data_9JJF
# 
_entry.id   9JJF 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_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   9JJF         pdb_00009jjf 10.2210/pdb9jjf/pdb 
WWPDB D_1300051477 ?            ?                   
EMDB  EMD-61525    ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2024-11-06 
2 'Structure model' 1 1 2024-11-27 
3 'Structure model' 1 2 2024-12-18 
# 
_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             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Data collection'     
2 3 'Structure model' 'Data collection'     
3 3 'Structure model' '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' em_admin        
2 3 'Structure model' citation        
3 3 'Structure model' citation_author 
4 3 'Structure model' em_admin        
# 
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' '_em_admin.last_update'             
2 3 'Structure model' '_citation.journal_volume'          
3 3 'Structure model' '_citation.page_first'              
4 3 'Structure model' '_citation.page_last'               
5 3 'Structure model' '_citation.pdbx_database_id_DOI'    
6 3 'Structure model' '_citation.pdbx_database_id_PubMed' 
7 3 'Structure model' '_citation.title'                   
8 3 'Structure model' '_citation_author.identifier_ORCID' 
9 3 'Structure model' '_em_admin.last_update'             
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9JJF 
_pdbx_database_status.recvd_initial_deposition_date   2024-09-13 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_database_related.db_name        EMDB 
_pdbx_database_related.details        'Nematostella vectensis TRPM2 monomer in complex with ADPRP/Ca2+' 
_pdbx_database_related.db_id          EMD-61525 
_pdbx_database_related.content_type   'associated EM volume' 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              zzhang01@pku.edu.cn 
_pdbx_contact_author.name_first         Zhe 
_pdbx_contact_author.name_last          Zhang 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-4932-4343 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Jiang, Y.'    1 0000-0003-3985-2027 
'Zhang, Z.'    2 0000-0002-4932-4343 
'Toth, B.'     3 ?                   
'Szollosi, A.' 4 ?                   
'Csanady, L.'  5 ?                   
# 
_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            Proc.Natl.Acad.Sci.USA 
_citation.journal_id_ASTM           PNASA6 
_citation.journal_id_CSD            0040 
_citation.journal_id_ISSN           1091-6490 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            121 
_citation.language                  ? 
_citation.page_first                e2415548121 
_citation.page_last                 e2415548121 
_citation.title                     'A conserved mechanism couples cytosolic domain movements to pore gating in the TRPM2 channel.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1073/pnas.2415548121 
_citation.pdbx_database_id_PubMed   39514307 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Toth, B.'     1 ?                   
primary 'Jiang, Y.'    2 0000-0003-3985-2027 
primary 'Szollosi, A.' 3 0000-0002-5570-4609 
primary 'Zhang, Z.'    4 0000-0002-4932-4343 
primary 'Csanady, L.'  5 0000-0002-6547-5889 
# 
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 'Transient receptor potential cation channel subfamily M member-like 2' 176663.438 1 ? ? ? ? 
2 branched    man '2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose' 424.401    1 ? ? ? ? 
3 non-polymer syn 'CALCIUM ION' 40.078     1 ? ? ? ? 
4 non-polymer syn 
;[(2R,3R,4R,5R)-5-(6-AMINO-9H-PURIN-9-YL)-3-HYDROXY-4-(PHOSPHONOOXY)TETRAHYDROFURAN-2-YL]METHYL [(2R,3S,4R,5R)-3,4,5-TRIHYDROXYTETRAHYDROFURAN-2-YL]METHYL DIHYDROGEN DIPHOSPHATE
;
639.296    1 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        nvTRPM2 
# 
_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       
;MGKDSFTPLYDGGDSSHVHLNKFGSNQLSQSKKSWIARNFSRRECIRFVPKSHDVSRCKCGRPRERHSQQALESGQGSEE
WNVASCTTKHPTNAYGEIDFEGYGGQKRAPYLRMSHDTDANLVITLMLKRWNLEIPNLVISVTGGAKSFVLKPRLREMFR
RGLIKAAKTTGAWIITGGTNTGVMKHVGEAVKEQQLMFGSDTQVNVIGIATWGIVDKQSDLISEKNGKYPALYSMEPTPG
HQGAMLDPNHSHFFLVDDGTEGKYGVEIGMRSRIEEAIMKVKTDSRSEAGSIGVPVVLLVLEGGPNTVATMYELIKKKVP
AVVIDGSGRAASVVGFAYNHTIKRNVDGQTINVIDPQYEDEVRAKVVEVFGAKGADKTYSMIKDVLEDEKMISVYSLDGE
ISQDIDLAILKALLKANRSSPVAQLNLALAWNRIDLAKSDIFTEEQQWTTETLSAAMLTALLDDKAEFAELFLQNGLSMR
EFLSLDILCKLYAEVPGNTTIKPLLQKEMGKRQVKTIDMDVVGEVIEELMGDMFESYYRKDGHYFGELASYAEGLVLKNR
KSSKDLLANINRIDPLPTPYLDVFLWAVLCNRRELARVLWEAGREPMAAALMASRLLKRMASRAQEDNTITDISSDLYDH
ARLFEERAVGVLDECFNENETLSQTLLVRELDHYSRMTALELAVSAESQDFIAHTSCQVLLTRLWMGTMAMNTRWWKVLV
CLYLPVLIFPIIYFVPDEQHERQAAEREHQKSLNQKSSKVKSHKEKNDAPVVPVYRSKEEKAVSNDEEARVGTENEEEDF
QLEDYIPEIREDDSMEVIMRNKKLGFCDRIMHFYSAPFSKFVGNVVGYLAFIFLYAYVVLFNFPRFDPAKTLGGIHPTEI
VLYFWVFTILIEEIRQLAAKPPKYIKDKVSVYFSDTWNFVDIFSLTVFIIAIILRFFTNSRIFTASRIILSLDIIFFIVR
SLQIFSVNRLLGPKLVMIQKMMQDLAQFIIILAVFTIAYGIALHAVMFPSPGIYARNNTWVTITSVVQYPYWQMYGELFL
DEIQGEKPKEFGEVDPDGRWLSPLLLAIYMVFTNILLLNLLIAIFNYTFERVQEDSDKVWKFQRYDLVQEYHSRPVFAPP
LVLLGHILIFIRWVWRMCRCGHPPRGSTMKIGLSPAEMEQMDNWEFQAAEMYIHQQQQKNSGTLEERVRALGDRVDCINS
QLNRVLDSMSGTRAHALTDGNGLEGGHDSEGRLARMEVELSSNSESLQKILALLQQQPPVKGQAAVPIQLTLLHYKARSS
PYPGSTAKRFAVQDNMVDWQVPFPDYKPVNYTAPVVLANPVWADKDLMAMSPRPELPYNQMDHTCNVNRVSYNGTYVVKD
GLPLNPMGRTGMQGRGLLGRFGPNHAADPVVTRWKRTSAGVMLQGGKKVLEFVAIQRKDNNQWAIPGGMVEPGQLVTQAL
KAEFGEEAMAKLNVSQEEKERIAKQIERLFQQGQEIYKGYVDDPRNTDNAWMETVAVNFHDDKGDLFGDITLQAGDDAAA
VRWQRVSGNIPLYASHVSILEKVAKMRDAAFSNSLEVLFQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MGKDSFTPLYDGGDSSHVHLNKFGSNQLSQSKKSWIARNFSRRECIRFVPKSHDVSRCKCGRPRERHSQQALESGQGSEE
WNVASCTTKHPTNAYGEIDFEGYGGQKRAPYLRMSHDTDANLVITLMLKRWNLEIPNLVISVTGGAKSFVLKPRLREMFR
RGLIKAAKTTGAWIITGGTNTGVMKHVGEAVKEQQLMFGSDTQVNVIGIATWGIVDKQSDLISEKNGKYPALYSMEPTPG
HQGAMLDPNHSHFFLVDDGTEGKYGVEIGMRSRIEEAIMKVKTDSRSEAGSIGVPVVLLVLEGGPNTVATMYELIKKKVP
AVVIDGSGRAASVVGFAYNHTIKRNVDGQTINVIDPQYEDEVRAKVVEVFGAKGADKTYSMIKDVLEDEKMISVYSLDGE
ISQDIDLAILKALLKANRSSPVAQLNLALAWNRIDLAKSDIFTEEQQWTTETLSAAMLTALLDDKAEFAELFLQNGLSMR
EFLSLDILCKLYAEVPGNTTIKPLLQKEMGKRQVKTIDMDVVGEVIEELMGDMFESYYRKDGHYFGELASYAEGLVLKNR
KSSKDLLANINRIDPLPTPYLDVFLWAVLCNRRELARVLWEAGREPMAAALMASRLLKRMASRAQEDNTITDISSDLYDH
ARLFEERAVGVLDECFNENETLSQTLLVRELDHYSRMTALELAVSAESQDFIAHTSCQVLLTRLWMGTMAMNTRWWKVLV
CLYLPVLIFPIIYFVPDEQHERQAAEREHQKSLNQKSSKVKSHKEKNDAPVVPVYRSKEEKAVSNDEEARVGTENEEEDF
QLEDYIPEIREDDSMEVIMRNKKLGFCDRIMHFYSAPFSKFVGNVVGYLAFIFLYAYVVLFNFPRFDPAKTLGGIHPTEI
VLYFWVFTILIEEIRQLAAKPPKYIKDKVSVYFSDTWNFVDIFSLTVFIIAIILRFFTNSRIFTASRIILSLDIIFFIVR
SLQIFSVNRLLGPKLVMIQKMMQDLAQFIIILAVFTIAYGIALHAVMFPSPGIYARNNTWVTITSVVQYPYWQMYGELFL
DEIQGEKPKEFGEVDPDGRWLSPLLLAIYMVFTNILLLNLLIAIFNYTFERVQEDSDKVWKFQRYDLVQEYHSRPVFAPP
LVLLGHILIFIRWVWRMCRCGHPPRGSTMKIGLSPAEMEQMDNWEFQAAEMYIHQQQQKNSGTLEERVRALGDRVDCINS
QLNRVLDSMSGTRAHALTDGNGLEGGHDSEGRLARMEVELSSNSESLQKILALLQQQPPVKGQAAVPIQLTLLHYKARSS
PYPGSTAKRFAVQDNMVDWQVPFPDYKPVNYTAPVVLANPVWADKDLMAMSPRPELPYNQMDHTCNVNRVSYNGTYVVKD
GLPLNPMGRTGMQGRGLLGRFGPNHAADPVVTRWKRTSAGVMLQGGKKVLEFVAIQRKDNNQWAIPGGMVEPGQLVTQAL
KAEFGEEAMAKLNVSQEEKERIAKQIERLFQQGQEIYKGYVDDPRNTDNAWMETVAVNFHDDKGDLFGDITLQAGDDAAA
VRWQRVSGNIPLYASHVSILEKVAKMRDAAFSNSLEVLFQ
;
_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 
3 'CALCIUM ION' CA  
4 
;[(2R,3R,4R,5R)-5-(6-AMINO-9H-PURIN-9-YL)-3-HYDROXY-4-(PHOSPHONOOXY)TETRAHYDROFURAN-2-YL]METHYL [(2R,3S,4R,5R)-3,4,5-TRIHYDROXYTETRAHYDROFURAN-2-YL]METHYL DIHYDROGEN DIPHOSPHATE
;
A2R 
# 
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    GLY n 
1 3    LYS n 
1 4    ASP n 
1 5    SER n 
1 6    PHE n 
1 7    THR n 
1 8    PRO n 
1 9    LEU n 
1 10   TYR n 
1 11   ASP n 
1 12   GLY n 
1 13   GLY n 
1 14   ASP n 
1 15   SER n 
1 16   SER n 
1 17   HIS n 
1 18   VAL n 
1 19   HIS n 
1 20   LEU n 
1 21   ASN n 
1 22   LYS n 
1 23   PHE n 
1 24   GLY n 
1 25   SER n 
1 26   ASN n 
1 27   GLN n 
1 28   LEU n 
1 29   SER n 
1 30   GLN n 
1 31   SER n 
1 32   LYS n 
1 33   LYS n 
1 34   SER n 
1 35   TRP n 
1 36   ILE n 
1 37   ALA n 
1 38   ARG n 
1 39   ASN n 
1 40   PHE n 
1 41   SER n 
1 42   ARG n 
1 43   ARG n 
1 44   GLU n 
1 45   CYS n 
1 46   ILE n 
1 47   ARG n 
1 48   PHE n 
1 49   VAL n 
1 50   PRO n 
1 51   LYS n 
1 52   SER n 
1 53   HIS n 
1 54   ASP n 
1 55   VAL n 
1 56   SER n 
1 57   ARG n 
1 58   CYS n 
1 59   LYS n 
1 60   CYS n 
1 61   GLY n 
1 62   ARG n 
1 63   PRO n 
1 64   ARG n 
1 65   GLU n 
1 66   ARG n 
1 67   HIS n 
1 68   SER n 
1 69   GLN n 
1 70   GLN n 
1 71   ALA n 
1 72   LEU n 
1 73   GLU n 
1 74   SER n 
1 75   GLY n 
1 76   GLN n 
1 77   GLY n 
1 78   SER n 
1 79   GLU n 
1 80   GLU n 
1 81   TRP n 
1 82   ASN n 
1 83   VAL n 
1 84   ALA n 
1 85   SER n 
1 86   CYS n 
1 87   THR n 
1 88   THR n 
1 89   LYS n 
1 90   HIS n 
1 91   PRO n 
1 92   THR n 
1 93   ASN n 
1 94   ALA n 
1 95   TYR n 
1 96   GLY n 
1 97   GLU n 
1 98   ILE n 
1 99   ASP n 
1 100  PHE n 
1 101  GLU n 
1 102  GLY n 
1 103  TYR n 
1 104  GLY n 
1 105  GLY n 
1 106  GLN n 
1 107  LYS n 
1 108  ARG n 
1 109  ALA n 
1 110  PRO n 
1 111  TYR n 
1 112  LEU n 
1 113  ARG n 
1 114  MET n 
1 115  SER n 
1 116  HIS n 
1 117  ASP n 
1 118  THR n 
1 119  ASP n 
1 120  ALA n 
1 121  ASN n 
1 122  LEU n 
1 123  VAL n 
1 124  ILE n 
1 125  THR n 
1 126  LEU n 
1 127  MET n 
1 128  LEU n 
1 129  LYS n 
1 130  ARG n 
1 131  TRP n 
1 132  ASN n 
1 133  LEU n 
1 134  GLU n 
1 135  ILE n 
1 136  PRO n 
1 137  ASN n 
1 138  LEU n 
1 139  VAL n 
1 140  ILE n 
1 141  SER n 
1 142  VAL n 
1 143  THR n 
1 144  GLY n 
1 145  GLY n 
1 146  ALA n 
1 147  LYS n 
1 148  SER n 
1 149  PHE n 
1 150  VAL n 
1 151  LEU n 
1 152  LYS n 
1 153  PRO n 
1 154  ARG n 
1 155  LEU n 
1 156  ARG n 
1 157  GLU n 
1 158  MET n 
1 159  PHE n 
1 160  ARG n 
1 161  ARG n 
1 162  GLY n 
1 163  LEU n 
1 164  ILE n 
1 165  LYS n 
1 166  ALA n 
1 167  ALA n 
1 168  LYS n 
1 169  THR n 
1 170  THR n 
1 171  GLY n 
1 172  ALA n 
1 173  TRP n 
1 174  ILE n 
1 175  ILE n 
1 176  THR n 
1 177  GLY n 
1 178  GLY n 
1 179  THR n 
1 180  ASN n 
1 181  THR n 
1 182  GLY n 
1 183  VAL n 
1 184  MET n 
1 185  LYS n 
1 186  HIS n 
1 187  VAL n 
1 188  GLY n 
1 189  GLU n 
1 190  ALA n 
1 191  VAL n 
1 192  LYS n 
1 193  GLU n 
1 194  GLN n 
1 195  GLN n 
1 196  LEU n 
1 197  MET n 
1 198  PHE n 
1 199  GLY n 
1 200  SER n 
1 201  ASP n 
1 202  THR n 
1 203  GLN n 
1 204  VAL n 
1 205  ASN n 
1 206  VAL n 
1 207  ILE n 
1 208  GLY n 
1 209  ILE n 
1 210  ALA n 
1 211  THR n 
1 212  TRP n 
1 213  GLY n 
1 214  ILE n 
1 215  VAL n 
1 216  ASP n 
1 217  LYS n 
1 218  GLN n 
1 219  SER n 
1 220  ASP n 
1 221  LEU n 
1 222  ILE n 
1 223  SER n 
1 224  GLU n 
1 225  LYS n 
1 226  ASN n 
1 227  GLY n 
1 228  LYS n 
1 229  TYR n 
1 230  PRO n 
1 231  ALA n 
1 232  LEU n 
1 233  TYR n 
1 234  SER n 
1 235  MET n 
1 236  GLU n 
1 237  PRO n 
1 238  THR n 
1 239  PRO n 
1 240  GLY n 
1 241  HIS n 
1 242  GLN n 
1 243  GLY n 
1 244  ALA n 
1 245  MET n 
1 246  LEU n 
1 247  ASP n 
1 248  PRO n 
1 249  ASN n 
1 250  HIS n 
1 251  SER n 
1 252  HIS n 
1 253  PHE n 
1 254  PHE n 
1 255  LEU n 
1 256  VAL n 
1 257  ASP n 
1 258  ASP n 
1 259  GLY n 
1 260  THR n 
1 261  GLU n 
1 262  GLY n 
1 263  LYS n 
1 264  TYR n 
1 265  GLY n 
1 266  VAL n 
1 267  GLU n 
1 268  ILE n 
1 269  GLY n 
1 270  MET n 
1 271  ARG n 
1 272  SER n 
1 273  ARG n 
1 274  ILE n 
1 275  GLU n 
1 276  GLU n 
1 277  ALA n 
1 278  ILE n 
1 279  MET n 
1 280  LYS n 
1 281  VAL n 
1 282  LYS n 
1 283  THR n 
1 284  ASP n 
1 285  SER n 
1 286  ARG n 
1 287  SER n 
1 288  GLU n 
1 289  ALA n 
1 290  GLY n 
1 291  SER n 
1 292  ILE n 
1 293  GLY n 
1 294  VAL n 
1 295  PRO n 
1 296  VAL n 
1 297  VAL n 
1 298  LEU n 
1 299  LEU n 
1 300  VAL n 
1 301  LEU n 
1 302  GLU n 
1 303  GLY n 
1 304  GLY n 
1 305  PRO n 
1 306  ASN n 
1 307  THR n 
1 308  VAL n 
1 309  ALA n 
1 310  THR n 
1 311  MET n 
1 312  TYR n 
1 313  GLU n 
1 314  LEU n 
1 315  ILE n 
1 316  LYS n 
1 317  LYS n 
1 318  LYS n 
1 319  VAL n 
1 320  PRO n 
1 321  ALA n 
1 322  VAL n 
1 323  VAL n 
1 324  ILE n 
1 325  ASP n 
1 326  GLY n 
1 327  SER n 
1 328  GLY n 
1 329  ARG n 
1 330  ALA n 
1 331  ALA n 
1 332  SER n 
1 333  VAL n 
1 334  VAL n 
1 335  GLY n 
1 336  PHE n 
1 337  ALA n 
1 338  TYR n 
1 339  ASN n 
1 340  HIS n 
1 341  THR n 
1 342  ILE n 
1 343  LYS n 
1 344  ARG n 
1 345  ASN n 
1 346  VAL n 
1 347  ASP n 
1 348  GLY n 
1 349  GLN n 
1 350  THR n 
1 351  ILE n 
1 352  ASN n 
1 353  VAL n 
1 354  ILE n 
1 355  ASP n 
1 356  PRO n 
1 357  GLN n 
1 358  TYR n 
1 359  GLU n 
1 360  ASP n 
1 361  GLU n 
1 362  VAL n 
1 363  ARG n 
1 364  ALA n 
1 365  LYS n 
1 366  VAL n 
1 367  VAL n 
1 368  GLU n 
1 369  VAL n 
1 370  PHE n 
1 371  GLY n 
1 372  ALA n 
1 373  LYS n 
1 374  GLY n 
1 375  ALA n 
1 376  ASP n 
1 377  LYS n 
1 378  THR n 
1 379  TYR n 
1 380  SER n 
1 381  MET n 
1 382  ILE n 
1 383  LYS n 
1 384  ASP n 
1 385  VAL n 
1 386  LEU n 
1 387  GLU n 
1 388  ASP n 
1 389  GLU n 
1 390  LYS n 
1 391  MET n 
1 392  ILE n 
1 393  SER n 
1 394  VAL n 
1 395  TYR n 
1 396  SER n 
1 397  LEU n 
1 398  ASP n 
1 399  GLY n 
1 400  GLU n 
1 401  ILE n 
1 402  SER n 
1 403  GLN n 
1 404  ASP n 
1 405  ILE n 
1 406  ASP n 
1 407  LEU n 
1 408  ALA n 
1 409  ILE n 
1 410  LEU n 
1 411  LYS n 
1 412  ALA n 
1 413  LEU n 
1 414  LEU n 
1 415  LYS n 
1 416  ALA n 
1 417  ASN n 
1 418  ARG n 
1 419  SER n 
1 420  SER n 
1 421  PRO n 
1 422  VAL n 
1 423  ALA n 
1 424  GLN n 
1 425  LEU n 
1 426  ASN n 
1 427  LEU n 
1 428  ALA n 
1 429  LEU n 
1 430  ALA n 
1 431  TRP n 
1 432  ASN n 
1 433  ARG n 
1 434  ILE n 
1 435  ASP n 
1 436  LEU n 
1 437  ALA n 
1 438  LYS n 
1 439  SER n 
1 440  ASP n 
1 441  ILE n 
1 442  PHE n 
1 443  THR n 
1 444  GLU n 
1 445  GLU n 
1 446  GLN n 
1 447  GLN n 
1 448  TRP n 
1 449  THR n 
1 450  THR n 
1 451  GLU n 
1 452  THR n 
1 453  LEU n 
1 454  SER n 
1 455  ALA n 
1 456  ALA n 
1 457  MET n 
1 458  LEU n 
1 459  THR n 
1 460  ALA n 
1 461  LEU n 
1 462  LEU n 
1 463  ASP n 
1 464  ASP n 
1 465  LYS n 
1 466  ALA n 
1 467  GLU n 
1 468  PHE n 
1 469  ALA n 
1 470  GLU n 
1 471  LEU n 
1 472  PHE n 
1 473  LEU n 
1 474  GLN n 
1 475  ASN n 
1 476  GLY n 
1 477  LEU n 
1 478  SER n 
1 479  MET n 
1 480  ARG n 
1 481  GLU n 
1 482  PHE n 
1 483  LEU n 
1 484  SER n 
1 485  LEU n 
1 486  ASP n 
1 487  ILE n 
1 488  LEU n 
1 489  CYS n 
1 490  LYS n 
1 491  LEU n 
1 492  TYR n 
1 493  ALA n 
1 494  GLU n 
1 495  VAL n 
1 496  PRO n 
1 497  GLY n 
1 498  ASN n 
1 499  THR n 
1 500  THR n 
1 501  ILE n 
1 502  LYS n 
1 503  PRO n 
1 504  LEU n 
1 505  LEU n 
1 506  GLN n 
1 507  LYS n 
1 508  GLU n 
1 509  MET n 
1 510  GLY n 
1 511  LYS n 
1 512  ARG n 
1 513  GLN n 
1 514  VAL n 
1 515  LYS n 
1 516  THR n 
1 517  ILE n 
1 518  ASP n 
1 519  MET n 
1 520  ASP n 
1 521  VAL n 
1 522  VAL n 
1 523  GLY n 
1 524  GLU n 
1 525  VAL n 
1 526  ILE n 
1 527  GLU n 
1 528  GLU n 
1 529  LEU n 
1 530  MET n 
1 531  GLY n 
1 532  ASP n 
1 533  MET n 
1 534  PHE n 
1 535  GLU n 
1 536  SER n 
1 537  TYR n 
1 538  TYR n 
1 539  ARG n 
1 540  LYS n 
1 541  ASP n 
1 542  GLY n 
1 543  HIS n 
1 544  TYR n 
1 545  PHE n 
1 546  GLY n 
1 547  GLU n 
1 548  LEU n 
1 549  ALA n 
1 550  SER n 
1 551  TYR n 
1 552  ALA n 
1 553  GLU n 
1 554  GLY n 
1 555  LEU n 
1 556  VAL n 
1 557  LEU n 
1 558  LYS n 
1 559  ASN n 
1 560  ARG n 
1 561  LYS n 
1 562  SER n 
1 563  SER n 
1 564  LYS n 
1 565  ASP n 
1 566  LEU n 
1 567  LEU n 
1 568  ALA n 
1 569  ASN n 
1 570  ILE n 
1 571  ASN n 
1 572  ARG n 
1 573  ILE n 
1 574  ASP n 
1 575  PRO n 
1 576  LEU n 
1 577  PRO n 
1 578  THR n 
1 579  PRO n 
1 580  TYR n 
1 581  LEU n 
1 582  ASP n 
1 583  VAL n 
1 584  PHE n 
1 585  LEU n 
1 586  TRP n 
1 587  ALA n 
1 588  VAL n 
1 589  LEU n 
1 590  CYS n 
1 591  ASN n 
1 592  ARG n 
1 593  ARG n 
1 594  GLU n 
1 595  LEU n 
1 596  ALA n 
1 597  ARG n 
1 598  VAL n 
1 599  LEU n 
1 600  TRP n 
1 601  GLU n 
1 602  ALA n 
1 603  GLY n 
1 604  ARG n 
1 605  GLU n 
1 606  PRO n 
1 607  MET n 
1 608  ALA n 
1 609  ALA n 
1 610  ALA n 
1 611  LEU n 
1 612  MET n 
1 613  ALA n 
1 614  SER n 
1 615  ARG n 
1 616  LEU n 
1 617  LEU n 
1 618  LYS n 
1 619  ARG n 
1 620  MET n 
1 621  ALA n 
1 622  SER n 
1 623  ARG n 
1 624  ALA n 
1 625  GLN n 
1 626  GLU n 
1 627  ASP n 
1 628  ASN n 
1 629  THR n 
1 630  ILE n 
1 631  THR n 
1 632  ASP n 
1 633  ILE n 
1 634  SER n 
1 635  SER n 
1 636  ASP n 
1 637  LEU n 
1 638  TYR n 
1 639  ASP n 
1 640  HIS n 
1 641  ALA n 
1 642  ARG n 
1 643  LEU n 
1 644  PHE n 
1 645  GLU n 
1 646  GLU n 
1 647  ARG n 
1 648  ALA n 
1 649  VAL n 
1 650  GLY n 
1 651  VAL n 
1 652  LEU n 
1 653  ASP n 
1 654  GLU n 
1 655  CYS n 
1 656  PHE n 
1 657  ASN n 
1 658  GLU n 
1 659  ASN n 
1 660  GLU n 
1 661  THR n 
1 662  LEU n 
1 663  SER n 
1 664  GLN n 
1 665  THR n 
1 666  LEU n 
1 667  LEU n 
1 668  VAL n 
1 669  ARG n 
1 670  GLU n 
1 671  LEU n 
1 672  ASP n 
1 673  HIS n 
1 674  TYR n 
1 675  SER n 
1 676  ARG n 
1 677  MET n 
1 678  THR n 
1 679  ALA n 
1 680  LEU n 
1 681  GLU n 
1 682  LEU n 
1 683  ALA n 
1 684  VAL n 
1 685  SER n 
1 686  ALA n 
1 687  GLU n 
1 688  SER n 
1 689  GLN n 
1 690  ASP n 
1 691  PHE n 
1 692  ILE n 
1 693  ALA n 
1 694  HIS n 
1 695  THR n 
1 696  SER n 
1 697  CYS n 
1 698  GLN n 
1 699  VAL n 
1 700  LEU n 
1 701  LEU n 
1 702  THR n 
1 703  ARG n 
1 704  LEU n 
1 705  TRP n 
1 706  MET n 
1 707  GLY n 
1 708  THR n 
1 709  MET n 
1 710  ALA n 
1 711  MET n 
1 712  ASN n 
1 713  THR n 
1 714  ARG n 
1 715  TRP n 
1 716  TRP n 
1 717  LYS n 
1 718  VAL n 
1 719  LEU n 
1 720  VAL n 
1 721  CYS n 
1 722  LEU n 
1 723  TYR n 
1 724  LEU n 
1 725  PRO n 
1 726  VAL n 
1 727  LEU n 
1 728  ILE n 
1 729  PHE n 
1 730  PRO n 
1 731  ILE n 
1 732  ILE n 
1 733  TYR n 
1 734  PHE n 
1 735  VAL n 
1 736  PRO n 
1 737  ASP n 
1 738  GLU n 
1 739  GLN n 
1 740  HIS n 
1 741  GLU n 
1 742  ARG n 
1 743  GLN n 
1 744  ALA n 
1 745  ALA n 
1 746  GLU n 
1 747  ARG n 
1 748  GLU n 
1 749  HIS n 
1 750  GLN n 
1 751  LYS n 
1 752  SER n 
1 753  LEU n 
1 754  ASN n 
1 755  GLN n 
1 756  LYS n 
1 757  SER n 
1 758  SER n 
1 759  LYS n 
1 760  VAL n 
1 761  LYS n 
1 762  SER n 
1 763  HIS n 
1 764  LYS n 
1 765  GLU n 
1 766  LYS n 
1 767  ASN n 
1 768  ASP n 
1 769  ALA n 
1 770  PRO n 
1 771  VAL n 
1 772  VAL n 
1 773  PRO n 
1 774  VAL n 
1 775  TYR n 
1 776  ARG n 
1 777  SER n 
1 778  LYS n 
1 779  GLU n 
1 780  GLU n 
1 781  LYS n 
1 782  ALA n 
1 783  VAL n 
1 784  SER n 
1 785  ASN n 
1 786  ASP n 
1 787  GLU n 
1 788  GLU n 
1 789  ALA n 
1 790  ARG n 
1 791  VAL n 
1 792  GLY n 
1 793  THR n 
1 794  GLU n 
1 795  ASN n 
1 796  GLU n 
1 797  GLU n 
1 798  GLU n 
1 799  ASP n 
1 800  PHE n 
1 801  GLN n 
1 802  LEU n 
1 803  GLU n 
1 804  ASP n 
1 805  TYR n 
1 806  ILE n 
1 807  PRO n 
1 808  GLU n 
1 809  ILE n 
1 810  ARG n 
1 811  GLU n 
1 812  ASP n 
1 813  ASP n 
1 814  SER n 
1 815  MET n 
1 816  GLU n 
1 817  VAL n 
1 818  ILE n 
1 819  MET n 
1 820  ARG n 
1 821  ASN n 
1 822  LYS n 
1 823  LYS n 
1 824  LEU n 
1 825  GLY n 
1 826  PHE n 
1 827  CYS n 
1 828  ASP n 
1 829  ARG n 
1 830  ILE n 
1 831  MET n 
1 832  HIS n 
1 833  PHE n 
1 834  TYR n 
1 835  SER n 
1 836  ALA n 
1 837  PRO n 
1 838  PHE n 
1 839  SER n 
1 840  LYS n 
1 841  PHE n 
1 842  VAL n 
1 843  GLY n 
1 844  ASN n 
1 845  VAL n 
1 846  VAL n 
1 847  GLY n 
1 848  TYR n 
1 849  LEU n 
1 850  ALA n 
1 851  PHE n 
1 852  ILE n 
1 853  PHE n 
1 854  LEU n 
1 855  TYR n 
1 856  ALA n 
1 857  TYR n 
1 858  VAL n 
1 859  VAL n 
1 860  LEU n 
1 861  PHE n 
1 862  ASN n 
1 863  PHE n 
1 864  PRO n 
1 865  ARG n 
1 866  PHE n 
1 867  ASP n 
1 868  PRO n 
1 869  ALA n 
1 870  LYS n 
1 871  THR n 
1 872  LEU n 
1 873  GLY n 
1 874  GLY n 
1 875  ILE n 
1 876  HIS n 
1 877  PRO n 
1 878  THR n 
1 879  GLU n 
1 880  ILE n 
1 881  VAL n 
1 882  LEU n 
1 883  TYR n 
1 884  PHE n 
1 885  TRP n 
1 886  VAL n 
1 887  PHE n 
1 888  THR n 
1 889  ILE n 
1 890  LEU n 
1 891  ILE n 
1 892  GLU n 
1 893  GLU n 
1 894  ILE n 
1 895  ARG n 
1 896  GLN n 
1 897  LEU n 
1 898  ALA n 
1 899  ALA n 
1 900  LYS n 
1 901  PRO n 
1 902  PRO n 
1 903  LYS n 
1 904  TYR n 
1 905  ILE n 
1 906  LYS n 
1 907  ASP n 
1 908  LYS n 
1 909  VAL n 
1 910  SER n 
1 911  VAL n 
1 912  TYR n 
1 913  PHE n 
1 914  SER n 
1 915  ASP n 
1 916  THR n 
1 917  TRP n 
1 918  ASN n 
1 919  PHE n 
1 920  VAL n 
1 921  ASP n 
1 922  ILE n 
1 923  PHE n 
1 924  SER n 
1 925  LEU n 
1 926  THR n 
1 927  VAL n 
1 928  PHE n 
1 929  ILE n 
1 930  ILE n 
1 931  ALA n 
1 932  ILE n 
1 933  ILE n 
1 934  LEU n 
1 935  ARG n 
1 936  PHE n 
1 937  PHE n 
1 938  THR n 
1 939  ASN n 
1 940  SER n 
1 941  ARG n 
1 942  ILE n 
1 943  PHE n 
1 944  THR n 
1 945  ALA n 
1 946  SER n 
1 947  ARG n 
1 948  ILE n 
1 949  ILE n 
1 950  LEU n 
1 951  SER n 
1 952  LEU n 
1 953  ASP n 
1 954  ILE n 
1 955  ILE n 
1 956  PHE n 
1 957  PHE n 
1 958  ILE n 
1 959  VAL n 
1 960  ARG n 
1 961  SER n 
1 962  LEU n 
1 963  GLN n 
1 964  ILE n 
1 965  PHE n 
1 966  SER n 
1 967  VAL n 
1 968  ASN n 
1 969  ARG n 
1 970  LEU n 
1 971  LEU n 
1 972  GLY n 
1 973  PRO n 
1 974  LYS n 
1 975  LEU n 
1 976  VAL n 
1 977  MET n 
1 978  ILE n 
1 979  GLN n 
1 980  LYS n 
1 981  MET n 
1 982  MET n 
1 983  GLN n 
1 984  ASP n 
1 985  LEU n 
1 986  ALA n 
1 987  GLN n 
1 988  PHE n 
1 989  ILE n 
1 990  ILE n 
1 991  ILE n 
1 992  LEU n 
1 993  ALA n 
1 994  VAL n 
1 995  PHE n 
1 996  THR n 
1 997  ILE n 
1 998  ALA n 
1 999  TYR n 
1 1000 GLY n 
1 1001 ILE n 
1 1002 ALA n 
1 1003 LEU n 
1 1004 HIS n 
1 1005 ALA n 
1 1006 VAL n 
1 1007 MET n 
1 1008 PHE n 
1 1009 PRO n 
1 1010 SER n 
1 1011 PRO n 
1 1012 GLY n 
1 1013 ILE n 
1 1014 TYR n 
1 1015 ALA n 
1 1016 ARG n 
1 1017 ASN n 
1 1018 ASN n 
1 1019 THR n 
1 1020 TRP n 
1 1021 VAL n 
1 1022 THR n 
1 1023 ILE n 
1 1024 THR n 
1 1025 SER n 
1 1026 VAL n 
1 1027 VAL n 
1 1028 GLN n 
1 1029 TYR n 
1 1030 PRO n 
1 1031 TYR n 
1 1032 TRP n 
1 1033 GLN n 
1 1034 MET n 
1 1035 TYR n 
1 1036 GLY n 
1 1037 GLU n 
1 1038 LEU n 
1 1039 PHE n 
1 1040 LEU n 
1 1041 ASP n 
1 1042 GLU n 
1 1043 ILE n 
1 1044 GLN n 
1 1045 GLY n 
1 1046 GLU n 
1 1047 LYS n 
1 1048 PRO n 
1 1049 LYS n 
1 1050 GLU n 
1 1051 PHE n 
1 1052 GLY n 
1 1053 GLU n 
1 1054 VAL n 
1 1055 ASP n 
1 1056 PRO n 
1 1057 ASP n 
1 1058 GLY n 
1 1059 ARG n 
1 1060 TRP n 
1 1061 LEU n 
1 1062 SER n 
1 1063 PRO n 
1 1064 LEU n 
1 1065 LEU n 
1 1066 LEU n 
1 1067 ALA n 
1 1068 ILE n 
1 1069 TYR n 
1 1070 MET n 
1 1071 VAL n 
1 1072 PHE n 
1 1073 THR n 
1 1074 ASN n 
1 1075 ILE n 
1 1076 LEU n 
1 1077 LEU n 
1 1078 LEU n 
1 1079 ASN n 
1 1080 LEU n 
1 1081 LEU n 
1 1082 ILE n 
1 1083 ALA n 
1 1084 ILE n 
1 1085 PHE n 
1 1086 ASN n 
1 1087 TYR n 
1 1088 THR n 
1 1089 PHE n 
1 1090 GLU n 
1 1091 ARG n 
1 1092 VAL n 
1 1093 GLN n 
1 1094 GLU n 
1 1095 ASP n 
1 1096 SER n 
1 1097 ASP n 
1 1098 LYS n 
1 1099 VAL n 
1 1100 TRP n 
1 1101 LYS n 
1 1102 PHE n 
1 1103 GLN n 
1 1104 ARG n 
1 1105 TYR n 
1 1106 ASP n 
1 1107 LEU n 
1 1108 VAL n 
1 1109 GLN n 
1 1110 GLU n 
1 1111 TYR n 
1 1112 HIS n 
1 1113 SER n 
1 1114 ARG n 
1 1115 PRO n 
1 1116 VAL n 
1 1117 PHE n 
1 1118 ALA n 
1 1119 PRO n 
1 1120 PRO n 
1 1121 LEU n 
1 1122 VAL n 
1 1123 LEU n 
1 1124 LEU n 
1 1125 GLY n 
1 1126 HIS n 
1 1127 ILE n 
1 1128 LEU n 
1 1129 ILE n 
1 1130 PHE n 
1 1131 ILE n 
1 1132 ARG n 
1 1133 TRP n 
1 1134 VAL n 
1 1135 TRP n 
1 1136 ARG n 
1 1137 MET n 
1 1138 CYS n 
1 1139 ARG n 
1 1140 CYS n 
1 1141 GLY n 
1 1142 HIS n 
1 1143 PRO n 
1 1144 PRO n 
1 1145 ARG n 
1 1146 GLY n 
1 1147 SER n 
1 1148 THR n 
1 1149 MET n 
1 1150 LYS n 
1 1151 ILE n 
1 1152 GLY n 
1 1153 LEU n 
1 1154 SER n 
1 1155 PRO n 
1 1156 ALA n 
1 1157 GLU n 
1 1158 MET n 
1 1159 GLU n 
1 1160 GLN n 
1 1161 MET n 
1 1162 ASP n 
1 1163 ASN n 
1 1164 TRP n 
1 1165 GLU n 
1 1166 PHE n 
1 1167 GLN n 
1 1168 ALA n 
1 1169 ALA n 
1 1170 GLU n 
1 1171 MET n 
1 1172 TYR n 
1 1173 ILE n 
1 1174 HIS n 
1 1175 GLN n 
1 1176 GLN n 
1 1177 GLN n 
1 1178 GLN n 
1 1179 LYS n 
1 1180 ASN n 
1 1181 SER n 
1 1182 GLY n 
1 1183 THR n 
1 1184 LEU n 
1 1185 GLU n 
1 1186 GLU n 
1 1187 ARG n 
1 1188 VAL n 
1 1189 ARG n 
1 1190 ALA n 
1 1191 LEU n 
1 1192 GLY n 
1 1193 ASP n 
1 1194 ARG n 
1 1195 VAL n 
1 1196 ASP n 
1 1197 CYS n 
1 1198 ILE n 
1 1199 ASN n 
1 1200 SER n 
1 1201 GLN n 
1 1202 LEU n 
1 1203 ASN n 
1 1204 ARG n 
1 1205 VAL n 
1 1206 LEU n 
1 1207 ASP n 
1 1208 SER n 
1 1209 MET n 
1 1210 SER n 
1 1211 GLY n 
1 1212 THR n 
1 1213 ARG n 
1 1214 ALA n 
1 1215 HIS n 
1 1216 ALA n 
1 1217 LEU n 
1 1218 THR n 
1 1219 ASP n 
1 1220 GLY n 
1 1221 ASN n 
1 1222 GLY n 
1 1223 LEU n 
1 1224 GLU n 
1 1225 GLY n 
1 1226 GLY n 
1 1227 HIS n 
1 1228 ASP n 
1 1229 SER n 
1 1230 GLU n 
1 1231 GLY n 
1 1232 ARG n 
1 1233 LEU n 
1 1234 ALA n 
1 1235 ARG n 
1 1236 MET n 
1 1237 GLU n 
1 1238 VAL n 
1 1239 GLU n 
1 1240 LEU n 
1 1241 SER n 
1 1242 SER n 
1 1243 ASN n 
1 1244 SER n 
1 1245 GLU n 
1 1246 SER n 
1 1247 LEU n 
1 1248 GLN n 
1 1249 LYS n 
1 1250 ILE n 
1 1251 LEU n 
1 1252 ALA n 
1 1253 LEU n 
1 1254 LEU n 
1 1255 GLN n 
1 1256 GLN n 
1 1257 GLN n 
1 1258 PRO n 
1 1259 PRO n 
1 1260 VAL n 
1 1261 LYS n 
1 1262 GLY n 
1 1263 GLN n 
1 1264 ALA n 
1 1265 ALA n 
1 1266 VAL n 
1 1267 PRO n 
1 1268 ILE n 
1 1269 GLN n 
1 1270 LEU n 
1 1271 THR n 
1 1272 LEU n 
1 1273 LEU n 
1 1274 HIS n 
1 1275 TYR n 
1 1276 LYS n 
1 1277 ALA n 
1 1278 ARG n 
1 1279 SER n 
1 1280 SER n 
1 1281 PRO n 
1 1282 TYR n 
1 1283 PRO n 
1 1284 GLY n 
1 1285 SER n 
1 1286 THR n 
1 1287 ALA n 
1 1288 LYS n 
1 1289 ARG n 
1 1290 PHE n 
1 1291 ALA n 
1 1292 VAL n 
1 1293 GLN n 
1 1294 ASP n 
1 1295 ASN n 
1 1296 MET n 
1 1297 VAL n 
1 1298 ASP n 
1 1299 TRP n 
1 1300 GLN n 
1 1301 VAL n 
1 1302 PRO n 
1 1303 PHE n 
1 1304 PRO n 
1 1305 ASP n 
1 1306 TYR n 
1 1307 LYS n 
1 1308 PRO n 
1 1309 VAL n 
1 1310 ASN n 
1 1311 TYR n 
1 1312 THR n 
1 1313 ALA n 
1 1314 PRO n 
1 1315 VAL n 
1 1316 VAL n 
1 1317 LEU n 
1 1318 ALA n 
1 1319 ASN n 
1 1320 PRO n 
1 1321 VAL n 
1 1322 TRP n 
1 1323 ALA n 
1 1324 ASP n 
1 1325 LYS n 
1 1326 ASP n 
1 1327 LEU n 
1 1328 MET n 
1 1329 ALA n 
1 1330 MET n 
1 1331 SER n 
1 1332 PRO n 
1 1333 ARG n 
1 1334 PRO n 
1 1335 GLU n 
1 1336 LEU n 
1 1337 PRO n 
1 1338 TYR n 
1 1339 ASN n 
1 1340 GLN n 
1 1341 MET n 
1 1342 ASP n 
1 1343 HIS n 
1 1344 THR n 
1 1345 CYS n 
1 1346 ASN n 
1 1347 VAL n 
1 1348 ASN n 
1 1349 ARG n 
1 1350 VAL n 
1 1351 SER n 
1 1352 TYR n 
1 1353 ASN n 
1 1354 GLY n 
1 1355 THR n 
1 1356 TYR n 
1 1357 VAL n 
1 1358 VAL n 
1 1359 LYS n 
1 1360 ASP n 
1 1361 GLY n 
1 1362 LEU n 
1 1363 PRO n 
1 1364 LEU n 
1 1365 ASN n 
1 1366 PRO n 
1 1367 MET n 
1 1368 GLY n 
1 1369 ARG n 
1 1370 THR n 
1 1371 GLY n 
1 1372 MET n 
1 1373 GLN n 
1 1374 GLY n 
1 1375 ARG n 
1 1376 GLY n 
1 1377 LEU n 
1 1378 LEU n 
1 1379 GLY n 
1 1380 ARG n 
1 1381 PHE n 
1 1382 GLY n 
1 1383 PRO n 
1 1384 ASN n 
1 1385 HIS n 
1 1386 ALA n 
1 1387 ALA n 
1 1388 ASP n 
1 1389 PRO n 
1 1390 VAL n 
1 1391 VAL n 
1 1392 THR n 
1 1393 ARG n 
1 1394 TRP n 
1 1395 LYS n 
1 1396 ARG n 
1 1397 THR n 
1 1398 SER n 
1 1399 ALA n 
1 1400 GLY n 
1 1401 VAL n 
1 1402 MET n 
1 1403 LEU n 
1 1404 GLN n 
1 1405 GLY n 
1 1406 GLY n 
1 1407 LYS n 
1 1408 LYS n 
1 1409 VAL n 
1 1410 LEU n 
1 1411 GLU n 
1 1412 PHE n 
1 1413 VAL n 
1 1414 ALA n 
1 1415 ILE n 
1 1416 GLN n 
1 1417 ARG n 
1 1418 LYS n 
1 1419 ASP n 
1 1420 ASN n 
1 1421 ASN n 
1 1422 GLN n 
1 1423 TRP n 
1 1424 ALA n 
1 1425 ILE n 
1 1426 PRO n 
1 1427 GLY n 
1 1428 GLY n 
1 1429 MET n 
1 1430 VAL n 
1 1431 GLU n 
1 1432 PRO n 
1 1433 GLY n 
1 1434 GLN n 
1 1435 LEU n 
1 1436 VAL n 
1 1437 THR n 
1 1438 GLN n 
1 1439 ALA n 
1 1440 LEU n 
1 1441 LYS n 
1 1442 ALA n 
1 1443 GLU n 
1 1444 PHE n 
1 1445 GLY n 
1 1446 GLU n 
1 1447 GLU n 
1 1448 ALA n 
1 1449 MET n 
1 1450 ALA n 
1 1451 LYS n 
1 1452 LEU n 
1 1453 ASN n 
1 1454 VAL n 
1 1455 SER n 
1 1456 GLN n 
1 1457 GLU n 
1 1458 GLU n 
1 1459 LYS n 
1 1460 GLU n 
1 1461 ARG n 
1 1462 ILE n 
1 1463 ALA n 
1 1464 LYS n 
1 1465 GLN n 
1 1466 ILE n 
1 1467 GLU n 
1 1468 ARG n 
1 1469 LEU n 
1 1470 PHE n 
1 1471 GLN n 
1 1472 GLN n 
1 1473 GLY n 
1 1474 GLN n 
1 1475 GLU n 
1 1476 ILE n 
1 1477 TYR n 
1 1478 LYS n 
1 1479 GLY n 
1 1480 TYR n 
1 1481 VAL n 
1 1482 ASP n 
1 1483 ASP n 
1 1484 PRO n 
1 1485 ARG n 
1 1486 ASN n 
1 1487 THR n 
1 1488 ASP n 
1 1489 ASN n 
1 1490 ALA n 
1 1491 TRP n 
1 1492 MET n 
1 1493 GLU n 
1 1494 THR n 
1 1495 VAL n 
1 1496 ALA n 
1 1497 VAL n 
1 1498 ASN n 
1 1499 PHE n 
1 1500 HIS n 
1 1501 ASP n 
1 1502 ASP n 
1 1503 LYS n 
1 1504 GLY n 
1 1505 ASP n 
1 1506 LEU n 
1 1507 PHE n 
1 1508 GLY n 
1 1509 ASP n 
1 1510 ILE n 
1 1511 THR n 
1 1512 LEU n 
1 1513 GLN n 
1 1514 ALA n 
1 1515 GLY n 
1 1516 ASP n 
1 1517 ASP n 
1 1518 ALA n 
1 1519 ALA n 
1 1520 ALA n 
1 1521 VAL n 
1 1522 ARG n 
1 1523 TRP n 
1 1524 GLN n 
1 1525 ARG n 
1 1526 VAL n 
1 1527 SER n 
1 1528 GLY n 
1 1529 ASN n 
1 1530 ILE n 
1 1531 PRO n 
1 1532 LEU n 
1 1533 TYR n 
1 1534 ALA n 
1 1535 SER n 
1 1536 HIS n 
1 1537 VAL n 
1 1538 SER n 
1 1539 ILE n 
1 1540 LEU n 
1 1541 GLU n 
1 1542 LYS n 
1 1543 VAL n 
1 1544 ALA n 
1 1545 LYS n 
1 1546 MET n 
1 1547 ARG n 
1 1548 ASP n 
1 1549 ALA n 
1 1550 ALA n 
1 1551 PHE n 
1 1552 SER n 
1 1553 ASN n 
1 1554 SER n 
1 1555 LEU n 
1 1556 GLU n 
1 1557 VAL n 
1 1558 LEU n 
1 1559 PHE n 
1 1560 GLN 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                   1560 
_entity_src_gen.gene_src_common_name               'starlet sea anemone' 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'TRPM2, v1g248535' 
_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      'Nematostella vectensis' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     45351 
_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      'Homo sapiens' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     9606 
_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                   ? 
# 
_pdbx_entity_branch.entity_id   2 
_pdbx_entity_branch.type        oligosaccharide 
# 
loop_
_pdbx_entity_branch_descriptor.ordinal 
_pdbx_entity_branch_descriptor.entity_id 
_pdbx_entity_branch_descriptor.descriptor 
_pdbx_entity_branch_descriptor.type 
_pdbx_entity_branch_descriptor.program 
_pdbx_entity_branch_descriptor.program_version 
1 2 DGlcpNAcb1-4DGlcpNAcb1-ROH                            'Glycam Condensed Sequence' GMML       1.0   
2 2 'WURCS=2.0/1,2,1/[a2122h-1b_1-5_2*NCC/3=O]/1-1/a4-b1' WURCS                       PDB2Glycan 1.1.0 
3 2 '[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}}'       LINUCS                      PDB-CARE   ?     
# 
_pdbx_entity_branch_link.link_id                    1 
_pdbx_entity_branch_link.entity_id                  2 
_pdbx_entity_branch_link.entity_branch_list_num_1   2 
_pdbx_entity_branch_link.comp_id_1                  NAG 
_pdbx_entity_branch_link.atom_id_1                  C1 
_pdbx_entity_branch_link.leaving_atom_id_1          O1 
_pdbx_entity_branch_link.entity_branch_list_num_2   1 
_pdbx_entity_branch_link.comp_id_2                  NAG 
_pdbx_entity_branch_link.atom_id_2                  O4 
_pdbx_entity_branch_link.leaving_atom_id_2          HO4 
_pdbx_entity_branch_link.value_order                sing 
_pdbx_entity_branch_link.details                    ? 
# 
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 
A2R non-polymer                  . 
