33749   -13.68889 1.000 26.46710 ? 171 ALA A N     1 
ATOM   1334 C  CA    . ALA A 1 171 ? 34.27189  3.57648   -13.01188 1.000 23.11828 ? 171 ALA A CA    1 
ATOM   1335 C  C     . ALA A 1 171 ? 34.37986  3.35248   -11.50388 1.000 22.34996 ? 171 ALA A C     1 
ATOM   1336 O  O     . ALA A 1 171 ? 33.75285  2.44148   -10.95589 1.000 31.37967 ? 171 ALA A O     1 
ATOM   1337 C  CB    . ALA A 1 171 ? 33.22389  4.64649   -13.30689 1.000 26.31146 ? 171 ALA A CB    1 
ATOM   1338 N  N     . PRO A 1 172 ? 35.17385  4.16747   -10.81186 1.000 14.75626 ? 172 PRO A N     1 
ATOM   1339 C  CA    . PRO A 1 172 ? 35.29783  4.02047   -9.35686  1.000 19.99110 ? 172 PRO A CA    1 
ATOM   1340 C  C     . PRO A 1 172 ? 33.99882  4.37447   -8.64688  1.000 24.44786 ? 172 PRO A C     1 
ATOM   1341 O  O     . PRO A 1 172 ? 33.07583  4.96447   -9.21189  1.000 17.46682 ? 172 PRO A O     1 
ATOM   1342 C  CB    . PRO A 1 172 ? 36.41883  4.99746   -8.99384  1.000 21.99077 ? 172 PRO A CB    1 
ATOM   1343 C  CG    . PRO A 1 172 ? 36.41885  5.99747   -10.10084 1.000 23.66175 ? 172 PRO A CG    1 
ATOM   1344 C  CD    . PRO A 1 172 ? 36.05186  5.22847   -11.33285 1.000 19.07186 ? 172 PRO A CD    1 
ATOM   1345 N  N     . ASP A 1 173 ? 33.94280  3.99746   -7.37288  1.000 21.46015 ? 173 ASP A N     1 
ATOM   1346 C  CA    . ASP A 1 173 ? 32.76879  4.24846   -6.55590  1.000 24.60166 ? 173 ASP A CA    1 
ATOM   1347 C  C     . ASP A 1 173 ? 32.69379  5.71646   -6.14490  1.000 20.54825 ? 173 ASP A C     1 
ATOM   1348 O  O     . ASP A 1 173 ? 33.72278  6.38146   -5.99088  1.000 28.00235 ? 173 ASP A O     1 
ATOM   1349 C  CB    . ASP A 1 173 ? 32.78977  3.36346   -5.31290  1.000 20.92560 ? 173 ASP A CB    1 
ATOM   1350 C  CG    . ASP A 1 173 ? 32.17877  1.99946   -5.55992  1.000 22.35956 ? 173 ASP A CG    1 
ATOM   1351 O  OD1   . ASP A 1 173 ? 31.01278  1.94246   -6.00394  1.000 28.80498 ? 173 ASP A OD1   1 
ATOM   1352 O  OD2   . ASP A 1 173 ? 32.86476  0.98446   -5.32091  1.000 25.87471 ? 173 ASP A OD2   1 
ATOM   1353 N  N     . PRO A 1 174 ? 31.48678  6.24846   -5.97291  1.000 20.40402 ? 174 PRO A N     1 
ATOM   1354 C  CA    . PRO A 1 174 ? 31.33978  7.64146   -5.54391  1.000 21.06285 ? 174 PRO A CA    1 
ATOM   1355 C  C     . PRO A 1 174 ? 31.75676  7.80745   -4.09390  1.000 17.17963 ? 174 PRO A C     1 
ATOM   1356 O  O     . PRO A 1 174 ? 31.84474  6.82045   -3.34691  1.000 18.82678 ? 174 PRO A O     1 
ATOM   1357 C  CB    . PRO A 1 174 ? 29.83978  7.90946   -5.73193  1.000 18.56815 ? 174 PRO A CB    1 
ATOM   1358 C  CG    . PRO A 1 174 ? 29.20678  6.56746   -5.60895  1.000 26.49111 ? 174 PRO A CG    1 
ATOM   1359 C  CD    . PRO A 1 174 ? 30.18479  5.60347   -6.21593  1.000 21.52315 ? 174 PRO A CD    1 
ATOM   1360 N  N     . PRO A 1 175 ? 32.03375  9.03745   -3.65889  1.000 21.93031 ? 175 PRO A N     1 
ATOM   1361 C  CA    . PRO A 1 175 ? 32.45573  9.25145   -2.26989  1.000 20.80086 ? 175 PRO A CA    1 
ATOM   1362 C  C     . PRO A 1 175 ? 31.37072  8.86145   -1.27791  1.000 25.69603 ? 175 PRO A C     1 
ATOM   1363 O  O     . PRO A 1 175 ? 30.18272  8.78845   -1.60292  1.000 32.52148 ? 175 PRO A O     1 
ATOM   1364 C  CB    . PRO A 1 175 ? 32.74273  10.75745  -2.21388  1.000 23.27596 ? 175 PRO A CB    1 
ATOM   1365 C  CG    . PRO A 1 175 ? 33.00076  11.14945  -3.63287  1.000 18.12916 ? 175 PRO A CG    1 
ATOM   1366 C  CD    . PRO A 1 175 ? 32.10777  10.27346  -4.45589  1.000 21.74493 ? 175 PRO A CD    1 
ATOM   1367 N  N     . ALA A 1 176 ? 31.80070  8.60744   -0.04090  1.000 28.64409 ? 176 ALA A N     1 
ATOM   1368 C  CA    . ALA A 1 176 ? 30.87768  8.23344   1.02309   1.000 22.79873 ? 176 ALA A CA    1 
ATOM   1369 C  C     . ALA A 1 176 ? 30.00668  9.39344   1.48508   1.000 29.70255 ? 176 ALA A C     1 
ATOM   1370 O  O     . ALA A 1 176 ? 29.03466  9.16244   2.21206   1.000 33.23003 ? 176 ALA A O     1 
ATOM   1371 C  CB    . ALA A 1 176 ? 31.65166  7.66443   2.21309   1.000 17.63833 ? 176 ALA A CB    1 
ATOM   1372 N  N     . ALA A 1 177 ? 30.32768  10.62244  1.08809   1.000 29.23079 ? 177 ALA A N     1 
ATOM   1373 C  CA    . ALA A 1 177 ? 29.52868  11.79344  1.42908   1.000 23.22046 ? 177 ALA A CA    1 
ATOM   1374 C  C     . ALA A 1 177 ? 29.37170  12.64344  0.17908   1.000 30.63773 ? 177 ALA A C     1 
ATOM   1375 O  O     . ALA A 1 177 ? 30.36471  13.13844  -0.36091  1.000 31.30024 ? 177 ALA A O     1 
ATOM   1376 C  CB    . ALA A 1 177 ? 30.17567  12.60043  2.55809   1.000 30.94334 ? 177 ALA A CB    1 
ATOM   1377 N  N     . MET A 1 178 ? 28.12771  12.80645  -0.28094  1.000 26.76551 ? 178 MET A N     1 
ATOM   1378 C  CA    . MET A 1 178 ? 27.84073  13.55145  -1.49594  1.000 27.43195 ? 178 MET A CA    1 
ATOM   1379 C  C     . MET A 1 178 ? 27.30673  14.94045  -1.16595  1.000 28.23637 ? 178 MET A C     1 
ATOM   1380 O  O     . MET A 1 178 ? 26.69971  15.14545  -0.10995  1.000 30.03882 ? 178 MET A O     1 
ATOM   1381 C  CB    . MET A 1 178 ? 26.81174  12.81146  -2.35496  1.000 33.14844 ? 178 MET A CB    1 
ATOM   1382 C  CG    . MET A 1 178 ? 27.25575  11.44346  -2.83696  1.000 30.37259 ? 178 MET A CG    1 
ATOM   1383 S  SD    . MET A 1 178 ? 25.97976  10.65546  -3.83398  1.000 32.00313 ? 178 MET A SD    1 
ATOM   1384 C  CE    . MET A 1 178 ? 26.76876  9.10246   -4.24197  1.000 23.98571 ? 178 MET A CE    1 
ATOM   1385 N  N     . PRO A 1 179 ? 27.52674  15.91346  -2.04494  1.000 24.51529 ? 179 PRO A N     1 
ATOM   1386 C  CA    . PRO A 1 179 ? 26.92574  17.23646  -1.85194  1.000 27.23112 ? 179 PRO A CA    1 
ATOM   1387 C  C     . PRO A 1 179 ? 25.41174  17.14746  -1.89197  1.000 27.64077 ? 179 PRO A C     1 
ATOM   1388 O  O     . PRO A 1 179 ? 24.82976  16.74746  -2.91198  1.000 27.11220 ? 179 PRO A O     1 
ATOM   1389 C  CB    . PRO A 1 179 ? 27.46976  18.04946  -3.03793  1.000 24.52909 ? 179 PRO A CB    1 
ATOM   1390 C  CG    . PRO A 1 179 ? 28.71177  17.33246  -3.45292  1.000 25.57463 ? 179 PRO A CG    1 
ATOM   1391 C  CD    . PRO A 1 179 ? 28.43076  15.88046  -3.20692  1.000 27.06378 ? 179 PRO A CD    1 
ATOM   1392 N  N     . PRO A 1 180 ? 24.73873  17.50546  -0.80398  1.000 23.72733 ? 180 PRO A N     1 
ATOM   1393 C  CA    . PRO A 1 180 ? 23.28472  17.35846  -0.74700  1.000 25.51757 ? 180 PRO A CA    1 
ATOM   1394 C  C     . PRO A 1 180 ? 22.59674  18.43946  -1.56000  1.000 26.70563 ? 180 PRO A C     1 
ATOM   1395 O  O     . PRO A 1 180 ? 23.21375  19.46046  -1.89999  1.000 30.94695 ? 180 PRO A O     1 
ATOM   1396 C  CB    . PRO A 1 180 ? 22.97870  17.50645  0.75100   1.000 29.57082 ? 180 PRO A CB    1 
ATOM   1397 C  CG    . PRO A 1 180 ? 24.05770  18.40845  1.24602   1.000 26.51060 ? 180 PRO A CG    1 
ATOM   1398 C  CD    . PRO A 1 180 ? 25.28971  18.07045  0.44103   1.000 28.07771 ? 180 PRO A CD    1 
ATOM   1399 N  N     . PRO A 1 181 ? 21.32374  18.24747  -1.90502  1.000 28.24063 ? 181 PRO A N     1 
ATOM   1400 C  CA    . PRO A 1 181 ? 20.57176  19.32047  -2.56303  1.000 29.06691 ? 181 PRO A CA    1 
ATOM   1401 C  C     . PRO A 1 181 ? 20.40474  20.51647  -1.63903  1.000 26.68398 ? 181 PRO A C     1 
ATOM   1402 O  O     . PRO A 1 181 ? 20.46572  20.40546  -0.41203  1.000 28.60682 ? 181 PRO A O     1 
ATOM   1403 C  CB    . PRO A 1 181 ? 19.21876  18.66847  -2.87906  1.000 27.19108 ? 181 PRO A CB    1 
ATOM   1404 C  CG    . PRO A 1 181 ? 19.48576  17.19747  -2.86006  1.000 30.88839 ? 181 PRO A CG    1 
ATOM   1405 C  CD    . PRO A 1 181 ? 20.54974  16.99647  -1.82604  1.000 29.05103 ? 181 PRO A CD    1 
ATOM   1406 N  N     . ALA A 1 182 ? 20.19376  21.67847  -2.25103  1.000 28.52548 ? 182 ALA A N     1 
ATOM   1407 C  CA    . ALA A 1 182 ? 20.00675  22.90147  -1.48303  1.000 26.61450 ? 182 ALA A CA    1 
ATOM   1408 C  C     . ALA A 1 182 ? 18.72373  22.82647  -0.66705  1.000 27.97952 ? 182 ALA A C     1 
ATOM   1409 O  O     . ALA A 1 182 ? 17.72174  22.25147  -1.10307  1.000 30.08323 ? 182 ALA A O     1 
ATOM   1410 C  CB    . ALA A 1 182 ? 19.97376  24.11547  -2.41002  1.000 31.42360 ? 182 ALA A CB    1 
ATOM   1411 N  N     . GLU A 1 183 ? 18.75872  23.40946  0.52595   1.000 29.52360 ? 183 GLU A N     1 
ATOM   1412 C  CA    . GLU A 1 183 ? 17.61470  23.35646  1.42094   1.000 22.23292 ? 183 GLU A CA    1 
ATOM   1413 C  C     . GLU A 1 183 ? 16.59471  24.43046  1.06292   1.000 28.00602 ? 183 GLU A C     1 
ATOM   1414 O  O     . GLU A 1 183 ? 16.92672  25.46347  0.47393   1.000 27.57932 ? 183 GLU A O     1 
ATOM   1415 C  CB    . GLU A 1 183 ? 18.06168  23.51945  2.87394   1.000 29.57093 ? 183 GLU A CB    1 
ATOM   1416 C  CG    . GLU A 1 183 ? 19.06767  22.47245  3.32596   1.000 31.64379 ? 183 GLU A CG    1 
ATOM   1417 C  CD    . GLU A 1 183 ? 18.98565  22.18545  4.81195   0.000 29.79874 ? 183 GLU A CD    1 
ATOM   1418 O  OE1   . GLU A 1 183 ? 18.10464  22.76345  5.48294   0.000 29.60852 ? 183 GLU A OE1   1 
ATOM   1419 O  OE2   . GLU A 1 183 ? 19.79764  21.37644  5.30696   0.000 29.77572 ? 183 GLU A OE2   1 
ATOM   1420 N  N     . ASP A 1 184 ? 15.33670  24.16446  1.42190   1.000 24.65391 ? 184 ASP A N     1 
ATOM   1421 C  CA    . ASP A 1 184 ? 14.22371  25.08547  1.18889   1.000 23.92106 ? 184 ASP A CA    1 
ATOM   1422 C  C     . ASP A 1 184 ? 14.05073  25.38347  -0.30111  1.000 32.48095 ? 184 ASP A C     1 
ATOM   1423 O  O     . ASP A 1 184 ? 14.01074  26.53847  -0.73011  1.000 34.27279 ? 184 ASP A O     1 
ATOM   1424 C  CB    . ASP A 1 184 ? 14.39970  26.37546  1.99390   1.000 21.08493 ? 184 ASP A CB    1 
ATOM   1425 C  CG    . ASP A 1 184 ? 14.49468  26.12046  3.48490   1.000 26.63140 ? 184 ASP A CG    1 
ATOM   1426 O  OD1   . ASP A 1 184 ? 13.82267  25.18646  3.97189   1.000 17.58870 ? 184 ASP A OD1   1 
ATOM   1427 O  OD2   . ASP A 1 184 ? 15.24367  26.84946  4.16791   1.000 20.86702 ? 184 ASP A OD2   1 
ATOM   1428 N  N     . MET A 1 185 ? 13.94874  24.31848  -1.09412  1.000 28.76385 ? 185 MET A N     1 
ATOM   1429 C  CA    . MET A 1 185 ? 13.66176  24.42448  -2.51512  1.000 27.94477 ? 185 MET A CA    1 
ATOM   1430 C  C     . MET A 1 185 ? 12.26277  23.90249  -2.79514  1.000 29.90442 ? 185 MET A C     1 
ATOM   1431 O  O     . MET A 1 185 ? 11.94176  22.77248  -2.40215  1.000 19.99207 ? 185 MET A O     1 
ATOM   1432 C  CB    . MET A 1 185 ? 14.68778  23.63948  -3.34111  1.000 30.69018 ? 185 MET A CB    1 
ATOM   1433 C  CG    . MET A 1 185 ? 16.05178  24.30648  -3.43708  1.000 31.41843 ? 185 MET A CG    1 
ATOM   1434 S  SD    . MET A 1 185 ? 16.00479  25.85248  -4.36708  1.000 24.44920 ? 185 MET A SD    1 
ATOM   1435 C  CE    . MET A 1 185 ? 17.72679  26.34348  -4.30505  1.000 25.82808 ? 185 MET A CE    1 
ATOM   1436 N  N     . PRO A 1 186 ? 11.40778  24.68549  -3.45915  1.000 31.95169 ? 186 PRO A N     1 
ATOM   1437 C  CA    . PRO A 1 186 ? 10.02278  24.22949  -3.67218  1.000 28.16828 ? 186 PRO A CA    1 
ATOM   1438 C  C     . PRO A 1 186 ? 9.91479   22.98650  -4.54018  1.000 24.67797 ? 186 PRO A C     1 
ATOM   1439 O  O     . PRO A 1 186 ? 9.11679   22.09350  -4.23120  1.000 24.13426 ? 186 PRO A O     1 
ATOM   1440 C  CB    . PRO A 1 186 ? 9.35479   25.44650  -4.33018  1.000 29.49089 ? 186 PRO A CB    1 
ATOM   1441 C  CG    . PRO A 1 186 ? 10.48180  26.23250  -4.92116  1.000 29.76312 ? 186 PRO A CG    1 
ATOM   1442 C  CD    . PRO A 1 186 ? 11.63979  26.03749  -3.99115  1.000 23.96693 ? 186 PRO A CD    1 
ATOM   1443 N  N     . SER A 1 187 ? 10.69681  22.89750  -5.61917  1.000 30.87079 ? 187 SER A N     1 
ATOM   1444 C  CA    . SER A 1 187 ? 10.61682  21.73150  -6.49218  1.000 26.02277 ? 187 SER A CA    1 
ATOM   1445 C  C     . SER A 1 187 ? 11.27181  20.50050  -5.88117  1.000 26.68665 ? 187 SER A C     1 
ATOM   1446 O  O     . SER A 1 187 ? 11.00681  19.38350  -6.33718  1.000 30.46889 ? 187 SER A O     1 
ATOM   1447 C  CB    . SER A 1 187 ? 11.25284  22.04051  -7.84717  1.000 25.47625 ? 187 SER A CB    1 
ATOM   1448 O  OG    . SER A 1 187 ? 10.60885  23.13751  -8.47017  1.000 33.96338 ? 187 SER A OG    1 
ATOM   1449 N  N     . ALA A 1 188 ? 12.11879  20.67549  -4.86616  1.000 20.09254 ? 188 ALA A N     1 
ATOM   1450 C  CA    . ALA A 1 188 ? 12.76678  19.56349  -4.18015  1.000 21.12185 ? 188 ALA A CA    1 
ATOM   1451 C  C     . ALA A 1 188 ? 12.05276  19.19049  -2.88516  1.000 23.91174 ? 188 ALA A C     1 
ATOM   1452 O  O     . ALA A 1 188 ? 12.67475  18.64448  -1.96716  1.000 20.53490 ? 188 ALA A O     1 
ATOM   1453 C  CB    . ALA A 1 188 ? 14.23378  19.89149  -3.90513  1.000 18.65099 ? 188 ALA A CB    1 
ATOM   1454 N  N     . ALA A 1 189 ? 10.75776  19.47949  -2.79218  1.000 21.25273 ? 189 ALA A N     1 
ATOM   1455 C  CA    . ALA A 1 189 ? 10.00674  19.12949  -1.59719  1.000 22.10270 ? 189 ALA A CA    1 
ATOM   1456 C  C     . ALA A 1 189 ? 9.74174   17.62549  -1.56920  1.000 20.74929 ? 189 ALA A C     1 
ATOM   1457 O  O     . ALA A 1 189 ? 9.39275   17.03549  -2.59721  1.000 28.14655 ? 189 ALA A O     1 
ATOM   1458 C  CB    . ALA A 1 189 ? 8.68774   19.89749  -1.54521  1.000 24.31821 ? 189 ALA A CB    1 
ATOM   1459 N  N     . PRO A 1 190 ? 9.90072   16.97848  -0.41220  1.000 21.13082 ? 190 PRO A N     1 
ATOM   1460 C  CA    . PRO A 1 190 ? 9.72472   15.51648  -0.36021  1.000 16.96271 ? 190 PRO A CA    1 
ATOM   1461 C  C     . PRO A 1 190 ? 8.31372   15.05748  -0.68124  1.000 19.84190 ? 190 PRO A C     1 
ATOM   1462 O  O     . PRO A 1 190 ? 8.13873   13.95549  -1.21624  1.000 21.35157 ? 190 PRO A O     1 
ATOM   1463 C  CB    . PRO A 1 190 ? 10.11369  15.16948  1.08479   1.000 27.82318 ? 190 PRO A CB    1 
ATOM   1464 C  CG    . PRO A 1 190 ? 10.94469  16.32447  1.55081   1.000 19.59231 ? 190 PRO A CG    1 
ATOM   1465 C  CD    . PRO A 1 190 ? 10.37170  17.52648  0.86981   1.000 20.74120 ? 190 PRO A CD    1 
ATOM   1466 N  N     . ALA A 1 191 ? 7.29672   15.86349  -0.36925  1.000 24.29431 ? 191 ALA A N     1 
ATOM   1467 C  CA    . ALA A 1 191 ? 5.92272   15.47249  -0.65527  1.000 25.12706 ? 191 ALA A CA    1 
ATOM   1468 C  C     . ALA A 1 191 ? 5.62274   15.42650  -2.14627  1.000 24.39088 ? 191 ALA A C     1 
ATOM   1469 O  O     . ALA A 1 191 ? 4.59475   14.86250  -2.53529  1.000 36.84577 ? 191 ALA A O     1 
ATOM   1470 C  CB    . ALA A 1 191 ? 4.94871   16.42149  0.04072   1.000 27.83872 ? 191 ALA A CB    1 
ATOM   1471 N  N     . ALA A 1 192 ? 6.48476   16.00450  -2.98126  1.000 31.03323 ? 192 ALA A N     1 
ATOM   1472 C  CA    . ALA A 1 192 ? 6.33678   15.93950  -4.42626  1.000 22.13002 ? 192 ALA A CA    1 
ATOM   1473 C  C     . ALA A 1 192 ? 7.50079   15.23550  -5.10925  1.000 20.12982 ? 192 ALA A C     1 
ATOM   1474 O  O     . ALA A 1 192 ? 7.49481   15.11551  -6.34025  1.000 22.63340 ? 192 ALA A O     1 
ATOM   1475 C  CB    . ALA A 1 192 ? 6.17679   17.34950  -5.01126  1.000 23.24970 ? 192 ALA A CB    1 
ATOM   1476 N  N     . THR A 1 193 ? 8.49677   14.76850  -4.35323  1.000 20.64737 ? 193 THR A N     1 
ATOM   1477 C  CA    . THR A 1 193 ? 9.66778   14.10550  -4.91722  1.000 23.84518 ? 193 THR A CA    1 
ATOM   1478 C  C     . THR A 1 193 ? 9.93277   12.76749  -4.23422  1.000 22.34965 ? 193 THR A C     1 
ATOM   1479 O  O     . THR A 1 193 ? 11.06877  12.28549  -4.22220  1.000 21.95220 ? 193 THR A O     1 
ATOM   1480 C  CB    . THR A 1 193 ? 10.90478  14.99950  -4.82220  1.000 22.06241 ? 193 THR A CB    1 
ATOM   1481 O  OG1   . THR A 1 193 ? 11.04876  15.47749  -3.47919  1.000 24.23143 ? 193 THR A OG1   1 
ATOM   1482 C  CG2   . THR A 1 193 ? 10.78180  16.18250  -5.76519  1.000 25.81007 ? 193 THR A CG2   1 
ATOM   1483 N  N     . GLY A 1 194 ? 8.89876   12.15749  -3.66324  1.000 21.79743 ? 194 GLY A N     1 
ATOM   1484 C  CA    . GLY A 1 194 ? 9.04075   10.86249  -3.03324  1.000 22.73244 ? 194 GLY A CA    1 
ATOM   1485 C  C     . GLY A 1 194 ? 8.78176   9.72050   -4.00025  1.000 24.98730 ? 194 GLY A C     1 
ATOM   1486 O  O     . GLY A 1 194 ? 8.06878   9.86750   -4.98826  1.000 26.84228 ? 194 GLY A O     1 
ATOM   1487 N  N     . VAL A 1 195 ? 9.37875   8.57049   -3.70024  1.000 18.06783 ? 195 VAL A N     1 
ATOM   1488 C  CA    . VAL A 1 195 ? 9.22176   7.37550   -4.52725  1.000 24.85471 ? 195 VAL A CA    1 
ATOM   1489 C  C     . VAL A 1 195 ? 7.83376   6.79050   -4.29027  1.000 27.92881 ? 195 VAL A C     1 
ATOM   1490 O  O     . VAL A 1 195 ? 7.55174   6.29450   -3.19028  1.000 29.31612 ? 195 VAL A O     1 
ATOM   1491 C  CB    . VAL A 1 195 ? 10.31776  6.34149   -4.22824  1.000 24.71961 ? 195 VAL A CB    1 
ATOM   1492 C  CG1   . VAL A 1 195 ? 10.10077  5.08550   -5.05724  1.000 22.35096 ? 195 VAL A CG1   1 
ATOM   1493 C  CG2   . VAL A 1 195 ? 11.69176  6.93449   -4.49721  1.000 24.09592 ? 195 VAL A CG2   1 
ATOM   1494 N  N     . PRO A 1 196 ? 6.94677   6.82050   -5.27929  1.000 19.74472 ? 196 PRO A N     1 
ATOM   1495 C  CA    . PRO A 1 196 ? 5.59077   6.30751   -5.07331  1.000 29.95435 ? 196 PRO A CA    1 
ATOM   1496 C  C     . PRO A 1 196 ? 5.54377   4.78851   -5.14531  1.000 26.60903 ? 196 PRO A C     1 
ATOM   1497 O  O     . PRO A 1 196 ? 6.44978   4.12751   -5.65730  1.000 25.74525 ? 196 PRO A O     1 
ATOM   1498 C  CB    . PRO A 1 196 ? 4.80379   6.93651   -6.22632  1.000 22.28787 ? 196 PRO A CB    1 
ATOM   1499 C  CG    . PRO A 1 196 ? 5.81381   7.06251   -7.31730  1.000 29.86082 ? 196 PRO A CG    1 
ATOM   1500 C  CD    . PRO A 1 196 ? 7.13880   7.34351   -6.64428  1.000 25.04231 ? 196 PRO A CD    1 
ATOM   1501 N  N     . THR A 1 197 ? 4.45576   4.24151   -4.61633  1.000 34.01787 ? 197 THR A N     1 
ATOM   1502 C  CA    . THR A 1 197 ? 4.22276   2.80651   -4.63234  1.000 30.64485 ? 197 THR A CA    1 
ATOM   1503 C  C     . THR A 1 197 ? 3.38278   2.41951   -5.84736  1.000 27.40306 ? 197 THR A C     1 
ATOM   1504 O  O     . THR A 1 197 ? 2.89879   3.26752   -6.59936  1.000 32.06626 ? 197 THR A O     1 
ATOM   1505 C  CB    . THR A 1 197 ? 3.53474   2.36150   -3.34235  1.000 32.59997 ? 197 THR A CB    1 
ATOM   1506 O  OG1   . THR A 1 197 ? 2.24174   2.97251   -3.25537  1.000 25.75114 ? 197 THR A OG1   1 
ATOM   1507 C  CG2   . THR A 1 197 ? 4.36272   2.76650   -2.13134  1.000 36.55394 ? 197 THR A CG2   1 
ATOM   1508 N  N     . TRP A 1 198 ? 3.20778   1.10851   -6.03536  1.000 24.72711 ? 198 TRP A N     1 
ATOM   1509 C  CA    . TRP A 1 198 ? 2.45979   0.62652   -7.19038  1.000 32.83841 ? 198 TRP A CA    1 
ATOM   1510 C  C     . TRP A 1 198 ? 0.96979   0.92652   -7.08440  1.000 31.90171 ? 198 TRP A C     1 
ATOM   1511 O  O     . TRP A 1 198 ? 0.29481   1.02053   -8.11541  1.000 26.24176 ? 198 TRP A O     1 
ATOM   1512 C  CB    . TRP A 1 198 ? 2.68179   -0.87748  -7.37938  1.000 35.80724 ? 198 TRP A CB    1 
ATOM   1513 C  CG    . TRP A 1 198 ? 2.11577   -1.72848  -6.28039  1.000 33.84739 ? 198 TRP A CG    1 
ATOM   1514 C  CD1   . TRP A 1 198 ? 2.75476   -2.13149  -5.14438  1.000 34.66868 ? 198 TRP A CD1   1 
ATOM   1515 C  CD2   . TRP A 1 198 ? 0.79777   -2.28748  -6.22041  1.000 36.20536 ? 198 TRP A CD2   1 
ATOM   1516 N  NE1   . TRP A 1 198 ? 1.91574   -2.90249  -4.37840  1.000 35.46655 ? 198 TRP A NE1   1 
ATOM   1517 C  CE2   . TRP A 1 198 ? 0.70875   -3.01449  -5.01742  1.000 37.28655 ? 198 TRP A CE2   1 
ATOM   1518 C  CE3   . TRP A 1 198 ? -0.31521  -2.24248  -7.06543  1.000 38.40360 ? 198 TRP A CE3   1 
ATOM   1519 C  CZ2   . TRP A 1 198 ? -0.45025  -3.68849  -4.63744  1.000 34.55834 ? 198 TRP A CZ2   1 
ATOM   1520 C  CZ3   . TRP A 1 198 ? -1.46322  -2.91348  -6.68745  1.000 36.97822 ? 198 TRP A CZ3   1 
ATOM   1521 C  CH2   . TRP A 1 198 ? -1.52224  -3.62648  -5.48345  1.000 34.27311 ? 198 TRP A CH2   1 
ATOM   1522 N  N     . GLN A 1 199 ? 0.44077   1.08252   -5.86841  1.000 34.61915 ? 199 GLN A N     1 
ATOM   1523 C  CA    . GLN A 1 199 ? -0.97423  1.41052   -5.72343  1.000 33.42950 ? 199 GLN A CA    1 
ATOM   1524 C  C     . GLN A 1 199 ? -1.24022  2.86852   -6.07742  1.000 34.71353 ? 199 GLN A C     1 
ATOM   1525 O  O     . GLN A 1 199 ? -2.29421  3.19753   -6.63344  1.000 37.69666 ? 199 GLN A O     1 
ATOM   1526 C  CB    . GLN A 1 199 ? -1.44825  1.12152   -4.29743  1.000 33.14818 ? 199 GLN A CB    1 
ATOM   1527 C  CG    . GLN A 1 199 ? -1.17026  -0.28549  -3.79343  1.000 41.90049 ? 199 GLN A CG    1 
ATOM   1528 C  CD    . GLN A 1 199 ? 0.19373   -0.41549  -3.14441  1.000 31.72945 ? 199 GLN A CD    1 
ATOM   1529 O  OE1   . GLN A 1 199 ? 1.15974   0.21851   -3.56940  1.000 34.22600 ? 199 GLN A OE1   1 
ATOM   1530 N  NE2   . GLN A 1 199 ? 0.27871   -1.23850  -2.10542  1.000 26.04101 ? 199 GLN A NE2   1 
ATOM   1531 N  N     . GLU A 1 200 ? -0.29522  3.75452   -5.75941  1.000 34.43631 ? 200 GLU A N     1 
ATOM   1532 C  CA    . GLU A 1 200 ? -0.49022  5.18252   -5.97240  1.000 33.24357 ? 200 GLU A CA    1 
ATOM   1533 C  C     . GLU A 1 200 ? -0.28719  5.59952   -7.42240  1.000 35.27314 ? 200 GLU A C     1 
ATOM   1534 O  O     . GLU A 1 200 ? -0.74219  6.68253   -7.80740  1.000 34.25808 ? 200 GLU A O     1 
ATOM   1535 C  CB    . GLU A 1 200 ? 0.45577   5.97251   -5.06639  1.000 35.15962 ? 200 GLU A CB    1 
ATOM   1536 C  CG    . GLU A 1 200 ? 0.27775   5.66251   -3.59039  1.000 31.97943 ? 200 GLU A CG    1 
ATOM   1537 C  CD    . GLU A 1 200 ? 1.40973   6.19350   -2.73637  1.000 35.21782 ? 200 GLU A CD    1 
ATOM   1538 O  OE1   . GLU A 1 200 ? 2.27474   6.91951   -3.27236  1.000 37.94556 ? 200 GLU A OE1   1 
ATOM   1539 O  OE2   . GLU A 1 200 ? 1.43572   5.88050   -1.52837  1.000 20.99271 ? 200 GLU A OE2   1 
ATOM   1540 N  N     . VAL A 1 201 ? 0.38082   4.77453   -8.23439  1.000 31.85126 ? 201 VAL A N     1 
ATOM   1541 C  CA    . VAL A 1 201 ? 0.54984   5.08853   -9.65139  1.000 32.03161 ? 201 VAL A CA    1 
ATOM   1542 C  C     . VAL A 1 201 ? -0.62315  4.61454   -10.49541 1.000 36.89979 ? 201 VAL A C     1 
ATOM   1543 O  O     . VAL A 1 201 ? -0.66413  4.90654   -11.70041 1.000 38.60684 ? 201 VAL A O     1 
ATOM   1544 C  CB    . VAL A 1 201 ? 1.85585   4.48953   -10.21037 1.000 34.78562 ? 201 VAL A CB    1 
ATOM   1545 C  CG1   . VAL A 1 201 ? 3.05383   4.99853   -9.42235  1.000 32.40303 ? 201 VAL A CG1   1 
ATOM   1546 C  CG2   . VAL A 1 201 ? 1.79884   2.97253   -10.19138 1.000 33.63826 ? 201 VAL A CG2   1 
ATOM   1547 N  N     . GLY A 1 202 ? -1.57516  3.89154   -9.90943  1.000 30.74351 ? 202 GLY A N     1 
ATOM   1548 C  CA    . GLY A 1 202 ? -2.76715  3.48854   -10.62945 1.000 29.58685 ? 202 GLY A CA    1 
ATOM   1549 C  C     . GLY A 1 202 ? -2.81415  2.02254   -11.00445 1.000 34.72200 ? 202 GLY A C     1 
ATOM   1550 O  O     . GLY A 1 202 ? -3.11113  1.68255   -12.15346 1.000 39.95661 ? 202 GLY A O     1 
ATOM   1551 N  N     . PHE A 1 203 ? -2.53016  1.14054   -10.04945 1.000 35.55345 ? 203 PHE A N     1 
ATOM   1552 C  CA    . PHE A 1 203 ? -2.60716  -0.29546  -10.27046 1.000 35.32127 ? 203 PHE A CA    1 
ATOM   1553 C  C     . PHE A 1 203 ? -3.51618  -0.92846  -9.22847  1.000 36.37396 ? 203 PHE A C     1 
ATOM   1554 O  O     . PHE A 1 203 ? -3.68020  -0.40547  -8.12247  1.000 40.75371 ? 203 PHE A O     1 
ATOM   1555 C  CB    . PHE A 1 203 ? -1.22116  -0.95346  -10.23544 1.000 29.79880 ? 203 PHE A CB    1 
ATOM   1556 C  CG    . PHE A 1 203 ? -0.48114  -0.87546  -11.53943 1.000 28.93657 ? 203 PHE A CG    1 
ATOM   1557 C  CD1   . PHE A 1 203 ? -0.91913  -1.59246  -12.64144 1.000 23.89635 ? 203 PHE A CD1   1 
ATOM   1558 C  CD2   . PHE A 1 203 ? 0.65486   -0.09346  -11.66341 1.000 32.55699 ? 203 PHE A CD2   1 
ATOM   1559 C  CE1   . PHE A 1 203 ? -0.24311  -1.52645  -13.84542 1.000 30.40410 ? 203 PHE A CE1   1 
ATOM   1560 C  CE2   . PHE A 1 203 ? 1.33788   -0.02446  -12.86440 1.000 39.10755 ? 203 PHE A CE2   1 
ATOM   1561 C  CZ    . PHE A 1 203 ? 0.88789   -0.74245  -13.95640 1.000 35.17780 ? 203 PHE A CZ    1 
ATOM   1562 N  N     . LYS A 1 204 ? -4.10518  -2.06546  -9.59449  1.000 34.63054 ? 204 LYS A N     1 
ATOM   1563 C  CA    . LYS A 1 204 ? -5.10319  -2.72946  -8.76750  1.000 40.90176 ? 204 LYS A CA    1 
ATOM   1564 C  C     . LYS A 1 204 ? -4.67420  -4.09546  -8.25450  1.000 42.56710 ? 204 LYS A C     1 
ATOM   1565 O  O     . LYS A 1 204 ? -5.05222  -4.46047  -7.13851  1.000 44.55557 ? 204 LYS A O     1 
ATOM   1566 C  CB    . LYS A 1 204 ? -6.42418  -2.88846  -9.54152  1.000 40.60235 ? 204 LYS A CB    1 
ATOM   1567 C  CG    . LYS A 1 204 ? -7.32218  -1.65046  -9.55353  1.000 38.40812 ? 204 LYS A CG    1 
ATOM   1568 C  CD    . LYS A 1 204 ? -6.73416  -0.51345  -10.37752 0.000 39.84068 ? 204 LYS A CD    1 
ATOM   1569 C  CE    . LYS A 1 204 ? -6.42214  -0.96045  -11.79752 0.000 39.96670 ? 204 LYS A CE    1 
ATOM   1570 N  NZ    . LYS A 1 204 ? -5.73013  0.10555   -12.57450 0.000 39.37432 ? 204 LYS A NZ    1 
ATOM   1571 N  N     . GLU A 1 205 ? -3.90519  -4.86046  -9.02849  1.000 45.46422 ? 205 GLU A N     1 
ATOM   1572 C  CA    . GLU A 1 205 ? -3.46020  -6.17647  -8.59849  1.000 40.88303 ? 205 GLU A CA    1 
ATOM   1573 C  C     . GLU A 1 205 ? -1.98020  -6.14247  -8.25747  1.000 32.08739 ? 205 GLU A C     1 
ATOM   1574 O  O     . GLU A 1 205 ? -1.18619  -5.57547  -9.02045  1.000 20.68129 ? 205 GLU A O     1 
ATOM   1575 C  CB    . GLU A 1 205 ? -3.72218  -7.22446  -9.68750  1.000 42.60998 ? 205 GLU A CB    1 
ATOM   1576 C  CG    . GLU A 1 205 ? -5.18818  -7.36746  -10.06852 1.000 42.24789 ? 205 GLU A CG    1 
ATOM   1577 C  CD    . GLU A 1 205 ? -5.44717  -8.56045  -10.96953 1.000 46.63121 ? 205 GLU A CD    1 
ATOM   1578 O  OE1   . GLU A 1 205 ? -4.68217  -9.54446  -10.89252 1.000 49.33858 ? 205 GLU A OE1   1 
ATOM   1579 O  OE2   . GLU A 1 205 ? -6.41615  -8.51245  -11.75754 1.000 44.83287 ? 205 GLU A OE2   1 
ATOM   1580 N  N     . PRO A 1 206 ? -1.57322  -6.73447  -7.13946  1.000 37.41702 ? 206 PRO A N     1 
ATOM   1581 C  CA    . PRO A 1 206 ? -0.17023  -6.65848  -6.71844  1.000 29.79350 ? 206 PRO A CA    1 
ATOM   1582 C  C     . PRO A 1 206 ? 0.72178   -7.48748  -7.62343  1.000 31.43918 ? 206 PRO A C     1 
ATOM   1583 O  O     . PRO A 1 206 ? 0.25079   -8.42147  -8.29044  1.000 31.78185 ? 206 PRO A O     1 
ATOM   1584 C  CB    . PRO A 1 206 ? -0.20125  -7.22748  -5.29244  1.000 28.39555 ? 206 PRO A CB    1 
ATOM   1585 C  CG    . PRO A 1 206 ? -1.37525  -8.14448  -5.29147  1.000 33.40144 ? 206 PRO A CG    1 
ATOM   1586 C  CD    . PRO A 1 206 ? -2.39624  -7.50148  -6.18748  1.000 33.81130 ? 206 PRO A CD    1 
ATOM   1587 N  N     . PRO A 1 207 ? 2.01579   -7.17548  -7.67841  1.000 28.13181 ? 207 PRO A N     1 
ATOM   1588 C  CA    . PRO A 1 207 ? 2.92880   -7.97548  -8.49940  1.000 29.41002 ? 207 PRO A CA    1 
ATOM   1589 C  C     . PRO A 1 207 ? 3.13879   -9.36148  -7.91040  1.000 30.84351 ? 207 PRO A C     1 
ATOM   1590 O  O     . PRO A 1 207 ? 2.98377   -9.58348  -6.70740  1.000 32.05258 ? 207 PRO A O     1 
ATOM   1591 C  CB    . PRO A 1 207 ? 4.22680   -7.16048  -8.48038  1.000 24.58793 ? 207 PRO A CB    1 
ATOM   1592 C  CG    . PRO A 1 207 ? 4.15678   -6.38248  -7.21238  1.000 27.00500 ? 207 PRO A CG    1 
ATOM   1593 C  CD    . PRO A 1 207 ? 2.70378   -6.05548  -7.01440  1.000 32.06016 ? 207 PRO A CD    1 
ATOM   1594 N  N     . LEU A 1 208 ? 3.49980   -10.30148 -8.78240  1.000 26.42931 ? 208 LEU A N     1 
ATOM   1595 C  CA    . LEU A 1 208 ? 3.69079   -11.68948 -8.39140  1.000 27.09269 ? 208 LEU A CA    1 
ATOM   1596 C  C     . LEU A 1 208 ? 5.10379   -12.19548 -8.65038  1.000 23.15368 ? 208 LEU A C     1 
ATOM   1597 O  O     . LEU A 1 208 ? 5.37579   -13.37548 -8.40638  1.000 32.06677 ? 208 LEU A O     1 
ATOM   1598 C  CB    . LEU A 1 208 ? 2.68680   -12.59047 -9.12342  1.000 28.82333 ? 208 LEU A CB    1 
ATOM   1599 C  CG    . LEU A 1 208 ? 1.21680   -12.16647 -9.06644  1.000 30.38032 ? 208 LEU A CG    1 
ATOM   1600 C  CD1   . LEU A 1 208 ? 0.34481   -13.12147 -9.86846  1.000 33.58529 ? 208 LEU A CD1   1 
ATOM   1601 C  CD2   . LEU A 1 208 ? 0.73278   -12.07248 -7.62745  1.000 34.77626 ? 208 LEU A CD2   1 
ATOM   1602 N  N     . THR A 1 209 ? 6.00480   -11.34348 -9.13336  1.000 22.16024 ? 209 THR A N     1 
ATOM   1603 C  CA    . THR A 1 209 ? 7.34581   -11.78748 -9.48135  1.000 25.70873 ? 209 THR A CA    1 
ATOM   1604 C  C     . THR A 1 209 ? 8.16579   -12.06949 -8.22433  1.000 26.39273 ? 209 THR A C     1 
ATOM   1605 O  O     . THR A 1 209 ? 7.86977   -11.58449 -7.12834  1.000 21.86679 ? 209 THR A O     1 
ATOM   1606 C  CB    . THR A 1 209 ? 8.05082   -10.73848 -10.34733 1.000 24.30653 ? 209 THR A CB    1 
ATOM   1607 O  OG1   . THR A 1 209 ? 9.30683   -11.25648 -10.80531 1.000 20.94465 ? 209 THR A OG1   1 
ATOM   1608 C  CG2   . THR A 1 209 ? 8.29281   -9.46248  -9.55632  1.000 25.01104 ? 209 THR A CG2   1 
ATOM   1609 N  N     . VAL A 1 210 ? 9.21579   -12.87149 -8.40032  1.000 27.04648 ? 210 VAL A N     1 
ATOM   1610 C  CA    . VAL A 1 210 ? 10.09477  -13.25549 -7.30231  1.000 28.35918 ? 210 VAL A CA    1 
ATOM   1611 C  C     . VAL A 1 210 ? 11.43377  -12.53450 -7.36829  1.000 23.04291 ? 210 VAL A C     1 
ATOM   1612 O  O     . VAL A 1 210 ? 12.32376  -12.82050 -6.56527  1.000 25.18487 ? 210 VAL A O     1 
ATOM   1613 C  CB    . VAL A 1 210 ? 10.29477  -14.77850 -7.26631  1.000 30.36476 ? 210 VAL A CB    1 
ATOM   1614 C  CG1   . VAL A 1 210 ? 8.94976   -15.47849 -7.12633  1.000 21.02845 ? 210 VAL A CG1   1 
ATOM   1615 C  CG2   . VAL A 1 210 ? 11.00678  -15.25249 -8.52630  1.000 24.87510 ? 210 VAL A CG2   1 
ATOM   1616 N  N     . PHE A 1 211 ? 11.59479  -11.60249 -8.30428  1.000 25.07745 ? 211 PHE A N     1 
ATOM   1617 C  CA    . PHE A 1 211 ? 12.84179  -10.87550 -8.49726  1.000 23.52646 ? 211 PHE A CA    1 
ATOM   1618 C  C     . PHE A 1 211 ? 12.65479  -9.43550  -8.03726  1.000 24.49342 ? 211 PHE A C     1 
ATOM   1619 O  O     . PHE A 1 211 ? 11.86180  -8.68949  -8.62327  1.000 23.73516 ? 211 PHE A O     1 
ATOM   1620 C  CB    . PHE A 1 211 ? 13.28081  -10.92749 -9.96125  1.000 27.86127 ? 211 PHE A CB    1 
ATOM   1621 C  CG    . PHE A 1 211 ? 13.30082  -12.31449 -10.53726 1.000 25.37089 ? 211 PHE A CG    1 
ATOM   1622 C  CD1   . PHE A 1 211 ? 14.25681  -13.23249 -10.13325 1.000 25.69974 ? 211 PHE A CD1   1 
ATOM   1623 C  CD2   . PHE A 1 211 ? 12.36383  -12.70248 -11.48027 1.000 26.93098 ? 211 PHE A CD2   1 
ATOM   1624 C  CE1   . PHE A 1 211 ? 14.27582  -14.51049 -10.65625 1.000 20.38217 ? 211 PHE A CE1   1 
ATOM   1625 C  CE2   . PHE A 1 211 ? 12.37884  -13.98048 -12.00928 1.000 25.00553 ? 211 PHE A CE2   1 
ATOM   1626 C  CZ    . PHE A 1 211 ? 13.33783  -14.88549 -11.59527 1.000 18.27134 ? 211 PHE A CZ    1 
ATOM   1627 N  N     . LYS A 1 212 ? 13.38877  -9.05150  -6.99524  1.000 24.63111 ? 212 LYS A N     1 
ATOM   1628 C  CA    . LYS A 1 212 ? 13.31677  -7.70750  -6.43924  1.000 21.63338 ? 212 LYS A CA    1 
ATOM   1629 C  C     . LYS A 1 212 ? 14.35678  -6.81850  -7.11122  1.000 21.89550 ? 212 LYS A C     1 
ATOM   1630 O  O     . LYS A 1 212 ? 15.52178  -7.20850  -7.24320  1.000 25.98086 ? 212 LYS A O     1 
ATOM   1631 C  CB    . LYS A 1 212 ? 13.54274  -7.74051  -4.92624  1.000 25.78826 ? 212 LYS A CB    1 
ATOM   1632 C  CG    . LYS A 1 212 ? 12.62173  -8.69751  -4.18325  1.000 29.21505 ? 212 LYS A CG    1 
ATOM   1633 C  CD    . LYS A 1 212 ? 11.23973  -8.09751  -3.96927  1.000 24.82734 ? 212 LYS A CD    1 
ATOM   1634 C  CE    . LYS A 1 212 ? 11.22771  -7.15551  -2.77727  0.000 26.75577 ? 212 LYS A CE    1 
ATOM   1635 N  NZ    . LYS A 1 212 ? 11.52269  -7.87452  -1.50627  0.000 27.90900 ? 212 LYS A NZ    1 
ATOM   1636 N  N     . GLY A 1 213 ? 13.93479  -5.62750  -7.53522  1.000 21.68930 ? 213 GLY A N     1 
ATOM   1637 C  CA    . GLY A 1 213 ? 14.84180  -4.72350  -8.20421  1.000 23.49535 ? 213 GLY A CA    1 
ATOM   1638 C  C     . GLY A 1 213 ? 15.74879  -3.97651  -7.24519  1.000 26.60716 ? 213 GLY A C     1 
ATOM   1639 O  O     . GLY A 1 213 ? 15.49977  -3.88951  -6.04219  1.000 26.74772 ? 213 GLY A O     1 
ATOM   1640 N  N     . GLY A 1 214 ? 16.82779  -3.43050  -7.80017  1.000 23.39751 ? 214 GLY A N     1 
ATOM   1641 C  CA    . GLY A 1 214 ? 17.75478  -2.63951  -7.01515  1.000 18.57768 ? 214 GLY A CA    1 
ATOM   1642 C  C     . GLY A 1 214 ? 19.21279  -2.97151  -7.25413  1.000 22.45112 ? 214 GLY A C     1 
ATOM   1643 O  O     . GLY A 1 214 ? 19.54579  -4.06551  -7.72013  1.000 22.47902 ? 214 GLY A O     1 
ATOM   1644 N  N     . GLU A 1 215 ? 20.09478  -2.02251  -6.93412  1.000 25.92587 ? 215 GLU A N     1 
ATOM   1645 C  CA    . GLU A 1 215 ? 21.52679  -2.25652  -7.08710  1.000 20.03312 ? 215 GLU A CA    1 
ATOM   1646 C  C     . GLU A 1 215 ? 22.04277  -3.22952  -6.03409  1.000 23.02528 ? 215 GLU A C     1 
ATOM   1647 O  O     . GLU A 1 215 ? 22.88377  -4.08652  -6.33308  1.000 20.71465 ? 215 GLU A O     1 
ATOM   1648 C  CB    . GLU A 1 215 ? 22.28279  -0.92952  -7.00908  1.000 25.45160 ? 215 GLU A CB    1 
ATOM   1649 C  CG    . GLU A 1 215 ? 23.78779  -1.05252  -7.17406  1.000 21.32223 ? 215 GLU A CG    1 
ATOM   1650 C  CD    . GLU A 1 215 ? 24.49979  0.26548   -6.95104  1.000 17.36409 ? 215 GLU A CD    1 
ATOM   1651 O  OE1   . GLU A 1 215 ? 23.85778  1.20448   -6.43605  1.000 19.59991 ? 215 GLU A OE1   1 
ATOM   1652 O  OE2   . GLU A 1 215 ? 25.69679  0.36348   -7.29002  1.000 14.60400 ? 215 GLU A OE2   1 
ATOM   1653 N  N     . THR A 1 216 ? 21.55475  -3.11252  -4.79710  1.000 19.38806 ? 216 THR A N     1 
ATOM   1654 C  CA    . THR A 1 216 ? 21.97273  -4.03353  -3.74509  1.000 17.80738 ? 216 THR A CA    1 
ATOM   1655 C  C     . THR A 1 216 ? 21.56973  -5.46453  -4.07811  1.000 21.08087 ? 216 THR A C     1 
ATOM   1656 O  O     . THR A 1 216 ? 22.32873  -6.40753  -3.82410  1.000 22.60134 ? 216 THR A O     1 
ATOM   1657 C  CB    . THR A 1 216 ? 21.37571  -3.60553  -2.40210  1.000 19.86885 ? 216 THR A CB    1 
ATOM   1658 O  OG1   . THR A 1 216 ? 21.72271  -2.24053  -2.13609  1.000 17.15831 ? 216 THR A OG1   1 
ATOM   1659 C  CG2   . THR A 1 216 ? 21.90369  -4.48354  -1.27710  1.000 19.96931 ? 216 THR A CG2   1 
ATOM   1660 N  N     . GLU A 1 217 ? 20.37774  -5.64552  -4.65312  1.000 21.12182 ? 217 GLU A N     1 
ATOM   1661 C  CA    . GLU A 1 217 ? 19.96075  -6.97552  -5.08314  1.000 21.94379 ? 217 GLU A CA    1 
ATOM   1662 C  C     . GLU A 1 217 ? 20.72576  -7.43452  -6.31713  1.000 19.92457 ? 217 GLU A C     1 
ATOM   1663 O  O     . GLU A 1 217 ? 20.92877  -8.63952  -6.50513  1.000 26.46887 ? 217 GLU A O     1 
ATOM   1664 C  CB    . GLU A 1 217 ? 18.45575  -6.99352  -5.35516  1.000 22.82462 ? 217 GLU A CB    1 
ATOM   1665 C  CG    . GLU A 1 217 ? 17.59273  -7.06152  -4.10417  1.000 21.78952 ? 217 GLU A CG    1 
ATOM   1666 C  CD    . GLU A 1 217 ? 17.52272  -8.45852  -3.51618  1.000 26.57746 ? 217 GLU A CD    1 
ATOM   1667 O  OE1   . GLU A 1 217 ? 18.00473  -9.40652  -4.16917  1.000 23.98221 ? 217 GLU A OE1   1 
ATOM   1668 O  OE2   . GLU A 1 217 ? 16.98070  -8.60852  -2.40119  1.000 34.93725 ? 217 GLU A OE2   1 
ATOM   1669 N  N     . ALA A 1 218 ? 21.15578  -6.49752  -7.16512  1.000 16.45030 ? 218 ALA A N     1 
ATOM   1670 C  CA    . ALA A 1 218 ? 21.91080  -6.87151  -8.35711  1.000 22.41625 ? 218 ALA A CA    1 
ATOM   1671 C  C     . ALA A 1 218 ? 23.31779  -7.32952  -7.99809  1.000 19.53126 ? 218 ALA A C     1 
ATOM   1672 O  O     . ALA A 1 218 ? 23.79980  -8.34351  -8.51808  1.000 21.25346 ? 218 ALA A O     1 
ATOM   1673 C  CB    . ALA A 1 218 ? 21.96181  -5.70051  -9.33810  1.000 21.49362 ? 218 ALA A CB    1 
ATOM   1674 N  N     . LEU A 1 219 ? 23.99378  -6.59252  -7.11307  1.000 22.82342 ? 219 LEU A N     1 
ATOM   1675 C  CA    . LEU A 1 219 ? 25.33777  -6.97752  -6.70005  1.000 23.43397 ? 219 LEU A CA    1 
ATOM   1676 C  C     . LEU A 1 219 ? 25.33176  -8.27953  -5.90906  1.000 20.55113 ? 219 LEU A C     1 
ATOM   1677 O  O     . LEU A 1 219 ? 26.32176  -9.01953  -5.93105  1.000 19.03686 ? 219 LEU A O     1 
ATOM   1678 C  CB    . LEU A 1 219 ? 25.97076  -5.85553  -5.87604  1.000 18.44885 ? 219 LEU A CB    1 
ATOM   1679 C  CG    . LEU A 1 219 ? 26.09277  -4.49953  -6.57603  1.000 17.46285 ? 219 LEU A CG    1 
ATOM   1680 C  CD1   . LEU A 1 219 ? 26.47076  -3.41153  -5.58302  1.000 20.91165 ? 219 LEU A CD1   1 
ATOM   1681 C  CD2   . LEU A 1 219 ? 27.10379  -4.56952  -7.71002  1.000 20.56118 ? 219 LEU A CD2   1 
ATOM   1682 N  N     . ALA A 1 220 ? 24.23275  -8.57553  -5.21208  1.000 15.63878 ? 220 ALA A N     1 
ATOM   1683 C  CA    . ALA A 1 220 ? 24.15173  -9.82153  -4.45808  1.000 20.41985 ? 220 ALA A CA    1 
ATOM   1684 C  C     . ALA A 1 220 ? 23.97074  -11.01653 -5.38509  1.000 16.80490 ? 220 ALA A C     1 
ATOM   1685 O  O     . ALA A 1 220 ? 24.57874  -12.07153 -5.17208  1.000 27.33190 ? 220 ALA A O     1 
ATOM   1686 C  CB    . ALA A 1 220 ? 23.01172  -9.74953  -3.44310  1.000 21.19388 ? 220 ALA A CB    1 
ATOM   1687 N  N     . ARG A 1 221 ? 23.13806  -10.87259 -6.41846  1.000 25.27438 ? 221 ARG A N     1 
ATOM   1688 C  CA    . ARG A 1 221 ? 22.95712  -11.95358 -7.37910  1.000 26.08319 ? 221 ARG A CA    1 
ATOM   1689 C  C     . ARG A 1 221 ? 24.18190  -12.14343 -8.26281  1.000 21.20373 ? 221 ARG A C     1 
ATOM   1690 O  O     . ARG A 1 221 ? 24.36912  -13.23145 -8.81782  1.000 22.54603 ? 221 ARG A O     1 
ATOM   1691 C  CB    . ARG A 1 221 ? 21.72128  -11.69173 -8.24207  1.000 23.03015 ? 221 ARG A CB    1 
ATOM   1692 C  CG    . ARG A 1 221 ? 21.20117  -12.92411 -8.96417  1.000 18.63029 ? 221 ARG A CG    1 
ATOM   1693 C  CD    . ARG A 1 221 ? 19.86942  -12.65399 -9.64327  1.000 18.88880 ? 221 ARG A CD    1 
ATOM   1694 N  NE    . ARG A 1 221 ? 19.24393  -13.88828 -10.10104 1.000 17.53017 ? 221 ARG A NE    1 
ATOM   1695 C  CZ    . ARG A 1 221 ? 18.42984  -14.63154 -9.36413  1.000 19.69429 ? 221 ARG A CZ    1 
ATOM   1696 N  NH1   . ARG A 1 221 ? 18.10369  -14.28366 -8.13031  1.000 20.81344 ? 221 ARG A NH1   1 
ATOM   1697 N  NH2   . ARG A 1 221 ? 17.93135  -15.75267 -9.87743  1.000 18.74437 ? 221 ARG A NH2   1 
ATOM   1698 N  N     . LEU A 1 222 ? 25.01679  -11.11252 -8.40507  1.000 21.37937 ? 222 LEU A N     1 
ATOM   1699 C  CA    . LEU A 1 222 ? 26.25380  -11.26152 -9.16306  1.000 24.14659 ? 222 LEU A CA    1 
ATOM   1700 C  C     . LEU A 1 222 ? 27.25379  -12.12452 -8.40404  1.000 23.61802 ? 222 LEU A C     1 
ATOM   1701 O  O     . LEU A 1 222 ? 27.83879  -13.05752 -8.96704  1.000 22.55769 ? 222 LEU A O     1 
ATOM   1702 C  CB    . LEU A 1 222 ? 26.84781  -9.88752  -9.47004  1.000 21.52780 ? 222 LEU A CB    1 
ATOM   1703 C  CG    . LEU A 1 222 ? 28.06082  -9.85652  -10.40302 1.000 23.72694 ? 222 LEU A CG    1 
ATOM   1704 C  CD1   . LEU A 1 222 ? 27.66684  -10.27751 -11.81103 1.000 18.01755 ? 222 LEU A CD1   1 
ATOM   1705 C  CD2   . LEU A 1 222 ? 28.70483  -8.47952  -10.40701 1.000 19.17481 ? 222 LEU A CD2   1 
ATOM   1706 N  N     . GLU A 1 223 ? 27.45977  -11.82853 -7.11704  1.000 26.89659 ? 223 GLU A N     1 
ATOM   1707 C  CA    . GLU A 1 223 ? 28.38076  -12.62453 -6.31303  1.000 21.15183 ? 223 GLU A CA    1 
ATOM   1708 C  C     . GLU A 1 223 ? 27.88975  -14.05553 -6.14804  1.000 25.79340 ? 223 GLU A C     1 
ATOM   1709 O  O     . GLU A 1 223 ? 28.70275  -14.98353 -6.06303  1.000 25.06813 ? 223 GLU A O     1 
ATOM   1710 C  CB    . GLU A 1 223 ? 28.58374  -11.97054 -4.94402  1.000 26.43483 ? 223 GLU A CB    1 
ATOM   1711 C  CG    . GLU A 1 223 ? 29.28974  -10.62254 -4.99001  1.000 27.95467 ? 223 GLU A CG    1 
ATOM   1712 C  CD    . GLU A 1 223 ? 30.77174  -10.74454 -5.29798  1.000 30.56315 ? 223 GLU A CD    1 
ATOM   1713 O  OE1   . GLU A 1 223 ? 31.30674  -11.87154 -5.22798  1.000 32.54239 ? 223 GLU A OE1   1 
ATOM   1714 O  OE2   . GLU A 1 223 ? 31.40175  -9.71154  -5.60697  1.000 23.57462 ? 223 GLU A OE2   1 
ATOM   1715 N  N     . ALA A 1 224 ? 26.56975  -14.25453 -6.09706  1.000 24.97555 ? 224 ALA A N     1 
ATOM   1716 C  CA    . ALA A 1 224 ? 26.03275  -15.60853 -6.01707  1.000 23.74484 ? 224 ALA A CA    1 
ATOM   1717 C  C     . ALA A 1 224 ? 26.32976  -16.39452 -7.28807  1.000 24.32335 ? 224 ALA A C     1 
ATOM   1718 O  O     . ALA A 1 224 ? 26.59776  -17.60052 -7.23107  1.000 24.19844 ? 224 ALA A O     1 
ATOM   1719 C  CB    . ALA A 1 224 ? 24.52874  -15.56153 -5.75110  1.000 29.29931 ? 224 ALA A CB    1 
ATOM   1720 N  N     . ALA A 1 225 ? 26.28978  -15.72752 -8.44407  1.000 24.14575 ? 225 ALA A N     1 
ATOM   1721 C  CA    . ALA A 1 225 ? 26.62980  -16.39852 -9.69307  1.000 25.13210 ? 225 ALA A CA    1 
ATOM   1722 C  C     . ALA A 1 225 ? 28.11780  -16.70752 -9.77605  1.000 25.67121 ? 225 ALA A C     1 
ATOM   1723 O  O     . ALA A 1 225 ? 28.50881  -17.69452 -10.40904 1.000 35.25476 ? 225 ALA A O     1 
ATOM   1724 C  CB    . ALA A 1 225 ? 26.19682  -15.54251 -10.88507 1.000 27.51719 ? 225 ALA A CB    1 
ATOM   1725 N  N     . PHE A 1 226 ? 28.95679  -15.88852 -9.14703  1.000 28.12889 ? 226 PHE A N     1 
ATOM   1726 C  CA    . PHE A 1 226 ? 30.39879  -16.09052 -9.14501  1.000 24.35339 ? 226 PHE A CA    1 
ATOM   1727 C  C     . PHE A 1 226 ? 30.88777  -16.87753 -7.93500  1.000 25.45076 ? 226 PHE A C     1 
ATOM   1728 O  O     . PHE A 1 226 ? 32.09977  -16.95053 -7.70999  1.000 27.22065 ? 226 PHE A O     1 
ATOM   1729 C  CB    . PHE A 1 226 ? 31.11980  -14.74053 -9.21299  1.000 23.52353 ? 226 PHE A CB    1 
ATOM   1730 C  CG    . PHE A 1 226 ? 31.14282  -14.13552 -10.58699 1.000 21.35703 ? 226 PHE A CG    1 
ATOM   1731 C  CD1   . PHE A 1 226 ? 30.05083  -13.43552 -11.07000 1.000 28.06687 ? 226 PHE A CD1   1 
ATOM   1732 C  CD2   . PHE A 1 226 ? 32.25883  -14.26552 -11.39597 1.000 25.23707 ? 226 PHE A CD2   1 
ATOM   1733 C  CE1   . PHE A 1 226 ? 30.07085  -12.87851 -12.33300 1.000 30.29888 ? 226 PHE A CE1   1 
ATOM   1734 C  CE2   . PHE A 1 226 ? 32.28485  -13.70952 -12.65997 1.000 22.03545 ? 226 PHE A CE2   1 
ATOM   1735 C  CZ    . PHE A 1 226 ? 31.18886  -13.01551 -13.12899 1.000 25.33536 ? 226 PHE A CZ    1 
ATOM   1736 N  N     . GLN A 1 227 ? 29.97976  -17.46253 -7.15002  1.000 29.22166 ? 227 GLN A N     1 
ATOM   1737 C  CA    . GLN A 1 227 ? 30.40774  -18.29354 -6.03002  1.000 33.01016 ? 227 GLN A CA    1 
ATOM   1738 C  C     . GLN A 1 227 ? 31.06775  -19.57854 -6.50801  1.000 29.72014 ? 227 GLN A C     1 
ATOM   1739 O  O     . GLN A 1 227 ? 31.94173  -20.11954 -5.82000  1.000 24.23394 ? 227 GLN A O     1 
ATOM   1740 C  CB    . GLN A 1 227 ? 29.22073  -18.60854 -5.12004  1.000 31.84960 ? 227 GLN A CB    1 
ATOM   1741 C  CG    . GLN A 1 227 ? 28.93671  -17.53354 -4.08504  1.000 30.52160 ? 227 GLN A CG    1 
ATOM   1742 C  CD    . GLN A 1 227 ? 30.06770  -17.38255 -3.08502  1.000 40.03325 ? 227 GLN A CD    1 
ATOM   1743 O  OE1   . GLN A 1 227 ? 30.69769  -18.36355 -2.69001  1.000 36.86411 ? 227 GLN A OE1   1 
ATOM   1744 N  NE2   . GLN A 1 227 ? 30.33469  -16.14755 -2.67501  1.000 38.96229 ? 227 GLN A NE2   1 
ATOM   1745 N  N     . ASP A 1 228 ? 30.66576  -20.08053 -7.67602  1.000 28.65572 ? 228 ASP A N     1 
ATOM   1746 C  CA    . ASP A 1 228 ? 31.28077  -21.24953 -8.30001  1.000 26.75144 ? 228 ASP A CA    1 
ATOM   1747 C  C     . ASP A 1 228 ? 31.97679  -20.80453 -9.57900  1.000 21.89398 ? 228 ASP A C     1 
ATOM   1748 O  O     . ASP A 1 228 ? 31.33881  -20.70452 -10.63801 1.000 25.15205 ? 228 ASP A O     1 
ATOM   1749 C  CB    . ASP A 1 228 ? 30.23477  -22.32653 -8.59903  1.000 22.67549 ? 228 ASP A CB    1 
ATOM   1750 C  CG    . ASP A 1 228 ? 30.85478  -23.63553 -9.05203  1.000 19.00204 ? 228 ASP A CG    1 
ATOM   1751 O  OD1   . ASP A 1 228 ? 32.08477  -23.79753 -8.90601  1.000 28.63723 ? 228 ASP A OD1   1 
ATOM   1752 O  OD2   . ASP A 1 228 ? 30.11278  -24.50152 -9.55904  1.000 21.04927 ? 228 ASP A OD2   1 
ATOM   1753 N  N     . PRO A 1 229 ? 33.27879  -20.51053 -9.53398  1.000 28.20382 ? 229 PRO A N     1 
ATOM   1754 C  CA    . PRO A 1 229 ? 33.95981  -20.04553 -10.75297 1.000 27.51471 ? 229 PRO A CA    1 
ATOM   1755 C  C     . PRO A 1 229 ? 34.02882  -21.09652 -11.84697 1.000 23.33906 ? 229 PRO A C     1 
ATOM   1756 O  O     . PRO A 1 229 ? 34.13184  -20.73752 -13.02597 1.000 25.42399 ? 229 PRO A O     1 
ATOM   1757 C  CB    . PRO A 1 229 ? 35.35680  -19.66353 -10.24795 1.000 21.54165 ? 229 PRO A CB    1 
ATOM   1758 C  CG    . PRO A 1 229 ? 35.54878  -20.48753 -9.01395  1.000 19.43360 ? 229 PRO A CG    1 
ATOM   1759 C  CD    . PRO A 1 229 ? 34.18977  -20.58653 -8.37997  1.000 25.21747 ? 229 PRO A CD    1 
ATOM   1760 N  N     . LYS A 1 230 ? 33.98382  -22.38452 -11.49698 1.000 24.20775 ? 230 LYS A N     1 
ATOM   1761 C  CA    . LYS A 1 230 ? 33.98583  -23.42252 -12.52098 1.000 25.08530 ? 230 LYS A CA    1 
ATOM   1762 C  C     . LYS A 1 230 ? 32.69884  -23.40751 -13.33400 1.000 22.90647 ? 230 LYS A C     1 
ATOM   1763 O  O     . LYS A 1 230 ? 32.72286  -23.69651 -14.53600 1.000 29.58595 ? 230 LYS A O     1 
ATOM   1764 C  CB    . LYS A 1 230 ? 34.19782  -24.79352 -11.87898 1.000 23.40182 ? 230 LYS A CB    1 
ATOM   1765 C  CG    . LYS A 1 230 ? 35.55181  -24.95653 -11.20596 1.000 30.18217 ? 230 LYS A CG    1 
ATOM   1766 C  CD    . LYS A 1 230 ? 35.72180  -26.35353 -10.62896 1.000 29.77816 ? 230 LYS A CD    1 
ATOM   1767 C  CE    . LYS A 1 230 ? 37.08379  -26.51353 -9.97394  0.000 32.13290 ? 230 LYS A CE    1 
ATOM   1768 N  NZ    . LYS A 1 230 ? 37.27177  -27.87554 -9.40395  0.000 33.20561 ? 230 LYS A NZ    1 
ATOM   1769 N  N     . TRP A 1 231 ? 31.56983  -23.07451 -12.70302 1.000 23.75732 ? 231 TRP A N     1 
ATOM   1770 C  CA    . TRP A 1 231 ? 30.31885  -22.95251 -13.44303 1.000 23.31165 ? 231 TRP A CA    1 
ATOM   1771 C  C     . TRP A 1 231 ? 30.33986  -21.75251 -14.37903 1.000 24.01231 ? 231 TRP A C     1 
ATOM   1772 O  O     . TRP A 1 231 ? 29.73888  -21.79850 -15.45804 1.000 23.32626 ? 231 TRP A O     1 
ATOM   1773 C  CB    . TRP A 1 231 ? 29.14083  -22.84951 -12.47305 1.000 23.28795 ? 231 TRP A CB    1 
ATOM   1774 C  CG    . TRP A 1 231 ? 27.81584  -22.65151 -13.14807 1.000 23.40571 ? 231 TRP A CG    1 
ATOM   1775 C  CD1   . TRP A 1 231 ? 26.94685  -23.62350 -13.54709 1.000 19.49352 ? 231 TRP A CD1   1 
ATOM   1776 C  CD2   . TRP A 1 231 ? 27.20785  -21.40150 -13.49808 1.000 24.30265 ? 231 TRP A CD2   1 
ATOM   1777 N  NE1   . TRP A 1 231 ? 25.83686  -23.05850 -14.12610 1.000 22.44473 ? 231 TRP A NE1   1 
ATOM   1778 C  CE2   . TRP A 1 231 ? 25.97286  -21.69450 -14.10910 1.000 24.28406 ? 231 TRP A CE2   1 
ATOM   1779 C  CE3   . TRP A 1 231 ? 27.58885  -20.06350 -13.35507 1.000 26.50509 ? 231 TRP A CE3   1 
ATOM   1780 C  CZ2   . TRP A 1 231 ? 25.11687  -20.70050 -14.57611 1.000 17.42993 ? 231 TRP A CZ2   1 
ATOM   1781 C  CZ3   . TRP A 1 231 ? 26.73786  -19.07850 -13.82108 1.000 26.37674 ? 231 TRP A CZ3   1 
ATOM   1782 C  CH2   . TRP A 1 231 ? 25.51587  -19.40150 -14.42310 1.000 18.78846 ? 231 TRP A CH2   1 
ATOM   1783 N  N     . VAL A 1 232 ? 31.02186  -20.67551 -13.98302 1.000 26.88712 ? 232 VAL A N     1 
ATOM   1784 C  CA    . VAL A 1 232 ? 31.06987  -19.47351 -14.81001 1.000 22.13597 ? 232 VAL A CA    1 
ATOM   1785 C  C     . VAL A 1 232 ? 31.92289  -19.71250 -16.05000 1.000 20.60895 ? 232 VAL A C     1 
ATOM   1786 O  O     . VAL A 1 232 ? 31.53491  -19.35550 -17.16900 1.000 32.13229 ? 232 VAL A O     1 
ATOM   1787 C  CB    . VAL A 1 232 ? 31.58986  -18.28151 -13.98700 1.000 26.23587 ? 232 VAL A CB    1 
ATOM   1788 C  CG1   . VAL A 1 232 ? 31.95388  -17.12151 -14.89799 1.000 21.38083 ? 232 VAL A CG1   1 
ATOM   1789 C  CG2   . VAL A 1 232 ? 30.55085  -17.85051 -12.96501 1.000 25.71844 ? 232 VAL A CG2   1 
ATOM   1790 N  N     . ALA A 1 233 ? 33.09689  -20.32251 -15.87098 1.000 23.58174 ? 233 ALA A N     1 
ATOM   1791 C  CA    . ALA A 1 233 ? 34.00890  -20.51850 -16.99297 1.000 24.97240 ? 233 ALA A CA    1 
ATOM   1792 C  C     . ALA A 1 233 ? 33.45792  -21.52650 -17.99298 1.000 24.59620 ? 233 ALA A C     1 
ATOM   1793 O  O     . ALA A 1 233 ? 33.59694  -21.34249 -19.20798 1.000 21.15906 ? 233 ALA A O     1 
ATOM   1794 C  CB    . ALA A 1 233 ? 35.37890  -20.96251 -16.48295 1.000 22.74886 ? 233 ALA A CB    1 
ATOM   1795 N  N     . GLY A 1 234 ? 32.82791  -22.59450 -17.50800 1.000 27.17510 ? 234 GLY A N     1 
ATOM   1796 C  CA    . GLY A 1 234 ? 32.30192  -23.61950 -18.38601 1.000 31.71805 ? 234 GLY A CA    1 
ATOM   1797 C  C     . GLY A 1 234 ? 30.86993  -23.38049 -18.81703 1.000 20.55791 ? 234 GLY A C     1 
ATOM   1798 O  O     . GLY A 1 234 ? 30.15293  -24.32549 -19.15804 1.000 20.98975 ? 234 GLY A O     1 
ATOM   1799 N  N     . PHE A 1 235 ? 30.44293  -22.12049 -18.81103 1.000 24.07539 ? 235 PHE A N     1 
ATOM   1800 C  CA    . PHE A 1 235 ? 29.07394  -21.79049 -19.18405 1.000 25.07011 ? 235 PHE A CA    1 
ATOM   1801 C  C     . PHE A 1 235 ? 28.86796  -21.97748 -20.68305 1.000 20.28023 ? 235 PHE A C     1 
ATOM   1802 O  O     . PHE A 1 235 ? 29.60397  -21.41448 -21.49804 1.000 21.74243 ? 235 PHE A O     1 
ATOM   1803 C  CB    . PHE A 1 235 ? 28.74893  -20.35149 -18.78105 1.000 23.05323 ? 235 PHE A CB    1 
ATOM   1804 C  CG    . PHE A 1 235 ? 27.37494  -19.89748 -19.19607 1.000 20.44662 ? 235 PHE A CG    1 
ATOM   1805 C  CD1   . PHE A 1 235 ? 26.28093  -20.11948 -18.37709 1.000 26.69004 ? 235 PHE A CD1   1 
ATOM   1806 C  CD2   . PHE A 1 235 ? 27.17896  -19.24048 -20.40007 1.000 18.36788 ? 235 PHE A CD2   1 
ATOM   1807 C  CE1   . PHE A 1 235 ? 25.01693  -19.70148 -18.75210 1.000 18.86891 ? 235 PHE A CE1   1 
ATOM   1808 C  CE2   . PHE A 1 235 ? 25.91797  -18.82148 -20.78209 1.000 21.67041 ? 235 PHE A CE2   1 
ATOM   1809 C  CZ    . PHE A 1 235 ? 24.83695  -19.05148 -19.95610 1.000 21.46407 ? 235 PHE A CZ    1 
ATOM   1810 N  N     . GLN A 1 236 ? 27.86096  -22.77148 -21.04307 1.000 25.42623 ? 236 GLN A N     1 
ATOM   1811 C  CA    . GLN A 1 236 ? 27.44598  -22.93947 -22.43108 1.000 21.84261 ? 236 GLN A CA    1 
ATOM   1812 C  C     . GLN A 1 236 ? 25.93998  -22.74147 -22.50210 1.000 21.32339 ? 236 GLN A C     1 
ATOM   1813 O  O     . GLN A 1 236 ? 25.18197  -23.51347 -21.90512 1.000 22.24696 ? 236 GLN A O     1 
ATOM   1814 C  CB    . GLN A 1 236 ? 27.84899  -24.31447 -22.97508 1.000 17.99368 ? 236 GLN A CB    1 
ATOM   1815 C  CG    . GLN A 1 236 ? 29.35299  -24.55347 -22.97806 1.000 26.80320 ? 236 GLN A CG    1 
ATOM   1816 C  CD    . GLN A 1 236 ? 29.77100  -25.66947 -23.91505 1.000 21.55640 ? 236 GLN A CD    1 
ATOM   1817 O  OE1   . GLN A 1 236 ? 29.06301  -25.99547 -24.86806 1.000 30.89360 ? 236 GLN A OE1   1 
ATOM   1818 N  NE2   . GLN A 1 236 ? 30.93000  -26.26047 -23.65004 1.000 17.16196 ? 236 GLN A NE2   1 
ATOM   1819 N  N     . LYS A 1 237 ? 25.51300  -21.70847 -23.23010 1.000 18.87221 ? 237 LYS A N     1 
ATOM   1820 C  CA    . LYS A 1 237 ? 24.10300  -21.32446 -23.23512 1.000 18.84683 ? 237 LYS A CA    1 
ATOM   1821 C  C     . LYS A 1 237 ? 23.18000  -22.41146 -23.77614 1.000 24.13407 ? 237 LYS A C     1 
ATOM   1822 O  O     . LYS A 1 237 ? 22.17299  -22.71546 -23.11316 1.000 25.06319 ? 237 LYS A O     1 
ATOM   1823 C  CB    . LYS A 1 237 ? 23.93701  -20.00946 -24.00612 1.000 17.56477 ? 237 LYS A CB    1 
ATOM   1824 C  CG    . LYS A 1 237 ? 22.54801  -19.39746 -23.92314 1.000 16.94437 ? 237 LYS A CG    1 
ATOM   1825 C  CD    . LYS A 1 237 ? 22.23499  -18.92546 -22.51214 1.000 17.35334 ? 237 LYS A CD    1 
ATOM   1826 C  CE    . LYS A 1 237 ? 20.95899  -18.10046 -22.47616 1.000 22.61878 ? 237 LYS A CE    1 
ATOM   1827 N  NZ    . LYS A 1 237 ? 21.07001  -16.86846 -23.30615 1.000 21.64107 ? 237 LYS A NZ    1 
ATOM   1828 N  N     . PRO A 1 238 ? 23.43502  -23.03046 -24.93814 1.000 20.70936 ? 238 PRO A N     1 
ATOM   1829 C  CA    . PRO A 1 238 ? 22.49403  -24.04645 -25.44016 1.000 17.94592 ? 238 PRO A CA    1 
ATOM   1830 C  C     . PRO A 1 238 ? 22.41201  -25.29946 -24.58116 1.000 25.46823 ? 238 PRO A C     1 
ATOM   1831 O  O     . PRO A 1 238 ? 21.50001  -26.10845 -24.79518 1.000 20.31287 ? 238 PRO A O     1 
ATOM   1832 C  CB    . PRO A 1 238 ? 23.03905  -24.37445 -26.83815 1.000 21.40335 ? 238 PRO A CB    1 
ATOM   1833 C  CG    . PRO A 1 238 ? 23.88206  -23.20245 -27.20713 1.000 19.03364 ? 238 PRO A CG    1 
ATOM   1834 C  CD    . PRO A 1 238 ? 24.50204  -22.76545 -25.92112 1.000 21.57150 ? 238 PRO A CD    1 
ATOM   1835 N  N     . ASP A 1 239 ? 23.31900  -25.48746 -23.62315 1.000 20.30060 ? 239 ASP A N     1 
ATOM   1836 C  CA    . ASP A 1 239 ? 23.32998  -26.67246 -22.77715 1.000 19.10475 ? 239 ASP A CA    1 
ATOM   1837 C  C     . ASP A 1 239 ? 22.63096  -26.45047 -21.44116 1.000 21.56357 ? 239 ASP A C     1 
ATOM   1838 O  O     . ASP A 1 239 ? 22.73995  -27.29647 -20.54817 1.000 17.03511 ? 239 ASP A O     1 
ATOM   1839 C  CB    . ASP A 1 239 ? 24.76898  -27.13447 -22.53813 1.000 25.15669 ? 239 ASP A CB    1 
ATOM   1840 C  CG    . ASP A 1 239 ? 25.54400  -27.31446 -23.82812 1.000 25.59203 ? 239 ASP A CG    1 
ATOM   1841 O  OD1   . ASP A 1 239 ? 24.90701  -27.42846 -24.89613 1.000 29.43864 ? 239 ASP A OD1   1 
ATOM   1842 O  OD2   . ASP A 1 239 ? 26.79100  -27.34747 -23.77210 1.000 25.16534 ? 239 ASP A OD2   1 
ATOM   1843 N  N     . THR A 1 240 ? 21.91496  -25.34247 -21.28617 1.000 26.66319 ? 240 THR A N     1 
ATOM   1844 C  CA    . THR A 1 240 ? 21.26194  -25.01147 -20.03018 1.000 22.19292 ? 240 THR A CA    1 
ATOM   1845 C  C     . THR A 1 240 ? 19.84894  -25.58547 -19.98120 1.000 24.59296 ? 240 THR A C     1 
ATOM   1846 O  O     . THR A 1 240 ? 19.23896  -25.89646 -21.00721 1.000 24.71165 ? 240 THR A O     1 
ATOM   1847 C  CB    . THR A 1 240 ? 21.22194  -23.49547 -19.83118 1.000 18.13163 ? 240 THR A CB    1 
ATOM   1848 O  OG1   . THR A 1 240 ? 20.64396  -22.87746 -20.98718 1.000 17.54384 ? 240 THR A OG1   1 
ATOM   1849 C  CG2   . THR A 1 240 ? 22.62594  -22.95047 -19.62115 1.000 19.61009 ? 240 THR A CG2   1 
ATOM   1850 N  N     . ASP A 1 241 ? 19.32992  -25.71847 -18.75921 1.000 26.59573 ? 241 ASP A N     1 
ATOM   1851 C  CA    . ASP A 1 241 ? 18.02492  -26.32847 -18.53723 1.000 20.95748 ? 241 ASP A CA    1 
ATOM   1852 C  C     . ASP A 1 241 ? 16.93992  -25.25847 -18.57825 1.000 20.08559 ? 241 ASP A C     1 
ATOM   1853 O  O     . ASP A 1 241 ? 16.93891  -24.36347 -17.72324 1.000 24.41233 ? 241 ASP A O     1 
ATOM   1854 C  CB    . ASP A 1 241 ? 17.99290  -27.04947 -17.19724 1.000 19.44218 ? 241 ASP A CB    1 
ATOM   1855 C  CG    . ASP A 1 241 ? 16.80989  -27.99747 -17.06126 1.000 22.23288 ? 241 ASP A CG    1 
ATOM   1856 O  OD1   . ASP A 1 241 ? 15.75190  -27.74847 -17.67527 1.000 21.79194 ? 241 ASP A OD1   1 
ATOM   1857 O  OD2   . ASP A 1 241 ? 16.93888  -29.00047 -16.32826 1.000 24.11335 ? 241 ASP A OD2   1 
ATOM   1858 N  N     . PRO A 1 242 ? 16.00893  -25.30746 -19.53726 1.000 22.91845 ? 242 PRO A N     1 
ATOM   1859 C  CA    . PRO A 1 242 ? 14.90194  -24.34046 -19.53328 1.000 17.55189 ? 242 PRO A CA    1 
ATOM   1860 C  C     . PRO A 1 242 ? 13.78292  -24.69646 -18.57229 1.000 22.38664 ? 242 PRO A C     1 
ATOM   1861 O  O     . PRO A 1 242 ? 12.94592  -23.83346 -18.27830 1.000 16.95092 ? 242 PRO A O     1 
ATOM   1862 C  CB    . PRO A 1 242 ? 14.41096  -24.36945 -20.98528 1.000 18.51942 ? 242 PRO A CB    1 
ATOM   1863 C  CG    . PRO A 1 242 ? 14.70296  -25.76345 -21.42628 1.000 19.44874 ? 242 PRO A CG    1 
ATOM   1864 C  CD    . PRO A 1 242 ? 15.98195  -26.17146 -20.73027 1.000 21.52873 ? 242 PRO A CD    1 
ATOM   1865 N  N     . SER A 1 243 ? 13.73791  -25.93246 -18.07930 1.000 17.64253 ? 243 SER A N     1 
ATOM   1866 C  CA    . SER A 1 243 ? 12.72690  -26.37046 -17.11832 1.000 19.52656 ? 243 SER A CA    1 
ATOM   1867 C  C     . SER A 1 243 ? 13.23887  -26.29247 -15.68531 1.000 22.22880 ? 243 SER A C     1 
ATOM   1868 O  O     . SER A 1 243 ? 12.96586  -27.17647 -14.86931 1.000 24.85214 ? 243 SER A O     1 
ATOM   1869 C  CB    . SER A 1 243 ? 12.26690  -27.78646 -17.44733 1.000 23.47000 ? 243 SER A CB    1 
ATOM   1870 O  OG    . SER A 1 243 ? 13.33989  -28.70746 -17.34731 1.000 22.59476 ? 243 SER A OG    1 
ATOM   1871 N  N     . ALA A 1 244 ? 13.98787  -25.24247 -15.35529 1.000 17.20954 ? 244 ALA A N     1 
ATOM   1872 C  CA    . ALA A 1 244 ? 14.54085  -25.04748 -14.02128 1.000 21.05201 ? 244 ALA A CA    1 
ATOM   1873 C  C     . ALA A 1 244 ? 13.97984  -23.75648 -13.44529 1.000 23.93315 ? 244 ALA A C     1 
ATOM   1874 O  O     . ALA A 1 244 ? 14.24285  -22.67148 -13.97628 1.000 23.52245 ? 244 ALA A O     1 
ATOM   1875 C  CB    . ALA A 1 244 ? 16.06985  -25.00448 -14.06026 1.000 20.05885 ? 244 ALA A CB    1 
ATOM   1876 N  N     . TRP A 1 245 ? 13.20983  -23.87448 -12.36630 1.000 23.29320 ? 245 TRP A N     1 
ATOM   1877 C  CA    . TRP A 1 245 ? 12.58682  -22.72448 -11.72730 1.000 20.82899 ? 245 TRP A CA    1 
ATOM   1878 C  C     . TRP A 1 245 ? 12.96680  -22.55049 -10.26430 1.000 20.04856 ? 245 TRP A C     1 
ATOM   1879 O  O     . TRP A 1 245 ? 13.01879  -21.41249 -9.79229  1.000 20.14536 ? 245 TRP A O     1 
ATOM   1880 C  CB    . TRP A 1 245 ? 11.05582  -22.81448 -11.84033 1.000 24.29166 ? 245 TRP A CB    1 
ATOM   1881 C  CG    . TRP A 1 245 ? 10.48581  -24.07348 -11.27534 1.000 20.09984 ? 245 TRP A CG    1 
ATOM   1882 C  CD1   . TRP A 1 245 ? 10.33182  -25.26548 -11.92035 1.000 25.94865 ? 245 TRP A CD1   1 
ATOM   1883 C  CD2   . TRP A 1 245 ? 9.99279   -24.26949 -9.94635  1.000 23.28241 ? 245 TRP A CD2   1 
ATOM   1884 N  NE1   . TRP A 1 245 ? 9.77280   -26.19248 -11.07536 1.000 26.24040 ? 245 TRP A NE1   1 
ATOM   1885 C  CE2   . TRP A 1 245 ? 9.55479   -25.60548 -9.85636  1.000 24.64602 ? 245 TRP A CE2   1 
ATOM   1886 C  CE3   . TRP A 1 245 ? 9.87877   -23.44649 -8.82235  1.000 24.81058 ? 245 TRP A CE3   1 
ATOM   1887 C  CZ2   . TRP A 1 245 ? 9.01177   -26.13749 -8.68837  1.000 27.14052 ? 245 TRP A CZ2   1 
ATOM   1888 C  CZ3   . TRP A 1 245 ? 9.33876   -23.97549 -7.66436  1.000 22.33760 ? 245 TRP A CZ3   1 
ATOM   1889 C  CH2   . TRP A 1 245 ? 8.91175   -25.30749 -7.60637  1.000 29.18446 ? 245 TRP A CH2   1 
ATOM   1890 N  N     . GLU A 1 246 ? 13.21978  -23.63949 -9.53230  1.000 28.07290 ? 246 GLU A N     1 
ATOM   1891 C  CA    . GLU A 1 246 ? 13.71576  -23.51450 -8.16329  1.000 23.59490 ? 246 GLU A CA    1 
ATOM   1892 C  C     . GLU A 1 246 ? 15.05476  -22.79050 -8.13927  1.000 17.73445 ? 246 GLU A C     1 
ATOM   1893 O  O     . GLU A 1 246 ? 15.26875  -21.87150 -7.33926  1.000 14.97205 ? 246 GLU A O     1 
ATOM   1894 C  CB    . GLU A 1 246 ? 13.84275  -24.89650 -7.52229  1.000 22.36273 ? 246 GLU A CB    1 
ATOM   1895 C  CG    . GLU A 1 246 ? 12.52374  -25.51950 -7.10732  1.000 25.97002 ? 246 GLU A CG    1 
ATOM   1896 C  CD    . GLU A 1 246 ? 12.67573  -26.96150 -6.67232  1.000 26.18158 ? 246 GLU A CD    1 
ATOM   1897 O  OE1   . GLU A 1 246 ? 13.14875  -27.78050 -7.48631  1.000 32.21019 ? 246 GLU A OE1   1 
ATOM   1898 O  OE2   . GLU A 1 246 ? 12.33072  -27.27551 -5.51432  1.000 33.58301 ? 246 GLU A OE2   1 
ATOM   1899 N  N     . LYS A 1 247 ? 15.97378  -23.20350 -9.00725  1.000 16.44314 ? 247 LYS A N     1 
ATOM   1900 C  CA    . LYS A 1 247 ? 17.23978  -22.50850 -9.22223  1.000 21.07741 ? 247 LYS A CA    1 
ATOM   1901 C  C     . LYS A 1 247 ? 17.39981  -22.32750 -10.72423 1.000 19.01992 ? 247 LYS A C     1 
ATOM   1902 O  O     . LYS A 1 247 ? 17.83381  -23.26349 -11.41923 1.000 18.24971 ? 247 LYS A O     1 
ATOM   1903 C  CB    . LYS A 1 247 ? 18.41677  -23.27950 -8.63422  1.000 16.50379 ? 247 LYS A CB    1 
ATOM   1904 C  CG    . LYS A 1 247 ? 19.75778  -22.58351 -8.81819  1.000 20.76354 ? 247 LYS A CG    1 
ATOM   1905 C  CD    . LYS A 1 247 ? 20.93977  -23.48951 -8.49218  0.000 19.70345 ? 247 LYS A CD    1 
ATOM   1906 C  CE    . LYS A 1 247 ? 21.06775  -23.75652 -6.99818  0.000 19.43367 ? 247 LYS A CE    1 
ATOM   1907 N  NZ    . LYS A 1 247 ? 20.21774  -24.88752 -6.53220  0.000 19.34287 ? 247 LYS A NZ    1 
ATOM   1908 N  N     . PRO A 1 248 ? 17.04082  -21.16349 -11.26523 1.000 19.00970 ? 248 PRO A N     1 
ATOM   1909 C  CA    . PRO A 1 248 ? 17.17884  -20.94849 -12.71023 1.000 17.77436 ? 248 PRO A CA    1 
ATOM   1910 C  C     . PRO A 1 248 ? 18.61484  -21.17249 -13.15921 1.000 15.21407 ? 248 PRO A C     1 
ATOM   1911 O  O     . PRO A 1 248 ? 19.54984  -20.55049 -12.64819 1.000 15.47971 ? 248 PRO A O     1 
ATOM   1912 C  CB    . PRO A 1 248 ? 16.74384  -19.48949 -12.89523 1.000 16.32513 ? 248 PRO A CB    1 
ATOM   1913 C  CG    . PRO A 1 248 ? 15.88883  -19.18949 -11.70524 1.000 21.05937 ? 248 PRO A CG    1 
ATOM   1914 C  CD    . PRO A 1 248 ? 16.47581  -19.98949 -10.57924 1.000 20.05917 ? 248 PRO A CD    1 
ATOM   1915 N  N     . ALA A 1 249 ? 18.78386  -22.08749 -14.11721 1.000 16.98773 ? 249 ALA A N     1 
ATOM   1916 C  CA    . ALA A 1 249 ? 20.07487  -22.49649 -14.68019 1.000 19.03253 ? 249 ALA A CA    1 
ATOM   1917 C  C     . ALA A 1 249 ? 20.81288  -21.36549 -15.39117 1.000 14.75900 ? 249 ALA A C     1 
ATOM   1918 O  O     . ALA A 1 249 ? 21.82489  -21.65948 -16.03016 1.000 14.86366 ? 249 ALA A O     1 
ATOM   1919 C  CB    . ALA A 1 249 ? 19.87588  -23.67448 -15.64020 1.000 19.18281 ? 249 ALA A CB    1 
ATOM   1920 N  N     . THR A 1 250 ? 20.37088  -20.11248 -15.31518 1.000 14.91039 ? 250 THR A N     1 
ATOM   1921 C  CA    . THR A 1 250 ? 21.08889  -18.97248 -15.86816 1.000 15.17235 ? 250 THR A CA    1 
ATOM   1922 C  C     . THR A 1 250 ? 21.17688  -17.88149 -14.80016 1.000 13.50079 ? 250 THR A C     1 
ATOM   1923 O  O     . THR A 1 250 ? 20.63486  -18.01649 -13.70016 1.000 15.39011 ? 250 THR A O     1 
ATOM   1924 C  CB    . THR A 1 250 ? 20.41291  -18.45648 -17.14617 1.000 14.62863 ? 250 THR A CB    1 
ATOM   1925 O  OG1   . THR A 1 250 ? 18.99391  -18.39348 -16.96119 1.000 16.69891 ? 250 THR A OG1   1 
ATOM   1926 C  CG2   . THR A 1 250 ? 20.72493  -19.36447 -18.32517 1.000 16.22217 ? 250 THR A CG2   1 
ATOM   1927 N  N     . THR A 1 251 ? 21.86088  -16.78049 -15.12814 1.000 18.34252 ? 251 THR A N     1 
ATOM   1928 C  CA    . THR A 1 251 ? 22.15487  -15.76949 -14.11213 1.000 17.34311 ? 251 THR A CA    1 
ATOM   1929 C  C     . THR A 1 251 ? 20.92886  -14.93849 -13.74715 1.000 20.26976 ? 251 THR A C     1 
ATOM   1930 O  O     . THR A 1 251 ? 20.84185  -14.43450 -12.62115 1.000 15.55883 ? 251 THR A O     1 
ATOM   1931 C  CB    . THR A 1 251 ? 23.28288  -14.85349 -14.58711 1.000 19.51061 ? 251 THR A CB    1 
ATOM   1932 O  OG1   . THR A 1 251 ? 22.86090  -14.14149 -15.75712 1.000 15.22539 ? 251 THR A OG1   1 
ATOM   1933 C  CG2   . THR A 1 251 ? 24.52988  -15.66649 -14.91510 1.000 14.74822 ? 251 THR A CG2   1 
ATOM   1934 N  N     . VAL A 1 252 ? 19.97888  -14.79549 -14.67316 1.000 19.30549 ? 252 VAL A N     1 
ATOM   1935 C  CA    . VAL A 1 252 ? 18.78988  -13.96348 -14.49518 1.000 16.28827 ? 252 VAL A CA    1 
ATOM   1936 C  C     . VAL A 1 252 ? 19.22387  -12.54949 -14.12517 1.000 19.15401 ? 252 VAL A C     1 
ATOM   1937 O  O     . VAL A 1 252 ? 18.71686  -11.95749 -13.16517 1.000 17.79433 ? 252 VAL A O     1 
ATOM   1938 C  CB    . VAL A 1 252 ? 17.82886  -14.55249 -13.44320 1.000 20.40559 ? 252 VAL A CB    1 
ATOM   1939 C  CG1   . VAL A 1 252 ? 16.43186  -13.96248 -13.61021 1.000 16.86546 ? 252 VAL A CG1   1 
ATOM   1940 C  CG2   . VAL A 1 252 ? 17.77886  -16.06649 -13.55520 1.000 20.71566 ? 252 VAL A CG2   1 
ATOM   1941 N  N     . LEU A 1 253 ? 20.17589  -12.00549 -14.88015 1.000 14.96732 ? 253 LEU A N     1 
ATOM   1942 C  CA    . LEU A 1 253 ? 20.65389  -10.64449 -14.68514 1.000 17.07318 ? 253 LEU A CA    1 
ATOM   1943 C  C     . LEU A 1 253 ? 20.12390  -9.68548  -15.74214 1.000 17.12521 ? 253 LEU A C     1 
ATOM   1944 O  O     . LEU A 1 253 ? 20.51491  -8.51448  -15.75213 1.000 19.43102 ? 253 LEU A O     1 
ATOM   1945 C  CB    . LEU A 1 253 ? 22.18389  -10.61949 -14.67111 1.000 18.09749 ? 253 LEU A CB    1 
ATOM   1946 C  CG    . LEU A 1 253 ? 22.87187  -11.31950 -13.49711 1.000 13.35923 ? 253 LEU A CG    1 
ATOM   1947 C  CD1   . LEU A 1 253 ? 24.38087  -11.33250 -13.68108 1.000 17.24875 ? 253 LEU A CD1   1 
ATOM   1948 C  CD2   . LEU A 1 253 ? 22.49785  -10.65550 -12.18211 1.000 16.64652 ? 253 LEU A CD2   1 
ATOM   1949 N  N     . SER A 1 254 ? 19.24692  -10.15448 -16.62816 1.000 26.47183 ? 254 SER A N     1 
ATOM   1950 C  CA    . SER A 1 254 ? 18.70193  -9.28147  -17.66416 1.000 28.87913 ? 254 SER A CA    1 
ATOM   1951 C  C     . SER A 1 254 ? 17.88493  -8.11147  -17.12017 1.000 29.38995 ? 254 SER A C     1 
ATOM   1952 O  O     . SER A 1 254 ? 18.01094  -7.00647  -17.67817 1.000 33.66496 ? 254 SER A O     1 
ATOM   1953 C  CB    . SER A 1 254 ? 17.87595  -10.11047 -18.65818 1.000 30.27600 ? 254 SER A CB    1 
ATOM   1954 O  OG    . SER A 1 254 ? 17.00994  -11.01547 -17.99820 1.000 33.22790 ? 254 SER A OG    1 
ATOM   1955 N  N     . PRO A 1 255 ? 17.04891  -8.25548  -16.08218 1.000 19.22587 ? 255 PRO A N     1 
ATOM   1956 C  CA    . PRO A 1 255 ? 16.34691  -7.06248  -15.58019 1.000 25.27288 ? 255 PRO A CA    1 
ATOM   1957 C  C     . PRO A 1 255 ? 17.28490  -6.03448  -14.97417 1.000 24.10791 ? 255 PRO A C     1 
ATOM   1958 O  O     . PRO A 1 255 ? 17.06390  -4.82848  -15.13917 1.000 18.40207 ? 255 PRO A O     1 
ATOM   1959 C  CB    . PRO A 1 255 ? 15.37589  -7.63348  -14.53621 1.000 17.74424 ? 255 PRO A CB    1 
ATOM   1960 C  CG    . PRO A 1 255 ? 15.25189  -9.07548  -14.87122 1.000 23.72188 ? 255 PRO A CG    1 
ATOM   1961 C  CD    . PRO A 1 255 ? 16.59590  -9.47048  -15.38020 1.000 21.70650 ? 255 PRO A CD    1 
ATOM   1962 N  N     . TYR A 1 256 ? 18.33389  -6.47848  -14.27716 1.000 21.15900 ? 256 TYR A N     1 
ATOM   1963 C  CA    . TYR A 1 256 ? 19.26888  -5.53649  -13.67414 1.000 19.21753 ? 256 TYR A CA    1 
ATOM   1964 C  C     . TYR A 1 256 ? 20.15490  -4.87549  -14.72313 1.000 22.74439 ? 256 TYR A C     1 
ATOM   1965 O  O     . TYR A 1 256 ? 20.60790  -3.74249  -14.52611 1.000 19.85663 ? 256 TYR A O     1 
ATOM   1966 C  CB    . TYR A 1 256 ? 20.11786  -6.24449  -12.61913 1.000 26.52559 ? 256 TYR A CB    1 
ATOM   1967 C  CG    . TYR A 1 256 ? 19.30485  -7.03350  -11.61815 1.000 29.09207 ? 256 TYR A CG    1 
ATOM   1968 C  CD1   . TYR A 1 256 ? 18.70283  -6.40750  -10.53315 1.000 26.30731 ? 256 TYR A CD1   1 
ATOM   1969 C  CD2   . TYR A 1 256 ? 19.13485  -8.40550  -11.75815 1.000 26.81120 ? 256 TYR A CD2   1 
ATOM   1970 C  CE1   . TYR A 1 256 ? 17.95582  -7.12550  -9.61717  1.000 22.99432 ? 256 TYR A CE1   1 
ATOM   1971 C  CE2   . TYR A 1 256 ? 18.39083  -9.13050  -10.84717 1.000 27.69264 ? 256 TYR A CE2   1 
ATOM   1972 C  CZ    . TYR A 1 256 ? 17.80382  -8.48650  -9.77917  1.000 25.06371 ? 256 TYR A CZ    1 
ATOM   1973 O  OH    . TYR A 1 256 ? 17.06180  -9.20550  -8.87119  1.000 27.49126 ? 256 TYR A OH    1 
ATOM   1974 N  N     . LEU A 1 257 ? 20.41191  -5.56148  -15.83912 1.000 23.44589 ? 257 LEU A N     1 
ATOM   1975 C  CA    . LEU A 1 257 ? 21.16893  -4.95448  -16.92711 1.000 20.42330 ? 257 LEU A CA    1 
ATOM   1976 C  C     . LEU A 1 257 ? 20.29695  -4.05348  -17.79112 1.000 18.54920 ? 257 LEU A C     1 
ATOM   1977 O  O     . LEU A 1 257 ? 20.79296  -3.06647  -18.34711 1.000 15.77517 ? 257 LEU A O     1 
ATOM   1978 C  CB    . LEU A 1 257 ? 21.82094  -6.03848  -17.78910 1.000 22.59291 ? 257 LEU A CB    1 
ATOM   1979 C  CG    . LEU A 1 257 ? 22.93793  -6.85948  -17.14209 1.000 16.43435 ? 257 LEU A CG    1 
ATOM   1980 C  CD1   . LEU A 1 257 ? 23.32194  -8.03548  -18.02709 1.000 14.04126 ? 257 LEU A CD1   1 
ATOM   1981 C  CD2   . LEU A 1 257 ? 24.15093  -5.98849  -16.85507 1.000 18.29193 ? 257 LEU A CD2   1 
ATOM   1982 N  N     . LYS A 1 258 ? 19.01195  -4.36947  -17.88014 1.000 19.51479 ? 258 LYS A N     1 
ATOM   1983 C  CA    . LYS A 1 258 ? 18.07296  -3.56247  -18.70515 1.000 19.53656 ? 258 LYS A CA    1 
ATOM   1984 C  C     . LYS A 1 258 ? 17.88795  -2.18547  -18.07415 1.000 22.00428 ? 258 LYS A C     1 
ATOM   1985 O  O     . LYS A 1 258 ? 18.12397  -1.20247  -18.76814 1.000 24.88751 ? 258 LYS A O     1 
ATOM   1986 C  CB    . LYS A 1 258 ? 16.72096  -4.25647  -18.84718 1.000 19.39068 ? 258 LYS A CB    1 
ATOM   1987 C  CG    . LYS A 1 258 ? 15.63197  -3.47246  -19.55819 1.000 18.04442 ? 258 LYS A CG    1 
ATOM   1988 C  CD    . LYS A 1 258 ? 14.49996  -3.13346  -18.63421 1.000 19.30155 ? 258 LYS A CD    1 
ATOM   1989 C  CE    . LYS A 1 258 ? 13.84797  -1.81646  -18.98121 1.000 24.65067 ? 258 LYS A CE    1 
ATOM   1990 N  NZ    . LYS A 1 258 ? 12.50698  -2.01746  -19.56623 1.000 22.51580 ? 258 LYS A NZ    1 
ATOM   1991 N  N     . PHE A 1 259 ? 17.47193  -2.15247  -16.80716 1.000 21.58476 ? 259 PHE A N     1 
ATOM   1992 C  CA    . PHE A 1 259 ? 17.23993  -0.88848  -16.11916 1.000 20.95909 ? 259 PHE A CA    1 
ATOM   1993 C  C     . PHE A 1 259 ? 18.53292  -0.16748  -15.76913 1.000 21.85789 ? 259 PHE A C     1 
ATOM   1994 O  O     . PHE A 1 259 ? 18.50192  1.03952   -15.50713 1.000 15.58967 ? 259 PHE A O     1 
ATOM   1995 C  CB    . PHE A 1 259 ? 16.42491  -1.12048  -14.84517 1.000 27.63891 ? 259 PHE A CB    1 
ATOM   1996 C  CG    . PHE A 1 259 ? 14.99291  -1.48148  -15.09919 1.000 24.03201 ? 259 PHE A CG    1 
ATOM   1997 C  CD1   . PHE A 1 259 ? 14.08492  -0.51547  -15.49920 1.000 22.11146 ? 259 PHE A CD1   1 
ATOM   1998 C  CD2   . PHE A 1 259 ? 14.54990  -2.78148  -14.92820 1.000 21.94682 ? 259 PHE A CD2   1 
ATOM   1999 C  CE1   . PHE A 1 259 ? 12.76492  -0.84047  -15.73222 1.000 26.29489 ? 259 PHE A CE1   1 
ATOM   2000 C  CE2   . PHE A 1 259 ? 13.22991  -3.11347  -15.16022 1.000 17.05444 ? 259 PHE A CE2   1 
ATOM   2001 C  CZ    . PHE A 1 259 ? 12.33692  -2.14147  -15.56124 1.000 24.54271 ? 259 PHE A CZ    1 
ATOM   2002 N  N     . GLY A 1 260 ? 19.65892  -0.87048  -15.75412 1.000 23.37723 ? 260 GLY A N     1 
ATOM   2003 C  CA    . GLY A 1 260 ? 20.92292  -0.28049  -15.37510 1.000 21.25035 ? 260 GLY A CA    1 
ATOM   2004 C  C     . GLY A 1 260 ? 21.33489  -0.50249  -13.93809 1.000 21.91014 ? 260 GLY A C     1 
ATOM   2005 O  O     . GLY A 1 260 ? 22.32789  0.09051   -13.50207 1.000 15.78263 ? 260 GLY A O     1 
ATOM   2006 N  N     . CYS A 1 261 ? 20.60488  -1.33249  -13.18711 1.000 25.62908 ? 261 CYS A N     1 
ATOM   2007 C  CA    . CYS A 1 261 ? 21.00086  -1.64650  -11.81910 1.000 19.95161 ? 261 CYS A CA    1 
ATOM   2008 C  C     . CYS A 1 261 ? 22.33386  -2.37850  -11.76508 1.000 22.68343 ? 261 CYS A C     1 
ATOM   2009 O  O     . CYS A 1 261 ? 23.01684  -2.32651  -10.73607 1.000 24.41226 ? 261 CYS A O     1 
ATOM   2010 C  CB    . CYS A 1 261 ? 19.91885  -2.48550  -11.13712 1.000 25.80405 ? 261 CYS A CB    1 
ATOM   2011 S  SG    . CYS A 1 261 ? 18.28785  -1.70850  -11.07914 1.000 21.57397 ? 261 CYS A SG    1 
ATOM   2012 N  N     . LEU A 1 262 ? 22.71687  -3.05350  -12.84408 1.000 26.28299 ? 262 LEU A N     1 
ATOM   2013 C  CA    . LEU A 1 262 ? 23.99387  -3.74250  -12.94306 1.000 20.93406 ? 262 LEU A CA    1 
ATOM   2014 C  C     . LEU A 1 262 ? 24.77489  -3.18350  -14.12305 1.000 21.67103 ? 262 LEU A C     1 
ATOM   2015 O  O     . LEU A 1 262 ? 24.20191  -2.89949  -15.18006 1.000 25.94668 ? 262 LEU A O     1 
ATOM   2016 C  CB    . LEU A 1 262 ? 23.79487  -5.25350  -13.10807 1.000 22.65516 ? 262 LEU A CB    1 
ATOM   2017 C  CG    . LEU A 1 262 ? 25.05487  -6.12250  -13.14406 1.000 20.78725 ? 262 LEU A CG    1 
ATOM   2018 C  CD1   . LEU A 1 262 ? 25.80385  -6.04451  -11.82104 1.000 18.95229 ? 262 LEU A CD1   1 
ATOM   2019 C  CD2   . LEU A 1 262 ? 24.70587  -7.56350  -13.48407 1.000 18.34458 ? 262 LEU A CD2   1 
ATOM   2020 N  N     . SER A 1 263 ? 26.06689  -2.92850  -13.91603 1.000 16.94044 ? 263 SER A N     1 
ATOM   2021 C  CA    . SER A 1 263 ? 26.95591  -2.48350  -15.01401 1.000 21.02123 ? 263 SER A CA    1 
ATOM   2022 C  C     . SER A 1 263 ? 27.50692  -3.67950  -15.80101 1.000 24.06011 ? 263 SER A C     1 
ATOM   2023 O  O     . SER A 1 263 ? 28.05191  -4.59950  -15.19300 1.000 15.79400 ? 263 SER A O     1 
ATOM   2024 C  CB    . SER A 1 263 ? 28.09690  -1.63850  -14.56999 1.000 16.45975 ? 263 SER A CB    1 
ATOM   2025 O  OG    . SER A 1 263 ? 29.20591  -1.77850  -15.43298 1.000 23.67089 ? 263 SER A OG    1 
ATOM   2026 N  N     . ALA A 1 264 ? 27.37694  -3.60549  -17.11701 1.000 19.81858 ? 264 ALA A N     1 
ATOM   2027 C  CA    . ALA A 1 264 ? 27.95995  -4.62949  -17.97601 1.000 21.06248 ? 264 ALA A CA    1 
ATOM   2028 C  C     . ALA A 1 264 ? 29.48095  -4.57749  -17.95298 1.000 20.42188 ? 264 ALA A C     1 
ATOM   2029 O  O     . ALA A 1 264 ? 30.13695  -5.61649  -18.08898 1.000 22.01140 ? 264 ALA A O     1 
ATOM   2030 C  CB    . ALA A 1 264 ? 27.44397  -4.47748  -19.40601 1.000 23.45411 ? 264 ALA A CB    1 
ATOM   2031 N  N     . ARG A 1 265 ? 30.05526  -3.38209  -17.78888 1.000 16.99367 ? 265 ARG A N     1 
ATOM   2032 C  CA    . ARG A 1 265 ? 31.50705  -3.25778  -17.70537 1.000 23.27716 ? 265 ARG A CA    1 
ATOM   2033 C  C     . ARG A 1 265 ? 32.05041  -3.99143  -16.48662 1.000 26.14399 ? 265 ARG A C     1 
ATOM   2034 O  O     . ARG A 1 265 ? 33.12607  -4.59959  -16.54469 1.000 25.05844 ? 265 ARG A O     1 
ATOM   2035 C  CB    . ARG A 1 265 ? 31.90518  -1.78241  -17.65743 1.000 21.62409 ? 265 ARG A CB    1 
ATOM   2036 C  CG    . ARG A 1 265 ? 31.36697  -0.93997  -18.80248 1.000 20.67051 ? 265 ARG A CG    1 
ATOM   2037 C  CD    . ARG A 1 265 ? 32.37649  -0.82432  -19.92972 1.000 22.85911 ? 265 ARG A CD    1 
ATOM   2038 N  NE    . ARG A 1 265 ? 31.95028  0.12821   -20.94857 1.000 29.05978 ? 265 ARG A NE    1 
ATOM   2039 C  CZ    . ARG A 1 265 ? 32.16668  1.43543   -20.89009 1.000 26.46800 ? 265 ARG A CZ    1 
ATOM   2040 N  NH1   . ARG A 1 265 ? 32.79259  1.98740   -19.86354 1.000 31.57905 ? 265 ARG A NH1   1 
ATOM   2041 N  NH2   . ARG A 1 265 ? 31.74315  2.20871   -21.88598 1.000 25.79227 ? 265 ARG A NH2   1 
ATOM   2042 N  N     . LEU A 1 266 ? 31.32091  -3.94050  -15.36995 1.000 18.43315 ? 266 LEU A N     1 
ATOM   2043 C  CA    . LEU A 1 266 ? 31.75089  -4.65751  -14.17395 1.000 24.83919 ? 266 LEU A CA    1 
ATOM   2044 C  C     . LEU A 1 266 ? 31.53289  -6.15751  -14.32596 1.000 23.15892 ? 266 LEU A C     1 
ATOM   2045 O  O     . LEU A 1 266 ? 32.34388  -6.95951  -13.84895 1.000 24.08510 ? 266 LEU A O     1 
ATOM   2046 C  CB    . LEU A 1 266 ? 31.00987  -4.12551  -12.94696 1.000 27.29102 ? 266 LEU A CB    1 
ATOM   2047 C  CG    . LEU A 1 266 ? 31.49185  -4.64752  -11.59195 1.000 29.93226 ? 266 LEU A CG    1 
ATOM   2048 C  CD1   . LEU A 1 266 ? 32.95585  -4.29552  -11.37893 1.000 31.82074 ? 266 LEU A CD1   1 
ATOM   2049 C  CD2   . LEU A 1 266 ? 30.63583  -4.09252  -10.46596 1.000 25.29736 ? 266 LEU A CD2   1 
ATOM   2050 N  N     . PHE A 1 267 ? 30.43990  -6.55450  -14.98497 1.000 20.95954 ? 267 PHE A N     1 
ATOM   2051 C  CA    . PHE A 1 267 ? 30.21890  -7.96750  -15.27598 1.000 23.99252 ? 267 PHE A CA    1 
ATOM   2052 C  C     . PHE A 1 267 ? 31.32591  -8.51950  -16.16597 1.000 20.95991 ? 267 PHE A C     1 
ATOM   2053 O  O     . PHE A 1 267 ? 31.84991  -9.61150  -15.91796 1.000 25.42435 ? 267 PHE A O     1 
ATOM   2054 C  CB    . PHE A 1 267 ? 28.84791  -8.15150  -15.93300 1.000 21.94250 ? 267 PHE A CB    1 
ATOM   2055 C  CG    . PHE A 1 267 ? 28.35291  -9.57550  -15.94902 1.000 23.59426 ? 267 PHE A CG    1 
ATOM   2056 C  CD1   . PHE A 1 267 ? 29.02490  -10.57750 -15.26701 1.000 26.73633 ? 267 PHE A CD1   1 
ATOM   2057 C  CD2   . PHE A 1 267 ? 27.20592  -9.90949  -16.65204 1.000 17.37681 ? 267 PHE A CD2   1 
ATOM   2058 C  CE1   . PHE A 1 267 ? 28.56489  -11.88250 -15.28802 1.000 26.33013 ? 267 PHE A CE1   1 
ATOM   2059 C  CE2   . PHE A 1 267 ? 26.74092  -11.21149 -16.67505 1.000 15.98984 ? 267 PHE A CE2   1 
ATOM   2060 C  CZ    . PHE A 1 267 ? 27.42090  -12.19849 -15.99304 1.000 17.36890 ? 267 PHE A CZ    1 
ATOM   2061 N  N     . HIS A 1 268 ? 31.70693  -7.76950  -17.20296 1.000 23.58135 ? 268 HIS A N     1 
ATOM   2062 C  CA    . HIS A 1 268 ? 32.76894  -8.22250  -18.09694 1.000 24.57771 ? 268 HIS A CA    1 
ATOM   2063 C  C     . HIS A 1 268 ? 34.11193  -8.28450  -17.37792 1.000 24.61505 ? 268 HIS A C     1 
ATOM   2064 O  O     . HIS A 1 268 ? 34.92593  -9.17450  -17.64792 1.000 19.69624 ? 268 HIS A O     1 
ATOM   2065 C  CB    . HIS A 1 268 ? 32.85396  -7.30349  -19.31494 1.000 16.61557 ? 268 HIS A CB    1 
ATOM   2066 C  CG    . HIS A 1 268 ? 33.86498  -7.73849  -20.32993 1.000 23.01922 ? 268 HIS A CG    1 
ATOM   2067 N  ND1   . HIS A 1 268 ? 33.62999  -8.76049  -21.22393 1.000 24.29031 ? 268 HIS A ND1   1 
ATOM   2068 C  CD2   . HIS A 1 268 ? 35.11698  -7.29349  -20.58891 1.000 28.82926 ? 268 HIS A CD2   1 
ATOM   2069 C  CE1   . HIS A 1 268 ? 34.69100  -8.92249  -21.99392 1.000 28.26014 ? 268 HIS A CE1   1 
ATOM   2070 N  NE2   . HIS A 1 268 ? 35.60800  -8.04449  -21.62890 1.000 27.21285 ? 268 HIS A NE2   1 
ATOM   2071 N  N     . ALA A 1 269 ? 34.35992  -7.34851  -16.45892 1.000 27.02689 ? 269 ALA A N     1 
ATOM   2072 C  CA    . ALA A 1 269 ? 35.61491  -7.36051  -15.71490 1.000 23.04148 ? 269 ALA A CA    1 
ATOM   2073 C  C     . ALA A 1 269 ? 35.67289  -8.51951  -14.72890 1.000 23.21632 ? 269 ALA A C     1 
ATOM   2074 O  O     . ALA A 1 269 ? 36.75489  -9.05752  -14.46989 1.000 26.16702 ? 269 ALA A O     1 
ATOM   2075 C  CB    . ALA A 1 269 ? 35.80990  -6.03151  -14.98589 1.000 23.38870 ? 269 ALA A CB    1 
ATOM   2076 N  N     . ARG A 1 270 ? 34.52697  -8.91490  -14.16897 1.000 26.85551 ? 270 ARG A N     1 
ATOM   2077 C  CA    . ARG A 1 270 ? 34.50516  -10.06113 -13.26721 1.000 25.49099 ? 270 ARG A CA    1 
ATOM   2078 C  C     . ARG A 1 270 ? 34.63885  -11.37438 -14.02659 1.000 22.36748 ? 270 ARG A C     1 
ATOM   2079 O  O     . ARG A 1 270 ? 35.14820  -12.35716 -13.47602 1.000 28.29517 ? 270 ARG A O     1 
ATOM   2080 C  CB    . ARG A 1 270 ? 33.22103  -10.05535 -12.43730 1.000 25.68540 ? 270 ARG A CB    1 
ATOM   2081 C  CG    . ARG A 1 270 ? 33.13766  -8.92491  -11.42274 1.000 31.32794 ? 270 ARG A CG    1 
ATOM   2082 C  CD    . ARG A 1 270 ? 34.18887  -9.07535  -10.33395 1.000 25.96145 ? 270 ARG A CD    1 
ATOM   2083 N  NE    . ARG A 1 270 ? 34.02505  -10.31616 -9.58596  1.000 23.99813 ? 270 ARG A NE    1 
ATOM   2084 C  CZ    . ARG A 1 270 ? 33.22761  -10.45863 -8.53593  1.000 25.83430 ? 270 ARG A CZ    1 
ATOM   2085 N  NH1   . ARG A 1 270 ? 32.49722  -9.45347  -8.08099  1.000 19.14687 ? 270 ARG A NH1   1 
ATOM   2086 N  NH2   . ARG A 1 270 ? 33.16019  -11.63973 -7.92772  1.000 20.05314 ? 270 ARG A NH2   1 
ATOM   2087 N  N     . LEU A 1 271 ? 34.19089  -11.41251 -15.28393 1.000 21.67642 ? 271 LEU A N     1 
ATOM   2088 C  CA    . LEU A 1 271 ? 34.31690  -12.63251 -16.07594 1.000 22.15729 ? 271 LEU A CA    1 
ATOM   2089 C  C     . LEU A 1 271 ? 35.76791  -12.90151 -16.44892 1.000 23.15819 ? 271 LEU A C     1 
ATOM   2090 O  O     . LEU A 1 271 ? 36.20591  -14.05851 -16.46891 1.000 19.34590 ? 271 LEU A O     1 
ATOM   2091 C  CB    . LEU A 1 271 ? 33.45292  -12.53750 -17.33295 1.000 20.37965 ? 271 LEU A CB    1 
ATOM   2092 C  CG    . LEU A 1 271 ? 31.93492  -12.59350 -17.15397 1.000 28.36102 ? 271 LEU A CG    1 
ATOM   2093 C  CD1   . LEU A 1 271 ? 31.23394  -12.35749 -18.48198 1.000 25.37726 ? 271 LEU A CD1   1 
ATOM   2094 C  CD2   . LEU A 1 271 ? 31.51391  -13.92350 -16.55798 1.000 26.14014 ? 271 LEU A CD2   1 
ATOM   2095 N  N     . LEU A 1 272 ? 36.53192  -11.84751 -16.74890 1.000 23.60471 ? 272 LEU A N     1 
ATOM   2096 C  CA    . LEU A 1 272 ? 37.92492  -12.03651 -17.13988 1.000 22.74045 ? 272 LEU A CA    1 
ATOM   2097 C  C     . LEU A 1 272 ? 38.78290  -12.49852 -15.96987 1.000 18.35305 ? 272 LEU A C     1 
ATOM   2098 O  O     . LEU A 1 272 ? 39.76790  -13.21752 -16.17286 1.000 18.08006 ? 272 LEU A O     1 
ATOM   2099 C  CB    . LEU A 1 272 ? 38.48393  -10.74451 -17.73687 1.000 17.14091 ? 272 LEU A CB    1 
ATOM   2100 C  CG    . LEU A 1 272 ? 37.77495  -10.24450 -18.99788 1.000 24.91627 ? 272 LEU A CG    1 
ATOM   2101 C  CD1   . LEU A 1 272 ? 38.51296  -9.06050  -19.60486 1.000 24.43837 ? 272 LEU A CD1   1 
ATOM   2102 C  CD2   . LEU A 1 272 ? 37.62497  -11.36750 -20.01288 1.000 26.33776 ? 272 LEU A CD2   1 
ATOM   2103 N  N     . GLU A 1 273 ? 38.42888  -12.10152 -14.74487 1.000 25.94472 ? 273 GLU A N     1 
ATOM   2104 C  CA    . GLU A 1 273 ? 39.15587  -12.58752 -13.57586 1.000 20.68347 ? 273 GLU A CA    1 
ATOM   2105 C  C     . GLU A 1 273 ? 39.01986  -14.09852 -13.43487 1.000 21.14597 ? 273 GLU A C     1 
ATOM   2106 O  O     . GLU A 1 273 ? 39.97685  -14.78453 -13.05786 1.000 24.12662 ? 273 GLU A O     1 
ATOM   2107 C  CB    . GLU A 1 273 ? 38.65485  -11.88253 -12.31487 1.000 22.11542 ? 273 GLU A CB    1 
ATOM   2108 C  CG    . GLU A 1 273 ? 38.83585  -10.37453 -12.32886 1.000 23.64282 ? 273 GLU A CG    1 
ATOM   2109 C  CD    . GLU A 1 273 ? 38.27983  -9.71053  -11.08487 1.000 34.50863 ? 273 GLU A CD    1 
ATOM   2110 O  OE1   . GLU A 1 273 ? 37.78982  -10.43453 -10.19288 1.000 39.98594 ? 273 GLU A OE1   1 
ATOM   2111 O  OE2   . GLU A 1 273 ? 38.32983  -8.46553  -10.99786 1.000 35.27450 ? 273 GLU A OE2   1 
ATOM   2112 N  N     . VAL A 1 274 ? 37.83787  -14.63352 -13.73989 1.000 18.00341 ? 274 VAL A N     1 
ATOM   2113 C  CA    . VAL A 1 274 ? 37.63186  -16.07652 -13.67790 1.000 21.40341 ? 274 VAL A CA    1 
ATOM   2114 C  C     . VAL A 1 274 ? 38.25288  -16.76052 -14.88889 1.000 23.54288 ? 274 VAL A C     1 
ATOM   2115 O  O     . VAL A 1 274 ? 38.79488  -17.86652 -14.77989 1.000 27.41062 ? 274 VAL A O     1 
ATOM   2116 C  CB    . VAL A 1 274 ? 36.12886  -16.38752 -13.55392 1.000 28.32915 ? 274 VAL A CB    1 
ATOM   2117 C  CG1   . VAL A 1 274 ? 35.89385  -17.88852 -13.46493 1.000 22.45483 ? 274 VAL A CG1   1 
ATOM   2118 C  CG2   . VAL A 1 274 ? 35.53884  -15.67852 -12.34093 1.000 25.38146 ? 274 VAL A CG2   1 
ATOM   2119 N  N     . TYR A 1 275 ? 38.19590  -16.11651 -16.05789 1.000 21.34913 ? 275 TYR A N     1 
ATOM   2120 C  CA    . TYR A 1 275 ? 38.74992  -16.72351 -17.26488 1.000 19.43808 ? 275 TYR A CA    1 
ATOM   2121 C  C     . TYR A 1 275 ? 40.27191  -16.78151 -17.22186 1.000 24.76909 ? 275 TYR A C     1 
ATOM   2122 O  O     . TYR A 1 275 ? 40.86892  -17.72951 -17.74585 1.000 20.76399 ? 275 TYR A O     1 
ATOM   2123 C  CB    . TYR A 1 275 ? 38.28994  -15.95451 -18.50589 1.000 22.01021 ? 275 TYR A CB    1 
ATOM   2124 C  CG    . TYR A 1 275 ? 36.81094  -16.07050 -18.80991 1.000 26.24499 ? 275 TYR A CG    1 
ATOM   2125 C  CD1   . TYR A 1 275 ? 36.00893  -16.98250 -18.13593 1.000 20.19456 ? 275 TYR A CD1   1 
ATOM   2126 C  CD2   . TYR A 1 275 ? 36.22096  -15.27150 -19.78092 1.000 18.37756 ? 275 TYR A CD2   1 
ATOM   2127 C  CE1   . TYR A 1 275 ? 34.65893  -17.08850 -18.41395 1.000 24.59226 ? 275 TYR A CE1   1 
ATOM   2128 C  CE2   . TYR A 1 275 ? 34.87396  -15.37149 -20.06794 1.000 24.55707 ? 275 TYR A CE2   1 
ATOM   2129 C  CZ    . TYR A 1 275 ? 34.09695  -16.28149 -19.38195 1.000 26.63524 ? 275 TYR A CZ    1 
ATOM   2130 O  OH    . TYR A 1 275 ? 32.75395  -16.38349 -19.66597 1.000 21.89602 ? 275 TYR A OH    1 
ATOM   2131 N  N     . ARG A 1 276 ? 40.91697  -15.78793 -16.60608 1.000 20.83881 ? 276 ARG A N     1 
ATOM   2132 C  CA    . ARG A 1 276 ? 42.37549  -15.77504 -16.56280 1.000 17.51396 ? 276 ARG A CA    1 
ATOM   2133 C  C     . ARG A 1 276 ? 42.92573  -16.87812 -15.66816 1.000 21.21885 ? 276 ARG A C     1 
ATOM   2134 O  O     . ARG A 1 276 ? 44.04784  -17.34823 -15.88882 1.000 17.08423 ? 276 ARG A O     1 
ATOM   2135 C  CB    . ARG A 1 276 ? 42.87402  -14.40565 -16.10169 1.000 17.78438 ? 276 ARG A CB    1 
ATOM   2136 C  CG    . ARG A 1 276 ? 42.86292  -13.35554 -17.20189 1.000 17.78272 ? 276 ARG A CG    1 
ATOM   2137 C  CD    . ARG A 1 276 ? 43.20103  -11.97322 -16.67151 0.000 19.17290 ? 276 ARG A CD    1 
ATOM   2138 N  NE    . ARG A 1 276 ? 42.10332  -11.39967 -15.90263 0.000 20.29318 ? 276 ARG A NE    1 
ATOM   2139 C  CZ    . ARG A 1 276 ? 42.08927  -10.16217 -15.42673 0.000 21.12609 ? 276 ARG A CZ    1 
ATOM   2140 N  NH1   . ARG A 1 276 ? 43.10511  -9.33645  -15.61787 0.000 20.88685 ? 276 ARG A NH1   1 
ATOM   2141 N  NH2   . ARG A 1 276 ? 41.02819  -9.74142  -14.74454 0.000 22.42765 ? 276 ARG A NH2   1 
ATOM   2142 N  N     . ARG A 1 277 ? 42.15888  -17.30558 -14.66518 1.000 23.31888 ? 277 ARG A N     1 
ATOM   2143 C  CA    . ARG A 1 277 ? 42.55708  -18.41011 -13.80287 1.000 21.21042 ? 277 ARG A CA    1 
ATOM   2144 C  C     . ARG A 1 277 ? 41.99822  -19.75207 -14.25717 1.000 25.95657 ? 277 ARG A C     1 
ATOM   2145 O  O     . ARG A 1 277 ? 42.40150  -20.78791 -13.71708 1.000 28.27490 ? 277 ARG A O     1 
ATOM   2146 C  CB    . ARG A 1 277 ? 42.12254  -18.14247 -12.35666 1.000 23.43836 ? 277 ARG A CB    1 
ATOM   2147 C  CG    . ARG A 1 277 ? 42.89057  -17.02407 -11.67164 1.000 23.88813 ? 277 ARG A CG    1 
ATOM   2148 C  CD    . ARG A 1 277 ? 42.51588  -16.90613 -10.20040 1.000 35.81415 ? 277 ARG A CD    1 
ATOM   2149 N  NE    . ARG A 1 277 ? 41.12080  -16.52496 -10.01532 0.297 28.16288 ? 277 ARG A NE    1 
ATOM   2150 C  CZ    . ARG A 1 277 ? 40.69495  -15.27474 -9.89680  0.155 28.26534 ? 277 ARG A CZ    1 
ATOM   2151 N  NH1   . ARG A 1 277 ? 41.53317  -14.25192 -9.93816  0.000 28.66318 ? 277 ARG A NH1   1 
ATOM   2152 N  NH2   . ARG A 1 277 ? 39.39532  -15.04488 -9.73246  0.000 27.86611 ? 277 ARG A NH2   1 
ATOM   2153 N  N     . HIS A 1 278 ? 41.08688  -19.76152 -15.22586 1.000 21.94891 ? 278 HIS A N     1 
ATOM   2154 C  CA    . HIS A 1 278 ? 40.53688  -20.99852 -15.78087 1.000 27.98223 ? 278 HIS A CA    1 
ATOM   2155 C  C     . HIS A 1 278 ? 40.82991  -21.03451 -17.27387 1.000 22.94974 ? 278 HIS A C     1 
ATOM   2156 O  O     . HIS A 1 278 ? 40.08492  -20.43751 -18.07188 1.000 18.10447 ? 278 HIS A O     1 
ATOM   2157 C  CB    . HIS A 1 278 ? 39.03588  -21.09852 -15.51390 1.000 26.79902 ? 278 HIS A CB    1 
ATOM   2158 C  CG    . HIS A 1 278 ? 38.69186  -21.18952 -14.05890 1.000 27.90552 ? 278 HIS A CG    1 
ATOM   2159 N  ND1   . HIS A 1 278 ? 38.67885  -20.09153 -13.22790 1.000 26.15914 ? 278 HIS A ND1   1 
ATOM   2160 C  CD2   . HIS A 1 278 ? 38.36384  -22.25152 -13.28391 1.000 24.78442 ? 278 HIS A CD2   1 
ATOM   2161 C  CE1   . HIS A 1 278 ? 38.34983  -20.46953 -12.00590 1.000 27.77260 ? 278 HIS A CE1   1 
ATOM   2162 N  NE2   . HIS A 1 278 ? 38.15383  -21.77553 -12.01291 1.000 25.76399 ? 278 HIS A NE2   1 
ATOM   2163 N  N     . PRO A 1 279 ? 41.89291  -21.72351 -17.69985 1.000 24.73314 ? 279 PRO A N     1 
ATOM   2164 C  CA    . PRO A 1 279 ? 42.32893  -21.59151 -19.10185 1.000 24.26196 ? 279 PRO A CA    1 
ATOM   2165 C  C     . PRO A 1 279 ? 41.36995  -22.20451 -20.10586 1.000 21.36084 ? 279 PRO A C     1 
ATOM   2166 O  O     . PRO A 1 279 ? 41.21997  -21.66850 -21.21086 1.000 25.47741 ? 279 PRO A O     1 
ATOM   2167 C  CB    . PRO A 1 279 ? 43.68993  -22.30151 -19.10583 1.000 27.90393 ? 279 PRO A CB    1 
ATOM   2168 C  CG    . PRO A 1 279 ? 43.59591  -23.29052 -17.99183 1.000 29.22218 ? 279 PRO A CG    1 
ATOM   2169 C  CD    . PRO A 1 279 ? 42.75490  -22.63652 -16.92984 1.000 24.48229 ? 279 PRO A CD    1 
ATOM   2170 N  N     . ALA A 1 280 ? 40.71494  -23.31451 -19.76088 1.000 19.83311 ? 280 ALA A N     1 
ATOM   2171 C  CA    . ALA A 1 280 ? 39.80295  -23.99550 -20.67489 1.000 27.38553 ? 280 ALA A CA    1 
ATOM   2172 C  C     . ALA A 1 280 ? 38.39395  -23.41750 -20.63991 1.000 23.68564 ? 280 ALA A C     1 
ATOM   2173 O  O     . ALA A 1 280 ? 37.42396  -24.14950 -20.87793 1.000 26.30520 ? 280 ALA A O     1 
ATOM   2174 C  CB    . ALA A 1 280 ? 39.76995  -25.49250 -20.36490 1.000 27.83212 ? 280 ALA A CB    1 
ATOM   2175 N  N     . HIS A 1 281 ? 38.25295  -22.12550 -20.35691 1.000 17.09769 ? 281 HIS A N     1 
ATOM   2176 C  CA    . HIS A 1 281 ? 36.93295  -21.52350 -20.26293 1.000 20.03680 ? 281 HIS A CA    1 
ATOM   2177 C  C     . HIS A 1 281 ? 36.24997  -21.50749 -21.62694 1.000 24.50938 ? 281 HIS A C     1 
ATOM   2178 O  O     . HIS A 1 281 ? 36.88999  -21.58649 -22.67893 1.000 25.93691 ? 281 HIS A O     1 
ATOM   2179 C  CB    . HIS A 1 281 ? 37.02695  -20.10350 -19.70192 1.000 24.90874 ? 281 HIS A CB    1 
ATOM   2180 C  CG    . HIS A 1 281 ? 37.67396  -19.12650 -20.63291 1.000 26.88107 ? 281 HIS A CG    1 
ATOM   2181 N  ND1   . HIS A 1 281 ? 36.97598  -18.45949 -21.61692 1.000 25.62935 ? 281 HIS A ND1   1 
ATOM   2182 C  CD2   . HIS A 1 281 ? 38.95596  -18.70250 -20.72889 1.000 22.75381 ? 281 HIS A CD2   1 
ATOM   2183 C  CE1   . HIS A 1 281 ? 37.79899  -17.66749 -22.27890 1.000 24.64443 ? 281 HIS A CE1   1 
ATOM   2184 N  NE2   . HIS A 1 281 ? 39.00698  -17.79650 -21.75988 1.000 29.12582 ? 281 HIS A NE2   1 
ATOM   2185 N  N     . SER A 1 282 ? 34.92497  -21.40349 -21.59496 1.000 26.80127 ? 282 SER A N     1 
ATOM   2186 C  CA    . SER A 1 282 ? 34.14199  -21.40848 -22.82097 1.000 21.19311 ? 282 SER A CA    1 
ATOM   2187 C  C     . SER A 1 282 ? 34.35801  -20.12048 -23.60896 1.000 22.35988 ? 282 SER A C     1 
ATOM   2188 O  O     . SER A 1 282 ? 34.60700  -19.05048 -23.04596 1.000 23.41565 ? 282 SER A O     1 
ATOM   2189 C  CB    . SER A 1 282 ? 32.65799  -21.58648 -22.50299 1.000 27.26647 ? 282 SER A CB    1 
ATOM   2190 O  OG    . SER A 1 282 ? 32.22297  -20.63248 -21.54900 1.000 22.90455 ? 282 SER A OG    1 
ATOM   2191 N  N     . GLN A 1 283 ? 34.26003  -20.23648 -24.92496 1.000 23.99850 ? 283 GLN A N     1 
ATOM   2192 C  CA    . GLN A 1 283 ? 34.43004  -19.13047 -25.84996 1.000 23.90173 ? 283 GLN A CA    1 
ATOM   2193 C  C     . GLN A 1 283 ? 33.08305  -18.66947 -26.38698 1.000 22.00324 ? 283 GLN A C     1 
ATOM   2194 O  O     . GLN A 1 283 ? 32.10005  -19.41647 -26.35599 1.000 22.68126 ? 283 GLN A O     1 
ATOM   2195 C  CB    . GLN A 1 283 ? 35.33906  -19.54847 -27.01195 1.000 21.79037 ? 283 GLN A CB    1 
ATOM   2196 C  CG    . GLN A 1 283 ? 36.77205  -19.85047 -26.60093 1.000 28.31095 ? 283 GLN A CG    1 
ATOM   2197 C  CD    . GLN A 1 283 ? 37.50105  -18.62748 -26.07791 1.000 24.17186 ? 283 GLN A CD    1 
ATOM   2198 O  OE1   . GLN A 1 283 ? 38.31803  -18.72148 -25.16290 1.000 25.31694 ? 283 GLN A OE1   1 
ATOM   2199 N  NE2   . GLN A 1 283 ? 37.21506  -17.47047 -26.66491 1.000 25.83232 ? 283 GLN A NE2   1 
ATOM   2200 N  N     . PRO A 1 284 ? 32.99506  -17.43247 -26.87097 1.000 21.80077 ? 284 PRO A N     1 
ATOM   2201 C  CA    . PRO A 1 284 ? 31.74307  -16.95146 -27.46899 1.000 24.26489 ? 284 PRO A CA    1 
ATOM   2202 C  C     . PRO A 1 284 ? 31.34009  -17.80646 -28.65700 1.000 16.44128 ? 284 PRO A C     1 
ATOM   2203 O  O     . PRO A 1 284 ? 32.18910  -18.47146 -29.26999 1.000 19.58227 ? 284 PRO A O     1 
ATOM   2204 C  CB    . PRO A 1 284 ? 32.09108  -15.51946 -27.90498 1.000 22.29645 ? 284 PRO A CB    1 
ATOM   2205 C  CG    . PRO A 1 284 ? 33.19507  -15.11347 -26.99696 1.000 22.00645 ? 284 PRO A CG    1 
ATOM   2206 C  CD    . PRO A 1 284 ? 33.99906  -16.35847 -26.75796 1.000 22.64394 ? 284 PRO A CD    1 
ATOM   2207 N  N     . PRO A 1 285 ? 30.05009  -17.81745 -29.02002 1.000 22.00920 ? 285 PRO A N     1 
ATOM   2208 C  CA    . PRO A 1 285 ? 28.93408  -17.07745 -28.41603 1.000 19.86428 ? 285 PRO A CA    1 
ATOM   2209 C  C     . PRO A 1 285 ? 28.27207  -17.82146 -27.25905 1.000 23.14492 ? 285 PRO A C     1 
ATOM   2210 O  O     . PRO A 1 285 ? 27.44606  -17.25646 -26.54806 1.000 27.70065 ? 285 PRO A O     1 
ATOM   2211 C  CB    . PRO A 1 285 ? 27.97810  -16.90745 -29.59905 1.000 19.01864 ? 285 PRO A CB    1 
ATOM   2212 C  CG    . PRO A 1 285 ? 28.15311  -18.18644 -30.36905 1.000 19.74387 ? 285 PRO A CG    1 
ATOM   2213 C  CD    . PRO A 1 285 ? 29.62111  -18.54345 -30.23003 1.000 18.08574 ? 285 PRO A CD    1 
ATOM   2214 N  N     . VAL A 1 286 ? 28.61506  -19.09546 -27.04405 1.000 23.26134 ? 286 VAL A N     1 
ATOM   2215 C  CA    . VAL A 1 286 ? 27.96504  -19.88346 -25.99806 1.000 20.92908 ? 286 VAL A CA    1 
ATOM   2216 C  C     . VAL A 1 286 ? 28.43402  -19.52547 -24.59805 1.000 25.29910 ? 286 VAL A C     1 
ATOM   2217 O  O     . VAL A 1 286 ? 27.79901  -19.94047 -23.62106 1.000 25.42608 ? 286 VAL A O     1 
ATOM   2218 C  CB    . VAL A 1 286 ? 28.18904  -21.38946 -26.22806 1.000 21.38326 ? 286 VAL A CB    1 
ATOM   2219 C  CG1   . VAL A 1 286 ? 27.64906  -21.80545 -27.58807 1.000 32.44987 ? 286 VAL A CG1   1 
ATOM   2220 C  CG2   . VAL A 1 286 ? 29.66604  -21.73146 -26.10704 1.000 17.88697 ? 286 VAL A CG2   1 
ATOM   2221 N  N     . SER A 1 287 ? 29.52002  -18.76847 -24.46903 1.000 26.37435 ? 287 SER A N     1 
ATOM   2222 C  CA    . SER A 1 287 ? 30.04800  -18.42347 -23.16002 1.000 27.91406 ? 287 SER A CA    1 
ATOM   2223 C  C     . SER A 1 287 ? 29.19699  -17.33847 -22.50303 1.000 25.07634 ? 287 SER A C     1 
ATOM   2224 O  O     . SER A 1 287 ? 28.31700  -16.73447 -23.12304 1.000 24.63008 ? 287 SER A O     1 
ATOM   2225 C  CB    . SER A 1 287 ? 31.50000  -17.96248 -23.27300 1.000 29.03765 ? 287 SER A CB    1 
ATOM   2226 O  OG    . SER A 1 287 ? 31.60602  -16.80447 -24.08199 1.000 30.62849 ? 287 SER A OG    1 
ATOM   2227 N  N     . LEU A 1 288 ? 29.46897  -17.09848 -21.21803 1.000 24.51516 ? 288 LEU A N     1 
ATOM   2228 C  CA    . LEU A 1 288 ? 28.78697  -16.01748 -20.51203 1.000 24.37697 ? 288 LEU A CA    1 
ATOM   2229 C  C     . LEU A 1 288 ? 29.19598  -14.66048 -21.06602 1.000 21.58021 ? 288 LEU A C     1 
ATOM   2230 O  O     . LEU A 1 288 ? 28.37198  -13.74148 -21.14803 1.000 24.44350 ? 288 LEU A O     1 
ATOM   2231 C  CB    . LEU A 1 288 ? 29.07794  -16.09949 -19.01403 1.000 22.07314 ? 288 LEU A CB    1 
ATOM   2232 C  CG    . LEU A 1 288 ? 27.88893  -16.43449 -18.11305 1.000 21.58119 ? 288 LEU A CG    1 
ATOM   2233 C  CD1   . LEU A 1 288 ? 28.30691  -16.45049 -16.65104 1.000 20.32479 ? 288 LEU A CD1   1 
ATOM   2234 C  CD2   . LEU A 1 288 ? 26.75093  -15.45049 -18.33906 1.000 19.30330 ? 288 LEU A CD2   1 
ATOM   2235 N  N     . ARG A 1 289 ? 30.46618  -14.51653 -21.45170 1.000 22.36802 ? 289 ARG A N     1 
ATOM   2236 C  CA    . ARG A 1 289 ? 30.90319  -13.29681 -22.12040 1.000 24.00690 ? 289 ARG A CA    1 
ATOM   2237 C  C     . ARG A 1 289 ? 30.25741  -13.15582 -23.49148 1.000 22.22709 ? 289 ARG A C     1 
ATOM   2238 O  O     . ARG A 1 289 ? 29.95947  -12.03667 -23.92424 1.000 20.72804 ? 289 ARG A O     1 
ATOM   2239 C  CB    . ARG A 1 289 ? 32.42595  -13.28604 -22.24765 1.000 22.27160 ? 289 ARG A CB    1 
ATOM   2240 C  CG    . ARG A 1 289 ? 33.00299  -11.97636 -22.75492 1.000 21.99926 ? 289 ARG A CG    1 
ATOM   2241 C  CD    . ARG A 1 289 ? 34.49623  -12.09861 -23.00461 1.000 24.88617 ? 289 ARG A CD    1 
ATOM   2242 N  NE    . ARG A 1 289 ? 34.80424  -12.37999 -24.40138 1.000 28.76263 ? 289 ARG A NE    1 
ATOM   2243 C  CZ    . ARG A 1 289 ? 35.11671  -11.45488 -25.29862 1.000 27.70390 ? 289 ARG A CZ    1 
ATOM   2244 N  NH1   . ARG A 1 289 ? 35.16235  -10.17129 -24.98103 1.000 26.63845 ? 289 ARG A NH1   1 
ATOM   2245 N  NH2   . ARG A 1 289 ? 35.39279  -11.82688 -26.54513 1.000 34.47004 ? 289 ARG A NH2   1 
ATOM   2246 N  N     . GLY A 1 290 ? 30.03503  -14.27447 -24.18401 1.000 23.15240 ? 290 GLY A N     1 
ATOM   2247 C  CA    . GLY A 1 290 ? 29.35804  -14.21646 -25.46902 1.000 22.19271 ? 290 GLY A CA    1 
ATOM   2248 C  C     . GLY A 1 290 ? 27.93804  -13.69946 -25.35304 1.000 21.09985 ? 290 GLY A C     1 
ATOM   2249 O  O     . GLY A 1 290 ? 27.45806  -12.97646 -26.22804 1.000 16.37176 ? 290 GLY A O     1 
ATOM   2250 N  N     . GLN A 1 291 ? 27.24903  -14.05546 -24.26605 1.000 24.53262 ? 291 GLN A N     1 
ATOM   2251 C  CA    . GLN A 1 291 ? 25.88602  -13.57246 -24.06507 1.000 19.88278 ? 291 GLN A CA    1 
ATOM   2252 C  C     . GLN A 1 291 ? 25.85902  -12.06046 -23.88506 1.000 19.68176 ? 291 GLN A C     1 
ATOM   2253 O  O     . GLN A 1 291 ? 24.92803  -11.38946 -24.34708 1.000 13.63838 ? 291 GLN A O     1 
ATOM   2254 C  CB    . GLN A 1 291 ? 25.25001  -14.27447 -22.86608 1.000 20.45119 ? 291 GLN A CB    1 
ATOM   2255 C  CG    . GLN A 1 291 ? 25.15300  -15.78247 -23.02409 1.000 20.13758 ? 291 GLN A CG    1 
ATOM   2256 C  CD    . GLN A 1 291 ? 24.44202  -16.18746 -24.30110 1.000 23.23775 ? 291 GLN A CD    1 
ATOM   2257 O  OE1   . GLN A 1 291 ? 23.36003  -15.68846 -24.60912 1.000 23.09221 ? 291 GLN A OE1   1 
ATOM   2258 N  NE2   . GLN A 1 291 ? 25.05503  -17.09046 -25.05909 1.000 26.97351 ? 291 GLN A NE2   1 
ATOM   2259 N  N     . LEU A 1 292 ? 26.87202  -11.50347 -23.21605 1.000 16.51962 ? 292 LEU A N     1 
ATOM   2260 C  CA    . LEU A 1 292 ? 27.00102  -10.05247 -23.16304 1.000 14.29650 ? 292 LEU A CA    1 
ATOM   2261 C  C     . LEU A 1 292 ? 27.32904  -9.47446  -24.53303 1.000 18.38219 ? 292 LEU A C     1 
ATOM   2262 O  O     . LEU A 1 292 ? 26.91005  -8.35446  -24.84903 1.000 16.17165 ? 292 LEU A O     1 
ATOM   2263 C  CB    . LEU A 1 292 ? 28.07200  -9.64847  -22.14902 1.000 20.14876 ? 292 LEU A CB    1 
ATOM   2264 C  CG    . LEU A 1 292 ? 27.71098  -9.77948  -20.66903 1.000 15.34747 ? 292 LEU A CG    1 
ATOM   2265 C  CD1   . LEU A 1 292 ? 28.85497  -9.28248  -19.79701 1.000 17.78839 ? 292 LEU A CD1   1 
ATOM   2266 C  CD2   . LEU A 1 292 ? 26.43198  -9.01748  -20.36304 1.000 13.21362 ? 292 LEU A CD2   1 
ATOM   2267 N  N     . LEU A 1 293 ? 28.07305  -10.21846 -25.35502 1.000 17.05276 ? 293 LEU A N     1 
ATOM   2268 C  CA    . LEU A 1 293 ? 28.35107  -9.76146  -26.71102 1.000 22.19852 ? 293 LEU A CA    1 
ATOM   2269 C  C     . LEU A 1 293 ? 27.10209  -9.80145  -27.58104 1.000 17.13338 ? 293 LEU A C     1 
ATOM   2270 O  O     . LEU A 1 293 ? 26.97110  -8.99345  -28.50704 1.000 24.77844 ? 293 LEU A O     1 
ATOM   2271 C  CB    . LEU A 1 293 ? 29.46808  -10.60046 -27.33300 1.000 21.53854 ? 293 LEU A CB    1 
ATOM   2272 C  CG    . LEU A 1 293 ? 30.85907  -10.44546 -26.71498 1.000 23.72423 ? 293 LEU A CG    1 
ATOM   2273 C  CD1   . LEU A 1 293 ? 31.85308  -11.38346 -27.38297 1.000 27.21766 ? 293 LEU A CD1   1 
ATOM   2274 C  CD2   . LEU A 1 293 ? 31.32907  -9.00246  -26.81197 1.000 23.74832 ? 293 LEU A CD2   1 
ATOM   2275 N  N     . TRP A 1 294 ? 26.18208  -10.73245 -27.30705 1.000 19.46934 ? 294 TRP A N     1 
ATOM   2276 C  CA    . TRP A 1 294 ? 24.88109  -10.69645 -27.96907 1.000 19.83239 ? 294 TRP A CA    1 
ATOM   2277 C  C     . TRP A 1 294 ? 24.15309  -9.39545  -27.65808 1.000 18.71858 ? 294 TRP A C     1 
ATOM   2278 O  O     . TRP A 1 294 ? 23.50510  -8.80944  -28.53309 1.000 25.32263 ? 294 TRP A O     1 
ATOM   2279 C  CB    . TRP A 1 294 ? 24.02808  -11.89345 -27.54209 1.000 18.44934 ? 294 TRP A CB    1 
ATOM   2280 C  CG    . TRP A 1 294 ? 24.45409  -13.20745 -28.12609 1.000 19.70281 ? 294 TRP A CG    1 
ATOM   2281 C  CD1   . TRP A 1 294 ? 25.08208  -14.22945 -27.47608 1.000 20.72446 ? 294 TRP A CD1   1 
ATOM   2282 C  CD2   . TRP A 1 294 ? 24.27011  -13.64644 -29.47709 1.000 18.75949 ? 294 TRP A CD2   1 
ATOM   2283 N  NE1   . TRP A 1 294 ? 25.30709  -15.27445 -28.33808 1.000 16.44085 ? 294 TRP A NE1   1 
ATOM   2284 C  CE2   . TRP A 1 294 ? 24.81711  -14.94144 -29.57409 1.000 20.95709 ? 294 TRP A CE2   1 
ATOM   2285 C  CE3   . TRP A 1 294 ? 23.69813  -13.06944 -30.61510 1.000 25.49957 ? 294 TRP A CE3   1 
ATOM   2286 C  CZ2   . TRP A 1 294 ? 24.80912  -15.66844 -30.76209 1.000 27.61682 ? 294 TRP A CZ2   1 
ATOM   2287 C  CZ3   . TRP A 1 294 ? 23.69214  -13.79243 -31.79410 1.000 25.58523 ? 294 TRP A CZ3   1 
ATOM   2288 C  CH2   . TRP A 1 294 ? 24.24414  -15.07843 -31.85810 1.000 30.35473 ? 294 TRP A CH2   1 
ATOM   2289 N  N     . ARG A 1 295 ? 24.25216  -8.92887  -26.41196 1.000 17.53921 ? 295 ARG A N     1 
ATOM   2290 C  CA    . ARG A 1 295 ? 23.64436  -7.65691  -26.03872 1.000 14.00469 ? 295 ARG A CA    1 
ATOM   2291 C  C     . ARG A 1 295 ? 24.34323  -6.49010  -26.72680 1.000 19.33815 ? 295 ARG A C     1 
ATOM   2292 O  O     . ARG A 1 295 ? 23.69562  -5.50562  -27.10120 1.000 14.46716 ? 295 ARG A O     1 
ATOM   2293 C  CB    . ARG A 1 295 ? 23.68016  -7.50014  -24.51800 1.000 14.37859 ? 295 ARG A CB    1 
ATOM   2294 C  CG    . ARG A 1 295 ? 23.13081  -6.18904  -23.98612 1.000 14.05096 ? 295 ARG A CG    1 
ATOM   2295 C  CD    . ARG A 1 295 ? 23.10997  -6.20578  -22.46496 1.000 17.01013 ? 295 ARG A CD    1 
ATOM   2296 N  NE    . ARG A 1 295 ? 22.77818  -4.90585  -21.89505 1.000 18.14814 ? 295 ARG A NE    1 
ATOM   2297 C  CZ    . ARG A 1 295 ? 23.67254  -3.98524  -21.56250 1.000 14.66240 ? 295 ARG A CZ    1 
ATOM   2298 N  NH1   . ARG A 1 295 ? 24.96758  -4.18196  -21.74582 1.000 17.98552 ? 295 ARG A NH1   1 
ATOM   2299 N  NH2   . ARG A 1 295 ? 23.25730  -2.83889  -21.03190 1.000 20.72054 ? 295 ARG A NH2   1 
ATOM   2300 N  N     . GLU A 1 296 ? 25.66408  -6.58545  -26.90905 1.000 20.16919 ? 296 GLU A N     1 
ATOM   2301 C  CA    . GLU A 1 296 ? 26.39409  -5.53145  -27.60903 1.000 20.84001 ? 296 GLU A CA    1 
ATOM   2302 C  C     . GLU A 1 296 ? 26.13412  -5.58045  -29.10804 1.000 25.72040 ? 296 GLU A C     1 
ATOM   2303 O  O     . GLU A 1 296 ? 26.07813  -4.53644  -29.76803 1.000 33.21775 ? 296 GLU A O     1 
ATOM   2304 C  CB    . GLU A 1 296 ? 27.89209  -5.64946  -27.33101 1.000 23.24852 ? 296 GLU A CB    1 
ATOM   2305 C  CG    . GLU A 1 296 ? 28.29307  -5.28146  -25.92000 1.000 26.09983 ? 296 GLU A CG    1 
ATOM   2306 C  CD    . GLU A 1 296 ? 28.04907  -3.82046  -25.61100 1.000 24.61996 ? 296 GLU A CD    1 
ATOM   2307 O  OE1   . GLU A 1 296 ? 28.48008  -2.96046  -26.40899 1.000 19.68934 ? 296 GLU A OE1   1 
ATOM   2308 O  OE2   . GLU A 1 296 ? 27.42305  -3.53246  -24.57101 1.000 32.65902 ? 296 GLU A OE2   1 
ATOM   2309 N  N     . PHE A 1 297 ? 25.98412  -6.78344  -29.66204 1.000 25.44717 ? 297 PHE A N     1 
ATOM   2310 C  CA    . PHE A 1 297 ? 25.78914  -6.91944  -31.10105 1.000 26.28631 ? 297 PHE A CA    1 
ATOM   2311 C  C     . PHE A 1 297 ? 24.44715  -6.34343  -31.53307 1.000 28.92586 ? 297 PHE A C     1 
ATOM   2312 O  O     . PHE A 1 297 ? 24.37217  -5.57443  -32.49806 1.000 32.95481 ? 297 PHE A O     1 
ATOM   2313 C  CB    . PHE A 1 297 ? 25.90815  -8.39044  -31.50405 1.000 24.24667 ? 297 PHE A CB    1 
ATOM   2314 C  CG    . PHE A 1 297 ? 25.50917  -8.66543  -32.92406 1.000 28.29647 ? 297 PHE A CG    1 
ATOM   2315 C  CD1   . PHE A 1 297 ? 26.21619  -8.10843  -33.97604 1.000 28.61169 ? 297 PHE A CD1   1 
ATOM   2316 C  CD2   . PHE A 1 297 ? 24.43417  -9.49043  -33.20708 1.000 25.82869 ? 297 PHE A CD2   1 
ATOM   2317 C  CE1   . PHE A 1 297 ? 25.85221  -8.36342  -35.28405 1.000 26.06109 ? 297 PHE A CE1   1 
ATOM   2318 C  CE2   . PHE A 1 297 ? 24.06619  -9.74942  -34.51208 1.000 23.60254 ? 297 PHE A CE2   1 
ATOM   2319 C  CZ    . PHE A 1 297 ? 24.77621  -9.18542  -35.55207 1.000 26.70899 ? 297 PHE A CZ    1 
ATOM   2320 N  N     . PHE A 1 298 ? 23.37314  -6.69643  -30.82308 1.000 17.80714 ? 298 PHE A N     1 
ATOM   2321 C  CA    . PHE A 1 298 ? 22.05215  -6.20443  -31.19810 1.000 24.43085 ? 298 PHE A CA    1 
ATOM   2322 C  C     . PHE A 1 298 ? 21.91315  -4.70743  -30.95010 1.000 22.29855 ? 298 PHE A C     1 
ATOM   2323 O  O     . PHE A 1 298 ? 21.17316  -4.02943  -31.67111 1.000 21.95224 ? 298 PHE A O     1 
ATOM   2324 C  CB    . PHE A 1 298 ? 20.97113  -6.97743  -30.44212 1.000 22.60736 ? 298 PHE A CB    1 
ATOM   2325 C  CG    . PHE A 1 298 ? 20.86414  -8.41943  -30.84813 1.000 20.29883 ? 298 PHE A CG    1 
ATOM   2326 C  CD1   . PHE A 1 298 ? 21.20216  -8.81843  -32.13212 1.000 22.45138 ? 298 PHE A CD1   1 
ATOM   2327 C  CD2   . PHE A 1 298 ? 20.43212  -9.37643  -29.94614 1.000 16.62294 ? 298 PHE A CD2   1 
ATOM   2328 C  CE1   . PHE A 1 298 ? 21.10516  -10.14442 -32.50913 1.000 18.85870 ? 298 PHE A CE1   1 
ATOM   2329 C  CE2   . PHE A 1 298 ? 20.33413  -10.70543 -30.31714 1.000 23.42634 ? 298 PHE A CE2   1 
ATOM   2330 C  CZ    . PHE A 1 298 ? 20.67114  -11.08943 -31.60014 1.000 23.97818 ? 298 PHE A CZ    1 
ATOM   2331 N  N     . TYR A 1 299 ? 22.61213  -4.17544  -29.94509 1.000 20.19944 ? 299 TYR A N     1 
ATOM   2332 C  CA    . TYR A 1 299 ? 22.57513  -2.73644  -29.70508 1.000 24.64658 ? 299 TYR A CA    1 
ATOM   2333 C  C     . TYR A 1 299 ? 23.31015  -1.96643  -30.79307 1.000 21.86278 ? 299 TYR A C     1 
ATOM   2334 O  O     . TYR A 1 299 ? 22.95415  -0.81943  -31.08707 1.000 30.93034 ? 299 TYR A O     1 
ATOM   2335 C  CB    . TYR A 1 299 ? 23.16611  -2.41244  -28.33407 1.000 20.82692 ? 299 TYR A CB    1 
ATOM   2336 C  CG    . TYR A 1 299 ? 22.13109  -2.15745  -27.26409 1.000 22.48612 ? 299 TYR A CG    1 
ATOM   2337 C  CD1   . TYR A 1 299 ? 21.61908  -3.19845  -26.50110 1.000 17.05755 ? 299 TYR A CD1   1 
ATOM   2338 C  CD2   . TYR A 1 299 ? 21.66609  -0.87245  -27.01509 1.000 20.54215 ? 299 TYR A CD2   1 
ATOM   2339 C  CE1   . TYR A 1 299 ? 20.67307  -2.96745  -25.52211 1.000 18.38834 ? 299 TYR A CE1   1 
ATOM   2340 C  CE2   . TYR A 1 299 ? 20.72008  -0.63145  -26.03710 1.000 19.20796 ? 299 TYR A CE2   1 
ATOM   2341 C  CZ    . TYR A 1 299 ? 20.22706  -1.68445  -25.29311 1.000 19.65224 ? 299 TYR A CZ    1 
ATOM   2342 O  OH    . TYR A 1 299 ? 19.28505  -1.44945  -24.31813 1.000 15.15822 ? 299 TYR A OH    1 
ATOM   2343 N  N     . THR A 1 300 ? 24.33216  -2.57343  -31.40005 1.000 21.40433 ? 300 THR A N     1 
ATOM   2344 C  CA    . THR A 1 300 ? 25.07717  -1.89943  -32.45604 1.000 19.43844 ? 300 THR A CA    1 
ATOM   2345 C  C     . THR A 1 300 ? 24.30019  -1.88743  -33.76805 1.000 23.20905 ? 300 THR A C     1 
ATOM   2346 O  O     . THR A 1 300 ? 24.32821  -0.89042  -34.50005 1.000 21.33084 ? 300 THR A O     1 
ATOM   2347 C  CB    . THR A 1 300 ? 26.43918  -2.57043  -32.64802 1.000 21.49360 ? 300 THR A CB    1 
ATOM   2348 O  OG1   . THR A 1 300 ? 27.12016  -2.64144  -31.38801 1.000 24.09158 ? 300 THR A OG1   1 
ATOM   2349 C  CG2   . THR A 1 300 ? 27.29019  -1.78243  -33.63201 1.000 24.79266 ? 300 THR A CG2   1 
ATOM   2350 N  N     . VAL A 1 301 ? 23.59720  -2.97842  -34.07707 1.000 25.07864 ? 301 VAL A N     1 
ATOM   2351 C  CA    . VAL A 1 301 ? 22.86122  -3.05642  -35.33508 1.000 24.44131 ? 301 VAL A CA    1 
ATOM   2352 C  C     . VAL A 1 301 ? 21.57622  -2.24242  -35.26509 1.000 22.75107 ? 301 VAL A C     1 
ATOM   2353 O  O     . VAL A 1 301 ? 21.24423  -1.50841  -36.20210 1.000 24.98273 ? 301 VAL A O     1 
ATOM   2354 C  CB    . VAL A 1 301 ? 22.57622  -4.52642  -35.69309 1.000 23.60177 ? 301 VAL A CB    1 
ATOM   2355 C  CG1   . VAL A 1 301 ? 21.94224  -4.62341  -37.07310 1.000 27.80443 ? 301 VAL A CG1   1 
ATOM   2356 C  CG2   . VAL A 1 301 ? 23.85022  -5.34442  -35.62607 1.000 22.97060 ? 301 VAL A CG2   1 
ATOM   2357 N  N     . GLY A 1 302 ? 20.83620  -2.35742  -34.16011 1.000 25.02824 ? 302 GLY A N     1 
ATOM   2358 C  CA    . GLY A 1 302 ? 19.56420  -1.66442  -34.05212 1.000 23.52113 ? 302 GLY A CA    1 
ATOM   2359 C  C     . GLY A 1 302 ? 19.69320  -0.15642  -34.00112 1.000 27.14722 ? 302 GLY A C     1 
ATOM   2360 O  O     . GLY A 1 302 ? 18.80621  0.56159   -34.47213 1.000 30.00600 ? 302 GLY A O     1 
ATOM   2361 N  N     . SER A 1 303 ? 20.79219  0.34758   -33.43410 1.000 24.94676 ? 303 SER A N     1 
ATOM   2362 C  CA    . SER A 1 303 ? 20.98119  1.78958   -33.33309 1.000 25.54309 ? 303 SER A CA    1 
ATOM   2363 C  C     . SER A 1 303 ? 21.29822  2.43158   -34.67708 1.000 26.25548 ? 303 SER A C     1 
ATOM   2364 O  O     . SER A 1 303 ? 21.17022  3.65358   -34.81008 1.000 22.15133 ? 303 SER A O     1 
ATOM   2365 C  CB    . SER A 1 303 ? 22.09218  2.10357   -32.32807 1.000 27.00052 ? 303 SER A CB    1 
ATOM   2366 O  OG    . SER A 1 303 ? 23.28318  1.40457   -32.64506 1.000 22.39359 ? 303 SER A OG    1 
ATOM   2367 N  N     . THR A 1 304 ? 21.70123  1.64459   -35.67208 1.000 29.84007 ? 304 THR A N     1 
ATOM   2368 C  CA    . THR A 1 304 ? 22.04025  2.16859   -36.98707 1.000 25.85793 ? 304 THR A CA    1 
ATOM   2369 C  C     . THR A 1 304 ? 21.06427  1.73660   -38.07209 1.000 28.98277 ? 304 THR A C     1 
ATOM   2370 O  O     . THR A 1 304 ? 21.26428  2.08860   -39.24008 1.000 37.92609 ? 304 THR A O     1 
ATOM   2371 C  CB    . THR A 1 304 ? 23.46026  1.73959   -37.37605 1.000 22.54738 ? 304 THR A CB    1 
ATOM   2372 O  OG1   . THR A 1 304 ? 23.51325  0.31359   -37.50006 1.000 24.82410 ? 304 THR A OG1   1 
ATOM   2373 C  CG2   . THR A 1 304 ? 24.45824  2.18758   -36.31903 1.000 24.41596 ? 304 THR A CG2   1 
ATOM   2374 N  N     . THR A 1 305 ? 20.01626  0.99060   -37.72511 1.000 27.29224 ? 305 THR A N     1 
ATOM   2375 C  CA    . THR A 1 305 ? 19.04627  0.51460   -38.70112 1.000 29.61811 ? 305 THR A CA    1 
ATOM   2376 C  C     . THR A 1 305 ? 17.69327  1.15360   -38.43314 1.000 32.51600 ? 305 THR A C     1 
ATOM   2377 O  O     . THR A 1 305 ? 17.16725  1.02860   -37.31615 1.000 32.10435 ? 305 THR A O     1 
ATOM   2378 C  CB    . THR A 1 305 ? 18.93427  -1.00840  -38.65513 1.000 30.22740 ? 305 THR A CB    1 
ATOM   2379 O  OG1   . THR A 1 305 ? 20.20127  -1.59340  -38.98011 1.000 27.53549 ? 305 THR A OG1   1 
ATOM   2380 C  CG2   . THR A 1 305 ? 17.88928  -1.49339  -39.64815 1.000 28.68679 ? 305 THR A CG2   1 
ATOM   2381 N  N     . PRO A 1 306 ? 17.09629  1.83761   -39.40715 1.000 30.26840 ? 306 PRO A N     1 
ATOM   2382 C  CA    . PRO A 1 306 ? 15.78828  2.45861   -39.17517 1.000 31.32224 ? 306 PRO A CA    1 
ATOM   2383 C  C     . PRO A 1 306 ? 14.68328  1.42061   -39.07619 1.000 34.84021 ? 306 PRO A C     1 
ATOM   2384 O  O     . PRO A 1 306 ? 14.72329  0.36961   -39.72219 1.000 36.45939 ? 306 PRO A O     1 
ATOM   2385 C  CB    . PRO A 1 306 ? 15.59430  3.35661   -40.40517 1.000 26.98204 ? 306 PRO A CB    1 
ATOM   2386 C  CG    . PRO A 1 306 ? 16.95631  3.47461   -41.03214 1.000 36.31848 ? 306 PRO A CG    1 
ATOM   2387 C  CD    . PRO A 1 306 ? 17.65031  2.18861   -40.72414 1.000 35.85885 ? 306 PRO A CD    1 
ATOM   2388 N  N     . ASN A 1 307 ? 13.68127  1.73561   -38.25020 1.000 31.78899 ? 307 ASN A N     1 
ATOM   2389 C  CA    . ASN A 1 307 ? 12.50926  0.87961   -38.05622 1.000 33.28975 ? 307 ASN A CA    1 
ATOM   2390 C  C     . ASN A 1 307 ? 12.91226  -0.52639  -37.61822 1.000 34.07045 ? 307 ASN A C     1 
ATOM   2391 O  O     . ASN A 1 307 ? 12.35626  -1.52439  -38.08123 1.000 35.26711 ? 307 ASN A O     1 
ATOM   2392 C  CB    . ASN A 1 307 ? 11.64628  0.82862   -39.31923 1.000 31.35317 ? 307 ASN A CB    1 
ATOM   2393 C  CG    . ASN A 1 307 ? 11.15329  2.19762   -39.74524 1.000 41.30132 ? 307 ASN A CG    1 
ATOM   2394 O  OD1   . ASN A 1 307 ? 10.08029  2.63962   -39.33425 1.000 46.13958 ? 307 ASN A OD1   1 
ATOM   2395 N  ND2   . ASN A 1 307 ? 11.93831  2.87762   -40.57422 1.000 36.96507 ? 307 ASN A ND2   1 
ATOM   2396 N  N     . PHE A 1 308 ? 13.88824  -0.60640  -36.71121 1.000 26.97134 ? 308 PHE A N     1 
ATOM   2397 C  CA    . PHE A 1 308 ? 14.39323  -1.90040  -36.27120 1.000 32.89268 ? 308 PHE A CA    1 
ATOM   2398 C  C     . PHE A 1 308 ? 13.36322  -2.68340  -35.46722 1.000 34.35406 ? 308 PHE A C     1 
ATOM   2399 O  O     . PHE A 1 308 ? 13.44522  -3.91440  -35.41222 1.000 36.69817 ? 308 PHE A O     1 
ATOM   2400 C  CB    . PHE A 1 308 ? 15.66822  -1.71140  -35.44718 1.000 31.19424 ? 308 PHE A CB    1 
ATOM   2401 C  CG    . PHE A 1 308 ? 16.47421  -2.96841  -35.27717 1.000 29.42664 ? 308 PHE A CG    1 
ATOM   2402 C  CD1   . PHE A 1 308 ? 17.35123  -3.38140  -36.26616 1.000 27.15066 ? 308 PHE A CD1   1 
ATOM   2403 C  CD2   . PHE A 1 308 ? 16.35920  -3.73241  -34.12818 1.000 26.94427 ? 308 PHE A CD2   1 
ATOM   2404 C  CE1   . PHE A 1 308 ? 18.09722  -4.53541  -36.11416 1.000 32.18790 ? 308 PHE A CE1   1 
ATOM   2405 C  CE2   . PHE A 1 308 ? 17.10219  -4.88741  -33.97017 1.000 28.47402 ? 308 PHE A CE2   1 
ATOM   2406 C  CZ    . PHE A 1 308 ? 17.97221  -5.28941  -34.96416 1.000 32.57654 ? 308 PHE A CZ    1 
ATOM   2407 N  N     . HIS A 1 309 ? 12.39921  -2.00540  -34.84823 1.000 32.38967 ? 309 HIS A N     1 
ATOM   2408 C  CA    . HIS A 1 309 ? 11.35920  -2.66040  -34.06725 1.000 31.79027 ? 309 HIS A CA    1 
ATOM   2409 C  C     . HIS A 1 309 ? 10.10021  -2.93940  -34.87827 1.000 35.04233 ? 309 HIS A C     1 
ATOM   2410 O  O     . HIS A 1 309 ? 9.06420   -3.28040  -34.29729 1.000 36.24598 ? 309 HIS A O     1 
ATOM   2411 C  CB    . HIS A 1 309 ? 11.00600  -1.82000  -32.84100 1.000 27.27094 ? 309 HIS A CB    1 
ATOM   2412 C  CG    . HIS A 1 309 ? 10.37400  -0.50300  -33.17000 1.000 34.58248 ? 309 HIS A CG    1 
ATOM   2413 N  ND1   . HIS A 1 309 ? 11.09300  0.56700   -33.65700 1.000 34.61758 ? 309 HIS A ND1   1 
ATOM   2414 C  CD2   . HIS A 1 309 ? 9.09100   -0.08200  -33.07500 1.000 37.81753 ? 309 HIS A CD2   1 
ATOM   2415 C  CE1   . HIS A 1 309 ? 10.28000  1.59000   -33.85200 1.000 34.61685 ? 309 HIS A CE1   1 
ATOM   2416 N  NE2   . HIS A 1 309 ? 9.05900   1.22200   -33.50600 1.000 28.15452 ? 309 HIS A NE2   1 
ATOM   2417 N  N     . ARG A 1 310 ? 10.16351  -2.80284  -36.20006 1.000 35.90434 ? 310 ARG A N     1 
ATOM   2418 C  CA    . ARG A 1 310 ? 9.02515   -3.03441  -37.07517 1.000 35.17826 ? 310 ARG A CA    1 
ATOM   2419 C  C     . ARG A 1 310 ? 9.45940   -3.90715  -38.24502 1.000 37.39663 ? 310 ARG A C     1 
ATOM   2420 O  O     . ARG A 1 310 ? 10.64638  -4.18448  -38.43748 1.000 35.55004 ? 310 ARG A O     1 
ATOM   2421 C  CB    . ARG A 1 310 ? 8.43469   -1.71217  -37.58708 1.000 31.95434 ? 310 ARG A CB    1 
ATOM   2422 C  CG    . ARG A 1 310 ? 8.01111   -0.74832  -36.49000 0.000 35.19138 ? 310 ARG A CG    1 
ATOM   2423 C  CD    . ARG A 1 310 ? 7.60189   0.59759   -37.06565 0.000 36.04520 ? 310 ARG A CD    1 
ATOM   2424 N  NE    . ARG A 1 310 ? 7.27015   1.55977   -36.02167 0.000 35.65410 ? 310 ARG A NE    1 
ATOM   2425 C  CZ    . ARG A 1 310 ? 6.94512   2.82568   -36.24542 0.000 35.54837 ? 310 ARG A CZ    1 
ATOM   2426 N  NH1   . ARG A 1 310 ? 6.89899   3.32122   -37.47124 0.000 35.91753 ? 310 ARG A NH1   1 
ATOM   2427 N  NH2   . ARG A 1 310 ? 6.66051   3.61469   -35.21326 0.000 35.17174 ? 310 ARG A NH2   1 
ATOM   2428 N  N     . MET A 1 311 ? 8.47727   -4.34538  -39.03130 1.000 33.08802 ? 311 MET A N     1 
ATOM   2429 C  CA    . MET A 1 311 ? 8.73529   -5.11337  -40.24230 1.000 37.10799 ? 311 MET A CA    1 
ATOM   2430 C  C     . MET A 1 311 ? 8.70531   -4.24437  -41.49330 1.000 37.49656 ? 311 MET A C     1 
ATOM   2431 O  O     . MET A 1 311 ? 9.57832   -4.36837  -42.35729 1.000 40.86176 ? 311 MET A O     1 
ATOM   2432 C  CB    . MET A 1 311 ? 7.71829   -6.25437  -40.37832 1.000 37.65051 ? 311 MET A CB    1 
ATOM   2433 C  CG    . MET A 1 311 ? 8.04330   -7.24037  -41.49132 1.000 38.35423 ? 311 MET A CG    1 
ATOM   2434 S  SD    . MET A 1 311 ? 6.73830   -8.44937  -41.78434 1.000 45.79286 ? 311 MET A SD    1 
ATOM   2435 C  CE    . MET A 1 311 ? 5.48232   -7.41936  -42.53636 1.000 36.73581 ? 311 MET A CE    1 
ATOM   2436 N  N     . ALA A 1 312 ? 7.71331   -3.36537  -41.60631 1.000 42.92426 ? 312 ALA A N     1 
ATOM   2437 C  CA    . ALA A 1 312 ? 7.64933   -2.45636  -42.73931 1.000 36.58921 ? 312 ALA A CA    1 
ATOM   2438 C  C     . ALA A 1 312 ? 8.67433   -1.34237  -42.57829 1.000 35.96456 ? 312 ALA A C     1 
ATOM   2439 O  O     . ALA A 1 312 ? 8.84531   -0.78537  -41.49028 1.000 38.76504 ? 312 ALA A O     1 
ATOM   2440 C  CB    . ALA A 1 312 ? 6.24433   -1.87136  -42.87333 1.000 26.50249 ? 312 ALA A CB    1 
ATOM   2441 N  N     . GLY A 1 313 ? 9.36535   -1.02436  -43.67128 1.000 39.38812 ? 313 GLY A N     1 
ATOM   2442 C  CA    . GLY A 1 313 ? 10.42035  -0.03437  -43.62526 1.000 33.16749 ? 313 GLY A CA    1 
ATOM   2443 C  C     . GLY A 1 313 ? 11.68134  -0.47537  -42.91824 1.000 38.15080 ? 313 GLY A C     1 
ATOM   2444 O  O     . GLY A 1 313 ? 12.51233  0.37363   -42.58022 1.000 33.77391 ? 313 GLY A O     1 
ATOM   2445 N  N     . ASN A 1 314 ? 11.85433  -1.77337  -42.68124 1.000 39.35735 ? 314 ASN A N     1 
ATOM   2446 C  CA    . ASN A 1 314 ? 13.04832  -2.29138  -42.01922 1.000 38.05471 ? 314 ASN A CA    1 
ATOM   2447 C  C     . ASN A 1 314 ? 13.91433  -3.01637  -43.03921 1.000 37.09779 ? 314 ASN A C     1 
ATOM   2448 O  O     . ASN A 1 314 ? 13.50034  -4.06537  -43.55922 1.000 31.87140 ? 314 ASN A O     1 
ATOM   2449 C  CB    . ASN A 1 314 ? 12.66530  -3.23138  -40.87323 1.000 35.30526 ? 314 ASN A CB    1 
ATOM   2450 C  CG    . ASN A 1 314 ? 13.83929  -3.56338  -39.96722 1.000 33.37577 ? 314 ASN A CG    1 
ATOM   2451 O  OD1   . ASN A 1 314 ? 13.90827  -4.65139  -39.39522 1.000 38.53502 ? 314 ASN A OD1   1 
ATOM   2452 N  ND2   . ASN A 1 314 ? 14.76829  -2.62539  -39.83420 1.000 34.01297 ? 314 ASN A ND2   1 
ATOM   2453 N  N     . PRO A 1 315 ? 15.10934  -2.51137  -43.36219 1.000 39.60788 ? 315 PRO A N     1 
ATOM   2454 C  CA    . PRO A 1 315 ? 15.91535  -3.15337  -44.41118 1.000 37.87704 ? 315 PRO A CA    1 
ATOM   2455 C  C     . PRO A 1 315 ? 16.49835  -4.49638  -44.00718 1.000 31.98024 ? 315 PRO A C     1 
ATOM   2456 O  O     . PRO A 1 315 ? 16.78036  -5.31537  -44.88918 1.000 28.60245 ? 315 PRO A O     1 
ATOM   2457 C  CB    . PRO A 1 315 ? 17.02236  -2.12537  -44.68016 1.000 35.21057 ? 315 PRO A CB    1 
ATOM   2458 C  CG    . PRO A 1 315 ? 17.15734  -1.38738  -43.39216 1.000 32.19009 ? 315 PRO A CG    1 
ATOM   2459 C  CD    . PRO A 1 315 ? 15.76833  -1.31438  -42.81118 1.000 35.59060 ? 315 PRO A CD    1 
ATOM   2460 N  N     . VAL A 1 316 ? 16.69033  -4.75138  -42.70918 1.000 37.09566 ? 316 VAL A N     1 
ATOM   2461 C  CA    . VAL A 1 316 ? 17.27332  -6.01538  -42.26517 1.000 35.92589 ? 316 VAL A CA    1 
ATOM   2462 C  C     . VAL A 1 316 ? 16.23731  -7.11238  -42.07819 1.000 36.67320 ? 316 VAL A C     1 
ATOM   2463 O  O     . VAL A 1 316 ? 16.61331  -8.28638  -41.93219 1.000 30.39313 ? 316 VAL A O     1 
ATOM   2464 C  CB    . VAL A 1 316 ? 18.05530  -5.83239  -40.94916 1.000 34.04865 ? 316 VAL A CB    1 
ATOM   2465 C  CG1   . VAL A 1 316 ? 19.11330  -4.75139  -41.10714 1.000 26.80510 ? 316 VAL A CG1   1 
ATOM   2466 C  CG2   . VAL A 1 316 ? 17.10528  -5.50039  -39.80817 1.000 34.46269 ? 316 VAL A CG2   1 
ATOM   2467 N  N     . CYS A 1 317 ? 14.95031  -6.77738  -42.07721 1.000 34.83412 ? 317 CYS A N     1 
ATOM   2468 C  CA    . CYS A 1 317 ? 13.88531  -7.74838  -41.86723 1.000 34.08484 ? 317 CYS A CA    1 
ATOM   2469 C  C     . CYS A 1 317 ? 13.25633  -8.12337  -43.20124 1.000 31.38472 ? 317 CYS A C     1 
ATOM   2470 O  O     . CYS A 1 317 ? 12.85734  -7.24637  -43.97525 1.000 33.36236 ? 317 CYS A O     1 
ATOM   2471 C  CB    . CYS A 1 317 ? 12.82029  -7.19738  -40.92025 1.000 37.38842 ? 317 CYS A CB    1 
ATOM   2472 S  SG    . CYS A 1 317 ? 11.40329  -8.28938  -40.67827 1.000 44.24249 ? 317 CYS A SG    1 
ATOM   2473 N  N     . LYS A 1 318 ? 13.18533  -9.42437  -43.46625 1.000 31.40139 ? 318 LYS A N     1 
ATOM   2474 C  CA    . LYS A 1 318 ? 12.54335  -9.93637  -44.69526 1.000 30.38537 ? 318 LYS A CA    1 
ATOM   2475 C  C     . LYS A 1 318 ? 11.03034  -9.78736  -44.57928 1.000 35.61512 ? 318 LYS A C     1 
ATOM   2476 O  O     . LYS A 1 318 ? 10.47833  -10.07337 -43.51629 1.000 39.23384 ? 318 LYS A O     1 
ATOM   2477 C  CB    . LYS A 1 318 ? 12.90635  -11.40437 -44.89526 1.000 34.04012 ? 318 LYS A CB    1 
ATOM   2478 C  CG    . LYS A 1 318 ? 12.36936  -12.06436 -46.15527 1.000 38.16292 ? 318 LYS A CG    1 
ATOM   2479 C  CD    . LYS A 1 318 ? 13.32537  -13.09336 -46.70426 1.000 36.46852 ? 318 LYS A CD    1 
ATOM   2480 C  CE    . LYS A 1 318 ? 12.65638  -14.07236 -47.64027 1.000 40.27673 ? 318 LYS A CE    1 
ATOM   2481 N  NZ    . LYS A 1 318 ? 13.08241  -13.86435 -49.04327 1.000 36.60889 ? 318 LYS A NZ    1 
ATOM   2482 N  N     . GLN A 1 319 ? 10.39936  -9.37636  -45.66129 1.000 32.99409 ? 319 GLN A N     1 
ATOM   2483 C  CA    . GLN A 1 319 ? 8.95236   -9.19636  -45.66731 1.000 42.32629 ? 319 GLN A CA    1 
ATOM   2484 C  C     . GLN A 1 319 ? 8.25736   -10.55135 -45.74233 1.000 38.64128 ? 319 GLN A C     1 
ATOM   2485 O  O     . GLN A 1 319 ? 8.44937   -11.30535 -46.70233 1.000 42.12832 ? 319 GLN A O     1 
ATOM   2486 C  CB    . GLN A 1 319 ? 8.53638   -8.30835  -46.83632 1.000 37.46283 ? 319 GLN A CB    1 
ATOM   2487 C  CG    . GLN A 1 319 ? 9.17738   -6.93235  -46.81030 1.000 38.33879 ? 319 GLN A CG    1 
ATOM   2488 C  CD    . GLN A 1 319 ? 8.96736   -6.22136  -45.48630 1.000 40.77601 ? 319 GLN A CD    1 
ATOM   2489 O  OE1   . GLN A 1 319 ? 7.83736   -6.06936  -45.02132 1.000 39.00678 ? 319 GLN A OE1   1 
ATOM   2490 N  NE2   . GLN A 1 319 ? 10.06036  -5.78836  -44.86728 1.000 42.42491 ? 319 GLN A NE2   1 
ATOM   2491 N  N     . ILE A 1 320 ? 7.45235   -10.85836 -44.72834 1.000 44.16847 ? 320 ILE A N     1 
ATOM   2492 C  CA    . ILE A 1 320 ? 6.72834   -12.12036 -44.63436 1.000 41.65771 ? 320 ILE A CA    1 
ATOM   2493 C  C     . ILE A 1 320 ? 5.24734   -11.80935 -44.48138 1.000 41.97338 ? 320 ILE A C     1 
ATOM   2494 O  O     . ILE A 1 320 ? 4.86433   -10.97936 -43.64738 1.000 48.15271 ? 320 ILE A O     1 
ATOM   2495 C  CB    . ILE A 1 320 ? 7.23432   -12.97836 -43.46035 1.000 43.45563 ? 320 ILE A CB    1 
ATOM   2496 C  CG1   . ILE A 1 320 ? 8.72032   -13.29936 -43.64033 1.000 45.67609 ? 320 ILE A CG1   1 
ATOM   2497 C  CG2   . ILE A 1 320 ? 6.41932   -14.25836 -43.33837 1.000 45.31272 ? 320 ILE A CG2   1 
ATOM   2498 C  CD1   . ILE A 1 320 ? 9.31831   -14.10737 -42.51032 1.000 45.62289 ? 320 ILE A CD1   1 
ATOM   2499 N  N     . ASP A 1 321 ? 4.41300   -12.48200 -45.28400 1.000 42.70366 ? 321 ASP A N     1 
ATOM   2500 C  CA    . ASP A 1 321 ? 2.96500   -12.27500 -45.25500 1.000 46.92930 ? 321 ASP A CA    1 
ATOM   2501 C  C     . ASP A 1 321 ? 2.37000   -12.97200 -44.03100 1.000 47.03413 ? 321 ASP A C     1 
ATOM   2502 O  O     . ASP A 1 321 ? 1.69300   -13.99900 -44.11600 1.000 43.67407 ? 321 ASP A O     1 
ATOM   2503 C  CB    . ASP A 1 321 ? 2.32700   -12.77400 -46.54300 1.000 55.50333 ? 321 ASP A CB    1 
ATOM   2504 C  CG    . ASP A 1 321 ? 2.44500   -11.77700 -47.67500 1.000 56.09770 ? 321 ASP A CG    1 
ATOM   2505 O  OD1   . ASP A 1 321 ? 3.58200   -11.49900 -48.11100 1.000 63.65090 ? 321 ASP A OD1   1 
ATOM   2506 O  OD2   . ASP A 1 321 ? 1.39700   -11.27000 -48.12900 1.000 60.05404 ? 321 ASP A OD2   1 
ATOM   2507 N  N     . TRP A 1 322 ? 2.63400   -12.38000 -42.86800 1.000 50.42324 ? 322 TRP A N     1 
ATOM   2508 C  CA    . TRP A 1 322 ? 2.09929   -12.90636 -41.62443 1.000 43.64740 ? 322 TRP A CA    1 
ATOM   2509 C  C     . TRP A 1 322 ? 0.57929   -12.80635 -41.61845 1.000 38.87656 ? 322 TRP A C     1 
ATOM   2510 O  O     . TRP A 1 322 ? 0.00030   -11.83835 -42.12146 1.000 47.86112 ? 322 TRP A O     1 
ATOM   2511 C  CB    . TRP A 1 322 ? 2.68128   -12.15736 -40.42642 1.000 33.65587 ? 322 TRP A CB    1 
ATOM   2512 C  CG    . TRP A 1 322 ? 4.17227   -12.26637 -40.29640 1.000 32.99281 ? 322 TRP A CG    1 
ATOM   2513 C  CD1   . TRP A 1 322 ? 5.08728   -11.27537 -40.50338 1.000 32.10998 ? 322 TRP A CD1   1 
ATOM   2514 C  CD2   . TRP A 1 322 ? 4.92127   -13.43137 -39.92839 1.000 33.37081 ? 322 TRP A CD2   1 
ATOM   2515 N  NE1   . TRP A 1 322 ? 6.35728   -11.75037 -40.28536 1.000 33.98322 ? 322 TRP A NE1   1 
ATOM   2516 C  CE2   . TRP A 1 322 ? 6.28327   -13.07137 -39.93137 1.000 34.67279 ? 322 TRP A CE2   1 
ATOM   2517 C  CE3   . TRP A 1 322 ? 4.57126   -14.74337 -39.59640 1.000 31.37892 ? 322 TRP A CE3   1 
ATOM   2518 C  CZ2   . TRP A 1 322 ? 7.29526   -13.97537 -39.61435 1.000 38.55401 ? 322 TRP A CZ2   1 
ATOM   2519 C  CZ3   . TRP A 1 322 ? 5.57825   -15.64037 -39.28339 1.000 32.29804 ? 322 TRP A CZ3   1 
ATOM   2520 C  CH2   . TRP A 1 322 ? 6.92325   -15.25237 -39.29536 1.000 33.61645 ? 322 TRP A CH2   1 
ATOM   2521 N  N     . ASP A 1 323 ? -0.06672  -13.81536 -41.04547 1.000 37.31775 ? 323 ASP A N     1 
ATOM   2522 C  CA    . ASP A 1 323 ? -1.51872  -13.88035 -41.04049 1.000 41.70463 ? 323 ASP A CA    1 
ATOM   2523 C  C     . ASP A 1 323 ? -2.09673  -13.07636 -39.88349 1.000 45.65911 ? 323 ASP A C     1 
ATOM   2524 O  O     . ASP A 1 323 ? -1.46375  -12.90336 -38.83848 1.000 43.25348 ? 323 ASP A O     1 
ATOM   2525 C  CB    . ASP A 1 323 ? -1.98872  -15.33135 -40.94450 1.000 39.99798 ? 323 ASP A CB    1 
ATOM   2526 C  CG    . ASP A 1 323 ? -1.37871  -16.21335 -42.01249 1.000 44.66323 ? 323 ASP A CG    1 
ATOM   2527 O  OD1   . ASP A 1 323 ? -1.01669  -15.68635 -43.08549 1.000 45.83456 ? 323 ASP A OD1   1 
ATOM   2528 O  OD2   . ASP A 1 323 ? -1.26271  -17.43435 -41.77850 1.000 39.16286 ? 323 ASP A OD2   1 
ATOM   2529 N  N     . ASP A 1 324 ? -3.31873  -12.58735 -40.08251 1.000 48.45503 ? 324 ASP A N     1 
ATOM   2530 C  CA    . ASP A 1 324 ? -4.06374  -11.86736 -39.05452 1.000 46.69640 ? 324 ASP A CA    1 
ATOM   2531 C  C     . ASP A 1 324 ? -5.07875  -12.84036 -38.46454 1.000 43.12620 ? 324 ASP A C     1 
ATOM   2532 O  O     . ASP A 1 324 ? -6.17675  -13.01035 -38.99956 1.000 43.31497 ? 324 ASP A O     1 
ATOM   2533 C  CB    . ASP A 1 324 ? -4.73673  -10.62935 -39.64053 1.000 39.25258 ? 324 ASP A CB    1 
ATOM   2534 C  CG    . ASP A 1 324 ? -5.24375  -9.67236  -38.57353 1.000 45.14358 ? 324 ASP A CG    1 
ATOM   2535 O  OD1   . ASP A 1 324 ? -5.70076  -10.13936 -37.50954 1.000 40.42555 ? 324 ASP A OD1   1 
ATOM   2536 O  OD2   . ASP A 1 324 ? -5.18274  -8.44535  -38.80153 1.000 51.63075 ? 324 ASP A OD2   1 
ATOM   2537 N  N     . ASN A 1 325 ? -4.70677  -13.48036 -37.35654 1.000 39.22882 ? 325 ASN A N     1 
ATOM   2538 C  CA    . ASN A 1 325 ? -5.54578  -14.47936 -36.69655 1.000 37.96482 ? 325 ASN A CA    1 
ATOM   2539 C  C     . ASN A 1 325 ? -5.65881  -14.11337 -35.22355 1.000 42.76170 ? 325 ASN A C     1 
ATOM   2540 O  O     . ASN A 1 325 ? -4.85982  -14.57037 -34.39354 1.000 40.09228 ? 325 ASN A O     1 
ATOM   2541 C  CB    . ASN A 1 325 ? -4.97478  -15.88536 -36.88155 1.000 40.23185 ? 325 ASN A CB    1 
ATOM   2542 C  CG    . ASN A 1 325 ? -5.99679  -16.97236 -36.60957 1.000 39.87048 ? 325 ASN A CG    1 
ATOM   2543 O  OD1   . ASN A 1 325 ? -6.77280  -16.89136 -35.65758 1.000 42.44197 ? 325 ASN A OD1   1 
ATOM   2544 N  ND2   . ASN A 1 325 ? -6.00478  -17.99736 -37.45457 1.000 37.35579 ? 325 ASN A ND2   1 
ATOM   2545 N  N     . PRO A 1 326 ? -6.63981  -13.28237 -34.86056 1.000 48.01780 ? 326 PRO A N     1 
ATOM   2546 C  CA    . PRO A 1 326 ? -6.78283  -12.89437 -33.44757 1.000 44.56587 ? 326 PRO A CA    1 
ATOM   2547 C  C     . PRO A 1 326 ? -7.13285  -14.05537 -32.53257 1.000 39.28089 ? 326 PRO A C     1 
ATOM   2548 O  O     . PRO A 1 326 ? -6.80387  -14.01238 -31.33957 1.000 33.57554 ? 326 PRO A O     1 
ATOM   2549 C  CB    . PRO A 1 326 ? -7.90483  -11.84537 -33.48358 1.000 42.92233 ? 326 PRO A CB    1 
ATOM   2550 C  CG    . PRO A 1 326 ? -7.95081  -11.37236 -34.90358 1.000 30.49170 ? 326 PRO A CG    1 
ATOM   2551 C  CD    . PRO A 1 326 ? -7.58380  -12.56336 -35.73058 1.000 44.34504 ? 326 PRO A CD    1 
ATOM   2552 N  N     . GLU A 1 327 ? -7.79684  -15.09037 -33.05159 1.000 43.90241 ? 327 GLU A N     1 
ATOM   2553 C  CA    . GLU A 1 327 ? -8.14386  -16.23837 -32.21860 1.000 43.86366 ? 327 GLU A CA    1 
ATOM   2554 C  C     . GLU A 1 327 ? -6.89686  -16.97238 -31.74358 1.000 39.84893 ? 327 GLU A C     1 
ATOM   2555 O  O     . GLU A 1 327 ? -6.79388  -17.33538 -30.56558 1.000 31.78928 ? 327 GLU A O     1 
ATOM   2556 C  CB    . GLU A 1 327 ? -9.06685  -17.18737 -32.98462 1.000 44.40842 ? 327 GLU A CB    1 
ATOM   2557 C  CG    . GLU A 1 327 ? -10.44084 -16.61436 -33.31263 1.000 49.03786 ? 327 GLU A CG    1 
ATOM   2558 C  CD    . GLU A 1 327 ? -10.44282 -15.74136 -34.55563 1.000 48.14502 ? 327 GLU A CD    1 
ATOM   2559 O  OE1   . GLU A 1 327 ? -9.35181  -15.37936 -35.04261 1.000 45.75589 ? 327 GLU A OE1   1 
ATOM   2560 O  OE2   . GLU A 1 327 ? -11.54281 -15.42036 -35.05165 1.000 50.31170 ? 327 GLU A OE2   1 
ATOM   2561 N  N     . PHE A 1 328 ? -5.93885  -17.20238 -32.64557 1.000 40.14341 ? 328 PHE A N     1 
ATOM   2562 C  CA    . PHE A 1 328 ? -4.68686  -17.83538 -32.24455 1.000 38.20048 ? 328 PHE A CA    1 
ATOM   2563 C  C     . PHE A 1 328 ? -3.84887  -16.91438 -31.36753 1.000 33.50948 ? 328 PHE A C     1 
ATOM   2564 O  O     . PHE A 1 328 ? -3.13888  -17.38939 -30.47353 1.000 37.08627 ? 328 PHE A O     1 
ATOM   2565 C  CB    . PHE A 1 328 ? -3.88984  -18.26138 -33.47754 1.000 29.40648 ? 328 PHE A CB    1 
ATOM   2566 C  CG    . PHE A 1 328 ? -4.42183  -19.49537 -34.14855 1.000 26.67466 ? 328 PHE A CG    1 
ATOM   2567 C  CD1   . PHE A 1 328 ? -5.17884  -20.41337 -33.44057 1.000 36.93749 ? 328 PHE A CD1   1 
ATOM   2568 C  CD2   . PHE A 1 328 ? -4.16081  -19.73937 -35.48555 1.000 24.28536 ? 328 PHE A CD2   1 
ATOM   2569 C  CE1   . PHE A 1 328 ? -5.66784  -21.55137 -34.05558 1.000 30.19133 ? 328 PHE A CE1   1 
ATOM   2570 C  CE2   . PHE A 1 328 ? -4.64680  -20.87437 -36.10656 1.000 26.72124 ? 328 PHE A CE2   1 
ATOM   2571 C  CZ    . PHE A 1 328 ? -5.40182  -21.78137 -35.39058 1.000 34.79873 ? 328 PHE A CZ    1 
ATOM   2572 N  N     . LEU A 1 329 ? -3.91686  -15.60238 -31.60453 1.000 33.40291 ? 329 LEU A N     1 
ATOM   2573 C  CA    . LEU A 1 329 ? -3.16187  -14.66439 -30.77952 1.000 37.60389 ? 329 LEU A CA    1 
ATOM   2574 C  C     . LEU A 1 329 ? -3.73190  -14.58739 -29.36952 1.000 37.35657 ? 329 LEU A C     1 
ATOM   2575 O  O     . LEU A 1 329 ? -2.97791  -14.52940 -28.39151 1.000 27.16523 ? 329 LEU A O     1 
ATOM   2576 C  CB    . LEU A 1 329 ? -3.15186  -13.28238 -31.43251 1.000 31.01930 ? 329 LEU A CB    1 
ATOM   2577 C  CG    . LEU A 1 329 ? -2.46487  -12.16539 -30.64450 1.000 28.90032 ? 329 LEU A CG    1 
ATOM   2578 C  CD1   . LEU A 1 329 ? -1.00688  -12.50839 -30.38348 1.000 38.66555 ? 329 LEU A CD1   1 
ATOM   2579 C  CD2   . LEU A 1 329 ? -2.58286  -10.83739 -31.37649 1.000 31.92790 ? 329 LEU A CD2   1 
ATOM   2580 N  N     . ALA A 1 330 ? -5.06090  -14.58839 -29.24555 1.000 41.30607 ? 330 ALA A N     1 
ATOM   2581 C  CA    . ALA A 1 330 ? -5.67992  -14.51639 -27.92655 1.000 36.86041 ? 330 ALA A CA    1 
ATOM   2582 C  C     . ALA A 1 330 ? -5.43693  -15.79240 -27.13056 1.000 33.37359 ? 330 ALA A C     1 
ATOM   2583 O  O     . ALA A 1 330 ? -5.16095  -15.73440 -25.92655 1.000 31.65752 ? 330 ALA A O     1 
ATOM   2584 C  CB    . ALA A 1 330 ? -7.17792  -14.24439 -28.06458 1.000 39.37518 ? 330 ALA A CB    1 
ATOM   2585 N  N     . ALA A 1 331 ? -5.53192  -16.95239 -27.78356 1.000 33.12426 ? 331 ALA A N     1 
ATOM   2586 C  CA    . ALA A 1 331 ? -5.28394  -18.21040 -27.08656 1.000 31.82948 ? 331 ALA A CA    1 
ATOM   2587 C  C     . ALA A 1 331 ? -3.83094  -18.33640 -26.65154 1.000 29.41612 ? 331 ALA A C     1 
ATOM   2588 O  O     . ALA A 1 331 ? -3.54396  -18.96940 -25.62954 1.000 31.32746 ? 331 ALA A O     1 
ATOM   2589 C  CB    . ALA A 1 331 ? -5.67793  -19.39039 -27.97557 1.000 25.85799 ? 331 ALA A CB    1 
ATOM   2590 N  N     . TRP A 1 332 ? -2.90493  -17.73740 -27.40252 1.000 26.01786 ? 332 TRP A N     1 
ATOM   2591 C  CA    . TRP A 1 332 ? -1.49194  -17.82040 -27.05250 1.000 25.77796 ? 332 TRP A CA    1 
ATOM   2592 C  C     . TRP A 1 332 ? -1.13595  -16.87341 -25.91149 1.000 29.64979 ? 332 TRP A C     1 
ATOM   2593 O  O     . TRP A 1 332 ? -0.38297  -17.24841 -25.00648 1.000 25.65568 ? 332 TRP A O     1 
ATOM   2594 C  CB    . TRP A 1 332 ? -0.62992  -17.52540 -28.28149 1.000 23.18960 ? 332 TRP A CB    1 
ATOM   2595 C  CG    . TRP A 1 332 ? 0.83308   -17.40940 -27.98247 1.000 25.99120 ? 332 TRP A CG    1 
ATOM   2596 C  CD1   . TRP A 1 332 ? 1.71707   -18.43341 -27.80046 1.000 28.11705 ? 332 TRP A CD1   1 
ATOM   2597 C  CD2   . TRP A 1 332 ? 1.58508   -16.19941 -27.83645 1.000 27.43001 ? 332 TRP A CD2   1 
ATOM   2598 N  NE1   . TRP A 1 332 ? 2.97207   -17.93441 -27.54743 1.000 26.73316 ? 332 TRP A NE1   1 
ATOM   2599 C  CE2   . TRP A 1 332 ? 2.91807   -16.56541 -27.56543 1.000 26.06587 ? 332 TRP A CE2   1 
ATOM   2600 C  CE3   . TRP A 1 332 ? 1.26008   -14.84141 -27.90945 1.000 31.51650 ? 332 TRP A CE3   1 
ATOM   2601 C  CZ2   . TRP A 1 332 ? 3.92407   -15.62241 -27.36541 1.000 24.77649 ? 332 TRP A CZ2   1 
ATOM   2602 C  CZ3   . TRP A 1 332 ? 2.26108   -13.90841 -27.71143 1.000 24.74542 ? 332 TRP A CZ3   1 
ATOM   2603 C  CH2   . TRP A 1 332 ? 3.57707   -14.30241 -27.44341 1.000 19.65836 ? 332 TRP A CH2   1 
ATOM   2604 N  N     . ARG A 1 333 ? -1.66398  -15.64810 -25.92931 1.000 26.57696 ? 333 ARG A N     1 
ATOM   2605 C  CA    . ARG A 1 333 ? -1.33554  -14.69115 -24.87975 1.000 29.63759 ? 333 ARG A CA    1 
ATOM   2606 C  C     . ARG A 1 333 ? -2.07076  -14.96893 -23.57591 1.000 27.70901 ? 333 ARG A C     1 
ATOM   2607 O  O     . ARG A 1 333 ? -1.66013  -14.45548 -22.52963 1.000 32.86732 ? 333 ARG A O     1 
ATOM   2608 C  CB    . ARG A 1 333 ? -1.64048  -13.26356 -25.33917 1.000 28.56984 ? 333 ARG A CB    1 
ATOM   2609 C  CG    . ARG A 1 333 ? -3.11786  -12.96330 -25.51446 1.000 29.43849 ? 333 ARG A CG    1 
ATOM   2610 C  CD    . ARG A 1 333 ? -3.36976  -11.46482 -25.52789 1.000 30.43403 ? 333 ARG A CD    1 
ATOM   2611 N  NE    . ARG A 1 333 ? -4.74008  -11.14466 -25.90665 1.000 27.13906 ? 333 ARG A NE    1 
ATOM   2612 C  CZ    . ARG A 1 333 ? -5.11589  -10.80116 -27.13091 1.000 36.12518 ? 333 ARG A CZ    1 
ATOM   2613 N  NH1   . ARG A 1 333 ? -4.24298  -10.70511 -28.12012 1.000 37.95283 ? 333 ARG A NH1   1 
ATOM   2614 N  NH2   . ARG A 1 333 ? -6.39935  -10.54575 -27.36822 1.000 44.82522 ? 333 ARG A NH2   1 
ATOM   2615 N  N     . GLU A 1 334 ? -3.13899  -15.76341 -23.61052 1.000 28.30857 ? 334 GLU A N     1 
ATOM   2616 C  CA    . GLU A 1 334 ? -3.91701  -16.07842 -22.42153 1.000 28.30687 ? 334 GLU A CA    1 
ATOM   2617 C  C     . GLU A 1 334 ? -3.64102  -17.48042 -21.89253 1.000 33.80125 ? 334 GLU A C     1 
ATOM   2618 O  O     . GLU A 1 334 ? -4.33703  -17.93342 -20.97755 1.000 30.55420 ? 334 GLU A O     1 
ATOM   2619 C  CB    . GLU A 1 334 ? -5.41000  -15.91041 -22.71056 1.000 23.90755 ? 334 GLU A CB    1 
ATOM   2620 C  CG    . GLU A 1 334 ? -5.80699  -14.48841 -23.06656 1.000 24.05559 ? 334 GLU A CG    1 
ATOM   2621 C  CD    . GLU A 1 334 ? -7.25099  -14.38341 -23.51058 1.000 28.33392 ? 334 GLU A CD    1 
ATOM   2622 O  OE1   . GLU A 1 334 ? -7.92699  -15.43140 -23.58659 1.000 26.01866 ? 334 GLU A OE1   1 
ATOM   2623 O  OE2   . GLU A 1 334 ? -7.70898  -13.25440 -23.78358 1.000 32.42303 ? 334 GLU A OE2   1 
ATOM   2624 N  N     . ALA A 1 335 ? -2.64801  -18.17442 -22.45352 1.000 31.02437 ? 335 ALA A N     1 
ATOM   2625 C  CA    . ALA A 1 335 ? -2.22702  -19.49942 -21.99652 1.000 23.50953 ? 335 ALA A CA    1 
ATOM   2626 C  C     . ALA A 1 335 ? -3.39502  -20.48842 -22.00254 1.000 32.67793 ? 335 ALA A C     1 
ATOM   2627 O  O     . ALA A 1 335 ? -3.79304  -21.03342 -20.97155 1.000 31.69787 ? 335 ALA A O     1 
ATOM   2628 C  CB    . ALA A 1 335 ? -1.57604  -19.41943 -20.61151 1.000 23.07512 ? 335 ALA A CB    1 
ATOM   2629 N  N     . ARG A 1 336 ? -3.94145  -20.71078 -23.19831 1.000 31.06920 ? 336 ARG A N     1 
ATOM   2630 C  CA    . ARG A 1 336 ? -5.02887  -21.66682 -23.37447 1.000 28.52560 ? 336 ARG A CA    1 
ATOM   2631 C  C     . ARG A 1 336 ? -4.92826  -22.32610 -24.74504 1.000 32.49335 ? 336 ARG A C     1 
ATOM   2632 O  O     . ARG A 1 336 ? -5.93002  -22.48998 -25.44985 1.000 25.45049 ? 336 ARG A O     1 
ATOM   2633 C  CB    . ARG A 1 336 ? -6.39540  -21.00268 -23.18758 1.000 31.50772 ? 336 ARG A CB    1 
ATOM   2634 C  CG    . ARG A 1 336 ? -6.58552  -19.71705 -23.97580 1.000 30.64204 ? 336 ARG A CG    1 
ATOM   2635 C  CD    . ARG A 1 336 ? -7.98130  -19.15421 -23.76543 1.000 25.12795 ? 336 ARG A CD    1 
ATOM   2636 N  NE    . ARG A 1 336 ? -8.17468  -17.88486 -24.45551 1.000 25.35137 ? 336 ARG A NE    1 
ATOM   2637 C  CZ    . ARG A 1 336 ? -8.58544  -17.76994 -25.71084 1.000 31.39403 ? 336 ARG A CZ    1 
ATOM   2638 N  NH1   . ARG A 1 336 ? -8.84188  -18.83383 -26.45450 1.000 27.68634 ? 336 ARG A NH1   1 
ATOM   2639 N  NH2   . ARG A 1 336 ? -8.74367  -16.55719 -26.23307 1.000 30.71625 ? 336 ARG A NH2   1 
ATOM   2640 N  N     . THR A 1 337 ? -3.71498  -22.71341 -25.13355 1.000 31.52488 ? 337 THR A N     1 
ATOM   2641 C  CA    . THR A 1 337 ? -3.47396  -23.34440 -26.42555 1.000 26.28818 ? 337 THR A CA    1 
ATOM   2642 C  C     . THR A 1 337 ? -3.64196  -24.85640 -26.39156 1.000 18.02265 ? 337 THR A C     1 
ATOM   2643 O  O     . THR A 1 337 ? -3.58895  -25.49240 -27.44956 1.000 20.46086 ? 337 THR A O     1 
ATOM   2644 C  CB    . THR A 1 337 ? -2.06395  -23.00840 -26.92553 1.000 27.98063 ? 337 THR A CB    1 
ATOM   2645 O  OG1   . THR A 1 337 ? -1.09396  -23.54241 -26.01452 1.000 25.78216 ? 337 THR A OG1   1 
ATOM   2646 C  CG2   . THR A 1 337 ? -1.88094  -21.50440 -27.02452 1.000 33.43961 ? 337 THR A CG2   1 
ATOM   2647 N  N     . GLY A 1 338 ? -3.84298  -25.44441 -25.21457 1.000 26.73733 ? 338 GLY A N     1 
ATOM   2648 C  CA    . GLY A 1 338 ? -3.95698  -26.87941 -25.08157 1.000 24.11223 ? 338 GLY A CA    1 
ATOM   2649 C  C     . GLY A 1 338 ? -2.64799  -27.60941 -24.87955 1.000 22.21765 ? 338 GLY A C     1 
ATOM   2650 O  O     . GLY A 1 338 ? -2.66800  -28.79641 -24.53156 1.000 23.33897 ? 338 GLY A O     1 
ATOM   2651 N  N     . PHE A 1 339 ? -1.51098  -26.94241 -25.08654 1.000 17.97603 ? 339 PHE A N     1 
ATOM   2652 C  CA    . PHE A 1 339 ? -0.20899  -27.55841 -24.88152 1.000 21.96253 ? 339 PHE A CA    1 
ATOM   2653 C  C     . PHE A 1 339 ? 0.33199   -27.13742 -23.52551 1.000 21.61301 ? 339 PHE A C     1 
ATOM   2654 O  O     . PHE A 1 339 ? 0.63799   -25.94942 -23.33450 1.000 22.72002 ? 339 PHE A O     1 
ATOM   2655 C  CB    . PHE A 1 339 ? 0.75803   -27.15741 -25.99250 1.000 22.84868 ? 339 PHE A CB    1 
ATOM   2656 C  CG    . PHE A 1 339 ? 0.35705   -27.64941 -27.35351 1.000 17.42890 ? 339 PHE A CG    1 
ATOM   2657 C  CD1   . PHE A 1 339 ? 0.72905   -28.91140 -27.78551 1.000 20.04434 ? 339 PHE A CD1   1 
ATOM   2658 C  CD2   . PHE A 1 339 ? -0.38994  -26.85040 -28.20352 1.000 17.25309 ? 339 PHE A CD2   1 
ATOM   2659 C  CE1   . PHE A 1 339 ? 0.36207   -29.36940 -29.03752 1.000 22.81495 ? 339 PHE A CE1   1 
ATOM   2660 C  CE2   . PHE A 1 339 ? -0.75992  -27.30140 -29.45652 1.000 19.69381 ? 339 PHE A CE2   1 
ATOM   2661 C  CZ    . PHE A 1 339 ? -0.38391  -28.56240 -29.87352 1.000 20.44546 ? 339 PHE A CZ    1 
ATOM   2662 N  N     . PRO A 1 340 ? 0.46398   -28.05142 -22.56051 1.000 20.64274 ? 340 PRO A N     1 
ATOM   2663 C  CA    . PRO A 1 340 ? 0.91896   -27.64243 -21.22050 1.000 21.95200 ? 340 PRO A CA    1 
ATOM   2664 C  C     . PRO A 1 340 ? 2.31296   -27.04443 -21.20148 1.000 21.59247 ? 340 PRO A C     1 
ATOM   2665 O  O     . PRO A 1 340 ? 2.60594   -26.21543 -20.33147 1.000 25.30168 ? 340 PRO A O     1 
ATOM   2666 C  CB    . PRO A 1 340 ? 0.85294   -28.94943 -20.41751 1.000 20.11058 ? 340 PRO A CB    1 
ATOM   2667 C  CG    . PRO A 1 340 ? -0.12905  -29.79943 -21.15452 1.000 22.65411 ? 340 PRO A CG    1 
ATOM   2668 C  CD    . PRO A 1 340 ? 0.07097   -29.46842 -22.60252 1.000 25.42682 ? 340 PRO A CD    1 
ATOM   2669 N  N     . TRP A 1 341 ? 3.18697   -27.43743 -22.13047 1.000 16.24887 ? 341 TRP A N     1 
ATOM   2670 C  CA    . TRP A 1 341 ? 4.52497   -26.85543 -22.16644 1.000 20.98475 ? 341 TRP A CA    1 
ATOM   2671 C  C     . TRP A 1 341 ? 4.47898   -25.39143 -22.58744 1.000 18.39422 ? 341 TRP A C     1 
ATOM   2672 O  O     . TRP A 1 341 ? 5.20497   -24.55843 -22.03442 1.000 23.84565 ? 341 TRP A O     1 
ATOM   2673 C  CB    . TRP A 1 341 ? 5.42598   -27.66143 -23.10243 1.000 18.44244 ? 341 TRP A CB    1 
ATOM   2674 C  CG    . TRP A 1 341 ? 6.77999   -27.04843 -23.30641 1.000 21.60696 ? 341 TRP A CG    1 
ATOM   2675 C  CD1   . TRP A 1 341 ? 7.24501   -26.44843 -24.43940 1.000 22.40571 ? 341 TRP A CD1   1 
ATOM   2676 C  CD2   . TRP A 1 341 ? 7.84097   -26.96744 -22.34539 1.000 20.38940 ? 341 TRP A CD2   1 
ATOM   2677 N  NE1   . TRP A 1 341 ? 8.53100   -26.00343 -24.24638 1.000 23.10755 ? 341 TRP A NE1   1 
ATOM   2678 C  CE2   . TRP A 1 341 ? 8.91998   -26.30944 -22.96937 1.000 22.18278 ? 341 TRP A CE2   1 
ATOM   2679 C  CE3   . TRP A 1 341 ? 7.98395   -27.38944 -21.02039 1.000 22.49853 ? 341 TRP A CE3   1 
ATOM   2680 C  CZ2   . TRP A 1 341 ? 10.12498  -26.06344 -22.31335 1.000 17.47765 ? 341 TRP A CZ2   1 
ATOM   2681 C  CZ3   . TRP A 1 341 ? 9.18194   -27.14445 -20.37137 1.000 17.04561 ? 341 TRP A CZ3   1 
ATOM   2682 C  CH2   . TRP A 1 341 ? 10.23595  -26.48645 -21.01835 1.000 15.17756 ? 341 TRP A CH2   1 
ATOM   2683 N  N     . ILE A 1 342 ? 3.62700   -25.05942 -23.55745 1.000 20.45488 ? 342 ILE A N     1 
ATOM   2684 C  CA    . ILE A 1 342 ? 3.53001   -23.67742 -24.01745 1.000 25.40361 ? 342 ILE A CA    1 
ATOM   2685 C  C     . ILE A 1 342 ? 2.75499   -22.82643 -23.01746 1.000 20.44251 ? 342 ILE A C     1 
ATOM   2686 O  O     . ILE A 1 342 ? 3.14399   -21.69143 -22.72145 1.000 19.42633 ? 342 ILE A O     1 
ATOM   2687 C  CB    . ILE A 1 342 ? 2.89103   -23.62842 -25.41746 1.000 29.38924 ? 342 ILE A CB    1 
ATOM   2688 C  CG1   . ILE A 1 342 ? 3.69904   -24.47441 -26.40345 1.000 17.62466 ? 342 ILE A CG1   1 
ATOM   2689 C  CG2   . ILE A 1 342 ? 2.78004   -22.18942 -25.90845 1.000 22.81090 ? 342 ILE A CG2   1 
ATOM   2690 C  CD1   . ILE A 1 342 ? 5.12704   -24.01242 -26.57842 1.000 26.62740 ? 342 ILE A CD1   1 
ATOM   2691 N  N     . ASP A 1 343 ? 1.65698   -23.35943 -22.47747 1.000 19.14908 ? 343 ASP A N     1 
ATOM   2692 C  CA    . ASP A 1 343 ? 0.82397   -22.58343 -21.56448 1.000 22.29380 ? 343 ASP A CA    1 
ATOM   2693 C  C     . ASP A 1 343 ? 1.52395   -22.31843 -20.23647 1.000 23.96731 ? 343 ASP A C     1 
ATOM   2694 O  O     . ASP A 1 343 ? 1.24694   -21.30343 -19.58747 1.000 21.58843 ? 343 ASP A O     1 
ATOM   2695 C  CB    . ASP A 1 343 ? -0.50403  -23.30243 -21.32851 1.000 26.76617 ? 343 ASP A CB    1 
ATOM   2696 C  CG    . ASP A 1 343 ? -1.32502  -23.43842 -22.59552 1.000 25.13665 ? 343 ASP A CG    1 
ATOM   2697 O  OD1   . ASP A 1 343 ? -1.27900  -22.51542 -23.43652 1.000 24.55838 ? 343 ASP A OD1   1 
ATOM   2698 O  OD2   . ASP A 1 343 ? -2.01502  -24.46742 -22.75253 1.000 25.22873 ? 343 ASP A OD2   1 
ATOM   2699 N  N     . ALA A 1 344 ? 2.42194   -23.21044 -19.81246 1.000 23.86648 ? 344 ALA A N     1 
ATOM   2700 C  CA    . ALA A 1 344 ? 3.13892   -22.98744 -18.56145 1.000 19.67032 ? 344 ALA A CA    1 
ATOM   2701 C  C     . ALA A 1 344 ? 4.17293   -21.87744 -18.69843 1.000 21.26097 ? 344 ALA A C     1 
ATOM   2702 O  O     . ALA A 1 344 ? 4.44091   -21.15945 -17.72842 1.000 23.78233 ? 344 ALA A O     1 
ATOM   2703 C  CB    . ALA A 1 344 ? 3.80691   -24.27944 -18.09344 1.000 22.83411 ? 344 ALA A CB    1 
ATOM   2704 N  N     . ILE A 1 345 ? 4.76395   -21.72344 -19.88442 1.000 25.00844 ? 345 ILE A N     1 
ATOM   2705 C  CA    . ILE A 1 345 ? 5.72695   -20.64844 -20.09940 1.000 19.91705 ? 345 ILE A CA    1 
ATOM   2706 C  C     . ILE A 1 345 ? 5.01895   -19.30044 -20.13241 1.000 25.71615 ? 345 ILE A C     1 
ATOM   2707 O  O     . ILE A 1 345 ? 5.49695   -18.31844 -19.55140 1.000 26.19688 ? 345 ILE A O     1 
ATOM   2708 C  CB    . ILE A 1 345 ? 6.52897   -20.90344 -21.38839 1.000 20.26585 ? 345 ILE A CB    1 
ATOM   2709 C  CG1   . ILE A 1 345 ? 7.28297   -22.23044 -21.29038 1.000 20.39973 ? 345 ILE A CG1   1 
ATOM   2710 C  CG2   . ILE A 1 345 ? 7.49498   -19.75944 -21.65237 1.000 20.59404 ? 345 ILE A CG2   1 
ATOM   2711 C  CD1   . ILE A 1 345 ? 8.00899   -22.61444 -22.55737 1.000 19.02079 ? 345 ILE A CD1   1 
ATOM   2712 N  N     . MET A 1 346 ? 3.86696   -19.23144 -20.80743 1.000 28.57937 ? 346 MET A N     1 
ATOM   2713 C  CA    . MET A 1 346 ? 3.09797   -17.99243 -20.82943 1.000 21.70463 ? 346 MET A CA    1 
ATOM   2714 C  C     . MET A 1 346 ? 2.58295   -17.63244 -19.44244 1.000 28.23363 ? 346 MET A C     1 
ATOM   2715 O  O     . MET A 1 346 ? 2.43194   -16.44744 -19.12444 1.000 28.62984 ? 346 MET A O     1 
ATOM   2716 C  CB    . MET A 1 346 ? 1.93798   -18.11043 -21.81845 1.000 28.91888 ? 346 MET A CB    1 
ATOM   2717 C  CG    . MET A 1 346 ? 2.36600   -18.46642 -23.23445 1.000 30.96463 ? 346 MET A CG    1 
ATOM   2718 S  SD    . MET A 1 346 ? 3.54402   -17.29142 -23.93042 1.000 16.37071 ? 346 MET A SD    1 
ATOM   2719 C  CE    . MET A 1 346 ? 2.58502   -15.77942 -23.88843 1.000 28.07537 ? 346 MET A CE    1 
ATOM   2720 N  N     . THR A 1 347 ? 2.30493   -18.63744 -18.60645 1.000 21.84128 ? 347 THR A N     1 
ATOM   2721 C  CA    . THR A 1 347 ? 1.94091   -18.36544 -17.22045 1.000 20.46536 ? 347 THR A CA    1 
ATOM   2722 C  C     . THR A 1 347 ? 3.13690   -17.83445 -16.43943 1.000 23.94182 ? 347 THR A C     1 
ATOM   2723 O  O     . THR A 1 347 ? 2.99989   -16.89945 -15.64143 1.000 19.27787 ? 347 THR A O     1 
ATOM   2724 C  CB    . THR A 1 347 ? 1.38590   -19.62945 -16.56246 1.000 20.81703 ? 347 THR A CB    1 
ATOM   2725 O  OG1   . THR A 1 347 ? 0.20991   -20.05644 -17.26148 1.000 21.43179 ? 347 THR A OG1   1 
ATOM   2726 C  CG2   . THR A 1 347 ? 1.03588   -19.36945 -15.10447 1.000 24.84544 ? 347 THR A CG2   1 
ATOM   2727 N  N     . GLN A 1 348 ? 4.31890   -18.41545 -16.66142 1.000 26.20394 ? 348 GLN A N     1 
ATOM   2728 C  CA    . GLN A 1 348 ? 5.52989   -17.89746 -16.03240 1.000 22.45015 ? 348 GLN A CA    1 
ATOM   2729 C  C     . GLN A 1 348 ? 5.83690   -16.48145 -16.50239 1.000 24.71276 ? 348 GLN A C     1 
ATOM   2730 O  O     . GLN A 1 348 ? 6.48089   -15.71146 -15.77937 1.000 26.26691 ? 348 GLN A O     1 
ATOM   2731 C  CB    . GLN A 1 348 ? 6.70690   -18.82946 -16.32738 1.000 26.27588 ? 348 GLN A CB    1 
ATOM   2732 C  CG    . GLN A 1 348 ? 7.98189   -18.50246 -15.56636 1.000 18.17418 ? 348 GLN A CG    1 
ATOM   2733 C  CD    . GLN A 1 348 ? 9.13489   -19.40946 -15.94835 1.000 23.98260 ? 348 GLN A CD    1 
ATOM   2734 O  OE1   . GLN A 1 348 ? 9.30091   -19.76546 -17.11534 1.000 20.70406 ? 348 GLN A OE1   1 
ATOM   2735 N  NE2   . GLN A 1 348 ? 9.93587   -19.79447 -14.96133 1.000 28.25810 ? 348 GLN A NE2   1 
ATOM   2736 N  N     . LEU A 1 349 ? 5.37692   -16.11745 -17.70239 1.000 23.19173 ? 349 LEU A N     1 
ATOM   2737 C  CA    . LEU A 1 349 ? 5.59793   -14.76745 -18.20838 1.000 22.00499 ? 349 LEU A CA    1 
ATOM   2738 C  C     . LEU A 1 349 ? 4.77092   -13.74245 -17.44139 1.000 25.96106 ? 349 LEU A C     1 
ATOM   2739 O  O     . LEU A 1 349 ? 5.28092   -12.67945 -17.06838 1.000 23.24882 ? 349 LEU A O     1 
ATOM   2740 C  CB    . LEU A 1 349 ? 5.27296   -14.71144 -19.70139 1.000 19.31162 ? 349 LEU A CB    1 
ATOM   2741 C  CG    . LEU A 1 349 ? 5.26897   -13.32644 -20.35038 1.000 20.66278 ? 349 LEU A CG    1 
ATOM   2742 C  CD1   . LEU A 1 349 ? 6.61797   -12.64544 -20.19036 1.000 20.77833 ? 349 LEU A CD1   1 
ATOM   2743 C  CD2   . LEU A 1 349 ? 4.88599   -13.42643 -21.81839 1.000 27.97165 ? 349 LEU A CD2   1 
ATOM   2744 N  N     . VAL A 1 350 ? 3.49092   -14.04045 -17.19841 1.000 25.67842 ? 350 VAL A N     1 
ATOM   2745 C  CA    . VAL A 1 350 ? 2.61891   -13.08945 -16.50942 1.000 24.70724 ? 350 VAL A CA    1 
ATOM   2746 C  C     . VAL A 1 350 ? 2.76889   -13.12845 -14.99842 1.000 20.11915 ? 350 VAL A C     1 
ATOM   2747 O  O     . VAL A 1 350 ? 2.27488   -12.22446 -14.31442 1.000 24.94242 ? 350 VAL A O     1 
ATOM   2748 C  CB    . VAL A 1 350 ? 1.14192   -13.33144 -16.88045 1.000 25.59476 ? 350 VAL A CB    1 
ATOM   2749 C  CG1   . VAL A 1 350 ? 0.94394   -13.19344 -18.38345 1.000 22.25096 ? 350 VAL A CG1   1 
ATOM   2750 C  CG2   . VAL A 1 350 ? 0.69091   -14.70145 -16.40046 1.000 23.23580 ? 350 VAL A CG2   1 
ATOM   2751 N  N     A THR A 1 351 ? 3.43488   -14.14546 -14.45441 0.364 22.14221 ? 351 THR A N     1 
ATOM   2752 N  N     B THR A 1 351 ? 3.43288   -14.14846 -14.45941 0.636 22.05535 ? 351 THR A N     1 
ATOM   2753 C  CA    A THR A 1 351 ? 3.65585   -14.24346 -13.01541 0.364 23.65729 ? 351 THR A CA    1 
ATOM   2754 C  CA    B THR A 1 351 ? 3.65785   -14.26846 -13.02441 0.636 23.59087 ? 351 THR A CA    1 
ATOM   2755 C  C     A THR A 1 351 ? 5.03085   -13.73247 -12.60039 0.364 22.76524 ? 351 THR A C     1 
ATOM   2756 C  C     B THR A 1 351 ? 5.02485   -13.73847 -12.60639 0.636 22.88561 ? 351 THR A C     1 
ATOM   2757 O  O     A THR A 1 351 ? 5.13784   -12.92047 -11.67838 0.364 24.40487 ? 351 THR A O     1 
ATOM   2758 O  O     B THR A 1 351 ? 5.11784   -12.91447 -11.69238 0.636 24.37248 ? 351 THR A O     1 
ATOM   2759 C  CB    A THR A 1 351 ? 3.47484   -15.69246 -12.54242 0.364 24.84171 ? 351 THR A CB    1 
ATOM   2760 C  CB    B THR A 1 351 ? 3.51085   -15.73246 -12.58442 0.636 24.94364 ? 351 THR A CB    1 
ATOM   2761 O  OG1   A THR A 1 351 ? 4.30586   -16.56046 -13.32141 0.364 23.63350 ? 351 THR A OG1   1 
ATOM   2762 O  OG1   B THR A 1 351 ? 2.20085   -16.20746 -12.92144 0.636 23.60727 ? 351 THR A OG1   1 
ATOM   2763 C  CG2   A THR A 1 351 ? 2.02085   -16.12346 -12.67644 0.364 23.50986 ? 351 THR A CG2   1 
ATOM   2764 C  CG2   B THR A 1 351 ? 3.72182   -15.86347 -11.08342 0.636 26.95658 ? 351 THR A CG2   1 
ATOM   2765 N  N     . TRP A 1 352 ? 6.08886   -14.19247 -13.26537 1.000 23.44006 ? 352 TRP A N     1 
ATOM   2766 C  CA    . TRP A 1 352 ? 7.44885   -13.77147 -12.94835 1.000 24.15673 ? 352 TRP A CA    1 
ATOM   2767 C  C     . TRP A 1 352 ? 7.95087   -12.64147 -13.83434 1.000 22.87450 ? 352 TRP A C     1 
ATOM   2768 O  O     . TRP A 1 352 ? 8.68286   -11.76847 -13.35733 1.000 26.12989 ? 352 TRP A O     1 
ATOM   2769 C  CB    . TRP A 1 352 ? 8.41485   -14.95647 -13.06034 1.000 26.45684 ? 352 TRP A CB    1 
ATOM   2770 C  CG    . TRP A 1 352 ? 8.30084   -15.95147 -11.94935 1.000 24.88824 ? 352 TRP A CG    1 
ATOM   2771 C  CD1   . TRP A 1 352 ? 7.30682   -16.03348 -11.01936 1.000 25.06967 ? 352 TRP A CD1   1 
ATOM   2772 C  CD2   . TRP A 1 352 ? 9.22283   -17.00448 -11.64634 1.000 22.95943 ? 352 TRP A CD2   1 
ATOM   2773 N  NE1   . TRP A 1 352 ? 7.54981   -17.07848 -10.15736 1.000 22.19744 ? 352 TRP A NE1   1 
ATOM   2774 C  CE2   . TRP A 1 352 ? 8.72081   -17.68748 -10.52135 1.000 28.07414 ? 352 TRP A CE2   1 
ATOM   2775 C  CE3   . TRP A 1 352 ? 10.42384  -17.43748 -12.21832 1.000 21.02686 ? 352 TRP A CE3   1 
ATOM   2776 C  CZ2   . TRP A 1 352 ? 9.37680   -18.78048 -9.95734  1.000 28.82244 ? 352 TRP A CZ2   1 
ATOM   2777 C  CZ3   . TRP A 1 352 ? 11.07383  -18.52148 -11.65631 1.000 19.76166 ? 352 TRP A CZ3   1 
ATOM   2778 C  CH2   . TRP A 1 352 ? 10.54881  -19.18048 -10.53832 1.000 28.32268 ? 352 TRP A CH2   1 
ATOM   2779 N  N     . GLY A 1 353 ? 7.58189   -12.63346 -15.11235 1.000 22.06149 ? 353 GLY A N     1 
ATOM   2780 C  CA    . GLY A 1 353 ? 8.13491   -11.67646 -16.04633 1.000 22.03024 ? 353 GLY A CA    1 
ATOM   2781 C  C     . GLY A 1 353 ? 9.47091   -12.06946 -16.63131 1.000 25.12631 ? 353 GLY A C     1 
ATOM   2782 O  O     . GLY A 1 353 ? 10.12992  -11.22746 -17.25430 1.000 22.71400 ? 353 GLY A O     1 
ATOM   2783 N  N     . TRP A 1 354 ? 9.89191   -13.31946 -16.45131 1.000 19.32757 ? 354 TRP A N     1 
ATOM   2784 C  CA    . TRP A 1 354 ? 11.16892  -13.79846 -16.95629 1.000 21.95964 ? 354 TRP A CA    1 
ATOM   2785 C  C     . TRP A 1 354 ? 11.05292  -15.28646 -17.24230 1.000 23.63047 ? 354 TRP A C     1 
ATOM   2786 O  O     . TRP A 1 354 ? 10.44790  -16.02946 -16.46431 1.000 20.37709 ? 354 TRP A O     1 
ATOM   2787 C  CB    . TRP A 1 354 ? 12.30190  -13.53947 -15.95528 1.000 27.44458 ? 354 TRP A CB    1 
ATOM   2788 C  CG    . TRP A 1 354 ? 13.62691  -14.11247 -16.37126 1.000 22.91381 ? 354 TRP A CG    1 
ATOM   2789 C  CD1   . TRP A 1 354 ? 14.62292  -13.46747 -17.04424 1.000 24.30954 ? 354 TRP A CD1   1 
ATOM   2790 C  CD2   . TRP A 1 354 ? 14.10090  -15.44547 -16.13626 1.000 20.56697 ? 354 TRP A CD2   1 
ATOM   2791 N  NE1   . TRP A 1 354 ? 15.68692  -14.31347 -17.24523 1.000 22.34463 ? 354 TRP A NE1   1 
ATOM   2792 C  CE2   . TRP A 1 354 ? 15.39091  -15.53547 -16.69724 1.000 19.07666 ? 354 TRP A CE2   1 
ATOM   2793 C  CE3   . TRP A 1 354 ? 13.55889  -16.57247 -15.50827 1.000 22.17030 ? 354 TRP A CE3   1 
ATOM   2794 C  CZ2   . TRP A 1 354 ? 16.14591  -16.70447 -16.64923 1.000 19.19328 ? 354 TRP A CZ2   1 
ATOM   2795 C  CZ3   . TRP A 1 354 ? 14.31089  -17.73347 -15.46326 1.000 16.26593 ? 354 TRP A CZ3   1 
ATOM   2796 C  CH2   . TRP A 1 354 ? 15.58989  -17.79047 -16.03024 1.000 15.52676 ? 354 TRP A CH2   1 
ATOM   2797 N  N     . MET A 1 355 ? 11.62993  -15.71446 -18.36129 1.000 22.83587 ? 355 MET A N     1 
ATOM   2798 C  CA    . MET A 1 355 ? 11.69694  -17.12646 -18.70630 1.000 21.53711 ? 355 MET A CA    1 
ATOM   2799 C  C     . MET A 1 355 ? 13.09394  -17.44746 -19.21328 1.000 23.55238 ? 355 MET A C     1 
ATOM   2800 O  O     . MET A 1 355 ? 13.87395  -16.55546 -19.55426 1.000 23.39157 ? 355 MET A O     1 
ATOM   2801 C  CB    . MET A 1 355 ? 10.65495  -17.51845 -19.76632 1.000 23.68394 ? 355 MET A CB    1 
ATOM   2802 C  CG    . MET A 1 355 ? 9.22295   -17.16245 -19.41434 1.000 21.38336 ? 355 MET A CG    1 
ATOM   2803 S  SD    . MET A 1 355 ? 8.71096   -15.59945 -20.14934 1.000 18.39778 ? 355 MET A SD    1 
ATOM   2804 C  CE    . MET A 1 355 ? 8.67399   -16.03544 -21.88434 1.000 18.31395 ? 355 MET A CE    1 
ATOM   2805 N  N     . HIS A 1 356 ? 13.39994  -18.74046 -19.25328 1.000 23.68022 ? 356 HIS A N     1 
ATOM   2806 C  CA    . HIS A 1 356 ? 14.65195  -19.19046 -19.84226 1.000 18.32585 ? 356 HIS A CA    1 
ATOM   2807 C  C     . HIS A 1 356 ? 14.66897  -18.86545 -21.33126 1.000 18.77836 ? 356 HIS A C     1 
ATOM   2808 O  O     . HIS A 1 356 ? 13.62398  -18.76745 -21.97827 1.000 26.02990 ? 356 HIS A O     1 
ATOM   2809 C  CB    . HIS A 1 356 ? 14.82894  -20.69246 -19.62526 1.000 18.96307 ? 356 HIS A CB    1 
ATOM   2810 C  CG    . HIS A 1 356 ? 16.21395  -21.18546 -19.90024 1.000 19.13319 ? 356 HIS A CG    1 
ATOM   2811 N  ND1   . HIS A 1 356 ? 17.17693  -21.28047 -18.91823 1.000 22.23260 ? 356 HIS A ND1   1 
ATOM   2812 C  CD2   . HIS A 1 356 ? 16.79896  -21.61346 -21.04324 1.000 19.85077 ? 356 HIS A CD2   1 
ATOM   2813 C  CE1   . HIS A 1 356 ? 18.29494  -21.74447 -19.44521 1.000 22.91774 ? 356 HIS A CE1   1 
ATOM   2814 N  NE2   . HIS A 1 356 ? 18.09296  -21.95446 -20.73422 1.000 18.82087 ? 356 HIS A NE2   1 
ATOM   2815 N  N     . HIS A 1 357 ? 15.87598  -18.69145 -21.87524 1.000 20.61700 ? 357 HIS A N     1 
ATOM   2816 C  CA    . HIS A 1 357 ? 16.00100  -18.34945 -23.28924 1.000 23.40798 ? 357 HIS A CA    1 
ATOM   2817 C  C     . HIS A 1 357 ? 15.37102  -19.42044 -24.17225 1.000 20.63912 ? 357 HIS A C     1 
ATOM   2818 O  O     . HIS A 1 357 ? 14.62803  -19.11044 -25.11126 1.000 13.79126 ? 357 HIS A O     1 
ATOM   2819 C  CB    . HIS A 1 357 ? 17.47101  -18.14445 -23.65521 1.000 22.56479 ? 357 HIS A CB    1 
ATOM   2820 C  CG    . HIS A 1 357 ? 17.68003  -17.63644 -25.04621 1.000 16.95000 ? 357 HIS A CG    1 
ATOM   2821 N  ND1   . HIS A 1 357 ? 18.84904  -17.84144 -25.74719 1.000 21.52626 ? 357 HIS A ND1   1 
ATOM   2822 C  CD2   . HIS A 1 357 ? 16.86905  -16.92744 -25.86722 1.000 19.72151 ? 357 HIS A CD2   1 
ATOM   2823 C  CE1   . HIS A 1 357 ? 18.74906  -17.28144 -26.94019 1.000 25.25721 ? 357 HIS A CE1   1 
ATOM   2824 N  NE2   . HIS A 1 357 ? 17.55706  -16.72144 -27.03821 1.000 24.24942 ? 357 HIS A NE2   1 
ATOM   2825 N  N     . LEU A 1 358 ? 15.65301  -20.69345 -23.88025 1.000 23.32620 ? 358 LEU A N     1 
ATOM   2826 C  CA    . LEU A 1 358 ? 15.02902  -21.77744 -24.63026 1.000 15.63596 ? 358 LEU A CA    1 
ATOM   2827 C  C     . LEU A 1 358 ? 13.53201  -21.85644 -24.36329 1.000 19.05703 ? 358 LEU A C     1 
ATOM   2828 O  O     . LEU A 1 358 ? 12.77703  -22.32944 -25.21930 1.000 18.84146 ? 358 LEU A O     1 
ATOM   2829 C  CB    . LEU A 1 358 ? 15.70301  -23.10844 -24.29426 1.000 20.74127 ? 358 LEU A CB    1 
ATOM   2830 C  CG    . LEU A 1 358 ? 17.09202  -23.32344 -24.90124 1.000 14.62300 ? 358 LEU A CG    1 
ATOM   2831 C  CD1   . LEU A 1 358 ? 17.65101  -24.68045 -24.50423 1.000 16.79487 ? 358 LEU A CD1   1 
ATOM   2832 C  CD2   . LEU A 1 358 ? 17.03404  -23.18744 -26.41424 1.000 13.97580 ? 358 LEU A CD2   1 
ATOM   2833 N  N     . ALA A 1 359 ? 13.08300  -21.40644 -23.18829 1.000 19.37367 ? 359 ALA A N     1 
ATOM   2834 C  CA    . ALA A 1 359 ? 11.64899  -21.33244 -22.93131 1.000 19.59999 ? 359 ALA A CA    1 
ATOM   2835 C  C     . ALA A 1 359 ? 10.99301  -20.26944 -23.80332 1.000 17.42202 ? 359 ALA A C     1 
ATOM   2836 O  O     . ALA A 1 359 ? 9.89002   -20.47643 -24.32234 1.000 14.04999 ? 359 ALA A O     1 
ATOM   2837 C  CB    . ALA A 1 359 ? 11.39197  -21.05445 -21.45132 1.000 17.02581 ? 359 ALA A CB    1 
ATOM   2838 N  N     . ARG A 1 360 ? 11.65757  -19.12320 -23.97537 1.000 15.12529 ? 360 ARG A N     1 
ATOM   2839 C  CA    . ARG A 1 360 ? 11.17017  -18.11223 -24.90512 1.000 18.11811 ? 360 ARG A CA    1 
ATOM   2840 C  C     . ARG A 1 360 ? 11.27265  -18.57367 -26.35182 1.000 18.47530 ? 360 ARG A C     1 
ATOM   2841 O  O     . ARG A 1 360 ? 10.52617  -18.07867 -27.20228 1.000 23.30995 ? 360 ARG A O     1 
ATOM   2842 C  CB    . ARG A 1 360 ? 11.94335  -16.80397 -24.72285 1.000 18.00472 ? 360 ARG A CB    1 
ATOM   2843 C  CG    . ARG A 1 360 ? 12.04968  -16.33841 -23.27996 1.000 17.98204 ? 360 ARG A CG    1 
ATOM   2844 C  CD    . ARG A 1 360 ? 12.70097  -14.96866 -23.17589 1.000 16.13956 ? 360 ARG A CD    1 
ATOM   2845 N  NE    . ARG A 1 360 ? 13.06661  -14.64808 -21.80103 1.000 24.33941 ? 360 ARG A NE    1 
ATOM   2846 C  CZ    . ARG A 1 360 ? 13.45384  -13.44981 -21.38525 1.000 18.17236 ? 360 ARG A CZ    1 
ATOM   2847 N  NH1   . ARG A 1 360 ? 13.50924  -12.41614 -22.20905 1.000 17.18558 ? 360 ARG A NH1   1 
ATOM   2848 N  NH2   . ARG A 1 360 ? 13.79158  -13.28405 -20.10981 1.000 20.89200 ? 360 ARG A NH2   1 
ATOM   2849 N  N     . HIS A 1 361 ? 12.17905  -19.50843 -26.64630 1.000 17.73250 ? 361 HIS A N     1 
ATOM   2850 C  CA    . HIS A 1 361 ? 12.29907  -20.02842 -28.00430 1.000 18.71273 ? 361 HIS A CA    1 
ATOM   2851 C  C     . HIS A 1 361 ? 11.07208  -20.84142 -28.39732 1.000 20.58208 ? 361 HIS A C     1 
ATOM   2852 O  O     . HIS A 1 361 ? 10.59710  -20.74542 -29.53433 1.000 21.44967 ? 361 HIS A O     1 
ATOM   2853 C  CB    . HIS A 1 361 ? 13.56407  -20.87943 -28.12828 1.000 19.01641 ? 361 HIS A CB    1 
ATOM   2854 C  CG    . HIS A 1 361 ? 14.74908  -20.13243 -28.65526 1.000 23.89005 ? 361 HIS A CG    1 
ATOM   2855 N  ND1   . HIS A 1 361 ? 15.33710  -20.42942 -29.86625 1.000 19.63813 ? 361 HIS A ND1   1 
ATOM   2856 C  CD2   . HIS A 1 361 ? 15.45808  -19.10143 -28.13725 1.000 19.67646 ? 361 HIS A CD2   1 
ATOM   2857 C  CE1   . HIS A 1 361 ? 16.35711  -19.61442 -30.07024 1.000 23.97607 ? 361 HIS A CE1   1 
ATOM   2858 N  NE2   . HIS A 1 361 ? 16.45109  -18.79843 -29.03723 1.000 28.68482 ? 361 HIS A NE2   1 
ATOM   2859 N  N     . SER A 1 362 ? 10.54506  -21.64442 -27.47033 1.000 19.55104 ? 362 SER A N     1 
ATOM   2860 C  CA    . SER A 1 362 ? 9.42007   -22.51542 -27.79235 1.000 21.48707 ? 362 SER A CA    1 
ATOM   2861 C  C     . SER A 1 362 ? 8.15407   -21.71142 -28.06537 1.000 23.30680 ? 362 SER A C     1 
ATOM   2862 O  O     . SER A 1 362 ? 7.43409   -21.97941 -29.03338 1.000 22.98506 ? 362 SER A O     1 
ATOM   2863 C  CB    . SER A 1 362 ? 9.18905   -23.51242 -26.65636 1.000 16.44871 ? 362 SER A CB    1 
ATOM   2864 O  OG    . SER A 1 362 ? 10.32304  -24.33843 -26.45935 1.000 20.13152 ? 362 SER A OG    1 
ATOM   2865 N  N     . VAL A 1 363 ? 7.86506   -20.72042 -27.21837 1.000 21.25963 ? 363 VAL A N     1 
ATOM   2866 C  CA    . VAL A 1 363 ? 6.63906   -19.94542 -27.38539 1.000 22.13161 ? 363 VAL A CA    1 
ATOM   2867 C  C     . VAL A 1 363 ? 6.74208   -19.00841 -28.58138 1.000 26.18791 ? 363 VAL A C     1 
ATOM   2868 O  O     . VAL A 1 363 ? 5.74009   -18.74141 -29.25640 1.000 26.12727 ? 363 VAL A O     1 
ATOM   2869 C  CB    . VAL A 1 363 ? 6.31105   -19.17942 -26.09039 1.000 23.85501 ? 363 VAL A CB    1 
ATOM   2870 C  CG1   . VAL A 1 363 ? 5.88803   -20.14942 -24.99840 1.000 24.92730 ? 363 VAL A CG1   1 
ATOM   2871 C  CG2   . VAL A 1 363 ? 7.50804   -18.35742 -25.63837 1.000 21.38947 ? 363 VAL A CG2   1 
ATOM   2872 N  N     . ALA A 1 364 ? 7.94009   -18.49441 -28.86936 1.000 26.77589 ? 364 ALA A N     1 
ATOM   2873 C  CA    . ALA A 1 364 ? 8.10311   -17.62941 -30.03335 1.000 24.84104 ? 364 ALA A CA    1 
ATOM   2874 C  C     . ALA A 1 364 ? 8.05113   -18.43341 -31.32536 1.000 23.43581 ? 364 ALA A C     1 
ATOM   2875 O  O     . ALA A 1 364 ? 7.52914   -17.95640 -32.34036 1.000 28.77301 ? 364 ALA A O     1 
ATOM   2876 C  CB    . ALA A 1 364 ? 9.41511   -16.85241 -29.93433 1.000 20.70473 ? 364 ALA A CB    1 
ATOM   2877 N  N     . CYS A 1 365 ? 8.58712   -19.65541 -31.30935 1.000 25.29284 ? 365 CYS A N     1 
ATOM   2878 C  CA    . CYS A 1 365 ? 8.51014   -20.50740 -32.49136 1.000 26.00386 ? 365 CYS A CA    1 
ATOM   2879 C  C     . CYS A 1 365 ? 7.08914   -21.00640 -32.71538 1.000 25.31729 ? 365 CYS A C     1 
ATOM   2880 O  O     . CYS A 1 365 ? 6.63516   -21.10739 -33.86039 1.000 27.43192 ? 365 CYS A O     1 
ATOM   2881 C  CB    . CYS A 1 365 ? 9.48014   -21.68040 -32.35735 1.000 26.23258 ? 365 CYS A CB    1 
ATOM   2882 S  SG    . CYS A 1 365 ? 9.49016   -22.81240 -33.76635 1.000 29.08217 ? 365 CYS A SG    1 
ATOM   2883 N  N     . PHE A 1 366 ? 6.36913   -21.31240 -31.63339 1.000 21.80824 ? 366 PHE A N     1 
ATOM   2884 C  CA    . PHE A 1 366 ? 5.00113   -21.80640 -31.76342 1.000 22.54138 ? 366 PHE A CA    1 
ATOM   2885 C  C     . PHE A 1 366 ? 4.08014   -20.74339 -32.34943 1.000 28.16365 ? 366 PHE A C     1 
ATOM   2886 O  O     . PHE A 1 366 ? 3.17715   -21.05939 -33.13244 1.000 22.24506 ? 366 PHE A O     1 
ATOM   2887 C  CB    . PHE A 1 366 ? 4.48611   -22.27440 -30.40243 1.000 21.31899 ? 366 PHE A CB    1 
ATOM   2888 C  CG    . PHE A 1 366 ? 3.14511   -22.94940 -30.45645 1.000 20.18249 ? 366 PHE A CG    1 
ATOM   2889 C  CD1   . PHE A 1 366 ? 3.05111   -24.31140 -30.68946 1.000 26.52983 ? 366 PHE A CD1   1 
ATOM   2890 C  CD2   . PHE A 1 366 ? 1.97910   -22.22640 -30.26746 1.000 22.96791 ? 366 PHE A CD2   1 
ATOM   2891 C  CE1   . PHE A 1 366 ? 1.82011   -24.93940 -30.73848 1.000 28.82651 ? 366 PHE A CE1   1 
ATOM   2892 C  CE2   . PHE A 1 366 ? 0.74510   -22.84640 -30.31549 1.000 26.04946 ? 366 PHE A CE2   1 
ATOM   2893 C  CZ    . PHE A 1 366 ? 0.66510   -24.20539 -30.55049 1.000 32.17395 ? 366 PHE A CZ    1 
ATOM   2894 N  N     . LEU A 1 367 ? 4.29213   -19.47840 -31.98442 1.000 29.18310 ? 367 LEU A N     1 
ATOM   2895 C  CA    . LEU A 1 367 ? 3.42114   -18.41039 -32.46143 1.000 27.09970 ? 367 LEU A CA    1 
ATOM   2896 C  C     . LEU A 1 367 ? 3.73317   -18.02539 -33.90242 1.000 27.60340 ? 367 LEU A C     1 