;[(2R,3R,4R,5R)-5-(6-AMINO-9H-PURIN-9-YL)-3-HYDROXY-4-(PHOSPHONOOXY)TETRAHYDROFURAN-2-YL]METHYL [(2R,3S,4R,5R)-3,4,5-TRIHYDROXYTETRAHYDROFURAN-2-YL]METHYL DIHYDROGEN DIPHOSPHATE
;
? 'C15 H24 N5 O17 P3' 639.296 
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 
CA  non-polymer                  . 'CALCIUM ION' ? 'Ca 2'              40.078  
CYS 'L-peptide linking'          y CYSTEINE ? 'C3 H7 N O2 S'      121.158 
GLN 'L-peptide linking'          y GLUTAMINE ? 'C5 H10 N2 O3'      146.144 
GLU 'L-peptide linking'          y 'GLUTAMIC ACID' ? 'C5 H9 N O4'        147.129 
GLY 'peptide linking'            y GLYCINE ? 'C2 H5 N O2'        75.067  
HIS 'L-peptide linking'          y HISTIDINE ? 'C6 H10 N3 O2 1'    156.162 
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 
NAG 'D-saccharide, beta linking' . 2-acetamido-2-deoxy-beta-D-glucopyranose 
;N-acetyl-beta-D-glucosamine; 2-acetamido-2-deoxy-beta-D-glucose; 2-acetamido-2-deoxy-D-glucose; 2-acetamido-2-deoxy-glucose; N-ACETYL-D-GLUCOSAMINE
;
'C8 H15 N O6'       221.208 
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_chem_comp_identifier.comp_id 
_pdbx_chem_comp_identifier.type 
_pdbx_chem_comp_identifier.program 
_pdbx_chem_comp_identifier.program_version 
_pdbx_chem_comp_identifier.identifier 
NAG 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DGlcpNAcb                      
NAG 'COMMON NAME'                         GMML     1.0 N-acetyl-b-D-glucopyranosamine 
NAG 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-GlcpNAc                    
NAG 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 GlcNAc                         
# 
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    GLY 2    2    ?    ?   ?   A . n 
A 1 3    LYS 3    3    ?    ?   ?   A . n 
A 1 4    ASP 4    4    ?    ?   ?   A . n 
A 1 5    SER 5    5    ?    ?   ?   A . n 
A 1 6    PHE 6    6    ?    ?   ?   A . n 
A 1 7    THR 7    7    ?    ?   ?   A . n 
A 1 8    PRO 8    8    ?    ?   ?   A . n 
A 1 9    LEU 9    9    ?    ?   ?   A . n 
A 1 10   TYR 10   10   ?    ?   ?   A . n 
A 1 11   ASP 11   11   ?    ?   ?   A . n 
A 1 12   GLY 12   12   ?    ?   ?   A . n 
A 1 13   GLY 13   13   ?    ?   ?   A . n 
A 1 14   ASP 14   14   ?    ?   ?   A . n 
A 1 15   SER 15   15   ?    ?   ?   A . n 
A 1 16   SER 16   16   ?    ?   ?   A . n 
A 1 17   HIS 17   17   ?    ?   ?   A . n 
A 1 18   VAL 18   18   ?    ?   ?   A . n 
A 1 19   HIS 19   19   ?    ?   ?   A . n 
A 1 20   LEU 20   20   ?    ?   ?   A . n 
A 1 21   ASN 21   21   ?    ?   ?   A . n 
A 1 22   LYS 22   22   ?    ?   ?   A . n 
A 1 23   PHE 23   23   ?    ?   ?   A . n 
A 1 24   GLY 24   24   ?    ?   ?   A . n 
A 1 25   SER 25   25   ?    ?   ?   A . n 
A 1 26   ASN 26   26   ?    ?   ?   A . n 
A 1 27   GLN 27   27   ?    ?   ?   A . n 
A 1 28   LEU 28   28   ?    ?   ?   A . n 
A 1 29   SER 29   29   ?    ?   ?   A . n 
A 1 30   GLN 30   30   ?    ?   ?   A . n 
A 1 31   SER 31   31   ?    ?   ?   A . n 
A 1 32   LYS 32   32   ?    ?   ?   A . n 
A 1 33   LYS 33   33   ?    ?   ?   A . n 
A 1 34   SER 34   34   ?    ?   ?   A . n 
A 1 35   TRP 35   35   ?    ?   ?   A . n 
A 1 36   ILE 36   36   ?    ?   ?   A . n 
A 1 37   ALA 37   37   ?    ?   ?   A . n 
A 1 38   ARG 38   38   ?    ?   ?   A . n 
A 1 39   ASN 39   39   ?    ?   ?   A . n 
A 1 40   PHE 40   40   ?    ?   ?   A . n 
A 1 41   SER 41   41   ?    ?   ?   A . n 
A 1 42   ARG 42   42   ?    ?   ?   A . n 
A 1 43   ARG 43   43   ?    ?   ?   A . n 
A 1 44   GLU 44   44   ?    ?   ?   A . n 
A 1 45   CYS 45   45   ?    ?   ?   A . n 
A 1 46   ILE 46   46   ?    ?   ?   A . n 
A 1 47   ARG 47   47   ?    ?   ?   A . n 
A 1 48   PHE 48   48   ?    ?   ?   A . n 
A 1 49   VAL 49   49   ?    ?   ?   A . n 
A 1 50   PRO 50   50   ?    ?   ?   A . n 
A 1 51   LYS 51   51   ?    ?   ?   A . n 
A 1 52   SER 52   52   ?    ?   ?   A . n 
A 1 53   HIS 53   53   ?    ?   ?   A . n 
A 1 54   ASP 54   54   ?    ?   ?   A . n 
A 1 55   VAL 55   55   ?    ?   ?   A . n 
A 1 56   SER 56   56   ?    ?   ?   A . n 
A 1 57   ARG 57   57   ?    ?   ?   A . n 
A 1 58   CYS 58   58   ?    ?   ?   A . n 
A 1 59   LYS 59   59   ?    ?   ?   A . n 
A 1 60   CYS 60   60   ?    ?   ?   A . n 
A 1 61   GLY 61   61   ?    ?   ?   A . n 
A 1 62   ARG 62   62   ?    ?   ?   A . n 
A 1 63   PRO 63   63   ?    ?   ?   A . n 
A 1 64   ARG 64   64   ?    ?   ?   A . n 
A 1 65   GLU 65   65   ?    ?   ?   A . n 
A 1 66   ARG 66   66   ?    ?   ?   A . n 
A 1 67   HIS 67   67   ?    ?   ?   A . n 
A 1 68   SER 68   68   ?    ?   ?   A . n 
A 1 69   GLN 69   69   ?    ?   ?   A . n 
A 1 70   GLN 70   70   ?    ?   ?   A . n 
A 1 71   ALA 71   71   ?    ?   ?   A . n 
A 1 72   LEU 72   72   ?    ?   ?   A . n 
A 1 73   GLU 73   73   ?    ?   ?   A . n 
A 1 74   SER 74   74   ?    ?   ?   A . n 
A 1 75   GLY 75   75   ?    ?   ?   A . n 
A 1 76   GLN 76   76   ?    ?   ?   A . n 
A 1 77   GLY 77   77   ?    ?   ?   A . n 
A 1 78   SER 78   78   ?    ?   ?   A . n 
A 1 79   GLU 79   79   ?    ?   ?   A . n 
A 1 80   GLU 80   80   ?    ?   ?   A . n 
A 1 81   TRP 81   81   ?    ?   ?   A . n 
A 1 82   ASN 82   82   ?    ?   ?   A . n 
A 1 83   VAL 83   83   ?    ?   ?   A . n 
A 1 84   ALA 84   84   ?    ?   ?   A . n 
A 1 85   SER 85   85   ?    ?   ?   A . n 
A 1 86   CYS 86   86   ?    ?   ?   A . n 
A 1 87   THR 87   87   ?    ?   ?   A . n 
A 1 88   THR 88   88   ?    ?   ?   A . n 
A 1 89   LYS 89   89   ?    ?   ?   A . n 
A 1 90   HIS 90   90   ?    ?   ?   A . n 
A 1 91   PRO 91   91   ?    ?   ?   A . n 
A 1 92   THR 92   92   ?    ?   ?   A . n 
A 1 93   ASN 93   93   ?    ?   ?   A . n 
A 1 94   ALA 94   94   94   ALA ALA A . n 
A 1 95   TYR 95   95   95   TYR TYR A . n 
A 1 96   GLY 96   96   96   GLY GLY A . n 
A 1 97   GLU 97   97   97   GLU GLU A . n 
A 1 98   ILE 98   98   98   ILE ILE A . n 
A 1 99   ASP 99   99   99   ASP ASP A . n 
A 1 100  PHE 100  100  100  PHE PHE A . n 
A 1 101  GLU 101  101  101  GLU GLU A . n 
A 1 102  GLY 102  102  102  GLY GLY A . n 
A 1 103  TYR 103  103  103  TYR TYR A . n 
A 1 104  GLY 104  104  104  GLY GLY A . n 
A 1 105  GLY 105  105  105  GLY GLY A . n 
A 1 106  GLN 106  106  106  GLN GLN A . n 
A 1 107  LYS 107  107  107  LYS LYS A . n 
A 1 108  ARG 108  108  108  ARG ARG A . n 
A 1 109  ALA 109  109  109  ALA ALA A . n 
A 1 110  PRO 110  110  110  PRO PRO A . n 
A 1 111  TYR 111  111  111  TYR TYR A . n 
A 1 112  LEU 112  112  112  LEU LEU A . n 
A 1 113  ARG 113  113  113  ARG ARG A . n 
A 1 114  MET 114  114  114  MET MET A . n 
A 1 115  SER 115  115  115  SER SER A . n 
A 1 116  HIS 116  116  116  HIS HIS A . n 
A 1 117  ASP 117  117  117  ASP ASP A . n 
A 1 118  THR 118  118  118  THR THR A . n 
A 1 119  ASP 119  119  119  ASP ASP A . n 
A 1 120  ALA 120  120  120  ALA ALA A . n 
A 1 121  ASN 121  121  121  ASN ASN A . n 
A 1 122  LEU 122  122  122  LEU LEU A . n 
A 1 123  VAL 123  123  123  VAL VAL A . n 
A 1 124  ILE 124  124  124  ILE ILE A . n 
A 1 125  THR 125  125  125  THR THR A . n 
A 1 126  LEU 126  126  126  LEU LEU A . n 
A 1 127  MET 127  127  127  MET MET A . n 
A 1 128  LEU 128  128  128  LEU LEU A . n 
A 1 129  LYS 129  129  129  LYS LYS A . n 
A 1 130  ARG 130  130  130  ARG ARG A . n 
A 1 131  TRP 131  131  131  TRP TRP A . n 
A 1 132  ASN 132  132  132  ASN ASN A . n 
A 1 133  LEU 133  133  133  LEU LEU A . n 
A 1 134  GLU 134  134  134  GLU GLU A . n 
A 1 135  ILE 135  135  135  ILE ILE A . n 
A 1 136  PRO 136  136  136  PRO PRO A . n 
A 1 137  ASN 137  137  137  ASN ASN A . n 
A 1 138  LEU 138  138  138  LEU LEU A . n 
A 1 139  VAL 139  139  139  VAL VAL A . n 
A 1 140  ILE 140  140  140  ILE ILE A . n 
A 1 141  SER 141  141  141  SER SER A . n 
A 1 142  VAL 142  142  142  VAL VAL A . n 
A 1 143  THR 143  143  143  THR THR A . n 
A 1 144  GLY 144  144  144  GLY GLY A . n 
A 1 145  GLY 145  145  145  GLY GLY A . n 
A 1 146  ALA 146  146  146  ALA ALA A . n 
A 1 147  LYS 147  147  147  LYS LYS A . n 
A 1 148  SER 148  148  148  SER SER A . n 
A 1 149  PHE 149  149  149  PHE PHE A . n 
A 1 150  VAL 150  150  150  VAL VAL A . n 
A 1 151  LEU 151  151  151  LEU LEU A . n 
A 1 152  LYS 152  152  152  LYS LYS A . n 
A 1 153  PRO 153  153  153  PRO PRO A . n 
A 1 154  ARG 154  154  154  ARG ARG A . n 
A 1 155  LEU 155  155  155  LEU LEU A . n 
A 1 156  ARG 156  156  156  ARG ARG A . n 
A 1 157  GLU 157  157  157  GLU GLU A . n 
A 1 158  MET 158  158  158  MET MET A . n 
A 1 159  PHE 159  159  159  PHE PHE A . n 
A 1 160  ARG 160  160  160  ARG ARG A . n 
A 1 161  ARG 161  161  161  ARG ARG A . n 
A 1 162  GLY 162  162  162  GLY GLY A . n 
A 1 163  LEU 163  163  163  LEU LEU A . n 
A 1 164  ILE 164  164  164  ILE ILE A . n 
A 1 165  LYS 165  165  165  LYS LYS A . n 
A 1 166  ALA 166  166  166  ALA ALA A . n 
A 1 167  ALA 167  167  167  ALA ALA A . n 
A 1 168  LYS 168  168  168  LYS LYS A . n 
A 1 169  THR 169  169  169  THR THR A . n 
A 1 170  THR 170  170  170  THR THR A . n 
A 1 171  GLY 171  171  171  GLY GLY A . n 
A 1 172  ALA 172  172  172  ALA ALA A . n 
A 1 173  TRP 173  173  173  TRP TRP A . n 
A 1 174  ILE 174  174  174  ILE ILE A . n 
A 1 175  ILE 175  175  175  ILE ILE A . n 
A 1 176  THR 176  176  176  THR THR A . n 
A 1 177  GLY 177  177  177  GLY GLY A . n 
A 1 178  GLY 178  178  178  GLY GLY A . n 
A 1 179  THR 179  179  179  THR THR A . n 
A 1 180  ASN 180  180  180  ASN ASN A . n 
A 1 181  THR 181  181  181  THR THR A . n 
A 1 182  GLY 182  182  182  GLY GLY A . n 
A 1 183  VAL 183  183  183  VAL VAL A . n 
A 1 184  MET 184  184  184  MET MET A . n 
A 1 185  LYS 185  185  185  LYS LYS A . n 
A 1 186  HIS 186  186  186  HIS HIS A . n 
A 1 187  VAL 187  187  187  VAL VAL A . n 
A 1 188  GLY 188  188  188  GLY GLY A . n 
A 1 189  GLU 189  189  189  GLU GLU A . n 
A 1 190  ALA 190  190  190  ALA ALA A . n 
A 1 191  VAL 191  191  191  VAL VAL A . n 
A 1 192  LYS 192  192  192  LYS LYS A . n 
A 1 193  GLU 193  193  193  GLU GLU A . n 
A 1 194  GLN 194  194  194  GLN GLN A . n 
A 1 195  GLN 195  195  195  GLN GLN A . n 
A 1 196  LEU 196  196  196  LEU LEU A . n 
A 1 197  MET 197  197  197  MET MET A . n 
A 1 198  PHE 198  198  198  PHE PHE A . n 
A 1 199  GLY 199  199  199  GLY GLY A . n 
A 1 200  SER 200  200  200  SER SER A . n 
A 1 201  ASP 201  201  201  ASP ASP A . n 
A 1 202  THR 202  202  202  THR THR A . n 
A 1 203  GLN 203  203  203  GLN GLN A . n 
A 1 204  VAL 204  204  204  VAL VAL A . n 
A 1 205  ASN 205  205  205  ASN ASN A . n 
A 1 206  VAL 206  206  206  VAL VAL A . n 
A 1 207  ILE 207  207  207  ILE ILE A . n 
A 1 208  GLY 208  208  208  GLY GLY A . n 
A 1 209  ILE 209  209  209  ILE ILE A . n 
A 1 210  ALA 210  210  210  ALA ALA A . n 
A 1 211  THR 211  211  211  THR THR A . n 
A 1 212  TRP 212  212  212  TRP TRP A . n 
A 1 213  GLY 213  213  213  GLY GLY A . n 
A 1 214  ILE 214  214  214  ILE ILE A . n 
A 1 215  VAL 215  215  215  VAL VAL A . n 
A 1 216  ASP 216  216  216  ASP ASP A . n 
A 1 217  LYS 217  217  ?    ?   ?   A . n 
A 1 218  GLN 218  218  ?    ?   ?   A . n 
A 1 219  SER 219  219  ?    ?   ?   A . n 
A 1 220  ASP 220  220  ?    ?   ?   A . n 
A 1 221  LEU 221  221  ?    ?   ?   A . n 
A 1 222  ILE 222  222  ?    ?   ?   A . n 
A 1 223  SER 223  223  ?    ?   ?   A . n 
A 1 224  GLU 224  224  ?    ?   ?   A . n 
A 1 225  LYS 225  225  ?    ?   ?   A . n 
A 1 226  ASN 226  226  ?    ?   ?   A . n 
A 1 227  GLY 227  227  ?    ?   ?   A . n 
A 1 228  LYS 228  228  ?    ?   ?   A . n 
A 1 229  TYR 229  229  ?    ?   ?   A . n 
A 1 230  PRO 230  230  ?    ?   ?   A . n 
A 1 231  ALA 231  231  ?    ?   ?   A . n 
A 1 232  LEU 232  232  ?    ?   ?   A . n 
A 1 233  TYR 233  233  ?    ?   ?   A . n 
A 1 234  SER 234  234  ?    ?   ?   A . n 
A 1 235  MET 235  235  ?    ?   ?   A . n 
A 1 236  GLU 236  236  ?    ?   ?   A . n 
A 1 237  PRO 237  237  ?    ?   ?   A . n 
A 1 238  THR 238  238  ?    ?   ?   A . n 
A 1 239  PRO 239  239  ?    ?   ?   A . n 
A 1 240  GLY 240  240  ?    ?   ?   A . n 
A 1 241  HIS 241  241  ?    ?   ?   A . n 
A 1 242  GLN 242  242  ?    ?   ?   A . n 
A 1 243  GLY 243  243  243  GLY GLY A . n 
A 1 244  ALA 244  244  244  ALA ALA A . n 
A 1 245  MET 245  245  245  MET MET A . n 
A 1 246  LEU 246  246  246  LEU LEU A . n 
A 1 247  ASP 247  247  247  ASP ASP A . n 
A 1 248  PRO 248  248  248  PRO PRO A . n 
A 1 249  ASN 249  249  249  ASN ASN A . n 
A 1 250  HIS 250  250  250  HIS HIS A . n 
A 1 251  SER 251  251  251  SER SER A . n 
A 1 252  HIS 252  252  252  HIS HIS A . n 
A 1 253  PHE 253  253  253  PHE PHE A . n 
A 1 254  PHE 254  254  254  PHE PHE A . n 
A 1 255  LEU 255  255  255  LEU LEU A . n 
A 1 256  VAL 256  256  256  VAL VAL A . n 
A 1 257  ASP 257  257  257  ASP ASP A . n 
A 1 258  ASP 258  258  258  ASP ASP A . n 
A 1 259  GLY 259  259  259  GLY GLY A . n 
A 1 260  THR 260  260  260  THR THR A . n 
A 1 261  GLU 261  261  261  GLU GLU A . n 
A 1 262  GLY 262  262  262  GLY GLY A . n 
A 1 263  LYS 263  263  263  LYS LYS A . n 
A 1 264  TYR 264  264  264  TYR TYR A . n 
A 1 265  GLY 265  265  265  GLY GLY A . n 
A 1 266  VAL 266  266  266  VAL VAL A . n 
A 1 267  GLU 267  267  267  GLU GLU A . n 
A 1 268  ILE 268  268  268  ILE ILE A . n 
A 1 269  GLY 269  269  269  GLY GLY A . n 
A 1 270  MET 270  270  270  MET MET A . n 
A 1 271  ARG 271  271  271  ARG ARG A . n 
A 1 272  SER 272  272  272  SER SER A . n 
A 1 273  ARG 273  273  273  ARG ARG A . n 
A 1 274  ILE 274  274  274  ILE ILE A . n 
A 1 275  GLU 275  275  275  GLU GLU A . n 
A 1 276  GLU 276  276  276  GLU GLU A . n 
A 1 277  ALA 277  277  277  ALA ALA A . n 
A 1 278  ILE 278  278  278  ILE ILE A . n 
A 1 279  MET 279  279  279  MET MET A . n 
A 1 280  LYS 280  280  280  LYS LYS A . n 
A 1 281  VAL 281  281  281  VAL VAL A . n 
A 1 282  LYS 282  282  ?    ?   ?   A . n 
A 1 283  THR 283  283  ?    ?   ?   A . n 
A 1 284  ASP 284  284  ?    ?   ?   A . n 
A 1 285  SER 285  285  ?    ?   ?   A . n 
A 1 286  ARG 286  286  ?    ?   ?   A . n 
A 1 287  SER 287  287  ?    ?   ?   A . n 
A 1 288  GLU 288  288  ?    ?   ?   A . n 
A 1 289  ALA 289  289  ?    ?   ?   A . n 
A 1 290  GLY 290  290  ?    ?   ?   A . n 
A 1 291  SER 291  291  ?    ?   ?   A . n 
A 1 292  ILE 292  292  292  ILE ILE A . n 
A 1 293  GLY 293  293  293  GLY GLY A . n 
A 1 294  VAL 294  294  294  VAL VAL A . n 
A 1 295  PRO 295  295  295  PRO PRO A . n 
A 1 296  VAL 296  296  296  VAL VAL A . n 
A 1 297  VAL 297  297  297  VAL VAL A . n 
A 1 298  LEU 298  298  298  LEU LEU A . n 
A 1 299  LEU 299  299  299  LEU LEU A . n 
A 1 300  VAL 300  300  300  VAL VAL A . n 
A 1 301  LEU 301  301  301  LEU LEU A . n 
A 1 302  GLU 302  302  302  GLU GLU A . n 
A 1 303  GLY 303  303  303  GLY GLY A . n 
A 1 304  GLY 304  304  304  GLY GLY A . n 
A 1 305  PRO 305  305  305  PRO PRO A . n 
A 1 306  ASN 306  306  306  ASN ASN A . n 
A 1 307  THR 307  307  307  THR THR A . n 
A 1 308  VAL 308  308  308  VAL VAL A . n 
A 1 309  ALA 309  309  309  ALA ALA A . n 
A 1 310  THR 310  310  310  THR THR A . n 
A 1 311  MET 311  311  311  MET MET A . n 
A 1 312  TYR 312  312  312  TYR TYR A . n 
A 1 313  GLU 313  313  313  GLU GLU A . n 
A 1 314  LEU 314  314  314  LEU LEU A . n 
A 1 315  ILE 315  315  315  ILE ILE A . n 
A 1 316  LYS 316  316  316  LYS LYS A . n 
A 1 317  LYS 317  317  317  LYS LYS A . n 
A 1 318  LYS 318  318  318  LYS LYS A . n 
A 1 319  VAL 319  319  319  VAL VAL A . n 
A 1 320  PRO 320  320  320  PRO PRO A . n 
A 1 321  ALA 321  321  321  ALA ALA A . n 
A 1 322  VAL 322  322  322  VAL VAL A . n 
A 1 323  VAL 323  323  323  VAL VAL A . n 
A 1 324  ILE 324  324  324  ILE ILE A . n 
A 1 325  ASP 325  325  325  ASP ASP A . n 
A 1 326  GLY 326  326  326  GLY GLY A . n 
A 1 327  SER 327  327  327  SER SER A . n 
A 1 328  GLY 328  328  328  GLY GLY A . n 
A 1 329  ARG 329  329  329  ARG ARG 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  SER 332  332  332  SER SER A . n 
A 1 333  VAL 333  333  333  VAL VAL A . n 
A 1 334  VAL 334  334  334  VAL VAL A . n 
A 1 335  GLY 335  335  335  GLY GLY A . n 
A 1 336  PHE 336  336  336  PHE PHE A . n 
A 1 337  ALA 337  337  337  ALA ALA A . n 
A 1 338  TYR 338  338  338  TYR TYR A . n 
A 1 339  ASN 339  339  339  ASN ASN A . n 
A 1 340  HIS 340  340  340  HIS HIS A . n 
A 1 341  THR 341  341  341  THR THR A . n 
A 1 342  ILE 342  342  342  ILE ILE A . n 
A 1 343  LYS 343  343  343  LYS LYS A . n 
A 1 344  ARG 344  344  344  ARG ARG A . n 
A 1 345  ASN 345  345  345  ASN ASN A . n 
A 1 346  VAL 346  346  346  VAL VAL A . n 
A 1 347  ASP 347  347  347  ASP ASP A . n 
A 1 348  GLY 348  348  348  GLY GLY A . n 
A 1 349  GLN 349  349  349  GLN GLN A . n 
A 1 350  THR 350  350  350  THR THR A . n 
A 1 351  ILE 351  351  351  ILE ILE A . n 
A 1 352  ASN 352  352  352  ASN ASN A . n 
A 1 353  VAL 353  353  353  VAL VAL A . n 
A 1 354  ILE 354  354  354  ILE ILE A . n 
A 1 355  ASP 355  355  355  ASP ASP A . n 
A 1 356  PRO 356  356  356  PRO PRO A . n 
A 1 357  GLN 357  357  357  GLN GLN A . n 
A 1 358  TYR 358  358  358  TYR TYR A . n 
A 1 359  GLU 359  359  359  GLU GLU A . n 
A 1 360  ASP 360  360  360  ASP ASP A . n 
A 1 361  GLU 361  361  361  GLU GLU A . n 
A 1 362  VAL 362  362  362  VAL VAL A . n 
A 1 363  ARG 363  363  363  ARG ARG A . n 
A 1 364  ALA 364  364  364  ALA ALA A . n 
A 1 365  LYS 365  365  365  LYS LYS A . n 
A 1 366  VAL 366  366  366  VAL VAL A . n 
A 1 367  VAL 367  367  367  VAL VAL A . n 
A 1 368  GLU 368  368  368  GLU GLU A . n 
A 1 369  VAL 369  369  369  VAL VAL A . n 
A 1 370  PHE 370  370  370  PHE PHE A . n 
A 1 371  GLY 371  371  371  GLY GLY A . n 
A 1 372  ALA 372  372  372  ALA ALA A . n 
A 1 373  LYS 373  373  373  LYS LYS A . n 
A 1 374  GLY 374  374  374  GLY GLY A . n 
A 1 375  ALA 375  375  375  ALA ALA A . n 
A 1 376  ASP 376  376  376  ASP ASP A . n 
A 1 377  LYS 377  377  377  LYS LYS A . n 
A 1 378  THR 378  378  378  THR THR A . n 
A 1 379  TYR 379  379  379  TYR TYR A . n 
A 1 380  SER 380  380  380  SER SER A . n 
A 1 381  MET 381  381  381  MET MET A . n 
A 1 382  ILE 382  382  382  ILE ILE A . n 
A 1 383  LYS 383  383  383  LYS LYS A . n 
A 1 384  ASP 384  384  384  ASP ASP A . n 
A 1 385  VAL 385  385  385  VAL VAL A . n 
A 1 386  LEU 386  386  386  LEU LEU A . n 
A 1 387  GLU 387  387  387  GLU GLU A . n 
A 1 388  ASP 388  388  388  ASP ASP A . n 
A 1 389  GLU 389  389  389  GLU GLU A . n 
A 1 390  LYS 390  390  390  LYS LYS A . n 
A 1 391  MET 391  391  391  MET MET A . n 
A 1 392  ILE 392  392  392  ILE ILE A . n 
A 1 393  SER 393  393  393  SER SER A . n 
A 1 394  VAL 394  394  394  VAL VAL A . n 
A 1 395  TYR 395  395  395  TYR TYR A . n 
A 1 396  SER 396  396  396  SER SER A . n 
A 1 397  LEU 397  397  397  LEU LEU A . n 
A 1 398  ASP 398  398  398  ASP ASP A . n 
A 1 399  GLY 399  399  399  GLY GLY A . n 
A 1 400  GLU 400  400  400  GLU GLU A . n 
A 1 401  ILE 401  401  401  ILE ILE A . n 
A 1 402  SER 402  402  402  SER SER A . n 
A 1 403  GLN 403  403  403  GLN GLN A . n 
A 1 404  ASP 404  404  404  ASP ASP A . n 
A 1 405  ILE 405  405  405  ILE ILE A . n 
A 1 406  ASP 406  406  406  ASP ASP A . n 
A 1 407  LEU 407  407  407  LEU LEU A . n 
A 1 408  ALA 408  408  408  ALA ALA A . n 
A 1 409  ILE 409  409  409  ILE ILE A . n 
A 1 410  LEU 410  410  410  LEU LEU A . n 
A 1 411  LYS 411  411  411  LYS LYS A . n 
A 1 412  ALA 412  412  412  ALA ALA A . n 
A 1 413  LEU 413  413  413  LEU LEU A . n 
A 1 414  LEU 414  414  414  LEU LEU A . n 
A 1 415  LYS 415  415  415  LYS LYS A . n 
A 1 416  ALA 416  416  416  ALA ALA A . n 
A 1 417  ASN 417  417  417  ASN ASN A . n 
A 1 418  ARG 418  418  418  ARG ARG A . n 
A 1 419  SER 419  419  419  SER SER A . n 
A 1 420  SER 420  420  420  SER SER A . n 
A 1 421  PRO 421  421  421  PRO PRO A . n 
A 1 422  VAL 422  422  422  VAL VAL A . n 
A 1 423  ALA 423  423  423  ALA ALA A . n 
A 1 424  GLN 424  424  424  GLN GLN A . n 
A 1 425  LEU 425  425  425  LEU LEU A . n 
A 1 426  ASN 426  426  426  ASN ASN A . n 
A 1 427  LEU 427  427  427  LEU LEU A . n 
A 1 428  ALA 428  428  428  ALA ALA A . n 
A 1 429  LEU 429  429  429  LEU LEU A . n 
A 1 430  ALA 430  430  430  ALA ALA A . n 
A 1 431  TRP 431  431  431  TRP TRP A . n 
A 1 432  ASN 432  432  432  ASN ASN A . n 
A 1 433  ARG 433  433  433  ARG ARG A . n 
A 1 434  ILE 434  434  434  ILE ILE A . n 
A 1 435  ASP 435  435  435  ASP ASP A . n 
A 1 436  LEU 436  436  436  LEU LEU A . n 
A 1 437  ALA 437  437  437  ALA ALA A . n 
A 1 438  LYS 438  438  438  LYS LYS A . n 
A 1 439  SER 439  439  439  SER SER A . n 
A 1 440  ASP 440  440  440  ASP ASP A . n 
A 1 441  ILE 441  441  441  ILE ILE A . n 
A 1 442  PHE 442  442  442  PHE PHE A . n 
A 1 443  THR 443  443  443  THR THR A . n 
A 1 444  GLU 444  444  444  GLU GLU A . n 
A 1 445  GLU 445  445  445  GLU GLU A . n 
A 1 446  GLN 446  446  446  GLN GLN A . n 
A 1 447  GLN 447  447  447  GLN GLN A . n 
A 1 448  TRP 448  448  448  TRP TRP A . n 
A 1 449  THR 449  449  449  THR THR A . n 
A 1 450  THR 450  450  450  THR THR A . n 
A 1 451  GLU 451  451  451  GLU GLU A . n 
A 1 452  THR 452  452  452  THR THR A . n 
A 1 453  LEU 453  453  453  LEU LEU A . n 
A 1 454  SER 454  454  454  SER SER A . n 
A 1 455  ALA 455  455  455  ALA ALA A . n 
A 1 456  ALA 456  456  456  ALA ALA A . n 
A 1 457  MET 457  457  457  MET MET A . n 
A 1 458  LEU 458  458  458  LEU LEU A . n 
A 1 459  THR 459  459  459  THR THR A . n 
A 1 460  ALA 460  460  460  ALA ALA A . n 
A 1 461  LEU 461  461  461  LEU LEU A . n 
A 1 462  LEU 462  462  462  LEU LEU A . n 
A 1 463  ASP 463  463  463  ASP ASP A . n 
A 1 464  ASP 464  464  464  ASP ASP A . n 
A 1 465  LYS 465  465  465  LYS LYS A . n 
A 1 466  ALA 466  466  466  ALA ALA A . n 
A 1 467  GLU 467  467  467  GLU GLU A . n 
A 1 468  PHE 468  468  468  PHE PHE A . n 
A 1 469  ALA 469  469  469  ALA ALA A . n 
A 1 470  GLU 470  470  470  GLU GLU A . n 
A 1 471  LEU 471  471  471  LEU LEU A . n 
A 1 472  PHE 472  472  472  PHE PHE A . n 
A 1 473  LEU 473  473  473  LEU LEU A . n 
A 1 474  GLN 474  474  474  GLN GLN A . n 
A 1 475  ASN 475  475  475  ASN ASN A . n 
A 1 476  GLY 476  476  476  GLY GLY A . n 
A 1 477  LEU 477  477  477  LEU LEU A . n 
A 1 478  SER 478  478  478  SER SER A . n 
A 1 479  MET 479  479  479  MET MET A . n 
A 1 480  ARG 480  480  480  ARG ARG A . n 
A 1 481  GLU 481  481  481  GLU GLU A . n 
A 1 482  PHE 482  482  482  PHE PHE A . n 
A 1 483  LEU 483  483  483  LEU LEU A . n 
A 1 484  SER 484  484  484  SER SER A . n 
A 1 485  LEU 485  485  485  LEU LEU A . n 
A 1 486  ASP 486  486  486  ASP ASP A . n 
A 1 487  ILE 487  487  487  ILE ILE A . n 
A 1 488  LEU 488  488  488  LEU LEU A . n 
A 1 489  CYS 489  489  489  CYS CYS A . n 
A 1 490  LYS 490  490  490  LYS LYS A . n 
A 1 491  LEU 491  491  491  LEU LEU A . n 
A 1 492  TYR 492  492  492  TYR TYR A . n 
A 1 493  ALA 493  493  493  ALA ALA A . n 
A 1 494  GLU 494  494  494  GLU GLU A . n 
A 1 495  VAL 495  495  495  VAL VAL A . n 
A 1 496  PRO 496  496  496  PRO PRO A . n 
A 1 497  GLY 497  497  497  GLY GLY A . n 
A 1 498  ASN 498  498  498  ASN ASN A . n 
A 1 499  THR 499  499  499  THR THR A . n 
A 1 500  THR 500  500  500  THR THR A . n 
A 1 501  ILE 501  501  501  ILE ILE A . n 
A 1 502  LYS 502  502  502  LYS LYS A . n 
A 1 503  PRO 503  503  503  PRO PRO A . n 
A 1 504  LEU 504  504  504  LEU LEU A . n 
A 1 505  LEU 505  505  505  LEU LEU A . n 
A 1 506  GLN 506  506  506  GLN GLN A . n 
A 1 507  LYS 507  507  507  LYS LYS A . n 
A 1 508  GLU 508  508  508  GLU GLU A . n 
A 1 509  MET 509  509  509  MET MET A . n 
A 1 510  GLY 510  510  510  GLY GLY A . n 
A 1 511  LYS 511  511  511  LYS LYS A . n 
A 1 512  ARG 512  512  512  ARG ARG A . n 
A 1 513  GLN 513  513  513  GLN GLN A . n 
A 1 514  VAL 514  514  514  VAL VAL A . n 
A 1 515  LYS 515  515  515  LYS LYS A . n 
A 1 516  THR 516  516  516  THR THR A . n 
A 1 517  ILE 517  517  517  ILE ILE A . n 
A 1 518  ASP 518  518  518  ASP ASP A . n 
A 1 519  MET 519  519  519  MET MET A . n 
A 1 520  ASP 520  520  520  ASP ASP A . n 
A 1 521  VAL 521  521  521  VAL VAL A . n 
A 1 522  VAL 522  522  522  VAL VAL A . n 
A 1 523  GLY 523  523  523  GLY GLY A . n 
A 1 524  GLU 524  524  524  GLU GLU A . n 
A 1 525  VAL 525  525  525  VAL VAL A . n 
A 1 526  ILE 526  526  526  ILE ILE A . n 
A 1 527  GLU 527  527  527  GLU GLU A . n 
A 1 528  GLU 528  528  528  GLU GLU A . n 
A 1 529  LEU 529  529  529  LEU LEU A . n 
A 1 530  MET 530  530  530  MET MET A . n 
A 1 531  GLY 531  531  531  GLY GLY A . n 
A 1 532  ASP 532  532  532  ASP ASP A . n 
A 1 533  MET 533  533  533  MET MET A . n 
A 1 534  PHE 534  534  534  PHE PHE A . n 
A 1 535  GLU 535  535  535  GLU GLU A . n 
A 1 536  SER 536  536  536  SER SER A . n 
A 1 537  TYR 537  537  537  TYR TYR A . n 
A 1 538  TYR 538  538  538  TYR TYR A . n 
A 1 539  ARG 539  539  539  ARG ARG A . n 
A 1 540  LYS 540  540  540  LYS LYS A . n 
A 1 541  ASP 541  541  541  ASP ASP A . n 
A 1 542  GLY 542  542  542  GLY GLY A . n 
A 1 543  HIS 543  543  543  HIS HIS A . n 
A 1 544  TYR 544  544  544  TYR TYR A . n 
A 1 545  PHE 545  545  545  PHE PHE A . n 
A 1 546  GLY 546  546  ?    ?   ?   A . n 
A 1 547  GLU 547  547  ?    ?   ?   A . n 
A 1 548  LEU 548  548  ?    ?   ?   A . n 
A 1 549  ALA 549  549  ?    ?   ?   A . n 
A 1 550  SER 550  550  ?    ?   ?   A . n 
A 1 551  TYR 551  551  ?    ?   ?   A . n 
A 1 552  ALA 552  552  ?    ?   ?   A . n 
A 1 553  GLU 553  553  ?    ?   ?   A . n 
A 1 554  GLY 554  554  ?    ?   ?   A . n 
A 1 555  LEU 555  555  ?    ?   ?   A . n 
A 1 556  VAL 556  556  ?    ?   ?   A . n 
A 1 557  LEU 557  557  ?    ?   ?   A . n 
A 1 558  LYS 558  558  ?    ?   ?   A . n 
A 1 559  ASN 559  559  ?    ?   ?   A . n 
A 1 560  ARG 560  560  ?    ?   ?   A . n 
A 1 561  LYS 561  561  ?    ?   ?   A . n 
A 1 562  SER 562  562  ?    ?   ?   A . n 
A 1 563  SER 563  563  ?    ?   ?   A . n 
A 1 564  LYS 564  564  ?    ?   ?   A . n 
A 1 565  ASP 565  565  ?    ?   ?   A . n 
A 1 566  LEU 566  566  ?    ?   ?   A . n 
A 1 567  LEU 567  567  ?    ?   ?   A . n 
A 1 568  ALA 568  568  ?    ?   ?   A . n 
A 1 569  ASN 569  569  ?    ?   ?   A . n 
A 1 570  ILE 570  570  ?    ?   ?   A . n 
A 1 571  ASN 571  571  ?    ?   ?   A . n 
A 1 572  ARG 572  572  ?    ?   ?   A . n 
A 1 573  ILE 573  573  ?    ?   ?   A . n 
A 1 574  ASP 574  574  ?    ?   ?   A . n 
A 1 575  PRO 575  575  575  PRO PRO A . n 
A 1 576  LEU 576  576  576  LEU LEU A . n 
A 1 577  PRO 577  577  577  PRO PRO A . n 
A 1 578  THR 578  578  578  THR THR A . n 
A 1 579  PRO 579  579  579  PRO PRO A . n 
A 1 580  TYR 580  580  580  TYR TYR A . n 
A 1 581  LEU 581  581  581  LEU LEU A . n 
A 1 582  ASP 582  582  582  ASP ASP A . n 
A 1 583  VAL 583  583  583  VAL VAL A . n 
A 1 584  PHE 584  584  584  PHE PHE A . n 
A 1 585  LEU 585  585  585  LEU LEU A . n 
A 1 586  TRP 586  586  586  TRP TRP A . n 
A 1 587  ALA 587  587  587  ALA ALA A . n 
A 1 588  VAL 588  588  588  VAL VAL A . n 
A 1 589  LEU 589  589  589  LEU LEU A . n 
A 1 590  CYS 590  590  590  CYS CYS A . n 
A 1 591  ASN 591  591  591  ASN ASN A . n 
A 1 592  ARG 592  592  592  ARG ARG A . n 
A 1 593  ARG 593  593  593  ARG ARG A . n 
A 1 594  GLU 594  594  594  GLU GLU A . n 
A 1 595  LEU 595  595  595  LEU LEU A . n 
A 1 596  ALA 596  596  596  ALA ALA A . n 
A 1 597  ARG 597  597  597  ARG ARG A . n 
A 1 598  VAL 598  598  598  VAL VAL A . n 
A 1 599  LEU 599  599  599  LEU LEU A . n 
A 1 600  TRP 600  600  600  TRP TRP A . n 
A 1 601  GLU 601  601  601  GLU GLU A . n 
A 1 602  ALA 602  602  602  ALA ALA A . n 
A 1 603  GLY 603  603  603  GLY GLY A . n 
A 1 604  ARG 604  604  604  ARG ARG A . n 
A 1 605  GLU 605  605  605  GLU GLU A . n 
A 1 606  PRO 606  606  606  PRO PRO A . n 
A 1 607  MET 607  607  607  MET MET A . n 
A 1 608  ALA 608  608  608  ALA ALA A . n 
A 1 609  ALA 609  609  609  ALA ALA A . n 
A 1 610  ALA 610  610  610  ALA ALA A . n 
A 1 611  LEU 611  611  611  LEU LEU A . n 
A 1 612  MET 612  612  612  MET MET A . n 
A 1 613  ALA 613  613  613  ALA ALA A . n 
A 1 614  SER 614  614  614  SER SER A . n 
A 1 615  ARG 615  615  615  ARG ARG A . n 
A 1 616  LEU 616  616  616  LEU LEU A . n 
A 1 617  LEU 617  617  617  LEU LEU A . n 
A 1 618  LYS 618  618  618  LYS LYS A . n 
A 1 619  ARG 619  619  619  ARG ARG A . n 
A 1 620  MET 620  620  620  MET MET A . n 
A 1 621  ALA 621  621  621  ALA ALA A . n 
A 1 622  SER 622  622  622  SER SER A . n 
A 1 623  ARG 623  623  623  ARG ARG A . n 
A 1 624  ALA 624  624  624  ALA ALA A . n 
A 1 625  GLN 625  625  625  GLN GLN A . n 
A 1 626  GLU 626  626  626  GLU GLU A . n 
A 1 627  ASP 627  627  627  ASP ASP A . n 
A 1 628  ASN 628  628  628  ASN ASN A . n 
A 1 629  THR 629  629  629  THR THR A . n 
A 1 630  ILE 630  630  630  ILE ILE A . n 
A 1 631  THR 631  631  631  THR THR A . n 
A 1 632  ASP 632  632  632  ASP ASP A . n 
A 1 633  ILE 633  633  633  ILE ILE A . n 
A 1 634  SER 634  634  634  SER SER A . n 
A 1 635  SER 635  635  635  SER SER A . n 
A 1 636  ASP 636  636  636  ASP ASP A . n 
A 1 637  LEU 637  637  637  LEU LEU A . n 
A 1 638  TYR 638  638  638  TYR TYR A . n 
A 1 639  ASP 639  639  639  ASP ASP A . n 
A 1 640  HIS 640  640  640  HIS HIS A . n 
A 1 641  ALA 641  641  641  ALA ALA A . n 
A 1 642  ARG 642  642  642  ARG ARG A . n 
A 1 643  LEU 643  643  643  LEU LEU A . n 
A 1 644  PHE 644  644  644  PHE PHE A . n 
A 1 645  GLU 645  645  645  GLU GLU A . n 
A 1 646  GLU 646  646  646  GLU GLU A . n 
A 1 647  ARG 647  647  647  ARG ARG A . n 
A 1 648  ALA 648  648  648  ALA ALA A . n 
A 1 649  VAL 649  649  649  VAL VAL A . n 
A 1 650  GLY 650  650  650  GLY GLY A . n 
A 1 651  VAL 651  651  651  VAL VAL A . n 
A 1 652  LEU 652  652  652  LEU LEU A . n 
A 1 653  ASP 653  653  653  ASP ASP A . n 
A 1 654  GLU 654  654  654  GLU GLU A . n 
A 1 655  CYS 655  655  655  CYS CYS A . n 
A 1 656  PHE 656  656  656  PHE PHE A . n 
A 1 657  ASN 657  657  657  ASN ASN A . n 
A 1 658  GLU 658  658  658  GLU GLU A . n 
A 1 659  ASN 659  659  659  ASN ASN A . n 
A 1 660  GLU 660  660  660  GLU GLU A . n 
A 1 661  THR 661  661  661  THR THR A . n 
A 1 662  LEU 662  662  662  LEU LEU A . n 
A 1 663  SER 663  663  663  SER SER A . n 
A 1 664  GLN 664  664  664  GLN GLN A . n 
A 1 665  THR 665  665  665  THR THR A . n 
A 1 666  LEU 666  666  666  LEU LEU A . n 
A 1 667  LEU 667  667  667  LEU LEU A . n 
A 1 668  VAL 668  668  668  VAL VAL A . n 
A 1 669  ARG 669  669  669  ARG ARG A . n 
A 1 670  GLU 670  670  670  GLU GLU A . n 
A 1 671  LEU 671  671  671  LEU LEU A . n 
A 1 672  ASP 672  672  672  ASP ASP A . n 
A 1 673  HIS 673  673  673  HIS HIS A . n 
A 1 674  TYR 674  674  674  TYR TYR A . n 
A 1 675  SER 675  675  675  SER SER A . n 
A 1 676  ARG 676  676  676  ARG ARG A . n 
A 1 677  MET 677  677  677  MET MET A . n 
A 1 678  THR 678  678  678  THR THR A . n 
A 1 679  ALA 679  679  679  ALA ALA A . n 
A 1 680  LEU 680  680  680  LEU LEU A . n 
A 1 681  GLU 681  681  681  GLU GLU A . n 
A 1 682  LEU 682  682  682  LEU LEU A . n 
A 1 683  ALA 683  683  683  ALA ALA A . n 
A 1 684  VAL 684  684  684  VAL VAL A . n 
A 1 685  SER 685  685  685  SER SER A . n 
A 1 686  ALA 686  686  686  ALA ALA A . n 
A 1 687  GLU 687  687  687  GLU GLU A . n 
A 1 688  SER 688  688  688  SER SER A . n 
A 1 689  GLN 689  689  689  GLN GLN A . n 
A 1 690  ASP 690  690  690  ASP ASP A . n 
A 1 691  PHE 691  691  691  PHE PHE A . n 
A 1 692  ILE 692  692  692  ILE ILE A . n 
A 1 693  ALA 693  693  693  ALA ALA A . n 
A 1 694  HIS 694  694  694  HIS HIS A . n 
A 1 695  THR 695  695  695  THR THR A . n 
A 1 696  SER 696  696  696  SER SER A . n 
A 1 697  CYS 697  697  697  CYS CYS A . n 
A 1 698  GLN 698  698  698  GLN GLN A . n 
A 1 699  VAL 699  699  699  VAL VAL A . n 
A 1 700  LEU 700  700  700  LEU LEU A . n 
A 1 701  LEU 701  701  701  LEU LEU A . n 
A 1 702  THR 702  702  702  THR THR A . n 
A 1 703  ARG 703  703  703  ARG ARG A . n 
A 1 704  LEU 704  704  704  LEU LEU A . n 
A 1 705  TRP 705  705  705  TRP TRP A . n 
A 1 706  MET 706  706  706  MET MET A . n 
A 1 707  GLY 707  707  707  GLY GLY A . n 
A 1 708  THR 708  708  708  THR THR A . n 
A 1 709  MET 709  709  709  MET MET A . n 
A 1 710  ALA 710  710  710  ALA ALA A . n 
A 1 711  MET 711  711  711  MET MET A . n 
A 1 712  ASN 712  712  712  ASN ASN A . n 
A 1 713  THR 713  713  713  THR THR A . n 
A 1 714  ARG 714  714  714  ARG ARG A . n 
A 1 715  TRP 715  715  715  TRP TRP A . n 
A 1 716  TRP 716  716  716  TRP TRP A . n 
A 1 717  LYS 717  717  717  LYS LYS A . n 
A 1 718  VAL 718  718  718  VAL VAL A . n 
A 1 719  LEU 719  719  719  LEU LEU A . n 
A 1 720  VAL 720  720  720  VAL VAL A . n 
A 1 721  CYS 721  721  721  CYS CYS A . n 
A 1 722  LEU 722  722  722  LEU LEU A . n 
A 1 723  TYR 723  723  723  TYR TYR A . n 
A 1 724  LEU 724  724  724  LEU LEU A . n 
A 1 725  PRO 725  725  725  PRO PRO A . n 
A 1 726  VAL 726  726  726  VAL VAL A . n 
A 1 727  LEU 727  727  727  LEU LEU A . n 
A 1 728  ILE 728  728  728  ILE ILE A . n 
A 1 729  PHE 729  729  729  PHE PHE A . n 
A 1 730  PRO 730  730  730  PRO PRO A . n 
A 1 731  ILE 731  731  731  ILE ILE A . n 
A 1 732  ILE 732  732  732  ILE ILE A . n 
A 1 733  TYR 733  733  733  TYR TYR A . n 
A 1 734  PHE 734  734  734  PHE PHE A . n 
A 1 735  VAL 735  735  735  VAL VAL A . n 
A 1 736  PRO 736  736  736  PRO PRO A . n 
A 1 737  ASP 737  737  ?    ?   ?   A . n 
A 1 738  GLU 738  738  ?    ?   ?   A . n 
A 1 739  GLN 739  739  ?    ?   ?   A . n 
A 1 740  HIS 740  740  ?    ?   ?   A . n 
A 1 741  GLU 741  741  ?    ?   ?   A . n 
A 1 742  ARG 742  742  ?    ?   ?   A . n 
A 1 743  GLN 743  743  ?    ?   ?   A . n 
A 1 744  ALA 744  744  ?    ?   ?   A . n 
A 1 745  ALA 745  745  ?    ?   ?   A . n 
A 1 746  GLU 746  746  ?    ?   ?   A . n 
A 1 747  ARG 747  747  ?    ?   ?   A . n 
A 1 748  GLU 748  748  ?    ?   ?   A . n 
A 1 749  HIS 749  749  ?    ?   ?   A . n 
A 1 750  GLN 750  750  ?    ?   ?   A . n 
A 1 751  LYS 751  751  ?    ?   ?   A . n 
A 1 752  SER 752  752  ?    ?   ?   A . n 
A 1 753  LEU 753  753  ?    ?   ?   A . n 
A 1 754  ASN 754  754  ?    ?   ?   A . n 
A 1 755  GLN 755  755  ?    ?   ?   A . n 
A 1 756  LYS 756  756  ?    ?   ?   A . n 
A 1 757  SER 757  757  ?    ?   ?   A . n 
A 1 758  SER 758  758  ?    ?   ?   A . n 
A 1 759  LYS 759  759  ?    ?   ?   A . n 
A 1 760  VAL 760  760  ?    ?   ?   A . n 
A 1 761  LYS 761  761  ?    ?   ?   A . n 
A 1 762  SER 762  762  ?    ?   ?   A . n 
A 1 763  HIS 763  763  ?    ?   ?   A . n 
A 1 764  LYS 764  764  ?    ?   ?   A . n 
A 1 765  GLU 765  765  ?    ?   ?   A . n 
A 1 766  LYS 766  766  ?    ?   ?   A . n 
A 1 767  ASN 767  767  ?    ?   ?   A . n 
A 1 768  ASP 768  768  ?    ?   ?   A . n 
A 1 769  ALA 769  769  ?    ?   ?   A . n 
A 1 770  PRO 770  770  ?    ?   ?   A . n 
A 1 771  VAL 771  771  ?    ?   ?   A . n 
A 1 772  VAL 772  772  ?    ?   ?   A . n 
A 1 773  PRO 773  773  ?    ?   ?   A . n 
A 1 774  VAL 774  774  ?    ?   ?   A . n 
A 1 775  TYR 775  775  ?    ?   ?   A . n 
A 1 776  ARG 776  776  ?    ?   ?   A . n 
A 1 777  SER 777  777  ?    ?   ?   A . n 
A 1 778  LYS 778  778  ?    ?   ?   A . n 
A 1 779  GLU 779  779  ?    ?   ?   A . n 
A 1 780  GLU 780  780  ?    ?   ?   A . n 
A 1 781  LYS 781  781  ?    ?   ?   A . n 
A 1 782  ALA 782  782  ?    ?   ?   A . n 
A 1 783  VAL 783  783  ?    ?   ?   A . n 
A 1 784  SER 784  784  ?    ?   ?   A . n 
A 1 785  ASN 785  785  ?    ?   ?   A . n 
A 1 786  ASP 786  786  ?    ?   ?   A . n 
A 1 787  GLU 787  787  ?    ?   ?   A . n 
A 1 788  GLU 788  788  ?    ?   ?   A . n 
A 1 789  ALA 789  789  ?    ?   ?   A . n 
A 1 790  ARG 790  790  ?    ?   ?   A . n 
A 1 791  VAL 791  791  ?    ?   ?   A . n 
A 1 792  GLY 792  792  ?    ?   ?   A . n 
A 1 793  THR 793  793  ?    ?   ?   A . n 
A 1 794  GLU 794  794  ?    ?   ?   A . n 
A 1 795  ASN 795  795  ?    ?   ?   A . n 
A 1 796  GLU 796  796  ?    ?   ?   A . n 
A 1 797  GLU 797  797  ?    ?   ?   A . n 
A 1 798  GLU 798  798  ?    ?   ?   A . n 
A 1 799  ASP 799  799  ?    ?   ?   A . n 
A 1 800  PHE 800  800  ?    ?   ?   A . n 
A 1 801  GLN 801  801  ?    ?   ?   A . n 
A 1 802  LEU 802  802  ?    ?   ?   A . n 
A 1 803  GLU 803  803  ?    ?   ?   A . n 
A 1 804  ASP 804  804  ?    ?   ?   A . n 
A 1 805  TYR 805  805  ?    ?   ?   A . n 
A 1 806  ILE 806  806  ?    ?   ?   A . n 
A 1 807  PRO 807  807  ?    ?   ?   A . n 
A 1 808  GLU 808  808  ?    ?   ?   A . n 
A 1 809  ILE 809  809  ?    ?   ?   A . n 
A 1 810  ARG 810  810  ?    ?   ?   A . n 
A 1 811  GLU 811  811  ?    ?   ?   A . n 
A 1 812  ASP 812  812  ?    ?   ?   A . n 
A 1 813  ASP 813  813  ?    ?   ?   A . n 
A 1 814  SER 814  814  ?    ?   ?   A . n 
A 1 815  MET 815  815  ?    ?   ?   A . n 
A 1 816  GLU 816  816  ?    ?   ?   A . n 
A 1 817  VAL 817  817  ?    ?   ?   A . n 
A 1 818  ILE 818  818  ?    ?   ?   A . n 
A 1 819  MET 819  819  ?    ?   ?   A . n 
A 1 820  ARG 820  820  ?    ?   ?   A . n 
A 1 821  ASN 821  821  ?    ?   ?   A . n 
A 1 822  LYS 822  822  ?    ?   ?   A . n 
A 1 823  LYS 823  823  ?    ?   ?   A . n 
A 1 824  LEU 824  824  ?    ?   ?   A . n 
A 1 825  GLY 825  825  ?    ?   ?   A . n 
A 1 826  PHE 826  826  826  PHE PHE A . n 
A 1 827  CYS 827  827  827  CYS CYS A . n 
A 1 828  ASP 828  828  828  ASP ASP A . n 
A 1 829  ARG 829  829  829  ARG ARG A . n 
A 1 830  ILE 830  830  830  ILE ILE A . n 
A 1 831  MET 831  831  831  MET MET A . n 
A 1 832  HIS 832  832  832  HIS HIS A . n 
A 1 833  PHE 833  833  833  PHE PHE A . n 
A 1 834  TYR 834  834  834  TYR TYR A . n 
A 1 835  SER 835  835  835  SER SER A . n 
A 1 836  ALA 836  836  836  ALA ALA A . n 
A 1 837  PRO 837  837  837  PRO PRO A . n 
A 1 838  PHE 838  838  838  PHE PHE A . n 
A 1 839  SER 839  839  839  SER SER A . n 
A 1 840  LYS 840  840  840  LYS LYS A . n 
A 1 841  PHE 841  841  841  PHE PHE A . n 
A 1 842  VAL 842  842  842  VAL VAL A . n 
A 1 843  GLY 843  843  843  GLY GLY A . n 
A 1 844  ASN 844  844  844  ASN ASN A . n 
A 1 845  VAL 845  845  845  VAL VAL A . n 
A 1 846  VAL 846  846  846  VAL VAL A . n 
A 1 847  GLY 847  847  847  GLY GLY A . n 
A 1 848  TYR 848  848  848  TYR TYR A . n 
A 1 849  LEU 849  849  849  LEU LEU A . n 
A 1 850  ALA 850  850  850  ALA ALA A . n 
A 1 851  PHE 851  851  851  PHE PHE A . n 
A 1 852  ILE 852  852  852  ILE ILE A . n 
A 1 853  PHE 853  853  853  PHE PHE A . n 
A 1 854  LEU 854  854  854  LEU LEU A . n 
A 1 855  TYR 855  855  855  TYR TYR A . n 
A 1 856  ALA 856  856  856  ALA ALA A . n 
A 1 857  TYR 857  857  857  TYR TYR A . n 
A 1 858  VAL 858  858  858  VAL VAL A . n 
A 1 859  VAL 859  859  859  VAL VAL A . n 
A 1 860  LEU 860  860  860  LEU LEU A . n 
A 1 861  PHE 861  861  861  PHE PHE A . n 
A 1 862  ASN 862  862  862  ASN ASN A . n 
A 1 863  PHE 863  863  863  PHE PHE A . n 
A 1 864  PRO 864  864  864  PRO PRO A . n 
A 1 865  ARG 865  865  865  ARG ARG A . n 
A 1 866  PHE 866  866  866  PHE PHE A . n 
A 1 867  ASP 867  867  867  ASP ASP A . n 
A 1 868  PRO 868  868  868  PRO PRO A . n 
A 1 869  ALA 869  869  869  ALA ALA A . n 
A 1 870  LYS 870  870  870  LYS LYS A . n 
A 1 871  THR 871  871  871  THR THR A . n 
A 1 872  LEU 872  872  872  LEU LEU A . n 
A 1 873  GLY 873  873  873  GLY GLY A . n 
A 1 874  GLY 874  874  874  GLY GLY A . n 
A 1 875  ILE 875  875  875  ILE ILE A . n 
A 1 876  HIS 876  876  876  HIS HIS A . n 
A 1 877  PRO 877  877  877  PRO PRO A . n 
A 1 878  THR 878  878  878  THR THR A . n 
A 1 879  GLU 879  879  879  GLU GLU A . n 
A 1 880  ILE 880  880  880  ILE ILE A . n 
A 1 881  VAL 881  881  881  VAL VAL A . n 
A 1 882  LEU 882  882  882  LEU LEU A . n 
A 1 883  TYR 883  883  883  TYR TYR A . n 
A 1 884  PHE 884  884  884  PHE PHE A . n 
A 1 885  TRP 885  885  885  TRP TRP A . n 
A 1 886  VAL 886  886  886  VAL VAL A . n 
A 1 887  PHE 887  887  887  PHE PHE A . n 
A 1 888  THR 888  888  888  THR THR A . n 
A 1 889  ILE 889  889  889  ILE ILE A . n 
A 1 890  LEU 890  890  890  LEU LEU A . n 
A 1 891  ILE 891  891  891  ILE ILE A . n 
A 1 892  GLU 892  892  892  GLU GLU A . n 
A 1 893  GLU 893  893  893  GLU GLU A . n 
A 1 894  ILE 894  894  894  ILE ILE A . n 
A 1 895  ARG 895  895  895  ARG ARG A . n 
A 1 896  GLN 896  896  896  GLN GLN A . n 
A 1 897  LEU 897  897  897  LEU LEU A . n 
A 1 898  ALA 898  898  898  ALA ALA A . n 
A 1 899  ALA 899  899  899  ALA ALA A . n 
A 1 900  LYS 900  900  900  LYS LYS A . n 
A 1 901  PRO 901  901  901  PRO PRO A . n 
A 1 902  PRO 902  902  902  PRO PRO A . n 
A 1 903  LYS 903  903  903  LYS LYS A . n 
A 1 904  TYR 904  904  904  TYR TYR A . n 
A 1 905  ILE 905  905  905  ILE ILE A . n 
A 1 906  LYS 906  906  906  LYS LYS A . n 
A 1 907  ASP 907  907  907  ASP ASP A . n 
A 1 908  LYS 908  908  908  LYS LYS A . n 
A 1 909  VAL 909  909  909  VAL VAL A . n 
A 1 910  SER 910  910  910  SER SER A . n 
A 1 911  VAL 911  911  911  VAL VAL A . n 
A 1 912  TYR 912  912  912  TYR TYR A . n 
A 1 913  PHE 913  913  913  PHE PHE A . n 
A 1 914  SER 914  914  914  SER SER A . n 
A 1 915  ASP 915  915  915  ASP ASP A . n 
A 1 916  THR 916  916  916  THR THR A . n 
A 1 917  TRP 917  917  917  TRP TRP A . n 
A 1 918  ASN 918  918  918  ASN ASN A . n 
A 1 919  PHE 919  919  919  PHE PHE A . n 
A 1 920  VAL 920  920  920  VAL VAL A . n 
A 1 921  ASP 921  921  921  ASP ASP A . n 
A 1 922  ILE 922  922  922  ILE ILE A . n 
A 1 923  PHE 923  923  923  PHE PHE A . n 
A 1 924  SER 924  924  924  SER SER A . n 
A 1 925  LEU 925  925  925  LEU LEU A . n 
A 1 926  THR 926  926  926  THR THR A . n 
A 1 927  VAL 927  927  927  VAL VAL A . n 
A 1 928  PHE 928  928  928  PHE PHE A . n 
A 1 929  ILE 929  929  929  ILE ILE A . n 
A 1 930  ILE 930  930  930  ILE ILE A . n 
A 1 931  ALA 931  931  931  ALA ALA A . n 
A 1 932  ILE 932  932  932  ILE ILE A . n 
A 1 933  ILE 933  933  933  ILE ILE A . n 
A 1 934  LEU 934  934  934  LEU LEU A . n 
A 1 935  ARG 935  935  935  ARG ARG A . n 
A 1 936  PHE 936  936  936  PHE PHE A . n 
A 1 937  PHE 937  937  937  PHE PHE A . n 
A 1 938  THR 938  938  938  THR THR A . n 
A 1 939  ASN 939  939  939  ASN ASN A . n 
A 1 940  SER 940  940  940  SER SER A . n 
A 1 941  ARG 941  941  941  ARG ARG A . n 
A 1 942  ILE 942  942  942  ILE ILE A . n 
A 1 943  PHE 943  943  943  PHE PHE A . n 
A 1 944  THR 944  944  944  THR THR A . n 
A 1 945  ALA 945  945  945  ALA ALA A . n 
A 1 946  SER 946  946  946  SER SER A . n 
A 1 947  ARG 947  947  947  ARG ARG A . n 
A 1 948  ILE 948  948  948  ILE ILE A . n 
A 1 949  ILE 949  949  949  ILE ILE A . n 
A 1 950  LEU 950  950  950  LEU LEU A . n 
A 1 951  SER 951  951  951  SER SER A . n 
A 1 952  LEU 952  952  952  LEU LEU A . n 
A 1 953  ASP 953  953  953  ASP ASP A . n 
A 1 954  ILE 954  954  954  ILE ILE A . n 
A 1 955  ILE 955  955  955  ILE ILE A . n 
A 1 956  PHE 956  956  956  PHE PHE A . n 
A 1 957  PHE 957  957  957  PHE PHE A . n 
A 1 958  ILE 958  958  958  ILE ILE A . n 
A 1 959  VAL 959  959  959  VAL VAL A . n 
A 1 960  ARG 960  960  960  ARG ARG A . n 
A 1 961  SER 961  961  961  SER SER A . n 
A 1 962  LEU 962  962  962  LEU LEU A . n 
A 1 963  GLN 963  963  963  GLN GLN A . n 
A 1 964  ILE 964  964  964  ILE ILE A . n 
A 1 965  PHE 965  965  965  PHE PHE A . n 
A 1 966  SER 966  966  966  SER SER A . n 
A 1 967  VAL 967  967  967  VAL VAL A . n 
A 1 968  ASN 968  968  968  ASN ASN A . n 
A 1 969  ARG 969  969  969  ARG ARG A . n 
A 1 970  LEU 970  970  970  LEU LEU A . n 
A 1 971  LEU 971  971  971  LEU LEU A . n 
A 1 972  GLY 972  972  972  GLY GLY A . n 
A 1 973  PRO 973  973  973  PRO PRO A . n 
A 1 974  LYS 974  974  974  LYS LYS A . n 
A 1 975  LEU 975  975  975  LEU LEU A . n 
A 1 976  VAL 976  976  976  VAL VAL A . n 
A 1 977  MET 977  977  977  MET MET A . n 
A 1 978  ILE 978  978  978  ILE ILE A . n 
A 1 979  GLN 979  979  979  GLN GLN A . n 