ATOM   2897 O  O     . LEU A 1 367 ? 2.82018   -17.71538 -34.67544 1.000 26.29788 ? 367 LEU A O     1 
ATOM   2898 C  CB    . LEU A 1 367 ? 3.54513   -17.18940 -31.54842 1.000 22.95238 ? 367 LEU A CB    1 
ATOM   2899 C  CG    . LEU A 1 367 ? 2.69914   -15.96839 -31.91143 1.000 25.66305 ? 367 LEU A CG    1 
ATOM   2900 C  CD1   . LEU A 1 367 ? 1.22214   -16.24639 -31.68746 1.000 30.37785 ? 367 LEU A CD1   1 
ATOM   2901 C  CD2   . LEU A 1 367 ? 3.14613   -14.75140 -31.11742 1.000 23.71751 ? 367 LEU A CD2   1 
ATOM   2902 N  N     . THR A 1 368 ? 5.01017   -18.04739 -34.28440 1.000 29.85910 ? 368 THR A N     1 
ATOM   2903 C  CA    . THR A 1 368 ? 5.41719   -17.55939 -35.59640 1.000 30.37308 ? 368 THR A CA    1 
ATOM   2904 C  C     . THR A 1 368 ? 5.56521   -18.68738 -36.61040 1.000 29.10008 ? 368 THR A C     1 
ATOM   2905 O  O     . THR A 1 368 ? 4.60021   -19.39638 -36.91041 1.000 30.71779 ? 368 THR A O     1 
ATOM   2906 C  CB    . THR A 1 368 ? 6.73219   -16.78239 -35.49137 1.000 29.79844 ? 368 THR A CB    1 
ATOM   2907 O  OG1   . THR A 1 368 ? 7.75918   -17.64539 -34.98736 1.000 27.81233 ? 368 THR A OG1   1 
ATOM   2908 C  CG2   . THR A 1 368 ? 6.57318   -15.58839 -34.55937 1.000 21.05961 ? 368 THR A CG2   1 
ATOM   2909 N  N     . ARG A 1 369 ? 6.78006   -18.86730 -37.12929 1.000 28.45604 ? 369 ARG A N     1 
ATOM   2910 C  CA    . ARG A 1 369 ? 7.04296   -19.75814 -38.25530 1.000 27.89190 ? 369 ARG A CA    1 
ATOM   2911 C  C     . ARG A 1 369 ? 6.76227   -21.22599 -37.95018 1.000 31.20153 ? 369 ARG A C     1 
ATOM   2912 O  O     . ARG A 1 369 ? 6.88072   -22.07718 -38.83741 1.000 33.88964 ? 369 ARG A O     1 
ATOM   2913 C  CB    . ARG A 1 369 ? 8.49655   -19.60316 -38.70611 1.000 34.51476 ? 369 ARG A CB    1 
ATOM   2914 C  CG    . ARG A 1 369 ? 9.50133   -19.83170 -37.58933 1.000 31.46610 ? 369 ARG A CG    1 
ATOM   2915 C  CD    . ARG A 1 369 ? 10.92461  -19.88627 -38.11279 1.000 33.46967 ? 369 ARG A CD    1 
ATOM   2916 N  NE    . ARG A 1 369 ? 11.87678  -20.16629 -37.04511 1.000 30.90983 ? 369 ARG A NE    1 
ATOM   2917 C  CZ    . ARG A 1 369 ? 12.15164  -21.38033 -36.58803 1.000 31.80052 ? 369 ARG A CZ    1 
ATOM   2918 N  NH1   . ARG A 1 369 ? 11.56415  -22.45593 -37.08668 1.000 26.86532 ? 369 ARG A NH1   1 
ATOM   2919 N  NH2   . ARG A 1 369 ? 13.03535  -21.51864 -35.60364 1.000 23.82256 ? 369 ARG A NH2   1 
ATOM   2920 N  N     . GLY A 1 370 ? 6.39420   -21.53838 -36.71140 1.000 25.03953 ? 370 GLY A N     1 
ATOM   2921 C  CA    . GLY A 1 370 ? 6.19119   -22.92038 -36.32340 1.000 27.09636 ? 370 GLY A CA    1 
ATOM   2922 C  C     . GLY A 1 370 ? 4.77620   -23.43138 -36.50143 1.000 29.28150 ? 370 GLY A C     1 
ATOM   2923 O  O     . GLY A 1 370 ? 4.55521   -24.40738 -37.22343 1.000 29.66840 ? 370 GLY A O     1 
ATOM   2924 N  N     . ASP A 1 371 ? 3.80819   -22.78638 -35.85044 1.000 26.12609 ? 371 ASP A N     1 
ATOM   2925 C  CA    . ASP A 1 371 ? 2.44719   -23.31238 -35.83246 1.000 26.99054 ? 371 ASP A CA    1 
ATOM   2926 C  C     . ASP A 1 371 ? 1.41320   -22.28138 -36.26447 1.000 21.63883 ? 371 ASP A C     1 
ATOM   2927 O  O     . ASP A 1 371 ? 0.67521   -22.50137 -37.22949 1.000 16.31925 ? 371 ASP A O     1 
ATOM   2928 C  CB    . ASP A 1 371 ? 2.10216   -23.83538 -34.43547 1.000 21.09844 ? 371 ASP A CB    1 
ATOM   2929 C  CG    . ASP A 1 371 ? 2.88216   -25.08039 -34.07046 1.000 29.23725 ? 371 ASP A CG    1 
ATOM   2930 O  OD1   . ASP A 1 371 ? 4.11615   -24.98539 -33.89744 1.000 33.96646 ? 371 ASP A OD1   1 
ATOM   2931 O  OD2   . ASP A 1 371 ? 2.25915   -26.15739 -33.95047 1.000 30.33092 ? 371 ASP A OD2   1 
ATOM   2932 N  N     . LEU A 1 372 ? 1.34319   -21.15638 -35.55247 1.000 22.24853 ? 372 LEU A N     1 
ATOM   2933 C  CA    . LEU A 1 372 ? 0.26019   -20.20138 -35.74348 1.000 23.59707 ? 372 LEU A CA    1 
ATOM   2934 C  C     . LEU A 1 372 ? 0.51121   -19.21337 -36.87548 1.000 24.55358 ? 372 LEU A C     1 
ATOM   2935 O  O     . LEU A 1 372 ? -0.45078  -18.62337 -37.38149 1.000 18.52379 ? 372 LEU A O     1 
ATOM   2936 C  CB    . LEU A 1 372 ? 0.00817   -19.43338 -34.44249 1.000 26.94885 ? 372 LEU A CB    1 
ATOM   2937 C  CG    . LEU A 1 372 ? -0.17485  -20.30438 -33.19749 1.000 27.50348 ? 372 LEU A CG    1 
ATOM   2938 C  CD1   . LEU A 1 372 ? -0.48387  -19.45239 -31.97649 1.000 26.76778 ? 372 LEU A CD1   1 
ATOM   2939 C  CD2   . LEU A 1 372 ? -1.26385  -21.34338 -33.41851 1.000 31.52692 ? 372 LEU A CD2   1 
ATOM   2940 N  N     . TYR A 1 373 ? 1.76922   -19.01537 -37.27546 1.000 26.86255 ? 373 TYR A N     1 
ATOM   2941 C  CA    . TYR A 1 373 ? 2.13223   -18.10837 -38.36845 1.000 27.97006 ? 373 TYR A CA    1 
ATOM   2942 C  C     . TYR A 1 373 ? 1.67123   -16.67737 -38.10045 1.000 27.48985 ? 373 TYR A C     1 
ATOM   2943 O  O     . TYR A 1 373 ? 1.42225   -15.90837 -39.03145 1.000 31.59569 ? 373 TYR A O     1 
ATOM   2944 C  CB    . TYR A 1 373 ? 1.58825   -18.60836 -39.71046 1.000 27.67219 ? 373 TYR A CB    1 
ATOM   2945 C  CG    . TYR A 1 373 ? 2.56827   -18.47536 -40.85544 1.000 26.00877 ? 373 TYR A CG    1 
ATOM   2946 C  CD1   . TYR A 1 373 ? 3.73827   -19.22236 -40.88043 1.000 31.84947 ? 373 TYR A CD1   1 
ATOM   2947 C  CD2   . TYR A 1 373 ? 2.31829   -17.61336 -41.91544 1.000 33.04335 ? 373 TYR A CD2   1 
ATOM   2948 C  CE1   . TYR A 1 373 ? 4.63729   -19.10936 -41.92441 1.000 37.83195 ? 373 TYR A CE1   1 
ATOM   2949 C  CE2   . TYR A 1 373 ? 3.21231   -17.49435 -42.96543 1.000 34.25907 ? 373 TYR A CE2   1 
ATOM   2950 C  CZ    . TYR A 1 373 ? 4.36930   -18.24336 -42.96441 1.000 31.79990 ? 373 TYR A CZ    1 
ATOM   2951 O  OH    . TYR A 1 373 ? 5.26232   -18.13135 -44.00540 1.000 28.80613 ? 373 TYR A OH    1 
ATOM   2952 N  N     . VAL A 1 374 ? 1.55721   -16.31037 -36.82645 1.000 25.77978 ? 374 VAL A N     1 
ATOM   2953 C  CA    . VAL A 1 374 ? 1.18721   -14.95137 -36.44645 1.000 29.65110 ? 374 VAL A CA    1 
ATOM   2954 C  C     . VAL A 1 374 ? 2.43421   -14.07438 -36.45343 1.000 25.78689 ? 374 VAL A C     1 
ATOM   2955 O  O     . VAL A 1 374 ? 3.54821   -14.54138 -36.19141 1.000 21.96033 ? 374 VAL A O     1 
ATOM   2956 C  CB    . VAL A 1 374 ? 0.48719   -14.95038 -35.07146 1.000 29.35755 ? 374 VAL A CB    1 
ATOM   2957 C  CG1   . VAL A 1 374 ? 0.04519   -13.54738 -34.67646 1.000 29.38684 ? 374 VAL A CG1   1 
ATOM   2958 C  CG2   . VAL A 1 374 ? -0.70781  -15.89238 -35.08948 1.000 31.87824 ? 374 VAL A CG2   1 
ATOM   2959 N  N     . SER A 1 375 ? 2.24622   -12.79438 -36.77243 1.000 24.70363 ? 375 SER A N     1 
ATOM   2960 C  CA    . SER A 1 375 ? 3.36322   -11.86538 -36.88641 1.000 28.24791 ? 375 SER A CA    1 
ATOM   2961 C  C     . SER A 1 375 ? 4.16720   -11.80538 -35.59439 1.000 25.65095 ? 375 SER A C     1 
ATOM   2962 O  O     . SER A 1 375 ? 3.61819   -11.89739 -34.49340 1.000 28.11089 ? 375 SER A O     1 
ATOM   2963 C  CB    . SER A 1 375 ? 2.85323   -10.46837 -37.24541 1.000 25.66413 ? 375 SER A CB    1 
ATOM   2964 O  OG    . SER A 1 375 ? 3.92123   -9.54038  -37.32339 1.000 20.83484 ? 375 SER A OG    1 
ATOM   2965 N  N     . TRP A 1 376 ? 5.48621   -11.65338 -35.74037 1.000 27.97443 ? 376 TRP A N     1 
ATOM   2966 C  CA    . TRP A 1 376 ? 6.35519   -11.53239 -34.57736 1.000 29.33498 ? 376 TRP A CA    1 
ATOM   2967 C  C     . TRP A 1 376 ? 6.17418   -10.20339 -33.85936 1.000 27.36136 ? 376 TRP A C     1 
ATOM   2968 O  O     . TRP A 1 376 ? 6.51516   -10.10240 -32.67535 1.000 25.84426 ? 376 TRP A O     1 
ATOM   2969 C  CB    . TRP A 1 376 ? 7.81719   -11.70839 -34.98834 1.000 27.22757 ? 376 TRP A CB    1 
ATOM   2970 C  CG    . TRP A 1 376 ? 8.26821   -10.73939 -36.03733 1.000 32.56693 ? 376 TRP A CG    1 
ATOM   2971 C  CD1   . TRP A 1 376 ? 8.22023   -10.91538 -37.39033 1.000 31.80586 ? 376 TRP A CD1   1 
ATOM   2972 C  CD2   . TRP A 1 376 ? 8.83821   -9.44139  -35.82231 1.000 28.66524 ? 376 TRP A CD2   1 
ATOM   2973 N  NE1   . TRP A 1 376 ? 8.72324   -9.80838  -38.02932 1.000 30.10335 ? 376 TRP A NE1   1 
ATOM   2974 C  CE2   . TRP A 1 376 ? 9.10923   -8.88939  -37.08931 1.000 32.46113 ? 376 TRP A CE2   1 
ATOM   2975 C  CE3   . TRP A 1 376 ? 9.14420   -8.69340  -34.68131 1.000 29.63370 ? 376 TRP A CE3   1 
ATOM   2976 C  CZ2   . TRP A 1 376 ? 9.67124   -7.62439  -37.24830 1.000 30.52584 ? 376 TRP A CZ2   1 
ATOM   2977 C  CZ3   . TRP A 1 376 ? 9.70220   -7.43740  -34.84029 1.000 29.55187 ? 376 TRP A CZ3   1 
ATOM   2978 C  CH2   . TRP A 1 376 ? 9.96022   -6.91639  -36.11429 1.000 29.03443 ? 376 TRP A CH2   1 
ATOM   2979 N  N     . GLU A 1 377 ? 5.65419   -9.18239  -34.54636 1.000 24.83164 ? 377 GLU A N     1 
ATOM   2980 C  CA    . GLU A 1 377 ? 5.39018   -7.91139  -33.88136 1.000 28.84986 ? 377 GLU A CA    1 
ATOM   2981 C  C     . GLU A 1 377 ? 4.28817   -8.05639  -32.84138 1.000 27.99695 ? 377 GLU A C     1 
ATOM   2982 O  O     . GLU A 1 377 ? 4.38015   -7.48640  -31.74838 1.000 29.42293 ? 377 GLU A O     1 
ATOM   2983 C  CB    . GLU A 1 377 ? 5.02020   -6.83939  -34.90736 1.000 29.11542 ? 377 GLU A CB    1 
ATOM   2984 C  CG    . GLU A 1 377 ? 6.08022   -6.58139  -35.96435 1.000 29.88319 ? 377 GLU A CG    1 
ATOM   2985 C  CD    . GLU A 1 377 ? 5.84423   -5.28438  -36.71635 1.000 29.70670 ? 377 GLU A CD    1 
ATOM   2986 O  OE1   . GLU A 1 377 ? 5.65022   -4.24138  -36.05834 1.000 36.21553 ? 377 GLU A OE1   1 
ATOM   2987 O  OE2   . GLU A 1 377 ? 5.84425   -5.30738  -37.96435 1.000 29.66177 ? 377 GLU A OE2   1 
ATOM   2988 N  N     . ARG A 1 378 ? 3.24025   -8.82170  -33.16104 1.000 25.78811 ? 378 ARG A N     1 
ATOM   2989 C  CA    . ARG A 1 378 ? 2.16727   -9.04728  -32.19856 1.000 25.20171 ? 378 ARG A CA    1 
ATOM   2990 C  C     . ARG A 1 378 ? 2.65350   -9.84074  -30.99292 1.000 27.81689 ? 378 ARG A C     1 
ATOM   2991 O  O     . ARG A 1 378 ? 2.13881   -9.65850  -29.88447 1.000 29.56020 ? 378 ARG A O     1 
ATOM   2992 C  CB    . ARG A 1 378 ? 0.99819   -9.76679  -32.87119 1.000 30.76334 ? 378 ARG A CB    1 
ATOM   2993 C  CG    . ARG A 1 378 ? 0.48508   -9.10174  -34.14414 1.000 29.45718 ? 378 ARG A CG    1 
ATOM   2994 C  CD    . ARG A 1 378 ? -0.13567  -7.73566  -33.87548 1.000 29.36358 ? 378 ARG A CD    1 
ATOM   2995 N  NE    . ARG A 1 378 ? 0.84896   -6.65998  -33.90131 1.000 33.45916 ? 378 ARG A NE    1 
ATOM   2996 C  CZ    . ARG A 1 378 ? 1.22199   -6.01216  -34.99662 1.000 34.94221 ? 378 ARG A CZ    1 
ATOM   2997 N  NH1   . ARG A 1 378 ? 0.71335   -6.30766  -36.18170 1.000 37.68095 ? 378 ARG A NH1   1 
ATOM   2998 N  NH2   . ARG A 1 378 ? 2.12831   -5.04367  -34.90068 1.000 32.92535 ? 378 ARG A NH2   1 
ATOM   2999 N  N     . GLY A 1 379 ? 3.63314   -10.72640 -31.18640 1.000 27.68974 ? 379 GLY A N     1 
ATOM   3000 C  CA    . GLY A 1 379 ? 4.22412   -11.42140 -30.05839 1.000 27.10808 ? 379 GLY A CA    1 
ATOM   3001 C  C     . GLY A 1 379 ? 5.21611   -10.57641 -29.29137 1.000 23.82133 ? 379 GLY A C     1 
ATOM   3002 O  O     . GLY A 1 379 ? 5.38309   -10.76041 -28.08137 1.000 24.44025 ? 379 GLY A O     1 
ATOM   3003 N  N     . MET A 1 380 ? 5.88312   -9.64241  -29.97336 1.000 25.83436 ? 380 MET A N     1 
ATOM   3004 C  CA    . MET A 1 380 ? 6.82311   -8.75641  -29.29334 1.000 27.24542 ? 380 MET A CA    1 
ATOM   3005 C  C     . MET A 1 380 ? 6.09310   -7.76841  -28.39235 1.000 26.38061 ? 380 MET A C     1 
ATOM   3006 O  O     . MET A 1 380 ? 6.58209   -7.43042  -27.30834 1.000 25.77729 ? 380 MET A O     1 
ATOM   3007 C  CB    . MET A 1 380 ? 7.68013   -8.01641  -30.32033 1.000 25.57061 ? 380 MET A CB    1 
ATOM   3008 C  CG    . MET A 1 380 ? 8.76012   -7.13441  -29.71531 1.000 19.13429 ? 380 MET A CG    1 
ATOM   3009 S  SD    . MET A 1 380 ? 9.62814   -6.15941  -30.95829 1.000 25.96070 ? 380 MET A SD    1 
ATOM   3010 C  CE    . MET A 1 380 ? 8.29515   -5.13140  -31.57131 1.000 27.64210 ? 380 MET A CE    1 
ATOM   3011 N  N     A GLU A 1 381 ? 4.92711   -7.28641  -28.83037 0.907 26.60435 ? 381 GLU A N     1 
ATOM   3012 N  N     B GLU A 1 381 ? 4.91511   -7.30241  -28.81837 0.093 26.47647 ? 381 GLU A N     1 
ATOM   3013 C  CA    A GLU A 1 381 ? 4.14910   -6.36941  -28.00638 0.907 26.57658 ? 381 GLU A CA    1 
ATOM   3014 C  CA    B GLU A 1 381 ? 4.15610   -6.36341  -27.99838 0.093 26.61112 ? 381 GLU A CA    1 
ATOM   3015 C  C     A GLU A 1 381 ? 3.64108   -7.04941  -26.74139 0.907 25.81552 ? 381 GLU A C     1 
ATOM   3016 C  C     B GLU A 1 381 ? 3.59108   -7.03741  -26.75339 0.093 26.00616 ? 381 GLU A C     1 
ATOM   3017 O  O     A GLU A 1 381 ? 3.51906   -6.39942  -25.69638 0.907 25.64086 ? 381 GLU A O     1 
ATOM   3018 O  O     B GLU A 1 381 ? 3.37406   -6.37142  -25.73439 0.093 25.74888 ? 381 GLU A O     1 
ATOM   3019 C  CB    A GLU A 1 381 ? 2.98311   -5.80540  -28.81639 0.907 26.30462 ? 381 GLU A CB    1 
ATOM   3020 C  CB    B GLU A 1 381 ? 3.03411   -5.73141  -28.82339 0.093 26.88777 ? 381 GLU A CB    1 
ATOM   3021 C  CG    A GLU A 1 381 ? 3.41213   -4.97740  -30.01938 0.907 26.25880 ? 381 GLU A CG    1 
ATOM   3022 C  CG    B GLU A 1 381 ? 1.83611   -6.63740  -29.05441 0.093 27.65262 ? 381 GLU A CG    1 
ATOM   3023 C  CD    A GLU A 1 381 ? 2.36415   -4.94940  -31.11540 0.907 29.66322 ? 381 GLU A CD    1 
ATOM   3024 C  CD    B GLU A 1 381 ? 0.98813   -6.20440  -30.23242 0.093 29.25209 ? 381 GLU A CD    1 
ATOM   3025 O  OE1   A GLU A 1 381 ? 1.34714   -5.66239  -30.98642 0.907 30.91387 ? 381 GLU A OE1   1 
ATOM   3026 O  OE1   B GLU A 1 381 ? 1.43615   -5.32639  -30.99941 0.093 30.13098 ? 381 GLU A OE1   1 
ATOM   3027 O  OE2   A GLU A 1 381 ? 2.55916   -4.21739  -32.10939 0.907 28.96144 ? 381 GLU A OE2   1 
ATOM   3028 O  OE2   B GLU A 1 381 ? -0.12687  -6.74439  -30.39344 0.093 28.65854 ? 381 GLU A OE2   1 
ATOM   3029 N  N     . VAL A 1 382 ? 3.34708   -8.34841  -26.81239 1.000 27.15971 ? 382 VAL A N     1 
ATOM   3030 C  CA    . VAL A 1 382 ? 2.90406   -9.07342  -25.62640 1.000 27.99290 ? 382 VAL A CA    1 
ATOM   3031 C  C     . VAL A 1 382 ? 4.06804   -9.26742  -24.66439 1.000 24.80268 ? 382 VAL A C     1 
ATOM   3032 O  O     . VAL A 1 382 ? 3.91602   -9.12643  -23.44439 1.000 25.76443 ? 382 VAL A O     1 
ATOM   3033 C  CB    . VAL A 1 382 ? 2.26406   -10.41541 -26.02642 1.000 29.19859 ? 382 VAL A CB    1 
ATOM   3034 C  CG1   . VAL A 1 382 ? 1.90004   -11.22542 -24.78943 1.000 22.30175 ? 382 VAL A CG1   1 
ATOM   3035 C  CG2   . VAL A 1 382 ? 1.03607   -10.17841 -26.89044 1.000 27.20949 ? 382 VAL A CG2   1 
ATOM   3036 N  N     . PHE A 1 383 ? 5.25105   -9.58742  -25.19537 1.000 22.19222 ? 383 PHE A N     1 
ATOM   3037 C  CA    . PHE A 1 383 ? 6.43704   -9.66443  -24.35035 1.000 20.65069 ? 383 PHE A CA    1 
ATOM   3038 C  C     . PHE A 1 383 ? 6.82403   -8.29443  -23.81034 1.000 23.37774 ? 383 PHE A C     1 
ATOM   3039 O  O     . PHE A 1 383 ? 7.34501   -8.19643  -22.69433 1.000 24.76361 ? 383 PHE A O     1 
ATOM   3040 C  CB    . PHE A 1 383 ? 7.60805   -10.27243 -25.12434 1.000 24.00699 ? 383 PHE A CB    1 
ATOM   3041 C  CG    . PHE A 1 383 ? 7.60004   -11.77743 -25.16634 1.000 22.53898 ? 383 PHE A CG    1 
ATOM   3042 C  CD1   . PHE A 1 383 ? 6.42404   -12.48842 -24.99736 1.000 20.57483 ? 383 PHE A CD1   1 
ATOM   3043 C  CD2   . PHE A 1 383 ? 8.77805   -12.47943 -25.36233 1.000 15.50175 ? 383 PHE A CD2   1 
ATOM   3044 C  CE1   . PHE A 1 383 ? 6.42104   -13.87142 -25.03537 1.000 23.41095 ? 383 PHE A CE1   1 
ATOM   3045 C  CE2   . PHE A 1 383 ? 8.78204   -13.86143 -25.40033 1.000 20.13147 ? 383 PHE A CE2   1 
ATOM   3046 C  CZ    . PHE A 1 383 ? 7.60304   -14.55743 -25.23535 1.000 19.57098 ? 383 PHE A CZ    1 
ATOM   3047 N  N     A GLU A 1 384 ? 6.58104   -7.23043  -24.57834 0.644 26.47220 ? 384 GLU A N     1 
ATOM   3048 N  N     B GLU A 1 384 ? 6.57604   -7.23243  -24.58134 0.356 26.38237 ? 384 GLU A N     1 
ATOM   3049 C  CA    A GLU A 1 384 ? 6.93304   -5.89243  -24.11533 0.644 26.35690 ? 384 GLU A CA    1 
ATOM   3050 C  CA    B GLU A 1 384 ? 6.92004   -5.88743  -24.13133 0.356 26.36026 ? 384 GLU A CA    1 
ATOM   3051 C  C     A GLU A 1 384 ? 6.12202   -5.49443  -22.88834 0.644 26.65641 ? 384 GLU A C     1 
ATOM   3052 C  C     B GLU A 1 384 ? 6.11302   -5.47943  -22.90534 0.356 26.89633 ? 384 GLU A C     1 
ATOM   3053 O  O     A GLU A 1 384 ? 6.58801   -4.69244  -22.07033 0.644 27.00595 ? 384 GLU A O     1 
ATOM   3054 O  O     B GLU A 1 384 ? 6.56601   -4.64644  -22.11333 0.356 26.56721 ? 384 GLU A O     1 
ATOM   3055 C  CB    A GLU A 1 384 ? 6.73400   -4.88500  -25.24500 0.644 25.84384 ? 384 GLU A CB    1 
ATOM   3056 C  CB    B GLU A 1 384 ? 6.70100   -4.88900  -25.26600 0.356 25.88192 ? 384 GLU A CB    1 
ATOM   3057 C  CG    A GLU A 1 384 ? 7.10400   -3.45500  -24.88500 0.644 24.95936 ? 384 GLU A CG    1 
ATOM   3058 C  CG    B GLU A 1 384 ? 7.98300   -4.26600  -25.79000 0.356 25.59923 ? 384 GLU A CG    1 
ATOM   3059 C  CD    A GLU A 1 384 ? 7.42300   -2.61100  -26.10200 0.644 28.25601 ? 384 GLU A CD    1 
ATOM   3060 C  CD    B GLU A 1 384 ? 8.05200   -4.24500  -27.30300 0.356 25.90234 ? 384 GLU A CD    1 
ATOM   3061 O  OE1   A GLU A 1 384 ? 7.80300   -3.18900  -27.14200 0.644 28.11036 ? 384 GLU A OE1   1 
ATOM   3062 O  OE1   B GLU A 1 384 ? 6.98800   -4.33200  -27.95100 0.356 24.80875 ? 384 GLU A OE1   1 
ATOM   3063 O  OE2   A GLU A 1 384 ? 7.29500   -1.37200  -26.01900 0.644 27.29925 ? 384 GLU A OE2   1 
ATOM   3064 O  OE2   B GLU A 1 384 ? 9.17400   -4.14800  -27.84300 0.356 22.36367 ? 384 GLU A OE2   1 
ATOM   3065 N  N     . GLU A 1 385 ? 4.92402   -6.05543  -22.73036 1.000 26.06484 ? 385 GLU A N     1 
ATOM   3066 C  CA    . GLU A 1 385 ? 4.08200   -5.70443  -21.59237 1.000 26.73067 ? 385 GLU A CA    1 
ATOM   3067 C  C     . GLU A 1 385 ? 4.55098   -6.38644  -20.31137 1.000 26.31795 ? 385 GLU A C     1 
ATOM   3068 O  O     . GLU A 1 385 ? 4.70997   -5.73144  -19.27636 1.000 17.48058 ? 385 GLU A O     1 
ATOM   3069 C  CB    . GLU A 1 385 ? 2.62600   -6.06943  -21.89040 1.000 30.45145 ? 385 GLU A CB    1 
ATOM   3070 C  CG    . GLU A 1 385 ? 1.66799   -5.81343  -20.73841 1.000 28.36220 ? 385 GLU A CG    1 
ATOM   3071 C  CD    . GLU A 1 385 ? 0.25199   -6.26143  -21.04943 1.000 36.96467 ? 385 GLU A CD    1 
ATOM   3072 O  OE1   . GLU A 1 385 ? -0.01799  -6.61942  -22.21544 1.000 30.31585 ? 385 GLU A OE1   1 
ATOM   3073 O  OE2   . GLU A 1 385 ? -0.58902  -6.25743  -20.12645 1.000 33.65238 ? 385 GLU A OE2   1 
ATOM   3074 N  N     . HIS A 1 386 ? 4.78898   -7.69744  -20.36437 1.000 28.63656 ? 386 HIS A N     1 
ATOM   3075 C  CA    . HIS A 1 386 ? 5.00096   -8.48644  -19.15637 1.000 26.38970 ? 386 HIS A CA    1 
ATOM   3076 C  C     . HIS A 1 386 ? 6.46495   -8.70045  -18.79635 1.000 23.33130 ? 386 HIS A C     1 
ATOM   3077 O  O     . HIS A 1 386 ? 6.77693   -8.83345  -17.60834 1.000 24.22215 ? 386 HIS A O     1 
ATOM   3078 C  CB    . HIS A 1 386 ? 4.31796   -9.85244  -19.29139 1.000 27.19041 ? 386 HIS A CB    1 
ATOM   3079 C  CG    . HIS A 1 386 ? 2.82596   -9.77644  -19.38641 1.000 32.54907 ? 386 HIS A CG    1 
ATOM   3080 N  ND1   . HIS A 1 386 ? 2.14898   -9.89143  -20.58142 1.000 28.86720 ? 386 HIS A ND1   1 
ATOM   3081 C  CD2   . HIS A 1 386 ? 1.88095   -9.58844  -18.43542 1.000 24.89786 ? 386 HIS A CD2   1 
ATOM   3082 C  CE1   . HIS A 1 386 ? 0.85097   -9.78243  -20.36144 1.000 28.63161 ? 386 HIS A CE1   1 
ATOM   3083 N  NE2   . HIS A 1 386 ? 0.66096   -9.59644  -19.06744 1.000 21.38928 ? 386 HIS A NE2   1 
ATOM   3084 N  N     . LEU A 1 387 ? 7.36897   -8.74845  -19.77433 1.000 20.79357 ? 387 LEU A N     1 
ATOM   3085 C  CA    . LEU A 1 387 ? 8.77696   -8.99145  -19.47531 1.000 20.69595 ? 387 LEU A CA    1 
ATOM   3086 C  C     . LEU A 1 387 ? 9.34695   -7.86445  -18.62630 1.000 28.24169 ? 387 LEU A C     1 
ATOM   3087 O  O     . LEU A 1 387 ? 9.28296   -6.69245  -19.00930 1.000 25.27579 ? 387 LEU A O     1 
ATOM   3088 C  CB    . LEU A 1 387 ? 9.58398   -9.13045  -20.76630 1.000 21.51541 ? 387 LEU A CB    1 
ATOM   3089 C  CG    . LEU A 1 387 ? 9.55699   -10.47644 -21.49131 1.000 20.42724 ? 387 LEU A CG    1 
ATOM   3090 C  CD1   . LEU A 1 387 ? 10.37201  -10.39944 -22.77229 1.000 14.79703 ? 387 LEU A CD1   1 
ATOM   3091 C  CD2   . LEU A 1 387 ? 10.08698  -11.57745 -20.58930 1.000 25.01943 ? 387 LEU A CD2   1 
ATOM   3092 N  N     . ILE A 1 388 ? 9.90693   -8.22446  -17.46529 1.000 24.26225 ? 388 ILE A N     1 
ATOM   3093 C  CA    . ILE A 1 388 ? 10.59092  -7.24846  -16.61928 1.000 24.50661 ? 388 ILE A CA    1 
ATOM   3094 C  C     . ILE A 1 388 ? 11.97093  -6.89546  -17.14526 1.000 26.05518 ? 388 ILE A C     1 
ATOM   3095 O  O     . ILE A 1 388 ? 12.64992  -6.04547  -16.55524 1.000 26.93021 ? 388 ILE A O     1 
ATOM   3096 C  CB    . ILE A 1 388 ? 10.71990  -7.75747  -15.16928 1.000 22.58595 ? 388 ILE A CB    1 
ATOM   3097 C  CG1   . ILE A 1 388 ? 11.56490  -9.03047  -15.12027 1.000 25.90955 ? 388 ILE A CG1   1 
ATOM   3098 C  CG2   . ILE A 1 388 ? 9.34589   -8.00647  -14.56630 1.000 19.55327 ? 388 ILE A CG2   1 
ATOM   3099 C  CD1   . ILE A 1 388 ? 11.78287  -9.56547  -13.71927 1.000 25.51236 ? 388 ILE A CD1   1 
ATOM   3100 N  N     . ASP A 1 389 ? 12.40995  -7.52846  -18.23425 1.000 22.38346 ? 389 ASP A N     1 
ATOM   3101 C  CA    . ASP A 1 389 ? 13.67396  -7.21546  -18.88823 1.000 24.78966 ? 389 ASP A CA    1 
ATOM   3102 C  C     . ASP A 1 389 ? 13.45398  -6.61145  -20.27123 1.000 27.92012 ? 389 ASP A C     1 
ATOM   3103 O  O     . ASP A 1 389 ? 14.25099  -6.83345  -21.18722 1.000 27.68958 ? 389 ASP A O     1 
ATOM   3104 C  CB    . ASP A 1 389 ? 14.54896  -8.46446  -18.98622 1.000 20.45519 ? 389 ASP A CB    1 
ATOM   3105 C  CG    . ASP A 1 389 ? 13.79696  -9.66246  -19.54324 1.000 24.46323 ? 389 ASP A CG    1 
ATOM   3106 O  OD1   . ASP A 1 389 ? 13.23898  -9.55945  -20.65725 1.000 21.79725 ? 389 ASP A OD1   1 
ATOM   3107 O  OD2   . ASP A 1 389 ? 13.77095  -10.71246 -18.86824 1.000 19.80203 ? 389 ASP A OD2   1 
ATOM   3108 N  N     . GLN A 1 390 ? 12.37198  -5.85045  -20.43125 1.000 20.00501 ? 390 GLN A N     1 
ATOM   3109 C  CA    . GLN A 1 390 ? 11.97700  -5.32345  -21.73125 1.000 22.19455 ? 390 GLN A CA    1 
ATOM   3110 C  C     . GLN A 1 390 ? 13.03701  -4.38845  -22.29923 1.000 21.44970 ? 390 GLN A C     1 
ATOM   3111 O  O     . GLN A 1 390 ? 13.10101  -3.21245  -21.93123 1.000 22.23146 ? 390 GLN A O     1 
ATOM   3112 C  CB    . GLN A 1 390 ? 10.63000  -4.60544  -21.61727 1.000 26.28997 ? 390 GLN A CB    1 
ATOM   3113 C  CG    . GLN A 1 390 ? 10.06302  -4.12544  -22.94028 1.000 25.96014 ? 390 GLN A CG    1 
ATOM   3114 C  CD    . GLN A 1 390 ? 10.46403  -2.70144  -23.27327 1.000 25.29965 ? 390 GLN A CD    1 
ATOM   3115 O  OE1   . GLN A 1 390 ? 10.39302  -1.81044  -22.42626 1.000 22.46065 ? 390 GLN A OE1   1 
ATOM   3116 N  NE2   . GLN A 1 390 ? 10.89605  -2.48143  -24.50926 1.000 28.44894 ? 390 GLN A NE2   1 
ATOM   3117 N  N     . ASP A 1 391 ? 13.87303  -4.90644  -23.19322 1.000 21.19550 ? 391 ASP A N     1 
ATOM   3118 C  CA    . ASP A 1 391 ? 14.88504  -4.11644  -23.88120 1.000 25.04995 ? 391 ASP A CA    1 
ATOM   3119 C  C     . ASP A 1 391 ? 14.45606  -3.93244  -25.32921 1.000 19.62667 ? 391 ASP A C     1 
ATOM   3120 O  O     . ASP A 1 391 ? 14.15107  -4.91044  -26.01622 1.000 26.17767 ? 391 ASP A O     1 
ATOM   3121 C  CB    . ASP A 1 391 ? 16.25804  -4.78845  -23.79918 1.000 20.67746 ? 391 ASP A CB    1 
ATOM   3122 C  CG    . ASP A 1 391 ? 17.37405  -3.90645  -24.32716 1.000 15.74692 ? 391 ASP A CG    1 
ATOM   3123 O  OD1   . ASP A 1 391 ? 17.38607  -3.61044  -25.54016 1.000 22.50889 ? 391 ASP A OD1   1 
ATOM   3124 O  OD2   . ASP A 1 391 ? 18.23903  -3.49945  -23.52415 1.000 15.11867 ? 391 ASP A OD2   1 
ATOM   3125 N  N     . HIS A 1 392 ? 14.44307  -2.67844  -25.78620 1.000 21.18448 ? 392 HIS A N     1 
ATOM   3126 C  CA    . HIS A 1 392 ? 13.88709  -2.36043  -27.09921 1.000 20.94936 ? 392 HIS A CA    1 
ATOM   3127 C  C     . HIS A 1 392 ? 14.61111  -3.10043  -28.21820 1.000 21.53053 ? 392 HIS A C     1 
ATOM   3128 O  O     . HIS A 1 392 ? 13.97500  -3.57100  -29.17300 1.000 22.98936 ? 392 HIS A O     1 
ATOM   3129 C  CB    . HIS A 1 392 ? 13.93900  -0.85200  -27.32300 1.000 24.94844 ? 392 HIS A CB    1 
ATOM   3130 C  CG    . HIS A 1 392 ? 13.58500  -0.42700  -28.71400 1.000 21.61609 ? 392 HIS A CG    1 
ATOM   3131 N  ND1   . HIS A 1 392 ? 12.29100  -0.16200  -29.10600 1.000 27.22495 ? 392 HIS A ND1   1 
ATOM   3132 C  CD2   . HIS A 1 392 ? 14.36000  -0.20600  -29.80300 1.000 25.04750 ? 392 HIS A CD2   1 
ATOM   3133 C  CE1   . HIS A 1 392 ? 12.28200  0.19700   -30.37700 1.000 25.94295 ? 392 HIS A CE1   1 
ATOM   3134 N  NE2   . HIS A 1 392 ? 13.52500  0.17800   -30.82400 1.000 30.72804 ? 392 HIS A NE2   1 
ATOM   3135 N  N     . TYR A 1 393 ? 15.93211  -3.23443  -28.11518 1.000 23.27513 ? 393 TYR A N     1 
ATOM   3136 C  CA    . TYR A 1 393 ? 16.72512  -3.76143  -29.22117 1.000 22.29528 ? 393 TYR A CA    1 
ATOM   3137 C  C     . TYR A 1 393 ? 16.89012  -5.27743  -29.18918 1.000 21.77217 ? 393 TYR A C     1 
ATOM   3138 O  O     . TYR A 1 393 ? 17.03313  -5.89543  -30.25118 1.000 30.60670 ? 393 TYR A O     1 
ATOM   3139 C  CB    . TYR A 1 393 ? 18.10012  -3.08543  -29.23915 1.000 22.72072 ? 393 TYR A CB    1 
ATOM   3140 C  CG    . TYR A 1 393 ? 18.07013  -1.67343  -29.79215 1.000 21.24413 ? 393 TYR A CG    1 
ATOM   3141 C  CD1   . TYR A 1 393 ? 17.35915  -1.37642  -30.94816 1.000 29.36189 ? 393 TYR A CD1   1 
ATOM   3142 C  CD2   . TYR A 1 393 ? 18.74313  -0.63843  -29.15513 1.000 21.71583 ? 393 TYR A CD2   1 
ATOM   3143 C  CE1   . TYR A 1 393 ? 17.32516  -0.09142  -31.45815 1.000 27.31007 ? 393 TYR A CE1   1 
ATOM   3144 C  CE2   . TYR A 1 393 ? 18.71414  0.65157   -29.65813 1.000 26.49022 ? 393 TYR A CE2   1 
ATOM   3145 C  CZ    . TYR A 1 393 ? 18.00315  0.91758   -30.81014 1.000 29.21413 ? 393 TYR A CZ    1 
ATOM   3146 O  OH    . TYR A 1 393 ? 17.96816  2.19658   -31.31613 1.000 30.61278 ? 393 TYR A OH    1 
ATOM   3147 N  N     . LEU A 1 394 ? 16.85210  -5.88943  -28.00218 1.000 20.98006 ? 394 LEU A N     1 
ATOM   3148 C  CA    . LEU A 1 394 ? 16.97209  -7.36743  -27.83518 1.000 22.42810 ? 394 LEU A CA    1 
ATOM   3149 C  C     . LEU A 1 394 ? 15.63110  -8.04643  -28.13521 1.000 23.51532 ? 394 LEU A C     1 
ATOM   3150 O  O     . LEU A 1 394 ? 15.62611  -9.01543  -28.87821 1.000 20.35366 ? 394 LEU A O     1 
ATOM   3151 C  CB    . LEU A 1 394 ? 17.42807  -7.66144  -26.40518 1.000 19.45703 ? 394 LEU A CB    1 
ATOM   3152 C  CG    . LEU A 1 394 ? 18.66507  -6.90044  -25.93316 1.000 19.01144 ? 394 LEU A CG    1 
ATOM   3153 C  CD1   . LEU A 1 394 ? 18.94304  -7.17445  -24.46915 1.000 16.55715 ? 394 LEU A CD1   1 
ATOM   3154 C  CD2   . LEU A 1 394 ? 19.88008  -7.25244  -26.77214 1.000 16.81599 ? 394 LEU A CD2   1 
ATOM   3155 N  N     . ASN A 1 395 ? 14.55009  -7.50943  -27.58122 1.000 25.39285 ? 395 ASN A N     1 
ATOM   3156 C  CA    . ASN A 1 395 ? 13.17309  -7.99243  -27.80224 1.000 20.43129 ? 395 ASN A CA    1 
ATOM   3157 C  C     . ASN A 1 395 ? 12.90811  -8.01542  -29.31025 1.000 24.66954 ? 395 ASN A C     1 
ATOM   3158 O  O     . ASN A 1 395 ? 12.23512  -8.90142  -29.77426 1.000 29.84094 ? 395 ASN A O     1 
ATOM   3159 C  CB    . ASN A 1 395 ? 12.21700  -7.14100  -26.94700 1.000 20.04384 ? 395 ASN A CB    1 
ATOM   3160 C  CG    . ASN A 1 395 ? 11.01300  -7.93400  -26.49200 1.000 22.03056 ? 395 ASN A CG    1 
ATOM   3161 O  OD1   . ASN A 1 395 ? 11.11400  -9.13600  -26.27800 1.000 20.29985 ? 395 ASN A OD1   1 
ATOM   3162 N  ND2   . ASN A 1 395 ? 9.89500   -7.23300  -26.29100 1.000 24.65422 ? 395 ASN A ND2   1 
ATOM   3163 N  N     . ALA A 1 396 ? 13.49513  -7.09642  -30.05224 1.000 22.48161 ? 396 ALA A N     1 
ATOM   3164 C  CA    . ALA A 1 396 ? 13.18915  -7.02241  -31.48524 1.000 22.74452 ? 396 ALA A CA    1 
ATOM   3165 C  C     . ALA A 1 396 ? 14.07816  -7.97641  -32.28123 1.000 23.72274 ? 396 ALA A C     1 
ATOM   3166 O  O     . ALA A 1 396 ? 13.55017  -8.71141  -33.10824 1.000 25.41882 ? 396 ALA A O     1 
ATOM   3167 C  CB    . ALA A 1 396 ? 13.33716  -5.59441  -31.92923 1.000 21.58121 ? 396 ALA A CB    1 
ATOM   3168 N  N     . ALA A 1 397 ? 15.37616  -7.94242  -32.02621 1.000 21.23270 ? 397 ALA A N     1 
ATOM   3169 C  CA    . ALA A 1 397 ? 16.29117  -8.74741  -32.84620 1.000 26.51066 ? 397 ALA A CA    1 
ATOM   3170 C  C     . ALA A 1 397 ? 16.12216  -10.22042 -32.48921 1.000 22.95732 ? 397 ALA A C     1 
ATOM   3171 O  O     . ALA A 1 397 ? 16.42217  -11.05941 -33.33620 1.000 26.85873 ? 397 ALA A O     1 
ATOM   3172 C  CB    . ALA A 1 397 ? 17.70117  -8.25842  -32.68917 1.000 23.28893 ? 397 ALA A CB    1 
ATOM   3173 N  N     . ASN A 1 398 ? 15.62214  -10.49142 -31.29621 1.000 20.51476 ? 398 ASN A N     1 
ATOM   3174 C  CA    . ASN A 1 398 ? 15.38213  -11.88742 -30.95122 1.000 22.22389 ? 398 ASN A CA    1 
ATOM   3175 C  C     . ASN A 1 398 ? 14.05414  -12.39242 -31.50025 1.000 24.04972 ? 398 ASN A C     1 
ATOM   3176 O  O     . ASN A 1 398 ? 13.95114  -13.56641 -31.87125 1.000 22.00561 ? 398 ASN A O     1 
ATOM   3177 C  CB    . ASN A 1 398 ? 15.43011  -12.07543 -29.43522 1.000 23.62179 ? 398 ASN A CB    1 
ATOM   3178 C  CG    . ASN A 1 398 ? 16.84610  -12.19943 -28.90620 1.000 18.06759 ? 398 ASN A CG    1 
ATOM   3179 O  OD1   . ASN A 1 398 ? 17.38510  -13.30143 -28.79820 1.000 15.97726 ? 398 ASN A OD1   1 
ATOM   3180 N  ND2   . ASN A 1 398 ? 17.45510  -11.06943 -28.56919 1.000 24.87274 ? 398 ASN A ND2   1 
ATOM   3181 N  N     . TRP A 1 399 ? 13.03114  -11.53541 -31.55526 1.000 24.99008 ? 399 TRP A N     1 
ATOM   3182 C  CA    . TRP A 1 399 ? 11.77615  -11.94441 -32.17728 1.000 27.47947 ? 399 TRP A CA    1 
ATOM   3183 C  C     . TRP A 1 399 ? 11.91917  -12.07540 -33.68728 1.000 27.25974 ? 399 TRP A C     1 
ATOM   3184 O  O     . TRP A 1 399 ? 11.27318  -12.93540 -34.29629 1.000 25.99785 ? 399 TRP A O     1 
ATOM   3185 C  CB    . TRP A 1 399 ? 10.65815  -10.96441 -31.82429 1.000 26.91461 ? 399 TRP A CB    1 
ATOM   3186 C  CG    . TRP A 1 399 ? 9.92413   -11.34241 -30.57330 1.000 24.78747 ? 399 TRP A CG    1 
ATOM   3187 C  CD1   . TRP A 1 399 ? 10.15811  -10.87842 -29.31230 1.000 23.06884 ? 399 TRP A CD1   1 
ATOM   3188 C  CD2   . TRP A 1 399 ? 8.84312   -12.27441 -30.46332 1.000 23.26955 ? 399 TRP A CD2   1 
ATOM   3189 N  NE1   . TRP A 1 399 ? 9.28509   -11.45942 -28.42431 1.000 23.24738 ? 399 TRP A NE1   1 
ATOM   3190 C  CE2   . TRP A 1 399 ? 8.46810   -12.32141 -29.10633 1.000 23.80934 ? 399 TRP A CE2   1 
ATOM   3191 C  CE3   . TRP A 1 399 ? 8.15314   -13.07341 -31.38134 1.000 25.26376 ? 399 TRP A CE3   1 
ATOM   3192 C  CZ2   . TRP A 1 399 ? 7.43410   -13.13441 -28.64435 1.000 22.86643 ? 399 TRP A CZ2   1 
ATOM   3193 C  CZ3   . TRP A 1 399 ? 7.12713   -13.87940 -30.92136 1.000 22.86478 ? 399 TRP A CZ3   1 
ATOM   3194 C  CH2   . TRP A 1 399 ? 6.77811   -13.90441 -29.56536 1.000 22.40893 ? 399 TRP A CH2   1 
ATOM   3195 N  N     . MET A 1 400 ? 12.75419  -11.23840 -34.30826 1.000 27.88364 ? 400 MET A N     1 
ATOM   3196 C  CA    . MET A 1 400 ? 13.10221  -11.44840 -35.70726 1.000 28.08876 ? 400 MET A CA    1 
ATOM   3197 C  C     . MET A 1 400 ? 13.99621  -12.66740 -35.88925 1.000 25.25742 ? 400 MET A C     1 
ATOM   3198 O  O     . MET A 1 400 ? 14.04822  -13.22740 -36.98925 1.000 32.63157 ? 400 MET A O     1 
ATOM   3199 C  CB    . MET A 1 400 ? 13.78722  -10.20640 -36.28024 1.000 32.41493 ? 400 MET A CB    1 
ATOM   3200 C  CG    . MET A 1 400 ? 12.88322  -8.98740  -36.37825 1.000 27.96577 ? 400 MET A CG    1 
ATOM   3201 S  SD    . MET A 1 400 ? 13.69424  -7.56639  -37.13723 1.000 37.14471 ? 400 MET A SD    1 
ATOM   3202 C  CE    . MET A 1 400 ? 14.99522  -7.23840  -35.95121 1.000 28.61524 ? 400 MET A CE    1 
ATOM   3203 N  N     . TRP A 1 401 ? 14.69919  -13.08540 -34.83424 1.000 26.02406 ? 401 TRP A N     1 
ATOM   3204 C  CA    . TRP A 1 401 ? 15.48319  -14.31441 -34.89523 1.000 28.88204 ? 401 TRP A CA    1 
ATOM   3205 C  C     . TRP A 1 401 ? 14.57519  -15.53740 -34.91225 1.000 26.08533 ? 401 TRP A C     1 
ATOM   3206 O  O     . TRP A 1 401 ? 14.72320  -16.42340 -35.76125 1.000 26.71611 ? 401 TRP A O     1 
ATOM   3207 C  CB    . TRP A 1 401 ? 16.44817  -14.37341 -33.70822 1.000 27.79044 ? 401 TRP A CB    1 
ATOM   3208 C  CG    . TRP A 1 401 ? 17.44717  -15.49641 -33.76420 1.000 29.60274 ? 401 TRP A CG    1 
ATOM   3209 C  CD1   . TRP A 1 401 ? 17.18317  -16.83641 -33.74021 1.000 24.19727 ? 401 TRP A CD1   1 
ATOM   3210 C  CD2   . TRP A 1 401 ? 18.87217  -15.37142 -33.82518 1.000 32.57623 ? 401 TRP A CD2   1 
ATOM   3211 N  NE1   . TRP A 1 401 ? 18.35417  -17.55141 -33.79820 1.000 24.70116 ? 401 TRP A NE1   1 
ATOM   3212 C  CE2   . TRP A 1 401 ? 19.40617  -16.67542 -33.84918 1.000 27.89414 ? 401 TRP A CE2   1 
ATOM   3213 C  CE3   . TRP A 1 401 ? 19.74917  -14.28342 -33.86617 1.000 31.61415 ? 401 TRP A CE3   1 
ATOM   3214 C  CZ2   . TRP A 1 401 ? 20.77517  -16.92042 -33.91516 1.000 30.84145 ? 401 TRP A CZ2   1 
ATOM   3215 C  CZ3   . TRP A 1 401 ? 21.10717  -14.52842 -33.93315 1.000 30.88495 ? 401 TRP A CZ3   1 
ATOM   3216 C  CH2   . TRP A 1 401 ? 21.60717  -15.83642 -33.95514 1.000 28.52385 ? 401 TRP A CH2   1 
ATOM   3217 N  N     . LEU A 1 402 ? 13.62317  -15.60041 -33.97926 1.000 19.41621 ? 402 LEU A N     1 
ATOM   3218 C  CA    . LEU A 1 402 ? 12.75917  -16.76740 -33.85028 1.000 27.42009 ? 402 LEU A CA    1 
ATOM   3219 C  C     . LEU A 1 402 ? 11.69118  -16.84340 -34.93230 1.000 28.81664 ? 402 LEU A C     1 
ATOM   3220 O  O     . LEU A 1 402 ? 11.08519  -17.90540 -35.10831 1.000 27.85226 ? 402 LEU A O     1 
ATOM   3221 C  CB    . LEU A 1 402 ? 12.09215  -16.77741 -32.47229 1.000 32.92321 ? 402 LEU A CB    1 
ATOM   3222 C  CG    . LEU A 1 402 ? 12.80513  -17.55141 -31.35928 1.000 27.29582 ? 402 LEU A CG    1 
ATOM   3223 C  CD1   . LEU A 1 402 ? 12.83913  -19.03741 -31.68529 1.000 25.09703 ? 402 LEU A CD1   1 
ATOM   3224 C  CD2   . LEU A 1 402 ? 14.21213  -17.01942 -31.13126 1.000 25.91347 ? 402 LEU A CD2   1 
ATOM   3225 N  N     . SER A 1 403 ? 11.44220  -15.75340 -35.65330 1.000 35.59134 ? 403 SER A N     1 
ATOM   3226 C  CA    . SER A 1 403 ? 10.46121  -15.74139 -36.73031 1.000 37.14952 ? 403 SER A CA    1 
ATOM   3227 C  C     . SER A 1 403 ? 11.10323  -15.84239 -38.10630 1.000 37.81578 ? 403 SER A C     1 
ATOM   3228 O  O     . SER A 1 403 ? 10.42525  -15.60238 -39.11131 1.000 40.74804 ? 403 SER A O     1 
ATOM   3229 C  CB    . SER A 1 403 ? 9.60222   -14.47839 -36.64732 1.000 39.52682 ? 403 SER A CB    1 
ATOM   3230 O  OG    . SER A 1 403 ? 10.38422  -13.31239 -36.84130 1.000 40.41863 ? 403 SER A OG    1 
ATOM   3231 N  N     . ALA A 1 404 ? 12.38924  -16.19139 -38.17228 1.000 36.85067 ? 404 ALA A N     1 
ATOM   3232 C  CA    . ALA A 1 404 ? 13.14425  -16.28839 -39.42127 1.000 33.48175 ? 404 ALA A CA    1 
ATOM   3233 C  C     . ALA A 1 404 ? 13.12527  -14.98638 -40.21427 1.000 34.22634 ? 404 ALA A C     1 
ATOM   3234 O  O     . ALA A 1 404 ? 13.29829  -14.99538 -41.43727 1.000 30.90284 ? 404 ALA A O     1 
ATOM   3235 C  CB    . ALA A 1 404 ? 12.64027  -17.44438 -40.29329 1.000 30.49849 ? 404 ALA A CB    1 
ATOM   3236 N  N     . SER A 1 405 ? 12.91826  -13.85638 -39.53927 1.000 35.11542 ? 405 SER A N     1 
ATOM   3237 C  CA    . SER A 1 405 ? 12.85827  -12.56938 -40.21726 1.000 32.91130 ? 405 SER A CA    1 
ATOM   3238 C  C     . SER A 1 405 ? 14.23328  -11.94638 -40.40824 1.000 32.26128 ? 405 SER A C     1 
ATOM   3239 O  O     . SER A 1 405 ? 14.45529  -11.24338 -41.40124 1.000 35.53981 ? 405 SER A O     1 
ATOM   3240 C  CB    . SER A 1 405 ? 11.95526  -11.60938 -39.43727 1.000 29.79894 ? 405 SER A CB    1 
ATOM   3241 O  OG    . SER A 1 405 ? 10.64526  -12.13438 -39.31530 1.000 34.95367 ? 405 SER A OG    1 
ATOM   3242 N  N     . ALA A 1 406 ? 15.16226  -12.19739 -39.48823 1.000 24.62062 ? 406 ALA A N     1 
ATOM   3243 C  CA    . ALA A 1 406 ? 16.51027  -11.66239 -39.59321 1.000 30.56343 ? 406 ALA A CA    1 
ATOM   3244 C  C     . ALA A 1 406 ? 17.46125  -12.56640 -38.82319 1.000 35.81239 ? 406 ALA A C     1 
ATOM   3245 O  O     . ALA A 1 406 ? 17.04624  -13.34140 -37.95620 1.000 35.64888 ? 406 ALA A O     1 
ATOM   3246 C  CB    . ALA A 1 406 ? 16.59126  -10.22539 -39.06820 1.000 32.54821 ? 406 ALA A CB    1 
ATOM   3247 N  N     . PHE A 1 407 ? 18.74726  -12.46940 -39.17117 1.000 34.43795 ? 407 PHE A N     1 
ATOM   3248 C  CA    . PHE A 1 407 ? 19.82725  -13.20540 -38.51716 1.000 35.45326 ? 407 PHE A CA    1 
ATOM   3249 C  C     . PHE A 1 407 ? 19.69325  -14.71440 -38.70417 1.000 36.54823 ? 407 PHE A C     1 
ATOM   3250 O  O     . PHE A 1 407 ? 20.63625  -15.37440 -39.15216 1.000 28.41047 ? 407 PHE A O     1 
ATOM   3251 C  CB    . PHE A 1 407 ? 19.89122  -12.86041 -37.02716 1.000 31.87731 ? 407 PHE A CB    1 
ATOM   3252 C  CG    . PHE A 1 407 ? 19.89922  -11.38441 -36.74615 1.000 34.03704 ? 407 PHE A CG    1 
ATOM   3253 C  CD1   . PHE A 1 407 ? 21.01423  -10.61541 -37.03713 1.000 34.55943 ? 407 PHE A CD1   1 
ATOM   3254 C  CD2   . PHE A 1 407 ? 18.79421  -10.76641 -36.18517 1.000 31.03740 ? 407 PHE A CD2   1 
ATOM   3255 C  CE1   . PHE A 1 407 ? 21.02423  -9.25641  -36.77913 1.000 30.30225 ? 407 PHE A CE1   1 
ATOM   3256 C  CE2   . PHE A 1 407 ? 18.79821  -9.40841  -35.92416 1.000 30.28857 ? 407 PHE A CE2   1 
ATOM   3257 C  CZ    . PHE A 1 407 ? 19.91522  -8.65341  -36.22114 1.000 27.77786 ? 407 PHE A CZ    1 
ATOM   3258 N  N     . PHE A 1 408 ? 18.53624  -15.27040 -38.35819 1.000 36.23357 ? 408 PHE A N     1 
ATOM   3259 C  CA    . PHE A 1 408 ? 18.27724  -16.69640 -38.49020 1.000 34.05536 ? 408 PHE A CA    1 
ATOM   3260 C  C     . PHE A 1 408 ? 17.56826  -16.97139 -39.80921 1.000 33.87791 ? 408 PHE A C     1 
ATOM   3261 O  O     . PHE A 1 408 ? 16.69227  -16.20739 -40.22522 1.000 38.01748 ? 408 PHE A O     1 
ATOM   3262 C  CB    . PHE A 1 408 ? 17.43422  -17.20140 -37.31821 1.000 34.83664 ? 408 PHE A CB    1 
ATOM   3263 C  CG    . PHE A 1 408 ? 17.48221  -18.68940 -37.13022 1.000 35.50127 ? 408 PHE A CG    1 
ATOM   3264 C  CD1   . PHE A 1 408 ? 18.65221  -19.31140 -36.73020 1.000 37.97787 ? 408 PHE A CD1   1 
ATOM   3265 C  CD2   . PHE A 1 408 ? 16.35322  -19.46540 -37.33424 1.000 33.35041 ? 408 PHE A CD2   1 
ATOM   3266 C  CE1   . PHE A 1 408 ? 18.70020  -20.68041 -36.55020 1.000 38.60472 ? 408 PHE A CE1   1 
ATOM   3267 C  CE2   . PHE A 1 408 ? 16.39421  -20.83340 -37.15424 1.000 35.33224 ? 408 PHE A CE2   1 
ATOM   3268 C  CZ    . PHE A 1 408 ? 17.56920  -21.44240 -36.76222 1.000 38.44317 ? 408 PHE A CZ    1 
ATOM   3269 N  N     . SER A 1 409 ? 17.95327  -18.06839 -40.46721 1.000 35.88592 ? 409 SER A N     1 
ATOM   3270 C  CA    . SER A 1 409 ? 17.38629  -18.39738 -41.76822 1.000 33.68926 ? 409 SER A CA    1 
ATOM   3271 C  C     . SER A 1 409 ? 17.06829  -19.87938 -41.92323 1.000 33.21391 ? 409 SER A C     1 
ATOM   3272 O  O     . SER A 1 409 ? 16.78930  -20.32038 -43.04623 1.000 34.34680 ? 409 SER A O     1 
ATOM   3273 C  CB    . SER A 1 409 ? 18.33330  -17.95538 -42.89020 1.000 35.83119 ? 409 SER A CB    1 
ATOM   3274 O  OG    . SER A 1 409 ? 19.60730  -18.55639 -42.74418 1.000 39.44890 ? 409 SER A OG    1 
ATOM   3275 N  N     . GLN A 1 410 ? 17.09427  -20.66139 -40.84423 1.000 29.67240 ? 410 GLN A N     1 
ATOM   3276 C  CA    . GLN A 1 410 ? 16.82727  -22.09739 -40.91524 1.000 36.34511 ? 410 GLN A CA    1 
ATOM   3277 C  C     . GLN A 1 410 ? 15.40426  -22.34639 -40.42026 1.000 40.09349 ? 410 GLN A C     1 
ATOM   3278 O  O     . GLN A 1 410 ? 15.16524  -22.72239 -39.27227 1.000 34.53733 ? 410 GLN A O     1 
ATOM   3279 C  CB    . GLN A 1 410 ? 17.86025  -22.87639 -40.10722 1.000 28.91064 ? 410 GLN A CB    1 
ATOM   3280 C  CG    . GLN A 1 410 ? 17.75725  -24.38139 -40.26623 1.000 32.65783 ? 410 GLN A CG    1 
ATOM   3281 C  CD    . GLN A 1 410 ? 17.86227  -24.82139 -41.71323 1.000 39.23410 ? 410 GLN A CD    1 
ATOM   3282 O  OE1   . GLN A 1 410 ? 16.88628  -25.28138 -42.30625 1.000 38.76126 ? 410 GLN A OE1   1 
ATOM   3283 N  NE2   . GLN A 1 410 ? 19.05128  -24.68339 -42.29021 1.000 38.06933 ? 410 GLN A NE2   1 
ATOM   3284 N  N     . TYR A 1 411 ? 14.44427  -22.13338 -41.32027 1.000 40.08818 ? 411 TYR A N     1 
ATOM   3285 C  CA    . TYR A 1 411 ? 13.03527  -22.28838 -40.98330 1.000 35.04509 ? 411 TYR A CA    1 
ATOM   3286 C  C     . TYR A 1 411 ? 12.59726  -23.74338 -40.88031 1.000 31.79581 ? 411 TYR A C     1 
ATOM   3287 O  O     . TYR A 1 411 ? 11.49725  -24.00538 -40.37933 1.000 28.58951 ? 411 TYR A O     1 
ATOM   3288 C  CB    . TYR A 1 411 ? 12.16528  -21.55637 -42.01131 1.000 38.93906 ? 411 TYR A CB    1 
ATOM   3289 C  CG    . TYR A 1 411 ? 12.56631  -21.79637 -43.45030 1.000 36.42061 ? 411 TYR A CG    1 
ATOM   3290 C  CD1   . TYR A 1 411 ? 12.09531  -22.89937 -44.14831 1.000 33.99790 ? 411 TYR A CD1   1 
ATOM   3291 C  CD2   . TYR A 1 411 ? 13.40832  -20.91237 -44.11329 1.000 37.55171 ? 411 TYR A CD2   1 
ATOM   3292 C  CE1   . TYR A 1 411 ? 12.45733  -23.12036 -45.46331 1.000 34.36167 ? 411 TYR A CE1   1 
ATOM   3293 C  CE2   . TYR A 1 411 ? 13.77634  -21.12537 -45.42828 1.000 37.70108 ? 411 TYR A CE2   1 
ATOM   3294 C  CZ    . TYR A 1 411 ? 13.29735  -22.23036 -46.09829 1.000 34.12243 ? 411 TYR A CZ    1 
ATOM   3295 O  OH    . TYR A 1 411 ? 13.65837  -22.44636 -47.40729 1.000 33.92925 ? 411 TYR A OH    1 
ATOM   3296 N  N     . PHE A 1 412 ? 13.41827  -24.69238 -41.33630 1.000 33.96374 ? 412 PHE A N     1 
ATOM   3297 C  CA    . PHE A 1 412 ? 13.07026  -26.10238 -41.19231 1.000 34.04209 ? 412 PHE A CA    1 
ATOM   3298 C  C     . PHE A 1 412 ? 13.17124  -26.57938 -39.74931 1.000 32.75302 ? 412 PHE A C     1 
ATOM   3299 O  O     . PHE A 1 412 ? 12.60523  -27.62638 -39.41532 1.000 27.00467 ? 412 PHE A O     1 
ATOM   3300 C  CB    . PHE A 1 412 ? 13.96228  -26.96438 -42.08630 1.000 32.62140 ? 412 PHE A CB    1 
ATOM   3301 C  CG    . PHE A 1 412 ? 13.54030  -26.98437 -43.52831 1.000 40.31647 ? 412 PHE A CG    1 
ATOM   3302 C  CD1   . PHE A 1 412 ? 12.49130  -27.78837 -43.94532 1.000 38.43563 ? 412 PHE A CD1   1 
ATOM   3303 C  CD2   . PHE A 1 412 ? 14.19531  -26.20637 -44.46829 1.000 39.59257 ? 412 PHE A CD2   1 
ATOM   3304 C  CE1   . PHE A 1 412 ? 12.10032  -27.81236 -45.27033 1.000 30.09620 ? 412 PHE A CE1   1 
ATOM   3305 C  CE2   . PHE A 1 412 ? 13.80933  -26.22736 -45.79630 1.000 31.60475 ? 412 PHE A CE2   1 
ATOM   3306 C  CZ    . PHE A 1 412 ? 12.76034  -27.03136 -46.19632 1.000 38.01134 ? 412 PHE A CZ    1 
ATOM   3307 N  N     . ARG A 1 413 ? 13.87602  -25.84347 -38.89301 1.000 31.65016 ? 413 ARG A N     1 
ATOM   3308 C  CA    . ARG A 1 413 ? 14.01209  -26.20023 -37.48236 1.000 29.32832 ? 413 ARG A CA    1 
ATOM   3309 C  C     . ARG A 1 413 ? 12.79172  -25.67775 -36.73602 1.000 24.04312 ? 413 ARG A C     1 
ATOM   3310 O  O     . ARG A 1 413 ? 12.66870  -24.47753 -36.48319 1.000 27.87205 ? 413 ARG A O     1 
ATOM   3311 C  CB    . ARG A 1 413 ? 15.30290  -25.62863 -36.90741 1.000 25.84130 ? 413 ARG A CB    1 
ATOM   3312 C  CG    . ARG A 1 413 ? 15.56333  -25.99783 -35.45579 1.000 22.87651 ? 413 ARG A CG    1 
ATOM   3313 C  CD    . ARG A 1 413 ? 15.79449  -27.49164 -35.29309 1.000 29.51136 ? 413 ARG A CD    1 
ATOM   3314 N  NE    . ARG A 1 413 ? 16.18853  -27.83611 -33.93219 1.000 26.04165 ? 413 ARG A NE    1 
ATOM   3315 C  CZ    . ARG A 1 413 ? 15.34047  -28.15218 -32.96308 1.000 34.52962 ? 413 ARG A CZ    1 
ATOM   3316 N  NH1   . ARG A 1 413 ? 14.03413  -28.18292 -33.17023 1.000 34.73647 ? 413 ARG A NH1   1 
ATOM   3317 N  NH2   . ARG A 1 413 ? 15.81504  -28.44510 -31.75560 1.000 36.42716 ? 413 ARG A NH2   1 
ATOM   3318 N  N     . VAL A 1 414 ? 11.88119  -26.58039 -36.38233 1.000 22.80774 ? 414 VAL A N     1 
ATOM   3319 C  CA    . VAL A 1 414 ? 10.65018  -26.23439 -35.68235 1.000 30.46430 ? 414 VAL A CA    1 
ATOM   3320 C  C     . VAL A 1 414 ? 10.66216  -26.93440 -34.33135 1.000 28.35788 ? 414 VAL A C     1 
ATOM   3321 O  O     . VAL A 1 414 ? 10.76115  -28.16640 -34.26535 1.000 31.49545 ? 414 VAL A O     1 
ATOM   3322 C  CB    . VAL A 1 414 ? 9.40219   -26.62239 -36.49137 1.000 30.00770 ? 414 VAL A CB    1 
ATOM   3323 C  CG1   . VAL A 1 414 ? 8.13918   -26.27739 -35.71839 1.000 31.64826 ? 414 VAL A CG1   1 
ATOM   3324 C  CG2   . VAL A 1 414 ? 9.41121   -25.92338 -37.84136 1.000 26.95848 ? 414 VAL A CG2   1 
ATOM   3325 N  N     . TYR A 1 415 ? 10.56514  -26.15140 -33.26035 1.000 31.10337 ? 415 TYR A N     1 
ATOM   3326 C  CA    . TYR A 1 415 ? 10.54412  -26.70441 -31.91235 1.000 32.48406 ? 415 TYR A CA    1 
ATOM   3327 C  C     . TYR A 1 415 ? 9.21112   -27.39641 -31.65637 1.000 31.33934 ? 415 TYR A C     1 
ATOM   3328 O  O     . TYR A 1 415 ? 8.15012   -26.77040 -31.75339 1.000 35.06343 ? 415 TYR A O     1 
ATOM   3329 C  CB    . TYR A 1 415 ? 10.78311  -25.60041 -30.88734 1.000 35.09384 ? 415 TYR A CB    1 
ATOM   3330 C  CG    . TYR A 1 415 ? 12.18311  -25.02741 -30.91432 1.000 33.46580 ? 415 TYR A CG    1 
ATOM   3331 C  CD1   . TYR A 1 415 ? 13.29011  -25.85842 -31.01131 1.000 33.61119 ? 415 TYR A CD1   1 
ATOM   3332 C  CD2   . TYR A 1 415 ? 12.39611  -23.65641 -30.85031 1.000 26.36310 ? 415 TYR A CD2   1 
ATOM   3333 C  CE1   . TYR A 1 415 ? 14.57211  -25.34142 -31.03828 1.000 36.10737 ? 415 TYR A CE1   1 
ATOM   3334 C  CE2   . TYR A 1 415 ? 13.67411  -23.12942 -30.87729 1.000 24.68113 ? 415 TYR A CE2   1 
ATOM   3335 C  CZ    . TYR A 1 415 ? 14.75811  -23.97742 -30.97128 1.000 30.41159 ? 415 TYR A CZ    1 
ATOM   3336 O  OH    . TYR A 1 415 ? 16.03311  -23.46142 -30.99925 1.000 27.79309 ? 415 TYR A OH    1 
ATOM   3337 N  N     . SER A 1 416 ? 9.26311   -28.68241 -31.33338 1.000 25.99017 ? 416 SER A N     1 
ATOM   3338 C  CA    . SER A 1 416 ? 8.04410   -29.42141 -31.02640 1.000 29.66042 ? 416 SER A CA    1 
ATOM   3339 C  C     . SER A 1 416 ? 7.53308   -29.01241 -29.64940 1.000 29.18837 ? 416 SER A C     1 
ATOM   3340 O  O     . SER A 1 416 ? 8.28007   -29.09342 -28.66839 1.000 28.81098 ? 416 SER A O     1 
ATOM   3341 C  CB    . SER A 1 416 ? 8.30510   -30.92541 -31.07240 1.000 35.13224 ? 416 SER A CB    1 
ATOM   3342 O  OG    . SER A 1 416 ? 7.11410   -31.65941 -30.84242 1.000 36.36050 ? 416 SER A OG    1 
ATOM   3343 N  N     . PRO A 1 417 ? 6.27408   -28.57741 -29.53042 1.000 26.25752 ? 417 PRO A N     1 
ATOM   3344 C  CA    . PRO A 1 417 ? 5.77206   -28.11341 -28.22843 1.000 29.55556 ? 417 PRO A CA    1 
ATOM   3345 C  C     . PRO A 1 417 ? 5.50404   -29.24442 -27.24744 1.000 29.45001 ? 417 PRO A C     1 
ATOM   3346 O  O     . PRO A 1 417 ? 4.95703   -29.01642 -26.16444 1.000 19.60981 ? 417 PRO A O     1 
ATOM   3347 C  CB    . PRO A 1 417 ? 4.47907   -27.37941 -28.59945 1.000 26.05434 ? 417 PRO A CB    1 
ATOM   3348 C  CG    . PRO A 1 417 ? 4.02109   -28.05340 -29.84845 1.000 20.65815 ? 417 PRO A CG    1 
ATOM   3349 C  CD    . PRO A 1 417 ? 5.27210   -28.42640 -30.59944 1.000 29.03357 ? 417 PRO A CD    1 
ATOM   3350 N  N     . VAL A 1 418 ? 5.88705   -30.46941 -27.61443 1.000 33.81807 ? 418 VAL A N     1 
ATOM   3351 C  CA    . VAL A 1 418 ? 5.68103   -31.64242 -26.77944 1.000 30.78089 ? 418 VAL A CA    1 
ATOM   3352 C  C     . VAL A 1 418 ? 6.99703   -32.30442 -26.39442 1.000 35.49001 ? 418 VAL A C     1 
ATOM   3353 O  O     . VAL A 1 418 ? 7.19701   -32.67043 -25.23042 1.000 34.94543 ? 418 VAL A O     1 
ATOM   3354 C  CB    . VAL A 1 418 ? 4.74904   -32.65841 -27.47346 1.000 31.08095 ? 418 VAL A CB    1 
ATOM   3355 C  CG1   . VAL A 1 418 ? 4.55303   -33.88542 -26.59947 1.000 35.18713 ? 418 VAL A CG1   1 
ATOM   3356 C  CG2   . VAL A 1 418 ? 3.41105   -32.01241 -27.80848 1.000 31.66537 ? 418 VAL A CG2   1 
ATOM   3357 N  N     . VAL A 1 419 ? 7.91404   -32.45842 -27.35141 1.000 36.84280 ? 419 VAL A N     1 
ATOM   3358 C  CA    . VAL A 1 419 ? 9.15404   -33.18042 -27.08639 1.000 32.11254 ? 419 VAL A CA    1 
ATOM   3359 C  C     . VAL A 1 419 ? 10.20103  -32.27743 -26.43938 1.000 36.45020 ? 419 VAL A C     1 
ATOM   3360 O  O     . VAL A 1 419 ? 11.05601  -32.75843 -25.68536 1.000 38.21993 ? 419 VAL A O     1 
ATOM   3361 C  CB    . VAL A 1 419 ? 9.68205   -33.80742 -28.38939 1.000 34.52815 ? 419 VAL A CB    1 
ATOM   3362 C  CG1   . VAL A 1 419 ? 10.87105  -34.71742 -28.11237 1.000 39.66081 ? 419 VAL A CG1   1 
ATOM   3363 C  CG2   . VAL A 1 419 ? 8.57306   -34.57041 -29.09741 1.000 36.81748 ? 419 VAL A CG2   1 
ATOM   3364 N  N     . PHE A 1 420 ? 10.15203  -30.96943 -26.70637 1.000 35.24317 ? 420 PHE A N     1 
ATOM   3365 C  CA    . PHE A 1 420 ? 11.18903  -30.06643 -26.21135 1.000 33.07580 ? 420 PHE A CA    1 
ATOM   3366 C  C     . PHE A 1 420 ? 11.22700  -30.05143 -24.68635 1.000 27.85586 ? 420 PHE A C     1 
ATOM   3367 O  O     . PHE A 1 420 ? 12.28699  -30.23844 -24.07834 1.000 27.51234 ? 420 PHE A O     1 
ATOM   3368 C  CB    . PHE A 1 420 ? 10.96104  -28.65743 -26.76135 1.000 27.33963 ? 420 PHE A CB    1 
ATOM   3369 C  CG    . PHE A 1 420 ? 12.13604  -27.73643 -26.58233 1.000 29.56552 ? 420 PHE A CG    1 
ATOM   3370 C  CD1   . PHE A 1 420 ? 12.29602  -27.00743 -25.41332 1.000 24.86835 ? 420 PHE A CD1   1 
ATOM   3371 C  CD2   . PHE A 1 420 ? 13.08005  -27.59543 -27.58531 1.000 30.07756 ? 420 PHE A CD2   1 
ATOM   3372 C  CE1   . PHE A 1 420 ? 13.37502  -26.15944 -25.24830 1.000 21.04809 ? 420 PHE A CE1   1 
ATOM   3373 C  CE2   . PHE A 1 420 ? 14.16205  -26.74843 -27.42630 1.000 26.65905 ? 420 PHE A CE2   1 
ATOM   3374 C  CZ    . PHE A 1 420 ? 14.30904  -26.03043 -26.25729 1.000 20.54493 ? 420 PHE A CZ    1 
ATOM   3375 N  N     . GLY A 1 421 ? 10.07700  -29.82643 -24.04937 1.000 26.59058 ? 421 GLY A N     1 
ATOM   3376 C  CA    . GLY A 1 421 ? 10.03697  -29.81544 -22.59837 1.000 17.67416 ? 421 GLY A CA    1 
ATOM   3377 C  C     . GLY A 1 421 ? 10.24196  -31.17444 -21.96437 1.000 19.79063 ? 421 GLY A C     1 
ATOM   3378 O  O     . GLY A 1 421 ? 10.63294  -31.24745 -20.79436 1.000 22.29573 ? 421 GLY A O     1 
ATOM   3379 N  N     . LYS A 1 422 ? 9.99697   -32.25144 -22.71138 1.000 23.26519 ? 422 LYS A N     1 
ATOM   3380 C  CA    . LYS A 1 422 ? 10.09896  -33.59644 -22.16038 1.000 25.82214 ? 422 LYS A CA    1 
ATOM   3381 C  C     . LYS A 1 422 ? 11.53496  -34.10644 -22.11036 1.000 28.53103 ? 422 LYS A C     1 
ATOM   3382 O  O     . LYS A 1 422 ? 11.83494  -34.99245 -21.30136 1.000 16.38602 ? 422 LYS A O     1 
ATOM   3383 C  CB    . LYS A 1 422 ? 9.22397   -34.55644 -22.97340 1.000 25.42840 ? 422 LYS A CB    1 
ATOM   3384 C  CG    . LYS A 1 422 ? 9.04596   -35.93644 -22.35641 1.000 28.07834 ? 422 LYS A CG    1 
ATOM   3385 C  CD    . LYS A 1 422 ? 7.74696   -36.58644 -22.81443 1.000 18.97821 ? 422 LYS A CD    1 
ATOM   3386 C  CE    . LYS A 1 422 ? 7.61399   -36.56343 -24.32843 1.000 29.17171 ? 422 LYS A CE    1 
ATOM   3387 N  NZ    . LYS A 1 422 ? 8.74100   -37.26743 -25.00242 1.000 27.59896 ? 422 LYS A NZ    1 
ATOM   3388 N  N     . LYS A 1 423 ? 12.42797  -33.57044 -22.94235 1.000 31.24867 ? 423 LYS A N     1 
ATOM   3389 C  CA    . LYS A 1 423 ? 13.82197  -33.99245 -22.91133 1.000 23.50249 ? 423 LYS A CA    1 
ATOM   3390 C  C     . LYS A 1 423 ? 14.58395  -33.41445 -21.72531 1.000 24.76120 ? 423 LYS A C     1 
ATOM   3391 O  O     . LYS A 1 423 ? 15.67695  -33.90045 -21.41530 1.000 29.48591 ? 423 LYS A O     1 
ATOM   3392 C  CB    . LYS A 1 423 ? 14.51899  -33.61344 -24.22231 1.000 24.61641 ? 423 LYS A CB    1 
ATOM   3393 C  CG    . LYS A 1 423 ? 15.23799  -32.27344 -24.20930 0.000 25.41110 ? 423 LYS A CG    1 
ATOM   3394 C  CD    . LYS A 1 423 ? 14.85101  -31.41644 -25.40730 0.000 27.35586 ? 423 LYS A CD    1 
ATOM   3395 C  CE    . LYS A 1 423 ? 14.79303  -32.22343 -26.69630 0.000 31.10722 ? 423 LYS A CE    1 
ATOM   3396 N  NZ    . LYS A 1 423 ? 16.11604  -32.78543 -27.07729 0.000 31.36491 ? 423 LYS A NZ    1 
ATOM   3397 N  N     . TYR A 1 424 ? 14.03494  -32.40245 -21.05732 1.000 22.61756 ? 424 TYR A N     1 
ATOM   3398 C  CA    . TYR A 1 424 ? 14.61793  -31.83546 -19.84631 1.000 27.44500 ? 424 TYR A CA    1 
ATOM   3399 C  C     . TYR A 1 424 ? 13.87491  -32.23246 -18.58132 1.000 25.54547 ? 424 TYR A C     1 
ATOM   3400 O  O     . TYR A 1 424 ? 14.50689  -32.49847 -17.55731 1.000 25.48257 ? 424 TYR A O     1 
ATOM   3401 C  CB    . TYR A 1 424 ? 14.65193  -30.30446 -19.93430 1.000 23.02298 ? 424 TYR A CB    1 
ATOM   3402 C  CG    . TYR A 1 424 ? 15.52195  -29.74346 -21.03628 1.000 20.69136 ? 424 TYR A CG    1 
ATOM   3403 C  CD1   . TYR A 1 424 ? 16.89895  -29.65646 -20.88526 1.000 24.73656 ? 424 TYR A CD1   1 
ATOM   3404 C  CD2   . TYR A 1 424 ? 14.96297  -29.27745 -22.21929 1.000 22.13020 ? 424 TYR A CD2   1 
ATOM   3405 C  CE1   . TYR A 1 424 ? 17.69696  -29.13546 -21.88525 1.000 20.90994 ? 424 TYR A CE1   1 
ATOM   3406 C  CE2   . TYR A 1 424 ? 15.75198  -28.75445 -23.22528 1.000 18.11005 ? 424 TYR A CE2   1 
ATOM   3407 C  CZ    . TYR A 1 424 ? 17.11798  -28.68545 -23.05226 1.000 14.16663 ? 424 TYR A CZ    1 
ATOM   3408 O  OH    . TYR A 1 424 ? 17.90800  -28.16445 -24.05124 1.000 14.34445 ? 424 TYR A OH    1 
ATOM   3409 N  N     . ASP A 1 425 ? 12.54391  -32.27746 -18.62734 1.000 24.26774 ? 425 ASP A N     1 
ATOM   3410 C  CA    . ASP A 1 425 ? 11.72389  -32.55646 -17.45035 1.000 28.19640 ? 425 ASP A CA    1 
ATOM   3411 C  C     . ASP A 1 425 ? 10.63689  -33.54746 -17.83937 1.000 29.98673 ? 425 ASP A C     1 
ATOM   3412 O  O     . ASP A 1 425 ? 9.52790   -33.15645 -18.22839 1.000 29.85520 ? 425 ASP A O     1 
ATOM   3413 C  CB    . ASP A 1 425 ? 11.11788  -31.27146 -16.88336 1.000 24.92450 ? 425 ASP A CB    1 
ATOM   3414 C  CG    . ASP A 1 425 ? 10.60586  -31.43747 -15.46537 1.000 30.12028 ? 425 ASP A CG    1 
ATOM   3415 O  OD1   . ASP A 1 425 ? 10.38385  -32.58847 -15.03437 1.000 35.49671 ? 425 ASP A OD1   1 
ATOM   3416 O  OD2   . ASP A 1 425 ? 10.42185  -30.40947 -14.78037 1.000 27.42915 ? 425 ASP A OD2   1 
ATOM   3417 N  N     . PRO A 1 426 ? 10.91989  -34.84946 -17.74937 1.000 30.54197 ? 426 PRO A N     1 
ATOM   3418 C  CA    . PRO A 1 426 ? 9.89589   -35.83946 -18.11639 1.000 31.80659 ? 426 PRO A CA    1 
ATOM   3419 C  C     . PRO A 1 426 ? 8.75388   -35.92546 -17.11941 1.000 32.36529 ? 426 PRO A C     1 
ATOM   3420 O  O     . PRO A 1 426 ? 7.62788   -36.25045 -17.51643 1.000 31.09994 ? 426 PRO A O     1 
ATOM   3421 C  CB    . PRO A 1 426 ? 10.68889  -37.15246 -18.18539 1.000 32.12631 ? 426 PRO A CB    1 
ATOM   3422 C  CG    . PRO A 1 426 ? 11.84188  -36.93746 -17.26437 1.000 29.37197 ? 426 PRO A CG    1 
ATOM   3423 C  CD    . PRO A 1 426 ? 12.19888  -35.48046 -17.37536 1.000 26.03445 ? 426 PRO A CD    1 
ATOM   3424 N  N     . GLU A 1 427 ? 9.00286   -35.64646 -15.83641 1.000 32.74499 ? 427 GLU A N     1 
ATOM   3425 C  CA    . GLU A 1 427 ? 7.92584   -35.69246 -14.85242 1.000 29.29061 ? 427 GLU A CA    1 
ATOM   3426 C  C     . GLU A 1 427 ? 6.99485   -34.49446 -14.97643 1.000 33.57173 ? 427 GLU A C     1 
ATOM   3427 O  O     . GLU A 1 427 ? 5.82384   -34.57946 -14.59045 1.000 28.96839 ? 427 GLU A O     1 
ATOM   3428 C  CB    . GLU A 1 427 ? 8.50182   -35.77147 -13.43941 1.000 27.82073 ? 427 GLU A CB    1 
ATOM   3429 C  CG    . GLU A 1 427 ? 8.74881   -37.18847 -12.95541 1.000 27.52787 ? 427 GLU A CG    1 
ATOM   3430 C  CD    . GLU A 1 427 ? 7.46381   -37.98047 -12.80744 0.916 34.32826 ? 427 GLU A CD    1 
ATOM   3431 O  OE1   . GLU A 1 427 ? 6.43680   -37.38247 -12.42245 0.000 31.69843 ? 427 GLU A OE1   1 
ATOM   3432 O  OE2   . GLU A 1 427 ? 7.47681   -39.19847 -13.08344 0.000 31.85369 ? 427 GLU A OE2   1 
ATOM   3433 N  N     . GLY A 1 428 ? 7.48986   -33.37946 -15.50742 1.000 36.20783 ? 428 GLY A N     1 
ATOM   3434 C  CA    . GLY A 1 428 ? 6.66786   -32.19746 -15.67743 1.000 27.76300 ? 428 GLY A CA    1 
ATOM   3435 C  C     . GLY A 1 428 ? 6.60085   -31.33046 -14.43943 1.000 27.81355 ? 428 GLY A C     1 
ATOM   3436 O  O     . GLY A 1 428 ? 5.56184   -30.72746 -14.15444 1.000 29.11366 ? 428 GLY A O     1 
ATOM   3437 N  N     . ARG A 1 429 ? 7.70111   -31.25379 -13.68459 1.000 32.28594 ? 429 ARG A N     1 
ATOM   3438 C  CA    . ARG A 1 429 ? 7.72993   -30.41235 -12.49260 1.000 30.55080 ? 429 ARG A CA    1 
ATOM   3439 C  C     . ARG A 1 429 ? 7.50276   -28.94915 -12.84603 1.000 27.54844 ? 429 ARG A C     1 
ATOM   3440 O  O     . ARG A 1 429 ? 6.85109   -28.21524 -12.09374 1.000 22.59510 ? 429 ARG A O     1 
ATOM   3441 C  CB    . ARG A 1 429 ? 9.06026   -30.58438 -11.75927 1.000 31.22848 ? 429 ARG A CB    1 
ATOM   3442 C  CG    . ARG A 1 429 ? 9.28137   -31.97106 -11.17822 1.000 36.98992 ? 429 ARG A CG    1 
ATOM   3443 C  CD    . ARG A 1 429 ? 10.65491  -32.08219 -10.53600 0.000 36.29432 ? 429 ARG A CD    1 
ATOM   3444 N  NE    . ARG A 1 429 ? 10.84273  -33.35897 -9.85767  0.000 37.61185 ? 429 ARG A NE    1 
ATOM   3445 C  CZ    . ARG A 1 429 ? 10.61147  -33.56245 -8.56793  0.000 38.28767 ? 429 ARG A CZ    1 
ATOM   3446 N  NH1   . ARG A 1 429 ? 10.18267  -32.58943 -7.78065  0.000 38.36060 ? 429 ARG A NH1   1 
ATOM   3447 N  NH2   . ARG A 1 429 ? 10.81717  -34.77205 -8.05471  0.000 38.74554 ? 429 ARG A NH2   1 
ATOM   3448 N  N     . PHE A 1 430 ? 8.03284   -28.50647 -13.98939 1.000 31.09066 ? 430 PHE A N     1 
ATOM   3449 C  CA    . PHE A 1 430 ? 7.80985   -27.13047 -14.41839 1.000 25.57013 ? 430 PHE A CA    1 
ATOM   3450 C  C     . PHE A 1 430 ? 6.34286   -26.87546 -14.74141 1.000 23.61299 ? 430 PHE A C     1 
ATOM   3451 O  O     . PHE A 1 430 ? 5.83886   -25.77246 -14.49842 1.000 23.67749 ? 430 PHE A O     1 
ATOM   3452 C  CB    . PHE A 1 430 ? 8.68987   -26.81746 -15.63138 1.000 17.50484 ? 430 PHE A CB    1 
ATOM   3453 C  CG    . PHE A 1 430 ? 8.51688   -25.42446 -16.17138 1.000 25.13694 ? 430 PHE A CG    1 
ATOM   3454 C  CD1   . PHE A 1 430 ? 9.24488   -24.36846 -15.64936 1.000 25.65270 ? 430 PHE A CD1   1 
ATOM   3455 C  CD2   . PHE A 1 430 ? 7.63790   -25.17345 -17.21439 1.000 26.84802 ? 430 PHE A CD2   1 
ATOM   3456 C  CE1   . PHE A 1 430 ? 9.09289   -23.08746 -16.14936 1.000 20.57650 ? 430 PHE A CE1   1 
ATOM   3457 C  CE2   . PHE A 1 430 ? 7.48091   -23.89545 -17.71739 1.000 23.92216 ? 430 PHE A CE2   1 
ATOM   3458 C  CZ    . PHE A 1 430 ? 8.20990   -22.85146 -17.18337 1.000 19.09746 ? 430 PHE A CZ    1 
ATOM   3459 N  N     . ILE A 1 431 ? 5.64586   -27.87646 -15.27643 1.000 26.83895 ? 431 ILE A N     1 
ATOM   3460 C  CA    . ILE A 1 431 ? 4.24387   -27.69845 -15.64145 1.000 23.57768 ? 431 ILE A CA    1 
ATOM   3461 C  C     . ILE A 1 431 ? 3.34985   -27.75846 -14.40846 1.000 26.75235 ? 431 ILE A C     1 
ATOM   3462 O  O     . ILE A 1 431 ? 2.38885   -26.99046 -14.28848 1.000 23.18935 ? 431 ILE A O     1 
ATOM   3463 C  CB    . ILE A 1 431 ? 3.83488   -28.74245 -16.69646 1.000 23.20968 ? 431 ILE A CB    1 
ATOM   3464 C  CG1   . ILE A 1 431 ? 4.62390   -28.52745 -17.98945 1.000 23.27469 ? 431 ILE A CG1   1 
ATOM   3465 C  CG2   . ILE A 1 431 ? 2.33889   -28.67745 -16.96848 1.000 28.93661 ? 431 ILE A CG2   1 
ATOM   3466 C  CD1   . ILE A 1 431 ? 4.26792   -29.50144 -19.08846 1.000 22.13008 ? 431 ILE A CD1   1 
ATOM   3467 N  N     . ARG A 1 432 ? 3.65131   -28.66117 -13.47148 1.000 16.23701 ? 432 ARG A N     1 
ATOM   3468 C  CA    . ARG A 1 432 ? 2.83904   -28.78199 -12.26646 1.000 27.34030 ? 432 ARG A CA    1 
ATOM   3469 C  C     . ARG A 1 432 ? 2.93022   -27.54957 -11.37633 1.000 23.53471 ? 432 ARG A C     1 
ATOM   3470 O  O     . ARG A 1 432 ? 2.02136   -27.31437 -10.57294 1.000 30.10437 ? 432 ARG A O     1 
ATOM   3471 C  CB    . ARG A 1 432 ? 3.25101   -30.02394 -11.47394 1.000 30.22251 ? 432 ARG A CB    1 
ATOM   3472 C  CG    . ARG A 1 432 ? 3.10909   -31.32801 -12.24161 1.000 35.04046 ? 432 ARG A CG    1 
ATOM   3473 C  CD    . ARG A 1 432 ? 3.59584   -32.51062 -11.41944 1.000 32.68183 ? 432 ARG A CD    1 
ATOM   3474 N  NE    . ARG A 1 432 ? 3.78177   -33.70322 -12.23754 1.000 40.33951 ? 432 ARG A NE    1 
ATOM   3475 C  CZ    . ARG A 1 432 ? 2.84548   -34.61498 -12.46160 1.000 34.74891 ? 432 ARG A CZ    1 
ATOM   3476 N  NH1   . ARG A 1 432 ? 1.63461   -34.50593 -11.93969 1.000 33.24640 ? 432 ARG A NH1   1 
ATOM   3477 N  NH2   . ARG A 1 432 ? 3.13084   -35.66184 -13.23056 1.000 35.30972 ? 432 ARG A NH2   1 
ATOM   3478 N  N     . LYS A 1 433 ? 3.99781   -26.75847 -11.50145 1.000 20.49187 ? 433 LYS A N     1 
ATOM   3479 C  CA    . LYS A 1 433 ? 4.14880   -25.57247 -10.66344 1.000 24.09371 ? 433 LYS A CA    1 
ATOM   3480 C  C     . LYS A 1 433 ? 3.28681   -24.41947 -11.16445 1.000 23.65037 ? 433 LYS A C     1 
ATOM   3481 O  O     . LYS A 1 433 ? 2.48780   -23.85747 -10.40746 1.000 29.48215 ? 433 LYS A O     1 
ATOM   3482 C  CB    . LYS A 1 433 ? 5.61880   -25.15247 -10.60242 1.000 26.64139 ? 433 LYS A CB    1 
ATOM   3483 C  CG    . LYS A 1 433 ? 5.85579   -23.83348 -9.87941  1.000 20.74829 ? 433 LYS A CG    1 
ATOM   3484 C  CD    . LYS A 1 433 ? 5.35477   -23.89248 -8.44442  1.000 24.76331 ? 433 LYS A CD    1 
ATOM   3485 C  CE    . LYS A 1 433 ? 5.36976   -22.51748 -7.79141  1.000 21.50040 ? 433 LYS A CE    1 
ATOM   3486 N  NZ    . LYS A 1 433 ? 6.73976   -21.94349 -7.70939  1.000 23.85310 ? 433 LYS A NZ    1 
ATOM   3487 N  N     . PHE A 1 434 ? 3.43383   -24.05346 -12.43745 1.000 17.87470 ? 434 PHE A N     1 
ATOM   3488 C  CA    . PHE A 1 434 ? 2.71984   -22.91046 -12.99046 1.000 21.56524 ? 434 PHE A CA    1 
ATOM   3489 C  C     . PHE A 1 434 ? 1.31985   -23.25546 -13.47748 1.000 20.08263 ? 434 PHE A C     1 
ATOM   3490 O  O     . PHE A 1 434 ? 0.49785   -22.34745 -13.64849 1.000 22.90501 ? 434 PHE A O     1 
ATOM   3491 C  CB    . PHE A 1 434 ? 3.52586   -22.29146 -14.13744 1.000 19.12614 ? 434 PHE A CB    1 
ATOM   3492 C  CG    . PHE A 1 434 ? 4.88185   -21.80046 -13.72242 1.000 23.15037 ? 434 PHE A CG    1 
ATOM   3493 C  CD1   . PHE A 1 434 ? 5.04985   -20.51246 -13.24041 1.000 23.14238 ? 434 PHE A CD1   1 
ATOM   3494 C  CD2   . PHE A 1 434 ? 5.98885   -22.62946 -13.80341 1.000 24.02254 ? 434 PHE A CD2   1 
ATOM   3495 C  CE1   . PHE A 1 434 ? 6.29684   -20.06047 -12.85239 1.000 26.57052 ? 434 PHE A CE1   1 
ATOM   3496 C  CE2   . PHE A 1 434 ? 7.23785   -22.18347 -13.41638 1.000 25.56222 ? 434 PHE A CE2   1 
ATOM   3497 C  CZ    . PHE A 1 434 ? 7.39284   -20.89647 -12.94138 1.000 22.83947 ? 434 PHE A CZ    1 
ATOM   3498 N  N     . LEU A 1 435 ? 1.02785   -24.53746 -13.70449 1.000 25.37199 ? 435 LEU A N     1 
ATOM   3499 C  CA    . LEU A 1 435 ? -0.30015  -25.00245 -14.09851 1.000 23.76167 ? 435 LEU A CA    1 
ATOM   3500 C  C     . LEU A 1 435 ? -0.76317  -26.02145 -13.06352 1.000 25.82107 ? 435 LEU A C     1 
ATOM   3501 O  O     . LEU A 1 435 ? -0.67116  -27.23845 -13.28952 1.000 26.51339 ? 435 LEU A O     1 
ATOM   3502 C  CB    . LEU A 1 435 ? -0.29113  -25.59645 -15.50551 1.000 19.90014 ? 435 LEU A CB    1 
ATOM   3503 C  CG    . LEU A 1 435 ? 0.05989   -24.62244 -16.63150 1.000 26.02346 ? 435 LEU A CG    1 
ATOM   3504 C  CD1   . LEU A 1 435 ? 0.06891   -25.32944 -17.97751 1.000 24.11194 ? 435 LEU A CD1   1 
ATOM   3505 C  CD2   . LEU A 1 435 ? -0.91011  -23.44944 -16.64151 1.000 15.48049 ? 435 LEU A CD2   1 
ATOM   3506 N  N     . PRO A 1 436 ? -1.26718  -25.56246 -11.91453 1.000 23.56999 ? 436 PRO A N     1 
ATOM   3507 C  CA    . PRO A 1 436 ? -1.67020  -26.50146 -10.85554 1.000 27.20511 ? 436 PRO A CA    1 
ATOM   3508 C  C     . PRO A 1 436 ? -2.89520  -27.33346 -11.20056 1.000 29.38187 ? 436 PRO A C     1 
ATOM   3509 O  O     . PRO A 1 436 ? -3.22921  -28.24646 -10.43357 1.000 27.34359 ? 436 PRO A O     1 
ATOM   3510 C  CB    . PRO A 1 436 ? -1.94422  -25.58346 -9.65854  1.000 30.36195 ? 436 PRO A CB    1 
ATOM   3511 C  CG    . PRO A 1 436 ? -2.30521  -24.27146 -10.27254 1.000 32.13869 ? 436 PRO A CG    1 
ATOM   3512 C  CD    . PRO A 1 436 ? -1.47719  -24.15746 -11.52152 1.000 21.24984 ? 436 PRO A CD    1 
ATOM   3513 N  N     . VAL A 1 437 ? -3.57518  -27.05345 -12.31357 1.000 32.07162 ? 437 VAL A N     1 
ATOM   3514 C  CA    . VAL A 1 437 ? -4.69917  -27.88245 -12.73359 1.000 27.07070 ? 437 VAL A CA    1 
ATOM   3515 C  C     . VAL A 1 437 ? -4.24617  -29.23345 -13.26558 1.000 28.37502 ? 437 VAL A C     1 
ATOM   3516 O  O     . VAL A 1 437 ? -5.07217  -30.13945 -13.42460 1.000 28.10411 ? 437 VAL A O     1 
ATOM   3517 C  CB    . VAL A 1 437 ? -5.54216  -27.13744 -13.79060 1.000 21.79916 ? 437 VAL A CB    1 
ATOM   3518 C  CG1   . VAL A 1 437 ? -4.88614  -27.22244 -15.16159 1.000 25.26487 ? 437 VAL A CG1   1 
ATOM   3519 C  CG2   . VAL A 1 437 ? -6.97016  -27.67244 -13.82362 1.000 25.08806 ? 437 VAL A CG2   1 
ATOM   3520 N  N     . LEU A 1 438 ? -2.95016  -29.39345 -13.53357 1.000 28.93389 ? 438 LEU A N     1 
ATOM   3521 C  CA    . LEU A 1 438 ? -2.37816  -30.64545 -14.01156 1.000 27.23157 ? 438 LEU A CA    1 
ATOM   3522 C  C     . LEU A 1 438 ? -1.43918  -31.26745 -12.98155 1.000 29.08556 ? 438 LEU A C     1 
ATOM   3523 O  O     . LEU A 1 438 ? -0.53217  -32.02445 -13.33554 1.000 35.12930 ? 438 LEU A O     1 
ATOM   3524 C  CB    . LEU A 1 438 ? -1.64414  -30.42044 -15.33255 1.000 28.96218 ? 438 LEU A CB    1 
ATOM   3525 C  CG    . LEU A 1 438 ? -2.48012  -29.91744 -16.51156 1.000 26.70189 ? 438 LEU A CG    1 
ATOM   3526 C  CD1   . LEU A 1 438 ? -1.60310  -29.20144 -17.52454 1.000 15.30723 ? 438 LEU A CD1   1 
ATOM   3527 C  CD2   . LEU A 1 438 ? -3.21611  -31.07144 -17.16658 1.000 23.02508 ? 438 LEU A CD2   1 
ATOM   3528 N  N     . LYS A 1 439 ? -1.65020  -30.95646 -11.69855 1.000 27.12209 ? 439 LYS A N     1 
ATOM   3529 C  CA    . LYS A 1 439 ? -0.73221  -31.41246 -10.65954 1.000 33.90892 ? 439 LYS A CA    1 
ATOM   3530 C  C     . LYS A 1 439 ? -0.80322  -32.92146 -10.45255 1.000 35.73726 ? 439 LYS A C     1 
ATOM   3531 O  O     . LYS A 1 439 ? 0.21578   -33.54947 -10.14353 1.000 35.37259 ? 439 LYS A O     1 
ATOM   3532 C  CB    . LYS A 1 439 ? -1.02423  -30.68447 -9.34554  1.000 31.70089 ? 439 LYS A CB    1 
ATOM   3533 C  CG    . LYS A 1 439 ? -2.43024  -30.90447 -8.80956  1.000 28.49740 ? 439 LYS A CG    1 
ATOM   3534 C  CD    . LYS A 1 439 ? -2.64226  -30.20647 -7.47756  0.000 31.83861 ? 439 LYS A CD    1 
ATOM   3535 C  CE    . LYS A 1 439 ? -4.04927  -30.44547 -6.95259  0.000 32.93319 ? 439 LYS A CE    1 
ATOM   3536 N  NZ    . LYS A 1 439 ? -4.27029  -29.79647 -5.63159  0.000 33.26535 ? 439 LYS A NZ    1 
ATOM   3537 N  N     . ASP A 1 440 ? -1.98122  -33.52046 -10.61857 1.000 26.12764 ? 440 ASP A N     1 
ATOM   3538 C  CA    . ASP A 1 440 ? -2.17222  -34.94446 -10.37857 1.000 32.79584 ? 440 ASP A CA    1 
ATOM   3539 C  C     . ASP A 1 440 ? -2.17120  -35.76646 -11.66158 1.000 33.40040 ? 440 ASP A C     1 
ATOM   3540 O  O     . ASP A 1 440 ? -2.42121  -36.97446 -11.60958 1.000 32.01862 ? 440 ASP A O     1 
ATOM   3541 C  CB    . ASP A 1 440 ? -3.47224  -35.17846 -9.60659  1.000 33.94457 ? 440 ASP A CB    1 
ATOM   3542 C  CG    . ASP A 1 440 ? -3.45226  -34.54947 -8.22459  1.000 41.29971 ? 440 ASP A CG    1 
ATOM   3543 O  OD1   . ASP A 1 440 ? -2.39427  -34.59747 -7.56258  1.000 38.16295 ? 440 ASP A OD1   1 
ATOM   3544 O  OD2   . ASP A 1 440 ? -4.49326  -34.00247 -7.80461  1.000 34.16588 ? 440 ASP A OD2   1 
ATOM   3545 N  N     . MET A 1 441 ? -1.89619  -35.14645 -12.80357 1.000 32.77439 ? 441 MET A N     1 
ATOM   3546 C  CA    . MET A 1 441 ? -1.84617  -35.88745 -14.05357 1.000 29.32382 ? 441 MET A CA    1 
ATOM   3547 C  C     . MET A 1 441 ? -0.57717  -36.73545 -14.10556 1.000 28.17889 ? 441 MET A C     1 
ATOM   3548 O  O     . MET A 1 441 ? 0.50283   -36.25545 -13.74554 1.000 32.69518 ? 441 MET A O     1 
ATOM   3549 C  CB    . MET A 1 441 ? -1.88415  -34.92844 -15.24257 1.000 27.67102 ? 441 MET A CB    1 
ATOM   3550 C  CG    . MET A 1 441 ? -2.01513  -35.60944 -16.59657 1.000 28.67241 ? 441 MET A CG    1 
ATOM   3551 S  SD    . MET A 1 441 ? -3.62513  -36.38844 -16.82460 1.000 33.85549 ? 441 MET A SD    1 
ATOM   3552 C  CE    . MET A 1 441 ? -4.70813  -34.96943 -16.68161 1.000 32.86575 ? 441 MET A CE    1 
ATOM   3553 N  N     . PRO A 1 442 ? -0.67317  -37.99645 -14.52856 1.000 19.74257 ? 442 PRO A N     1 
ATOM   3554 C  CA    . PRO A 1 442 ? 0.53484   -38.81945 -14.66155 1.000 27.28386 ? 442 PRO A CA    1 
ATOM   3555 C  C     . PRO A 1 442 ? 1.49885   -38.22545 -15.67753 1.000 25.07112 ? 442 PRO A C     1 
ATOM   3556 O  O     . PRO A 1 442 ? 1.09787   -37.56545 -16.63953 1.000 26.31899 ? 442 PRO A O     1 
ATOM   3557 C  CB    . PRO A 1 442 ? -0.00716  -40.17645 -15.12856 1.000 24.38744 ? 442 PRO A CB    1 
ATOM   3558 C  CG    . PRO A 1 442 ? -1.42617  -40.19345 -14.67158 1.000 29.94946 ? 442 PRO A CG    1 
ATOM   3559 C  CD    . PRO A 1 442 ? -1.90116  -38.77345 -14.76858 1.000 28.57667 ? 442 PRO A CD    1 
ATOM   3560 N  N     . ALA A 1 443 ? 2.79185   -38.47145 -15.45051 1.000 32.04959 ? 443 ALA A N     1 
ATOM   3561 C  CA    . ALA A 1 443 ? 3.82386   -37.92345 -16.32349 1.000 26.00788 ? 443 ALA A CA    1 
ATOM   3562 C  C     . ALA A 1 443 ? 3.75488   -38.48845 -17.73550 1.000 22.12804 ? 443 ALA A C     1 
ATOM   3563 O  O     . ALA A 1 443 ? 4.35690   -37.91244 -18.64948 1.000 23.74737 ? 443 ALA A O     1 
ATOM   3564 C  CB    . ALA A 1 443 ? 5.20785   -38.18146 -15.72647 1.000 29.61425 ? 443 ALA A CB    1 
ATOM   3565 N  N     . LYS A 1 444 ? 3.03788   -39.59644 -17.93451 1.000 25.95360 ? 444 LYS A N     1 
ATOM   3566 C  CA    . LYS A 1 444 ? 2.93190   -40.18544 -19.26451 1.000 25.43872 ? 444 LYS A CA    1 
ATOM   3567 C  C     . LYS A 1 444 ? 2.07992   -39.32843 -20.19452 1.000 22.93274 ? 444 LYS A C     1 
ATOM   3568 O  O     . LYS A 1 444 ? 2.31794   -39.30943 -21.40652 1.000 29.16420 ? 444 LYS A O     1 
ATOM   3569 C  CB    . LYS A 1 444 ? 2.34990   -41.59444 -19.16053 1.000 21.26452 ? 444 LYS A CB    1 
ATOM   3570 C  CG    . LYS A 1 444 ? 2.43792   -42.41843 -20.43253 1.000 27.40037 ? 444 LYS A CG    1 
ATOM   3571 C  CD    . LYS A 1 444 ? 1.47391   -43.59043 -20.36855 1.000 25.05394 ? 444 LYS A CD    1 
ATOM   3572 C  CE    . LYS A 1 444 ? 1.57689   -44.31444 -19.03555 0.000 28.44009 ? 444 LYS A CE    1 
ATOM   3573 N  NZ    . LYS A 1 444 ? 0.33189   -45.06644 -18.71357 0.000 28.38078 ? 444 LYS A NZ    1 
ATOM   3574 N  N     . TYR A 1 445 ? 1.09091   -38.61743 -19.65154 1.000 22.88162 ? 445 TYR A N     1 
ATOM   3575 C  CA    . TYR A 1 445 ? 0.19393   -37.79243 -20.45155 1.000 25.72444 ? 445 TYR A CA    1 
ATOM   3576 C  C     . TYR A 1 445 ? 0.25992   -36.31743 -20.07954 1.000 27.09286 ? 445 TYR A C     1 
ATOM   3577 O  O     . TYR A 1 445 ? -0.60107  -35.54343 -20.51455 1.000 32.61069 ? 445 TYR A O     1 
ATOM   3578 C  CB    . TYR A 1 445 ? -1.25108  -38.28343 -20.31557 1.000 30.61898 ? 445 TYR A CB    1 
ATOM   3579 C  CG    . TYR A 1 445 ? -1.43008  -39.77643 -20.47358 1.000 30.16541 ? 445 TYR A CG    1 
ATOM   3580 C  CD1   . TYR A 1 445 ? -1.56906  -40.35042 -21.72958 1.000 33.78509 ? 445 TYR A CD1   1 
ATOM   3581 C  CD2   . TYR A 1 445 ? -1.47310  -40.60943 -19.36358 1.000 27.63512 ? 445 TYR A CD2   1 
ATOM   3582 C  CE1   . TYR A 1 445 ? -1.73906  -41.71542 -21.87659 1.000 34.49148 ? 445 TYR A CE1   1 
ATOM   3583 C  CE2   . TYR A 1 445 ? -1.64210  -41.97343 -19.49959 1.000 30.19953 ? 445 TYR A CE2   1 
ATOM   3584 C  CZ    . TYR A 1 445 ? -1.77508  -42.52143 -20.75759 1.000 34.89725 ? 445 TYR A CZ    1 
ATOM   3585 O  OH    . TYR A 1 445 ? -1.94108  -43.87942 -20.89860 1.000 40.34878 ? 445 TYR A OH    1 
ATOM   3586 N  N     . ILE A 1 446 ? 1.25091   -35.90044 -19.28652 1.000 27.60960 ? 446 ILE A N     1 
ATOM   3587 C  CA    . ILE A 1 446 ? 1.27791   -34.52244 -18.81352 1.000 24.47222 ? 446 ILE A CA    1 
ATOM   3588 C  C     . ILE A 1 446 ? 1.65293   -33.54743 -19.92351 1.000 27.17066 ? 446 ILE A C     1 
ATOM   3589 O  O     . ILE A 1 446 ? 1.33593   -32.35643 -19.82851 1.000 30.21447 ? 446 ILE A O     1 
ATOM   3590 C  CB    . ILE A 1 446 ? 2.22789   -34.38644 -17.60750 1.000 25.85247 ? 446 ILE A CB    1 
ATOM   3591 C  CG1   . ILE A 1 446 ? 1.90988   -33.11345 -16.81950 1.000 29.35538 ? 446 ILE A CG1   1 
ATOM   3592 C  CG2   . ILE A 1 446 ? 3.68090   -34.39344 -18.05948 1.000 27.06636 ? 446 ILE A CG2   1 
ATOM   3593 C  CD1   . ILE A 1 446 ? 2.70086   -32.97045 -15.54149 1.000 32.30909 ? 446 ILE A CD1   1 
ATOM   3594 N  N     . TYR A 1 447 ? 2.31394   -34.01843 -20.98150 1.000 26.44121 ? 447 TYR A N     1 
ATOM   3595 C  CA    . TYR A 1 447 ? 2.59696   -33.17043 -22.13149 1.000 21.18320 ? 447 TYR A CA    1 
ATOM   3596 C  C     . TYR A 1 447 ? 1.54498   -33.28842 -23.22451 1.000 27.23447 ? 447 TYR A C     1 
ATOM   3597 O  O     . TYR A 1 447 ? 1.42499   -32.37742 -24.05151 1.000 27.02995 ? 447 TYR A O     1 
ATOM   3598 C  CB    . TYR A 1 447 ? 3.97697   -33.49943 -22.71147 1.000 25.52065 ? 447 TYR A CB    1 
ATOM   3599 C  CG    . TYR A 1 447 ? 5.12696   -32.98943 -21.87146 1.000 19.81290 ? 447 TYR A CG    1 
ATOM   3600 C  CD1   . TYR A 1 447 ? 5.57096   -31.68043 -21.99044 1.000 18.48488 ? 447 TYR A CD1   1 
ATOM   3601 C  CD2   . TYR A 1 447 ? 5.76694   -33.81744 -20.95945 1.000 21.88987 ? 447 TYR A CD2   1 
ATOM   3602 C  CE1   . TYR A 1 447 ? 6.61995   -31.20844 -21.22443 1.000 24.90793 ? 447 TYR A CE1   1 
ATOM   3603 C  CE2   . TYR A 1 447 ? 6.81693   -33.35444 -20.18843 1.000 22.85254 ? 447 TYR A CE2   1 
ATOM   3604 C  CZ    . TYR A 1 447 ? 7.23993   -32.04944 -20.32542 1.000 24.18486 ? 447 TYR A CZ    1 
ATOM   3605 O  OH    . TYR A 1 447 ? 8.28492   -31.58445 -19.56040 1.000 22.65958 ? 447 TYR A OH    1 
ATOM   3606 N  N     . GLU A 1 448 ? 0.78597   -34.38342 -23.24853 1.000 23.23707 ? 448 GLU A N     1 
ATOM   3607 C  CA    . GLU A 1 448 ? -0.31401  -34.57642 -24.19254 1.000 24.55629 ? 448 GLU A CA    1 
ATOM   3608 C  C     . GLU A 1 448 ? -1.54502  -34.97542 -23.39056 1.000 31.13848 ? 448 GLU A C     1 
ATOM   3609 O  O     . GLU A 1 448 ? -1.92903  -36.15242 -23.36357 1.000 30.70601 ? 448 GLU A O     1 
ATOM   3610 C  CB    . GLU A 1 448 ? 0.02900   -35.63241 -25.24554 1.000 32.69415 ? 448 GLU A CB    1 
ATOM   3611 C  CG    . GLU A 1 448 ? 1.41701   -35.48841 -25.84652 1.000 27.11793 ? 448 GLU A CG    1 
ATOM   3612 C  CD    . GLU A 1 448 ? 1.67603   -36.48041 -26.96452 1.000 35.71313 ? 448 GLU A CD    1 
ATOM   3613 O  OE1   . GLU A 1 448 ? 0.86904   -36.53040 -27.91653 1.000 33.28879 ? 448 GLU A OE1   1 
ATOM   3614 O  OE2   . GLU A 1 448 ? 2.68403   -37.21441 -26.88751 1.000 34.15592 ? 448 GLU A OE2   1 
ATOM   3615 N  N     . PRO A 1 449 ? -2.18903  -34.01542 -22.71857 1.000 27.39560 ? 449 PRO A N     1 
ATOM   3616 C  CA    . PRO A 1 449 ? -3.34305  -34.36442 -21.87359 1.000 29.38260 ? 449 PRO A CA    1 
ATOM   3617 C  C     . PRO A 1 449 ? -4.54404  -34.85741 -22.65861 1.000 31.36496 ? 449 PRO A C     1 
ATOM   3618 O  O     . PRO A 1 449 ? -5.38905  -35.55541 -22.08363 1.000 25.64375 ? 449 PRO A O     1 
ATOM   3619 C  CB    . PRO A 1 449 ? -3.65206  -33.05342 -21.13959 1.000 23.26487 ? 449 PRO A CB    1 
ATOM   3620 C  CG    . PRO A 1 449 ? -3.13004  -31.99142 -22.04358 1.000 30.77413 ? 449 PRO A CG    1 
ATOM   3621 C  CD    . PRO A 1 449 ? -1.91303  -32.56942 -22.71056 1.000 26.31149 ? 449 PRO A CD    1 
ATOM   3622 N  N     . TRP A 1 450 ? -4.65001  -34.52441 -23.94661 1.000 30.90347 ? 450 TRP A N     1 
ATOM   3623 C  CA    . TRP A 1 450 ? -5.75200  -35.03440 -24.75363 1.000 32.55978 ? 450 TRP A CA    1 
ATOM   3624 C  C     . TRP A 1 450 ? -5.60600  -36.52040 -25.05063 1.000 31.49154 ? 450 TRP A C     1 
ATOM   3625 O  O     . TRP A 1 450 ? -6.60100  -37.17340 -25.38165 1.000 27.49718 ? 450 TRP A O     1 
ATOM   3626 C  CB    . TRP A 1 450 ? -5.86098  -34.24640 -26.06063 1.000 28.01081 ? 450 TRP A CB    1 
ATOM   3627 C  CG    . TRP A 1 450 ? -4.70197  -34.44540 -26.99061 1.000 28.15732 ? 450 TRP A CG    1 
ATOM   3628 C  CD1   . TRP A 1 450 ? -4.59096  -35.38439 -27.97361 1.000 25.06868 ? 450 TRP A CD1   1 
ATOM   3629 C  CD2   . TRP A 1 450 ? -3.48997  -33.68040 -27.02759 1.000 29.93004 ? 450 TRP A CD2   1 
ATOM   3630 N  NE1   . TRP A 1 450 ? -3.38594  -35.25539 -28.61959 1.000 29.97375 ? 450 TRP A NE1   1 
ATOM   3631 C  CE2   . TRP A 1 450 ? -2.69095  -34.21640 -28.05858 1.000 30.22289 ? 450 TRP A CE2   1 
ATOM   3632 C  CE3   . TRP A 1 450 ? -3.00298  -32.59640 -26.29158 1.000 25.27369 ? 450 TRP A CE3   1 
ATOM   3633 C  CZ2   . TRP A 1 450 ? -1.43295  -33.70440 -28.36956 1.000 24.74057 ? 450 TRP A CZ2   1 
ATOM   3634 C  CZ3   . TRP A 1 450 ? -1.75397  -32.09040 -26.60256 1.000 24.64484 ? 450 TRP A CZ3   1 
ATOM   3635 C  CH2   . TRP A 1 450 ? -0.98296  -32.64440 -27.63155 1.000 25.37767 ? 450 TRP A CH2   1 
ATOM   3636 N  N     . THR A 1 451 ? -4.39400  -37.06641 -24.93962 1.000 36.65266 ? 451 THR A N     1 
ATOM   3637 C  CA    . THR A 1 451 ? -4.17200  -38.49141 -25.15062 1.000 36.65002 ? 451 THR A CA    1 
ATOM   3638 C  C     . THR A 1 451 ? -4.49902  -39.33041 -23.92362 1.000 40.79677 ? 451 THR A C     1 
ATOM   3639 O  O     . THR A 1 451 ? -4.55202  -40.56141 -24.03263 1.000 43.57834 ? 451 THR A O     1 
ATOM   3640 C  CB    . THR A 1 451 ? -2.72000  -38.74641 -25.56360 1.000 37.15145 ? 451 THR A CB    1 
ATOM   3641 O  OG1   . THR A 1 451 ? -1.84101  -38.28741 -24.52858 1.000 38.54558 ? 451 THR A OG1   1 
ATOM   3642 C  CG2   . THR A 1 451 ? -2.39698  -38.01640 -26.85759 1.000 37.73640 ? 451 THR A CG2   1 
ATOM   3643 N  N     . ALA A 1 452 ? -4.71604  -38.70641 -22.77163 1.000 35.57815 ? 452 ALA A N     1 
ATOM   3644 C  CA    . ALA A 1 452 ? -5.04606  -39.46142 -21.57463 1.000 36.60725 ? 452 ALA A CA    1 
ATOM   3645 C  C     . ALA A 1 452 ? -6.48406  -39.96841 -21.65366 1.000 36.75518 ? 452 ALA A C     1 
ATOM   3646 O  O     . ALA A 1 452 ? -7.37705  -39.23841 -22.09667 1.000 40.69011 ? 452 ALA A O     1 
ATOM   3647 C  CB    . ALA A 1 452 ? -4.86508  -38.59942 -20.32663 1.000 33.02324 ? 452 ALA A CB    1 
ATOM   3648 N  N     . PRO A 1 453 ? -6.73807  -41.21041 -21.24567 1.000 32.34056 ? 453 PRO A N     1 
ATOM   3649 C  CA    . PRO A 1 453 ? -8.11507  -41.71541 -21.23269 1.000 41.78954 ? 453 PRO A CA    1 
ATOM   3650 C  C     . PRO A 1 453 ? -8.99008  -40.90441 -20.29070 1.000 42.41213 ? 453 PRO A C     1 
ATOM   3651 O  O     . PRO A 1 453 ? -8.51210  -40.23242 -19.37369 1.000 42.40977 ? 453 PRO A O     1 
ATOM   3652 C  CB    . PRO A 1 453 ? -7.96108  -43.16241 -20.74569 1.000 43.17218 ? 453 PRO A CB    1 
ATOM   3653 C  CG    . PRO A 1 453 ? -6.53708  -43.51642 -21.04067 1.000 46.21223 ? 453 PRO A CG    1 
ATOM   3654 C  CD    . PRO A 1 453 ? -5.76308  -42.24542 -20.86265 1.000 37.35922 ? 453 PRO A CD    1 
ATOM   3655 N  N     A LEU A 1 454 ? -10.30208 -40.97441 -20.53172 0.449 40.62102 ? 454 LEU A N     1 
ATOM   3656 N  N     B LEU A 1 454 ? -10.30208 -40.97341 -20.53972 0.551 40.61652 ? 454 LEU A N     1 
ATOM   3657 C  CA    A LEU A 1 454 ? -11.24109 -40.22041 -19.70873 0.449 40.79794 ? 454 LEU A CA    1 
ATOM   3658 C  CA    B LEU A 1 454 ? -11.25409 -40.23441 -19.71773 0.551 40.80615 ? 454 LEU A CA    1 
ATOM   3659 C  C     A LEU A 1 454 ? -11.21911 -40.68342 -18.25773 0.449 42.25077 ? 454 LEU A C     1 
ATOM   3660 C  C     B LEU A 1 454 ? -11.20411 -40.68042 -18.26273 0.551 42.24788 ? 454 LEU A C     1 
ATOM   3661 O  O     A LEU A 1 454 ? -11.47313 -39.88442 -17.34973 0.449 43.23698 ? 454 LEU A O     1 
ATOM   3662 O  O     B LEU A 1 454 ? -11.42313 -39.86742 -17.35773 0.551 43.25800 ? 454 LEU A O     1 
ATOM   3663 C  CB    A LEU A 1 454 ? -12.65208 -40.33141 -20.28875 0.449 40.52770 ? 454 LEU A CB    1 
ATOM   3664 C  CB    B LEU A 1 454 ? -12.66708 -40.40041 -20.28075 0.551 40.53974 ? 454 LEU A CB    1 
ATOM   3665 C  CG    A LEU A 1 454 ? -13.18907 -39.06740 -20.96476 0.449 40.48559 ? 454 LEU A CG    1 
ATOM   3666 C  CG    B LEU A 1 454 ? -13.39907 -39.12440 -20.70076 0.551 40.72436 ? 454 LEU A CG    1 
ATOM   3667 C  CD1   A LEU A 1 454 ? -14.15305 -39.42340 -22.08377 0.449 38.72058 ? 454 LEU A CD1   1 
ATOM   3668 C  CD1   B LEU A 1 454 ? -13.82009 -38.31741 -19.48276 0.551 42.47757 ? 454 LEU A CD1   1 
ATOM   3669 C  CD2   A LEU A 1 454 ? -13.86608 -38.16641 -19.94276 0.449 41.77601 ? 454 LEU A CD2   1 
ATOM   3670 C  CD2   B LEU A 1 454 ? -12.52706 -38.28740 -21.62474 0.551 36.83068 ? 454 LEU A CD2   1 
ATOM   3671 N  N     . GLU A 1 455 ? -10.91412 -41.96042 -18.01773 1.000 43.20640 ? 455 GLU A N     1 
ATOM   3672 C  CA    . GLU A 1 455 ? -10.80114 -42.44142 -16.64473 1.000 39.18498 ? 455 GLU A CA    1 
ATOM   3673 C  C     . GLU A 1 455 ? -9.58715  -41.83543 -15.95171 1.000 39.70259 ? 455 GLU A C     1 
ATOM   3674 O  O     . GLU A 1 455 ? -9.63217  -41.53743 -14.75271 1.000 42.91481 ? 455 GLU A O     1 
ATOM   3675 C  CB    . GLU A 1 455 ? -10.73314 -43.96842 -16.62874 1.000 39.36626 ? 455 GLU A CB    1 
ATOM   3676 C  CG    . GLU A 1 455 ? -10.58717 -44.57943 -15.24474 0.000 41.39894 ? 455 GLU A CG    1 
ATOM   3677 C  CD    . GLU A 1 455 ? -9.19217  -45.11643 -14.98772 0.000 40.68680 ? 455 GLU A CD    1 
ATOM   3678 O  OE1   . GLU A 1 455 ? -8.39616  -45.18943 -15.94771 0.000 41.36573 ? 455 GLU A OE1   1 
ATOM   3679 O  OE2   . GLU A 1 455 ? -8.89019  -45.46644 -13.82771 0.000 39.73965 ? 455 GLU A OE2   1 
ATOM   3680 N  N     . VAL A 1 456 ? -8.49514  -41.63543 -16.69369 1.000 41.75603 ? 456 VAL A N     1 
ATOM   3681 C  CA    . VAL A 1 456 ? -7.32815  -40.96943 -16.12467 1.000 41.40325 ? 456 VAL A CA    1 
ATOM   3682 C  C     . VAL A 1 456 ? -7.58915  -39.47743 -15.96967 1.000 38.60747 ? 456 VAL A C     1 
ATOM   3683 O  O     . VAL A 1 456 ? -7.11316  -38.85144 -15.01366 1.000 39.23813 ? 456 VAL A O     1 
ATOM   3684 C  CB    . VAL A 1 456 ? -6.08413  -41.24443 -16.99166 1.000 37.83648 ? 456 VAL A CB    1 
ATOM   3685 C  CG1   . VAL A 1 456 ? -4.84514  -40.62644 -16.36263 1.000 35.55438 ? 456 VAL A CG1   1 
ATOM   3686 C  CG2   . VAL A 1 456 ? -5.89613  -42.74143 -17.18666 1.000 38.21649 ? 456 VAL A CG2   1 
ATOM   3687 N  N     . GLN A 1 457 ? -8.34913  -38.88243 -16.89268 1.000 41.42051 ? 457 GLN A N     1 
ATOM   3688 C  CA    . GLN A 1 457 ? -8.68213  -37.46643 -16.77368 1.000 40.76047 ? 457 GLN A CA    1 
ATOM   3689 C  C     . GLN A 1 457 ? -9.58515  -37.21143 -15.57170 1.000 39.61571 ? 457 GLN A C     1 
ATOM   3690 O  O     . GLN A 1 457 ? -9.41716  -36.21143 -14.86469 1.000 34.23423 ? 457 GLN A O     1 
ATOM   3691 C  CB    . GLN A 1 457 ? -9.34711  -36.97142 -18.05869 1.000 39.98536 ? 457 GLN A CB    1 
ATOM   3692 C  CG    . GLN A 1 457 ? -8.45409  -37.01842 -19.28868 1.000 35.37155 ? 457 GLN A CG    1 
ATOM   3693 C  CD    . GLN A 1 457 ? -9.14507  -36.49241 -20.53269 1.000 35.15928 ? 457 GLN A CD    1 
ATOM   3694 O  OE1   . GLN A 1 457 ? -8.66105  -36.67141 -21.64968 1.000 36.19831 ? 457 GLN A OE1   1 
ATOM   3695 N  NE2   . GLN A 1 457 ? -10.28307 -35.83441 -20.34370 1.000 35.38366 ? 457 GLN A NE2   1 
ATOM   3696 N  N     . ARG A 1 458 ? -10.54617 -38.10639 -15.32462 1.000 42.49267 ? 458 ARG A N     1 
ATOM   3697 C  CA    . ARG A 1 458 ? -11.42503 -37.95520 -14.16843 1.000 35.19812 ? 458 ARG A CA    1 
ATOM   3698 C  C     . ARG A 1 458 ? -10.66628 -38.16261 -12.86367 1.000 40.57187 ? 458 ARG A C     1 
ATOM   3699 O  O     . ARG A 1 458 ? -10.88220 -37.43065 -11.89042 1.000 38.50613 ? 458 ARG A O     1 
ATOM   3700 C  CB    . ARG A 1 458 ? -12.59230 -38.93843 -14.26209 1.000 37.84586 ? 458 ARG A CB    1 
ATOM   3701 C  CG    . ARG A 1 458 ? -13.61443 -38.61815 -15.34010 1.000 42.85522 ? 458 ARG A CG    1 
ATOM   3702 C  CD    . ARG A 1 458 ? -14.54408 -37.49582 -14.91480 1.000 49.69910 ? 458 ARG A CD    1 
ATOM   3703 N  NE    . ARG A 1 458 ? -15.63008 -37.30454 -15.86853 1.000 58.50422 ? 458 ARG A NE    1 
ATOM   3704 C  CZ    . ARG A 1 458 ? -16.76811 -37.98512 -15.85334 0.000 56.65220 ? 458 ARG A CZ    1 
ATOM   3705 N  NH1   . ARG A 1 458 ? -17.00435 -38.91690 -14.94420 0.000 56.85002 ? 458 ARG A NH1   1 
ATOM   3706 N  NH2   . ARG A 1 458 ? -17.69177 -37.72555 -16.77439 0.000 57.04093 ? 458 ARG A NH2   1 
ATOM   3707 N  N     . LYS A 1 459 ? -9.77619  -39.15744 -12.82370 1.000 35.16838 ? 459 LYS A N     1 
ATOM   3708 C  CA    . LYS A 1 459 ? -9.05621  -39.45944 -11.59069 1.000 36.70626 ? 459 LYS A CA    1 
ATOM   3709 C  C     . LYS A 1 459 ? -8.06022  -38.35945 -11.24168 1.000 38.65040 ? 459 LYS A C     1 
ATOM   3710 O  O     . LYS A 1 459 ? -7.94523  -37.96745 -10.07467 1.000 24.31839 ? 459 LYS A O     1 
ATOM   3711 C  CB    . LYS A 1 459 ? -8.34721  -40.80845 -11.71569 1.000 33.58484 ? 459 LYS A CB    1 
ATOM   3712 C  CG    . LYS A 1 459 ? -7.52423  -41.19345 -10.49768 1.000 32.66807 ? 459 LYS A CG    1 
ATOM   3713 C  CD    . LYS A 1 459 ? -7.09723  -42.65045 -10.55768 0.000 31.44996 ? 459 LYS A CD    1 
ATOM   3714 C  CE    . LYS A 1 459 ? -8.30324  -43.57545 -10.54170 0.000 31.63594 ? 459 LYS A CE    1 
ATOM   3715 N  NZ    . LYS A 1 459 ? -7.90624  -45.01045 -10.55470 0.000 30.85416 ? 459 LYS A NZ    1 
ATOM   3716 N  N     . ALA A 1 460 ? -7.33420  -37.84845 -12.23766 1.000 35.99443 ? 460 ALA A N     1 
ATOM   3717 C  CA    . ALA A 1 460 ? -6.38120  -36.77245 -11.99664 1.000 34.40422 ? 460 ALA A CA    1 
ATOM   3718 C  C     . ALA A 1 460 ? -7.05720  -35.43845 -11.71265 1.000 31.82354 ? 460 ALA A C     1 
ATOM   3719 O  O     . ALA A 1 460 ? -6.37321  -34.49145 -11.30864 1.000 31.37071 ? 460 ALA A O     1 
ATOM   3720 C  CB    . ALA A 1 460 ? -5.43718  -36.62945 -13.19163 1.000 33.67684 ? 460 ALA A CB    1 
ATOM   3721 N  N     . GLY A 1 461 ? -8.36920  -35.34044 -11.90867 1.000 30.43301 ? 461 GLY A N     1 
ATOM   3722 C  CA    . GLY A 1 461 ? -9.06920  -34.09744 -11.65468 1.000 36.34476 ? 461 GLY A CA    1 
ATOM   3723 C  C     . GLY A 1 461 ? -8.91218  -33.05544 -12.73467 1.000 27.23212 ? 461 GLY A C     1 
ATOM   3724 O  O     . GLY A 1 461 ? -9.01219  -31.85844 -12.44867 1.000 28.75821 ? 461 GLY A O     1 
ATOM   3725 N  N     . CYS A 1 462 ? -8.66917  -33.47544 -13.97667 1.000 29.68381 ? 462 CYS A N     1 
ATOM   3726 C  CA    . CYS A 1 462 ? -8.48615  -32.53143 -15.07766 1.000 32.44194 ? 462 CYS A CA    1 
ATOM   3727 C  C     . CYS A 1 462 ? -9.02013  -33.18843 -16.34867 1.000 36.71822 ? 462 CYS A C     1 
ATOM   3728 O  O     . CYS A 1 462 ? -8.36012  -34.05743 -16.92467 1.000 34.60891 ? 462 CYS A O     1 
ATOM   3729 C  CB    . CYS A 1 462 ? -7.02414  -32.13544 -15.22464 1.000 31.69856 ? 462 CYS A CB    1 
ATOM   3730 S  SG    . CYS A 1 462 ? -6.72412  -30.91043 -16.51363 1.000 24.30252 ? 462 CYS A SG    1 
ATOM   3731 N  N     . VAL A 1 463 ? -10.20812 -32.76942 -16.77169 1.000 35.88683 ? 463 VAL A N     1 
ATOM   3732 C  CA    . VAL A 1 463 ? -10.83110 -33.26042 -17.99570 1.000 26.74191 ? 463 VAL A CA    1 
ATOM   3733 C  C     . VAL A 1 463 ? -10.53508 -32.26542 -19.10769 1.000 34.11880 ? 463 VAL A C     1 
ATOM   3734 O  O     . VAL A 1 463 ? -10.83508 -31.07242 -18.97869 1.000 35.07239 ? 463 VAL A O     1 
ATOM   3735 C  CB    . VAL A 1 463 ? -12.34511 -33.45342 -17.81672 1.000 38.83859 ? 463 VAL A CB    1 
ATOM   3736 C  CG1   . VAL A 1 463 ? -12.98109 -33.89141 -19.12874 1.000 40.86092 ? 463 VAL A CG1   1 
ATOM   3737 C  CG2   . VAL A 1 463 ? -12.62213 -34.46642 -16.71973 1.000 39.04767 ? 463 VAL A CG2   1 
ATOM   3738 N  N     . VAL A 1 464 ? -9.94107  -32.75141 -20.19568 1.000 36.58175 ? 464 VAL A N     1 
ATOM   3739 C  CA    . VAL A 1 464 ? -9.63705  -31.89041 -21.33468 1.000 36.79100 ? 464 VAL A CA    1 
ATOM   3740 C  C     . VAL A 1 464 ? -10.94404 -31.43940 -21.97070 1.000 33.51437 ? 464 VAL A C     1 
ATOM   3741 O  O     . VAL A 1 464 ? -11.71003 -32.25340 -22.49971 1.000 32.98576 ? 464 VAL A O     1 
ATOM   3742 C  CB    . VAL A 1 464 ? -8.74304  -32.61441 -22.34867 1.000 35.15491 ? 464 VAL A CB    1 
ATOM   3743 C  CG1   . VAL A 1 464 ? -8.55802  -31.76340 -23.59166 1.000 29.02744 ? 464 VAL A CG1   1 
ATOM   3744 C  CG2   . VAL A 1 464 ? -7.39905  -32.94641 -21.72265 1.000 29.69596 ? 464 VAL A CG2   1 
ATOM   3745 N  N     . GLY A 1 465 ? -11.20404 -30.13540 -21.92169 1.000 34.87742 ? 465 GLY A N     1 
ATOM   3746 C  CA    . GLY A 1 465 ? -12.43403 -29.55240 -22.41271 1.000 29.88947 ? 465 GLY A CA    1 
ATOM   3747 C  C     . GLY A 1 465 ? -13.28204 -28.91040 -21.33572 1.000 28.82815 ? 465 GLY A C     1 
ATOM   3748 O  O     . GLY A 1 465 ? -14.12104 -28.05440 -21.65073 1.000 28.02065 ? 465 GLY A O     1 
ATOM   3749 N  N     . ARG A 1 466 ? -13.09630 -29.30062 -20.07766 1.000 32.51444 ? 466 ARG A N     1 
ATOM   3750 C  CA    . ARG A 1 466 ? -13.79523 -28.71768 -18.93957 1.000 31.45244 ? 466 ARG A CA    1 
ATOM   3751 C  C     . ARG A 1 466 ? -12.87184 -27.95969 -18.00209 1.000 30.42586 ? 466 ARG A C     1 
ATOM   3752 O  O     . ARG A 1 466 ? -13.21123 -26.85811 -17.56459 1.000 30.02996 ? 466 ARG A O     1 
ATOM   3753 C  CB    . ARG A 1 466 ? -14.52102 -29.81270 -18.14962 1.000 29.01643 ? 466 ARG A CB    1 
ATOM   3754 C  CG    . ARG A 1 466 ? -15.28972 -29.30395 -16.94290 1.000 27.15764 ? 466 ARG A CG    1 
ATOM   3755 C  CD    . ARG A 1 466 ? -15.66063 -30.44307 -16.00765 1.000 34.75788 ? 466 ARG A CD    1 
ATOM   3756 N  NE    . ARG A 1 466 ? -14.48247 -31.05043 -15.39955 1.000 28.94521 ? 466 ARG A NE    1 
ATOM   3757 C  CZ    . ARG A 1 466 ? -14.51874 -32.04422 -14.52220 1.000 29.34361 ? 466 ARG A CZ    1 
ATOM   3758 N  NH1   . ARG A 1 466 ? -15.66349 -32.57947 -14.13044 1.000 30.35496 ? 466 ARG A NH1   1 
ATOM   3759 N  NH2   . ARG A 1 466 ? -13.37779 -32.51138 -14.02355 1.000 27.45898 ? 466 ARG A NH2   1 
ATOM   3760 N  N     . ASP A 1 467 ? -11.70910 -28.52442 -17.68670 1.000 31.78230 ? 467 ASP A N     1 
ATOM   3761 C  CA    . ASP A 1 467 ? -10.72611 -27.88942 -16.81668 1.000 31.23451 ? 467 ASP A CA    1 
ATOM   3762 C  C     . ASP A 1 467 ? -9.52010  -27.35242 -17.56866 1.000 25.52348 ? 467 ASP A C     1 
ATOM   3763 O  O     . ASP A 1 467 ? -9.02310  -26.27442 -17.23465 1.000 29.05956 ? 467 ASP A O     1 
ATOM   3764 C  CB    . ASP A 1 467 ? -10.25513 -28.88043 -15.74568 1.000 27.84519 ? 467 ASP A CB    1 
ATOM   3765 C  CG    . ASP A 1 467 ? -11.40914 -29.57543 -15.04570 1.000 31.08532 ? 467 ASP A CG    1 
ATOM   3766 O  OD1   . ASP A 1 467 ? -12.46814 -28.93943 -14.85871 1.000 30.06670 ? 467 ASP A OD1   1 
ATOM   3767 O  OD2   . ASP A 1 467 ? -11.25815 -30.76243 -14.68670 1.000 29.65042 ? 467 ASP A OD2   1 
ATOM   3768 N  N     . TYR A 1 468 ? -9.04009  -28.07542 -18.57965 1.000 23.32068 ? 468 TYR A N     1 
ATOM   3769 C  CA    . TYR A 1 468 ? -7.92907  -27.63842 -19.40864 1.000 27.79051 ? 468 TYR A CA    1 
ATOM   3770 C  C     . TYR A 1 468 ? -8.33905  -27.70741 -20.87564 1.000 29.00842 ? 468 TYR A C     1 
ATOM   3771 O  O     . TYR A 1 468 ? -8.95904  -28.69041 -21.30166 1.000 30.40798 ? 468 TYR A O     1 
ATOM   3772 C  CB    . TYR A 1 468 ? -6.68208  -28.50142 -19.16562 1.000 27.22531 ? 468 TYR A CB    1 
ATOM   3773 C  CG    . TYR A 1 468 ? -5.43607  -27.96142 -19.82260 1.000 27.97955 ? 468 TYR A CG    1 
ATOM   3774 C  CD1   . TYR A 1 468 ? -4.72207  -26.91843 -19.24758 1.000 27.34201 ? 468 TYR A CD1   1 
ATOM   3775 C  CD2   . TYR A 1 468 ? -4.97505  -28.49042 -21.01859 1.000 19.15403 ? 468 TYR A CD2   1 
ATOM   3776 C  CE1   . TYR A 1 468 ? -3.58506  -26.41843 -19.84656 1.000 28.19633 ? 468 TYR A CE1   1 
ATOM   3777 C  CE2   . TYR A 1 468 ? -3.84004  -27.99942 -21.62457 1.000 18.92740 ? 468 TYR A CE2   1 
ATOM   3778 C  CZ    . TYR A 1 468 ? -3.14805  -26.96342 -21.03456 1.000 24.70131 ? 468 TYR A CZ    1 
ATOM   3779 O  OH    . TYR A 1 468 ? -2.01504  -26.46842 -21.63554 1.000 20.28479 ? 468 TYR A OH    1 
ATOM   3780 N  N     . PRO A 1 469 ? -8.02404  -26.68241 -21.66463 1.000 24.86684 ? 469 PRO A N     1 
ATOM   3781 C  CA    . PRO A 1 469 ? -8.51101  -26.64040 -23.04964 1.000 24.56459 ? 469 PRO A CA    1 
ATOM   3782 C  C     . PRO A 1 469 ? -7.81300  -27.66040 -23.93663 1.000 31.97755 ? 469 PRO A C     1 
ATOM   3783 O  O     . PRO A 1 469 ? -6.70301  -28.12241 -23.66062 1.000 29.70927 ? 469 PRO A O     1 
ATOM   3784 C  CB    . PRO A 1 469 ? -8.19001  -25.20840 -23.49263 1.000 27.54707 ? 469 PRO A CB    1 
ATOM   3785 C  CG    . PRO A 1 469 ? -7.04202  -24.79841 -22.62461 1.000 26.08135 ? 469 PRO A CG    1 
ATOM   3786 C  CD    . PRO A 1 469 ? -7.28404  -25.46341 -21.29762 1.000 26.65755 ? 469 PRO A CD    1 
ATOM   3787 N  N     . ALA A 1 470 ? -8.49499  -28.01440 -25.02465 1.000 35.76532 ? 470 ALA A N     1 
ATOM   3788 C  CA    . ALA A 1 470 ? -7.94097  -28.93840 -25.99564 1.000 29.34132 ? 470 ALA A CA    1 
ATOM   3789 C  C     . ALA A 1 470 ? -6.90096  -28.22839 -26.85862 1.000 25.41415 ? 470 ALA A C     1 
ATOM   3790 O  O     . ALA A 1 470 ? -6.87896  -26.99839 -26.93062 1.000 21.05349 ? 470 ALA A O     1 
ATOM   3791 C  CB    . ALA A 1 470 ? -9.05596  -29.52439 -26.85966 1.000 26.00857 ? 470 ALA A CB    1 
ATOM   3792 N  N     . PRO A 1 471 ? -6.00495  -28.98239 -27.49761 1.000 24.70485 ? 471 PRO A N     1 
ATOM   3793 C  CA    . PRO A 1 471 ? -5.01494  -28.35139 -28.38059 1.000 22.36451 ? 471 PRO A CA    1 
ATOM   3794 C  C     . PRO A 1 471 ? -5.69492  -27.64039 -29.54060 1.000 22.27813 ? 471 PRO A C     1 
ATOM   3795 O  O     . PRO A 1 471 ? -6.54291  -28.21138 -30.23162 1.000 20.57177 ? 471 PRO A O     1 
ATOM   3796 C  CB    . PRO A 1 471 ? -4.15893  -29.53139 -28.85658 1.000 25.21441 ? 471 PRO A CB    1 
ATOM   3797 C  CG    . PRO A 1 471 ? -5.01794  -30.73739 -28.64160 1.000 22.40544 ? 471 PRO A CG    1 
ATOM   3798 C  CD    . PRO A 1 471 ? -5.79895  -30.43739 -27.40561 1.000 24.26517 ? 471 PRO A CD    1 
ATOM   3799 N  N     . ILE A 1 472 ? -5.31491  -26.37839 -29.74859 1.000 22.21374 ? 472 ILE A N     1 
ATOM   3800 C  CA    . ILE A 1 472 ? -5.95989  -25.57038 -30.77760 1.000 24.21437 ? 472 ILE A CA    1 
ATOM   3801 C  C     . ILE A 1 472 ? -5.57887  -26.05438 -32.17159 1.000 22.52207 ? 472 ILE A C     1 
ATOM   3802 O  O     . ILE A 1 472 ? -6.34986  -25.88737 -33.12261 1.000 27.58722 ? 472 ILE A O     1 
ATOM   3803 C  CB    . ILE A 1 472 ? -5.61289  -24.08238 -30.58559 1.000 22.59006 ? 472 ILE A CB    1 
ATOM   3804 C  CG1   . ILE A 1 472 ? -4.10589  -23.85739 -30.72056 1.000 18.91771 ? 472 ILE A CG1   1 
ATOM   3805 C  CG2   . ILE A 1 472 ? -6.10591  -23.59239 -29.23259 1.000 25.14364 ? 472 ILE A CG2   1 
ATOM   3806 C  CD1   . ILE A 1 472 ? -3.69089  -22.40839 -30.58155 1.000 24.28014 ? 472 ILE A CD1   1 
ATOM   3807 N  N     . VAL A 1 473 ? -4.39787  -26.65738 -32.32058 1.000 18.34385 ? 473 VAL A N     1 
ATOM   3808 C  CA    . VAL A 1 473 ? -3.89885  -27.09538 -33.61757 1.000 24.19517 ? 473 VAL A CA    1 
ATOM   3809 C  C     . VAL A 1 473 ? -3.20386  -28.44138 -33.46557 1.000 23.80639 ? 473 VAL A C     1 
ATOM   3810 O  O     . VAL A 1 473 ? -2.77088  -28.82838 -32.37956 1.000 17.78433 ? 473 VAL A O     1 
ATOM   3811 C  CB    . VAL A 1 473 ? -2.92184  -26.07537 -34.24955 1.000 22.38822 ? 473 VAL A CB    1 
ATOM   3812 C  CG1   . VAL A 1 473 ? -3.64783  -24.80037 -34.64456 1.000 24.25545 ? 473 VAL A CG1   1 
ATOM   3813 C  CG2   . VAL A 1 473 ? -1.78186  -25.77138 -33.29054 1.000 21.51132 ? 473 VAL A CG2   1 
ATOM   3814 N  N     . ASP A 1 474 ? -3.10784  -29.15537 -34.58357 1.000 28.60073 ? 474 ASP A N     1 
ATOM   3815 C  CA    . ASP A 1 474 ? -2.27684  -30.34837 -34.67956 1.000 23.36722 ? 474 ASP A CA    1 
ATOM   3816 C  C     . ASP A 1 474 ? -0.91483  -29.92838 -35.21954 1.000 24.77557 ? 474 ASP A C     1 
ATOM   3817 O  O     . ASP A 1 474 ? -0.82182  -29.40737 -36.33653 1.000 26.54752 ? 474 ASP A O     1 
ATOM   3818 C  CB    . ASP A 1 474 ? -2.92783  -31.39437 -35.58357 1.000 30.17713 ? 474 ASP A CB    1 
ATOM   3819 C  CG    . ASP A 1 474 ? -2.20183  -32.72937 -35.55457 1.000 30.01518 ? 474 ASP A CG    1 
ATOM   3820 O  OD1   . ASP A 1 474 ? -1.24785  -32.87738 -34.76255 1.000 28.33679 ? 474 ASP A OD1   1 
ATOM   3821 O  OD2   . ASP A 1 474 ? -2.58882  -33.63237 -36.32658 1.000 29.64995 ? 474 ASP A OD2   1 
ATOM   3822 N  N     . HIS A 1 475 ? 0.13415   -30.14338 -34.42152 1.000 26.89497 ? 475 HIS A N     1 
ATOM   3823 C  CA    . HIS A 1 475 ? 1.46216   -29.65738 -34.78850 1.000 25.89868 ? 475 HIS A CA    1 
ATOM   3824 C  C     . HIS A 1 475 ? 1.92118   -30.24938 -36.11549 1.000 23.57965 ? 475 HIS A C     1 
ATOM   3825 O  O     . HIS A 1 475 ? 2.42419   -29.52837 -36.98548 1.000 27.54862 ? 475 HIS A O     1 
ATOM   3826 C  CB    . HIS A 1 475 ? 2.46514   -29.97939 -33.67949 1.000 27.15485 ? 475 HIS A CB    1 
ATOM   3827 C  CG    . HIS A 1 475 ? 3.85115   -29.48239 -33.95546 1.000 25.05247 ? 475 HIS A CG    1 
ATOM   3828 N  ND1   . HIS A 1 475 ? 4.97914   -30.18139 -33.58445 1.000 36.61552 ? 475 HIS A ND1   1 
ATOM   3829 C  CD2   . HIS A 1 475 ? 4.29016   -28.35639 -34.56445 1.000 29.26959 ? 475 HIS A CD2   1 
ATOM   3830 C  CE1   . HIS A 1 475 ? 6.05415   -29.50839 -33.95443 1.000 27.03031 ? 475 HIS A CE1   1 
ATOM   3831 N  NE2   . HIS A 1 475 ? 5.66316   -28.39539 -34.55143 1.000 27.84337 ? 475 HIS A NE2   1 
ATOM   3832 N  N     . ALA A 1 476 ? 1.74818   -31.56138 -36.29250 1.000 21.45147 ? 476 ALA A N     1 
ATOM   3833 C  CA    . ALA A 1 476 ? 2.17820   -32.20037 -37.53150 1.000 25.33773 ? 476 ALA A CA    1 
ATOM   3834 C  C     . ALA A 1 476 ? 1.45922   -31.62237 -38.74351 1.000 26.85835 ? 476 ALA A C     1 
ATOM   3835 O  O     . ALA A 1 476 ? 2.01623   -31.60536 -39.84650 1.000 37.34068 ? 476 ALA A O     1 
ATOM   3836 C  CB    . ALA A 1 476 ? 1.95419   -33.71037 -37.44851 1.000 31.17258 ? 476 ALA A CB    1 
ATOM   3837 N  N     . VAL A 1 477 ? 0.23321   -31.13937 -38.55952 1.000 22.75160 ? 477 VAL A N     1 
ATOM   3838 C  CA    . VAL A 1 477 ? -0.51277  -30.51536 -39.64753 1.000 26.73938 ? 477 VAL A CA    1 
ATOM   3839 C  C     . VAL A 1 477 ? -0.16476  -29.03836 -39.78152 1.000 26.57510 ? 477 VAL A C     1 
ATOM   3840 O  O     . VAL A 1 477 ? -0.04375  -28.52036 -40.89452 1.000 27.12090 ? 477 VAL A O     1 
ATOM   3841 C  CB    . VAL A 1 477 ? -2.02577  -30.72036 -39.42656 1.000 22.01016 ? 477 VAL A CB    1 
ATOM   3842 C  CG1   . VAL A 1 477 ? -2.82175  -30.08935 -40.55857 1.000 28.76616 ? 477 VAL A CG1   1 
ATOM   3843 C  CG2   . VAL A 1 477 ? -2.34878  -32.20236 -39.30057 1.000 20.86740 ? 477 VAL A CG2   1 
ATOM   3844 N  N     . ALA A 1 478 ? 0.01322   -28.34136 -38.65752 1.000 27.81853 ? 478 ALA A N     1 
ATOM   3845 C  CA    . ALA A 1 478 ? 0.27622   -26.90836 -38.70551 1.000 28.47527 ? 478 ALA A CA    1 
ATOM   3846 C  C     . ALA A 1 478 ? 1.72123   -26.60537 -39.08448 1.000 21.98714 ? 478 ALA A C     1 
ATOM   3847 O  O     . ALA A 1 478 ? 1.98424   -25.63136 -39.79748 1.000 24.62409 ? 478 ALA A O     1 
ATOM   3848 C  CB    . ALA A 1 478 ? -0.06480  -26.26737 -37.35951 1.000 21.79222 ? 478 ALA A CB    1 
ATOM   3849 N  N     . SER A 1 479 ? 2.66922   -27.42237 -38.61947 1.000 25.27028 ? 479 SER A N     1 
ATOM   3850 C  CA    . SER A 1 479 ? 4.07923   -27.13937 -38.87445 1.000 26.10078 ? 479 SER A CA    1 
ATOM   3851 C  C     . SER A 1 479 ? 4.41225   -27.27337 -40.35545 1.000 29.29951 ? 479 SER A C     1 
ATOM   3852 O  O     . SER A 1 479 ? 5.05426   -26.39137 -40.93643 1.000 31.86415 ? 479 SER A O     1 
ATOM   3853 C  CB    . SER A 1 479 ? 4.96321   -28.06338 -38.03644 1.000 28.18612 ? 479 SER A CB    1 
ATOM   3854 O  OG    . SER A 1 479 ? 4.67221   -29.42437 -38.29845 1.000 33.26162 ? 479 SER A OG    1 
ATOM   3855 N  N     . LYS A 1 480 ? 3.98126   -28.37136 -40.98446 1.000 29.24711 ? 480 LYS A N     1 
ATOM   3856 C  CA    . LYS A 1 480 ? 4.28028   -28.57436 -42.39945 1.000 32.86759 ? 480 LYS A CA    1 
ATOM   3857 C  C     . LYS A 1 480 ? 3.66129   -27.48735 -43.26746 1.000 35.14246 ? 480 LYS A C     1 
ATOM   3858 O  O     . LYS A 1 480 ? 4.21031   -27.14835 -44.32245 1.000 40.25192 ? 480 LYS A O     1 
ATOM   3859 C  CB    . LYS A 1 480 ? 3.79428   -29.95036 -42.85746 1.000 34.91812 ? 480 LYS A CB    1 
ATOM   3860 C  CG    . LYS A 1 480 ? 4.39927   -31.11836 -42.09946 0.000 38.93368 ? 480 LYS A CG    1 
ATOM   3861 C  CD    . LYS A 1 480 ? 4.44728   -32.38236 -42.95146 0.000 43.01882 ? 480 LYS A CD    1 
ATOM   3862 C  CE    . LYS A 1 480 ? 3.13229   -32.64235 -43.67648 0.000 45.02902 ? 480 LYS A CE    1 
ATOM   3863 N  NZ    . LYS A 1 480 ? 3.15931   -32.15735 -45.08848 0.000 46.25872 ? 480 LYS A NZ    1 
ATOM   3864 N  N     . ALA A 1 481 ? 2.52129   -26.93535 -42.84847 1.000 35.12235 ? 481 ALA A N     1 
ATOM   3865 C  CA    . ALA A 1 481 ? 1.93130   -25.82135 -43.58148 1.000 30.09064 ? 481 ALA A CA    1 
ATOM   3866 C  C     . ALA A 1 481 ? 2.80330   -24.57835 -43.46946 1.000 27.66773 ? 481 ALA A C     1 
ATOM   3867 O  O     . ALA A 1 481 ? 3.07732   -23.90635 -44.47145 1.000 31.09738 ? 481 ALA A O     1 
ATOM   3868 C  CB    . ALA A 1 481 ? 0.51929   -25.54335 -43.06550 1.000 34.88557 ? 481 ALA A CB    1 
ATOM   3869 N  N     . CYS A 1 482 ? 3.26128   -24.26336 -42.25545 1.000 28.82634 ? 482 CYS A N     1 
ATOM   3870 C  CA    . CYS A 1 482 ? 4.10328   -23.08836 -42.06044 1.000 30.57710 ? 482 CYS A CA    1 
ATOM   3871 C  C     . CYS A 1 482 ? 5.48029   -23.26536 -42.68642 1.000 29.39645 ? 482 CYS A C     1 
ATOM   3872 O  O     . CYS A 1 482 ? 6.06030   -22.29536 -43.18540 1.000 34.88005 ? 482 CYS A O     1 
ATOM   3873 C  CB    . CYS A 1 482 ? 4.23726   -22.77937 -40.56943 1.000 28.70305 ? 482 CYS A CB    1 
ATOM   3874 S  SG    . CYS A 1 482 ? 2.67325   -22.43037 -39.72946 1.000 27.67991 ? 482 CYS A SG    1 
ATOM   3875 N  N     . ILE A 1 483 ? 6.02029   -24.48736 -42.66841 1.000 30.46089 ? 483 ILE A N     1 
ATOM   3876 C  CA    . ILE A 1 483 ? 7.33930   -24.72636 -43.24939 1.000 32.18568 ? 483 ILE A CA    1 
ATOM   3877 C  C     . ILE A 1 483 ? 7.31332   -24.48736 -44.75339 1.000 33.15464 ? 483 ILE A C     1 
ATOM   3878 O  O     . ILE A 1 483 ? 8.21533   -23.84936 -45.31138 1.000 39.22167 ? 483 ILE A O     1 
ATOM   3879 C  CB    . ILE A 1 483 ? 7.82529   -26.14836 -42.90939 1.000 30.81194 ? 483 ILE A CB    1 
ATOM   3880 C  CG1   . ILE A 1 483 ? 8.19427   -26.25037 -41.42838 1.000 32.23046 ? 483 ILE A CG1   1 
ATOM   3881 C  CG2   . ILE A 1 483 ? 9.00830   -26.53636 -43.78437 1.000 32.25060 ? 483 ILE A CG2   1 
ATOM   3882 C  CD1   . ILE A 1 483 ? 8.64526   -27.63437 -41.00938 1.000 28.62459 ? 483 ILE A CD1   1 
ATOM   3883 N  N     . ALA A 1 484 ? 6.27833   -24.98735 -45.43241 1.000 32.59729 ? 484 ALA A N     1 
ATOM   3884 C  CA    . ALA A 1 484 ? 6.19035   -24.81835 -46.87941 1.000 37.20503 ? 484 ALA A CA    1 
ATOM   3885 C  C     . ALA A 1 484 ? 5.99936   -23.35834 -47.26941 1.000 37.14570 ? 484 ALA A C     1 
ATOM   3886 O  O     . ALA A 1 484 ? 6.48338   -22.93334 -48.32540 1.000 33.32576 ? 484 ALA A O     1 
ATOM   3887 C  CB    . ALA A 1 484 ? 5.05136   -25.67034 -47.43943 1.000 34.00830 ? 484 ALA A CB    1 
ATOM   3888 N  N     . ARG A 1 485 ? 5.30511   -22.57753 -46.43815 1.000 36.42285 ? 485 ARG A N     1 
ATOM   3889 C  CA    . ARG A 1 485 ? 5.09144   -21.17046 -46.75903 1.000 35.77316 ? 485 ARG A CA    1 
ATOM   3890 C  C     . ARG A 1 485 ? 6.35585   -20.34534 -46.54764 1.000 35.28237 ? 485 ARG A C     1 
ATOM   3891 O  O     . ARG A 1 485 ? 6.53694   -19.31519 -47.20668 1.000 45.20837 ? 485 ARG A O     1 
ATOM   3892 C  CB    . ARG A 1 485 ? 3.93554   -20.61415 -45.92613 1.000 30.43253 ? 485 ARG A CB    1 
ATOM   3893 C  CG    . ARG A 1 485 ? 2.60507   -21.31396 -46.17785 1.000 31.35075 ? 485 ARG A CG    1 
ATOM   3894 C  CD    . ARG A 1 485 ? 1.59159   -21.02274 -45.07780 1.000 25.79290 ? 485 ARG A CD    1 
ATOM   3895 N  NE    . ARG A 1 485 ? 1.13267   -19.63925 -45.09772 1.000 28.53209 ? 485 ARG A NE    1 
ATOM   3896 C  CZ    . ARG A 1 485 ? 0.27179   -19.12336 -44.23097 1.000 29.02164 ? 485 ARG A CZ    1 
ATOM   3897 N  NH1   . ARG A 1 485 ? -0.23847  -19.84806 -43.24843 1.000 24.44640 ? 485 ARG A NH1   1 
ATOM   3898 N  NH2   . ARG A 1 485 ? -0.08503  -17.84801 -44.35216 1.000 32.61439 ? 485 ARG A NH2   1 
ATOM   3899 N  N     . MET A 1 486 ? 7.23934   -20.77535 -45.64238 1.000 35.63966 ? 486 MET A N     1 
ATOM   3900 C  CA    . MET A 1 486 ? 8.50334   -20.06936 -45.45936 1.000 34.61940 ? 486 MET A CA    1 
ATOM   3901 C  C     . MET A 1 486 ? 9.42936   -20.28235 -46.65034 1.000 36.34974 ? 486 MET A C     1 
ATOM   3902 O  O     . MET A 1 486 ? 10.16337  -19.36935 -47.04333 1.000 38.95656 ? 486 MET A O     1 
ATOM   3903 C  CB    . MET A 1 486 ? 9.18132   -20.52236 -44.16535 1.000 35.94302 ? 486 MET A CB    1 
ATOM   3904 C  CG    . MET A 1 486 ? 8.41230   -20.17936 -42.89836 1.000 40.72913 ? 486 MET A CG    1 
ATOM   3905 S  SD    . MET A 1 486 ? 8.15330   -18.40736 -42.68536 1.000 34.62050 ? 486 MET A SD    1 
ATOM   3906 C  CE    . MET A 1 486 ? 9.84130   -17.81337 -42.72533 1.000 36.81269 ? 486 MET A CE    1 
ATOM   3907 N  N     . ALA A 1 487 ? 9.40736   -21.48135 -47.23735 1.000 36.47659 ? 487 ALA A N     1 
ATOM   3908 C  CA    . ALA A 1 487 ? 10.24538  -21.75035 -48.40034 1.000 35.23613 ? 487 ALA A CA    1 
ATOM   3909 C  C     . ALA A 1 487 ? 9.80240   -20.92934 -49.60434 1.000 40.31840 ? 487 ALA A C     1 
ATOM   3910 O  O     . ALA A 1 487 ? 10.63641  -20.49134 -50.40533 1.000 43.44853 ? 487 ALA A O     1 
ATOM   3911 C  CB    . ALA A 1 487 ? 10.22438  -23.24335 -48.73034 1.000 42.18726 ? 487 ALA A CB    1 
ATOM   3912 N  N     . ALA A 1 488 ? 8.49340   -20.71034 -49.75036 1.000 41.50535 ? 488 ALA A N     1 
ATOM   3913 C  CA    . ALA A 1 488 ? 8.00642   -19.86934 -50.83736 1.000 39.64812 ? 488 ALA A CA    1 
ATOM   3914 C  C     . ALA A 1 488 ? 8.38642   -18.41034 -50.62735 1.000 35.09109 ? 488 ALA A C     1 
ATOM   3915 O  O     . ALA A 1 488 ? 8.63044   -17.68833 -51.60035 1.000 40.99627 ? 488 ALA A O     1 
ATOM   3916 C  CB    . ALA A 1 488 ? 6.49042   -20.01133 -50.97539 1.000 36.69600 ? 488 ALA A CB    1 
ATOM   3917 N  N     . ALA A 1 489 ? 8.44540   -17.96234 -49.37135 1.000 37.24911 ? 489 ALA A N     1 
ATOM   3918 C  CA    . ALA A 1 489 ? 8.84240   -16.58534 -49.09734 1.000 38.43181 ? 489 ALA A CA    1 
ATOM   3919 C  C     . ALA A 1 489 ? 10.31641  -16.36434 -49.40732 1.000 39.43719 ? 489 ALA A C     1 
ATOM   3920 O  O     . ALA A 1 489 ? 10.68042  -15.36434 -50.03731 1.000 39.80599 ? 489 ALA A O     1 
ATOM   3921 C  CB    . ALA A 1 489 ? 8.54038   -16.23135 -47.64134 1.000 36.66692 ? 489 ALA A CB    1 
ATOM   3922 N  N     . TYR A 1 490 ? 11.17840  -17.29035 -48.97931 1.000 39.07781 ? 490 TYR A N     1 
ATOM   3923 C  CA    . TYR A 1 490 ? 12.60940  -17.15235 -49.22328 1.000 38.13347 ? 490 TYR A CA    1 
ATOM   3924 C  C     . TYR A 1 490 ? 12.96242  -17.25034 -50.70128 1.000 38.76898 ? 490 TYR A C     1 
ATOM   3925 O  O     . TYR A 1 490 ? 14.04843  -16.81135 -51.09426 1.000 43.84644 ? 490 TYR A O     1 
ATOM   3926 C  CB    . TYR A 1 490 ? 13.38239  -18.20035 -48.42028 1.000 39.96436 ? 490 TYR A CB    1 
ATOM   3927 C  CG    . TYR A 1 490 ? 13.66537  -17.78036 -46.99427 1.000 35.65430 ? 490 TYR A CG    1 
ATOM   3928 C  CD1   . TYR A 1 490 ? 12.67135  -17.82136 -46.02629 1.000 31.18351 ? 490 TYR A CD1   1 
ATOM   3929 C  CD2   . TYR A 1 490 ? 14.92636  -17.33736 -46.61825 1.000 33.51269 ? 490 TYR A CD2   1 
ATOM   3930 C  CE1   . TYR A 1 490 ? 12.92633  -17.43537 -44.72328 1.000 31.47947 ? 490 TYR A CE1   1 
ATOM   3931 C  CE2   . TYR A 1 490 ? 15.19034  -16.95037 -45.31824 1.000 31.52634 ? 490 TYR A CE2   1 
ATOM   3932 C  CZ    . TYR A 1 490 ? 14.18833  -17.00037 -44.37626 1.000 29.31345 ? 490 TYR A CZ    1 
ATOM   3933 O  OH    . TYR A 1 490 ? 14.44931  -16.61537 -43.08025 1.000 29.78518 ? 490 TYR A OH    1 
ATOM   3934 N  N     . ARG A 1 491 ? 12.07194  -17.80564 -51.52714 1.000 43.23721 ? 491 ARG A N     1 
ATOM   3935 C  CA    . ARG A 1 491 ? 12.32606  -17.84922 -52.96254 1.000 34.24190 ? 491 ARG A CA    1 
ATOM   3936 C  C     . ARG A 1 491 ? 12.29187  -16.45716 -53.58024 1.000 41.61844 ? 491 ARG A C     1 
ATOM   3937 O  O     . ARG A 1 491 ? 12.95527  -16.21521 -54.59493 1.000 50.35023 ? 491 ARG A O     1 
ATOM   3938 C  CB    . ARG A 1 491 ? 11.30991  -18.76182 -53.64931 1.000 31.48611 ? 491 ARG A CB    1 
ATOM   3939 N  N     . ARG A 1 492 ? 11.53349  -15.53721 -52.99137 1.000 44.86301 ? 492 ARG A N     1 
ATOM   3940 C  CA    . ARG A 1 492 ? 11.47864  -14.16361 -53.47825 1.000 46.06575 ? 492 ARG A CA    1 
ATOM   3941 C  C     . ARG A 1 492 ? 12.78115  -13.42896 -53.17805 1.000 45.36634 ? 492 ARG A C     1 
ATOM   3942 O  O     . ARG A 1 492 ? 13.15788  -12.49744 -53.88897 1.000 58.36971 ? 492 ARG A O     1 
ATOM   3943 C  CB    . ARG A 1 492 ? 10.29847  -13.41383 -52.85568 1.000 47.20609 ? 492 ARG A CB    1 
ATOM   3944 C  CG    . ARG A 1 492 ? 8.93133   -13.91160 -53.29839 1.000 54.88426 ? 492 ARG A CG    1 
ATOM   3945 C  CD    . ARG A 1 492 ? 7.82811   -12.99985 -52.78219 1.000 61.10962 ? 492 ARG A CD    1 
ATOM   3946 N  NE    . ARG A 1 492 ? 6.50999   -13.39430 -53.26531 1.000 57.84070 ? 492 ARG A NE    1 
ATOM   3947 C  CZ    . ARG A 1 492 ? 5.65791   -14.15087 -52.58710 1.000 59.99169 ? 492 ARG A CZ    1 
ATOM   3948 N  NH1   . ARG A 1 492 ? 5.95306   -14.61744 -51.38476 1.000 57.42035 ? 492 ARG A NH1   1 
ATOM   3949 N  NH2   . ARG A 1 492 ? 4.47903   -14.44496 -53.12790 1.000 60.72900 ? 492 ARG A NH2   1 
HETATM 3950 P  PA    . FAD B 2 .   ? 22.41695  -15.09547 -19.28613 1.000 16.23581 ? 601 FAD A PA    1 
HETATM 3951 O  O1A   . FAD B 2 .   ? 22.96693  -15.25148 -17.92412 1.000 12.59547 ? 601 FAD A O1A   1 
HETATM 3952 O  O2A   . FAD B 2 .   ? 22.41696  -16.29347 -20.15213 1.000 16.12341 ? 601 FAD A O2A   1 
HETATM 3953 O  O5B   . FAD B 2 .   ? 23.19696  -13.93847 -20.06111 1.000 14.29928 ? 601 FAD A O5B   1 
HETATM 3954 C  C5B   . FAD B 2 .   ? 23.62595  -12.81148 -19.29910 1.000 12.48021 ? 601 FAD A C5B   1 
HETATM 3955 C  C4B   . FAD B 2 .   ? 23.20097  -11.54347 -19.99710 1.000 18.54722 ? 601 FAD A C4B   1 
HETATM 3956 O  O4B   . FAD B 2 .   ? 23.56799  -11.59247 -21.39110 1.000 22.34437 ? 601 FAD A O4B   1 
HETATM 3957 C  C3B   . FAD B 2 .   ? 21.69497  -11.27847 -20.00612 1.000 14.94503 ? 601 FAD A C3B   1 
HETATM 3958 O  O3B   . FAD B 2 .   ? 21.31595  -10.69847 -18.76913 1.000 14.52342 ? 601 FAD A O3B   1 
HETATM 3959 C  C2B   . FAD B 2 .   ? 21.55299  -10.33947 -21.20712 1.000 14.59067 ? 601 FAD A C2B   1 
HETATM 3960 O  O2B   . FAD B 2 .   ? 21.86898  -8.99547  -20.92111 1.000 13.78095 ? 601 FAD A O2B   1 
HETATM 3961 C  C1B   . FAD B 2 .   ? 22.58000  -10.92746 -22.17311 1.000 18.41024 ? 601 FAD A C1B   1 
HETATM 3962 N  N9A   . FAD B 2 .   ? 21.97001  -11.87946 -23.09912 1.000 20.28522 ? 601 FAD A N9A   1 
HETATM 3963 C  C8A   . FAD B 2 .   ? 21.76401  -13.21846 -22.91213 1.000 18.40096 ? 601 FAD A C8A   1 
HETATM 3964 N  N7A   . FAD B 2 .   ? 21.17002  -13.80246 -23.92014 1.000 20.74915 ? 601 FAD A N7A   1 
HETATM 3965 C  C5A   . FAD B 2 .   ? 20.97704  -12.78045 -24.83514 1.000 18.28053 ? 601 FAD A C5A   1 
HETATM 3966 C  C6A   . FAD B 2 .   ? 20.39706  -12.76345 -26.11615 1.000 20.50923 ? 601 FAD A C6A   1 
HETATM 3967 N  N6A   . FAD B 2 .   ? 19.89006  -13.83844 -26.71016 1.000 18.09378 ? 601 FAD A N6A   1 
HETATM 3968 N  N1A   . FAD B 2 .   ? 20.35407  -11.57544 -26.76315 1.000 21.88809 ? 601 FAD A N1A   1 
HETATM 3969 C  C2A   . FAD B 2 .   ? 20.86706  -10.50045 -26.15813 1.000 18.27334 ? 601 FAD A C2A   1 
HETATM 3970 N  N3A   . FAD B 2 .   ? 21.43504  -10.39845 -24.96313 1.000 17.10998 ? 601 FAD A N3A   1 
HETATM 3971 C  C4A   . FAD B 2 .   ? 21.46103  -11.58745 -24.33913 1.000 19.82529 ? 601 FAD A C4A   1 
HETATM 3972 N  N1    . FAD B 2 .   ? 16.74900  -10.29500 -23.38300 1.000 20.73340 ? 601 FAD A N1    1 
HETATM 3973 C  C2    . FAD B 2 .   ? 16.51600  -9.19700  -22.66400 1.000 21.53793 ? 601 FAD A C2    1 
HETATM 3974 O  O2    . FAD B 2 .   ? 17.32300  -8.81300  -21.81000 1.000 19.00374 ? 601 FAD A O2    1 
HETATM 3975 N  N3    . FAD B 2 .   ? 15.41400  -8.42500  -22.87100 1.000 16.88873 ? 601 FAD A N3    1 
HETATM 3976 C  C4    . FAD B 2 .   ? 14.43500  -8.76400  -23.76500 1.000 19.78083 ? 601 FAD A C4    1 
HETATM 3977 O  O4    . FAD B 2 .   ? 13.46500  -8.00600  -23.93000 1.000 20.28284 ? 601 FAD A O4    1 
HETATM 3978 C  C4X   . FAD B 2 .   ? 14.59600  -10.00600 -24.45700 1.000 16.71698 ? 601 FAD A C4X   1 
HETATM 3979 N  N5    . FAD B 2 .   ? 13.65000  -10.40900 -25.26300 1.000 17.41288 ? 601 FAD A N5    1 
HETATM 3980 C  C5X   . FAD B 2 .   ? 13.79600  -11.63700 -25.85100 1.000 18.72958 ? 601 FAD A C5X   1 
HETATM 3981 C  C6    . FAD B 2 .   ? 12.78500  -12.09600 -26.71900 1.000 23.29684 ? 601 FAD A C6    1 
HETATM 3982 C  C7    . FAD B 2 .   ? 12.88600  -13.32000 -27.34900 1.000 25.09809 ? 601 FAD A C7    1 
HETATM 3983 C  C7M   . FAD B 2 .   ? 11.80300  -13.78100 -28.28800 1.000 23.66091 ? 601 FAD A C7M   1 
HETATM 3984 C  C8    . FAD B 2 .   ? 14.03800  -14.13500 -27.12900 1.000 18.80501 ? 601 FAD A C8    1 
HETATM 3985 C  C8M   . FAD B 2 .   ? 14.19400  -15.47700 -27.79600 1.000 22.11802 ? 601 FAD A C8M   1 
HETATM 3986 C  C9    . FAD B 2 .   ? 15.06700  -13.64800 -26.35300 1.000 16.21858 ? 601 FAD A C9    1 
HETATM 3987 C  C9A   . FAD B 2 .   ? 14.96900  -12.41600 -25.69100 1.000 19.90123 ? 601 FAD A C9A   1 
HETATM 3988 N  N10   . FAD B 2 .   ? 15.97000  -11.93000 -24.85100 1.000 22.95257 ? 601 FAD A N10   1 
HETATM 3989 C  C10   . FAD B 2 .   ? 15.80900  -10.72400 -24.20600 1.000 19.04159 ? 601 FAD A C10   1 
HETATM 3990 C  "C1'" . FAD B 2 .   ? 17.22804  -12.68045 -24.65820 1.000 18.95330 ? 601 FAD A "C1'" 1 
HETATM 3991 C  "C2'" . FAD B 2 .   ? 17.32802  -13.79645 -23.63820 1.000 21.12148 ? 601 FAD A "C2'" 1 
HETATM 3992 O  "O2'" . FAD B 2 .   ? 16.17002  -14.62445 -23.69122 1.000 24.12658 ? 601 FAD A "O2'" 1 
HETATM 3993 C  "C3'" . FAD B 2 .   ? 17.52300  -13.21045 -22.23820 1.000 23.20495 ? 601 FAD A "C3'" 1 
HETATM 3994 O  "O3'" . FAD B 2 .   ? 18.55500  -12.22946 -22.25518 1.000 16.89004 ? 601 FAD A "O3'" 1 
HETATM 3995 C  "C4'" . FAD B 2 .   ? 17.85898  -14.26346 -21.19119 1.000 18.60117 ? 601 FAD A "C4'" 1 
HETATM 3996 O  "O4'" . FAD B 2 .   ? 16.79998  -15.21646 -21.16121 1.000 20.80543 ? 601 FAD A "O4'" 1 
HETATM 3997 C  "C5'" . FAD B 2 .   ? 18.04796  -13.62646 -19.83219 1.000 17.09276 ? 601 FAD A "C5'" 1 
HETATM 3998 O  "O5'" . FAD B 2 .   ? 18.54094  -14.58047 -18.89318 1.000 14.31065 ? 601 FAD A "O5'" 1 
HETATM 3999 P  P     . FAD B 2 .   ? 19.86993  -14.28347 -18.08816 1.000 15.07222 ? 601 FAD A P     1 
HETATM 4000 O  O1P   . FAD B 2 .   ? 19.91393  -12.88248 -17.61816 1.000 11.89587 ? 601 FAD A O1P   1 
HETATM 4001 O  O2P   . FAD B 2 .   ? 19.96792  -15.38048 -17.10517 1.000 16.30816 ? 601 FAD A O2P   1 
HETATM 4002 O  O3P   . FAD B 2 .   ? 20.95795  -14.48647 -19.22715 1.000 15.51508 ? 601 FAD A O3P   1 
HETATM 4003 CL CL    . CL  C 3 .   ? 12.11410  -30.33641 -30.67734 1.000 31.09538 ? 602 CL  A CL    1 
HETATM 4004 O  O     . HOH D 4 .   ? 13.03674  13.69848  -2.21817  1.000 25.94379 ? 701 HOH A O     1 
HETATM 4005 O  O     . HOH D 4 .   ? 18.35380  0.58649   -7.86213  1.000 16.45322 ? 702 HOH A O     1 
HETATM 4006 O  O     . HOH D 4 .   ? 14.32494  10.70453  -15.35916 1.000 25.18618 ? 703 HOH A O     1 
HETATM 4007 O  O     . HOH D 4 .   ? -1.67865  -16.39634 -45.47550 1.000 36.14696 ? 704 HOH A O     1 
HETATM 4008 O  O     . HOH D 4 .   ? 5.53990   -9.76746  -15.72937 1.000 25.33681 ? 705 HOH A O     1 
HETATM 4009 O  O     . HOH D 4 .   ? 9.56026   -22.49738 -40.24735 1.000 33.00474 ? 706 HOH A O     1 
HETATM 4010 O  O     . HOH D 4 .   ? 11.56883  -28.54948 -13.36934 1.000 27.62972 ? 707 HOH A O     1 
HETATM 4011 O  O     . HOH D 4 .   ? 30.76085  5.26948   -10.65893 1.000 25.78715 ? 708 HOH A O     1 
HETATM 4012 O  O     . HOH D 4 .   ? 19.63129  -11.33339 -41.18316 1.000 31.66302 ? 709 HOH A O     1 
HETATM 4013 O  O     . HOH D 4 .   ? -4.60800  -30.33441 -24.36859 1.000 19.79651 ? 710 HOH A O     1 
HETATM 4014 O  O     . HOH D 4 .   ? 23.35177  15.00147  -3.94701  1.000 21.98493 ? 711 HOH A O     1 
HETATM 4015 O  O     . HOH D 4 .   ? -14.02110 -24.51442 -17.06672 1.000 28.87799 ? 712 HOH A O     1 
HETATM 4016 O  O     . HOH D 4 .   ? 5.12802   10.22956  -20.85130 1.000 35.76905 ? 713 HOH A O     1 
HETATM 4017 O  O     . HOH D 4 .   ? 17.03034  -20.80237 -45.55423 1.000 37.90783 ? 714 HOH A O     1 
HETATM 4018 O  O     . HOH D 4 .   ? 27.64913  6.12055   -28.69697 1.000 25.61216 ? 715 HOH A O     1 
HETATM 4019 O  O     . HOH D 4 .   ? 14.61473  -3.66452  -3.63521  1.000 22.39757 ? 716 HOH A O     1 
HETATM 4020 O  O     . HOH D 4 .   ? 38.18204  -8.39548  -24.27686 1.000 25.41711 ? 717 HOH A O     1 
HETATM 4021 O  O     . HOH D 4 .   ? 18.97975  -10.98452 -6.02517  1.000 21.34168 ? 718 HOH A O     1 
HETATM 4022 O  O     . HOH D 4 .   ? 1.95490   -9.79445  -15.25542 1.000 27.84221 ? 719 HOH A O     1 
HETATM 4023 O  O     . HOH D 4 .   ? 25.40104  4.50053   -22.67101 1.000 22.09926 ? 720 HOH A O     1 
HETATM 4024 O  O     . HOH D 4 .   ? 24.68017  6.57656   -30.89602 1.000 42.44779 ? 721 HOH A O     1 
HETATM 4025 O  O     . HOH D 4 .   ? 39.35797  1.86949   -18.73581 1.000 19.31516 ? 722 HOH A O     1 
HETATM 4026 O  O     . HOH D 4 .   ? 7.09784   16.18452  -8.72525  1.000 29.91589 ? 723 HOH A O     1 
HETATM 4027 O  O     . HOH D 4 .   ? 13.60343  -11.74835 -50.58425 1.000 25.11186 ? 724 HOH A O     1 
HETATM 4028 O  O     . HOH D 4 .   ? 36.38009  -13.74247 -28.17091 1.000 13.05076 ? 725 HOH A O     1 
HETATM 4029 O  O     . HOH D 4 .   ? 5.53839   -17.19334 -48.56239 1.000 37.51178 ? 726 HOH A O     1 
HETATM 4030 O  O     . HOH D 4 .   ? 17.88096  -17.56046 -20.32821 1.000 16.21871 ? 727 HOH A O     1 
HETATM 4031 O  O     . HOH D 4 .   ? 11.35692  -21.36146 -17.89132 1.000 21.60254 ? 728 HOH A O     1 
HETATM 4032 O  O     . HOH D 4 .   ? 9.00429   -10.51937 -41.27332 1.000 37.96610 ? 729 HOH A O     1 
HETATM 4033 O  O     . HOH D 4 .   ? 16.94908  -0.99644  -26.19316 1.000 20.12627 ? 730 HOH A O     1 
HETATM 4034 O  O     . HOH D 4 .   ? 26.61103  -5.80447  -23.22703 1.000 21.16867 ? 731 HOH A O     1 
HETATM 4035 O  O     . HOH D 4 .   ? 33.20695  3.34650   -16.91990 1.000 39.45035 ? 732 HOH A O     1 
HETATM 4036 O  O     . HOH D 4 .   ? 8.55506   -26.35942 -28.09138 1.000 23.81464 ? 733 HOH A O     1 
HETATM 4037 O  O     . HOH D 4 .   ? 29.48125  5.32357   -36.33795 1.000 36.01632 ? 734 HOH A O     1 
HETATM 4038 O  O     . HOH D 4 .   ? 13.95803  -0.79145  -23.14721 1.000 19.35364 ? 735 HOH A O     1 
HETATM 4039 O  O     . HOH D 4 .   ? 24.99892  4.73951   -15.07302 1.000 20.17211 ? 736 HOH A O     1 
HETATM 4040 O  O     . HOH D 4 .   ? 5.02937   -14.73334 -46.93839 1.000 29.96187 ? 737 HOH A O     1 
HETATM 4041 O  O     . HOH D 4 .   ? 33.31292  19.75249  -13.38684 1.000 17.73542 ? 738 HOH A O     1 
HETATM 4042 O  O     . HOH D 4 .   ? 34.07006  -7.47847  -25.55792 1.000 30.98283 ? 739 HOH A O     1 
HETATM 4043 O  O     . HOH D 4 .   ? 32.72200  6.07451   -20.43189 1.000 26.82624 ? 740 HOH A O     1 
HETATM 4044 O  O     . HOH D 4 .   ? 20.48798  6.62553   -18.78508 1.000 23.38605 ? 741 HOH A O     1 
HETATM 4045 O  O     . HOH D 4 .   ? 21.29189  -27.05048 -17.07619 1.000 13.40753 ? 742 HOH A O     1 
HETATM 4046 O  O     . HOH D 4 .   ? 11.21872  8.39748   -1.43121  1.000 19.81003 ? 743 HOH A O     1 
HETATM 4047 O  O     . HOH D 4 .   ? 21.81905  -17.32045 -26.49214 1.000 29.31441 ? 744 HOH A O     1 
HETATM 4048 O  O     . HOH D 4 .   ? -10.94111 -24.14242 -16.59467 1.000 30.07921 ? 745 HOH A O     1 
HETATM 4049 O  O     . HOH D 4 .   ? -0.87904  -15.50943 -19.89348 1.000 21.85211 ? 746 HOH A O     1 
HETATM 4050 O  O     . HOH D 4 .   ? 38.76096  -3.56051  -18.72384 1.000 21.99749 ? 747 HOH A O     1 
HETATM 4051 O  O     . HOH D 4 .   ? 22.80127  -12.51340 -39.83711 1.000 37.25411 ? 748 HOH A O     1 
HETATM 4052 O  O     . HOH D 4 .   ? 11.09913  -2.81142  -29.78426 1.000 11.80359 ? 749 HOH A O     1 
HETATM 4053 O  O     . HOH D 4 .   ? 33.54899  18.40550  -17.81184 1.000 37.24776 ? 750 HOH A O     1 
HETATM 4054 O  O     . HOH D 4 .   ? 22.05707  2.71155   -25.03607 1.000 19.58853 ? 751 HOH A O     1 
HETATM 4055 O  O     . HOH D 4 .   ? 15.45373  -11.02151 -4.45822  1.000 29.26204 ? 752 HOH A O     1 
HETATM 4056 O  O     . HOH D 4 .   ? 22.13168  -0.40854  0.24892   1.000 28.17741 ? 753 HOH A O     1 
HETATM 4057 O  O     . HOH D 4 .   ? -8.75086  -24.02737 -32.85864 1.000 19.49793 ? 754 HOH A O     1 
HETATM 4058 O  O     . HOH D 4 .   ? 11.46701  10.28755  -20.16820 1.000 20.71793 ? 755 HOH A O     1 
HETATM 4059 O  O     . HOH D 4 .   ? -0.51511  -5.48945  -14.59444 1.000 24.84911 ? 756 HOH A O     1 
HETATM 4060 O  O     . HOH D 4 .   ? 39.41101  -15.11749 -23.22887 1.000 21.04331 ? 757 HOH A O     1 
HETATM 4061 O  O     . HOH D 4 .   ? 20.24582  -25.00550 -12.24620 1.000 26.63863 ? 758 HOH A O     1 
HETATM 4062 O  O     . HOH D 4 .   ? 10.23972  23.36548  0.12982   1.000 19.61467 ? 759 HOH A O     1 
HETATM 4063 O  O     . HOH D 4 .   ? -5.01019  -39.95545 -12.97763 1.000 31.03788 ? 760 HOH A O     1 
HETATM 4064 O  O     . HOH D 4 .   ? 30.08306  14.85052  -22.84890 1.000 25.53934 ? 761 HOH A O     1 
HETATM 4065 O  O     . HOH D 4 .   ? 34.21792  12.32649  -14.29385 1.000 25.47008 ? 762 HOH A O     1 
HETATM 4066 O  O     . HOH D 4 .   ? 25.25995  -1.36748  -17.81303 1.000 19.47257 ? 763 HOH A O     1 
HETATM 4067 O  O     . HOH D 4 .   ? 27.32222  -15.51542 -36.99605 1.000 27.48285 ? 764 HOH A O     1 
HETATM 4068 O  O     . HOH D 4 .   ? 27.87076  0.17846   -4.96999  1.000 25.69371 ? 765 HOH A O     1 
HETATM 4069 O  O     . HOH D 4 .   ? 41.91097  -16.81050 -20.62584 1.000 29.79660 ? 766 HOH A O     1 
HETATM 4070 O  O     . HOH D 4 .   ? 22.36092  7.50651   -14.85205 1.000 19.19538 ? 767 HOH A O     1 
HETATM 4071 O  O     . HOH D 4 .   ? 4.56276   -16.13749 -6.91840  1.000 32.71506 ? 768 HOH A O     1 
HETATM 4072 O  O     . HOH D 4 .   ? 33.91482  12.09346  -7.85585  1.000 23.30055 ? 769 HOH A O     1 
HETATM 4073 O  O     . HOH D 4 .   ? 14.40879  -26.53949 -10.39229 1.000 26.32986 ? 770 HOH A O     1 
HETATM 4074 O  O     . HOH D 4 .   ? -4.57980  -27.94136 -37.21759 1.000 30.44370 ? 771 HOH A O     1 
HETATM 4075 O  O     . HOH D 4 .   ? 24.43073  -0.70854  -3.10305  1.000 20.70236 ? 772 HOH A O     1 
HETATM 4076 O  O     . HOH D 4 .   ? 14.81321  1.45559   -34.36118 1.000 31.90823 ? 773 HOH A O     1 
HETATM 4077 O  O     . HOH D 4 .   ? -2.71506  -7.47043  -17.97048 1.000 19.94357 ? 774 HOH A O     1 
HETATM 4078 O  O     . HOH D 4 .   ? 32.15305  8.26752   -22.97190 1.000 21.98573 ? 775 HOH A O     1 
HETATM 4079 O  O     . HOH D 4 .   ? -3.68280  -11.18037 -35.04151 1.000 40.07907 ? 776 HOH A O     1 
HETATM 4080 O  O     . HOH D 4 .   ? 6.10777   -29.13248 -8.95143  1.000 23.64689 ? 777 HOH A O     1 
HETATM 4081 O  O     . HOH D 4 .   ? 22.55180  27.40547  -4.83597  1.000 27.66056 ? 778 HOH A O     1 
HETATM 4082 O  O     . HOH D 4 .   ? 10.61097  0.67955   -18.91125 1.000 31.83803 ? 779 HOH A O     1 
HETATM 4083 O  O     . HOH D 4 .   ? 13.12796  8.48253   -16.93619 1.000 21.04404 ? 780 HOH A O     1 
HETATM 4084 O  O     . HOH D 4 .   ? 7.84094   7.20754   -16.39027 1.000 33.26572 ? 781 HOH A O     1 
HETATM 4085 O  O     . HOH D 4 .   ? 36.00302  -15.55648 -24.10492 1.000 14.50775 ? 782 HOH A O     1 
HETATM 4086 O  O     . HOH D 4 .   ? 3.91471   -1.14550  -2.08936  1.000 35.87953 ? 783 HOH A O     1 
HETATM 4087 O  O     . HOH D 4 .   ? 25.75809  22.82554  -23.78594 1.000 19.02414 ? 784 HOH A O     1 
HETATM 4088 O  O     . HOH D 4 .   ? 38.19903  -11.29249 -23.83287 1.000 22.43049 ? 785 HOH A O     1 
HETATM 4089 O  O     . HOH D 4 .   ? 34.04793  9.47349   -15.14786 1.000 17.63130 ? 786 HOH A O     1 
HETATM 4090 O  O     . HOH D 4 .   ? 24.08622  -13.63241 -36.75510 1.000 26.61769 ? 787 HOH A O     1 
HETATM 4091 O  O     . HOH D 4 .   ? 26.75370  -9.19054  -2.45104  1.000 31.10979 ? 788 HOH A O     1 
HETATM 4092 O  O     . HOH D 4 .   ? 19.19509  -23.44243 -29.24921 1.000 14.81816 ? 789 HOH A O     1 
HETATM 4093 O  O     . HOH D 4 .   ? 12.41541  -9.66035  -48.65126 1.000 36.45863 ? 790 HOH A O     1 
HETATM 4094 O  O     . HOH D 4 .   ? 37.36395  -6.12950  -18.53387 1.000 29.69716 ? 791 HOH A O     1 
HETATM 4095 O  O     . HOH D 4 .   ? 20.61606  -21.66644 -27.63418 1.000 3.91192  ? 792 HOH A O     1 
HETATM 4096 O  O     . HOH D 4 .   ? 35.12896  5.45450   -17.34886 1.000 38.22273 ? 793 HOH A O     1 
HETATM 4097 O  O     . HOH D 4 .   ? 30.64429  6.15558   -39.17893 1.000 32.59860 ? 794 HOH A O     1 
HETATM 4098 O  O     . HOH D 4 .   ? 25.74671  -4.06454  -2.39504  1.000 18.77872 ? 795 HOH A O     1 
HETATM 4099 O  O     . HOH D 4 .   ? 20.04120  -23.53341 -36.55519 1.000 23.39318 ? 796 HOH A O     1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    C C   . GLY A 3   ? 0.62027 0.53615 0.69886 -0.05555 0.00607  -0.04003 3   GLY A C   
2    O O   . GLY A 3   ? 0.65245 0.56862 0.74379 -0.06115 0.00535  -0.04705 3   GLY A O   
3    N N   . VAL A 4   ? 0.61340 0.53763 0.68541 -0.04848 -0.00030 -0.03944 4   VAL A N   
4    C CA  . VAL A 4   ? 0.52950 0.46957 0.60835 -0.04734 -0.00486 -0.04206 4   VAL A CA  
5    C C   . VAL A 4   ? 0.47134 0.41661 0.54443 -0.04507 -0.00167 -0.03505 4   VAL A C   
6    O O   . VAL A 4   ? 0.46784 0.40488 0.53183 -0.04411 0.00327  -0.02877 4   VAL A O   
7    C CB  . VAL A 4   ? 0.47705 0.42115 0.55097 -0.04136 -0.01328 -0.04620 4   VAL A CB  
8    C CG1 . VAL A 4   ? 0.39411 0.33243 0.47301 -0.04333 -0.01717 -0.05389 4   VAL A CG1 
9    C CG2 . VAL A 4   ? 0.40034 0.34019 0.45889 -0.03453 -0.01321 -0.04077 4   VAL A CG2 
10   N N   . LYS A 5   ? 0.41937 0.37742 0.49691 -0.04371 -0.00499 -0.03637 5   LYS A N   
11   C CA  . LYS A 5   ? 0.33942 0.30301 0.41263 -0.04191 -0.00246 -0.03073 5   LYS A CA  
12   C C   . LYS A 5   ? 0.30636 0.27321 0.36899 -0.03511 -0.00686 -0.02868 5   LYS A C   
13   O O   . LYS A 5   ? 0.30188 0.27476 0.36525 -0.03255 -0.01233 -0.03244 5   LYS A O   
14   C CB  . LYS A 5   ? 0.27877 0.25344 0.36421 -0.04513 -0.00217 -0.03347 5   LYS A CB  
15   C CG  . LYS A 5   ? 0.28211 0.26247 0.36264 -0.04286 -0.00033 -0.02838 5   LYS A CG  
16   C CD  . LYS A 5   ? 0.22701 0.21680 0.32007 -0.04629 0.00142  -0.03098 5   LYS A CD  
17   C CE  . LYS A 5   ? 0.24565 0.23979 0.33278 -0.04387 0.00325  -0.02611 5   LYS A CE  
18   N NZ  . LYS A 5   ? 0.25186 0.25078 0.33208 -0.03813 -0.00312 -0.02599 5   LYS A NZ  
19   N N   . ASN A 6   ? 0.31349 0.27582 0.36614 -0.03206 -0.00432 -0.02301 6   ASN A N   
20   C CA  . ASN A 6   ? 0.30556 0.27193 0.35021 -0.02656 -0.00671 -0.02086 6   ASN A CA  
21   C C   . ASN A 6   ? 0.27008 0.23982 0.31210 -0.02624 -0.00370 -0.01576 6   ASN A C   
22   O O   . ASN A 6   ? 0.25833 0.22164 0.29643 -0.02653 -0.00024 -0.01202 6   ASN A O   
23   C CB  . ASN A 6   ? 0.32090 0.28004 0.35784 -0.02247 -0.00739 -0.02034 6   ASN A CB  
24   C CG  . ASN A 6   ? 0.37452 0.32919 0.41258 -0.02239 -0.01053 -0.02575 6   ASN A CG  
25   O OD1 . ASN A 6   ? 0.37958 0.33905 0.41983 -0.02207 -0.01443 -0.02997 6   ASN A OD1 
26   N ND2 . ASN A 6   ? 0.36854 0.31281 0.40394 -0.02221 -0.00925 -0.02587 6   ASN A ND2 
27   N N   . SER A 7   ? 0.27470 0.25311 0.31755 -0.02528 -0.00525 -0.01573 7   SER A N   
28   C CA  . SER A 7   ? 0.30313 0.28527 0.34468 -0.02556 -0.00283 -0.01195 7   SER A CA  
29   C C   . SER A 7   ? 0.25467 0.24094 0.29058 -0.02166 -0.00426 -0.01023 7   SER A C   
30   O O   . SER A 7   ? 0.21633 0.20391 0.25005 -0.01921 -0.00653 -0.01217 7   SER A O   
31   C CB  . SER A 7   ? 0.25578 0.24438 0.30480 -0.02855 -0.00255 -0.01372 7   SER A CB  
32   O OG  . SER A 7   ? 0.20799 0.20180 0.25862 -0.02680 -0.00703 -0.01728 7   SER A OG  
33   N N   . ILE A 8   ? 0.28707 0.27486 0.32048 -0.02129 -0.00249 -0.00687 8   ILE A N   
34   C CA  . ILE A 8   ? 0.26223 0.25482 0.29258 -0.01863 -0.00334 -0.00573 8   ILE A CA  
35   C C   . ILE A 8   ? 0.24646 0.24390 0.27795 -0.02025 -0.00255 -0.00471 8   ILE A C   
36   O O   . ILE A 8   ? 0.27588 0.27164 0.30760 -0.02205 -0.00048 -0.00307 8   ILE A O   
37   C CB  . ILE A 8   ? 0.25897 0.24879 0.28529 -0.01563 -0.00325 -0.00360 8   ILE A CB  
38   C CG1 . ILE A 8   ? 0.25140 0.23567 0.27632 -0.01333 -0.00404 -0.00478 8   ILE A CG1 
39   C CG2 . ILE A 8   ? 0.23304 0.22965 0.25934 -0.01364 -0.00411 -0.00359 8   ILE A CG2 
40   C CD1 . ILE A 8   ? 0.31102 0.29266 0.33227 -0.00908 -0.00493 -0.00331 8   ILE A CD1 
41   N N   . ILE A 9   ? 0.19758 0.19968 0.22874 -0.01953 -0.00358 -0.00565 9   ILE A N   
42   C CA  . ILE A 9   ? 0.19091 0.19675 0.22222 -0.02052 -0.00302 -0.00485 9   ILE A CA  
43   C C   . ILE A 9   ? 0.22304 0.23134 0.25201 -0.01919 -0.00278 -0.00379 9   ILE A C   
44   O O   . ILE A 9   ? 0.24438 0.25438 0.27254 -0.01835 -0.00273 -0.00484 9   ILE A O   
45   C CB  . ILE A 9   ? 0.18948 0.19703 0.22156 -0.02062 -0.00446 -0.00694 9   ILE A CB  
46   C CG1 . ILE A 9   ? 0.23788 0.24797 0.26846 -0.02086 -0.00387 -0.00605 9   ILE A CG1 
47   C CG2 . ILE A 9   ? 0.27223 0.27787 0.30089 -0.01862 -0.00588 -0.00870 9   ILE A CG2 
48   C CD1 . ILE A 9   ? 0.26355 0.27492 0.29660 -0.02246 -0.00234 -0.00495 9   ILE A CD1 
49   N N   . TRP A 10  ? 0.29841 0.30653 0.32619 -0.01902 -0.00242 -0.00206 10  TRP A N   
50   C CA  . TRP A 10  ? 0.24545 0.25685 0.27276 -0.01759 -0.00325 -0.00208 10  TRP A CA  
51   C C   . TRP A 10  ? 0.23247 0.24732 0.26017 -0.01919 -0.00271 -0.00255 10  TRP A C   
52   O O   . TRP A 10  ? 0.21043 0.22436 0.23678 -0.02044 -0.00211 -0.00176 10  TRP A O   
53   C CB  . TRP A 10  ? 0.23079 0.23916 0.25473 -0.01567 -0.00433 -0.00052 10  TRP A CB  
54   C CG  . TRP A 10  ? 0.25995 0.27235 0.28490 -0.01312 -0.00683 -0.00174 10  TRP A CG  
55   C CD1 . TRP A 10  ? 0.31889 0.33774 0.34948 -0.01301 -0.00708 -0.00427 10  TRP A CD1 
56   C CD2 . TRP A 10  ? 0.30328 0.31353 0.32383 -0.01012 -0.00952 -0.00109 10  TRP A CD2 
57   N NE1 . TRP A 10  ? 0.24149 0.26424 0.27424 -0.01053 -0.01001 -0.00591 10  TRP A NE1 
58   C CE2 . TRP A 10  ? 0.23874 0.25612 0.26467 -0.00819 -0.01234 -0.00407 10  TRP A CE2 
59   C CE3 . TRP A 10  ? 0.28978 0.29209 0.30171 -0.00871 -0.00961 0.00148  10  TRP A CE3 
60   C CZ2 . TRP A 10  ? 0.24030 0.25807 0.26398 -0.00429 -0.01678 -0.00511 10  TRP A CZ2 
61   C CZ3 . TRP A 10  ? 0.29475 0.29524 0.30139 -0.00452 -0.01350 0.00127  10  TRP A CZ3 
62   C CH2 . TRP A 10  ? 0.33686 0.34545 0.34961 -0.00204 -0.01780 -0.00225 10  TRP A CH2 
63   N N   . PHE A 11  ? 0.22547 0.24370 0.25518 -0.01924 -0.00231 -0.00405 11  PHE A N   
64   C CA  . PHE A 11  ? 0.23568 0.25562 0.26537 -0.02113 -0.00124 -0.00464 11  PHE A CA  
65   C C   . PHE A 11  ? 0.23322 0.25740 0.26591 -0.02099 -0.00247 -0.00593 11  PHE A C   
66   O O   . PHE A 11  ? 0.31010 0.33835 0.34753 -0.02021 -0.00261 -0.00785 11  PHE A O   
67   C CB  . PHE A 11  ? 0.24325 0.26222 0.27216 -0.02199 0.00120  -0.00560 11  PHE A CB  
68   C CG  . PHE A 11  ? 0.22471 0.23905 0.24934 -0.02146 0.00103  -0.00505 11  PHE A CG  
69   C CD1 . PHE A 11  ? 0.18635 0.19856 0.20843 -0.02192 0.00053  -0.00457 11  PHE A CD1 
70   C CD2 . PHE A 11  ? 0.20208 0.21433 0.22548 -0.01997 0.00078  -0.00568 11  PHE A CD2 
71   C CE1 . PHE A 11  ? 0.18862 0.19760 0.20797 -0.02061 -0.00085 -0.00502 11  PHE A CE1 
72   C CE2 . PHE A 11  ? 0.19082 0.19917 0.21062 -0.01900 -0.00065 -0.00615 11  PHE A CE2 
73   C CZ  . PHE A 11  ? 0.19096 0.19813 0.20922 -0.01917 -0.00178 -0.00598 11  PHE A CZ  
74   N N   . ARG A 12  ? 0.26202 0.28557 0.29242 -0.02143 -0.00362 -0.00548 12  ARG A N   
75   C CA  . ARG A 12  ? 0.24411 0.27137 0.27693 -0.02157 -0.00551 -0.00761 12  ARG A CA  
76   C C   . ARG A 12  ? 0.29556 0.32194 0.32765 -0.02452 -0.00374 -0.00831 12  ARG A C   
77   O O   . ARG A 12  ? 0.36978 0.39871 0.40633 -0.02680 -0.00210 -0.01051 12  ARG A O   
78   C CB  . ARG A 12  ? 0.29717 0.32248 0.32540 -0.01877 -0.00889 -0.00687 12  ARG A CB  
79   C CG  . ARG A 12  ? 0.26510 0.28793 0.29124 -0.01544 -0.01035 -0.00547 12  ARG A CG  
80   C CD  . ARG A 12  ? 0.23850 0.25464 0.25911 -0.01588 -0.00784 -0.00221 12  ARG A CD  
81   N NE  . ARG A 12  ? 0.25947 0.27169 0.27396 -0.01636 -0.00698 -0.00086 12  ARG A NE  
82   C CZ  . ARG A 12  ? 0.33947 0.34616 0.34602 -0.01384 -0.00806 0.00054  12  ARG A CZ  
83   N NH1 . ARG A 12  ? 0.39074 0.39459 0.39404 -0.01018 -0.01085 0.00091  12  ARG A NH1 
84   N NH2 . ARG A 12  ? 0.41991 0.42275 0.42043 -0.01447 -0.00617 0.00157  12  ARG A NH2 
85   N N   . LYS A 13  ? 0.33617 0.35848 0.36290 -0.02458 -0.00348 -0.00668 13  LYS A N   
86   C CA  . LYS A 13  ? 0.28748 0.30697 0.31212 -0.02651 -0.00154 -0.00681 13  LYS A CA  
87   C C   . LYS A 13  ? 0.23385 0.25006 0.25622 -0.02596 0.00005  -0.00507 13  LYS A C   
88   O O   . LYS A 13  ? 0.21908 0.23579 0.24263 -0.02494 -0.00006 -0.00436 13  LYS A O   
89   C CB  . LYS A 13  ? 0.30492 0.32265 0.32570 -0.02619 -0.00274 -0.00711 13  LYS A CB  
90   C CG  . LYS A 13  ? 0.19671 0.21731 0.21909 -0.02623 -0.00562 -0.00978 13  LYS A CG  
91   C CD  . LYS A 13  ? 0.32530 0.34255 0.34149 -0.02538 -0.00681 -0.01014 13  LYS A CD  
92   C CE  . LYS A 13  ? 0.41813 0.43788 0.43540 -0.02506 -0.01088 -0.01375 13  LYS A CE  
93   N NZ  . LYS A 13  ? 0.33540 0.35057 0.34470 -0.02386 -0.01208 -0.01440 13  LYS A NZ  
94   N N   . GLY A 14  ? 0.34909 0.36181 0.36831 -0.02615 0.00090  -0.00489 14  GLY A N   
95   C CA  . GLY A 14  ? 0.33837 0.34861 0.35605 -0.02472 0.00103  -0.00421 14  GLY A CA  
96   C C   . GLY A 14  ? 0.33678 0.34507 0.35324 -0.02447 0.00170  -0.00421 14  GLY A C   
97   O O   . GLY A 14  ? 0.31916 0.32718 0.33580 -0.02287 0.00056  -0.00412 14  GLY A O   
98   N N   . LEU A 15  ? 0.28065 0.28721 0.29587 -0.02619 0.00391  -0.00468 15  LEU A N   
99   C CA  . LEU A 15  ? 0.24560 0.24880 0.25780 -0.02601 0.00598  -0.00461 15  LEU A CA  
100  C C   . LEU A 15  ? 0.25194 0.24711 0.25564 -0.02376 0.00566  -0.00394 15  LEU A C   
101  O O   . LEU A 15  ? 0.25426 0.24208 0.25122 -0.02441 0.00854  -0.00355 15  LEU A O   
102  C CB  . LEU A 15  ? 0.33634 0.33978 0.35050 -0.02914 0.00988  -0.00567 15  LEU A CB  
103  C CG  . LEU A 15  ? 0.22591 0.23792 0.24928 -0.03066 0.00883  -0.00743 15  LEU A CG  
104  C CD1 . LEU A 15  ? 0.24069 0.25402 0.26859 -0.03434 0.01265  -0.00970 15  LEU A CD1 
105  C CD2 . LEU A 15  ? 0.28286 0.29976 0.31020 -0.02861 0.00710  -0.00750 15  LEU A CD2 
106  N N   . ARG A 16  ? 0.21291 0.20887 0.21682 -0.02094 0.00213  -0.00412 16  ARG A N   
107  C CA  . ARG A 16  ? 0.23582 0.22531 0.23273 -0.01755 -0.00001 -0.00439 16  ARG A CA  
108  C C   . ARG A 16  ? 0.27848 0.27108 0.27867 -0.01494 -0.00403 -0.00584 16  ARG A C   
109  O O   . ARG A 16  ? 0.26643 0.26570 0.27464 -0.01633 -0.00452 -0.00625 16  ARG A O   
110  C CB  . ARG A 16  ? 0.23426 0.22247 0.23067 -0.01691 -0.00079 -0.00453 16  ARG A CB  
111  C CG  . ARG A 16  ? 0.30212 0.29850 0.30758 -0.01732 -0.00229 -0.00534 16  ARG A CG  
112  C CD  . ARG A 16  ? 0.26102 0.25585 0.26550 -0.01645 -0.00235 -0.00579 16  ARG A CD  
113  N NE  . ARG A 16  ? 0.30067 0.30237 0.31279 -0.01650 -0.00275 -0.00673 16  ARG A NE  
114  C CZ  . ARG A 16  ? 0.24486 0.24984 0.25956 -0.01893 -0.00077 -0.00614 16  ARG A CZ  
115  N NH1 . ARG A 16  ? 0.23652 0.24029 0.24881 -0.02135 0.00055  -0.00530 16  ARG A NH1 
116  N NH2 . ARG A 16  ? 0.27721 0.28651 0.29694 -0.01879 -0.00003 -0.00677 16  ARG A NH2 
117  N N   . LEU A 17  ? 0.26686 0.25359 0.26019 -0.01094 -0.00711 -0.00690 17  LEU A N   
118  C CA  . LEU A 17  ? 0.29645 0.28644 0.29405 -0.00816 -0.01207 -0.00957 17  LEU A CA  
119  C C   . LEU A 17  ? 0.25345 0.24667 0.25621 -0.00567 -0.01569 -0.01176 17  LEU A C   
120  O O   . LEU A 17  ? 0.27363 0.27389 0.28646 -0.00541 -0.01848 -0.01456 17  LEU A O   
121  C CB  . LEU A 17  ? 0.29141 0.27325 0.27817 -0.00434 -0.01451 -0.01049 17  LEU A CB  
122  C CG  . LEU A 17  ? 0.28067 0.26280 0.26708 -0.00564 -0.01306 -0.01055 17  LEU A CG  
123  C CD1 . LEU A 17  ? 0.22078 0.20331 0.20718 -0.00971 -0.00658 -0.00787 17  LEU A CD1 
124  C CD2 . LEU A 17  ? 0.30557 0.27817 0.27900 -0.00095 -0.01589 -0.01188 17  LEU A CD2 
125  N N   . HIS A 18  ? 0.29071 0.27893 0.28761 -0.00395 -0.01530 -0.01095 18  HIS A N   
126  C CA  . HIS A 18  ? 0.30952 0.30137 0.31209 -0.00118 -0.01827 -0.01331 18  HIS A CA  
127  C C   . HIS A 18  ? 0.25938 0.25978 0.27282 -0.00528 -0.01468 -0.01295 18  HIS A C   
128  O O   . HIS A 18  ? 0.27390 0.27356 0.28553 -0.00904 -0.01043 -0.01030 18  HIS A O   
129  C CB  . HIS A 18  ? 0.29782 0.27939 0.28862 0.00264  -0.01898 -0.01245 18  HIS A CB  
130  C CG  . HIS A 18  ? 0.32625 0.30444 0.31373 -0.00115 -0.01352 -0.00956 18  HIS A CG  
131  N ND1 . HIS A 18  ? 0.27766 0.25037 0.25853 -0.00493 -0.00888 -0.00680 18  HIS A ND1 
132  C CD2 . HIS A 18  ? 0.30966 0.28952 0.30030 -0.00178 -0.01206 -0.00972 18  HIS A CD2 
133  C CE1 . HIS A 18  ? 0.25253 0.22405 0.23342 -0.00793 -0.00539 -0.00570 18  HIS A CE1 
134  N NE2 . HIS A 18  ? 0.24063 0.21575 0.22633 -0.00594 -0.00735 -0.00726 18  HIS A NE2 
135  N N   . ASP A 19  ? 0.34484 0.35318 0.36951 -0.00437 -0.01637 -0.01606 19  ASP A N   
136  C CA  . ASP A 19  ? 0.23209 0.24722 0.26570 -0.00776 -0.01223 -0.01591 19  ASP A CA  
137  C C   . ASP A 19  ? 0.21747 0.23359 0.25139 -0.01263 -0.00831 -0.01306 19  ASP A C   
138  O O   . ASP A 19  ? 0.31478 0.32910 0.34474 -0.01485 -0.00510 -0.01059 19  ASP A O   
139  C CB  . ASP A 19  ? 0.24834 0.26044 0.27763 -0.00676 -0.01037 -0.01508 19  ASP A CB  
140  C CG  . ASP A 19  ? 0.32112 0.33918 0.35793 -0.00922 -0.00611 -0.01544 19  ASP A CG  
141  O OD1 . ASP A 19  ? 0.30365 0.32827 0.35012 -0.01127 -0.00451 -0.01676 19  ASP A OD1 
142  O OD2 . ASP A 19  ? 0.30059 0.31567 0.33278 -0.00922 -0.00393 -0.01447 19  ASP A OD2 
143  N N   . ASN A 20  ? 0.31159 0.33017 0.35004 -0.01376 -0.00929 -0.01392 20  ASN A N   
144  C CA  . ASN A 20  ? 0.28985 0.30857 0.32844 -0.01732 -0.00638 -0.01159 20  ASN A CA  
145  C C   . ASN A 20  ? 0.25388 0.27737 0.30272 -0.01928 -0.00545 -0.01355 20  ASN A C   
146  O O   . ASN A 20  ? 0.20713 0.23094 0.25884 -0.01917 -0.00789 -0.01536 20  ASN A O   
147  C CB  . ASN A 20  ? 0.28462 0.29886 0.31616 -0.01685 -0.00772 -0.01037 20  ASN A CB  
148  C CG  . ASN A 20  ? 0.24410 0.25803 0.27428 -0.01951 -0.00486 -0.00780 20  ASN A CG  
149  O OD1 . ASN A 20  ? 0.33557 0.35162 0.37001 -0.02139 -0.00295 -0.00720 20  ASN A OD1 
150  N ND2 . ASN A 20  ? 0.21184 0.22262 0.23590 -0.01942 -0.00433 -0.00650 20  ASN A ND2 
151  N N   . PRO A 21  ? 0.27883 0.30521 0.33295 -0.02130 -0.00139 -0.01348 21  PRO A N   
152  C CA  . PRO A 21  ? 0.21969 0.24949 0.28394 -0.02414 0.00122  -0.01536 21  PRO A CA  
153  C C   . PRO A 21  ? 0.23216 0.25796 0.29380 -0.02657 0.00271  -0.01315 21  PRO A C   
154  O O   . PRO A 21  ? 0.29071 0.31769 0.36017 -0.02889 0.00384  -0.01518 21  PRO A O   
155  C CB  . PRO A 21  ? 0.26291 0.29422 0.32958 -0.02568 0.00690  -0.01480 21  PRO A CB  
156  C CG  . PRO A 21  ? 0.26419 0.29114 0.31932 -0.02426 0.00711  -0.01146 21  PRO A CG  
157  C CD  . PRO A 21  ? 0.32018 0.34578 0.37056 -0.02127 0.00164  -0.01188 21  PRO A CD  
158  N N   . ALA A 22  ? 0.24946 0.27061 0.30118 -0.02602 0.00268  -0.00955 22  ALA A N   
159  C CA  . ALA A 22  ? 0.25855 0.27569 0.30743 -0.02711 0.00327  -0.00778 22  ALA A CA  
160  C C   . ALA A 22  ? 0.25018 0.26713 0.29999 -0.02589 -0.00084 -0.00981 22  ALA A C   
161  O O   . ALA A 22  ? 0.30216 0.31660 0.35352 -0.02707 -0.00050 -0.01008 22  ALA A O   
162  C CB  . ALA A 22  ? 0.23072 0.24445 0.27046 -0.02619 0.00381  -0.00432 22  ALA A CB  
163  N N   . LEU A 23  ? 0.22893 0.24689 0.27625 -0.02327 -0.00449 -0.01122 23  LEU A N   
164  C CA  . LEU A 23  ? 0.24639 0.26260 0.29196 -0.02144 -0.00828 -0.01326 23  LEU A CA  
165  C C   . LEU A 23  ? 0.20967 0.22882 0.26431 -0.02166 -0.01106 -0.01784 23  LEU A C   
166  O O   . LEU A 23  ? 0.22951 0.24680 0.28517 -0.02173 -0.01305 -0.01979 23  LEU A O   
167  C CB  . LEU A 23  ? 0.25092 0.26473 0.28825 -0.01831 -0.01055 -0.01299 23  LEU A CB  
168  C CG  . LEU A 23  ? 0.19426 0.20415 0.22611 -0.01554 -0.01412 -0.01494 23  LEU A CG  
169  C CD1 . LEU A 23  ? 0.30326 0.31075 0.33288 -0.01644 -0.01253 -0.01386 23  LEU A CD1 
170  C CD2 . LEU A 23  ? 0.22823 0.23322 0.24965 -0.01257 -0.01491 -0.01405 23  LEU A CD2 
171  N N   . LEU A 24  ? 0.23905 0.26322 0.30129 -0.02169 -0.01139 -0.02026 24  LEU A N   
172  C CA  . LEU A 24  ? 0.25655 0.28561 0.33053 -0.02192 -0.01451 -0.02591 24  LEU A CA  
173  C C   . LEU A 24  ? 0.25899 0.28846 0.34181 -0.02682 -0.01062 -0.02679 24  LEU A C   
174  O O   . LEU A 24  ? 0.31838 0.34968 0.40933 -0.02763 -0.01366 -0.03156 24  LEU A O   
175  C CB  . LEU A 24  ? 0.21494 0.25051 0.29685 -0.02059 -0.01518 -0.02873 24  LEU A CB  
176  C CG  . LEU A 24  ? 0.19653 0.23005 0.26943 -0.01518 -0.01947 -0.02842 24  LEU A CG  
177  C CD1 . LEU A 24  ? 0.27088 0.31046 0.35167 -0.01383 -0.01906 -0.03076 24  LEU A CD1 
178  C CD2 . LEU A 24  ? 0.21836 0.24920 0.28685 -0.01062 -0.02712 -0.03191 24  LEU A CD2 
179  N N   . GLU A 25  ? 0.26037 0.28699 0.34086 -0.02995 -0.00406 -0.02248 25  GLU A N   
180  C CA  . GLU A 25  ? 0.28315 0.30674 0.36877 -0.03446 0.00056  -0.02241 25  GLU A CA  
181  C C   . GLU A 25  ? 0.27426 0.29145 0.35370 -0.03391 -0.00165 -0.02162 25  GLU A C   
182  O O   . GLU A 25  ? 0.31630 0.33179 0.40234 -0.03658 -0.00144 -0.02456 25  GLU A O   
183  C CB  . GLU A 25  ? 0.23606 0.25569 0.31697 -0.03675 0.00791  -0.01760 25  GLU A CB  
184  C CG  . GLU A 25  ? 0.24087 0.25358 0.32284 -0.04099 0.01367  -0.01631 25  GLU A CG  
185  C CD  . GLU A 25  ? 0.29533 0.31229 0.39321 -0.04573 0.01712  -0.02131 25  GLU A CD  
186  O OE1 . GLU A 25  ? 0.21180 0.23744 0.31950 -0.04592 0.01751  -0.02463 25  GLU A OE1 
187  O OE2 . GLU A 25  ? 0.33429 0.34602 0.43572 -0.04932 0.01957  -0.02237 25  GLU A OE2 
188  N N   . ALA A 26  ? 0.28818 0.30188 0.35581 -0.03061 -0.00347 -0.01819 26  ALA A N   
189  C CA  . ALA A 26  ? 0.25673 0.26479 0.31844 -0.02943 -0.00509 -0.01759 26  ALA A CA  
190  C C   . ALA A 26  ? 0.26781 0.27664 0.33174 -0.02766 -0.01075 -0.02253 26  ALA A C   
191  O O   . ALA A 26  ? 0.25972 0.26371 0.32139 -0.02745 -0.01178 -0.02347 26  ALA A O   
192  C CB  . ALA A 26  ? 0.28876 0.29472 0.33968 -0.02645 -0.00506 -0.01357 26  ALA A CB  
193  N N   . CYS A 27  ? 0.30008 0.31397 0.36721 -0.02568 -0.01490 -0.02592 27  CYS A N   
194  C CA  . CYS A 27  ? 0.34316 0.35702 0.41093 -0.02303 -0.02143 -0.03121 27  CYS A CA  
195  C C   . CYS A 27  ? 0.22673 0.24525 0.30959 -0.02593 -0.02342 -0.03745 27  CYS A C   
196  O O   . CYS A 27  ? 0.23690 0.25506 0.32135 -0.02400 -0.02955 -0.04283 27  CYS A O   
197  C CB  . CYS A 27  ? 0.28594 0.30090 0.34687 -0.01807 -0.02591 -0.03188 27  CYS A CB  
198  S SG  . CYS A 27  ? 0.41113 0.42006 0.45529 -0.01525 -0.02333 -0.02589 27  CYS A SG  
199  N N   . LYS A 28  ? 0.26998 0.29257 0.36391 -0.03057 -0.01816 -0.03729 28  LYS A N   
200  C CA  . LYS A 28  ? 0.29560 0.32419 0.40698 -0.03429 -0.01868 -0.04385 28  LYS A CA  
201  C C   . LYS A 28  ? 0.29227 0.31485 0.40675 -0.03832 -0.01695 -0.04546 28  LYS A C   
202  O O   . LYS A 28  ? 0.29493 0.31038 0.40446 -0.04137 -0.01021 -0.04041 28  LYS A O   
203  C CB  . LYS A 28  ? 0.28962 0.32366 0.41088 -0.03816 -0.01173 -0.04280 28  LYS A CB  
204  C CG  . LYS A 28  ? 0.34009 0.38521 0.48099 -0.03967 -0.01376 -0.05067 28  LYS A CG  
205  C CD  . LYS A 28  ? 0.32896 0.37480 0.48528 -0.04649 -0.01004 -0.05544 28  LYS A CD  
206  C CE  . LYS A 28  ? 0.34826 0.40682 0.52723 -0.04939 -0.00895 -0.06288 28  LYS A CE  
207  N NZ  . LYS A 28  ? 0.35980 0.42792 0.54481 -0.04297 -0.02020 -0.06978 28  LYS A NZ  
208  N N   . ASP A 29  ? 0.31977 0.34419 0.44140 -0.03780 -0.02354 -0.05272 29  ASP A N   
209  C CA  . ASP A 29  ? 0.29130 0.30982 0.41711 -0.04166 -0.02289 -0.05574 29  ASP A CA  
210  C C   . ASP A 29  ? 0.23789 0.24482 0.34686 -0.03976 -0.02117 -0.05004 29  ASP A C   
211  O O   . ASP A 29  ? 0.23675 0.23611 0.34660 -0.04338 -0.01776 -0.04997 29  ASP A O   
212  C CB  . ASP A 29  ? 0.27150 0.29086 0.41225 -0.04979 -0.01453 -0.05679 29  ASP A CB  
213  C CG  . ASP A 29  ? 0.25403 0.28644 0.41505 -0.05218 -0.01552 -0.06376 29  ASP A CG  
214  O OD1 . ASP A 29  ? 0.36260 0.40303 0.52612 -0.04686 -0.02431 -0.06845 29  ASP A OD1 
215  O OD2 . ASP A 29  ? 0.27321 0.30735 0.44734 -0.05908 -0.00722 -0.06468 29  ASP A OD2 
216  N N   . ALA A 30  ? 0.23294 0.23808 0.32711 -0.03413 -0.02317 -0.04559 30  ALA A N   
217  C CA  . ALA A 30  ? 0.27221 0.26845 0.35239 -0.03198 -0.02106 -0.04055 30  ALA A CA  
218  C C   . ALA A 30  ? 0.22970 0.22135 0.30282 -0.02805 -0.02717 -0.04447 30  ALA A C   
219  O O   . ALA A 30  ? 0.31254 0.30738 0.38574 -0.02487 -0.03393 -0.04943 30  ALA A O   
220  C CB  . ALA A 30  ? 0.22803 0.22521 0.29760 -0.02875 -0.01880 -0.03414 30  ALA A CB  
221  N N   . LYS A 31  ? 0.25279 0.23600 0.31864 -0.02762 -0.02492 -0.04236 31  LYS A N   
222  C CA  . LYS A 31  ? 0.28642 0.26380 0.34333 -0.02349 -0.02934 -0.04539 31  LYS A CA  
223  C C   . LYS A 31  ? 0.29952 0.27490 0.34215 -0.01828 -0.02812 -0.04085 31  LYS A C   
224  O O   . LYS A 31  ? 0.29950 0.27266 0.33312 -0.01380 -0.03204 -0.04330 31  LYS A O   
225  C CB  . LYS A 31  ? 0.29337 0.26210 0.35183 -0.02598 -0.02754 -0.04688 31  LYS A CB  
226  C CG  . LYS A 31  ? 0.32912 0.29133 0.37970 -0.02207 -0.03242 -0.05149 31  LYS A CG  
227  C CD  . LYS A 31  ? 0.33068 0.29595 0.38721 -0.02188 -0.04025 -0.05987 31  LYS A CD  
228  C CE  . LYS A 31  ? 0.39560 0.35253 0.44308 -0.01804 -0.04513 -0.06495 31  LYS A CE  
229  N NZ  . LYS A 31  ? 0.28292 0.24218 0.33556 -0.01718 -0.05419 -0.07409 31  LYS A NZ  
230  N N   . HIS A 32  ? 0.25118 0.22695 0.29146 -0.01875 -0.02260 -0.03467 32  HIS A N   
231  C CA  . HIS A 32  ? 0.34162 0.31748 0.37181 -0.01477 -0.02066 -0.03089 32  HIS A CA  
232  C C   . HIS A 32  ? 0.31099 0.29210 0.34332 -0.01631 -0.01684 -0.02577 32  HIS A C   
233  O O   . HIS A 32  ? 0.28328 0.26338 0.31952 -0.01883 -0.01368 -0.02309 32  HIS A O   
234  C CB  . HIS A 32  ? 0.35128 0.32083 0.37584 -0.01242 -0.01867 -0.03012 32  HIS A CB  
235  C CG  . HIS A 32  ? 0.41729 0.38058 0.43784 -0.01034 -0.02221 -0.03529 32  HIS A CG  
236  N ND1 . HIS A 32  ? 0.34945 0.30731 0.37510 -0.01278 -0.02366 -0.03865 32  HIS A ND1 
237  C CD2 . HIS A 32  ? 0.36951 0.32996 0.38043 -0.00604 -0.02433 -0.03791 32  HIS A CD2 
238  C CE1 . HIS A 32  ? 0.38006 0.33269 0.39998 -0.00991 -0.02733 -0.04349 32  HIS A CE1 
239  N NE2 . HIS A 32  ? 0.37618 0.33002 0.38632 -0.00551 -0.02776 -0.04302 32  HIS A NE2 
240  N N   . VAL A 33  ? 0.26005 0.24524 0.28842 -0.01459 -0.01710 -0.02448 33  VAL A N   
241  C CA  . VAL A 33  ? 0.31162 0.30153 0.34122 -0.01575 -0.01401 -0.02029 33  VAL A CA  
242  C C   . VAL A 33  ? 0.31329 0.30325 0.33643 -0.01327 -0.01133 -0.01772 33  VAL A C   
243  O O   . VAL A 33  ? 0.33379 0.32137 0.35022 -0.01055 -0.01161 -0.01913 33  VAL A O   
244  C CB  . VAL A 33  ? 0.27816 0.27242 0.30935 -0.01603 -0.01600 -0.02112 33  VAL A CB  
245  C CG1 . VAL A 33  ? 0.34351 0.34185 0.37590 -0.01743 -0.01275 -0.01716 33  VAL A CG1 
246  C CG2 . VAL A 33  ? 0.29804 0.29413 0.33835 -0.01822 -0.01899 -0.02515 33  VAL A CG2 
247  N N   . TYR A 34  ? 0.25207 0.24456 0.27726 -0.01410 -0.00858 -0.01439 34  TYR A N   
248  C CA  . TYR A 34  ? 0.30048 0.29500 0.32310 -0.01212 -0.00621 -0.01289 34  TYR A CA  
249  C C   . TYR A 34  ? 0.26262 0.26222 0.28631 -0.01343 -0.00477 -0.01067 34  TYR A C   
250  O O   . TYR A 34  ? 0.23011 0.23139 0.25670 -0.01465 -0.00447 -0.00867 34  TYR A O   
251  C CB  . TYR A 34  ? 0.31600 0.30869 0.34013 -0.01069 -0.00557 -0.01201 34  TYR A CB  
252  C CG  . TYR A 34  ? 0.33538 0.32182 0.35794 -0.00920 -0.00668 -0.01432 34  TYR A CG  
253  C CD1 . TYR A 34  ? 0.36288 0.34816 0.38216 -0.00599 -0.00597 -0.01634 34  TYR A CD1 
254  C CD2 . TYR A 34  ? 0.30597 0.28718 0.33052 -0.01125 -0.00781 -0.01482 34  TYR A CD2 
255  C CE1 . TYR A 34  ? 0.31773 0.29650 0.33483 -0.00432 -0.00713 -0.01881 34  TYR A CE1 
256  C CE2 . TYR A 34  ? 0.36759 0.34217 0.39081 -0.01023 -0.00891 -0.01737 34  TYR A CE2 
257  C CZ  . TYR A 34  ? 0.35164 0.32487 0.37067 -0.00647 -0.00897 -0.01937 34  TYR A CZ  
258  O OH  . TYR A 34  ? 0.43133 0.39720 0.44830 -0.00515 -0.01021 -0.02226 34  TYR A OH  
259  N N   . PRO A 35  ? 0.28123 0.28190 0.30134 -0.01315 -0.00362 -0.01096 35  PRO A N   
260  C CA  . PRO A 35  ? 0.25585 0.26046 0.27695 -0.01461 -0.00189 -0.00925 35  PRO A CA  
261  C C   . PRO A 35  ? 0.26505 0.27362 0.28908 -0.01408 0.00051  -0.00912 35  PRO A C   
262  O O   . PRO A 35  ? 0.23876 0.24723 0.26134 -0.01300 0.00313  -0.01046 35  PRO A O   
263  C CB  . PRO A 35  ? 0.21787 0.21939 0.23251 -0.01430 -0.00134 -0.00983 35  PRO A CB  
264  C CG  . PRO A 35  ? 0.33090 0.32710 0.34050 -0.01204 -0.00344 -0.01208 35  PRO A CG  
265  C CD  . PRO A 35  ? 0.32891 0.32532 0.34215 -0.01134 -0.00368 -0.01292 35  PRO A CD  
266  N N   . VAL A 36  ? 0.25547 0.26759 0.28372 -0.01454 -0.00034 -0.00796 36  VAL A N   
267  C CA  . VAL A 36  ? 0.20611 0.22301 0.23895 -0.01312 0.00012  -0.00879 36  VAL A CA  
268  C C   . VAL A 36  ? 0.27018 0.29192 0.30597 -0.01495 0.00039  -0.00861 36  VAL A C   
269  O O   . VAL A 36  ? 0.25127 0.27188 0.28527 -0.01625 -0.00096 -0.00701 36  VAL A O   
270  C CB  . VAL A 36  ? 0.21878 0.23379 0.25235 -0.01050 -0.00256 -0.00821 36  VAL A CB  
271  C CG1 . VAL A 36  ? 0.19455 0.21516 0.23327 -0.00780 -0.00356 -0.00975 36  VAL A CG1 
272  C CG2 . VAL A 36  ? 0.22033 0.22974 0.25131 -0.00902 -0.00270 -0.00890 36  VAL A CG2 
273  N N   . PHE A 37  ? 0.23790 0.26512 0.27888 -0.01521 0.00251  -0.01078 37  PHE A N   
274  C CA  . PHE A 37  ? 0.25074 0.28356 0.29679 -0.01687 0.00222  -0.01189 37  PHE A CA  
275  C C   . PHE A 37  ? 0.26506 0.30519 0.31972 -0.01426 0.00053  -0.01491 37  PHE A C   
276  O O   . PHE A 37  ? 0.26424 0.30814 0.32427 -0.01381 0.00363  -0.01745 37  PHE A O   
277  C CB  . PHE A 37  ? 0.25549 0.28824 0.30146 -0.02057 0.00690  -0.01262 37  PHE A CB  
278  C CG  . PHE A 37  ? 0.23582 0.27325 0.28702 -0.02309 0.00661  -0.01413 37  PHE A CG  
279  C CD1 . PHE A 37  ? 0.23751 0.28332 0.29946 -0.02375 0.00750  -0.01803 37  PHE A CD1 
280  C CD2 . PHE A 37  ? 0.26767 0.30153 0.31401 -0.02473 0.00532  -0.01236 37  PHE A CD2 
281  C CE1 . PHE A 37  ? 0.27281 0.32305 0.34047 -0.02632 0.00661  -0.02032 37  PHE A CE1 
282  C CE2 . PHE A 37  ? 0.23267 0.26993 0.28316 -0.02699 0.00477  -0.01419 37  PHE A CE2 
283  C CZ  . PHE A 37  ? 0.23121 0.27651 0.29232 -0.02797 0.00518  -0.01827 37  PHE A CZ  
284  N N   . VAL A 38  ? 0.21082 0.25259 0.26632 -0.01202 -0.00439 -0.01494 38  VAL A N   
285  C CA  . VAL A 38  ? 0.25147 0.29998 0.31466 -0.00809 -0.00787 -0.01829 38  VAL A CA  
286  C C   . VAL A 38  ? 0.26207 0.32017 0.33592 -0.01057 -0.00732 -0.02256 38  VAL A C   
287  O O   . VAL A 38  ? 0.30816 0.36636 0.38075 -0.01270 -0.00902 -0.02249 38  VAL A O   
288  C CB  . VAL A 38  ? 0.24314 0.28702 0.29995 -0.00366 -0.01389 -0.01652 38  VAL A CB  
289  C CG1 . VAL A 38  ? 0.37437 0.42430 0.43802 0.00197  -0.01873 -0.02030 38  VAL A CG1 
290  C CG2 . VAL A 38  ? 0.25153 0.28498 0.29857 -0.00272 -0.01309 -0.01242 38  VAL A CG2 
291  N N   . LEU A 39  ? 0.30970 0.37586 0.39469 -0.01052 -0.00452 -0.02675 39  LEU A N   
292  C CA  . LEU A 39  ? 0.35765 0.43385 0.45577 -0.01390 -0.00255 -0.03181 39  LEU A CA  
293  C C   . LEU A 39  ? 0.40793 0.49535 0.51946 -0.00917 -0.00742 -0.03756 39  LEU A C   
294  O O   . LEU A 39  ? 0.34417 0.43315 0.45823 -0.00486 -0.00744 -0.03854 39  LEU A O   
295  C CB  . LEU A 39  ? 0.33763 0.41370 0.43853 -0.01897 0.00699  -0.03242 39  LEU A CB  
296  C CG  . LEU A 39  ? 0.31009 0.39504 0.42496 -0.02413 0.01165  -0.03762 39  LEU A CG  
297  C CD1 . LEU A 39  ? 0.39569 0.47204 0.50273 -0.03040 0.01933  -0.03481 39  LEU A CD1 
298  C CD2 . LEU A 39  ? 0.38632 0.48143 0.51579 -0.02316 0.01580  -0.04294 39  LEU A CD2 
299  N N   A ASP A 40  ? 0.39927 0.49444 0.51950 -0.00949 -0.01213 -0.04190 40  ASP A N   
300  N N   B ASP A 40  ? 0.39924 0.49442 0.51949 -0.00954 -0.01208 -0.04190 40  ASP A N   
301  C CA  A ASP A 40  ? 0.42393 0.53094 0.55814 -0.00426 -0.01846 -0.04851 40  ASP A CA  
302  C CA  B ASP A 40  ? 0.42397 0.53104 0.55826 -0.00435 -0.01843 -0.04854 40  ASP A CA  
303  C C   A ASP A 40  ? 0.46403 0.58452 0.61868 -0.00867 -0.01225 -0.05540 40  ASP A C   
304  C C   B ASP A 40  ? 0.46394 0.58437 0.61856 -0.00876 -0.01212 -0.05537 40  ASP A C   
305  O O   A ASP A 40  ? 0.43799 0.56219 0.59959 -0.01520 -0.00906 -0.05798 40  ASP A O   
306  O O   B ASP A 40  ? 0.43812 0.56211 0.59958 -0.01539 -0.00867 -0.05786 40  ASP A O   
307  C CB  A ASP A 40  ? 0.44651 0.55471 0.57907 -0.00146 -0.02798 -0.05050 40  ASP A CB  
308  C CB  B ASP A 40  ? 0.44626 0.55465 0.57914 -0.00181 -0.02777 -0.05060 40  ASP A CB  
309  C CG  A ASP A 40  ? 0.46689 0.58558 0.61095 0.00616  -0.03697 -0.05722 40  ASP A CG  
310  C CG  B ASP A 40  ? 0.43471 0.52839 0.54657 -0.00054 -0.03046 -0.04338 40  ASP A CG  
311  O OD1 A ASP A 40  ? 0.43152 0.54640 0.56998 0.01345  -0.04060 -0.05562 40  ASP A OD1 
312  O OD1 B ASP A 40  ? 0.42513 0.50899 0.52518 0.00113  -0.02816 -0.03768 40  ASP A OD1 
313  O OD2 A ASP A 40  ? 0.46477 0.59518 0.62359 0.00514  -0.04081 -0.06450 40  ASP A OD2 
314  O OD2 B ASP A 40  ? 0.45985 0.55186 0.56756 -0.00141 -0.03451 -0.04387 40  ASP A OD2 
315  N N   . PRO A 41  ? 0.46969 0.59729 0.63461 -0.00561 -0.00970 -0.05878 41  PRO A N   
316  C CA  . PRO A 41  ? 0.42550 0.56611 0.61090 -0.01042 -0.00188 -0.06563 41  PRO A CA  
317  C C   . PRO A 41  ? 0.53228 0.68935 0.73914 -0.00993 -0.00789 -0.07495 41  PRO A C   
318  O O   . PRO A 41  ? 0.58763 0.75657 0.81410 -0.01523 -0.00083 -0.08151 41  PRO A O   
319  C CB  . PRO A 41  ? 0.39794 0.54041 0.58621 -0.00574 0.00172  -0.06638 41  PRO A CB  
320  C CG  . PRO A 41  ? 0.48762 0.62411 0.66478 0.00358  -0.00883 -0.06352 41  PRO A CG  
321  C CD  . PRO A 41  ? 0.43691 0.56013 0.59500 0.00221  -0.01304 -0.05661 41  PRO A CD  
322  N N   . HIS A 42  ? 0.50603 0.66383 0.70975 -0.00374 -0.02045 -0.07614 42  HIS A N   
323  C CA  . HIS A 42  ? 0.52742 0.70038 0.75027 -0.00222 -0.02845 -0.08566 42  HIS A CA  
324  C C   . HIS A 42  ? 0.57354 0.74172 0.78924 -0.00587 -0.03315 -0.08496 42  HIS A C   
325  O O   . HIS A 42  ? 0.58096 0.75624 0.80323 -0.00165 -0.04408 -0.09094 42  HIS A O   
326  C CB  . HIS A 42  ? 0.57104 0.74917 0.79641 0.00978  -0.04073 -0.08929 42  HIS A CB  
327  C CG  . HIS A 42  ? 0.59483 0.77616 0.82546 0.01454  -0.03693 -0.08983 42  HIS A CG  
328  N ND1 . HIS A 42  ? 0.57299 0.73921 0.78371 0.01735  -0.03389 -0.08126 42  HIS A ND1 
329  C CD2 . HIS A 42  ? 0.58432 0.78238 0.83850 0.01701  -0.03553 -0.09848 42  HIS A CD2 
330  C CE1 . HIS A 42  ? 0.51688 0.68931 0.73717 0.02156  -0.03100 -0.08433 42  HIS A CE1 
331  N NE2 . HIS A 42  ? 0.61695 0.80887 0.86360 0.02164  -0.03169 -0.09467 42  HIS A NE2 
332  N N   . PHE A 43  ? 0.50533 0.66105 0.70697 -0.01308 -0.02541 -0.07803 43  PHE A N   
333  C CA  . PHE A 43  ? 0.51348 0.66333 0.70705 -0.01647 -0.02899 -0.07704 43  PHE A CA  
334  C C   . PHE A 43  ? 0.57242 0.73567 0.78783 -0.02241 -0.02897 -0.08666 43  PHE A C   
335  O O   . PHE A 43  ? 0.56616 0.72881 0.77959 -0.02263 -0.03617 -0.08925 43  PHE A O   
336  C CB  . PHE A 43  ? 0.49169 0.62587 0.66694 -0.02237 -0.02033 -0.06808 43  PHE A CB  
337  C CG  . PHE A 43  ? 0.45948 0.58374 0.61963 -0.02273 -0.02529 -0.06468 43  PHE A CG  
338  C CD1 . PHE A 43  ? 0.46314 0.58910 0.62920 -0.02913 -0.02421 -0.06846 43  PHE A CD1 
339  C CD2 . PHE A 43  ? 0.43698 0.54962 0.57707 -0.01693 -0.03026 -0.05794 43  PHE A CD2 
340  C CE1 . PHE A 43  ? 0.52178 0.63829 0.67349 -0.02900 -0.02853 -0.06564 43  PHE A CE1 
341  C CE2 . PHE A 43  ? 0.45724 0.56086 0.58358 -0.01717 -0.03374 -0.05507 43  PHE A CE2 
342  C CZ  . PHE A 43  ? 0.41959 0.52526 0.55146 -0.02287 -0.03311 -0.05895 43  PHE A CZ  
343  N N   . LEU A 44  ? 0.55183 0.72685 0.78824 -0.02749 -0.02053 -0.09241 44  LEU A N   
344  C CA  . LEU A 44  ? 0.53475 0.72347 0.79511 -0.03424 -0.01913 -0.10248 44  LEU A CA  
345  C C   . LEU A 44  ? 0.64278 0.85038 0.92504 -0.02769 -0.03080 -0.11363 44  LEU A C   
346  O O   . LEU A 44  ? 0.63527 0.85521 0.93801 -0.03223 -0.03309 -0.12332 44  LEU A O   
347  C CB  . LEU A 44  ? 0.46417 0.65591 0.73725 -0.04370 -0.00283 -0.10377 44  LEU A CB  
348  C CG  . LEU A 44  ? 0.44044 0.61275 0.69139 -0.04962 0.00845  -0.09339 44  LEU A CG  
349  C CD1 . LEU A 44  ? 0.34679 0.52023 0.60872 -0.05893 0.02469  -0.09522 44  LEU A CD1 
350  C CD2 . LEU A 44  ? 0.43111 0.59204 0.66783 -0.05261 0.00463  -0.09007 44  LEU A CD2 
351  N N   . GLN A 45  ? 0.82172 1.03146 1.10035 -0.01693 -0.03859 -0.11296 45  GLN A N   
352  C CA  . GLN A 45  ? 0.84142 1.06696 1.13704 -0.00821 -0.05202 -0.12303 45  GLN A CA  
353  C C   . GLN A 45  ? 0.85226 1.06947 1.12974 0.00036  -0.06763 -0.12160 45  GLN A C   
354  O O   . GLN A 45  ? 0.90669 1.13081 1.18830 0.01111  -0.08050 -0.12694 45  GLN A O   
355  C CB  . GLN A 45  ? 0.77265 1.00449 1.07447 -0.00023 -0.05206 -0.12383 45  GLN A CB  
356  C CG  . GLN A 45  ? 0.78569 1.03002 1.11059 -0.00714 -0.03800 -0.12850 45  GLN A CG  
357  C CD  . GLN A 45  ? 0.75020 0.98056 1.05772 -0.00899 -0.02568 -0.11819 45  GLN A CD  
358  O OE1 . GLN A 45  ? 0.74314 0.97477 1.05018 -0.00187 -0.02590 -0.11741 45  GLN A OE1 
359  N NE2 . GLN A 45  ? 0.70721 0.92366 0.99992 -0.01806 -0.01542 -0.11063 45  GLN A NE2 
360  N N   . GLN A 46  ? 0.72323 0.92493 0.97977 -0.00360 -0.06661 -0.11460 46  GLN A N   
361  C CA  . GLN A 46  ? 0.70027 0.89250 0.93782 0.00383  -0.07981 -0.11311 46  GLN A CA  
362  C C   . GLN A 46  ? 0.66894 0.86243 0.91060 -0.00276 -0.08205 -0.11807 46  GLN A C   
363  O O   . GLN A 46  ? 0.70972 0.90241 0.94556 0.00332  -0.09499 -0.12226 46  GLN A O   
364  C CB  . GLN A 46  ? 0.63599 0.80652 0.84146 0.00683  -0.07737 -0.09981 46  GLN A CB  
365  C CG  . GLN A 46  ? 0.60229 0.76055 0.79512 -0.00284 -0.06703 -0.09249 46  GLN A CG  
366  C CD  . GLN A 46  ? 0.55847 0.69733 0.72241 0.00043  -0.06554 -0.08079 46  GLN A CD  
367  O OE1 . GLN A 46  ? 0.52761 0.65737 0.68260 -0.00583 -0.05543 -0.07371 46  GLN A OE1 
368  N NE2 . GLN A 46  ? 0.57680 0.70879 0.72597 0.01043  -0.07558 -0.07905 46  GLN A NE2 
369  N N   . LYS A 50  ? 0.46791 0.64466 0.73097 -0.05914 -0.03379 -0.11963 50  LYS A N   
370  C CA  . LYS A 50  ? 0.37630 0.53691 0.61302 -0.05562 -0.03953 -0.11294 50  LYS A CA  
371  C C   . LYS A 50  ? 0.36471 0.50726 0.58109 -0.06004 -0.02760 -0.10149 50  LYS A C   
372  O O   . LYS A 50  ? 0.41738 0.54648 0.61564 -0.06027 -0.02872 -0.09687 50  LYS A O   
373  C CB  . LYS A 50  ? 0.53209 0.69120 0.75396 -0.04298 -0.05207 -0.10989 50  LYS A CB  
374  N N   . VAL A 51  ? 0.37887 0.52114 0.59813 -0.06293 -0.01649 -0.09739 51  VAL A N   
375  C CA  . VAL A 51  ? 0.32444 0.45014 0.52499 -0.06618 -0.00568 -0.08716 51  VAL A CA  
376  C C   . VAL A 51  ? 0.29937 0.42520 0.51238 -0.07628 0.00839  -0.08933 51  VAL A C   
377  O O   . VAL A 51  ? 0.29372 0.43266 0.52673 -0.07831 0.01251  -0.09505 51  VAL A O   
378  C CB  . VAL A 51  ? 0.39221 0.51349 0.57868 -0.05892 -0.00564 -0.07891 51  VAL A CB  
379  C CG1 . VAL A 51  ? 0.37501 0.47990 0.54306 -0.06182 0.00432  -0.06947 51  VAL A CG1 
380  C CG2 . VAL A 51  ? 0.38446 0.50397 0.55807 -0.04946 -0.01823 -0.07670 51  VAL A CG2 
381  N N   . SER A 52  ? 0.26280 0.37329 0.46350 -0.08231 0.01613  -0.08490 52  SER A N   
382  C CA  A SER A 52  ? 0.27201 0.37788 0.47966 -0.09196 0.03067  -0.08575 52  SER A CA  
383  C CA  B SER A 52  ? 0.26581 0.37174 0.47354 -0.09196 0.03067  -0.08578 52  SER A CA  
384  C C   . SER A 52  ? 0.27331 0.37053 0.46834 -0.09057 0.04028  -0.07758 52  SER A C   
385  O O   . SER A 52  ? 0.28744 0.37990 0.46642 -0.08293 0.03571  -0.07063 52  SER A O   
386  C CB  A SER A 52  ? 0.25372 0.34431 0.45138 -0.09834 0.03473  -0.08438 52  SER A CB  
387  C CB  B SER A 52  ? 0.25607 0.34677 0.45392 -0.09838 0.03475  -0.08445 52  SER A CB  
388  O OG  A SER A 52  ? 0.29352 0.37562 0.49372 -0.10740 0.04987  -0.08392 52  SER A OG  
389  O OG  B SER A 52  ? 0.29161 0.36573 0.46274 -0.09349 0.03311  -0.07469 52  SER A OG  
390  N N   . VAL A 53  ? 0.27273 0.36714 0.47484 -0.09830 0.05418  -0.07881 53  VAL A N   
391  C CA  . VAL A 53  ? 0.26314 0.34737 0.45150 -0.09720 0.06407  -0.07154 53  VAL A CA  
392  C C   . VAL A 53  ? 0.29158 0.35278 0.45190 -0.09673 0.06749  -0.06209 53  VAL A C   
393  O O   . VAL A 53  ? 0.33629 0.38752 0.48013 -0.09310 0.07166  -0.05513 53  VAL A O   
394  C CB  . VAL A 53  ? 0.24798 0.33618 0.45230 -0.10527 0.07878  -0.07622 53  VAL A CB  
395  C CG1 . VAL A 53  ? 0.31905 0.39213 0.51911 -0.11522 0.09022  -0.07603 53  VAL A CG1 
396  C CG2 . VAL A 53  ? 0.25822 0.34179 0.45236 -0.10167 0.08631  -0.07078 53  VAL A CG2 
397  N N   . ASN A 54  ? 0.26474 0.31723 0.41915 -0.09967 0.06510  -0.06214 54  ASN A N   
398  C CA  . ASN A 54  ? 0.28389 0.31499 0.41243 -0.09822 0.06736  -0.05380 54  ASN A CA  
399  C C   . ASN A 54  ? 0.32367 0.35333 0.43683 -0.08842 0.05692  -0.04773 54  ASN A C   
400  O O   . ASN A 54  ? 0.32935 0.34654 0.42391 -0.08472 0.05956  -0.04057 54  ASN A O   
401  C CB  . ASN A 54  ? 0.28033 0.30277 0.40767 -0.10364 0.06742  -0.05618 54  ASN A CB  
402  C CG  . ASN A 54  ? 0.27770 0.28858 0.40691 -0.11347 0.08199  -0.05758 54  ASN A CG  
403  O OD1 . ASN A 54  ? 0.28699 0.28710 0.40599 -0.11458 0.09268  -0.05298 54  ASN A OD1 
404  N ND2 . ASN A 54  ? 0.28349 0.29522 0.42468 -0.12070 0.08277  -0.06409 54  ASN A ND2 
405  N N   . ARG A 55  ? 0.33559 0.37731 0.45596 -0.08406 0.04510  -0.05081 55  ARG A N   
406  C CA  . ARG A 55  ? 0.35043 0.38995 0.45665 -0.07565 0.03635  -0.04530 55  ARG A CA  
407  C C   . ARG A 55  ? 0.32720 0.37203 0.43261 -0.07053 0.03608  -0.04249 55  ARG A C   
408  O O   . ARG A 55  ? 0.39036 0.42750 0.48046 -0.06549 0.03439  -0.03622 55  ARG A O   
409  C CB  . ARG A 55  ? 0.23898 0.28716 0.35040 -0.07245 0.02484  -0.04916 55  ARG A CB  