A 1 980  LYS 980  980  980  LYS LYS A . n 
A 1 981  MET 981  981  981  MET MET A . n 
A 1 982  MET 982  982  982  MET MET A . n 
A 1 983  GLN 983  983  983  GLN GLN A . n 
A 1 984  ASP 984  984  984  ASP ASP A . n 
A 1 985  LEU 985  985  985  LEU LEU A . n 
A 1 986  ALA 986  986  986  ALA ALA A . n 
A 1 987  GLN 987  987  987  GLN GLN A . n 
A 1 988  PHE 988  988  988  PHE PHE A . n 
A 1 989  ILE 989  989  989  ILE ILE A . n 
A 1 990  ILE 990  990  990  ILE ILE A . n 
A 1 991  ILE 991  991  991  ILE ILE A . n 
A 1 992  LEU 992  992  992  LEU LEU A . n 
A 1 993  ALA 993  993  993  ALA ALA A . n 
A 1 994  VAL 994  994  994  VAL VAL A . n 
A 1 995  PHE 995  995  995  PHE PHE A . n 
A 1 996  THR 996  996  996  THR THR A . n 
A 1 997  ILE 997  997  997  ILE ILE A . n 
A 1 998  ALA 998  998  998  ALA ALA A . n 
A 1 999  TYR 999  999  999  TYR TYR A . n 
A 1 1000 GLY 1000 1000 1000 GLY GLY A . n 
A 1 1001 ILE 1001 1001 1001 ILE ILE A . n 
A 1 1002 ALA 1002 1002 1002 ALA ALA A . n 
A 1 1003 LEU 1003 1003 1003 LEU LEU A . n 
A 1 1004 HIS 1004 1004 1004 HIS HIS A . n 
A 1 1005 ALA 1005 1005 1005 ALA ALA A . n 
A 1 1006 VAL 1006 1006 1006 VAL VAL A . n 
A 1 1007 MET 1007 1007 1007 MET MET A . n 
A 1 1008 PHE 1008 1008 1008 PHE PHE A . n 
A 1 1009 PRO 1009 1009 1009 PRO PRO A . n 
A 1 1010 SER 1010 1010 1010 SER SER A . n 
A 1 1011 PRO 1011 1011 1011 PRO PRO A . n 
A 1 1012 GLY 1012 1012 1012 GLY GLY A . n 
A 1 1013 ILE 1013 1013 1013 ILE ILE A . n 
A 1 1014 TYR 1014 1014 1014 TYR TYR A . n 
A 1 1015 ALA 1015 1015 1015 ALA ALA A . n 
A 1 1016 ARG 1016 1016 1016 ARG ARG A . n 
A 1 1017 ASN 1017 1017 1017 ASN ASN A . n 
A 1 1018 ASN 1018 1018 1018 ASN ASN A . n 
A 1 1019 THR 1019 1019 1019 THR THR A . n 
A 1 1020 TRP 1020 1020 1020 TRP TRP A . n 
A 1 1021 VAL 1021 1021 1021 VAL VAL A . n 
A 1 1022 THR 1022 1022 1022 THR THR A . n 
A 1 1023 ILE 1023 1023 1023 ILE ILE A . n 
A 1 1024 THR 1024 1024 1024 THR THR A . n 
A 1 1025 SER 1025 1025 1025 SER SER A . n 
A 1 1026 VAL 1026 1026 1026 VAL VAL A . n 
A 1 1027 VAL 1027 1027 1027 VAL VAL A . n 
A 1 1028 GLN 1028 1028 1028 GLN GLN A . n 
A 1 1029 TYR 1029 1029 1029 TYR TYR A . n 
A 1 1030 PRO 1030 1030 1030 PRO PRO A . n 
A 1 1031 TYR 1031 1031 1031 TYR TYR A . n 
A 1 1032 TRP 1032 1032 1032 TRP TRP A . n 
A 1 1033 GLN 1033 1033 1033 GLN GLN A . n 
A 1 1034 MET 1034 1034 1034 MET MET A . n 
A 1 1035 TYR 1035 1035 1035 TYR TYR A . n 
A 1 1036 GLY 1036 1036 1036 GLY GLY A . n 
A 1 1037 GLU 1037 1037 1037 GLU GLU A . n 
A 1 1038 LEU 1038 1038 1038 LEU LEU A . n 
A 1 1039 PHE 1039 1039 1039 PHE PHE A . n 
A 1 1040 LEU 1040 1040 1040 LEU LEU A . n 
A 1 1041 ASP 1041 1041 1041 ASP ASP A . n 
A 1 1042 GLU 1042 1042 1042 GLU GLU A . n 
A 1 1043 ILE 1043 1043 1043 ILE ILE A . n 
A 1 1044 GLN 1044 1044 1044 GLN GLN A . n 
A 1 1045 GLY 1045 1045 1045 GLY GLY A . n 
A 1 1046 GLU 1046 1046 1046 GLU GLU A . n 
A 1 1047 LYS 1047 1047 1047 LYS LYS A . n 
A 1 1048 PRO 1048 1048 1048 PRO PRO A . n 
A 1 1049 LYS 1049 1049 1049 LYS LYS A . n 
A 1 1050 GLU 1050 1050 1050 GLU GLU A . n 
A 1 1051 PHE 1051 1051 1051 PHE PHE A . n 
A 1 1052 GLY 1052 1052 1052 GLY GLY A . n 
A 1 1053 GLU 1053 1053 1053 GLU GLU A . n 
A 1 1054 VAL 1054 1054 1054 VAL VAL A . n 
A 1 1055 ASP 1055 1055 1055 ASP ASP A . n 
A 1 1056 PRO 1056 1056 1056 PRO PRO A . n 
A 1 1057 ASP 1057 1057 1057 ASP ASP A . n 
A 1 1058 GLY 1058 1058 1058 GLY GLY A . n 
A 1 1059 ARG 1059 1059 1059 ARG ARG A . n 
A 1 1060 TRP 1060 1060 1060 TRP TRP A . n 
A 1 1061 LEU 1061 1061 1061 LEU LEU A . n 
A 1 1062 SER 1062 1062 1062 SER SER A . n 
A 1 1063 PRO 1063 1063 1063 PRO PRO A . n 
A 1 1064 LEU 1064 1064 1064 LEU LEU A . n 
A 1 1065 LEU 1065 1065 1065 LEU LEU A . n 
A 1 1066 LEU 1066 1066 1066 LEU LEU A . n 
A 1 1067 ALA 1067 1067 1067 ALA ALA A . n 
A 1 1068 ILE 1068 1068 1068 ILE ILE A . n 
A 1 1069 TYR 1069 1069 1069 TYR TYR A . n 
A 1 1070 MET 1070 1070 1070 MET MET A . n 
A 1 1071 VAL 1071 1071 1071 VAL VAL A . n 
A 1 1072 PHE 1072 1072 1072 PHE PHE A . n 
A 1 1073 THR 1073 1073 1073 THR THR A . n 
A 1 1074 ASN 1074 1074 1074 ASN ASN A . n 
A 1 1075 ILE 1075 1075 1075 ILE ILE A . n 
A 1 1076 LEU 1076 1076 1076 LEU LEU A . n 
A 1 1077 LEU 1077 1077 1077 LEU LEU A . n 
A 1 1078 LEU 1078 1078 1078 LEU LEU A . n 
A 1 1079 ASN 1079 1079 1079 ASN ASN A . n 
A 1 1080 LEU 1080 1080 1080 LEU LEU A . n 
A 1 1081 LEU 1081 1081 1081 LEU LEU A . n 
A 1 1082 ILE 1082 1082 1082 ILE ILE A . n 
A 1 1083 ALA 1083 1083 1083 ALA ALA A . n 
A 1 1084 ILE 1084 1084 1084 ILE ILE A . n 
A 1 1085 PHE 1085 1085 1085 PHE PHE A . n 
A 1 1086 ASN 1086 1086 1086 ASN ASN A . n 
A 1 1087 TYR 1087 1087 1087 TYR TYR A . n 
A 1 1088 THR 1088 1088 1088 THR THR A . n 
A 1 1089 PHE 1089 1089 1089 PHE PHE A . n 
A 1 1090 GLU 1090 1090 1090 GLU GLU A . n 
A 1 1091 ARG 1091 1091 1091 ARG ARG A . n 
A 1 1092 VAL 1092 1092 1092 VAL VAL A . n 
A 1 1093 GLN 1093 1093 1093 GLN GLN A . n 
A 1 1094 GLU 1094 1094 1094 GLU GLU A . n 
A 1 1095 ASP 1095 1095 1095 ASP ASP A . n 
A 1 1096 SER 1096 1096 1096 SER SER A . n 
A 1 1097 ASP 1097 1097 1097 ASP ASP A . n 
A 1 1098 LYS 1098 1098 1098 LYS LYS A . n 
A 1 1099 VAL 1099 1099 1099 VAL VAL A . n 
A 1 1100 TRP 1100 1100 1100 TRP TRP A . n 
A 1 1101 LYS 1101 1101 1101 LYS LYS A . n 
A 1 1102 PHE 1102 1102 1102 PHE PHE A . n 
A 1 1103 GLN 1103 1103 1103 GLN GLN A . n 
A 1 1104 ARG 1104 1104 1104 ARG ARG A . n 
A 1 1105 TYR 1105 1105 1105 TYR TYR A . n 
A 1 1106 ASP 1106 1106 1106 ASP ASP A . n 
A 1 1107 LEU 1107 1107 1107 LEU LEU A . n 
A 1 1108 VAL 1108 1108 1108 VAL VAL A . n 
A 1 1109 GLN 1109 1109 1109 GLN GLN A . n 
A 1 1110 GLU 1110 1110 1110 GLU GLU A . n 
A 1 1111 TYR 1111 1111 1111 TYR TYR A . n 
A 1 1112 HIS 1112 1112 1112 HIS HIS A . n 
A 1 1113 SER 1113 1113 1113 SER SER A . n 
A 1 1114 ARG 1114 1114 1114 ARG ARG A . n 
A 1 1115 PRO 1115 1115 1115 PRO PRO A . n 
A 1 1116 VAL 1116 1116 1116 VAL VAL A . n 
A 1 1117 PHE 1117 1117 1117 PHE PHE A . n 
A 1 1118 ALA 1118 1118 1118 ALA ALA A . n 
A 1 1119 PRO 1119 1119 1119 PRO PRO A . n 
A 1 1120 PRO 1120 1120 1120 PRO PRO A . n 
A 1 1121 LEU 1121 1121 1121 LEU LEU A . n 
A 1 1122 VAL 1122 1122 1122 VAL VAL A . n 
A 1 1123 LEU 1123 1123 1123 LEU LEU A . n 
A 1 1124 LEU 1124 1124 1124 LEU LEU A . n 
A 1 1125 GLY 1125 1125 1125 GLY GLY A . n 
A 1 1126 HIS 1126 1126 1126 HIS HIS A . n 
A 1 1127 ILE 1127 1127 1127 ILE ILE A . n 
A 1 1128 LEU 1128 1128 1128 LEU LEU A . n 
A 1 1129 ILE 1129 1129 1129 ILE ILE A . n 
A 1 1130 PHE 1130 1130 1130 PHE PHE A . n 
A 1 1131 ILE 1131 1131 1131 ILE ILE A . n 
A 1 1132 ARG 1132 1132 ?    ?   ?   A . n 
A 1 1133 TRP 1133 1133 ?    ?   ?   A . n 
A 1 1134 VAL 1134 1134 ?    ?   ?   A . n 
A 1 1135 TRP 1135 1135 ?    ?   ?   A . n 
A 1 1136 ARG 1136 1136 ?    ?   ?   A . n 
A 1 1137 MET 1137 1137 ?    ?   ?   A . n 
A 1 1138 CYS 1138 1138 ?    ?   ?   A . n 
A 1 1139 ARG 1139 1139 ?    ?   ?   A . n 
A 1 1140 CYS 1140 1140 ?    ?   ?   A . n 
A 1 1141 GLY 1141 1141 ?    ?   ?   A . n 
A 1 1142 HIS 1142 1142 ?    ?   ?   A . n 
A 1 1143 PRO 1143 1143 ?    ?   ?   A . n 
A 1 1144 PRO 1144 1144 ?    ?   ?   A . n 
A 1 1145 ARG 1145 1145 ?    ?   ?   A . n 
A 1 1146 GLY 1146 1146 ?    ?   ?   A . n 
A 1 1147 SER 1147 1147 ?    ?   ?   A . n 
A 1 1148 THR 1148 1148 ?    ?   ?   A . n 
A 1 1149 MET 1149 1149 ?    ?   ?   A . n 
A 1 1150 LYS 1150 1150 1150 LYS LYS A . n 
A 1 1151 ILE 1151 1151 1151 ILE ILE A . n 
A 1 1152 GLY 1152 1152 1152 GLY GLY A . n 
A 1 1153 LEU 1153 1153 1153 LEU LEU A . n 
A 1 1154 SER 1154 1154 1154 SER SER A . n 
A 1 1155 PRO 1155 1155 1155 PRO PRO A . n 
A 1 1156 ALA 1156 1156 1156 ALA ALA A . n 
A 1 1157 GLU 1157 1157 1157 GLU GLU A . n 
A 1 1158 MET 1158 1158 1158 MET MET A . n 
A 1 1159 GLU 1159 1159 1159 GLU GLU A . n 
A 1 1160 GLN 1160 1160 1160 GLN GLN A . n 
A 1 1161 MET 1161 1161 1161 MET MET A . n 
A 1 1162 ASP 1162 1162 1162 ASP ASP A . n 
A 1 1163 ASN 1163 1163 1163 ASN ASN A . n 
A 1 1164 TRP 1164 1164 1164 TRP TRP A . n 
A 1 1165 GLU 1165 1165 1165 GLU GLU A . n 
A 1 1166 PHE 1166 1166 1166 PHE PHE A . n 
A 1 1167 GLN 1167 1167 1167 GLN GLN A . n 
A 1 1168 ALA 1168 1168 1168 ALA ALA A . n 
A 1 1169 ALA 1169 1169 1169 ALA ALA A . n 
A 1 1170 GLU 1170 1170 1170 GLU GLU A . n 
A 1 1171 MET 1171 1171 1171 MET MET A . n 
A 1 1172 TYR 1172 1172 1172 TYR TYR A . n 
A 1 1173 ILE 1173 1173 1173 ILE ILE A . n 
A 1 1174 HIS 1174 1174 1174 HIS HIS A . n 
A 1 1175 GLN 1175 1175 1175 GLN GLN A . n 
A 1 1176 GLN 1176 1176 1176 GLN GLN A . n 
A 1 1177 GLN 1177 1177 1177 GLN GLN A . n 
A 1 1178 GLN 1178 1178 1178 GLN GLN A . n 
A 1 1179 LYS 1179 1179 1179 LYS LYS A . n 
A 1 1180 ASN 1180 1180 1180 ASN ASN A . n 
A 1 1181 SER 1181 1181 1181 SER SER A . n 
A 1 1182 GLY 1182 1182 1182 GLY GLY A . n 
A 1 1183 THR 1183 1183 1183 THR THR A . n 
A 1 1184 LEU 1184 1184 1184 LEU LEU A . n 
A 1 1185 GLU 1185 1185 1185 GLU GLU A . n 
A 1 1186 GLU 1186 1186 1186 GLU GLU A . n 
A 1 1187 ARG 1187 1187 1187 ARG ARG A . n 
A 1 1188 VAL 1188 1188 1188 VAL VAL A . n 
A 1 1189 ARG 1189 1189 1189 ARG ARG A . n 
A 1 1190 ALA 1190 1190 1190 ALA ALA A . n 
A 1 1191 LEU 1191 1191 1191 LEU LEU A . n 
A 1 1192 GLY 1192 1192 1192 GLY GLY A . n 
A 1 1193 ASP 1193 1193 1193 ASP ASP A . n 
A 1 1194 ARG 1194 1194 1194 ARG ARG A . n 
A 1 1195 VAL 1195 1195 1195 VAL VAL A . n 
A 1 1196 ASP 1196 1196 1196 ASP ASP A . n 
A 1 1197 CYS 1197 1197 1197 CYS CYS A . n 
A 1 1198 ILE 1198 1198 1198 ILE ILE A . n 
A 1 1199 ASN 1199 1199 1199 ASN ASN A . n 
A 1 1200 SER 1200 1200 1200 SER SER A . n 
A 1 1201 GLN 1201 1201 1201 GLN GLN A . n 
A 1 1202 LEU 1202 1202 1202 LEU LEU A . n 
A 1 1203 ASN 1203 1203 1203 ASN ASN A . n 
A 1 1204 ARG 1204 1204 1204 ARG ARG A . n 
A 1 1205 VAL 1205 1205 1205 VAL VAL A . n 
A 1 1206 LEU 1206 1206 1206 LEU LEU A . n 
A 1 1207 ASP 1207 1207 ?    ?   ?   A . n 
A 1 1208 SER 1208 1208 ?    ?   ?   A . n 
A 1 1209 MET 1209 1209 ?    ?   ?   A . n 
A 1 1210 SER 1210 1210 ?    ?   ?   A . n 
A 1 1211 GLY 1211 1211 ?    ?   ?   A . n 
A 1 1212 THR 1212 1212 ?    ?   ?   A . n 
A 1 1213 ARG 1213 1213 ?    ?   ?   A . n 
A 1 1214 ALA 1214 1214 ?    ?   ?   A . n 
A 1 1215 HIS 1215 1215 ?    ?   ?   A . n 
A 1 1216 ALA 1216 1216 ?    ?   ?   A . n 
A 1 1217 LEU 1217 1217 ?    ?   ?   A . n 
A 1 1218 THR 1218 1218 ?    ?   ?   A . n 
A 1 1219 ASP 1219 1219 ?    ?   ?   A . n 
A 1 1220 GLY 1220 1220 ?    ?   ?   A . n 
A 1 1221 ASN 1221 1221 ?    ?   ?   A . n 
A 1 1222 GLY 1222 1222 ?    ?   ?   A . n 
A 1 1223 LEU 1223 1223 ?    ?   ?   A . n 
A 1 1224 GLU 1224 1224 ?    ?   ?   A . n 
A 1 1225 GLY 1225 1225 ?    ?   ?   A . n 
A 1 1226 GLY 1226 1226 ?    ?   ?   A . n 
A 1 1227 HIS 1227 1227 ?    ?   ?   A . n 
A 1 1228 ASP 1228 1228 ?    ?   ?   A . n 
A 1 1229 SER 1229 1229 ?    ?   ?   A . n 
A 1 1230 GLU 1230 1230 ?    ?   ?   A . n 
A 1 1231 GLY 1231 1231 ?    ?   ?   A . n 
A 1 1232 ARG 1232 1232 ?    ?   ?   A . n 
A 1 1233 LEU 1233 1233 ?    ?   ?   A . n 
A 1 1234 ALA 1234 1234 ?    ?   ?   A . n 
A 1 1235 ARG 1235 1235 ?    ?   ?   A . n 
A 1 1236 MET 1236 1236 ?    ?   ?   A . n 
A 1 1237 GLU 1237 1237 ?    ?   ?   A . n 
A 1 1238 VAL 1238 1238 ?    ?   ?   A . n 
A 1 1239 GLU 1239 1239 ?    ?   ?   A . n 
A 1 1240 LEU 1240 1240 ?    ?   ?   A . n 
A 1 1241 SER 1241 1241 ?    ?   ?   A . n 
A 1 1242 SER 1242 1242 ?    ?   ?   A . n 
A 1 1243 ASN 1243 1243 ?    ?   ?   A . n 
A 1 1244 SER 1244 1244 ?    ?   ?   A . n 
A 1 1245 GLU 1245 1245 ?    ?   ?   A . n 
A 1 1246 SER 1246 1246 ?    ?   ?   A . n 
A 1 1247 LEU 1247 1247 ?    ?   ?   A . n 
A 1 1248 GLN 1248 1248 ?    ?   ?   A . n 
A 1 1249 LYS 1249 1249 ?    ?   ?   A . n 
A 1 1250 ILE 1250 1250 ?    ?   ?   A . n 
A 1 1251 LEU 1251 1251 ?    ?   ?   A . n 
A 1 1252 ALA 1252 1252 ?    ?   ?   A . n 
A 1 1253 LEU 1253 1253 ?    ?   ?   A . n 
A 1 1254 LEU 1254 1254 ?    ?   ?   A . n 
A 1 1255 GLN 1255 1255 ?    ?   ?   A . n 
A 1 1256 GLN 1256 1256 ?    ?   ?   A . n 
A 1 1257 GLN 1257 1257 ?    ?   ?   A . n 
A 1 1258 PRO 1258 1258 ?    ?   ?   A . n 
A 1 1259 PRO 1259 1259 ?    ?   ?   A . n 
A 1 1260 VAL 1260 1260 ?    ?   ?   A . n 
A 1 1261 LYS 1261 1261 ?    ?   ?   A . n 
A 1 1262 GLY 1262 1262 ?    ?   ?   A . n 
A 1 1263 GLN 1263 1263 ?    ?   ?   A . n 
A 1 1264 ALA 1264 1264 ?    ?   ?   A . n 
A 1 1265 ALA 1265 1265 ?    ?   ?   A . n 
A 1 1266 VAL 1266 1266 ?    ?   ?   A . n 
A 1 1267 PRO 1267 1267 ?    ?   ?   A . n 
A 1 1268 ILE 1268 1268 ?    ?   ?   A . n 
A 1 1269 GLN 1269 1269 ?    ?   ?   A . n 
A 1 1270 LEU 1270 1270 ?    ?   ?   A . n 
A 1 1271 THR 1271 1271 ?    ?   ?   A . n 
A 1 1272 LEU 1272 1272 ?    ?   ?   A . n 
A 1 1273 LEU 1273 1273 ?    ?   ?   A . n 
A 1 1274 HIS 1274 1274 ?    ?   ?   A . n 
A 1 1275 TYR 1275 1275 ?    ?   ?   A . n 
A 1 1276 LYS 1276 1276 ?    ?   ?   A . n 
A 1 1277 ALA 1277 1277 ?    ?   ?   A . n 
A 1 1278 ARG 1278 1278 ?    ?   ?   A . n 
A 1 1279 SER 1279 1279 ?    ?   ?   A . n 
A 1 1280 SER 1280 1280 ?    ?   ?   A . n 
A 1 1281 PRO 1281 1281 ?    ?   ?   A . n 
A 1 1282 TYR 1282 1282 ?    ?   ?   A . n 
A 1 1283 PRO 1283 1283 ?    ?   ?   A . n 
A 1 1284 GLY 1284 1284 ?    ?   ?   A . n 
A 1 1285 SER 1285 1285 ?    ?   ?   A . n 
A 1 1286 THR 1286 1286 ?    ?   ?   A . n 
A 1 1287 ALA 1287 1287 ?    ?   ?   A . n 
A 1 1288 LYS 1288 1288 ?    ?   ?   A . n 
A 1 1289 ARG 1289 1289 ?    ?   ?   A . n 
A 1 1290 PHE 1290 1290 ?    ?   ?   A . n 
A 1 1291 ALA 1291 1291 ?    ?   ?   A . n 
A 1 1292 VAL 1292 1292 ?    ?   ?   A . n 
A 1 1293 GLN 1293 1293 ?    ?   ?   A . n 
A 1 1294 ASP 1294 1294 ?    ?   ?   A . n 
A 1 1295 ASN 1295 1295 ?    ?   ?   A . n 
A 1 1296 MET 1296 1296 ?    ?   ?   A . n 
A 1 1297 VAL 1297 1297 ?    ?   ?   A . n 
A 1 1298 ASP 1298 1298 ?    ?   ?   A . n 
A 1 1299 TRP 1299 1299 ?    ?   ?   A . n 
A 1 1300 GLN 1300 1300 ?    ?   ?   A . n 
A 1 1301 VAL 1301 1301 ?    ?   ?   A . n 
A 1 1302 PRO 1302 1302 ?    ?   ?   A . n 
A 1 1303 PHE 1303 1303 ?    ?   ?   A . n 
A 1 1304 PRO 1304 1304 ?    ?   ?   A . n 
A 1 1305 ASP 1305 1305 ?    ?   ?   A . n 
A 1 1306 TYR 1306 1306 ?    ?   ?   A . n 
A 1 1307 LYS 1307 1307 ?    ?   ?   A . n 
A 1 1308 PRO 1308 1308 ?    ?   ?   A . n 
A 1 1309 VAL 1309 1309 ?    ?   ?   A . n 
A 1 1310 ASN 1310 1310 ?    ?   ?   A . n 
A 1 1311 TYR 1311 1311 ?    ?   ?   A . n 
A 1 1312 THR 1312 1312 ?    ?   ?   A . n 
A 1 1313 ALA 1313 1313 ?    ?   ?   A . n 
A 1 1314 PRO 1314 1314 ?    ?   ?   A . n 
A 1 1315 VAL 1315 1315 ?    ?   ?   A . n 
A 1 1316 VAL 1316 1316 ?    ?   ?   A . n 
A 1 1317 LEU 1317 1317 ?    ?   ?   A . n 
A 1 1318 ALA 1318 1318 ?    ?   ?   A . n 
A 1 1319 ASN 1319 1319 ?    ?   ?   A . n 
A 1 1320 PRO 1320 1320 ?    ?   ?   A . n 
A 1 1321 VAL 1321 1321 ?    ?   ?   A . n 
A 1 1322 TRP 1322 1322 ?    ?   ?   A . n 
A 1 1323 ALA 1323 1323 ?    ?   ?   A . n 
A 1 1324 ASP 1324 1324 ?    ?   ?   A . n 
A 1 1325 LYS 1325 1325 ?    ?   ?   A . n 
A 1 1326 ASP 1326 1326 ?    ?   ?   A . n 
A 1 1327 LEU 1327 1327 ?    ?   ?   A . n 
A 1 1328 MET 1328 1328 ?    ?   ?   A . n 
A 1 1329 ALA 1329 1329 ?    ?   ?   A . n 
A 1 1330 MET 1330 1330 ?    ?   ?   A . n 
A 1 1331 SER 1331 1331 ?    ?   ?   A . n 
A 1 1332 PRO 1332 1332 ?    ?   ?   A . n 
A 1 1333 ARG 1333 1333 ?    ?   ?   A . n 
A 1 1334 PRO 1334 1334 ?    ?   ?   A . n 
A 1 1335 GLU 1335 1335 ?    ?   ?   A . n 
A 1 1336 LEU 1336 1336 ?    ?   ?   A . n 
A 1 1337 PRO 1337 1337 ?    ?   ?   A . n 
A 1 1338 TYR 1338 1338 ?    ?   ?   A . n 
A 1 1339 ASN 1339 1339 ?    ?   ?   A . n 
A 1 1340 GLN 1340 1340 ?    ?   ?   A . n 
A 1 1341 MET 1341 1341 ?    ?   ?   A . n 
A 1 1342 ASP 1342 1342 ?    ?   ?   A . n 
A 1 1343 HIS 1343 1343 ?    ?   ?   A . n 
A 1 1344 THR 1344 1344 ?    ?   ?   A . n 
A 1 1345 CYS 1345 1345 ?    ?   ?   A . n 
A 1 1346 ASN 1346 1346 ?    ?   ?   A . n 
A 1 1347 VAL 1347 1347 ?    ?   ?   A . n 
A 1 1348 ASN 1348 1348 ?    ?   ?   A . n 
A 1 1349 ARG 1349 1349 ?    ?   ?   A . n 
A 1 1350 VAL 1350 1350 ?    ?   ?   A . n 
A 1 1351 SER 1351 1351 ?    ?   ?   A . n 
A 1 1352 TYR 1352 1352 ?    ?   ?   A . n 
A 1 1353 ASN 1353 1353 ?    ?   ?   A . n 
A 1 1354 GLY 1354 1354 ?    ?   ?   A . n 
A 1 1355 THR 1355 1355 ?    ?   ?   A . n 
A 1 1356 TYR 1356 1356 ?    ?   ?   A . n 
A 1 1357 VAL 1357 1357 ?    ?   ?   A . n 
A 1 1358 VAL 1358 1358 ?    ?   ?   A . n 
A 1 1359 LYS 1359 1359 ?    ?   ?   A . n 
A 1 1360 ASP 1360 1360 ?    ?   ?   A . n 
A 1 1361 GLY 1361 1361 ?    ?   ?   A . n 
A 1 1362 LEU 1362 1362 ?    ?   ?   A . n 
A 1 1363 PRO 1363 1363 ?    ?   ?   A . n 
A 1 1364 LEU 1364 1364 ?    ?   ?   A . n 
A 1 1365 ASN 1365 1365 ?    ?   ?   A . n 
A 1 1366 PRO 1366 1366 ?    ?   ?   A . n 
A 1 1367 MET 1367 1367 ?    ?   ?   A . n 
A 1 1368 GLY 1368 1368 ?    ?   ?   A . n 
A 1 1369 ARG 1369 1369 ?    ?   ?   A . n 
A 1 1370 THR 1370 1370 ?    ?   ?   A . n 
A 1 1371 GLY 1371 1371 ?    ?   ?   A . n 
A 1 1372 MET 1372 1372 ?    ?   ?   A . n 
A 1 1373 GLN 1373 1373 ?    ?   ?   A . n 
A 1 1374 GLY 1374 1374 ?    ?   ?   A . n 
A 1 1375 ARG 1375 1375 ?    ?   ?   A . n 
A 1 1376 GLY 1376 1376 ?    ?   ?   A . n 
A 1 1377 LEU 1377 1377 ?    ?   ?   A . n 
A 1 1378 LEU 1378 1378 ?    ?   ?   A . n 
A 1 1379 GLY 1379 1379 ?    ?   ?   A . n 
A 1 1380 ARG 1380 1380 ?    ?   ?   A . n 
A 1 1381 PHE 1381 1381 ?    ?   ?   A . n 
A 1 1382 GLY 1382 1382 ?    ?   ?   A . n 
A 1 1383 PRO 1383 1383 ?    ?   ?   A . n 
A 1 1384 ASN 1384 1384 ?    ?   ?   A . n 
A 1 1385 HIS 1385 1385 ?    ?   ?   A . n 
A 1 1386 ALA 1386 1386 ?    ?   ?   A . n 
A 1 1387 ALA 1387 1387 ?    ?   ?   A . n 
A 1 1388 ASP 1388 1388 ?    ?   ?   A . n 
A 1 1389 PRO 1389 1389 ?    ?   ?   A . n 
A 1 1390 VAL 1390 1390 ?    ?   ?   A . n 
A 1 1391 VAL 1391 1391 ?    ?   ?   A . n 
A 1 1392 THR 1392 1392 ?    ?   ?   A . n 
A 1 1393 ARG 1393 1393 ?    ?   ?   A . n 
A 1 1394 TRP 1394 1394 ?    ?   ?   A . n 
A 1 1395 LYS 1395 1395 ?    ?   ?   A . n 
A 1 1396 ARG 1396 1396 ?    ?   ?   A . n 
A 1 1397 THR 1397 1397 ?    ?   ?   A . n 
A 1 1398 SER 1398 1398 ?    ?   ?   A . n 
A 1 1399 ALA 1399 1399 ?    ?   ?   A . n 
A 1 1400 GLY 1400 1400 ?    ?   ?   A . n 
A 1 1401 VAL 1401 1401 ?    ?   ?   A . n 
A 1 1402 MET 1402 1402 ?    ?   ?   A . n 
A 1 1403 LEU 1403 1403 ?    ?   ?   A . n 
A 1 1404 GLN 1404 1404 ?    ?   ?   A . n 
A 1 1405 GLY 1405 1405 ?    ?   ?   A . n 
A 1 1406 GLY 1406 1406 ?    ?   ?   A . n 
A 1 1407 LYS 1407 1407 ?    ?   ?   A . n 
A 1 1408 LYS 1408 1408 ?    ?   ?   A . n 
A 1 1409 VAL 1409 1409 ?    ?   ?   A . n 
A 1 1410 LEU 1410 1410 ?    ?   ?   A . n 
A 1 1411 GLU 1411 1411 ?    ?   ?   A . n 
A 1 1412 PHE 1412 1412 ?    ?   ?   A . n 
A 1 1413 VAL 1413 1413 ?    ?   ?   A . n 
A 1 1414 ALA 1414 1414 ?    ?   ?   A . n 
A 1 1415 ILE 1415 1415 ?    ?   ?   A . n 
A 1 1416 GLN 1416 1416 ?    ?   ?   A . n 
A 1 1417 ARG 1417 1417 ?    ?   ?   A . n 
A 1 1418 LYS 1418 1418 ?    ?   ?   A . n 
A 1 1419 ASP 1419 1419 ?    ?   ?   A . n 
A 1 1420 ASN 1420 1420 ?    ?   ?   A . n 
A 1 1421 ASN 1421 1421 ?    ?   ?   A . n 
A 1 1422 GLN 1422 1422 ?    ?   ?   A . n 
A 1 1423 TRP 1423 1423 ?    ?   ?   A . n 
A 1 1424 ALA 1424 1424 ?    ?   ?   A . n 
A 1 1425 ILE 1425 1425 ?    ?   ?   A . n 
A 1 1426 PRO 1426 1426 ?    ?   ?   A . n 
A 1 1427 GLY 1427 1427 ?    ?   ?   A . n 
A 1 1428 GLY 1428 1428 ?    ?   ?   A . n 
A 1 1429 MET 1429 1429 ?    ?   ?   A . n 
A 1 1430 VAL 1430 1430 ?    ?   ?   A . n 
A 1 1431 GLU 1431 1431 ?    ?   ?   A . n 
A 1 1432 PRO 1432 1432 ?    ?   ?   A . n 
A 1 1433 GLY 1433 1433 ?    ?   ?   A . n 
A 1 1434 GLN 1434 1434 ?    ?   ?   A . n 
A 1 1435 LEU 1435 1435 ?    ?   ?   A . n 
A 1 1436 VAL 1436 1436 ?    ?   ?   A . n 
A 1 1437 THR 1437 1437 ?    ?   ?   A . n 
A 1 1438 GLN 1438 1438 ?    ?   ?   A . n 
A 1 1439 ALA 1439 1439 ?    ?   ?   A . n 
A 1 1440 LEU 1440 1440 ?    ?   ?   A . n 
A 1 1441 LYS 1441 1441 ?    ?   ?   A . n 
A 1 1442 ALA 1442 1442 ?    ?   ?   A . n 
A 1 1443 GLU 1443 1443 ?    ?   ?   A . n 
A 1 1444 PHE 1444 1444 ?    ?   ?   A . n 
A 1 1445 GLY 1445 1445 ?    ?   ?   A . n 
A 1 1446 GLU 1446 1446 ?    ?   ?   A . n 
A 1 1447 GLU 1447 1447 ?    ?   ?   A . n 
A 1 1448 ALA 1448 1448 ?    ?   ?   A . n 
A 1 1449 MET 1449 1449 ?    ?   ?   A . n 
A 1 1450 ALA 1450 1450 ?    ?   ?   A . n 
A 1 1451 LYS 1451 1451 ?    ?   ?   A . n 
A 1 1452 LEU 1452 1452 ?    ?   ?   A . n 
A 1 1453 ASN 1453 1453 ?    ?   ?   A . n 
A 1 1454 VAL 1454 1454 ?    ?   ?   A . n 
A 1 1455 SER 1455 1455 ?    ?   ?   A . n 
A 1 1456 GLN 1456 1456 ?    ?   ?   A . n 
A 1 1457 GLU 1457 1457 ?    ?   ?   A . n 
A 1 1458 GLU 1458 1458 ?    ?   ?   A . n 
A 1 1459 LYS 1459 1459 ?    ?   ?   A . n 
A 1 1460 GLU 1460 1460 ?    ?   ?   A . n 
A 1 1461 ARG 1461 1461 ?    ?   ?   A . n 
A 1 1462 ILE 1462 1462 ?    ?   ?   A . n 
A 1 1463 ALA 1463 1463 ?    ?   ?   A . n 
A 1 1464 LYS 1464 1464 ?    ?   ?   A . n 
A 1 1465 GLN 1465 1465 ?    ?   ?   A . n 
A 1 1466 ILE 1466 1466 ?    ?   ?   A . n 
A 1 1467 GLU 1467 1467 ?    ?   ?   A . n 
A 1 1468 ARG 1468 1468 ?    ?   ?   A . n 
A 1 1469 LEU 1469 1469 ?    ?   ?   A . n 
A 1 1470 PHE 1470 1470 ?    ?   ?   A . n 
A 1 1471 GLN 1471 1471 ?    ?   ?   A . n 
A 1 1472 GLN 1472 1472 ?    ?   ?   A . n 
A 1 1473 GLY 1473 1473 ?    ?   ?   A . n 
A 1 1474 GLN 1474 1474 ?    ?   ?   A . n 
A 1 1475 GLU 1475 1475 ?    ?   ?   A . n 
A 1 1476 ILE 1476 1476 ?    ?   ?   A . n 
A 1 1477 TYR 1477 1477 ?    ?   ?   A . n 
A 1 1478 LYS 1478 1478 ?    ?   ?   A . n 
A 1 1479 GLY 1479 1479 ?    ?   ?   A . n 
A 1 1480 TYR 1480 1480 ?    ?   ?   A . n 
A 1 1481 VAL 1481 1481 ?    ?   ?   A . n 
A 1 1482 ASP 1482 1482 ?    ?   ?   A . n 
A 1 1483 ASP 1483 1483 ?    ?   ?   A . n 
A 1 1484 PRO 1484 1484 ?    ?   ?   A . n 
A 1 1485 ARG 1485 1485 ?    ?   ?   A . n 
A 1 1486 ASN 1486 1486 ?    ?   ?   A . n 
A 1 1487 THR 1487 1487 ?    ?   ?   A . n 
A 1 1488 ASP 1488 1488 ?    ?   ?   A . n 
A 1 1489 ASN 1489 1489 ?    ?   ?   A . n 
A 1 1490 ALA 1490 1490 ?    ?   ?   A . n 
A 1 1491 TRP 1491 1491 ?    ?   ?   A . n 
A 1 1492 MET 1492 1492 ?    ?   ?   A . n 
A 1 1493 GLU 1493 1493 ?    ?   ?   A . n 
A 1 1494 THR 1494 1494 ?    ?   ?   A . n 
A 1 1495 VAL 1495 1495 ?    ?   ?   A . n 
A 1 1496 ALA 1496 1496 ?    ?   ?   A . n 
A 1 1497 VAL 1497 1497 ?    ?   ?   A . n 
A 1 1498 ASN 1498 1498 ?    ?   ?   A . n 
A 1 1499 PHE 1499 1499 ?    ?   ?   A . n 
A 1 1500 HIS 1500 1500 ?    ?   ?   A . n 
A 1 1501 ASP 1501 1501 ?    ?   ?   A . n 
A 1 1502 ASP 1502 1502 ?    ?   ?   A . n 
A 1 1503 LYS 1503 1503 ?    ?   ?   A . n 
A 1 1504 GLY 1504 1504 ?    ?   ?   A . n 
A 1 1505 ASP 1505 1505 ?    ?   ?   A . n 
A 1 1506 LEU 1506 1506 ?    ?   ?   A . n 
A 1 1507 PHE 1507 1507 ?    ?   ?   A . n 
A 1 1508 GLY 1508 1508 ?    ?   ?   A . n 
A 1 1509 ASP 1509 1509 ?    ?   ?   A . n 
A 1 1510 ILE 1510 1510 ?    ?   ?   A . n 
A 1 1511 THR 1511 1511 ?    ?   ?   A . n 
A 1 1512 LEU 1512 1512 ?    ?   ?   A . n 
A 1 1513 GLN 1513 1513 ?    ?   ?   A . n 
A 1 1514 ALA 1514 1514 ?    ?   ?   A . n 
A 1 1515 GLY 1515 1515 ?    ?   ?   A . n 
A 1 1516 ASP 1516 1516 ?    ?   ?   A . n 
A 1 1517 ASP 1517 1517 ?    ?   ?   A . n 
A 1 1518 ALA 1518 1518 ?    ?   ?   A . n 
A 1 1519 ALA 1519 1519 ?    ?   ?   A . n 
A 1 1520 ALA 1520 1520 ?    ?   ?   A . n 
A 1 1521 VAL 1521 1521 ?    ?   ?   A . n 
A 1 1522 ARG 1522 1522 ?    ?   ?   A . n 
A 1 1523 TRP 1523 1523 ?    ?   ?   A . n 
A 1 1524 GLN 1524 1524 ?    ?   ?   A . n 
A 1 1525 ARG 1525 1525 ?    ?   ?   A . n 
A 1 1526 VAL 1526 1526 ?    ?   ?   A . n 
A 1 1527 SER 1527 1527 ?    ?   ?   A . n 
A 1 1528 GLY 1528 1528 ?    ?   ?   A . n 
A 1 1529 ASN 1529 1529 ?    ?   ?   A . n 
A 1 1530 ILE 1530 1530 ?    ?   ?   A . n 
A 1 1531 PRO 1531 1531 ?    ?   ?   A . n 
A 1 1532 LEU 1532 1532 ?    ?   ?   A . n 
A 1 1533 TYR 1533 1533 ?    ?   ?   A . n 
A 1 1534 ALA 1534 1534 ?    ?   ?   A . n 
A 1 1535 SER 1535 1535 ?    ?   ?   A . n 
A 1 1536 HIS 1536 1536 ?    ?   ?   A . n 
A 1 1537 VAL 1537 1537 ?    ?   ?   A . n 
A 1 1538 SER 1538 1538 ?    ?   ?   A . n 
A 1 1539 ILE 1539 1539 ?    ?   ?   A . n 
A 1 1540 LEU 1540 1540 ?    ?   ?   A . n 
A 1 1541 GLU 1541 1541 ?    ?   ?   A . n 
A 1 1542 LYS 1542 1542 ?    ?   ?   A . n 
A 1 1543 VAL 1543 1543 ?    ?   ?   A . n 
A 1 1544 ALA 1544 1544 ?    ?   ?   A . n 
A 1 1545 LYS 1545 1545 ?    ?   ?   A . n 
A 1 1546 MET 1546 1546 ?    ?   ?   A . n 
A 1 1547 ARG 1547 1547 ?    ?   ?   A . n 
A 1 1548 ASP 1548 1548 ?    ?   ?   A . n 
A 1 1549 ALA 1549 1549 ?    ?   ?   A . n 
A 1 1550 ALA 1550 1550 ?    ?   ?   A . n 
A 1 1551 PHE 1551 1551 ?    ?   ?   A . n 
A 1 1552 SER 1552 1552 ?    ?   ?   A . n 
A 1 1553 ASN 1553 1553 ?    ?   ?   A . n 
A 1 1554 SER 1554 1554 ?    ?   ?   A . n 
A 1 1555 LEU 1555 1555 ?    ?   ?   A . n 
A 1 1556 GLU 1556 1556 ?    ?   ?   A . n 
A 1 1557 VAL 1557 1557 ?    ?   ?   A . n 
A 1 1558 LEU 1558 1558 ?    ?   ?   A . n 
A 1 1559 PHE 1559 1559 ?    ?   ?   A . n 
A 1 1560 GLN 1560 1560 ?    ?   ?   A . n 
# 
loop_
_pdbx_branch_scheme.asym_id 
_pdbx_branch_scheme.entity_id 
_pdbx_branch_scheme.mon_id 
_pdbx_branch_scheme.num 
_pdbx_branch_scheme.pdb_asym_id 
_pdbx_branch_scheme.pdb_mon_id 
_pdbx_branch_scheme.pdb_seq_num 
_pdbx_branch_scheme.auth_asym_id 
_pdbx_branch_scheme.auth_mon_id 
_pdbx_branch_scheme.auth_seq_num 
_pdbx_branch_scheme.hetero 
B 2 NAG 1 B NAG 1 B NAG 1 n 
B 2 NAG 2 B NAG 2 B NAG 2 n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 A2R ? ? A2R ? ? 'SUBJECT OF INVESTIGATION' ? 
2 CA  ? ? CA  ? ? 'SUBJECT OF INVESTIGATION' ? 
3 NAG ? ? NAG ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 3 CA  1 4000 4000 CA  CA  A . 
D 4 A2R 1 4001 4001 A2R A2R A . 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9JJF 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     1.00 
_cell.length_a_esd                 ? 
_cell.length_b                     1.00 
_cell.length_b_esd                 ? 
_cell.length_c                     1.00 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        ? 
_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                         9JJF 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                1 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1' 
_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                   9JJF 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_refine.pdbx_refine_id                           'ELECTRON MICROSCOPY' 
_refine.entry_id                                 9JJF 
_refine.pdbx_diffrn_id                           ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             ? 
_refine.ls_d_res_high                            . 
_refine.ls_percent_reflns_obs                    ? 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       ? 
_refine.ls_R_factor_R_free                       ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_number_reflns_R_free                  ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.B_iso_mean                               ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
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 
'ELECTRON MICROSCOPY' ? 0.007  ? 7786  ? f_bond_d           ? ? 
'ELECTRON MICROSCOPY' ? 0.963  ? 10562 ? f_angle_d          ? ? 
'ELECTRON MICROSCOPY' ? 11.297 ? 2877  ? f_dihedral_angle_d ? ? 
'ELECTRON MICROSCOPY' ? 0.159  ? 1210  ? f_chiral_restr     ? ? 
'ELECTRON MICROSCOPY' ? 0.008  ? 1318  ? f_plane_restr      ? ? 
# 
_struct.entry_id                     9JJF 
_struct.title                        'Nematostella vectensis TRPM2 protomer in complex with ADPRP/Ca2+' 
_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        9JJF 
_struct_keywords.text            'Nematostella vectensis, TRPM2, ADPRP, Ca2+, MEMBRANE PROTEIN' 
_struct_keywords.pdbx_keywords   'MEMBRANE PROTEIN' 
# 
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                    TMP2L_NEMVE 
_struct_ref.pdbx_db_accession          A7T1N0 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MGKDSFTPLYDGGDSSHVHLNKFGSNQLSQSKKSWIARNFSRRECIRFVPKSHDVSRCKCGRPRERHSQQALESGQGSEE
WNVASCTTKHPTNAYGEIDFEGYGGQKRAPYLRMSHDTDANLVITLMLKRWNLEIPNLVISVTGGAKSFVLKPRLREMFR
RGLIKAAKTTGAWIITGGTNTGVMKHVGEAVKEQQLMFGSDTQVNVIGIATWGIVDKQSDLISEKNGKYPALYSMEPTPG
HQGAMLDPNHSHFFLVDDGTEGKYGVEIGMRSRIEEAIMKVKTDSRSEAGSIGVPVVLLVLEGGPNTVATMYELIKKKVP
AVVIDGSGRAASVVGFAYNHTIKRNVDGQTINVIDPQYEDEVRAKVVEVFGAKGADKTYSMIKDVLEDEKMISVYSLDGE
ISQDIDLAILKALLKANRSSPVAQLNLALAWNRIDLAKSDIFTEEQQWTTETLSAAMLTALLDDKAEFAELFLQNGLSMR
EFLSLDILCKLYAEVPGNTTIKPLLQKEMGKRQVKTIDMDVVGEVIEELMGDMFESYYRKDGHYFGELASYAEGLVLKNR
KSSKDLLANINRIDPLPTPYLDVFLWAVLCNRRELARVLWEAGREPMAAALMASRLLKRMASRAQEDNTITDISSDLYDH
ARLFEERAVGVLDECFNENETLSQTLLVRELDHYSRMTALELAVSAESQDFIAHTSCQVLLTRLWMGTMAMNTRWWKVLV
CLYLPVLIFPIIYFVPDEQHERQAAEREHQKSLNQKSSKVKSHKEKNDAPVVPVYRSKEEKAVSNDEEARVGTENEEEDF
QLEDYIPEIREDDSMEVIMRNKKLGFCDRIMHFYSAPFSKFVGNVVGYLAFIFLYAYVVLFNFPRFDPAKTLGGIHPTEI
VLYFWVFTILIEEIRQLAAKPPKYIKDKVSVYFSDTWNFVDIFSLTVFIIAIILRFFTNSRIFTASRIILSLDIIFFIVR
SLQIFSVNRLLGPKLVMIQKMMQDLAQFIIILAVFTIAYGIALHAVMFPSPGIYARNNTWVTITSVVQYPYWQMYGELFL
DEIQGEKPKEFGEVDPDGRWLSPLLLAIYMVFTNILLLNLLIAIFNYTFERVQEDSDKVWKFQRYDLVQEYHSRPVFAPP
LVLLGHILIFIRWVWRMCRCGHPPRGSTMKIGLSPAEMEQMDNWEFQAAEMYIHQQQQKNSGTLEERVRALGDRVDCINS
QLNRVLDSMSGTRAHALTDGNGLEGGHDSEGRLARMEVELSSNSESLQKILALLQQQPPVKGQAAVPIQLTLLHYKARSS
PYPGSTAKRFAVQDNMVDWQVPFPDYKPVNYTAPVVLANPVWADKDLMAMSPRPELPYNQMDHTCNVNRVSYNGTYVVKD
GLPLNPMGRTGMQGRGLLGRFGPNHAADPVVTRWKRTSAGVMLQGGKKVLEFVAIQRKDNNQWAIPGGMVEPGQLVTQAL
KAEFGEEAMAKLNVSQEEKERIAKQIERLFQQGQEIYKGYVDDPRNTDNAWMETVAVNFHDDKGDLFGDITLQAGDDAAA
VRWQRVSGNIPLYASHVSILEKVAKMRDAAF
;
_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              9JJF 
_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                 1551 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             A7T1N0 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  1551 
_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       1551 
# 
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 9JJF SER A 1552 ? UNP A7T1N0 ? ? 'expression tag' 1552 1 
1 9JJF ASN A 1553 ? UNP A7T1N0 ? ? 'expression tag' 1553 2 
1 9JJF SER A 1554 ? UNP A7T1N0 ? ? 'expression tag' 1554 3 
1 9JJF LEU A 1555 ? UNP A7T1N0 ? ? 'expression tag' 1555 4 
1 9JJF GLU A 1556 ? UNP A7T1N0 ? ? 'expression tag' 1556 5 
1 9JJF VAL A 1557 ? UNP A7T1N0 ? ? 'expression tag' 1557 6 
1 9JJF LEU A 1558 ? UNP A7T1N0 ? ? 'expression tag' 1558 7 
1 9JJF PHE A 1559 ? UNP A7T1N0 ? ? 'expression tag' 1559 8 
1 9JJF GLN A 1560 ? UNP A7T1N0 ? ? 'expression tag' 1560 9 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'electron microscopy' 
_pdbx_struct_assembly_auth_evidence.details                'not applicable' 
# 
_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   ? 
_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 ASP A 119  ? ARG A 130  ? ASP A 119  ARG A 130  1 ? 12 
HELX_P HELX_P2  AA2 LYS A 152  ? THR A 169  ? LYS A 152  THR A 169  1 ? 18 
HELX_P HELX_P3  AA3 GLY A 182  ? GLU A 193  ? GLY A 182  GLU A 193  1 ? 12 
HELX_P HELX_P4  AA4 TYR A 264  ? VAL A 281  ? TYR A 264  VAL A 281  1 ? 18 
HELX_P HELX_P5  AA5 GLY A 304  ? LYS A 317  ? GLY A 304  LYS A 317  1 ? 14 
HELX_P HELX_P6  AA6 ALA A 330  ? ASN A 339  ? ALA A 330  ASN A 339  1 ? 10 
HELX_P HELX_P7  AA7 TYR A 358  ? VAL A 369  ? TYR A 358  VAL A 369  1 ? 12 
HELX_P HELX_P8  AA8 GLY A 374  ? LEU A 386  ? GLY A 374  LEU A 386  1 ? 13 
HELX_P HELX_P9  AA9 ASP A 404  ? ASN A 417  ? ASP A 404  ASN A 417  1 ? 14 
HELX_P HELX_P10 AB1 SER A 420  ? ASN A 432  ? SER A 420  ASN A 432  1 ? 13 
HELX_P HELX_P11 AB2 ARG A 433  ? ILE A 441  ? ARG A 433  ILE A 441  1 ? 9  
HELX_P HELX_P12 AB3 LEU A 453  ? ASP A 463  ? LEU A 453  ASP A 463  1 ? 11 
HELX_P HELX_P13 AB4 LYS A 465  ? GLY A 476  ? LYS A 465  GLY A 476  1 ? 12 
HELX_P HELX_P14 AB5 SER A 478  ? LEU A 483  ? SER A 478  LEU A 483  1 ? 6  
HELX_P HELX_P15 AB6 SER A 484  ? TYR A 492  ? SER A 484  TYR A 492  1 ? 9  
HELX_P HELX_P16 AB7 THR A 500  ? GLN A 513  ? THR A 500  GLN A 513  1 ? 14 
HELX_P HELX_P17 AB8 ASP A 518  ? GLY A 531  ? ASP A 518  GLY A 531  1 ? 14 
HELX_P HELX_P18 AB9 SER A 536  ? ASP A 541  ? SER A 536  ASP A 541  1 ? 6  
HELX_P HELX_P19 AC1 GLY A 542  ? PHE A 545  ? GLY A 542  PHE A 545  5 ? 4  
HELX_P HELX_P20 AC2 THR A 578  ? CYS A 590  ? THR A 578  CYS A 590  1 ? 13 
HELX_P HELX_P21 AC3 ARG A 592  ? GLY A 603  ? ARG A 592  GLY A 603  1 ? 12 
HELX_P HELX_P22 AC4 GLU A 605  ? ASP A 627  ? GLU A 605  ASP A 627  1 ? 23 
HELX_P HELX_P23 AC5 ILE A 633  ? GLU A 658  ? ILE A 633  GLU A 658  1 ? 26 
HELX_P HELX_P24 AC6 ASN A 659  ? LEU A 667  ? ASN A 659  LEU A 667  1 ? 9  
HELX_P HELX_P25 AC7 LEU A 671  ? SER A 675  ? LEU A 671  SER A 675  5 ? 5  
HELX_P HELX_P26 AC8 THR A 678  ? ALA A 686  ? THR A 678  ALA A 686  1 ? 9  
HELX_P HELX_P27 AC9 SER A 688  ? ALA A 693  ? SER A 688  ALA A 693  1 ? 6  
HELX_P HELX_P28 AD1 HIS A 694  ? MET A 706  ? HIS A 694  MET A 706  1 ? 13 
HELX_P HELX_P29 AD2 ARG A 714  ? CYS A 721  ? ARG A 714  CYS A 721  1 ? 8  
HELX_P HELX_P30 AD3 LEU A 727  ? ILE A 732  ? LEU A 727  ILE A 732  1 ? 6  
HELX_P HELX_P31 AD4 CYS A 827  ? SER A 835  ? CYS A 827  SER A 835  1 ? 9  
HELX_P HELX_P32 AD5 ALA A 836  ? PHE A 861  ? ALA A 836  PHE A 861  1 ? 26 
HELX_P HELX_P33 AD6 LYS A 870  ? ILE A 875  ? LYS A 870  ILE A 875  5 ? 6  
HELX_P HELX_P34 AD7 HIS A 876  ? ALA A 899  ? HIS A 876  ALA A 899  1 ? 24 
HELX_P HELX_P35 AD8 TYR A 904  ? PHE A 913  ? TYR A 904  PHE A 913  1 ? 10 
HELX_P HELX_P36 AD9 ASP A 915  ? ARG A 935  ? ASP A 915  ARG A 935  1 ? 21 
HELX_P HELX_P37 AE1 ASN A 939  ? SER A 961  ? ASN A 939  SER A 961  1 ? 23 
HELX_P HELX_P38 AE2 SER A 961  ? SER A 966  ? SER A 961  SER A 966  1 ? 6  
HELX_P HELX_P39 AE3 LEU A 970  ? PHE A 1008 ? LEU A 970  PHE A 1008 1 ? 39 
HELX_P HELX_P40 AE4 ASN A 1018 ? TYR A 1035 ? ASN A 1018 TYR A 1035 1 ? 18 
HELX_P HELX_P41 AE5 PHE A 1039 ? GLN A 1044 ? PHE A 1039 GLN A 1044 1 ? 6  
HELX_P HELX_P42 AE6 ASP A 1057 ? ASN A 1074 ? ASP A 1057 ASN A 1074 1 ? 18 
HELX_P HELX_P43 AE7 LEU A 1076 ? GLU A 1094 ? LEU A 1076 GLU A 1094 1 ? 19 
HELX_P HELX_P44 AE8 ASP A 1095 ? SER A 1113 ? ASP A 1095 SER A 1113 1 ? 19 
HELX_P HELX_P45 AE9 LEU A 1121 ? ILE A 1131 ? LEU A 1121 ILE A 1131 1 ? 11 
HELX_P HELX_P46 AF1 SER A 1154 ? GLY A 1182 ? SER A 1154 GLY A 1182 1 ? 29 
HELX_P HELX_P47 AF2 THR A 1183 ? LEU A 1206 ? THR A 1183 LEU A 1206 1 ? 24 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
covale1 covale one  ? A ASN 1017 ND2 ? ? ? 1_555 B NAG . C1 ? ? A ASN 1017 B NAG 1    1_555 ? ? ? ? ? ? ? 1.432 ? N-Glycosylation 
covale2 covale both ? B NAG .    O4  ? ? ? 1_555 B NAG . C1 ? ? B NAG 1    B NAG 2    1_555 ? ? ? ? ? ? ? 1.435 ? ?               
metalc1 metalc ?    ? A GLU 893  OE1 ? ? ? 1_555 C CA  . CA ? ? A GLU 893  A CA  4000 1_555 ? ? ? ? ? ? ? 2.994 ? ?               
metalc2 metalc ?    ? A GLU 893  OE2 ? ? ? 1_555 C CA  . CA ? ? A GLU 893  A CA  4000 1_555 ? ? ? ? ? ? ? 2.734 ? ?               
metalc3 metalc ?    ? A GLN 896  OE1 ? ? ? 1_555 C CA  . CA ? ? A GLN 896  A CA  4000 1_555 ? ? ? ? ? ? ? 2.512 ? ?               
metalc4 metalc ?    ? A ASN 918  OD1 ? ? ? 1_555 C CA  . CA ? ? A ASN 918  A CA  4000 1_555 ? ? ? ? ? ? ? 2.570 ? ?               
metalc5 metalc ?    ? A ASP 921  OD2 ? ? ? 1_555 C CA  . CA ? ? A ASP 921  A CA  4000 1_555 ? ? ? ? ? ? ? 2.522 ? ?               
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
covale ? ? 
metalc ? ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  OE1 ? A GLU 893 ? A GLU 893 ? 1_555 CA ? C CA . ? A CA 4000 ? 1_555 OE2 ? A GLU 893 ? A GLU 893 ? 1_555 44.6  ? 
2  OE1 ? A GLU 893 ? A GLU 893 ? 1_555 CA ? C CA . ? A CA 4000 ? 1_555 OE1 ? A GLN 896 ? A GLN 896 ? 1_555 63.4  ? 
3  OE2 ? A GLU 893 ? A GLU 893 ? 1_555 CA ? C CA . ? A CA 4000 ? 1_555 OE1 ? A GLN 896 ? A GLN 896 ? 1_555 73.7  ? 
4  OE1 ? A GLU 893 ? A GLU 893 ? 1_555 CA ? C CA . ? A CA 4000 ? 1_555 OD1 ? A ASN 918 ? A ASN 918 ? 1_555 67.8  ? 
5  OE2 ? A GLU 893 ? A GLU 893 ? 1_555 CA ? C CA . ? A CA 4000 ? 1_555 OD1 ? A ASN 918 ? A ASN 918 ? 1_555 112.2 ? 
6  OE1 ? A GLN 896 ? A GLN 896 ? 1_555 CA ? C CA . ? A CA 4000 ? 1_555 OD1 ? A ASN 918 ? A ASN 918 ? 1_555 81.4  ? 
7  OE1 ? A GLU 893 ? A GLU 893 ? 1_555 CA ? C CA . ? A CA 4000 ? 1_555 OD2 ? A ASP 921 ? A ASP 921 ? 1_555 76.7  ? 
8  OE2 ? A GLU 893 ? A GLU 893 ? 1_555 CA ? C CA . ? A CA 4000 ? 1_555 OD2 ? A ASP 921 ? A ASP 921 ? 1_555 66.4  ? 
9  OE1 ? A GLN 896 ? A GLN 896 ? 1_555 CA ? C CA . ? A CA 4000 ? 1_555 OD2 ? A ASP 921 ? A ASP 921 ? 1_555 137.0 ? 
10 OD1 ? A ASN 918 ? A ASN 918 ? 1_555 CA ? C CA . ? A CA 4000 ? 1_555 OD2 ? A ASP 921 ? A ASP 921 ? 1_555 98.7  ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      NAG 
_pdbx_modification_feature.label_asym_id                      B 
_pdbx_modification_feature.label_seq_id                       . 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     ASN 
_pdbx_modification_feature.modified_residue_label_asym_id     A 
_pdbx_modification_feature.modified_residue_label_seq_id      1017 
_pdbx_modification_feature.modified_residue_label_alt_id      ? 
_pdbx_modification_feature.auth_comp_id                       NAG 
_pdbx_modification_feature.auth_asym_id                       B 
_pdbx_modification_feature.auth_seq_id                        1 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      ASN 
_pdbx_modification_feature.modified_residue_auth_asym_id      A 
_pdbx_modification_feature.modified_residue_auth_seq_id       1017 
_pdbx_modification_feature.modified_residue_PDB_ins_code      ? 
_pdbx_modification_feature.modified_residue_symmetry          1_555 
_pdbx_modification_feature.comp_id_linking_atom               C1 
_pdbx_modification_feature.modified_residue_id_linking_atom   ND2 
_pdbx_modification_feature.modified_residue_id                ASN 
_pdbx_modification_feature.ref_pcm_id                         1 
_pdbx_modification_feature.ref_comp_id                        NAG 
_pdbx_modification_feature.type                               N-Glycosylation 
_pdbx_modification_feature.category                           Carbohydrate 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   9 
_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 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? parallel      
AA1 6 7 ? parallel      
AA1 7 8 ? parallel      
AA1 8 9 ? 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 TYR A 95  ? ILE A 98  ? TYR A 95  ILE A 98  
AA1 2 ALA A 109 ? MET A 114 ? ALA A 109 MET A 114 
AA1 3 HIS A 252 ? VAL A 256 ? HIS A 252 VAL A 256 
AA1 4 VAL A 206 ? THR A 211 ? VAL A 206 THR A 211 
AA1 5 TRP A 173 ? THR A 176 ? TRP A 173 THR A 176 
AA1 6 VAL A 139 ? GLY A 144 ? VAL A 139 GLY A 144 
AA1 7 VAL A 296 ? LEU A 301 ? VAL A 296 LEU A 301 
AA1 8 ALA A 321 ? VAL A 323 ? ALA A 321 VAL A 323 
AA1 9 ILE A 392 ? VAL A 394 ? ILE A 392 VAL A 394 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N ILE A 98  ? N ILE A 98  O ALA A 109 ? O ALA A 109 
AA1 2 3 N LEU A 112 ? N LEU A 112 O LEU A 255 ? O LEU A 255 
AA1 3 4 O HIS A 252 ? O HIS A 252 N GLY A 208 ? N GLY A 208 
AA1 4 5 O ILE A 209 ? O ILE A 209 N THR A 176 ? N THR A 176 
AA1 5 6 O ILE A 175 ? O ILE A 175 N ILE A 140 ? N ILE A 140 
AA1 6 7 N VAL A 139 ? N VAL A 139 O VAL A 297 ? O VAL A 297 
AA1 7 8 N LEU A 298 ? N LEU A 298 O VAL A 322 ? O VAL A 322 
AA1 8 9 N VAL A 323 ? N VAL A 323 O SER A 393 ? O SER A 393 
# 
_pdbx_entry_details.entry_id                   9JJF 
_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   Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 TYR A 338  ? ? -93.06  -63.08 
2  1 THR A 350  ? ? 60.33   67.75  
3  1 PHE A 442  ? ? -107.11 43.40  
4  1 ASN A 475  ? ? -92.91  -63.59 
5  1 GLU A 494  ? ? -97.07  40.18  
6  1 GLU A 605  ? ? 34.44   65.93  
7  1 ASN A 659  ? ? 58.70   71.72  
8  1 THR A 938  ? ? 46.42   24.22  
9  1 SER A 961  ? ? -67.91  8.05   
10 1 PHE A 1039 ? ? -94.29  51.71  
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9JJF 
_em_3d_fitting.method            ? 
_em_3d_fitting.target_criteria   ? 
_em_3d_fitting.details           ? 
_em_3d_fitting.overall_b_value   ? 
_em_3d_fitting.ref_space         ? 
_em_3d_fitting.ref_protocol      ? 
# 
_em_3d_reconstruction.entry_id                    9JJF 
_em_3d_reconstruction.id                          1 
_em_3d_reconstruction.method                      ? 
_em_3d_reconstruction.algorithm                   ? 
_em_3d_reconstruction.citation_id                 ? 
_em_3d_reconstruction.details                     ? 
_em_3d_reconstruction.resolution                  2.65 
_em_3d_reconstruction.resolution_method           'FSC 0.143 CUT-OFF' 
_em_3d_reconstruction.magnification_calibration   ? 
_em_3d_reconstruction.nominal_pixel_size          ? 
_em_3d_reconstruction.actual_pixel_size           ? 
_em_3d_reconstruction.num_particles               474307 
_em_3d_reconstruction.euler_angles_details        ? 
_em_3d_reconstruction.num_class_averages          ? 
_em_3d_reconstruction.refinement_type             ? 
_em_3d_reconstruction.image_processing_id         1 
_em_3d_reconstruction.symmetry_type               POINT 
# 
_em_buffer.id            1 
_em_buffer.specimen_id   1 
_em_buffer.name          ? 
_em_buffer.details       ? 
_em_buffer.pH            8 
# 
_em_entity_assembly.id                   1 
_em_entity_assembly.parent_id            0 
_em_entity_assembly.source               RECOMBINANT 
_em_entity_assembly.type                 COMPLEX 
_em_entity_assembly.name                 'nvTRPM2 protomer in complex with ADPRP/Ca2+' 
_em_entity_assembly.details              ? 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       1 
# 
_em_imaging.entry_id                        9JJF 
_em_imaging.id                              1 
_em_imaging.astigmatism                     ? 
_em_imaging.electron_beam_tilt_params       ? 
_em_imaging.residual_tilt                   ? 
_em_imaging.microscope_model                'FEI TITAN KRIOS' 
_em_imaging.specimen_holder_type            ? 
_em_imaging.specimen_holder_model           ? 
_em_imaging.details                         ? 
_em_imaging.date                            ? 
_em_imaging.accelerating_voltage            300 
_em_imaging.illumination_mode               'FLOOD BEAM' 
_em_imaging.mode                            'BRIGHT FIELD' 
_em_imaging.nominal_cs                      ? 
_em_imaging.nominal_defocus_min             1000 
_em_imaging.nominal_defocus_max             2200 
_em_imaging.calibrated_defocus_min          ? 
_em_imaging.calibrated_defocus_max          ? 
_em_imaging.tilt_angle_min                  ? 
_em_imaging.tilt_angle_max                  ? 
_em_imaging.nominal_magnification           ? 
_em_imaging.calibrated_magnification        ? 
_em_imaging.electron_source                 'FIELD EMISSION GUN' 
_em_imaging.citation_id                     ? 
_em_imaging.temperature                     ? 
_em_imaging.detector_distance               ? 
_em_imaging.recording_temperature_minimum   ? 
_em_imaging.recording_temperature_maximum   ? 
_em_imaging.alignment_procedure             ? 
_em_imaging.c2_aperture_diameter            ? 
_em_imaging.specimen_id                     1 
_em_imaging.cryogen                         ? 
# 
_em_vitrification.entry_id              9JJF 
_em_vitrification.id                    1 
_em_vitrification.specimen_id           1 
_em_vitrification.cryogen_name          ETHANE 
_em_vitrification.humidity              ? 
_em_vitrification.temp                  ? 
_em_vitrification.chamber_temperature   ? 
_em_vitrification.instrument            ? 
_em_vitrification.method                ? 
_em_vitrification.time_resolved_state   ? 
_em_vitrification.citation_id           ? 
_em_vitrification.details               ? 
# 
_em_experiment.entry_id                9JJF 
_em_experiment.id                      1 
_em_experiment.reconstruction_method   'SINGLE PARTICLE' 
_em_experiment.aggregation_state       PARTICLE 
_em_experiment.entity_assembly_id      1 
# 
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 GLY 2    ? A GLY 2    
3   1 Y 1 A LYS 3    ? A LYS 3    
4   1 Y 1 A ASP 4    ? A ASP 4    
5   1 Y 1 A SER 5    ? A SER 5    
6   1 Y 1 A PHE 6    ? A PHE 6    
7   1 Y 1 A THR 7    ? A THR 7    
8   1 Y 1 A PRO 8    ? A PRO 8    
9   1 Y 1 A LEU 9    ? A LEU 9    
10  1 Y 1 A TYR 10   ? A TYR 10   
11  1 Y 1 A ASP 11   ? A ASP 11   
12  1 Y 1 A GLY 12   ? A GLY 12   
13  1 Y 1 A GLY 13   ? A GLY 13   
14  1 Y 1 A ASP 14   ? A ASP 14   
15  1 Y 1 A SER 15   ? A SER 15   
16  1 Y 1 A SER 16   ? A SER 16   
17  1 Y 1 A HIS 17   ? A HIS 17   
18  1 Y 1 A VAL 18   ? A VAL 18   
19  1 Y 1 A HIS 19   ? A HIS 19   
20  1 Y 1 A LEU 20   ? A LEU 20   
21  1 Y 1 A ASN 21   ? A ASN 21   
22  1 Y 1 A LYS 22   ? A LYS 22   
23  1 Y 1 A PHE 23   ? A PHE 23   
24  1 Y 1 A GLY 24   ? A GLY 24   
25  1 Y 1 A SER 25   ? A SER 25   
26  1 Y 1 A ASN 26   ? A ASN 26   
27  1 Y 1 A GLN 27   ? A GLN 27   
28  1 Y 1 A LEU 28   ? A LEU 28   
29  1 Y 1 A SER 29   ? A SER 29   
30  1 Y 1 A GLN 30   ? A GLN 30   
31  1 Y 1 A SER 31   ? A SER 31   
32  1 Y 1 A LYS 32   ? A LYS 32   
33  1 Y 1 A LYS 33   ? A LYS 33   
34  1 Y 1 A SER 34   ? A SER 34   
35  1 Y 1 A TRP 35   ? A TRP 35   
36  1 Y 1 A ILE 36   ? A ILE 36   
37  1 Y 1 A ALA 37   ? A ALA 37   
38  1 Y 1 A ARG 38   ? A ARG 38   
39  1 Y 1 A ASN 39   ? A ASN 39   
40  1 Y 1 A PHE 40   ? A PHE 40   
41  1 Y 1 A SER 41   ? A SER 41   
42  1 Y 1 A ARG 42   ? A ARG 42   
43  1 Y 1 A ARG 43   ? A ARG 43   
44  1 Y 1 A GLU 44   ? A GLU 44   
45  1 Y 1 A CYS 45   ? A CYS 45   
46  1 Y 1 A ILE 46   ? A ILE 46   
47  1 Y 1 A ARG 47   ? A ARG 47   
48  1 Y 1 A PHE 48   ? A PHE 48   
49  1 Y 1 A VAL 49   ? A VAL 49   
50  1 Y 1 A PRO 50   ? A PRO 50   
51  1 Y 1 A LYS 51   ? A LYS 51   
52  1 Y 1 A SER 52   ? A SER 52   
53  1 Y 1 A HIS 53   ? A HIS 53   
54  1 Y 1 A ASP 54   ? A ASP 54   
55  1 Y 1 A VAL 55   ? A VAL 55   
56  1 Y 1 A SER 56   ? A SER 56   
57  1 Y 1 A ARG 57   ? A ARG 57   
58  1 Y 1 A CYS 58   ? A CYS 58   
59  1 Y 1 A LYS 59   ? A LYS 59   
60  1 Y 1 A CYS 60   ? A CYS 60   
61  1 Y 1 A GLY 61   ? A GLY 61   
62  1 Y 1 A ARG 62   ? A ARG 62   
63  1 Y 1 A PRO 63   ? A PRO 63   
64  1 Y 1 A ARG 64   ? A ARG 64   
65  1 Y 1 A GLU 65   ? A GLU 65   
66  1 Y 1 A ARG 66   ? A ARG 66   
67  1 Y 1 A HIS 67   ? A HIS 67   
68  1 Y 1 A SER 68   ? A SER 68   
69  1 Y 1 A GLN 69   ? A GLN 69   
70  1 Y 1 A GLN 70   ? A GLN 70   
71  1 Y 1 A ALA 71   ? A ALA 71   
72  1 Y 1 A LEU 72   ? A LEU 72   
73  1 Y 1 A GLU 73   ? A GLU 73   
74  1 Y 1 A SER 74   ? A SER 74   
75  1 Y 1 A GLY 75   ? A GLY 75   
76  1 Y 1 A GLN 76   ? A GLN 76   
77  1 Y 1 A GLY 77   ? A GLY 77   
78  1 Y 1 A SER 78   ? A SER 78   
79  1 Y 1 A GLU 79   ? A GLU 79   
80  1 Y 1 A GLU 80   ? A GLU 80   
81  1 Y 1 A TRP 81   ? A TRP 81   
82  1 Y 1 A ASN 82   ? A ASN 82   
83  1 Y 1 A VAL 83   ? A VAL 83   
84  1 Y 1 A ALA 84   ? A ALA 84   
85  1 Y 1 A SER 85   ? A SER 85   
86  1 Y 1 A CYS 86   ? A CYS 86   
87  1 Y 1 A THR 87   ? A THR 87   
88  1 Y 1 A THR 88   ? A THR 88   
89  1 Y 1 A LYS 89   ? A LYS 89   
90  1 Y 1 A HIS 90   ? A HIS 90   
91  1 Y 1 A PRO 91   ? A PRO 91   
92  1 Y 1 A THR 92   ? A THR 92   
93  1 Y 1 A ASN 93   ? A ASN 93   
94  1 Y 1 A LYS 217  ? A LYS 217  
95  1 Y 1 A GLN 218  ? A GLN 218  
96  1 Y 1 A SER 219  ? A SER 219  
97  1 Y 1 A ASP 220  ? A ASP 220  
98  1 Y 1 A LEU 221  ? A LEU 221  
99  1 Y 1 A ILE 222  ? A ILE 222  
100 1 Y 1 A SER 223  ? A SER 223  
101 1 Y 1 A GLU 224  ? A GLU 224  
102 1 Y 1 A LYS 225  ? A LYS 225  
103 1 Y 1 A ASN 226  ? A ASN 226  
104 1 Y 1 A GLY 227  ? A GLY 227  
105 1 Y 1 A LYS 228  ? A LYS 228  
106 1 Y 1 A TYR 229  ? A TYR 229  
107 1 Y 1 A PRO 230  ? A PRO 230  
108 1 Y 1 A ALA 231  ? A ALA 231  
109 1 Y 1 A LEU 232  ? A LEU 232  
110 1 Y 1 A TYR 233  ? A TYR 233  
111 1 Y 1 A SER 234  ? A SER 234  
112 1 Y 1 A MET 235  ? A MET 235  
113 1 Y 1 A GLU 236  ? A GLU 236  
114 1 Y 1 A PRO 237  ? A PRO 237  
115 1 Y 1 A THR 238  ? A THR 238  
116 1 Y 1 A PRO 239  ? A PRO 239  
117 1 Y 1 A GLY 240  ? A GLY 240  
118 1 Y 1 A HIS 241  ? A HIS 241  
119 1 Y 1 A GLN 242  ? A GLN 242  
120 1 Y 1 A LYS 282  ? A LYS 282  
121 1 Y 1 A THR 283  ? A THR 283  
122 1 Y 1 A ASP 284  ? A ASP 284  
123 1 Y 1 A SER 285  ? A SER 285  
124 1 Y 1 A ARG 286  ? A ARG 286  
125 1 Y 1 A SER 287  ? A SER 287  
126 1 Y 1 A GLU 288  ? A GLU 288  
127 1 Y 1 A ALA 289  ? A ALA 289  
128 1 Y 1 A GLY 290  ? A GLY 290  
129 1 Y 1 A SER 291  ? A SER 291  
130 1 Y 1 A GLY 546  ? A GLY 546  
131 1 Y 1 A GLU 547  ? A GLU 547  
132 1 Y 1 A LEU 548  ? A LEU 548  
133 1 Y 1 A ALA 549  ? A ALA 549  
134 1 Y 1 A SER 550  ? A SER 550  
135 1 Y 1 A TYR 551  ? A TYR 551  
136 1 Y 1 A ALA 552  ? A ALA 552  
137 1 Y 1 A GLU 553  ? A GLU 553  
138 1 Y 1 A GLY 554  ? A GLY 554  
139 1 Y 1 A LEU 555  ? A LEU 555  
140 1 Y 1 A VAL 556  ? A VAL 556  
141 1 Y 1 A LEU 557  ? A LEU 557  
142 1 Y 1 A LYS 558  ? A LYS 558  
143 1 Y 1 A ASN 559  ? A ASN 559  
144 1 Y 1 A ARG 560  ? A ARG 560  
145 1 Y 1 A LYS 561  ? A LYS 561  
146 1 Y 1 A SER 562  ? A SER 562  
147 1 Y 1 A SER 563  ? A SER 563  
148 1 Y 1 A LYS 564  ? A LYS 564  
149 1 Y 1 A ASP 565  ? A ASP 565  
150 1 Y 1 A LEU 566  ? A LEU 566  
151 1 Y 1 A LEU 567  ? A LEU 567  
152 1 Y 1 A ALA 568  ? A ALA 568  
153 1 Y 1 A ASN 569  ? A ASN 569  
154 1 Y 1 A ILE 570  ? A ILE 570  
155 1 Y 1 A ASN 571  ? A ASN 571  
156 1 Y 1 A ARG 572  ? A ARG 572  
157 1 Y 1 A ILE 573  ? A ILE 573  
158 1 Y 1 A ASP 574  ? A ASP 574  
159 1 Y 1 A ASP 737  ? A ASP 737  
160 1 Y 1 A GLU 738  ? A GLU 738  
161 1 Y 1 A GLN 739  ? A GLN 739  
162 1 Y 1 A HIS 740  ? A HIS 740  
163 1 Y 1 A GLU 741  ? A GLU 741  
164 1 Y 1 A ARG 742  ? A ARG 742  
165 1 Y 1 A GLN 743  ? A GLN 743  
166 1 Y 1 A ALA 744  ? A ALA 744  
167 1 Y 1 A ALA 745  ? A ALA 745  
168 1 Y 1 A GLU 746  ? A GLU 746  
169 1 Y 1 A ARG 747  ? A ARG 747  
170 1 Y 1 A GLU 748  ? A GLU 748  
171 1 Y 1 A HIS 749  ? A HIS 749  
172 1 Y 1 A GLN 750  ? A GLN 750  
173 1 Y 1 A LYS 751  ? A LYS 751  
174 1 Y 1 A SER 752  ? A SER 752  
175 1 Y 1 A LEU 753  ? A LEU 753  
176 1 Y 1 A ASN 754  ? A ASN 754  
177 1 Y 1 A GLN 755  ? A GLN 755  
178 1 Y 1 A LYS 756  ? A LYS 756  
179 1 Y 1 A SER 757  ? A SER 757  
180 1 Y 1 A SER 758  ? A SER 758  
181 1 Y 1 A LYS 759  ? A LYS 759  
182 1 Y 1 A VAL 760  ? A VAL 760  
183 1 Y 1 A LYS 761  ? A LYS 761  
184 1 Y 1 A SER 762  ? A SER 762  
185 1 Y 1 A HIS 763  ? A HIS 763  
186 1 Y 1 A LYS 764  ? A LYS 764  
187 1 Y 1 A GLU 765  ? A GLU 765  
188 1 Y 1 A LYS 766  ? A LYS 766  
189 1 Y 1 A ASN 767  ? A ASN 767  
190 1 Y 1 A ASP 768  ? A ASP 768  
191 1 Y 1 A ALA 769  ? A ALA 769  
192 1 Y 1 A PRO 770  ? A PRO 770  
193 1 Y 1 A VAL 771  ? A VAL 771  
194 1 Y 1 A VAL 772  ? A VAL 772  
195 1 Y 1 A PRO 773  ? A PRO 773  
196 1 Y 1 A VAL 774  ? A VAL 774  
197 1 Y 1 A TYR 775  ? A TYR 775  
198 1 Y 1 A ARG 776  ? A ARG 776  
199 1 Y 1 A SER 777  ? A SER 777  
200 1 Y 1 A LYS 778  ? A LYS 778  
201 1 Y 1 A GLU 779  ? A GLU 779  
202 1 Y 1 A GLU 780  ? A GLU 780  
203 1 Y 1 A LYS 781  ? A LYS 781  
204 1 Y 1 A ALA 782  ? A ALA 782  
205 1 Y 1 A VAL 783  ? A VAL 783  
206 1 Y 1 A SER 784  ? A SER 784  
207 1 Y 1 A ASN 785  ? A ASN 785  
208 1 Y 1 A ASP 786  ? A ASP 786  
209 1 Y 1 A GLU 787  ? A GLU 787  
210 1 Y 1 A GLU 788  ? A GLU 788  
211 1 Y 1 A ALA 789  ? A ALA 789  
212 1 Y 1 A ARG 790  ? A ARG 790  
213 1 Y 1 A VAL 791  ? A VAL 791  
214 1 Y 1 A GLY 792  ? A GLY 792  
215 1 Y 1 A THR 793  ? A THR 793  
216 1 Y 1 A GLU 794  ? A GLU 794  
217 1 Y 1 A ASN 795  ? A ASN 795  
218 1 Y 1 A GLU 796  ? A GLU 796  
219 1 Y 1 A GLU 797  ? A GLU 797  
220 1 Y 1 A GLU 798  ? A GLU 798  
221 1 Y 1 A ASP 799  ? A ASP 799  
222 1 Y 1 A PHE 800  ? A PHE 800  
223 1 Y 1 A GLN 801  ? A GLN 801  
224 1 Y 1 A LEU 802  ? A LEU 802  
225 1 Y 1 A GLU 803  ? A GLU 803  
226 1 Y 1 A ASP 804  ? A ASP 804  
227 1 Y 1 A TYR 805  ? A TYR 805  
228 1 Y 1 A ILE 806  ? A ILE 806  
229 1 Y 1 A PRO 807  ? A PRO 807  
230 1 Y 1 A GLU 808  ? A GLU 808  
231 1 Y 1 A ILE 809  ? A ILE 809  
232 1 Y 1 A ARG 810  ? A ARG 810  
233 1 Y 1 A GLU 811  ? A GLU 811  
234 1 Y 1 A ASP 812  ? A ASP 812  
235 1 Y 1 A ASP 813  ? A ASP 813  
236 1 Y 1 A SER 814  ? A SER 814  
237 1 Y 1 A MET 815  ? A MET 815  
238 1 Y 1 A GLU 816  ? A GLU 816  
239 1 Y 1 A VAL 817  ? A VAL 817  
240 1 Y 1 A ILE 818  ? A ILE 818  
241 1 Y 1 A MET 819  ? A MET 819  
242 1 Y 1 A ARG 820  ? A ARG 820  
243 1 Y 1 A ASN 821  ? A ASN 821  
244 1 Y 1 A LYS 822  ? A LYS 822  
245 1 Y 1 A LYS 823  ? A LYS 823  
246 1 Y 1 A LEU 824  ? A LEU 824  
247 1 Y 1 A GLY 825  ? A GLY 825  
248 1 Y 1 A ARG 1132 ? A ARG 1132 
249 1 Y 1 A TRP 1133 ? A TRP 1133 
250 1 Y 1 A VAL 1134 ? A VAL 1134 
251 1 Y 1 A TRP 1135 ? A TRP 1135 
252 1 Y 1 A ARG 1136 ? A ARG 1136 
253 1 Y 1 A MET 1137 ? A MET 1137 
254 1 Y 1 A CYS 1138 ? A CYS 1138 
255 1 Y 1 A ARG 1139 ? A ARG 1139 
256 1 Y 1 A CYS 1140 ? A CYS 1140 
257 1 Y 1 A GLY 1141 ? A GLY 1141 
258 1 Y 1 A HIS 1142 ? A HIS 1142 
259 1 Y 1 A PRO 1143 ? A PRO 1143 
260 1 Y 1 A PRO 1144 ? A PRO 1144 
261 1 Y 1 A ARG 1145 ? A ARG 1145 
262 1 Y 1 A GLY 1146 ? A GLY 1146 
263 1 Y 1 A SER 1147 ? A SER 1147 
264 1 Y 1 A THR 1148 ? A THR 1148 
265 1 Y 1 A MET 1149 ? A MET 1149 
266 1 Y 1 A ASP 1207 ? A ASP 1207 
267 1 Y 1 A SER 1208 ? A SER 1208 
268 1 Y 1 A MET 1209 ? A MET 1209 
269 1 Y 1 A SER 1210 ? A SER 1210 
270 1 Y 1 A GLY 1211 ? A GLY 1211 
271 1 Y 1 A THR 1212 ? A THR 1212 
272 1 Y 1 A ARG 1213 ? A ARG 1213 
273 1 Y 1 A ALA 1214 ? A ALA 1214 
274 1 Y 1 A HIS 1215 ? A HIS 1215 
275 1 Y 1 A ALA 1216 ? A ALA 1216 
276 1 Y 1 A LEU 1217 ? A LEU 1217 
277 1 Y 1 A THR 1218 ? A THR 1218 
278 1 Y 1 A ASP 1219 ? A ASP 1219 
279 1 Y 1 A GLY 1220 ? A GLY 1220 
280 1 Y 1 A ASN 1221 ? A ASN 1221 
281 1 Y 1 A GLY 1222 ? A GLY 1222 
282 1 Y 1 A LEU 1223 ? A LEU 1223 
283 1 Y 1 A GLU 1224 ? A GLU 1224 
284 1 Y 1 A GLY 1225 ? A GLY 1225 
285 1 Y 1 A GLY 1226 ? A GLY 1226 
286 1 Y 1 A HIS 1227 ? A HIS 1227 
287 1 Y 1 A ASP 1228 ? A ASP 1228 
288 1 Y 1 A SER 1229 ? A SER 1229 
289 1 Y 1 A GLU 1230 ? A GLU 1230 
290 1 Y 1 A GLY 1231 ? A GLY 1231 
291 1 Y 1 A ARG 1232 ? A ARG 1232 
292 1 Y 1 A LEU 1233 ? A LEU 1233 
293 1 Y 1 A ALA 1234 ? A ALA 1234 
294 1 Y 1 A ARG 1235 ? A ARG 1235 
295 1 Y 1 A MET 1236 ? A MET 1236 
296 1 Y 1 A GLU 1237 ? A GLU 1237 
297 1 Y 1 A VAL 1238 ? A VAL 1238 
298 1 Y 1 A GLU 1239 ? A GLU 1239 
299 1 Y 1 A LEU 1240 ? A LEU 1240 
300 1 Y 1 A SER 1241 ? A SER 1241 
301 1 Y 1 A SER 1242 ? A SER 1242 
302 1 Y 1 A ASN 1243 ? A ASN 1243 
303 1 Y 1 A SER 1244 ? A SER 1244 
304 1 Y 1 A GLU 1245 ? A GLU 1245 
305 1 Y 1 A SER 1246 ? A SER 1246 
306 1 Y 1 A LEU 1247 ? A LEU 1247 
307 1 Y 1 A GLN 1248 ? A GLN 1248 
308 1 Y 1 A LYS 1249 ? A LYS 1249 
309 1 Y 1 A ILE 1250 ? A ILE 1250 
310 1 Y 1 A LEU 1251 ? A LEU 1251 
311 1 Y 1 A ALA 1252 ? A ALA 1252 
312 1 Y 1 A LEU 1253 ? A LEU 1253 
313 1 Y 1 A LEU 1254 ? A LEU 1254 
314 1 Y 1 A GLN 1255 ? A GLN 1255 
315 1 Y 1 A GLN 1256 ? A GLN 1256 
316 1 Y 1 A GLN 1257 ? A GLN 1257 
317 1 Y 1 A PRO 1258 ? A PRO 1258 
318 1 Y 1 A PRO 1259 ? A PRO 1259 
319 1 Y 1 A VAL 1260 ? A VAL 1260 
320 1 Y 1 A LYS 1261 ? A LYS 1261 
321 1 Y 1 A GLY 1262 ? A GLY 1262 
322 1 Y 1 A GLN 1263 ? A GLN 1263 
323 1 Y 1 A ALA 1264 ? A ALA 1264 
324 1 Y 1 A ALA 1265 ? A ALA 1265 
325 1 Y 1 A VAL 1266 ? A VAL 1266 
326 1 Y 1 A PRO 1267 ? A PRO 1267 
327 1 Y 1 A ILE 1268 ? A ILE 1268 
328 1 Y 1 A GLN 1269 ? A GLN 1269 
329 1 Y 1 A LEU 1270 ? A LEU 1270 
330 1 Y 1 A THR 1271 ? A THR 1271 
331 1 Y 1 A LEU 1272 ? A LEU 1272 
332 1 Y 1 A LEU 1273 ? A LEU 1273 
333 1 Y 1 A HIS 1274 ? A HIS 1274 
334 1 Y 1 A TYR 1275 ? A TYR 1275 
335 1 Y 1 A LYS 1276 ? A LYS 1276 
336 1 Y 1 A ALA 1277 ? A ALA 1277 
337 1 Y 1 A ARG 1278 ? A ARG 1278 
338 1 Y 1 A SER 1279 ? A SER 1279 
339 1 Y 1 A SER 1280 ? A SER 1280 
340 1 Y 1 A PRO 1281 ? A PRO 1281 
341 1 Y 1 A TYR 1282 ? A TYR 1282 
342 1 Y 1 A PRO 1283 ? A PRO 1283 
343 1 Y 1 A GLY 1284 ? A GLY 1284 
344 1 Y 1 A SER 1285 ? A SER 1285 
345 1 Y 1 A THR 1286 ? A THR 1286 
346 1 Y 1 A ALA 1287 ? A ALA 1287 
347 1 Y 1 A LYS 1288 ? A LYS 1288 
348 1 Y 1 A ARG 1289 ? A ARG 1289 
349 1 Y 1 A PHE 1290 ? A PHE 1290 
350 1 Y 1 A ALA 1291 ? A ALA 1291 
351 1 Y 1 A VAL 1292 ? A VAL 1292 
352 1 Y 1 A GLN 1293 ? A GLN 1293 
353 1 Y 1 A ASP 1294 ? A ASP 1294 
354 1 Y 1 A ASN 1295 ? A ASN 1295 
355 1 Y 1 A MET 1296 ? A MET 1296 
356 1 Y 1 A VAL 1297 ? A VAL 1297 
357 1 Y 1 A ASP 1298 ? A ASP 1298 
358 1 Y 1 A TRP 1299 ? A TRP 1299 
359 1 Y 1 A GLN 1300 ? A GLN 1300 
360 1 Y 1 A VAL 1301 ? A VAL 1301 
361 1 Y 1 A PRO 1302 ? A PRO 1302 
362 1 Y 1 A PHE 1303 ? A PHE 1303 
363 1 Y 1 A PRO 1304 ? A PRO 1304 
364 1 Y 1 A ASP 1305 ? A ASP 1305 
365 1 Y 1 A TYR 1306 ? A TYR 1306 
366 1 Y 1 A LYS 1307 ? A LYS 1307 
367 1 Y 1 A PRO 1308 ? A PRO 1308 
368 1 Y 1 A VAL 1309 ? A VAL 1309 
369 1 Y 1 A ASN 1310 ? A ASN 1310 
370 1 Y 1 A TYR 1311 ? A TYR 1311 
371 1 Y 1 A THR 1312 ? A THR 1312 
372 1 Y 1 A ALA 1313 ? A ALA 1313 
373 1 Y 1 A PRO 1314 ? A PRO 1314 
374 1 Y 1 A VAL 1315 ? A VAL 1315 
375 1 Y 1 A VAL 1316 ? A VAL 1316 
376 1 Y 1 A LEU 1317 ? A LEU 1317 
377 1 Y 1 A ALA 1318 ? A ALA 1318 
378 1 Y 1 A ASN 1319 ? A ASN 1319 
379 1 Y 1 A PRO 1320 ? A PRO 1320 
380 1 Y 1 A VAL 1321 ? A VAL 1321 
381 1 Y 1 A TRP 1322 ? A TRP 1322 
382 1 Y 1 A ALA 1323 ? A ALA 1323 
383 1 Y 1 A ASP 1324 ? A ASP 1324 
384 1 Y 1 A LYS 1325 ? A LYS 1325 
385 1 Y 1 A ASP 1326 ? A ASP 1326 
386 1 Y 1 A LEU 1327 ? A LEU 1327 
387 1 Y 1 A MET 1328 ? A MET 1328 
388 1 Y 1 A ALA 1329 ? A ALA 1329 
389 1 Y 1 A MET 1330 ? A MET 1330 
390 1 Y 1 A SER 1331 ? A SER 1331 
391 1 Y 1 A PRO 1332 ? A PRO 1332 
392 1 Y 1 A ARG 1333 ? A ARG 1333 
393 1 Y 1 A PRO 1334 ? A PRO 1334 
394 1 Y 1 A GLU 1335 ? A GLU 1335 
395 1 Y 1 A LEU 1336 ? A LEU 1336 
396 1 Y 1 A PRO 1337 ? A PRO 1337 
397 1 Y 1 A TYR 1338 ? A TYR 1338 
398 1 Y 1 A ASN 1339 ? A ASN 1339 
399 1 Y 1 A GLN 1340 ? A GLN 1340 
400 1 Y 1 A MET 1341 ? A MET 1341 
401 1 Y 1 A ASP 1342 ? A ASP 1342 
402 1 Y 1 A HIS 1343 ? A HIS 1343 
403 1 Y 1 A THR 1344 ? A THR 1344 
404 1 Y 1 A CYS 1345 ? A CYS 1345 
405 1 Y 1 A ASN 1346 ? A ASN 1346 
406 1 Y 1 A VAL 1347 ? A VAL 1347 
407 1 Y 1 A ASN 1348 ? A ASN 1348 
408 1 Y 1 A ARG 1349 ? A ARG 1349 
409 1 Y 1 A VAL 1350 ? A VAL 1350 
410 1 Y 1 A SER 1351 ? A SER 1351 
411 1 Y 1 A TYR 1352 ? A TYR 1352 
412 1 Y 1 A ASN 1353 ? A ASN 1353 
413 1 Y 1 A GLY 1354 ? A GLY 1354 
414 1 Y 1 A THR 1355 ? A THR 1355 
415 1 Y 1 A TYR 1356 ? A TYR 1356 
416 1 Y 1 A VAL 1357 ? A VAL 1357 
417 1 Y 1 A VAL 1358 ? A VAL 1358 
418 1 Y 1 A LYS 1359 ? A LYS 1359 
419 1 Y 1 A ASP 1360 ? A ASP 1360 
420 1 Y 1 A GLY 1361 ? A GLY 1361 
421 1 Y 1 A LEU 1362 ? A LEU 1362 
422 1 Y 1 A PRO 1363 ? A PRO 1363 
423 1 Y 1 A LEU 1364 ? A LEU 1364 
424 1 Y 1 A ASN 1365 ? A ASN 1365 
425 1 Y 1 A PRO 1366 ? A PRO 1366 
426 1 Y 1 A MET 1367 ? A MET 1367 
427 1 Y 1 A GLY 1368 ? A GLY 1368 
428 1 Y 1 A ARG 1369 ? A ARG 1369 
429 1 Y 1 A THR 1370 ? A THR 1370 
430 1 Y 1 A GLY 1371 ? A GLY 1371 
431 1 Y 1 A MET 1372 ? A MET 1372 
432 1 Y 1 A GLN 1373 ? A GLN 1373 
433 1 Y 1 A GLY 1374 ? A GLY 1374 
434 1 Y 1 A ARG 1375 ? A ARG 1375 
435 1 Y 1 A GLY 1376 ? A GLY 1376 
436 1 Y 1 A LEU 1377 ? A LEU 1377 
437 1 Y 1 A LEU 1378 ? A LEU 1378 
438 1 Y 1 A GLY 1379 ? A GLY 1379 
439 1 Y 1 A ARG 1380 ? A ARG 1380 
440 1 Y 1 A PHE 1381 ? A PHE 1381 
441 1 Y 1 A GLY 1382 ? A GLY 1382 
442 1 Y 1 A PRO 1383 ? A PRO 1383 
443 1 Y 1 A ASN 1384 ? A ASN 1384 
444 1 Y 1 A HIS 1385 ? A HIS 1385 
445 1 Y 1 A ALA 1386 ? A ALA 1386 
446 1 Y 1 A ALA 1387 ? A ALA 1387 
447 1 Y 1 A ASP 1388 ? A ASP 1388 
448 1 Y 1 A PRO 1389 ? A PRO 1389 
449 1 Y 1 A VAL 1390 ? A VAL 1390 
450 1 Y 1 A VAL 1391 ? A VAL 1391 
451 1 Y 1 A THR 1392 ? A THR 1392 
452 1 Y 1 A ARG 1393 ? A ARG 1393 
453 1 Y 1 A TRP 1394 ? A TRP 1394 
454 1 Y 1 A LYS 1395 ? A LYS 1395 
455 1 Y 1 A ARG 1396 ? A ARG 1396 
456 1 Y 1 A THR 1397 ? A THR 1397 
457 1 Y 1 A SER 1398 ? A SER 1398 
458 1 Y 1 A ALA 1399 ? A ALA 1399 
459 1 Y 1 A GLY 1400 ? A GLY 1400 
460 1 Y 1 A VAL 1401 ? A VAL 1401 
461 1 Y 1 A MET 1402 ? A MET 1402 
462 1 Y 1 A LEU 1403 ? A LEU 1403 
463 1 Y 1 A GLN 1404 ? A GLN 1404 
464 1 Y 1 A GLY 1405 ? A GLY 1405 
465 1 Y 1 A GLY 1406 ? A GLY 1406 
466 1 Y 1 A LYS 1407 ? A LYS 1407 
467 1 Y 1 A LYS 1408 ? A LYS 1408 
468 1 Y 1 A VAL 1409 ? A VAL 1409 
469 1 Y 1 A LEU 1410 ? A LEU 1410 
470 1 Y 1 A GLU 1411 ? A GLU 1411 
471 1 Y 1 A PHE 1412 ? A PHE 1412 
472 1 Y 1 A VAL 1413 ? A VAL 1413 
473 1 Y 1 A ALA 1414 ? A ALA 1414 
474 1 Y 1 A ILE 1415 ? A ILE 1415 
475 1 Y 1 A GLN 1416 ? A GLN 1416 
476 1 Y 1 A ARG 1417 ? A ARG 1417 
477 1 Y 1 A LYS 1418 ? A LYS 1418 
478 1 Y 1 A ASP 1419 ? A ASP 1419 
479 1 Y 1 A ASN 1420 ? A ASN 1420 
480 1 Y 1 A ASN 1421 ? A ASN 1421 
481 1 Y 1 A GLN 1422 ? A GLN 1422 
482 1 Y 1 A TRP 1423 ? A TRP 1423 
483 1 Y 1 A ALA 1424 ? A ALA 1424 
484 1 Y 1 A ILE 1425 ? A ILE 1425 
485 1 Y 1 A PRO 1426 ? A PRO 1426 
486 1 Y 1 A GLY 1427 ? A GLY 1427 
487 1 Y 1 A GLY 1428 ? A GLY 1428 
488 1 Y 1 A MET 1429 ? A MET 1429 
489 1 Y 1 A VAL 1430 ? A VAL 1430 
490 1 Y 1 A GLU 1431 ? A GLU 1431 
491 1 Y 1 A PRO 1432 ? A PRO 1432 
492 1 Y 1 A GLY 1433 ? A GLY 1433 
493 1 Y 1 A GLN 1434 ? A GLN 1434 
494 1 Y 1 A LEU 1435 ? A LEU 1435 
495 1 Y 1 A VAL 1436 ? A VAL 1436 
496 1 Y 1 A THR 1437 ? A THR 1437 
497 1 Y 1 A GLN 1438 ? A GLN 1438 
498 1 Y 1 A ALA 1439 ? A ALA 1439 
499 1 Y 1 A LEU 1440 ? A LEU 1440 
500 1 Y 1 A LYS 1441 ? A LYS 1441 
501 1 Y 1 A ALA 1442 ? A ALA 1442 
502 1 Y 1 A GLU 1443 ? A GLU 1443 
503 1 Y 1 A PHE 1444 ? A PHE 1444 
504 1 Y 1 A GLY 1445 ? A GLY 1445 
505 1 Y 1 A GLU 1446 ? A GLU 1446 
506 1 Y 1 A GLU 1447 ? A GLU 1447 
507 1 Y 1 A ALA 1448 ? A ALA 1448 
508 1 Y 1 A MET 1449 ? A MET 1449 
509 1 Y 1 A ALA 1450 ? A ALA 1450 
510 1 Y 1 A LYS 1451 ? A LYS 1451 
511 1 Y 1 A LEU 1452 ? A LEU 1452 
512 1 Y 1 A ASN 1453 ? A ASN 1453 
513 1 Y 1 A VAL 1454 ? A VAL 1454 
514 1 Y 1 A SER 1455 ? A SER 1455 
515 1 Y 1 A GLN 1456 ? A GLN 1456 
516 1 Y 1 A GLU 1457 ? A GLU 1457 
517 1 Y 1 A GLU 1458 ? A GLU 1458 
518 1 Y 1 A LYS 1459 ? A LYS 1459 
519 1 Y 1 A GLU 1460 ? A GLU 1460 
520 1 Y 1 A ARG 1461 ? A ARG 1461 
521 1 Y 1 A ILE 1462 ? A ILE 1462 
522 1 Y 1 A ALA 1463 ? A ALA 1463 
523 1 Y 1 A LYS 1464 ? A LYS 1464 
524 1 Y 1 A GLN 1465 ? A GLN 1465 
525 1 Y 1 A ILE 1466 ? A ILE 1466 
526 1 Y 1 A GLU 1467 ? A GLU 1467 
527 1 Y 1 A ARG 1468 ? A ARG 1468 
528 1 Y 1 A LEU 1469 ? A LEU 1469 
529 1 Y 1 A PHE 1470 ? A PHE 1470 
530 1 Y 1 A GLN 1471 ? A GLN 1471 
531 1 Y 1 A GLN 1472 ? A GLN 1472 
532 1 Y 1 A GLY 1473 ? A GLY 1473 
533 1 Y 1 A GLN 1474 ? A GLN 1474 
534 1 Y 1 A GLU 1475 ? A GLU 1475 
535 1 Y 1 A ILE 1476 ? A ILE 1476 
536 1 Y 1 A TYR 1477 ? A TYR 1477 
537 1 Y 1 A LYS 1478 ? A LYS 1478 
538 1 Y 1 A GLY 1479 ? A GLY 1479 
539 1 Y 1 A TYR 1480 ? A TYR 1480 
540 1 Y 1 A VAL 1481 ? A VAL 1481 
541 1 Y 1 A ASP 1482 ? A ASP 1482 
542 1 Y 1 A ASP 1483 ? A ASP 1483 
543 1 Y 1 A PRO 1484 ? A PRO 1484 
544 1 Y 1 A ARG 1485 ? A ARG 1485 
545 1 Y 1 A ASN 1486 ? A ASN 1486 
546 1 Y 1 A THR 1487 ? A THR 1487 
547 1 Y 1 A ASP 1488 ? A ASP 1488 
548 1 Y 1 A ASN 1489 ? A ASN 1489 
549 1 Y 1 A ALA 1490 ? A ALA 1490 
550 1 Y 1 A TRP 1491 ? A TRP 1491 
551 1 Y 1 A MET 1492 ? A MET 1492 
552 1 Y 1 A GLU 1493 ? A GLU 1493 
553 1 Y 1 A THR 1494 ? A THR 1494 
554 1 Y 1 A VAL 1495 ? A VAL 1495 
555 1 Y 1 A ALA 1496 ? A ALA 1496 
556 1 Y 1 A VAL 1497 ? A VAL 1497 
557 1 Y 1 A ASN 1498 ? A ASN 1498 
558 1 Y 1 A PHE 1499 ? A PHE 1499 
559 1 Y 1 A HIS 1500 ? A HIS 1500 
560 1 Y 1 A ASP 1501 ? A ASP 1501 
561 1 Y 1 A ASP 1502 ? A ASP 1502 
562 1 Y 1 A LYS 1503 ? A LYS 1503 
563 1 Y 1 A GLY 1504 ? A GLY 1504 
564 1 Y 1 A ASP 1505 ? A ASP 1505 
565 1 Y 1 A LEU 1506 ? A LEU 1506 
566 1 Y 1 A PHE 1507 ? A PHE 1507 
567 1 Y 1 A GLY 1508 ? A GLY 1508 
568 1 Y 1 A ASP 1509 ? A ASP 1509 
569 1 Y 1 A ILE 1510 ? A ILE 1510 
570 1 Y 1 A THR 1511 ? A THR 1511 
571 1 Y 1 A LEU 1512 ? A LEU 1512 
572 1 Y 1 A GLN 1513 ? A GLN 1513 
573 1 Y 1 A ALA 1514 ? A ALA 1514 
574 1 Y 1 A GLY 1515 ? A GLY 1515 
575 1 Y 1 A ASP 1516 ? A ASP 1516 
576 1 Y 1 A ASP 1517 ? A ASP 1517 
577 1 Y 1 A ALA 1518 ? A ALA 1518 
578 1 Y 1 A ALA 1519 ? A ALA 1519 
579 1 Y 1 A ALA 1520 ? A ALA 1520 
580 1 Y 1 A VAL 1521 ? A VAL 1521 
581 1 Y 1 A ARG 1522 ? A ARG 1522 
582 1 Y 1 A TRP 1523 ? A TRP 1523 
583 1 Y 1 A GLN 1524 ? A GLN 1524 
584 1 Y 1 A ARG 1525 ? A ARG 1525 
585 1 Y 1 A VAL 1526 ? A VAL 1526 
586 1 Y 1 A SER 1527 ? A SER 1527 
587 1 Y 1 A GLY 1528 ? A GLY 1528 
588 1 Y 1 A ASN 1529 ? A ASN 1529 
589 1 Y 1 A ILE 1530 ? A ILE 1530 
590 1 Y 1 A PRO 1531 ? A PRO 1531 
591 1 Y 1 A LEU 1532 ? A LEU 1532 
592 1 Y 1 A TYR 1533 ? A TYR 1533 
593 1 Y 1 A ALA 1534 ? A ALA 1534 
594 1 Y 1 A SER 1535 ? A SER 1535 
595 1 Y 1 A HIS 1536 ? A HIS 1536 
596 1 Y 1 A VAL 1537 ? A VAL 1537 
597 1 Y 1 A SER 1538 ? A SER 1538 
598 1 Y 1 A ILE 1539 ? A ILE 1539 
599 1 Y 1 A LEU 1540 ? A LEU 1540 
600 1 Y 1 A GLU 1541 ? A GLU 1541 
601 1 Y 1 A LYS 1542 ? A LYS 1542 
602 1 Y 1 A VAL 1543 ? A VAL 1543 
603 1 Y 1 A ALA 1544 ? A ALA 1544 
604 1 Y 1 A LYS 1545 ? A LYS 1545 
605 1 Y 1 A MET 1546 ? A MET 1546 
606 1 Y 1 A ARG 1547 ? A ARG 1547 
607 1 Y 1 A ASP 1548 ? A ASP 1548 
608 1 Y 1 A ALA 1549 ? A ALA 1549 
609 1 Y 1 A ALA 1550 ? A ALA 1550 
610 1 Y 1 A PHE 1551 ? A PHE 1551 
611 1 Y 1 A SER 1552 ? A SER 1552 
612 1 Y 1 A ASN 1553 ? A ASN 1553 
613 1 Y 1 A SER 1554 ? A SER 1554 
614 1 Y 1 A LEU 1555 ? A LEU 1555 
615 1 Y 1 A GLU 1556 ? A GLU 1556 
616 1 Y 1 A VAL 1557 ? A VAL 1557 
617 1 Y 1 A LEU 1558 ? A LEU 1558 
618 1 Y 1 A PHE 1559 ? A PHE 1559 
619 1 Y 1 A GLN 1560 ? A GLN 1560 
# 
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 
A2R OP3    O  N N 1   
A2R "P2'"  P  N N 2   
A2R OP1    O  N N 3   
A2R OP2    O  N N 4   
A2R "O2'"  O  N N 5   
A2R "C2'"  C  N R 6   
A2R "C1'"  C  N R 7   
A2R N9     N  Y N 8   
A2R C4     C  Y N 9   
A2R N3     N  Y N 10  
A2R C2     C  Y N 11  
A2R N1     N  Y N 12  
A2R C6     C  Y N 13  
A2R N6     N  N N 14  
A2R C5     C  Y N 15  
A2R N7     N  Y N 16  
A2R C8     C  Y N 17  
A2R "O4'"  O  N N 18  
A2R "C3'"  C  N R 19  
A2R "O3'"  O  N N 20  
A2R "C4'"  C  N R 21  
A2R "C5'"  C  N N 22  
A2R "O5'"  O  N N 23  
A2R P      P  N S 24  
A2R O1     O  N N 25  
A2R O2     O  N N 26  
A2R O3     O  N N 27  
A2R P1     P  N S 28  
A2R O11    O  N N 29  
A2R O12    O  N N 30  
A2R "O15'" O  N N 31  
A2R "C15'" C  N N 32  
A2R "C14'" C  N R 33  
A2R "C13'" C  N S 34  
A2R "O13'" O  N N 35  
A2R "C12'" C  N R 36  
A2R "O12'" O  N N 37  
A2R "C11'" C  N R 38  
A2R "O14'" O  N N 39  
A2R "O11'" O  N N 40  
A2R HOP3   H  N N 41  
A2R HOP1   H  N N 42  
A2R "H2'"  H  N N 43  
A2R "H1'"  H  N N 44  
A2R H2     H  N N 45  
A2R HN61   H  N N 46  
A2R HN62   H  N N 47  
A2R H8     H  N N 48  
A2R "H3'"  H  N N 49  
A2R "HO3'" H  N N 50  
A2R "H4'"  H  N N 51  
A2R "H5'1" H  N N 52  
A2R "H5'2" H  N N 53  
A2R HO2    H  N N 54  
A2R HO11   H  N N 55  
A2R "H5'3" H  N N 56  
A2R "H5'4" H  N N 57  
A2R "H14'" H  N N 58  
A2R "H13'" H  N N 59  
A2R "H16'" H  N N 60  
A2R "H12'" H  N N 61  
A2R "H15'" H  N N 62  
A2R "H11'" H  N N 63  
A2R "H17'" H  N N 64  
ALA N      N  N N 65  
ALA CA     C  N S 66  
ALA C      C  N N 67  
ALA O      O  N N 68  
ALA CB     C  N N 69  
ALA OXT    O  N N 70  
ALA H      H  N N 71  
ALA H2     H  N N 72  
ALA HA     H  N N 73  
ALA HB1    H  N N 74  
ALA HB2    H  N N 75  
ALA HB3    H  N N 76  
ALA HXT    H  N N 77  
ARG N      N  N N 78  
ARG CA     C  N S 79  
ARG C      C  N N 80  
ARG O      O  N N 81  
ARG CB     C  N N 82  
ARG CG     C  N N 83  
ARG CD     C  N N 84  
ARG NE     N  N N 85  
ARG CZ     C  N N 86  
ARG NH1    N  N N 87  
ARG NH2    N  N N 88  
ARG OXT    O  N N 89  
ARG H      H  N N 90  
ARG H2     H  N N 91  
ARG HA     H  N N 92  
ARG HB2    H  N N 93  
ARG HB3    H  N N 94  
ARG HG2    H  N N 95  
ARG HG3    H  N N 96  
ARG HD2    H  N N 97  
ARG HD3    H  N N 98  
ARG HE     H  N N 99  
ARG HH11   H  N N 100 
ARG HH12   H  N N 101 
ARG HH21   H  N N 102 
ARG HH22   H  N N 103 
ARG HXT    H  N N 104 
ASN N      N  N N 105 
ASN CA     C  N S 106 
ASN C      C  N N 107 
ASN O      O  N N 108 
ASN CB     C  N N 109 
ASN CG     C  N N 110 
ASN OD1    O  N N 111 
ASN ND2    N  N N 112 
ASN OXT    O  N N 113 
ASN H      H  N N 114 
ASN H2     H  N N 115 
ASN HA     H  N N 116 
ASN HB2    H  N N 117 
ASN HB3    H  N N 118 
ASN HD21   H  N N 119 
ASN HD22   H  N N 120 
ASN HXT    H  N N 121 
ASP N      N  N N 122 
ASP CA     C  N S 123 
ASP C      C  N N 124 
ASP O      O  N N 125 
ASP CB     C  N N 126 
ASP CG     C  N N 127 
ASP OD1    O  N N 128 
ASP OD2    O  N N 129 
ASP OXT    O  N N 130 
ASP H      H  N N 131 
ASP H2     H  N N 132 
ASP HA     H  N N 133 
ASP HB2    H  N N 134 
ASP HB3    H  N N 135 
ASP HD2    H  N N 136 
ASP HXT    H  N N 137 
CA  CA     CA N N 138 
CYS N      N  N N 139 
CYS CA     C  N R 140 
CYS C      C  N N 141 
CYS O      O  N N 142 
CYS CB     C  N N 143 
CYS SG     S  N N 144 
CYS OXT    O  N N 145 
CYS H      H  N N 146 
CYS H2     H  N N 147 
CYS HA     H  N N 148 
CYS HB2    H  N N 149 
CYS HB3    H  N N 150 
CYS HG     H  N N 151 
CYS HXT    H  N N 152 
GLN N      N  N N 153 
GLN CA     C  N S 154 
GLN C      C  N N 155 
GLN O      O  N N 156 
GLN CB     C  N N 157 
GLN CG     C  N N 158 
GLN CD     C  N N 159 
GLN OE1    O  N N 160 
GLN NE2    N  N N 161 
GLN OXT    O  N N 162 
GLN H      H  N N 163 
GLN H2     H  N N 164 
GLN HA     H  N N 165 
GLN HB2    H  N N 166 
GLN HB3    H  N N 167 
GLN HG2    H  N N 168 
GLN HG3    H  N N 169 
GLN HE21   H  N N 170 
GLN HE22   H  N N 171 
GLN HXT    H  N N 172 
GLU N      N  N N 173 
GLU CA     C  N S 174 
GLU C      C  N N 175 
GLU O      O  N N 176 
GLU CB     C  N N 177 
GLU CG     C  N N 178 
GLU CD     C  N N 179 
GLU OE1    O  N N 180 
GLU OE2    O  N N 181 
GLU OXT    O  N N 182 
GLU H      H  N N 183 
GLU H2     H  N N 184 
GLU HA     H  N N 185 
GLU HB2    H  N N 186 
GLU HB3    H  N N 187 
GLU HG2    H  N N 188 
GLU HG3    H  N N 189 
GLU HE2    H  N N 190 
GLU HXT    H  N N 191 
GLY N      N  N N 192 
GLY CA     C  N N 193 
GLY C      C  N N 194 
GLY O      O  N N 195 
GLY OXT    O  N N 196 
GLY H      H  N N 197 
GLY H2     H  N N 198 
GLY HA2    H  N N 199 
GLY HA3    H  N N 200 
GLY HXT    H  N N 201 
HIS N      N  N N 202 
HIS CA     C  N S 203 
HIS C      C  N N 204 
HIS O      O  N N 205 
HIS CB     C  N N 206 
HIS CG     C  Y N 207 
HIS ND1    N  Y N 208 
HIS CD2    C  Y N 209 
HIS CE1    C  Y N 210 
HIS NE2    N  Y N 211 
HIS OXT    O  N N 212 
HIS H      H  N N 213 
HIS H2     H  N N 214 
HIS HA     H  N N 215 
HIS HB2    H  N N 216 
HIS HB3    H  N N 217 
HIS HD1    H  N N 218 
HIS HD2    H  N N 219 
HIS HE1    H  N N 220 
HIS HE2    H  N N 221 
HIS HXT    H  N N 222 
ILE N      N  N N 223 
ILE CA     C  N S 224 
ILE C      C  N N 225 
ILE O      O  N N 226 
ILE CB     C  N S 227 
ILE CG1    C  N N 228 
ILE CG2    C  N N 229 
ILE CD1    C  N N 230 
ILE OXT    O  N N 231 
ILE H      H  N N 232 
ILE H2     H  N N 233 
ILE HA     H  N N 234 
ILE HB     H  N N 235 
ILE HG12   H  N N 236 
ILE HG13   H  N N 237 
ILE HG21   H  N N 238 
ILE HG22   H  N N 239 
ILE HG23   H  N N 240 
ILE HD11   H  N N 241 
ILE HD12   H  N N 242 
ILE HD13   H  N N 243 
ILE HXT    H  N N 244 
LEU N      N  N N 245 
LEU CA     C  N S 246 
LEU C      C  N N 247 
LEU O      O  N N 248 
LEU CB     C  N N 249 
LEU CG     C  N N 250 
LEU CD1    C  N N 251 
LEU CD2    C  N N 252 
LEU OXT    O  N N 253 
LEU H      H  N N 254 
LEU H2     H  N N 255 
LEU HA     H  N N 256 
LEU HB2    H  N N 257 
LEU HB3    H  N N 258 
LEU HG     H  N N 259 
LEU HD11   H  N N 260 
LEU HD12   H  N N 261 
LEU HD13   H  N N 262 
LEU HD21   H  N N 263 
LEU HD22   H  N N 264 
LEU HD23   H  N N 265 
LEU HXT    H  N N 266 
LYS N      N  N N 267 
LYS CA     C  N S 268 
LYS C      C  N N 269 
LYS O      O  N N 270 
LYS CB     C  N N 271 
LYS CG     C  N N 272 
LYS CD     C  N N 273 
LYS CE     C  N N 274 
LYS NZ     N  N N 275 
LYS OXT    O  N N 276 
LYS H      H  N N 277 
LYS H2     H  N N 278 
LYS HA     H  N N 279 
LYS HB2    H  N N 280 
LYS HB3    H  N N 281 
LYS HG2    H  N N 282 
LYS HG3    H  N N 283 
LYS HD2    H  N N 284 
LYS HD3    H  N N 285 
LYS HE2    H  N N 286 
LYS HE3    H  N N 287 
LYS HZ1    H  N N 288 
LYS HZ2    H  N N 289 
LYS HZ3    H  N N 290 
LYS HXT    H  N N 291 
MET N      N  N N 292 
MET CA     C  N S 293 
MET C      C  N N 294 
MET O      O  N N 295 
MET CB     C  N N 296 
MET CG     C  N N 297 
MET SD     S  N N 298 
MET CE     C  N N 299 
MET OXT    O  N N 300 
MET H      H  N N 301 
MET H2     H  N N 302 
MET HA     H  N N 303 
MET HB2    H  N N 304 
MET HB3    H  N N 305 
MET HG2    H  N N 306 
MET HG3    H  N N 307 
MET HE1    H  N N 308 
MET HE2    H  N N 309 
MET HE3    H  N N 310 
MET HXT    H  N N 311 
NAG C1     C  N R 312 
NAG C2     C  N R 313 
NAG C3     C  N R 314 
NAG C4     C  N S 315 
NAG C5     C  N R 316 
NAG C6     C  N N 317 
NAG C7     C  N N 318 
NAG C8     C  N N 319 
NAG N2     N  N N 320 
NAG O1     O  N N 321 
NAG O3     O  N N 322 
NAG O4     O  N N 323 
NAG O5     O  N N 324 
NAG O6     O  N N 325 
NAG O7     O  N N 326 
NAG H1     H  N N 327 
NAG H2     H  N N 328 
NAG H3     H  N N 329 
NAG H4     H  N N 330 
NAG H5     H  N N 331 
NAG H61    H  N N 332 
NAG H62    H  N N 333 
NAG H81    H  N N 334 
NAG H82    H  N N 335 
NAG H83    H  N N 336 
NAG HN2    H  N N 337 
NAG HO1    H  N N 338 
NAG HO3    H  N N 339 
NAG HO4    H  N N 340 
NAG HO6    H  N N 341 
PHE N      N  N N 342 
PHE CA     C  N S 343 
PHE C      C  N N 344 
PHE O      O  N N 345 
PHE CB     C  N N 346 
PHE CG     C  Y N 347 
PHE CD1    C  Y N 348 
PHE CD2    C  Y N 349 
PHE CE1    C  Y N 350 
PHE CE2    C  Y N 351 
PHE CZ     C  Y N 352 
PHE OXT    O  N N 353 
PHE H      H  N N 354 
PHE H2     H  N N 355 
PHE HA     H  N N 356 
PHE HB2    H  N N 357 
PHE HB3    H  N N 358 
PHE HD1    H  N N 359 
PHE HD2    H  N N 360 
PHE HE1    H  N N 361 
PHE HE2    H  N N 362 
PHE HZ     H  N N 363 
PHE HXT    H  N N 364 
PRO N      N  N N 365 
PRO CA     C  N S 366 
PRO C      C  N N 367 
PRO O      O  N N 368 
PRO CB     C  N N 369 
PRO CG     C  N N 370 
PRO CD     C  N N 371 
PRO OXT    O  N N 372 
PRO H      H  N N 373 
PRO HA     H  N N 374 
PRO HB2    H  N N 375 
PRO HB3    H  N N 376 
PRO HG2    H  N N 377 
PRO HG3    H  N N 378 
PRO HD2    H  N N 379 
PRO HD3    H  N N 380 
PRO HXT    H  N N 381 
SER N      N  N N 382 
SER CA     C  N S 383 
SER C      C  N N 384 
SER O      O  N N 385 
SER CB     C  N N 386 
SER OG     O  N N 387 
SER OXT    O  N N 388 
SER H      H  N N 389 
SER H2     H  N N 390 
SER HA     H  N N 391 
SER HB2    H  N N 392 
SER HB3    H  N N 393 
SER HG     H  N N 394 
SER HXT    H  N N 395 
THR N      N  N N 396 
THR CA     C  N S 397 
THR C      C  N N 398 
THR O      O  N N 399 
THR CB     C  N R 400 
THR OG1    O  N N 401 
THR CG2    C  N N 402 
THR OXT    O  N N 403 
THR H      H  N N 404 
THR H2     H  N N 405 
THR HA     H  N N 406 
THR HB     H  N N 407 
THR HG1    H  N N 408 
THR HG21   H  N N 409 
THR HG22   H  N N 410 
THR HG23   H  N N 411 
THR HXT    H  N N 412 
TRP N      N  N N 413 
TRP CA     C  N S 414 
TRP C      C  N N 415 
TRP O      O  N N 416 
TRP CB     C  N N 417 
TRP CG     C  Y N 418 
TRP CD1    C  Y N 419 
TRP CD2    C  Y N 420 
TRP NE1    N  Y N 421 
TRP CE2    C  Y N 422 
TRP CE3    C  Y N 423 
TRP CZ2    C  Y N 424 
TRP CZ3    C  Y N 425 
TRP CH2    C  Y N 426 
TRP OXT    O  N N 427 
TRP H      H  N N 428 
TRP H2     H  N N 429 
TRP HA     H  N N 430 
TRP HB2    H  N N 431 
TRP HB3    H  N N 432 
TRP HD1    H  N N 433 
TRP HE1    H  N N 434 
TRP HE3    H  N N 435 
TRP HZ2    H  N N 436 
TRP HZ3    H  N N 437 
TRP HH2    H  N N 438 
TRP HXT    H  N N 439 
TYR N      N  N N 440 
TYR CA     C  N S 441 
TYR C      C  N N 442 
TYR O      O  N N 443 
TYR CB     C  N N 444 
TYR CG     C  Y N 445 
TYR CD1    C  Y N 446 
TYR CD2    C  Y N 447 
TYR CE1    C  Y N 448 
TYR CE2    C  Y N 449 
TYR CZ     C  Y N 450 
TYR OH     O  N N 451 
TYR OXT    O  N N 452 
TYR H      H  N N 453 
TYR H2     H  N N 454 
TYR HA     H  N N 455 
TYR HB2    H  N N 456 
TYR HB3    H  N N 457 
TYR HD1    H  N N 458 
TYR HD2    H  N N 459 
TYR HE1    H  N N 460 
TYR HE2    H  N N 461 
TYR HH     H  N N 462 
TYR HXT    H  N N 463 
VAL N      N  N N 464 
VAL CA     C  N S 465 
VAL C      C  N N 466 
VAL O      O  N N 467 
VAL CB     C  N N 468 
VAL CG1    C  N N 469 
VAL CG2    C  N N 470 
VAL OXT    O  N N 471 
VAL H      H  N N 472 
VAL H2     H  N N 473 
VAL HA     H  N N 474 
VAL HB     H  N N 475 
VAL HG11   H  N N 476 
VAL HG12   H  N N 477 
VAL HG13   H  N N 478 
VAL HG21   H  N N 479 
VAL HG22   H  N N 480 
VAL HG23   H  N N 481 
VAL HXT    H  N N 482 
# 
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 
A2R OP3    "P2'"  sing N N 1   
A2R OP3    HOP3   sing N N 2   
A2R "P2'"  OP2    doub N N 3   
A2R "P2'"  OP1    sing N N 4   
A2R "P2'"  "O2'"  sing N N 5   
A2R OP1    HOP1   sing N N 6   
A2R "O2'"  "C2'"  sing N N 7   
A2R "C2'"  "C1'"  sing N N 8   
A2R "C2'"  "C3'"  sing N N 9   
A2R "C2'"  "H2'"  sing N N 10  
A2R "C1'"  N9     sing N N 11  
A2R "C1'"  "O4'"  sing N N 12  
A2R "C1'"  "H1'"  sing N N 13  
A2R N9     C4     sing Y N 14  
A2R N9     C8     sing Y N 15  
A2R C4     C5     doub Y N 16  
A2R C4     N3     sing Y N 17  
A2R N3     C2     doub Y N 18  
A2R C2     N1     sing Y N 19  
A2R C2     H2     sing N N 20  
A2R N1     C6     doub Y N 21  
A2R C6     N6     sing N N 22  
A2R C6     C5     sing Y N 23  
A2R N6     HN61   sing N N 24  
A2R N6     HN62   sing N N 25  
A2R C5     N7     sing Y N 26  
A2R N7     C8     doub Y N 27  
A2R C8     H8     sing N N 28  
A2R "O4'"  "C4'"  sing N N 29  
A2R "C3'"  "C4'"  sing N N 30  
A2R "C3'"  "O3'"  sing N N 31  
A2R "C3'"  "H3'"  sing N N 32  
A2R "O3'"  "HO3'" sing N N 33  
A2R "C4'"  "C5'"  sing N N 34  
A2R "C4'"  "H4'"  sing N N 35  
A2R "C5'"  "O5'"  sing N N 36  
A2R "C5'"  "H5'1" sing N N 37  
A2R "C5'"  "H5'2" sing N N 38  
A2R "O5'"  P      sing N N 39  
A2R P      O1     doub N N 40  
A2R P      O3     sing N N 41  
A2R P      O2     sing N N 42  
A2R O2     HO2    sing N N 43  
A2R O3     P1     sing N N 44  
A2R P1     "O15'" sing N N 45  
A2R P1     O12    doub N N 46  
A2R P1     O11    sing N N 47  
A2R O11    HO11   sing N N 48  
A2R "O15'" "C15'" sing N N 49  
A2R "C15'" "C14'" sing N N 50  
A2R "C15'" "H5'3" sing N N 51  
A2R "C15'" "H5'4" sing N N 52  
A2R "C14'" "C13'" sing N N 53  
A2R "C14'" "O14'" sing N N 54  
A2R "C14'" "H14'" sing N N 55  
A2R "C13'" "O13'" sing N N 56  
A2R "C13'" "C12'" sing N N 57  
A2R "C13'" "H13'" sing N N 58  
A2R "O13'" "H16'" sing N N 59  
A2R "C12'" "O12'" sing N N 60  
A2R "C12'" "C11'" sing N N 61  
A2R "C12'" "H12'" sing N N 62  
A2R "O12'" "H15'" sing N N 63  
A2R "C11'" "O14'" sing N N 64  
A2R "C11'" "O11'" sing N N 65  
A2R "C11'" "H11'" sing N N 66  
A2R "O11'" "H17'" sing N N 67  
ALA N      CA     sing N N 68  
ALA N      H      sing N N 69  
ALA N      H2     sing N N 70  
ALA CA     C      sing N N 71  
ALA CA     CB     sing N N 72  
ALA CA     HA     sing N N 73  
ALA C      O      doub N N 74  
ALA C      OXT    sing N N 75  
ALA CB     HB1    sing N N 76  
ALA CB     HB2    sing N N 77  
ALA CB     HB3    sing N N 78  
ALA OXT    HXT    sing N N 79  
ARG N      CA     sing N N 80  
ARG N      H      sing N N 81  
ARG N      H2     sing N N 82  
ARG CA     C      sing N N 83  
ARG CA     CB     sing N N 84  
ARG CA     HA     sing N N 85  
ARG C      O      doub N N 86  
ARG C      OXT    sing N N 87  
ARG CB     CG     sing N N 88  
ARG CB     HB2    sing N N 89  
ARG CB     HB3    sing N N 90  
ARG CG     CD     sing N N 91  
ARG CG     HG2    sing N N 92  
ARG CG     HG3    sing N N 93  
ARG CD     NE     sing N N 94  
ARG CD     HD2    sing N N 95  
ARG CD     HD3    sing N N 96  
ARG NE     CZ     sing N N 97  
ARG NE     HE     sing N N 98  
ARG CZ     NH1    sing N N 99  
ARG CZ     NH2    doub N N 100 
ARG NH1    HH11   sing N N 101 
ARG NH1    HH12   sing N N 102 
ARG NH2    HH21   sing N N 103 
ARG NH2    HH22   sing N N 104 
ARG OXT    HXT    sing N N 105 
ASN N      CA     sing N N 106 
ASN N      H      sing N N 107 
ASN N      H2     sing N N 108 
ASN CA     C      sing N N 109 
ASN CA     CB     sing N N 110 
ASN CA     HA     sing N N 111 
ASN C      O      doub N N 112 
ASN C      OXT    sing N N 113 
ASN CB     CG     sing N N 114 
ASN CB     HB2    sing N N 115 
ASN CB     HB3    sing N N 116 
ASN CG     OD1    doub N N 117 
ASN CG     ND2    sing N N 118 
ASN ND2    HD21   sing N N 119 
ASN ND2    HD22   sing N N 120 
ASN OXT    HXT    sing N N 121 
ASP N      CA     sing N N 122 
ASP N      H      sing N N 123 
ASP N      H2     sing N N 124 
ASP CA     C      sing N N 125 
ASP CA     CB     sing N N 126 
ASP CA     HA     sing N N 127 
ASP C      O      doub N N 128 
ASP C      OXT    sing N N 129 
ASP CB     CG     sing N N 130 
ASP CB     HB2    sing N N 131 
ASP CB     HB3    sing N N 132 
ASP CG     OD1    doub N N 133 
ASP CG     OD2    sing N N 134 
ASP OD2    HD2    sing N N 135 
ASP OXT    HXT    sing N N 136 
CYS N      CA     sing N N 137 
CYS N      H      sing N N 138 
CYS N      H2     sing N N 139 
CYS CA     C      sing N N 140 
CYS CA     CB     sing N N 141 
CYS CA     HA     sing N N 142 
CYS C      O      doub N N 143 
CYS C      OXT    sing N N 144 
CYS CB     SG     sing N N 145 
CYS CB     HB2    sing N N 146 
CYS CB     HB3    sing N N 147 
CYS SG     HG     sing N N 148 
CYS OXT    HXT    sing N N 149 
GLN N      CA     sing N N 150 
GLN N      H      sing N N 151 
GLN N      H2     sing N N 152 
GLN CA     C      sing N N 153 
GLN CA     CB     sing N N 154 
GLN CA     HA     sing N N 155 
GLN C      O      doub N N 156 
GLN C      OXT    sing N N 157 
GLN CB     CG     sing N N 158 
GLN CB     HB2    sing N N 159 
GLN CB     HB3    sing N N 160 
GLN CG     CD     sing N N 161 
GLN CG     HG2    sing N N 162 
GLN CG     HG3    sing N N 163 
GLN CD     OE1    doub N N 164 
GLN CD     NE2    sing N N 165 
GLN NE2    HE21   sing N N 166 
GLN NE2    HE22   sing N N 167 
GLN OXT    HXT    sing N N 168 
GLU N      CA     sing N N 169 
GLU N      H      sing N N 170 
GLU N      H2     sing N N 171 
GLU CA     C      sing N N 172 
GLU CA     CB     sing N N 173 
GLU CA     HA     sing N N 174 
GLU C      O      doub N N 175 
GLU C      OXT    sing N N 176 
GLU CB     CG     sing N N 177 
GLU CB     HB2    sing N N 178 
GLU CB     HB3    sing N N 179 
GLU CG     CD     sing N N 180 
GLU CG     HG2    sing N N 181 
GLU CG     HG3    sing N N 182 
GLU CD     OE1    doub N N 183 
GLU CD     OE2    sing N N 184 
GLU OE2    HE2    sing N N 185 
GLU OXT    HXT    sing N N 186 
GLY N      CA     sing N N 187 
GLY N      H      sing N N 188 
GLY N      H2     sing N N 189 
GLY CA     C      sing N N 190 
GLY CA     HA2    sing N N 191 
GLY CA     HA3    sing N N 192 
GLY C      O      doub N N 193 
GLY C      OXT    sing N N 194 
GLY OXT    HXT    sing N N 195 
HIS N      CA     sing N N 196 
HIS N      H      sing N N 197 
HIS N      H2     sing N N 198 
HIS CA     C      sing N N 199 
HIS CA     CB     sing N N 200 
HIS CA     HA     sing N N 201 
HIS C      O      doub N N 202 
HIS C      OXT    sing N N 203 
HIS CB     CG     sing N N 204 
HIS CB     HB2    sing N N 205 
HIS CB     HB3    sing N N 206 
HIS CG     ND1    sing Y N 207 
HIS CG     CD2    doub Y N 208 
HIS ND1    CE1    doub Y N 209 
HIS ND1    HD1    sing N N 210 
HIS CD2    NE2    sing Y N 211 
HIS CD2    HD2    sing N N 212 
HIS CE1    NE2    sing Y N 213 
HIS CE1    HE1    sing N N 214 
HIS NE2    HE2    sing N N 215 
HIS OXT    HXT    sing N N 216 
ILE N      CA     sing N N 217 
ILE N      H      sing N N 218 
ILE N      H2     sing N N 219 
ILE CA     C      sing N N 220 
ILE CA     CB     sing N N 221 
ILE CA     HA     sing N N 222 
ILE C      O      doub N N 223 
ILE C      OXT    sing N N 224 
ILE CB     CG1    sing N N 225 
ILE CB     CG2    sing N N 226 
ILE CB     HB     sing N N 227 
ILE CG1    CD1    sing N N 228 
ILE CG1    HG12   sing N N 229 
ILE CG1    HG13   sing N N 230 
ILE CG2    HG21   sing N N 231 
ILE CG2    HG22   sing N N 232 
ILE CG2    HG23   sing N N 233 
ILE CD1    HD11   sing N N 234 
ILE CD1    HD12   sing N N 235 
ILE CD1    HD13   sing N N 236 
ILE OXT    HXT    sing N N 237 
LEU N      CA     sing N N 238 
LEU N      H      sing N N 239 
LEU N      H2     sing N N 240 
LEU CA     C      sing N N 241 
LEU CA     CB     sing N N 242 
LEU CA     HA     sing N N 243 
LEU C      O      doub N N 244 
LEU C      OXT    sing N N 245 
LEU CB     CG     sing N N 246 
LEU CB     HB2    sing N N 247 
LEU CB     HB3    sing N N 248 
LEU CG     CD1    sing N N 249 
LEU CG     CD2    sing N N 250 
LEU CG     HG     sing N N 251 
LEU CD1    HD11   sing N N 252 
LEU CD1    HD12   sing N N 253 
LEU CD1    HD13   sing N N 254 
LEU CD2    HD21   sing N N 255 
LEU CD2    HD22   sing N N 256 
LEU CD2    HD23   sing N N 257 
LEU OXT    HXT    sing N N 258 
LYS N      CA     sing N N 259 
LYS N      H      sing N N 260 
LYS N      H2     sing N N 261 
LYS CA     C      sing N N 262 
LYS CA     CB     sing N N 263 
LYS CA     HA     sing N N 264 
LYS C      O      doub N N 265 
LYS C      OXT    sing N N 266 
LYS CB     CG     sing N N 267 
LYS CB     HB2    sing N N 268 
LYS CB     HB3    sing N N 269 
LYS CG     CD     sing N N 270 
LYS CG     HG2    sing N N 271 
LYS CG     HG3    sing N N 272 
LYS CD     CE     sing N N 273 
LYS CD     HD2    sing N N 274 
LYS CD     HD3    sing N N 275 
LYS CE     NZ     sing N N 276 
LYS CE     HE2    sing N N 277 
LYS CE     HE3    sing N N 278 
LYS NZ     HZ1    sing N N 279 
LYS NZ     HZ2    sing N N 280 
LYS NZ     HZ3    sing N N 281 
LYS OXT    HXT    sing N N 282 
MET N      CA     sing N N 283 
MET N      H      sing N N 284 
MET N      H2     sing N N 285 
MET CA     C      sing N N 286 
MET CA     CB     sing N N 287 
MET CA     HA     sing N N 288 
MET C      O      doub N N 289 
MET C      OXT    sing N N 290 
MET CB     CG     sing N N 291 
MET CB     HB2    sing N N 292 
MET CB     HB3    sing N N 293 
MET CG     SD     sing N N 294 
MET CG     HG2    sing N N 295 
MET CG     HG3    sing N N 296 
MET SD     CE     sing N N 297 
MET CE     HE1    sing N N 298 
MET CE     HE2    sing N N 299 
MET CE     HE3    sing N N 300 
MET OXT    HXT    sing N N 301 
NAG C1     C2     sing N N 302 
NAG C1     O1     sing N N 303 
NAG C1     O5     sing N N 304 
NAG C1     H1     sing N N 305 
NAG C2     C3     sing N N 306 
NAG C2     N2     sing N N 307 
NAG C2     H2     sing N N 308 
NAG C3     C4     sing N N 309 
NAG C3     O3     sing N N 310 
NAG C3     H3     sing N N 311 
NAG C4     C5     sing N N 312 
NAG C4     O4     sing N N 313 
NAG C4     H4     sing N N 314 
NAG C5     C6     sing N N 315 
NAG C5     O5     sing N N 316 
NAG C5     H5     sing N N 317 
NAG C6     O6     sing N N 318 
NAG C6     H61    sing N N 319 
NAG C6     H62    sing N N 320 
NAG C7     C8     sing N N 321 
NAG C7     N2     sing N N 322 
NAG C7     O7     doub N N 323 
NAG C8     H81    sing N N 324 
NAG C8     H82    sing N N 325 
NAG C8     H83    sing N N 326 
NAG N2     HN2    sing N N 327 
NAG O1     HO1    sing N N 328 
NAG O3     HO3    sing N N 329 
NAG O4     HO4    sing N N 330 
NAG O6     HO6    sing N N 331 
PHE N      CA     sing N N 332 
PHE N      H      sing N N 333 
PHE N      H2     sing N N 334 
PHE CA     C      sing N N 335 
PHE CA     CB     sing N N 336 
PHE CA     HA     sing N N 337 
PHE C      O      doub N N 338 
PHE C      OXT    sing N N 339 
PHE CB     CG     sing N N 340 
PHE CB     HB2    sing N N 341 
PHE CB     HB3    sing N N 342 
PHE CG     CD1    doub Y N 343 
PHE CG     CD2    sing Y N 344 
PHE CD1    CE1    sing Y N 345 
PHE CD1    HD1    sing N N 346 
PHE CD2    CE2    doub Y N 347 
PHE CD2    HD2    sing N N 348 
PHE CE1    CZ     doub Y N 349 
PHE CE1    HE1    sing N N 350 
PHE CE2    CZ     sing Y N 351 
PHE CE2    HE2    sing N N 352 
PHE CZ     HZ     sing N N 353 
PHE OXT    HXT    sing N N 354 
PRO N      CA     sing N N 355 
PRO N      CD     sing N N 356 
PRO N      H      sing N N 357 
PRO CA     C      sing N N 358 
PRO CA     CB     sing N N 359 
PRO CA     HA     sing N N 360 
PRO C      O      doub N N 361 
PRO C      OXT    sing N N 362 
PRO CB     CG     sing N N 363 
PRO CB     HB2    sing N N 364 
PRO CB     HB3    sing N N 365 
PRO CG     CD     sing N N 366 
PRO CG     HG2    sing N N 367 
PRO CG     HG3    sing N N 368 
PRO CD     HD2    sing N N 369 
PRO CD     HD3    sing N N 370 
PRO OXT    HXT    sing N N 371 
SER N      CA     sing N N 372 
SER N      H      sing N N 373 
SER N      H2     sing N N 374 
SER CA     C      sing N N 375 
SER CA     CB     sing N N 376 
SER CA     HA     sing N N 377 
SER C      O      doub N N 378 
SER C      OXT    sing N N 379 
SER CB     OG     sing N N 380 
SER CB     HB2    sing N N 381 
SER CB     HB3    sing N N 382 
SER OG     HG     sing N N 383 
SER OXT    HXT    sing N N 384 
THR N      CA     sing N N 385 
THR N      H      sing N N 386 
THR N      H2     sing N N 387 
THR CA     C      sing N N 388 
THR CA     CB     sing N N 389 
THR CA     HA     sing N N 390 
THR C      O      doub N N 391 
THR C      OXT    sing N N 392 
THR CB     OG1    sing N N 393 
THR CB     CG2    sing N N 394 
THR CB     HB     sing N N 395 
THR OG1    HG1    sing N N 396 
THR CG2    HG21   sing N N 397 
THR CG2    HG22   sing N N 398 
THR CG2    HG23   sing N N 399 
THR OXT    HXT    sing N N 400 
TRP N      CA     sing N N 401 
TRP N      H      sing N N 402 
TRP N      H2     sing N N 403 
TRP CA     C      sing N N 404 
TRP CA     CB     sing N N 405 
TRP CA     HA     sing N N 406 
TRP C      O      doub N N 407 
TRP C      OXT    sing N N 408 
TRP CB     CG     sing N N 409 
TRP CB     HB2    sing N N 410 
TRP CB     HB3    sing N N 411 
TRP CG     CD1    doub Y N 412 
TRP CG     CD2    sing Y N 413 
TRP CD1    NE1    sing Y N 414 
TRP CD1    HD1    sing N N 415 
TRP CD2    CE2    doub Y N 416 
TRP CD2    CE3    sing Y N 417 
TRP NE1    CE2    sing Y N 418 
TRP NE1    HE1    sing N N 419 
TRP CE2    CZ2    sing Y N 420 
TRP CE3    CZ3    doub Y N 421 
TRP CE3    HE3    sing N N 422 
TRP CZ2    CH2    doub Y N 423 
TRP CZ2    HZ2    sing N N 424 
TRP CZ3    CH2    sing Y N 425 
TRP CZ3    HZ3    sing N N 426 
TRP CH2    HH2    sing N N 427 
TRP OXT    HXT    sing N N 428 
TYR N      CA     sing N N 429 
TYR N      H      sing N N 430 
TYR N      H2     sing N N 431 
TYR CA     C      sing N N 432 
TYR CA     CB     sing N N 433 
TYR CA     HA     sing N N 434 
TYR C      O      doub N N 435 
TYR C      OXT    sing N N 436 
TYR CB     CG     sing N N 437 
TYR CB     HB2    sing N N 438 
TYR CB     HB3    sing N N 439 
TYR CG     CD1    doub Y N 440 
TYR CG     CD2    sing Y N 441 
TYR CD1    CE1    sing Y N 442 
TYR CD1    HD1    sing N N 443 
TYR CD2    CE2    doub Y N 444 
TYR CD2    HD2    sing N N 445 
TYR CE1    CZ     doub Y N 446 
TYR CE1    HE1    sing N N 447 
TYR CE2    CZ     sing Y N 448 
TYR CE2    HE2    sing N N 449 
TYR CZ     OH     sing N N 450 
TYR OH     HH     sing N N 451 
TYR OXT    HXT    sing N N 452 
VAL N      CA     sing N N 453 
VAL N      H      sing N N 454 
VAL N      H2     sing N N 455 
VAL CA     C      sing N N 456 
VAL CA     CB     sing N N 457 
VAL CA     HA     sing N N 458 
VAL C      O      doub N N 459 
VAL C      OXT    sing N N 460 
VAL CB     CG1    sing N N 461 
VAL CB     CG2    sing N N 462 
VAL CB     HB     sing N N 463 
VAL CG1    HG11   sing N N 464 
VAL CG1    HG12   sing N N 465 
VAL CG1    HG13   sing N N 466 
VAL CG2    HG21   sing N N 467 
VAL CG2    HG22   sing N N 468 
VAL CG2    HG23   sing N N 469 
VAL OXT    HXT    sing N N 470 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2024-09-13 
_em_admin.deposition_site    PDBJ 
_em_admin.entry_id           9JJF 
_em_admin.last_update        2024-12-18 
_em_admin.map_release_date   2024-11-06 
_em_admin.title              'Nematostella vectensis TRPM2 protomer in complex with ADPRP/Ca2+' 
# 
_em_ctf_correction.details                  ? 