410  C CG  . ARG A 55  ? 0.26171 0.30634 0.35826 -0.06459 0.01733  -0.04353 55  ARG A CG  
411  C CD  . ARG A 55  ? 0.22439 0.27152 0.31985 -0.06189 0.00795  -0.04625 55  ARG A CD  
412  N NE  . ARG A 55  ? 0.22743 0.28815 0.33395 -0.05817 -0.00006 -0.05108 55  ARG A NE  
413  C CZ  . ARG A 55  ? 0.22844 0.29890 0.34985 -0.06046 -0.00418 -0.05923 55  ARG A CZ  
414  N NH1 . ARG A 55  ? 0.29265 0.36110 0.42098 -0.06751 -0.00043 -0.06372 55  ARG A NH1 
415  N NH2 . ARG A 55  ? 0.26593 0.34785 0.39539 -0.05533 -0.01265 -0.06334 55  ARG A NH2 
416  N N   . TYR A 56  ? 0.30403 0.36221 0.42666 -0.07165 0.03766  -0.04763 56  TYR A N   
417  C CA  . TYR A 56  ? 0.31008 0.37312 0.43225 -0.06643 0.03716  -0.04552 56  TYR A CA  
418  C C   . TYR A 56  ? 0.30731 0.35824 0.41713 -0.06764 0.04733  -0.04043 56  TYR A C   
419  O O   . TYR A 56  ? 0.28290 0.32969 0.38140 -0.06223 0.04558  -0.03567 56  TYR A O   
420  C CB  . TYR A 56  ? 0.36281 0.44374 0.50744 -0.06654 0.03581  -0.05308 56  TYR A CB  
421  C CG  . TYR A 56  ? 0.29832 0.38579 0.44273 -0.05886 0.03033  -0.05176 56  TYR A CG  
422  C CD1 . TYR A 56  ? 0.37251 0.45882 0.51543 -0.05791 0.03733  -0.04989 56  TYR A CD1 
423  C CD2 . TYR A 56  ? 0.20609 0.29910 0.35007 -0.05236 0.01847  -0.05231 56  TYR A CD2 
424  C CE1 . TYR A 56  ? 0.35646 0.44757 0.49881 -0.05090 0.03234  -0.04891 56  TYR A CE1 
425  C CE2 . TYR A 56  ? 0.30570 0.40246 0.44818 -0.04539 0.01386  -0.05087 56  TYR A CE2 
426  C CZ  . TYR A 56  ? 0.42546 0.52154 0.56779 -0.04479 0.02067  -0.04931 56  TYR A CZ  
427  O OH  . TYR A 56  ? 0.51398 0.61275 0.65457 -0.03787 0.01611  -0.04813 56  TYR A OH  
428  N N   . ASN A 57  ? 0.30421 0.34820 0.41512 -0.07466 0.05812  -0.04154 57  ASN A N   
429  C CA  . ASN A 57  ? 0.28969 0.31866 0.38452 -0.07520 0.06783  -0.03628 57  ASN A CA  
430  C C   . ASN A 57  ? 0.29640 0.30878 0.36812 -0.07156 0.06467  -0.02931 57  ASN A C   
431  O O   . ASN A 57  ? 0.35322 0.35443 0.40883 -0.06827 0.06769  -0.02440 57  ASN A O   
432  C CB  . ASN A 57  ? 0.27869 0.30223 0.37894 -0.08383 0.08126  -0.03905 57  ASN A CB  
433  C CG  . ASN A 57  ? 0.42380 0.43068 0.50582 -0.08383 0.09217  -0.03385 57  ASN A CG  
434  O OD1 . ASN A 57  ? 0.59085 0.57862 0.65313 -0.08436 0.09581  -0.02885 57  ASN A OD1 
435  N ND2 . ASN A 57  ? 0.42133 0.43451 0.50870 -0.08253 0.09712  -0.03517 57  ASN A ND2 
436  N N   . PHE A 58  ? 0.28939 0.30020 0.35946 -0.07165 0.05830  -0.02938 58  PHE A N   
437  C CA  . PHE A 58  ? 0.29483 0.29308 0.34594 -0.06709 0.05383  -0.02368 58  PHE A CA  
438  C C   . PHE A 58  ? 0.33636 0.33975 0.38331 -0.05971 0.04594  -0.02090 58  PHE A C   
439  O O   . PHE A 58  ? 0.33070 0.32410 0.36239 -0.05550 0.04476  -0.01622 58  PHE A O   
440  C CB  . PHE A 58  ? 0.28033 0.27743 0.33247 -0.06861 0.04889  -0.02524 58  PHE A CB  
441  C CG  . PHE A 58  ? 0.27399 0.25656 0.30763 -0.06504 0.04668  -0.02022 58  PHE A CG  
442  C CD1 . PHE A 58  ? 0.27462 0.25956 0.30237 -0.05848 0.03844  -0.01749 58  PHE A CD1 
443  C CD2 . PHE A 58  ? 0.26229 0.22851 0.28487 -0.06816 0.05310  -0.01857 58  PHE A CD2 
444  C CE1 . PHE A 58  ? 0.26224 0.23569 0.27558 -0.05492 0.03630  -0.01386 58  PHE A CE1 
445  C CE2 . PHE A 58  ? 0.26824 0.22144 0.27434 -0.06384 0.05031  -0.01450 58  PHE A CE2 
446  C CZ  . PHE A 58  ? 0.28863 0.24657 0.29121 -0.05711 0.04168  -0.01248 58  PHE A CZ  
447  N N   . LEU A 59  ? 0.28621 0.30465 0.34666 -0.05790 0.04028  -0.02410 59  LEU A N   
448  C CA  . LEU A 59  ? 0.26811 0.29044 0.32514 -0.05156 0.03395  -0.02167 59  LEU A CA  
449  C C   . LEU A 59  ? 0.33683 0.35567 0.38867 -0.04984 0.03893  -0.01977 59  LEU A C   
450  O O   . LEU A 59  ? 0.30766 0.32087 0.34842 -0.04536 0.03615  -0.01608 59  LEU A O   
451  C CB  . LEU A 59  ? 0.28787 0.32476 0.35875 -0.04964 0.02709  -0.02555 59  LEU A CB  
452  C CG  . LEU A 59  ? 0.21249 0.25314 0.28123 -0.04356 0.02142  -0.02356 59  LEU A CG  
453  C CD1 . LEU A 59  ? 0.19428 0.22854 0.25134 -0.04022 0.01617  -0.01943 59  LEU A CD1 
454  C CD2 . LEU A 59  ? 0.22374 0.27746 0.30618 -0.04154 0.01620  -0.02805 59  LEU A CD2 
455  N N   . LEU A 60  ? 0.33630 0.35854 0.39654 -0.05342 0.04651  -0.02280 60  LEU A N   
456  C CA  . LEU A 60  ? 0.27121 0.28949 0.32570 -0.05168 0.05212  -0.02142 60  LEU A CA  
457  C C   . LEU A 60  ? 0.32000 0.32012 0.35362 -0.05088 0.05643  -0.01655 60  LEU A C   
458  O O   . LEU A 60  ? 0.30940 0.30386 0.33181 -0.04618 0.05494  -0.01385 60  LEU A O   
459  C CB  . LEU A 60  ? 0.22992 0.25566 0.29864 -0.05621 0.06081  -0.02621 60  LEU A CB  
460  C CG  . LEU A 60  ? 0.22472 0.26945 0.31556 -0.05605 0.05599  -0.03221 60  LEU A CG  
461  C CD1 . LEU A 60  ? 0.24882 0.30155 0.35568 -0.06098 0.06563  -0.03779 60  LEU A CD1 
462  C CD2 . LEU A 60  ? 0.27775 0.32847 0.36834 -0.04888 0.04788  -0.03127 60  LEU A CD2 
463  N N   . GLU A 61  ? 0.28457 0.27454 0.31212 -0.05502 0.06132  -0.01571 61  GLU A N   
464  C CA  . GLU A 61  ? 0.29270 0.26367 0.29840 -0.05302 0.06412  -0.01102 61  GLU A CA  
465  C C   . GLU A 61  ? 0.29218 0.26071 0.28846 -0.04665 0.05396  -0.00801 61  GLU A C   
466  O O   . GLU A 61  ? 0.35411 0.31110 0.33413 -0.04223 0.05332  -0.00498 61  GLU A O   
467  C CB  . GLU A 61  ? 0.35048 0.31022 0.35151 -0.05836 0.07045  -0.01074 61  GLU A CB  
468  C CG  . GLU A 61  ? 0.34927 0.30654 0.35582 -0.06529 0.08330  -0.01318 61  GLU A CG  
469  C CD  . GLU A 61  ? 0.40347 0.34801 0.40521 -0.07119 0.08991  -0.01296 61  GLU A CD  
470  O OE1 . GLU A 61  ? 0.29745 0.23923 0.29620 -0.07015 0.08324  -0.01209 61  GLU A OE1 
471  O OE2 . GLU A 61  ? 0.47371 0.41025 0.47441 -0.07699 0.10238  -0.01378 61  GLU A OE2 
472  N N   . SER A 62  ? 0.32037 0.29949 0.32667 -0.04597 0.04606  -0.00924 62  SER A N   
473  C CA  . SER A 62  ? 0.29030 0.26912 0.29072 -0.04055 0.03749  -0.00705 62  SER A CA  
474  C C   . SER A 62  ? 0.30390 0.28829 0.30562 -0.03652 0.03408  -0.00691 62  SER A C   
475  O O   . SER A 62  ? 0.27981 0.25971 0.27298 -0.03209 0.02952  -0.00507 62  SER A O   
476  C CB  . SER A 62  ? 0.33764 0.32484 0.34711 -0.04120 0.03153  -0.00837 62  SER A CB  
477  O OG  . SER A 62  ? 0.31261 0.29404 0.32069 -0.04487 0.03431  -0.00898 62  SER A OG  
478  N N   . LEU A 63  ? 0.25516 0.24941 0.26824 -0.03782 0.03596  -0.00939 63  LEU A N   
479  C CA  . LEU A 63  ? 0.26371 0.26188 0.27747 -0.03397 0.03319  -0.00945 63  LEU A CA  
480  C C   . LEU A 63  ? 0.32396 0.31096 0.32399 -0.03183 0.03746  -0.00801 63  LEU A C   
481  O O   . LEU A 63  ? 0.34594 0.33087 0.34020 -0.02759 0.03325  -0.00726 63  LEU A O   
482  C CB  . LEU A 63  ? 0.29461 0.30556 0.32372 -0.03505 0.03391  -0.01284 63  LEU A CB  
483  C CG  . LEU A 63  ? 0.20620 0.22782 0.24691 -0.03511 0.02761  -0.01451 63  LEU A CG  
484  C CD1 . LEU A 63  ? 0.28468 0.31806 0.33943 -0.03468 0.02749  -0.01832 63  LEU A CD1 
485  C CD2 . LEU A 63  ? 0.26843 0.28876 0.30404 -0.03137 0.02035  -0.01202 63  LEU A CD2 
486  N N   . GLU A 64  ? 0.33634 0.31503 0.33024 -0.03477 0.04605  -0.00784 64  GLU A N   
487  C CA  . GLU A 64  ? 0.35569 0.32066 0.33252 -0.03218 0.05053  -0.00613 64  GLU A CA  
488  C C   . GLU A 64  ? 0.30145 0.25406 0.26158 -0.02773 0.04508  -0.00331 64  GLU A C   
489  O O   . GLU A 64  ? 0.33924 0.28223 0.28515 -0.02327 0.04436  -0.00244 64  GLU A O   
490  C CB  . GLU A 64  ? 0.34147 0.29854 0.31439 -0.03681 0.06249  -0.00634 64  GLU A CB  
491  C CG  . GLU A 64  ? 0.41041 0.38042 0.40117 -0.04086 0.06871  -0.01023 64  GLU A CG  
492  C CD  . GLU A 64  ? 0.39872 0.36014 0.38540 -0.04569 0.08233  -0.01077 64  GLU A CD  
493  O OE1 . GLU A 64  ? 0.43931 0.38223 0.40612 -0.04546 0.08707  -0.00739 64  GLU A OE1 
494  O OE2 . GLU A 64  ? 0.33730 0.31000 0.34054 -0.04953 0.08854  -0.01476 64  GLU A OE2 
495  N N   . ASP A 65  ? 0.29172 0.24451 0.25337 -0.02834 0.04084  -0.00243 65  ASP A N   
496  C CA  . ASP A 65  ? 0.31309 0.25673 0.26200 -0.02337 0.03451  -0.00067 65  ASP A CA  
497  C C   . ASP A 65  ? 0.32873 0.28013 0.28219 -0.01913 0.02582  -0.00176 65  ASP A C   
498  O O   . ASP A 65  ? 0.32316 0.26704 0.26539 -0.01401 0.02129  -0.00157 65  ASP A O   
499  C CB  . ASP A 65  ? 0.32383 0.26669 0.27485 -0.02505 0.03273  0.00001  65  ASP A CB  
500  C CG  . ASP A 65  ? 0.28427 0.21441 0.21986 -0.01974 0.02830  0.00167  65  ASP A CG  
501  O OD1 . ASP A 65  ? 0.28180 0.21373 0.21547 -0.01456 0.02092  0.00102  65  ASP A OD1 
502  O OD2 . ASP A 65  ? 0.29403 0.21213 0.21980 -0.02062 0.03207  0.00322  65  ASP A OD2 
503  N N   . LEU A 66  ? 0.30747 0.27317 0.27706 -0.02108 0.02329  -0.00323 66  LEU A N   
504  C CA  . LEU A 66  ? 0.27446 0.24643 0.24878 -0.01804 0.01659  -0.00429 66  LEU A CA  
505  C C   . LEU A 66  ? 0.35425 0.32250 0.32247 -0.01547 0.01764  -0.00522 66  LEU A C   
506  O O   . LEU A 66  ? 0.26574 0.23129 0.22913 -0.01158 0.01220  -0.00612 66  LEU A O   
507  C CB  . LEU A 66  ? 0.23815 0.22321 0.22816 -0.02048 0.01466  -0.00514 66  LEU A CB  
508  C CG  . LEU A 66  ? 0.23708 0.22618 0.23297 -0.02288 0.01359  -0.00467 66  LEU A CG  
509  C CD1 . LEU A 66  ? 0.20442 0.20436 0.21261 -0.02428 0.01166  -0.00555 66  LEU A CD1 
510  C CD2 . LEU A 66  ? 0.27732 0.26288 0.26871 -0.02035 0.00892  -0.00404 66  LEU A CD2 
511  N N   . GLN A 67  ? 0.38562 0.35400 0.35471 -0.01759 0.02467  -0.00565 67  GLN A N   
512  C CA  . GLN A 67  ? 0.35936 0.32409 0.32244 -0.01500 0.02651  -0.00682 67  GLN A CA  
513  C C   . GLN A 67  ? 0.31114 0.26035 0.25399 -0.01080 0.02630  -0.00600 67  GLN A C   
514  O O   . GLN A 67  ? 0.34337 0.28884 0.27942 -0.00671 0.02269  -0.00742 67  GLN A O   
515  C CB  . GLN A 67  ? 0.31310 0.28164 0.28227 -0.01816 0.03521  -0.00789 67  GLN A CB  
516  C CG  . GLN A 67  ? 0.27521 0.24040 0.23874 -0.01537 0.03817  -0.00944 67  GLN A CG  
517  C CD  . GLN A 67  ? 0.32821 0.29982 0.29808 -0.01236 0.03081  -0.01107 67  GLN A CD  
518  O OE1 . GLN A 67  ? 0.33848 0.32110 0.32263 -0.01344 0.03004  -0.01243 67  GLN A OE1 
519  N NE2 . GLN A 67  ? 0.26133 0.22535 0.22034 -0.00835 0.02509  -0.01127 67  GLN A NE2 
520  N N   . ARG A 68  ? 0.33952 0.27836 0.27143 -0.01132 0.02972  -0.00392 68  ARG A N   
521  C CA  . ARG A 68  ? 0.37589 0.29790 0.28593 -0.00608 0.02838  -0.00295 68  ARG A CA  
522  C C   . ARG A 68  ? 0.35991 0.28270 0.26879 -0.00116 0.01694  -0.00414 68  ARG A C   
523  O O   . ARG A 68  ? 0.32728 0.24063 0.22212 0.00463  0.01230  -0.00530 68  ARG A O   
524  C CB  . ARG A 68  ? 0.37618 0.28492 0.27368 -0.00774 0.03537  -0.00014 68  ARG A CB  
525  C CG  . ARG A 68  ? 0.40535 0.30920 0.29989 -0.01212 0.04816  0.00053  68  ARG A CG  
526  C CD  . ARG A 68  ? 0.45740 0.34557 0.33819 -0.01418 0.05562  0.00340  68  ARG A CD  
527  N NE  . ARG A 68  ? 0.42391 0.31950 0.31767 -0.01841 0.05402  0.00371  68  ARG A NE  
528  C CZ  . ARG A 68  ? 0.37886 0.28312 0.28799 -0.02570 0.06088  0.00275  68  ARG A CZ  
529  N NH1 . ARG A 68  ? 0.38726 0.29524 0.30286 -0.02987 0.07025  0.00125  68  ARG A NH1 
530  N NH2 . ARG A 68  ? 0.40839 0.31808 0.32722 -0.02866 0.05810  0.00268  68  ARG A NH2 
531  N N   . SER A 69  ? 0.38556 0.31955 0.30924 -0.00321 0.01232  -0.00441 69  SER A N   
532  C CA  . SER A 69  ? 0.34944 0.28626 0.27550 0.00079  0.00244  -0.00629 69  SER A CA  
533  C C   . SER A 69  ? 0.36786 0.31265 0.30242 0.00187  -0.00261 -0.00933 69  SER A C   
534  O O   . SER A 69  ? 0.44743 0.39037 0.37884 0.00636  -0.01023 -0.01205 69  SER A O   
535  C CB  . SER A 69  ? 0.26664 0.21231 0.20542 -0.00197 0.00061  -0.00572 69  SER A CB  
536  O OG  . SER A 69  ? 0.27538 0.21214 0.20539 -0.00253 0.00446  -0.00336 69  SER A OG  
537  N N   . PHE A 70  ? 0.34120 0.29461 0.28690 -0.00199 0.00119  -0.00938 70  PHE A N   
538  C CA  . PHE A 70  ? 0.34427 0.30308 0.29674 -0.00108 -0.00281 -0.01209 70  PHE A CA  
539  C C   . PHE A 70  ? 0.37256 0.32130 0.31070 0.00297  -0.00260 -0.01371 70  PHE A C   
540  O O   . PHE A 70  ? 0.38478 0.33317 0.32262 0.00587  -0.00887 -0.01694 70  PHE A O   
541  C CB  . PHE A 70  ? 0.30970 0.27910 0.27670 -0.00534 0.00070  -0.01156 70  PHE A CB  
542  C CG  . PHE A 70  ? 0.33760 0.31655 0.31815 -0.00819 -0.00177 -0.01094 70  PHE A CG  
543  C CD1 . PHE A 70  ? 0.31516 0.29783 0.30228 -0.00754 -0.00766 -0.01281 70  PHE A CD1 
544  C CD2 . PHE A 70  ? 0.29958 0.28348 0.28631 -0.01162 0.00215  -0.00893 70  PHE A CD2 
545  C CE1 . PHE A 70  ? 0.28592 0.27602 0.28403 -0.01021 -0.00852 -0.01208 70  PHE A CE1 
546  C CE2 . PHE A 70  ? 0.26914 0.26020 0.26577 -0.01367 0.00008  -0.00836 70  PHE A CE2 
547  C CZ  . PHE A 70  ? 0.26432 0.25799 0.26593 -0.01293 -0.00471 -0.00964 70  PHE A CZ  
548  N N   . GLN A 71  ? 0.36343 0.30341 0.28948 0.00303  0.00498  -0.01188 71  GLN A N   
549  C CA  . GLN A 71  ? 0.41261 0.34100 0.32209 0.00730  0.00622  -0.01324 71  GLN A CA  
550  C C   . GLN A 71  ? 0.43991 0.35634 0.33257 0.01362  -0.00111 -0.01455 71  GLN A C   
551  O O   . GLN A 71  ? 0.41877 0.32853 0.30119 0.01830  -0.00531 -0.01749 71  GLN A O   
552  C CB  . GLN A 71  ? 0.41364 0.33486 0.31413 0.00538  0.01776  -0.01094 71  GLN A CB  
553  C CG  . GLN A 71  ? 0.42932 0.36046 0.34307 0.00185  0.02393  -0.01184 71  GLN A CG  
554  C CD  . GLN A 71  ? 0.48905 0.41527 0.39761 -0.00084 0.03621  -0.01041 71  GLN A CD  
555  O OE1 . GLN A 71  ? 0.46214 0.37902 0.36040 -0.00198 0.04107  -0.00794 71  GLN A OE1 
556  N NE2 . GLN A 71  ? 0.44676 0.37896 0.36293 -0.00193 0.04172  -0.01225 71  GLN A NE2 
557  N N   . ALA A 72  ? 0.39451 0.30778 0.28381 0.01446  -0.00337 -0.01287 72  ALA A N   
558  C CA  . ALA A 72  ? 0.42939 0.33199 0.30368 0.02155  -0.01175 -0.01460 72  ALA A CA  
559  C C   . ALA A 72  ? 0.45402 0.36691 0.34150 0.02365  -0.02322 -0.01946 72  ALA A C   
560  O O   . ALA A 72  ? 0.52486 0.43118 0.40272 0.03018  -0.03198 -0.02244 72  ALA A O   
561  C CB  . ALA A 72  ? 0.49819 0.39371 0.36504 0.02224  -0.01043 -0.01145 72  ALA A CB  
562  N N   . ARG A 73  ? 0.35689 0.28509 0.26594 0.01845  -0.02331 -0.02062 73  ARG A N   
563  C CA  . ARG A 73  ? 0.45381 0.39200 0.37754 0.01891  -0.03226 -0.02532 73  ARG A CA  
564  C C   . ARG A 73  ? 0.39553 0.33808 0.32659 0.01710  -0.03259 -0.02808 73  ARG A C   
565  O O   . ARG A 73  ? 0.38588 0.33802 0.33287 0.01502  -0.03729 -0.03139 73  ARG A O   
566  C CB  . ARG A 73  ? 0.40674 0.35762 0.34917 0.01435  -0.03207 -0.02422 73  ARG A CB  
567  C CG  . ARG A 73  ? 0.40238 0.34912 0.33864 0.01644  -0.03242 -0.02209 73  ARG A CG  
568  C CD  . ARG A 73  ? 0.27275 0.23138 0.22631 0.01158  -0.03053 -0.02069 73  ARG A CD  
569  N NE  . ARG A 73  ? 0.26964 0.22348 0.21684 0.01354  -0.03025 -0.01865 73  ARG A NE  
570  C CZ  . ARG A 73  ? 0.39604 0.35127 0.34554 0.01772  -0.03715 -0.02144 73  ARG A CZ  
571  N NH1 . ARG A 73  ? 0.39057 0.35309 0.35029 0.01996  -0.04489 -0.02688 73  ARG A NH1 
572  N NH2 . ARG A 73  ? 0.32069 0.27003 0.26304 0.01971  -0.03622 -0.01924 73  ARG A NH2 
573  N N   . GLY A 74  ? 0.40752 0.34259 0.32731 0.01774  -0.02703 -0.02694 74  GLY A N   
574  C CA  . GLY A 74  ? 0.39037 0.32750 0.31474 0.01703  -0.02736 -0.02976 74  GLY A CA  
575  C C   . GLY A 74  ? 0.37841 0.32580 0.31891 0.01116  -0.02148 -0.02763 74  GLY A C   
576  O O   . GLY A 74  ? 0.40215 0.35148 0.34822 0.01054  -0.02242 -0.03006 74  GLY A O   
577  N N   . SER A 75  ? 0.34151 0.29461 0.28886 0.00731  -0.01594 -0.02346 75  SER A N   
578  C CA  . SER A 75  ? 0.35226 0.31455 0.31370 0.00277  -0.01144 -0.02167 75  SER A CA  
579  C C   . SER A 75  ? 0.38948 0.35112 0.34765 0.00130  -0.00269 -0.01862 75  SER A C   
580  O O   . SER A 75  ? 0.39898 0.35163 0.34303 0.00348  0.00117  -0.01806 75  SER A O   
581  C CB  . SER A 75  ? 0.30551 0.27707 0.28118 -0.00078 -0.01356 -0.02052 75  SER A CB  
582  O OG  . SER A 75  ? 0.35059 0.32908 0.33735 -0.00413 -0.01020 -0.01892 75  SER A OG  
583  N N   . ARG A 76  ? 0.28320 0.25389 0.25421 -0.00229 0.00058  -0.01697 76  ARG A N   
584  C CA  . ARG A 76  ? 0.32618 0.29899 0.29842 -0.00405 0.00833  -0.01538 76  ARG A CA  
585  C C   . ARG A 76  ? 0.30825 0.29174 0.29529 -0.00747 0.00872  -0.01399 76  ARG A C   
586  O O   . ARG A 76  ? 0.39720 0.38517 0.39239 -0.00764 0.00504  -0.01450 76  ARG A O   
587  C CB  . ARG A 76  ? 0.34289 0.31327 0.31196 -0.00195 0.01210  -0.01734 76  ARG A CB  
588  C CG  . ARG A 76  ? 0.32535 0.30044 0.29968 -0.00386 0.02038  -0.01690 76  ARG A CG  
589  C CD  . ARG A 76  ? 0.26091 0.23273 0.23084 -0.00108 0.02471  -0.01932 76  ARG A CD  
590  N NE  . ARG A 76  ? 0.26498 0.23799 0.23884 0.00137  0.01919  -0.02140 76  ARG A NE  
591  C CZ  . ARG A 76  ? 0.32812 0.30889 0.31412 0.00151  0.01911  -0.02234 76  ARG A CZ  
592  N NH1 . ARG A 76  ? 0.27293 0.26271 0.26977 -0.00027 0.02341  -0.02206 76  ARG A NH1 
593  N NH2 . ARG A 76  ? 0.29144 0.27032 0.27863 0.00375  0.01426  -0.02399 76  ARG A NH2 
594  N N   . LEU A 77  ? 0.25123 0.23747 0.24061 -0.01009 0.01320  -0.01241 77  LEU A N   
595  C CA  . LEU A 77  ? 0.21864 0.21441 0.22062 -0.01278 0.01309  -0.01165 77  LEU A CA  
596  C C   . LEU A 77  ? 0.31169 0.31371 0.32199 -0.01227 0.01566  -0.01329 77  LEU A C   
597  O O   . LEU A 77  ? 0.27739 0.27803 0.28547 -0.01164 0.02102  -0.01473 77  LEU A O   
598  C CB  . LEU A 77  ? 0.28913 0.28540 0.29114 -0.01580 0.01647  -0.01030 77  LEU A CB  
599  C CG  . LEU A 77  ? 0.29498 0.30044 0.30874 -0.01841 0.01591  -0.01015 77  LEU A CG  
600  C CD1 . LEU A 77  ? 0.29898 0.30670 0.31582 -0.01794 0.00984  -0.00907 77  LEU A CD1 
601  C CD2 . LEU A 77  ? 0.24641 0.25082 0.25942 -0.02170 0.01995  -0.00958 77  LEU A CD2 
602  N N   . LEU A 78  ? 0.28816 0.29643 0.30746 -0.01211 0.01203  -0.01322 78  LEU A N   
603  C CA  . LEU A 78  ? 0.26530 0.27960 0.29287 -0.01038 0.01271  -0.01503 78  LEU A CA  
604  C C   . LEU A 78  ? 0.27852 0.30143 0.31580 -0.01209 0.01268  -0.01533 78  LEU A C   
605  O O   . LEU A 78  ? 0.24630 0.27027 0.28482 -0.01288 0.00876  -0.01369 78  LEU A O   
606  C CB  . LEU A 78  ? 0.20747 0.21962 0.23541 -0.00770 0.00794  -0.01494 78  LEU A CB  
607  C CG  . LEU A 78  ? 0.21890 0.22301 0.23880 -0.00596 0.00712  -0.01581 78  LEU A CG  
608  C CD1 . LEU A 78  ? 0.27813 0.27915 0.29917 -0.00466 0.00268  -0.01561 78  LEU A CD1 
609  C CD2 . LEU A 78  ? 0.22814 0.23130 0.24586 -0.00368 0.01165  -0.01827 78  LEU A CD2 
610  N N   . VAL A 79  ? 0.27454 0.30360 0.31899 -0.01264 0.01719  -0.01795 79  VAL A N   
611  C CA  . VAL A 79  ? 0.26171 0.30018 0.31733 -0.01407 0.01645  -0.01966 79  VAL A CA  
612  C C   . VAL A 79  ? 0.24240 0.28814 0.30749 -0.00990 0.01355  -0.02254 79  VAL A C   
613  O O   . VAL A 79  ? 0.26081 0.31245 0.33378 -0.00899 0.01758  -0.02613 79  VAL A O   
614  C CB  . VAL A 79  ? 0.28143 0.32293 0.34135 -0.01830 0.02353  -0.02157 79  VAL A CB  
615  C CG1 . VAL A 79  ? 0.28234 0.33424 0.35534 -0.02006 0.02165  -0.02435 79  VAL A CG1 
616  C CG2 . VAL A 79  ? 0.26876 0.30047 0.31672 -0.02133 0.02633  -0.01851 79  VAL A CG2 
617  N N   . LEU A 80  ? 0.25487 0.29971 0.31896 -0.00703 0.00688  -0.02113 80  LEU A N   
618  C CA  . LEU A 80  ? 0.26907 0.31828 0.33942 -0.00177 0.00297  -0.02345 80  LEU A CA  
619  C C   . LEU A 80  ? 0.29850 0.35873 0.38081 -0.00121 0.00037  -0.02705 80  LEU A C   
620  O O   . LEU A 80  ? 0.27622 0.33764 0.35838 -0.00387 -0.00162 -0.02626 80  LEU A O   
621  C CB  . LEU A 80  ? 0.25340 0.29408 0.31509 0.00131  -0.00249 -0.02013 80  LEU A CB  
622  C CG  . LEU A 80  ? 0.20420 0.23496 0.25681 0.00142  -0.00109 -0.01804 80  LEU A CG  
623  C CD1 . LEU A 80  ? 0.20995 0.23199 0.25536 0.00304  -0.00530 -0.01492 80  LEU A CD1 
624  C CD2 . LEU A 80  ? 0.28102 0.31269 0.33635 0.00475  0.00137  -0.02106 80  LEU A CD2 
625  N N   . ARG A 81  ? 0.26243 0.33100 0.35564 0.00266  -0.00002 -0.03166 81  ARG A N   
626  C CA  . ARG A 81  ? 0.32859 0.40938 0.43572 0.00412  -0.00364 -0.03664 81  ARG A CA  
627  C C   . ARG A 81  ? 0.28013 0.35911 0.38431 0.01117  -0.01316 -0.03643 81  ARG A C   
628  O O   . ARG A 81  ? 0.28963 0.35995 0.38497 0.01579  -0.01542 -0.03386 81  ARG A O   
629  C CB  . ARG A 81  ? 0.29885 0.39138 0.42190 0.00476  0.00119  -0.04289 81  ARG A CB  
630  C CG  . ARG A 81  ? 0.37690 0.47453 0.50737 -0.00283 0.01030  -0.04497 81  ARG A CG  
631  C CD  . ARG A 81  ? 0.31994 0.40575 0.43644 -0.00665 0.01802  -0.04034 81  ARG A CD  
632  N NE  . ARG A 81  ? 0.30395 0.39210 0.42529 -0.01322 0.02765  -0.04211 81  ARG A NE  
633  C CZ  . ARG A 81  ? 0.34410 0.42188 0.45329 -0.01645 0.03523  -0.03891 81  ARG A CZ  
634  N NH1 . ARG A 81  ? 0.23271 0.29872 0.32590 -0.01386 0.03362  -0.03450 81  ARG A NH1 
635  N NH2 . ARG A 81  ? 0.20510 0.28353 0.31784 -0.02231 0.04457  -0.04048 81  ARG A NH2 
636  N N   . GLY A 82  ? 0.32733 0.41322 0.43782 0.01212  -0.01876 -0.03930 82  GLY A N   
637  C CA  . GLY A 82  ? 0.37599 0.45919 0.48183 0.01952  -0.02831 -0.03945 82  GLY A CA  
638  C C   . GLY A 82  ? 0.41557 0.49039 0.50867 0.01801  -0.03194 -0.03526 82  GLY A C   
639  O O   . GLY A 82  ? 0.42915 0.50383 0.52112 0.01132  -0.02816 -0.03378 82  GLY A O   
640  N N   . LYS A 83  ? 0.40684 0.47325 0.48893 0.02490  -0.03919 -0.03331 83  LYS A N   
641  C CA  . LYS A 83  ? 0.39088 0.44752 0.45868 0.02445  -0.04214 -0.02920 83  LYS A CA  
642  C C   . LYS A 83  ? 0.32662 0.36725 0.37791 0.02343  -0.03850 -0.02196 83  LYS A C   
643  O O   . LYS A 83  ? 0.40749 0.44224 0.45560 0.02650  -0.03755 -0.02051 83  LYS A O   
644  C CB  . LYS A 83  ? 0.45483 0.51067 0.51872 0.03281  -0.05229 -0.03182 83  LYS A CB  
645  C CG  . LYS A 83  ? 0.43874 0.50863 0.51615 0.03219  -0.05701 -0.03874 83  LYS A CG  
646  C CD  . LYS A 83  ? 0.47464 0.54191 0.54523 0.04144  -0.06844 -0.04141 83  LYS A CD  
647  C CE  . LYS A 83  ? 0.50045 0.58131 0.58432 0.04020  -0.07380 -0.04891 83  LYS A CE  
648  N NZ  . LYS A 83  ? 0.52457 0.60315 0.60151 0.05040  -0.08650 -0.05256 83  LYS A NZ  
649  N N   . PRO A 84  ? 0.35174 0.38539 0.39339 0.01899  -0.03618 -0.01789 84  PRO A N   
650  C CA  . PRO A 84  ? 0.41675 0.43681 0.44572 0.01703  -0.03193 -0.01190 84  PRO A CA  
651  C C   . PRO A 84  ? 0.29203 0.29879 0.30797 0.02358  -0.03525 -0.00906 84  PRO A C   
652  O O   . PRO A 84  ? 0.26852 0.26555 0.27836 0.02260  -0.03150 -0.00566 84  PRO A O   
653  C CB  . PRO A 84  ? 0.33581 0.35326 0.35908 0.01203  -0.02967 -0.00947 84  PRO A CB  
654  C CG  . PRO A 84  ? 0.28882 0.31915 0.32387 0.00920  -0.03046 -0.01397 84  PRO A CG  
655  C CD  . PRO A 84  ? 0.34471 0.38339 0.38854 0.01486  -0.03644 -0.01919 84  PRO A CD  
656  N N   . GLU A 85  ? 0.39329 0.39831 0.40409 0.03046  -0.04239 -0.01060 85  GLU A N   
657  C CA  . GLU A 85  ? 0.37151 0.36105 0.36686 0.03764  -0.04565 -0.00752 85  GLU A CA  
658  C C   . GLU A 85  ? 0.42651 0.41584 0.42642 0.04264  -0.04707 -0.00921 85  GLU A C   
659  O O   . GLU A 85  ? 0.43265 0.40656 0.41916 0.04752  -0.04790 -0.00588 85  GLU A O   
660  C CB  . GLU A 85  ? 0.33716 0.32386 0.32375 0.04498  -0.05408 -0.00912 85  GLU A CB  
661  C CG  . GLU A 85  ? 0.48839 0.47132 0.46591 0.04141  -0.05291 -0.00704 85  GLU A CG  
662  C CD  . GLU A 85  ? 0.35659 0.35672 0.34992 0.03608  -0.05321 -0.01184 85  GLU A CD  
663  O OE1 . GLU A 85  ? 0.37536 0.39033 0.38659 0.03540  -0.05443 -0.01700 85  GLU A OE1 
664  O OE2 . GLU A 85  ? 0.27765 0.27569 0.26523 0.03248  -0.05160 -0.01055 85  GLU A OE2 
665  N N   . GLU A 86  ? 0.41435 0.41931 0.43215 0.04153  -0.04668 -0.01431 86  GLU A N   
666  C CA  . GLU A 86  ? 0.36445 0.37081 0.38802 0.04667  -0.04778 -0.01683 86  GLU A CA  
667  C C   . GLU A 86  ? 0.35135 0.35916 0.38085 0.04072  -0.04006 -0.01615 86  GLU A C   
668  O O   . GLU A 86  ? 0.44708 0.45136 0.47708 0.04467  -0.03990 -0.01703 86  GLU A O   
669  C CB  . GLU A 86  ? 0.35922 0.38273 0.39949 0.05165  -0.05353 -0.02445 86  GLU A CB  
670  C CG  . GLU A 86  ? 0.43440 0.45960 0.47149 0.05741  -0.06251 -0.02687 86  GLU A CG  
671  C CD  . GLU A 86  ? 0.42733 0.47289 0.48553 0.06028  -0.06762 -0.03575 86  GLU A CD  
672  O OE1 . GLU A 86  ? 0.52426 0.58054 0.59784 0.06005  -0.06452 -0.03977 86  GLU A OE1 
673  O OE2 . GLU A 86  ? 0.38381 0.43476 0.44370 0.06261  -0.07446 -0.03917 86  GLU A OE2 
674  N N   . VAL A 87  ? 0.34082 0.35280 0.37371 0.03208  -0.03422 -0.01488 87  VAL A N   
675  C CA  . VAL A 87  ? 0.38314 0.39653 0.42058 0.02699  -0.02779 -0.01483 87  VAL A CA  
676  C C   . VAL A 87  ? 0.38689 0.38619 0.41280 0.02332  -0.02420 -0.00981 87  VAL A C   
677  O O   . VAL A 87  ? 0.32063 0.31483 0.34561 0.02311  -0.02171 -0.00975 87  VAL A O   
678  C CB  . VAL A 87  ? 0.31401 0.33998 0.36200 0.02051  -0.02383 -0.01709 87  VAL A CB  
679  C CG1 . VAL A 87  ? 0.21620 0.24093 0.26499 0.01592  -0.01764 -0.01658 87  VAL A CG1 
680  C CG2 . VAL A 87  ? 0.38190 0.42255 0.44424 0.02316  -0.02604 -0.02304 87  VAL A CG2 
681  N N   . PHE A 88  ? 0.33684 0.32998 0.35464 0.02034  -0.02373 -0.00618 88  PHE A N   
682  C CA  . PHE A 88  ? 0.35725 0.33910 0.36727 0.01580  -0.01948 -0.00230 88  PHE A CA  
683  C C   . PHE A 88  ? 0.40965 0.37685 0.41071 0.01935  -0.01960 -0.00030 88  PHE A C   
684  O O   . PHE A 88  ? 0.41215 0.37412 0.41327 0.01573  -0.01600 0.00017  88  PHE A O   
685  C CB  . PHE A 88  ? 0.36531 0.34392 0.36905 0.01245  -0.01833 0.00073  88  PHE A CB  
686  C CG  . PHE A 88  ? 0.37566 0.36493 0.38698 0.00677  -0.01609 -0.00047 88  PHE A CG  
687  C CD1 . PHE A 88  ? 0.24767 0.24215 0.26606 0.00281  -0.01303 -0.00204 88  PHE A CD1 
688  C CD2 . PHE A 88  ? 0.30598 0.29858 0.31578 0.00597  -0.01729 -0.00014 88  PHE A CD2 
689  C CE1 . PHE A 88  ? 0.32580 0.32777 0.34898 -0.00161 -0.01113 -0.00285 88  PHE A CE1 
690  C CE2 . PHE A 88  ? 0.30642 0.30719 0.32227 0.00108  -0.01518 -0.00120 88  PHE A CE2 
691  C CZ  . PHE A 88  ? 0.32007 0.32514 0.34234 -0.00259 -0.01205 -0.00237 88  PHE A CZ  
692  N N   . PRO A 89  ? 0.44805 0.40711 0.44068 0.02644  -0.02380 0.00069  89  PRO A N   
693  C CA  . PRO A 89  ? 0.39526 0.33825 0.37835 0.02986  -0.02336 0.00269  89  PRO A CA  
694  C C   . PRO A 89  ? 0.45385 0.39976 0.44444 0.03101  -0.02284 -0.00058 89  PRO A C   
695  O O   . PRO A 89  ? 0.37260 0.30582 0.35751 0.03038  -0.02046 0.00075  89  PRO A O   
696  C CB  . PRO A 89  ? 0.30079 0.23661 0.27384 0.03910  -0.02953 0.00342  89  PRO A CB  
697  C CG  . PRO A 89  ? 0.43234 0.37531 0.40508 0.03817  -0.03156 0.00358  89  PRO A CG  
698  C CD  . PRO A 89  ? 0.49347 0.45496 0.48254 0.03180  -0.02935 0.00023  89  PRO A CD  
699  N N   . ARG A 90  ? 0.45937 0.42105 0.46245 0.03241  -0.02440 -0.00510 90  ARG A N   
700  C CA  . ARG A 90  ? 0.42460 0.38906 0.43402 0.03353  -0.02297 -0.00846 90  ARG A CA  
701  C C   . ARG A 90  ? 0.43854 0.40247 0.44972 0.02579  -0.01782 -0.00822 90  ARG A C   
702  O O   . ARG A 90  ? 0.43136 0.38734 0.44014 0.02574  -0.01631 -0.00895 90  ARG A O   
703  C CB  . ARG A 90  ? 0.44819 0.42958 0.47067 0.03677  -0.02466 -0.01355 90  ARG A CB  
704  C CG  . ARG A 90  ? 0.44152 0.42678 0.47047 0.03747  -0.02174 -0.01729 90  ARG A CG  
705  C CD  . ARG A 90  ? 0.38270 0.38374 0.42332 0.03344  -0.01818 -0.02056 90  ARG A CD  
706  N NE  . ARG A 90  ? 0.32547 0.33953 0.37573 0.03580  -0.02099 -0.02328 90  ARG A NE  
707  C CZ  . ARG A 90  ? 0.38069 0.40843 0.44201 0.03218  -0.01775 -0.02632 90  ARG A CZ  
708  N NH1 . ARG A 90  ? 0.36162 0.39073 0.42364 0.02672  -0.01152 -0.02648 90  ARG A NH1 
709  N NH2 . ARG A 90  ? 0.45964 0.49902 0.53092 0.03419  -0.02091 -0.02951 90  ARG A NH2 
710  N N   . VAL A 91  ? 0.46654 0.43844 0.48163 0.01969  -0.01570 -0.00765 91  VAL A N   
711  C CA  . VAL A 91  ? 0.45113 0.42344 0.46800 0.01340  -0.01209 -0.00808 91  VAL A CA  
712  C C   . VAL A 91  ? 0.45636 0.41732 0.46720 0.00898  -0.01031 -0.00518 91  VAL A C   
713  O O   . VAL A 91  ? 0.42531 0.38547 0.43807 0.00451  -0.00839 -0.00639 91  VAL A O   
714  C CB  . VAL A 91  ? 0.43055 0.41502 0.45354 0.00930  -0.01062 -0.00890 91  VAL A CB  
715  C CG1 . VAL A 91  ? 0.45463 0.45045 0.48520 0.01244  -0.01087 -0.01224 91  VAL A CG1 
716  C CG2 . VAL A 91  ? 0.39871 0.38357 0.41944 0.00682  -0.01111 -0.00593 91  VAL A CG2 
717  N N   . PHE A 92  ? 0.49922 0.45106 0.50271 0.01019  -0.01072 -0.00176 92  PHE A N   
718  C CA  . PHE A 92  ? 0.46003 0.40013 0.45843 0.00548  -0.00741 0.00077  92  PHE A CA  
719  C C   . PHE A 92  ? 0.43546 0.36429 0.43154 0.00581  -0.00652 -0.00043 92  PHE A C   
720  O O   . PHE A 92  ? 0.40423 0.32878 0.40251 0.00011  -0.00372 -0.00120 92  PHE A O   
721  C CB  . PHE A 92  ? 0.45945 0.39025 0.44791 0.00708  -0.00696 0.00503  92  PHE A CB  
722  C CG  . PHE A 92  ? 0.35094 0.28987 0.34084 0.00434  -0.00636 0.00629  92  PHE A CG  
723  C CD1 . PHE A 92  ? 0.38671 0.33591 0.38539 -0.00148 -0.00444 0.00466  92  PHE A CD1 
724  C CD2 . PHE A 92  ? 0.44850 0.38383 0.42988 0.00824  -0.00822 0.00883  92  PHE A CD2 
725  C CE1 . PHE A 92  ? 0.42938 0.38516 0.42899 -0.00365 -0.00385 0.00564  92  PHE A CE1 
726  C CE2 . PHE A 92  ? 0.45785 0.39992 0.43993 0.00586  -0.00773 0.00959  92  PHE A CE2 
727  C CZ  . PHE A 92  ? 0.44119 0.39353 0.43275 -0.00024 -0.00526 0.00804  92  PHE A CZ  
728  N N   . ARG A 93  ? 0.47993 0.40417 0.47246 0.01260  -0.00918 -0.00126 93  ARG A N   
729  C CA  . ARG A 93  ? 0.44334 0.35579 0.43283 0.01372  -0.00862 -0.00271 93  ARG A CA  
730  C C   . ARG A 93  ? 0.39559 0.31619 0.39229 0.01401  -0.00943 -0.00758 93  ARG A C   
731  O O   . ARG A 93  ? 0.47562 0.38839 0.47173 0.01202  -0.00845 -0.00972 93  ARG A O   
732  C CB  . ARG A 93  ? 0.36986 0.27074 0.35004 0.02197  -0.01119 -0.00114 93  ARG A CB  
733  C CG  . ARG A 93  ? 0.38562 0.26992 0.35315 0.02206  -0.00942 0.00402  93  ARG A CG  
734  C CD  . ARG A 93  ? 0.42192 0.31248 0.38673 0.02369  -0.01108 0.00665  93  ARG A CD  
735  N NE  . ARG A 93  ? 0.46685 0.33915 0.41609 0.02530  -0.00936 0.01171  93  ARG A NE  
736  C CZ  . ARG A 93  ? 0.51954 0.39199 0.46193 0.02711  -0.01044 0.01453  93  ARG A CZ  
737  N NH1 . ARG A 93  ? 0.46976 0.36020 0.42082 0.02708  -0.01345 0.01258  93  ARG A NH1 
738  N NH2 . ARG A 93  ? 0.52924 0.38192 0.45447 0.02901  -0.00814 0.01935  93  ARG A NH2 
739  N N   . GLU A 94  ? 0.41880 0.35404 0.42169 0.01631  -0.01081 -0.00962 94  GLU A N   
740  C CA  . GLU A 94  ? 0.42834 0.36994 0.43581 0.01688  -0.01046 -0.01397 94  GLU A CA  
741  C C   . GLU A 94  ? 0.43049 0.37409 0.44019 0.01019  -0.00897 -0.01534 94  GLU A C   
742  O O   . GLU A 94  ? 0.41533 0.35623 0.42452 0.01004  -0.00898 -0.01879 94  GLU A O   
743  C CB  . GLU A 94  ? 0.40008 0.35600 0.41370 0.02037  -0.01085 -0.01569 94  GLU A CB  
744  C CG  . GLU A 94  ? 0.36676 0.32883 0.38358 0.02059  -0.00884 -0.01976 94  GLU A CG  
745  C CD  . GLU A 94  ? 0.36233 0.33851 0.38638 0.02235  -0.00744 -0.02141 94  GLU A CD  
746  O OE1 . GLU A 94  ? 0.32396 0.30524 0.35201 0.02589  -0.00939 -0.02098 94  GLU A OE1 
747  O OE2 . GLU A 94  ? 0.38568 0.36720 0.41107 0.02020  -0.00434 -0.02340 94  GLU A OE2 
748  N N   . TRP A 95  ? 0.38591 0.33391 0.39770 0.00527  -0.00818 -0.01312 95  TRP A N   
749  C CA  . TRP A 95  ? 0.40012 0.35151 0.41496 -0.00012 -0.00773 -0.01481 95  TRP A CA  
750  C C   . TRP A 95  ? 0.38411 0.32726 0.39956 -0.00531 -0.00684 -0.01440 95  TRP A C   
751  O O   . TRP A 95  ? 0.48557 0.43162 0.50513 -0.00943 -0.00734 -0.01686 95  TRP A O   
752  C CB  . TRP A 95  ? 0.36158 0.32428 0.37964 -0.00199 -0.00728 -0.01346 95  TRP A CB  
753  C CG  . TRP A 95  ? 0.34588 0.31714 0.36511 0.00164  -0.00699 -0.01446 95  TRP A CG  
754  C CD1 . TRP A 95  ? 0.37599 0.34724 0.39453 0.00592  -0.00668 -0.01711 95  TRP A CD1 
755  C CD2 . TRP A 95  ? 0.36818 0.34914 0.39038 0.00090  -0.00620 -0.01328 95  TRP A CD2 
756  N NE1 . TRP A 95  ? 0.40686 0.38785 0.42879 0.00747  -0.00509 -0.01775 95  TRP A NE1 
757  C CE2 . TRP A 95  ? 0.35147 0.33823 0.37569 0.00424  -0.00496 -0.01545 95  TRP A CE2 
758  C CE3 . TRP A 95  ? 0.36171 0.34672 0.38535 -0.00239 -0.00603 -0.01095 95  TRP A CE3 
759  C CZ2 . TRP A 95  ? 0.34599 0.34227 0.37436 0.00368  -0.00338 -0.01547 95  TRP A CZ2 
760  C CZ3 . TRP A 95  ? 0.32446 0.31823 0.35097 -0.00239 -0.00519 -0.01085 95  TRP A CZ3 
761  C CH2 . TRP A 95  ? 0.32576 0.32501 0.35497 0.00030  -0.00381 -0.01314 95  TRP A CH2 
762  N N   . GLY A 96  ? 0.34180 0.27436 0.35329 -0.00507 -0.00538 -0.01168 96  GLY A N   
763  C CA  . GLY A 96  ? 0.40417 0.32805 0.41680 -0.01084 -0.00278 -0.01126 96  GLY A CA  
764  C C   . GLY A 96  ? 0.39874 0.33004 0.41670 -0.01604 -0.00092 -0.01009 96  GLY A C   
765  O O   . GLY A 96  ? 0.44631 0.38057 0.47158 -0.02102 -0.00074 -0.01327 96  GLY A O   
766  N N   . VAL A 97  ? 0.37486 0.30940 0.38959 -0.01452 0.00000  -0.00612 97  VAL A N   
767  C CA  . VAL A 97  ? 0.36204 0.30458 0.38105 -0.01833 0.00159  -0.00505 97  VAL A CA  
768  C C   . VAL A 97  ? 0.38333 0.31690 0.40145 -0.02309 0.00676  -0.00280 97  VAL A C   
769  O O   . VAL A 97  ? 0.37604 0.29675 0.38537 -0.02158 0.00919  0.00047  97  VAL A O   
770  C CB  . VAL A 97  ? 0.37576 0.32580 0.39157 -0.01450 0.00010  -0.00251 97  VAL A CB  
771  C CG1 . VAL A 97  ? 0.37318 0.33181 0.39343 -0.01806 0.00131  -0.00210 97  VAL A CG1 
772  C CG2 . VAL A 97  ? 0.33991 0.29706 0.35674 -0.01005 -0.00335 -0.00477 97  VAL A CG2 
773  N N   . THR A 98  ? 0.32338 0.26310 0.35026 -0.02859 0.00877  -0.00472 98  THR A N   
774  C CA  . THR A 98  ? 0.34434 0.27771 0.37253 -0.03394 0.01515  -0.00312 98  THR A CA  
775  C C   . THR A 98  ? 0.31947 0.26132 0.35010 -0.03551 0.01723  -0.00168 98  THR A C   
776  O O   . THR A 98  ? 0.36678 0.30319 0.39703 -0.03947 0.02361  0.00013  98  THR A O   
777  C CB  . THR A 98  ? 0.33052 0.26281 0.37015 -0.04015 0.01697  -0.00808 98  THR A CB  
778  O OG1 . THR A 98  ? 0.34209 0.28850 0.39266 -0.04082 0.01221  -0.01317 98  THR A OG1 
779  C CG2 . THR A 98  ? 0.34254 0.26345 0.37853 -0.03913 0.01584  -0.00946 98  THR A CG2 
780  N N   . GLN A 99  ? 0.27864 0.23247 0.31114 -0.03266 0.01276  -0.00248 99  GLN A N   
781  C CA  . GLN A 99  ? 0.30106 0.26246 0.33548 -0.03371 0.01428  -0.00145 99  GLN A CA  
782  C C   . GLN A 99  ? 0.34973 0.31817 0.37957 -0.02882 0.00973  -0.00028 99  GLN A C   
783  O O   . GLN A 99  ? 0.25747 0.23088 0.28908 -0.02645 0.00536  -0.00248 99  GLN A O   
784  C CB  . GLN A 99  ? 0.25390 0.22471 0.30178 -0.03786 0.01431  -0.00609 99  GLN A CB  
785  C CG  . GLN A 99  ? 0.28956 0.26735 0.34002 -0.03890 0.01656  -0.00540 99  GLN A CG  
786  C CD  . GLN A 99  ? 0.32140 0.30950 0.38585 -0.04154 0.01519  -0.01071 99  GLN A CD  
787  O OE1 . GLN A 99  ? 0.28601 0.28082 0.35335 -0.03908 0.00912  -0.01372 99  GLN A OE1 
788  N NE2 . GLN A 99  ? 0.28523 0.27420 0.35811 -0.04621 0.02099  -0.01213 99  GLN A NE2 
789  N N   . LEU A 100 ? 0.30069 0.26886 0.32439 -0.02752 0.01119  0.00286  100 LEU A N   
790  C CA  . LEU A 100 ? 0.31635 0.29135 0.33712 -0.02382 0.00742  0.00345  100 LEU A CA  
791  C C   . LEU A 100 ? 0.34305 0.32405 0.36607 -0.02566 0.00900  0.00349  100 LEU A C   
792  O O   . LEU A 100 ? 0.34317 0.31939 0.36223 -0.02705 0.01318  0.00556  100 LEU A O   
793  C CB  . LEU A 100 ? 0.35309 0.32173 0.36357 -0.01925 0.00603  0.00638  100 LEU A CB  
794  C CG  . LEU A 100 ? 0.35944 0.33544 0.36837 -0.01599 0.00235  0.00629  100 LEU A CG  
795  C CD1 . LEU A 100 ? 0.21518 0.20039 0.23113 -0.01529 -0.00074 0.00330  100 LEU A CD1 
796  C CD2 . LEU A 100 ? 0.36549 0.33511 0.36492 -0.01087 -0.00001 0.00830  100 LEU A CD2 
797  N N   . CYS A 101 ? 0.31356 0.30365 0.34163 -0.02539 0.00613  0.00126  101 CYS A N   
798  C CA  . CYS A 101 ? 0.31722 0.31282 0.34762 -0.02656 0.00703  0.00080  101 CYS A CA  
799  C C   . CYS A 101 ? 0.27391 0.27368 0.30073 -0.02398 0.00409  0.00122  101 CYS A C   
800  O O   . CYS A 101 ? 0.23233 0.23485 0.25997 -0.02245 0.00128  0.00007  101 CYS A O   
801  C CB  . CYS A 101 ? 0.30495 0.30629 0.34459 -0.02849 0.00622  -0.00275 101 CYS A CB  
802  S SG  . CYS A 101 ? 0.31942 0.31836 0.36776 -0.03260 0.00958  -0.00506 101 CYS A SG  
803  N N   . PHE A 102 ? 0.28447 0.28422 0.30737 -0.02376 0.00526  0.00254  102 PHE A N   
804  C CA  . PHE A 102 ? 0.32162 0.32546 0.34260 -0.02223 0.00275  0.00216  102 PHE A CA  
805  C C   . PHE A 102 ? 0.35551 0.35980 0.37450 -0.02302 0.00464  0.00244  102 PHE A C   
806  O O   . PHE A 102 ? 0.31604 0.31607 0.33211 -0.02381 0.00811  0.00374  102 PHE A O   
807  C CB  . PHE A 102 ? 0.29427 0.29655 0.31049 -0.01932 0.00018  0.00295  102 PHE A CB  
808  C CG  . PHE A 102 ? 0.30710 0.30161 0.31506 -0.01764 0.00118  0.00534  102 PHE A CG  
809  C CD1 . PHE A 102 ? 0.36467 0.35710 0.36589 -0.01653 0.00114  0.00612  102 PHE A CD1 
810  C CD2 . PHE A 102 ? 0.28166 0.26921 0.28680 -0.01681 0.00217  0.00679  102 PHE A CD2 
811  C CE1 . PHE A 102 ? 0.31956 0.30251 0.30995 -0.01423 0.00214  0.00856  102 PHE A CE1 
812  C CE2 . PHE A 102 ? 0.27242 0.24996 0.26711 -0.01480 0.00354  0.00948  102 PHE A CE2 
813  C CZ  . PHE A 102 ? 0.37245 0.34740 0.35903 -0.01329 0.00353  0.01050  102 PHE A CZ  
814  N N   . GLU A 103 ? 0.36055 0.36899 0.38054 -0.02288 0.00300  0.00114  103 GLU A N   
815  C CA  . GLU A 103 ? 0.29455 0.30324 0.31265 -0.02326 0.00446  0.00089  103 GLU A CA  
816  C C   . GLU A 103 ? 0.27814 0.28273 0.28808 -0.02185 0.00458  0.00221  103 GLU A C   
817  O O   . GLU A 103 ? 0.28135 0.28540 0.28821 -0.02007 0.00148  0.00229  103 GLU A O   
818  C CB  . GLU A 103 ? 0.21216 0.22412 0.23185 -0.02331 0.00260  -0.00076 103 GLU A CB  
819  C CG  . GLU A 103 ? 0.22075 0.23266 0.23949 -0.02341 0.00401  -0.00153 103 GLU A CG  
820  C CD  . GLU A 103 ? 0.28602 0.29852 0.30445 -0.02336 0.00240  -0.00285 103 GLU A CD  
821  O OE1 . GLU A 103 ? 0.26910 0.28151 0.28561 -0.02378 0.00103  -0.00318 103 GLU A OE1 
822  O OE2 . GLU A 103 ? 0.28232 0.29496 0.30257 -0.02280 0.00253  -0.00384 103 GLU A OE2 
823  N N   . HIS A 104 ? 0.27637 0.27802 0.28268 -0.02219 0.00802  0.00279  104 HIS A N   
824  C CA  . HIS A 104 ? 0.22581 0.22141 0.22140 -0.02023 0.00838  0.00408  104 HIS A CA  
825  C C   . HIS A 104 ? 0.30835 0.30614 0.30128 -0.01883 0.00405  0.00221  104 HIS A C   
826  O O   . HIS A 104 ? 0.31070 0.31287 0.30859 -0.02009 0.00342  0.00032  104 HIS A O   
827  C CB  . HIS A 104 ? 0.28130 0.27276 0.27328 -0.02112 0.01444  0.00490  104 HIS A CB  
828  C CG  . HIS A 104 ? 0.30194 0.28468 0.27966 -0.01862 0.01551  0.00650  104 HIS A CG  
829  N ND1 . HIS A 104 ? 0.27167 0.24581 0.23949 -0.01649 0.01539  0.00905  104 HIS A ND1 
830  C CD2 . HIS A 104 ? 0.35250 0.33238 0.32241 -0.01725 0.01639  0.00578  104 HIS A CD2 
831  C CE1 . HIS A 104 ? 0.35704 0.32298 0.31060 -0.01364 0.01593  0.00996  104 HIS A CE1 
832  N NE2 . HIS A 104 ? 0.38388 0.35343 0.33865 -0.01420 0.01662  0.00786  104 HIS A NE2 
833  N N   . ASP A 105 ? 0.29255 0.28655 0.27737 -0.01599 0.00077  0.00240  105 ASP A N   
834  C CA  . ASP A 105 ? 0.28927 0.28561 0.27251 -0.01471 -0.00405 -0.00036 105 ASP A CA  
835  C C   . ASP A 105 ? 0.31866 0.30712 0.28808 -0.01129 -0.00513 0.00003  105 ASP A C   
836  O O   . ASP A 105 ? 0.36472 0.34561 0.32496 -0.00872 -0.00425 0.00259  105 ASP A O   
837  C CB  . ASP A 105 ? 0.27751 0.27945 0.26727 -0.01394 -0.00912 -0.00226 105 ASP A CB  
838  C CG  . ASP A 105 ? 0.38837 0.39564 0.38259 -0.01475 -0.01289 -0.00626 105 ASP A CG  
839  O OD1 . ASP A 105 ? 0.43850 0.44292 0.42655 -0.01407 -0.01398 -0.00768 105 ASP A OD1 
840  O OD2 . ASP A 105 ? 0.36387 0.37769 0.36777 -0.01632 -0.01426 -0.00828 105 ASP A OD2 
841  N N   . THR A 106 ? 0.43146 0.42016 0.39789 -0.01102 -0.00698 -0.00257 106 THR A N   
842  C CA  . THR A 106 ? 0.36166 0.34198 0.31316 -0.00744 -0.00812 -0.00277 106 THR A CA  
843  C C   . THR A 106 ? 0.39984 0.38230 0.34974 -0.00473 -0.01660 -0.00700 106 THR A C   
844  O O   . THR A 106 ? 0.42269 0.40007 0.36227 -0.00233 -0.01890 -0.00898 106 THR A O   
845  C CB  . THR A 106 ? 0.31564 0.29307 0.26336 -0.00880 -0.00287 -0.00290 106 THR A CB  
846  O OG1 . THR A 106 ? 0.36701 0.35127 0.32427 -0.01143 -0.00461 -0.00617 106 THR A OG1 
847  C CG2 . THR A 106 ? 0.40818 0.38452 0.35904 -0.01114 0.00530  0.00028  106 THR A CG2 
848  N N   . GLU A 107 ? 0.41192 0.40218 0.37259 -0.00503 -0.02129 -0.00903 107 GLU A N   
849  C CA  . GLU A 107 ? 0.40441 0.39903 0.36746 -0.00277 -0.02956 -0.01418 107 GLU A CA  
850  C C   . GLU A 107 ? 0.43657 0.42569 0.38912 0.00387  -0.03535 -0.01391 107 GLU A C   
851  O O   . GLU A 107 ? 0.50238 0.48562 0.44912 0.00576  -0.03254 -0.00948 107 GLU A O   
852  C CB  . GLU A 107 ? 0.39328 0.39976 0.37472 -0.00663 -0.03080 -0.01725 107 GLU A CB  
853  C CG  . GLU A 107 ? 0.39256 0.40241 0.38186 -0.01228 -0.02668 -0.01849 107 GLU A CG  
854  C CD  . GLU A 107 ? 0.29751 0.31689 0.30266 -0.01612 -0.02721 -0.02179 107 GLU A CD  
855  O OE1 . GLU A 107 ? 0.37624 0.40116 0.38813 -0.01459 -0.03006 -0.02302 107 GLU A OE1 
856  O OE2 . GLU A 107 ? 0.27785 0.29830 0.28814 -0.02052 -0.02425 -0.02320 107 GLU A OE2 
857  N N   . PRO A 108 ? 0.43471 0.42466 0.38398 0.00788  -0.04389 -0.01892 108 PRO A N   
858  C CA  . PRO A 108 ? 0.43641 0.41954 0.37325 0.01580  -0.05074 -0.01894 108 PRO A CA  
859  C C   . PRO A 108 ? 0.42358 0.41133 0.36898 0.01751  -0.05232 -0.01794 108 PRO A C   
860  O O   . PRO A 108 ? 0.46141 0.43869 0.39421 0.02178  -0.05116 -0.01339 108 PRO A O   
861  C CB  . PRO A 108 ? 0.46908 0.45651 0.40685 0.01897  -0.06092 -0.02651 108 PRO A CB  
862  C CG  . PRO A 108 ? 0.45959 0.44874 0.40044 0.01337  -0.05719 -0.02838 108 PRO A CG  
863  C CD  . PRO A 108 ? 0.43842 0.43335 0.39265 0.00597  -0.04789 -0.02490 108 PRO A CD  
864  N N   . TYR A 109 ? 0.45598 0.45819 0.42200 0.01427  -0.05431 -0.02216 109 TYR A N   
865  C CA  . TYR A 109 ? 0.46486 0.47190 0.43958 0.01610  -0.05537 -0.02170 109 TYR A CA  
866  C C   . TYR A 109 ? 0.42620 0.42808 0.39920 0.01284  -0.04633 -0.01505 109 TYR A C   
867  O O   . TYR A 109 ? 0.48799 0.48597 0.45818 0.01631  -0.04668 -0.01262 109 TYR A O   
868  C CB  . TYR A 109 ? 0.51721 0.54088 0.51483 0.01259  -0.05766 -0.02793 109 TYR A CB  
869  C CG  . TYR A 109 ? 0.44780 0.47730 0.45613 0.01314  -0.05630 -0.02730 109 TYR A CG  
870  C CD1 . TYR A 109 ? 0.55488 0.58353 0.56074 0.02093  -0.06318 -0.02870 109 TYR A CD1 
871  C CD2 . TYR A 109 ? 0.49038 0.52513 0.50991 0.00661  -0.04843 -0.02550 109 TYR A CD2 
872  C CE1 . TYR A 109 ? 0.55454 0.58809 0.56995 0.02184  -0.06178 -0.02844 109 TYR A CE1 
873  C CE2 . TYR A 109 ? 0.49367 0.53290 0.52171 0.00740  -0.04698 -0.02521 109 TYR A CE2 
874  C CZ  . TYR A 109 ? 0.53440 0.57334 0.56092 0.01484  -0.05342 -0.02675 109 TYR A CZ  
875  O OH  . TYR A 109 ? 0.46095 0.50400 0.49578 0.01600  -0.05183 -0.02677 109 TYR A OH  
876  N N   . ALA A 110 ? 0.40503 0.40654 0.37982 0.00657  -0.03872 -0.01257 110 ALA A N   
877  C CA  . ALA A 110 ? 0.45173 0.44983 0.42704 0.00333  -0.03098 -0.00748 110 ALA A CA  
878  C C   . ALA A 110 ? 0.39309 0.37678 0.35122 0.00659  -0.02814 -0.00242 110 ALA A C   
879  O O   . ALA A 110 ? 0.41022 0.38990 0.36801 0.00640  -0.02470 0.00087  110 ALA A O   
880  C CB  . ALA A 110 ? 0.41670 0.41819 0.39822 -0.00310 -0.02480 -0.00694 110 ALA A CB  
881  N N   . LYS A 111 ? 0.45967 0.43430 0.40265 0.00944  -0.02898 -0.00186 111 LYS A N   
882  C CA  . LYS A 111 ? 0.50136 0.46015 0.42601 0.01226  -0.02473 0.00319  111 LYS A CA  
883  C C   . LYS A 111 ? 0.44921 0.40052 0.36545 0.01884  -0.02967 0.00439  111 LYS A C   
884  O O   . LYS A 111 ? 0.49914 0.43889 0.40616 0.01941  -0.02453 0.00913  111 LYS A O   
885  C CB  . LYS A 111 ? 0.49416 0.44386 0.40251 0.01449  -0.02439 0.00322  111 LYS A CB  
886  C CG  . LYS A 111 ? 0.47698 0.43024 0.39037 0.00856  -0.01741 0.00322  111 LYS A CG  
887  C CD  . LYS A 111 ? 0.43011 0.37442 0.32701 0.01138  -0.01743 0.00253  111 LYS A CD  
888  C CE  . LYS A 111 ? 0.36445 0.31306 0.26761 0.00610  -0.01088 0.00190  111 LYS A CE  
889  N NZ  . LYS A 111 ? 0.32739 0.26797 0.21511 0.00899  -0.01121 0.00038  111 LYS A NZ  
890  N N   . VAL A 112 ? 0.48114 0.43871 0.40101 0.02395  -0.03962 -0.00026 112 VAL A N   
891  C CA  . VAL A 112 ? 0.40537 0.35701 0.31877 0.03129  -0.04548 0.00011  112 VAL A CA  
892  C C   . VAL A 112 ? 0.41057 0.37021 0.33986 0.02860  -0.04334 0.00038  112 VAL A C   
893  O O   . VAL A 112 ? 0.42688 0.37690 0.34883 0.03204  -0.04258 0.00358  112 VAL A O   
894  C CB  . VAL A 112 ? 0.46724 0.42404 0.38043 0.03847  -0.05781 -0.00613 112 VAL A CB  
895  C CG1 . VAL A 112 ? 0.33867 0.28934 0.24516 0.04742  -0.06487 -0.00623 112 VAL A CG1 
896  C CG2 . VAL A 112 ? 0.36021 0.30756 0.25551 0.04152  -0.06027 -0.00668 112 VAL A CG2 
897  N N   . ARG A 113 ? 0.42230 0.39800 0.37199 0.02260  -0.04197 -0.00291 113 ARG A N   
898  C CA  . ARG A 113 ? 0.40989 0.39286 0.37362 0.02013  -0.03960 -0.00301 113 ARG A CA  
899  C C   . ARG A 113 ? 0.38324 0.35719 0.34236 0.01617  -0.03095 0.00253  113 ARG A C   
900  O O   . ARG A 113 ? 0.36584 0.33558 0.32486 0.01786  -0.03015 0.00418  113 ARG A O   
901  C CB  . ARG A 113 ? 0.39923 0.39871 0.38259 0.01442  -0.03884 -0.00734 113 ARG A CB  
902  C CG  . ARG A 113 ? 0.40173 0.40767 0.39780 0.01142  -0.03516 -0.00731 113 ARG A CG  
903  C CD  . ARG A 113 ? 0.38277 0.40036 0.39319 0.00488  -0.03182 -0.00999 113 ARG A CD  
904  N NE  . ARG A 113 ? 0.40842 0.42242 0.41436 0.00002  -0.02688 -0.00751 113 ARG A NE  
905  C CZ  . ARG A 113 ? 0.30897 0.32913 0.32313 -0.00535 -0.02342 -0.00873 113 ARG A CZ  
906  N NH1 . ARG A 113 ? 0.34236 0.37176 0.36892 -0.00739 -0.02321 -0.01206 113 ARG A NH1 
907  N NH2 . ARG A 113 ? 0.33809 0.35423 0.34736 -0.00848 -0.01964 -0.00663 113 ARG A NH2 
908  N N   . ASP A 114 ? 0.38464 0.35591 0.34096 0.01093  -0.02452 0.00482  114 ASP A N   
909  C CA  . ASP A 114 ? 0.39268 0.35742 0.34778 0.00657  -0.01640 0.00884  114 ASP A CA  
910  C C   . ASP A 114 ? 0.45490 0.40212 0.39266 0.01024  -0.01417 0.01318  114 ASP A C   
911  O O   . ASP A 114 ? 0.45788 0.39930 0.39616 0.00857  -0.00996 0.01555  114 ASP A O   
912  C CB  . ASP A 114 ? 0.45678 0.42416 0.41460 0.00080  -0.01054 0.00930  114 ASP A CB  
913  C CG  . ASP A 114 ? 0.40299 0.38474 0.37615 -0.00297 -0.01176 0.00569  114 ASP A CG  
914  O OD1 . ASP A 114 ? 0.34379 0.33359 0.32603 -0.00193 -0.01595 0.00295  114 ASP A OD1 
915  O OD2 . ASP A 114 ? 0.35043 0.33467 0.32610 -0.00677 -0.00808 0.00555  114 ASP A OD2 
916  N N   . ALA A 115 ? 0.45009 0.38732 0.37121 0.01534  -0.01683 0.01417  115 ALA A N   
917  C CA  . ALA A 115 ? 0.43981 0.35724 0.34084 0.01953  -0.01434 0.01876  115 ALA A CA  
918  C C   . ALA A 115 ? 0.44128 0.35447 0.34117 0.02491  -0.01919 0.01893  115 ALA A C   
919  O O   . ALA A 115 ? 0.60212 0.49918 0.48981 0.02619  -0.01492 0.02314  115 ALA A O   
920  C CB  . ALA A 115 ? 0.43601 0.34275 0.31710 0.02536  -0.01759 0.01930  115 ALA A CB  
921  N N   . ALA A 116 ? 0.41551 0.34250 0.32821 0.02803  -0.02751 0.01419  116 ALA A N   
922  C CA  . ALA A 116 ? 0.46567 0.39084 0.38020 0.03317  -0.03186 0.01358  116 ALA A CA  
923  C C   . ALA A 116 ? 0.46235 0.39070 0.38900 0.02706  -0.02549 0.01460  116 ALA A C   
924  O O   . ALA A 116 ? 0.45153 0.36932 0.37261 0.02964  -0.02458 0.01673  116 ALA A O   
925  C CB  . ALA A 116 ? 0.43884 0.37940 0.36566 0.03810  -0.04193 0.00729  116 ALA A CB  
926  N N   . VAL A 117 ? 0.41694 0.35861 0.35908 0.01939  -0.02145 0.01290  117 VAL A N   
927  C CA  . VAL A 117 ? 0.49545 0.44021 0.44842 0.01399  -0.01633 0.01318  117 VAL A CA  
928  C C   . VAL A 117 ? 0.47371 0.40402 0.41772 0.01009  -0.00824 0.01761  117 VAL A C   
929  O O   . VAL A 117 ? 0.50350 0.42873 0.44984 0.00839  -0.00530 0.01845  117 VAL A O   
930  C CB  . VAL A 117 ? 0.42092 0.38225 0.39050 0.00795  -0.01498 0.01005  117 VAL A CB  
931  C CG1 . VAL A 117 ? 0.34089 0.30474 0.32000 0.00341  -0.01090 0.00979  117 VAL A CG1 
932  C CG2 . VAL A 117 ? 0.41258 0.38723 0.39151 0.01087  -0.02149 0.00549  117 VAL A CG2 
933  N N   . ARG A 118 ? 0.43538 0.35864 0.36942 0.00840  -0.00406 0.02007  118 ARG A N   
934  C CA  . ARG A 118 ? 0.53148 0.44114 0.45804 0.00407  0.00506  0.02387  118 ARG A CA  
935  C C   . ARG A 118 ? 0.53013 0.42065 0.44136 0.00859  0.00575  0.02733  118 ARG A C   
936  O O   . ARG A 118 ? 0.49008 0.37172 0.40164 0.00439  0.01234  0.02914  118 ARG A O   
937  C CB  . ARG A 118 ? 0.54687 0.45203 0.46427 0.00234  0.00983  0.02563  118 ARG A CB  
938  C CG  . ARG A 118 ? 0.46200 0.38359 0.39371 -0.00255 0.01054  0.02253  118 ARG A CG  
939  C CD  . ARG A 118 ? 0.65497 0.57106 0.57615 -0.00317 0.01505  0.02401  118 ARG A CD  
940  N NE  . ARG A 118 ? 0.50961 0.44038 0.44337 -0.00684 0.01503  0.02088  118 ARG A NE  
941  C CZ  . ARG A 118 ? 0.48838 0.42521 0.43376 -0.01301 0.02131  0.01998  118 ARG A CZ  
942  N NH1 . ARG A 118 ? 0.51942 0.45050 0.46768 -0.01713 0.02840  0.02138  118 ARG A NH1 
943  N NH2 . ARG A 118 ? 0.54184 0.49058 0.49660 -0.01492 0.02021  0.01715  118 ARG A NH2 
944  N N   . ARG A 119 ? 0.53599 0.41938 0.43360 0.01740  -0.00134 0.02790  119 ARG A N   
945  C CA  . ARG A 119 ? 0.50074 0.36427 0.38168 0.02325  -0.00178 0.03123  119 ARG A CA  
946  C C   . ARG A 119 ? 0.46911 0.33657 0.36088 0.02438  -0.00485 0.02919  119 ARG A C   
947  O O   . ARG A 119 ? 0.57708 0.42732 0.45791 0.02674  -0.00268 0.03205  119 ARG A O   
948  C CB  . ARG A 119 ? 0.58472 0.43969 0.44745 0.03377  -0.01004 0.03172  119 ARG A CB  
949  C CG  . ARG A 119 ? 0.55086 0.39235 0.39393 0.03423  -0.00563 0.03521  119 ARG A CG  
950  C CD  . ARG A 119 ? 0.55248 0.38471 0.37601 0.04575  -0.01540 0.03503  119 ARG A CD  
951  N NE  . ARG A 119 ? 0.53406 0.38459 0.36726 0.04719  -0.02323 0.02990  119 ARG A NE  
952  C CZ  . ARG A 119 ? 0.51486 0.38351 0.36441 0.05064  -0.03332 0.02415  119 ARG A CZ  
953  N NH1 . ARG A 119 ? 0.50951 0.38157 0.36782 0.05363  -0.03716 0.02264  119 ARG A NH1 
954  N NH2 . ARG A 119 ? 0.50034 0.38378 0.35801 0.05088  -0.03916 0.01946  119 ARG A NH2 
955  N N   . LEU A 120 ? 0.53663 0.42489 0.44841 0.02279  -0.00925 0.02437  120 LEU A N   
956  C CA  . LEU A 120 ? 0.49451 0.38684 0.41655 0.02364  -0.01132 0.02207  120 LEU A CA  
957  C C   . LEU A 120 ? 0.44954 0.34145 0.38066 0.01491  -0.00355 0.02236  120 LEU A C   
958  O O   . LEU A 120 ? 0.53450 0.41820 0.46514 0.01533  -0.00241 0.02255  120 LEU A O   
959  C CB  . LEU A 120 ? 0.45301 0.36640 0.39145 0.02568  -0.01822 0.01667  120 LEU A CB  
960  C CG  . LEU A 120 ? 0.49685 0.41364 0.43092 0.03461  -0.02729 0.01449  120 LEU A CG  
961  C CD1 . LEU A 120 ? 0.55976 0.49859 0.51331 0.03447  -0.03191 0.00860  120 LEU A CD1 
962  C CD2 . LEU A 120 ? 0.53580 0.43736 0.45652 0.04387  -0.03170 0.01583  120 LEU A CD2 
963  N N   . ALA A 121 ? 0.44948 0.35015 0.38922 0.00736  0.00126  0.02182  121 ALA A N   
964  C CA  . ALA A 121 ? 0.42679 0.32827 0.37646 -0.00058 0.00761  0.02107  121 ALA A CA  
965  C C   . ALA A 121 ? 0.47691 0.35860 0.41534 -0.00346 0.01539  0.02488  121 ALA A C   
966  O O   . ALA A 121 ? 0.48304 0.36123 0.42813 -0.00849 0.01953  0.02386  121 ALA A O   
967  C CB  . ALA A 121 ? 0.33684 0.25309 0.29877 -0.00671 0.00983  0.01898  121 ALA A CB  
968  N N   . ALA A 122 ? 0.40069 0.26844 0.32158 -0.00049 0.01776  0.02902  122 ALA A N   
969  C CA  . ALA A 122 ? 0.54655 0.39257 0.45419 -0.00316 0.02654  0.03318  122 ALA A CA  
970  C C   . ALA A 122 ? 0.53791 0.36825 0.43645 0.00147  0.02468  0.03457  122 ALA A C   
971  O O   . ALA A 122 ? 0.53050 0.34751 0.42757 -0.00346 0.03189  0.03582  122 ALA A O   
972  C CB  . ALA A 122 ? 0.47715 0.31030 0.36507 -0.00026 0.02976  0.03749  122 ALA A CB  
973  N N   . GLU A 123 ? 0.58329 0.41503 0.47648 0.01097  0.01512  0.03387  123 GLU A N   
974  C CA  . GLU A 123 ? 0.56247 0.38029 0.44773 0.01661  0.01239  0.03461  123 GLU A CA  
975  C C   . GLU A 123 ? 0.50735 0.33392 0.41026 0.01183  0.01277  0.03058  123 GLU A C   
976  O O   . GLU A 123 ? 0.49610 0.30745 0.39361 0.01222  0.01498  0.03145  123 GLU A O   
977  C CB  . GLU A 123 ? 0.56774 0.38827 0.44620 0.02846  0.00132  0.03357  123 GLU A CB  
978  C CG  . GLU A 123 ? 0.63675 0.44678 0.49529 0.03488  -0.00095 0.03695  123 GLU A CG  
979  C CD  . GLU A 123 ? 0.67445 0.49372 0.53238 0.04585  -0.01338 0.03383  123 GLU A CD  
980  O OE1 . GLU A 123 ? 0.58063 0.41626 0.45551 0.04757  -0.01903 0.02903  123 GLU A OE1 
981  O OE2 . GLU A 123 ? 0.65442 0.46466 0.49513 0.05282  -0.01743 0.03572  123 GLU A OE2 
982  N N   . ALA A 124 ? 0.56096 0.41025 0.48338 0.00762  0.01062  0.02612  124 ALA A N   
983  C CA  . ALA A 124 ? 0.49432 0.35243 0.43225 0.00360  0.01033  0.02184  124 ALA A CA  
984  C C   . ALA A 124 ? 0.52805 0.38508 0.47477 -0.00678 0.01820  0.02092  124 ALA A C   
985  O O   . ALA A 124 ? 0.56525 0.42467 0.52195 -0.01009 0.01826  0.01738  124 ALA A O   
986  C CB  . ALA A 124 ? 0.45186 0.33319 0.40448 0.00483  0.00421  0.01744  124 ALA A CB  
987  N N   . GLY A 125 ? 0.54787 0.40177 0.49173 -0.01174 0.02463  0.02338  125 GLY A N   
988  C CA  . GLY A 125 ? 0.48990 0.34513 0.44505 -0.02163 0.03215  0.02152  125 GLY A CA  
989  C C   . GLY A 125 ? 0.51733 0.39509 0.49121 -0.02580 0.02978  0.01681  125 GLY A C   
990  O O   . GLY A 125 ? 0.54444 0.42748 0.53205 -0.03193 0.03160  0.01270  125 GLY A O   
991  N N   . VAL A 126 ? 0.44807 0.33844 0.42239 -0.02234 0.02540  0.01698  126 VAL A N   
992  C CA  . VAL A 126 ? 0.36656 0.27654 0.35583 -0.02498 0.02259  0.01302  126 VAL A CA  
993  C C   . VAL A 126 ? 0.35192 0.26558 0.34222 -0.02864 0.02749  0.01420  126 VAL A C   
994  O O   . VAL A 126 ? 0.49738 0.40536 0.47542 -0.02542 0.02843  0.01787  126 VAL A O   
995  C CB  . VAL A 126 ? 0.43012 0.35151 0.42018 -0.01881 0.01458  0.01177  126 VAL A CB  
996  C CG1 . VAL A 126 ? 0.38955 0.32805 0.39208 -0.02142 0.01252  0.00837  126 VAL A CG1 
997  C CG2 . VAL A 126 ? 0.40965 0.32780 0.39934 -0.01495 0.01057  0.01014  126 VAL A CG2 
998  N N   . GLU A 127 ? 0.35763 0.28066 0.36231 -0.03478 0.03018  0.01062  127 GLU A N   
999  C CA  . GLU A 127 ? 0.35411 0.28225 0.36221 -0.03821 0.03506  0.01081  127 GLU A CA  
1000 C C   . GLU A 127 ? 0.27007 0.21123 0.27904 -0.03450 0.02941  0.01030  127 GLU A C   
1001 O O   . GLU A 127 ? 0.25846 0.21064 0.27523 -0.03308 0.02332  0.00724  127 GLU A O   
1002 C CB  . GLU A 127 ? 0.33522 0.27044 0.36064 -0.04533 0.03892  0.00606  127 GLU A CB  
1003 C CG  . GLU A 127 ? 0.44245 0.38554 0.47447 -0.04848 0.04364  0.00512  127 GLU A CG  
1004 C CD  . GLU A 127 ? 0.52750 0.48034 0.57959 -0.05462 0.04588  -0.00095 127 GLU A CD  
1005 O OE1 . GLU A 127 ? 0.42539 0.37736 0.48532 -0.05697 0.04410  -0.00434 127 GLU A OE1 
1006 O OE2 . GLU A 127 ? 0.67274 0.63438 0.73323 -0.05674 0.04897  -0.00290 127 GLU A OE2 
1007 N N   . VAL A 128 ? 0.33114 0.26967 0.33101 -0.03300 0.03185  0.01323  128 VAL A N   
1008 C CA  . VAL A 128 ? 0.27663 0.22546 0.27608 -0.02974 0.02701  0.01278  128 VAL A CA  
1009 C C   . VAL A 128 ? 0.30612 0.26338 0.31449 -0.03364 0.03085  0.01075  128 VAL A C   
1010 O O   . VAL A 128 ? 0.31155 0.26268 0.31722 -0.03655 0.03842  0.01209  128 VAL A O   
1011 C CB  . VAL A 128 ? 0.28731 0.22764 0.26999 -0.02435 0.02547  0.01654  128 VAL A CB  
1012 C CG1 . VAL A 128 ? 0.43103 0.38230 0.41493 -0.02172 0.02034  0.01519  128 VAL A CG1 
1013 C CG2 . VAL A 128 ? 0.33034 0.26243 0.30500 -0.01958 0.02122  0.01800  128 VAL A CG2 
1014 N N   . VAL A 129 ? 0.34911 0.31956 0.36750 -0.03340 0.02609  0.00745  129 VAL A N   
1015 C CA  . VAL A 129 ? 0.27379 0.25312 0.30096 -0.03570 0.02813  0.00498  129 VAL A CA  
1016 C C   . VAL A 129 ? 0.29881 0.28410 0.32201 -0.03210 0.02335  0.00516  129 VAL A C   
1017 O O   . VAL A 129 ? 0.24637 0.23680 0.27129 -0.02992 0.01741  0.00401  129 VAL A O   
1018 C CB  . VAL A 129 ? 0.29367 0.28193 0.33668 -0.03852 0.02653  0.00013  129 VAL A CB  
1019 C CG1 . VAL A 129 ? 0.29041 0.28760 0.34285 -0.03999 0.02841  -0.00282 129 VAL A CG1 
1020 C CG2 . VAL A 129 ? 0.38107 0.36333 0.42912 -0.04251 0.03056  -0.00085 129 VAL A CG2 
1021 N N   . THR A 130 ? 0.29441 0.27824 0.31203 -0.03172 0.02657  0.00639  130 THR A N   
1022 C CA  . THR A 130 ? 0.25979 0.24736 0.27246 -0.02865 0.02255  0.00644  130 THR A CA  
1023 C C   . THR A 130 ? 0.25306 0.24637 0.27116 -0.02989 0.02526  0.00440  130 THR A C   
1024 O O   . THR A 130 ? 0.23697 0.22581 0.24888 -0.03005 0.03027  0.00557  130 THR A O   
1025 C CB  . THR A 130 ? 0.27396 0.25255 0.27140 -0.02541 0.02217  0.00959  130 THR A CB  
1026 O OG1 . THR A 130 ? 0.35338 0.32302 0.34328 -0.02664 0.02953  0.01167  130 THR A OG1 
1027 C CG2 . THR A 130 ? 0.30309 0.27667 0.29586 -0.02301 0.01850  0.01106  130 THR A CG2 
1028 N N   . PRO A 131 ? 0.24180 0.24404 0.27022 -0.03015 0.02205  0.00124  131 PRO A N   
1029 C CA  . PRO A 131 ? 0.24008 0.24773 0.27354 -0.03017 0.02358  -0.00106 131 PRO A CA  
1030 C C   . PRO A 131 ? 0.22517 0.23304 0.25133 -0.02743 0.02019  -0.00065 131 PRO A C   
1031 O O   . PRO A 131 ? 0.23522 0.24205 0.25631 -0.02594 0.01567  0.00034  131 PRO A O   
1032 C CB  . PRO A 131 ? 0.19753 0.21295 0.24375 -0.03062 0.02030  -0.00480 131 PRO A CB  
1033 C CG  . PRO A 131 ? 0.19429 0.20841 0.23773 -0.02957 0.01514  -0.00395 131 PRO A CG  
1034 C CD  . PRO A 131 ? 0.21379 0.22030 0.24892 -0.03001 0.01716  -0.00055 131 PRO A CD  
1035 N N   . ILE A 132 ? 0.24495 0.25442 0.27167 -0.02699 0.02283  -0.00196 132 ILE A N   
1036 C CA  . ILE A 132 ? 0.24638 0.25543 0.26685 -0.02477 0.02013  -0.00225 132 ILE A CA  
1037 C C   . ILE A 132 ? 0.22293 0.23753 0.25055 -0.02368 0.01633  -0.00489 132 ILE A C   
1038 O O   . ILE A 132 ? 0.20377 0.22316 0.24077 -0.02367 0.01740  -0.00741 132 ILE A O   
1039 C CB  . ILE A 132 ? 0.23865 0.24435 0.25332 -0.02422 0.02524  -0.00223 132 ILE A CB  
1040 C CG1 . ILE A 132 ? 0.22415 0.22111 0.22688 -0.02422 0.02844  0.00087  132 ILE A CG1 
1041 C CG2 . ILE A 132 ? 0.21313 0.21859 0.22293 -0.02206 0.02220  -0.00350 132 ILE A CG2 
1042 C CD1 . ILE A 132 ? 0.25987 0.25391 0.26522 -0.02679 0.03583  0.00192  132 ILE A CD1 
1043 N N   . SER A 133 ? 0.21240 0.22587 0.23553 -0.02259 0.01192  -0.00463 133 SER A N   
1044 C CA  . SER A 133 ? 0.27931 0.29465 0.30541 -0.02114 0.00869  -0.00645 133 SER A CA  
1045 C C   . SER A 133 ? 0.24665 0.25837 0.26572 -0.02071 0.00641  -0.00610 133 SER A C   
1046 O O   . SER A 133 ? 0.23107 0.24135 0.24946 -0.01936 0.00471  -0.00723 133 SER A O   
1047 C CB  . SER A 133 ? 0.28871 0.30622 0.31986 -0.02124 0.00600  -0.00690 133 SER A CB  
1048 O OG  . SER A 133 ? 0.26569 0.28235 0.29602 -0.02290 0.00640  -0.00510 133 SER A OG  
1049 N N   . HIS A 134 ? 0.26464 0.27429 0.27843 -0.02171 0.00622  -0.00489 134 HIS A N   
1050 C CA  . HIS A 134 ? 0.20638 0.21352 0.21569 -0.02204 0.00428  -0.00560 134 HIS A CA  
1051 C C   . HIS A 134 ? 0.27024 0.27450 0.27552 -0.02100 0.00538  -0.00700 134 HIS A C   
1052 O O   . HIS A 134 ? 0.22556 0.22684 0.22836 -0.02128 0.00414  -0.00822 134 HIS A O   
1053 C CB  . HIS A 134 ? 0.25505 0.26224 0.26172 -0.02282 0.00261  -0.00511 134 HIS A CB  
1054 C CG  . HIS A 134 ? 0.20119 0.20727 0.20594 -0.02382 0.00050  -0.00697 134 HIS A CG  
1055 N ND1 . HIS A 134 ? 0.27219 0.27860 0.28006 -0.02559 -0.00002 -0.00779 134 HIS A ND1 
1056 C CD2 . HIS A 134 ? 0.25327 0.25745 0.25341 -0.02354 -0.00096 -0.00863 134 HIS A CD2 
1057 C CE1 . HIS A 134 ? 0.20256 0.20802 0.20960 -0.02705 -0.00127 -0.01004 134 HIS A CE1 
1058 N NE2 . HIS A 134 ? 0.20683 0.21129 0.20941 -0.02565 -0.00254 -0.01086 134 HIS A NE2 
1059 N N   . THR A 135 ? 0.22556 0.22987 0.22991 -0.01996 0.00835  -0.00698 135 THR A N   
1060 C CA  . THR A 135 ? 0.25010 0.25159 0.25031 -0.01847 0.01011  -0.00856 135 THR A CA  
1061 C C   . THR A 135 ? 0.26079 0.26519 0.26742 -0.01676 0.01257  -0.00989 135 THR A C   
1062 O O   . THR A 135 ? 0.25642 0.26532 0.27086 -0.01696 0.01276  -0.00981 135 THR A O   
1063 C CB  . THR A 135 ? 0.21905 0.21732 0.21147 -0.01804 0.01231  -0.00799 135 THR A CB  
1064 O OG1 . THR A 135 ? 0.22406 0.22368 0.21875 -0.01846 0.01631  -0.00630 135 THR A OG1 
1065 C CG2 . THR A 135 ? 0.22779 0.22393 0.21458 -0.01863 0.00825  -0.00774 135 THR A CG2 
1066 N N   . LEU A 136 ? 0.30818 0.31028 0.31208 -0.01477 0.01406  -0.01180 136 LEU A N   
1067 C CA  . LEU A 136 ? 0.23120 0.23706 0.24246 -0.01231 0.01614  -0.01400 136 LEU A CA  
1068 C C   . LEU A 136 ? 0.25769 0.26773 0.27399 -0.01312 0.02194  -0.01416 136 LEU A C   
1069 O O   . LEU A 136 ? 0.26136 0.27794 0.28895 -0.01307 0.02308  -0.01560 136 LEU A O   
1070 C CB  . LEU A 136 ? 0.31697 0.31847 0.32354 -0.00945 0.01616  -0.01627 136 LEU A CB  
1071 C CG  . LEU A 136 ? 0.28404 0.28005 0.28673 -0.00841 0.01159  -0.01659 136 LEU A CG  
1072 C CD1 . LEU A 136 ? 0.31949 0.30956 0.31642 -0.00567 0.01216  -0.01890 136 LEU A CD1 
1073 C CD2 . LEU A 136 ? 0.24425 0.24305 0.25360 -0.00637 0.00871  -0.01696 136 LEU A CD2 
1074 N N   . TYR A 137 ? 0.29915 0.30482 0.30689 -0.01388 0.02580  -0.01299 137 TYR A N   
1075 C CA  . TYR A 137 ? 0.32753 0.33415 0.33699 -0.01500 0.03308  -0.01264 137 TYR A CA  
1076 C C   . TYR A 137 ? 0.31352 0.31554 0.31553 -0.01729 0.03377  -0.00906 137 TYR A C   
1077 O O   . TYR A 137 ? 0.33085 0.33042 0.32758 -0.01757 0.02820  -0.00745 137 TYR A O   
1078 C CB  . TYR A 137 ? 0.33646 0.33916 0.33901 -0.01298 0.03838  -0.01420 137 TYR A CB  
1079 C CG  . TYR A 137 ? 0.32375 0.33055 0.33361 -0.00989 0.03833  -0.01811 137 TYR A CG  
1080 C CD1 . TYR A 137 ? 0.32104 0.33635 0.34563 -0.00937 0.04250  -0.02107 137 TYR A CD1 
1081 C CD2 . TYR A 137 ? 0.34840 0.35035 0.35097 -0.00731 0.03405  -0.01935 137 TYR A CD2 
1082 C CE1 . TYR A 137 ? 0.30290 0.32217 0.33447 -0.00540 0.04170  -0.02515 137 TYR A CE1 
1083 C CE2 . TYR A 137 ? 0.33013 0.33418 0.33800 -0.00367 0.03377  -0.02285 137 TYR A CE2 
1084 C CZ  . TYR A 137 ? 0.36068 0.37356 0.38286 -0.00225 0.03729  -0.02572 137 TYR A CZ  
1085 O OH  . TYR A 137 ? 0.36782 0.38307 0.39566 0.00246  0.03625  -0.02969 137 TYR A OH  
1086 N N   . ASP A 138 ? 0.23749 0.23794 0.23933 -0.01880 0.04111  -0.00805 138 ASP A N   
1087 C CA  . ASP A 138 ? 0.34914 0.34157 0.33957 -0.01985 0.04291  -0.00441 138 ASP A CA  
1088 C C   . ASP A 138 ? 0.39317 0.37623 0.36603 -0.01718 0.04355  -0.00377 138 ASP A C   
1089 O O   . ASP A 138 ? 0.41623 0.39576 0.38424 -0.01637 0.05062  -0.00456 138 ASP A O   
1090 C CB  . ASP A 138 ? 0.35721 0.34922 0.35288 -0.02280 0.05157  -0.00349 138 ASP A CB  
1091 C CG  . ASP A 138 ? 0.35340 0.33501 0.33617 -0.02351 0.05330  0.00073  138 ASP A CG  
1092 O OD1 . ASP A 138 ? 0.42211 0.39882 0.39382 -0.02123 0.04654  0.00249  138 ASP A OD1 
1093 O OD2 . ASP A 138 ? 0.28970 0.26772 0.27372 -0.02626 0.06151  0.00200  138 ASP A OD2 
1094 N N   . THR A 139 ? 0.39561 0.37494 0.35936 -0.01565 0.03610  -0.00296 139 THR A N   
1095 C CA  . THR A 139 ? 0.34627 0.31739 0.29399 -0.01265 0.03453  -0.00356 139 THR A CA  
1096 C C   . THR A 139 ? 0.47630 0.43636 0.40838 -0.01129 0.04120  -0.00110 139 THR A C   
1097 O O   . THR A 139 ? 0.43750 0.39052 0.35699 -0.00876 0.04392  -0.00214 139 THR A O   
1098 C CB  . THR A 139 ? 0.39805 0.36876 0.34183 -0.01162 0.02488  -0.00401 139 THR A CB  
1099 O OG1 . THR A 139 ? 0.53329 0.50384 0.47788 -0.01231 0.02284  -0.00133 139 THR A OG1 
1100 C CG2 . THR A 139 ? 0.35065 0.32912 0.30619 -0.01295 0.01992  -0.00664 139 THR A CG2 
1101 N N   . ASP A 140 ? 0.47650 0.43325 0.40757 -0.01273 0.04430  0.00221  140 ASP A N   
1102 C CA  . ASP A 140 ? 0.46042 0.40411 0.37500 -0.01165 0.05220  0.00515  140 ASP A CA  
1103 C C   . ASP A 140 ? 0.48256 0.42679 0.40163 -0.01369 0.06408  0.00418  140 ASP A C   
1104 O O   . ASP A 140 ? 0.45751 0.39014 0.36029 -0.01203 0.07156  0.00546  140 ASP A O   
1105 C CB  . ASP A 140 ? 0.48741 0.42609 0.39996 -0.01289 0.05294  0.00895  140 ASP A CB  
1106 C CG  . ASP A 140 ? 0.55653 0.49327 0.46236 -0.00970 0.04183  0.00965  140 ASP A CG  
1107 O OD1 . ASP A 140 ? 0.58114 0.51573 0.47743 -0.00599 0.03511  0.00774  140 ASP A OD1 
1108 O OD2 . ASP A 140 ? 0.49815 0.43586 0.40909 -0.01085 0.03978  0.01153  140 ASP A OD2 
1109 N N   . MET A 141 ? 0.45716 0.41455 0.39792 -0.01685 0.06593  0.00155  141 MET A N   
1110 C CA  . MET A 141 ? 0.45462 0.41541 0.40354 -0.01847 0.07657  -0.00073 141 MET A CA  
1111 C C   . MET A 141 ? 0.45939 0.41829 0.40042 -0.01482 0.07706  -0.00349 141 MET A C   
1112 O O   . MET A 141 ? 0.48794 0.44213 0.42356 -0.01450 0.08733  -0.00419 141 MET A O   
1113 C CB  . MET A 141 ? 0.39647 0.37274 0.37131 -0.02160 0.07606  -0.00387 141 MET A CB  
1114 C CG  . MET A 141 ? 0.47541 0.45936 0.46372 -0.02240 0.08469  -0.00805 141 MET A CG  
1115 S SD  . MET A 141 ? 0.45631 0.44851 0.45085 -0.01795 0.07805  -0.01283 141 MET A SD  
1116 C CE  . MET A 141 ? 0.35471 0.35640 0.36256 -0.01827 0.06537  -0.01338 141 MET A CE  
1117 N N   . LEU A 142 ? 0.40681 0.36858 0.34686 -0.01223 0.06669  -0.00529 142 LEU A N   
1118 C CA  . LEU A 142 ? 0.45392 0.41299 0.38628 -0.00878 0.06631  -0.00831 142 LEU A CA  
1119 C C   . LEU A 142 ? 0.48616 0.42990 0.39349 -0.00574 0.06956  -0.00670 142 LEU A C   
1120 O O   . LEU A 142 ? 0.49643 0.43552 0.39586 -0.00349 0.07562  -0.00874 142 LEU A O   
1121 C CB  . LEU A 142 ? 0.48567 0.44923 0.42169 -0.00748 0.05471  -0.01043 142 LEU A CB  
1122 C CG  . LEU A 142 ? 0.34300 0.31902 0.29976 -0.00936 0.05070  -0.01194 142 LEU A CG  
1123 C CD1 . LEU A 142 ? 0.42623 0.40306 0.38268 -0.00867 0.04040  -0.01302 142 LEU A CD1 
1124 C CD2 . LEU A 142 ? 0.40343 0.38624 0.37234 -0.00844 0.05635  -0.01545 142 LEU A CD2 
1125 N N   . VAL A 143 ? 0.49781 0.43291 0.39146 -0.00495 0.06533  -0.00331 143 VAL A N   
1126 C CA  . VAL A 143 ? 0.46830 0.38710 0.33543 -0.00089 0.06688  -0.00182 143 VAL A CA  
1127 C C   . VAL A 143 ? 0.53013 0.43962 0.38833 -0.00175 0.08162  0.00065  143 VAL A C   
1128 O O   . VAL A 143 ? 0.51123 0.40829 0.34941 0.00168  0.08699  0.00048  143 VAL A O   
1129 C CB  . VAL A 143 ? 0.47570 0.38818 0.33154 0.00113  0.05730  0.00068  143 VAL A CB  
1130 C CG1 . VAL A 143 ? 0.57582 0.47079 0.40254 0.00678  0.05652  0.00146  143 VAL A CG1 
1131 C CG2 . VAL A 143 ? 0.49125 0.41460 0.35955 0.00081  0.04450  -0.00220 143 VAL A CG2 
1132 N N   . ALA A 144 ? 0.46407 0.37875 0.33666 -0.00653 0.08893  0.00261  144 ALA A N   
1133 C CA  . ALA A 144 ? 0.50672 0.41270 0.37309 -0.00862 0.10448  0.00469  144 ALA A CA  
1134 C C   . ALA A 144 ? 0.49359 0.40586 0.36914 -0.00911 0.11402  0.00050  144 ALA A C   
1135 O O   . ALA A 144 ? 0.56692 0.46766 0.42743 -0.00812 0.12588  0.00120  144 ALA A O   
1136 C CB  . ALA A 144 ? 0.49105 0.40161 0.37279 -0.01430 0.10928  0.00702  144 ALA A CB  
1137 N N   . ARG A 145 ? 0.44375 0.37343 0.34306 -0.01012 0.10924  -0.00395 145 ARG A N   
1138 C CA  . ARG A 145 ? 0.51493 0.45195 0.42509 -0.00969 0.11719  -0.00863 145 ARG A CA  
1139 C C   . ARG A 145 ? 0.52230 0.44967 0.41240 -0.00413 0.11612  -0.01042 145 ARG A C   
1140 O O   . ARG A 145 ? 0.50010 0.42677 0.38972 -0.00295 0.12636  -0.01324 145 ARG A O   
1141 C CB  . ARG A 145 ? 0.51608 0.47243 0.45447 -0.01084 0.11052  -0.01292 145 ARG A CB  
1142 C CG  . ARG A 145 ? 0.54308 0.50987 0.50248 -0.01599 0.11090  -0.01232 145 ARG A CG  
1143 C CD  . ARG A 145 ? 0.60752 0.57908 0.58088 -0.01999 0.12580  -0.01434 145 ARG A CD  
1144 N NE  . ARG A 145 ? 0.65537 0.64105 0.64858 -0.01846 0.12797  -0.02077 145 ARG A NE  
1145 C CZ  . ARG A 145 ? 0.53549 0.53784 0.55436 -0.01925 0.12235  -0.02492 145 ARG A CZ  
1146 N NH1 . ARG A 145 ? 0.46698 0.47418 0.49498 -0.02201 0.11474  -0.02339 145 ARG A NH1 
1147 N NH2 . ARG A 145 ? 0.41145 0.42530 0.44635 -0.01653 0.12403  -0.03103 145 ARG A NH2 
1148 N N   . ASN A 146 ? 0.52039 0.44064 0.39473 -0.00068 0.10399  -0.00945 146 ASN A N   
1149 C CA  . ASN A 146 ? 0.56558 0.47655 0.42105 0.00458  0.10102  -0.01193 146 ASN A CA  
1150 C C   . ASN A 146 ? 0.59037 0.48122 0.41525 0.00774  0.10774  -0.00910 146 ASN A C   
1151 O O   . ASN A 146 ? 0.59117 0.47232 0.39740 0.01259  0.10579  -0.01141 146 ASN A O   
1152 C CB  . ASN A 146 ? 0.48221 0.39548 0.33676 0.00641  0.08468  -0.01334 146 ASN A CB  
1153 C CG  . ASN A 146 ? 0.52338 0.43283 0.36892 0.01062  0.08074  -0.01797 146 ASN A CG  
1154 O OD1 . ASN A 146 ? 0.52210 0.44007 0.38169 0.01077  0.08225  -0.02170 146 ASN A OD1 
1155 N ND2 . ASN A 146 ? 0.61592 0.51202 0.43772 0.01451  0.07504  -0.01817 146 ASN A ND2 
1156 N N   . GLY A 147 ? 0.54621 0.42903 0.36395 0.00543  0.11556  -0.00427 147 GLY A N   
1157 C CA  . GLY A 147 ? 0.54834 0.40944 0.33471 0.00871  0.12341  -0.00092 147 GLY A CA  
1158 C C   . GLY A 147 ? 0.53785 0.38572 0.30436 0.01107  0.11533  0.00377  147 GLY A C   
1159 O O   . GLY A 147 ? 0.60094 0.42810 0.33753 0.01504  0.12040  0.00683  147 GLY A O   
1160 N N   . GLY A 148 ? 0.49817 0.35641 0.27922 0.00935  0.10312  0.00434  148 GLY A N   
1161 C CA  . GLY A 148 ? 0.55151 0.39941 0.31674 0.01221  0.09410  0.00797  148 GLY A CA  
1162 C C   . GLY A 148 ? 0.56439 0.41581 0.32672 0.01646  0.07640  0.00467  148 GLY A C   
1163 O O   . GLY A 148 ? 0.54341 0.39245 0.30134 0.01829  0.06666  0.00647  148 GLY A O   
1164 N N   . ALA A 149 ? 0.51002 0.36702 0.27547 0.01801  0.07219  -0.00051 149 ALA A N   
1165 C CA  . ALA A 149 ? 0.51119 0.37246 0.27680 0.02089  0.05630  -0.00469 149 ALA A CA  
1166 C C   . ALA A 149 ? 0.54630 0.42667 0.34040 0.01649  0.05239  -0.00849 149 ALA A C   
1167 O O   . ALA A 149 ? 0.57896 0.46652 0.38662 0.01360  0.06128  -0.00937 149 ALA A O   
1168 C CB  . ALA A 149 ? 0.63034 0.47757 0.37008 0.02732  0.05335  -0.00804 149 ALA A CB  
1169 N N   . ALA A 150 ? 0.54763 0.43566 0.35049 0.01628  0.03916  -0.01096 150 ALA A N   
1170 C CA  . ALA A 150 ? 0.39101 0.29429 0.21776 0.01238  0.03517  -0.01416 150 ALA A CA  
1171 C C   . ALA A 150 ? 0.54001 0.44105 0.36199 0.01450  0.03273  -0.01955 150 ALA A C   
1172 O O   . ALA A 150 ? 0.41204 0.30200 0.21401 0.01899  0.02836  -0.02199 150 ALA A O   
1173 C CB  . ALA A 150 ? 0.46553 0.37729 0.30401 0.01061  0.02370  -0.01465 150 ALA A CB  
1174 N N   . PRO A 151 ? 0.55307 0.46346 0.39214 0.01186  0.03511  -0.02174 151 PRO A N   
1175 C CA  . PRO A 151 ? 0.38449 0.29204 0.21970 0.01380  0.03242  -0.02703 151 PRO A CA  
1176 C C   . PRO A 151 ? 0.43729 0.34512 0.27212 0.01365  0.01939  -0.03082 151 PRO A C   
1177 O O   . PRO A 151 ? 0.42356 0.33883 0.26976 0.01077  0.01297  -0.02981 151 PRO A O   
1178 C CB  . PRO A 151 ? 0.42121 0.33927 0.27691 0.01114  0.03708  -0.02781 151 PRO A CB  
1179 C CG  . PRO A 151 ? 0.36201 0.28667 0.22859 0.00866  0.04500  -0.02335 151 PRO A CG  
1180 C CD  . PRO A 151 ? 0.40917 0.33168 0.27027 0.00775  0.04062  -0.01976 151 PRO A CD  
1181 N N   . LEU A 152 ? 0.47019 0.36991 0.29241 0.01665  0.01582  -0.03581 152 LEU A N   
1182 C CA  . LEU A 152 ? 0.43263 0.33231 0.25509 0.01618  0.00372  -0.04086 152 LEU A CA  
1183 C C   . LEU A 152 ? 0.48878 0.39096 0.32174 0.01379  0.00187  -0.04543 152 LEU A C   
1184 O O   . LEU A 152 ? 0.50931 0.41221 0.34584 0.01200  -0.00724 -0.05006 152 LEU A O   
1185 C CB  . LEU A 152 ? 0.42216 0.30898 0.22017 0.02178  -0.00162 -0.04414 152 LEU A CB  
1186 C CG  . LEU A 152 ? 0.51141 0.39266 0.29530 0.02521  -0.00271 -0.04021 152 LEU A CG  
1187 C CD1 . LEU A 152 ? 0.46265 0.32991 0.22066 0.03183  -0.00976 -0.04434 152 LEU A CD1 
1188 C CD2 . LEU A 152 ? 0.41570 0.30792 0.21581 0.02192  -0.00964 -0.03853 152 LEU A CD2 
1189 N N   . THR A 153 ? 0.41833 0.32153 0.25672 0.01381  0.01023  -0.04463 153 THR A N   
1190 C CA  . THR A 153 ? 0.44269 0.34629 0.28961 0.01234  0.00900  -0.04844 153 THR A CA  
1191 C C   . THR A 153 ? 0.41256 0.32563 0.27817 0.00972  0.01400  -0.04504 153 THR A C   
1192 O O   . THR A 153 ? 0.40961 0.32791 0.27986 0.01008  0.02080  -0.04085 153 THR A O   
1193 C CB  . THR A 153 ? 0.45405 0.34741 0.28692 0.01687  0.01307  -0.05237 153 THR A CB  
1194 O OG1 . THR A 153 ? 0.45337 0.34853 0.28743 0.01916  0.02425  -0.04938 153 THR A OG1 
1195 C CG2 . THR A 153 ? 0.50663 0.38906 0.31728 0.02075  0.00895  -0.05539 153 THR A CG2 
1196 N N   A MET A 154 ? 0.43483 0.34911 0.31055 0.00716  0.01044  -0.04719 154 MET A N   
1197 N N   B MET A 154 ? 0.42821 0.34256 0.30403 0.00713  0.01044  -0.04715 154 MET A N   
1198 C CA  A MET A 154 ? 0.41920 0.34022 0.31005 0.00591  0.01397  -0.04460 154 MET A CA  
1199 C CA  B MET A 154 ? 0.42175 0.34291 0.31266 0.00593  0.01408  -0.04451 154 MET A CA  
1200 C C   A MET A 154 ? 0.40099 0.32100 0.29120 0.01034  0.02172  -0.04517 154 MET A C   
1201 C C   B MET A 154 ? 0.40073 0.32081 0.29085 0.01038  0.02184  -0.04512 154 MET A C   
1202 O O   A MET A 154 ? 0.39548 0.32331 0.29734 0.01072  0.02613  -0.04256 154 MET A O   
1203 O O   B MET A 154 ? 0.39204 0.31997 0.29362 0.01079  0.02641  -0.04247 154 MET A O   
1204 C CB  A MET A 154 ? 0.40156 0.32053 0.29948 0.00262  0.00877  -0.04670 154 MET A CB  
1205 C CB  B MET A 154 ? 0.39894 0.31832 0.29730 0.00262  0.00895  -0.04648 154 MET A CB  
1206 C CG  A MET A 154 ? 0.37264 0.29642 0.28352 0.00192  0.01095  -0.04391 154 MET A CG  
1207 C CG  B MET A 154 ? 0.37146 0.29428 0.28136 0.00288  0.01182  -0.04433 154 MET A CG  
1208 S SD  A MET A 154 ? 0.34437 0.28016 0.26730 -0.00123 0.01104  -0.03835 154 MET A SD  
1209 S SD  B MET A 154 ? 0.34800 0.28358 0.27066 0.00160  0.01450  -0.03859 154 MET A SD  
1210 C CE  A MET A 154 ? 0.30719 0.24367 0.24078 -0.00157 0.01107  -0.03696 154 MET A CE  
1211 C CE  B MET A 154 ? 0.34403 0.28256 0.27021 -0.00422 0.00814  -0.03724 154 MET A CE  
1212 N N   . GLN A 155 ? 0.41861 0.32951 0.29598 0.01397  0.02326  -0.04920 155 GLN A N   
1213 C CA  . GLN A 155 ? 0.40935 0.31956 0.28633 0.01868  0.03123  -0.05055 155 GLN A CA  
1214 C C   . GLN A 155 ? 0.41756 0.33403 0.29608 0.01966  0.03972  -0.04726 155 GLN A C   
1215 O O   . GLN A 155 ? 0.43201 0.35527 0.32145 0.02152  0.04631  -0.04706 155 GLN A O   
1216 C CB  . GLN A 155 ? 0.44799 0.34599 0.30868 0.02241  0.03122  -0.05576 155 GLN A CB  
1217 C CG  . GLN A 155 ? 0.55625 0.45190 0.40872 0.02747  0.04102  -0.05685 155 GLN A CG  
1218 C CD  . GLN A 155 ? 0.53809 0.43861 0.40265 0.03090  0.04692  -0.05832 155 GLN A CD  
1219 O OE1 . GLN A 155 ? 0.51537 0.42038 0.38258 0.03360  0.05632  -0.05814 155 GLN A OE1 
1220 N NE2 . GLN A 155 ? 0.51228 0.41141 0.38418 0.03103  0.04163  -0.06011 155 GLN A NE2 
1221 N N   . SER A 156 ? 0.41334 0.32733 0.28141 0.01852  0.03967  -0.04498 156 SER A N   
1222 C CA  . SER A 156 ? 0.38972 0.30729 0.25774 0.01870  0.04858  -0.04145 156 SER A CA  
1223 C C   . SER A 156 ? 0.42936 0.35854 0.31470 0.01464  0.04821  -0.03717 156 SER A C   
1224 O O   . SER A 156 ? 0.39288 0.32817 0.28620 0.01421  0.05646  -0.03521 156 SER A O   
1225 C CB  . SER A 156 ? 0.43138 0.33859 0.27797 0.02001  0.04882  -0.04039 156 SER A CB  
1226 O OG  . SER A 156 ? 0.38893 0.29529 0.23282 0.01770  0.03840  -0.03954 156 SER A OG  
1227 N N   . PHE A 157 ? 0.37574 0.30798 0.26744 0.01144  0.03923  -0.03613 157 PHE A N   
1228 C CA  . PHE A 157 ? 0.38246 0.32471 0.28909 0.00790  0.03841  -0.03234 157 PHE A CA  
1229 C C   . PHE A 157 ? 0.38397 0.33473 0.30797 0.00823  0.04009  -0.03309 157 PHE A C   
1230 O O   . PHE A 157 ? 0.40646 0.36596 0.34281 0.00687  0.04360  -0.03098 157 PHE A O   
1231 C CB  . PHE A 157 ? 0.35415 0.29658 0.26126 0.00469  0.02897  -0.03135 157 PHE A CB  
1232 C CG  . PHE A 157 ? 0.34203 0.29353 0.26243 0.00134  0.02793  -0.02759 157 PHE A CG  
1233 C CD1 . PHE A 157 ? 0.38205 0.33462 0.29979 0.00029  0.03009  -0.02411 157 PHE A CD1 
1234 C CD2 . PHE A 157 ? 0.38829 0.34557 0.32211 -0.00036 0.02485  -0.02753 157 PHE A CD2 
1235 C CE1 . PHE A 157 ? 0.33304 0.29327 0.26262 -0.00264 0.02905  -0.02104 157 PHE A CE1 
1236 C CE2 . PHE A 157 ? 0.28905 0.25383 0.23370 -0.00303 0.02379  -0.02444 157 PHE A CE2 
1237 C CZ  . PHE A 157 ? 0.33032 0.29707 0.27353 -0.00430 0.02579  -0.02139 157 PHE A CZ  
1238 N N   . THR A 158 ? 0.39073 0.33826 0.31538 0.01035  0.03711  -0.03641 158 THR A N   
1239 C CA  . THR A 158 ? 0.36892 0.32271 0.30778 0.01221  0.03763  -0.03748 158 THR A CA  
1240 C C   . THR A 158 ? 0.36631 0.32640 0.31240 0.01529  0.04644  -0.03902 158 THR A C   
1241 O O   . THR A 158 ? 0.43640 0.40633 0.39822 0.01584  0.04763  -0.03911 158 THR A O   
1242 C CB  . THR A 158 ? 0.36544 0.31129 0.30028 0.01455  0.03311  -0.04069 158 THR A CB  
1243 O OG1 . THR A 158 ? 0.33123 0.27206 0.26184 0.01061  0.02599  -0.03970 158 THR A OG1 
1244 C CG2 . THR A 158 ? 0.35330 0.30375 0.30054 0.01787  0.03271  -0.04177 158 THR A CG2 
1245 N N   . LYS A 159 ? 0.38572 0.34033 0.32077 0.01738  0.05281  -0.04072 159 LYS A N   
1246 C CA  . LYS A 159 ? 0.41268 0.37314 0.35468 0.01969  0.06306  -0.04253 159 LYS A CA  
1247 C C   . LYS A 159 ? 0.35367 0.32064 0.30168 0.01579  0.06920  -0.03914 159 LYS A C   
1248 O O   . LYS A 159 ? 0.36892 0.34349 0.32815 0.01633  0.07809  -0.04078 159 LYS A O   
1249 C CB  . LYS A 159 ? 0.42557 0.37619 0.35153 0.02327  0.06901  -0.04544 159 LYS A CB  
1250 C CG  . LYS A 159 ? 0.53155 0.47853 0.45720 0.02855  0.06731  -0.05043 159 LYS A CG  
1251 C CD  . LYS A 159 ? 0.45958 0.40043 0.38190 0.02797  0.05601  -0.05051 159 LYS A CD  
1252 C CE  . LYS A 159 ? 0.49341 0.42507 0.40828 0.03295  0.05467  -0.05529 159 LYS A CE  
1253 N NZ  . LYS A 159 ? 0.47985 0.40363 0.39070 0.03133  0.04485  -0.05532 159 LYS A NZ  
1254 N N   . LEU A 160 ? 0.39417 0.35828 0.33573 0.01187  0.06498  -0.03488 160 LEU A N   
1255 C CA  . LEU A 160 ? 0.35779 0.32639 0.30434 0.00815  0.07045  -0.03145 160 LEU A CA  
1256 C C   . LEU A 160 ? 0.39950 0.38047 0.36680 0.00574  0.06696  -0.03081 160 LEU A C   
1257 O O   . LEU A 160 ? 0.46392 0.45285 0.44397 0.00373  0.07362  -0.03079 160 LEU A O   
1258 C CB  . LEU A 160 ? 0.42122 0.38029 0.35050 0.00612  0.06734  -0.02743 160 LEU A CB  
1259 C CG  . LEU A 160 ? 0.48192 0.44188 0.41220 0.00257  0.07274  -0.02329 160 LEU A CG  
1260 C CD1 . LEU A 160 ? 0.48971 0.44730 0.41734 0.00278  0.08664  -0.02366 160 LEU A CD1 
1261 C CD2 . LEU A 160 ? 0.43891 0.38924 0.35206 0.00201  0.06685  -0.01980 160 LEU A CD2 
1262 N N   . VAL A 161 ? 0.37666 0.35873 0.34730 0.00581  0.05695  -0.03064 161 VAL A N   
1263 C CA  . VAL A 161 ? 0.37535 0.36743 0.36297 0.00435  0.05297  -0.03021 161 VAL A CA  
1264 C C   . VAL A 161 ? 0.38426 0.38531 0.38778 0.00798  0.05516  -0.03471 161 VAL A C   
1265 O O   . VAL A 161 ? 0.31912 0.33045 0.33896 0.00715  0.05483  -0.03555 161 VAL A O   
1266 C CB  . VAL A 161 ? 0.41557 0.40429 0.39983 0.00348  0.04276  -0.02855 161 VAL A CB  
1267 C CG1 . VAL A 161 ? 0.42871 0.41097 0.40042 0.00022  0.04029  -0.02510 161 VAL A CG1 
1268 C CG2 . VAL A 161 ? 0.40841 0.39102 0.38737 0.00713  0.03878  -0.03138 161 VAL A CG2 
1269 N N   . ASP A 162 ? 0.44261 0.44009 0.44208 0.01252  0.05684  -0.03825 162 ASP A N   
1270 C CA  . ASP A 162 ? 0.37279 0.37939 0.38796 0.01696  0.05940  -0.04328 162 ASP A CA  
1271 C C   . ASP A 162 ? 0.37717 0.39244 0.40343 0.01534  0.07065  -0.04516 162 ASP A C   
1272 O O   . ASP A 162 ? 0.29527 0.32303 0.34151 0.01709  0.07241  -0.04934 162 ASP A O   
1273 C CB  . ASP A 162 ? 0.38748 0.38682 0.39446 0.02265  0.05848  -0.04672 162 ASP A CB  
1274 C CG  . ASP A 162 ? 0.38985 0.38102 0.38941 0.02429  0.04812  -0.04574 162 ASP A CG  
1275 O OD1 . ASP A 162 ? 0.36240 0.35736 0.36940 0.02350  0.04179  -0.04423 162 ASP A OD1 
1276 O OD2 . ASP A 162 ? 0.32471 0.30475 0.31039 0.02624  0.04675  -0.04666 162 ASP A OD2 
1277 N N   . ARG A 163 ? 0.41280 0.42115 0.42631 0.01209  0.07839  -0.04242 163 ARG A N   
1278 C CA  . ARG A 163 ? 0.35685 0.37096 0.37891 0.00957  0.09092  -0.04359 163 ARG A CA  
1279 C C   . ARG A 163 ? 0.36281 0.38554 0.39931 0.00427  0.09111  -0.04175 163 ARG A C   
1280 O O   . ARG A 163 ? 0.31864 0.35243 0.37391 0.00255  0.09864  -0.04511 163 ARG A O   
1281 C CB  . ARG A 163 ? 0.39281 0.39342 0.39263 0.00837  0.09916  -0.04070 163 ARG A CB  
1282 C CG  . ARG A 163 ? 0.43008 0.43266 0.43365 0.00872  0.11407  -0.04383 163 ARG A CG  
1283 C CD  . ARG A 163 ? 0.53381 0.51963 0.51026 0.00875  0.12123  -0.04071 163 ARG A CD  
1284 N NE  . ARG A 163 ? 0.51087 0.48532 0.46757 0.01292  0.11230  -0.04049 163 ARG A NE  
1285 C CZ  . ARG A 163 ? 0.57016 0.54125 0.52146 0.01812  0.11353  -0.04474 163 ARG A CZ  
1286 N NH1 . ARG A 163 ? 0.54963 0.52837 0.51374 0.02047  0.12334  -0.04961 163 ARG A NH1 
1287 N NH2 . ARG A 163 ? 0.55391 0.51396 0.48748 0.02099  0.10479  -0.04465 163 ARG A NH2 
1288 N N   . VAL A 164 ? 0.41221 0.43036 0.44122 0.00153  0.08305  -0.03701 164 VAL A N   
1289 C CA  . VAL A 164 ? 0.29290 0.31807 0.33441 -0.00317 0.08234  -0.03538 164 VAL A CA  
1290 C C   . VAL A 164 ? 0.26625 0.30472 0.32921 -0.00109 0.07537  -0.03967 164 VAL A C   
1291 O O   . VAL A 164 ? 0.30217 0.35154 0.38396 -0.00367 0.07839  -0.04225 164 VAL A O   
1292 C CB  . VAL A 164 ? 0.34673 0.36273 0.37322 -0.00596 0.07591  -0.02940 164 VAL A CB  
1293 C CG1 . VAL A 164 ? 0.33609 0.35833 0.37466 -0.01052 0.07522  -0.02788 164 VAL A CG1 
1294 C CG2 . VAL A 164 ? 0.38412 0.38643 0.38840 -0.00673 0.08155  -0.02578 164 VAL A CG2 