_em_ctf_correction.em_image_processing_id   1 
_em_ctf_correction.id                       1 
_em_ctf_correction.type                     NONE 
# 
_em_entity_assembly_molwt.entity_assembly_id   1 
_em_entity_assembly_molwt.experimental_flag    YES 
_em_entity_assembly_molwt.id                   1 
_em_entity_assembly_molwt.units                MEGADALTONS 
_em_entity_assembly_molwt.value                0.17 
# 
_em_entity_assembly_naturalsource.cell                 ? 
_em_entity_assembly_naturalsource.cellular_location    ? 
_em_entity_assembly_naturalsource.entity_assembly_id   1 
_em_entity_assembly_naturalsource.id                   2 
_em_entity_assembly_naturalsource.ncbi_tax_id          45351 
_em_entity_assembly_naturalsource.organism             'Nematostella vectensis' 
_em_entity_assembly_naturalsource.organelle            ? 
_em_entity_assembly_naturalsource.organ                ? 
_em_entity_assembly_naturalsource.strain               ? 
_em_entity_assembly_naturalsource.tissue               ? 
_em_entity_assembly_naturalsource.details              ? 
# 
_em_entity_assembly_recombinant.cell                 ? 
_em_entity_assembly_recombinant.entity_assembly_id   1 
_em_entity_assembly_recombinant.id                   2 
_em_entity_assembly_recombinant.ncbi_tax_id          9606 
_em_entity_assembly_recombinant.organism             'Homo sapiens' 
_em_entity_assembly_recombinant.plasmid              ? 
_em_entity_assembly_recombinant.strain               ? 
# 
_em_image_processing.details              ? 
_em_image_processing.id                   1 
_em_image_processing.image_recording_id   1 
# 
_em_image_recording.average_exposure_time               ? 
_em_image_recording.avg_electron_dose_per_subtomogram   ? 
_em_image_recording.avg_electron_dose_per_image         60 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       ? 
_em_image_recording.film_or_detector_model              'GATAN K3 (6k x 4k)' 
_em_image_recording.id                                  1 
_em_image_recording.imaging_id                          1 
_em_image_recording.num_diffraction_images              ? 
_em_image_recording.num_grids_imaged                    ? 
_em_image_recording.num_real_images                     ? 
# 
loop_
_em_software.category 
_em_software.details 
_em_software.id 
_em_software.image_processing_id 
_em_software.fitting_id 
_em_software.imaging_id 
_em_software.name 
_em_software.version 
'MODEL REFINEMENT'              ? 1  ? ? ? PHENIX 1.21_5207: 
'IMAGE ACQUISITION'             ? 2  1 1 1 ?      ?          
'PARTICLE SELECTION'            ? 3  1 1 1 ?      ?          
'VOLUME SELECTION'              ? 4  1 1 1 ?      ?          
CLASSIFICATION                  ? 5  1 1 1 ?      ?          
MASKING                         ? 6  1 1 1 ?      ?          
RECONSTRUCTION                  ? 7  1 1 1 ?      ?          
'INITIAL EULER ASSIGNMENT'      ? 8  1 1 1 ?      ?          
'FINAL EULER ASSIGNMENT'        ? 9  1 1 1 ?      ?          
'CTF CORRECTION'                ? 10 1 1 1 ?      ?          
'LAYERLINE INDEXING'            ? 11 1 1 1 ?      ?          
'DIFFRACTION INDEXING'          ? 12 1 1 1 ?      ?          
'MODEL FITTING'                 ? 13 1 1 1 ?      ?          
'SERIES ALIGNMENT'              ? 14 1 1 1 ?      ?          
'MOLECULAR REPLACEMENT'         ? 15 1 1 1 ?      ?          
'LATTICE DISTORTION CORRECTION' ? 16 1 1 1 ?      ?          
'SYMMETRY DETERMINATION'        ? 17 1 1 1 ?      ?          
'CRYSTALLOGRAPHY MERGING'       ? 18 1 1 1 ?      ?          
OTHER                           ? 19 1 1 1 ?      ?          
# 
_em_specimen.concentration           6 
_em_specimen.details                 ? 
_em_specimen.embedding_applied       NO 
_em_specimen.experiment_id           1 
_em_specimen.id                      1 
_em_specimen.shadowing_applied       NO 
_em_specimen.staining_applied        NO 
_em_specimen.vitrification_applied   YES 
# 
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, China)'    China YFA1302300 1 
'National Natural Science Foundation of China (NSFC)' China 32171201   2 
# 
loop_
_pdbx_entity_branch_list.entity_id 
_pdbx_entity_branch_list.comp_id 
_pdbx_entity_branch_list.num 
_pdbx_entity_branch_list.hetero 
2 NAG 1 n 
2 NAG 2 n 
# 
_atom_sites.entry_id                    9JJF 
_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]   1.000000 
_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]   1.000000 
_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]   1.000000 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
CA 
N  
O  
P  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N      . ALA A 1 94   ? 135.820 121.922 219.491 1.00 50.57 ? 94   ALA A N      1 
ATOM   2    C  CA     . ALA A 1 94   ? 135.576 122.601 218.223 1.00 50.57 ? 94   ALA A CA     1 
ATOM   3    C  C      . ALA A 1 94   ? 136.839 123.291 217.723 1.00 50.57 ? 94   ALA A C      1 
ATOM   4    O  O      . ALA A 1 94   ? 137.231 124.331 218.234 1.00 50.57 ? 94   ALA A O      1 
ATOM   5    C  CB     . ALA A 1 94   ? 134.443 123.604 218.367 1.00 50.57 ? 94   ALA A CB     1 
ATOM   6    N  N      . TYR A 1 95   ? 137.460 122.700 216.707 1.00 48.69 ? 95   TYR A N      1 
ATOM   7    C  CA     . TYR A 1 95   ? 138.739 123.152 216.181 1.00 48.69 ? 95   TYR A CA     1 
ATOM   8    C  C      . TYR A 1 95   ? 138.738 122.896 214.684 1.00 48.69 ? 95   TYR A C      1 
ATOM   9    O  O      . TYR A 1 95   ? 138.207 121.881 214.230 1.00 48.69 ? 95   TYR A O      1 
ATOM   10   C  CB     . TYR A 1 95   ? 139.910 122.427 216.864 1.00 48.69 ? 95   TYR A CB     1 
ATOM   11   C  CG     . TYR A 1 95   ? 139.937 120.927 216.642 1.00 48.69 ? 95   TYR A CG     1 
ATOM   12   C  CD1    . TYR A 1 95   ? 139.199 120.073 217.453 1.00 48.69 ? 95   TYR A CD1    1 
ATOM   13   C  CD2    . TYR A 1 95   ? 140.723 120.362 215.642 1.00 48.69 ? 95   TYR A CD2    1 
ATOM   14   C  CE1    . TYR A 1 95   ? 139.219 118.708 217.259 1.00 48.69 ? 95   TYR A CE1    1 
ATOM   15   C  CE2    . TYR A 1 95   ? 140.748 118.998 215.440 1.00 48.69 ? 95   TYR A CE2    1 
ATOM   16   C  CZ     . TYR A 1 95   ? 139.998 118.176 216.254 1.00 48.69 ? 95   TYR A CZ     1 
ATOM   17   O  OH     . TYR A 1 95   ? 140.026 116.815 216.062 1.00 48.69 ? 95   TYR A OH     1 
ATOM   18   N  N      . GLY A 1 96   ? 139.330 123.804 213.919 1.00 47.03 ? 96   GLY A N      1 
ATOM   19   C  CA     . GLY A 1 96   ? 139.243 123.630 212.483 1.00 47.03 ? 96   GLY A CA     1 
ATOM   20   C  C      . GLY A 1 96   ? 139.729 124.813 211.683 1.00 47.03 ? 96   GLY A C      1 
ATOM   21   O  O      . GLY A 1 96   ? 140.820 125.318 211.938 1.00 47.03 ? 96   GLY A O      1 
ATOM   22   N  N      . GLU A 1 97   ? 138.927 125.286 210.731 1.00 50.71 ? 97   GLU A N      1 
ATOM   23   C  CA     . GLU A 1 97   ? 139.388 126.335 209.832 1.00 50.71 ? 97   GLU A CA     1 
ATOM   24   C  C      . GLU A 1 97   ? 138.203 127.140 209.318 1.00 50.71 ? 97   GLU A C      1 
ATOM   25   O  O      . GLU A 1 97   ? 137.351 126.596 208.611 1.00 50.71 ? 97   GLU A O      1 
ATOM   26   C  CB     . GLU A 1 97   ? 140.173 125.708 208.683 1.00 50.71 ? 97   GLU A CB     1 
ATOM   27   C  CG     . GLU A 1 97   ? 140.989 126.669 207.872 1.00 50.71 ? 97   GLU A CG     1 
ATOM   28   C  CD     . GLU A 1 97   ? 141.833 125.968 206.830 1.00 50.71 ? 97   GLU A CD     1 
ATOM   29   O  OE1    . GLU A 1 97   ? 141.703 124.733 206.695 1.00 50.71 ? 97   GLU A OE1    1 
ATOM   30   O  OE2    . GLU A 1 97   ? 142.646 126.641 206.166 1.00 50.71 ? 97   GLU A OE2    1 
ATOM   31   N  N      . ILE A 1 98   ? 138.150 128.430 209.661 1.00 54.89 ? 98   ILE A N      1 
ATOM   32   C  CA     . ILE A 1 98   ? 137.087 129.304 209.176 1.00 54.89 ? 98   ILE A CA     1 
ATOM   33   C  C      . ILE A 1 98   ? 137.369 129.671 207.728 1.00 54.89 ? 98   ILE A C      1 
ATOM   34   O  O      . ILE A 1 98   ? 138.500 130.028 207.365 1.00 54.89 ? 98   ILE A O      1 
ATOM   35   C  CB     . ILE A 1 98   ? 136.960 130.586 210.025 1.00 54.89 ? 98   ILE A CB     1 
ATOM   36   C  CG1    . ILE A 1 98   ? 136.896 130.305 211.519 1.00 54.89 ? 98   ILE A CG1    1 
ATOM   37   C  CG2    . ILE A 1 98   ? 135.726 131.383 209.637 1.00 54.89 ? 98   ILE A CG2    1 
ATOM   38   C  CD1    . ILE A 1 98   ? 138.174 130.664 212.206 1.00 54.89 ? 98   ILE A CD1    1 
ATOM   39   N  N      . ASP A 1 99   ? 136.331 129.586 206.899 1.00 61.39 ? 99   ASP A N      1 
ATOM   40   C  CA     . ASP A 1 99   ? 136.294 130.204 205.580 1.00 61.39 ? 99   ASP A CA     1 
ATOM   41   C  C      . ASP A 1 99   ? 135.328 131.379 205.680 1.00 61.39 ? 99   ASP A C      1 
ATOM   42   O  O      . ASP A 1 99   ? 134.109 131.183 205.722 1.00 61.39 ? 99   ASP A O      1 
ATOM   43   C  CB     . ASP A 1 99   ? 135.847 129.202 204.515 1.00 61.39 ? 99   ASP A CB     1 
ATOM   44   C  CG     . ASP A 1 99   ? 136.074 129.702 203.097 1.00 61.39 ? 99   ASP A CG     1 
ATOM   45   O  OD1    . ASP A 1 99   ? 136.575 130.832 202.918 1.00 61.39 ? 99   ASP A OD1    1 
ATOM   46   O  OD2    . ASP A 1 99   ? 135.752 128.954 202.151 1.00 61.39 ? 99   ASP A OD2    1 
ATOM   47   N  N      . PHE A 1 100  ? 135.870 132.593 205.728 1.00 63.12 ? 100  PHE A N      1 
ATOM   48   C  CA     . PHE A 1 100  ? 135.034 133.778 205.870 1.00 63.12 ? 100  PHE A CA     1 
ATOM   49   C  C      . PHE A 1 100  ? 134.314 134.076 204.561 1.00 63.12 ? 100  PHE A C      1 
ATOM   50   O  O      . PHE A 1 100  ? 134.924 134.071 203.487 1.00 63.12 ? 100  PHE A O      1 
ATOM   51   C  CB     . PHE A 1 100  ? 135.877 134.972 206.307 1.00 63.12 ? 100  PHE A CB     1 
ATOM   52   C  CG     . PHE A 1 100  ? 136.405 134.854 207.707 1.00 63.12 ? 100  PHE A CG     1 
ATOM   53   C  CD1    . PHE A 1 100  ? 135.589 135.129 208.791 1.00 63.12 ? 100  PHE A CD1    1 
ATOM   54   C  CD2    . PHE A 1 100  ? 137.716 134.469 207.940 1.00 63.12 ? 100  PHE A CD2    1 
ATOM   55   C  CE1    . PHE A 1 100  ? 136.067 135.023 210.080 1.00 63.12 ? 100  PHE A CE1    1 
ATOM   56   C  CE2    . PHE A 1 100  ? 138.199 134.357 209.229 1.00 63.12 ? 100  PHE A CE2    1 
ATOM   57   C  CZ     . PHE A 1 100  ? 137.372 134.638 210.299 1.00 63.12 ? 100  PHE A CZ     1 
ATOM   58   N  N      . GLU A 1 101  ? 133.013 134.347 204.658 1.00 72.05 ? 101  GLU A N      1 
ATOM   59   C  CA     . GLU A 1 101  ? 132.139 134.398 203.493 1.00 72.05 ? 101  GLU A CA     1 
ATOM   60   C  C      . GLU A 1 101  ? 132.358 135.657 202.665 1.00 72.05 ? 101  GLU A C      1 
ATOM   61   O  O      . GLU A 1 101  ? 131.653 136.656 202.845 1.00 72.05 ? 101  GLU A O      1 
ATOM   62   C  CB     . GLU A 1 101  ? 130.676 134.309 203.934 1.00 72.05 ? 101  GLU A CB     1 
ATOM   63   C  CG     . GLU A 1 101  ? 130.306 133.000 204.621 1.00 72.05 ? 101  GLU A CG     1 
ATOM   64   C  CD     . GLU A 1 101  ? 130.346 131.808 203.685 1.00 72.05 ? 101  GLU A CD     1 
ATOM   65   O  OE1    . GLU A 1 101  ? 130.044 131.979 202.485 1.00 72.05 ? 101  GLU A OE1    1 
ATOM   66   O  OE2    . GLU A 1 101  ? 130.678 130.697 204.151 1.00 72.05 ? 101  GLU A OE2    1 
ATOM   67   N  N      . GLY A 1 102  ? 133.327 135.612 201.756 1.00 74.13 ? 102  GLY A N      1 
ATOM   68   C  CA     . GLY A 1 102  ? 133.584 136.716 200.845 1.00 74.13 ? 102  GLY A CA     1 
ATOM   69   C  C      . GLY A 1 102  ? 134.115 137.972 201.500 1.00 74.13 ? 102  GLY A C      1 
ATOM   70   O  O      . GLY A 1 102  ? 133.736 139.080 201.103 1.00 74.13 ? 102  GLY A O      1 
ATOM   71   N  N      . TYR A 1 103  ? 134.988 137.828 202.497 1.00 74.90 ? 103  TYR A N      1 
ATOM   72   C  CA     . TYR A 1 103  ? 135.507 138.963 203.247 1.00 74.90 ? 103  TYR A CA     1 
ATOM   73   C  C      . TYR A 1 103  ? 136.931 139.324 202.842 1.00 74.90 ? 103  TYR A C      1 
ATOM   74   O  O      . TYR A 1 103  ? 137.612 140.051 203.573 1.00 74.90 ? 103  TYR A O      1 
ATOM   75   C  CB     . TYR A 1 103  ? 135.437 138.680 204.748 1.00 74.90 ? 103  TYR A CB     1 
ATOM   76   C  CG     . TYR A 1 103  ? 134.032 138.646 205.316 1.00 74.90 ? 103  TYR A CG     1 
ATOM   77   C  CD1    . TYR A 1 103  ? 132.961 139.204 204.622 1.00 74.90 ? 103  TYR A CD1    1 
ATOM   78   C  CD2    . TYR A 1 103  ? 133.776 138.046 206.545 1.00 74.90 ? 103  TYR A CD2    1 
ATOM   79   C  CE1    . TYR A 1 103  ? 131.677 139.170 205.137 1.00 74.90 ? 103  TYR A CE1    1 
ATOM   80   C  CE2    . TYR A 1 103  ? 132.495 138.007 207.069 1.00 74.90 ? 103  TYR A CE2    1 
ATOM   81   C  CZ     . TYR A 1 103  ? 131.450 138.571 206.360 1.00 74.90 ? 103  TYR A CZ     1 
ATOM   82   O  OH     . TYR A 1 103  ? 130.173 138.537 206.875 1.00 74.90 ? 103  TYR A OH     1 
ATOM   83   N  N      . GLY A 1 104  ? 137.392 138.833 201.695 1.00 77.19 ? 104  GLY A N      1 
ATOM   84   C  CA     . GLY A 1 104  ? 138.714 139.167 201.206 1.00 77.19 ? 104  GLY A CA     1 
ATOM   85   C  C      . GLY A 1 104  ? 139.757 138.110 201.499 1.00 77.19 ? 104  GLY A C      1 
ATOM   86   O  O      . GLY A 1 104  ? 140.183 137.949 202.647 1.00 77.19 ? 104  GLY A O      1 
ATOM   87   N  N      . GLY A 1 105  ? 140.177 137.382 200.467 1.00 77.40 ? 105  GLY A N      1 
ATOM   88   C  CA     . GLY A 1 105  ? 141.222 136.390 200.624 1.00 77.40 ? 105  GLY A CA     1 
ATOM   89   C  C      . GLY A 1 105  ? 140.761 134.962 200.418 1.00 77.40 ? 105  GLY A C      1 
ATOM   90   O  O      . GLY A 1 105  ? 139.813 134.505 201.065 1.00 77.40 ? 105  GLY A O      1 
ATOM   91   N  N      . GLN A 1 106  ? 141.432 134.249 199.510 1.00 76.76 ? 106  GLN A N      1 
ATOM   92   C  CA     . GLN A 1 106  ? 141.125 132.840 199.286 1.00 76.76 ? 106  GLN A CA     1 
ATOM   93   C  C      . GLN A 1 106  ? 141.573 131.978 200.458 1.00 76.76 ? 106  GLN A C      1 
ATOM   94   O  O      . GLN A 1 106  ? 140.908 130.989 200.791 1.00 76.76 ? 106  GLN A O      1 
ATOM   95   C  CB     . GLN A 1 106  ? 141.788 132.368 197.987 1.00 76.76 ? 106  GLN A CB     1 
ATOM   96   C  CG     . GLN A 1 106  ? 141.511 130.918 197.596 1.00 76.76 ? 106  GLN A CG     1 
ATOM   97   C  CD     . GLN A 1 106  ? 140.066 130.674 197.212 1.00 76.76 ? 106  GLN A CD     1 
ATOM   98   O  OE1    . GLN A 1 106  ? 139.452 131.483 196.517 1.00 76.76 ? 106  GLN A OE1    1 
ATOM   99   N  NE2    . GLN A 1 106  ? 139.514 129.554 197.664 1.00 76.76 ? 106  GLN A NE2    1 
ATOM   100  N  N      . LYS A 1 107  ? 142.677 132.349 201.105 1.00 70.36 ? 107  LYS A N      1 
ATOM   101  C  CA     . LYS A 1 107  ? 143.278 131.515 202.137 1.00 70.36 ? 107  LYS A CA     1 
ATOM   102  C  C      . LYS A 1 107  ? 142.433 131.542 203.404 1.00 70.36 ? 107  LYS A C      1 
ATOM   103  O  O      . LYS A 1 107  ? 142.166 132.610 203.963 1.00 70.36 ? 107  LYS A O      1 
ATOM   104  C  CB     . LYS A 1 107  ? 144.700 131.984 202.429 1.00 70.36 ? 107  LYS A CB     1 
ATOM   105  C  CG     . LYS A 1 107  ? 145.660 131.786 201.268 1.00 70.36 ? 107  LYS A CG     1 
ATOM   106  C  CD     . LYS A 1 107  ? 147.070 132.214 201.636 1.00 70.36 ? 107  LYS A CD     1 
ATOM   107  C  CE     . LYS A 1 107  ? 148.008 132.103 200.443 1.00 70.36 ? 107  LYS A CE     1 
ATOM   108  N  NZ     . LYS A 1 107  ? 148.223 130.688 200.030 1.00 70.36 ? 107  LYS A NZ     1 
ATOM   109  N  N      . ARG A 1 108  ? 142.011 130.363 203.846 1.00 60.01 ? 108  ARG A N      1 
ATOM   110  C  CA     . ARG A 1 108  ? 141.215 130.206 205.048 1.00 60.01 ? 108  ARG A CA     1 
ATOM   111  C  C      . ARG A 1 108  ? 142.102 130.334 206.285 1.00 60.01 ? 108  ARG A C      1 
ATOM   112  O  O      . ARG A 1 108  ? 143.330 130.399 206.196 1.00 60.01 ? 108  ARG A O      1 
ATOM   113  C  CB     . ARG A 1 108  ? 140.512 128.855 205.028 1.00 60.01 ? 108  ARG A CB     1 
ATOM   114  C  CG     . ARG A 1 108  ? 139.502 128.674 203.923 1.00 60.01 ? 108  ARG A CG     1 
ATOM   115  C  CD     . ARG A 1 108  ? 138.960 127.256 203.939 1.00 60.01 ? 108  ARG A CD     1 
ATOM   116  N  NE     . ARG A 1 108  ? 137.987 127.028 202.877 1.00 60.01 ? 108  ARG A NE     1 
ATOM   117  C  CZ     . ARG A 1 108  ? 137.411 125.857 202.634 1.00 60.01 ? 108  ARG A CZ     1 
ATOM   118  N  NH1    . ARG A 1 108  ? 137.714 124.801 203.375 1.00 60.01 ? 108  ARG A NH1    1 
ATOM   119  N  NH2    . ARG A 1 108  ? 136.533 125.742 201.648 1.00 60.01 ? 108  ARG A NH2    1 
ATOM   120  N  N      . ALA A 1 109  ? 141.474 130.356 207.457 1.00 49.45 ? 109  ALA A N      1 
ATOM   121  C  CA     . ALA A 1 109  ? 142.191 130.635 208.703 1.00 49.45 ? 109  ALA A CA     1 
ATOM   122  C  C      . ALA A 1 109  ? 141.860 129.608 209.774 1.00 49.45 ? 109  ALA A C      1 
ATOM   123  O  O      . ALA A 1 109  ? 140.701 129.554 210.229 1.00 49.45 ? 109  ALA A O      1 
ATOM   124  C  CB     . ALA A 1 109  ? 141.856 132.040 209.194 1.00 49.45 ? 109  ALA A CB     1 
ATOM   125  N  N      . PRO A 1 110  ? 142.813 128.788 210.215 1.00 46.31 ? 110  PRO A N      1 
ATOM   126  C  CA     . PRO A 1 110  ? 142.492 127.778 211.227 1.00 46.31 ? 110  PRO A CA     1 
ATOM   127  C  C      . PRO A 1 110  ? 142.309 128.365 212.615 1.00 46.31 ? 110  PRO A C      1 
ATOM   128  O  O      . PRO A 1 110  ? 142.929 129.362 212.985 1.00 46.31 ? 110  PRO A O      1 
ATOM   129  C  CB     . PRO A 1 110  ? 143.697 126.835 211.180 1.00 46.31 ? 110  PRO A CB     1 
ATOM   130  C  CG     . PRO A 1 110  ? 144.779 127.639 210.647 1.00 46.31 ? 110  PRO A CG     1 
ATOM   131  C  CD     . PRO A 1 110  ? 144.171 128.601 209.681 1.00 46.31 ? 110  PRO A CD     1 
ATOM   132  N  N      . TYR A 1 111  ? 141.439 127.717 213.384 1.00 47.71 ? 111  TYR A N      1 
ATOM   133  C  CA     . TYR A 1 111  ? 141.118 128.117 214.744 1.00 47.71 ? 111  TYR A CA     1 
ATOM   134  C  C      . TYR A 1 111  ? 141.265 126.926 215.671 1.00 47.71 ? 111  TYR A C      1 
ATOM   135  O  O      . TYR A 1 111  ? 141.102 125.774 215.257 1.00 47.71 ? 111  TYR A O      1 
ATOM   136  C  CB     . TYR A 1 111  ? 139.690 128.675 214.865 1.00 47.71 ? 111  TYR A CB     1 
ATOM   137  C  CG     . TYR A 1 111  ? 138.570 127.667 214.674 1.00 47.71 ? 111  TYR A CG     1 
ATOM   138  C  CD1    . TYR A 1 111  ? 138.134 127.315 213.402 1.00 47.71 ? 111  TYR A CD1    1 
ATOM   139  C  CD2    . TYR A 1 111  ? 137.910 127.114 215.768 1.00 47.71 ? 111  TYR A CD2    1 
ATOM   140  C  CE1    . TYR A 1 111  ? 137.102 126.419 213.224 1.00 47.71 ? 111  TYR A CE1    1 
ATOM   141  C  CE2    . TYR A 1 111  ? 136.881 126.211 215.594 1.00 47.71 ? 111  TYR A CE2    1 
ATOM   142  C  CZ     . TYR A 1 111  ? 136.485 125.869 214.320 1.00 47.71 ? 111  TYR A CZ     1 
ATOM   143  O  OH     . TYR A 1 111  ? 135.459 124.973 214.141 1.00 47.71 ? 111  TYR A OH     1 
ATOM   144  N  N      . LEU A 1 112  ? 141.533 127.219 216.939 1.00 48.08 ? 112  LEU A N      1 
ATOM   145  C  CA     . LEU A 1 112  ? 141.696 126.182 217.947 1.00 48.08 ? 112  LEU A CA     1 
ATOM   146  C  C      . LEU A 1 112  ? 141.069 126.627 219.256 1.00 48.08 ? 112  LEU A C      1 
ATOM   147  O  O      . LEU A 1 112  ? 141.503 127.619 219.844 1.00 48.08 ? 112  LEU A O      1 
ATOM   148  C  CB     . LEU A 1 112  ? 143.173 125.853 218.157 1.00 48.08 ? 112  LEU A CB     1 
ATOM   149  C  CG     . LEU A 1 112  ? 143.468 124.840 219.259 1.00 48.08 ? 112  LEU A CG     1 
ATOM   150  C  CD1    . LEU A 1 112  ? 142.851 123.495 218.954 1.00 48.08 ? 112  LEU A CD1    1 
ATOM   151  C  CD2    . LEU A 1 112  ? 144.959 124.715 219.459 1.00 48.08 ? 112  LEU A CD2    1 
ATOM   152  N  N      . ARG A 1 113  ? 140.051 125.896 219.697 1.00 52.43 ? 113  ARG A N      1 
ATOM   153  C  CA     . ARG A 1 113  ? 139.558 125.998 221.063 1.00 52.43 ? 113  ARG A CA     1 
ATOM   154  C  C      . ARG A 1 113  ? 140.632 125.527 222.033 1.00 52.43 ? 113  ARG A C      1 
ATOM   155  O  O      . ARG A 1 113  ? 141.295 124.514 221.801 1.00 52.43 ? 113  ARG A O      1 
ATOM   156  C  CB     . ARG A 1 113  ? 138.306 125.141 221.218 1.00 52.43 ? 113  ARG A CB     1 
ATOM   157  C  CG     . ARG A 1 113  ? 137.715 125.048 222.606 1.00 52.43 ? 113  ARG A CG     1 
ATOM   158  C  CD     . ARG A 1 113  ? 136.964 126.291 223.005 1.00 52.43 ? 113  ARG A CD     1 
ATOM   159  N  NE     . ARG A 1 113  ? 136.365 126.115 224.323 1.00 52.43 ? 113  ARG A NE     1 
ATOM   160  C  CZ     . ARG A 1 113  ? 135.173 125.565 224.531 1.00 52.43 ? 113  ARG A CZ     1 
ATOM   161  N  NH1    . ARG A 1 113  ? 134.449 125.137 223.507 1.00 52.43 ? 113  ARG A NH1    1 
ATOM   162  N  NH2    . ARG A 1 113  ? 134.705 125.440 225.763 1.00 52.43 ? 113  ARG A NH2    1 
ATOM   163  N  N      . MET A 1 114  ? 140.807 126.262 223.126 1.00 53.73 ? 114  MET A N      1 
ATOM   164  C  CA     . MET A 1 114  ? 141.903 126.010 224.051 1.00 53.73 ? 114  MET A CA     1 
ATOM   165  C  C      . MET A 1 114  ? 141.404 126.190 225.476 1.00 53.73 ? 114  MET A C      1 
ATOM   166  O  O      . MET A 1 114  ? 140.205 126.330 225.726 1.00 53.73 ? 114  MET A O      1 
ATOM   167  C  CB     . MET A 1 114  ? 143.081 126.945 223.753 1.00 53.73 ? 114  MET A CB     1 
ATOM   168  C  CG     . MET A 1 114  ? 143.900 126.578 222.544 1.00 53.73 ? 114  MET A CG     1 
ATOM   169  S  SD     . MET A 1 114  ? 145.018 127.914 222.145 1.00 53.73 ? 114  MET A SD     1 
ATOM   170  C  CE     . MET A 1 114  ? 145.945 127.964 223.661 1.00 53.73 ? 114  MET A CE     1 
ATOM   171  N  N      . SER A 1 115  ? 142.344 126.170 226.415 1.00 57.18 ? 115  SER A N      1 
ATOM   172  C  CA     . SER A 1 115  ? 142.084 126.541 227.795 1.00 57.18 ? 115  SER A CA     1 
ATOM   173  C  C      . SER A 1 115  ? 143.365 127.124 228.367 1.00 57.18 ? 115  SER A C      1 
ATOM   174  O  O      . SER A 1 115  ? 144.451 126.927 227.819 1.00 57.18 ? 115  SER A O      1 
ATOM   175  C  CB     . SER A 1 115  ? 141.599 125.350 228.629 1.00 57.18 ? 115  SER A CB     1 
ATOM   176  O  OG     . SER A 1 115  ? 142.619 124.383 228.782 1.00 57.18 ? 115  SER A OG     1 
ATOM   177  N  N      . HIS A 1 116  ? 143.233 127.865 229.467 1.00 59.27 ? 116  HIS A N      1 
ATOM   178  C  CA     . HIS A 1 116  ? 144.422 128.426 230.096 1.00 59.27 ? 116  HIS A CA     1 
ATOM   179  C  C      . HIS A 1 116  ? 145.203 127.393 230.896 1.00 59.27 ? 116  HIS A C      1 
ATOM   180  O  O      . HIS A 1 116  ? 146.324 127.683 231.323 1.00 59.27 ? 116  HIS A O      1 
ATOM   181  C  CB     . HIS A 1 116  ? 144.059 129.607 231.002 1.00 59.27 ? 116  HIS A CB     1 
ATOM   182  C  CG     . HIS A 1 116  ? 143.246 129.227 232.198 1.00 59.27 ? 116  HIS A CG     1 
ATOM   183  N  ND1    . HIS A 1 116  ? 143.810 128.815 233.387 1.00 59.27 ? 116  HIS A ND1    1 
ATOM   184  C  CD2    . HIS A 1 116  ? 141.909 129.203 232.390 1.00 59.27 ? 116  HIS A CD2    1 
ATOM   185  C  CE1    . HIS A 1 116  ? 142.853 128.545 234.256 1.00 59.27 ? 116  HIS A CE1    1 
ATOM   186  N  NE2    . HIS A 1 116  ? 141.689 128.773 233.676 1.00 59.27 ? 116  HIS A NE2    1 
ATOM   187  N  N      . ASP A 1 117  ? 144.636 126.206 231.118 1.00 60.52 ? 117  ASP A N      1 
ATOM   188  C  CA     . ASP A 1 117  ? 145.384 125.107 231.711 1.00 60.52 ? 117  ASP A CA     1 
ATOM   189  C  C      . ASP A 1 117  ? 146.450 124.577 230.758 1.00 60.52 ? 117  ASP A C      1 
ATOM   190  O  O      . ASP A 1 117  ? 147.435 123.988 231.214 1.00 60.52 ? 117  ASP A O      1 
ATOM   191  C  CB     . ASP A 1 117  ? 144.415 123.983 232.102 1.00 60.52 ? 117  ASP A CB     1 
ATOM   192  C  CG     . ASP A 1 117  ? 145.005 123.002 233.109 1.00 60.52 ? 117  ASP A CG     1 
ATOM   193  O  OD1    . ASP A 1 117  ? 146.131 123.220 233.601 1.00 60.52 ? 117  ASP A OD1    1 
ATOM   194  O  OD2    . ASP A 1 117  ? 144.331 121.994 233.404 1.00 60.52 ? 117  ASP A OD2    1 
ATOM   195  N  N      . THR A 1 118  ? 146.275 124.786 229.451 1.00 58.35 ? 118  THR A N      1 
ATOM   196  C  CA     . THR A 1 118  ? 147.193 124.246 228.457 1.00 58.35 ? 118  THR A CA     1 
ATOM   197  C  C      . THR A 1 118  ? 148.547 124.931 228.547 1.00 58.35 ? 118  THR A C      1 
ATOM   198  O  O      . THR A 1 118  ? 148.633 126.162 228.538 1.00 58.35 ? 118  THR A O      1 
ATOM   199  C  CB     . THR A 1 118  ? 146.627 124.424 227.048 1.00 58.35 ? 118  THR A CB     1 
ATOM   200  O  OG1    . THR A 1 118  ? 146.469 125.819 226.766 1.00 58.35 ? 118  THR A OG1    1 
ATOM   201  C  CG2    . THR A 1 118  ? 145.289 123.732 226.913 1.00 58.35 ? 118  THR A CG2    1 
ATOM   202  N  N      . ASP A 1 119  ? 149.602 124.131 228.656 1.00 58.47 ? 119  ASP A N      1 
ATOM   203  C  CA     . ASP A 1 119  ? 150.946 124.676 228.584 1.00 58.47 ? 119  ASP A CA     1 
ATOM   204  C  C      . ASP A 1 119  ? 151.248 125.139 227.164 1.00 58.47 ? 119  ASP A C      1 
ATOM   205  O  O      . ASP A 1 119  ? 150.759 124.577 226.181 1.00 58.47 ? 119  ASP A O      1 
ATOM   206  C  CB     . ASP A 1 119  ? 151.977 123.651 229.066 1.00 58.47 ? 119  ASP A CB     1 
ATOM   207  C  CG     . ASP A 1 119  ? 151.857 122.308 228.365 1.00 58.47 ? 119  ASP A CG     1 
ATOM   208  O  OD1    . ASP A 1 119  ? 150.893 122.095 227.601 1.00 58.47 ? 119  ASP A OD1    1 
ATOM   209  O  OD2    . ASP A 1 119  ? 152.741 121.453 228.584 1.00 58.47 ? 119  ASP A OD2    1 
ATOM   210  N  N      . ALA A 1 120  ? 152.045 126.196 227.065 1.00 56.36 ? 120  ALA A N      1 
ATOM   211  C  CA     . ALA A 1 120  ? 152.256 126.839 225.780 1.00 56.36 ? 120  ALA A CA     1 
ATOM   212  C  C      . ALA A 1 120  ? 153.230 126.088 224.888 1.00 56.36 ? 120  ALA A C      1 
ATOM   213  O  O      . ALA A 1 120  ? 153.289 126.386 223.693 1.00 56.36 ? 120  ALA A O      1 
ATOM   214  C  CB     . ALA A 1 120  ? 152.746 128.268 225.991 1.00 56.36 ? 120  ALA A CB     1 
ATOM   215  N  N      . ASN A 1 121  ? 153.984 125.128 225.433 1.00 56.97 ? 121  ASN A N      1 
ATOM   216  C  CA     . ASN A 1 121  ? 154.882 124.325 224.607 1.00 56.97 ? 121  ASN A CA     1 
ATOM   217  C  C      . ASN A 1 121  ? 154.096 123.450 223.642 1.00 56.97 ? 121  ASN A C      1 
ATOM   218  O  O      . ASN A 1 121  ? 154.500 123.269 222.484 1.00 56.97 ? 121  ASN A O      1 
ATOM   219  C  CB     . ASN A 1 121  ? 155.780 123.472 225.500 1.00 56.97 ? 121  ASN A CB     1 
ATOM   220  C  CG     . ASN A 1 121  ? 156.738 124.305 226.321 1.00 56.97 ? 121  ASN A CG     1 
ATOM   221  O  OD1    . ASN A 1 121  ? 157.325 125.265 225.823 1.00 56.97 ? 121  ASN A OD1    1 
ATOM   222  N  ND2    . ASN A 1 121  ? 156.894 123.951 227.590 1.00 56.97 ? 121  ASN A ND2    1 
ATOM   223  N  N      . LEU A 1 122  ? 152.953 122.929 224.101 1.00 55.94 ? 122  LEU A N      1 
ATOM   224  C  CA     . LEU A 1 122  ? 152.038 122.198 223.232 1.00 55.94 ? 122  LEU A CA     1 
ATOM   225  C  C      . LEU A 1 122  ? 151.489 123.099 222.136 1.00 55.94 ? 122  LEU A C      1 
ATOM   226  O  O      . LEU A 1 122  ? 151.343 122.672 220.987 1.00 55.94 ? 122  LEU A O      1 
ATOM   227  C  CB     . LEU A 1 122  ? 150.903 121.607 224.072 1.00 55.94 ? 122  LEU A CB     1 
ATOM   228  C  CG     . LEU A 1 122  ? 149.908 120.585 223.515 1.00 55.94 ? 122  LEU A CG     1 
ATOM   229  C  CD1    . LEU A 1 122  ? 149.492 119.662 224.642 1.00 55.94 ? 122  LEU A CD1    1 
ATOM   230  C  CD2    . LEU A 1 122  ? 148.669 121.225 222.905 1.00 55.94 ? 122  LEU A CD2    1 
ATOM   231  N  N      . VAL A 1 123  ? 151.219 124.360 222.463 1.00 54.31 ? 123  VAL A N      1 
ATOM   232  C  CA     . VAL A 1 123  ? 150.638 125.274 221.486 1.00 54.31 ? 123  VAL A CA     1 
ATOM   233  C  C      . VAL A 1 123  ? 151.675 125.675 220.445 1.00 54.31 ? 123  VAL A C      1 
ATOM   234  O  O      . VAL A 1 123  ? 151.364 125.797 219.252 1.00 54.31 ? 123  VAL A O      1 
ATOM   235  C  CB     . VAL A 1 123  ? 150.044 126.488 222.218 1.00 54.31 ? 123  VAL A CB     1 
ATOM   236  C  CG1    . VAL A 1 123  ? 149.396 127.452 221.251 1.00 54.31 ? 123  VAL A CG1    1 
ATOM   237  C  CG2    . VAL A 1 123  ? 149.053 126.015 223.250 1.00 54.31 ? 123  VAL A CG2    1 
ATOM   238  N  N      . ILE A 1 124  ? 152.932 125.827 220.861 1.00 54.33 ? 124  ILE A N      1 
ATOM   239  C  CA     . ILE A 1 124  ? 153.967 126.203 219.905 1.00 54.33 ? 124  ILE A CA     1 
ATOM   240  C  C      . ILE A 1 124  ? 154.342 125.021 219.021 1.00 54.33 ? 124  ILE A C      1 
ATOM   241  O  O      . ILE A 1 124  ? 154.536 125.185 217.811 1.00 54.33 ? 124  ILE A O      1 
ATOM   242  C  CB     . ILE A 1 124  ? 155.181 126.808 220.633 1.00 54.33 ? 124  ILE A CB     1 
ATOM   243  C  CG1    . ILE A 1 124  ? 154.743 128.072 221.362 1.00 54.33 ? 124  ILE A CG1    1 
ATOM   244  C  CG2    . ILE A 1 124  ? 156.300 127.162 219.668 1.00 54.33 ? 124  ILE A CG2    1 
ATOM   245  C  CD1    . ILE A 1 124  ? 154.064 129.074 220.474 1.00 54.33 ? 124  ILE A CD1    1 
ATOM   246  N  N      . THR A 1 125  ? 154.397 123.805 219.580 1.00 55.84 ? 125  THR A N      1 
ATOM   247  C  CA     . THR A 1 125  ? 154.635 122.665 218.700 1.00 55.84 ? 125  THR A CA     1 
ATOM   248  C  C      . THR A 1 125  ? 153.426 122.369 217.818 1.00 55.84 ? 125  THR A C      1 
ATOM   249  O  O      . THR A 1 125  ? 153.609 121.870 216.706 1.00 55.84 ? 125  THR A O      1 
ATOM   250  C  CB     . THR A 1 125  ? 155.067 121.419 219.491 1.00 55.84 ? 125  THR A CB     1 
ATOM   251  O  OG1    . THR A 1 125  ? 155.539 120.420 218.578 1.00 55.84 ? 125  THR A OG1    1 
ATOM   252  C  CG2    . THR A 1 125  ? 153.937 120.825 220.300 1.00 55.84 ? 125  THR A CG2    1 
ATOM   253  N  N      . LEU A 1 126  ? 152.222 122.776 218.232 1.00 54.44 ? 126  LEU A N      1 
ATOM   254  C  CA     . LEU A 1 126  ? 151.057 122.678 217.360 1.00 54.44 ? 126  LEU A CA     1 
ATOM   255  C  C      . LEU A 1 126  ? 151.159 123.652 216.195 1.00 54.44 ? 126  LEU A C      1 
ATOM   256  O  O      . LEU A 1 126  ? 150.951 123.273 215.039 1.00 54.44 ? 126  LEU A O      1 
ATOM   257  C  CB     . LEU A 1 126  ? 149.784 122.919 218.175 1.00 54.44 ? 126  LEU A CB     1 
ATOM   258  C  CG     . LEU A 1 126  ? 148.403 122.717 217.547 1.00 54.44 ? 126  LEU A CG     1 
ATOM   259  C  CD1    . LEU A 1 126  ? 147.481 122.120 218.591 1.00 54.44 ? 126  LEU A CD1    1 
ATOM   260  C  CD2    . LEU A 1 126  ? 147.809 124.029 217.043 1.00 54.44 ? 126  LEU A CD2    1 
ATOM   261  N  N      . MET A 1 127  ? 151.501 124.903 216.472 1.00 51.93 ? 127  MET A N      1 
ATOM   262  C  CA     . MET A 1 127  ? 151.549 125.889 215.402 1.00 51.93 ? 127  MET A CA     1 
ATOM   263  C  C      . MET A 1 127  ? 152.863 125.869 214.634 1.00 51.93 ? 127  MET A C      1 
ATOM   264  O  O      . MET A 1 127  ? 153.014 126.646 213.689 1.00 51.93 ? 127  MET A O      1 
ATOM   265  C  CB     . MET A 1 127  ? 151.273 127.285 215.964 1.00 51.93 ? 127  MET A CB     1 
ATOM   266  C  CG     . MET A 1 127  ? 152.371 127.888 216.806 1.00 51.93 ? 127  MET A CG     1 
ATOM   267  S  SD     . MET A 1 127  ? 151.786 129.411 217.569 1.00 51.93 ? 127  MET A SD     1 
ATOM   268  C  CE     . MET A 1 127  ? 151.470 130.419 216.127 1.00 51.93 ? 127  MET A CE     1 
ATOM   269  N  N      . LEU A 1 128  ? 153.814 125.008 215.007 1.00 53.43 ? 128  LEU A N      1 
ATOM   270  C  CA     . LEU A 1 128  ? 155.001 124.796 214.189 1.00 53.43 ? 128  LEU A CA     1 
ATOM   271  C  C      . LEU A 1 128  ? 155.049 123.444 213.492 1.00 53.43 ? 128  LEU A C      1 
ATOM   272  O  O      . LEU A 1 128  ? 155.813 123.298 212.534 1.00 53.43 ? 128  LEU A O      1 
ATOM   273  C  CB     . LEU A 1 128  ? 156.278 124.958 215.025 1.00 53.43 ? 128  LEU A CB     1 
ATOM   274  C  CG     . LEU A 1 128  ? 156.611 126.359 215.539 1.00 53.43 ? 128  LEU A CG     1 
ATOM   275  C  CD1    . LEU A 1 128  ? 157.879 126.323 216.366 1.00 53.43 ? 128  LEU A CD1    1 
ATOM   276  C  CD2    . LEU A 1 128  ? 156.736 127.347 214.401 1.00 53.43 ? 128  LEU A CD2    1 
ATOM   277  N  N      . LYS A 1 129  ? 154.268 122.456 213.932 1.00 55.25 ? 129  LYS A N      1 
ATOM   278  C  CA     . LYS A 1 129  ? 154.221 121.163 213.264 1.00 55.25 ? 129  LYS A CA     1 
ATOM   279  C  C      . LYS A 1 129  ? 152.878 120.891 212.610 1.00 55.25 ? 129  LYS A C      1 
ATOM   280  O  O      . LYS A 1 129  ? 152.828 120.494 211.442 1.00 55.25 ? 129  LYS A O      1 
ATOM   281  C  CB     . LYS A 1 129  ? 154.541 120.043 214.264 1.00 55.25 ? 129  LYS A CB     1 
ATOM   282  C  CG     . LYS A 1 129  ? 155.886 120.187 214.951 1.00 55.25 ? 129  LYS A CG     1 
ATOM   283  C  CD     . LYS A 1 129  ? 157.032 120.084 213.963 1.00 55.25 ? 129  LYS A CD     1 
ATOM   284  C  CE     . LYS A 1 129  ? 158.369 120.037 214.683 1.00 55.25 ? 129  LYS A CE     1 
ATOM   285  N  NZ     . LYS A 1 129  ? 158.696 121.329 215.340 1.00 55.25 ? 129  LYS A NZ     1 
ATOM   286  N  N      . ARG A 1 130  ? 151.780 121.094 213.341 1.00 53.29 ? 130  ARG A N      1 
ATOM   287  C  CA     . ARG A 1 130  ? 150.459 120.784 212.811 1.00 53.29 ? 130  ARG A CA     1 
ATOM   288  C  C      . ARG A 1 130  ? 150.012 121.822 211.790 1.00 53.29 ? 130  ARG A C      1 
ATOM   289  O  O      . ARG A 1 130  ? 149.522 121.467 210.713 1.00 53.29 ? 130  ARG A O      1 
ATOM   290  C  CB     . ARG A 1 130  ? 149.445 120.687 213.952 1.00 53.29 ? 130  ARG A CB     1 
ATOM   291  C  CG     . ARG A 1 130  ? 149.357 119.332 214.669 1.00 53.29 ? 130  ARG A CG     1 
ATOM   292  C  CD     . ARG A 1 130  ? 150.508 119.063 215.638 1.00 53.29 ? 130  ARG A CD     1 
ATOM   293  N  NE     . ARG A 1 130  ? 150.284 117.850 216.423 1.00 53.29 ? 130  ARG A NE     1 
ATOM   294  C  CZ     . ARG A 1 130  ? 149.698 117.828 217.618 1.00 53.29 ? 130  ARG A CZ     1 
ATOM   295  N  NH1    . ARG A 1 130  ? 149.293 118.958 218.183 1.00 53.29 ? 130  ARG A NH1    1 
ATOM   296  N  NH2    . ARG A 1 130  ? 149.529 116.679 218.256 1.00 53.29 ? 130  ARG A NH2    1 
ATOM   297  N  N      . TRP A 1 131  ? 150.182 123.105 212.100 1.00 50.93 ? 131  TRP A N      1 
ATOM   298  C  CA     . TRP A 1 131  ? 149.724 124.164 211.212 1.00 50.93 ? 131  TRP A CA     1 
ATOM   299  C  C      . TRP A 1 131  ? 150.800 124.656 210.258 1.00 50.93 ? 131  TRP A C      1 
ATOM   300  O  O      . TRP A 1 131  ? 150.481 125.443 209.360 1.00 50.93 ? 131  TRP A O      1 
ATOM   301  C  CB     . TRP A 1 131  ? 149.194 125.353 212.015 1.00 50.93 ? 131  TRP A CB     1 
ATOM   302  C  CG     . TRP A 1 131  ? 147.925 125.092 212.748 1.00 50.93 ? 131  TRP A CG     1 
ATOM   303  C  CD1    . TRP A 1 131  ? 147.188 123.945 212.741 1.00 50.93 ? 131  TRP A CD1    1 
ATOM   304  C  CD2    . TRP A 1 131  ? 147.218 126.018 213.573 1.00 50.93 ? 131  TRP A CD2    1 
ATOM   305  N  NE1    . TRP A 1 131  ? 146.076 124.093 213.531 1.00 50.93 ? 131  TRP A NE1    1 
ATOM   306  C  CE2    . TRP A 1 131  ? 146.069 125.361 214.049 1.00 50.93 ? 131  TRP A CE2    1 
ATOM   307  C  CE3    . TRP A 1 131  ? 147.450 127.338 213.962 1.00 50.93 ? 131  TRP A CE3    1 
ATOM   308  C  CZ2    . TRP A 1 131  ? 145.155 125.979 214.894 1.00 50.93 ? 131  TRP A CZ2    1 
ATOM   309  C  CZ3    . TRP A 1 131  ? 146.542 127.951 214.790 1.00 50.93 ? 131  TRP A CZ3    1 
ATOM   310  C  CH2    . TRP A 1 131  ? 145.411 127.272 215.255 1.00 50.93 ? 131  TRP A CH2    1 
ATOM   311  N  N      . ASN A 1 132  ? 152.054 124.234 210.462 1.00 54.19 ? 132  ASN A N      1 
ATOM   312  C  CA     . ASN A 1 132  ? 153.168 124.435 209.527 1.00 54.19 ? 132  ASN A CA     1 
ATOM   313  C  C      . ASN A 1 132  ? 153.464 125.915 209.282 1.00 54.19 ? 132  ASN A C      1 
ATOM   314  O  O      . ASN A 1 132  ? 153.504 126.384 208.143 1.00 54.19 ? 132  ASN A O      1 
ATOM   315  C  CB     . ASN A 1 132  ? 152.922 123.699 208.206 1.00 54.19 ? 132  ASN A CB     1 
ATOM   316  C  CG     . ASN A 1 132  ? 153.023 122.195 208.350 1.00 54.19 ? 132  ASN A CG     1 
ATOM   317  O  OD1    . ASN A 1 132  ? 153.928 121.683 209.008 1.00 54.19 ? 132  ASN A OD1    1 
ATOM   318  N  ND2    . ASN A 1 132  ? 152.089 121.476 207.738 1.00 54.19 ? 132  ASN A ND2    1 
ATOM   319  N  N      . LEU A 1 133  ? 153.668 126.655 210.366 1.00 48.30 ? 133  LEU A N      1 
ATOM   320  C  CA     . LEU A 1 133  ? 154.178 128.013 210.266 1.00 48.30 ? 133  LEU A CA     1 
ATOM   321  C  C      . LEU A 1 133  ? 155.693 127.972 210.381 1.00 48.30 ? 133  LEU A C      1 
ATOM   322  O  O      . LEU A 1 133  ? 156.247 127.173 211.139 1.00 48.30 ? 133  LEU A O      1 
ATOM   323  C  CB     . LEU A 1 133  ? 153.602 128.924 211.353 1.00 48.30 ? 133  LEU A CB     1 
ATOM   324  C  CG     . LEU A 1 133  ? 152.185 129.499 211.263 1.00 48.30 ? 133  LEU A CG     1 
ATOM   325  C  CD1    . LEU A 1 133  ? 151.147 128.473 211.641 1.00 48.30 ? 133  LEU A CD1    1 
ATOM   326  C  CD2    . LEU A 1 133  ? 152.052 130.719 212.148 1.00 48.30 ? 133  LEU A CD2    1 
ATOM   327  N  N      . GLU A 1 134  ? 156.363 128.817 209.608 1.00 44.97 ? 134  GLU A N      1 
ATOM   328  C  CA     . GLU A 1 134  ? 157.809 128.917 209.722 1.00 44.97 ? 134  GLU A CA     1 
ATOM   329  C  C      . GLU A 1 134  ? 158.184 129.686 210.983 1.00 44.97 ? 134  GLU A C      1 
ATOM   330  O  O      . GLU A 1 134  ? 157.464 130.586 211.422 1.00 44.97 ? 134  GLU A O      1 
ATOM   331  C  CB     . GLU A 1 134  ? 158.397 129.579 208.471 1.00 44.97 ? 134  GLU A CB     1 
ATOM   332  C  CG     . GLU A 1 134  ? 157.825 130.952 208.119 1.00 44.97 ? 134  GLU A CG     1 
ATOM   333  C  CD     . GLU A 1 134  ? 158.597 132.108 208.733 1.00 44.97 ? 134  GLU A CD     1 
ATOM   334  O  OE1    . GLU A 1 134  ? 159.764 131.906 209.126 1.00 44.97 ? 134  GLU A OE1    1 
ATOM   335  O  OE2    . GLU A 1 134  ? 158.036 133.221 208.812 1.00 44.97 ? 134  GLU A OE2    1 
ATOM   336  N  N      . ILE A 1 135  ? 159.308 129.301 211.582 1.00 43.96 ? 135  ILE A N      1 
ATOM   337  C  CA     . ILE A 1 135  ? 159.814 129.956 212.787 1.00 43.96 ? 135  ILE A CA     1 
ATOM   338  C  C      . ILE A 1 135  ? 160.265 131.361 212.410 1.00 43.96 ? 135  ILE A C      1 
ATOM   339  O  O      . ILE A 1 135  ? 161.213 131.520 211.627 1.00 43.96 ? 135  ILE A O      1 
ATOM   340  C  CB     . ILE A 1 135  ? 160.956 129.159 213.432 1.00 43.96 ? 135  ILE A CB     1 
ATOM   341  C  CG1    . ILE A 1 135  ? 160.453 127.798 213.906 1.00 43.96 ? 135  ILE A CG1    1 
ATOM   342  C  CG2    . ILE A 1 135  ? 161.550 129.933 214.596 1.00 43.96 ? 135  ILE A CG2    1 
ATOM   343  C  CD1    . ILE A 1 135  ? 161.554 126.857 214.332 1.00 43.96 ? 135  ILE A CD1    1 
ATOM   344  N  N      . PRO A 1 136  ? 159.621 132.397 212.932 1.00 40.32 ? 136  PRO A N      1 
ATOM   345  C  CA     . PRO A 1 136  ? 159.849 133.747 212.419 1.00 40.32 ? 136  PRO A CA     1 
ATOM   346  C  C      . PRO A 1 136  ? 161.104 134.375 213.001 1.00 40.32 ? 136  PRO A C      1 
ATOM   347  O  O      . PRO A 1 136  ? 161.644 133.940 214.019 1.00 40.32 ? 136  PRO A O      1 
ATOM   348  C  CB     . PRO A 1 136  ? 158.601 134.499 212.882 1.00 40.32 ? 136  PRO A CB     1 
ATOM   349  C  CG     . PRO A 1 136  ? 158.262 133.830 214.154 1.00 40.32 ? 136  PRO A CG     1 
ATOM   350  C  CD     . PRO A 1 136  ? 158.605 132.384 213.997 1.00 40.32 ? 136  PRO A CD     1 
ATOM   351  N  N      . ASN A 1 137  ? 161.558 135.428 212.329 1.00 39.66 ? 137  ASN A N      1 
ATOM   352  C  CA     . ASN A 1 137  ? 162.679 136.221 212.806 1.00 39.66 ? 137  ASN A CA     1 
ATOM   353  C  C      . ASN A 1 137  ? 162.260 137.258 213.833 1.00 39.66 ? 137  ASN A C      1 
ATOM   354  O  O      . ASN A 1 137  ? 163.122 137.957 214.372 1.00 39.66 ? 137  ASN A O      1 
ATOM   355  C  CB     . ASN A 1 137  ? 163.364 136.919 211.632 1.00 39.66 ? 137  ASN A CB     1 
ATOM   356  C  CG     . ASN A 1 137  ? 164.053 135.950 210.701 1.00 39.66 ? 137  ASN A CG     1 
ATOM   357  O  OD1    . ASN A 1 137  ? 164.696 134.999 211.141 1.00 39.66 ? 137  ASN A OD1    1 