1295 N N   . GLY A 165 ? 0.29790 0.29824 0.32558 0.00899  0.01544  0.00049  165 GLY A N   
1296 C CA  . GLY A 165 ? 0.38146 0.38139 0.41238 0.00899  0.01393  0.00082  165 GLY A CA  
1297 C C   . GLY A 165 ? 0.36401 0.36414 0.39276 0.00873  0.01171  0.00051  165 GLY A C   
1298 O O   . GLY A 165 ? 0.37699 0.37755 0.40199 0.00852  0.01158  -0.00022 165 GLY A O   
1299 N N   . ASP A 166 ? 0.37226 0.37199 0.40343 0.00870  0.00994  0.00110  166 ASP A N   
1300 C CA  . ASP A 166 ? 0.30097 0.30064 0.33007 0.00838  0.00793  0.00083  166 ASP A CA  
1301 C C   . ASP A 166 ? 0.33689 0.33717 0.36374 0.00850  0.00714  0.00086  166 ASP A C   
1302 O O   . ASP A 166 ? 0.29878 0.29925 0.32711 0.00882  0.00730  0.00150  166 ASP A O   
1303 C CB  . ASP A 166 ? 0.34237 0.34121 0.37439 0.00820  0.00617  0.00150  166 ASP A CB  
1304 C CG  . ASP A 166 ? 0.33825 0.33646 0.37290 0.00808  0.00673  0.00157  166 ASP A CG  
1305 O OD1 . ASP A 166 ? 0.43027 0.42861 0.46352 0.00801  0.00818  0.00079  166 ASP A OD1 
1306 O OD2 . ASP A 166 ? 0.27088 0.26844 0.30917 0.00802  0.00563  0.00241  166 ASP A OD2 
1307 N N   . PRO A 167 ? 0.37744 0.37802 0.40102 0.00825  0.00636  0.00019  167 PRO A N   
1308 C CA  . PRO A 167 ? 0.30778 0.30888 0.32963 0.00838  0.00561  0.00017  167 PRO A CA  
1309 C C   . PRO A 167 ? 0.37420 0.37467 0.39772 0.00837  0.00393  0.00070  167 PRO A C   
1310 O O   . PRO A 167 ? 0.29973 0.29935 0.32524 0.00815  0.00307  0.00106  167 PRO A O   
1311 C CB  . PRO A 167 ? 0.30852 0.30998 0.32703 0.00806  0.00530  -0.00073 167 PRO A CB  
1312 C CG  . PRO A 167 ? 0.36227 0.36304 0.38114 0.00767  0.00509  -0.00097 167 PRO A CG  
1313 C CD  . PRO A 167 ? 0.33747 0.33791 0.35908 0.00784  0.00624  -0.00057 167 PRO A CD  
1314 N N   . PRO A 168 ? 0.28734 0.28811 0.31022 0.00856  0.00337  0.00077  168 PRO A N   
1315 C CA  . PRO A 168 ? 0.30388 0.30387 0.32804 0.00847  0.00172  0.00110  168 PRO A CA  
1316 C C   . PRO A 168 ? 0.32316 0.32228 0.34580 0.00791  0.00035  0.00064  168 PRO A C   
1317 O O   . PRO A 168 ? 0.39116 0.39053 0.41107 0.00767  0.00058  -0.00009 168 PRO A O   
1318 C CB  . PRO A 168 ? 0.36446 0.36501 0.38753 0.00876  0.00162  0.00096  168 PRO A CB  
1319 C CG  . PRO A 168 ? 0.24342 0.24500 0.26609 0.00911  0.00325  0.00114  168 PRO A CG  
1320 C CD  . PRO A 168 ? 0.30339 0.30513 0.32474 0.00888  0.00419  0.00067  168 PRO A CD  
1321 N N   . ALA A 169 ? 0.35482 0.35285 0.37926 0.00764  -0.00112 0.00114  169 ALA A N   
1322 C CA  . ALA A 169 ? 0.29584 0.29278 0.31864 0.00699  -0.00259 0.00087  169 ALA A CA  
1323 C C   . ALA A 169 ? 0.26910 0.26593 0.28854 0.00680  -0.00302 0.00001  169 ALA A C   
1324 O O   . ALA A 169 ? 0.32327 0.32058 0.34266 0.00717  -0.00274 -0.00018 169 ALA A O   
1325 C CB  . ALA A 169 ? 0.41282 0.40852 0.43820 0.00669  -0.00434 0.00168  169 ALA A CB  
1326 N N   . PRO A 170 ? 0.27698 0.27316 0.29373 0.00622  -0.00357 -0.00051 170 PRO A N   
1327 C CA  . PRO A 170 ? 0.34502 0.34097 0.35871 0.00600  -0.00377 -0.00140 170 PRO A CA  
1328 C C   . PRO A 170 ? 0.26092 0.25576 0.27490 0.00586  -0.00510 -0.00139 170 PRO A C   
1329 O O   . PRO A 170 ? 0.30369 0.29742 0.31922 0.00555  -0.00651 -0.00074 170 PRO A O   
1330 C CB  . PRO A 170 ? 0.31497 0.31016 0.32609 0.00528  -0.00414 -0.00172 170 PRO A CB  
1331 C CG  . PRO A 170 ? 0.33197 0.32651 0.34514 0.00502  -0.00489 -0.00081 170 PRO A CG  
1332 C CD  . PRO A 170 ? 0.28651 0.28214 0.30297 0.00573  -0.00386 -0.00029 170 PRO A CD  
1333 N N   . ALA A 171 ? 0.33260 0.32774 0.34529 0.00608  -0.00468 -0.00213 171 ALA A N   
1334 C CA  . ALA A 171 ? 0.29045 0.28453 0.30342 0.00599  -0.00575 -0.00231 171 ALA A CA  
1335 C C   . ALA A 171 ? 0.28221 0.27433 0.29266 0.00506  -0.00724 -0.00269 171 ALA A C   
1336 O O   . ALA A 171 ? 0.39758 0.38935 0.40536 0.00455  -0.00706 -0.00305 171 ALA A O   
1337 C CB  . ALA A 171 ? 0.33087 0.32570 0.34315 0.00645  -0.00480 -0.00310 171 ALA A CB  
1338 N N   . PRO A 172 ? 0.18628 0.17700 0.19739 0.00476  -0.00876 -0.00256 172 PRO A N   
1339 C CA  . PRO A 172 ? 0.25426 0.24284 0.26247 0.00374  -0.01035 -0.00292 172 PRO A CA  
1340 C C   . PRO A 172 ? 0.31220 0.30022 0.31649 0.00343  -0.00956 -0.00431 172 PRO A C   
1341 O O   . PRO A 172 ? 0.22335 0.21256 0.22775 0.00405  -0.00804 -0.00500 172 PRO A O   
1342 C CB  . PRO A 172 ? 0.27930 0.26669 0.28956 0.00359  -0.01208 -0.00253 172 PRO A CB  
1343 C CG  . PRO A 172 ? 0.29895 0.28782 0.31227 0.00457  -0.01097 -0.00246 172 PRO A CG  
1344 C CD  . PRO A 172 ? 0.23972 0.23064 0.25428 0.00525  -0.00920 -0.00202 172 PRO A CD  
1345 N N   . ASP A 173 ? 0.27615 0.26224 0.27700 0.00241  -0.01062 -0.00466 173 ASP A N   
1346 C CA  . ASP A 173 ? 0.31756 0.30279 0.31440 0.00196  -0.00976 -0.00602 173 ASP A CA  
1347 C C   . ASP A 173 ? 0.26668 0.25088 0.26319 0.00200  -0.00997 -0.00702 173 ASP A C   
1348 O O   . ASP A 173 ? 0.36084 0.34410 0.35902 0.00189  -0.01154 -0.00663 173 ASP A O   
1349 C CB  . ASP A 173 ? 0.27297 0.25623 0.26588 0.00075  -0.01081 -0.00599 173 ASP A CB  
1350 C CG  . ASP A 173 ? 0.29109 0.27535 0.28312 0.00068  -0.00976 -0.00563 173 ASP A CG  
1351 O OD1 . ASP A 173 ? 0.37243 0.35806 0.36396 0.00113  -0.00780 -0.00637 173 ASP A OD1 
1352 O OD2 . ASP A 173 ? 0.33576 0.31947 0.32789 0.00018  -0.01096 -0.00457 173 ASP A OD2 
1353 N N   . PRO A 174 ? 0.26540 0.24975 0.26011 0.00216  -0.00838 -0.00833 174 PRO A N   
1354 C CA  . PRO A 174 ? 0.27420 0.25745 0.26864 0.00219  -0.00839 -0.00944 174 PRO A CA  
1355 C C   . PRO A 174 ? 0.22728 0.20753 0.21793 0.00094  -0.00992 -0.01008 174 PRO A C   
1356 O O   . PRO A 174 ? 0.24957 0.22865 0.23711 0.00002  -0.01062 -0.00979 174 PRO A O   
1357 C CB  . PRO A 174 ? 0.24253 0.22683 0.23615 0.00264  -0.00607 -0.01061 174 PRO A CB  
1358 C CG  . PRO A 174 ? 0.34343 0.32825 0.33486 0.00227  -0.00528 -0.01042 174 PRO A CG  
1359 C CD  . PRO A 174 ? 0.27960 0.26523 0.27295 0.00235  -0.00641 -0.00884 174 PRO A CD  
1360 N N   . PRO A 175 ? 0.28791 0.26673 0.27861 0.00081  -0.01057 -0.01092 175 PRO A N   
1361 C CA  . PRO A 175 ? 0.27597 0.25168 0.26268 -0.00049 -0.01219 -0.01162 175 PRO A CA  
1362 C C   . PRO A 175 ? 0.34021 0.31451 0.32161 -0.00132 -0.01089 -0.01291 175 PRO A C   
1363 O O   . PRO A 175 ? 0.42626 0.40190 0.40751 -0.00078 -0.00855 -0.01364 175 PRO A O   
1364 C CB  . PRO A 175 ? 0.30707 0.28189 0.29542 -0.00025 -0.01260 -0.01251 175 PRO A CB  
1365 C CG  . PRO A 175 ? 0.23912 0.21658 0.23312 0.00111  -0.01205 -0.01152 175 PRO A CG  
1366 C CD  . PRO A 175 ? 0.28391 0.26379 0.27850 0.00180  -0.01011 -0.01109 175 PRO A CD  
1367 N N   . ALA A 176 ? 0.37995 0.35144 0.35695 -0.00271 -0.01250 -0.01313 176 ALA A N   
1368 C CA  . ALA A 176 ? 0.30839 0.27811 0.27975 -0.00371 -0.01134 -0.01431 176 ALA A CA  
1369 C C   . ALA A 176 ? 0.39680 0.36536 0.36639 -0.00370 -0.00958 -0.01644 176 ALA A C   
1370 O O   . ALA A 176 ? 0.44322 0.41069 0.40869 -0.00432 -0.00787 -0.01760 176 ALA A O   
1371 C CB  . ALA A 176 ? 0.24550 0.21230 0.21237 -0.00532 -0.01377 -0.01381 176 ALA A CB  
1372 N N   . ALA A 177 ? 0.38972 0.35844 0.36247 -0.00303 -0.00984 -0.01697 177 ALA A N   
1373 C CA  . ALA A 177 ? 0.31419 0.28194 0.28614 -0.00288 -0.00810 -0.01900 177 ALA A CA  
1374 C C   . ALA A 177 ? 0.40526 0.37558 0.38325 -0.00131 -0.00717 -0.01880 177 ALA A C   
1375 O O   . ALA A 177 ? 0.41232 0.38310 0.39384 -0.00089 -0.00886 -0.01789 177 ALA A O   
1376 C CB  . ALA A 177 ? 0.41432 0.37853 0.38285 -0.00407 -0.00977 -0.02015 177 ALA A CB  
1377 N N   . MET A 178 ? 0.35522 0.32722 0.33453 -0.00048 -0.00454 -0.01955 178 MET A N   
1378 C CA  . MET A 178 ? 0.36097 0.33549 0.34584 0.00098  -0.00360 -0.01923 178 MET A CA  
1379 C C   . MET A 178 ? 0.37133 0.34469 0.35683 0.00122  -0.00242 -0.02105 178 MET A C   
1380 O O   . MET A 178 ? 0.39620 0.36737 0.37777 0.00043  -0.00130 -0.02280 178 MET A O   
1381 C CB  . MET A 178 ? 0.43182 0.40920 0.41847 0.00181  -0.00169 -0.01865 178 MET A CB  
1382 C CG  . MET A 178 ? 0.39621 0.37497 0.38284 0.00172  -0.00259 -0.01692 178 MET A CG  
1383 S SD  . MET A 178 ? 0.41514 0.39706 0.40377 0.00260  -0.00039 -0.01646 178 MET A SD  
1384 C CE  . MET A 178 ? 0.31341 0.29625 0.30169 0.00231  -0.00179 -0.01459 178 MET A CE  
1385 N N   . PRO A 179 ? 0.32214 0.29680 0.31253 0.00227  -0.00257 -0.02067 179 PRO A N   
1386 C CA  . PRO A 179 ? 0.35634 0.33018 0.34814 0.00265  -0.00127 -0.02233 179 PRO A CA  
1387 C C   . PRO A 179 ? 0.36116 0.33607 0.35300 0.00311  0.00155  -0.02334 179 PRO A C   
1388 O O   . PRO A 179 ? 0.35247 0.33025 0.34742 0.00404  0.00244  -0.02226 179 PRO A O   
1389 C CB  . PRO A 179 ? 0.31955 0.29524 0.31720 0.00380  -0.00207 -0.02109 179 PRO A CB  
1390 C CG  . PRO A 179 ? 0.33242 0.30869 0.33061 0.00360  -0.00429 -0.01919 179 PRO A CG  
1391 C CD  . PRO A 179 ? 0.35226 0.32896 0.34707 0.00305  -0.00401 -0.01871 179 PRO A CD  
1392 N N   . PRO A 180 ? 0.31348 0.28611 0.30194 0.00242  0.00303  -0.02542 180 PRO A N   
1393 C CA  . PRO A 180 ? 0.33581 0.30936 0.32438 0.00276  0.00587  -0.02643 180 PRO A CA  
1394 C C   . PRO A 180 ? 0.34840 0.32366 0.34263 0.00408  0.00718  -0.02672 180 PRO A C   
1395 O O   . PRO A 180 ? 0.40122 0.37620 0.39842 0.00454  0.00610  -0.02660 180 PRO A O   
1396 C CB  . PRO A 180 ? 0.39019 0.36026 0.37311 0.00148  0.00694  -0.02865 180 PRO A CB  
1397 C CG  . PRO A 180 ? 0.35260 0.32013 0.33456 0.00094  0.00500  -0.02927 180 PRO A CG  
1398 C CD  . PRO A 180 ? 0.37118 0.34013 0.35551 0.00123  0.00219  -0.02701 180 PRO A CD  
1399 N N   . PRO A 181 ? 0.36660 0.34366 0.36276 0.00471  0.00942  -0.02697 181 PRO A N   
1400 C CA  . PRO A 181 ? 0.37479 0.35324 0.37639 0.00589  0.01071  -0.02734 181 PRO A CA  
1401 C C   . PRO A 181 ? 0.34574 0.32143 0.34670 0.00560  0.01179  -0.02963 181 PRO A C   
1402 O O   . PRO A 181 ? 0.37278 0.34557 0.36858 0.00444  0.01234  -0.03129 181 PRO A O   
1403 C CB  . PRO A 181 ? 0.34988 0.33046 0.35280 0.00632  0.01285  -0.02728 181 PRO A CB  
1404 C CG  . PRO A 181 ? 0.39767 0.37886 0.39709 0.00566  0.01208  -0.02613 181 PRO A CG  
1405 C CD  . PRO A 181 ? 0.37718 0.35537 0.37126 0.00441  0.01064  -0.02666 181 PRO A CD  
1406 N N   . ALA A 182 ? 0.36704 0.34354 0.37326 0.00663  0.01209  -0.02971 182 ALA A N   
1407 C CA  . ALA A 182 ? 0.34360 0.31757 0.35006 0.00649  0.01321  -0.03192 182 ALA A CA  
1408 C C   . ALA A 182 ? 0.36175 0.33477 0.36657 0.00621  0.01632  -0.03398 182 ALA A C   
1409 O O   . ALA A 182 ? 0.38700 0.36229 0.39374 0.00672  0.01783  -0.03345 182 ALA A O   
1410 C CB  . ALA A 182 ? 0.40184 0.37716 0.41495 0.00775  0.01293  -0.03133 182 ALA A CB  
1411 N N   . GLU A 183 ? 0.38364 0.35322 0.38491 0.00533  0.01731  -0.03637 183 GLU A N   
1412 C CA  . GLU A 183 ? 0.29248 0.26069 0.29159 0.00490  0.02051  -0.03854 183 GLU A CA  
1413 C C   . GLU A 183 ? 0.36321 0.33234 0.36855 0.00608  0.02276  -0.03955 183 GLU A C   
1414 O O   . GLU A 183 ? 0.35610 0.32565 0.36614 0.00691  0.02179  -0.03921 183 GLU A O   
1415 C CB  . GLU A 183 ? 0.38918 0.35304 0.38134 0.00334  0.02078  -0.04080 183 GLU A CB  
1416 C CG  . GLU A 183 ? 0.41790 0.38058 0.40383 0.00207  0.01841  -0.03979 183 GLU A CG  
1417 C CD  . GLU A 183 ? 0.39840 0.35725 0.37657 0.00039  0.01959  -0.04190 183 GLU A CD  
1418 O OE1 . GLU A 183 ? 0.39678 0.35392 0.37428 0.00023  0.02254  -0.04425 183 GLU A OE1 
1419 O OE2 . GLU A 183 ? 0.40037 0.35786 0.37312 -0.00080 0.01760  -0.04117 183 GLU A OE2 
1420 N N   . ASP A 184 ? 0.32055 0.29001 0.32618 0.00613  0.02581  -0.04071 184 ASP A N   
1421 C CA  . ASP A 184 ? 0.30897 0.27926 0.32066 0.00719  0.02832  -0.04178 184 ASP A CA  
1422 C C   . ASP A 184 ? 0.41359 0.38763 0.43292 0.00872  0.02701  -0.03943 184 ASP A C   
1423 O O   . ASP A 184 ? 0.43447 0.40871 0.45903 0.00961  0.02692  -0.03959 184 ASP A O   
1424 C CB  . ASP A 184 ? 0.27430 0.24121 0.28562 0.00692  0.02933  -0.04433 184 ASP A CB  
1425 C CG  . ASP A 184 ? 0.34852 0.31146 0.35189 0.00530  0.03078  -0.04680 184 ASP A CG  
1426 O OD1 . ASP A 184 ? 0.23511 0.19807 0.23511 0.00468  0.03264  -0.04717 184 ASP A OD1 
1427 O OD2 . ASP A 184 ? 0.27759 0.23730 0.27796 0.00457  0.03003  -0.04834 184 ASP A OD2 
1428 N N   . MET A 185 ? 0.36539 0.34232 0.38519 0.00896  0.02594  -0.03721 185 MET A N   
1429 C CA  . MET A 185 ? 0.35164 0.33217 0.37796 0.01026  0.02481  -0.03491 185 MET A CA  
1430 C C   . MET A 185 ? 0.37465 0.35748 0.40410 0.01074  0.02692  -0.03474 185 MET A C   
1431 O O   . MET A 185 ? 0.25032 0.23332 0.27597 0.01004  0.02772  -0.03479 185 MET A O   
1432 C CB  . MET A 185 ? 0.38640 0.36851 0.41117 0.01018  0.02175  -0.03241 185 MET A CB  
1433 C CG  . MET A 185 ? 0.39634 0.37704 0.42038 0.01006  0.01935  -0.03198 185 MET A CG  
1434 S SD  . MET A 185 ? 0.30514 0.28688 0.33694 0.01142  0.01882  -0.03134 185 MET A SD  
1435 C CE  . MET A 185 ? 0.32397 0.30379 0.35359 0.01094  0.01598  -0.03084 185 MET A CE  
1436 N N   . PRO A 186 ? 0.39764 0.38224 0.43414 0.01190  0.02779  -0.03445 186 PRO A N   
1437 C CA  . PRO A 186 ? 0.34785 0.33459 0.38783 0.01233  0.02984  -0.03436 186 PRO A CA  
1438 C C   . PRO A 186 ? 0.30278 0.29242 0.34245 0.01235  0.02836  -0.03206 186 PRO A C   
1439 O O   . PRO A 186 ? 0.29605 0.28638 0.33455 0.01197  0.02996  -0.03238 186 PRO A O   
1440 C CB  . PRO A 186 ? 0.36146 0.34949 0.40957 0.01361  0.03032  -0.03415 186 PRO A CB  
1441 C CG  . PRO A 186 ? 0.36470 0.35239 0.41377 0.01398  0.02767  -0.03303 186 PRO A CG  
1442 C CD  . PRO A 186 ? 0.29473 0.27936 0.33655 0.01283  0.02699  -0.03422 186 PRO A CD  
1443 N N   . SER A 187 ? 0.38034 0.37161 0.42100 0.01276  0.02546  -0.02978 187 SER A N   
1444 C CA  . SER A 187 ? 0.31818 0.31208 0.35849 0.01276  0.02406  -0.02769 187 SER A CA  
1445 C C   . SER A 187 ? 0.32933 0.32208 0.36256 0.01160  0.02362  -0.02782 187 SER A C   
1446 O O   . SER A 187 ? 0.37691 0.37147 0.40930 0.01143  0.02317  -0.02661 187 SER A O   
1447 C CB  . SER A 187 ? 0.30961 0.30541 0.35296 0.01349  0.02129  -0.02529 187 SER A CB  
1448 O OG  . SER A 187 ? 0.41446 0.41144 0.46455 0.01454  0.02150  -0.02488 187 SER A OG  
1449 N N   . ALA A 188 ? 0.24850 0.23822 0.27670 0.01078  0.02364  -0.02922 188 ALA A N   
1450 C CA  . ALA A 188 ? 0.26426 0.25258 0.28569 0.00960  0.02314  -0.02936 188 ALA A CA  
1451 C C   . ALA A 188 ? 0.30149 0.28784 0.31921 0.00871  0.02588  -0.03146 188 ALA A C   
1452 O O   . ALA A 188 ? 0.26157 0.24561 0.27305 0.00756  0.02571  -0.03218 188 ALA A O   
1453 C CB  . ALA A 188 ? 0.23483 0.22104 0.25278 0.00911  0.02102  -0.02929 188 ALA A CB  
1454 N N   . ALA A 189 ? 0.26627 0.25345 0.28779 0.00917  0.02843  -0.03240 189 ALA A N   
1455 C CA  . ALA A 189 ? 0.27872 0.26409 0.29699 0.00833  0.03140  -0.03438 189 ALA A CA  
1456 C C   . ALA A 189 ? 0.26223 0.24873 0.27742 0.00766  0.03146  -0.03342 189 ALA A C   
1457 O O   . ALA A 189 ? 0.35379 0.34330 0.37236 0.00825  0.03046  -0.03160 189 ALA A O   
1458 C CB  . ALA A 189 ? 0.30464 0.29070 0.32865 0.00909  0.03426  -0.03563 189 ALA A CB  
1459 N N   . PRO A 190 ? 0.27006 0.25408 0.27874 0.00638  0.03257  -0.03458 190 PRO A N   
1460 C CA  . PRO A 190 ? 0.21799 0.20292 0.22359 0.00568  0.03250  -0.03356 190 PRO A CA  
1461 C C   . PRO A 190 ? 0.25222 0.23956 0.26212 0.00611  0.03466  -0.03339 190 PRO A C   
1462 O O   . PRO A 190 ? 0.27063 0.25998 0.28065 0.00603  0.03382  -0.03187 190 PRO A O   
1463 C CB  . PRO A 190 ? 0.35933 0.34062 0.35720 0.00417  0.03355  -0.03509 190 PRO A CB  
1464 C CG  . PRO A 190 ? 0.25652 0.23516 0.25274 0.00405  0.03282  -0.03634 190 PRO A CG  
1465 C CD  . PRO A 190 ? 0.26818 0.24830 0.27159 0.00541  0.03357  -0.03671 190 PRO A CD  
1466 N N   . ALA A 191 ? 0.30740 0.29458 0.32109 0.00657  0.03743  -0.03493 191 ALA A N   
1467 C CA  . ALA A 191 ? 0.31559 0.30510 0.33402 0.00698  0.03953  -0.03477 191 ALA A CA  
1468 C C   . ALA A 191 ? 0.30283 0.29609 0.32783 0.00815  0.03752  -0.03264 191 ALA A C   
1469 O O   . ALA A 191 ? 0.45859 0.45411 0.48727 0.00839  0.03850  -0.03204 191 ALA A O   
1470 C CB  . ALA A 191 ? 0.34934 0.33768 0.37073 0.00723  0.04306  -0.03699 191 ALA A CB  
1471 N N   . ALA A 192 ? 0.38625 0.38013 0.41274 0.00881  0.03474  -0.03148 192 ALA A N   
1472 C CA  . ALA A 192 ? 0.27065 0.26780 0.30239 0.00977  0.03255  -0.02933 192 ALA A CA  
1473 C C   . ALA A 192 ? 0.24623 0.24393 0.27468 0.00954  0.02936  -0.02752 192 ALA A C   
1474 O O   . ALA A 192 ? 0.27594 0.27614 0.30788 0.01021  0.02741  -0.02569 192 ALA A O   
1475 C CB  . ALA A 192 ? 0.28260 0.28040 0.32038 0.01091  0.03222  -0.02932 192 ALA A CB  
1476 N N   . THR A 193 ? 0.25575 0.25112 0.27764 0.00858  0.02879  -0.02796 193 THR A N   
1477 C CA  . THR A 193 ? 0.29715 0.29282 0.31604 0.00834  0.02592  -0.02634 193 THR A CA  
1478 C C   . THR A 193 ? 0.28048 0.27512 0.29358 0.00718  0.02607  -0.02633 193 THR A C   
1479 O O   . THR A 193 ? 0.27704 0.27078 0.28626 0.00669  0.02411  -0.02557 193 THR A O   
1480 C CB  . THR A 193 ? 0.27570 0.26956 0.29301 0.00841  0.02430  -0.02649 193 THR A CB  
1481 O OG1 . THR A 193 ? 0.30548 0.29617 0.31904 0.00769  0.02589  -0.02857 193 THR A OG1 
1482 C CG2 . THR A 193 ? 0.32069 0.31599 0.34399 0.00961  0.02355  -0.02589 193 THR A CG2 
1483 N N   . GLY A 194 ? 0.27357 0.26833 0.28631 0.00672  0.02838  -0.02708 194 GLY A N   
1484 C CA  . GLY A 194 ? 0.28741 0.28129 0.29503 0.00561  0.02864  -0.02694 194 GLY A CA  
1485 C C   . GLY A 194 ? 0.31449 0.31106 0.32385 0.00576  0.02744  -0.02518 194 GLY A C   
1486 O O   . GLY A 194 ? 0.33532 0.33450 0.35007 0.00660  0.02724  -0.02441 194 GLY A O   
1487 N N   . VAL A 195 ? 0.22866 0.22447 0.23337 0.00487  0.02655  -0.02455 195 VAL A N   
1488 C CA  . VAL A 195 ? 0.31356 0.31156 0.31925 0.00486  0.02543  -0.02301 195 VAL A CA  
1489 C C   . VAL A 195 ? 0.35147 0.35059 0.35910 0.00464  0.02776  -0.02343 195 VAL A C   
1490 O O   . VAL A 195 ? 0.37081 0.36822 0.37484 0.00370  0.02960  -0.02432 195 VAL A O   
1491 C CB  . VAL A 195 ? 0.31405 0.31073 0.31445 0.00399  0.02381  -0.02223 195 VAL A CB  
1492 C CG1 . VAL A 195 ? 0.28297 0.28177 0.28450 0.00395  0.02288  -0.02082 195 VAL A CG1 
1493 C CG2 . VAL A 195 ? 0.30690 0.30260 0.30603 0.00424  0.02151  -0.02175 195 VAL A CG2 
1494 N N   . PRO A 196 ? 0.24503 0.24692 0.25825 0.00541  0.02772  -0.02276 196 PRO A N   
1495 C CA  . PRO A 196 ? 0.37308 0.37617 0.38888 0.00521  0.02992  -0.02313 196 PRO A CA  
1496 C C   . PRO A 196 ? 0.33125 0.33494 0.34483 0.00445  0.02946  -0.02221 196 PRO A C   
1497 O O   . PRO A 196 ? 0.32102 0.32484 0.33234 0.00429  0.02720  -0.02108 196 PRO A O   
1498 C CB  . PRO A 196 ? 0.27272 0.27859 0.29553 0.00632  0.02939  -0.02249 196 PRO A CB  
1499 C CG  . PRO A 196 ? 0.36837 0.37504 0.39116 0.00683  0.02630  -0.02111 196 PRO A CG  
1500 C CD  . PRO A 196 ? 0.30999 0.31401 0.32750 0.00644  0.02559  -0.02156 196 PRO A CD  
1501 N N   . THR A 197 ? 0.42466 0.42868 0.43918 0.00398  0.03177  -0.02273 197 THR A N   
1502 C CA  . THR A 197 ? 0.38221 0.38687 0.39528 0.00323  0.03167  -0.02194 197 THR A CA  
1503 C C   . THR A 197 ? 0.33820 0.34604 0.35696 0.00380  0.03079  -0.02090 197 THR A C   
1504 O O   . THR A 197 ? 0.39501 0.40452 0.41884 0.00472  0.03041  -0.02078 197 THR A O   
1505 C CB  . THR A 197 ? 0.40831 0.41141 0.41893 0.00227  0.03472  -0.02300 197 THR A CB  
1506 O OG1 . THR A 197 ? 0.31949 0.32372 0.33522 0.00271  0.03717  -0.02387 197 THR A OG1 
1507 C CG2 . THR A 197 ? 0.46156 0.46127 0.46605 0.00158  0.03545  -0.02405 197 THR A CG2 
1508 N N   . TRP A 198 ? 0.30434 0.31293 0.32224 0.00319  0.03035  -0.02011 198 TRP A N   
1509 C CA  . TRP A 198 ? 0.40450 0.41593 0.42728 0.00356  0.02926  -0.01912 198 TRP A CA  
1510 C C   . TRP A 198 ? 0.39030 0.40324 0.41858 0.00378  0.03143  -0.01966 198 TRP A C   
1511 O O   . TRP A 198 ? 0.31606 0.33143 0.34958 0.00434  0.03035  -0.01895 198 TRP A O   
1512 C CB  . TRP A 198 ? 0.44283 0.45447 0.46322 0.00278  0.02828  -0.01825 198 TRP A CB  
1513 C CG  . TRP A 198 ? 0.41903 0.42963 0.43739 0.00178  0.03063  -0.01874 198 TRP A CG  
1514 C CD1 . TRP A 198 ? 0.43221 0.44022 0.44482 0.00091  0.03154  -0.01912 198 TRP A CD1 
1515 C CD2 . TRP A 198 ? 0.44715 0.45923 0.46926 0.00148  0.03233  -0.01879 198 TRP A CD2 
1516 N NE1 . TRP A 198 ? 0.44252 0.45024 0.45481 0.00007  0.03380  -0.01939 198 TRP A NE1 
1517 C CE2 . TRP A 198 ? 0.46275 0.47299 0.48098 0.00043  0.03439  -0.01922 198 TRP A CE2 
1518 C CE3 . TRP A 198 ? 0.47198 0.48673 0.50046 0.00196  0.03221  -0.01845 198 TRP A CE3 
1519 C CZ2 . TRP A 198 ? 0.42715 0.43817 0.44775 -0.00013 0.03654  -0.01934 198 TRP A CZ2 
1520 C CZ3 . TRP A 198 ? 0.45278 0.46836 0.48386 0.00142  0.03420  -0.01859 198 TRP A CZ3 
1521 C CH2 . TRP A 198 ? 0.42043 0.43417 0.44763 0.00040  0.03644  -0.01905 198 TRP A CH2 
1522 N N   . GLN A 199 ? 0.42554 0.43703 0.45280 0.00331  0.03446  -0.02088 199 GLN A N   
1523 C CA  . GLN A 199 ? 0.40812 0.42100 0.44105 0.00355  0.03682  -0.02147 199 GLN A CA  
1524 C C   . GLN A 199 ? 0.42264 0.43619 0.46013 0.00464  0.03693  -0.02195 199 GLN A C   
1525 O O   . GLN A 199 ? 0.45750 0.47323 0.50157 0.00521  0.03729  -0.02173 199 GLN A O   
1526 C CB  . GLN A 199 ? 0.40610 0.41705 0.43633 0.00266  0.04033  -0.02268 199 GLN A CB  
1527 C CG  . GLN A 199 ? 0.51889 0.52884 0.54429 0.00149  0.04043  -0.02219 199 GLN A CG  
1528 C CD  . GLN A 199 ? 0.39353 0.40067 0.41137 0.00090  0.03950  -0.02230 199 GLN A CD  
1529 O OE1 . GLN A 199 ? 0.42575 0.43243 0.44225 0.00144  0.03739  -0.02211 199 GLN A OE1 
1530 N NE2 . GLN A 199 ? 0.32375 0.32895 0.33674 -0.00025 0.04101  -0.02250 199 GLN A NE2 
1531 N N   . GLU A 200 ? 0.42082 0.43248 0.45512 0.00491  0.03653  -0.02255 200 GLU A N   
1532 C CA  . GLU A 200 ? 0.40428 0.41621 0.44262 0.00590  0.03683  -0.02311 200 GLU A CA  
1533 C C   . GLU A 200 ? 0.42795 0.44206 0.47020 0.00682  0.03370  -0.02170 200 GLU A C   
1534 O O   . GLU A 200 ? 0.41309 0.42814 0.46042 0.00769  0.03379  -0.02181 200 GLU A O   
1535 C CB  . GLU A 200 ? 0.43119 0.44013 0.46459 0.00576  0.03753  -0.02434 200 GLU A CB  
1536 C CG  . GLU A 200 ? 0.39325 0.39966 0.42216 0.00475  0.04065  -0.02582 200 GLU A CG  
1537 C CD  . GLU A 200 ? 0.43742 0.44064 0.46006 0.00435  0.04063  -0.02680 200 GLU A CD  
1538 O OE1 . GLU A 200 ? 0.47205 0.47512 0.49459 0.00496  0.03843  -0.02644 200 GLU A OE1 
1539 O OE2 . GLU A 200 ? 0.25970 0.26049 0.27743 0.00335  0.04278  -0.02789 200 GLU A OE2 
1540 N N   . VAL A 201 ? 0.38512 0.39996 0.42513 0.00661  0.03100  -0.02036 201 VAL A N   
1541 C CA  . VAL A 201 ? 0.38567 0.40249 0.42890 0.00735  0.02809  -0.01896 201 VAL A CA  
1542 C C   . VAL A 201 ? 0.44455 0.46411 0.49337 0.00746  0.02753  -0.01806 201 VAL A C   
1543 O O   . VAL A 201 ? 0.46456 0.48585 0.51648 0.00801  0.02515  -0.01686 201 VAL A O   
1544 C CB  . VAL A 201 ? 0.42238 0.43862 0.46070 0.00709  0.02549  -0.01800 201 VAL A CB  
1545 C CG1 . VAL A 201 ? 0.39478 0.40837 0.42802 0.00697  0.02572  -0.01875 201 VAL A CG1 
1546 C CG2 . VAL A 201 ? 0.40861 0.42510 0.44439 0.00621  0.02527  -0.01756 201 VAL A CG2 
1547 N N   . GLY A 202 ? 0.36599 0.38596 0.41616 0.00689  0.02958  -0.01855 202 GLY A N   
1548 C CA  . GLY A 202 ? 0.34852 0.37107 0.40458 0.00696  0.02915  -0.01777 202 GLY A CA  
1549 C C   . GLY A 202 ? 0.41392 0.43723 0.46813 0.00616  0.02802  -0.01700 202 GLY A C   
1550 O O   . GLY A 202 ? 0.47865 0.50390 0.53563 0.00626  0.02568  -0.01582 202 GLY A O   
1551 N N   . PHE A 203 ? 0.42656 0.44825 0.47606 0.00530  0.02960  -0.01762 203 PHE A N   
1552 C CA  . PHE A 203 ? 0.42400 0.44620 0.47184 0.00447  0.02885  -0.01699 203 PHE A CA  
1553 C C   . PHE A 203 ? 0.43719 0.45908 0.48577 0.00375  0.03188  -0.01773 203 PHE A C   
1554 O O   . PHE A 203 ? 0.49347 0.51387 0.54112 0.00368  0.03466  -0.01888 203 PHE A O   
1555 C CB  . PHE A 203 ? 0.35692 0.37739 0.39792 0.00402  0.02738  -0.01670 203 PHE A CB  
1556 C CG  . PHE A 203 ? 0.34583 0.36714 0.38648 0.00446  0.02413  -0.01563 203 PHE A CG  
1557 C CD1 . PHE A 203 ? 0.28054 0.30376 0.32365 0.00432  0.02221  -0.01467 203 PHE A CD1 
1558 C CD2 . PHE A 203 ? 0.39305 0.41315 0.43082 0.00495  0.02304  -0.01561 203 PHE A CD2 
1559 C CE1 . PHE A 203 ? 0.36302 0.38682 0.40538 0.00464  0.01939  -0.01375 203 PHE A CE1 
1560 C CE2 . PHE A 203 ? 0.47591 0.49671 0.51328 0.00531  0.02029  -0.01461 203 PHE A CE2 
1561 C CZ  . PHE A 203 ? 0.42483 0.44744 0.46432 0.00515  0.01853  -0.01369 203 PHE A CZ  
1562 N N   . LYS A 204 ? 0.41414 0.43736 0.46431 0.00317  0.03139  -0.01708 204 LYS A N   
1563 C CA  . LYS A 204 ? 0.49295 0.51629 0.54484 0.00247  0.03414  -0.01755 204 LYS A CA  
1564 C C   . LYS A 204 ? 0.51616 0.53822 0.56298 0.00139  0.03442  -0.01737 204 LYS A C   
1565 O O   . LYS A 204 ? 0.54221 0.56310 0.58760 0.00072  0.03726  -0.01801 204 LYS A O   
1566 C CB  . LYS A 204 ? 0.48566 0.51186 0.54519 0.00263  0.03369  -0.01694 204 LYS A CB  
1567 C CG  . LYS A 204 ? 0.45532 0.48271 0.52131 0.00348  0.03496  -0.01736 204 LYS A CG  
1568 C CD  . LYS A 204 ? 0.47312 0.50082 0.53983 0.00447  0.03264  -0.01698 204 LYS A CD  
1569 C CE  . LYS A 204 ? 0.47412 0.50331 0.54113 0.00452  0.02874  -0.01559 204 LYS A CE  
1570 N NZ  . LYS A 204 ? 0.46665 0.49588 0.53352 0.00539  0.02653  -0.01512 204 LYS A NZ  
1571 N N   . GLU A 205 ? 0.55371 0.57589 0.59783 0.00118  0.03166  -0.01650 205 GLU A N   
1572 C CA  . GLU A 205 ? 0.49758 0.51855 0.53725 0.00020  0.03173  -0.01622 205 GLU A CA  
1573 C C   . GLU A 205 ? 0.38920 0.40783 0.42215 0.00012  0.03080  -0.01626 205 GLU A C   
1574 O O   . GLU A 205 ? 0.24496 0.26371 0.27713 0.00078  0.02860  -0.01596 205 GLU A O   
1575 C CB  . GLU A 205 ? 0.51815 0.54086 0.55997 -0.00009 0.02944  -0.01528 205 GLU A CB  
1576 C CG  . GLU A 205 ? 0.51048 0.53556 0.55919 -0.00013 0.03000  -0.01511 205 GLU A CG  
1577 C CD  . GLU A 205 ? 0.56508 0.59148 0.61521 -0.00068 0.02793  -0.01431 205 GLU A CD  
1578 O OE1 . GLU A 205 ? 0.60128 0.62645 0.64692 -0.00128 0.02720  -0.01406 205 GLU A OE1 
1579 O OE2 . GLU A 205 ? 0.53965 0.56827 0.59553 -0.00052 0.02697  -0.01393 205 GLU A OE2 
1580 N N   . PRO A 206 ? 0.45902 0.47550 0.48715 -0.00071 0.03233  -0.01653 206 PRO A N   
1581 C CA  . PRO A 206 ? 0.36530 0.37946 0.38726 -0.00084 0.03142  -0.01654 206 PRO A CA  
1582 C C   . PRO A 206 ? 0.38664 0.40105 0.40686 -0.00090 0.02853  -0.01558 206 PRO A C   
1583 O O   . PRO A 206 ? 0.38973 0.40558 0.41226 -0.00118 0.02768  -0.01500 206 PRO A O   
1584 C CB  . PRO A 206 ? 0.34971 0.36166 0.36753 -0.00190 0.03385  -0.01691 206 PRO A CB  
1585 C CG  . PRO A 206 ? 0.41148 0.42483 0.43278 -0.00246 0.03515  -0.01664 206 PRO A CG  
1586 C CD  . PRO A 206 ? 0.41348 0.42951 0.44168 -0.00163 0.03498  -0.01676 206 PRO A CD  
1587 N N   . PRO A 207 ? 0.34652 0.35952 0.36285 -0.00066 0.02702  -0.01543 207 PRO A N   
1588 C CA  . PRO A 207 ? 0.36324 0.37631 0.37790 -0.00072 0.02453  -0.01459 207 PRO A CA  
1589 C C   . PRO A 207 ? 0.38276 0.39466 0.39449 -0.00176 0.02487  -0.01417 207 PRO A C   
1590 O O   . PRO A 207 ? 0.39943 0.40976 0.40866 -0.00246 0.02676  -0.01444 207 PRO A O   
1591 C CB  . PRO A 207 ? 0.30371 0.31536 0.31516 -0.00023 0.02333  -0.01463 207 PRO A CB  
1592 C CG  . PRO A 207 ? 0.33558 0.34552 0.34497 -0.00040 0.02539  -0.01548 207 PRO A CG  
1593 C CD  . PRO A 207 ? 0.39777 0.40904 0.41133 -0.00033 0.02753  -0.01607 207 PRO A CD  
1594 N N   . LEU A 208 ? 0.32655 0.33911 0.33853 -0.00188 0.02301  -0.01349 208 LEU A N   
1595 C CA  . LEU A 208 ? 0.33596 0.34759 0.34586 -0.00281 0.02307  -0.01298 208 LEU A CA  
1596 C C   . LEU A 208 ? 0.28763 0.29796 0.29415 -0.00285 0.02115  -0.01241 208 LEU A C   
1597 O O   . LEU A 208 ? 0.40130 0.41081 0.40628 -0.00357 0.02094  -0.01189 208 LEU A O   
1598 C CB  . LEU A 208 ? 0.35593 0.36947 0.36976 -0.00309 0.02287  -0.01275 208 LEU A CB  
1599 C CG  . LEU A 208 ? 0.37357 0.38881 0.39193 -0.00301 0.02450  -0.01318 208 LEU A CG  
1600 C CD1 . LEU A 208 ? 0.41228 0.42933 0.43448 -0.00335 0.02384  -0.01286 208 LEU A CD1 
1601 C CD2 . LEU A 208 ? 0.43016 0.44409 0.44708 -0.00359 0.02734  -0.01357 208 LEU A CD2 
1602 N N   . THR A 209 ? 0.27541 0.28553 0.28105 -0.00211 0.01981  -0.01245 209 THR A N   
1603 C CA  . THR A 209 ? 0.32153 0.33061 0.32468 -0.00207 0.01803  -0.01190 209 THR A CA  
1604 C C   . THR A 209 ? 0.33246 0.33905 0.33129 -0.00273 0.01844  -0.01163 209 THR A C   
1605 O O   . THR A 209 ? 0.27608 0.28156 0.27319 -0.00306 0.01997  -0.01200 209 THR A O   
1606 C CB  . THR A 209 ? 0.30343 0.31301 0.30710 -0.00111 0.01663  -0.01196 209 THR A CB  
1607 O OG1 . THR A 209 ? 0.26173 0.27049 0.26359 -0.00107 0.01502  -0.01142 209 THR A OG1 
1608 C CG2 . THR A 209 ? 0.31316 0.32172 0.31542 -0.00078 0.01739  -0.01242 209 THR A CG2 
1609 N N   . VAL A 210 ? 0.34165 0.34728 0.33872 -0.00295 0.01704  -0.01096 210 VAL A N   
1610 C CA  . VAL A 210 ? 0.36037 0.36362 0.35353 -0.00363 0.01694  -0.01045 210 VAL A CA  
1611 C C   . VAL A 210 ? 0.29400 0.29618 0.28535 -0.00314 0.01549  -0.01028 210 VAL A C   
1612 O O   . VAL A 210 ? 0.32281 0.32300 0.31110 -0.00366 0.01493  -0.00974 210 VAL A O   
1613 C CB  . VAL A 210 ? 0.38608 0.38880 0.37883 -0.00437 0.01648  -0.00968 210 VAL A CB  
1614 C CG1 . VAL A 210 ? 0.26688 0.27059 0.26152 -0.00493 0.01798  -0.00982 210 VAL A CG1 
1615 C CG2 . VAL A 210 ? 0.31572 0.31926 0.31017 -0.00386 0.01474  -0.00940 210 VAL A CG2 
1616 N N   . PHE A 211 ? 0.31871 0.32212 0.31200 -0.00218 0.01480  -0.01064 211 PHE A N   
1617 C CA  . PHE A 211 ? 0.29970 0.30232 0.29188 -0.00166 0.01345  -0.01045 211 PHE A CA  
1618 C C   . PHE A 211 ? 0.31217 0.31453 0.30393 -0.00125 0.01413  -0.01114 211 PHE A C   
1619 O O   . PHE A 211 ? 0.30116 0.30512 0.29555 -0.00064 0.01469  -0.01168 211 PHE A O   
1620 C CB  . PHE A 211 ? 0.35333 0.35739 0.34788 -0.00092 0.01214  -0.01025 211 PHE A CB  
1621 C CG  . PHE A 211 ? 0.32138 0.32583 0.31676 -0.00128 0.01167  -0.00982 211 PHE A CG  
1622 C CD1 . PHE A 211 ? 0.32661 0.32955 0.32031 -0.00178 0.01096  -0.00914 211 PHE A CD1 
1623 C CD2 . PHE A 211 ? 0.33967 0.34593 0.33766 -0.00117 0.01187  -0.01010 211 PHE A CD2 
1624 C CE1 . PHE A 211 ? 0.25885 0.26204 0.25354 -0.00210 0.01062  -0.00883 211 PHE A CE1 
1625 C CE2 . PHE A 211 ? 0.31497 0.32145 0.31367 -0.00155 0.01145  -0.00985 211 PHE A CE2 
1626 C CZ  . PHE A 211 ? 0.23074 0.23566 0.22783 -0.00199 0.01091  -0.00925 211 PHE A CZ  
1627 N N   . LYS A 212 ? 0.31569 0.31595 0.30423 -0.00163 0.01400  -0.01111 212 LYS A N   
1628 C CA  . LYS A 212 ? 0.27823 0.27781 0.26593 -0.00136 0.01465  -0.01187 212 LYS A CA  
1629 C C   . LYS A 212 ? 0.28126 0.28094 0.26973 -0.00054 0.01310  -0.01173 212 LYS A C   
1630 O O   . LYS A 212 ? 0.33362 0.33247 0.32107 -0.00061 0.01158  -0.01099 212 LYS A O   
1631 C CB  . LYS A 212 ? 0.33314 0.33015 0.31655 -0.00233 0.01529  -0.01200 212 LYS A CB  
1632 C CG  . LYS A 212 ? 0.37708 0.37369 0.35927 -0.00327 0.01687  -0.01197 212 LYS A CG  
1633 C CD  . LYS A 212 ? 0.32065 0.31821 0.30446 -0.00314 0.01917  -0.01302 212 LYS A CD  
1634 C CE  . LYS A 212 ? 0.34684 0.34233 0.32743 -0.00354 0.02039  -0.01389 212 LYS A CE  
1635 N NZ  . LYS A 212 ? 0.36392 0.35686 0.33963 -0.00484 0.02073  -0.01351 212 LYS A NZ  
1636 N N   . GLY A 213 ? 0.27762 0.27832 0.26816 0.00023  0.01353  -0.01236 213 GLY A N   
1637 C CA  . GLY A 213 ? 0.30010 0.30099 0.29163 0.00100  0.01220  -0.01218 213 GLY A CA  
1638 C C   . GLY A 213 ? 0.34118 0.33985 0.32992 0.00077  0.01173  -0.01239 213 GLY A C   
1639 O O   . GLY A 213 ? 0.34443 0.34144 0.33042 0.00006  0.01268  -0.01293 213 GLY A O   
1640 N N   . GLY A 214 ? 0.30033 0.29892 0.28975 0.00131  0.01025  -0.01195 214 GLY A N   
1641 C CA  . GLY A 214 ? 0.24066 0.23726 0.22794 0.00113  0.00952  -0.01212 214 GLY A CA  
1642 C C   . GLY A 214 ? 0.29012 0.28596 0.27696 0.00111  0.00760  -0.01113 214 GLY A C   
1643 O O   . GLY A 214 ? 0.29016 0.28648 0.27746 0.00097  0.00700  -0.01034 214 GLY A O   
1644 N N   . GLU A 215 ? 0.33474 0.32935 0.32097 0.00124  0.00666  -0.01121 215 GLU A N   
1645 C CA  . GLU A 215 ? 0.26039 0.25419 0.24659 0.00120  0.00481  -0.01025 215 GLU A CA  
1646 C C   . GLU A 215 ? 0.29999 0.29183 0.28303 0.00012  0.00406  -0.00973 215 GLU A C   
1647 O O   . GLU A 215 ? 0.27055 0.26231 0.25420 0.00000  0.00290  -0.00871 215 GLU A O   
1648 C CB  . GLU A 215 ? 0.32911 0.32214 0.31580 0.00159  0.00397  -0.01047 215 GLU A CB  
1649 C CG  . GLU A 215 ? 0.27688 0.26914 0.26412 0.00159  0.00207  -0.00946 215 GLU A CG  
1650 C CD  . GLU A 215 ? 0.22695 0.21824 0.21456 0.00184  0.00122  -0.00972 215 GLU A CD  
1651 O OE1 . GLU A 215 ? 0.25576 0.24650 0.24244 0.00184  0.00206  -0.01079 215 GLU A OE1 
1652 O OE2 . GLU A 215 ? 0.19160 0.18264 0.18065 0.00203  -0.00022 -0.00889 215 GLU A OE2 
1653 N N   . THR A 216 ? 0.25562 0.24575 0.23528 -0.00072 0.00475  -0.01038 216 THR A N   
1654 C CA  . THR A 216 ? 0.23742 0.22552 0.21366 -0.00187 0.00400  -0.00977 216 THR A CA  
1655 C C   . THR A 216 ? 0.27835 0.26742 0.25522 -0.00211 0.00441  -0.00907 216 THR A C   
1656 O O   . THR A 216 ? 0.29817 0.28631 0.27426 -0.00266 0.00313  -0.00801 216 THR A O   
1657 C CB  . THR A 216 ? 0.26558 0.25164 0.23770 -0.00278 0.00500  -0.01073 216 THR A CB  
1658 O OG1 . THR A 216 ? 0.23170 0.21682 0.20341 -0.00254 0.00468  -0.01154 216 THR A OG1 
1659 C CG2 . THR A 216 ? 0.26899 0.25266 0.23709 -0.00409 0.00395  -0.00994 216 THR A CG2 
1660 N N   . GLU A 217 ? 0.27769 0.26861 0.25624 -0.00171 0.00610  -0.00962 217 GLU A N   
1661 C CA  . GLU A 217 ? 0.28741 0.27938 0.26698 -0.00189 0.00648  -0.00904 217 GLU A CA  
1662 C C   . GLU A 217 ? 0.26034 0.25365 0.24305 -0.00120 0.00535  -0.00827 217 GLU A C   
1663 O O   . GLU A 217 ? 0.34306 0.33645 0.32618 -0.00151 0.00498  -0.00754 217 GLU A O   
1664 C CB  . GLU A 217 ? 0.29764 0.29120 0.27839 -0.00171 0.00849  -0.00986 217 GLU A CB  
1665 C CG  . GLU A 217 ? 0.28602 0.27823 0.26365 -0.00263 0.01001  -0.01044 217 GLU A CG  
1666 C CD  . GLU A 217 ? 0.34761 0.33890 0.32331 -0.00363 0.01002  -0.00963 217 GLU A CD  
1667 O OE1 . GLU A 217 ? 0.31397 0.30594 0.29131 -0.00352 0.00900  -0.00874 217 GLU A OE1 
1668 O OE2 . GLU A 217 ? 0.45504 0.44484 0.42758 -0.00455 0.01114  -0.00990 217 GLU A OE2 
1669 N N   . ALA A 218 ? 0.21526 0.20955 0.20022 -0.00029 0.00491  -0.00844 218 ALA A N   
1670 C CA  . ALA A 218 ? 0.28952 0.28495 0.27724 0.00034  0.00407  -0.00777 218 ALA A CA  
1671 C C   . ALA A 218 ? 0.25363 0.24755 0.24092 -0.00000 0.00242  -0.00678 218 ALA A C   
1672 O O   . ALA A 218 ? 0.27488 0.26911 0.26355 -0.00001 0.00198  -0.00609 218 ALA A O   
1673 C CB  . ALA A 218 ? 0.27661 0.27339 0.26666 0.00134  0.00414  -0.00813 218 ALA A CB  
1674 N N   . LEU A 219 ? 0.29646 0.28868 0.28204 -0.00032 0.00147  -0.00671 219 LEU A N   
1675 C CA  . LEU A 219 ? 0.30475 0.29547 0.29016 -0.00072 -0.00034 -0.00567 219 LEU A CA  
1676 C C   . LEU A 219 ? 0.26929 0.25877 0.25279 -0.00170 -0.00072 -0.00496 219 LEU A C   
1677 O O   . LEU A 219 ? 0.24995 0.23881 0.23455 -0.00190 -0.00203 -0.00389 219 LEU A O   
1678 C CB  . LEU A 219 ? 0.24271 0.23177 0.22650 -0.00095 -0.00141 -0.00583 219 LEU A CB  
1679 C CG  . LEU A 219 ? 0.22922 0.21926 0.21503 -0.00002 -0.00120 -0.00642 219 LEU A CG  
1680 C CD1 . LEU A 219 ? 0.27423 0.26241 0.25791 -0.00043 -0.00203 -0.00685 219 LEU A CD1 
1681 C CD2 . LEU A 219 ? 0.26688 0.25800 0.25635 0.00074  -0.00195 -0.00563 219 LEU A CD2 
1682 N N   . ALA A 220 ? 0.20806 0.19717 0.18897 -0.00234 0.00047  -0.00546 220 ALA A N   
1683 C CA  . ALA A 220 ? 0.26964 0.25757 0.24865 -0.00333 0.00022  -0.00469 220 ALA A CA  
1684 C C   . ALA A 220 ? 0.22245 0.21186 0.20420 -0.00303 0.00066  -0.00427 220 ALA A C   
1685 O O   . ALA A 220 ? 0.35596 0.34453 0.33800 -0.00351 -0.00032 -0.00322 220 ALA A O   
1686 C CB  . ALA A 220 ? 0.28094 0.26798 0.25635 -0.00413 0.00159  -0.00537 220 ALA A CB  
1687 N N   . ARG A 221 ? 0.32832 0.31983 0.31216 -0.00228 0.00204  -0.00508 221 ARG A N   
1688 C CA  . ARG A 221 ? 0.33729 0.33013 0.32362 -0.00202 0.00244  -0.00486 221 ARG A CA  
1689 C C   . ARG A 221 ? 0.27445 0.26760 0.26359 -0.00142 0.00137  -0.00426 221 ARG A C   
1690 O O   . ARG A 221 ? 0.29075 0.28428 0.28162 -0.00142 0.00138  -0.00387 221 ARG A O   
1691 C CB  . ARG A 221 ? 0.29750 0.29241 0.28514 -0.00147 0.00401  -0.00587 221 ARG A CB  
1692 C CG  . ARG A 221 ? 0.24086 0.23684 0.23016 -0.00154 0.00459  -0.00583 221 ARG A CG  
1693 C CD  . ARG A 221 ? 0.24317 0.24102 0.23350 -0.00119 0.00595  -0.00677 221 ARG A CD  
1694 N NE  . ARG A 221 ? 0.22533 0.22393 0.21680 -0.00149 0.00648  -0.00677 221 ARG A NE  
1695 C CZ  . ARG A 221 ? 0.25323 0.25144 0.24363 -0.00227 0.00722  -0.00671 221 ARG A CZ  
1696 N NH1 . ARG A 221 ? 0.26863 0.26567 0.25651 -0.00285 0.00767  -0.00667 221 ARG A NH1 
1697 N NH2 . ARG A 221 ? 0.24049 0.23940 0.23230 -0.00251 0.00758  -0.00671 221 ARG A NH2 
1698 N N   . LEU A 222 ? 0.27653 0.26948 0.26630 -0.00092 0.00057  -0.00422 222 LEU A N   
1699 C CA  . LEU A 222 ? 0.31060 0.30369 0.30317 -0.00040 -0.00034 -0.00358 222 LEU A CA  
1700 C C   . LEU A 222 ? 0.30448 0.29586 0.29704 -0.00107 -0.00180 -0.00238 222 LEU A C   
1701 O O   . LEU A 222 ? 0.29018 0.28175 0.28516 -0.00093 -0.00201 -0.00182 222 LEU A O   
1702 C CB  . LEU A 222 ? 0.27708 0.27040 0.27048 0.00026  -0.00077 -0.00378 222 LEU A CB  
1703 C CG  . LEU A 222 ? 0.30372 0.29744 0.30036 0.00091  -0.00134 -0.00323 222 LEU A CG  
1704 C CD1 . LEU A 222 ? 0.23017 0.22564 0.22878 0.00154  -0.00007 -0.00368 222 LEU A CD1 
1705 C CD2 . LEU A 222 ? 0.24594 0.23949 0.24312 0.00136  -0.00198 -0.00325 222 LEU A CD2 
1706 N N   . GLU A 223 ? 0.34750 0.33711 0.33734 -0.00184 -0.00286 -0.00196 223 GLU A N   
1707 C CA  . GLU A 223 ? 0.27540 0.26324 0.26503 -0.00259 -0.00454 -0.00065 223 GLU A CA  
1708 C C   . GLU A 223 ? 0.33431 0.32198 0.32374 -0.00316 -0.00410 -0.00019 223 GLU A C   
1709 O O   . GLU A 223 ? 0.32480 0.31171 0.31597 -0.00342 -0.00519 0.00093  223 GLU A O   
1710 C CB  . GLU A 223 ? 0.34420 0.32998 0.33022 -0.00344 -0.00580 -0.00038 223 GLU A CB  
1711 C CG  . GLU A 223 ? 0.36335 0.34893 0.34986 -0.00300 -0.00665 -0.00065 223 GLU A CG  
1712 C CD  . GLU A 223 ? 0.39537 0.38061 0.38528 -0.00273 -0.00838 0.00046  223 GLU A CD  
1713 O OE1 . GLU A 223 ? 0.42009 0.40485 0.41152 -0.00305 -0.00918 0.00155  223 GLU A OE1 
1714 O OE2 . GLU A 223 ? 0.30630 0.29177 0.29766 -0.00219 -0.00890 0.00028  223 GLU A OE2 
1715 N N   . ALA A 224 ? 0.32432 0.31267 0.31197 -0.00337 -0.00252 -0.00098 224 ALA A N   
1716 C CA  . ALA A 224 ? 0.30871 0.29703 0.29646 -0.00390 -0.00198 -0.00060 224 ALA A CA  
1717 C C   . ALA A 224 ? 0.31428 0.30393 0.30597 -0.00321 -0.00157 -0.00064 224 ALA A C   
1718 O O   . ALA A 224 ? 0.31245 0.30157 0.30541 -0.00359 -0.00193 0.00014  224 ALA A O   
1719 C CB  . ALA A 224 ? 0.37962 0.36855 0.36507 -0.00423 -0.00027 -0.00151 224 ALA A CB  
1720 N N   . ALA A 225 ? 0.31085 0.30213 0.30444 -0.00224 -0.00078 -0.00154 225 ALA A N   
1721 C CA  . ALA A 225 ? 0.32188 0.31422 0.31880 -0.00163 -0.00029 -0.00170 225 ALA A CA  
1722 C C   . ALA A 225 ? 0.32814 0.31959 0.32765 -0.00146 -0.00156 -0.00070 225 ALA A C   
1723 O O   . ALA A 225 ? 0.44860 0.44020 0.45072 -0.00131 -0.00132 -0.00050 225 ALA A O   
1724 C CB  . ALA A 225 ? 0.35120 0.34534 0.34899 -0.00075 0.00081  -0.00283 225 ALA A CB  
1725 N N   . PHE A 226 ? 0.35974 0.35023 0.35880 -0.00150 -0.00288 -0.00009 226 PHE A N   
1726 C CA  . PHE A 226 ? 0.31127 0.30091 0.31314 -0.00137 -0.00425 0.00098  226 PHE A CA  
1727 C C   . PHE A 226 ? 0.32603 0.31376 0.32722 -0.00233 -0.00593 0.00239  226 PHE A C   
1728 O O   . PHE A 226 ? 0.34800 0.33482 0.35144 -0.00235 -0.00746 0.00347  226 PHE A O   
1729 C CB  . PHE A 226 ? 0.30061 0.29028 0.30290 -0.00088 -0.00494 0.00094  226 PHE A CB  
1730 C CG  . PHE A 226 ? 0.27192 0.26328 0.27626 0.00015  -0.00361 0.00005  226 PHE A CG  
1731 C CD1 . PHE A 226 ? 0.35707 0.34971 0.35964 0.00049  -0.00230 -0.00111 226 PHE A CD1 
1732 C CD2 . PHE A 226 ? 0.31972 0.31134 0.32784 0.00074  -0.00365 0.00044  226 PHE A CD2 
1733 C CE1 . PHE A 226 ? 0.38432 0.37839 0.38851 0.00134  -0.00123 -0.00178 226 PHE A CE1 
1734 C CE2 . PHE A 226 ? 0.27822 0.27122 0.28781 0.00159  -0.00234 -0.00032 226 PHE A CE2 
1735 C CZ  . PHE A 226 ? 0.32033 0.31452 0.32778 0.00186  -0.00122 -0.00138 226 PHE A CZ  
1736 N N   . GLN A 227 ? 0.37498 0.36207 0.37324 -0.00316 -0.00573 0.00249  227 GLN A N   
1737 C CA  . GLN A 227 ? 0.42387 0.40906 0.42130 -0.00417 -0.00735 0.00398  227 GLN A CA  
1738 C C   . GLN A 227 ? 0.38088 0.36599 0.38237 -0.00405 -0.00761 0.00480  227 GLN A C   
1739 O O   . GLN A 227 ? 0.31152 0.29515 0.31411 -0.00459 -0.00942 0.00631  227 GLN A O   
1740 C CB  . GLN A 227 ? 0.41080 0.39532 0.40402 -0.00512 -0.00678 0.00388  227 GLN A CB  
1741 C CG  . GLN A 227 ? 0.39581 0.37926 0.38461 -0.00569 -0.00729 0.00369  227 GLN A CG  
1742 C CD  . GLN A 227 ? 0.51727 0.49861 0.50519 -0.00639 -0.00981 0.00513  227 GLN A CD  
1743 O OE1 . GLN A 227 ? 0.47710 0.45730 0.46627 -0.00694 -0.01121 0.00659  227 GLN A OE1 
1744 N NE2 . GLN A 227 ? 0.50457 0.48533 0.49049 -0.00641 -0.01052 0.00474  227 GLN A NE2 
1745 N N   . ASP A 228 ? 0.36613 0.35273 0.36992 -0.00339 -0.00588 0.00383  228 ASP A N   
1746 C CA  . ASP A 228 ? 0.34063 0.32722 0.34858 -0.00315 -0.00576 0.00427  228 ASP A CA  
1747 C C   . ASP A 228 ? 0.27757 0.26535 0.28895 -0.00205 -0.00492 0.00352  228 ASP A C   
1748 O O   . ASP A 228 ? 0.31833 0.30752 0.32981 -0.00149 -0.00315 0.00214  228 ASP A O   
1749 C CB  . ASP A 228 ? 0.28895 0.27601 0.29661 -0.00343 -0.00438 0.00370  228 ASP A CB  
1750 C CG  . ASP A 228 ? 0.24117 0.22784 0.25297 -0.00335 -0.00437 0.00423  228 ASP A CG  
1751 O OD1 . ASP A 228 ? 0.36249 0.34831 0.37728 -0.00322 -0.00564 0.00533  228 ASP A OD1 
1752 O OD2 . ASP A 228 ? 0.26676 0.25395 0.27907 -0.00342 -0.00309 0.00353  228 ASP A OD2 
1753 N N   . PRO A 229 ? 0.35674 0.34395 0.37092 -0.00177 -0.00614 0.00441  229 PRO A N   
1754 C CA  . PRO A 229 ? 0.34658 0.33487 0.36399 -0.00075 -0.00512 0.00371  229 PRO A CA  
1755 C C   . PRO A 229 ? 0.29245 0.28128 0.31305 -0.00032 -0.00353 0.00309  229 PRO A C   
1756 O O   . PRO A 229 ? 0.31806 0.30798 0.33995 0.00044  -0.00201 0.00203  229 PRO A O   
1757 C CB  . PRO A 229 ? 0.27038 0.25769 0.29042 -0.00073 -0.00700 0.00508  229 PRO A CB  
1758 C CG  . PRO A 229 ? 0.24437 0.23002 0.26399 -0.00170 -0.00892 0.00661  229 PRO A CG  
1759 C CD  . PRO A 229 ? 0.31934 0.30485 0.33395 -0.00241 -0.00854 0.00614  229 PRO A CD  
1760 N N   . LYS A 230 ? 0.30331 0.29130 0.32517 -0.00083 -0.00382 0.00370  230 LYS A N   
1761 C CA  . LYS A 230 ? 0.31334 0.30169 0.33811 -0.00049 -0.00222 0.00293  230 LYS A CA  
1762 C C   . LYS A 230 ? 0.28621 0.27579 0.30834 -0.00037 -0.00038 0.00122  230 LYS A C   
1763 O O   . LYS A 230 ? 0.37004 0.36028 0.39381 0.00015  0.00125  0.00007  230 LYS A O   
1764 C CB  . LYS A 230 ? 0.29176 0.27883 0.31858 -0.00111 -0.00308 0.00407  230 LYS A CB  
1765 C CG  . LYS A 230 ? 0.37687 0.36270 0.40722 -0.00121 -0.00499 0.00586  230 LYS A CG  
1766 C CD  . LYS A 230 ? 0.37141 0.35598 0.40404 -0.00182 -0.00585 0.00707  230 LYS A CD  
1767 C CE  . LYS A 230 ? 0.40033 0.38369 0.43688 -0.00193 -0.00797 0.00900  230 LYS A CE  
1768 N NZ  . LYS A 230 ? 0.41351 0.39557 0.45258 -0.00254 -0.00895 0.01036  230 LYS A NZ  
1769 N N   . TRP A 231 ? 0.29825 0.28809 0.31632 -0.00089 -0.00060 0.00103  231 TRP A N   
1770 C CA  . TRP A 231 ? 0.29294 0.28405 0.30875 -0.00079 0.00094  -0.00048 231 TRP A CA  
1771 C C   . TRP A 231 ? 0.30160 0.29395 0.31681 -0.00003 0.00178  -0.00147 231 TRP A C   
1772 O O   . TRP A 231 ? 0.29269 0.28605 0.30756 0.00027  0.00318  -0.00275 231 TRP A O   
1773 C CB  . TRP A 231 ? 0.29389 0.28497 0.30598 -0.00153 0.00057  -0.00034 231 TRP A CB  
1774 C CG  . TRP A 231 ? 0.29558 0.28804 0.30568 -0.00146 0.00196  -0.00177 231 TRP A CG  
1775 C CD1 . TRP A 231 ? 0.24587 0.23867 0.25613 -0.00178 0.00287  -0.00246 231 TRP A CD1 
1776 C CD2 . TRP A 231 ? 0.30725 0.30093 0.31521 -0.00106 0.00245  -0.00261 231 TRP A CD2 
1777 N NE1 . TRP A 231 ? 0.28341 0.27759 0.29180 -0.00164 0.00380  -0.00364 231 TRP A NE1 
1778 C CE2 . TRP A 231 ? 0.30697 0.30173 0.31399 -0.00118 0.00357  -0.00372 231 TRP A CE2 
1779 C CE3 . TRP A 231 ? 0.33538 0.32932 0.34237 -0.00064 0.00198  -0.00250 231 TRP A CE3 
1780 C CZ2 . TRP A 231 ? 0.22029 0.21639 0.22558 -0.00087 0.00417  -0.00462 231 TRP A CZ2 
1781 C CZ3 . TRP A 231 ? 0.33391 0.32915 0.33914 -0.00031 0.00269  -0.00345 231 TRP A CZ3 
1782 C CH2 . TRP A 231 ? 0.23770 0.23402 0.24215 -0.00042 0.00375  -0.00445 231 TRP A CH2 
1783 N N   . VAL A 232 ? 0.33812 0.33033 0.35314 0.00024  0.00086  -0.00085 232 VAL A N   
1784 C CA  . VAL A 232 ? 0.27774 0.27106 0.29226 0.00094  0.00157  -0.00162 232 VAL A CA  
1785 C C   . VAL A 232 ? 0.25726 0.25083 0.27495 0.00159  0.00270  -0.00206 232 VAL A C   
1786 O O   . VAL A 232 ? 0.40309 0.39767 0.42013 0.00201  0.00404  -0.00316 232 VAL A O   
1787 C CB  . VAL A 232 ? 0.33009 0.32303 0.34372 0.00099  0.00021  -0.00082 232 VAL A CB  
1788 C CG1 . VAL A 232 ? 0.26809 0.26199 0.28229 0.00177  0.00087  -0.00135 232 VAL A CG1 
1789 C CG2 . VAL A 232 ? 0.32485 0.31768 0.33465 0.00040  -0.00037 -0.00083 232 VAL A CG2 
1790 N N   . ALA A 233 ? 0.29407 0.28666 0.31526 0.00165  0.00221  -0.00117 233 ALA A N   
1791 C CA  . ALA A 233 ? 0.31054 0.30323 0.33506 0.00227  0.00348  -0.00158 233 ALA A CA  
1792 C C   . ALA A 233 ? 0.30565 0.29855 0.33034 0.00225  0.00520  -0.00285 233 ALA A C   
1793 O O   . ALA A 233 ? 0.26182 0.25524 0.28689 0.00272  0.00678  -0.00386 233 ALA A O   
1794 C CB  . ALA A 233 ? 0.28133 0.27291 0.31011 0.00232  0.00249  -0.00025 233 ALA A CB  
1795 N N   . GLY A 234 ? 0.33862 0.33102 0.36289 0.00165  0.00492  -0.00282 234 GLY A N   
1796 C CA  . GLY A 234 ? 0.39605 0.38848 0.42060 0.00154  0.00639  -0.00405 234 GLY A CA  
1797 C C   . GLY A 234 ? 0.25562 0.24909 0.27640 0.00130  0.00697  -0.00523 234 GLY A C   
1798 O O   . GLY A 234 ? 0.26123 0.25462 0.28167 0.00091  0.00762  -0.00605 234 GLY A O   
1799 N N   . PHE A 235 ? 0.30070 0.29514 0.31892 0.00151  0.00668  -0.00531 235 PHE A N   
1800 C CA  . PHE A 235 ? 0.31400 0.30953 0.32903 0.00131  0.00707  -0.00628 235 PHE A CA  
1801 C C   . PHE A 235 ? 0.25326 0.24925 0.26804 0.00153  0.00858  -0.00768 235 PHE A C   
1802 O O   . PHE A 235 ? 0.27153 0.26762 0.28697 0.00206  0.00932  -0.00791 235 PHE A O   
1803 C CB  . PHE A 235 ? 0.28891 0.28527 0.30174 0.00153  0.00638  -0.00594 235 PHE A CB  
1804 C CG  . PHE A 235 ? 0.25640 0.25398 0.26650 0.00140  0.00675  -0.00684 235 PHE A CG  
1805 C CD1 . PHE A 235 ? 0.33593 0.33374 0.34442 0.00084  0.00628  -0.00677 235 PHE A CD1 
1806 C CD2 . PHE A 235 ? 0.23006 0.22853 0.23931 0.00181  0.00754  -0.00766 235 PHE A CD2 
1807 C CE1 . PHE A 235 ? 0.23712 0.23612 0.24369 0.00074  0.00659  -0.00754 235 PHE A CE1 
1808 C CE2 . PHE A 235 ? 0.27222 0.27184 0.27932 0.00167  0.00765  -0.00834 235 PHE A CE2 
1809 C CZ  . PHE A 235 ? 0.26987 0.26980 0.27586 0.00116  0.00717  -0.00830 235 PHE A CZ  
1810 N N   . GLN A 236 ? 0.31873 0.31491 0.33244 0.00105  0.00901  -0.00861 236 GLN A N   
1811 C CA  . GLN A 236 ? 0.27358 0.27011 0.28623 0.00106  0.01020  -0.01003 236 GLN A CA  
1812 C C   . GLN A 236 ? 0.26752 0.26514 0.27753 0.00063  0.00984  -0.01061 236 GLN A C   
1813 O O   . GLN A 236 ? 0.27925 0.27678 0.28926 0.00007  0.00945  -0.01060 236 GLN A O   
1814 C CB  . GLN A 236 ? 0.22454 0.21994 0.23920 0.00083  0.01120  -0.01079 236 GLN A CB  
1815 C CG  . GLN A 236 ? 0.33537 0.32972 0.35330 0.00129  0.01173  -0.01026 236 GLN A CG  
1816 C CD  . GLN A 236 ? 0.26869 0.26200 0.28836 0.00120  0.01326  -0.01143 236 GLN A CD  
1817 O OE1 . GLN A 236 ? 0.38756 0.38095 0.40530 0.00089  0.01410  -0.01285 236 GLN A OE1 
1818 N NE2 . GLN A 236 ? 0.21214 0.20438 0.23556 0.00145  0.01359  -0.01087 236 GLN A NE2 
1819 N N   . LYS A 237 ? 0.23680 0.23543 0.24482 0.00089  0.00995  -0.01101 237 LYS A N   
1820 C CA  . LYS A 237 ? 0.23677 0.23659 0.24273 0.00057  0.00943  -0.01136 237 LYS A CA  
1821 C C   . LYS A 237 ? 0.30387 0.30367 0.30945 -0.00009 0.00970  -0.01242 237 LYS A C   
1822 O O   . LYS A 237 ? 0.31555 0.31583 0.32091 -0.00055 0.00915  -0.01232 237 LYS A O   
1823 C CB  . LYS A 237 ? 0.22075 0.22157 0.22505 0.00100  0.00942  -0.01147 237 LYS A CB  
1824 C CG  . LYS A 237 ? 0.21297 0.21514 0.21570 0.00079  0.00874  -0.01159 237 LYS A CG  
1825 C CD  . LYS A 237 ? 0.21795 0.22044 0.22096 0.00081  0.00803  -0.01069 237 LYS A CD  
1826 C CE  . LYS A 237 ? 0.28454 0.28844 0.28643 0.00076  0.00756  -0.01079 237 LYS A CE  
1827 N NZ  . LYS A 237 ? 0.27219 0.27682 0.27325 0.00128  0.00748  -0.01075 237 LYS A NZ  
1828 N N   . PRO A 238 ? 0.26075 0.25992 0.26619 -0.00022 0.01057  -0.01350 238 PRO A N   
1829 C CA  . PRO A 238 ? 0.22595 0.22501 0.23090 -0.00094 0.01066  -0.01461 238 PRO A CA  
1830 C C   . PRO A 238 ? 0.32082 0.31910 0.32775 -0.00139 0.01058  -0.01442 238 PRO A C   
1831 O O   . PRO A 238 ? 0.25557 0.25389 0.26234 -0.00204 0.01049  -0.01518 238 PRO A O   
1832 C CB  . PRO A 238 ? 0.27028 0.26847 0.27448 -0.00096 0.01176  -0.01582 238 PRO A CB  
1833 C CG  . PRO A 238 ? 0.24041 0.23881 0.24397 -0.00026 0.01210  -0.01531 238 PRO A CG  
1834 C CD  . PRO A 238 ? 0.27189 0.27041 0.27732 0.00021  0.01157  -0.01388 238 PRO A CD  
1835 N N   . ASP A 239 ? 0.25498 0.25252 0.26384 -0.00113 0.01050  -0.01337 239 ASP A N   
1836 C CA  . ASP A 239 ? 0.23947 0.23613 0.25029 -0.00158 0.01034  -0.01296 239 ASP A CA  
1837 C C   . ASP A 239 ? 0.27055 0.26777 0.28099 -0.00186 0.00937  -0.01183 239 ASP A C   
1838 O O   . ASP A 239 ? 0.21299 0.20940 0.22487 -0.00223 0.00910  -0.01111 239 ASP A O   
1839 C CB  . ASP A 239 ? 0.31570 0.31102 0.32912 -0.00122 0.01073  -0.01238 239 ASP A CB  
1840 C CG  . ASP A 239 ? 0.32127 0.31591 0.33520 -0.00091 0.01202  -0.01353 239 ASP A CG  
1841 O OD1 . ASP A 239 ? 0.37050 0.36537 0.38266 -0.00118 0.01258  -0.01490 239 ASP A OD1 
1842 O OD2 . ASP A 239 ? 0.31541 0.30923 0.33153 -0.00043 0.01248  -0.01305 239 ASP A OD2 
1843 N N   . THR A 240 ? 0.33535 0.33384 0.34389 -0.00173 0.00893  -0.01164 240 THR A N   
1844 C CA  . THR A 240 ? 0.27878 0.27773 0.28672 -0.00198 0.00828  -0.01069 240 THR A CA  
1845 C C   . THR A 240 ? 0.30905 0.30868 0.31669 -0.00268 0.00828  -0.01120 240 THR A C   
1846 O O   . THR A 240 ? 0.31046 0.31056 0.31791 -0.00289 0.00853  -0.01233 240 THR A O   
1847 C CB  . THR A 240 ? 0.22754 0.22743 0.23395 -0.00146 0.00793  -0.01028 240 THR A CB  
1848 O OG1 . THR A 240 ? 0.22009 0.22109 0.22541 -0.00126 0.00813  -0.01122 240 THR A OG1 
1849 C CG2 . THR A 240 ? 0.24631 0.24545 0.25333 -0.00087 0.00777  -0.00954 240 THR A CG2 
1850 N N   . ASP A 241 ? 0.33446 0.33406 0.34200 -0.00309 0.00800  -0.01033 241 ASP A N   
1851 C CA  . ASP A 241 ? 0.26280 0.26298 0.27051 -0.00380 0.00811  -0.01062 241 ASP A CA  
1852 C C   . ASP A 241 ? 0.25163 0.25341 0.25812 -0.00370 0.00805  -0.01085 241 ASP A C   
1853 O O   . ASP A 241 ? 0.30669 0.30869 0.31218 -0.00348 0.00795  -0.01012 241 ASP A O   
1854 C CB  . ASP A 241 ? 0.24376 0.24300 0.25196 -0.00437 0.00802  -0.00950 241 ASP A CB  
1855 C CG  . ASP A 241 ? 0.27873 0.27826 0.28776 -0.00518 0.00830  -0.00978 241 ASP A CG  
1856 O OD1 . ASP A 241 ? 0.27275 0.27359 0.28166 -0.00531 0.00844  -0.01064 241 ASP A OD1 
1857 O OD2 . ASP A 241 ? 0.30259 0.30103 0.31258 -0.00573 0.00831  -0.00906 241 ASP A OD2 
1858 N N   . PRO A 242 ? 0.28711 0.28994 0.29374 -0.00389 0.00805  -0.01185 242 PRO A N   
1859 C CA  . PRO A 242 ? 0.21879 0.22321 0.22489 -0.00383 0.00792  -0.01196 242 PRO A CA  
1860 C C   . PRO A 242 ? 0.27963 0.28451 0.28645 -0.00445 0.00821  -0.01158 242 PRO A C   
1861 O O   . PRO A 242 ? 0.21045 0.21650 0.21710 -0.00436 0.00830  -0.01148 242 PRO A O   
1862 C CB  . PRO A 242 ? 0.23078 0.23597 0.23690 -0.00388 0.00760  -0.01308 242 PRO A CB  
1863 C CG  . PRO A 242 ? 0.24265 0.24671 0.24961 -0.00439 0.00777  -0.01368 242 PRO A CG  
1864 C CD  . PRO A 242 ? 0.26940 0.27194 0.27665 -0.00416 0.00810  -0.01297 242 PRO A CD  
1865 N N   . SER A 243 ? 0.21954 0.22349 0.22731 -0.00510 0.00844  -0.01135 243 SER A N   
1866 C CA  . SER A 243 ? 0.24308 0.24729 0.25155 -0.00578 0.00889  -0.01088 243 SER A CA  
1867 C C   . SER A 243 ? 0.27803 0.28114 0.28543 -0.00589 0.00920  -0.00966 243 SER A C   
1868 O O   . SER A 243 ? 0.31135 0.31371 0.31921 -0.00658 0.00954  -0.00904 243 SER A O   
1869 C CB  . SER A 243 ? 0.29257 0.29642 0.30277 -0.00653 0.00893  -0.01131 243 SER A CB  
1870 O OG  . SER A 243 ? 0.28192 0.28412 0.29245 -0.00661 0.00887  -0.01102 243 SER A OG  
1871 N N   . ALA A 244 ? 0.21506 0.21793 0.22090 -0.00527 0.00901  -0.00925 244 ALA A N   
1872 C CA  . ALA A 244 ? 0.26462 0.26628 0.26898 -0.00542 0.00908  -0.00812 244 ALA A CA  
1873 C C   . ALA A 244 ? 0.30132 0.30375 0.30428 -0.00518 0.00949  -0.00808 244 ALA A C   
1874 O O   . ALA A 244 ? 0.29603 0.29916 0.29856 -0.00446 0.00922  -0.00848 244 ALA A O   
1875 C CB  . ALA A 244 ? 0.25260 0.25298 0.25656 -0.00496 0.00838  -0.00764 244 ALA A CB  
1876 N N   . TRP A 245 ? 0.29350 0.29574 0.29580 -0.00580 0.01024  -0.00761 245 TRP A N   
1877 C CA  . TRP A 245 ? 0.26250 0.26532 0.26359 -0.00567 0.01093  -0.00768 245 TRP A CA  
1878 C C   . TRP A 245 ? 0.25401 0.25521 0.25253 -0.00611 0.01124  -0.00675 245 TRP A C   
1879 O O   . TRP A 245 ? 0.25579 0.25694 0.25271 -0.00580 0.01147  -0.00684 245 TRP A O   
1880 C CB  . TRP A 245 ? 0.30530 0.30962 0.30805 -0.00602 0.01189  -0.00821 245 TRP A CB  
1881 C CG  . TRP A 245 ? 0.25215 0.25594 0.25561 -0.00697 0.01249  -0.00775 245 TRP A CG  
1882 C CD1 . TRP A 245 ? 0.32555 0.32943 0.33095 -0.00735 0.01215  -0.00791 245 TRP A CD1 
1883 C CD2 . TRP A 245 ? 0.29317 0.29611 0.29534 -0.00772 0.01362  -0.00704 245 TRP A CD2 
1884 N NE1 . TRP A 245 ? 0.32936 0.33261 0.33505 -0.00826 0.01292  -0.00727 245 TRP A NE1 
1885 C CE2 . TRP A 245 ? 0.31005 0.31271 0.31367 -0.00852 0.01387  -0.00668 245 TRP A CE2 
1886 C CE3 . TRP A 245 ? 0.31355 0.31582 0.31332 -0.00786 0.01450  -0.00671 245 TRP A CE3 
1887 C CZ2 . TRP A 245 ? 0.34222 0.34400 0.34499 -0.00944 0.01500  -0.00588 245 TRP A CZ2 
1888 C CZ3 . TRP A 245 ? 0.28293 0.28424 0.28156 -0.00880 0.01569  -0.00602 245 TRP A CZ3 
1889 C CH2 . TRP A 245 ? 0.36921 0.37032 0.36935 -0.00958 0.01593  -0.00555 245 TRP A CH2 
1890 N N   . GLU A 246 ? 0.35630 0.35607 0.35427 -0.00689 0.01119  -0.00585 246 GLU A N   
1891 C CA  . GLU A 246 ? 0.30116 0.29910 0.29623 -0.00743 0.01119  -0.00483 246 GLU A CA  
1892 C C   . GLU A 246 ? 0.22769 0.22471 0.22143 -0.00685 0.00997  -0.00454 246 GLU A C   
1893 O O   . GLU A 246 ? 0.19378 0.19005 0.18504 -0.00687 0.01001  -0.00436 246 GLU A O   
1894 C CB  . GLU A 246 ? 0.28605 0.28258 0.28106 -0.00837 0.01108  -0.00375 246 GLU A CB  
1895 C CG  . GLU A 246 ? 0.33139 0.32838 0.32698 -0.00917 0.01247  -0.00373 246 GLU A CG  
1896 C CD  . GLU A 246 ? 0.33432 0.33003 0.33043 -0.01004 0.01225  -0.00264 246 GLU A CD  
1897 O OE1 . GLU A 246 ? 0.40987 0.40566 0.40832 -0.00984 0.01142  -0.00272 246 GLU A OE1 
1898 O OE2 . GLU A 246 ? 0.42912 0.42364 0.42324 -0.01096 0.01297  -0.00171 246 GLU A OE2 
1899 N N   . LYS A 247 ? 0.21077 0.20778 0.20622 -0.00638 0.00894  -0.00453 247 LYS A N   
1900 C CA  . LYS A 247 ? 0.26978 0.26624 0.26482 -0.00571 0.00784  -0.00435 247 LYS A CA  
1901 C C   . LYS A 247 ? 0.24247 0.24037 0.23983 -0.00486 0.00771  -0.00531 247 LYS A C   
1902 O O   . LYS A 247 ? 0.23213 0.22990 0.23137 -0.00482 0.00738  -0.00534 247 LYS A O   
1903 C CB  . LYS A 247 ? 0.21256 0.20714 0.20738 -0.00610 0.00670  -0.00309 247 LYS A CB  
1904 C CG  . LYS A 247 ? 0.26668 0.26070 0.26154 -0.00545 0.00552  -0.00281 247 LYS A CG  
1905 C CD  . LYS A 247 ? 0.25346 0.24587 0.24930 -0.00574 0.00430  -0.00158 247 LYS A CD  
1906 C CE  . LYS A 247 ? 0.25154 0.24207 0.24478 -0.00673 0.00367  -0.00022 247 LYS A CE  
1907 N NZ  . LYS A 247 ? 0.25057 0.24072 0.24365 -0.00763 0.00435  0.00022  247 LYS A NZ  
1908 N N   . PRO A 248 ? 0.24195 0.24114 0.23919 -0.00421 0.00799  -0.00612 248 PRO A N   
1909 C CA  . PRO A 248 ? 0.22530 0.22575 0.22430 -0.00348 0.00782  -0.00695 248 PRO A CA  
1910 C C   . PRO A 248 ? 0.19293 0.19248 0.19266 -0.00308 0.00699  -0.00660 248 PRO A C   
1911 O O   . PRO A 248 ? 0.19688 0.19555 0.19573 -0.00284 0.00637  -0.00600 248 PRO A O   
1912 C CB  . PRO A 248 ? 0.20679 0.20836 0.20513 -0.00290 0.00807  -0.00749 248 PRO A CB  
1913 C CG  . PRO A 248 ? 0.26731 0.26866 0.26419 -0.00342 0.00881  -0.00731 248 PRO A CG  
1914 C CD  . PRO A 248 ? 0.25573 0.25520 0.25122 -0.00414 0.00852  -0.00631 248 PRO A CD  
1915 N N   . ALA A 249 ? 0.21475 0.21446 0.21624 -0.00305 0.00703  -0.00701 249 ALA A N   
1916 C CA  . ALA A 249 ? 0.24049 0.23938 0.24328 -0.00269 0.00657  -0.00683 249 ALA A CA  
1917 C C   . ALA A 249 ? 0.18623 0.18558 0.18896 -0.00184 0.00636  -0.00710 249 ALA A C   
1918 O O   . ALA A 249 ? 0.18729 0.18613 0.19134 -0.00149 0.00624  -0.00711 249 ALA A O   
1919 C CB  . ALA A 249 ? 0.24177 0.24078 0.24630 -0.00288 0.00695  -0.00754 249 ALA A CB  
1920 N N   . THR A 250 ? 0.18827 0.18851 0.18975 -0.00150 0.00641  -0.00730 250 THR A N   
1921 C CA  . THR A 250 ? 0.19149 0.19207 0.19292 -0.00073 0.00616  -0.00738 250 THR A CA  
1922 C C   . THR A 250 ? 0.17093 0.17117 0.17087 -0.00066 0.00578  -0.00685 250 THR A C   
1923 O O   . THR A 250 ? 0.19544 0.19518 0.19413 -0.00123 0.00583  -0.00652 250 THR A O   
1924 C CB  . THR A 250 ? 0.18404 0.18613 0.18565 -0.00033 0.00658  -0.00832 250 THR A CB  
1925 O OG1 . THR A 250 ? 0.21007 0.21319 0.21122 -0.00068 0.00692  -0.00873 250 THR A OG1 
1926 C CG2 . THR A 250 ? 0.20387 0.20590 0.20660 -0.00033 0.00687  -0.00890 250 THR A CG2 
1927 N N   . THR A 251 ? 0.23218 0.23260 0.23215 -0.00001 0.00547  -0.00680 251 THR A N   
1928 C CA  . THR A 251 ? 0.22017 0.21997 0.21882 0.00004  0.00497  -0.00633 251 THR A CA  
1929 C C   . THR A 251 ? 0.25737 0.25804 0.25475 -0.00000 0.00552  -0.00685 251 THR A C   
1930 O O   . THR A 251 ? 0.19851 0.19837 0.19428 -0.00029 0.00539  -0.00660 251 THR A O   
1931 C CB  . THR A 251 ? 0.24739 0.24709 0.24683 0.00074  0.00447  -0.00609 251 THR A CB  
1932 O OG1 . THR A 251 ? 0.19247 0.19361 0.19242 0.00133  0.00497  -0.00676 251 THR A OG1 
1933 C CG2 . THR A 251 ? 0.18679 0.18561 0.18797 0.00081  0.00408  -0.00557 251 THR A CG2 
1934 N N   . VAL A 252 ? 0.24441 0.24661 0.24251 0.00023  0.00612  -0.00757 252 VAL A N   
1935 C CA  . VAL A 252 ? 0.20598 0.20923 0.20367 0.00030  0.00667  -0.00807 252 VAL A CA  
1936 C C   . VAL A 252 ? 0.24256 0.24559 0.23962 0.00079  0.00640  -0.00797 252 VAL A C   
1937 O O   . VAL A 252 ? 0.22583 0.22853 0.22175 0.00059  0.00675  -0.00810 252 VAL A O   
1938 C CB  . VAL A 252 ? 0.25853 0.26147 0.25532 -0.00046 0.00731  -0.00810 252 VAL A CB  
1939 C CG1 . VAL A 252 ? 0.21300 0.21741 0.21040 -0.00037 0.00811  -0.00875 252 VAL A CG1 
1940 C CG2 . VAL A 252 ? 0.26239 0.26497 0.25974 -0.00104 0.00736  -0.00792 252 VAL A CG2 
1941 N N   . LEU A 253 ? 0.18927 0.19236 0.18707 0.00140  0.00586  -0.00778 253 LEU A N   
1942 C CA  . LEU A 253 ? 0.21606 0.21898 0.21365 0.00191  0.00553  -0.00768 253 LEU A CA  
1943 C C   . LEU A 253 ? 0.21585 0.22031 0.21452 0.00256  0.00574  -0.00805 253 LEU A C   
1944 O O   . LEU A 253 ? 0.24500 0.24944 0.24385 0.00305  0.00547  -0.00794 253 LEU A O   
1945 C CB  . LEU A 253 ? 0.22930 0.23109 0.22723 0.00211  0.00471  -0.00702 253 LEU A CB  
1946 C CG  . LEU A 253 ? 0.17020 0.17026 0.16713 0.00148  0.00411  -0.00641 253 LEU A CG  
1947 C CD1 . LEU A 253 ? 0.21935 0.21855 0.21747 0.00174  0.00324  -0.00571 253 LEU A CD1 
1948 C CD2 . LEU A 253 ? 0.21282 0.21198 0.20769 0.00109  0.00404  -0.00649 253 LEU A CD2 
1949 N N   . SER A 254 ? 0.33356 0.33927 0.33298 0.00252  0.00609  -0.00842 254 SER A N   
1950 C CA  . SER A 254 ? 0.36326 0.37038 0.36364 0.00304  0.00607  -0.00862 254 SER A CA  
1951 C C   . SER A 254 ? 0.36943 0.37712 0.37013 0.00328  0.00633  -0.00884 254 SER A C   
1952 O O   . SER A 254 ? 0.42314 0.43140 0.42458 0.00387  0.00606  -0.00870 254 SER A O   
1953 C CB  . SER A 254 ? 0.38040 0.38860 0.38135 0.00279  0.00619  -0.00897 254 SER A CB  
1954 O OG  . SER A 254 ? 0.41781 0.42603 0.41867 0.00216  0.00662  -0.00927 254 SER A OG  
1955 N N   . PRO A 255 ? 0.24089 0.24842 0.24119 0.00287  0.00694  -0.00917 255 PRO A N   
1956 C CA  . PRO A 255 ? 0.31717 0.32510 0.31799 0.00316  0.00739  -0.00949 255 PRO A CA  
1957 C C   . PRO A 255 ? 0.30307 0.30983 0.30309 0.00348  0.00708  -0.00933 255 PRO A C   
1958 O O   . PRO A 255 ? 0.23029 0.23757 0.23133 0.00402  0.00711  -0.00946 255 PRO A O   
1959 C CB  . PRO A 255 ? 0.22207 0.22978 0.22235 0.00251  0.00835  -0.00990 255 PRO A CB  
1960 C CG  . PRO A 255 ? 0.29777 0.30560 0.29796 0.00198  0.00828  -0.00978 255 PRO A CG  
1961 C CD  . PRO A 255 ? 0.27272 0.27975 0.27227 0.00211  0.00742  -0.00930 255 PRO A CD  
1962 N N   . TYR A 256 ? 0.26678 0.27196 0.26521 0.00315  0.00669  -0.00902 256 TYR A N   
1963 C CA  . TYR A 256 ? 0.24284 0.24679 0.24055 0.00337  0.00620  -0.00886 256 TYR A CA  
1964 C C   . TYR A 256 ? 0.28690 0.29131 0.28598 0.00406  0.00548  -0.00840 256 TYR A C   
1965 O O   . TYR A 256 ? 0.25037 0.25437 0.24972 0.00444  0.00517  -0.00836 256 TYR A O   
1966 C CB  . TYR A 256 ? 0.33667 0.33877 0.33241 0.00272  0.00574  -0.00853 256 TYR A CB  
1967 C CG  . TYR A 256 ? 0.36992 0.37142 0.36402 0.00192  0.00649  -0.00881 256 TYR A CG  
1968 C CD1 . TYR A 256 ? 0.33541 0.33614 0.32801 0.00161  0.00721  -0.00937 256 TYR A CD1 
1969 C CD2 . TYR A 256 ? 0.34102 0.34263 0.33506 0.00144  0.00659  -0.00855 256 TYR A CD2 
1970 C CE1 . TYR A 256 ? 0.29421 0.29431 0.28516 0.00083  0.00809  -0.00959 256 TYR A CE1 
1971 C CE2 . TYR A 256 ? 0.35284 0.35389 0.34546 0.00067  0.00733  -0.00870 256 TYR A CE2 
1972 C CZ  . TYR A 256 ? 0.32033 0.32063 0.31134 0.00036  0.00812  -0.00919 256 TYR A CZ  
1973 O OH  . TYR A 256 ? 0.35181 0.35147 0.34126 -0.00046 0.00904  -0.00930 256 TYR A OH  
1974 N N   . LEU A 257 ? 0.29526 0.30042 0.29515 0.00419  0.00529  -0.00808 257 LEU A N   
1975 C CA  . LEU A 257 ? 0.25644 0.26206 0.25749 0.00480  0.00486  -0.00763 257 LEU A CA  
1976 C C   . LEU A 257 ? 0.23180 0.23892 0.23406 0.00528  0.00502  -0.00774 257 LEU A C   
1977 O O   . LEU A 257 ? 0.19631 0.20363 0.19944 0.00582  0.00470  -0.00736 257 LEU A O   
1978 C CB  . LEU A 257 ? 0.28387 0.28948 0.28508 0.00468  0.00478  -0.00733 257 LEU A CB  
1979 C CG  . LEU A 257 ? 0.20650 0.21065 0.20727 0.00433  0.00444  -0.00697 257 LEU A CG  
1980 C CD1 . LEU A 257 ? 0.17601 0.18027 0.17723 0.00420  0.00465  -0.00688 257 LEU A CD1 
1981 C CD2 . LEU A 257 ? 0.23014 0.23341 0.23146 0.00467  0.00382  -0.00645 257 LEU A CD2 
1982 N N   . LYS A 258 ? 0.24360 0.25173 0.24614 0.00507  0.00545  -0.00817 258 LYS A N   
1983 C CA  . LYS A 258 ? 0.24287 0.25251 0.24691 0.00548  0.00542  -0.00817 258 LYS A CA  
1984 C C   . LYS A 258 ? 0.27389 0.28340 0.27878 0.00591  0.00554  -0.00830 258 LYS A C   
1985 O O   . LYS A 258 ? 0.30987 0.31986 0.31588 0.00645  0.00513  -0.00787 258 LYS A O   
1986 C CB  . LYS A 258 ? 0.24049 0.25122 0.24505 0.00510  0.00576  -0.00858 258 LYS A CB  
1987 C CG  . LYS A 258 ? 0.22227 0.23457 0.22876 0.00544  0.00558  -0.00852 258 LYS A CG  
1988 C CD  . LYS A 258 ? 0.23767 0.25036 0.24534 0.00536  0.00632  -0.00906 258 LYS A CD  
1989 C CE  . LYS A 258 ? 0.30430 0.31803 0.31429 0.00595  0.00616  -0.00890 258 LYS A CE  
1990 N NZ  . LYS A 258 ? 0.27603 0.29138 0.28809 0.00583  0.00603  -0.00891 258 LYS A NZ  
1991 N N   . PHE A 259 ? 0.26901 0.27781 0.27330 0.00561  0.00616  -0.00888 259 PHE A N   
1992 C CA  . PHE A 259 ? 0.26098 0.26943 0.26594 0.00594  0.00647  -0.00923 259 PHE A CA  
1993 C C   . PHE A 259 ? 0.27303 0.28013 0.27733 0.00617  0.00591  -0.00897 259 PHE A C   
1994 O O   . PHE A 259 ? 0.19341 0.20030 0.19863 0.00657  0.00596  -0.00916 259 PHE A O   
1995 C CB  . PHE A 259 ? 0.34606 0.35391 0.35017 0.00545  0.00752  -0.01005 259 PHE A CB  
1996 C CG  . PHE A 259 ? 0.29938 0.30870 0.30503 0.00533  0.00822  -0.01036 259 PHE A CG  
1997 C CD1 . PHE A 259 ? 0.27376 0.28434 0.28204 0.00585  0.00847  -0.01048 259 PHE A CD1 
1998 C CD2 . PHE A 259 ? 0.27321 0.28266 0.27802 0.00470  0.00859  -0.01047 259 PHE A CD2 
1999 C CE1 . PHE A 259 ? 0.32564 0.33763 0.33581 0.00573  0.00900  -0.01069 259 PHE A CE1 
2000 C CE2 . PHE A 259 ? 0.21020 0.22103 0.21676 0.00455  0.00918  -0.01072 259 PHE A CE2 
2001 C CZ  . PHE A 259 ? 0.30369 0.31582 0.31300 0.00507  0.00936  -0.01083 259 PHE A CZ  
2002 N N   . GLY A 260 ? 0.29301 0.29918 0.29604 0.00592  0.00536  -0.00855 260 GLY A N   
2003 C CA  . GLY A 260 ? 0.26663 0.27149 0.26930 0.00605  0.00470  -0.00824 260 GLY A CA  
2004 C C   . GLY A 260 ? 0.27629 0.27930 0.27689 0.00545  0.00461  -0.00860 260 GLY A C   
2005 O O   . GLY A 260 ? 0.19917 0.20098 0.19952 0.00549  0.00390  -0.00841 260 GLY A O   
2006 N N   . CYS A 261 ? 0.32400 0.32670 0.32308 0.00483  0.00524  -0.00907 261 CYS A N   
2007 C CA  . CYS A 261 ? 0.25357 0.25434 0.25016 0.00411  0.00508  -0.00929 261 CYS A CA  
2008 C C   . CYS A 261 ? 0.28872 0.28845 0.28470 0.00382  0.00395  -0.00849 261 CYS A C   
2009 O O   . CYS A 261 ? 0.31179 0.30974 0.30603 0.00332  0.00327  -0.00842 261 CYS A O   
2010 C CB  . CYS A 261 ? 0.32819 0.32891 0.32333 0.00346  0.00611  -0.00980 261 CYS A CB  
2011 S SG  . CYS A 261 ? 0.27380 0.27573 0.27018 0.00374  0.00764  -0.01076 261 CYS A SG  
2012 N N   . LEU A 262 ? 0.33351 0.33421 0.33091 0.00409  0.00372  -0.00789 262 LEU A N   
2013 C CA  . LEU A 262 ? 0.26597 0.26586 0.26357 0.00394  0.00281  -0.00712 262 LEU A CA  
2014 C C   . LEU A 262 ? 0.27430 0.27499 0.27412 0.00467  0.00250  -0.00661 262 LEU A C   
2015 O O   . LEU A 262 ? 0.32758 0.32974 0.32854 0.00515  0.00306  -0.00671 262 LEU A O   
2016 C CB  . LEU A 262 ? 0.28782 0.28790 0.28507 0.00349  0.00306  -0.00693 262 LEU A CB  
2017 C CG  . LEU A 262 ? 0.26428 0.26346 0.26207 0.00329  0.00224  -0.00613 262 LEU A CG  
2018 C CD1 . LEU A 262 ? 0.24217 0.23941 0.23852 0.00271  0.00118  -0.00577 262 LEU A CD1 
2019 C CD2 . LEU A 262 ? 0.23320 0.23276 0.23105 0.00294  0.00269  -0.00608 262 LEU A CD2 
2020 N N   . SER A 263 ? 0.21452 0.21417 0.21497 0.00471  0.00157  -0.00602 263 SER A N   
2021 C CA  . SER A 263 ? 0.26525 0.26551 0.26795 0.00534  0.00141  -0.00542 263 SER A CA  
2022 C C   . SER A 263 ? 0.30333 0.30389 0.30695 0.00531  0.00163  -0.00496 263 SER A C   
2023 O O   . SER A 263 ? 0.19908 0.19863 0.20240 0.00483  0.00115  -0.00467 263 SER A O   
2024 C CB  . SER A 263 ? 0.20754 0.20671 0.21114 0.00545  0.00042  -0.00497 263 SER A CB  
2025 O OG  . SER A 263 ? 0.29807 0.29746 0.30386 0.00580  0.00027  -0.00420 263 SER A OG  
2026 N N   . ALA A 264 ? 0.24885 0.25064 0.25352 0.00579  0.00232  -0.00489 264 ALA A N   
2027 C CA  . ALA A 264 ? 0.26426 0.26621 0.26981 0.00579  0.00275  -0.00460 264 ALA A CA  
2028 C C   . ALA A 264 ? 0.25581 0.25687 0.26325 0.00593  0.00226  -0.00384 264 ALA A C   
2029 O O   . ALA A 264 ? 0.27581 0.27641 0.28412 0.00575  0.00238  -0.00358 264 ALA A O   
2030 C CB  . ALA A 264 ? 0.29404 0.29733 0.29978 0.00617  0.00360  -0.00474 264 ALA A CB  
2031 N N   . ARG A 265 ? 0.21215 0.21296 0.22058 0.00626  0.00173  -0.00347 265 ARG A N   
2032 C CA  . ARG A 265 ? 0.29126 0.29125 0.30191 0.00637  0.00115  -0.00269 265 ARG A CA  
2033 C C   . ARG A 265 ? 0.32808 0.32668 0.33859 0.00578  0.00004  -0.00243 265 ARG A C   
2034 O O   . ARG A 265 ? 0.31385 0.31188 0.32638 0.00573  -0.00025 -0.00179 265 ARG A O   
2035 C CB  . ARG A 265 ? 0.27000 0.26993 0.28169 0.00676  0.00067  -0.00240 265 ARG A CB  
2036 C CG  . ARG A 265 ? 0.25744 0.25864 0.26930 0.00732  0.00157  -0.00246 265 ARG A CG  
2037 C CD  . ARG A 265 ? 0.28433 0.28583 0.29838 0.00773  0.00225  -0.00174 265 ARG A CD  
2038 N NE  . ARG A 265 ? 0.36252 0.36503 0.37659 0.00819  0.00290  -0.00159 265 ARG A NE  
2039 C CZ  . ARG A 265 ? 0.32932 0.33183 0.34450 0.00852  0.00247  -0.00122 265 ARG A CZ  
2040 N NH1 . ARG A 265 ? 0.39403 0.39556 0.41027 0.00843  0.00139  -0.00107 265 ARG A NH1 
2041 N NH2 . ARG A 265 ? 0.32046 0.32388 0.33565 0.00890  0.00306  -0.00094 265 ARG A NH2 
2042 N N   . LEU A 266 ? 0.23141 0.22939 0.23958 0.00529  -0.00058 -0.00286 266 LEU A N   
2043 C CA  . LEU A 266 ? 0.31327 0.30978 0.32073 0.00459  -0.00174 -0.00253 266 LEU A CA  
2044 C C   . LEU A 266 ? 0.29203 0.28861 0.29930 0.00426  -0.00125 -0.00249 266 LEU A C   
2045 O O   . LEU A 266 ? 0.30375 0.29934 0.31204 0.00389  -0.00208 -0.00182 266 LEU A O   
2046 C CB  . LEU A 266 ? 0.34557 0.34122 0.35014 0.00408  -0.00234 -0.00306 266 LEU A CB  
2047 C CG  . LEU A 266 ? 0.38009 0.37390 0.38330 0.00322  -0.00379 -0.00262 266 LEU A CG  
2048 C CD1 . LEU A 266 ? 0.40356 0.39641 0.40908 0.00323  -0.00527 -0.00171 266 LEU A CD1 
2049 C CD2 . LEU A 266 ? 0.32282 0.31573 0.32264 0.00268  -0.00398 -0.00334 266 LEU A CD2 
2050 N N   . PHE A 267 ? 0.26415 0.26187 0.27034 0.00437  -0.00001 -0.00318 267 PHE A N   
2051 C CA  . PHE A 267 ? 0.30250 0.30034 0.30876 0.00409  0.00056  -0.00324 267 PHE A CA  
2052 C C   . PHE A 267 ? 0.26314 0.26101 0.27223 0.00442  0.00091  -0.00275 267 PHE A C   
2053 O O   . PHE A 267 ? 0.31957 0.31671 0.32973 0.00410  0.00065  -0.00235 267 PHE A O   
2054 C CB  . PHE A 267 ? 0.27658 0.27571 0.28142 0.00415  0.00173  -0.00410 267 PHE A CB  
2055 C CG  . PHE A 267 ? 0.29767 0.29677 0.30203 0.00369  0.00218  -0.00432 267 PHE A CG  
2056 C CD1 . PHE A 267 ? 0.33767 0.33557 0.34261 0.00322  0.00153  -0.00374 267 PHE A CD1 
2057 C CD2 . PHE A 267 ? 0.21883 0.21907 0.22234 0.00369  0.00314  -0.00505 267 PHE A CD2 
2058 C CE1 . PHE A 267 ? 0.33263 0.33045 0.33734 0.00279  0.00196  -0.00391 267 PHE A CE1 
2059 C CE2 . PHE A 267 ? 0.20138 0.20155 0.20461 0.00323  0.00352  -0.00529 267 PHE A CE2 
2060 C CZ  . PHE A 267 ? 0.21905 0.21801 0.22289 0.00279  0.00299  -0.00474 267 PHE A CZ  
2061 N N   . HIS A 268 ? 0.29562 0.29428 0.30608 0.00505  0.00158  -0.00274 268 HIS A N   
2062 C CA  . HIS A 268 ? 0.30735 0.30598 0.32051 0.00538  0.00224  -0.00235 268 HIS A CA  
2063 C C   . HIS A 268 ? 0.30736 0.30484 0.32306 0.00528  0.00108  -0.00139 268 HIS A C   
2064 O O   . HIS A 268 ? 0.24440 0.24147 0.26249 0.00528  0.00136  -0.00101 268 HIS A O   
2065 C CB  . HIS A 268 ? 0.20600 0.20560 0.21971 0.00599  0.00325  -0.00246 268 HIS A CB  
2066 C CG  . HIS A 268 ? 0.28629 0.28586 0.30247 0.00630  0.00433  -0.00219 268 HIS A CG  
2067 N ND1 . HIS A 268 ? 0.30240 0.30220 0.31832 0.00624  0.00564  -0.00276 268 HIS A ND1 
2068 C CD2 . HIS A 268 ? 0.35902 0.35828 0.37808 0.00665  0.00442  -0.00147 268 HIS A CD2 
2069 C CE1 . HIS A 268 ? 0.35195 0.35151 0.37030 0.00654  0.00664  -0.00246 268 HIS A CE1 
2070 N NE2 . HIS A 268 ? 0.33807 0.33737 0.35853 0.00681  0.00595  -0.00163 268 HIS A NE2 
2071 N N   . ALA A 269 ? 0.33822 0.33510 0.35358 0.00516  -0.00028 -0.00100 269 ALA A N   
2072 C CA  . ALA A 269 ? 0.28734 0.28305 0.30508 0.00496  -0.00173 -0.00002 269 ALA A CA  
2073 C C   . ALA A 269 ? 0.29008 0.28467 0.30737 0.00426  -0.00278 0.00037  269 ALA A C   
2074 O O   . ALA A 269 ? 0.32676 0.32057 0.34690 0.00413  -0.00361 0.00126  269 ALA A O   
2075 C CB  . ALA A 269 ? 0.29209 0.28731 0.30926 0.00492  -0.00301 0.00017  269 ALA A CB  
2076 N N   . ARG A 270 ? 0.33730 0.33181 0.35127 0.00378  -0.00275 -0.00020 270 ARG A N   
2077 C CA  . ARG A 270 ? 0.32060 0.31403 0.33391 0.00305  -0.00363 0.00025  270 ARG A CA  
2078 C C   . ARG A 270 ? 0.28026 0.27403 0.29556 0.00317  -0.00256 0.00024  270 ARG A C   
2079 O O   . ARG A 270 ? 0.35523 0.34803 0.37183 0.00273  -0.00340 0.00099  270 ARG A O   
2080 C CB  . ARG A 270 ? 0.32452 0.31771 0.33369 0.00247  -0.00371 -0.00035 270 ARG A CB  
2081 C CG  . ARG A 270 ? 0.39702 0.38936 0.40395 0.00215  -0.00490 -0.00036 270 ARG A CG  
2082 C CD  . ARG A 270 ? 0.32946 0.32003 0.33693 0.00152  -0.00702 0.00075  270 ARG A CD  
2083 N NE  . ARG A 270 ? 0.30531 0.29488 0.31163 0.00073  -0.00763 0.00129  270 ARG A NE  
2084 C CZ  . ARG A 270 ? 0.33018 0.31878 0.33263 -0.00008 -0.00802 0.00112  270 ARG A CZ  
2085 N NH1 . ARG A 270 ? 0.24655 0.23502 0.24592 -0.00020 -0.00777 0.00029  270 ARG A NH1 
2086 N NH2 . ARG A 270 ? 0.25751 0.24518 0.25924 -0.00080 -0.00857 0.00180  270 ARG A NH2 
2087 N N   . LEU A 271 ? 0.27101 0.26604 0.28655 0.00370  -0.00076 -0.00058 271 LEU A N   
2088 C CA  . LEU A 271 ? 0.27646 0.27168 0.29373 0.00379  0.00041  -0.00080 271 LEU A CA  
2089 C C   . LEU A 271 ? 0.28787 0.28262 0.30942 0.00412  0.00041  -0.00004 271 LEU A C   
2090 O O   . LEU A 271 ? 0.23906 0.23325 0.26275 0.00396  0.00056  0.00024  271 LEU A O   
2091 C CB  . LEU A 271 ? 0.25395 0.25047 0.26992 0.00416  0.00221  -0.00193 271 LEU A CB  
2092 C CG  . LEU A 271 ? 0.35598 0.35311 0.36850 0.00383  0.00246  -0.00273 271 LEU A CG  
2093 C CD1 . LEU A 271 ? 0.31807 0.31646 0.32970 0.00421  0.00393  -0.00367 271 LEU A CD1 
2094 C CD2 . LEU A 271 ? 0.32823 0.32472 0.34026 0.00319  0.00225  -0.00271 271 LEU A CD2 
2095 N N   . LEU A 272 ? 0.29290 0.28789 0.31608 0.00459  0.00032  0.00030  272 LEU A N   
2096 C CA  . LEU A 272 ? 0.28057 0.27520 0.30827 0.00493  0.00049  0.00104  272 LEU A CA  
2097 C C   . LEU A 272 ? 0.22468 0.21803 0.25462 0.00447  -0.00155 0.00228  272 LEU A C   
2098 O O   . LEU A 272 ? 0.22000 0.21293 0.25403 0.00460  -0.00141 0.00290  272 LEU A O   
2099 C CB  . LEU A 272 ? 0.20905 0.20427 0.23796 0.00551  0.00091  0.00117  272 LEU A CB  
2100 C CG  . LEU A 272 ? 0.30777 0.30418 0.33476 0.00596  0.00285  0.00018  272 LEU A CG  
2101 C CD1 . LEU A 272 ? 0.30097 0.29780 0.32978 0.00650  0.00331  0.00057  272 LEU A CD1 
2102 C CD2 . LEU A 272 ? 0.32556 0.32217 0.35298 0.00604  0.00474  -0.00054 272 LEU A CD2 
2103 N N   . GLU A 273 ? 0.32192 0.31457 0.34929 0.00389  -0.00346 0.00267  273 GLU A N   
2104 C CA  . GLU A 273 ? 0.25526 0.24651 0.28410 0.00328  -0.00566 0.00392  273 GLU A CA  
2105 C C   . GLU A 273 ? 0.26103 0.25177 0.29066 0.00291  -0.00550 0.00415  273 GLU A C   
2106 O O   . GLU A 273 ? 0.29788 0.28775 0.33107 0.00272  -0.00660 0.00527  273 GLU A O   
2107 C CB  . GLU A 273 ? 0.27498 0.26539 0.29991 0.00260  -0.00752 0.00410  273 GLU A CB  
2108 C CG  . GLU A 273 ? 0.29442 0.28511 0.31879 0.00290  -0.00790 0.00390  273 GLU A CG  
2109 C CD  . GLU A 273 ? 0.43376 0.42343 0.45398 0.00218  -0.00952 0.00383  273 GLU A CD  
2110 O OE1 . GLU A 273 ? 0.50431 0.49301 0.52196 0.00141  -0.01034 0.00404  273 GLU A OE1 
2111 O OE2 . GLU A 273 ? 0.44369 0.43343 0.46315 0.00236  -0.00988 0.00355  273 GLU A OE2 
2112 N N   . VAL A 274 ? 0.22204 0.21331 0.24869 0.00280  -0.00419 0.00314  274 VAL A N   
2113 C CA  . VAL A 274 ? 0.26500 0.25581 0.29242 0.00246  -0.00389 0.00324  274 VAL A CA  
2114 C C   . VAL A 274 ? 0.29060 0.28187 0.32205 0.00307  -0.00208 0.00288  274 VAL A C   
2115 O O   . VAL A 274 ? 0.33880 0.32935 0.37333 0.00293  -0.00225 0.00347  274 VAL A O   
2116 C CB  . VAL A 274 ? 0.35406 0.34526 0.37706 0.00206  -0.00316 0.00228  274 VAL A CB  
2117 C CG1 . VAL A 274 ? 0.27955 0.27022 0.30342 0.00166  -0.00288 0.00241  274 VAL A CG1 
2118 C CG2 . VAL A 274 ? 0.31825 0.30886 0.33727 0.00144  -0.00466 0.00255  274 VAL A CG2 
2119 N N   . TYR A 275 ? 0.26243 0.25479 0.29394 0.00374  -0.00027 0.00192  275 TYR A N   
2120 C CA  . TYR A 275 ? 0.23704 0.22969 0.27182 0.00427  0.00174  0.00140  275 TYR A CA  
2121 C C   . TYR A 275 ? 0.30294 0.29501 0.34316 0.00457  0.00129  0.00251  275 TYR A C   
2122 O O   . TYR A 275 ? 0.25111 0.24285 0.29498 0.00477  0.00242  0.00247  275 TYR A O   
2123 C CB  . TYR A 275 ? 0.26985 0.26366 0.30277 0.00480  0.00370  0.00020  275 TYR A CB  
2124 C CG  . TYR A 275 ? 0.32477 0.31925 0.35318 0.00456  0.00443  -0.00098 275 TYR A CG  
2125 C CD1 . TYR A 275 ? 0.24884 0.24292 0.27554 0.00396  0.00379  -0.00109 275 TYR A CD1 
2126 C CD2 . TYR A 275 ? 0.22555 0.22107 0.25164 0.00490  0.00570  -0.00190 275 TYR A CD2 
2127 C CE1 . TYR A 275 ? 0.30553 0.30028 0.32858 0.00372  0.00444  -0.00213 275 TYR A CE1 
2128 C CE2 . TYR A 275 ? 0.30483 0.30100 0.32723 0.00466  0.00618  -0.00289 275 TYR A CE2 
2129 C CZ  . TYR A 275 ? 0.33172 0.32755 0.35275 0.00408  0.00558  -0.00303 275 TYR A CZ  
2130 O OH  . TYR A 275 ? 0.27253 0.26908 0.29034 0.00383  0.00605  -0.00398 275 TYR A OH  
2131 N N   . ARG A 276 ? 0.25292 0.24483 0.29403 0.00459  -0.00032 0.00349  276 ARG A N   
2132 C CA  . ARG A 276 ? 0.20910 0.20055 0.25581 0.00486  -0.00088 0.00463  276 ARG A CA  
2133 C C   . ARG A 276 ? 0.25542 0.24569 0.30511 0.00437  -0.00257 0.00584  276 ARG A C   
2134 O O   . ARG A 276 ? 0.20131 0.19125 0.25657 0.00465  -0.00238 0.00657  276 ARG A O   
2135 C CB  . ARG A 276 ? 0.21247 0.20399 0.25927 0.00492  -0.00238 0.00535  276 ARG A CB  
2136 C CG  . ARG A 276 ? 0.21223 0.20484 0.25859 0.00558  -0.00049 0.00455  276 ARG A CG  
2137 C CD  . ARG A 276 ? 0.22994 0.22258 0.27597 0.00558  -0.00208 0.00517  276 ARG A CD  
2138 N NE  . ARG A 276 ? 0.24594 0.23850 0.28661 0.00511  -0.00332 0.00476  276 ARG A NE  
2139 C CZ  . ARG A 276 ? 0.25699 0.24952 0.29618 0.00505  -0.00455 0.00494  276 ARG A CZ  
2140 N NH1 . ARG A 276 ? 0.25280 0.24540 0.29541 0.00539  -0.00489 0.00560  276 ARG A NH1 
2141 N NH2 . ARG A 276 ? 0.27514 0.26752 0.30949 0.00462  -0.00537 0.00441  276 ARG A NH2 
2142 N N   . ARG A 277 ? 0.28337 0.27299 0.32965 0.00363  -0.00416 0.00612  277 ARG A N   
2143 C CA  . ARG A 277 ? 0.25630 0.24471 0.30489 0.00307  -0.00584 0.00737  277 ARG A CA  
2144 C C   . ARG A 277 ? 0.31637 0.30472 0.36515 0.00302  -0.00428 0.00665  277 ARG A C   
2145 O O   . ARG A 277 ? 0.34513 0.33251 0.39669 0.00265  -0.00534 0.00768  277 ARG A O   
2146 C CB  . ARG A 277 ? 0.28614 0.27358 0.33084 0.00214  -0.00860 0.00829  277 ARG A CB  
2147 C CG  . ARG A 277 ? 0.29178 0.27878 0.33707 0.00198  -0.01077 0.00929  277 ARG A CG  
2148 C CD  . ARG A 277 ? 0.44461 0.43029 0.48587 0.00092  -0.01351 0.01020  277 ARG A CD  
2149 N NE  . ARG A 277 ? 0.34971 0.33571 0.38464 0.00063  -0.01273 0.00899  277 ARG A NE  
2150 C CZ  . ARG A 277 ? 0.35203 0.33837 0.38356 0.00068  -0.01278 0.00828  277 ARG A CZ  
2151 N NH1 . ARG A 277 ? 0.35639 0.34278 0.38991 0.00097  -0.01362 0.00863  277 ARG A NH1 
2152 N NH2 . ARG A 277 ? 0.34861 0.33525 0.37492 0.00044  -0.01193 0.00720  277 ARG A NH2 
2153 N N   . HIS A 278 ? 0.26623 0.25551 0.31222 0.00333  -0.00194 0.00498  278 HIS A N   
2154 C CA  . HIS A 278 ? 0.34261 0.33182 0.38876 0.00328  -0.00031 0.00407  278 HIS A CA  
2155 C C   . HIS A 278 ? 0.27797 0.26787 0.32615 0.00404  0.00253  0.00276  278 HIS A C   
2156 O O   . HIS A 278 ? 0.21745 0.20828 0.26215 0.00427  0.00402  0.00144  278 HIS A O   
2157 C CB  . HIS A 278 ? 0.32942 0.31893 0.36989 0.00277  -0.00026 0.00323  278 HIS A CB  
2158 C CG  . HIS A 278 ? 0.34451 0.33314 0.38264 0.00193  -0.00271 0.00444  278 HIS A CG  
2159 N ND1 . HIS A 278 ? 0.32329 0.31179 0.35885 0.00166  -0.00442 0.00506  278 HIS A ND1 
2160 C CD2 . HIS A 278 ? 0.30539 0.29308 0.34323 0.00123  -0.00370 0.00514  278 HIS A CD2 
2161 C CE1 . HIS A 278 ? 0.34477 0.33223 0.37823 0.00081  -0.00629 0.00605  278 HIS A CE1 
2162 N NE2 . HIS A 278 ? 0.31905 0.30602 0.35385 0.00053  -0.00591 0.00619  278 HIS A NE2 
2163 N N   . PRO A 279 ? 0.29887 0.28828 0.35260 0.00440  0.00340  0.00307  279 PRO A N   
2164 C CA  . PRO A 279 ? 0.29209 0.28200 0.34775 0.00510  0.00624  0.00187  279 PRO A CA  
2165 C C   . PRO A 279 ? 0.25626 0.24641 0.30895 0.00508  0.00854  0.00000  279 PRO A C   
2166 O O   . PRO A 279 ? 0.30873 0.29951 0.35979 0.00545  0.01057  -0.00120 279 PRO A O   
2167 C CB  . PRO A 279 ? 0.33611 0.32525 0.39886 0.00539  0.00643  0.00279  279 PRO A CB  
2168 C CG  . PRO A 279 ? 0.35275 0.34093 0.41663 0.00478  0.00430  0.00394  279 PRO A CG  
2169 C CD  . PRO A 279 ? 0.29443 0.28274 0.35305 0.00416  0.00189  0.00456  279 PRO A CD  
2170 N N   . ALA A 280 ? 0.23737 0.22695 0.28925 0.00459  0.00823  -0.00024 280 ALA A N   
2171 C CA  . ALA A 280 ? 0.33384 0.32352 0.38317 0.00447  0.01022  -0.00203 280 ALA A CA  
2172 C C   . ALA A 280 ? 0.28876 0.27931 0.33188 0.00412  0.00981  -0.00278 280 ALA A C   
2173 O O   . ALA A 280 ? 0.32273 0.31322 0.36352 0.00373  0.01038  -0.00379 280 ALA A O   
2174 C CB  . ALA A 280 ? 0.33900 0.32764 0.39086 0.00411  0.01015  -0.00197 280 ALA A CB  
2175 N N   . HIS A 281 ? 0.20588 0.19720 0.24656 0.00424  0.00884  -0.00231 281 HIS A N   
2176 C CA  . HIS A 281 ? 0.24460 0.23678 0.27993 0.00393  0.00841  -0.00292 281 HIS A CA  
2177 C C   . HIS A 281 ? 0.30188 0.29466 0.33470 0.00408  0.01054  -0.00465 281 HIS A C   
2178 O O   . HIS A 281 ? 0.31944 0.31205 0.35399 0.00448  0.01240  -0.00534 281 HIS A O   
2179 C CB  . HIS A 281 ? 0.30663 0.29940 0.34039 0.00408  0.00704  -0.00210 281 HIS A CB  
2180 C CG  . HIS A 281 ? 0.33113 0.32447 0.36576 0.00472  0.00827  -0.00236 281 HIS A CG  
2181 N ND1 . HIS A 281 ? 0.31605 0.31029 0.34746 0.00491  0.00957  -0.00346 281 HIS A ND1 
2182 C CD2 . HIS A 281 ? 0.27765 0.27075 0.31614 0.00517  0.00836  -0.00156 281 HIS A CD2 
2183 C CE1 . HIS A 281 ? 0.30297 0.29745 0.33596 0.00544  0.01049  -0.00331 281 HIS A CE1 
2184 N NE2 . HIS A 281 ? 0.35847 0.35231 0.39587 0.00562  0.00985  -0.00220 281 HIS A NE2 
2185 N N   . SER A 282 ? 0.33209 0.32550 0.36073 0.00369  0.01025  -0.00534 282 SER A N   
2186 C CA  . SER A 282 ? 0.26181 0.25575 0.28769 0.00367  0.01185  -0.00689 282 SER A CA  
2187 C C   . SER A 282 ? 0.27678 0.27149 0.30131 0.00415  0.01255  -0.00706 282 SER A C   
2188 O O   . SER A 282 ? 0.29004 0.28522 0.31444 0.00440  0.01145  -0.00610 282 SER A O   
2189 C CB  . SER A 282 ? 0.33974 0.33425 0.36201 0.00311  0.01111  -0.00739 282 SER A CB  
2190 O OG  . SER A 282 ? 0.28489 0.28004 0.30534 0.00306  0.00953  -0.00651 282 SER A OG  
2191 N N   . GLN A 283 ? 0.29791 0.29262 0.32131 0.00423  0.01440  -0.00829 283 GLN A N   
2192 C CA  . GLN A 283 ? 0.29700 0.29230 0.31886 0.00460  0.01532  -0.00850 283 GLN A CA  
2193 C C   . GLN A 283 ? 0.27418 0.27037 0.29148 0.00430  0.01514  -0.00929 283 GLN A C   
2194 O O   . GLN A 283 ? 0.28332 0.27954 0.29892 0.00380  0.01487  -0.01004 283 GLN A O   
2195 C CB  . GLN A 283 ? 0.26995 0.26443 0.29355 0.00484  0.01766  -0.00926 283 GLN A CB  
2196 C CG  . GLN A 283 ? 0.35105 0.34477 0.37986 0.00524  0.01800  -0.00839 283 GLN A CG  
2197 C CD  . GLN A 283 ? 0.29792 0.29219 0.32831 0.00569  0.01701  -0.00698 283 GLN A CD  
2198 O OE1 . GLN A 283 ? 0.31129 0.30524 0.34540 0.00585  0.01590  -0.00581 283 GLN A OE1 
2199 N NE2 . GLN A 283 ? 0.31959 0.31465 0.34727 0.00587  0.01729  -0.00703 283 GLN A NE2 
2200 N N   . PRO A 284 ? 0.27195 0.26892 0.28746 0.00458  0.01519  -0.00905 284 PRO A N   
2201 C CA  . PRO A 284 ? 0.30421 0.30203 0.31571 0.00431  0.01495  -0.00969 284 PRO A CA  
2202 C C   . PRO A 284 ? 0.20593 0.20321 0.21555 0.00388  0.01635  -0.01113 284 PRO A C   
2203 O O   . PRO A 284 ? 0.24556 0.24178 0.25669 0.00392  0.01799  -0.01169 284 PRO A O   
2204 C CB  . PRO A 284 ? 0.27930 0.27775 0.29012 0.00477  0.01505  -0.00903 284 PRO A CB  
2205 C CG  . PRO A 284 ? 0.27456 0.27279 0.28880 0.00522  0.01449  -0.00785 284 PRO A CG  
2206 C CD  . PRO A 284 ? 0.28196 0.27909 0.29931 0.00515  0.01516  -0.00801 284 PRO A CD  
2207 N N   . PRO A 285 ? 0.27732 0.27521 0.28372 0.00341  0.01578  -0.01180 285 PRO A N   
2208 C CA  . PRO A 285 ? 0.25029 0.24943 0.25503 0.00332  0.01409  -0.01131 285 PRO A CA  
2209 C C   . PRO A 285 ? 0.29152 0.29079 0.29709 0.00299  0.01296  -0.01122 285 PRO A C   
2210 O O   . PRO A 285 ? 0.34919 0.34938 0.35392 0.00294  0.01171  -0.01076 285 PRO A O   
2211 C CB  . PRO A 285 ? 0.24060 0.24014 0.24188 0.00291  0.01429  -0.01218 285 PRO A CB  
2212 C CG  . PRO A 285 ? 0.25029 0.24862 0.25127 0.00245  0.01562  -0.01347 285 PRO A CG  
2213 C CD  . PRO A 285 ? 0.22861 0.22587 0.23270 0.00289  0.01693  -0.01323 285 PRO A CD  
2214 N N   . VAL A 286 ? 0.29276 0.29102 0.30005 0.00273  0.01347  -0.01165 286 VAL A N   
2215 C CA  . VAL A 286 ? 0.26300 0.26126 0.27094 0.00232  0.01248  -0.01152 286 VAL A CA  
2216 C C   . VAL A 286 ? 0.31775 0.31601 0.32749 0.00256  0.01136  -0.01018 286 VAL A C   
2217 O O   . VAL A 286 ? 0.31935 0.31768 0.32904 0.00219  0.01043  -0.00987 286 VAL A O   
2218 C CB  . VAL A 286 ? 0.26866 0.26575 0.27805 0.00194  0.01334  -0.01234 286 VAL A CB  
2219 C CG1 . VAL A 286 ? 0.40964 0.40652 0.41680 0.00155  0.01436  -0.01384 286 VAL A CG1 
2220 C CG2 . VAL A 286 ? 0.22364 0.21965 0.23634 0.00235  0.01416  -0.01189 286 VAL A CG2 
2221 N N   . SER A 287 ? 0.33093 0.32901 0.34216 0.00311  0.01141  -0.00937 287 SER A N   
2222 C CA  . SER A 287 ? 0.34997 0.34784 0.36280 0.00326  0.01019  -0.00812 287 SER A CA  
2223 C C   . SER A 287 ? 0.31442 0.31326 0.32510 0.00325  0.00903  -0.00770 287 SER A C   
2224 O O   . SER A 287 ? 0.30918 0.30898 0.31767 0.00326  0.00919  -0.00824 287 SER A O   
2225 C CB  . SER A 287 ? 0.36349 0.36086 0.37895 0.00380  0.01054  -0.00740 287 SER A CB  
2226 O OG  . SER A 287 ? 0.38380 0.38185 0.39810 0.00422  0.01108  -0.00749 287 SER A OG  
2227 N N   . LEU A 288 ? 0.30720 0.30569 0.31857 0.00319  0.00783  -0.00672 288 LEU A N   
2228 C CA  . LEU A 288 ? 0.30584 0.30502 0.31535 0.00320  0.00688  -0.00639 288 LEU A CA  
2229 C C   . LEU A 288 ? 0.27027 0.27003 0.27965 0.00379  0.00702  -0.00620 288 LEU A C   
2230 O O   . LEU A 288 ? 0.30682 0.30750 0.31443 0.00389  0.00680  -0.00639 288 LEU A O   
2231 C CB  . LEU A 288 ? 0.27680 0.27515 0.28672 0.00290  0.00561  -0.00543 288 LEU A CB  
2232 C CG  . LEU A 288 ? 0.27121 0.26966 0.27912 0.00229  0.00511  -0.00554 288 LEU A CG  
2233 C CD1 . LEU A 288 ? 0.25567 0.25303 0.26355 0.00192  0.00385  -0.00452 288 LEU A CD1 
2234 C CD2 . LEU A 288 ? 0.24266 0.24235 0.24843 0.00241  0.00528  -0.00611 288 LEU A CD2 
2235 N N   . ARG A 289 ? 0.27969 0.27894 0.29125 0.00419  0.00741  -0.00578 289 ARG A N   
2236 C CA  . ARG A 289 ? 0.30025 0.30002 0.31189 0.00473  0.00775  -0.00558 289 ARG A CA  
2237 C C   . ARG A 289 ? 0.27805 0.27858 0.28790 0.00481  0.00888  -0.00642 289 ARG A C   
2238 O O   . ARG A 289 ? 0.25919 0.26049 0.26790 0.00509  0.00883  -0.00632 289 ARG A O   
2239 C CB  . ARG A 289 ? 0.27748 0.27650 0.29224 0.00510  0.00808  -0.00492 289 ARG A CB  
2240 C CG  . ARG A 289 ? 0.27372 0.27316 0.28899 0.00563  0.00832  -0.00448 289 ARG A CG  
2241 C CD  . ARG A 289 ? 0.30934 0.30809 0.32813 0.00596  0.00893  -0.00389 289 ARG A CD  
2242 N NE  . ARG A 289 ? 0.35836 0.35712 0.37737 0.00615  0.01088  -0.00449 289 ARG A NE  
2243 C CZ  . ARG A 289 ? 0.34490 0.34407 0.36366 0.00651  0.01179  -0.00437 289 ARG A CZ  
2244 N NH1 . ARG A 289 ? 0.33128 0.33095 0.34991 0.00678  0.01090  -0.00367 289 ARG A NH1 
2245 N NH2 . ARG A 289 ? 0.43073 0.42968 0.44929 0.00656  0.01370  -0.00498 289 ARG A NH2 
2246 N N   . GLY A 290 ? 0.28997 0.29021 0.29951 0.00450  0.00982  -0.00724 290 GLY A N   
2247 C CA  . GLY A 290 ? 0.27836 0.27914 0.28573 0.00440  0.01069  -0.00809 290 GLY A CA  
2248 C C   . GLY A 290 ? 0.26493 0.26681 0.26996 0.00419  0.00983  -0.00831 290 GLY A C   
2249 O O   . GLY A 290 ? 0.20537 0.20794 0.20874 0.00428  0.00999  -0.00848 290 GLY A O   
2250 N N   . GLN A 291 ? 0.30839 0.31039 0.31335 0.00388  0.00893  -0.00825 291 GLN A N   
2251 C CA  . GLN A 291 ? 0.24971 0.25278 0.25297 0.00369  0.00825  -0.00845 291 GLN A CA  
2252 C C   . GLN A 291 ? 0.24701 0.25076 0.25005 0.00417  0.00771  -0.00783 291 GLN A C   
2253 O O   . GLN A 291 ? 0.17053 0.17529 0.17237 0.00420  0.00747  -0.00799 291 GLN A O   
2254 C CB  . GLN A 291 ? 0.25692 0.25983 0.26031 0.00324  0.00765  -0.00845 291 GLN A CB  
2255 C CG  . GLN A 291 ? 0.25303 0.25530 0.25681 0.00272  0.00811  -0.00904 291 GLN A CG  
2256 C CD  . GLN A 291 ? 0.29257 0.29529 0.29507 0.00246  0.00866  -0.01001 291 GLN A CD  
2257 O OE1 . GLN A 291 ? 0.29082 0.29459 0.29199 0.00234  0.00827  -0.01026 291 GLN A OE1 
2258 N NE2 . GLN A 291 ? 0.34002 0.34187 0.34298 0.00233  0.00955  -0.01058 291 GLN A NE2 
2259 N N   . LEU A 292 ? 0.20669 0.20989 0.21110 0.00452  0.00741  -0.00709 292 LEU A N   
2260 C CA  . LEU A 292 ? 0.17835 0.18204 0.18280 0.00499  0.00700  -0.00654 292 LEU A CA  
2261 C C   . LEU A 292 ? 0.23007 0.23413 0.23424 0.00532  0.00771  -0.00649 292 LEU A C   
2262 O O   . LEU A 292 ? 0.20202 0.20684 0.20559 0.00560  0.00742  -0.00622 292 LEU A O   
2263 C CB  . LEU A 292 ? 0.25222 0.25507 0.25827 0.00521  0.00641  -0.00579 292 LEU A CB  
2264 C CG  . LEU A 292 ? 0.19168 0.19409 0.19737 0.00486  0.00548  -0.00565 292 LEU A CG  
2265 C CD1 . LEU A 292 ? 0.22245 0.22390 0.22953 0.00501  0.00469  -0.00487 292 LEU A CD1 
2266 C CD2 . LEU A 292 ? 0.16486 0.16816 0.16904 0.00483  0.00518  -0.00598 292 LEU A CD2 
2267 N N   . LEU A 293 ? 0.21331 0.21674 0.21787 0.00527  0.00873  -0.00672 293 LEU A N   
2268 C CA  . LEU A 293 ? 0.27870 0.28229 0.28245 0.00545  0.00961  -0.00673 293 LEU A CA  
2269 C C   . LEU A 293 ? 0.21513 0.21948 0.21638 0.00510  0.00952  -0.00731 293 LEU A C   
2270 O O   . LEU A 293 ? 0.31221 0.31698 0.31228 0.00523  0.00967  -0.00705 293 LEU A O   
2271 C CB  . LEU A 293 ? 0.27033 0.27289 0.27514 0.00544  0.01096  -0.00696 293 LEU A CB  
2272 C CG  . LEU A 293 ? 0.29725 0.29910 0.30507 0.00583  0.01110  -0.00621 293 LEU A CG  
2273 C CD1 . LEU A 293 ? 0.34135 0.34222 0.35058 0.00580  0.01264  -0.00657 293 LEU A CD1 
2274 C CD2 . LEU A 293 ? 0.29721 0.29946 0.30566 0.00632  0.01086  -0.00532 293 LEU A CD2 
2275 N N   . TRP A 294 ? 0.24491 0.24941 0.24542 0.00461  0.00919  -0.00802 294 TRP A N   
2276 C CA  . TRP A 294 ? 0.24988 0.25524 0.24842 0.00424  0.00874  -0.00848 294 TRP A CA  
2277 C C   . TRP A 294 ? 0.23540 0.24187 0.23395 0.00455  0.00775  -0.00785 294 TRP A C   
2278 O O   . TRP A 294 ? 0.31923 0.32640 0.31651 0.00449  0.00741  -0.00774 294 TRP A O   
2279 C CB  . TRP A 294 ? 0.23243 0.23779 0.23076 0.00367  0.00849  -0.00926 294 TRP A CB  
2280 C CG  . TRP A 294 ? 0.24876 0.25309 0.24677 0.00326  0.00943  -0.01008 294 TRP A CG  
2281 C CD1 . TRP A 294 ? 0.26150 0.26490 0.26104 0.00316  0.00988  -0.01028 294 TRP A CD1 
2282 C CD2 . TRP A 294 ? 0.23759 0.24158 0.23360 0.00285  0.01003  -0.01084 294 TRP A CD2 
2283 N NE1 . TRP A 294 ? 0.20773 0.21027 0.20668 0.00278  0.01084  -0.01118 294 TRP A NE1 
2284 C CE2 . TRP A 294 ? 0.26563 0.26845 0.26219 0.00255  0.01099  -0.01161 294 TRP A CE2 
2285 C CE3 . TRP A 294 ? 0.32357 0.32802 0.31728 0.00264  0.00978  -0.01091 294 TRP A CE3 
2286 C CZ2 . TRP A 294 ? 0.35084 0.35287 0.34560 0.00206  0.01186  -0.01263 294 TRP A CZ2 
2287 C CZ3 . TRP A 294 ? 0.32563 0.32926 0.31723 0.00209  0.01050  -0.01183 294 TRP A CZ3 
2288 C CH2 . TRP A 294 ? 0.38630 0.38869 0.37835 0.00180  0.01160  -0.01276 294 TRP A CH2 
2289 N N   . ARG A 295 ? 0.21995 0.22652 0.21994 0.00484  0.00724  -0.00744 295 ARG A N   
2290 C CA  . ARG A 295 ? 0.17478 0.18224 0.17510 0.00518  0.00648  -0.00695 295 ARG A CA  
2291 C C   . ARG A 295 ? 0.24224 0.24975 0.24277 0.00567  0.00660  -0.00619 295 ARG A C   
2292 O O   . ARG A 295 ? 0.18034 0.18870 0.18065 0.00586  0.00608  -0.00581 295 ARG A O   
2293 C CB  . ARG A 295 ? 0.17923 0.18643 0.18066 0.00528  0.00607  -0.00683 295 ARG A CB  
2294 C CG  . ARG A 295 ? 0.17467 0.18256 0.17664 0.00564  0.00548  -0.00648 295 ARG A CG  
2295 C CD  . ARG A 295 ? 0.21218 0.21952 0.21461 0.00555  0.00521  -0.00658 295 ARG A CD  
2296 N NE  . ARG A 295 ? 0.22629 0.23397 0.22929 0.00591  0.00482  -0.00636 295 ARG A NE  
2297 C CZ  . ARG A 295 ? 0.18207 0.18919 0.18584 0.00631  0.00459  -0.00588 295 ARG A CZ  
2298 N NH1 . ARG A 295 ? 0.22427 0.23055 0.22854 0.00642  0.00468  -0.00546 295 ARG A NH1 
2299 N NH2 . ARG A 295 ? 0.25855 0.26590 0.26284 0.00660  0.00429  -0.00584 295 ARG A NH2 
2300 N N   . GLU A 296 ? 0.25284 0.25944 0.25405 0.00588  0.00732  -0.00590 296 GLU A N   
2301 C CA  . GLU A 296 ? 0.26124 0.26782 0.26277 0.00630  0.00761  -0.00513 296 GLU A CA  
2302 C C   . GLU A 296 ? 0.32366 0.33041 0.32318 0.00606  0.00812  -0.00518 296 GLU A C   
2303 O O   . GLU A 296 ? 0.41862 0.42578 0.41773 0.00628  0.00794  -0.00448 296 GLU A O   
2304 C CB  . GLU A 296 ? 0.29149 0.29707 0.29478 0.00657  0.00828  -0.00477 296 GLU A CB  
2305 C CG  . GLU A 296 ? 0.32709 0.33237 0.33222 0.00680  0.00751  -0.00446 296 GLU A CG  
2306 C CD  . GLU A 296 ? 0.30798 0.31382 0.31365 0.00720  0.00675  -0.00387 296 GLU A CD  
2307 O OE1 . GLU A 296 ? 0.24538 0.25138 0.25135 0.00751  0.00707  -0.00324 296 GLU A OE1 
2308 O OE2 . GLU A 296 ? 0.40971 0.41572 0.41547 0.00717  0.00594  -0.00406 296 GLU A OE2 
2309 N N   . PHE A 297 ? 0.32081 0.32712 0.31895 0.00555  0.00872  -0.00600 297 PHE A N   
2310 C CA  . PHE A 297 ? 0.33231 0.33846 0.32799 0.00518  0.00923  -0.00618 297 PHE A CA  
2311 C C   . PHE A 297 ? 0.36585 0.37308 0.36012 0.00495  0.00800  -0.00598 297 PHE A C   
2312 O O   . PHE A 297 ? 0.41728 0.42468 0.41018 0.00494  0.00787  -0.00535 297 PHE A O   
2313 C CB  . PHE A 297 ? 0.30714 0.31240 0.30172 0.00463  0.01013  -0.00728 297 PHE A CB  
2314 C CG  . PHE A 297 ? 0.35957 0.36452 0.35104 0.00405  0.01049  -0.00772 297 PHE A CG  
2315 C CD1 . PHE A 297 ? 0.36422 0.36859 0.35430 0.00409  0.01145  -0.00725 297 PHE A CD1 
2316 C CD2 . PHE A 297 ? 0.32881 0.33393 0.31863 0.00338  0.00987  -0.00859 297 PHE A CD2 
2317 C CE1 . PHE A 297 ? 0.33323 0.33709 0.31988 0.00343  0.01176  -0.00767 297 PHE A CE1 
2318 C CE2 . PHE A 297 ? 0.30184 0.30649 0.28847 0.00273  0.01003  -0.00904 297 PHE A CE2 
2319 C CZ  . PHE A 297 ? 0.34202 0.34597 0.32684 0.00273  0.01096  -0.00859 297 PHE A CZ  
2320 N N   . PHE A 298 ? 0.22463 0.23259 0.21938 0.00476  0.00706  -0.00643 298 PHE A N   
2321 C CA  . PHE A 298 ? 0.30839 0.31746 0.30241 0.00455  0.00583  -0.00623 298 PHE A CA  
2322 C C   . PHE A 298 ? 0.28066 0.29052 0.27607 0.00513  0.00513  -0.00517 298 PHE A C   
2323 O O   . PHE A 298 ? 0.27626 0.28684 0.27099 0.00504  0.00426  -0.00462 298 PHE A O   
2324 C CB  . PHE A 298 ? 0.28487 0.29453 0.27957 0.00420  0.00522  -0.00696 298 PHE A CB  
2325 C CG  . PHE A 298 ? 0.25633 0.26531 0.24962 0.00352  0.00566  -0.00800 298 PHE A CG  
2326 C CD1 . PHE A 298 ? 0.28466 0.29286 0.27553 0.00309  0.00617  -0.00830 298 PHE A CD1 
2327 C CD2 . PHE A 298 ? 0.20943 0.21844 0.20373 0.00327  0.00565  -0.00869 298 PHE A CD2 
2328 C CE1 . PHE A 298 ? 0.23984 0.24727 0.22944 0.00244  0.00664  -0.00939 298 PHE A CE1 
2329 C CE2 . PHE A 298 ? 0.29617 0.30450 0.28943 0.00265  0.00605  -0.00965 298 PHE A CE2 
2330 C CZ  . PHE A 298 ? 0.30419 0.31172 0.29516 0.00224  0.00654  -0.01006 298 PHE A CZ  
2331 N N   . TYR A 299 ? 0.25347 0.26314 0.25088 0.00570  0.00540  -0.00486 299 TYR A N   
2332 C CA  . TYR A 299 ? 0.30912 0.31936 0.30798 0.00627  0.00483  -0.00395 299 TYR A CA  
2333 C C   . TYR A 299 ? 0.27423 0.28415 0.27230 0.00644  0.00517  -0.00303 299 TYR A C   
2334 O O   . TYR A 299 ? 0.38868 0.39922 0.38731 0.00671  0.00448  -0.00216 299 TYR A O   
2335 C CB  . TYR A 299 ? 0.26017 0.27006 0.26109 0.00672  0.00498  -0.00398 299 TYR A CB  
2336 C CG  . TYR A 299 ? 0.28056 0.29115 0.28266 0.00679  0.00430  -0.00431 299 TYR A CG  
2337 C CD1 . TYR A 299 ? 0.21188 0.22242 0.21381 0.00640  0.00439  -0.00516 299 TYR A CD1 
2338 C CD2 . TYR A 299 ? 0.25525 0.26650 0.25877 0.00722  0.00371  -0.00379 299 TYR A CD2 
2339 C CE1 . TYR A 299 ? 0.22821 0.23931 0.23115 0.00642  0.00403  -0.00548 299 TYR A CE1 
2340 C CE2 . TYR A 299 ? 0.23777 0.24957 0.24247 0.00729  0.00336  -0.00421 299 TYR A CE2 
2341 C CZ  . TYR A 299 ? 0.24356 0.25527 0.24787 0.00687  0.00359  -0.00506 299 TYR A CZ  
2342 O OH  . TYR A 299 ? 0.18612 0.19829 0.19153 0.00689  0.00349  -0.00550 299 TYR A OH  
2343 N N   . THR A 300 ? 0.26915 0.27806 0.26606 0.00626  0.00632  -0.00317 300 THR A N   
2344 C CA  . THR A 300 ? 0.24470 0.25318 0.24070 0.00635  0.00693  -0.00230 300 THR A CA  
2345 C C   . THR A 300 ? 0.29334 0.30202 0.28647 0.00579  0.00647  -0.00207 300 THR A C   
2346 O O   . THR A 300 ? 0.26969 0.27853 0.26225 0.00588  0.00617  -0.00098 300 THR A O   
2347 C CB  . THR A 300 ? 0.27113 0.27841 0.26712 0.00634  0.00853  -0.00258 300 THR A CB  
2348 O OG1 . THR A 300 ? 0.30321 0.31026 0.30191 0.00677  0.00864  -0.00272 300 THR A OG1 
2349 C CG2 . THR A 300 ? 0.31327 0.32006 0.30867 0.00647  0.00940  -0.00159 300 THR A CG2 
2350 N N   . VAL A 301 ? 0.31765 0.32627 0.30894 0.00515  0.00628  -0.00302 301 VAL A N   
2351 C CA  . VAL A 301 ? 0.31059 0.31922 0.29884 0.00448  0.00566  -0.00288 301 VAL A CA  
2352 C C   . VAL A 301 ? 0.28845 0.29843 0.27756 0.00452  0.00379  -0.00218 301 VAL A C   
2353 O O   . VAL A 301 ? 0.31712 0.32728 0.30483 0.00431  0.00301  -0.00119 301 VAL A O   
2354 C CB  . VAL A 301 ? 0.30089 0.30887 0.28700 0.00372  0.00605  -0.00424 301 VAL A CB  
2355 C CG1 . VAL A 301 ? 0.35544 0.36312 0.33789 0.00289  0.00539  -0.00414 301 VAL A CG1 
2356 C CG2 . VAL A 301 ? 0.29334 0.30003 0.27941 0.00378  0.00797  -0.00497 301 VAL A CG2 
2357 N N   . GLY A 302 ? 0.31618 0.32707 0.30771 0.00476  0.00310  -0.00263 302 GLY A N   
2358 C CA  . GLY A 302 ? 0.29620 0.30841 0.28909 0.00481  0.00149  -0.00209 302 GLY A CA  
2359 C C   . GLY A 302 ? 0.34135 0.35406 0.33605 0.00546  0.00102  -0.00077 302 GLY A C   
2360 O O   . GLY A 302 ? 0.37714 0.39069 0.37227 0.00539  -0.00033 0.00008  302 GLY A O   
2361 N N   . SER A 303 ? 0.31322 0.32540 0.30924 0.00606  0.00201  -0.00054 303 SER A N   
2362 C CA  . SER A 303 ? 0.32000 0.33254 0.31798 0.00668  0.00162  0.00066  303 SER A CA  
2363 C C   . SER A 303 ? 0.32978 0.34197 0.32584 0.00647  0.00146  0.00193  303 SER A C   
2364 O O   . SER A 303 ? 0.27715 0.28978 0.27472 0.00686  0.00077  0.00313  303 SER A O   
2365 C CB  . SER A 303 ? 0.33800 0.34995 0.33794 0.00730  0.00261  0.00050  303 SER A CB  
2366 O OG  . SER A 303 ? 0.28051 0.29134 0.27900 0.00713  0.00394  0.00021  303 SER A OG  
2367 N N   . THR A 304 ? 0.37660 0.38789 0.36930 0.00583  0.00213  0.00170  304 THR A N   
2368 C CA  . THR A 304 ? 0.32720 0.33790 0.31738 0.00548  0.00218  0.00287  304 THR A CA  
2369 C C   . THR A 304 ? 0.36783 0.37857 0.35481 0.00458  0.00099  0.00297  304 THR A C   
2370 O O   . THR A 304 ? 0.48226 0.49234 0.46641 0.00411  0.00092  0.00394  304 THR A O   
2371 C CB  . THR A 304 ? 0.28627 0.29559 0.27485 0.00541  0.00419  0.00263  304 THR A CB  
2372 O OG1 . THR A 304 ? 0.31602 0.32466 0.30252 0.00485  0.00500  0.00118  304 THR A OG1 
2373 C CG2 . THR A 304 ? 0.30883 0.31808 0.30079 0.00624  0.00512  0.00266  304 THR A CG2 
2374 N N   . THR A 305 ? 0.34609 0.35752 0.33337 0.00426  0.00002  0.00203  305 THR A N   
2375 C CA  . THR A 305 ? 0.37647 0.38794 0.36094 0.00332  -0.00134 0.00204  305 THR A CA  
2376 C C   . THR A 305 ? 0.41177 0.42479 0.39890 0.00345  -0.00345 0.00274  305 THR A C   
2377 O O   . THR A 305 ? 0.40514 0.41913 0.39555 0.00391  -0.00359 0.00206  305 THR A O   
2378 C CB  . THR A 305 ? 0.38499 0.39588 0.36763 0.00270  -0.00073 0.00032  305 THR A CB  
2379 O OG1 . THR A 305 ? 0.35214 0.36153 0.33255 0.00259  0.00132  -0.00031 305 THR A OG1 
2380 C CG2 . THR A 305 ? 0.36644 0.37731 0.34621 0.00165  -0.00235 0.00026  305 THR A CG2 
2381 N N   . PRO A 306 ? 0.38362 0.39687 0.36957 0.00303  -0.00508 0.00412  306 PRO A N   
2382 C CA  . PRO A 306 ? 0.39541 0.41019 0.38450 0.00317  -0.00715 0.00488  306 PRO A CA  
2383 C C   . PRO A 306 ? 0.43976 0.45515 0.42886 0.00253  -0.00819 0.00381  306 PRO A C   
2384 O O   . PRO A 306 ? 0.46178 0.47626 0.44724 0.00165  -0.00808 0.00295  306 PRO A O   
2385 C CB  . PRO A 306 ? 0.34114 0.35570 0.32836 0.00273  -0.00865 0.00678  306 PRO A CB  
2386 C CG  . PRO A 306 ? 0.46103 0.47403 0.44488 0.00264  -0.00696 0.00712  306 PRO A CG  
2387 C CD  . PRO A 306 ? 0.45614 0.46821 0.43812 0.00245  -0.00504 0.00523  306 PRO A CD  
2388 N N   . ASN A 307 ? 0.39917 0.41608 0.39259 0.00298  -0.00913 0.00382  307 ASN A N   
2389 C CA  . ASN A 307 ? 0.41755 0.43531 0.41200 0.00245  -0.01020 0.00297  307 ASN A CA  
2390 C C   . ASN A 307 ? 0.42827 0.44526 0.42099 0.00214  -0.00870 0.00112  307 ASN A C   
2391 O O   . ASN A 307 ? 0.44410 0.46091 0.43498 0.00126  -0.00941 0.00038  307 ASN A O   
2392 C CB  . ASN A 307 ? 0.39370 0.41153 0.38605 0.00143  -0.01254 0.00388  307 ASN A CB  
2393 C CG  . ASN A 307 ? 0.51871 0.53736 0.51319 0.00171  -0.01429 0.00588  307 ASN A CG  
2394 O OD1 . ASN A 307 ? 0.57805 0.59820 0.57684 0.00199  -0.01562 0.00636  307 ASN A OD1 
2395 N ND2 . ASN A 307 ? 0.46506 0.48270 0.45675 0.00163  -0.01421 0.00710  307 ASN A ND2 
2396 N N   . PHE A 308 ? 0.33828 0.35477 0.33174 0.00283  -0.00671 0.00041  308 PHE A N   
2397 C CA  . PHE A 308 ? 0.41401 0.42969 0.40607 0.00258  -0.00525 -0.00118 308 PHE A CA  
2398 C C   . PHE A 308 ? 0.43143 0.44805 0.42581 0.00241  -0.00562 -0.00217 308 PHE A C   
2399 O O   . PHE A 308 ? 0.46184 0.47783 0.45470 0.00188  -0.00501 -0.00338 308 PHE A O   
2400 C CB  . PHE A 308 ? 0.39251 0.40748 0.38525 0.00337  -0.00331 -0.00147 308 PHE A CB  
2401 C CG  . PHE A 308 ? 0.37117 0.38494 0.36197 0.00308  -0.00178 -0.00279 308 PHE A CG  
2402 C CD1 . PHE A 308 ? 0.34399 0.35638 0.33123 0.00263  -0.00096 -0.00293 308 PHE A CD1 
2403 C CD2 . PHE A 308 ? 0.33906 0.35302 0.33167 0.00324  -0.00108 -0.00387 308 PHE A CD2 
2404 C CE1 . PHE A 308 ? 0.40860 0.41987 0.39453 0.00240  0.00053  -0.00416 308 PHE A CE1 
2405 C CE2 . PHE A 308 ? 0.35929 0.37213 0.35046 0.00298  0.00023  -0.00496 308 PHE A CE2 
2406 C CZ  . PHE A 308 ? 0.41273 0.42426 0.40077 0.00260  0.00103  -0.00513 308 PHE A CZ  
2407 N N   . HIS A 309 ? 0.40480 0.42287 0.40299 0.00282  -0.00649 -0.00169 309 HIS A N   
2408 C CA  . HIS A 309 ? 0.39602 0.41507 0.39679 0.00266  -0.00672 -0.00251 309 HIS A CA  
2409 C C   . HIS A 309 ? 0.43685 0.45674 0.43786 0.00185  -0.00876 -0.00220 309 HIS A C   
2410 O O   . HIS A 309 ? 0.45074 0.47173 0.45471 0.00174  -0.00918 -0.00261 309 HIS A O   
2411 C CB  . HIS A 309 ? 0.33703 0.35709 0.34205 0.00355  -0.00622 -0.00234 309 HIS A CB  
2412 C CG  . HIS A 309 ? 0.42843 0.44954 0.43601 0.00394  -0.00755 -0.00098 309 HIS A CG  
2413 N ND1 . HIS A 309 ? 0.42926 0.44993 0.43613 0.00437  -0.00768 0.00014  309 HIS A ND1 
2414 C CD2 . HIS A 309 ? 0.46771 0.49028 0.47890 0.00396  -0.00879 -0.00050 309 HIS A CD2 
2415 C CE1 . HIS A 309 ? 0.42788 0.44966 0.43774 0.00465  -0.00902 0.00128  309 HIS A CE1 
2416 N NE2 . HIS A 309 ? 0.34472 0.36768 0.35735 0.00442  -0.00971 0.00091  309 HIS A NE2 
2417 N N   . ARG A 310 ? 0.44897 0.46830 0.44693 0.00122  -0.01005 -0.00146 310 ARG A N   
2418 C CA  . ARG A 310 ? 0.43963 0.45957 0.43741 0.00032  -0.01232 -0.00103 310 ARG A CA  
2419 C C   . ARG A 310 ? 0.47004 0.48841 0.46245 -0.00075 -0.01263 -0.00154 310 ARG A C   
2420 O O   . ARG A 310 ? 0.44822 0.46513 0.43738 -0.00070 -0.01101 -0.00204 310 ARG A O   
2421 C CB  . ARG A 310 ? 0.39781 0.41872 0.39758 0.00055  -0.01418 0.00078  310 ARG A CB  
2422 C CG  . ARG A 310 ? 0.43653 0.45886 0.44172 0.00162  -0.01378 0.00124  310 ARG A CG  
2423 C CD  . ARG A 310 ? 0.44646 0.46952 0.45357 0.00190  -0.01549 0.00310  310 ARG A CD  
2424 N NE  . ARG A 310 ? 0.43939 0.46361 0.45169 0.00297  -0.01488 0.00341  310 ARG A NE  
2425 C CZ  . ARG A 310 ? 0.43688 0.46182 0.45198 0.00346  -0.01599 0.00493  310 ARG A CZ  
2426 N NH1 . ARG A 310 ? 0.44228 0.46695 0.45547 0.00296  -0.01792 0.00648  310 ARG A NH1 
2427 N NH2 . ARG A 310 ? 0.43023 0.45607 0.45007 0.00442  -0.01513 0.00490  310 ARG A NH2 
2428 N N   . MET A 311 ? 0.41565 0.43428 0.40727 -0.00177 -0.01472 -0.00143 311 MET A N   
2429 C CA  . MET A 311 ? 0.46888 0.48592 0.45513 -0.00295 -0.01532 -0.00192 311 MET A CA  
2430 C C   . MET A 311 ? 0.47491 0.49146 0.45833 -0.00345 -0.01712 -0.00032 311 MET A C   
2431 O O   . MET A 311 ? 0.51979 0.53459 0.49818 -0.00394 -0.01645 -0.00040 311 MET A O   
2432 C CB  . MET A 311 ? 0.47557 0.49287 0.46210 -0.00396 -0.01661 -0.00294 311 MET A CB  
2433 C CG  . MET A 311 ? 0.48703 0.50240 0.46785 -0.00523 -0.01687 -0.00391 311 MET A CG  
2434 S SD  . MET A 311 ? 0.58099 0.59666 0.56227 -0.00655 -0.01893 -0.00492 311 MET A SD  
2435 C CE  . MET A 311 ? 0.46525 0.48227 0.44828 -0.00704 -0.02258 -0.00288 311 MET A CE  
2436 N N   . ALA A 312 ? 0.54210 0.56010 0.52873 -0.00337 -0.01933 0.00118  312 ALA A N   
2437 C CA  . ALA A 312 ? 0.46277 0.48038 0.44707 -0.00383 -0.02123 0.00297  312 ALA A CA  
2438 C C   . ALA A 312 ? 0.45495 0.47226 0.43928 -0.00282 -0.01975 0.00400  312 ALA A C   
2439 O O   . ALA A 312 ? 0.48865 0.50698 0.47727 -0.00162 -0.01847 0.00402  312 ALA A O   
2440 C CB  . ALA A 312 ? 0.33307 0.35240 0.32150 -0.00403 -0.02419 0.00436  312 ALA A CB  
2441 N N   . GLY A 313 ? 0.50048 0.51624 0.47984 -0.00338 -0.01988 0.00482  313 GLY A N   
2442 C CA  . GLY A 313 ? 0.42197 0.43725 0.40099 -0.00255 -0.01839 0.00580  313 GLY A CA  
2443 C C   . GLY A 313 ? 0.48558 0.50002 0.46396 -0.00184 -0.01519 0.00439  313 GLY A C   
2444 O O   . GLY A 313 ? 0.42978 0.44416 0.40932 -0.00094 -0.01386 0.00509  313 GLY A O   
2445 N N   . ASN A 314 ? 0.50160 0.51537 0.47843 -0.00224 -0.01401 0.00249  314 ASN A N   
2446 C CA  . ASN A 314 ? 0.48552 0.49844 0.46194 -0.00163 -0.01112 0.00117  314 ASN A CA  
2447 C C   . ASN A 314 ? 0.47608 0.48685 0.44662 -0.00251 -0.00993 0.00043  314 ASN A C   
2448 O O   . ASN A 314 ? 0.41107 0.42107 0.37883 -0.00355 -0.01049 -0.00069 314 ASN A O   
2449 C CB  . ASN A 314 ? 0.44940 0.46311 0.42893 -0.00134 -0.01042 -0.00041 314 ASN A CB  
2450 C CG  . ASN A 314 ? 0.42491 0.43803 0.40519 -0.00054 -0.00773 -0.00142 314 ASN A CG  
2451 O OD1 . ASN A 314 ? 0.49022 0.50309 0.47084 -0.00064 -0.00673 -0.00290 314 ASN A OD1 
2452 N ND2 . ASN A 314 ? 0.43291 0.44578 0.41365 0.00023  -0.00665 -0.00053 314 ASN A ND2 
2453 N N   . PRO A 315 ? 0.50890 0.51856 0.47746 -0.00218 -0.00822 0.00094  315 PRO A N   
2454 C CA  . PRO A 315 ? 0.48960 0.49710 0.45246 -0.00307 -0.00690 0.00025  315 PRO A CA  
2455 C C   . PRO A 315 ? 0.41545 0.42201 0.37764 -0.00315 -0.00482 -0.00190 315 PRO A C   
2456 O O   . PRO A 315 ? 0.37480 0.37960 0.33236 -0.00414 -0.00414 -0.00291 315 PRO A O   
2457 C CB  . PRO A 315 ? 0.45626 0.46314 0.41843 -0.00251 -0.00548 0.00154  315 PRO A CB  
2458 C CG  . PRO A 315 ? 0.41555 0.42403 0.38349 -0.00112 -0.00511 0.00203  315 PRO A CG  
2459 C CD  . PRO A 315 ? 0.45684 0.46711 0.42834 -0.00103 -0.00738 0.00217  315 PRO A CD  
2460 N N   . VAL A 316 ? 0.47846 0.48598 0.44502 -0.00219 -0.00378 -0.00262 316 VAL A N   
2461 C CA  . VAL A 316 ? 0.46400 0.47064 0.43038 -0.00221 -0.00187 -0.00449 316 VAL A CA  
2462 C C   . VAL A 316 ? 0.47323 0.48023 0.43996 -0.00289 -0.00304 -0.00575 316 VAL A C   
2463 O O   . VAL A 316 ? 0.39429 0.40030 0.36020 -0.00317 -0.00168 -0.00736 316 VAL A O   
2464 C CB  . VAL A 316 ? 0.43859 0.44588 0.40922 -0.00096 -0.00023 -0.00461 316 VAL A CB  
2465 C CG1 . VAL A 316 ? 0.34695 0.35389 0.31763 -0.00030 0.00091  -0.00338 316 VAL A CG1 
2466 C CG2 . VAL A 316 ? 0.44166 0.45088 0.41689 -0.00036 -0.00159 -0.00430 316 VAL A CG2 
2467 N N   . CYS A 317 ? 0.44898 0.45735 0.41721 -0.00317 -0.00550 -0.00506 317 CYS A N   
2468 C CA  . CYS A 317 ? 0.43901 0.44790 0.40816 -0.00381 -0.00676 -0.00611 317 CYS A CA  
2469 C C   . CYS A 317 ? 0.40664 0.41452 0.37133 -0.00524 -0.00851 -0.00624 317 CYS A C   
2470 O O   . CYS A 317 ? 0.43213 0.44018 0.39531 -0.00561 -0.01026 -0.00479 317 CYS A O   
2471 C CB  . CYS A 317 ? 0.47838 0.48950 0.45271 -0.00321 -0.00826 -0.00534 317 CYS A CB  
2472 S SG  . CYS A 317 ? 0.56432 0.57630 0.54040 -0.00403 -0.00993 -0.00638 317 CYS A SG  
2473 N N   . LYS A 318 ? 0.40796 0.41467 0.37048 -0.00610 -0.00811 -0.00796 318 LYS A N   
2474 C CA  . LYS A 318 ? 0.39698 0.40251 0.35501 -0.00762 -0.00987 -0.00840 318 LYS A CA  
2475 C C   . LYS A 318 ? 0.46171 0.46897 0.42254 -0.00803 -0.01291 -0.00771 318 LYS A C   
2476 O O   . LYS A 318 ? 0.50542 0.51423 0.47105 -0.00747 -0.01299 -0.00804 318 LYS A O   
2477 C CB  . LYS A 318 ? 0.44469 0.44847 0.40020 -0.00835 -0.00842 -0.01061 318 LYS A CB  
2478 C CG  . LYS A 318 ? 0.49918 0.50132 0.44952 -0.01003 -0.00994 -0.01143 318 LYS A CG  
2479 C CD  . LYS A 318 ? 0.47999 0.47958 0.42606 -0.01062 -0.00754 -0.01335 318 LYS A CD  
2480 C CE  . LYS A 318 ? 0.53013 0.52815 0.47205 -0.01229 -0.00897 -0.01475 318 LYS A CE  
2481 N NZ  . LYS A 318 ? 0.48678 0.48246 0.42173 -0.01341 -0.00886 -0.01477 318 LYS A NZ  
2482 N N   . GLN A 319 ? 0.42963 0.43653 0.38746 -0.00905 -0.01533 -0.00676 319 GLN A N   
2483 C CA  . GLN A 319 ? 0.54635 0.55486 0.50700 -0.00953 -0.01847 -0.00594 319 GLN A CA  
2484 C C   . GLN A 319 ? 0.49996 0.50804 0.46020 -0.01058 -0.01927 -0.00766 319 GLN A C   
2485 O O   . GLN A 319 ? 0.54659 0.55258 0.50152 -0.01183 -0.01939 -0.00878 319 GLN A O   
2486 C CB  . GLN A 319 ? 0.48591 0.49407 0.44344 -0.01035 -0.02103 -0.00420 319 GLN A CB  
2487 C CG  . GLN A 319 ? 0.49667 0.50525 0.45477 -0.00937 -0.02038 -0.00235 319 GLN A CG  
2488 C CD  . GLN A 319 ? 0.52443 0.53536 0.48951 -0.00781 -0.01988 -0.00161 319 GLN A CD  
2489 O OE1 . GLN A 319 ? 0.49989 0.51266 0.46953 -0.00770 -0.02175 -0.00110 319 GLN A OE1 
2490 N NE2 . GLN A 319 ? 0.54504 0.55586 0.51105 -0.00664 -0.01728 -0.00159 319 GLN A NE2 
2491 N N   . ILE A 320 ? 0.56749 0.57742 0.53329 -0.01012 -0.01972 -0.00791 320 ILE A N   
2492 C CA  . ILE A 320 ? 0.53550 0.54531 0.50200 -0.01101 -0.02044 -0.00943 320 ILE A CA  
2493 C C   . ILE A 320 ? 0.53734 0.54921 0.50825 -0.01130 -0.02342 -0.00837 320 ILE A C   
2494 O O   . ILE A 320 ? 0.61319 0.62712 0.58927 -0.01022 -0.02352 -0.00716 320 ILE A O   
2495 C CB  . ILE A 320 ? 0.55729 0.56724 0.52659 -0.01021 -0.01773 -0.01088 320 ILE A CB  
2496 C CG1 . ILE A 320 ? 0.58739 0.59529 0.55280 -0.00992 -0.01485 -0.01187 320 ILE A CG1 
2497 C CG2 . ILE A 320 ? 0.58044 0.59034 0.55090 -0.01113 -0.01856 -0.01232 320 ILE A CG2 
2498 C CD1 . ILE A 320 ? 0.58582 0.59372 0.55392 -0.00914 -0.01229 -0.01310 320 ILE A CD1 
2499 N N   . ASP A 321 ? 0.54742 0.55868 0.51644 -0.01279 -0.02582 -0.00888 321 ASP A N   
2500 C CA  . ASP A 321 ? 0.59888 0.61202 0.57220 -0.01325 -0.02892 -0.00789 321 ASP A CA  
2501 C C   . ASP A 321 ? 0.59768 0.61244 0.57697 -0.01273 -0.02803 -0.00875 321 ASP A C   
2502 O O   . ASP A 321 ? 0.55497 0.56957 0.53487 -0.01370 -0.02904 -0.00986 321 ASP A O   
2503 C CB  . ASP A 321 ? 0.70933 0.72112 0.67842 -0.01511 -0.03190 -0.00815 321 ASP A CB  
2504 C CG  . ASP A 321 ? 0.71857 0.72951 0.68337 -0.01567 -0.03383 -0.00649 321 ASP A CG  
2505 O OD1 . ASP A 321 ? 0.81645 0.82568 0.77631 -0.01548 -0.03198 -0.00659 321 ASP A OD1 
2506 O OD2 . ASP A 321 ? 0.76775 0.77973 0.73430 -0.01631 -0.03721 -0.00501 321 ASP A OD2 
2507 N N   . TRP A 322 ? 0.63865 0.65490 0.62231 -0.01121 -0.02609 -0.00821 322 TRP A N   
2508 C CA  . TRP A 322 ? 0.55046 0.56824 0.53971 -0.01065 -0.02501 -0.00882 322 TRP A CA  
2509 C C   . TRP A 322 ? 0.48778 0.50747 0.48189 -0.01118 -0.02776 -0.00801 322 TRP A C   
2510 O O   . TRP A 322 ? 0.60085 0.62148 0.59617 -0.01125 -0.03003 -0.00639 322 TRP A O   
2511 C CB  . TRP A 322 ? 0.42249 0.44132 0.41496 -0.00900 -0.02255 -0.00829 322 TRP A CB  
2512 C CG  . TRP A 322 ? 0.41593 0.43308 0.40457 -0.00840 -0.01983 -0.00902 322 TRP A CG  
2513 C CD1 . TRP A 322 ? 0.40560 0.42226 0.39217 -0.00767 -0.01897 -0.00812 322 TRP A CD1 
2514 C CD2 . TRP A 322 ? 0.42176 0.43752 0.40865 -0.00849 -0.01764 -0.01072 322 TRP A CD2 
2515 N NE1 . TRP A 322 ? 0.43077 0.44589 0.41455 -0.00730 -0.01639 -0.00917 322 TRP A NE1 
2516 C CE2 . TRP A 322 ? 0.43964 0.45417 0.42360 -0.00778 -0.01555 -0.01075 322 TRP A CE2 
2517 C CE3 . TRP A 322 ? 0.39634 0.41178 0.38414 -0.00911 -0.01728 -0.01215 322 TRP A CE3 
2518 C CZ2 . TRP A 322 ? 0.48991 0.50294 0.47203 -0.00764 -0.01317 -0.01214 322 TRP A CZ2 
2519 C CZ3 . TRP A 322 ? 0.40917 0.42305 0.39496 -0.00898 -0.01491 -0.01352 322 TRP A CZ3 
2520 C CH2 . TRP A 322 ? 0.42716 0.43988 0.41023 -0.00824 -0.01291 -0.01350 322 TRP A CH2 
2521 N N   . ASP A 323 ? 0.46682 0.48708 0.46400 -0.01156 -0.02757 -0.00906 323 ASP A N   
2522 C CA  . ASP A 323 ? 0.52015 0.54217 0.52227 -0.01217 -0.03007 -0.00845 323 ASP A CA  
2523 C C   . ASP A 323 ? 0.56712 0.59158 0.57614 -0.01092 -0.02924 -0.00738 323 ASP A C   
2524 O O   . ASP A 323 ? 0.53617 0.56085 0.54641 -0.00974 -0.02639 -0.00768 323 ASP A O   
2525 C CB  . ASP A 323 ? 0.49853 0.52005 0.50116 -0.01320 -0.03019 -0.01005 323 ASP A CB  
2526 C CG  . ASP A 323 ? 0.56077 0.57965 0.55658 -0.01444 -0.03063 -0.01142 323 ASP A CG  
2527 O OD1 . ASP A 323 ? 0.57761 0.59528 0.56861 -0.01493 -0.03200 -0.01087 323 ASP A OD1 
2528 O OD2 . ASP A 323 ? 0.49161 0.50954 0.48686 -0.01494 -0.02954 -0.01306 323 ASP A OD2 
2529 N N   . ASP A 324 ? 0.60042 0.62664 0.61401 -0.01123 -0.03180 -0.00615 324 ASP A N   
2530 C CA  . ASP A 324 ? 0.57496 0.60356 0.59573 -0.01019 -0.03117 -0.00521 324 ASP A CA  
2531 C C   . ASP A 324 ? 0.52778 0.55749 0.55333 -0.01073 -0.03122 -0.00597 324 ASP A C   
2532 O O   . ASP A 324 ? 0.52891 0.55954 0.55731 -0.01167 -0.03402 -0.00544 324 ASP A O   
2533 C CB  . ASP A 324 ? 0.47938 0.50926 0.50279 -0.01009 -0.03383 -0.00322 324 ASP A CB  
2534 C CG  . ASP A 324 ? 0.55097 0.58301 0.58127 -0.00875 -0.03261 -0.00228 324 ASP A CG  
2535 O OD1 . ASP A 324 ? 0.48940 0.52250 0.52410 -0.00839 -0.03082 -0.00301 324 ASP A OD1 
2536 O OD2 . ASP A 324 ? 0.63263 0.66522 0.66389 -0.00810 -0.03337 -0.00081 324 ASP A OD2 
2537 N N   . ASN A 325 ? 0.47815 0.50773 0.50464 -0.01016 -0.02819 -0.00712 325 ASN A N   
2538 C CA  . ASN A 325 ? 0.46044 0.49090 0.49115 -0.01065 -0.02774 -0.00790 325 ASN A CA  
2539 C C   . ASN A 325 ? 0.51916 0.55096 0.55463 -0.00941 -0.02485 -0.00778 325 ASN A C   
2540 O O   . ASN A 325 ? 0.48625 0.51715 0.51992 -0.00889 -0.02204 -0.00871 325 ASN A O   
2541 C CB  . ASN A 325 ? 0.49125 0.51976 0.51761 -0.01151 -0.02696 -0.00961 325 ASN A CB  
2542 C CG  . ASN A 325 ? 0.48511 0.51435 0.51543 -0.01243 -0.02756 -0.01027 325 ASN A CG  
2543 O OD1 . ASN A 325 ? 0.51510 0.54612 0.55139 -0.01199 -0.02660 -0.00989 325 ASN A OD1 
2544 N ND2 . ASN A 325 ? 0.45486 0.48263 0.48187 -0.01376 -0.02908 -0.01130 325 ASN A ND2 
2545 N N   . PRO A 326 ? 0.58298 0.61689 0.62459 -0.00894 -0.02545 -0.00662 326 PRO A N   
2546 C CA  . PRO A 326 ? 0.53743 0.57248 0.58340 -0.00781 -0.02253 -0.00660 326 PRO A CA  
2547 C C   . PRO A 326 ? 0.46974 0.50490 0.51786 -0.00817 -0.02064 -0.00768 326 PRO A C   
2548 O O   . PRO A 326 ? 0.39718 0.43235 0.44619 -0.00737 -0.01766 -0.00806 326 PRO A O   
2549 C CB  . PRO A 326 ? 0.51373 0.55097 0.56615 -0.00746 -0.02401 -0.00517 326 PRO A CB  
2550 C CG  . PRO A 326 ? 0.35719 0.39413 0.40723 -0.00808 -0.02751 -0.00418 326 PRO A CG  
2551 C CD  . PRO A 326 ? 0.53503 0.57022 0.57966 -0.00936 -0.02875 -0.00522 326 PRO A CD  
2552 N N   . GLU A 327 ? 0.52800 0.56318 0.57691 -0.00941 -0.02236 -0.00814 327 GLU A N   
2553 C CA  . GLU A 327 ? 0.52677 0.56201 0.57783 -0.00983 -0.02063 -0.00908 327 GLU A CA  
2554 C C   . GLU A 327 ? 0.47838 0.51158 0.52412 -0.00964 -0.01822 -0.01025 327 GLU A C   
2555 O O   . GLU A 327 ? 0.37581 0.40904 0.42300 -0.00923 -0.01552 -0.01066 327 GLU A O   
2556 C CB  . GLU A 327 ? 0.53299 0.56851 0.58581 -0.01128 -0.02325 -0.00935 327 GLU A CB  
2557 C CG  . GLU A 327 ? 0.58871 0.62645 0.64805 -0.01158 -0.02564 -0.00814 327 GLU A CG  
2558 C CD  . GLU A 327 ? 0.57805 0.61576 0.63548 -0.01178 -0.02888 -0.00711 327 GLU A CD  
2559 O OE1 . GLU A 327 ? 0.55037 0.58650 0.60165 -0.01146 -0.02880 -0.00724 327 GLU A OE1 
2560 O OE2 . GLU A 327 ? 0.60338 0.64264 0.66559 -0.01229 -0.03155 -0.00610 327 GLU A OE2 
2561 N N   . PHE A 328 ? 0.48477 0.51612 0.52438 -0.00997 -0.01913 -0.01076 328 PHE A N   
2562 C CA  . PHE A 328 ? 0.46239 0.49180 0.49726 -0.00971 -0.01689 -0.01178 328 PHE A CA  
2563 C C   . PHE A 328 ? 0.40328 0.43261 0.43731 -0.00835 -0.01451 -0.01138 328 PHE A C   
2564 O O   . PHE A 328 ? 0.44936 0.47775 0.48201 -0.00797 -0.01211 -0.01198 328 PHE A O   
2565 C CB  . PHE A 328 ? 0.35369 0.38113 0.38249 -0.01040 -0.01833 -0.01247 328 PHE A CB  
2566 C CG  . PHE A 328 ? 0.31942 0.34622 0.34788 -0.01182 -0.01997 -0.01339 328 PHE A CG  
2567 C CD1 . PHE A 328 ? 0.44781 0.47530 0.48034 -0.01230 -0.01931 -0.01383 328 PHE A CD1 
2568 C CD2 . PHE A 328 ? 0.29114 0.31653 0.31506 -0.01275 -0.02213 -0.01386 328 PHE A CD2 
2569 C CE1 . PHE A 328 ? 0.36263 0.38947 0.39503 -0.01364 -0.02087 -0.01472 328 PHE A CE1 
2570 C CE2 . PHE A 328 ? 0.32242 0.34703 0.34584 -0.01413 -0.02369 -0.01485 328 PHE A CE2 
2571 C CZ  . PHE A 328 ? 0.42300 0.44837 0.45082 -0.01456 -0.02311 -0.01528 328 PHE A CZ  
2572 N N   . LEU A 329 ? 0.40135 0.43156 0.43625 -0.00764 -0.01526 -0.01033 329 LEU A N   
2573 C CA  . LEU A 329 ? 0.45478 0.48489 0.48911 -0.00638 -0.01313 -0.00997 329 LEU A CA  
2574 C C   . LEU A 329 ? 0.44975 0.48098 0.48865 -0.00586 -0.01089 -0.00994 329 LEU A C   
2575 O O   . LEU A 329 ? 0.32142 0.35186 0.35888 -0.00520 -0.00847 -0.01026 329 LEU A O   
2576 C CB  . LEU A 329 ? 0.37114 0.40189 0.40557 -0.00581 -0.01460 -0.00883 329 LEU A CB  
2577 C CG  . LEU A 329 ? 0.34432 0.37507 0.37868 -0.00451 -0.01267 -0.00839 329 LEU A CG  
2578 C CD1 . LEU A 329 ? 0.47040 0.49919 0.49952 -0.00419 -0.01092 -0.00912 329 LEU A CD1 
2579 C CD2 . LEU A 329 ? 0.38221 0.41367 0.41724 -0.00405 -0.01439 -0.00716 329 LEU A CD2 
2580 N N   . ALA A 330 ? 0.49734 0.53033 0.54177 -0.00620 -0.01164 -0.00954 330 ALA A N   
2581 C CA  . ALA A 330 ? 0.43919 0.47322 0.48811 -0.00579 -0.00931 -0.00953 330 ALA A CA  
2582 C C   . ALA A 330 ? 0.39576 0.42879 0.44349 -0.00626 -0.00740 -0.01046 330 ALA A C   
2583 O O   . ALA A 330 ? 0.37408 0.40678 0.42198 -0.00574 -0.00477 -0.01065 330 ALA A O   
2584 C CB  . ALA A 330 ? 0.46810 0.50430 0.52367 -0.00608 -0.01059 -0.00885 330 ALA A CB  
2585 N N   . ALA A 331 ? 0.39325 0.42565 0.43967 -0.00731 -0.00872 -0.01103 331 ALA A N   
2586 C CA  . ALA A 331 ? 0.37754 0.40889 0.42294 -0.00781 -0.00705 -0.01183 331 ALA A CA  
2587 C C   . ALA A 331 ? 0.34937 0.37877 0.38953 -0.00728 -0.00535 -0.01228 331 ALA A C   
2588 O O   . ALA A 331 ? 0.37394 0.40261 0.41376 -0.00728 -0.00324 -0.01261 331 ALA A O   
2589 C CB  . ALA A 331 ? 0.30212 0.33309 0.34727 -0.00906 -0.00900 -0.01242 331 ALA A CB  
2590 N N   . TRP A 332 ? 0.30796 0.33648 0.34413 -0.00686 -0.00625 -0.01222 332 TRP A N   
2591 C CA  . TRP A 332 ? 0.30705 0.33378 0.33862 -0.00634 -0.00477 -0.01258 332 TRP A CA  
2592 C C   . TRP A 332 ? 0.35585 0.38276 0.38794 -0.00531 -0.00273 -0.01212 332 TRP A C   
2593 O O   . TRP A 332 ? 0.30628 0.33202 0.33650 -0.00508 -0.00087 -0.01240 332 TRP A O   
2594 C CB  . TRP A 332 ? 0.27605 0.30173 0.30332 -0.00631 -0.00630 -0.01268 332 TRP A CB  
2595 C CG  . TRP A 332 ? 0.31346 0.33750 0.33659 -0.00567 -0.00485 -0.01289 332 TRP A CG  
2596 C CD1 . TRP A 332 ? 0.34186 0.36422 0.36223 -0.00593 -0.00385 -0.01364 332 TRP A CD1 
2597 C CD2 . TRP A 332 ? 0.33220 0.35612 0.35390 -0.00467 -0.00432 -0.01232 332 TRP A CD2 
2598 N NE1 . TRP A 332 ? 0.32568 0.34694 0.34312 -0.00515 -0.00277 -0.01351 332 TRP A NE1 
2599 C CE2 . TRP A 332 ? 0.31670 0.33888 0.33480 -0.00439 -0.00304 -0.01273 332 TRP A CE2 
2600 C CE3 . TRP A 332 ? 0.38300 0.40810 0.40638 -0.00399 -0.00483 -0.01146 332 TRP A CE3 
2601 C CZ2 . TRP A 332 ? 0.30121 0.32283 0.31735 -0.00349 -0.00231 -0.01233 332 TRP A CZ2 
2602 C CZ3 . TRP A 332 ? 0.29816 0.32263 0.31943 -0.00309 -0.00405 -0.01111 332 TRP A CZ3 
2603 C CH2 . TRP A 332 ? 0.23550 0.25826 0.25317 -0.00287 -0.00283 -0.01154 332 TRP A CH2 
2604 N N   . ARG A 333 ? 0.31563 0.34390 0.35027 -0.00470 -0.00312 -0.01142 333 ARG A N   
2605 C CA  . ARG A 333 ? 0.35425 0.38255 0.38930 -0.00375 -0.00121 -0.01112 333 ARG A CA  
2606 C C   . ARG A 333 ? 0.32855 0.35741 0.36685 -0.00383 0.00088  -0.01123 333 ARG A C   
2607 O O   . ARG A 333 ? 0.39427 0.42262 0.43192 -0.00322 0.00284  -0.01123 333 ARG A O   
2608 C CB  . ARG A 333 ? 0.33973 0.36918 0.37661 -0.00305 -0.00223 -0.01036 333 ARG A CB  
2609 C CG  . ARG A 333 ? 0.34817 0.37966 0.39070 -0.00328 -0.00318 -0.00988 333 ARG A CG  
2610 C CD  . ARG A 333 ? 0.35961 0.39214 0.40460 -0.00238 -0.00339 -0.00912 333 ARG A CD  
2611 N NE  . ARG A 333 ? 0.31534 0.34985 0.36597 -0.00260 -0.00476 -0.00851 333 ARG A NE  
2612 C CZ  . ARG A 333 ? 0.42863 0.46388 0.48008 -0.00287 -0.00756 -0.00780 333 ARG A CZ  
2613 N NH1 . ARG A 333 ? 0.45371 0.48786 0.50046 -0.00296 -0.00915 -0.00764 333 ARG A NH1 
2614 N NH2 . ARG A 333 ? 0.53630 0.57339 0.59346 -0.00309 -0.00879 -0.00718 333 ARG A NH2 
2615 N N   . GLU A 334 ? 0.33470 0.36452 0.37638 -0.00461 0.00055  -0.01134 334 GLU A N   
2616 C CA  . GLU A 334 ? 0.33339 0.36377 0.37837 -0.00479 0.00265  -0.01140 334 GLU A CA  
2617 C C   . GLU A 334 ? 0.40396 0.43311 0.44722 -0.00554 0.00369  -0.01188 334 GLU A C   
2618 O O   . GLU A 334 ? 0.36183 0.39137 0.40773 -0.00589 0.00536  -0.01189 334 GLU A O   
2619 C CB  . GLU A 334 ? 0.27497 0.30746 0.32595 -0.00511 0.00178  -0.01103 334 GLU A CB  
2620 C CG  . GLU A 334 ? 0.27552 0.30933 0.32915 -0.00433 0.00097  -0.01041 334 GLU A CG  
2621 C CD  . GLU A 334 ? 0.32693 0.36285 0.38679 -0.00471 -0.00035 -0.00993 334 GLU A CD  
2622 O OE1 . GLU A 334 ? 0.29677 0.33311 0.35871 -0.00562 -0.00072 -0.01013 334 GLU A OE1 
2623 O OE2 . GLU A 334 ? 0.37728 0.41443 0.44022 -0.00412 -0.00107 -0.00932 334 GLU A OE2 
2624 N N   . ALA A 335 ? 0.37068 0.39834 0.40976 -0.00580 0.00283  -0.01226 335 ALA A N   
2625 C CA  . ALA A 335 ? 0.27657 0.30285 0.31383 -0.00644 0.00372  -0.01268 335 ALA A CA  
2626 C C   . ALA A 335 ? 0.39111 0.41829 0.43221 -0.00741 0.00350  -0.01280 335 ALA A C   
2627 O O   . ALA A 335 ? 0.37818 0.40530 0.42089 -0.00774 0.00531  -0.01271 335 ALA A O   
2628 C CB  . ALA A 335 ? 0.27208 0.29720 0.30746 -0.00606 0.00616  -0.01255 335 ALA A CB  
2629 N N   . ARG A 336 ? 0.37002 0.39797 0.41250 -0.00793 0.00118  -0.01296 336 ARG A N   
2630 C CA  . ARG A 336 ? 0.33628 0.36507 0.38249 -0.00894 0.00053  -0.01312 336 ARG A CA  
2631 C C   . ARG A 336 ? 0.38723 0.41551 0.43186 -0.00967 -0.00205 -0.01368 336 ARG A C   
2632 O O   . ARG A 336 ? 0.29657 0.32604 0.34440 -0.01033 -0.00388 -0.01365 336 ARG A O   
2633 C CB  . ARG A 336 ? 0.37139 0.40239 0.42337 -0.00889 0.00049  -0.01255 336 ARG A CB  
2634 C CG  . ARG A 336 ? 0.35976 0.39191 0.41259 -0.00827 -0.00120 -0.01209 336 ARG A CG  
2635 C CD  . ARG A 336 ? 0.28702 0.32139 0.34634 -0.00825 -0.00121 -0.01151 336 ARG A CD  
2636 N NE  . ARG A 336 ? 0.28907 0.32454 0.34962 -0.00762 -0.00281 -0.01092 336 ARG A NE  
2637 C CZ  . ARG A 336 ? 0.36507 0.40124 0.42652 -0.00805 -0.00586 -0.01065 336 ARG A CZ  
2638 N NH1 . ARG A 336 ? 0.31834 0.35419 0.37943 -0.00914 -0.00768 -0.01106 336 ARG A NH1 
2639 N NH2 . ARG A 336 ? 0.35576 0.39288 0.41843 -0.00743 -0.00718 -0.00994 336 ARG A NH2 
2640 N N   . THR A 337 ? 0.37723 0.40365 0.41693 -0.00961 -0.00220 -0.01422 337 THR A N   
2641 C CA  . THR A 337 ? 0.31197 0.33751 0.34935 -0.01031 -0.00433 -0.01494 337 THR A CA  
2642 C C   . THR A 337 ? 0.20742 0.23204 0.24531 -0.01134 -0.00425 -0.01566 337 THR A C   
2643 O O   . THR A 337 ? 0.23909 0.26291 0.27542 -0.01209 -0.00600 -0.01643 337 THR A O   
2644 C CB  . THR A 337 ? 0.33574 0.35965 0.36774 -0.00974 -0.00436 -0.01524 337 THR A CB  
2645 O OG1 . THR A 337 ? 0.30908 0.33152 0.33901 -0.00944 -0.00227 -0.01541 337 THR A OG1 
2646 C CG2 . THR A 337 ? 0.40475 0.42951 0.43629 -0.00876 -0.00457 -0.01450 337 THR A CG2 
2647 N N   . GLY A 338 ? 0.31714 0.34173 0.35703 -0.01144 -0.00225 -0.01545 338 GLY A N   
2648 C CA  . GLY A 338 ? 0.28399 0.30762 0.32454 -0.01238 -0.00200 -0.01601 338 GLY A CA  
2649 C C   . GLY A 338 ? 0.26208 0.28348 0.29860 -0.01227 -0.00096 -0.01650 338 GLY A C   
2650 O O   . GLY A 338 ? 0.27633 0.29683 0.31362 -0.01294 -0.00034 -0.01681 338 GLY A O   
2651 N N   . PHE A 339 ? 0.20998 0.23047 0.24256 -0.01145 -0.00077 -0.01653 339 PHE A N   
2652 C CA  . PHE A 339 ? 0.26230 0.28072 0.29145 -0.01126 0.00023  -0.01690 339 PHE A CA  
2653 C C   . PHE A 339 ? 0.25811 0.27630 0.28679 -0.01052 0.00231  -0.01603 339 PHE A C   
2654 O O   . PHE A 339 ? 0.27232 0.29103 0.29991 -0.00966 0.00261  -0.01553 339 PHE A O   
2655 C CB  . PHE A 339 ? 0.27519 0.29260 0.30036 -0.01091 -0.00081 -0.01750 339 PHE A CB  
2656 C CG  . PHE A 339 ? 0.20680 0.22396 0.23146 -0.01178 -0.00283 -0.01848 339 PHE A CG  
2657 C CD1 . PHE A 339 ? 0.24086 0.25634 0.26439 -0.01252 -0.00295 -0.01954 339 PHE A CD1 
2658 C CD2 . PHE A 339 ? 0.20393 0.22241 0.22920 -0.01190 -0.00468 -0.01834 339 PHE A CD2 
2659 C CE1 . PHE A 339 ? 0.27639 0.29141 0.29906 -0.01341 -0.00481 -0.02058 339 PHE A CE1 
2660 C CE2 . PHE A 339 ? 0.23528 0.25334 0.25965 -0.01282 -0.00673 -0.01922 339 PHE A CE2 
2661 C CZ  . PHE A 339 ? 0.24589 0.26217 0.26878 -0.01361 -0.00676 -0.02041 339 PHE A CZ  
2662 N N   . PRO A 340 ? 0.24589 0.26321 0.27523 -0.01086 0.00371  -0.01579 340 PRO A N   
2663 C CA  . PRO A 340 ? 0.26284 0.27981 0.29143 -0.01030 0.00558  -0.01489 340 PRO A CA  
2664 C C   . PRO A 340 ? 0.25994 0.27571 0.28477 -0.00944 0.00583  -0.01480 340 PRO A C   
2665 O O   . PRO A 340 ? 0.30717 0.32303 0.33115 -0.00881 0.00689  -0.01411 340 PRO A O   
2666 C CB  . PRO A 340 ? 0.23949 0.25544 0.26918 -0.01104 0.00664  -0.01468 340 PRO A CB  
2667 C CG  . PRO A 340 ? 0.27054 0.28712 0.30310 -0.01198 0.00552  -0.01531 340 PRO A CG  
2668 C CD  . PRO A 340 ? 0.30611 0.32279 0.33720 -0.01187 0.00360  -0.01623 340 PRO A CD  
2669 N N   . TRP A 341 ? 0.19340 0.20798 0.21600 -0.00942 0.00496  -0.01550 341 TRP A N   
2670 C CA  . TRP A 341 ? 0.25480 0.26831 0.27422 -0.00860 0.00523  -0.01539 341 TRP A CA  
2671 C C   . TRP A 341 ? 0.22188 0.23653 0.24049 -0.00784 0.00467  -0.01519 341 TRP A C   
2672 O O   . TRP A 341 ? 0.29152 0.30590 0.30860 -0.00708 0.00535  -0.01464 341 TRP A O   
2673 C CB  . TRP A 341 ? 0.22374 0.23569 0.24131 -0.00880 0.00466  -0.01627 341 TRP A CB  
2674 C CG  . TRP A 341 ? 0.26510 0.27607 0.27980 -0.00797 0.00489  -0.01620 341 TRP A CG  
2675 C CD1 . TRP A 341 ? 0.27591 0.28680 0.28861 -0.00763 0.00408  -0.01674 341 TRP A CD1 
2676 C CD2 . TRP A 341 ? 0.25040 0.26029 0.26401 -0.00745 0.00596  -0.01548 341 TRP A CD2 
2677 N NE1 . TRP A 341 ? 0.28579 0.29569 0.29650 -0.00688 0.00472  -0.01642 341 TRP A NE1 
2678 C CE2 . TRP A 341 ? 0.27408 0.28337 0.28540 -0.00676 0.00576  -0.01566 341 TRP A CE2 
2679 C CE3 . TRP A 341 ? 0.27710 0.28639 0.29136 -0.00756 0.00698  -0.01465 341 TRP A CE3 
2680 C CZ2 . TRP A 341 ? 0.21525 0.22348 0.22534 -0.00616 0.00648  -0.01504 341 TRP A CZ2 
2681 C CZ3 . TRP A 341 ? 0.20895 0.21708 0.22162 -0.00701 0.00755  -0.01401 341 TRP A CZ3 
2682 C CH2 . TRP A 341 ? 0.18607 0.19374 0.19687 -0.00630 0.00725  -0.01422 341 TRP A CH2 
2683 N N   . ILE A 342 ? 0.24719 0.26308 0.26692 -0.00809 0.00331  -0.01556 342 ILE A N   
2684 C CA  . ILE A 342 ? 0.30966 0.32665 0.32891 -0.00741 0.00262  -0.01526 342 ILE A CA  
2685 C C   . ILE A 342 ? 0.24556 0.26396 0.26720 -0.00704 0.00349  -0.01448 342 ILE A C   
2686 O O   . ILE A 342 ? 0.23290 0.25156 0.25365 -0.00623 0.00388  -0.01402 342 ILE A O   
2687 C CB  . ILE A 342 ? 0.35981 0.37751 0.37933 -0.00789 0.00067  -0.01581 342 ILE A CB  
2688 C CG1 . ILE A 342 ? 0.21231 0.22834 0.22901 -0.00830 0.00007  -0.01676 342 ILE A CG1 
2689 C CG2 . ILE A 342 ? 0.27625 0.29506 0.29541 -0.00721 -0.00017 -0.01531 342 ILE A CG2 
2690 C CD1 . ILE A 342 ? 0.32789 0.34264 0.34119 -0.00755 0.00066  -0.01675 342 ILE A CD1 
2691 N N   . ASP A 343 ? 0.22783 0.24709 0.25266 -0.00764 0.00392  -0.01437 343 ASP A N   
2692 C CA  . ASP A 343 ? 0.26635 0.28695 0.29377 -0.00736 0.00496  -0.01374 343 ASP A CA  
2693 C C   . ASP A 343 ? 0.28843 0.30804 0.31418 -0.00690 0.00687  -0.01326 343 ASP A C   
2694 O O   . ASP A 343 ? 0.25782 0.27813 0.28431 -0.00636 0.00776  -0.01286 343 ASP A O   
2695 C CB  . ASP A 343 ? 0.32130 0.34298 0.35271 -0.00819 0.00511  -0.01374 343 ASP A CB  
2696 C CG  . ASP A 343 ? 0.29961 0.32242 0.33305 -0.00870 0.00299  -0.01414 343 ASP A CG  
2697 O OD1 . ASP A 343 ? 0.29228 0.31573 0.32510 -0.00826 0.00163  -0.01410 343 ASP A OD1 
2698 O OD2 . ASP A 343 ? 0.30000 0.32298 0.33560 -0.00960 0.00257  -0.01444 343 ASP A OD2 
2699 N N   . ALA A 344 ? 0.28846 0.30635 0.31201 -0.00713 0.00747  -0.01329 344 ALA A N   
2700 C CA  . ALA A 344 ? 0.23633 0.25308 0.25797 -0.00680 0.00899  -0.01274 344 ALA A CA  
2701 C C   . ALA A 344 ? 0.25751 0.27379 0.27652 -0.00588 0.00874  -0.01262 344 ALA A C   
2702 O O   . ALA A 344 ? 0.28988 0.30583 0.30791 -0.00547 0.00982  -0.01219 344 ALA A O   
2703 C CB  . ALA A 344 ? 0.27739 0.29243 0.29777 -0.00736 0.00945  -0.01263 344 ALA A CB  
2704 N N   . ILE A 345 ? 0.30543 0.32159 0.32318 -0.00559 0.00740  -0.01302 345 ILE A N   
2705 C CA  . ILE A 345 ? 0.24180 0.25760 0.25735 -0.00473 0.00715  -0.01286 345 ILE A CA  
2706 C C   . ILE A 345 ? 0.31426 0.33158 0.33126 -0.00419 0.00705  -0.01264 345 ILE A C   
2707 O O   . ILE A 345 ? 0.32077 0.33786 0.33674 -0.00354 0.00766  -0.01231 345 ILE A O   
2708 C CB  . ILE A 345 ? 0.24702 0.26219 0.26080 -0.00465 0.00594  -0.01334 345 ILE A CB  
2709 C CG1 . ILE A 345 ? 0.24962 0.26316 0.26233 -0.00512 0.00624  -0.01360 345 ILE A CG1 
2710 C CG2 . ILE A 345 ? 0.25194 0.26682 0.26372 -0.00378 0.00575  -0.01309 345 ILE A CG2 
2711 C CD1 . ILE A 345 ? 0.23294 0.24570 0.24406 -0.00515 0.00536  -0.01426 345 ILE A CD1 
2712 N N   . MET A 346 ? 0.34913 0.36799 0.36877 -0.00448 0.00621  -0.01281 346 MET A N   
2713 C CA  . MET A 346 ? 0.26084 0.28124 0.28260 -0.00398 0.00609  -0.01252 346 MET A CA  
2714 C C   . MET A 346 ? 0.34297 0.36360 0.36618 -0.00388 0.00794  -0.01225 346 MET A C   
2715 O O   . MET A 346 ? 0.34756 0.36878 0.37146 -0.00324 0.00840  -0.01204 346 MET A O   
2716 C CB  . MET A 346 ? 0.35072 0.37269 0.37538 -0.00442 0.00464  -0.01266 346 MET A CB  
2717 C CG  . MET A 346 ? 0.37738 0.39895 0.40018 -0.00468 0.00279  -0.01301 346 MET A CG  
2718 S SD  . MET A 346 ? 0.19381 0.21480 0.21341 -0.00378 0.00212  -0.01277 346 MET A SD  
2719 C CE  . MET A 346 ? 0.34036 0.36326 0.36312 -0.00317 0.00175  -0.01211 346 MET A CE  
2720 N N   . THR A 347 ? 0.26206 0.28213 0.28568 -0.00454 0.00909  -0.01227 347 THR A N   
2721 C CA  . THR A 347 ? 0.24451 0.26441 0.26867 -0.00455 0.01108  -0.01203 347 THR A CA  
2722 C C   . THR A 347 ? 0.29028 0.30856 0.31084 -0.00406 0.01183  -0.01184 347 THR A C   
2723 O O   . THR A 347 ? 0.23122 0.24951 0.25175 -0.00367 0.01299  -0.01176 347 THR A O   
2724 C CB  . THR A 347 ? 0.24872 0.26828 0.27395 -0.00548 0.01207  -0.01197 347 THR A CB  
2725 O OG1 . THR A 347 ? 0.25472 0.27586 0.28372 -0.00596 0.01132  -0.01215 347 THR A OG1 
2726 C CG2 . THR A 347 ? 0.29988 0.31902 0.32511 -0.00559 0.01432  -0.01171 347 THR A CG2 
2727 N N   . GLN A 348 ? 0.32037 0.33721 0.33806 -0.00409 0.01116  -0.01179 348 GLN A N   
2728 C CA  . GLN A 348 ? 0.27438 0.28972 0.28891 -0.00363 0.01152  -0.01154 348 GLN A CA  
2729 C C   . GLN A 348 ? 0.30292 0.31884 0.31722 -0.00273 0.01095  -0.01159 348 GLN A C   
2730 O O   . GLN A 348 ? 0.32349 0.33853 0.33600 -0.00231 0.01153  -0.01143 348 GLN A O   
2731 C CB  . GLN A 348 ? 0.32407 0.33793 0.33636 -0.00382 0.01079  -0.01145 348 GLN A CB  
2732 C CG  . GLN A 348 ? 0.22300 0.23518 0.23235 -0.00350 0.01106  -0.01106 348 GLN A CG  
2733 C CD  . GLN A 348 ? 0.29749 0.30835 0.30538 -0.00363 0.01031  -0.01094 348 GLN A CD  
2734 O OE1 . GLN A 348 ? 0.25568 0.26690 0.26408 -0.00356 0.00939  -0.01133 348 GLN A OE1 
2735 N NE2 . GLN A 348 ? 0.35279 0.36202 0.35886 -0.00385 0.01072  -0.01040 348 GLN A NE2 
2736 N N   . LEU A 349 ? 0.28261 0.29992 0.29866 -0.00249 0.00974  -0.01176 349 LEU A N   
2737 C CA  . LEU A 349 ? 0.26735 0.28527 0.28346 -0.00166 0.00912  -0.01167 349 LEU A CA  
2738 C C   . LEU A 349 ? 0.31651 0.33526 0.33464 -0.00133 0.01024  -0.01165 349 LEU A C   
2739 O O   . LEU A 349 ? 0.28263 0.30095 0.29977 -0.00071 0.01059  -0.01158 349 LEU A O   
2740 C CB  . LEU A 349 ? 0.23247 0.25154 0.24974 -0.00163 0.00741  -0.01174 349 LEU A CB  
2741 C CG  . LEU A 349 ? 0.24907 0.26903 0.26700 -0.00087 0.00660  -0.01147 349 LEU A CG  
2742 C CD1 . LEU A 349 ? 0.25188 0.27059 0.26701 -0.00023 0.00671  -0.01129 349 LEU A CD1 
2743 C CD2 . LEU A 349 ? 0.34106 0.36198 0.35976 -0.00105 0.00479  -0.01144 349 LEU A CD2 
2744 N N   . VAL A 350 ? 0.31152 0.33143 0.33271 -0.00176 0.01090  -0.01176 350 VAL A N   
2745 C CA  . VAL A 350 ? 0.29812 0.31887 0.32177 -0.00145 0.01219  -0.01183 350 VAL A CA  
2746 C C   . VAL A 350 ? 0.24103 0.26043 0.26297 -0.00167 0.01429  -0.01197 350 VAL A C   
2747 O O   . VAL A 350 ? 0.30163 0.32127 0.32480 -0.00136 0.01563  -0.01217 350 VAL A O   
2748 C CB  . VAL A 350 ? 0.30721 0.32986 0.33541 -0.00180 0.01211  -0.01185 350 VAL A CB  
2749 C CG1 . VAL A 350 ? 0.26396 0.28786 0.29362 -0.00166 0.00980  -0.01166 350 VAL A CG1 
2750 C CG2 . VAL A 350 ? 0.27731 0.29967 0.30588 -0.00274 0.01291  -0.01193 350 VAL A CG2 
2751 N N   A THR A 351 ? 0.26811 0.28598 0.28721 -0.00225 0.01462  -0.01186 351 THR A N   
2752 N N   B THR A 351 ? 0.26701 0.28488 0.28611 -0.00225 0.01461  -0.01186 351 THR A N   
2753 C CA  A THR A 351 ? 0.28859 0.30489 0.30539 -0.00261 0.01641  -0.01186 351 THR A CA  
2754 C CA  B THR A 351 ? 0.28775 0.30405 0.30455 -0.00262 0.01640  -0.01185 351 THR A CA  
2755 C C   A THR A 351 ? 0.27917 0.29371 0.29209 -0.00224 0.01610  -0.01174 351 THR A C   
2756 C C   B THR A 351 ? 0.28069 0.29523 0.29363 -0.00224 0.01609  -0.01174 351 THR A C   
2757 O O   A THR A 351 ? 0.30066 0.31435 0.31226 -0.00207 0.01725  -0.01193 351 THR A O   
2758 O O   B THR A 351 ? 0.30021 0.31394 0.31189 -0.00207 0.01725  -0.01194 351 THR A O   
2759 C CB  A THR A 351 ? 0.30400 0.31961 0.32026 -0.00357 0.01697  -0.01162 351 THR A CB  
2760 C CB  B THR A 351 ? 0.30531 0.32091 0.32152 -0.00358 0.01689  -0.01161 351 THR A CB  
2761 O OG1 A THR A 351 ? 0.28930 0.30441 0.30426 -0.00371 0.01536  -0.01141 351 THR A OG1 
2762 O OG1 B THR A 351 ? 0.28654 0.30378 0.30665 -0.00397 0.01721  -0.01171 351 THR A OG1 
2763 C CG2 A THR A 351 ? 0.28523 0.30248 0.30556 -0.00402 0.01769  -0.01174 351 THR A CG2 
2764 C CG2 B THR A 351 ? 0.33232 0.34614 0.34577 -0.00408 0.01868  -0.01146 351 THR A CG2 
2765 N N   . TRP A 352 ? 0.28852 0.30242 0.29968 -0.00215 0.01458  -0.01147 352 TRP A N   
2766 C CA  . TRP A 352 ? 0.29920 0.31149 0.30715 -0.00182 0.01410  -0.01127 352 TRP A CA  
2767 C C   . TRP A 352 ? 0.28262 0.29554 0.29097 -0.00091 0.01299  -0.01134 352 TRP A C   
2768 O O   . TRP A 352 ? 0.32474 0.33670 0.33138 -0.00051 0.01307  -0.01132 352 TRP A O   
2769 C CB  . TRP A 352 ? 0.32938 0.34044 0.33542 -0.00225 0.01328  -0.01086 352 TRP A CB  
2770 C CG  . TRP A 352 ? 0.31038 0.32018 0.31507 -0.00313 0.01427  -0.01055 352 TRP A CG  
2771 C CD1 . TRP A 352 ? 0.31251 0.32236 0.31767 -0.00366 0.01589  -0.01064 352 TRP A CD1 
2772 C CD2 . TRP A 352 ? 0.28713 0.29536 0.28986 -0.00362 0.01377  -0.01002 352 TRP A CD2 
2773 N NE1 . TRP A 352 ? 0.27725 0.28561 0.28055 -0.00449 0.01639  -0.01014 352 TRP A NE1 
2774 C CE2 . TRP A 352 ? 0.35247 0.35984 0.35438 -0.00447 0.01500  -0.00971 352 TRP A CE2 
2775 C CE3 . TRP A 352 ? 0.26322 0.27068 0.26503 -0.00342 0.01246  -0.00973 352 TRP A CE3 
2776 C CZ2 . TRP A 352 ? 0.36307 0.36882 0.36324 -0.00514 0.01477  -0.00902 352 TRP A CZ2 
2777 C CZ3 . TRP A 352 ? 0.24817 0.25408 0.24860 -0.00403 0.01229  -0.00913 352 TRP A CZ3 
2778 C CH2 . TRP A 352 ? 0.35715 0.36222 0.35677 -0.00489 0.01334  -0.00872 352 TRP A CH2 
2779 N N   . GLY A 353 ? 0.27113 0.28554 0.28157 -0.00065 0.01189  -0.01137 353 GLY A N   
2780 C CA  . GLY A 353 ? 0.27055 0.28542 0.28107 0.00012  0.01074  -0.01127 353 GLY A CA  
2781 C C   . GLY A 353 ? 0.31085 0.32469 0.31915 0.00023  0.00968  -0.01102 353 GLY A C   
2782 O O   . GLY A 353 ? 0.28041 0.29431 0.28831 0.00085  0.00892  -0.01086 353 GLY A O   
2783 N N   . TRP A 354 ? 0.23813 0.25102 0.24522 -0.00036 0.00968  -0.01095 354 TRP A N   
2784 C CA  . TRP A 354 ? 0.27238 0.28421 0.27777 -0.00027 0.00888  -0.01075 354 TRP A CA  
2785 C C   . TRP A 354 ? 0.29358 0.30514 0.29913 -0.00096 0.00876  -0.01086 354 TRP A C   
2786 O O   . TRP A 354 ? 0.25232 0.26368 0.25824 -0.00158 0.00949  -0.01086 354 TRP A O   
2787 C CB  . TRP A 354 ? 0.34313 0.35327 0.34637 -0.00016 0.00913  -0.01039 354 TRP A CB  
2788 C CG  . TRP A 354 ? 0.28651 0.29553 0.28858 -0.00010 0.00842  -0.01011 354 TRP A CG  
2789 C CD1 . TRP A 354 ? 0.30439 0.31322 0.30604 0.00051  0.00777  -0.00995 354 TRP A CD1 
2790 C CD2 . TRP A 354 ? 0.25733 0.26528 0.25885 -0.00067 0.00841  -0.00993 354 TRP A CD2 
2791 N NE1 . TRP A 354 ? 0.28009 0.28781 0.28109 0.00038  0.00744  -0.00973 354 TRP A NE1 
2792 C CE2 . TRP A 354 ? 0.23890 0.24605 0.23987 -0.00033 0.00777  -0.00971 354 TRP A CE2 
2793 C CE3 . TRP A 354 ? 0.27772 0.28528 0.27937 -0.00143 0.00891  -0.00988 354 TRP A CE3 
2794 C CZ2 . TRP A 354 ? 0.24082 0.24682 0.24161 -0.00069 0.00762  -0.00949 354 TRP A CZ2 
2795 C CZ3 . TRP A 354 ? 0.20345 0.20983 0.20475 -0.00181 0.00866  -0.00960 354 TRP A CZ3 
2796 C CH2 . TRP A 354 ? 0.19445 0.20007 0.19542 -0.00142 0.00801  -0.00943 354 TRP A CH2 
2797 N N   . MET A 355 ? 0.28363 0.29512 0.28891 -0.00088 0.00792  -0.01099 355 MET A N   
2798 C CA  . MET A 355 ? 0.26733 0.27830 0.27268 -0.00149 0.00778  -0.01122 355 MET A CA  
2799 C C   . MET A 355 ? 0.29370 0.30346 0.29773 -0.00126 0.00739  -0.01115 355 MET A C   
2800 O O   . MET A 355 ? 0.29196 0.30158 0.29523 -0.00063 0.00710  -0.01096 355 MET A O   
2801 C CB  . MET A 355 ? 0.29358 0.30585 0.30045 -0.00184 0.00722  -0.01173 355 MET A CB  
2802 C CG  . MET A 355 ? 0.26328 0.27698 0.27221 -0.00203 0.00753  -0.01177 355 MET A CG  
2803 S SD  . MET A 355 ? 0.22459 0.23985 0.23459 -0.00132 0.00685  -0.01170 355 MET A SD  
2804 C CE  . MET A 355 ? 0.22345 0.23916 0.23324 -0.00155 0.00537  -0.01207 355 MET A CE  
2805 N N   . HIS A 356 ? 0.29561 0.30447 0.29966 -0.00177 0.00747  -0.01129 356 HIS A N   
2806 C CA  . HIS A 356 ? 0.22841 0.23614 0.23175 -0.00159 0.00725  -0.01134 356 HIS A CA  
2807 C C   . HIS A 356 ? 0.23402 0.24238 0.23709 -0.00134 0.00677  -0.01191 356 HIS A C   
2808 O O   . HIS A 356 ? 0.32530 0.33482 0.32890 -0.00157 0.00638  -0.01232 356 HIS A O   
2809 C CB  . HIS A 356 ? 0.23666 0.24334 0.24051 -0.00223 0.00748  -0.01145 356 HIS A CB  
2810 C CG  . HIS A 356 ? 0.23937 0.24466 0.24295 -0.00202 0.00749  -0.01136 356 HIS A CG  
2811 N ND1 . HIS A 356 ? 0.27908 0.28316 0.28250 -0.00192 0.00755  -0.01056 356 HIS A ND1 
2812 C CD2 . HIS A 356 ? 0.24860 0.25347 0.25217 -0.00193 0.00747  -0.01198 356 HIS A CD2 
2813 C CE1 . HIS A 356 ? 0.28796 0.29105 0.29175 -0.00172 0.00757  -0.01063 356 HIS A CE1 
2814 N NE2 . HIS A 356 ? 0.23592 0.23944 0.23975 -0.00171 0.00766  -0.01155 356 HIS A NE2 
2815 N N   . HIS A 357 ? 0.25785 0.26539 0.26011 -0.00091 0.00676  -0.01187 357 HIS A N   
2816 C CA  . HIS A 357 ? 0.29333 0.30123 0.29484 -0.00072 0.00644  -0.01235 357 HIS A CA  
2817 C C   . HIS A 357 ? 0.25825 0.26615 0.25978 -0.00141 0.00626  -0.01323 357 HIS A C   
2818 O O   . HIS A 357 ? 0.17138 0.18016 0.17247 -0.00158 0.00565  -0.01361 357 HIS A O   
2819 C CB  . HIS A 357 ? 0.28324 0.29006 0.28406 -0.00022 0.00677  -0.01217 357 HIS A CB  
2820 C CG  . HIS A 357 ? 0.21244 0.21949 0.21209 -0.00002 0.00663  -0.01252 357 HIS A CG  
2821 N ND1 . HIS A 357 ? 0.27096 0.27694 0.27000 0.00019  0.00719  -0.01272 357 HIS A ND1 
2822 C CD2 . HIS A 357 ? 0.24741 0.25556 0.24636 -0.00004 0.00600  -0.01264 357 HIS A CD2 
2823 C CE1 . HIS A 357 ? 0.31857 0.32490 0.31619 0.00024  0.00701  -0.01298 357 HIS A CE1 
2824 N NE2 . HIS A 357 ? 0.30541 0.31304 0.30292 0.00010  0.00616  -0.01288 357 HIS A NE2 
2825 N N   . LEU A 358 ? 0.29245 0.29929 0.29454 -0.00186 0.00668  -0.01353 358 LEU A N   
2826 C CA  . LEU A 358 ? 0.19504 0.20175 0.19731 -0.00259 0.00652  -0.01446 358 LEU A CA  
2827 C C   . LEU A 358 ? 0.23757 0.24557 0.24093 -0.00311 0.00600  -0.01452 358 LEU A C   
2828 O O   . LEU A 358 ? 0.23472 0.24307 0.23810 -0.00367 0.00545  -0.01526 358 LEU A O   
2829 C CB  . LEU A 358 ? 0.25994 0.26515 0.26298 -0.00292 0.00714  -0.01470 358 LEU A CB  
2830 C CG  . LEU A 358 ? 0.18310 0.18695 0.18555 -0.00257 0.00774  -0.01498 358 LEU A CG  
2831 C CD1 . LEU A 358 ? 0.21062 0.21305 0.21446 -0.00291 0.00830  -0.01516 358 LEU A CD1 
2832 C CD2 . LEU A 358 ? 0.17547 0.17930 0.17626 -0.00269 0.00765  -0.01597 358 LEU A CD2 
2833 N N   . ALA A 359 ? 0.24105 0.24969 0.24536 -0.00297 0.00619  -0.01377 359 ALA A N   
2834 C CA  . ALA A 359 ? 0.24299 0.25300 0.24872 -0.00337 0.00589  -0.01378 359 ALA A CA  
2835 C C   . ALA A 359 ? 0.21498 0.22637 0.22060 -0.00313 0.00505  -0.01385 359 ALA A C   
2836 O O   . ALA A 359 ? 0.17159 0.18397 0.17828 -0.00363 0.00436  -0.01421 359 ALA A O   
2837 C CB  . ALA A 359 ? 0.21008 0.22024 0.21658 -0.00328 0.00659  -0.01302 359 ALA A CB  
2838 N N   . ARG A 360 ? 0.18623 0.19770 0.19076 -0.00239 0.00499  -0.01344 360 ARG A N   
2839 C CA  . ARG A 360 ? 0.22383 0.23643 0.22814 -0.00215 0.00409  -0.01338 360 ARG A CA  
2840 C C   . ARG A 360 ? 0.22898 0.24118 0.23182 -0.00256 0.00335  -0.01407 360 ARG A C   
2841 O O   . ARG A 360 ? 0.28990 0.30306 0.29271 -0.00273 0.00228  -0.01409 360 ARG A O   
2842 C CB  . ARG A 360 ? 0.22266 0.23526 0.22618 -0.00127 0.00427  -0.01273 360 ARG A CB  
2843 C CG  . ARG A 360 ? 0.22211 0.23468 0.22645 -0.00090 0.00505  -0.01217 360 ARG A CG  
2844 C CD  . ARG A 360 ? 0.19894 0.21158 0.20271 -0.00008 0.00506  -0.01161 360 ARG A CD  
2845 N NE  . ARG A 360 ? 0.30293 0.31502 0.30683 0.00018  0.00581  -0.01122 360 ARG A NE  
2846 C CZ  . ARG A 360 ? 0.22486 0.23699 0.22861 0.00081  0.00590  -0.01078 360 ARG A CZ  
2847 N NH1 . ARG A 360 ? 0.21214 0.22494 0.21590 0.00130  0.00534  -0.01057 360 ARG A NH1 
2848 N NH2 . ARG A 360 ? 0.25966 0.27102 0.26313 0.00088  0.00652  -0.01053 360 ARG A NH2 
2849 N N   . HIS A 361 ? 0.22048 0.23118 0.22209 -0.00277 0.00389  -0.01463 361 HIS A N   
2850 C CA  . HIS A 361 ? 0.23371 0.24373 0.23356 -0.00327 0.00342  -0.01548 361 HIS A CA  
2851 C C   . HIS A 361 ? 0.25692 0.26745 0.25766 -0.00419 0.00254  -0.01614 361 HIS A C   
2852 O O   . HIS A 361 ? 0.26824 0.27898 0.26776 -0.00464 0.00147  -0.01657 361 HIS A O   
2853 C CB  . HIS A 361 ? 0.23850 0.24672 0.23732 -0.00325 0.00447  -0.01601 361 HIS A CB  
2854 C CG  . HIS A 361 ? 0.30103 0.30857 0.29812 -0.00261 0.00496  -0.01577 361 HIS A CG  
2855 N ND1 . HIS A 361 ? 0.24826 0.25469 0.24321 -0.00285 0.00523  -0.01655 361 HIS A ND1 
2856 C CD2 . HIS A 361 ? 0.24755 0.25529 0.24478 -0.00179 0.00531  -0.01487 361 HIS A CD2 
2857 C CE1 . HIS A 361 ? 0.30364 0.30970 0.29764 -0.00218 0.00580  -0.01605 361 HIS A CE1 
2858 N NE2 . HIS A 361 ? 0.36252 0.36939 0.35798 -0.00153 0.00577  -0.01502 361 HIS A NE2 
2859 N N   . SER A 362 ? 0.24311 0.25380 0.24594 -0.00454 0.00291  -0.01617 362 SER A N   
2860 C CA  . SER A 362 ? 0.26709 0.27818 0.27114 -0.00546 0.00214  -0.01680 362 SER A CA  
2861 C C   . SER A 362 ? 0.28908 0.30200 0.29447 -0.00559 0.00087  -0.01640 362 SER A C   
2862 O O   . SER A 362 ? 0.28499 0.29819 0.29015 -0.00629 -0.00042 -0.01693 362 SER A O   
2863 C CB  . SER A 362 ? 0.20266 0.21349 0.20882 -0.00578 0.00297  -0.01674 362 SER A CB  
2864 O OG  . SER A 362 ? 0.25016 0.25926 0.25548 -0.00573 0.00395  -0.01705 362 SER A OG  
2865 N N   . VAL A 363 ? 0.26226 0.27636 0.26915 -0.00496 0.00117  -0.01547 363 VAL A N   
2866 C CA  . VAL A 363 ? 0.27204 0.28793 0.28092 -0.00501 0.00009  -0.01502 363 VAL A CA  
2867 C C   . VAL A 363 ? 0.32390 0.34009 0.33103 -0.00482 -0.00119 -0.01484 363 VAL A C   
2868 O O   . VAL A 363 ? 0.32241 0.33970 0.33060 -0.00524 -0.00270 -0.01473 363 VAL A O   
2869 C CB  . VAL A 363 ? 0.29280 0.30969 0.30388 -0.00440 0.00105  -0.01421 363 VAL A CB  
2870 C CG1 . VAL A 363 ? 0.30581 0.32256 0.31875 -0.00484 0.00210  -0.01431 363 VAL A CG1 
2871 C CG2 . VAL A 363 ? 0.26242 0.27857 0.27171 -0.00349 0.00195  -0.01374 363 VAL A CG2 
2872 N N   . ALA A 364 ? 0.33254 0.34775 0.33707 -0.00423 -0.00068 -0.01470 364 ALA A N   
2873 C CA  . ALA A 364 ? 0.30867 0.32398 0.31121 -0.00411 -0.00179 -0.01444 364 ALA A CA  
2874 C C   . ALA A 364 ? 0.29199 0.30633 0.29214 -0.00504 -0.00276 -0.01534 364 ALA A C   
2875 O O   . ALA A 364 ? 0.35976 0.37455 0.35892 -0.00541 -0.00434 -0.01515 364 ALA A O   
2876 C CB  . ALA A 364 ? 0.25717 0.27168 0.25784 -0.00324 -0.00081 -0.01400 364 ALA A CB  
2877 N N   . CYS A 365 ? 0.31633 0.32923 0.31546 -0.00547 -0.00189 -0.01633 365 CYS A N   
2878 C CA  . CYS A 365 ? 0.32648 0.33825 0.32330 -0.00643 -0.00267 -0.01742 365 CYS A CA  
2879 C C   . CYS A 365 ? 0.31682 0.32956 0.31556 -0.00736 -0.00426 -0.01769 365 CYS A C   
2880 O O   . CYS A 365 ? 0.34429 0.35676 0.34123 -0.00816 -0.00581 -0.01813 365 CYS A O   
2881 C CB  . CYS A 365 ? 0.33036 0.34027 0.32608 -0.00659 -0.00117 -0.01844 365 CYS A CB  
2882 S SG  . CYS A 365 ? 0.36807 0.37618 0.36073 -0.00780 -0.00175 -0.02009 365 CYS A SG  
2883 N N   . PHE A 366 ? 0.27081 0.28463 0.27317 -0.00732 -0.00392 -0.01740 366 PHE A N   
2884 C CA  . PHE A 366 ? 0.27891 0.29378 0.28378 -0.00819 -0.00532 -0.01759 366 PHE A CA  
2885 C C   . PHE A 366 ? 0.34928 0.36572 0.35509 -0.00824 -0.00722 -0.01676 366 PHE A C   
2886 O O   . PHE A 366 ? 0.27407 0.29086 0.28028 -0.00917 -0.00907 -0.01706 366 PHE A O   
2887 C CB  . PHE A 366 ? 0.26190 0.27759 0.27054 -0.00808 -0.00422 -0.01731 366 PHE A CB  
2888 C CG  . PHE A 366 ? 0.24619 0.26283 0.25783 -0.00902 -0.00537 -0.01757 366 PHE A CG  
2889 C CD1 . PHE A 366 ? 0.32699 0.34252 0.33850 -0.00993 -0.00544 -0.01863 366 PHE A CD1 
2890 C CD2 . PHE A 366 ? 0.27969 0.29833 0.29465 -0.00898 -0.00635 -0.01674 366 PHE A CD2 
2891 C CE1 . PHE A 366 ? 0.35478 0.37119 0.36931 -0.01084 -0.00655 -0.01885 366 PHE A CE1 
2892 C CE2 . PHE A 366 ? 0.31732 0.33692 0.33552 -0.00985 -0.00742 -0.01692 366 PHE A CE2 
2893 C CZ  . PHE A 366 ? 0.39535 0.41384 0.41328 -0.01080 -0.00755 -0.01796 366 PHE A CZ  
2894 N N   . LEU A 367 ? 0.36171 0.37907 0.36805 -0.00727 -0.00689 -0.01569 367 LEU A N   
2895 C CA  . LEU A 367 ? 0.33432 0.35323 0.34212 -0.00722 -0.00866 -0.01475 367 LEU A CA  
2896 C C   . LEU A 367 ? 0.34226 0.36034 0.34621 -0.00762 -0.01023 -0.01475 367 LEU A C   
2897 O O   . LEU A 367 ? 0.32523 0.34414 0.32983 -0.00822 -0.01242 -0.01434 367 LEU A O   
2898 C CB  . LEU A 367 ? 0.28073 0.30078 0.29057 -0.00605 -0.00766 -0.01367 367 LEU A CB  
2899 C CG  . LEU A 367 ? 0.31378 0.33550 0.32580 -0.00580 -0.00926 -0.01255 367 LEU A CG  
2900 C CD1 . LEU A 367 ? 0.37145 0.39479 0.38798 -0.00636 -0.01032 -0.01240 367 LEU A CD1 
2901 C CD2 . LEU A 367 ? 0.28861 0.31089 0.30165 -0.00459 -0.00803 -0.01171 367 LEU A CD2 
2902 N N   . THR A 368 ? 0.37271 0.38912 0.37269 -0.00736 -0.00916 -0.01515 368 THR A N   
2903 C CA  . THR A 368 ? 0.38087 0.39636 0.37681 -0.00767 -0.01028 -0.01504 368 THR A CA  
2904 C C   . THR A 368 ? 0.36652 0.38021 0.35894 -0.00885 -0.01081 -0.01642 368 THR A C   
2905 O O   . THR A 368 ? 0.38658 0.40051 0.38005 -0.00984 -0.01227 -0.01695 368 THR A O   
2906 C CB  . THR A 368 ? 0.37458 0.38930 0.36832 -0.00668 -0.00871 -0.01459 368 THR A CB  
2907 O OG1 . THR A 368 ? 0.35024 0.36354 0.34296 -0.00647 -0.00661 -0.01554 368 THR A OG1 
2908 C CG2 . THR A 368 ? 0.26228 0.27864 0.25925 -0.00558 -0.00834 -0.01331 368 THR A CG2 
2909 N N   . ARG A 369 ? 0.36034 0.37214 0.34871 -0.00878 -0.00953 -0.01706 369 ARG A N   
2910 C CA  . ARG A 369 ? 0.35525 0.36503 0.33948 -0.00988 -0.00987 -0.01842 369 ARG A CA  
2911 C C   . ARG A 369 ? 0.39700 0.40606 0.38245 -0.01059 -0.00944 -0.01985 369 ARG A C   
2912 O O   . ARG A 369 ? 0.43267 0.43998 0.41500 -0.01160 -0.00972 -0.02120 369 ARG A O   
2913 C CB  . ARG A 369 ? 0.44105 0.44901 0.42134 -0.00947 -0.00803 -0.01879 369 ARG A CB  
2914 C CG  . ARG A 369 ? 0.40188 0.40963 0.38406 -0.00842 -0.00551 -0.01889 369 ARG A CG  
2915 C CD  . ARG A 369 ? 0.42907 0.43488 0.40775 -0.00816 -0.00366 -0.01945 369 ARG A CD  
2916 N NE  . ARG A 369 ? 0.39601 0.40158 0.37684 -0.00723 -0.00151 -0.01949 369 ARG A NE  
2917 C CZ  . ARG A 369 ? 0.40723 0.41186 0.38919 -0.00743 -0.00038 -0.02057 369 ARG A CZ  
2918 N NH1 . ARG A 369 ? 0.34524 0.34905 0.32647 -0.00850 -0.00103 -0.02184 369 ARG A NH1 
2919 N NH2 . ARG A 369 ? 0.30558 0.31004 0.28954 -0.00658 0.00133  -0.02032 369 ARG A NH2 
2920 N N   . GLY A 370 ? 0.31710 0.32737 0.30692 -0.01012 -0.00870 -0.01960 370 GLY A N   
2921 C CA  . GLY A 370 ? 0.34290 0.35247 0.33417 -0.01072 -0.00812 -0.02078 370 GLY A CA  
2922 C C   . GLY A 370 ? 0.36948 0.38000 0.36309 -0.01176 -0.01015 -0.02100 370 GLY A C   
2923 O O   . GLY A 370 ? 0.37536 0.38457 0.36733 -0.01288 -0.01089 -0.02230 370 GLY A O   
2924 N N   . ASP A 371 ? 0.32744 0.34017 0.32506 -0.01143 -0.01102 -0.01979 371 ASP A N   
2925 C CA  . ASP A 371 ? 0.33692 0.35076 0.33783 -0.01233 -0.01271 -0.01990 371 ASP A CA  
2926 C C   . ASP A 371 ? 0.26799 0.28363 0.27056 -0.01247 -0.01505 -0.01869 371 ASP A C   
2927 O O   . ASP A 371 ? 0.20093 0.21644 0.20270 -0.01358 -0.01741 -0.01898 371 ASP A O   
2928 C CB  . ASP A 371 ? 0.26044 0.27528 0.26592 -0.01195 -0.01124 -0.01970 371 ASP A CB  
2929 C CG  . ASP A 371 ? 0.36443 0.37750 0.36895 -0.01212 -0.00945 -0.02088 371 ASP A CG  
2930 O OD1 . ASP A 371 ? 0.42552 0.43739 0.42766 -0.01141 -0.00774 -0.02102 371 ASP A OD1 
2931 O OD2 . ASP A 371 ? 0.37769 0.39058 0.38416 -0.01296 -0.00978 -0.02160 371 ASP A OD2 
2932 N N   . LEU A 372 ? 0.27436 0.29162 0.27937 -0.01137 -0.01451 -0.01733 372 LEU A N   
2933 C CA  . LEU A 372 ? 0.28979 0.30902 0.29777 -0.01138 -0.01653 -0.01608 372 LEU A CA  
2934 C C   . LEU A 372 ? 0.30318 0.32206 0.30769 -0.01142 -0.01818 -0.01538 372 LEU A C   
2935 O O   . LEU A 372 ? 0.22578 0.24592 0.23212 -0.01182 -0.02055 -0.01446 372 LEU A O   
2936 C CB  . LEU A 372 ? 0.33015 0.35120 0.34259 -0.01020 -0.01509 -0.01501 372 LEU A CB  
2937 C CG  . LEU A 372 ? 0.33603 0.35736 0.35162 -0.01010 -0.01316 -0.01549 372 LEU A CG  
2938 C CD1 . LEU A 372 ? 0.32484 0.34783 0.34438 -0.00905 -0.01178 -0.01447 372 LEU A CD1 
2939 C CD2 . LEU A 372 ? 0.38601 0.40772 0.40416 -0.01130 -0.01452 -0.01608 372 LEU A CD2 
2940 N N   . TYR A 373 ? 0.33455 0.35176 0.33434 -0.01105 -0.01699 -0.01570 373 TYR A N   
2941 C CA  . TYR A 373 ? 0.35006 0.36668 0.34600 -0.01114 -0.01828 -0.01502 373 TYR A CA  
2942 C C   . TYR A 373 ? 0.34232 0.36089 0.34128 -0.01029 -0.01911 -0.01324 373 TYR A C   
2943 O O   . TYR A 373 ? 0.39483 0.41350 0.39217 -0.01062 -0.02114 -0.01232 373 TYR A O   
2944 C CB  . TYR A 373 ? 0.34767 0.36324 0.34051 -0.01268 -0.02086 -0.01559 373 TYR A CB  
2945 C CG  . TYR A 373 ? 0.32953 0.34289 0.31579 -0.01308 -0.02081 -0.01601 373 TYR A CG  
2946 C CD1 . TYR A 373 ? 0.40535 0.41665 0.38814 -0.01301 -0.01845 -0.01741 373 TYR A CD1 
2947 C CD2 . TYR A 373 ? 0.41954 0.43280 0.40316 -0.01358 -0.02306 -0.01497 373 TYR A CD2 
2948 C CE1 . TYR A 373 ? 0.48378 0.49300 0.46067 -0.01340 -0.01810 -0.01787 373 TYR A CE1 
2949 C CE2 . TYR A 373 ? 0.43776 0.44887 0.41506 -0.01403 -0.02283 -0.01534 373 TYR A CE2 
2950 C CZ  . TYR A 373 ? 0.40839 0.41749 0.38237 -0.01393 -0.02023 -0.01684 373 TYR A CZ  
2951 O OH  . TYR A 373 ? 0.37326 0.38016 0.34108 -0.01438 -0.01971 -0.01727 373 TYR A OH  
2952 N N   . VAL A 374 ? 0.31875 0.33875 0.32202 -0.00923 -0.01754 -0.01274 374 VAL A N   
2953 C CA  . VAL A 374 ? 0.36614 0.38788 0.37259 -0.00830 -0.01791 -0.01121 374 VAL A CA  
2954 C C   . VAL A 374 ? 0.31848 0.33937 0.32193 -0.00734 -0.01649 -0.01075 374 VAL A C   
2955 O O   . VAL A 374 ? 0.27142 0.29086 0.27212 -0.00704 -0.01448 -0.01158 374 VAL A O   
2956 C CB  . VAL A 374 ? 0.35992 0.38339 0.37214 -0.00768 -0.01668 -0.01103 374 VAL A CB  
2957 C CG1 . VAL A 374 ? 0.35851 0.38371 0.37435 -0.00674 -0.01696 -0.00960 374 VAL A CG1 
2958 C CG2 . VAL A 374 ? 0.39056 0.41479 0.40588 -0.00870 -0.01795 -0.01150 374 VAL A CG2 
2959 N N   . SER A 375 ? 0.30419 0.32599 0.30845 -0.00686 -0.01762 -0.00934 375 SER A N   
2960 C CA  . SER A 375 ? 0.35020 0.37127 0.35182 -0.00602 -0.01656 -0.00873 375 SER A CA  
2961 C C   . SER A 375 ? 0.31691 0.33791 0.31980 -0.00490 -0.01375 -0.00910 375 SER A C   
2962 O O   . SER A 375 ? 0.34632 0.36848 0.35329 -0.00450 -0.01290 -0.00919 375 SER A O   
2963 C CB  . SER A 375 ? 0.31641 0.33875 0.31996 -0.00562 -0.01824 -0.00703 375 SER A CB  
2964 O OG  . SER A 375 ? 0.25622 0.27788 0.25753 -0.00479 -0.01718 -0.00639 375 SER A OG  
2965 N N   . TRP A 376 ? 0.34803 0.36757 0.34731 -0.00448 -0.01231 -0.00930 376 TRP A N   
2966 C CA  . TRP A 376 ? 0.36504 0.38435 0.36521 -0.00348 -0.00990 -0.00953 376 TRP A CA  
2967 C C   . TRP A 376 ? 0.33852 0.35916 0.34193 -0.00243 -0.00967 -0.00839 376 TRP A C   
2968 O O   . TRP A 376 ? 0.31866 0.33946 0.32385 -0.00170 -0.00795 -0.00858 376 TRP A O   
2969 C CB  . TRP A 376 ? 0.34042 0.35783 0.33627 -0.00333 -0.00855 -0.00997 376 TRP A CB  
2970 C CG  . TRP A 376 ? 0.40911 0.42607 0.40222 -0.00326 -0.00939 -0.00903 376 TRP A CG  
2971 C CD1 . TRP A 376 ? 0.40101 0.41705 0.39042 -0.00419 -0.01075 -0.00905 376 TRP A CD1 
2972 C CD2 . TRP A 376 ? 0.35938 0.37669 0.35308 -0.00229 -0.00891 -0.00790 376 TRP A CD2 
2973 N NE1 . TRP A 376 ? 0.38014 0.39593 0.36772 -0.00386 -0.01110 -0.00790 376 TRP A NE1 
2974 C CE2 . TRP A 376 ? 0.40880 0.42541 0.39917 -0.00267 -0.01000 -0.00717 376 TRP A CE2 
2975 C CE3 . TRP A 376 ? 0.37045 0.38847 0.36702 -0.00120 -0.00769 -0.00745 376 TRP A CE3 
2976 C CZ2 . TRP A 376 ? 0.38432 0.40102 0.37450 -0.00195 -0.00987 -0.00593 376 TRP A CZ2 
2977 C CZ3 . TRP A 376 ? 0.36945 0.38753 0.36585 -0.00049 -0.00762 -0.00635 376 TRP A CZ3 
2978 C CH2 . TRP A 376 ? 0.36411 0.38158 0.35749 -0.00085 -0.00870 -0.00556 376 TRP A CH2 
2979 N N   . GLU A 377 ? 0.30594 0.32744 0.31011 -0.00239 -0.01141 -0.00721 377 GLU A N   
2980 C CA  . GLU A 377 ? 0.35522 0.37800 0.36295 -0.00141 -0.01123 -0.00618 377 GLU A CA  
2981 C C   . GLU A 377 ? 0.34225 0.36655 0.35495 -0.00126 -0.01093 -0.00638 377 GLU A C   
2982 O O   . GLU A 377 ? 0.35932 0.38411 0.37450 -0.00040 -0.00946 -0.00631 377 GLU A O   
2983 C CB  . GLU A 377 ? 0.35840 0.38173 0.36612 -0.00147 -0.01333 -0.00476 377 GLU A CB  
2984 C CG  . GLU A 377 ? 0.37030 0.39210 0.37302 -0.00165 -0.01352 -0.00440 377 GLU A CG  
2985 C CD  . GLU A 377 ? 0.36774 0.39010 0.37088 -0.00146 -0.01523 -0.00273 377 GLU A CD  
2986 O OE1 . GLU A 377 ? 0.44858 0.47203 0.45541 -0.00054 -0.01495 -0.00192 377 GLU A OE1 
2987 O OE2 . GLU A 377 ? 0.36855 0.39017 0.36829 -0.00228 -0.01687 -0.00221 377 GLU A OE2 
2988 N N   . ARG A 378 ? 0.31356 0.33854 0.32773 -0.00213 -0.01225 -0.00667 378 ARG A N   
2989 C CA  . ARG A 378 ? 0.30403 0.33044 0.32308 -0.00207 -0.01180 -0.00688 378 ARG A CA  
2990 C C   . ARG A 378 ? 0.33744 0.36317 0.35630 -0.00185 -0.00934 -0.00796 378 ARG A C   
2991 O O   . ARG A 378 ? 0.35804 0.38467 0.38045 -0.00142 -0.00811 -0.00802 378 ARG A O   
2992 C CB  . ARG A 378 ? 0.37368 0.40086 0.39432 -0.00315 -0.01386 -0.00694 378 ARG A CB  
2993 C CG  . ARG A 378 ? 0.35704 0.38472 0.37749 -0.00360 -0.01669 -0.00580 378 ARG A CG  
2994 C CD  . ARG A 378 ? 0.35379 0.38309 0.37880 -0.00278 -0.01724 -0.00447 378 ARG A CD  
2995 N NE  . ARG A 378 ? 0.40654 0.43519 0.42956 -0.00189 -0.01649 -0.00382 378 ARG A NE  
2996 C CZ  . ARG A 378 ? 0.42643 0.45454 0.44668 -0.00204 -0.01810 -0.00283 378 ARG A CZ  
2997 N NH1 . ARG A 378 ? 0.46168 0.48967 0.48035 -0.00309 -0.02067 -0.00237 378 ARG A NH1 
2998 N NH2 . ARG A 378 ? 0.40152 0.42908 0.42042 -0.00118 -0.01717 -0.00226 378 ARG A NH2 
2999 N N   . GLY A 379 ? 0.33773 0.36182 0.35253 -0.00218 -0.00858 -0.00879 379 GLY A N   
3000 C CA  . GLY A 379 ? 0.33075 0.35404 0.34519 -0.00195 -0.00640 -0.00960 379 GLY A CA  
3001 C C   . GLY A 379 ? 0.28954 0.31229 0.30327 -0.00094 -0.00483 -0.00932 379 GLY A C   
3002 O O   . GLY A 379 ? 0.29709 0.31967 0.31185 -0.00061 -0.00316 -0.00967 379 GLY A O   
3003 N N   . MET A 380 ? 0.31576 0.33817 0.32766 -0.00050 -0.00538 -0.00866 380 MET A N   
3004 C CA  . MET A 380 ? 0.33394 0.35585 0.34541 0.00044  -0.00407 -0.00834 380 MET A CA  
3005 C C   . MET A 380 ? 0.32125 0.34444 0.33665 0.00109  -0.00366 -0.00788 380 MET A C   
3006 O O   . MET A 380 ? 0.31363 0.33639 0.32940 0.00168  -0.00211 -0.00806 380 MET A O   
3007 C CB  . MET A 380 ? 0.31387 0.33510 0.32260 0.00068  -0.00477 -0.00768 380 MET A CB  
3008 C CG  . MET A 380 ? 0.23274 0.25333 0.24095 0.00160  -0.00353 -0.00735 380 MET A CG  
3009 S SD  . MET A 380 ? 0.32028 0.34026 0.32585 0.00185  -0.00436 -0.00637 380 MET A SD  
3010 C CE  . MET A 380 ? 0.34002 0.36171 0.34854 0.00185  -0.00639 -0.00523 380 MET A CE  
3011 N N   A GLU A 381 ? 0.32259 0.34725 0.34100 0.00097  -0.00506 -0.00729 381 GLU A N   
3012 N N   B GLU A 381 ? 0.32096 0.34563 0.33940 0.00096  -0.00505 -0.00730 381 GLU A N   
3013 C CA  A GLU A 381 ? 0.32041 0.34631 0.34307 0.00158  -0.00454 -0.00693 381 GLU A CA  
3014 C CA  B GLU A 381 ? 0.32085 0.34674 0.34351 0.00158  -0.00452 -0.00693 381 GLU A CA  
3015 C C   A GLU A 381 ? 0.31005 0.33614 0.33468 0.00145  -0.00286 -0.00775 381 GLU A C   
3016 C C   B GLU A 381 ? 0.31239 0.33855 0.33718 0.00144  -0.00290 -0.00773 381 GLU A C   
3017 O O   A GLU A 381 ? 0.30710 0.33340 0.33374 0.00205  -0.00144 -0.00783 381 GLU A O   
3018 O O   B GLU A 381 ? 0.30826 0.33475 0.33534 0.00203  -0.00156 -0.00778 381 GLU A O   
3019 C CB  A GLU A 381 ? 0.31536 0.34283 0.34126 0.00140  -0.00654 -0.00604 381 GLU A CB  
3020 C CB  B GLU A 381 ? 0.32278 0.35022 0.34861 0.00145  -0.00653 -0.00600 381 GLU A CB  
3021 C CG  A GLU A 381 ? 0.31546 0.34273 0.33953 0.00152  -0.00825 -0.00500 381 GLU A CG  
3022 C CG  B GLU A 381 ? 0.33136 0.35981 0.35950 0.00060  -0.00752 -0.00625 381 GLU A CG  
3023 C CD  A GLU A 381 ? 0.35766 0.38603 0.38337 0.00087  -0.01079 -0.00420 381 GLU A CD  
3024 C CD  B GLU A 381 ? 0.35066 0.38023 0.38056 0.00021  -0.01017 -0.00522 381 GLU A CD  
3025 O OE1 A GLU A 381 ? 0.37235 0.40163 0.40061 0.00029  -0.01127 -0.00455 381 GLU A OE1 
3026 O OE1 B GLU A 381 ? 0.36237 0.39168 0.39079 0.00050  -0.01128 -0.00432 381 GLU A OE1 
3027 O OE2 A GLU A 381 ? 0.34922 0.37750 0.37368 0.00088  -0.01239 -0.00315 381 GLU A OE2 
3028 O OE2 B GLU A 381 ? 0.34181 0.37246 0.37462 -0.00043 -0.01121 -0.00525 381 GLU A OE2 
3029 N N   . VAL A 382 ? 0.32735 0.35327 0.35133 0.00064  -0.00293 -0.00837 382 VAL A N   
3030 C CA  . VAL A 382 ? 0.33735 0.36332 0.36293 0.00042  -0.00128 -0.00905 382 VAL A CA  
3031 C C   . VAL A 382 ? 0.29843 0.32282 0.32114 0.00074  0.00054  -0.00952 382 VAL A C   
3032 O O   . VAL A 382 ? 0.31026 0.33454 0.33414 0.00098  0.00219  -0.00979 382 VAL A O   
3033 C CB  . VAL A 382 ? 0.35245 0.37864 0.37832 -0.00059 -0.00199 -0.00950 382 VAL A CB  
3034 C CG1 . VAL A 382 ? 0.26470 0.29076 0.29191 -0.00086 -0.00016 -0.01011 382 VAL A CG1 
3035 C CG2 . VAL A 382 ? 0.32562 0.35343 0.35478 -0.00096 -0.00396 -0.00897 382 VAL A CG2 
3036 N N   . PHE A 383 ? 0.26709 0.29014 0.28598 0.00071  0.00026  -0.00961 383 PHE A N   
3037 C CA  . PHE A 383 ? 0.24888 0.27043 0.26532 0.00105  0.00169  -0.00988 383 PHE A CA  
3038 C C   . PHE A 383 ? 0.28325 0.30478 0.30022 0.00193  0.00227  -0.00948 383 PHE A C   
3039 O O   . PHE A 383 ? 0.30134 0.32197 0.31759 0.00218  0.00364  -0.00973 383 PHE A O   
3040 C CB  . PHE A 383 ? 0.29303 0.31325 0.30587 0.00085  0.00128  -0.01003 383 PHE A CB  
3041 C CG  . PHE A 383 ? 0.27499 0.29456 0.28682 0.00006  0.00144  -0.01070 383 PHE A CG  
3042 C CD1 . PHE A 383 ? 0.24907 0.26953 0.26315 -0.00057 0.00129  -0.01099 383 PHE A CD1 
3043 C CD2 . PHE A 383 ? 0.18733 0.20537 0.19629 -0.00006 0.00181  -0.01102 383 PHE A CD2 
3044 C CE1 . PHE A 383 ? 0.28547 0.30525 0.29878 -0.00131 0.00143  -0.01159 383 PHE A CE1 
3045 C CE2 . PHE A 383 ? 0.24642 0.26377 0.25471 -0.00077 0.00200  -0.01165 383 PHE A CE2 
3046 C CZ  . PHE A 383 ? 0.23834 0.25654 0.24873 -0.00141 0.00179  -0.01194 383 PHE A CZ  
3047 N N   A GLU A 384 ? 0.32176 0.34414 0.33992 0.00234  0.00117  -0.00883 384 GLU A N   
3048 N N   B GLU A 384 ? 0.32062 0.34300 0.33879 0.00234  0.00117  -0.00883 384 GLU A N   
3049 C CA  A GLU A 384 ? 0.32006 0.34238 0.33900 0.00318  0.00167  -0.00846 384 GLU A CA  
3050 C CA  B GLU A 384 ? 0.32009 0.34243 0.33905 0.00318  0.00164  -0.00845 384 GLU A CA  
3051 C C   A GLU A 384 ? 0.32271 0.34556 0.34455 0.00340  0.00302  -0.00880 384 GLU A C   
3052 C C   B GLU A 384 ? 0.32573 0.34860 0.34761 0.00341  0.00299  -0.00878 384 GLU A C   
3053 O O   A GLU A 384 ? 0.32740 0.34960 0.34910 0.00395  0.00404  -0.00890 384 GLU A O   
3054 O O   B GLU A 384 ? 0.32179 0.34405 0.34360 0.00397  0.00398  -0.00887 384 GLU A O   
3055 C CB  A GLU A 384 ? 0.31294 0.33612 0.33289 0.00351  0.00010  -0.00757 384 GLU A CB  
3056 C CB  B GLU A 384 ? 0.31339 0.33661 0.33340 0.00350  0.00006  -0.00756 384 GLU A CB  
3057 C CG  A GLU A 384 ? 0.30141 0.32452 0.32242 0.00438  0.00047  -0.00712 384 GLU A CG  
3058 C CG  B GLU A 384 ? 0.31105 0.33324 0.32837 0.00393  -0.00022 -0.00709 384 GLU A CG  
3059 C CD  A GLU A 384 ? 0.34324 0.36658 0.36378 0.00465  -0.00105 -0.00611 384 GLU A CD  
3060 C CD  B GLU A 384 ? 0.31529 0.33769 0.33119 0.00363  -0.00193 -0.00641 384 GLU A CD  
3061 O OE1 A GLU A 384 ? 0.34237 0.36535 0.36035 0.00418  -0.00205 -0.00589 384 GLU A OE1 
3062 O OE1 B GLU A 384 ? 0.30047 0.32402 0.31813 0.00324  -0.00324 -0.00608 384 GLU A OE1 
3063 O OE2 A GLU A 384 ? 0.33026 0.35405 0.35293 0.00530  -0.00118 -0.00554 384 GLU A OE2 
3064 O OE2 B GLU A 384 ? 0.27179 0.29314 0.28479 0.00374  -0.00197 -0.00618 384 GLU A OE2 