ATOM   358  N  ND2    . ASN A 1 137  ? 163.922 136.185 209.402 1.00 39.66 ? 137  ASN A ND2    1 
ATOM   359  N  N      . LEU A 1 138  ? 160.964 137.362 214.112 1.00 35.80 ? 138  LEU A N      1 
ATOM   360  C  CA     . LEU A 1 138  ? 160.366 138.390 214.946 1.00 35.80 ? 138  LEU A CA     1 
ATOM   361  C  C      . LEU A 1 138  ? 158.927 137.994 215.213 1.00 35.80 ? 138  LEU A C      1 
ATOM   362  O  O      . LEU A 1 138  ? 158.273 137.429 214.340 1.00 35.80 ? 138  LEU A O      1 
ATOM   363  C  CB     . LEU A 1 138  ? 160.405 139.753 214.248 1.00 35.80 ? 138  LEU A CB     1 
ATOM   364  C  CG     . LEU A 1 138  ? 159.817 140.979 214.940 1.00 35.80 ? 138  LEU A CG     1 
ATOM   365  C  CD1    . LEU A 1 138  ? 160.650 141.410 216.104 1.00 35.80 ? 138  LEU A CD1    1 
ATOM   366  C  CD2    . LEU A 1 138  ? 159.675 142.080 213.946 1.00 35.80 ? 138  LEU A CD2    1 
ATOM   367  N  N      . VAL A 1 139  ? 158.442 138.273 216.416 1.00 35.13 ? 139  VAL A N      1 
ATOM   368  C  CA     . VAL A 1 139  ? 157.020 138.189 216.717 1.00 35.13 ? 139  VAL A CA     1 
ATOM   369  C  C      . VAL A 1 139  ? 156.595 139.529 217.288 1.00 35.13 ? 139  VAL A C      1 
ATOM   370  O  O      . VAL A 1 139  ? 157.027 139.908 218.381 1.00 35.13 ? 139  VAL A O      1 
ATOM   371  C  CB     . VAL A 1 139  ? 156.681 137.050 217.682 1.00 35.13 ? 139  VAL A CB     1 
ATOM   372  C  CG1    . VAL A 1 139  ? 155.249 137.156 218.137 1.00 35.13 ? 139  VAL A CG1    1 
ATOM   373  C  CG2    . VAL A 1 139  ? 156.874 135.737 216.998 1.00 35.13 ? 139  VAL A CG2    1 
ATOM   374  N  N      . ILE A 1 140  ? 155.760 140.242 216.557 1.00 34.19 ? 140  ILE A N      1 
ATOM   375  C  CA     . ILE A 1 140  ? 155.183 141.491 217.026 1.00 34.19 ? 140  ILE A CA     1 
ATOM   376  C  C      . ILE A 1 140  ? 153.873 141.171 217.725 1.00 34.19 ? 140  ILE A C      1 
ATOM   377  O  O      . ILE A 1 140  ? 153.040 140.438 217.192 1.00 34.19 ? 140  ILE A O      1 
ATOM   378  C  CB     . ILE A 1 140  ? 154.961 142.457 215.855 1.00 34.19 ? 140  ILE A CB     1 
ATOM   379  C  CG1    . ILE A 1 140  ? 156.280 142.729 215.150 1.00 34.19 ? 140  ILE A CG1    1 
ATOM   380  C  CG2    . ILE A 1 140  ? 154.382 143.759 216.337 1.00 34.19 ? 140  ILE A CG2    1 
ATOM   381  C  CD1    . ILE A 1 140  ? 156.133 143.415 213.828 1.00 34.19 ? 140  ILE A CD1    1 
ATOM   382  N  N      . SER A 1 141  ? 153.690 141.692 218.923 1.00 37.21 ? 141  SER A N      1 
ATOM   383  C  CA     . SER A 1 141  ? 152.439 141.544 219.647 1.00 37.21 ? 141  SER A CA     1 
ATOM   384  C  C      . SER A 1 141  ? 151.792 142.918 219.717 1.00 37.21 ? 141  SER A C      1 
ATOM   385  O  O      . SER A 1 141  ? 152.250 143.780 220.464 1.00 37.21 ? 141  SER A O      1 
ATOM   386  C  CB     . SER A 1 141  ? 152.680 140.979 221.039 1.00 37.21 ? 141  SER A CB     1 
ATOM   387  O  OG     . SER A 1 141  ? 151.461 140.848 221.743 1.00 37.21 ? 141  SER A OG     1 
ATOM   388  N  N      . VAL A 1 142  ? 150.744 143.127 218.942 1.00 40.11 ? 142  VAL A N      1 
ATOM   389  C  CA     . VAL A 1 142  ? 150.078 144.421 218.883 1.00 40.11 ? 142  VAL A CA     1 
ATOM   390  C  C      . VAL A 1 142  ? 148.936 144.416 219.889 1.00 40.11 ? 142  VAL A C      1 
ATOM   391  O  O      . VAL A 1 142  ? 148.185 143.441 219.987 1.00 40.11 ? 142  VAL A O      1 
ATOM   392  C  CB     . VAL A 1 142  ? 149.583 144.711 217.459 1.00 40.11 ? 142  VAL A CB     1 
ATOM   393  C  CG1    . VAL A 1 142  ? 148.893 146.057 217.382 1.00 40.11 ? 142  VAL A CG1    1 
ATOM   394  C  CG2    . VAL A 1 142  ? 150.739 144.642 216.483 1.00 40.11 ? 142  VAL A CG2    1 
ATOM   395  N  N      . THR A 1 143  ? 148.824 145.493 220.661 1.00 46.34 ? 143  THR A N      1 
ATOM   396  C  CA     . THR A 1 143  ? 147.863 145.570 221.746 1.00 46.34 ? 143  THR A CA     1 
ATOM   397  C  C      . THR A 1 143  ? 147.249 146.960 221.766 1.00 46.34 ? 143  THR A C      1 
ATOM   398  O  O      . THR A 1 143  ? 147.955 147.961 221.604 1.00 46.34 ? 143  THR A O      1 
ATOM   399  C  CB     . THR A 1 143  ? 148.543 145.261 223.084 1.00 46.34 ? 143  THR A CB     1 
ATOM   400  O  OG1    . THR A 1 143  ? 149.178 143.983 223.005 1.00 46.34 ? 143  THR A OG1    1 
ATOM   401  C  CG2    . THR A 1 143  ? 147.541 145.194 224.178 1.00 46.34 ? 143  THR A CG2    1 
ATOM   402  N  N      . GLY A 1 144  ? 145.932 147.015 221.939 1.00 53.44 ? 144  GLY A N      1 
ATOM   403  C  CA     . GLY A 1 144  ? 145.261 148.284 222.100 1.00 53.44 ? 144  GLY A CA     1 
ATOM   404  C  C      . GLY A 1 144  ? 143.796 148.183 222.445 1.00 53.44 ? 144  GLY A C      1 
ATOM   405  O  O      . GLY A 1 144  ? 143.369 147.226 223.094 1.00 53.44 ? 144  GLY A O      1 
ATOM   406  N  N      . GLY A 1 145  ? 143.019 149.176 222.034 1.00 56.73 ? 145  GLY A N      1 
ATOM   407  C  CA     . GLY A 1 145  ? 141.607 149.168 222.327 1.00 56.73 ? 145  GLY A CA     1 
ATOM   408  C  C      . GLY A 1 145  ? 140.851 148.183 221.469 1.00 56.73 ? 145  GLY A C      1 
ATOM   409  O  O      . GLY A 1 145  ? 141.304 147.763 220.408 1.00 56.73 ? 145  GLY A O      1 
ATOM   410  N  N      . ALA A 1 146  ? 139.676 147.788 221.956 1.00 58.93 ? 146  ALA A N      1 
ATOM   411  C  CA     . ALA A 1 146  ? 138.813 146.887 221.204 1.00 58.93 ? 146  ALA A CA     1 
ATOM   412  C  C      . ALA A 1 146  ? 137.502 147.548 220.805 1.00 58.93 ? 146  ALA A C      1 
ATOM   413  O  O      . ALA A 1 146  ? 137.215 147.656 219.613 1.00 58.93 ? 146  ALA A O      1 
ATOM   414  C  CB     . ALA A 1 146  ? 138.558 145.617 222.018 1.00 58.93 ? 146  ALA A CB     1 
ATOM   415  N  N      . LYS A 1 147  ? 136.701 148.022 221.754 1.00 59.66 ? 147  LYS A N      1 
ATOM   416  C  CA     . LYS A 1 147  ? 135.457 148.697 221.404 1.00 59.66 ? 147  LYS A CA     1 
ATOM   417  C  C      . LYS A 1 147  ? 135.594 150.211 221.451 1.00 59.66 ? 147  LYS A C      1 
ATOM   418  O  O      . LYS A 1 147  ? 135.284 150.892 220.470 1.00 59.66 ? 147  LYS A O      1 
ATOM   419  C  CB     . LYS A 1 147  ? 134.321 148.239 222.326 1.00 59.66 ? 147  LYS A CB     1 
ATOM   420  C  CG     . LYS A 1 147  ? 133.918 146.779 222.155 1.00 59.66 ? 147  LYS A CG     1 
ATOM   421  C  CD     . LYS A 1 147  ? 133.175 146.553 220.850 1.00 59.66 ? 147  LYS A CD     1 
ATOM   422  C  CE     . LYS A 1 147  ? 132.787 145.091 220.674 1.00 59.66 ? 147  LYS A CE     1 
ATOM   423  N  NZ     . LYS A 1 147  ? 131.759 144.647 221.653 1.00 59.66 ? 147  LYS A NZ     1 
ATOM   424  N  N      . SER A 1 148  ? 136.062 150.753 222.572 1.00 60.07 ? 148  SER A N      1 
ATOM   425  C  CA     . SER A 1 148  ? 136.291 152.191 222.697 1.00 60.07 ? 148  SER A CA     1 
ATOM   426  C  C      . SER A 1 148  ? 137.692 152.527 222.184 1.00 60.07 ? 148  SER A C      1 
ATOM   427  O  O      . SER A 1 148  ? 138.620 152.815 222.935 1.00 60.07 ? 148  SER A O      1 
ATOM   428  C  CB     . SER A 1 148  ? 136.093 152.634 224.139 1.00 60.07 ? 148  SER A CB     1 
ATOM   429  O  OG     . SER A 1 148  ? 137.057 152.038 224.987 1.00 60.07 ? 148  SER A OG     1 
ATOM   430  N  N      . PHE A 1 149  ? 137.825 152.494 220.862 1.00 59.31 ? 149  PHE A N      1 
ATOM   431  C  CA     . PHE A 1 149  ? 139.102 152.709 220.191 1.00 59.31 ? 149  PHE A CA     1 
ATOM   432  C  C      . PHE A 1 149  ? 138.993 153.956 219.322 1.00 59.31 ? 149  PHE A C      1 
ATOM   433  O  O      . PHE A 1 149  ? 138.356 153.928 218.264 1.00 59.31 ? 149  PHE A O      1 
ATOM   434  C  CB     . PHE A 1 149  ? 139.483 151.489 219.358 1.00 59.31 ? 149  PHE A CB     1 
ATOM   435  C  CG     . PHE A 1 149  ? 140.804 151.612 218.660 1.00 59.31 ? 149  PHE A CG     1 
ATOM   436  C  CD1    . PHE A 1 149  ? 141.989 151.503 219.366 1.00 59.31 ? 149  PHE A CD1    1 
ATOM   437  C  CD2    . PHE A 1 149  ? 140.860 151.809 217.291 1.00 59.31 ? 149  PHE A CD2    1 
ATOM   438  C  CE1    . PHE A 1 149  ? 143.204 151.599 218.719 1.00 59.31 ? 149  PHE A CE1    1 
ATOM   439  C  CE2    . PHE A 1 149  ? 142.073 151.908 216.641 1.00 59.31 ? 149  PHE A CE2    1 
ATOM   440  C  CZ     . PHE A 1 149  ? 143.244 151.801 217.354 1.00 59.31 ? 149  PHE A CZ     1 
ATOM   441  N  N      . VAL A 1 150  ? 139.612 155.044 219.770 1.00 64.07 ? 150  VAL A N      1 
ATOM   442  C  CA     . VAL A 1 150  ? 139.630 156.308 219.045 1.00 64.07 ? 150  VAL A CA     1 
ATOM   443  C  C      . VAL A 1 150  ? 141.024 156.495 218.468 1.00 64.07 ? 150  VAL A C      1 
ATOM   444  O  O      . VAL A 1 150  ? 142.018 156.438 219.200 1.00 64.07 ? 150  VAL A O      1 
ATOM   445  C  CB     . VAL A 1 150  ? 139.239 157.483 219.957 1.00 64.07 ? 150  VAL A CB     1 
ATOM   446  C  CG1    . VAL A 1 150  ? 139.349 158.805 219.212 1.00 64.07 ? 150  VAL A CG1    1 
ATOM   447  C  CG2    . VAL A 1 150  ? 137.830 157.284 220.497 1.00 64.07 ? 150  VAL A CG2    1 
ATOM   448  N  N      . LEU A 1 151  ? 141.096 156.727 217.161 1.00 66.77 ? 151  LEU A N      1 
ATOM   449  C  CA     . LEU A 1 151  ? 142.354 156.725 216.431 1.00 66.77 ? 151  LEU A CA     1 
ATOM   450  C  C      . LEU A 1 151  ? 142.431 157.923 215.494 1.00 66.77 ? 151  LEU A C      1 
ATOM   451  O  O      . LEU A 1 151  ? 141.427 158.351 214.917 1.00 66.77 ? 151  LEU A O      1 
ATOM   452  C  CB     . LEU A 1 151  ? 142.526 155.408 215.640 1.00 66.77 ? 151  LEU A CB     1 
ATOM   453  C  CG     . LEU A 1 151  ? 141.707 155.072 214.381 1.00 66.77 ? 151  LEU A CG     1 
ATOM   454  C  CD1    . LEU A 1 151  ? 142.367 153.928 213.646 1.00 66.77 ? 151  LEU A CD1    1 
ATOM   455  C  CD2    . LEU A 1 151  ? 140.251 154.721 214.663 1.00 66.77 ? 151  LEU A CD2    1 
ATOM   456  N  N      . LYS A 1 152  ? 143.640 158.470 215.358 1.00 70.71 ? 152  LYS A N      1 
ATOM   457  C  CA     . LYS A 1 152  ? 144.011 159.616 214.534 1.00 70.71 ? 152  LYS A CA     1 
ATOM   458  C  C      . LYS A 1 152  ? 144.359 159.156 213.121 1.00 70.71 ? 152  LYS A C      1 
ATOM   459  O  O      . LYS A 1 152  ? 144.974 158.102 212.954 1.00 70.71 ? 152  LYS A O      1 
ATOM   460  C  CB     . LYS A 1 152  ? 145.206 160.351 215.134 1.00 70.71 ? 152  LYS A CB     1 
ATOM   461  C  CG     . LYS A 1 152  ? 144.935 161.046 216.457 1.00 70.71 ? 152  LYS A CG     1 
ATOM   462  C  CD     . LYS A 1 152  ? 146.173 161.798 216.934 1.00 70.71 ? 152  LYS A CD     1 
ATOM   463  C  CE     . LYS A 1 152  ? 145.946 162.450 218.289 1.00 70.71 ? 152  LYS A CE     1 
ATOM   464  N  NZ     . LYS A 1 152  ? 144.964 163.568 218.212 1.00 70.71 ? 152  LYS A NZ     1 
ATOM   465  N  N      . PRO A 1 153  ? 143.988 159.922 212.087 1.00 71.58 ? 153  PRO A N      1 
ATOM   466  C  CA     . PRO A 1 153  ? 144.183 159.423 210.710 1.00 71.58 ? 153  PRO A CA     1 
ATOM   467  C  C      . PRO A 1 153  ? 145.635 159.399 210.258 1.00 71.58 ? 153  PRO A C      1 
ATOM   468  O  O      . PRO A 1 153  ? 146.070 158.413 209.643 1.00 71.58 ? 153  PRO A O      1 
ATOM   469  C  CB     . PRO A 1 153  ? 143.334 160.387 209.870 1.00 71.58 ? 153  PRO A CB     1 
ATOM   470  C  CG     . PRO A 1 153  ? 143.266 161.639 210.683 1.00 71.58 ? 153  PRO A CG     1 
ATOM   471  C  CD     . PRO A 1 153  ? 143.263 161.205 212.118 1.00 71.58 ? 153  PRO A CD     1 
ATOM   472  N  N      . ARG A 1 154  ? 146.402 160.451 210.546 1.00 71.97 ? 154  ARG A N      1 
ATOM   473  C  CA     . ARG A 1 154  ? 147.822 160.427 210.221 1.00 71.97 ? 154  ARG A CA     1 
ATOM   474  C  C      . ARG A 1 154  ? 148.560 159.415 211.084 1.00 71.97 ? 154  ARG A C      1 
ATOM   475  O  O      . ARG A 1 154  ? 149.471 158.733 210.598 1.00 71.97 ? 154  ARG A O      1 
ATOM   476  C  CB     . ARG A 1 154  ? 148.416 161.826 210.381 1.00 71.97 ? 154  ARG A CB     1 
ATOM   477  C  CG     . ARG A 1 154  ? 149.864 161.960 209.953 1.00 71.97 ? 154  ARG A CG     1 
ATOM   478  C  CD     . ARG A 1 154  ? 150.290 163.415 209.988 1.00 71.97 ? 154  ARG A CD     1 
ATOM   479  N  NE     . ARG A 1 154  ? 149.577 164.188 208.975 1.00 71.97 ? 154  ARG A NE     1 
ATOM   480  C  CZ     . ARG A 1 154  ? 149.610 165.513 208.872 1.00 71.97 ? 154  ARG A CZ     1 
ATOM   481  N  NH1    . ARG A 1 154  ? 150.331 166.231 209.723 1.00 71.97 ? 154  ARG A NH1    1 
ATOM   482  N  NH2    . ARG A 1 154  ? 148.922 166.117 207.912 1.00 71.97 ? 154  ARG A NH2    1 
ATOM   483  N  N      . LEU A 1 155  ? 148.135 159.256 212.340 1.00 70.40 ? 155  LEU A N      1 
ATOM   484  C  CA     . LEU A 1 155  ? 148.744 158.250 213.201 1.00 70.40 ? 155  LEU A CA     1 
ATOM   485  C  C      . LEU A 1 155  ? 148.364 156.841 212.763 1.00 70.40 ? 155  LEU A C      1 
ATOM   486  O  O      . LEU A 1 155  ? 149.202 155.937 212.824 1.00 70.40 ? 155  LEU A O      1 
ATOM   487  C  CB     . LEU A 1 155  ? 148.354 158.496 214.661 1.00 70.40 ? 155  LEU A CB     1 
ATOM   488  C  CG     . LEU A 1 155  ? 149.083 157.747 215.786 1.00 70.40 ? 155  LEU A CG     1 
ATOM   489  C  CD1    . LEU A 1 155  ? 149.183 158.657 216.989 1.00 70.40 ? 155  LEU A CD1    1 
ATOM   490  C  CD2    . LEU A 1 155  ? 148.395 156.444 216.197 1.00 70.40 ? 155  LEU A CD2    1 
ATOM   491  N  N      . ARG A 1 156  ? 147.120 156.629 212.304 1.00 69.32 ? 156  ARG A N      1 
ATOM   492  C  CA     . ARG A 1 156  ? 146.756 155.287 211.854 1.00 69.32 ? 156  ARG A CA     1 
ATOM   493  C  C      . ARG A 1 156  ? 147.470 154.938 210.554 1.00 69.32 ? 156  ARG A C      1 
ATOM   494  O  O      . ARG A 1 156  ? 147.895 153.790 210.384 1.00 69.32 ? 156  ARG A O      1 
ATOM   495  C  CB     . ARG A 1 156  ? 145.230 155.120 211.701 1.00 69.32 ? 156  ARG A CB     1 
ATOM   496  C  CG     . ARG A 1 156  ? 144.580 155.660 210.417 1.00 69.32 ? 156  ARG A CG     1 
ATOM   497  C  CD     . ARG A 1 156  ? 143.060 155.579 210.367 1.00 69.32 ? 156  ARG A CD     1 
ATOM   498  N  NE     . ARG A 1 156  ? 142.416 156.582 211.206 1.00 69.32 ? 156  ARG A NE     1 
ATOM   499  C  CZ     . ARG A 1 156  ? 141.101 156.715 211.339 1.00 69.32 ? 156  ARG A CZ     1 
ATOM   500  N  NH1    . ARG A 1 156  ? 140.282 155.900 210.689 1.00 69.32 ? 156  ARG A NH1    1 
ATOM   501  N  NH2    . ARG A 1 156  ? 140.604 157.663 212.122 1.00 69.32 ? 156  ARG A NH2    1 
ATOM   502  N  N      . GLU A 1 157  ? 147.702 155.923 209.676 1.00 70.28 ? 157  GLU A N      1 
ATOM   503  C  CA     . GLU A 1 157  ? 148.390 155.613 208.431 1.00 70.28 ? 157  GLU A CA     1 
ATOM   504  C  C      . GLU A 1 157  ? 149.875 155.387 208.670 1.00 70.28 ? 157  GLU A C      1 
ATOM   505  O  O      . GLU A 1 157  ? 150.453 154.446 208.112 1.00 70.28 ? 157  GLU A O      1 
ATOM   506  C  CB     . GLU A 1 157  ? 148.168 156.723 207.401 1.00 70.28 ? 157  GLU A CB     1 
ATOM   507  C  CG     . GLU A 1 157  ? 148.804 156.438 206.042 1.00 70.28 ? 157  GLU A CG     1 
ATOM   508  C  CD     . GLU A 1 157  ? 148.170 155.255 205.321 1.00 70.28 ? 157  GLU A CD     1 
ATOM   509  O  OE1    . GLU A 1 157  ? 146.966 154.992 205.528 1.00 70.28 ? 157  GLU A OE1    1 
ATOM   510  O  OE2    . GLU A 1 157  ? 148.881 154.578 204.549 1.00 70.28 ? 157  GLU A OE2    1 
ATOM   511  N  N      . MET A 1 158  ? 150.490 156.213 209.527 1.00 68.89 ? 158  MET A N      1 
ATOM   512  C  CA     . MET A 1 158  ? 151.891 156.023 209.883 1.00 68.89 ? 158  MET A CA     1 
ATOM   513  C  C      . MET A 1 158  ? 152.109 154.700 210.604 1.00 68.89 ? 158  MET A C      1 
ATOM   514  O  O      . MET A 1 158  ? 153.061 153.972 210.293 1.00 68.89 ? 158  MET A O      1 
ATOM   515  C  CB     . MET A 1 158  ? 152.375 157.188 210.746 1.00 68.89 ? 158  MET A CB     1 
ATOM   516  C  CG     . MET A 1 158  ? 153.847 157.120 211.098 1.00 68.89 ? 158  MET A CG     1 
ATOM   517  S  SD     . MET A 1 158  ? 154.902 157.246 209.644 1.00 68.89 ? 158  MET A SD     1 
ATOM   518  C  CE     . MET A 1 158  ? 156.371 156.410 210.230 1.00 68.89 ? 158  MET A CE     1 
ATOM   519  N  N      . PHE A 1 159  ? 151.207 154.345 211.528 1.00 62.37 ? 159  PHE A N      1 
ATOM   520  C  CA     . PHE A 1 159  ? 151.351 153.097 212.263 1.00 62.37 ? 159  PHE A CA     1 
ATOM   521  C  C      . PHE A 1 159  ? 151.159 151.887 211.365 1.00 62.37 ? 159  PHE A C      1 
ATOM   522  O  O      . PHE A 1 159  ? 151.933 150.930 211.455 1.00 62.37 ? 159  PHE A O      1 
ATOM   523  C  CB     . PHE A 1 159  ? 150.371 153.033 213.432 1.00 62.37 ? 159  PHE A CB     1 
ATOM   524  C  CG     . PHE A 1 159  ? 150.389 151.712 214.146 1.00 62.37 ? 159  PHE A CG     1 
ATOM   525  C  CD1    . PHE A 1 159  ? 151.464 151.362 214.946 1.00 62.37 ? 159  PHE A CD1    1 
ATOM   526  C  CD2    . PHE A 1 159  ? 149.341 150.811 214.001 1.00 62.37 ? 159  PHE A CD2    1 
ATOM   527  C  CE1    . PHE A 1 159  ? 151.494 150.140 215.593 1.00 62.37 ? 159  PHE A CE1    1 
ATOM   528  C  CE2    . PHE A 1 159  ? 149.366 149.586 214.647 1.00 62.37 ? 159  PHE A CE2    1 
ATOM   529  C  CZ     . PHE A 1 159  ? 150.445 149.252 215.441 1.00 62.37 ? 159  PHE A CZ     1 
ATOM   530  N  N      . ARG A 1 160  ? 150.151 151.902 210.487 1.00 64.03 ? 160  ARG A N      1 
ATOM   531  C  CA     . ARG A 1 160  ? 149.937 150.713 209.675 1.00 64.03 ? 160  ARG A CA     1 
ATOM   532  C  C      . ARG A 1 160  ? 150.993 150.582 208.583 1.00 64.03 ? 160  ARG A C      1 
ATOM   533  O  O      . ARG A 1 160  ? 151.431 149.462 208.298 1.00 64.03 ? 160  ARG A O      1 
ATOM   534  C  CB     . ARG A 1 160  ? 148.519 150.688 209.096 1.00 64.03 ? 160  ARG A CB     1 
ATOM   535  C  CG     . ARG A 1 160  ? 148.186 151.638 207.962 1.00 64.03 ? 160  ARG A CG     1 
ATOM   536  C  CD     . ARG A 1 160  ? 146.732 151.450 207.577 1.00 64.03 ? 160  ARG A CD     1 
ATOM   537  N  NE     . ARG A 1 160  ? 145.836 151.866 208.651 1.00 64.03 ? 160  ARG A NE     1 
ATOM   538  C  CZ     . ARG A 1 160  ? 144.533 151.612 208.679 1.00 64.03 ? 160  ARG A CZ     1 
ATOM   539  N  NH1    . ARG A 1 160  ? 143.966 150.930 207.694 1.00 64.03 ? 160  ARG A NH1    1 
ATOM   540  N  NH2    . ARG A 1 160  ? 143.797 152.036 209.697 1.00 64.03 ? 160  ARG A NH2    1 
ATOM   541  N  N      . ARG A 1 161  ? 151.481 151.701 208.029 1.00 62.93 ? 161  ARG A N      1 
ATOM   542  C  CA     . ARG A 1 161  ? 152.557 151.627 207.047 1.00 62.93 ? 161  ARG A CA     1 
ATOM   543  C  C      . ARG A 1 161  ? 153.857 151.154 207.687 1.00 62.93 ? 161  ARG A C      1 
ATOM   544  O  O      . ARG A 1 161  ? 154.547 150.293 207.128 1.00 62.93 ? 161  ARG A O      1 
ATOM   545  C  CB     . ARG A 1 161  ? 152.745 152.986 206.377 1.00 62.93 ? 161  ARG A CB     1 
ATOM   546  C  CG     . ARG A 1 161  ? 153.761 152.988 205.250 1.00 62.93 ? 161  ARG A CG     1 
ATOM   547  C  CD     . ARG A 1 161  ? 153.864 154.366 204.624 1.00 62.93 ? 161  ARG A CD     1 
ATOM   548  N  NE     . ARG A 1 161  ? 154.339 155.359 205.583 1.00 62.93 ? 161  ARG A NE     1 
ATOM   549  C  CZ     . ARG A 1 161  ? 155.620 155.594 205.846 1.00 62.93 ? 161  ARG A CZ     1 
ATOM   550  N  NH1    . ARG A 1 161  ? 156.566 154.915 205.213 1.00 62.93 ? 161  ARG A NH1    1 
ATOM   551  N  NH2    . ARG A 1 161  ? 155.956 156.516 206.738 1.00 62.93 ? 161  ARG A NH2    1 
ATOM   552  N  N      . GLY A 1 162  ? 154.173 151.655 208.886 1.00 57.28 ? 162  GLY A N      1 
ATOM   553  C  CA     . GLY A 1 162  ? 155.374 151.209 209.570 1.00 57.28 ? 162  GLY A CA     1 
ATOM   554  C  C      . GLY A 1 162  ? 155.294 149.772 210.047 1.00 57.28 ? 162  GLY A C      1 
ATOM   555  O  O      . GLY A 1 162  ? 156.286 149.043 209.999 1.00 57.28 ? 162  GLY A O      1 
ATOM   556  N  N      . LEU A 1 163  ? 154.109 149.330 210.475 1.00 53.12 ? 163  LEU A N      1 
ATOM   557  C  CA     . LEU A 1 163  ? 153.970 147.965 210.968 1.00 53.12 ? 163  LEU A CA     1 
ATOM   558  C  C      . LEU A 1 163  ? 154.001 146.954 209.829 1.00 53.12 ? 163  LEU A C      1 
ATOM   559  O  O      . LEU A 1 163  ? 154.581 145.873 209.973 1.00 53.12 ? 163  LEU A O      1 
ATOM   560  C  CB     . LEU A 1 163  ? 152.681 147.834 211.776 1.00 53.12 ? 163  LEU A CB     1 
ATOM   561  C  CG     . LEU A 1 163  ? 152.431 146.474 212.422 1.00 53.12 ? 163  LEU A CG     1 
ATOM   562  C  CD1    . LEU A 1 163  ? 153.550 146.160 213.384 1.00 53.12 ? 163  LEU A CD1    1 
ATOM   563  C  CD2    . LEU A 1 163  ? 151.091 146.450 213.130 1.00 53.12 ? 163  LEU A CD2    1 
ATOM   564  N  N      . ILE A 1 164  ? 153.410 147.293 208.681 1.00 53.86 ? 164  ILE A N      1 
ATOM   565  C  CA     . ILE A 1 164  ? 153.507 146.411 207.522 1.00 53.86 ? 164  ILE A CA     1 
ATOM   566  C  C      . ILE A 1 164  ? 154.929 146.401 206.968 1.00 53.86 ? 164  ILE A C      1 
ATOM   567  O  O      . ILE A 1 164  ? 155.444 145.346 206.573 1.00 53.86 ? 164  ILE A O      1 
ATOM   568  C  CB     . ILE A 1 164  ? 152.459 146.817 206.467 1.00 53.86 ? 164  ILE A CB     1 
ATOM   569  C  CG1    . ILE A 1 164  ? 151.054 146.537 206.999 1.00 53.86 ? 164  ILE A CG1    1 
ATOM   570  C  CG2    . ILE A 1 164  ? 152.673 146.103 205.147 1.00 53.86 ? 164  ILE A CG2    1 
ATOM   571  C  CD1    . ILE A 1 164  ? 150.825 145.094 207.358 1.00 53.86 ? 164  ILE A CD1    1 
ATOM   572  N  N      . LYS A 1 165  ? 155.608 147.556 206.981 1.00 51.06 ? 165  LYS A N      1 
ATOM   573  C  CA     . LYS A 1 165  ? 157.005 147.599 206.562 1.00 51.06 ? 165  LYS A CA     1 
ATOM   574  C  C      . LYS A 1 165  ? 157.905 146.811 207.510 1.00 51.06 ? 165  LYS A C      1 
ATOM   575  O  O      . LYS A 1 165  ? 158.893 146.213 207.071 1.00 51.06 ? 165  LYS A O      1 
ATOM   576  C  CB     . LYS A 1 165  ? 157.464 149.056 206.463 1.00 51.06 ? 165  LYS A CB     1 
ATOM   577  C  CG     . LYS A 1 165  ? 158.865 149.262 205.907 1.00 51.06 ? 165  LYS A CG     1 
ATOM   578  C  CD     . LYS A 1 165  ? 158.936 148.880 204.440 1.00 51.06 ? 165  LYS A CD     1 
ATOM   579  C  CE     . LYS A 1 165  ? 160.334 149.085 203.888 1.00 51.06 ? 165  LYS A CE     1 
ATOM   580  N  NZ     . LYS A 1 165  ? 160.717 150.522 203.870 1.00 51.06 ? 165  LYS A NZ     1 
ATOM   581  N  N      . ALA A 1 166  ? 157.564 146.763 208.797 1.00 46.34 ? 166  ALA A N      1 
ATOM   582  C  CA     . ALA A 1 166  ? 158.355 145.985 209.740 1.00 46.34 ? 166  ALA A CA     1 
ATOM   583  C  C      . ALA A 1 166  ? 158.049 144.496 209.669 1.00 46.34 ? 166  ALA A C      1 
ATOM   584  O  O      . ALA A 1 166  ? 158.944 143.679 209.898 1.00 46.34 ? 166  ALA A O      1 
ATOM   585  C  CB     . ALA A 1 166  ? 158.127 146.494 211.162 1.00 46.34 ? 166  ALA A CB     1 
ATOM   586  N  N      . ALA A 1 167  ? 156.810 144.116 209.360 1.00 45.45 ? 167  ALA A N      1 
ATOM   587  C  CA     . ALA A 1 167  ? 156.455 142.702 209.353 1.00 45.45 ? 167  ALA A CA     1 
ATOM   588  C  C      . ALA A 1 167  ? 156.769 142.008 208.032 1.00 45.45 ? 167  ALA A C      1 
ATOM   589  O  O      . ALA A 1 167  ? 157.248 140.871 208.043 1.00 45.45 ? 167  ALA A O      1 
ATOM   590  C  CB     . ALA A 1 167  ? 154.973 142.526 209.687 1.00 45.45 ? 167  ALA A CB     1 
ATOM   591  N  N      . LYS A 1 168  ? 156.505 142.649 206.888 1.00 50.10 ? 168  LYS A N      1 
ATOM   592  C  CA     . LYS A 1 168  ? 156.711 141.968 205.611 1.00 50.10 ? 168  LYS A CA     1 
ATOM   593  C  C      . LYS A 1 168  ? 158.189 141.855 205.258 1.00 50.10 ? 168  LYS A C      1 
ATOM   594  O  O      . LYS A 1 168  ? 158.621 140.832 204.713 1.00 50.10 ? 168  LYS A O      1 
ATOM   595  C  CB     . LYS A 1 168  ? 155.954 142.675 204.489 1.00 50.10 ? 168  LYS A CB     1 
ATOM   596  C  CG     . LYS A 1 168  ? 154.457 142.447 204.495 1.00 50.10 ? 168  LYS A CG     1 
ATOM   597  C  CD     . LYS A 1 168  ? 153.805 143.090 203.277 1.00 50.10 ? 168  LYS A CD     1 
ATOM   598  C  CE     . LYS A 1 168  ? 152.298 142.894 203.271 1.00 50.10 ? 168  LYS A CE     1 
ATOM   599  N  NZ     . LYS A 1 168  ? 151.921 141.478 203.028 1.00 50.10 ? 168  LYS A NZ     1 
ATOM   600  N  N      . THR A 1 169  ? 158.980 142.889 205.556 1.00 43.93 ? 169  THR A N      1 
ATOM   601  C  CA     . THR A 1 169  ? 160.409 142.840 205.264 1.00 43.93 ? 169  THR A CA     1 
ATOM   602  C  C      . THR A 1 169  ? 161.155 141.877 206.175 1.00 43.93 ? 169  THR A C      1 
ATOM   603  O  O      . THR A 1 169  ? 162.238 141.411 205.810 1.00 43.93 ? 169  THR A O      1 
ATOM   604  C  CB     . THR A 1 169  ? 161.023 144.233 205.377 1.00 43.93 ? 169  THR A CB     1 
ATOM   605  O  OG1    . THR A 1 169  ? 160.777 144.755 206.687 1.00 43.93 ? 169  THR A OG1    1 
ATOM   606  C  CG2    . THR A 1 169  ? 160.432 145.163 204.333 1.00 43.93 ? 169  THR A CG2    1 
ATOM   607  N  N      . THR A 1 170  ? 160.593 141.560 207.335 1.00 41.33 ? 170  THR A N      1 
ATOM   608  C  CA     . THR A 1 170  ? 161.167 140.583 208.247 1.00 41.33 ? 170  THR A CA     1 
ATOM   609  C  C      . THR A 1 170  ? 160.581 139.194 208.028 1.00 41.33 ? 170  THR A C      1 
ATOM   610  O  O      . THR A 1 170  ? 161.320 138.210 207.928 1.00 41.33 ? 170  THR A O      1 
ATOM   611  C  CB     . THR A 1 170  ? 160.939 141.034 209.691 1.00 41.33 ? 170  THR A CB     1 
ATOM   612  O  OG1    . THR A 1 170  ? 161.639 142.260 209.927 1.00 41.33 ? 170  THR A OG1    1 
ATOM   613  C  CG2    . THR A 1 170  ? 161.411 139.987 210.663 1.00 41.33 ? 170  THR A CG2    1 
ATOM   614  N  N      . GLY A 1 171  ? 159.261 139.103 207.919 1.00 37.90 ? 171  GLY A N      1 
ATOM   615  C  CA     . GLY A 1 171  ? 158.595 137.820 207.943 1.00 37.90 ? 171  GLY A CA     1 
ATOM   616  C  C      . GLY A 1 171  ? 158.183 137.497 209.360 1.00 37.90 ? 171  GLY A C      1 
ATOM   617  O  O      . GLY A 1 171  ? 158.495 136.428 209.887 1.00 37.90 ? 171  GLY A O      1 
ATOM   618  N  N      . ALA A 1 172  ? 157.477 138.429 209.983 1.00 37.62 ? 172  ALA A N      1 
ATOM   619  C  CA     . ALA A 1 172  ? 157.178 138.375 211.402 1.00 37.62 ? 172  ALA A CA     1 
ATOM   620  C  C      . ALA A 1 172  ? 155.759 137.889 211.646 1.00 37.62 ? 172  ALA A C      1 
ATOM   621  O  O      . ALA A 1 172  ? 154.856 138.117 210.839 1.00 37.62 ? 172  ALA A O      1 
ATOM   622  C  CB     . ALA A 1 172  ? 157.361 139.750 212.040 1.00 37.62 ? 172  ALA A CB     1 
ATOM   623  N  N      . TRP A 1 173  ? 155.574 137.203 212.767 1.00 38.02 ? 173  TRP A N      1 
ATOM   624  C  CA     . TRP A 1 173  ? 154.236 136.917 213.250 1.00 38.02 ? 173  TRP A CA     1 
ATOM   625  C  C      . TRP A 1 173  ? 153.677 138.154 213.932 1.00 38.02 ? 173  TRP A C      1 
ATOM   626  O  O      . TRP A 1 173  ? 154.392 138.870 214.632 1.00 38.02 ? 173  TRP A O      1 
ATOM   627  C  CB     . TRP A 1 173  ? 154.245 135.756 214.241 1.00 38.02 ? 173  TRP A CB     1 
ATOM   628  C  CG     . TRP A 1 173  ? 154.598 134.425 213.672 1.00 38.02 ? 173  TRP A CG     1 
ATOM   629  C  CD1    . TRP A 1 173  ? 154.818 134.116 212.364 1.00 38.02 ? 173  TRP A CD1    1 
ATOM   630  C  CD2    . TRP A 1 173  ? 154.756 133.210 214.404 1.00 38.02 ? 173  TRP A CD2    1 
ATOM   631  N  NE1    . TRP A 1 173  ? 155.112 132.784 212.238 1.00 38.02 ? 173  TRP A NE1    1 
ATOM   632  C  CE2    . TRP A 1 173  ? 155.080 132.205 213.478 1.00 38.02 ? 173  TRP A CE2    1 
ATOM   633  C  CE3    . TRP A 1 173  ? 154.658 132.875 215.756 1.00 38.02 ? 173  TRP A CE3    1 
ATOM   634  C  CZ2    . TRP A 1 173  ? 155.306 130.888 213.860 1.00 38.02 ? 173  TRP A CZ2    1 
ATOM   635  C  CZ3    . TRP A 1 173  ? 154.891 131.572 216.133 1.00 38.02 ? 173  TRP A CZ3    1 
ATOM   636  C  CH2    . TRP A 1 173  ? 155.205 130.592 215.190 1.00 38.02 ? 173  TRP A CH2    1 
ATOM   637  N  N      . ILE A 1 174  ? 152.394 138.409 213.721 1.00 36.24 ? 174  ILE A N      1 
ATOM   638  C  CA     . ILE A 1 174  ? 151.687 139.468 214.424 1.00 36.24 ? 174  ILE A CA     1 
ATOM   639  C  C      . ILE A 1 174  ? 150.648 138.815 215.318 1.00 36.24 ? 174  ILE A C      1 
ATOM   640  O  O      . ILE A 1 174  ? 149.746 138.128 214.832 1.00 36.24 ? 174  ILE A O      1 
ATOM   641  C  CB     . ILE A 1 174  ? 151.050 140.476 213.458 1.00 36.24 ? 174  ILE A CB     1 
ATOM   642  C  CG1    . ILE A 1 174  ? 152.142 141.252 212.732 1.00 36.24 ? 174  ILE A CG1    1 
ATOM   643  C  CG2    . ILE A 1 174  ? 150.154 141.428 214.204 1.00 36.24 ? 174  ILE A CG2    1 
ATOM   644  C  CD1    . ILE A 1 174  ? 151.645 142.129 211.629 1.00 36.24 ? 174  ILE A CD1    1 
ATOM   645  N  N      . ILE A 1 175  ? 150.780 139.004 216.623 1.00 37.26 ? 175  ILE A N      1 
ATOM   646  C  CA     . ILE A 1 175  ? 149.833 138.449 217.581 1.00 37.26 ? 175  ILE A CA     1 
ATOM   647  C  C      . ILE A 1 175  ? 148.943 139.568 218.096 1.00 37.26 ? 175  ILE A C      1 
ATOM   648  O  O      . ILE A 1 175  ? 149.431 140.560 218.647 1.00 37.26 ? 175  ILE A O      1 
ATOM   649  C  CB     . ILE A 1 175  ? 150.544 137.728 218.733 1.00 37.26 ? 175  ILE A CB     1 
ATOM   650  C  CG1    . ILE A 1 175  ? 151.236 136.476 218.211 1.00 37.26 ? 175  ILE A CG1    1 
ATOM   651  C  CG2    . ILE A 1 175  ? 149.555 137.364 219.810 1.00 37.26 ? 175  ILE A CG2    1 
ATOM   652  C  CD1    . ILE A 1 175  ? 152.024 135.742 219.252 1.00 37.26 ? 175  ILE A CD1    1 
ATOM   653  N  N      . THR A 1 176  ? 147.639 139.418 217.896 1.00 41.17 ? 176  THR A N      1 
ATOM   654  C  CA     . THR A 1 176  ? 146.647 140.385 218.352 1.00 41.17 ? 176  THR A CA     1 
ATOM   655  C  C      . THR A 1 176  ? 145.525 139.576 218.998 1.00 41.17 ? 176  THR A C      1 
ATOM   656  O  O      . THR A 1 176  ? 145.682 138.398 219.338 1.00 41.17 ? 176  THR A O      1 
ATOM   657  C  CB     . THR A 1 176  ? 146.095 141.261 217.219 1.00 41.17 ? 176  THR A CB     1 
ATOM   658  O  OG1    . THR A 1 176  ? 145.432 140.430 216.267 1.00 41.17 ? 176  THR A OG1    1 
ATOM   659  C  CG2    . THR A 1 176  ? 147.172 142.060 216.510 1.00 41.17 ? 176  THR A CG2    1 
ATOM   660  N  N      . GLY A 1 177  ? 144.381 140.211 219.202 1.00 45.81 ? 177  GLY A N      1 
ATOM   661  C  CA     . GLY A 1 177  ? 143.179 139.483 219.539 1.00 45.81 ? 177  GLY A CA     1 
ATOM   662  C  C      . GLY A 1 177  ? 142.387 139.049 218.311 1.00 45.81 ? 177  GLY A C      1 
ATOM   663  O  O      . GLY A 1 177  ? 142.571 139.542 217.203 1.00 45.81 ? 177  GLY A O      1 
ATOM   664  N  N      . GLY A 1 178  ? 141.508 138.077 218.515 1.00 50.47 ? 178  GLY A N      1 
ATOM   665  C  CA     . GLY A 1 178  ? 140.565 137.676 217.490 1.00 50.47 ? 178  GLY A CA     1 
ATOM   666  C  C      . GLY A 1 178  ? 139.288 138.485 217.580 1.00 50.47 ? 178  GLY A C      1 
ATOM   667  O  O      . GLY A 1 178  ? 138.273 138.006 218.091 1.00 50.47 ? 178  GLY A O      1 
ATOM   668  N  N      . THR A 1 179  ? 139.336 139.732 217.133 1.00 53.99 ? 179  THR A N      1 
ATOM   669  C  CA     . THR A 1 179  ? 138.210 140.632 217.300 1.00 53.99 ? 179  THR A CA     1 
ATOM   670  C  C      . THR A 1 179  ? 138.143 141.553 216.092 1.00 53.99 ? 179  THR A C      1 
ATOM   671  O  O      . THR A 1 179  ? 139.163 142.087 215.657 1.00 53.99 ? 179  THR A O      1 
ATOM   672  C  CB     . THR A 1 179  ? 138.353 141.414 218.612 1.00 53.99 ? 179  THR A CB     1 
ATOM   673  O  OG1    . THR A 1 179  ? 138.247 140.510 219.720 1.00 53.99 ? 179  THR A OG1    1 
ATOM   674  C  CG2    . THR A 1 179  ? 137.313 142.500 218.743 1.00 53.99 ? 179  THR A CG2    1 
ATOM   675  N  N      . ASN A 1 180  ? 136.940 141.728 215.550 1.00 55.62 ? 180  ASN A N      1 
ATOM   676  C  CA     . ASN A 1 180  ? 136.736 142.495 214.330 1.00 55.62 ? 180  ASN A CA     1 
ATOM   677  C  C      . ASN A 1 180  ? 136.710 144.008 214.577 1.00 55.62 ? 180  ASN A C      1 
ATOM   678  O  O      . ASN A 1 180  ? 136.413 144.771 213.653 1.00 55.62 ? 180  ASN A O      1 
ATOM   679  C  CB     . ASN A 1 180  ? 135.433 142.039 213.664 1.00 55.62 ? 180  ASN A CB     1 
ATOM   680  C  CG     . ASN A 1 180  ? 135.398 142.312 212.174 1.00 55.62 ? 180  ASN A CG     1 
ATOM   681  O  OD1    . ASN A 1 180  ? 136.363 142.807 211.593 1.00 55.62 ? 180  ASN A OD1    1 
ATOM   682  N  ND2    . ASN A 1 180  ? 134.275 141.989 211.546 1.00 55.62 ? 180  ASN A ND2    1 
ATOM   683  N  N      . THR A 1 181  ? 137.014 144.476 215.785 1.00 55.92 ? 181  THR A N      1 
ATOM   684  C  CA     . THR A 1 181  ? 136.976 145.904 216.061 1.00 55.92 ? 181  THR A CA     1 
ATOM   685  C  C      . THR A 1 181  ? 138.141 146.305 216.955 1.00 55.92 ? 181  THR A C      1 
ATOM   686  O  O      . THR A 1 181  ? 138.628 145.516 217.768 1.00 55.92 ? 181  THR A O      1 
ATOM   687  C  CB     . THR A 1 181  ? 135.631 146.320 216.691 1.00 55.92 ? 181  THR A CB     1 
ATOM   688  O  OG1    . THR A 1 181  ? 135.630 147.729 216.958 1.00 55.92 ? 181  THR A OG1    1 
ATOM   689  C  CG2    . THR A 1 181  ? 135.342 145.543 217.962 1.00 55.92 ? 181  THR A CG2    1 
ATOM   690  N  N      . GLY A 1 182  ? 138.592 147.544 216.775 1.00 55.60 ? 182  GLY A N      1 
ATOM   691  C  CA     . GLY A 1 182  ? 139.666 148.101 217.570 1.00 55.60 ? 182  GLY A CA     1 
ATOM   692  C  C      . GLY A 1 182  ? 140.966 148.246 216.817 1.00 55.60 ? 182  GLY A C      1 
ATOM   693  O  O      . GLY A 1 182  ? 140.971 148.612 215.640 1.00 55.60 ? 182  GLY A O      1 
ATOM   694  N  N      . VAL A 1 183  ? 142.083 147.971 217.491 1.00 55.39 ? 183  VAL A N      1 
ATOM   695  C  CA     . VAL A 1 183  ? 143.363 147.958 216.799 1.00 55.39 ? 183  VAL A CA     1 
ATOM   696  C  C      . VAL A 1 183  ? 143.535 146.656 216.028 1.00 55.39 ? 183  VAL A C      1 
ATOM   697  O  O      . VAL A 1 183  ? 144.309 146.610 215.065 1.00 55.39 ? 183  VAL A O      1 
ATOM   698  C  CB     . VAL A 1 183  ? 144.508 148.211 217.802 1.00 55.39 ? 183  VAL A CB     1 
ATOM   699  C  CG1    . VAL A 1 183  ? 144.737 147.010 218.696 1.00 55.39 ? 183  VAL A CG1    1 
ATOM   700  C  CG2    . VAL A 1 183  ? 145.794 148.647 217.099 1.00 55.39 ? 183  VAL A CG2    1 
ATOM   701  N  N      . MET A 1 184  ? 142.791 145.610 216.402 1.00 53.91 ? 184  MET A N      1 
ATOM   702  C  CA     . MET A 1 184  ? 142.845 144.343 215.684 1.00 53.91 ? 184  MET A CA     1 
ATOM   703  C  C      . MET A 1 184  ? 142.267 144.485 214.285 1.00 53.91 ? 184  MET A C      1 
ATOM   704  O  O      . MET A 1 184  ? 142.822 143.944 213.321 1.00 53.91 ? 184  MET A O      1 
ATOM   705  C  CB     . MET A 1 184  ? 142.084 143.278 216.463 1.00 53.91 ? 184  MET A CB     1 
ATOM   706  C  CG     . MET A 1 184  ? 142.770 142.794 217.712 1.00 53.91 ? 184  MET A CG     1 
ATOM   707  S  SD     . MET A 1 184  ? 142.719 143.965 219.070 1.00 53.91 ? 184  MET A SD     1 
ATOM   708  C  CE     . MET A 1 184  ? 141.022 143.802 219.593 1.00 53.91 ? 184  MET A CE     1 
ATOM   709  N  N      . LYS A 1 185  ? 141.165 145.235 214.163 1.00 56.32 ? 185  LYS A N      1 
ATOM   710  C  CA     . LYS A 1 185  ? 140.568 145.531 212.865 1.00 56.32 ? 185  LYS A CA     1 
ATOM   711  C  C      . LYS A 1 185  ? 141.529 146.296 211.968 1.00 56.32 ? 185  LYS A C      1 
ATOM   712  O  O      . LYS A 1 185  ? 141.622 146.020 210.768 1.00 56.32 ? 185  LYS A O      1 
ATOM   713  C  CB     . LYS A 1 185  ? 139.283 146.337 213.055 1.00 56.32 ? 185  LYS A CB     1 
ATOM   714  C  CG     . LYS A 1 185  ? 138.559 146.680 211.764 1.00 56.32 ? 185  LYS A CG     1 
ATOM   715  C  CD     . LYS A 1 185  ? 137.310 147.497 212.022 1.00 56.32 ? 185  LYS A CD     1 
ATOM   716  C  CE     . LYS A 1 185  ? 136.601 147.842 210.723 1.00 56.32 ? 185  LYS A CE     1 
ATOM   717  N  NZ     . LYS A 1 185  ? 135.374 148.652 210.957 1.00 56.32 ? 185  LYS A NZ     1 
ATOM   718  N  N      . HIS A 1 186  ? 142.280 147.234 212.535 1.00 58.41 ? 186  HIS A N      1 
ATOM   719  C  CA     . HIS A 1 186  ? 143.138 148.058 211.698 1.00 58.41 ? 186  HIS A CA     1 
ATOM   720  C  C      . HIS A 1 186  ? 144.440 147.356 211.346 1.00 58.41 ? 186  HIS A C      1 
ATOM   721  O  O      . HIS A 1 186  ? 144.964 147.566 210.250 1.00 58.41 ? 186  HIS A O      1 
ATOM   722  C  CB     . HIS A 1 186  ? 143.380 149.400 212.380 1.00 58.41 ? 186  HIS A CB     1 
ATOM   723  C  CG     . HIS A 1 186  ? 142.125 150.196 212.557 1.00 58.41 ? 186  HIS A CG     1 
ATOM   724  N  ND1    . HIS A 1 186  ? 141.347 150.115 213.691 1.00 58.41 ? 186  HIS A ND1    1 
ATOM   725  C  CD2    . HIS A 1 186  ? 141.480 151.039 211.718 1.00 58.41 ? 186  HIS A CD2    1 
ATOM   726  C  CE1    . HIS A 1 186  ? 140.293 150.900 213.556 1.00 58.41 ? 186  HIS A CE1    1 
ATOM   727  N  NE2    . HIS A 1 186  ? 140.349 151.471 212.367 1.00 58.41 ? 186  HIS A NE2    1 
ATOM   728  N  N      . VAL A 1 187  ? 144.943 146.487 212.227 1.00 56.53 ? 187  VAL A N      1 
ATOM   729  C  CA     . VAL A 1 187  ? 146.057 145.614 211.861 1.00 56.53 ? 187  VAL A CA     1 
ATOM   730  C  C      . VAL A 1 187  ? 145.634 144.641 210.767 1.00 56.53 ? 187  VAL A C      1 
ATOM   731  O  O      . VAL A 1 187  ? 146.373 144.413 209.798 1.00 56.53 ? 187  VAL A O      1 
ATOM   732  C  CB     . VAL A 1 187  ? 146.597 144.888 213.109 1.00 56.53 ? 187  VAL A CB     1 
ATOM   733  C  CG1    . VAL A 1 187  ? 147.568 143.788 212.734 1.00 56.53 ? 187  VAL A CG1    1 
ATOM   734  C  CG2    . VAL A 1 187  ? 147.304 145.874 214.003 1.00 56.53 ? 187  VAL A CG2    1 
ATOM   735  N  N      . GLY A 1 188  ? 144.420 144.094 210.875 1.00 57.72 ? 188  GLY A N      1 
ATOM   736  C  CA     . GLY A 1 188  ? 143.926 143.198 209.845 1.00 57.72 ? 188  GLY A CA     1 
ATOM   737  C  C      . GLY A 1 188  ? 143.702 143.885 208.510 1.00 57.72 ? 188  GLY A C      1 
ATOM   738  O  O      . GLY A 1 188  ? 144.020 143.328 207.459 1.00 57.72 ? 188  GLY A O      1 
ATOM   739  N  N      . GLU A 1 189  ? 143.196 145.118 208.533 1.00 60.41 ? 189  GLU A N      1 
ATOM   740  C  CA     . GLU A 1 189  ? 143.038 145.864 207.291 1.00 60.41 ? 189  GLU A CA     1 
ATOM   741  C  C      . GLU A 1 189  ? 144.378 146.320 206.728 1.00 60.41 ? 189  GLU A C      1 
ATOM   742  O  O      . GLU A 1 189  ? 144.509 146.480 205.511 1.00 60.41 ? 189  GLU A O      1 
ATOM   743  C  CB     . GLU A 1 189  ? 142.117 147.063 207.503 1.00 60.41 ? 189  GLU A CB     1 
ATOM   744  C  CG     . GLU A 1 189  ? 140.657 146.696 207.686 1.00 60.41 ? 189  GLU A CG     1 
ATOM   745  C  CD     . GLU A 1 189  ? 139.775 147.906 207.919 1.00 60.41 ? 189  GLU A CD     1 
ATOM   746  O  OE1    . GLU A 1 189  ? 140.319 149.016 208.091 1.00 60.41 ? 189  GLU A OE1    1 
ATOM   747  O  OE2    . GLU A 1 189  ? 138.537 147.748 207.926 1.00 60.41 ? 189  GLU A OE2    1 
ATOM   748  N  N      . ALA A 1 190  ? 145.380 146.519 207.587 1.00 61.47 ? 190  ALA A N      1 
ATOM   749  C  CA     . ALA A 1 190  ? 146.722 146.829 207.108 1.00 61.47 ? 190  ALA A CA     1 
ATOM   750  C  C      . ALA A 1 190  ? 147.350 145.635 206.406 1.00 61.47 ? 190  ALA A C      1 
ATOM   751  O  O      . ALA A 1 190  ? 148.021 145.792 205.380 1.00 61.47 ? 190  ALA A O      1 
ATOM   752  C  CB     . ALA A 1 190  ? 147.598 147.268 208.275 1.00 61.47 ? 190  ALA A CB     1 
ATOM   753  N  N      . VAL A 1 191  ? 147.156 144.437 206.960 1.00 61.95 ? 191  VAL A N      1 
ATOM   754  C  CA     . VAL A 1 191  ? 147.639 143.223 206.311 1.00 61.95 ? 191  VAL A CA     1 
ATOM   755  C  C      . VAL A 1 191  ? 146.844 142.947 205.037 1.00 61.95 ? 191  VAL A C      1 
ATOM   756  O  O      . VAL A 1 191  ? 147.399 142.468 204.038 1.00 61.95 ? 191  VAL A O      1 
ATOM   757  C  CB     . VAL A 1 191  ? 147.588 142.055 207.319 1.00 61.95 ? 191  VAL A CB     1 
ATOM   758  C  CG1    . VAL A 1 191  ? 147.946 140.724 206.676 1.00 61.95 ? 191  VAL A CG1    1 
ATOM   759  C  CG2    . VAL A 1 191  ? 148.535 142.331 208.465 1.00 61.95 ? 191  VAL A CG2    1 
ATOM   760  N  N      . LYS A 1 192  ? 145.557 143.303 205.023 1.00 65.48 ? 192  LYS A N      1 
ATOM   761  C  CA     . LYS A 1 192  ? 144.719 143.048 203.855 1.00 65.48 ? 192  LYS A CA     1 
ATOM   762  C  C      . LYS A 1 192  ? 145.060 143.983 202.699 1.00 65.48 ? 192  LYS A C      1 
ATOM   763  O  O      . LYS A 1 192  ? 145.179 143.535 201.553 1.00 65.48 ? 192  LYS A O      1 
ATOM   764  C  CB     . LYS A 1 192  ? 143.243 143.169 204.250 1.00 65.48 ? 192  LYS A CB     1 
ATOM   765  C  CG     . LYS A 1 192  ? 142.220 142.871 203.152 1.00 65.48 ? 192  LYS A CG     1 
ATOM   766  C  CD     . LYS A 1 192  ? 141.625 144.139 202.535 1.00 65.48 ? 192  LYS A CD     1 
ATOM   767  C  CE     . LYS A 1 192  ? 140.712 144.863 203.513 1.00 65.48 ? 192  LYS A CE     1 
ATOM   768  N  NZ     . LYS A 1 192  ? 140.134 146.101 202.917 1.00 65.48 ? 192  LYS A NZ     1 
ATOM   769  N  N      . GLU A 1 193  ? 145.228 145.278 202.968 1.00 68.21 ? 193  GLU A N      1 
ATOM   770  C  CA     . GLU A 1 193  ? 145.373 146.245 201.885 1.00 68.21 ? 193  GLU A CA     1 
ATOM   771  C  C      . GLU A 1 193  ? 146.767 146.264 201.274 1.00 68.21 ? 193  GLU A C      1 
ATOM   772  O  O      . GLU A 1 193  ? 146.992 147.009 200.315 1.00 68.21 ? 193  GLU A O      1 
ATOM   773  C  CB     . GLU A 1 193  ? 145.026 147.656 202.369 1.00 68.21 ? 193  GLU A CB     1 
ATOM   774  C  CG     . GLU A 1 193  ? 146.075 148.283 203.270 1.00 68.21 ? 193  GLU A CG     1 
ATOM   775  C  CD     . GLU A 1 193  ? 145.663 149.650 203.774 1.00 68.21 ? 193  GLU A CD     1 
ATOM   776  O  OE1    . GLU A 1 193  ? 144.534 150.085 203.466 1.00 68.21 ? 193  GLU A OE1    1 
ATOM   777  O  OE2    . GLU A 1 193  ? 146.474 150.296 204.470 1.00 68.21 ? 193  GLU A OE2    1 
ATOM   778  N  N      . GLN A 1 194  ? 147.705 145.479 201.797 1.00 69.47 ? 194  GLN A N      1 
ATOM   779  C  CA     . GLN A 1 194  ? 149.059 145.424 201.267 1.00 69.47 ? 194  GLN A CA     1 
ATOM   780  C  C      . GLN A 1 194  ? 149.379 144.086 200.614 1.00 69.47 ? 194  GLN A C      1 
ATOM   781  O  O      . GLN A 1 194  ? 150.548 143.815 200.321 1.00 69.47 ? 194  GLN A O      1 
ATOM   782  C  CB     . GLN A 1 194  ? 150.063 145.728 202.377 1.00 69.47 ? 194  GLN A CB     1 
ATOM   783  C  CG     . GLN A 1 194  ? 149.960 147.139 202.915 1.00 69.47 ? 194  GLN A CG     1 
ATOM   784  C  CD     . GLN A 1 194  ? 150.426 148.177 201.917 1.00 69.47 ? 194  GLN A CD     1 
ATOM   785  O  OE1    . GLN A 1 194  ? 151.398 147.964 201.193 1.00 69.47 ? 194  GLN A OE1    1 
ATOM   786  N  NE2    . GLN A 1 194  ? 149.737 149.311 201.874 1.00 69.47 ? 194  GLN A NE2    1 
ATOM   787  N  N      . GLN A 1 195  ? 148.373 143.248 200.369 1.00 72.99 ? 195  GLN A N      1 
ATOM   788  C  CA     . GLN A 1 195  ? 148.584 141.953 199.737 1.00 72.99 ? 195  GLN A CA     1 
ATOM   789  C  C      . GLN A 1 195  ? 147.709 141.701 198.517 1.00 72.99 ? 195  GLN A C      1 
ATOM   790  O  O      . GLN A 1 195  ? 148.069 140.846 197.698 1.00 72.99 ? 195  GLN A O      1 
ATOM   791  C  CB     . GLN A 1 195  ? 148.357 140.819 200.749 1.00 72.99 ? 195  GLN A CB     1 
ATOM   792  C  CG     . GLN A 1 195  ? 146.924 140.705 201.236 1.00 72.99 ? 195  GLN A CG     1 
ATOM   793  C  CD     . GLN A 1 195  ? 146.746 139.641 202.296 1.00 72.99 ? 195  GLN A CD     1 
ATOM   794  O  OE1    . GLN A 1 195  ? 147.692 138.939 202.652 1.00 72.99 ? 195  GLN A OE1    1 
ATOM   795  N  NE2    . GLN A 1 195  ? 145.527 139.515 202.807 1.00 72.99 ? 195  GLN A NE2    1 
ATOM   796  N  N      . LEU A 1 196  ? 146.588 142.401 198.361 1.00 77.11 ? 196  LEU A N      1 
ATOM   797  C  CA     . LEU A 1 196  ? 145.682 142.159 197.245 1.00 77.11 ? 196  LEU A CA     1 
ATOM   798  C  C      . LEU A 1 196  ? 146.200 142.881 196.005 1.00 77.11 ? 196  LEU A C      1 
ATOM   799  O  O      . LEU A 1 196  ? 146.312 144.112 196.006 1.00 77.11 ? 196  LEU A O      1 
ATOM   800  C  CB     . LEU A 1 196  ? 144.271 142.618 197.603 1.00 77.11 ? 196  LEU A CB     1 
ATOM   801  C  CG     . LEU A 1 196  ? 143.626 141.838 198.753 1.00 77.11 ? 196  LEU A CG     1 
ATOM   802  C  CD1    . LEU A 1 196  ? 142.287 142.436 199.148 1.00 77.11 ? 196  LEU A CD1    1 
ATOM   803  C  CD2    . LEU A 1 196  ? 143.471 140.371 198.386 1.00 77.11 ? 196  LEU A CD2    1 
ATOM   804  N  N      . MET A 1 197  ? 146.488 142.103 194.953 1.00 79.84 ? 197  MET A N      1 
ATOM   805  C  CA     . MET A 1 197  ? 147.225 142.524 193.751 1.00 79.84 ? 197  MET A CA     1 
ATOM   806  C  C      . MET A 1 197  ? 148.609 143.061 194.141 1.00 79.84 ? 197  MET A C      1 
ATOM   807  O  O      . MET A 1 197  ? 148.962 144.221 193.916 1.00 79.84 ? 197  MET A O      1 
ATOM   808  C  CB     . MET A 1 197  ? 146.422 143.525 192.902 1.00 79.84 ? 197  MET A CB     1 
ATOM   809  C  CG     . MET A 1 197  ? 146.934 143.727 191.477 1.00 79.84 ? 197  MET A CG     1 
ATOM   810  S  SD     . MET A 1 197  ? 145.930 144.900 190.549 1.00 79.84 ? 197  MET A SD     1 
ATOM   811  C  CE     . MET A 1 197  ? 144.434 143.944 190.323 1.00 79.84 ? 197  MET A CE     1 
ATOM   812  N  N      . PHE A 1 198  ? 149.375 142.180 194.773 1.00 77.03 ? 198  PHE A N      1 
ATOM   813  C  CA     . PHE A 1 198  ? 150.757 142.433 195.170 1.00 77.03 ? 198  PHE A CA     1 
ATOM   814  C  C      . PHE A 1 198  ? 151.555 141.169 194.858 1.00 77.03 ? 198  PHE A C      1 
ATOM   815  O  O      . PHE A 1 198  ? 151.129 140.324 194.063 1.00 77.03 ? 198  PHE A O      1 
ATOM   816  C  CB     . PHE A 1 198  ? 150.842 142.858 196.644 1.00 77.03 ? 198  PHE A CB     1 
ATOM   817  C  CG     . PHE A 1 198  ? 150.451 144.287 196.892 1.00 77.03 ? 198  PHE A CG     1 
ATOM   818  C  CD1    . PHE A 1 198  ? 151.386 145.303 196.768 1.00 77.03 ? 198  PHE A CD1    1 
ATOM   819  C  CD2    . PHE A 1 198  ? 149.154 144.617 197.238 1.00 77.03 ? 198  PHE A CD2    1 
ATOM   820  C  CE1    . PHE A 1 198  ? 151.030 146.626 196.998 1.00 77.03 ? 198  PHE A CE1    1 
ATOM   821  C  CE2    . PHE A 1 198  ? 148.789 145.937 197.468 1.00 77.03 ? 198  PHE A CE2    1 
ATOM   822  C  CZ     . PHE A 1 198  ? 149.728 146.940 197.348 1.00 77.03 ? 198  PHE A CZ     1 
ATOM   823  N  N      . GLY A 1 199  ? 152.744 141.054 195.453 1.00 78.38 ? 199  GLY A N      1 
ATOM   824  C  CA     . GLY A 1 199  ? 153.557 139.870 195.262 1.00 78.38 ? 199  GLY A CA     1 
ATOM   825  C  C      . GLY A 1 199  ? 152.935 138.622 195.864 1.00 78.38 ? 199  GLY A C      1 
ATOM   826  O  O      . GLY A 1 199  ? 152.096 138.672 196.764 1.00 78.38 ? 199  GLY A O      1 
ATOM   827  N  N      . SER A 1 200  ? 153.367 137.471 195.344 1.00 77.92 ? 200  SER A N      1 
ATOM   828  C  CA     . SER A 1 200  ? 152.755 136.202 195.728 1.00 77.92 ? 200  SER A CA     1 
ATOM   829  C  C      . SER A 1 200  ? 153.258 135.710 197.079 1.00 77.92 ? 200  SER A C      1 
ATOM   830  O  O      . SER A 1 200  ? 152.467 135.227 197.897 1.00 77.92 ? 200  SER A O      1 
ATOM   831  C  CB     . SER A 1 200  ? 153.014 135.147 194.651 1.00 77.92 ? 200  SER A CB     1 
ATOM   832  O  OG     . SER A 1 200  ? 152.382 135.496 193.431 1.00 77.92 ? 200  SER A OG     1 
ATOM   833  N  N      . ASP A 1 201  ? 154.558 135.823 197.335 1.00 77.52 ? 201  ASP A N      1 
ATOM   834  C  CA     . ASP A 1 201  ? 155.149 135.356 198.590 1.00 77.52 ? 201  ASP A CA     1 
ATOM   835  C  C      . ASP A 1 201  ? 155.140 136.440 199.667 1.00 77.52 ? 201  ASP A C      1 
ATOM   836  O  O      . ASP A 1 201  ? 156.151 136.734 200.304 1.00 77.52 ? 201  ASP A O      1 
ATOM   837  C  CB     . ASP A 1 201  ? 156.559 134.835 198.330 1.00 77.52 ? 201  ASP A CB     1 
ATOM   838  C  CG     . ASP A 1 201  ? 157.442 135.843 197.605 1.00 77.52 ? 201  ASP A CG     1 
ATOM   839  O  OD1    . ASP A 1 201  ? 156.941 136.916 197.206 1.00 77.52 ? 201  ASP A OD1    1 
ATOM   840  O  OD2    . ASP A 1 201  ? 158.645 135.557 197.432 1.00 77.52 ? 201  ASP A OD2    1 
ATOM   841  N  N      . THR A 1 202  ? 153.968 137.038 199.879 1.00 73.84 ? 202  THR A N      1 
ATOM   842  C  CA     . THR A 1 202  ? 153.753 138.083 200.880 1.00 73.84 ? 202  THR A CA     1 
ATOM   843  C  C      . THR A 1 202  ? 152.581 137.628 201.743 1.00 73.84 ? 202  THR A C      1 
ATOM   844  O  O      . THR A 1 202  ? 151.425 137.951 201.454 1.00 73.84 ? 202  THR A O      1 
ATOM   845  C  CB     . THR A 1 202  ? 153.480 139.443 200.230 1.00 73.84 ? 202  THR A CB     1 
ATOM   846  O  OG1    . THR A 1 202  ? 152.324 139.348 199.387 1.00 73.84 ? 202  THR A OG1    1 
ATOM   847  C  CG2    . THR A 1 202  ? 154.676 139.913 199.407 1.00 73.84 ? 202  THR A CG2    1 
ATOM   848  N  N      . GLN A 1 203  ? 152.879 136.875 202.799 1.00 62.82 ? 203  GLN A N      1 
ATOM   849  C  CA     . GLN A 1 203  ? 151.851 136.352 203.694 1.00 62.82 ? 203  GLN A CA     1 
ATOM   850  C  C      . GLN A 1 203  ? 152.331 136.514 205.128 1.00 62.82 ? 203  GLN A C      1 
ATOM   851  O  O      . GLN A 1 203  ? 153.225 135.788 205.571 1.00 62.82 ? 203  GLN A O      1 
ATOM   852  C  CB     . GLN A 1 203  ? 151.537 134.888 203.390 1.00 62.82 ? 203  GLN A CB     1 
ATOM   853  C  CG     . GLN A 1 203  ? 150.445 134.306 204.271 1.00 62.82 ? 203  GLN A CG     1 
ATOM   854  C  CD     . GLN A 1 203  ? 150.099 132.878 203.908 1.00 62.82 ? 203  GLN A CD     1 
ATOM   855  O  OE1    . GLN A 1 203  ? 150.679 132.300 202.989 1.00 62.82 ? 203  GLN A OE1    1 
ATOM   856  N  NE2    . GLN A 1 203  ? 149.152 132.296 204.635 1.00 62.82 ? 203  GLN A NE2    1 
ATOM   857  N  N      . VAL A 1 204  ? 151.737 137.459 205.846 1.00 49.23 ? 204  VAL A N      1 
ATOM   858  C  CA     . VAL A 1 204  ? 152.044 137.684 207.252 1.00 49.23 ? 204  VAL A CA     1 
ATOM   859  C  C      . VAL A 1 204  ? 151.082 136.854 208.087 1.00 49.23 ? 204  VAL A C      1 
ATOM   860  O  O      . VAL A 1 204  ? 149.862 137.027 208.001 1.00 49.23 ? 204  VAL A O      1 
ATOM   861  C  CB     . VAL A 1 204  ? 151.946 139.173 207.614 1.00 49.23 ? 204  VAL A CB     1 
ATOM   862  C  CG1    . VAL A 1 204  ? 152.139 139.365 209.100 1.00 49.23 ? 204  VAL A CG1    1 
ATOM   863  C  CG2    . VAL A 1 204  ? 152.980 139.966 206.849 1.00 49.23 ? 204  VAL A CG2    1 
ATOM   864  N  N      . ASN A 1 205  ? 151.627 135.943 208.886 1.00 42.57 ? 205  ASN A N      1 
ATOM   865  C  CA     . ASN A 1 205  ? 150.819 135.102 209.760 1.00 42.57 ? 205  ASN A CA     1 
ATOM   866  C  C      . ASN A 1 205  ? 150.361 135.948 210.936 1.00 42.57 ? 205  ASN A C      1 
ATOM   867  O  O      . ASN A 1 205  ? 151.137 136.241 211.846 1.00 42.57 ? 205  ASN A O      1 
ATOM   868  C  CB     . ASN A 1 205  ? 151.613 133.887 210.218 1.00 42.57 ? 205  ASN A CB     1 
ATOM   869  C  CG     . ASN A 1 205  ? 152.012 132.995 209.071 1.00 42.57 ? 205  ASN A CG     1 
ATOM   870  O  OD1    . ASN A 1 205  ? 153.194 132.819 208.786 1.00 42.57 ? 205  ASN A OD1    1 
ATOM   871  N  ND2    . ASN A 1 205  ? 151.022 132.440 208.387 1.00 42.57 ? 205  ASN A ND2    1 
ATOM   872  N  N      . VAL A 1 206  ? 149.095 136.342 210.922 1.00 39.63 ? 206  VAL A N      1 
ATOM   873  C  CA     . VAL A 1 206  ? 148.542 137.237 211.928 1.00 39.63 ? 206  VAL A CA     1 
ATOM   874  C  C      . VAL A 1 206  ? 147.705 136.383 212.874 1.00 39.63 ? 206  VAL A C      1 
ATOM   875  O  O      . VAL A 1 206  ? 146.564 136.030 212.575 1.00 39.63 ? 206  VAL A O      1 
ATOM   876  C  CB     . VAL A 1 206  ? 147.728 138.363 211.292 1.00 39.63 ? 206  VAL A CB     1 
ATOM   877  C  CG1    . VAL A 1 206  ? 147.251 139.320 212.343 1.00 39.63 ? 206  VAL A CG1    1 
ATOM   878  C  CG2    . VAL A 1 206  ? 148.566 139.088 210.276 1.00 39.63 ? 206  VAL A CG2    1 
ATOM   879  N  N      . ILE A 1 207  ? 148.279 136.051 214.022 1.00 37.95 ? 207  ILE A N      1 
ATOM   880  C  CA     . ILE A 1 207  ? 147.645 135.153 214.979 1.00 37.95 ? 207  ILE A CA     1 
ATOM   881  C  C      . ILE A 1 207  ? 146.701 135.962 215.858 1.00 37.95 ? 207  ILE A C      1 
ATOM   882  O  O      . ILE A 1 207  ? 147.070 137.020 216.375 1.00 37.95 ? 207  ILE A O      1 
ATOM   883  C  CB     . ILE A 1 207  ? 148.705 134.420 215.821 1.00 37.95 ? 207  ILE A CB     1 
ATOM   884  C  CG1    . ILE A 1 207  ? 149.572 133.504 214.954 1.00 37.95 ? 207  ILE A CG1    1 
ATOM   885  C  CG2    . ILE A 1 207  ? 148.068 133.602 216.924 1.00 37.95 ? 207  ILE A CG2    1 
ATOM   886  C  CD1    . ILE A 1 207  ? 150.898 134.085 214.522 1.00 37.95 ? 207  ILE A CD1    1 
ATOM   887  N  N      . GLY A 1 208  ? 145.471 135.487 216.002 1.00 39.67 ? 208  GLY A N      1 
ATOM   888  C  CA     . GLY A 1 208  ? 144.533 136.131 216.891 1.00 39.67 ? 208  GLY A CA     1 
ATOM   889  C  C      . GLY A 1 208  ? 144.244 135.311 218.125 1.00 39.67 ? 208  GLY A C      1 
ATOM   890  O  O      . GLY A 1 208  ? 143.537 134.305 218.050 1.00 39.67 ? 208  GLY A O      1 
ATOM   891  N  N      . ILE A 1 209  ? 144.768 135.726 219.271 1.00 43.34 ? 209  ILE A N      1 
ATOM   892  C  CA     . ILE A 1 209  ? 144.499 135.039 220.527 1.00 43.34 ? 209  ILE A CA     1 
ATOM   893  C  C      . ILE A 1 209  ? 143.342 135.765 221.199 1.00 43.34 ? 209  ILE A C      1 
ATOM   894  O  O      . ILE A 1 209  ? 143.491 136.900 221.649 1.00 43.34 ? 209  ILE A O      1 
ATOM   895  C  CB     . ILE A 1 209  ? 145.736 134.993 221.429 1.00 43.34 ? 209  ILE A CB     1 
ATOM   896  C  CG1    . ILE A 1 209  ? 146.868 134.251 220.727 1.00 43.34 ? 209  ILE A CG1    1 
ATOM   897  C  CG2    . ILE A 1 209  ? 145.411 134.304 222.735 1.00 43.34 ? 209  ILE A CG2    1 
ATOM   898  C  CD1    . ILE A 1 209  ? 148.175 134.308 221.463 1.00 43.34 ? 209  ILE A CD1    1 
ATOM   899  N  N      . ALA A 1 210  ? 142.184 135.117 221.250 1.00 47.49 ? 210  ALA A N      1 
ATOM   900  C  CA     . ALA A 1 210  ? 140.974 135.701 221.803 1.00 47.49 ? 210  ALA A CA     1 
ATOM   901  C  C      . ALA A 1 210  ? 140.382 134.745 222.823 1.00 47.49 ? 210  ALA A C      1 
ATOM   902  O  O      . ALA A 1 210  ? 140.955 133.698 223.133 1.00 47.49 ? 210  ALA A O      1 
ATOM   903  C  CB     . ALA A 1 210  ? 139.945 136.002 220.711 1.00 47.49 ? 210  ALA A CB     1 
ATOM   904  N  N      . THR A 1 211  ? 139.220 135.109 223.346 1.00 53.34 ? 211  THR A N      1 
ATOM   905  C  CA     . THR A 1 211  ? 138.469 134.226 224.219 1.00 53.34 ? 211  THR A CA     1 
ATOM   906  C  C      . THR A 1 211  ? 137.367 133.542 223.424 1.00 53.34 ? 211  THR A C      1 
ATOM   907  O  O      . THR A 1 211  ? 136.798 134.116 222.494 1.00 53.34 ? 211  THR A O      1 
ATOM   908  C  CB     . THR A 1 211  ? 137.859 134.985 225.400 1.00 53.34 ? 211  THR A CB     1 
ATOM   909  O  OG1    . THR A 1 211  ? 136.880 135.908 224.922 1.00 53.34 ? 211  THR A OG1    1 
ATOM   910  C  CG2    . THR A 1 211  ? 138.917 135.764 226.132 1.00 53.34 ? 211  THR A CG2    1 
ATOM   911  N  N      . TRP A 1 212  ? 137.082 132.293 223.792 1.00 54.59 ? 212  TRP A N      1 
ATOM   912  C  CA     . TRP A 1 212  ? 135.943 131.591 223.217 1.00 54.59 ? 212  TRP A CA     1 
ATOM   913  C  C      . TRP A 1 212  ? 134.624 132.133 223.746 1.00 54.59 ? 212  TRP A C      1 
ATOM   914  O  O      . TRP A 1 212  ? 133.585 131.949 223.104 1.00 54.59 ? 212  TRP A O      1 
ATOM   915  C  CB     . TRP A 1 212  ? 136.075 130.092 223.496 1.00 54.59 ? 212  TRP A CB     1 
ATOM   916  C  CG     . TRP A 1 212  ? 134.977 129.229 222.951 1.00 54.59 ? 212  TRP A CG     1 
ATOM   917  C  CD1    . TRP A 1 212  ? 133.984 128.622 223.661 1.00 54.59 ? 212  TRP A CD1    1 
ATOM   918  C  CD2    . TRP A 1 212  ? 134.754 128.886 221.581 1.00 54.59 ? 212  TRP A CD2    1 
ATOM   919  N  NE1    . TRP A 1 212  ? 133.163 127.917 222.822 1.00 54.59 ? 212  TRP A NE1    1 
ATOM   920  C  CE2    . TRP A 1 212  ? 133.613 128.066 221.537 1.00 54.59 ? 212  TRP A CE2    1 
ATOM   921  C  CE3    . TRP A 1 212  ? 135.406 129.197 220.387 1.00 54.59 ? 212  TRP A CE3    1 
ATOM   922  C  CZ2    . TRP A 1 212  ? 133.114 127.547 220.348 1.00 54.59 ? 212  TRP A CZ2    1 
ATOM   923  C  CZ3    . TRP A 1 212  ? 134.909 128.682 219.208 1.00 54.59 ? 212  TRP A CZ3    1 
ATOM   924  C  CH2    . TRP A 1 212  ? 133.775 127.867 219.196 1.00 54.59 ? 212  TRP A CH2    1 
ATOM   925  N  N      . GLY A 1 213  ? 134.648 132.826 224.879 1.00 58.01 ? 213  GLY A N      1 
ATOM   926  C  CA     . GLY A 1 213  ? 133.460 133.383 225.478 1.00 58.01 ? 213  GLY A CA     1 
ATOM   927  C  C      . GLY A 1 213  ? 132.941 134.667 224.877 1.00 58.01 ? 213  GLY A C      1 
ATOM   928  O  O      . GLY A 1 213  ? 132.001 135.242 225.429 1.00 58.01 ? 213  GLY A O      1 
ATOM   929  N  N      . ILE A 1 214  ? 133.513 135.165 223.783 1.00 56.15 ? 214  ILE A N      1 
ATOM   930  C  CA     . ILE A 1 214  ? 132.993 136.365 223.136 1.00 56.15 ? 214  ILE A CA     1 
ATOM   931  C  C      . ILE A 1 214  ? 132.656 136.158 221.672 1.00 56.15 ? 214  ILE A C      1 
ATOM   932  O  O      . ILE A 1 214  ? 132.037 137.047 221.068 1.00 56.15 ? 214  ILE A O      1 
ATOM   933  C  CB     . ILE A 1 214  ? 133.957 137.564 223.272 1.00 56.15 ? 214  ILE A CB     1 
ATOM   934  C  CG1    . ILE A 1 214  ? 135.249 137.313 222.498 1.00 56.15 ? 214  ILE A CG1    1 
ATOM   935  C  CG2    . ILE A 1 214  ? 134.212 137.902 224.728 1.00 56.15 ? 214  ILE A CG2    1 
ATOM   936  C  CD1    . ILE A 1 214  ? 136.126 138.535 222.388 1.00 56.15 ? 214  ILE A CD1    1 
ATOM   937  N  N      . VAL A 1 215  ? 133.032 135.034 221.073 1.00 56.09 ? 215  VAL A N      1 
ATOM   938  C  CA     . VAL A 1 215  ? 132.834 134.836 219.643 1.00 56.09 ? 215  VAL A CA     1 
ATOM   939  C  C      . VAL A 1 215  ? 131.386 134.453 219.370 1.00 56.09 ? 215  VAL A C      1 
ATOM   940  O  O      . VAL A 1 215  ? 130.635 134.122 220.294 1.00 56.09 ? 215  VAL A O      1 
ATOM   941  C  CB     . VAL A 1 215  ? 133.805 133.777 219.101 1.00 56.09 ? 215  VAL A CB     1 
ATOM   942  C  CG1    . VAL A 1 215  ? 135.225 134.242 219.297 1.00 56.09 ? 215  VAL A CG1    1 
ATOM   943  C  CG2    . VAL A 1 215  ? 133.581 132.458 219.802 1.00 56.09 ? 215  VAL A CG2    1 
ATOM   944  N  N      . ASP A 1 216  ? 130.985 134.506 218.104 1.00 57.17 ? 216  ASP A N      1 
ATOM   945  C  CA     . ASP A 1 216  ? 129.625 134.150 217.714 1.00 57.17 ? 216  ASP A CA     1 
ATOM   946  C  C      . ASP A 1 216  ? 129.547 132.714 217.206 1.00 57.17 ? 216  ASP A C      1 
ATOM   947  O  O      . ASP A 1 216  ? 129.420 132.478 216.005 1.00 57.17 ? 216  ASP A O      1 
ATOM   948  C  CB     . ASP A 1 216  ? 129.109 135.113 216.644 1.00 57.17 ? 216  ASP A CB     1 
ATOM   949  C  CG     . ASP A 1 216  ? 128.868 136.507 217.185 1.00 57.17 ? 216  ASP A CG     1 
ATOM   950  O  OD1    . ASP A 1 216  ? 128.534 136.630 218.382 1.00 57.17 ? 216  ASP A OD1    1 
ATOM   951  O  OD2    . ASP A 1 216  ? 129.018 137.479 216.416 1.00 57.17 ? 216  ASP A OD2    1 
ATOM   952  N  N      . GLY A 1 243  ? 130.182 138.648 222.506 1.00 56.33 ? 243  GLY A N      1 
ATOM   953  C  CA     . GLY A 1 243  ? 131.058 139.781 222.728 1.00 56.33 ? 243  GLY A CA     1 
ATOM   954  C  C      . GLY A 1 243  ? 131.481 140.472 221.449 1.00 56.33 ? 243  GLY A C      1 
ATOM   955  O  O      . GLY A 1 243  ? 131.135 141.634 221.233 1.00 56.33 ? 243  GLY A O      1 
ATOM   956  N  N      . ALA A 1 244  ? 132.223 139.763 220.600 1.00 56.72 ? 244  ALA A N      1 
ATOM   957  C  CA     . ALA A 1 244  ? 132.666 140.328 219.334 1.00 56.72 ? 244  ALA A CA     1 
ATOM   958  C  C      . ALA A 1 244  ? 132.966 139.212 218.346 1.00 56.72 ? 244  ALA A C      1 
ATOM   959  O  O      . ALA A 1 244  ? 133.342 138.103 218.731 1.00 56.72 ? 244  ALA A O      1 
ATOM   960  C  CB     . ALA A 1 244  ? 133.901 141.213 219.512 1.00 56.72 ? 244  ALA A CB     1 
ATOM   961  N  N      . MET A 1 245  ? 132.814 139.533 217.067 1.00 59.17 ? 245  MET A N      1 
ATOM   962  C  CA     . MET A 1 245  ? 133.111 138.602 215.992 1.00 59.17 ? 245  MET A CA     1 
ATOM   963  C  C      . MET A 1 245  ? 134.616 138.568 215.736 1.00 59.17 ? 245  MET A C      1 
ATOM   964  O  O      . MET A 1 245  ? 135.320 139.556 215.953 1.00 59.17 ? 245  MET A O      1 
ATOM   965  C  CB     . MET A 1 245  ? 132.349 139.020 214.730 1.00 59.17 ? 245  MET A CB     1 
ATOM   966  C  CG     . MET A 1 245  ? 132.409 138.059 213.554 1.00 59.17 ? 245  MET A CG     1 
ATOM   967  S  SD     . MET A 1 245  ? 131.391 138.600 212.169 1.00 59.17 ? 245  MET A SD     1 
ATOM   968  C  CE     . MET A 1 245  ? 131.824 137.375 210.937 1.00 59.17 ? 245  MET A CE     1 
ATOM   969  N  N      . LEU A 1 246  ? 135.109 137.405 215.309 1.00 53.96 ? 246  LEU A N      1 
ATOM   970  C  CA     . LEU A 1 246  ? 136.499 137.267 214.901 1.00 53.96 ? 246  LEU A CA     1 
ATOM   971  C  C      . LEU A 1 246  ? 136.779 138.122 213.671 1.00 53.96 ? 246  LEU A C      1 
ATOM   972  O  O      . LEU A 1 246  ? 135.928 138.289 212.796 1.00 53.96 ? 246  LEU A O      1 
ATOM   973  C  CB     . LEU A 1 246  ? 136.827 135.807 214.593 1.00 53.96 ? 246  LEU A CB     1 
ATOM   974  C  CG     . LEU A 1 246  ? 136.788 134.771 215.717 1.00 53.96 ? 246  LEU A CG     1 
ATOM   975  C  CD1    . LEU A 1 246  ? 136.979 133.382 215.142 1.00 53.96 ? 246  LEU A CD1    1 
ATOM   976  C  CD2    . LEU A 1 246  ? 137.846 135.052 216.748 1.00 53.96 ? 246  LEU A CD2    1 
ATOM   977  N  N      . ASP A 1 247  ? 137.979 138.675 213.618 1.00 52.99 ? 247  ASP A N      1 
ATOM   978  C  CA     . ASP A 1 247  ? 138.378 139.517 212.498 1.00 52.99 ? 247  ASP A CA     1 
ATOM   979  C  C      . ASP A 1 247  ? 138.680 138.635 211.293 1.00 52.99 ? 247  ASP A C      1 
ATOM   980  O  O      . ASP A 1 247  ? 139.511 137.728 211.400 1.00 52.99 ? 247  ASP A O      1 
ATOM   981  C  CB     . ASP A 1 247  ? 139.604 140.335 212.884 1.00 52.99 ? 247  ASP A CB     1 
ATOM   982  C  CG     . ASP A 1 247  ? 139.907 141.471 211.915 1.00 52.99 ? 247  ASP A CG     1 
ATOM   983  O  OD1    . ASP A 1 247  ? 139.112 141.741 211.002 1.00 52.99 ? 247  ASP A OD1    1 
ATOM   984  O  OD2    . ASP A 1 247  ? 140.971 142.098 212.061 1.00 52.99 ? 247  ASP A OD2    1 
ATOM   985  N  N      . PRO A 1 248  ? 138.029 138.845 210.143 1.00 56.05 ? 248  PRO A N      1 
ATOM   986  C  CA     . PRO A 1 248  ? 138.275 137.970 208.987 1.00 56.05 ? 248  PRO A CA     1 
ATOM   987  C  C      . PRO A 1 248  ? 139.618 138.164 208.296 1.00 56.05 ? 248  PRO A C      1 
ATOM   988  O  O      . PRO A 1 248  ? 139.887 137.461 207.316 1.00 56.05 ? 248  PRO A O      1 
ATOM   989  C  CB     . PRO A 1 248  ? 137.124 138.324 208.037 1.00 56.05 ? 248  PRO A CB     1 
ATOM   990  C  CG     . PRO A 1 248  ? 136.699 139.681 208.438 1.00 56.05 ? 248  PRO A CG     1 
ATOM   991  C  CD     . PRO A 1 248  ? 136.871 139.726 209.918 1.00 56.05 ? 248  PRO A CD     1 
ATOM   992  N  N      . ASN A 1 249  ? 140.474 139.071 208.756 1.00 52.21 ? 249  ASN A N      1 
ATOM   993  C  CA     . ASN A 1 249  ? 141.768 139.288 208.131 1.00 52.21 ? 249  ASN A CA     1 
ATOM   994  C  C      . ASN A 1 249  ? 142.912 138.678 208.926 1.00 52.21 ? 249  ASN A C      1 
ATOM   995  O  O      . ASN A 1 249  ? 144.077 138.877 208.571 1.00 52.21 ? 249  ASN A O      1 
ATOM   996  C  CB     . ASN A 1 249  ? 142.006 140.778 207.931 1.00 52.21 ? 249  ASN A CB     1 
ATOM   997  C  CG     . ASN A 1 249  ? 140.978 141.415 207.027 1.00 52.21 ? 249  ASN A CG     1 
ATOM   998  O  OD1    . ASN A 1 249  ? 140.201 142.268 207.454 1.00 52.21 ? 249  ASN A OD1    1 
ATOM   999  N  ND2    . ASN A 1 249  ? 140.962 141.000 205.768 1.00 52.21 ? 249  ASN A ND2    1 
ATOM   1000 N  N      . HIS A 1 250  ? 142.609 137.951 209.994 1.00 44.49 ? 250  HIS A N      1 
ATOM   1001 C  CA     . HIS A 1 250  ? 143.606 137.200 210.737 1.00 44.49 ? 250  HIS A CA     1 
ATOM   1002 C  C      . HIS A 1 250  ? 143.833 135.834 210.110 1.00 44.49 ? 250  HIS A C      1 
ATOM   1003 O  O      . HIS A 1 250  ? 142.982 135.294 209.402 1.00 44.49 ? 250  HIS A O      1 
ATOM   1004 C  CB     . HIS A 1 250  ? 143.188 137.057 212.195 1.00 44.49 ? 250  HIS A CB     1 
ATOM   1005 C  CG     . HIS A 1 250  ? 143.470 138.271 213.018 1.00 44.49 ? 250  HIS A CG     1 
ATOM   1006 N  ND1    . HIS A 1 250  ? 142.764 139.443 212.880 1.00 44.49 ? 250  HIS A ND1    1 
ATOM   1007 C  CD2    . HIS A 1 250  ? 144.344 138.477 214.028 1.00 44.49 ? 250  HIS A CD2    1 
ATOM   1008 C  CE1    . HIS A 1 250  ? 143.217 140.333 213.742 1.00 44.49 ? 250  HIS A CE1    1 
ATOM   1009 N  NE2    . HIS A 1 250  ? 144.179 139.772 214.449 1.00 44.49 ? 250  HIS A NE2    1 
ATOM   1010 N  N      . SER A 1 251  ? 145.007 135.276 210.387 1.00 40.75 ? 251  SER A N      1 
ATOM   1011 C  CA     . SER A 1 251  ? 145.458 134.049 209.748 1.00 40.75 ? 251  SER A CA     1 
ATOM   1012 C  C      . SER A 1 251  ? 145.282 132.816 210.613 1.00 40.75 ? 251  SER A C      1 
ATOM   1013 O  O      . SER A 1 251  ? 145.053 131.732 210.077 1.00 40.75 ? 251  SER A O      1 
ATOM   1014 C  CB     . SER A 1 251  ? 146.932 134.175 209.359 1.00 40.75 ? 251  SER A CB     1 
ATOM   1015 O  OG     . SER A 1 251  ? 147.119 135.215 208.419 1.00 40.75 ? 251  SER A OG     1 
ATOM   1016 N  N      . HIS A 1 252  ? 145.410 132.941 211.930 1.00 40.95 ? 252  HIS A N      1 
ATOM   1017 C  CA     . HIS A 1 252  ? 145.307 131.811 212.838 1.00 40.95 ? 252  HIS A CA     1 
ATOM   1018 C  C      . HIS A 1 252  ? 144.591 132.290 214.090 1.00 40.95 ? 252  HIS A C      1 
ATOM   1019 O  O      . HIS A 1 252  ? 144.601 133.478 214.408 1.00 40.95 ? 252  HIS A O      1 
ATOM   1020 C  CB     . HIS A 1 252  ? 146.693 131.240 213.171 1.00 40.95 ? 252  HIS A CB     1 
ATOM   1021 C  CG     . HIS A 1 252  ? 147.456 130.784 211.966 1.00 40.95 ? 252  HIS A CG     1 
ATOM   1022 N  ND1    . HIS A 1 252  ? 148.224 131.642 211.211 1.00 40.95 ? 252  HIS A ND1    1 
ATOM   1023 C  CD2    . HIS A 1 252  ? 147.548 129.575 211.370 1.00 40.95 ? 252  HIS A CD2    1 
ATOM   1024 C  CE1    . HIS A 1 252  ? 148.761 130.979 210.204 1.00 40.95 ? 252  HIS A CE1    1 
ATOM   1025 N  NE2    . HIS A 1 252  ? 148.361 129.723 210.274 1.00 40.95 ? 252  HIS A NE2    1 
ATOM   1026 N  N      . PHE A 1 253  ? 143.957 131.362 214.799 1.00 43.72 ? 253  PHE A N      1 
ATOM   1027 C  CA     . PHE A 1 253  ? 143.127 131.738 215.935 1.00 43.72 ? 253  PHE A CA     1 
ATOM   1028 C  C      . PHE A 1 253  ? 143.338 130.812 217.117 1.00 43.72 ? 253  PHE A C      1 
ATOM   1029 O  O      . PHE A 1 253  ? 143.250 129.590 216.986 1.00 43.72 ? 253  PHE A O      1 
ATOM   1030 C  CB     . PHE A 1 253  ? 141.647 131.733 215.563 1.00 43.72 ? 253  PHE A CB     1 
ATOM   1031 C  CG     . PHE A 1 253  ? 141.247 132.832 214.640 1.00 43.72 ? 253  PHE A CG     1 
ATOM   1032 C  CD1    . PHE A 1 253  ? 140.993 134.099 215.127 1.00 43.72 ? 253  PHE A CD1    1 
ATOM   1033 C  CD2    . PHE A 1 253  ? 141.114 132.598 213.284 1.00 43.72 ? 253  PHE A CD2    1 
ATOM   1034 C  CE1    . PHE A 1 253  ? 140.611 135.112 214.279 1.00 43.72 ? 253  PHE A CE1    1 
ATOM   1035 C  CE2    . PHE A 1 253  ? 140.735 133.610 212.428 1.00 43.72 ? 253  PHE A CE2    1 
ATOM   1036 C  CZ     . PHE A 1 253  ? 140.478 134.866 212.928 1.00 43.72 ? 253  PHE A CZ     1 
ATOM   1037 N  N      . PHE A 1 254  ? 143.562 131.415 218.275 1.00 46.02 ? 254  PHE A N      1 
ATOM   1038 C  CA     . PHE A 1 254  ? 143.649 130.725 219.554 1.00 46.02 ? 254  PHE A CA     1 
ATOM   1039 C  C      . PHE A 1 254  ? 142.504 131.240 220.409 1.00 46.02 ? 254  PHE A C      1 
ATOM   1040 O  O      . PHE A 1 254  ? 142.467 132.425 220.749 1.00 46.02 ? 254  PHE A O      1 
ATOM   1041 C  CB     . PHE A 1 254  ? 144.995 130.992 220.220 1.00 46.02 ? 254  PHE A CB     1 
ATOM   1042 C  CG     . PHE A 1 254  ? 146.150 130.333 219.539 1.00 46.02 ? 254  PHE A CG     1 
ATOM   1043 C  CD1    . PHE A 1 254  ? 145.959 129.218 218.746 1.00 46.02 ? 254  PHE A CD1    1 
ATOM   1044 C  CD2    . PHE A 1 254  ? 147.425 130.849 219.665 1.00 46.02 ? 254  PHE A CD2    1 
ATOM   1045 C  CE1    . PHE A 1 254  ? 147.020 128.618 218.120 1.00 46.02 ? 254  PHE A CE1    1 
ATOM   1046 C  CE2    . PHE A 1 254  ? 148.490 130.256 219.031 1.00 46.02 ? 254  PHE A CE2    1 
ATOM   1047 C  CZ     . PHE A 1 254  ? 148.285 129.142 218.253 1.00 46.02 ? 254  PHE A CZ     1 
ATOM   1048 N  N      . LEU A 1 255  ? 141.562 130.369 220.739 1.00 49.38 ? 255  LEU A N      1 
ATOM   1049 C  CA     . LEU A 1 255  ? 140.339 130.761 221.424 1.00 49.38 ? 255  LEU A CA     1 
ATOM   1050 C  C      . LEU A 1 255  ? 140.375 130.110 222.802 1.00 49.38 ? 255  LEU A C      1 
ATOM   1051 O  O      . LEU A 1 255  ? 139.901 128.992 222.989 1.00 49.38 ? 255  LEU A O      1 
ATOM   1052 C  CB     . LEU A 1 255  ? 139.130 130.339 220.603 1.00 49.38 ? 255  LEU A CB     1 
ATOM   1053 C  CG     . LEU A 1 255  ? 139.160 130.973 219.211 1.00 49.38 ? 255  LEU A CG     1 
ATOM   1054 C  CD1    . LEU A 1 255  ? 138.074 130.426 218.307 1.00 49.38 ? 255  LEU A CD1    1 
ATOM   1055 C  CD2    . LEU A 1 255  ? 139.070 132.486 219.313 1.00 49.38 ? 255  LEU A CD2    1 
ATOM   1056 N  N      . VAL A 1 256  ? 140.971 130.808 223.761 1.00 53.32 ? 256  VAL A N      1 
ATOM   1057 C  CA     . VAL A 1 256  ? 141.243 130.267 225.087 1.00 53.32 ? 256  VAL A CA     1 
ATOM   1058 C  C      . VAL A 1 256  ? 140.135 130.687 226.048 1.00 53.32 ? 256  VAL A C      1 
ATOM   1059 O  O      . VAL A 1 256  ? 139.752 131.862 226.099 1.00 53.32 ? 256  VAL A O      1 
ATOM   1060 C  CB     . VAL A 1 256  ? 142.646 130.693 225.571 1.00 53.32 ? 256  VAL A CB     1 
ATOM   1061 C  CG1    . VAL A 1 256  ? 142.879 132.182 225.401 1.00 53.32 ? 256  VAL A CG1    1 
ATOM   1062 C  CG2    . VAL A 1 256  ? 142.864 130.319 227.017 1.00 53.32 ? 256  VAL A CG2    1 
ATOM   1063 N  N      . ASP A 1 257  ? 139.589 129.719 226.785 1.00 57.25 ? 257  ASP A N      1 
ATOM   1064 C  CA     . ASP A 1 257  ? 138.531 129.993 227.747 1.00 57.25 ? 257  ASP A CA     1 
ATOM   1065 C  C      . ASP A 1 257  ? 138.624 129.021 228.914 1.00 57.25 ? 257  ASP A C      1 
ATOM   1066 O  O      . ASP A 1 257  ? 139.326 128.011 228.853 1.00 57.25 ? 257  ASP A O      1 
ATOM   1067 C  CB     . ASP A 1 257  ? 137.140 129.898 227.111 1.00 57.25 ? 257  ASP A CB     1 
ATOM   1068 C  CG     . ASP A 1 257  ? 136.845 128.524 226.514 1.00 57.25 ? 257  ASP A CG     1 
ATOM   1069 O  OD1    . ASP A 1 257  ? 137.768 127.706 226.338 1.00 57.25 ? 257  ASP A OD1    1 
ATOM   1070 O  OD2    . ASP A 1 257  ? 135.660 128.248 226.246 1.00 57.25 ? 257  ASP A OD2    1 
ATOM   1071 N  N      . ASP A 1 258  ? 137.894 129.337 229.982 1.00 61.61 ? 258  ASP A N      1 
ATOM   1072 C  CA     . ASP A 1 258  ? 137.615 128.353 231.024 1.00 61.61 ? 258  ASP A CA     1 
ATOM   1073 C  C      . ASP A 1 258  ? 136.172 128.376 231.504 1.00 61.61 ? 258  ASP A C      1 
ATOM   1074 O  O      . ASP A 1 258  ? 135.735 127.404 232.129 1.00 61.61 ? 258  ASP A O      1 
ATOM   1075 C  CB     . ASP A 1 258  ? 138.534 128.572 232.230 1.00 61.61 ? 258  ASP A CB     1 
ATOM   1076 C  CG     . ASP A 1 258  ? 138.736 127.311 233.067 1.00 61.61 ? 258  ASP A CG     1 
ATOM   1077 O  OD1    . ASP A 1 258  ? 138.260 126.225 232.672 1.00 61.61 ? 258  ASP A OD1    1 
ATOM   1078 O  OD2    . ASP A 1 258  ? 139.379 127.408 234.133 1.00 61.61 ? 258  ASP A OD2    1 
ATOM   1079 N  N      . GLY A 1 259  ? 135.407 129.426 231.230 1.00 62.88 ? 259  GLY A N      1 
ATOM   1080 C  CA     . GLY A 1 259  ? 134.087 129.544 231.807 1.00 62.88 ? 259  GLY A CA     1 
ATOM   1081 C  C      . GLY A 1 259  ? 133.079 130.247 230.927 1.00 62.88 ? 259  GLY A C      1 
ATOM   1082 O  O      . GLY A 1 259  ? 133.080 130.082 229.704 1.00 62.88 ? 259  GLY A O      1 
ATOM   1083 N  N      . THR A 1 260  ? 132.222 131.050 231.551 1.00 65.40 ? 260  THR A N      1 
ATOM   1084 C  CA     . THR A 1 260  ? 131.069 131.629 230.885 1.00 65.40 ? 260  THR A CA     1 
ATOM   1085 C  C      . THR A 1 260  ? 131.483 132.806 230.001 1.00 65.40 ? 260  THR A C      1 
ATOM   1086 O  O      . THR A 1 260  ? 132.661 133.157 229.886 1.00 65.40 ? 260  THR A O      1 
ATOM   1087 C  CB     . THR A 1 260  ? 130.024 132.054 231.917 1.00 65.40 ? 260  THR A CB     1 
ATOM   1088 O  OG1    . THR A 1 260  ? 130.583 133.039 232.794 1.00 65.40 ? 260  THR A OG1    1 
ATOM   1089 C  CG2    . THR A 1 260  ? 129.564 130.858 232.742 1.00 65.40 ? 260  THR A CG2    1 
ATOM   1090 N  N      . GLU A 1 261  ? 130.490 133.426 229.372 1.00 67.13 ? 261  GLU A N      1 
ATOM   1091 C  CA     . GLU A 1 261  ? 130.715 134.520 228.444 1.00 67.13 ? 261  GLU A CA     1 
ATOM   1092 C  C      . GLU A 1 261  ? 131.007 135.816 229.193 1.00 67.13 ? 261  GLU A C      1 
ATOM   1093 O  O      . GLU A 1 261  ? 130.667 135.979 230.368 1.00 67.13 ? 261  GLU A O      1 
ATOM   1094 C  CB     . GLU A 1 261  ? 129.504 134.702 227.528 1.00 67.13 ? 261  GLU A CB     1 
ATOM   1095 C  CG     . GLU A 1 261  ? 129.314 133.588 226.501 1.00 67.13 ? 261  GLU A CG     1 
ATOM   1096 C  CD     . GLU A 1 261  ? 128.564 132.385 227.046 1.00 67.13 ? 261  GLU A CD     1 
ATOM   1097 O  OE1    . GLU A 1 261  ? 128.127 132.426 228.216 1.00 67.13 ? 261  GLU A OE1    1 
ATOM   1098 O  OE2    . GLU A 1 261  ? 128.412 131.396 226.299 1.00 67.13 ? 261  GLU A OE2    1 
ATOM   1099 N  N      . GLY A 1 262  ? 131.653 136.746 228.491 1.00 64.69 ? 262  GLY A N      1 
ATOM   1100 C  CA     . GLY A 1 262  ? 132.028 138.020 229.060 1.00 64.69 ? 262  GLY A CA     1 
ATOM   1101 C  C      . GLY A 1 262  ? 133.374 138.043 229.749 1.00 64.69 ? 262  GLY A C      1 
ATOM   1102 O  O      . GLY A 1 262  ? 133.842 139.126 230.121 1.00 64.69 ? 262  GLY A O      1 
ATOM   1103 N  N      . LYS A 1 263  ? 134.011 136.891 229.932 1.00 65.75 ? 263  LYS A N      1 
ATOM   1104 C  CA     . LYS A 1 263  ? 135.314 136.831 230.577 1.00 65.75 ? 263  LYS A CA     1 
ATOM   1105 C  C      . LYS A 1 263  ? 136.397 137.305 229.615 1.00 65.75 ? 263  LYS A C      1 
ATOM   1106 O  O      . LYS A 1 263  ? 136.372 136.986 228.423 1.00 65.75 ? 263  LYS A O      1 
ATOM   1107 C  CB     . LYS A 1 263  ? 135.602 135.403 231.047 1.00 65.75 ? 263  LYS A CB     1 
ATOM   1108 C  CG     . LYS A 1 263  ? 136.902 135.219 231.815 1.00 65.75 ? 263  LYS A CG     1 
ATOM   1109 C  CD     . LYS A 1 263  ? 136.860 135.901 233.172 1.00 65.75 ? 263  LYS A CD     1 
ATOM   1110 C  CE     . LYS A 1 263  ? 138.166 135.693 233.925 1.00 65.75 ? 263  LYS A CE     1 
ATOM   1111 N  NZ     . LYS A 1 263  ? 138.383 134.255 234.262 1.00 65.75 ? 263  LYS A NZ     1 
ATOM   1112 N  N      . TYR A 1 264  ? 137.350 138.078 230.143 1.00 60.53 ? 264  TYR A N      1 
ATOM   1113 C  CA     . TYR A 1 264  ? 138.427 138.667 229.360 1.00 60.53 ? 264  TYR A CA     1 
ATOM   1114 C  C      . TYR A 1 264  ? 139.824 138.283 229.829 1.00 60.53 ? 264  TYR A C      1 
ATOM   1115 O  O      . TYR A 1 264  ? 140.754 138.304 229.016 1.00 60.53 ? 264  TYR A O      1 
ATOM   1116 C  CB     . TYR A 1 264  ? 138.312 140.198 229.382 1.00 60.53 ? 264  TYR A CB     1 
ATOM   1117 C  CG     . TYR A 1 264  ? 137.163 140.735 228.567 1.00 60.53 ? 264  TYR A CG     1 
ATOM   1118 C  CD1    . TYR A 1 264  ? 136.665 140.025 227.486 1.00 60.53 ? 264  TYR A CD1    1 
ATOM   1119 C  CD2    . TYR A 1 264  ? 136.544 141.931 228.908 1.00 60.53 ? 264  TYR A CD2    1 
ATOM   1120 C  CE1    . TYR A 1 264  ? 135.612 140.507 226.743 1.00 60.53 ? 264  TYR A CE1    1 
ATOM   1121 C  CE2    . TYR A 1 264  ? 135.478 142.415 228.175 1.00 60.53 ? 264  TYR A CE2    1 
ATOM   1122 C  CZ     . TYR A 1 264  ? 135.020 141.699 227.090 1.00 60.53 ? 264  TYR A CZ     1 
ATOM   1123 O  OH     . TYR A 1 264  ? 133.963 142.171 226.349 1.00 60.53 ? 264  TYR A OH     1 
ATOM   1124 N  N      . GLY A 1 265  ? 139.996 137.925 231.101 1.00 61.49 ? 265  GLY A N      1 
ATOM   1125 C  CA     . GLY A 1 265  ? 141.311 137.664 231.654 1.00 61.49 ? 265  GLY A CA     1 
ATOM   1126 C  C      . GLY A 1 265  ? 141.936 136.346 231.264 1.00 61.49 ? 265  GLY A C      1 
ATOM   1127 O  O      . GLY A 1 265  ? 143.113 136.125 231.567 1.00 61.49 ? 265  GLY A O      1 
ATOM   1128 N  N      . VAL A 1 266  ? 141.183 135.464 230.607 1.00 59.15 ? 266  VAL A N      1 
ATOM   1129 C  CA     . VAL A 1 266  ? 141.731 134.175 230.201 1.00 59.15 ? 266  VAL A CA     1 
ATOM   1130 C  C      . VAL A 1 266  ? 142.537 134.301 228.908 1.00 59.15 ? 266  VAL A C      1 
ATOM   1131 O  O      . VAL A 1 266  ? 143.431 133.483 228.657 1.00 59.15 ? 266  VAL A O      1 
ATOM   1132 C  CB     . VAL A 1 266  ? 140.573 133.158 230.124 1.00 59.15 ? 266  VAL A CB     1 
ATOM   1133 C  CG1    . VAL A 1 266  ? 139.598 133.505 229.013 1.00 59.15 ? 266  VAL A CG1    1 
ATOM   1134 C  CG2    . VAL A 1 266  ? 141.077 131.721 230.014 1.00 59.15 ? 266  VAL A CG2    1 
ATOM   1135 N  N      . GLU A 1 267  ? 142.267 135.330 228.101 1.00 53.48 ? 267  GLU A N      1 
ATOM   1136 C  CA     . GLU A 1 267  ? 143.116 135.663 226.961 1.00 53.48 ? 267  GLU A CA     1 
ATOM   1137 C  C      . GLU A 1 267  ? 144.506 136.105 227.400 1.00 53.48 ? 267  GLU A C      1 
ATOM   1138 O  O      . GLU A 1 267  ? 145.497 135.790 226.730 1.00 53.48 ? 267  GLU A O      1 
ATOM   1139 C  CB     . GLU A 1 267  ? 142.446 136.771 226.148 1.00 53.48 ? 267  GLU A CB     1 
ATOM   1140 C  CG     . GLU A 1 267  ? 143.216 137.327 224.968 1.00 53.48 ? 267  GLU A CG     1 
ATOM   1141 C  CD     . GLU A 1 267  ? 142.463 138.465 224.302 1.00 53.48 ? 267  GLU A CD     1 
ATOM   1142 O  OE1    . GLU A 1 267  ? 141.319 138.744 224.721 1.00 53.48 ? 267  GLU A OE1    1 
ATOM   1143 O  OE2    . GLU A 1 267  ? 143.020 139.109 223.391 1.00 53.48 ? 267  GLU A OE2    1 
ATOM   1144 N  N      . ILE A 1 268  ? 144.590 136.793 228.540 1.00 53.79 ? 268  ILE A N      1 
ATOM   1145 C  CA     . ILE A 1 268  ? 145.777 137.566 228.896 1.00 53.79 ? 268  ILE A CA     1 
ATOM   1146 C  C      . ILE A 1 268  ? 146.937 136.649 229.268 1.00 53.79 ? 268  ILE A C      1 
ATOM   1147 O  O      . ILE A 1 268  ? 148.052 136.783 228.742 1.00 53.79 ? 268  ILE A O      1 
ATOM   1148 C  CB     . ILE A 1 268  ? 145.438 138.532 230.044 1.00 53.79 ? 268  ILE A CB     1 
ATOM   1149 C  CG1    . ILE A 1 268  ? 144.317 139.487 229.629 1.00 53.79 ? 268  ILE A CG1    1 
ATOM   1150 C  CG2    . ILE A 1 268  ? 146.657 139.293 230.462 1.00 53.79 ? 268  ILE A CG2    1 
ATOM   1151 C  CD1    . ILE A 1 268  ? 143.760 140.317 230.768 1.00 53.79 ? 268  ILE A CD1    1 
ATOM   1152 N  N      . GLY A 1 269  ? 146.690 135.706 230.178 1.00 51.20 ? 269  GLY A N      1 
ATOM   1153 C  CA     . GLY A 1 269  ? 147.756 134.833 230.640 1.00 51.20 ? 269  GLY A CA     1 
ATOM   1154 C  C      . GLY A 1 269  ? 148.234 133.871 229.572 1.00 51.20 ? 269  GLY A C      1 
ATOM   1155 O  O      . GLY A 1 269  ? 149.433 133.597 229.464 1.00 51.20 ? 269  GLY A O      1 
ATOM   1156 N  N      . MET A 1 270  ? 147.312 133.374 228.746 1.00 51.12 ? 270  MET A N      1 
ATOM   1157 C  CA     . MET A 1 270  ? 147.714 132.486 227.665 1.00 51.12 ? 270  MET A CA     1 
ATOM   1158 C  C      . MET A 1 270  ? 148.467 133.245 226.581 1.00 51.12 ? 270  MET A C      1 
ATOM   1159 O  O      . MET A 1 270  ? 149.415 132.707 226.000 1.00 51.12 ? 270  MET A O      1 
ATOM   1160 C  CB     . MET A 1 270  ? 146.498 131.776 227.074 1.00 51.12 ? 270  MET A CB     1 
ATOM   1161 C  CG     . MET A 1 270  ? 146.864 130.583 226.210 1.00 51.12 ? 270  MET A CG     1 
ATOM   1162 S  SD     . MET A 1 270  ? 147.578 129.292 227.250 1.00 51.12 ? 270  MET A SD     1 
ATOM   1163 C  CE     . MET A 1 270  ? 148.675 128.455 226.112 1.00 51.12 ? 270  MET A CE     1 
ATOM   1164 N  N      . ARG A 1 271  ? 148.086 134.500 226.321 1.00 46.26 ? 271  ARG A N      1 
ATOM   1165 C  CA     . ARG A 1 271  ? 148.821 135.314 225.359 1.00 46.26 ? 271  ARG A CA     1 
ATOM   1166 C  C      . ARG A 1 271  ? 150.214 135.657 225.870 1.00 46.26 ? 271  ARG A C      1 
ATOM   1167 O  O      . ARG A 1 271  ? 151.150 135.787 225.075 1.00 46.26 ? 271  ARG A O      1 