3065 N N   . GLU A 385 ? 0.31399 0.33792 0.33844 0.00294  0.00313  -0.00902 385 GLU A N   
3066 C CA  . GLU A 385 ? 0.32127 0.34571 0.34866 0.00310  0.00467  -0.00939 385 GLU A CA  
3067 C C   . GLU A 385 ? 0.31724 0.34029 0.34243 0.00282  0.00651  -0.01010 385 GLU A C   
3068 O O   . GLU A 385 ? 0.20554 0.22793 0.23071 0.00319  0.00793  -0.01041 385 GLU A O   
3069 C CB  . GLU A 385 ? 0.36651 0.39264 0.39786 0.00267  0.00419  -0.00930 385 GLU A CB  
3070 C CG  . GLU A 385 ? 0.33872 0.36544 0.37347 0.00277  0.00606  -0.00973 385 GLU A CG  
3071 C CD  . GLU A 385 ? 0.44565 0.47410 0.48474 0.00230  0.00558  -0.00960 385 GLU A CD  
3072 O OE1 . GLU A 385 ? 0.36103 0.39027 0.40057 0.00193  0.00349  -0.00910 385 GLU A OE1 
3073 O OE2 . GLU A 385 ? 0.40256 0.43150 0.44458 0.00225  0.00730  -0.00999 385 GLU A OE2 
3074 N N   . HIS A 386 ? 0.34746 0.36992 0.37068 0.00213  0.00644  -0.01034 386 HIS A N   
3075 C CA  . HIS A 386 ? 0.31992 0.34121 0.34156 0.00171  0.00805  -0.01084 386 HIS A CA  
3076 C C   . HIS A 386 ? 0.28314 0.30256 0.30078 0.00178  0.00824  -0.01088 386 HIS A C   
3077 O O   . HIS A 386 ? 0.29529 0.31354 0.31151 0.00164  0.00957  -0.01115 386 HIS A O   
3078 C CB  . HIS A 386 ? 0.32967 0.35138 0.35207 0.00086  0.00798  -0.01103 386 HIS A CB  
3079 C CG  . HIS A 386 ? 0.39550 0.41898 0.42224 0.00067  0.00805  -0.01102 386 HIS A CG  
3080 N ND1 . HIS A 386 ? 0.34769 0.37255 0.37658 0.00048  0.00630  -0.01071 386 HIS A ND1 
3081 C CD2 . HIS A 386 ? 0.29751 0.32154 0.32696 0.00061  0.00968  -0.01127 386 HIS A CD2 
3082 C CE1 . HIS A 386 ? 0.34281 0.36912 0.37593 0.00033  0.00671  -0.01070 386 HIS A CE1 
3083 N NE2 . HIS A 386 ? 0.25106 0.27693 0.28471 0.00043  0.00889  -0.01106 386 HIS A NE2 
3084 N N   . LEU A 387 ? 0.25173 0.27078 0.26755 0.00194  0.00697  -0.01058 387 LEU A N   
3085 C CA  . LEU A 387 ? 0.25214 0.26949 0.26472 0.00201  0.00712  -0.01056 387 LEU A CA  
3086 C C   . LEU A 387 ? 0.34818 0.36474 0.36014 0.00259  0.00781  -0.01052 387 LEU A C   
3087 O O   . LEU A 387 ? 0.31001 0.32718 0.32317 0.00320  0.00741  -0.01028 387 LEU A O   
3088 C CB  . LEU A 387 ? 0.26305 0.28024 0.27420 0.00212  0.00582  -0.01027 387 LEU A CB  
3089 C CG  . LEU A 387 ? 0.24957 0.26665 0.25992 0.00145  0.00528  -0.01050 387 LEU A CG  
3090 C CD1 . LEU A 387 ? 0.17891 0.19569 0.18762 0.00161  0.00424  -0.01029 387 LEU A CD1 
3091 C CD2 . LEU A 387 ? 0.30866 0.32441 0.31756 0.00099  0.00616  -0.01076 387 LEU A CD2 
3092 N N   . ILE A 388 ? 0.29890 0.31401 0.30894 0.00233  0.00876  -0.01072 388 ILE A N   
3093 C CA  . ILE A 388 ? 0.30275 0.31675 0.31163 0.00274  0.00927  -0.01075 388 ILE A CA  
3094 C C   . ILE A 388 ? 0.32318 0.33636 0.33044 0.00316  0.00831  -0.01034 388 ILE A C   
3095 O O   . ILE A 388 ? 0.33487 0.34710 0.34126 0.00350  0.00847  -0.01032 388 ILE A O   
3096 C CB  . ILE A 388 ? 0.27954 0.29207 0.28655 0.00219  0.01046  -0.01105 388 ILE A CB  
3097 C CG1 . ILE A 388 ? 0.32272 0.33413 0.32760 0.00166  0.01004  -0.01078 388 ILE A CG1 
3098 C CG2 . ILE A 388 ? 0.24032 0.25359 0.24902 0.00179  0.01173  -0.01146 388 ILE A CG2 
3099 C CD1 . ILE A 388 ? 0.31894 0.32873 0.32168 0.00103  0.01094  -0.01084 388 ILE A CD1 
3100 N N   . ASP A 389 ? 0.27673 0.29015 0.28359 0.00309  0.00740  -0.01006 389 ASP A N   
3101 C CA  . ASP A 389 ? 0.30781 0.32059 0.31349 0.00348  0.00666  -0.00965 389 ASP A CA  
3102 C C   . ASP A 389 ? 0.34670 0.36068 0.35346 0.00387  0.00577  -0.00931 389 ASP A C   
3103 O O   . ASP A 389 ? 0.34422 0.35791 0.34995 0.00394  0.00520  -0.00903 389 ASP A O   
3104 C CB  . ASP A 389 ? 0.25382 0.26554 0.25785 0.00305  0.00654  -0.00961 389 ASP A CB  
3105 C CG  . ASP A 389 ? 0.30422 0.31659 0.30867 0.00247  0.00646  -0.00989 389 ASP A CG  
3106 O OD1 . ASP A 389 ? 0.26979 0.28329 0.27511 0.00251  0.00585  -0.00989 389 ASP A OD1 
3107 O OD2 . ASP A 389 ? 0.24562 0.25728 0.24949 0.00191  0.00692  -0.01006 389 ASP A OD2 
3108 N N   . GLN A 390 ? 0.24532 0.26059 0.25419 0.00409  0.00568  -0.00930 390 GLN A N   
3109 C CA  . GLN A 390 ? 0.27228 0.28874 0.28227 0.00434  0.00464  -0.00884 390 GLN A CA  
3110 C C   . GLN A 390 ? 0.26327 0.27925 0.27247 0.00491  0.00414  -0.00826 390 GLN A C   
3111 O O   . GLN A 390 ? 0.27280 0.28882 0.28308 0.00546  0.00426  -0.00805 390 GLN A O   
3112 C CB  . GLN A 390 ? 0.32268 0.34056 0.33566 0.00451  0.00464  -0.00884 390 GLN A CB  
3113 C CG  . GLN A 390 ? 0.31760 0.33678 0.33199 0.00464  0.00330  -0.00822 390 GLN A CG  
3114 C CD  . GLN A 390 ? 0.30895 0.32823 0.32409 0.00537  0.00285  -0.00756 390 GLN A CD  
3115 O OE1 . GLN A 390 ? 0.27258 0.29172 0.28910 0.00584  0.00357  -0.00770 390 GLN A OE1 
3116 N NE2 . GLN A 390 ? 0.34913 0.36853 0.36327 0.00543  0.00172  -0.00686 390 GLN A NE2 
3117 N N   . ASP A 391 ? 0.26082 0.27629 0.26823 0.00477  0.00369  -0.00803 391 ASP A N   
3118 C CA  . ASP A 391 ? 0.31003 0.32507 0.31669 0.00524  0.00332  -0.00741 391 ASP A CA  
3119 C C   . ASP A 391 ? 0.24107 0.25699 0.24766 0.00515  0.00232  -0.00690 391 ASP A C   
3120 O O   . ASP A 391 ? 0.32434 0.34039 0.32990 0.00457  0.00200  -0.00717 391 ASP A O   
3121 C CB  . ASP A 391 ? 0.25577 0.26939 0.26049 0.00514  0.00375  -0.00748 391 ASP A CB  
3122 C CG  . ASP A 391 ? 0.19362 0.20673 0.19796 0.00565  0.00360  -0.00682 391 ASP A CG  
3123 O OD1 . ASP A 391 ? 0.27927 0.29280 0.28317 0.00570  0.00310  -0.00634 391 ASP A OD1 
3124 O OD2 . ASP A 391 ? 0.18593 0.19815 0.19036 0.00595  0.00395  -0.00674 391 ASP A OD2 
3125 N N   . HIS A 392 ? 0.26030 0.27672 0.26789 0.00565  0.00177  -0.00616 392 HIS A N   
3126 C CA  . HIS A 392 ? 0.25702 0.27431 0.26465 0.00552  0.00062  -0.00549 392 HIS A CA  
3127 C C   . HIS A 392 ? 0.26560 0.28214 0.27033 0.00508  0.00044  -0.00543 392 HIS A C   
3128 O O   . HIS A 392 ? 0.28421 0.30120 0.28809 0.00453  -0.00043 -0.00539 392 HIS A O   
3129 C CB  . HIS A 392 ? 0.30702 0.32472 0.31619 0.00617  0.00014  -0.00456 392 HIS A CB  
3130 C CG  . HIS A 392 ? 0.26472 0.28306 0.27353 0.00602  -0.00117 -0.00361 392 HIS A CG  
3131 N ND1 . HIS A 392 ? 0.33466 0.35431 0.34546 0.00586  -0.00231 -0.00322 392 HIS A ND1 
3132 C CD2 . HIS A 392 ? 0.30910 0.32685 0.31574 0.00595  -0.00153 -0.00288 392 HIS A CD2 
3133 C CE1 . HIS A 392 ? 0.31875 0.33855 0.32841 0.00565  -0.00352 -0.00224 392 HIS A CE1 
3134 N NE2 . HIS A 392 ? 0.38065 0.39927 0.38760 0.00569  -0.00297 -0.00205 392 HIS A NE2 
3135 N N   . TYR A 393 ? 0.28860 0.30392 0.29184 0.00526  0.00126  -0.00547 393 TYR A N   
3136 C CA  . TYR A 393 ? 0.27732 0.29182 0.27799 0.00493  0.00138  -0.00539 393 TYR A CA  
3137 C C   . TYR A 393 ? 0.27142 0.28520 0.27063 0.00432  0.00195  -0.00637 393 TYR A C   
3138 O O   . TYR A 393 ? 0.38416 0.39749 0.38126 0.00382  0.00186  -0.00655 393 TYR A O   
3139 C CB  . TYR A 393 ? 0.28313 0.29672 0.28343 0.00545  0.00205  -0.00485 393 TYR A CB  
3140 C CG  . TYR A 393 ? 0.26402 0.27811 0.26505 0.00590  0.00141  -0.00373 393 TYR A CG  
3141 C CD1 . TYR A 393 ? 0.36689 0.38161 0.36712 0.00559  0.00036  -0.00310 393 TYR A CD1 
3142 C CD2 . TYR A 393 ? 0.26956 0.28341 0.27213 0.00657  0.00172  -0.00325 393 TYR A CD2 
3143 C CE1 . TYR A 393 ? 0.34050 0.35564 0.34152 0.00597  -0.00032 -0.00192 393 TYR A CE1 
3144 C CE2 . TYR A 393 ? 0.32958 0.34385 0.33308 0.00697  0.00114  -0.00218 393 TYR A CE2 
3145 C CZ  . TYR A 393 ? 0.36411 0.37903 0.36687 0.00669  0.00014  -0.00147 393 TYR A CZ  
3146 O OH  . TYR A 393 ? 0.38136 0.39665 0.38514 0.00706  -0.00053 -0.00025 393 TYR A OH  
3147 N N   . LEU A 394 ? 0.26113 0.27470 0.26132 0.00431  0.00254  -0.00699 394 LEU A N   
3148 C CA  . LEU A 394 ? 0.28001 0.29288 0.27927 0.00373  0.00308  -0.00786 394 LEU A CA  
3149 C C   . LEU A 394 ? 0.29342 0.30716 0.29290 0.00310  0.00237  -0.00833 394 LEU A C   
3150 O O   . LEU A 394 ? 0.25404 0.26731 0.25199 0.00251  0.00233  -0.00886 394 LEU A O   
3151 C CB  . LEU A 394 ? 0.24226 0.25453 0.24249 0.00392  0.00382  -0.00811 394 LEU A CB  
3152 C CG  . LEU A 394 ? 0.23680 0.24827 0.23728 0.00452  0.00426  -0.00761 394 LEU A CG  
3153 C CD1 . LEU A 394 ? 0.20568 0.21652 0.20689 0.00456  0.00468  -0.00782 394 LEU A CD1 
3154 C CD2 . LEU A 394 ? 0.20974 0.22023 0.20896 0.00453  0.00476  -0.00751 394 LEU A CD2 
3155 N N   . ASN A 395 ? 0.31613 0.33104 0.31765 0.00322  0.00189  -0.00816 395 ASN A N   
3156 C CA  . ASN A 395 ? 0.25260 0.26857 0.25513 0.00266  0.00111  -0.00845 395 ASN A CA  
3157 C C   . ASN A 395 ? 0.30674 0.32290 0.30770 0.00222  -0.00003 -0.00823 395 ASN A C   
3158 O O   . ASN A 395 ? 0.37232 0.38864 0.37286 0.00151  -0.00059 -0.00874 395 ASN A O   
3159 C CB  . ASN A 395 ? 0.24633 0.26350 0.25175 0.00304  0.00101  -0.00817 395 ASN A CB  
3160 C CG  . ASN A 395 ? 0.27067 0.28864 0.27775 0.00250  0.00096  -0.00870 395 ASN A CG  
3161 O OD1 . ASN A 395 ? 0.24925 0.26659 0.25545 0.00198  0.00142  -0.00934 395 ASN A OD1 
3162 N ND2 . ASN A 395 ? 0.30254 0.32185 0.31236 0.00266  0.00051  -0.00839 395 ASN A ND2 
3163 N N   . ALA A 396 ? 0.27945 0.29541 0.27933 0.00257  -0.00034 -0.00749 396 ALA A N   
3164 C CA  . ALA A 396 ? 0.28338 0.29941 0.28140 0.00206  -0.00153 -0.00714 396 ALA A CA  
3165 C C   . ALA A 396 ? 0.29738 0.31192 0.29206 0.00155  -0.00090 -0.00779 396 ALA A C   
3166 O O   . ALA A 396 ? 0.31944 0.33381 0.31254 0.00074  -0.00165 -0.00826 396 ALA A O   
3167 C CB  . ALA A 396 ? 0.26838 0.28484 0.26677 0.00260  -0.00215 -0.00594 396 ALA A CB  
3168 N N   . ALA A 397 ? 0.26647 0.27993 0.26034 0.00199  0.00043  -0.00783 397 ALA A N   
3169 C CA  . ALA A 397 ? 0.33477 0.34676 0.32576 0.00157  0.00127  -0.00842 397 ALA A CA  
3170 C C   . ALA A 397 ? 0.28996 0.30141 0.28090 0.00102  0.00176  -0.00963 397 ALA A C   
3171 O O   . ALA A 397 ? 0.34051 0.35089 0.32910 0.00042  0.00210  -0.01037 397 ALA A O   
3172 C CB  . ALA A 397 ? 0.29434 0.30544 0.28510 0.00221  0.00253  -0.00803 397 ALA A CB  
3173 N N   . ASN A 398 ? 0.25799 0.27010 0.25138 0.00118  0.00182  -0.00983 398 ASN A N   
3174 C CA  . ASN A 398 ? 0.27974 0.29138 0.27329 0.00061  0.00220  -0.01085 398 ASN A CA  
3175 C C   . ASN A 398 ? 0.30264 0.31501 0.29613 -0.00019 0.00095  -0.01126 398 ASN A C   
3176 O O   . ASN A 398 ? 0.27735 0.28898 0.26979 -0.00089 0.00106  -0.01220 398 ASN A O   
3177 C CB  . ASN A 398 ? 0.29661 0.30843 0.29248 0.00098  0.00287  -0.01084 398 ASN A CB  
3178 C CG  . ASN A 398 ? 0.22672 0.23733 0.22244 0.00144  0.00408  -0.01078 398 ASN A CG  
3179 O OD1 . ASN A 398 ? 0.20070 0.21027 0.19609 0.00115  0.00482  -0.01141 398 ASN A OD1 
3180 N ND2 . ASN A 398 ? 0.31269 0.32342 0.30895 0.00215  0.00424  -0.01000 398 ASN A ND2 
3181 N N   . TRP A 399 ? 0.31361 0.32740 0.30850 -0.00011 -0.00030 -0.01057 399 TRP A N   
3182 C CA  . TRP A 399 ? 0.34482 0.35937 0.33990 -0.00091 -0.00175 -0.01082 399 TRP A CA  
3183 C C   . TRP A 399 ? 0.34345 0.35716 0.33513 -0.00157 -0.00258 -0.01097 399 TRP A C   
3184 O O   . TRP A 399 ? 0.32787 0.34136 0.31857 -0.00248 -0.00343 -0.01169 399 TRP A O   
3185 C CB  . TRP A 399 ? 0.33610 0.35242 0.33411 -0.00061 -0.00286 -0.00995 399 TRP A CB  
3186 C CG  . TRP A 399 ? 0.30782 0.32499 0.30900 -0.00054 -0.00237 -0.01024 399 TRP A CG  
3187 C CD1 . TRP A 399 ? 0.28535 0.30277 0.28839 0.00017  -0.00124 -0.01001 399 TRP A CD1 
3188 C CD2 . TRP A 399 ? 0.28789 0.30566 0.29059 -0.00127 -0.00292 -0.01081 399 TRP A CD2 
3189 N NE1 . TRP A 399 ? 0.28660 0.30469 0.29201 -0.00009 -0.00092 -0.01038 399 TRP A NE1 
3190 C CE2 . TRP A 399 ? 0.29360 0.31198 0.29907 -0.00095 -0.00192 -0.01084 399 TRP A CE2 
3191 C CE3 . TRP A 399 ? 0.31341 0.33117 0.31533 -0.00224 -0.00418 -0.01131 399 TRP A CE3 
3192 C CZ2 . TRP A 399 ? 0.28068 0.29976 0.28838 -0.00151 -0.00200 -0.01127 399 TRP A CZ2 
3193 C CZ3 . TRP A 399 ? 0.28198 0.30046 0.28632 -0.00279 -0.00443 -0.01176 399 TRP A CZ3 
3194 C CH2 . TRP A 399 ? 0.27498 0.29416 0.28229 -0.00241 -0.00328 -0.01171 399 TRP A CH2 
3195 N N   . MET A 400 ? 0.35220 0.36534 0.34191 -0.00120 -0.00233 -0.01033 400 MET A N   
3196 C CA  . MET A 400 ? 0.35652 0.36844 0.34229 -0.00188 -0.00267 -0.01057 400 MET A CA  
3197 C C   . MET A 400 ? 0.32193 0.33211 0.30562 -0.00225 -0.00112 -0.01188 400 MET A C   
3198 O O   . MET A 400 ? 0.41681 0.42581 0.39723 -0.00308 -0.00134 -0.01258 400 MET A O   
3199 C CB  . MET A 400 ? 0.41185 0.42358 0.39619 -0.00139 -0.00261 -0.00943 400 MET A CB  
3200 C CG  . MET A 400 ? 0.35440 0.36768 0.34049 -0.00115 -0.00435 -0.00807 400 MET A CG  
3201 S SD  . MET A 400 ? 0.47137 0.48428 0.45568 -0.00067 -0.00433 -0.00662 400 MET A SD  
3202 C CE  . MET A 400 ? 0.36280 0.37539 0.34906 0.00049  -0.00212 -0.00664 400 MET A CE  
3203 N N   . TRP A 401 ? 0.33113 0.34101 0.31665 -0.00168 0.00040  -0.01223 401 TRP A N   
3204 C CA  . TRP A 401 ? 0.36823 0.37654 0.35261 -0.00199 0.00182  -0.01344 401 TRP A CA  
3205 C C   . TRP A 401 ? 0.33274 0.34099 0.31740 -0.00286 0.00119  -0.01452 401 TRP A C   
3206 O O   . TRP A 401 ? 0.34199 0.34890 0.32421 -0.00363 0.00143  -0.01561 401 TRP A O   
3207 C CB  . TRP A 401 ? 0.35374 0.36182 0.34035 -0.00116 0.00331  -0.01328 401 TRP A CB  
3208 C CG  . TRP A 401 ? 0.37746 0.38389 0.36341 -0.00132 0.00488  -0.01429 401 TRP A CG  
3209 C CD1 . TRP A 401 ? 0.30922 0.31493 0.29524 -0.00196 0.00512  -0.01545 401 TRP A CD1 
3210 C CD2 . TRP A 401 ? 0.41561 0.42092 0.40122 -0.00079 0.00645  -0.01419 401 TRP A CD2 
3211 N NE1 . TRP A 401 ? 0.31620 0.32038 0.30196 -0.00186 0.00676  -0.01610 401 TRP A NE1 
3212 C CE2 . TRP A 401 ? 0.35677 0.36071 0.34237 -0.00113 0.00762  -0.01533 401 TRP A CE2 
3213 C CE3 . TRP A 401 ? 0.40341 0.40874 0.38904 -0.00007 0.00700  -0.01323 401 TRP A CE3 
3214 C CZ2 . TRP A 401 ? 0.39446 0.39711 0.38026 -0.00076 0.00932  -0.01552 401 TRP A CZ2 
3215 C CZ3 . TRP A 401 ? 0.39456 0.39864 0.38029 0.00027  0.00866  -0.01340 401 TRP A CZ3 
3216 C CH2 . TRP A 401 ? 0.36503 0.36780 0.35094 -0.00006 0.00982  -0.01453 401 TRP A CH2 
3217 N N   . LEU A 402 ? 0.24681 0.25643 0.23449 -0.00280 0.00046  -0.01427 402 LEU A N   
3218 C CA  . LEU A 402 ? 0.34787 0.35753 0.33644 -0.00359 -0.00005 -0.01520 402 LEU A CA  
3219 C C   . LEU A 402 ? 0.36593 0.37591 0.35306 -0.00454 -0.00191 -0.01544 402 LEU A C   
3220 O O   . LEU A 402 ? 0.35380 0.36344 0.34102 -0.00538 -0.00239 -0.01640 402 LEU A O   
3221 C CB  . LEU A 402 ? 0.41588 0.42686 0.40820 -0.00324 -0.00005 -0.01477 402 LEU A CB  
3222 C CG  . LEU A 402 ? 0.34439 0.35463 0.33809 -0.00293 0.00150  -0.01509 402 LEU A CG  
3223 C CD1 . LEU A 402 ? 0.31718 0.32619 0.31021 -0.00373 0.00186  -0.01635 402 LEU A CD1 
3224 C CD2 . LEU A 402 ? 0.32742 0.33682 0.32036 -0.00211 0.00276  -0.01466 402 LEU A CD2 
3225 N N   . SER A 403 ? 0.45195 0.46251 0.43785 -0.00448 -0.00309 -0.01453 403 SER A N   
3226 C CA  . SER A 403 ? 0.47213 0.48292 0.45646 -0.00545 -0.00515 -0.01456 403 SER A CA  
3227 C C   . SER A 403 ? 0.48282 0.49180 0.46221 -0.00609 -0.00513 -0.01505 403 SER A C   
3228 O O   . SER A 403 ? 0.52065 0.52963 0.49796 -0.00690 -0.00699 -0.01482 403 SER A O   
3229 C CB  . SER A 403 ? 0.50091 0.51356 0.48737 -0.00509 -0.00677 -0.01308 403 SER A CB  
3230 O OG  . SER A 403 ? 0.51261 0.52517 0.49794 -0.00433 -0.00630 -0.01205 403 SER A OG  
3231 N N   . ALA A 404 ? 0.47175 0.47916 0.44926 -0.00580 -0.00306 -0.01570 404 ALA A N   
3232 C CA  . ALA A 404 ? 0.43130 0.43680 0.40406 -0.00634 -0.00247 -0.01627 404 ALA A CA  
3233 C C   . ALA A 404 ? 0.44134 0.44716 0.41195 -0.00628 -0.00352 -0.01491 404 ALA A C   
3234 O O   . ALA A 404 ? 0.40119 0.40560 0.36737 -0.00709 -0.00383 -0.01520 404 ALA A O   
3235 C CB  . ALA A 404 ? 0.39487 0.39903 0.36491 -0.00770 -0.00319 -0.01778 404 ALA A CB  
3236 N N   . SER A 405 ? 0.45104 0.45857 0.42462 -0.00537 -0.00405 -0.01341 405 SER A N   
3237 C CA  . SER A 405 ? 0.42346 0.43142 0.39560 -0.00524 -0.00514 -0.01194 405 SER A CA  
3238 C C   . SER A 405 ? 0.41613 0.42309 0.38656 -0.00457 -0.00325 -0.01149 405 SER A C   
3239 O O   . SER A 405 ? 0.45891 0.46524 0.42619 -0.00487 -0.00370 -0.01071 405 SER A O   
3240 C CB  . SER A 405 ? 0.38186 0.39207 0.35830 -0.00458 -0.00658 -0.01059 405 SER A CB  
3241 O OG  . SER A 405 ? 0.44617 0.45739 0.42452 -0.00523 -0.00833 -0.01090 405 SER A OG  
3242 N N   . ALA A 406 ? 0.31874 0.32550 0.29124 -0.00373 -0.00121 -0.01188 406 ALA A N   
3243 C CA  . ALA A 406 ? 0.39462 0.40049 0.36616 -0.00307 0.00064  -0.01146 406 ALA A CA  
3244 C C   . ALA A 406 ? 0.46086 0.46591 0.43395 -0.00263 0.00278  -0.01252 406 ALA A C   
3245 O O   . ALA A 406 ? 0.45779 0.46333 0.43337 -0.00261 0.00270  -0.01319 406 ALA A O   
3246 C CB  . ALA A 406 ? 0.41848 0.42573 0.39247 -0.00209 0.00021  -0.00978 406 ALA A CB  
3247 N N   . PHE A 407 ? 0.44434 0.44810 0.41604 -0.00234 0.00469  -0.01259 407 PHE A N   
3248 C CA  . PHE A 407 ? 0.45691 0.45981 0.43035 -0.00185 0.00675  -0.01337 407 PHE A CA  
3249 C C   . PHE A 407 ? 0.47147 0.47318 0.44401 -0.00261 0.00733  -0.01510 407 PHE A C   
3250 O O   . PHE A 407 ? 0.36940 0.36945 0.34062 -0.00276 0.00921  -0.01605 407 PHE A O   
3251 C CB  . PHE A 407 ? 0.40969 0.41393 0.38757 -0.00089 0.00664  -0.01266 407 PHE A CB  
3252 C CG  . PHE A 407 ? 0.43623 0.44167 0.41536 -0.00016 0.00593  -0.01109 407 PHE A CG  
3253 C CD1 . PHE A 407 ? 0.44317 0.44805 0.42189 0.00036  0.00709  -0.01036 407 PHE A CD1 
3254 C CD2 . PHE A 407 ? 0.39706 0.40415 0.37806 0.00001  0.00420  -0.01037 407 PHE A CD2 
3255 C CE1 . PHE A 407 ? 0.38847 0.39437 0.36850 0.00101  0.00643  -0.00893 407 PHE A CE1 
3256 C CE2 . PHE A 407 ? 0.38679 0.39488 0.36915 0.00069  0.00362  -0.00901 407 PHE A CE2 
3257 C CZ  . PHE A 407 ? 0.35538 0.36285 0.33720 0.00118  0.00468  -0.00829 407 PHE A CZ  
3258 N N   . PHE A 408 ? 0.46689 0.46941 0.44041 -0.00308 0.00583  -0.01553 408 PHE A N   
3259 C CA  . PHE A 408 ? 0.43983 0.44131 0.41281 -0.00385 0.00614  -0.01714 408 PHE A CA  
3260 C C   . PHE A 408 ? 0.43926 0.43988 0.40807 -0.00507 0.00505  -0.01788 408 PHE A C   
3261 O O   . PHE A 408 ? 0.49172 0.49331 0.45947 -0.00538 0.00312  -0.01701 408 PHE A O   
3262 C CB  . PHE A 408 ? 0.44808 0.45085 0.42470 -0.00374 0.00520  -0.01717 408 PHE A CB  
3263 C CG  . PHE A 408 ? 0.45666 0.45834 0.43388 -0.00425 0.00599  -0.01865 408 PHE A CG  
3264 C CD1 . PHE A 408 ? 0.48801 0.48852 0.46645 -0.00381 0.00797  -0.01916 408 PHE A CD1 
3265 C CD2 . PHE A 408 ? 0.42947 0.43128 0.40642 -0.00516 0.00467  -0.01947 408 PHE A CD2 
3266 C CE1 . PHE A 408 ? 0.49601 0.49547 0.47533 -0.00425 0.00868  -0.02045 408 PHE A CE1 
3267 C CE2 . PHE A 408 ? 0.45467 0.45542 0.43238 -0.00564 0.00539  -0.02081 408 PHE A CE2 
3268 C CZ  . PHE A 408 ? 0.49408 0.49363 0.47296 -0.00517 0.00742  -0.02130 408 PHE A CZ  
3269 N N   . SER A 409 ? 0.46611 0.46480 0.43259 -0.00579 0.00625  -0.01951 409 SER A N   
3270 C CA  . SER A 409 ? 0.44023 0.43768 0.40212 -0.00709 0.00533  -0.02042 409 SER A CA  
3271 C C   . SER A 409 ? 0.43479 0.43096 0.39622 -0.00798 0.00556  -0.02235 409 SER A C   
3272 O O   . SER A 409 ? 0.45107 0.44568 0.40827 -0.00915 0.00518  -0.02347 409 SER A O   
3273 C CB  . SER A 409 ? 0.46938 0.46511 0.42694 -0.00729 0.00682  -0.02050 409 SER A CB  
3274 O OG  . SER A 409 ? 0.51543 0.50974 0.47370 -0.00684 0.00964  -0.02143 409 SER A OG  
3275 N N   . GLN A 410 ? 0.38843 0.38508 0.35391 -0.00754 0.00611  -0.02275 410 GLN A N   
3276 C CA  . GLN A 410 ? 0.47331 0.46874 0.43890 -0.00833 0.00641  -0.02453 410 GLN A CA  
3277 C C   . GLN A 410 ? 0.51954 0.51653 0.48730 -0.00879 0.00405  -0.02430 410 GLN A C   
3278 O O   . GLN A 410 ? 0.44742 0.44551 0.41933 -0.00830 0.00404  -0.02399 410 GLN A O   
3279 C CB  . GLN A 410 ? 0.37835 0.37305 0.34707 -0.00761 0.00867  -0.02508 410 GLN A CB  
3280 C CG  . GLN A 410 ? 0.42630 0.41942 0.39513 -0.00840 0.00931  -0.02699 410 GLN A CG  
3281 C CD  . GLN A 410 ? 0.51204 0.50288 0.47579 -0.00953 0.00985  -0.02866 410 GLN A CD  
3282 O OE1 . GLN A 410 ? 0.50690 0.49733 0.46851 -0.01068 0.00826  -0.02956 410 GLN A OE1 
3283 N NE2 . GLN A 410 ? 0.49848 0.48774 0.46024 -0.00927 0.01214  -0.02911 410 GLN A NE2 
3284 N N   . TYR A 411 ? 0.52042 0.51745 0.48530 -0.00980 0.00201  -0.02439 411 TYR A N   
3285 C CA  . TYR A 411 ? 0.45531 0.45390 0.42235 -0.01031 -0.00038 -0.02410 411 TYR A CA  
3286 C C   . TYR A 411 ? 0.41413 0.41181 0.38216 -0.01114 -0.00040 -0.02574 411 TYR A C   
3287 O O   . TYR A 411 ? 0.37212 0.37118 0.34297 -0.01146 -0.00204 -0.02549 411 TYR A O   
3288 C CB  . TYR A 411 ? 0.50557 0.50449 0.46945 -0.01116 -0.00281 -0.02351 411 TYR A CB  
3289 C CG  . TYR A 411 ? 0.47648 0.47296 0.43437 -0.01223 -0.00254 -0.02468 411 TYR A CG  
3290 C CD1 . TYR A 411 ? 0.44713 0.44199 0.40265 -0.01360 -0.00320 -0.02646 411 TYR A CD1 
3291 C CD2 . TYR A 411 ? 0.49221 0.48789 0.44669 -0.01195 -0.00157 -0.02404 411 TYR A CD2 
3292 C CE1 . TYR A 411 ? 0.45454 0.44693 0.40411 -0.01467 -0.00285 -0.02766 411 TYR A CE1 
3293 C CE2 . TYR A 411 ? 0.49685 0.49014 0.44548 -0.01300 -0.00113 -0.02512 411 TYR A CE2 
3294 C CZ  . TYR A 411 ? 0.45296 0.44455 0.39898 -0.01438 -0.00176 -0.02697 411 TYR A CZ  
3295 O OH  . TYR A 411 ? 0.45348 0.44246 0.39322 -0.01553 -0.00123 -0.02817 411 TYR A OH  
3296 N N   . PHE A 412 ? 0.44300 0.43839 0.40908 -0.01151 0.00144  -0.02741 412 PHE A N   
3297 C CA  . PHE A 412 ? 0.44388 0.43830 0.41127 -0.01225 0.00157  -0.02899 412 PHE A CA  
3298 C C   . PHE A 412 ? 0.42538 0.42092 0.39816 -0.01139 0.00241  -0.02848 412 PHE A C   
3299 O O   . PHE A 412 ? 0.35195 0.34730 0.32681 -0.01196 0.00203  -0.02933 412 PHE A O   
3300 C CB  . PHE A 412 ? 0.42801 0.41952 0.39194 -0.01284 0.00350  -0.03099 412 PHE A CB  
3301 C CG  . PHE A 412 ? 0.52787 0.51778 0.48619 -0.01423 0.00234  -0.03209 412 PHE A CG  
3302 C CD1 . PHE A 412 ? 0.50447 0.49386 0.46204 -0.01556 0.00047  -0.03326 412 PHE A CD1 
3303 C CD2 . PHE A 412 ? 0.52061 0.50943 0.47430 -0.01429 0.00306  -0.03193 412 PHE A CD2 
3304 C CE1 . PHE A 412 ? 0.40123 0.38898 0.35331 -0.01696 -0.00081 -0.03427 412 PHE A CE1 
3305 C CE2 . PHE A 412 ? 0.42189 0.40904 0.36991 -0.01570 0.00193  -0.03289 412 PHE A CE2 
3306 C CZ  . PHE A 412 ? 0.50353 0.49010 0.45062 -0.01705 -0.00008 -0.03407 412 PHE A CZ  
3307 N N   . ARG A 413 ? 0.41033 0.40692 0.38530 -0.01012 0.00348  -0.02710 413 ARG A N   
3308 C CA  . ARG A 413 ? 0.37905 0.37660 0.35869 -0.00934 0.00419  -0.02643 413 ARG A CA  
3309 C C   . ARG A 413 ? 0.31043 0.31035 0.29275 -0.00927 0.00231  -0.02515 413 ARG A C   
3310 O O   . ARG A 413 ? 0.35833 0.35974 0.34095 -0.00861 0.00171  -0.02373 413 ARG A O   
3311 C CB  . ARG A 413 ? 0.33457 0.33207 0.31521 -0.00812 0.00600  -0.02553 413 ARG A CB  
3312 C CG  . ARG A 413 ? 0.29534 0.29354 0.28033 -0.00739 0.00669  -0.02478 413 ARG A CG  
3313 C CD  . ARG A 413 ? 0.37938 0.37606 0.36585 -0.00786 0.00766  -0.02609 413 ARG A CD  
3314 N NE  . ARG A 413 ? 0.33401 0.33112 0.32434 -0.00718 0.00836  -0.02521 413 ARG A NE  
3315 C CZ  . ARG A 413 ? 0.44023 0.43848 0.43326 -0.00733 0.00748  -0.02458 413 ARG A CZ  
3316 N NH1 . ARG A 413 ? 0.44256 0.44182 0.43544 -0.00805 0.00590  -0.02475 413 ARG A NH1 
3317 N NH2 . ARG A 413 ? 0.46324 0.46160 0.45923 -0.00677 0.00818  -0.02372 413 ARG A NH2 
3318 N N   . VAL A 414 ? 0.29396 0.29419 0.27844 -0.00994 0.00148  -0.02567 414 VAL A N   
3319 C CA  . VAL A 414 ? 0.38924 0.39162 0.37665 -0.00998 -0.00011 -0.02462 414 VAL A CA  
3320 C C   . VAL A 414 ? 0.36109 0.36389 0.35249 -0.00961 0.00084  -0.02429 414 VAL A C   
3321 O O   . VAL A 414 ? 0.40097 0.40253 0.39318 -0.01014 0.00145  -0.02536 414 VAL A O   
3322 C CB  . VAL A 414 ? 0.38366 0.38620 0.37030 -0.01125 -0.00220 -0.02536 414 VAL A CB  
3323 C CG1 . VAL A 414 ? 0.40241 0.40727 0.39281 -0.01124 -0.00364 -0.02423 414 VAL A CG1 
3324 C CG2 . VAL A 414 ? 0.34671 0.34864 0.32895 -0.01172 -0.00330 -0.02557 414 VAL A CG2 
3325 N N   . TYR A 415 ? 0.39454 0.39895 0.38829 -0.00876 0.00098  -0.02280 415 TYR A N   
3326 C CA  . TYR A 415 ? 0.41077 0.41556 0.40791 -0.00846 0.00183  -0.02228 415 TYR A CA  
3327 C C   . TYR A 415 ? 0.39518 0.40083 0.39474 -0.00931 0.00075  -0.02249 415 TYR A C   
3328 O O   . TYR A 415 ? 0.44153 0.44878 0.44194 -0.00951 -0.00064 -0.02195 415 TYR A O   
3329 C CB  . TYR A 415 ? 0.44296 0.44906 0.44139 -0.00741 0.00225  -0.02073 415 TYR A CB  
3330 C CG  . TYR A 415 ? 0.42317 0.42839 0.41998 -0.00654 0.00344  -0.02041 415 TYR A CG  
3331 C CD1 . TYR A 415 ? 0.42577 0.42919 0.42211 -0.00649 0.00477  -0.02112 415 TYR A CD1 
3332 C CD2 . TYR A 415 ? 0.33311 0.33932 0.32924 -0.00578 0.00325  -0.01937 415 TYR A CD2 
3333 C CE1 . TYR A 415 ? 0.45796 0.46064 0.45331 -0.00571 0.00588  -0.02078 415 TYR A CE1 
3334 C CE2 . TYR A 415 ? 0.31246 0.31789 0.30741 -0.00502 0.00431  -0.01904 415 TYR A CE2 
3335 C CZ  . TYR A 415 ? 0.38573 0.38943 0.38035 -0.00499 0.00562  -0.01972 415 TYR A CZ  
3336 O OH  . TYR A 415 ? 0.35304 0.35603 0.34695 -0.00425 0.00668  -0.01935 415 TYR A OH  
3337 N N   . SER A 416 ? 0.32731 0.33190 0.32831 -0.00981 0.00138  -0.02323 416 SER A N   
3338 C CA  . SER A 416 ? 0.37266 0.37798 0.37632 -0.01064 0.00051  -0.02340 416 SER A CA  
3339 C C   . SER A 416 ? 0.36509 0.37207 0.37186 -0.01015 0.00086  -0.02194 416 SER A C   
3340 O O   . SER A 416 ? 0.36020 0.36677 0.36772 -0.00954 0.00220  -0.02126 416 SER A O   
3341 C CB  . SER A 416 ? 0.44230 0.44587 0.44669 -0.01132 0.00118  -0.02458 416 SER A CB  
3342 O OG  . SER A 416 ? 0.45675 0.46098 0.46380 -0.01220 0.00029  -0.02477 416 SER A OG  
3343 N N   . PRO A 417 ? 0.32675 0.33552 0.33540 -0.01045 -0.00030 -0.02141 417 PRO A N   
3344 C CA  . PRO A 417 ? 0.36709 0.37736 0.37853 -0.00999 0.00030  -0.02011 417 PRO A CA  
3345 C C   . PRO A 417 ? 0.36500 0.37490 0.37907 -0.01044 0.00118  -0.02000 417 PRO A C   
3346 O O   . PRO A 417 ? 0.23924 0.25024 0.25560 -0.01027 0.00177  -0.01902 417 PRO A O   
3347 C CB  . PRO A 417 ? 0.32161 0.33380 0.33454 -0.01027 -0.00123 -0.01976 417 PRO A CB  
3348 C CG  . PRO A 417 ? 0.25378 0.26535 0.26579 -0.01130 -0.00276 -0.02096 417 PRO A CG  
3349 C CD  . PRO A 417 ? 0.36179 0.37125 0.37010 -0.01124 -0.00222 -0.02196 417 PRO A CD  
3350 N N   . VAL A 418 ? 0.42097 0.42924 0.43472 -0.01104 0.00138  -0.02102 418 VAL A N   
3351 C CA  . VAL A 418 ? 0.38186 0.38956 0.39811 -0.01154 0.00215  -0.02092 418 VAL A CA  
3352 C C   . VAL A 418 ? 0.44243 0.44823 0.45781 -0.01120 0.00345  -0.02099 418 VAL A C   
3353 O O   . VAL A 418 ? 0.43509 0.44067 0.45200 -0.01106 0.00444  -0.02005 418 VAL A O   
3354 C CB  . VAL A 418 ? 0.38523 0.39275 0.40296 -0.01273 0.00106  -0.02202 418 VAL A CB  
3355 C CG1 . VAL A 418 ? 0.43651 0.44340 0.45704 -0.01326 0.00191  -0.02183 418 VAL A CG1 
3356 C CG2 . VAL A 418 ? 0.39147 0.40098 0.41068 -0.01311 -0.00040 -0.02179 418 VAL A CG2 
3357 N N   . VAL A 419 ? 0.46084 0.46520 0.47382 -0.01108 0.00350  -0.02204 419 VAL A N   
3358 C CA  . VAL A 419 ? 0.40163 0.40412 0.41438 -0.01079 0.00472  -0.02221 419 VAL A CA  
3359 C C   . VAL A 419 ? 0.45691 0.45944 0.46859 -0.00970 0.00556  -0.02107 419 VAL A C   
3360 O O   . VAL A 419 ? 0.47939 0.48086 0.49193 -0.00940 0.00650  -0.02051 419 VAL A O   
3361 C CB  . VAL A 419 ? 0.43341 0.43419 0.44431 -0.01119 0.00467  -0.02396 419 VAL A CB  
3362 C CG1 . VAL A 419 ? 0.49884 0.49767 0.51042 -0.01097 0.00601  -0.02422 419 VAL A CG1 
3363 C CG2 . VAL A 419 ? 0.46217 0.46294 0.47378 -0.01235 0.00354  -0.02515 419 VAL A CG2 
3364 N N   . PHE A 420 ? 0.44179 0.44549 0.45180 -0.00913 0.00512  -0.02066 420 PHE A N   
3365 C CA  . PHE A 420 ? 0.41473 0.41836 0.42364 -0.00813 0.00581  -0.01972 420 PHE A CA  
3366 C C   . PHE A 420 ? 0.34796 0.35189 0.35854 -0.00787 0.00642  -0.01831 420 PHE A C   
3367 O O   . PHE A 420 ? 0.34396 0.34680 0.35459 -0.00744 0.00716  -0.01773 420 PHE A O   
3368 C CB  . PHE A 420 ? 0.34225 0.34717 0.34936 -0.00765 0.00513  -0.01949 420 PHE A CB  
3369 C CG  . PHE A 420 ? 0.37102 0.37564 0.37670 -0.00668 0.00576  -0.01883 420 PHE A CG  
3370 C CD1 . PHE A 420 ? 0.31108 0.31637 0.31743 -0.00607 0.00610  -0.01753 420 PHE A CD1 
3371 C CD2 . PHE A 420 ? 0.37855 0.38211 0.38215 -0.00642 0.00605  -0.01955 420 PHE A CD2 
3372 C CE1 . PHE A 420 ? 0.26318 0.26816 0.26839 -0.00523 0.00653  -0.01694 420 PHE A CE1 
3373 C CE2 . PHE A 420 ? 0.33565 0.33898 0.33830 -0.00554 0.00664  -0.01889 420 PHE A CE2 
3374 C CZ  . PHE A 420 ? 0.25767 0.26173 0.26122 -0.00495 0.00678  -0.01757 420 PHE A CZ  
3375 N N   . GLY A 421 ? 0.33101 0.33634 0.34297 -0.00817 0.00611  -0.01771 421 GLY A N   
3376 C CA  . GLY A 421 ? 0.21766 0.22312 0.23075 -0.00806 0.00680  -0.01642 421 GLY A CA  
3377 C C   . GLY A 421 ? 0.24438 0.24853 0.25905 -0.00862 0.00734  -0.01623 421 GLY A C   
3378 O O   . GLY A 421 ? 0.27618 0.27983 0.29113 -0.00849 0.00794  -0.01507 421 GLY A O   
3379 N N   . LYS A 422 ? 0.28829 0.29176 0.30392 -0.00929 0.00707  -0.01731 422 LYS A N   
3380 C CA  . LYS A 422 ? 0.32045 0.32268 0.33800 -0.00988 0.00753  -0.01713 422 LYS A CA  
3381 C C   . LYS A 422 ? 0.35547 0.35585 0.37273 -0.00949 0.00807  -0.01707 422 LYS A C   
3382 O O   . LYS A 422 ? 0.20148 0.20081 0.22030 -0.00977 0.00849  -0.01634 422 LYS A O   
3383 C CB  . LYS A 422 ? 0.31501 0.31717 0.33398 -0.01080 0.00699  -0.01839 422 LYS A CB  
3384 C CG  . LYS A 422 ? 0.34808 0.34922 0.36955 -0.01154 0.00740  -0.01814 422 LYS A CG  
3385 C CD  . LYS A 422 ? 0.23198 0.23377 0.25533 -0.01252 0.00676  -0.01895 422 LYS A CD  
3386 C CE  . LYS A 422 ? 0.36156 0.36321 0.38362 -0.01275 0.00585  -0.02074 422 LYS A CE  
3387 N NZ  . LYS A 422 ? 0.34262 0.34223 0.36379 -0.01266 0.00626  -0.02183 422 LYS A NZ  
3388 N N   . LYS A 423 ? 0.39062 0.39056 0.40613 -0.00887 0.00809  -0.01774 423 LYS A N   
3389 C CA  . LYS A 423 ? 0.29300 0.29128 0.30871 -0.00844 0.00871  -0.01766 423 LYS A CA  
3390 C C   . LYS A 423 ? 0.30902 0.30720 0.32459 -0.00783 0.00893  -0.01598 423 LYS A C   
3391 O O   . LYS A 423 ? 0.36901 0.36581 0.38551 -0.00757 0.00929  -0.01553 423 LYS A O   
3392 C CB  . LYS A 423 ? 0.30786 0.30565 0.32180 -0.00802 0.00886  -0.01895 423 LYS A CB  
3393 C CG  . LYS A 423 ? 0.31835 0.31672 0.33044 -0.00710 0.00892  -0.01831 423 LYS A CG  
3394 C CD  . LYS A 423 ? 0.34347 0.34270 0.35323 -0.00701 0.00849  -0.01930 423 LYS A CD  
3395 C CE  . LYS A 423 ? 0.39154 0.38971 0.40068 -0.00759 0.00860  -0.02108 423 LYS A CE  
3396 N NZ  . LYS A 423 ? 0.39533 0.39167 0.40473 -0.00727 0.00970  -0.02168 423 LYS A NZ  
3397 N N   . TYR A 424 ? 0.28176 0.28129 0.29632 -0.00763 0.00868  -0.01508 424 TYR A N   
3398 C CA  . TYR A 424 ? 0.34312 0.34247 0.35719 -0.00721 0.00879  -0.01353 424 TYR A CA  
3399 C C   . TYR A 424 ? 0.31875 0.31823 0.33363 -0.00782 0.00890  -0.01239 424 TYR A C   
3400 O O   . TYR A 424 ? 0.31824 0.31669 0.33329 -0.00785 0.00899  -0.01114 424 TYR A O   
3401 C CB  . TYR A 424 ? 0.28738 0.28792 0.29946 -0.00651 0.00859  -0.01335 424 TYR A CB  
3402 C CG  . TYR A 424 ? 0.25827 0.25863 0.26927 -0.00585 0.00857  -0.01414 424 TYR A CG  
3403 C CD1 . TYR A 424 ? 0.30987 0.30910 0.32091 -0.00529 0.00880  -0.01366 424 TYR A CD1 
3404 C CD2 . TYR A 424 ? 0.27653 0.27781 0.28650 -0.00583 0.00830  -0.01528 424 TYR A CD2 
3405 C CE1 . TYR A 424 ? 0.26175 0.26080 0.27193 -0.00471 0.00899  -0.01435 424 TYR A CE1 
3406 C CE2 . TYR A 424 ? 0.22615 0.22714 0.23481 -0.00530 0.00841  -0.01593 424 TYR A CE2 
3407 C CZ  . TYR A 424 ? 0.17652 0.17641 0.18533 -0.00473 0.00887  -0.01548 424 TYR A CZ  
3408 O OH  . TYR A 424 ? 0.17926 0.17886 0.18690 -0.00422 0.00919  -0.01610 424 TYR A OH  
3409 N N   . ASP A 425 ? 0.30200 0.30267 0.31739 -0.00836 0.00890  -0.01273 425 ASP A N   
3410 C CA  . ASP A 425 ? 0.35144 0.35237 0.36752 -0.00897 0.00926  -0.01168 425 ASP A CA  
3411 C C   . ASP A 425 ? 0.37329 0.37458 0.39148 -0.00982 0.00927  -0.01238 425 ASP A C   
3412 O O   . ASP A 425 ? 0.37098 0.37377 0.38961 -0.01003 0.00913  -0.01295 425 ASP A O   
3413 C CB  . ASP A 425 ? 0.31001 0.31230 0.32471 -0.00868 0.00946  -0.01118 425 ASP A CB  
3414 C CG  . ASP A 425 ? 0.37589 0.37797 0.39057 -0.00923 0.01013  -0.00991 425 ASP A CG  
3415 O OD1 . ASP A 425 ? 0.44378 0.44505 0.45988 -0.00997 0.01037  -0.00946 425 ASP A OD1 
3416 O OD2 . ASP A 425 ? 0.34212 0.34476 0.35530 -0.00895 0.01048  -0.00936 425 ASP A OD2 
3417 N N   . PRO A 426 ? 0.38022 0.38016 0.40007 -0.01035 0.00936  -0.01232 426 PRO A N   
3418 C CA  . PRO A 426 ? 0.39542 0.39560 0.41749 -0.01122 0.00932  -0.01301 426 PRO A CA  
3419 C C   . PRO A 426 ? 0.40187 0.40290 0.42496 -0.01187 0.00981  -0.01203 426 PRO A C   
3420 O O   . PRO A 426 ? 0.38495 0.38694 0.40976 -0.01246 0.00969  -0.01268 426 PRO A O   
3421 C CB  . PRO A 426 ? 0.39959 0.39786 0.42321 -0.01151 0.00937  -0.01307 426 PRO A CB  
3422 C CG  . PRO A 426 ? 0.36540 0.36257 0.38803 -0.01103 0.00955  -0.01165 426 PRO A CG  
3423 C CD  . PRO A 426 ? 0.32366 0.32176 0.34377 -0.01017 0.00941  -0.01164 426 PRO A CD  
3424 N N   . GLU A 427 ? 0.40717 0.40777 0.42922 -0.01184 0.01038  -0.01049 427 GLU A N   
3425 C CA  . GLU A 427 ? 0.36297 0.36424 0.38570 -0.01250 0.01114  -0.00956 427 GLU A CA  
3426 C C   . GLU A 427 ? 0.41670 0.41994 0.43893 -0.01221 0.01137  -0.00996 427 GLU A C   
3427 O O   . GLU A 427 ? 0.35756 0.36179 0.38132 -0.01279 0.01199  -0.00974 427 GLU A O   
3428 C CB  . GLU A 427 ? 0.34528 0.34524 0.36654 -0.01266 0.01169  -0.00781 427 GLU A CB  
3429 C CG  . GLU A 427 ? 0.34156 0.33991 0.36446 -0.01342 0.01175  -0.00694 427 GLU A CG  
3430 C CD  . GLU A 427 ? 0.42666 0.42561 0.45205 -0.01439 0.01234  -0.00693 427 GLU A CD  
3431 O OE1 . GLU A 427 ? 0.39294 0.39323 0.41822 -0.01460 0.01309  -0.00679 427 GLU A OE1 
3432 O OE2 . GLU A 427 ? 0.39483 0.39291 0.42256 -0.01493 0.01211  -0.00707 427 GLU A OE2 
3433 N N   . GLY A 428 ? 0.45051 0.45431 0.47092 -0.01134 0.01092  -0.01049 428 GLY A N   
3434 C CA  . GLY A 428 ? 0.34302 0.34863 0.36321 -0.01100 0.01103  -0.01083 428 GLY A CA  
3435 C C   . GLY A 428 ? 0.34418 0.34988 0.36273 -0.01081 0.01200  -0.00977 428 GLY A C   
3436 O O   . GLY A 428 ? 0.35992 0.36698 0.37928 -0.01091 0.01266  -0.00976 428 GLY A O   
3437 N N   . ARG A 429 ? 0.40207 0.40626 0.41839 -0.01058 0.01210  -0.00888 429 ARG A N   
3438 C CA  . ARG A 429 ? 0.38089 0.38484 0.39507 -0.01048 0.01294  -0.00795 429 ARG A CA  
3439 C C   . ARG A 429 ? 0.34267 0.34802 0.35602 -0.00969 0.01292  -0.00857 429 ARG A C   
3440 O O   . ARG A 429 ? 0.27993 0.28585 0.29274 -0.00973 0.01392  -0.00828 429 ARG A O   
3441 C CB  . ARG A 429 ? 0.39089 0.39286 0.40279 -0.01039 0.01262  -0.00692 429 ARG A CB  
3442 C CG  . ARG A 429 ? 0.46411 0.46455 0.47679 -0.01122 0.01268  -0.00597 429 ARG A CG  
3443 C CD  . ARG A 429 ? 0.45658 0.45511 0.46732 -0.01108 0.01205  -0.00488 429 ARG A CD  
3444 N NE  . ARG A 429 ? 0.47354 0.47052 0.48502 -0.01193 0.01206  -0.00371 429 ARG A NE  
3445 C CZ  . ARG A 429 ? 0.48295 0.47893 0.49288 -0.01269 0.01268  -0.00232 429 ARG A CZ  
3446 N NH1 . ARG A 429 ? 0.48462 0.48087 0.49204 -0.01275 0.01350  -0.00205 429 ARG A NH1 
3447 N NH2 . ARG A 429 ? 0.48893 0.48347 0.49976 -0.01346 0.01253  -0.00118 429 ARG A NH2 
3448 N N   . PHE A 430 ? 0.38741 0.39322 0.40067 -0.00898 0.01190  -0.00942 430 PHE A N   
3449 C CA  . PHE A 430 ? 0.31722 0.32437 0.32995 -0.00824 0.01175  -0.00993 430 PHE A CA  
3450 C C   . PHE A 430 ? 0.29101 0.30004 0.30613 -0.00847 0.01208  -0.01044 430 PHE A C   
3451 O O   . PHE A 430 ? 0.29150 0.30156 0.30657 -0.00808 0.01255  -0.01046 430 PHE A O   
3452 C CB  . PHE A 430 ? 0.21529 0.22242 0.22740 -0.00754 0.01060  -0.01064 430 PHE A CB  
3453 C CG  . PHE A 430 ? 0.31168 0.32011 0.32330 -0.00679 0.01030  -0.01107 430 PHE A CG  
3454 C CD1 . PHE A 430 ? 0.31901 0.32703 0.32865 -0.00614 0.01044  -0.01064 430 PHE A CD1 
3455 C CD2 . PHE A 430 ? 0.33229 0.34228 0.34553 -0.00676 0.00972  -0.01185 430 PHE A CD2 
3456 C CE1 . PHE A 430 ? 0.25440 0.26358 0.26383 -0.00545 0.01016  -0.01098 430 PHE A CE1 
3457 C CE2 . PHE A 430 ? 0.29494 0.30609 0.30791 -0.00608 0.00933  -0.01208 430 PHE A CE2 
3458 C CZ  . PHE A 430 ? 0.23458 0.24532 0.24571 -0.00540 0.00961  -0.01165 430 PHE A CZ  
3459 N N   . ILE A 431 ? 0.33094 0.34040 0.34841 -0.00911 0.01180  -0.01084 431 ILE A N   
3460 C CA  . ILE A 431 ? 0.28810 0.29939 0.30836 -0.00940 0.01189  -0.01128 431 ILE A CA  
3461 C C   . ILE A 431 ? 0.32785 0.33942 0.34920 -0.00993 0.01350  -0.01056 431 ILE A C   
3462 O O   . ILE A 431 ? 0.28170 0.29474 0.30465 -0.00981 0.01410  -0.01067 431 ILE A O   
3463 C CB  . ILE A 431 ? 0.28264 0.29421 0.30501 -0.00997 0.01086  -0.01204 431 ILE A CB  
3464 C CG1 . ILE A 431 ? 0.28401 0.29534 0.30499 -0.00946 0.00945  -0.01289 431 ILE A CG1 
3465 C CG2 . ILE A 431 ? 0.35344 0.36686 0.37916 -0.01041 0.01084  -0.01232 431 ILE A CG2 
3466 C CD1 . ILE A 431 ? 0.26900 0.28035 0.29150 -0.01007 0.00840  -0.01383 431 ILE A CD1 
3467 N N   . ARG A 432 ? 0.19543 0.20551 0.21598 -0.01055 0.01430  -0.00978 432 ARG A N   
3468 C CA  . ARG A 432 ? 0.33585 0.34594 0.35701 -0.01117 0.01602  -0.00903 432 ARG A CA  
3469 C C   . ARG A 432 ? 0.28842 0.29843 0.30736 -0.01071 0.01714  -0.00870 432 ARG A C   
3470 O O   . ARG A 432 ? 0.37118 0.38167 0.39098 -0.01109 0.01875  -0.00842 432 ARG A O   
3471 C CB  . ARG A 432 ? 0.37322 0.38150 0.39360 -0.01198 0.01647  -0.00811 432 ARG A CB  
3472 C CG  . ARG A 432 ? 0.43346 0.44163 0.45629 -0.01254 0.01558  -0.00845 432 ARG A CG  
3473 C CD  . ARG A 432 ? 0.40445 0.41071 0.42660 -0.01328 0.01598  -0.00739 432 ARG A CD  
3474 N NE  . ARG A 432 ? 0.50093 0.50673 0.52506 -0.01364 0.01494  -0.00785 432 ARG A NE  
3475 C CZ  . ARG A 432 ? 0.42888 0.43522 0.45620 -0.01443 0.01509  -0.00803 432 ARG A CZ  
3476 N NH1 . ARG A 432 ? 0.40884 0.41632 0.43805 -0.01494 0.01630  -0.00772 432 ARG A NH1 
3477 N NH2 . ARG A 432 ? 0.43570 0.44139 0.46452 -0.01472 0.01409  -0.00859 432 ARG A NH2 
3478 N N   . LYS A 433 ? 0.25102 0.26036 0.26721 -0.00994 0.01641  -0.00879 433 LYS A N   
3479 C CA  . LYS A 433 ? 0.29748 0.30655 0.31141 -0.00952 0.01736  -0.00858 433 LYS A CA  
3480 C C   . LYS A 433 ? 0.29054 0.30158 0.30649 -0.00892 0.01760  -0.00932 433 LYS A C   
3481 O O   . LYS A 433 ? 0.36405 0.37557 0.38056 -0.00905 0.01919  -0.00927 433 LYS A O   
3482 C CB  . LYS A 433 ? 0.33134 0.33897 0.34194 -0.00895 0.01640  -0.00835 433 LYS A CB  
3483 C CG  . LYS A 433 ? 0.25760 0.26491 0.26583 -0.00847 0.01709  -0.00832 433 LYS A CG  
3484 C CD  . LYS A 433 ? 0.30928 0.31561 0.31600 -0.00921 0.01893  -0.00771 433 LYS A CD  
3485 C CE  . LYS A 433 ? 0.26870 0.27483 0.27339 -0.00877 0.01984  -0.00797 433 LYS A CE  
3486 N NZ  . LYS A 433 ? 0.29997 0.30477 0.30156 -0.00825 0.01864  -0.00779 433 LYS A NZ  
3487 N N   . PHE A 434 ? 0.21664 0.22878 0.23374 -0.00830 0.01607  -0.00998 434 PHE A N   
3488 C CA  . PHE A 434 ? 0.26213 0.27608 0.28116 -0.00768 0.01596  -0.01053 434 PHE A CA  
3489 C C   . PHE A 434 ? 0.24133 0.25710 0.26463 -0.00811 0.01604  -0.01083 434 PHE A C   
3490 O O   . PHE A 434 ? 0.27580 0.29311 0.30138 -0.00774 0.01634  -0.01108 434 PHE A O   
3491 C CB  . PHE A 434 ? 0.23147 0.24568 0.24955 -0.00687 0.01421  -0.01096 434 PHE A CB  
3492 C CG  . PHE A 434 ? 0.28417 0.29681 0.29863 -0.00636 0.01406  -0.01068 434 PHE A CG  
3493 C CD1 . PHE A 434 ? 0.28446 0.29713 0.29772 -0.00575 0.01462  -0.01067 434 PHE A CD1 
3494 C CD2 . PHE A 434 ? 0.29636 0.30747 0.30892 -0.00653 0.01336  -0.01042 434 PHE A CD2 
3495 C CE1 . PHE A 434 ? 0.32942 0.34061 0.33953 -0.00534 0.01434  -0.01039 434 PHE A CE1 
3496 C CE2 . PHE A 434 ? 0.31729 0.32700 0.32696 -0.00609 0.01310  -0.01008 434 PHE A CE2 
3497 C CZ  . PHE A 434 ? 0.28322 0.29298 0.29160 -0.00552 0.01353  -0.01005 434 PHE A CZ  
3498 N N   . LEU A 435 ? 0.30789 0.32351 0.33262 -0.00889 0.01572  -0.01077 435 LEU A N   
3499 C CA  . LEU A 435 ? 0.28554 0.30276 0.31454 -0.00945 0.01573  -0.01099 435 LEU A CA  
3500 C C   . LEU A 435 ? 0.31162 0.32811 0.34136 -0.01040 0.01734  -0.01039 435 LEU A C   
3501 O O   . LEU A 435 ? 0.32042 0.33627 0.35069 -0.01106 0.01679  -0.01032 435 LEU A O   
3502 C CB  . LEU A 435 ? 0.23603 0.25378 0.26630 -0.00959 0.01361  -0.01159 435 LEU A CB  
3503 C CG  . LEU A 435 ? 0.31356 0.33207 0.34314 -0.00878 0.01197  -0.01210 435 LEU A CG  
3504 C CD1 . LEU A 435 ? 0.28908 0.30776 0.31931 -0.00912 0.01000  -0.01274 435 LEU A CD1 
3505 C CD2 . LEU A 435 ? 0.17853 0.19890 0.21076 -0.00835 0.01228  -0.01209 435 LEU A CD2 
3506 N N   . PRO A 436 ? 0.28312 0.29957 0.31286 -0.01052 0.01944  -0.00998 436 PRO A N   
3507 C CA  . PRO A 436 ? 0.32938 0.34494 0.35934 -0.01149 0.02117  -0.00928 436 PRO A CA  
3508 C C   . PRO A 436 ? 0.35490 0.37184 0.38964 -0.01224 0.02130  -0.00933 436 PRO A C   
3509 O O   . PRO A 436 ? 0.32917 0.34537 0.36439 -0.01312 0.02260  -0.00870 436 PRO A O   
3510 C CB  . PRO A 436 ? 0.36993 0.38517 0.39852 -0.01137 0.02345  -0.00903 436 PRO A CB  
3511 C CG  . PRO A 436 ? 0.39130 0.40822 0.42160 -0.01044 0.02303  -0.00973 436 PRO A CG  
3512 C CD  . PRO A 436 ? 0.25363 0.27072 0.28305 -0.00982 0.02044  -0.01015 436 PRO A CD  
3513 N N   . VAL A 437 ? 0.38715 0.40600 0.42543 -0.01198 0.01992  -0.00998 437 VAL A N   
3514 C CA  . VAL A 437 ? 0.32181 0.34194 0.36482 -0.01275 0.01967  -0.01005 437 VAL A CA  
3515 C C   . VAL A 437 ? 0.33880 0.35790 0.38142 -0.01339 0.01826  -0.01012 437 VAL A C   
3516 O O   . VAL A 437 ? 0.33399 0.35369 0.38015 -0.01422 0.01822  -0.01008 437 VAL A O   
3517 C CB  . VAL A 437 ? 0.25300 0.27541 0.29986 -0.01234 0.01830  -0.01066 437 VAL A CB  
3518 C CG1 . VAL A 437 ? 0.29734 0.31969 0.34292 -0.01203 0.01550  -0.01131 437 VAL A CG1 
3519 C CG2 . VAL A 437 ? 0.29222 0.31624 0.34477 -0.01311 0.01878  -0.01054 437 VAL A CG2 
3520 N N   . LEU A 438 ? 0.34773 0.36524 0.38639 -0.01304 0.01718  -0.01025 438 LEU A N   
3521 C CA  . LEU A 438 ? 0.32677 0.34304 0.36486 -0.01356 0.01601  -0.01039 438 LEU A CA  
3522 C C   . LEU A 438 ? 0.35206 0.36613 0.38693 -0.01382 0.01703  -0.00953 438 LEU A C   
3523 O O   . LEU A 438 ? 0.42959 0.44226 0.46291 -0.01390 0.01600  -0.00962 438 LEU A O   
3524 C CB  . LEU A 438 ? 0.34918 0.36541 0.38584 -0.01299 0.01379  -0.01131 438 LEU A CB  
3525 C CG  . LEU A 438 ? 0.31898 0.33714 0.35843 -0.01286 0.01227  -0.01210 438 LEU A CG  
3526 C CD1 . LEU A 438 ? 0.17565 0.19362 0.21233 -0.01205 0.01064  -0.01275 438 LEU A CD1 
3527 C CD2 . LEU A 438 ? 0.27121 0.28973 0.31391 -0.01382 0.01126  -0.01254 438 LEU A CD2 
3528 N N   . LYS A 439 ? 0.32768 0.34132 0.36151 -0.01400 0.01905  -0.00867 439 LYS A N   
3529 C CA  . LYS A 439 ? 0.41556 0.42699 0.44584 -0.01428 0.01985  -0.00770 439 LYS A CA  
3530 C C   . LYS A 439 ? 0.43861 0.44900 0.47024 -0.01528 0.01990  -0.00710 439 LYS A C   
3531 O O   . LYS A 439 ? 0.43543 0.44393 0.46463 -0.01542 0.01947  -0.00651 439 LYS A O   
3532 C CB  . LYS A 439 ? 0.38829 0.39940 0.41680 -0.01435 0.02205  -0.00699 439 LYS A CB  
3533 C CG  . LYS A 439 ? 0.34621 0.35842 0.37815 -0.01509 0.02395  -0.00671 439 LYS A CG  
3534 C CD  . LYS A 439 ? 0.38952 0.40106 0.41914 -0.01523 0.02638  -0.00612 439 LYS A CD  
3535 C CE  . LYS A 439 ? 0.40179 0.41441 0.43511 -0.01598 0.02855  -0.00586 439 LYS A CE  
3536 N NZ  . LYS A 439 ? 0.40714 0.41889 0.43791 -0.01620 0.03122  -0.00538 439 LYS A NZ  
3537 N N   . ASP A 440 ? 0.31514 0.32670 0.35089 -0.01598 0.02035  -0.00720 440 ASP A N   
3538 C CA  . ASP A 440 ? 0.39932 0.40996 0.43681 -0.01700 0.02054  -0.00659 440 ASP A CA  
3539 C C   . ASP A 440 ? 0.40603 0.41699 0.44605 -0.01716 0.01856  -0.00757 440 ASP A C   
3540 O O   . ASP A 440 ? 0.38804 0.39836 0.43016 -0.01802 0.01855  -0.00725 440 ASP A O   
3541 C CB  . ASP A 440 ? 0.41257 0.42407 0.45309 -0.01784 0.02255  -0.00594 440 ASP A CB  
3542 C CG  . ASP A 440 ? 0.50698 0.51769 0.54453 -0.01791 0.02482  -0.00495 440 ASP A CG  
3543 O OD1 . ASP A 440 ? 0.46935 0.47807 0.50260 -0.01785 0.02486  -0.00421 440 ASP A OD1 
3544 O OD2 . ASP A 440 ? 0.41553 0.42752 0.45509 -0.01805 0.02656  -0.00494 440 ASP A OD2 
3545 N N   . MET A 441 ? 0.39793 0.40971 0.43764 -0.01641 0.01691  -0.00875 441 MET A N   
3546 C CA  . MET A 441 ? 0.35364 0.36546 0.39507 -0.01662 0.01504  -0.00982 441 MET A CA  
3547 C C   . MET A 441 ? 0.34064 0.35026 0.37977 -0.01662 0.01443  -0.00972 441 MET A C   
3548 O O   . MET A 441 ? 0.39937 0.40790 0.43500 -0.01597 0.01453  -0.00933 441 MET A O   
3549 C CB  . MET A 441 ? 0.33233 0.34549 0.37355 -0.01587 0.01351  -0.01102 441 MET A CB  
3550 C CG  . MET A 441 ? 0.34443 0.35771 0.38728 -0.01623 0.01157  -0.01226 441 MET A CG  
3551 S SD  . MET A 441 ? 0.40772 0.42245 0.45618 -0.01738 0.01137  -0.01244 441 MET A SD  
3552 C CE  . MET A 441 ? 0.39368 0.41094 0.44413 -0.01692 0.01187  -0.01221 441 MET A CE  
3553 N N   . PRO A 442 ? 0.23332 0.24221 0.27460 -0.01736 0.01379  -0.01005 442 PRO A N   
3554 C CA  . PRO A 442 ? 0.33007 0.33687 0.36972 -0.01732 0.01321  -0.01006 442 PRO A CA  
3555 C C   . PRO A 442 ? 0.30296 0.30950 0.34013 -0.01641 0.01192  -0.01120 442 PRO A C   
3556 O O   . PRO A 442 ? 0.31824 0.32610 0.35566 -0.01609 0.01098  -0.01231 442 PRO A O   
3557 C CB  . PRO A 442 ? 0.29235 0.29877 0.33549 -0.01830 0.01269  -0.01055 442 PRO A CB  
3558 C CG  . PRO A 442 ? 0.36120 0.36917 0.40757 -0.01900 0.01359  -0.01006 442 PRO A CG  
3559 C CD  . PRO A 442 ? 0.34344 0.35327 0.38907 -0.01832 0.01374  -0.01029 442 PRO A CD  
3560 N N   . ALA A 443 ? 0.39271 0.39746 0.42757 -0.01602 0.01187  -0.01083 443 ALA A N   
3561 C CA  . ALA A 443 ? 0.31711 0.32146 0.34961 -0.01515 0.01092  -0.01178 443 ALA A CA  
3562 C C   . ALA A 443 ? 0.26761 0.27186 0.30130 -0.01536 0.00970  -0.01348 443 ALA A C   
3563 O O   . ALA A 443 ? 0.28876 0.29299 0.32054 -0.01471 0.00895  -0.01448 443 ALA A O   
3564 C CB  . ALA A 443 ? 0.36411 0.36652 0.39458 -0.01477 0.01116  -0.01090 443 ALA A CB  
3565 N N   . LYS A 444 ? 0.31514 0.31921 0.35177 -0.01630 0.00953  -0.01385 444 LYS A N   
3566 C CA  . LYS A 444 ? 0.30841 0.31216 0.34598 -0.01665 0.00833  -0.01560 444 LYS A CA  
3567 C C   . LYS A 444 ? 0.27607 0.28165 0.31363 -0.01659 0.00730  -0.01661 444 LYS A C   
3568 O O   . LYS A 444 ? 0.35546 0.36072 0.39192 -0.01654 0.00618  -0.01808 444 LYS A O   
3569 C CB  . LYS A 444 ? 0.25467 0.25769 0.29559 -0.01774 0.00838  -0.01568 444 LYS A CB  
3570 C CG  . LYS A 444 ? 0.33246 0.33450 0.37413 -0.01820 0.00726  -0.01755 444 LYS A CG  
3571 C CD  . LYS A 444 ? 0.30149 0.30343 0.34702 -0.01939 0.00712  -0.01769 444 LYS A CD  
3572 C CE  . LYS A 444 ? 0.34410 0.34522 0.39127 -0.01972 0.00841  -0.01590 444 LYS A CE  
3573 N NZ  . LYS A 444 ? 0.34181 0.34362 0.39291 -0.02082 0.00856  -0.01552 444 LYS A NZ  
3574 N N   . TYR A 445 ? 0.27440 0.28181 0.31319 -0.01663 0.00767  -0.01582 445 TYR A N   
3575 C CA  . TYR A 445 ? 0.30957 0.31884 0.34901 -0.01660 0.00660  -0.01653 445 TYR A CA  
3576 C C   . TYR A 445 ? 0.32707 0.33761 0.36472 -0.01566 0.00704  -0.01584 445 TYR A C   
3577 O O   . TYR A 445 ? 0.39599 0.40829 0.43477 -0.01561 0.00634  -0.01607 445 TYR A O   
3578 C CB  . TYR A 445 ? 0.36972 0.38028 0.41338 -0.01757 0.00648  -0.01640 445 TYR A CB  
3579 C CG  . TYR A 445 ? 0.36361 0.37294 0.40960 -0.01859 0.00624  -0.01687 445 TYR A CG  
3580 C CD1 . TYR A 445 ? 0.40948 0.41831 0.45589 -0.01915 0.00461  -0.01848 445 TYR A CD1 
3581 C CD2 . TYR A 445 ? 0.33125 0.33983 0.37893 -0.01905 0.00763  -0.01570 445 TYR A CD2 
3582 C CE1 . TYR A 445 ? 0.41807 0.42569 0.46676 -0.02010 0.00440  -0.01903 445 TYR A CE1 
3583 C CE2 . TYR A 445 ? 0.36331 0.37073 0.41340 -0.01999 0.00742  -0.01608 445 TYR A CE2 
3584 C CZ  . TYR A 445 ? 0.42276 0.42971 0.47346 -0.02049 0.00581  -0.01780 445 TYR A CZ  
3585 O OH  . TYR A 445 ? 0.49139 0.49709 0.54460 -0.02144 0.00560  -0.01828 445 TYR A OH  
3586 N N   . ILE A 446 ? 0.33477 0.34443 0.36984 -0.01494 0.00808  -0.01499 446 ILE A N   
3587 C CA  . ILE A 446 ? 0.29519 0.30593 0.32871 -0.01412 0.00863  -0.01433 446 ILE A CA  
3588 C C   . ILE A 446 ? 0.32986 0.34115 0.36135 -0.01341 0.00739  -0.01522 446 ILE A C   
3589 O O   . ILE A 446 ? 0.36808 0.38072 0.39921 -0.01284 0.00745  -0.01491 446 ILE A O   
3590 C CB  . ILE A 446 ? 0.31385 0.32334 0.34509 -0.01369 0.00995  -0.01314 446 ILE A CB  
3591 C CG1 . ILE A 446 ? 0.35811 0.36874 0.38852 -0.01314 0.01088  -0.01236 446 ILE A CG1 
3592 C CG2 . ILE A 446 ? 0.33069 0.33863 0.35907 -0.01307 0.00943  -0.01351 446 ILE A CG2 
3593 C CD1 . ILE A 446 ? 0.39674 0.40608 0.42478 -0.01291 0.01212  -0.01116 446 ILE A CD1 
3594 N N   . TYR A 447 ? 0.32143 0.33163 0.35158 -0.01345 0.00636  -0.01631 447 TYR A N   
3595 C CA  . TYR A 447 ? 0.25538 0.26600 0.28348 -0.01294 0.00516  -0.01717 447 TYR A CA  
3596 C C   . TYR A 447 ? 0.33113 0.34279 0.36087 -0.01361 0.00359  -0.01813 447 TYR A C   
3597 O O   . TYR A 447 ? 0.32866 0.34117 0.35719 -0.01328 0.00251  -0.01850 447 TYR A O   
3598 C CB  . TYR A 447 ? 0.31188 0.32061 0.33717 -0.01258 0.00507  -0.01786 447 TYR A CB  
3599 C CG  . TYR A 447 ? 0.24053 0.24847 0.26379 -0.01171 0.00615  -0.01692 447 TYR A CG  
3600 C CD1 . TYR A 447 ? 0.22421 0.23278 0.24535 -0.01082 0.00607  -0.01665 447 TYR A CD1 
3601 C CD2 . TYR A 447 ? 0.26721 0.27372 0.29079 -0.01184 0.00711  -0.01622 447 TYR A CD2 
3602 C CE1 . TYR A 447 ? 0.30639 0.31419 0.32580 -0.01009 0.00690  -0.01581 447 TYR A CE1 
3603 C CE2 . TYR A 447 ? 0.28026 0.28599 0.30204 -0.01113 0.00784  -0.01529 447 TYR A CE2 
3604 C CZ  . TYR A 447 ? 0.29761 0.30400 0.31731 -0.01027 0.00772  -0.01514 447 TYR A CZ  
3605 O OH  . TYR A 447 ? 0.27913 0.28469 0.29714 -0.00963 0.00829  -0.01424 447 TYR A OH  
3606 N N   . GLU A 448 ? 0.27961 0.29117 0.31213 -0.01461 0.00334  -0.01847 448 GLU A N   
3607 C CA  . GLU A 448 ? 0.29531 0.30786 0.32986 -0.01542 0.00168  -0.01930 448 GLU A CA  
3608 C C   . GLU A 448 ? 0.37679 0.39062 0.41572 -0.01607 0.00220  -0.01854 448 GLU A C   
3609 O O   . GLU A 448 ? 0.37078 0.38398 0.41192 -0.01698 0.00213  -0.01888 448 GLU A O   
3610 C CB  . GLU A 448 ? 0.39927 0.41014 0.43282 -0.01614 0.00065  -0.02080 448 GLU A CB  
3611 C CG  . GLU A 448 ? 0.33060 0.33976 0.36000 -0.01552 0.00079  -0.02153 448 GLU A CG  
3612 C CD  . GLU A 448 ? 0.44039 0.44783 0.46871 -0.01629 -0.00011 -0.02323 448 GLU A CD  
3613 O OE1 . GLU A 448 ? 0.40942 0.41733 0.43807 -0.01705 -0.00180 -0.02413 448 GLU A OE1 
3614 O OE2 . GLU A 448 ? 0.42167 0.42721 0.44889 -0.01617 0.00084  -0.02368 448 GLU A OE2 
3615 N N   . PRO A 449 ? 0.32829 0.34388 0.36874 -0.01565 0.00285  -0.01752 449 PRO A N   
3616 C CA  . PRO A 449 ? 0.35162 0.36841 0.39638 -0.01625 0.00374  -0.01673 449 PRO A CA  
3617 C C   . PRO A 449 ? 0.37515 0.39299 0.42359 -0.01724 0.00210  -0.01736 449 PRO A C   
3618 O O   . PRO A 449 ? 0.30125 0.31961 0.35348 -0.01799 0.00276  -0.01692 449 PRO A O   
3619 C CB  . PRO A 449 ? 0.27352 0.29183 0.31861 -0.01544 0.00481  -0.01574 449 PRO A CB  
3620 C CG  . PRO A 449 ? 0.36948 0.38805 0.41174 -0.01467 0.00352  -0.01621 449 PRO A CG  
3621 C CD  . PRO A 449 ? 0.31488 0.33141 0.35343 -0.01462 0.00291  -0.01708 449 PRO A CD  
3622 N N   . TRP A 450 ? 0.36954 0.38766 0.41699 -0.01736 -0.00007 -0.01832 450 TRP A N   
3623 C CA  . TRP A 450 ? 0.38916 0.40809 0.43988 -0.01843 -0.00198 -0.01896 450 TRP A CA  
3624 C C   . TRP A 450 ? 0.37609 0.39329 0.42715 -0.01943 -0.00234 -0.01991 450 TRP A C   
3625 O O   . TRP A 450 ? 0.32411 0.34189 0.37877 -0.02047 -0.00348 -0.02026 450 TRP A O   
3626 C CB  . TRP A 450 ? 0.33194 0.35141 0.38093 -0.01836 -0.00437 -0.01964 450 TRP A CB  
3627 C CG  . TRP A 450 ? 0.33619 0.35360 0.38006 -0.01825 -0.00514 -0.02082 450 TRP A CG  
3628 C CD1 . TRP A 450 ? 0.29798 0.31389 0.34063 -0.01918 -0.00657 -0.02223 450 TRP A CD1 
3629 C CD2 . TRP A 450 ? 0.36041 0.37699 0.39981 -0.01717 -0.00438 -0.02075 450 TRP A CD2 
3630 N NE1 . TRP A 450 ? 0.36235 0.37652 0.40000 -0.01874 -0.00657 -0.02307 450 TRP A NE1 
3631 C CE2 . TRP A 450 ? 0.36600 0.38060 0.40173 -0.01750 -0.00527 -0.02212 450 TRP A CE2 
3632 C CE3 . TRP A 450 ? 0.30161 0.31885 0.33982 -0.01600 -0.00301 -0.01970 450 TRP A CE3 
3633 C CZ2 . TRP A 450 ? 0.29848 0.31186 0.32969 -0.01667 -0.00474 -0.02238 450 TRP A CZ2 
3634 C CZ3 . TRP A 450 ? 0.29554 0.31157 0.32928 -0.01520 -0.00269 -0.01995 450 TRP A CZ3 
3635 C CH2 . TRP A 450 ? 0.30654 0.32073 0.33696 -0.01552 -0.00351 -0.02124 450 TRP A CH2 
3636 N N   . THR A 451 ? 0.44328 0.45837 0.49099 -0.01915 -0.00142 -0.02033 451 THR A N   
3637 C CA  . THR A 451 ? 0.44368 0.45696 0.49189 -0.02003 -0.00152 -0.02122 451 THR A CA  
3638 C C   . THR A 451 ? 0.49513 0.50832 0.54664 -0.02042 0.00022  -0.02020 451 THR A C   
3639 O O   . THR A 451 ? 0.53027 0.54221 0.58330 -0.02128 0.00008  -0.02079 451 THR A O   
3640 C CB  . THR A 451 ? 0.45230 0.46330 0.49599 -0.01955 -0.00119 -0.02209 451 THR A CB  
3641 O OG1 . THR A 451 ? 0.47061 0.48132 0.51263 -0.01853 0.00072  -0.02092 451 THR A OG1 
3642 C CG2 . THR A 451 ? 0.46093 0.47178 0.50110 -0.01932 -0.00284 -0.02318 451 THR A CG2 
3643 N N   . ALA A 452 ? 0.42829 0.44265 0.48086 -0.01987 0.00190  -0.01870 452 ALA A N   
3644 C CA  . ALA A 452 ? 0.44046 0.45465 0.49580 -0.02031 0.00368  -0.01759 452 ALA A CA  
3645 C C   . ALA A 452 ? 0.44011 0.45570 0.50072 -0.02138 0.00307  -0.01755 452 ALA A C   
3646 O O   . ALA A 452 ? 0.48864 0.50613 0.55127 -0.02142 0.00201  -0.01763 452 ALA A O   
3647 C CB  . ALA A 452 ? 0.39515 0.41000 0.44958 -0.01949 0.00573  -0.01608 452 ALA A CB  
3648 N N   . PRO A 453 ? 0.38362 0.39833 0.44685 -0.02228 0.00366  -0.01738 453 PRO A N   
3649 C CA  . PRO A 453 ? 0.50102 0.51709 0.56971 -0.02334 0.00324  -0.01722 453 PRO A CA  
3650 C C   . PRO A 453 ? 0.50727 0.52545 0.57874 -0.02307 0.00479  -0.01580 453 PRO A C   
3651 O O   . PRO A 453 ? 0.50799 0.52617 0.57722 -0.02225 0.00666  -0.01479 453 PRO A O   
3652 C CB  . PRO A 453 ? 0.51855 0.53294 0.58886 -0.02417 0.00409  -0.01703 453 PRO A CB  
3653 C CG  . PRO A 453 ? 0.55934 0.57138 0.62513 -0.02370 0.00400  -0.01775 453 PRO A CG  
3654 C CD  . PRO A 453 ? 0.44851 0.46087 0.51010 -0.02241 0.00455  -0.01736 453 PRO A CD  
3655 N N   A LEU A 454 ? 0.48230 0.50226 0.55885 -0.02382 0.00401  -0.01577 454 LEU A N   
3656 N N   B LEU A 454 ? 0.48225 0.50220 0.55879 -0.02382 0.00400  -0.01578 454 LEU A N   
3657 C CA  A LEU A 454 ? 0.48271 0.50477 0.56265 -0.02362 0.00558  -0.01455 454 LEU A CA  
3658 C CA  B LEU A 454 ? 0.48279 0.50486 0.56280 -0.02364 0.00555  -0.01456 454 LEU A CA  
3659 C C   A LEU A 454 ? 0.50107 0.52255 0.58172 -0.02377 0.00857  -0.01315 454 LEU A C   
3660 C C   B LEU A 454 ? 0.50106 0.52252 0.58165 -0.02377 0.00856  -0.01315 454 LEU A C   
3661 O O   A LEU A 454 ? 0.51315 0.53561 0.59404 -0.02325 0.01059  -0.01212 454 LEU A O   
3662 O O   B LEU A 454 ? 0.51352 0.53592 0.59417 -0.02322 0.01058  -0.01213 454 LEU A O   
3663 C CB  A LEU A 454 ? 0.47664 0.50066 0.56257 -0.02449 0.00404  -0.01478 454 LEU A CB  
3664 C CB  B LEU A 454 ? 0.47676 0.50074 0.56283 -0.02454 0.00405  -0.01478 454 LEU A CB  
3665 C CG  A LEU A 454 ? 0.47511 0.50116 0.56200 -0.02394 0.00251  -0.01497 454 LEU A CG  
3666 C CG  B LEU A 454 ? 0.47766 0.50398 0.56570 -0.02404 0.00306  -0.01468 454 LEU A CG  
3667 C CD1 A LEU A 454 ? 0.45106 0.47811 0.54203 -0.02495 -0.00042 -0.01577 454 LEU A CD1 
3668 C CD1 B LEU A 454 ? 0.49883 0.52650 0.58862 -0.02341 0.00592  -0.01332 454 LEU A CD1 
3669 C CD2 A LEU A 454 ? 0.48987 0.51779 0.57963 -0.02340 0.00484  -0.01368 454 LEU A CD2 
3670 C CD2 B LEU A 454 ? 0.43025 0.45603 0.51312 -0.02319 0.00127  -0.01556 454 LEU A CD2 
3671 N N   . GLU A 455 ? 0.51367 0.53343 0.59455 -0.02453 0.00892  -0.01308 455 GLU A N   
3672 C CA  . GLU A 455 ? 0.46299 0.48191 0.54395 -0.02475 0.01163  -0.01161 455 GLU A CA  
3673 C C   . GLU A 455 ? 0.47189 0.48950 0.54713 -0.02373 0.01297  -0.01102 455 GLU A C   
3674 O O   . GLU A 455 ? 0.51280 0.53040 0.58737 -0.02359 0.01535  -0.00970 455 GLU A O   
3675 C CB  . GLU A 455 ? 0.46523 0.48254 0.54796 -0.02581 0.01143  -0.01164 455 GLU A CB  
3676 C CG  . GLU A 455 ? 0.49136 0.50755 0.57406 -0.02618 0.01405  -0.00997 455 GLU A CG  
3677 C CD  . GLU A 455 ? 0.48472 0.49834 0.56285 -0.02588 0.01419  -0.00979 455 GLU A CD  
3678 O OE1 . GLU A 455 ? 0.49446 0.50712 0.57013 -0.02549 0.01233  -0.01113 455 GLU A OE1 
3679 O OE2 . GLU A 455 ? 0.47346 0.48596 0.55050 -0.02606 0.01616  -0.00828 455 GLU A OE2 
3680 N N   . VAL A 456 ? 0.49968 0.51614 0.57071 -0.02307 0.01148  -0.01200 456 VAL A N   
3681 C CA  . VAL A 456 ? 0.49731 0.51266 0.56316 -0.02207 0.01247  -0.01149 456 VAL A CA  
3682 C C   . VAL A 456 ? 0.46166 0.47869 0.52655 -0.02118 0.01298  -0.01131 456 VAL A C   
3683 O O   . VAL A 456 ? 0.47073 0.48734 0.53280 -0.02060 0.01469  -0.01040 456 VAL A O   
3684 C CB  . VAL A 456 ? 0.45395 0.46756 0.51610 -0.02165 0.01084  -0.01261 456 VAL A CB  
3685 C CG1 . VAL A 456 ? 0.42708 0.43950 0.48433 -0.02068 0.01181  -0.01197 456 VAL A CG1 
3686 C CG2 . VAL A 456 ? 0.45881 0.47075 0.52249 -0.02256 0.01037  -0.01292 456 VAL A CG2 
3687 N N   . GLN A 457 ? 0.49590 0.51475 0.56314 -0.02110 0.01145  -0.01215 457 GLN A N   
3688 C CA  . GLN A 457 ? 0.48704 0.50758 0.55409 -0.02026 0.01190  -0.01194 457 GLN A CA  
3689 C C   . GLN A 457 ? 0.47120 0.49283 0.54119 -0.02049 0.01446  -0.01074 457 GLN A C   
3690 O O   . GLN A 457 ? 0.40358 0.42551 0.47165 -0.01975 0.01602  -0.01020 457 GLN A O   
3691 C CB  . GLN A 457 ? 0.47590 0.49810 0.54526 -0.02025 0.00947  -0.01295 457 GLN A CB  
3692 C CG  . GLN A 457 ? 0.41903 0.44013 0.48480 -0.01999 0.00709  -0.01421 457 GLN A CG  
3693 C CD  . GLN A 457 ? 0.41520 0.43783 0.48286 -0.02009 0.00459  -0.01506 457 GLN A CD  
3694 O OE1 . GLN A 457 ? 0.42942 0.45120 0.49475 -0.02018 0.00250  -0.01618 457 GLN A OE1 
3695 N NE2 . GLN A 457 ? 0.41589 0.44072 0.48780 -0.02011 0.00481  -0.01449 457 GLN A NE2 
3696 N N   . ARG A 458 ? 0.50590 0.52805 0.58058 -0.02154 0.01502  -0.01035 458 ARG A N   
3697 C CA  . ARG A 458 ? 0.41223 0.43529 0.48985 -0.02186 0.01775  -0.00920 458 ARG A CA  
3698 C C   . ARG A 458 ? 0.48226 0.50342 0.55587 -0.02182 0.02019  -0.00809 458 ARG A C   
3699 O O   . ARG A 458 ? 0.45624 0.47772 0.52910 -0.02153 0.02252  -0.00734 458 ARG A O   
3700 C CB  . ARG A 458 ? 0.44341 0.46739 0.52717 -0.02306 0.01770  -0.00901 458 ARG A CB  
3701 C CG  . ARG A 458 ? 0.50447 0.53066 0.59318 -0.02323 0.01558  -0.00980 458 ARG A CG  
3702 C CD  . ARG A 458 ? 0.58932 0.61770 0.68133 -0.02279 0.01706  -0.00931 458 ARG A CD  
3703 N NE  . ARG A 458 ? 0.69821 0.72877 0.79591 -0.02311 0.01498  -0.00982 458 ARG A NE  
3704 C CZ  . ARG A 458 ? 0.67225 0.70399 0.77628 -0.02412 0.01508  -0.00950 458 ARG A CZ  
3705 N NH1 . ARG A 458 ? 0.67450 0.70547 0.78006 -0.02493 0.01729  -0.00868 458 ARG A NH1 
3706 N NH2 . ARG A 458 ? 0.67486 0.70856 0.78388 -0.02438 0.01282  -0.00994 458 ARG A NH2 
3707 N N   . LYS A 459 ? 0.41540 0.43445 0.48639 -0.02217 0.01966  -0.00797 459 LYS A N   
3708 C CA  . LYS A 459 ? 0.43675 0.45385 0.50407 -0.02228 0.02167  -0.00673 459 LYS A CA  
3709 C C   . LYS A 459 ? 0.46343 0.47982 0.52529 -0.02119 0.02204  -0.00669 459 LYS A C   
3710 O O   . LYS A 459 ? 0.28291 0.29864 0.34244 -0.02116 0.02424  -0.00568 459 LYS A O   
3711 C CB  . LYS A 459 ? 0.39817 0.41325 0.46465 -0.02290 0.02075  -0.00658 459 LYS A CB  
3712 C CG  . LYS A 459 ? 0.38856 0.40145 0.45123 -0.02308 0.02240  -0.00515 459 LYS A CG  
3713 C CD  . LYS A 459 ? 0.37348 0.38458 0.43689 -0.02387 0.02169  -0.00480 459 LYS A CD  
3714 C CE  . LYS A 459 ? 0.37368 0.38561 0.44273 -0.02503 0.02221  -0.00452 459 LYS A CE  
3715 N NZ  . LYS A 459 ? 0.36407 0.37417 0.43408 -0.02583 0.02161  -0.00413 459 LYS A NZ  
3716 N N   . ALA A 460 ? 0.43051 0.44693 0.49018 -0.02036 0.01994  -0.00778 460 ALA A N   
3717 C CA  . ALA A 460 ? 0.41218 0.42801 0.46702 -0.01931 0.02011  -0.00780 460 ALA A CA  
3718 C C   . ALA A 460 ? 0.37866 0.39622 0.43427 -0.01873 0.02127  -0.00783 460 ALA A C   
3719 O O   . ALA A 460 ? 0.37437 0.39142 0.42615 -0.01794 0.02182  -0.00773 460 ALA A O   
3720 C CB  . ALA A 460 ? 0.40387 0.41925 0.45645 -0.01864 0.01764  -0.00894 460 ALA A CB  
3721 N N   . GLY A 461 ? 0.35869 0.37823 0.41939 -0.01911 0.02164  -0.00797 461 GLY A N   
3722 C CA  . GLY A 461 ? 0.43251 0.45374 0.49469 -0.01854 0.02283  -0.00802 461 GLY A CA  
3723 C C   . GLY A 461 ? 0.31676 0.33923 0.37871 -0.01758 0.02079  -0.00901 461 GLY A C   
3724 O O   . GLY A 461 ? 0.33604 0.35928 0.39736 -0.01683 0.02169  -0.00903 461 GLY A O   
3725 N N   . CYS A 462 ? 0.34765 0.37021 0.40999 -0.01763 0.01808  -0.00983 462 CYS A N   
3726 C CA  . CYS A 462 ? 0.38245 0.40601 0.44419 -0.01682 0.01597  -0.01069 462 CYS A CA  
3727 C C   . CYS A 462 ? 0.43528 0.45965 0.50020 -0.01743 0.01341  -0.01147 462 CYS A C   
3728 O O   . CYS A 462 ? 0.40967 0.43264 0.47268 -0.01777 0.01203  -0.01200 462 CYS A O   
3729 C CB  . CYS A 462 ? 0.37554 0.39746 0.43140 -0.01600 0.01532  -0.01095 462 CYS A CB  
3730 S SG  . CYS A 462 ? 0.28192 0.30490 0.33656 -0.01501 0.01298  -0.01183 462 CYS A SG  
3731 N N   . VAL A 463 ? 0.42240 0.44892 0.49222 -0.01759 0.01278  -0.01156 463 VAL A N   
3732 C CA  . VAL A 463 ? 0.30521 0.33262 0.37823 -0.01824 0.01011  -0.01227 463 VAL A CA  
3733 C C   . VAL A 463 ? 0.39902 0.42707 0.47027 -0.01750 0.00779  -0.01292 463 VAL A C   
3734 O O   . VAL A 463 ? 0.41036 0.43974 0.48249 -0.01675 0.00820  -0.01261 463 VAL A O   
3735 C CB  . VAL A 463 ? 0.45544 0.48485 0.53540 -0.01897 0.01056  -0.01184 463 VAL A CB  
3736 C CG1 . VAL A 463 ? 0.47970 0.50999 0.56284 -0.01969 0.00741  -0.01258 463 VAL A CG1 
3737 C CG2 . VAL A 463 ? 0.45780 0.48647 0.53936 -0.01976 0.01297  -0.01111 463 VAL A CG2 
3738 N N   . VAL A 464 ? 0.43142 0.45841 0.50011 -0.01775 0.00544  -0.01383 464 VAL A N   
3739 C CA  . VAL A 464 ? 0.43464 0.46201 0.50124 -0.01720 0.00313  -0.01442 464 VAL A CA  
3740 C C   . VAL A 464 ? 0.39064 0.42028 0.46247 -0.01755 0.00144  -0.01432 464 VAL A C   
3741 O O   . VAL A 464 ? 0.38266 0.41274 0.45791 -0.01859 -0.00004 -0.01465 464 VAL A O   
3742 C CB  . VAL A 464 ? 0.41585 0.44138 0.47849 -0.01754 0.00124  -0.01550 464 VAL A CB  
3743 C CG1 . VAL A 464 ? 0.33879 0.36473 0.39939 -0.01716 -0.00121 -0.01606 464 VAL A CG1 
3744 C CG2 . VAL A 464 ? 0.34902 0.37240 0.40689 -0.01706 0.00286  -0.01548 464 VAL A CG2 
3745 N N   . GLY A 465 ? 0.40712 0.43821 0.47985 -0.01670 0.00157  -0.01384 465 GLY A N   
3746 C CA  . GLY A 465 ? 0.34138 0.37475 0.41953 -0.01689 0.00010  -0.01352 465 GLY A CA  
3747 C C   . GLY A 465 ? 0.32582 0.36087 0.40864 -0.01649 0.00258  -0.01261 465 GLY A C   
3748 O O   . GLY A 465 ? 0.31356 0.35056 0.40053 -0.01623 0.00169  -0.01222 465 GLY A O   
3749 N N   . ARG A 466 ? 0.37294 0.40722 0.45524 -0.01647 0.00569  -0.01225 466 ARG A N   
3750 C CA  . ARG A 466 ? 0.35790 0.39337 0.44378 -0.01612 0.00859  -0.01150 466 ARG A CA  
3751 C C   . ARG A 466 ? 0.34686 0.38118 0.42800 -0.01513 0.01101  -0.01132 466 ARG A C   
3752 O O   . ARG A 466 ? 0.34095 0.37634 0.42371 -0.01439 0.01233  -0.01100 466 ARG A O   
3753 C CB  . ARG A 466 ? 0.32578 0.36132 0.41539 -0.01711 0.01046  -0.01112 466 ARG A CB  
3754 C CG  . ARG A 466 ? 0.30064 0.33726 0.39396 -0.01689 0.01380  -0.01040 466 ARG A CG  
3755 C CD  . ARG A 466 ? 0.39654 0.43252 0.49157 -0.01785 0.01612  -0.00995 466 ARG A CD  
3756 N NE  . ARG A 466 ? 0.32588 0.35934 0.41456 -0.01788 0.01727  -0.00995 466 ARG A NE  
3757 C CZ  . ARG A 466 ? 0.33132 0.36368 0.41993 -0.01866 0.01929  -0.00944 466 ARG A CZ  
3758 N NH1 . ARG A 466 ? 0.34181 0.37532 0.43623 -0.01949 0.02058  -0.00894 466 ARG A NH1 
3759 N NH2 . ARG A 466 ? 0.31017 0.34022 0.39293 -0.01863 0.01999  -0.00934 466 ARG A NH2 
3760 N N   . ASP A 467 ? 0.36667 0.39877 0.44215 -0.01512 0.01157  -0.01152 467 ASP A N   
3761 C CA  . ASP A 467 ? 0.36182 0.39257 0.43238 -0.01429 0.01355  -0.01133 467 ASP A CA  
3762 C C   . ASP A 467 ? 0.29158 0.32130 0.35690 -0.01353 0.01174  -0.01182 467 ASP A C   
3763 O O   . ASP A 467 ? 0.33720 0.36678 0.40016 -0.01261 0.01255  -0.01171 467 ASP A O   
3764 C CB  . ASP A 467 ? 0.32032 0.34924 0.38843 -0.01484 0.01570  -0.01097 467 ASP A CB  
3765 C CG  . ASP A 467 ? 0.35942 0.38916 0.43253 -0.01575 0.01751  -0.01044 467 ASP A CG  
3766 O OD1 . ASP A 467 ? 0.34431 0.37591 0.42218 -0.01564 0.01844  -0.01022 467 ASP A OD1 
3767 O OD2 . ASP A 467 ? 0.34184 0.37036 0.41438 -0.01657 0.01804  -0.01021 467 ASP A OD2 
3768 N N   . TYR A 468 ? 0.26455 0.29347 0.32806 -0.01393 0.00941  -0.01239 468 TYR A N   
3769 C CA  . TYR A 468 ? 0.32307 0.35100 0.38184 -0.01331 0.00771  -0.01289 468 TYR A CA  
3770 C C   . TYR A 468 ? 0.33773 0.36650 0.39795 -0.01369 0.00462  -0.01345 468 TYR A C   
3771 O O   . TYR A 468 ? 0.35452 0.38349 0.41736 -0.01467 0.00355  -0.01374 468 TYR A O   
3772 C CB  . TYR A 468 ? 0.31830 0.34386 0.37228 -0.01344 0.00815  -0.01312 468 TYR A CB  
3773 C CG  . TYR A 468 ? 0.32986 0.35430 0.37893 -0.01268 0.00699  -0.01355 468 TYR A CG  
3774 C CD1 . TYR A 468 ? 0.32285 0.34693 0.36909 -0.01170 0.00813  -0.01319 468 TYR A CD1 
3775 C CD2 . TYR A 468 ? 0.21894 0.24262 0.26621 -0.01299 0.00485  -0.01434 468 TYR A CD2 
3776 C CE1 . TYR A 468 ? 0.33537 0.35849 0.37747 -0.01103 0.00714  -0.01352 468 TYR A CE1 
3777 C CE2 . TYR A 468 ? 0.21787 0.24051 0.26078 -0.01233 0.00402  -0.01471 468 TYR A CE2 
3778 C CZ  . TYR A 468 ? 0.29187 0.31430 0.33237 -0.01134 0.00516  -0.01424 468 TYR A CZ  
3779 O OH  . TYR A 468 ? 0.23760 0.25905 0.27408 -0.01069 0.00439  -0.01455 468 TYR A OH  
3780 N N   . PRO A 469 ? 0.28570 0.31490 0.34423 -0.01300 0.00308  -0.01357 469 PRO A N   
3781 C CA  . PRO A 469 ? 0.28116 0.31118 0.34100 -0.01344 0.00003  -0.01396 469 PRO A CA  
3782 C C   . PRO A 469 ? 0.37681 0.40508 0.43311 -0.01410 -0.00158 -0.01488 469 PRO A C   
3783 O O   . PRO A 469 ? 0.35009 0.37649 0.40224 -0.01391 -0.00058 -0.01521 469 PRO A O   
3784 C CB  . PRO A 469 ? 0.31925 0.34989 0.37751 -0.01244 -0.00077 -0.01368 469 PRO A CB  
3785 C CG  . PRO A 469 ? 0.30254 0.33184 0.35660 -0.01155 0.00140  -0.01356 469 PRO A CG  
3786 C CD  . PRO A 469 ? 0.30943 0.33841 0.36503 -0.01184 0.00404  -0.01328 469 PRO A CD  
3787 N N   . ALA A 470 ? 0.42398 0.45281 0.48213 -0.01494 -0.00415 -0.01531 470 ALA A N   
3788 C CA  . ALA A 470 ? 0.34427 0.37141 0.39915 -0.01567 -0.00583 -0.01636 470 ALA A CA  
3789 C C   . ALA A 470 ? 0.29666 0.32277 0.34620 -0.01505 -0.00693 -0.01674 470 ALA A C   
3790 O O   . ALA A 470 ? 0.24119 0.26828 0.29047 -0.01423 -0.00714 -0.01611 470 ALA A O   
3791 C CB  . ALA A 470 ? 0.30058 0.32855 0.35907 -0.01688 -0.00831 -0.01673 470 ALA A CB  
3792 N N   . PRO A 471 ? 0.28976 0.31382 0.33509 -0.01542 -0.00747 -0.01776 471 PRO A N   
3793 C CA  . PRO A 471 ? 0.26217 0.28517 0.30241 -0.01492 -0.00840 -0.01815 471 PRO A CA  
3794 C C   . PRO A 471 ? 0.26057 0.28464 0.30126 -0.01525 -0.01119 -0.01805 471 PRO A C   
3795 O O   . PRO A 471 ? 0.23820 0.26257 0.28087 -0.01635 -0.01321 -0.01848 471 PRO A O   
3796 C CB  . PRO A 471 ? 0.30023 0.32086 0.33694 -0.01551 -0.00839 -0.01941 471 PRO A CB  
3797 C CG  . PRO A 471 ? 0.26338 0.28411 0.30381 -0.01660 -0.00859 -0.01978 471 PRO A CG  
3798 C CD  . PRO A 471 ? 0.28479 0.30731 0.32986 -0.01627 -0.00703 -0.01859 471 PRO A CD  
3799 N N   . ILE A 472 ? 0.26019 0.28476 0.29907 -0.01434 -0.01140 -0.01742 472 ILE A N   
3800 C CA  . ILE A 472 ? 0.28497 0.31063 0.32443 -0.01458 -0.01407 -0.01702 472 ILE A CA  
3801 C C   . ILE A 472 ? 0.26557 0.28955 0.30062 -0.01549 -0.01626 -0.01807 472 ILE A C   
3802 O O   . ILE A 472 ? 0.32925 0.35382 0.36512 -0.01628 -0.01900 -0.01798 472 ILE A O   
3803 C CB  . ILE A 472 ? 0.26434 0.29088 0.30310 -0.01334 -0.01357 -0.01599 472 ILE A CB  
3804 C CG1 . ILE A 472 ? 0.22040 0.24507 0.25332 -0.01264 -0.01243 -0.01639 472 ILE A CG1 
3805 C CG2 . ILE A 472 ? 0.29466 0.32279 0.33789 -0.01257 -0.01143 -0.01511 472 ILE A CG2 
3806 C CD1 . ILE A 472 ? 0.28837 0.31374 0.32042 -0.01146 -0.01201 -0.01544 472 ILE A CD1 
3807 N N   . VAL A 473 ? 0.21495 0.23673 0.24530 -0.01544 -0.01511 -0.01906 473 VAL A N   
3808 C CA  . VAL A 473 ? 0.29130 0.31116 0.31685 -0.01624 -0.01671 -0.02022 473 VAL A CA  
3809 C C   . VAL A 473 ? 0.28769 0.30546 0.31138 -0.01669 -0.01530 -0.02158 473 VAL A C   
3810 O O   . VAL A 473 ? 0.21107 0.22866 0.23600 -0.01611 -0.01294 -0.02143 473 VAL A O   
3811 C CB  . VAL A 473 ? 0.27030 0.28939 0.29096 -0.01551 -0.01679 -0.01998 473 VAL A CB  
3812 C CG1 . VAL A 473 ? 0.29281 0.31373 0.31506 -0.01527 -0.01870 -0.01868 473 VAL A CG1 
3813 C CG2 . VAL A 473 ? 0.25979 0.27840 0.27914 -0.01422 -0.01390 -0.01968 473 VAL A CG2 
3814 N N   . ASP A 474 ? 0.35000 0.36608 0.37062 -0.01779 -0.01683 -0.02291 474 ASP A N   
3815 C CA  . ASP A 474 ? 0.28536 0.29908 0.30341 -0.01819 -0.01556 -0.02439 474 ASP A CA  
3816 C C   . ASP A 474 ? 0.30565 0.31763 0.31808 -0.01756 -0.01460 -0.02486 474 ASP A C   
3817 O O   . ASP A 474 ? 0.32950 0.34089 0.33829 -0.01793 -0.01620 -0.02513 474 ASP A O   
3818 C CB  . ASP A 474 ? 0.37202 0.38466 0.38991 -0.01979 -0.01759 -0.02577 474 ASP A CB  
3819 C CG  . ASP A 474 ? 0.37127 0.38156 0.38761 -0.02022 -0.01613 -0.02733 474 ASP A CG  
3820 O OD1 . ASP A 474 ? 0.35036 0.36002 0.36629 -0.01928 -0.01360 -0.02719 474 ASP A OD1 
3821 O OD2 . ASP A 474 ? 0.36730 0.37631 0.38295 -0.02154 -0.01759 -0.02871 474 ASP A OD2 
3822 N N   . HIS A 475 ? 0.33298 0.34413 0.34478 -0.01666 -0.01201 -0.02486 475 HIS A N   
3823 C CA  . HIS A 475 ? 0.32235 0.33209 0.32958 -0.01590 -0.01084 -0.02510 475 HIS A CA  
3824 C C   . HIS A 475 ? 0.29530 0.30269 0.29793 -0.01684 -0.01159 -0.02678 475 HIS A C   
3825 O O   . HIS A 475 ? 0.34715 0.35388 0.34569 -0.01673 -0.01208 -0.02685 475 HIS A O   
3826 C CB  . HIS A 475 ? 0.33824 0.34737 0.34616 -0.01494 -0.00813 -0.02487 475 HIS A CB  
3827 C CG  . HIS A 475 ? 0.31336 0.32118 0.31735 -0.01411 -0.00680 -0.02499 475 HIS A CG  
3828 N ND1 . HIS A 475 ? 0.46065 0.46679 0.46378 -0.01374 -0.00480 -0.02558 475 HIS A ND1 
3829 C CD2 . HIS A 475 ? 0.36771 0.37568 0.36872 -0.01359 -0.00719 -0.02452 475 HIS A CD2 
3830 C CE1 . HIS A 475 ? 0.34059 0.34593 0.34051 -0.01302 -0.00396 -0.02552 475 HIS A CE1 
3831 N NE2 . HIS A 475 ? 0.35102 0.35743 0.34947 -0.01293 -0.00535 -0.02488 475 HIS A NE2 
3832 N N   . ALA A 476 ? 0.26863 0.27465 0.27178 -0.01783 -0.01163 -0.02819 476 ALA A N   
3833 C CA  . ALA A 476 ? 0.32018 0.32370 0.31884 -0.01881 -0.01215 -0.03003 476 ALA A CA  
3834 C C   . ALA A 476 ? 0.34028 0.34395 0.33626 -0.01975 -0.01495 -0.03014 476 ALA A C   
3835 O O   . ALA A 476 ? 0.47542 0.47713 0.46622 -0.02028 -0.01526 -0.03124 476 ALA A O   
3836 C CB  . ALA A 476 ? 0.39396 0.39610 0.39435 -0.01977 -0.01189 -0.03149 476 ALA A CB  
3837 N N   . VAL A 477 ? 0.28637 0.29228 0.28581 -0.02002 -0.01698 -0.02897 477 VAL A N   
3838 C CA  . VAL A 477 ? 0.33743 0.34369 0.33486 -0.02091 -0.01995 -0.02874 477 VAL A CA  
3839 C C   . VAL A 477 ? 0.33560 0.34291 0.33122 -0.01991 -0.02007 -0.02724 477 VAL A C   
3840 O O   . VAL A 477 ? 0.34431 0.35070 0.33546 -0.02045 -0.02157 -0.02737 477 VAL A O   
3841 C CB  . VAL A 477 ? 0.27516 0.28334 0.27778 -0.02171 -0.02224 -0.02815 477 VAL A CB  
3842 C CG1 . VAL A 477 ? 0.36120 0.36974 0.36204 -0.02271 -0.02565 -0.02778 477 VAL A CG1 
3843 C CG2 . VAL A 477 ? 0.26044 0.26748 0.26495 -0.02274 -0.02210 -0.02964 477 VAL A CG2 
3844 N N   . ALA A 478 ? 0.34965 0.35878 0.34854 -0.01850 -0.01847 -0.02579 478 ALA A N   
3845 C CA  . ALA A 478 ? 0.35795 0.36821 0.35578 -0.01753 -0.01861 -0.02431 478 ALA A CA  
3846 C C   . ALA A 478 ? 0.27808 0.28651 0.27081 -0.01689 -0.01679 -0.02475 478 ALA A C   
3847 O O   . ALA A 478 ? 0.31257 0.32090 0.30213 -0.01673 -0.01761 -0.02410 478 ALA A O   
3848 C CB  . ALA A 478 ? 0.27075 0.28344 0.27382 -0.01632 -0.01749 -0.02275 478 ALA A CB  
3849 N N   . SER A 479 ? 0.32036 0.32732 0.31247 -0.01653 -0.01433 -0.02575 479 SER A N   
3850 C CA  . SER A 479 ? 0.33275 0.33812 0.32084 -0.01581 -0.01236 -0.02609 479 SER A CA  
3851 C C   . SER A 479 ? 0.37594 0.37910 0.35820 -0.01684 -0.01325 -0.02731 479 SER A C   
3852 O O   . SER A 479 ? 0.40978 0.41246 0.38846 -0.01646 -0.01304 -0.02683 479 SER A O   
3853 C CB  . SER A 479 ? 0.35910 0.36339 0.34845 -0.01527 -0.00971 -0.02685 479 SER A CB  
3854 O OG  . SER A 479 ? 0.42377 0.42666 0.41336 -0.01637 -0.00990 -0.02845 479 SER A OG  
3855 N N   . LYS A 480 ? 0.37616 0.37784 0.35726 -0.01820 -0.01422 -0.02893 480 LYS A N   
3856 C CA  . LYS A 480 ? 0.42482 0.42409 0.39991 -0.01934 -0.01499 -0.03030 480 LYS A CA  
3857 C C   . LYS A 480 ? 0.45421 0.45422 0.42682 -0.01984 -0.01766 -0.02918 480 LYS A C   
3858 O O   . LYS A 480 ? 0.52139 0.51965 0.48835 -0.02031 -0.01778 -0.02962 480 LYS A O   
3859 C CB  . LYS A 480 ? 0.45149 0.44908 0.42616 -0.02081 -0.01579 -0.03227 480 LYS A CB  
3860 C CG  . LYS A 480 ? 0.50189 0.49847 0.47894 -0.02045 -0.01328 -0.03345 480 LYS A CG  
3861 C CD  . LYS A 480 ? 0.55552 0.54931 0.52969 -0.02188 -0.01338 -0.03588 480 LYS A CD  
3862 C CE  . LYS A 480 ? 0.58106 0.57496 0.55488 -0.02351 -0.01673 -0.03633 480 LYS A CE  
3863 N NZ  . LYS A 480 ? 0.59935 0.59162 0.56665 -0.02456 -0.01836 -0.03690 480 LYS A NZ  
3864 N N   . ALA A 481 ? 0.45171 0.45424 0.42854 -0.01978 -0.01976 -0.02767 481 ALA A N   
3865 C CA  . ALA A 481 ? 0.38820 0.39166 0.36345 -0.02012 -0.02238 -0.02630 481 ALA A CA  
3866 C C   . ALA A 481 ? 0.35789 0.36182 0.33155 -0.01881 -0.02102 -0.02494 481 ALA A C   
3867 O O   . ALA A 481 ? 0.40324 0.40618 0.37214 -0.01921 -0.02197 -0.02459 481 ALA A O   
3868 C CB  . ALA A 481 ? 0.44607 0.45224 0.42718 -0.02024 -0.02471 -0.02498 481 ALA A CB  
3869 N N   . CYS A 482 ? 0.37083 0.37616 0.34828 -0.01730 -0.01880 -0.02413 482 CYS A N   
3870 C CA  . CYS A 482 ? 0.39319 0.39900 0.36960 -0.01602 -0.01748 -0.02286 482 CYS A CA  
3871 C C   . CYS A 482 ? 0.38087 0.38416 0.35190 -0.01596 -0.01539 -0.02392 482 CYS A C   
3872 O O   . CYS A 482 ? 0.45142 0.45442 0.41944 -0.01556 -0.01520 -0.02307 482 CYS A O   
3873 C CB  . CYS A 482 ? 0.36706 0.37478 0.34874 -0.01455 -0.01570 -0.02189 482 CYS A CB  
3874 S SG  . CYS A 482 ? 0.35085 0.36162 0.33924 -0.01445 -0.01758 -0.02054 482 CYS A SG  
3875 N N   . ILE A 483 ? 0.39530 0.39675 0.36532 -0.01634 -0.01372 -0.02574 483 ILE A N   
3876 C CA  . ILE A 483 ? 0.41951 0.41850 0.38490 -0.01627 -0.01147 -0.02688 483 ILE A CA  
3877 C C   . ILE A 483 ? 0.43448 0.43165 0.39359 -0.01751 -0.01288 -0.02739 483 ILE A C   
3878 O O   . ILE A 483 ? 0.51297 0.50907 0.46821 -0.01720 -0.01170 -0.02714 483 ILE A O   
3879 C CB  . ILE A 483 ? 0.40236 0.39976 0.36859 -0.01647 -0.00950 -0.02876 483 ILE A CB  
3880 C CG1 . ILE A 483 ? 0.41810 0.41692 0.38959 -0.01510 -0.00765 -0.02804 483 ILE A CG1 
3881 C CG2 . ILE A 483 ? 0.42326 0.41777 0.38434 -0.01677 -0.00747 -0.03030 483 ILE A CG2 
3882 C CD1 . ILE A 483 ? 0.37243 0.36981 0.34536 -0.01525 -0.00585 -0.02961 483 ILE A CD1 
3883 N N   . ALA A 484 ? 0.42795 0.42470 0.38590 -0.01899 -0.01546 -0.02808 484 ALA A N   
3884 C CA  . ALA A 484 ? 0.48911 0.48390 0.44061 -0.02038 -0.01707 -0.02860 484 ALA A CA  
3885 C C   . ALA A 484 ? 0.48840 0.48442 0.43855 -0.02009 -0.01870 -0.02645 484 ALA A C   
3886 O O   . ALA A 484 ? 0.44259 0.43682 0.38681 -0.02070 -0.01878 -0.02651 484 ALA A O   
3887 C CB  . ALA A 484 ? 0.44900 0.44316 0.40000 -0.02209 -0.01982 -0.02971 484 ALA A CB  
3888 N N   . ARG A 485 ? 0.47648 0.47542 0.43201 -0.01918 -0.01993 -0.02454 485 ARG A N   
3889 C CA  . ARG A 485 ? 0.46804 0.46823 0.42295 -0.01884 -0.02152 -0.02242 485 ARG A CA  
3890 C C   . ARG A 485 ? 0.46234 0.46232 0.41591 -0.01750 -0.01887 -0.02167 485 ARG A C   
3891 O O   . ARG A 485 ? 0.58909 0.58893 0.53969 -0.01752 -0.01968 -0.02037 485 ARG A O   
3892 C CB  . ARG A 485 ? 0.39715 0.40048 0.35866 -0.01828 -0.02349 -0.02075 485 ARG A CB  
3893 C CG  . ARG A 485 ? 0.40801 0.41179 0.37138 -0.01963 -0.02642 -0.02122 485 ARG A CG  
3894 C CD  . ARG A 485 ? 0.33403 0.34090 0.30508 -0.01888 -0.02733 -0.01994 485 ARG A CD  
3895 N NE  . ARG A 485 ? 0.36744 0.37623 0.34042 -0.01830 -0.02901 -0.01770 485 ARG A NE  
3896 C CZ  . ARG A 485 ? 0.37056 0.38206 0.35007 -0.01756 -0.02977 -0.01636 485 ARG A CZ  
3897 N NH1 . ARG A 485 ? 0.31052 0.32321 0.29513 -0.01731 -0.02898 -0.01694 485 ARG A NH1 
3898 N NH2 . ARG A 485 ? 0.41506 0.42806 0.39608 -0.01706 -0.03128 -0.01439 485 ARG A NH2 
3899 N N   . MET A 486 ? 0.46614 0.46605 0.42196 -0.01639 -0.01580 -0.02238 486 MET A N   
3900 C CA  . MET A 486 ? 0.45372 0.45327 0.40838 -0.01520 -0.01326 -0.02178 486 MET A CA  
3901 C C   . MET A 486 ? 0.47887 0.47550 0.42675 -0.01598 -0.01199 -0.02291 486 MET A C   
3902 O O   . MET A 486 ? 0.51289 0.50911 0.45818 -0.01552 -0.01112 -0.02194 486 MET A O   
3903 C CB  . MET A 486 ? 0.46883 0.46900 0.42784 -0.01391 -0.01058 -0.02219 486 MET A CB  
3904 C CG  . MET A 486 ? 0.52640 0.52934 0.49178 -0.01301 -0.01132 -0.02096 486 MET A CG  
3905 S SD  . MET A 486 ? 0.44770 0.45284 0.41488 -0.01203 -0.01253 -0.01844 486 MET A SD  
3906 C CE  . MET A 486 ? 0.47676 0.48066 0.44130 -0.01098 -0.00961 -0.01822 486 MET A CE  
3907 N N   . ALA A 487 ? 0.48217 0.47666 0.42711 -0.01719 -0.01175 -0.02500 487 ALA A N   
3908 C CA  . ALA A 487 ? 0.46971 0.46117 0.40793 -0.01806 -0.01035 -0.02632 487 ALA A CA  
3909 C C   . ALA A 487 ? 0.53606 0.52684 0.46901 -0.01917 -0.01276 -0.02532 487 ALA A C   
3910 O O   . ALA A 487 ? 0.57799 0.56701 0.50585 -0.01937 -0.01142 -0.02530 487 ALA A O   
3911 C CB  . ALA A 487 ? 0.55906 0.54831 0.49556 -0.01918 -0.00967 -0.02890 487 ALA A CB  
3912 N N   . ALA A 488 ? 0.55023 0.54236 0.48443 -0.01994 -0.01634 -0.02441 488 ALA A N   
3913 C CA  . ALA A 488 ? 0.52838 0.52003 0.45804 -0.02099 -0.01904 -0.02314 488 ALA A CA  
3914 C C   . ALA A 488 ? 0.46977 0.46297 0.40056 -0.01977 -0.01881 -0.02073 488 ALA A C   
3915 O O   . ALA A 488 ? 0.54668 0.53868 0.47231 -0.02039 -0.01946 -0.01984 488 ALA A O   
3916 C CB  . ALA A 488 ? 0.48991 0.48280 0.42156 -0.02206 -0.02308 -0.02265 488 ALA A CB  
3917 N N   . ALA A 489 ? 0.49407 0.48982 0.43140 -0.01810 -0.01788 -0.01966 489 ALA A N   
3918 C CA  . ALA A 489 ? 0.50809 0.50527 0.44688 -0.01688 -0.01752 -0.01750 489 ALA A CA  
3919 C C   . ALA A 489 ? 0.52265 0.51804 0.45774 -0.01636 -0.01426 -0.01785 489 ALA A C   
3920 O O   . ALA A 489 ? 0.52848 0.52346 0.46050 -0.01636 -0.01445 -0.01645 489 ALA A O   
3921 C CB  . ALA A 489 ? 0.48219 0.48230 0.42869 -0.01531 -0.01721 -0.01653 489 ALA A CB  
3922 N N   . TYR A 490 ? 0.51832 0.51260 0.45386 -0.01594 -0.01125 -0.01965 490 TYR A N   
3923 C CA  . TYR A 490 ? 0.50783 0.50046 0.44060 -0.01540 -0.00796 -0.02006 490 TYR A CA  
3924 C C   . TYR A 490 ? 0.51949 0.50919 0.44437 -0.01686 -0.00773 -0.02081 490 TYR A C   
3925 O O   . TYR A 490 ? 0.58515 0.57360 0.50721 -0.01652 -0.00537 -0.02061 490 TYR A O   
3926 C CB  . TYR A 490 ? 0.53025 0.52237 0.46584 -0.01468 -0.00501 -0.02180 490 TYR A CB  
3927 C CG  . TYR A 490 ? 0.47268 0.46716 0.41486 -0.01294 -0.00401 -0.02073 490 TYR A CG  
3928 C CD1 . TYR A 490 ? 0.41354 0.41033 0.36096 -0.01254 -0.00578 -0.02014 490 TYR A CD1 
3929 C CD2 . TYR A 490 ? 0.44531 0.43961 0.38841 -0.01177 -0.00129 -0.02031 490 TYR A CD2 
3930 C CE1 . TYR A 490 ? 0.41483 0.41353 0.36772 -0.01106 -0.00483 -0.01923 490 TYR A CE1 
3931 C CE2 . TYR A 490 ? 0.41761 0.41387 0.36637 -0.01029 -0.00056 -0.01937 490 TYR A CE2 
3932 C CZ  . TYR A 490 ? 0.38734 0.38572 0.34072 -0.00997 -0.00231 -0.01886 490 TYR A CZ  
3933 O OH  . TYR A 490 ? 0.39104 0.39114 0.34952 -0.00861 -0.00152 -0.01799 490 TYR A OH  
3934 N N   . ARG A 491 ? 0.57770 0.56622 0.49890 -0.01852 -0.01012 -0.02166 491 ARG A N   
3935 C CA  . ARG A 491 ? 0.46748 0.45303 0.38052 -0.02008 -0.01016 -0.02232 491 ARG A CA  
3936 C C   . ARG A 491 ? 0.56169 0.54762 0.47200 -0.02017 -0.01160 -0.01989 491 ARG A C   
3937 O O   . ARG A 491 ? 0.67520 0.65876 0.57911 -0.02094 -0.01041 -0.02001 491 ARG A O   
3938 C CB  . ARG A 491 ? 0.43407 0.41829 0.34397 -0.02193 -0.01275 -0.02376 491 ARG A CB  
3939 N N   . ARG A 492 ? 0.60025 0.58901 0.51533 -0.01941 -0.01406 -0.01768 492 ARG A N   
3940 C CA  . ARG A 492 ? 0.61584 0.60517 0.52927 -0.01934 -0.01552 -0.01518 492 ARG A CA  
3941 C C   . ARG A 492 ? 0.60676 0.59612 0.52083 -0.01796 -0.01223 -0.01439 492 ARG A C   
3942 O O   . ARG A 492 ? 0.77292 0.76153 0.68334 -0.01818 -0.01226 -0.01289 492 ARG A O   
3943 C CB  . ARG A 492 ? 0.62733 0.61975 0.54654 -0.01881 -0.01888 -0.01314 492 ARG A CB  
3944 C CG  . ARG A 492 ? 0.72474 0.71726 0.64335 -0.02030 -0.02269 -0.01338 492 ARG A CG  
3945 C CD  . ARG A 492 ? 0.80065 0.79619 0.72505 -0.01973 -0.02588 -0.01108 492 ARG A CD  
3946 N NE  . ARG A 492 ? 0.75929 0.75499 0.68340 -0.02120 -0.02976 -0.01106 492 ARG A NE  
3947 C CZ  . ARG A 492 ? 0.78443 0.78154 0.71344 -0.02121 -0.03084 -0.01196 492 ARG A CZ  
3948 N NH1 . ARG A 492 ? 0.74964 0.74808 0.68399 -0.01986 -0.02837 -0.01294 492 ARG A NH1 
3949 N NH2 . ARG A 492 ? 0.79389 0.79105 0.72248 -0.02265 -0.03455 -0.01180 492 ARG A NH2 
# 