ATOM   1168 C  CB     . ARG A 1 271  ? 148.031 136.584 225.037 1.00 46.26 ? 271  ARG A CB     1 
ATOM   1169 C  CG     . ARG A 1 271  ? 148.637 137.452 223.949 1.00 46.26 ? 271  ARG A CG     1 
ATOM   1170 C  CD     . ARG A 1 271  ? 147.801 138.682 223.684 1.00 46.26 ? 271  ARG A CD     1 
ATOM   1171 N  NE     . ARG A 1 271  ? 148.457 139.581 222.743 1.00 46.26 ? 271  ARG A NE     1 
ATOM   1172 C  CZ     . ARG A 1 271  ? 147.947 140.738 222.344 1.00 46.26 ? 271  ARG A CZ     1 
ATOM   1173 N  NH1    . ARG A 1 271  ? 146.772 141.139 222.801 1.00 46.26 ? 271  ARG A NH1    1 
ATOM   1174 N  NH2    . ARG A 1 271  ? 148.613 141.494 221.486 1.00 46.26 ? 271  ARG A NH2    1 
ATOM   1175 N  N      . SER A 1 272  ? 150.384 135.775 227.188 1.00 48.44 ? 272  SER A N      1 
ATOM   1176 C  CA     . SER A 1 272  ? 151.729 135.983 227.719 1.00 48.44 ? 272  SER A CA     1 
ATOM   1177 C  C      . SER A 1 272  ? 152.567 134.709 227.645 1.00 48.44 ? 272  SER A C      1 
ATOM   1178 O  O      . SER A 1 272  ? 153.748 134.756 227.274 1.00 48.44 ? 272  SER A O      1 
ATOM   1179 C  CB     . SER A 1 272  ? 151.655 136.505 229.152 1.00 48.44 ? 272  SER A CB     1 
ATOM   1180 O  OG     . SER A 1 272  ? 151.072 135.552 230.019 1.00 48.44 ? 272  SER A OG     1 
ATOM   1181 N  N      . ARG A 1 273  ? 151.968 133.558 227.965 1.00 50.84 ? 273  ARG A N      1 
ATOM   1182 C  CA     . ARG A 1 273  ? 152.740 132.318 228.009 1.00 50.84 ? 273  ARG A CA     1 
ATOM   1183 C  C      . ARG A 1 273  ? 153.102 131.804 226.622 1.00 50.84 ? 273  ARG A C      1 
ATOM   1184 O  O      . ARG A 1 273  ? 154.173 131.207 226.456 1.00 50.84 ? 273  ARG A O      1 
ATOM   1185 C  CB     . ARG A 1 273  ? 151.976 131.247 228.777 1.00 50.84 ? 273  ARG A CB     1 
ATOM   1186 C  CG     . ARG A 1 273  ? 151.852 131.515 230.254 1.00 50.84 ? 273  ARG A CG     1 
ATOM   1187 C  CD     . ARG A 1 273  ? 151.053 130.416 230.893 1.00 50.84 ? 273  ARG A CD     1 
ATOM   1188 N  NE     . ARG A 1 273  ? 149.704 130.400 230.350 1.00 50.84 ? 273  ARG A NE     1 
ATOM   1189 C  CZ     . ARG A 1 273  ? 148.822 129.436 230.569 1.00 50.84 ? 273  ARG A CZ     1 
ATOM   1190 N  NH1    . ARG A 1 273  ? 149.142 128.395 231.322 1.00 50.84 ? 273  ARG A NH1    1 
ATOM   1191 N  NH2    . ARG A 1 273  ? 147.619 129.511 230.025 1.00 50.84 ? 273  ARG A NH2    1 
ATOM   1192 N  N      . ILE A 1 274  ? 152.241 132.025 225.621 1.00 49.27 ? 274  ILE A N      1 
ATOM   1193 C  CA     . ILE A 1 274  ? 152.568 131.625 224.253 1.00 49.27 ? 274  ILE A CA     1 
ATOM   1194 C  C      . ILE A 1 274  ? 153.774 132.399 223.739 1.00 49.27 ? 274  ILE A C      1 
ATOM   1195 O  O      . ILE A 1 274  ? 154.677 131.825 223.126 1.00 49.27 ? 274  ILE A O      1 
ATOM   1196 C  CB     . ILE A 1 274  ? 151.338 131.784 223.335 1.00 49.27 ? 274  ILE A CB     1 
ATOM   1197 C  CG1    . ILE A 1 274  ? 150.315 130.693 223.634 1.00 49.27 ? 274  ILE A CG1    1 
ATOM   1198 C  CG2    . ILE A 1 274  ? 151.713 131.737 221.861 1.00 49.27 ? 274  ILE A CG2    1 
ATOM   1199 C  CD1    . ILE A 1 274  ? 148.983 130.915 222.974 1.00 49.27 ? 274  ILE A CD1    1 
ATOM   1200 N  N      . GLU A 1 275  ? 153.860 133.688 224.058 1.00 47.10 ? 275  GLU A N      1 
ATOM   1201 C  CA     . GLU A 1 275  ? 155.002 134.463 223.589 1.00 47.10 ? 275  GLU A CA     1 
ATOM   1202 C  C      . GLU A 1 275  ? 156.253 134.199 224.419 1.00 47.10 ? 275  GLU A C      1 
ATOM   1203 O  O      . GLU A 1 275  ? 157.371 134.301 223.890 1.00 47.10 ? 275  GLU A O      1 
ATOM   1204 C  CB     . GLU A 1 275  ? 154.637 135.939 223.579 1.00 47.10 ? 275  GLU A CB     1 
ATOM   1205 C  CG     . GLU A 1 275  ? 153.434 136.175 222.702 1.00 47.10 ? 275  GLU A CG     1 
ATOM   1206 C  CD     . GLU A 1 275  ? 153.066 137.618 222.591 1.00 47.10 ? 275  GLU A CD     1 
ATOM   1207 O  OE1    . GLU A 1 275  ? 153.786 138.449 223.166 1.00 47.10 ? 275  GLU A OE1    1 
ATOM   1208 O  OE2    . GLU A 1 275  ? 152.035 137.915 221.959 1.00 47.10 ? 275  GLU A OE2    1 
ATOM   1209 N  N      . GLU A 1 276  ? 156.084 133.826 225.695 1.00 50.33 ? 276  GLU A N      1 
ATOM   1210 C  CA     . GLU A 1 276  ? 157.191 133.260 226.463 1.00 50.33 ? 276  GLU A CA     1 
ATOM   1211 C  C      . GLU A 1 276  ? 157.751 132.017 225.783 1.00 50.33 ? 276  GLU A C      1 
ATOM   1212 O  O      . GLU A 1 276  ? 158.969 131.868 225.634 1.00 50.33 ? 276  GLU A O      1 
ATOM   1213 C  CB     . GLU A 1 276  ? 156.735 132.911 227.878 1.00 50.33 ? 276  GLU A CB     1 
ATOM   1214 C  CG     . GLU A 1 276  ? 157.858 132.390 228.757 1.00 50.33 ? 276  GLU A CG     1 
ATOM   1215 C  CD     . GLU A 1 276  ? 157.371 131.866 230.091 1.00 50.33 ? 276  GLU A CD     1 
ATOM   1216 O  OE1    . GLU A 1 276  ? 156.143 131.819 230.300 1.00 50.33 ? 276  GLU A OE1    1 
ATOM   1217 O  OE2    . GLU A 1 276  ? 158.217 131.492 230.929 1.00 50.33 ? 276  GLU A OE2    1 
ATOM   1218 N  N      . ALA A 1 277  ? 156.868 131.125 225.335 1.00 51.26 ? 277  ALA A N      1 
ATOM   1219 C  CA     . ALA A 1 277  ? 157.313 129.907 224.673 1.00 51.26 ? 277  ALA A CA     1 
ATOM   1220 C  C      . ALA A 1 277  ? 157.844 130.160 223.267 1.00 51.26 ? 277  ALA A C      1 
ATOM   1221 O  O      . ALA A 1 277  ? 158.619 129.343 222.760 1.00 51.26 ? 277  ALA A O      1 
ATOM   1222 C  CB     . ALA A 1 277  ? 156.176 128.893 224.634 1.00 51.26 ? 277  ALA A CB     1 
ATOM   1223 N  N      . ILE A 1 278  ? 157.437 131.255 222.621 1.00 47.81 ? 278  ILE A N      1 
ATOM   1224 C  CA     . ILE A 1 278  ? 158.075 131.646 221.366 1.00 47.81 ? 278  ILE A CA     1 
ATOM   1225 C  C      . ILE A 1 278  ? 159.502 132.110 221.625 1.00 47.81 ? 278  ILE A C      1 
ATOM   1226 O  O      . ILE A 1 278  ? 160.427 131.767 220.878 1.00 47.81 ? 278  ILE A O      1 
ATOM   1227 C  CB     . ILE A 1 278  ? 157.255 132.726 220.636 1.00 47.81 ? 278  ILE A CB     1 
ATOM   1228 C  CG1    . ILE A 1 278  ? 155.908 132.189 220.190 1.00 47.81 ? 278  ILE A CG1    1 
ATOM   1229 C  CG2    . ILE A 1 278  ? 157.947 133.159 219.384 1.00 47.81 ? 278  ILE A CG2    1 
ATOM   1230 C  CD1    . ILE A 1 278  ? 154.958 133.256 219.713 1.00 47.81 ? 278  ILE A CD1    1 
ATOM   1231 N  N      . MET A 1 279  ? 159.715 132.872 222.700 1.00 48.57 ? 279  MET A N      1 
ATOM   1232 C  CA     . MET A 1 279  ? 161.084 133.237 223.054 1.00 48.57 ? 279  MET A CA     1 
ATOM   1233 C  C      . MET A 1 279  ? 161.907 132.048 223.539 1.00 48.57 ? 279  MET A C      1 
ATOM   1234 O  O      . MET A 1 279  ? 163.138 132.093 223.456 1.00 48.57 ? 279  MET A O      1 
ATOM   1235 C  CB     . MET A 1 279  ? 161.098 134.327 224.117 1.00 48.57 ? 279  MET A CB     1 
ATOM   1236 C  CG     . MET A 1 279  ? 160.608 135.658 223.634 1.00 48.57 ? 279  MET A CG     1 
ATOM   1237 S  SD     . MET A 1 279  ? 160.721 136.871 224.942 1.00 48.57 ? 279  MET A SD     1 
ATOM   1238 C  CE     . MET A 1 279  ? 159.511 136.164 226.038 1.00 48.57 ? 279  MET A CE     1 
ATOM   1239 N  N      . LYS A 1 280  ? 161.265 130.989 224.040 1.00 51.92 ? 280  LYS A N      1 
ATOM   1240 C  CA     . LYS A 1 280  ? 162.011 129.779 224.367 1.00 51.92 ? 280  LYS A CA     1 
ATOM   1241 C  C      . LYS A 1 280  ? 162.462 129.018 223.126 1.00 51.92 ? 280  LYS A C      1 
ATOM   1242 O  O      . LYS A 1 280  ? 163.422 128.246 223.208 1.00 51.92 ? 280  LYS A O      1 
ATOM   1243 C  CB     . LYS A 1 280  ? 161.185 128.854 225.260 1.00 51.92 ? 280  LYS A CB     1 
ATOM   1244 C  CG     . LYS A 1 280  ? 160.875 129.424 226.630 1.00 51.92 ? 280  LYS A CG     1 
ATOM   1245 C  CD     . LYS A 1 280  ? 162.130 129.567 227.466 1.00 51.92 ? 280  LYS A CD     1 
ATOM   1246 C  CE     . LYS A 1 280  ? 161.819 130.162 228.827 1.00 51.92 ? 280  LYS A CE     1 
ATOM   1247 N  NZ     . LYS A 1 280  ? 161.030 129.229 229.671 1.00 51.92 ? 280  LYS A NZ     1 
ATOM   1248 N  N      . VAL A 1 281  ? 161.802 129.209 221.988 1.00 49.77 ? 281  VAL A N      1 
ATOM   1249 C  CA     . VAL A 1 281  ? 162.224 128.551 220.757 1.00 49.77 ? 281  VAL A CA     1 
ATOM   1250 C  C      . VAL A 1 281  ? 162.809 129.571 219.794 1.00 49.77 ? 281  VAL A C      1 
ATOM   1251 O  O      . VAL A 1 281  ? 163.901 129.379 219.259 1.00 49.77 ? 281  VAL A O      1 
ATOM   1252 C  CB     . VAL A 1 281  ? 161.067 127.789 220.093 1.00 49.77 ? 281  VAL A CB     1 
ATOM   1253 C  CG1    . VAL A 1 281  ? 160.009 128.749 219.596 1.00 49.77 ? 281  VAL A CG1    1 
ATOM   1254 C  CG2    . VAL A 1 281  ? 161.587 126.940 218.948 1.00 49.77 ? 281  VAL A CG2    1 
ATOM   1255 N  N      . ILE A 1 292  ? 167.247 134.271 224.293 1.00 48.47 ? 292  ILE A N      1 
ATOM   1256 C  CA     . ILE A 1 292  ? 165.981 133.892 223.682 1.00 48.47 ? 292  ILE A CA     1 
ATOM   1257 C  C      . ILE A 1 292  ? 166.209 133.491 222.232 1.00 48.47 ? 292  ILE A C      1 
ATOM   1258 O  O      . ILE A 1 292  ? 167.229 133.833 221.635 1.00 48.47 ? 292  ILE A O      1 
ATOM   1259 C  CB     . ILE A 1 292  ? 164.951 135.028 223.779 1.00 48.47 ? 292  ILE A CB     1 
ATOM   1260 C  CG1    . ILE A 1 292  ? 165.422 136.241 222.983 1.00 48.47 ? 292  ILE A CG1    1 
ATOM   1261 C  CG2    . ILE A 1 292  ? 164.717 135.412 225.229 1.00 48.47 ? 292  ILE A CG2    1 
ATOM   1262 C  CD1    . ILE A 1 292  ? 164.386 137.316 222.853 1.00 48.47 ? 292  ILE A CD1    1 
ATOM   1263 N  N      . GLY A 1 293  ? 165.256 132.756 221.667 1.00 47.27 ? 293  GLY A N      1 
ATOM   1264 C  CA     . GLY A 1 293  ? 165.379 132.303 220.298 1.00 47.27 ? 293  GLY A CA     1 
ATOM   1265 C  C      . GLY A 1 293  ? 164.746 133.242 219.295 1.00 47.27 ? 293  GLY A C      1 
ATOM   1266 O  O      . GLY A 1 293  ? 165.395 133.665 218.334 1.00 47.27 ? 293  GLY A O      1 
ATOM   1267 N  N      . VAL A 1 294  ? 163.481 133.578 219.509 1.00 42.41 ? 294  VAL A N      1 
ATOM   1268 C  CA     . VAL A 1 294  ? 162.729 134.462 218.627 1.00 42.41 ? 294  VAL A CA     1 
ATOM   1269 C  C      . VAL A 1 294  ? 162.471 135.763 219.380 1.00 42.41 ? 294  VAL A C      1 
ATOM   1270 O  O      . VAL A 1 294  ? 161.884 135.735 220.468 1.00 42.41 ? 294  VAL A O      1 
ATOM   1271 C  CB     . VAL A 1 294  ? 161.413 133.821 218.166 1.00 42.41 ? 294  VAL A CB     1 
ATOM   1272 C  CG1    . VAL A 1 294  ? 160.627 134.790 217.301 1.00 42.41 ? 294  VAL A CG1    1 
ATOM   1273 C  CG2    . VAL A 1 294  ? 161.686 132.534 217.414 1.00 42.41 ? 294  VAL A CG2    1 
ATOM   1274 N  N      . PRO A 1 295  ? 162.885 136.906 218.852 1.00 39.14 ? 295  PRO A N      1 
ATOM   1275 C  CA     . PRO A 1 295  ? 162.720 138.168 219.583 1.00 39.14 ? 295  PRO A CA     1 
ATOM   1276 C  C      . PRO A 1 295  ? 161.300 138.715 219.570 1.00 39.14 ? 295  PRO A C      1 
ATOM   1277 O  O      . PRO A 1 295  ? 160.944 139.510 218.701 1.00 39.14 ? 295  PRO A O      1 
ATOM   1278 C  CB     . PRO A 1 295  ? 163.694 139.109 218.866 1.00 39.14 ? 295  PRO A CB     1 
ATOM   1279 C  CG     . PRO A 1 295  ? 163.833 138.544 217.516 1.00 39.14 ? 295  PRO A CG     1 
ATOM   1280 C  CD     . PRO A 1 295  ? 163.714 137.068 217.647 1.00 39.14 ? 295  PRO A CD     1 
ATOM   1281 N  N      . VAL A 1 296  ? 160.472 138.281 220.519 1.00 38.15 ? 296  VAL A N      1 
ATOM   1282 C  CA     . VAL A 1 296  ? 159.122 138.819 220.648 1.00 38.15 ? 296  VAL A CA     1 
ATOM   1283 C  C      . VAL A 1 296  ? 159.190 140.247 221.175 1.00 38.15 ? 296  VAL A C      1 
ATOM   1284 O  O      . VAL A 1 296  ? 159.916 140.539 222.131 1.00 38.15 ? 296  VAL A O      1 
ATOM   1285 C  CB     . VAL A 1 296  ? 158.280 137.922 221.568 1.00 38.15 ? 296  VAL A CB     1 
ATOM   1286 C  CG1    . VAL A 1 296  ? 156.878 138.476 221.748 1.00 38.15 ? 296  VAL A CG1    1 
ATOM   1287 C  CG2    . VAL A 1 296  ? 158.213 136.522 221.017 1.00 38.15 ? 296  VAL A CG2    1 
ATOM   1288 N  N      . VAL A 1 297  ? 158.437 141.148 220.541 1.00 36.11 ? 297  VAL A N      1 
ATOM   1289 C  CA     . VAL A 1 297  ? 158.325 142.541 220.946 1.00 36.11 ? 297  VAL A CA     1 
ATOM   1290 C  C      . VAL A 1 297  ? 156.840 142.852 221.130 1.00 36.11 ? 297  VAL A C      1 
ATOM   1291 O  O      . VAL A 1 297  ? 155.970 142.159 220.603 1.00 36.11 ? 297  VAL A O      1 
ATOM   1292 C  CB     . VAL A 1 297  ? 158.982 143.478 219.903 1.00 36.11 ? 297  VAL A CB     1 
ATOM   1293 C  CG1    . VAL A 1 297  ? 158.112 143.601 218.664 1.00 36.11 ? 297  VAL A CG1    1 
ATOM   1294 C  CG2    . VAL A 1 297  ? 159.363 144.832 220.490 1.00 36.11 ? 297  VAL A CG2    1 
ATOM   1295 N  N      . LEU A 1 298  ? 156.554 143.884 221.920 1.00 37.91 ? 298  LEU A N      1 
ATOM   1296 C  CA     . LEU A 1 298  ? 155.195 144.316 222.226 1.00 37.91 ? 298  LEU A CA     1 
ATOM   1297 C  C      . LEU A 1 298  ? 154.989 145.762 221.795 1.00 37.91 ? 298  LEU A C      1 
ATOM   1298 O  O      . LEU A 1 298  ? 155.754 146.644 222.190 1.00 37.91 ? 298  LEU A O      1 
ATOM   1299 C  CB     . LEU A 1 298  ? 154.913 144.164 223.721 1.00 37.91 ? 298  LEU A CB     1 
ATOM   1300 C  CG     . LEU A 1 298  ? 153.624 144.734 224.313 1.00 37.91 ? 298  LEU A CG     1 
ATOM   1301 C  CD1    . LEU A 1 298  ? 152.394 144.145 223.697 1.00 37.91 ? 298  LEU A CD1    1 
ATOM   1302 C  CD2    . LEU A 1 298  ? 153.593 144.531 225.816 1.00 37.91 ? 298  LEU A CD2    1 
ATOM   1303 N  N      . LEU A 1 299  ? 153.961 146.001 220.984 1.00 40.88 ? 299  LEU A N      1 
ATOM   1304 C  CA     . LEU A 1 299  ? 153.493 147.341 220.658 1.00 40.88 ? 299  LEU A CA     1 
ATOM   1305 C  C      . LEU A 1 299  ? 152.199 147.604 221.413 1.00 40.88 ? 299  LEU A C      1 
ATOM   1306 O  O      . LEU A 1 299  ? 151.294 146.767 221.403 1.00 40.88 ? 299  LEU A O      1 
ATOM   1307 C  CB     . LEU A 1 299  ? 153.253 147.511 219.160 1.00 40.88 ? 299  LEU A CB     1 
ATOM   1308 C  CG     . LEU A 1 299  ? 154.438 147.393 218.209 1.00 40.88 ? 299  LEU A CG     1 
ATOM   1309 C  CD1    . LEU A 1 299  ? 153.940 147.532 216.798 1.00 40.88 ? 299  LEU A CD1    1 
ATOM   1310 C  CD2    . LEU A 1 299  ? 155.488 148.432 218.492 1.00 40.88 ? 299  LEU A CD2    1 
ATOM   1311 N  N      . VAL A 1 300  ? 152.121 148.756 222.072 1.00 46.41 ? 300  VAL A N      1 
ATOM   1312 C  CA     . VAL A 1 300  ? 150.956 149.162 222.850 1.00 46.41 ? 300  VAL A CA     1 
ATOM   1313 C  C      . VAL A 1 300  ? 150.499 150.511 222.320 1.00 46.41 ? 300  VAL A C      1 
ATOM   1314 O  O      . VAL A 1 300  ? 151.292 151.458 222.276 1.00 46.41 ? 300  VAL A O      1 
ATOM   1315 C  CB     . VAL A 1 300  ? 151.277 149.246 224.350 1.00 46.41 ? 300  VAL A CB     1 
ATOM   1316 C  CG1    . VAL A 1 300  ? 150.110 149.832 225.112 1.00 46.41 ? 300  VAL A CG1    1 
ATOM   1317 C  CG2    . VAL A 1 300  ? 151.636 147.884 224.894 1.00 46.41 ? 300  VAL A CG2    1 
ATOM   1318 N  N      . LEU A 1 301  ? 149.231 150.605 221.918 1.00 54.28 ? 301  LEU A N      1 
ATOM   1319 C  CA     . LEU A 1 301  ? 148.725 151.864 221.376 1.00 54.28 ? 301  LEU A CA     1 
ATOM   1320 C  C      . LEU A 1 301  ? 147.224 151.984 221.597 1.00 54.28 ? 301  LEU A C      1 
ATOM   1321 O  O      . LEU A 1 301  ? 146.469 151.086 221.222 1.00 54.28 ? 301  LEU A O      1 
ATOM   1322 C  CB     . LEU A 1 301  ? 149.079 152.009 219.885 1.00 54.28 ? 301  LEU A CB     1 
ATOM   1323 C  CG     . LEU A 1 301  ? 148.477 151.203 218.727 1.00 54.28 ? 301  LEU A CG     1 
ATOM   1324 C  CD1    . LEU A 1 301  ? 148.733 151.916 217.416 1.00 54.28 ? 301  LEU A CD1    1 
ATOM   1325 C  CD2    . LEU A 1 301  ? 149.028 149.792 218.684 1.00 54.28 ? 301  LEU A CD2    1 
ATOM   1326 N  N      . GLU A 1 302  ? 146.816 153.086 222.241 1.00 59.42 ? 302  GLU A N      1 
ATOM   1327 C  CA     . GLU A 1 302  ? 145.420 153.548 222.313 1.00 59.42 ? 302  GLU A CA     1 
ATOM   1328 C  C      . GLU A 1 302  ? 144.509 152.544 223.015 1.00 59.42 ? 302  GLU A C      1 
ATOM   1329 O  O      . GLU A 1 302  ? 143.371 152.320 222.597 1.00 59.42 ? 302  GLU A O      1 
ATOM   1330 C  CB     . GLU A 1 302  ? 144.873 153.873 220.920 1.00 59.42 ? 302  GLU A CB     1 
ATOM   1331 C  CG     . GLU A 1 302  ? 145.688 154.894 220.169 1.00 59.42 ? 302  GLU A CG     1 
ATOM   1332 C  CD     . GLU A 1 302  ? 145.108 155.270 218.827 1.00 59.42 ? 302  GLU A CD     1 
ATOM   1333 O  OE1    . GLU A 1 302  ? 144.123 154.637 218.413 1.00 59.42 ? 302  GLU A OE1    1 
ATOM   1334 O  OE2    . GLU A 1 302  ? 145.635 156.203 218.185 1.00 59.42 ? 302  GLU A OE2    1 
ATOM   1335 N  N      . GLY A 1 303  ? 144.998 151.944 224.099 1.00 56.33 ? 303  GLY A N      1 
ATOM   1336 C  CA     . GLY A 1 303  ? 144.331 150.824 224.723 1.00 56.33 ? 303  GLY A CA     1 
ATOM   1337 C  C      . GLY A 1 303  ? 143.501 151.207 225.933 1.00 56.33 ? 303  GLY A C      1 
ATOM   1338 O  O      . GLY A 1 303  ? 143.179 152.370 226.166 1.00 56.33 ? 303  GLY A O      1 
ATOM   1339 N  N      . GLY A 1 304  ? 143.147 150.192 226.714 1.00 54.60 ? 304  GLY A N      1 
ATOM   1340 C  CA     . GLY A 1 304  ? 142.357 150.378 227.906 1.00 54.60 ? 304  GLY A CA     1 
ATOM   1341 C  C      . GLY A 1 304  ? 142.889 149.588 229.085 1.00 54.60 ? 304  GLY A C      1 
ATOM   1342 O  O      . GLY A 1 304  ? 144.101 149.497 229.301 1.00 54.60 ? 304  GLY A O      1 
ATOM   1343 N  N      . PRO A 1 305  ? 141.985 149.005 229.880 1.00 54.12 ? 305  PRO A N      1 
ATOM   1344 C  CA     . PRO A 1 305  ? 142.440 148.240 231.055 1.00 54.12 ? 305  PRO A CA     1 
ATOM   1345 C  C      . PRO A 1 305  ? 143.063 146.898 230.711 1.00 54.12 ? 305  PRO A C      1 
ATOM   1346 O  O      . PRO A 1 305  ? 144.096 146.533 231.288 1.00 54.12 ? 305  PRO A O      1 
ATOM   1347 C  CB     . PRO A 1 305  ? 141.152 148.066 231.874 1.00 54.12 ? 305  PRO A CB     1 
ATOM   1348 C  CG     . PRO A 1 305  ? 140.228 149.123 231.378 1.00 54.12 ? 305  PRO A CG     1 
ATOM   1349 C  CD     . PRO A 1 305  ? 140.538 149.263 229.925 1.00 54.12 ? 305  PRO A CD     1 
ATOM   1350 N  N      . ASN A 1 306  ? 142.463 146.133 229.795 1.00 53.46 ? 306  ASN A N      1 
ATOM   1351 C  CA     . ASN A 1 306  ? 143.061 144.855 229.431 1.00 53.46 ? 306  ASN A CA     1 
ATOM   1352 C  C      . ASN A 1 306  ? 144.305 145.031 228.577 1.00 53.46 ? 306  ASN A C      1 
ATOM   1353 O  O      . ASN A 1 306  ? 145.142 144.127 228.539 1.00 53.46 ? 306  ASN A O      1 
ATOM   1354 C  CB     . ASN A 1 306  ? 142.057 143.969 228.703 1.00 53.46 ? 306  ASN A CB     1 
ATOM   1355 C  CG     . ASN A 1 306  ? 140.975 143.455 229.615 1.00 53.46 ? 306  ASN A CG     1 
ATOM   1356 O  OD1    . ASN A 1 306  ? 141.232 143.115 230.768 1.00 53.46 ? 306  ASN A OD1    1 
ATOM   1357 N  ND2    . ASN A 1 306  ? 139.755 143.382 229.102 1.00 53.46 ? 306  ASN A ND2    1 
ATOM   1358 N  N      . THR A 1 307  ? 144.446 146.180 227.916 1.00 51.86 ? 307  THR A N      1 
ATOM   1359 C  CA     . THR A 1 307  ? 145.683 146.505 227.218 1.00 51.86 ? 307  THR A CA     1 
ATOM   1360 C  C      . THR A 1 307  ? 146.853 146.605 228.184 1.00 51.86 ? 307  THR A C      1 
ATOM   1361 O  O      . THR A 1 307  ? 147.899 145.983 227.972 1.00 51.86 ? 307  THR A O      1 
ATOM   1362 C  CB     . THR A 1 307  ? 145.502 147.807 226.451 1.00 51.86 ? 307  THR A CB     1 
ATOM   1363 O  OG1    . THR A 1 307  ? 144.578 147.599 225.380 1.00 51.86 ? 307  THR A OG1    1 
ATOM   1364 C  CG2    . THR A 1 307  ? 146.811 148.339 225.919 1.00 51.86 ? 307  THR A CG2    1 
ATOM   1365 N  N      . VAL A 1 308  ? 146.683 147.349 229.281 1.00 52.81 ? 308  VAL A N      1 
ATOM   1366 C  CA     . VAL A 1 308  ? 147.763 147.433 230.253 1.00 52.81 ? 308  VAL A CA     1 
ATOM   1367 C  C      . VAL A 1 308  ? 147.864 146.141 231.062 1.00 52.81 ? 308  VAL A C      1 
ATOM   1368 O  O      . VAL A 1 308  ? 148.942 145.824 231.572 1.00 52.81 ? 308  VAL A O      1 
ATOM   1369 C  CB     . VAL A 1 308  ? 147.602 148.685 231.146 1.00 52.81 ? 308  VAL A CB     1 
ATOM   1370 C  CG1    . VAL A 1 308  ? 146.495 148.521 232.159 1.00 52.81 ? 308  VAL A CG1    1 
ATOM   1371 C  CG2    . VAL A 1 308  ? 148.917 149.067 231.821 1.00 52.81 ? 308  VAL A CG2    1 
ATOM   1372 N  N      . ALA A 1 309  ? 146.796 145.336 231.115 1.00 50.19 ? 309  ALA A N      1 
ATOM   1373 C  CA     . ALA A 1 309  ? 146.885 144.030 231.767 1.00 50.19 ? 309  ALA A CA     1 
ATOM   1374 C  C      . ALA A 1 309  ? 147.767 143.067 230.976 1.00 50.19 ? 309  ALA A C      1 
ATOM   1375 O  O      . ALA A 1 309  ? 148.666 142.427 231.542 1.00 50.19 ? 309  ALA A O      1 
ATOM   1376 C  CB     . ALA A 1 309  ? 145.488 143.446 231.963 1.00 50.19 ? 309  ALA A CB     1 
ATOM   1377 N  N      . THR A 1 310  ? 147.528 142.958 229.663 1.00 49.94 ? 310  THR A N      1 
ATOM   1378 C  CA     . THR A 1 310  ? 148.391 142.151 228.803 1.00 49.94 ? 310  THR A CA     1 
ATOM   1379 C  C      . THR A 1 310  ? 149.794 142.723 228.747 1.00 49.94 ? 310  THR A C      1 
ATOM   1380 O  O      . THR A 1 310  ? 150.772 141.974 228.683 1.00 49.94 ? 310  THR A O      1 
ATOM   1381 C  CB     . THR A 1 310  ? 147.827 142.066 227.386 1.00 49.94 ? 310  THR A CB     1 
ATOM   1382 O  OG1    . THR A 1 310  ? 147.686 143.384 226.857 1.00 49.94 ? 310  THR A OG1    1 
ATOM   1383 C  CG2    . THR A 1 310  ? 146.494 141.363 227.355 1.00 49.94 ? 310  THR A CG2    1 
ATOM   1384 N  N      . MET A 1 311  ? 149.903 144.050 228.785 1.00 48.97 ? 311  MET A N      1 
ATOM   1385 C  CA     . MET A 1 311  ? 151.193 144.724 228.801 1.00 48.97 ? 311  MET A CA     1 
ATOM   1386 C  C      . MET A 1 311  ? 152.014 144.331 230.020 1.00 48.97 ? 311  MET A C      1 
ATOM   1387 O  O      . MET A 1 311  ? 153.183 143.953 229.897 1.00 48.97 ? 311  MET A O      1 
ATOM   1388 C  CB     . MET A 1 311  ? 150.937 146.223 228.773 1.00 48.97 ? 311  MET A CB     1 
ATOM   1389 C  CG     . MET A 1 311  ? 152.126 147.101 228.786 1.00 48.97 ? 311  MET A CG     1 
ATOM   1390 S  SD     . MET A 1 311  ? 151.471 148.763 228.735 1.00 48.97 ? 311  MET A SD     1 
ATOM   1391 C  CE     . MET A 1 311  ? 152.972 149.668 228.918 1.00 48.97 ? 311  MET A CE     1 
ATOM   1392 N  N      . TYR A 1 312  ? 151.395 144.358 231.198 1.00 52.03 ? 312  TYR A N      1 
ATOM   1393 C  CA     . TYR A 1 312  ? 152.081 143.972 232.424 1.00 52.03 ? 312  TYR A CA     1 
ATOM   1394 C  C      . TYR A 1 312  ? 152.414 142.487 232.450 1.00 52.03 ? 312  TYR A C      1 
ATOM   1395 O  O      . TYR A 1 312  ? 153.492 142.102 232.921 1.00 52.03 ? 312  TYR A O      1 
ATOM   1396 C  CB     . TYR A 1 312  ? 151.225 144.352 233.623 1.00 52.03 ? 312  TYR A CB     1 
ATOM   1397 C  CG     . TYR A 1 312  ? 151.780 143.901 234.945 1.00 52.03 ? 312  TYR A CG     1 
ATOM   1398 C  CD1    . TYR A 1 312  ? 152.950 144.451 235.451 1.00 52.03 ? 312  TYR A CD1    1 
ATOM   1399 C  CD2    . TYR A 1 312  ? 151.112 142.955 235.709 1.00 52.03 ? 312  TYR A CD2    1 
ATOM   1400 C  CE1    . TYR A 1 312  ? 153.460 144.043 236.668 1.00 52.03 ? 312  TYR A CE1    1 
ATOM   1401 C  CE2    . TYR A 1 312  ? 151.607 142.548 236.930 1.00 52.03 ? 312  TYR A CE2    1 
ATOM   1402 C  CZ     . TYR A 1 312  ? 152.784 143.094 237.404 1.00 52.03 ? 312  TYR A CZ     1 
ATOM   1403 O  OH     . TYR A 1 312  ? 153.283 142.689 238.619 1.00 52.03 ? 312  TYR A OH     1 
ATOM   1404 N  N      . GLU A 1 313  ? 151.514 141.638 231.942 1.00 50.41 ? 313  GLU A N      1 
ATOM   1405 C  CA     . GLU A 1 313  ? 151.807 140.207 231.937 1.00 50.41 ? 313  GLU A CA     1 
ATOM   1406 C  C      . GLU A 1 313  ? 152.904 139.849 230.941 1.00 50.41 ? 313  GLU A C      1 
ATOM   1407 O  O      . GLU A 1 313  ? 153.629 138.876 231.156 1.00 50.41 ? 313  GLU A O      1 
ATOM   1408 C  CB     . GLU A 1 313  ? 150.543 139.401 231.653 1.00 50.41 ? 313  GLU A CB     1 
ATOM   1409 C  CG     . GLU A 1 313  ? 149.526 139.452 232.779 1.00 50.41 ? 313  GLU A CG     1 
ATOM   1410 C  CD     . GLU A 1 313  ? 150.009 138.777 234.051 1.00 50.41 ? 313  GLU A CD     1 
ATOM   1411 O  OE1    . GLU A 1 313  ? 150.768 137.789 233.960 1.00 50.41 ? 313  GLU A OE1    1 
ATOM   1412 O  OE2    . GLU A 1 313  ? 149.624 139.234 235.148 1.00 50.41 ? 313  GLU A OE2    1 
ATOM   1413 N  N      . LEU A 1 314  ? 153.055 140.620 229.864 1.00 46.86 ? 314  LEU A N      1 
ATOM   1414 C  CA     . LEU A 1 314  ? 154.179 140.412 228.958 1.00 46.86 ? 314  LEU A CA     1 
ATOM   1415 C  C      . LEU A 1 314  ? 155.480 141.001 229.492 1.00 46.86 ? 314  LEU A C      1 
ATOM   1416 O  O      . LEU A 1 314  ? 156.554 140.471 229.191 1.00 46.86 ? 314  LEU A O      1 
ATOM   1417 C  CB     . LEU A 1 314  ? 153.860 140.995 227.583 1.00 46.86 ? 314  LEU A CB     1 
ATOM   1418 C  CG     . LEU A 1 314  ? 153.235 140.092 226.514 1.00 46.86 ? 314  LEU A CG     1 
ATOM   1419 C  CD1    . LEU A 1 314  ? 151.851 139.589 226.826 1.00 46.86 ? 314  LEU A CD1    1 
ATOM   1420 C  CD2    . LEU A 1 314  ? 153.190 140.874 225.238 1.00 46.86 ? 314  LEU A CD2    1 
ATOM   1421 N  N      . ILE A 1 315  ? 155.414 142.091 230.266 1.00 48.74 ? 315  ILE A N      1 
ATOM   1422 C  CA     . ILE A 1 315  ? 156.605 142.595 230.952 1.00 48.74 ? 315  ILE A CA     1 
ATOM   1423 C  C      . ILE A 1 315  ? 157.092 141.584 231.986 1.00 48.74 ? 315  ILE A C      1 
ATOM   1424 O  O      . ILE A 1 315  ? 158.302 141.384 232.159 1.00 48.74 ? 315  ILE A O      1 
ATOM   1425 C  CB     . ILE A 1 315  ? 156.319 143.980 231.575 1.00 48.74 ? 315  ILE A CB     1 
ATOM   1426 C  CG1    . ILE A 1 315  ? 156.133 145.030 230.484 1.00 48.74 ? 315  ILE A CG1    1 
ATOM   1427 C  CG2    . ILE A 1 315  ? 157.422 144.440 232.524 1.00 48.74 ? 315  ILE A CG2    1 
ATOM   1428 C  CD1    . ILE A 1 315  ? 157.322 145.200 229.619 1.00 48.74 ? 315  ILE A CD1    1 
ATOM   1429 N  N      . LYS A 1 316  ? 156.156 140.899 232.656 1.00 51.13 ? 316  LYS A N      1 
ATOM   1430 C  CA     . LYS A 1 316  ? 156.528 139.817 233.567 1.00 51.13 ? 316  LYS A CA     1 
ATOM   1431 C  C      . LYS A 1 316  ? 157.213 138.667 232.839 1.00 51.13 ? 316  LYS A C      1 
ATOM   1432 O  O      . LYS A 1 316  ? 158.069 137.988 233.418 1.00 51.13 ? 316  LYS A O      1 
ATOM   1433 C  CB     . LYS A 1 316  ? 155.296 139.294 234.304 1.00 51.13 ? 316  LYS A CB     1 
ATOM   1434 C  CG     . LYS A 1 316  ? 154.743 140.229 235.359 1.00 51.13 ? 316  LYS A CG     1 
ATOM   1435 C  CD     . LYS A 1 316  ? 153.462 139.666 235.945 1.00 51.13 ? 316  LYS A CD     1 
ATOM   1436 C  CE     . LYS A 1 316  ? 153.732 138.451 236.810 1.00 51.13 ? 316  LYS A CE     1 
ATOM   1437 N  NZ     . LYS A 1 316  ? 152.493 137.975 237.480 1.00 51.13 ? 316  LYS A NZ     1 
ATOM   1438 N  N      . LYS A 1 317  ? 156.864 138.441 231.576 1.00 49.22 ? 317  LYS A N      1 
ATOM   1439 C  CA     . LYS A 1 317  ? 157.510 137.433 230.752 1.00 49.22 ? 317  LYS A CA     1 
ATOM   1440 C  C      . LYS A 1 317  ? 158.718 137.975 230.000 1.00 49.22 ? 317  LYS A C      1 
ATOM   1441 O  O      . LYS A 1 317  ? 159.195 137.307 229.079 1.00 49.22 ? 317  LYS A O      1 
ATOM   1442 C  CB     . LYS A 1 317  ? 156.512 136.843 229.756 1.00 49.22 ? 317  LYS A CB     1 
ATOM   1443 C  CG     . LYS A 1 317  ? 155.303 136.189 230.389 1.00 49.22 ? 317  LYS A CG     1 
ATOM   1444 C  CD     . LYS A 1 317  ? 155.667 134.956 231.175 1.00 49.22 ? 317  LYS A CD     1 
ATOM   1445 C  CE     . LYS A 1 317  ? 154.422 134.278 231.715 1.00 49.22 ? 317  LYS A CE     1 
ATOM   1446 N  NZ     . LYS A 1 317  ? 154.749 133.058 232.502 1.00 49.22 ? 317  LYS A NZ     1 
ATOM   1447 N  N      . LYS A 1 318  ? 159.194 139.174 230.364 1.00 47.33 ? 318  LYS A N      1 
ATOM   1448 C  CA     . LYS A 1 318  ? 160.398 139.813 229.811 1.00 47.33 ? 318  LYS A CA     1 
ATOM   1449 C  C      . LYS A 1 318  ? 160.282 140.077 228.308 1.00 47.33 ? 318  LYS A C      1 
ATOM   1450 O  O      . LYS A 1 318  ? 161.264 140.003 227.570 1.00 47.33 ? 318  LYS A O      1 
ATOM   1451 C  CB     . LYS A 1 318  ? 161.663 139.007 230.126 1.00 47.33 ? 318  LYS A CB     1 
ATOM   1452 C  CG     . LYS A 1 318  ? 161.939 138.830 231.610 1.00 47.33 ? 318  LYS A CG     1 
ATOM   1453 C  CD     . LYS A 1 318  ? 162.318 140.145 232.267 1.00 47.33 ? 318  LYS A CD     1 
ATOM   1454 C  CE     . LYS A 1 318  ? 162.665 139.951 233.731 1.00 47.33 ? 318  LYS A CE     1 
ATOM   1455 N  NZ     . LYS A 1 318  ? 162.998 141.239 234.399 1.00 47.33 ? 318  LYS A NZ     1 
ATOM   1456 N  N      . VAL A 1 319  ? 159.078 140.402 227.851 1.00 42.71 ? 319  VAL A N      1 
ATOM   1457 C  CA     . VAL A 1 319  ? 158.857 140.870 226.487 1.00 42.71 ? 319  VAL A CA     1 
ATOM   1458 C  C      . VAL A 1 319  ? 159.078 142.380 226.476 1.00 42.71 ? 319  VAL A C      1 
ATOM   1459 O  O      . VAL A 1 319  ? 158.430 143.088 227.258 1.00 42.71 ? 319  VAL A O      1 
ATOM   1460 C  CB     . VAL A 1 319  ? 157.448 140.529 225.985 1.00 42.71 ? 319  VAL A CB     1 
ATOM   1461 C  CG1    . VAL A 1 319  ? 157.219 141.111 224.604 1.00 42.71 ? 319  VAL A CG1    1 
ATOM   1462 C  CG2    . VAL A 1 319  ? 157.225 139.041 225.966 1.00 42.71 ? 319  VAL A CG2    1 
ATOM   1463 N  N      . PRO A 1 320  ? 159.963 142.905 225.629 1.00 39.83 ? 320  PRO A N      1 
ATOM   1464 C  CA     . PRO A 1 320  ? 160.144 144.360 225.562 1.00 39.83 ? 320  PRO A CA     1 
ATOM   1465 C  C      . PRO A 1 320  ? 158.942 145.045 224.927 1.00 39.83 ? 320  PRO A C      1 
ATOM   1466 O  O      . PRO A 1 320  ? 158.501 144.680 223.836 1.00 39.83 ? 320  PRO A O      1 
ATOM   1467 C  CB     . PRO A 1 320  ? 161.407 144.520 224.709 1.00 39.83 ? 320  PRO A CB     1 
ATOM   1468 C  CG     . PRO A 1 320  ? 161.487 143.285 223.919 1.00 39.83 ? 320  PRO A CG     1 
ATOM   1469 C  CD     . PRO A 1 320  ? 160.930 142.195 224.779 1.00 39.83 ? 320  PRO A CD     1 
ATOM   1470 N  N      . ALA A 1 321  ? 158.411 146.039 225.627 1.00 40.04 ? 321  ALA A N      1 
ATOM   1471 C  CA     . ALA A 1 321  ? 157.228 146.764 225.194 1.00 40.04 ? 321  ALA A CA     1 
ATOM   1472 C  C      . ALA A 1 321  ? 157.619 148.078 224.537 1.00 40.04 ? 321  ALA A C      1 
ATOM   1473 O  O      . ALA A 1 321  ? 158.558 148.745 224.973 1.00 40.04 ? 321  ALA A O      1 
ATOM   1474 C  CB     . ALA A 1 321  ? 156.298 147.036 226.374 1.00 40.04 ? 321  ALA A CB     1 
ATOM   1475 N  N      . VAL A 1 322  ? 156.906 148.435 223.474 1.00 41.96 ? 322  VAL A N      1 
ATOM   1476 C  CA     . VAL A 1 322  ? 157.016 149.741 222.836 1.00 41.96 ? 322  VAL A CA     1 
ATOM   1477 C  C      . VAL A 1 322  ? 155.650 150.395 222.920 1.00 41.96 ? 322  VAL A C      1 
ATOM   1478 O  O      . VAL A 1 322  ? 154.666 149.852 222.410 1.00 41.96 ? 322  VAL A O      1 
ATOM   1479 C  CB     . VAL A 1 322  ? 157.476 149.639 221.378 1.00 41.96 ? 322  VAL A CB     1 
ATOM   1480 C  CG1    . VAL A 1 322  ? 157.468 151.007 220.725 1.00 41.96 ? 322  VAL A CG1    1 
ATOM   1481 C  CG2    . VAL A 1 322  ? 158.842 149.019 221.300 1.00 41.96 ? 322  VAL A CG2    1 
ATOM   1482 N  N      . VAL A 1 323  ? 155.587 151.554 223.560 1.00 49.13 ? 323  VAL A N      1 
ATOM   1483 C  CA     . VAL A 1 323  ? 154.336 152.250 223.816 1.00 49.13 ? 323  VAL A CA     1 
ATOM   1484 C  C      . VAL A 1 323  ? 154.277 153.459 222.900 1.00 49.13 ? 323  VAL A C      1 
ATOM   1485 O  O      . VAL A 1 323  ? 155.242 154.225 222.811 1.00 49.13 ? 323  VAL A O      1 
ATOM   1486 C  CB     . VAL A 1 323  ? 154.230 152.664 225.290 1.00 49.13 ? 323  VAL A CB     1 
ATOM   1487 C  CG1    . VAL A 1 323  ? 152.886 153.270 225.582 1.00 49.13 ? 323  VAL A CG1    1 
ATOM   1488 C  CG2    . VAL A 1 323  ? 154.476 151.482 226.149 1.00 49.13 ? 323  VAL A CG2    1 
ATOM   1489 N  N      . ILE A 1 324  ? 153.148 153.631 222.220 1.00 55.36 ? 324  ILE A N      1 
ATOM   1490 C  CA     . ILE A 1 324  ? 152.973 154.726 221.277 1.00 55.36 ? 324  ILE A CA     1 
ATOM   1491 C  C      . ILE A 1 324  ? 152.381 155.895 222.058 1.00 55.36 ? 324  ILE A C      1 
ATOM   1492 O  O      . ILE A 1 324  ? 151.173 155.970 222.271 1.00 55.36 ? 324  ILE A O      1 
ATOM   1493 C  CB     . ILE A 1 324  ? 152.098 154.314 220.094 1.00 55.36 ? 324  ILE A CB     1 
ATOM   1494 C  CG1    . ILE A 1 324  ? 152.655 153.039 219.459 1.00 55.36 ? 324  ILE A CG1    1 
ATOM   1495 C  CG2    . ILE A 1 324  ? 152.047 155.422 219.063 1.00 55.36 ? 324  ILE A CG2    1 
ATOM   1496 C  CD1    . ILE A 1 324  ? 154.078 153.163 218.967 1.00 55.36 ? 324  ILE A CD1    1 
ATOM   1497 N  N      . ASP A 1 325  ? 153.244 156.808 222.494 1.00 60.26 ? 325  ASP A N      1 
ATOM   1498 C  CA     . ASP A 1 325  ? 152.827 157.939 223.310 1.00 60.26 ? 325  ASP A CA     1 
ATOM   1499 C  C      . ASP A 1 325  ? 152.123 158.978 222.450 1.00 60.26 ? 325  ASP A C      1 
ATOM   1500 O  O      . ASP A 1 325  ? 152.405 159.126 221.258 1.00 60.26 ? 325  ASP A O      1 
ATOM   1501 C  CB     . ASP A 1 325  ? 154.036 158.566 224.005 1.00 60.26 ? 325  ASP A CB     1 
ATOM   1502 C  CG     . ASP A 1 325  ? 153.658 159.507 225.141 1.00 60.26 ? 325  ASP A CG     1 
ATOM   1503 O  OD1    . ASP A 1 325  ? 152.455 159.694 225.414 1.00 60.26 ? 325  ASP A OD1    1 
ATOM   1504 O  OD2    . ASP A 1 325  ? 154.580 160.066 225.770 1.00 60.26 ? 325  ASP A OD2    1 
ATOM   1505 N  N      . GLY A 1 326  ? 151.194 159.701 223.070 1.00 61.19 ? 326  GLY A N      1 
ATOM   1506 C  CA     . GLY A 1 326  ? 150.436 160.703 222.353 1.00 61.19 ? 326  GLY A CA     1 
ATOM   1507 C  C      . GLY A 1 326  ? 149.419 160.147 221.390 1.00 61.19 ? 326  GLY A C      1 
ATOM   1508 O  O      . GLY A 1 326  ? 148.903 160.892 220.551 1.00 61.19 ? 326  GLY A O      1 
ATOM   1509 N  N      . SER A 1 327  ? 149.120 158.855 221.478 1.00 61.18 ? 327  SER A N      1 
ATOM   1510 C  CA     . SER A 1 327  ? 148.207 158.192 220.563 1.00 61.18 ? 327  SER A CA     1 
ATOM   1511 C  C      . SER A 1 327  ? 146.805 158.052 221.136 1.00 61.18 ? 327  SER A C      1 
ATOM   1512 O  O      . SER A 1 327  ? 145.831 158.461 220.498 1.00 61.18 ? 327  SER A O      1 
ATOM   1513 C  CB     . SER A 1 327  ? 148.764 156.815 220.193 1.00 61.18 ? 327  SER A CB     1 
ATOM   1514 O  OG     . SER A 1 327  ? 148.779 155.957 221.320 1.00 61.18 ? 327  SER A OG     1 
ATOM   1515 N  N      . GLY A 1 328  ? 146.680 157.477 222.326 1.00 61.65 ? 328  GLY A N      1 
ATOM   1516 C  CA     . GLY A 1 328  ? 145.370 157.242 222.893 1.00 61.65 ? 328  GLY A CA     1 
ATOM   1517 C  C      . GLY A 1 328  ? 145.316 157.325 224.398 1.00 61.65 ? 328  GLY A C      1 
ATOM   1518 O  O      . GLY A 1 328  ? 146.199 157.905 225.030 1.00 61.65 ? 328  GLY A O      1 
ATOM   1519 N  N      . ARG A 1 329  ? 144.286 156.726 224.986 1.00 60.68 ? 329  ARG A N      1 
ATOM   1520 C  CA     . ARG A 1 329  ? 143.935 157.039 226.361 1.00 60.68 ? 329  ARG A CA     1 
ATOM   1521 C  C      . ARG A 1 329  ? 144.748 156.263 227.392 1.00 60.68 ? 329  ARG A C      1 
ATOM   1522 O  O      . ARG A 1 329  ? 144.826 156.702 228.543 1.00 60.68 ? 329  ARG A O      1 
ATOM   1523 C  CB     . ARG A 1 329  ? 142.440 156.800 226.565 1.00 60.68 ? 329  ARG A CB     1 
ATOM   1524 C  CG     . ARG A 1 329  ? 142.045 155.361 226.507 1.00 60.68 ? 329  ARG A CG     1 
ATOM   1525 C  CD     . ARG A 1 329  ? 140.550 155.182 226.520 1.00 60.68 ? 329  ARG A CD     1 
ATOM   1526 N  NE     . ARG A 1 329  ? 140.205 153.772 226.643 1.00 60.68 ? 329  ARG A NE     1 
ATOM   1527 C  CZ     . ARG A 1 329  ? 140.144 152.925 225.624 1.00 60.68 ? 329  ARG A CZ     1 
ATOM   1528 N  NH1    . ARG A 1 329  ? 140.409 153.332 224.392 1.00 60.68 ? 329  ARG A NH1    1 
ATOM   1529 N  NH2    . ARG A 1 329  ? 139.825 151.663 225.840 1.00 60.68 ? 329  ARG A NH2    1 
ATOM   1530 N  N      . ALA A 1 330  ? 145.352 155.131 227.026 1.00 60.48 ? 330  ALA A N      1 
ATOM   1531 C  CA     . ALA A 1 330  ? 146.209 154.398 227.950 1.00 60.48 ? 330  ALA A CA     1 
ATOM   1532 C  C      . ALA A 1 330  ? 147.656 154.303 227.506 1.00 60.48 ? 330  ALA A C      1 
ATOM   1533 O  O      . ALA A 1 330  ? 148.521 154.050 228.348 1.00 60.48 ? 330  ALA A O      1 
ATOM   1534 C  CB     . ALA A 1 330  ? 145.683 152.974 228.182 1.00 60.48 ? 330  ALA A CB     1 
ATOM   1535 N  N      . ALA A 1 331  ? 147.943 154.483 226.222 1.00 59.44 ? 331  ALA A N      1 
ATOM   1536 C  CA     . ALA A 1 331  ? 149.321 154.525 225.761 1.00 59.44 ? 331  ALA A CA     1 
ATOM   1537 C  C      . ALA A 1 331  ? 149.944 155.904 225.907 1.00 59.44 ? 331  ALA A C      1 
ATOM   1538 O  O      . ALA A 1 331  ? 151.148 156.049 225.679 1.00 59.44 ? 331  ALA A O      1 
ATOM   1539 C  CB     . ALA A 1 331  ? 149.400 154.072 224.306 1.00 59.44 ? 331  ALA A CB     1 
ATOM   1540 N  N      . SER A 1 332  ? 149.163 156.920 226.263 1.00 61.43 ? 332  SER A N      1 
ATOM   1541 C  CA     . SER A 1 332  ? 149.755 158.201 226.617 1.00 61.43 ? 332  SER A CA     1 
ATOM   1542 C  C      . SER A 1 332  ? 150.141 158.245 228.085 1.00 61.43 ? 332  SER A C      1 
ATOM   1543 O  O      . SER A 1 332  ? 151.197 158.796 228.423 1.00 61.43 ? 332  SER A O      1 
ATOM   1544 C  CB     . SER A 1 332  ? 148.796 159.350 226.302 1.00 61.43 ? 332  SER A CB     1 
ATOM   1545 O  OG     . SER A 1 332  ? 148.542 159.433 224.911 1.00 61.43 ? 332  SER A OG     1 
ATOM   1546 N  N      . VAL A 1 333  ? 149.301 157.643 228.940 1.00 60.83 ? 333  VAL A N      1 
ATOM   1547 C  CA     . VAL A 1 333  ? 149.502 157.671 230.388 1.00 60.83 ? 333  VAL A CA     1 
ATOM   1548 C  C      . VAL A 1 333  ? 150.823 157.013 230.756 1.00 60.83 ? 333  VAL A C      1 
ATOM   1549 O  O      . VAL A 1 333  ? 151.613 157.568 231.534 1.00 60.83 ? 333  VAL A O      1 
ATOM   1550 C  CB     . VAL A 1 333  ? 148.317 156.995 231.102 1.00 60.83 ? 333  VAL A CB     1 
ATOM   1551 C  CG1    . VAL A 1 333  ? 148.552 156.934 232.597 1.00 60.83 ? 333  VAL A CG1    1 
ATOM   1552 C  CG2    . VAL A 1 333  ? 147.033 157.734 230.804 1.00 60.83 ? 333  VAL A CG2    1 
ATOM   1553 N  N      . VAL A 1 334  ? 151.100 155.849 230.151 1.00 58.36 ? 334  VAL A N      1 
ATOM   1554 C  CA     . VAL A 1 334  ? 152.394 155.184 230.297 1.00 58.36 ? 334  VAL A CA     1 
ATOM   1555 C  C      . VAL A 1 334  ? 153.514 156.095 229.826 1.00 58.36 ? 334  VAL A C      1 
ATOM   1556 O  O      . VAL A 1 334  ? 154.528 156.260 230.518 1.00 58.36 ? 334  VAL A O      1 
ATOM   1557 C  CB     . VAL A 1 334  ? 152.410 153.854 229.521 1.00 58.36 ? 334  VAL A CB     1 
ATOM   1558 C  CG1    . VAL A 1 334  ? 153.756 153.171 229.694 1.00 58.36 ? 334  VAL A CG1    1 
ATOM   1559 C  CG2    . VAL A 1 334  ? 151.276 152.956 229.954 1.00 58.36 ? 334  VAL A CG2    1 
ATOM   1560 N  N      . GLY A 1 335  ? 153.321 156.737 228.666 1.00 61.51 ? 335  GLY A N      1 
ATOM   1561 C  CA     . GLY A 1 335  ? 154.271 157.738 228.213 1.00 61.51 ? 335  GLY A CA     1 
ATOM   1562 C  C      . GLY A 1 335  ? 154.371 158.900 229.178 1.00 61.51 ? 335  GLY A C      1 
ATOM   1563 O  O      . GLY A 1 335  ? 155.473 159.326 229.539 1.00 61.51 ? 335  GLY A O      1 
ATOM   1564 N  N      . PHE A 1 336  ? 153.224 159.333 229.715 1.00 65.71 ? 336  PHE A N      1 
ATOM   1565 C  CA     . PHE A 1 336  ? 153.220 160.401 230.703 1.00 65.71 ? 336  PHE A CA     1 
ATOM   1566 C  C      . PHE A 1 336  ? 153.808 159.941 232.031 1.00 65.71 ? 336  PHE A C      1 
ATOM   1567 O  O      . PHE A 1 336  ? 154.168 160.775 232.865 1.00 65.71 ? 336  PHE A O      1 
ATOM   1568 C  CB     . PHE A 1 336  ? 151.793 160.927 230.886 1.00 65.71 ? 336  PHE A CB     1 
ATOM   1569 C  CG     . PHE A 1 336  ? 151.703 162.149 231.747 1.00 65.71 ? 336  PHE A CG     1 
ATOM   1570 C  CD1    . PHE A 1 336  ? 152.126 163.377 231.271 1.00 65.71 ? 336  PHE A CD1    1 
ATOM   1571 C  CD2    . PHE A 1 336  ? 151.204 162.067 233.035 1.00 65.71 ? 336  PHE A CD2    1 
ATOM   1572 C  CE1    . PHE A 1 336  ? 152.052 164.502 232.063 1.00 65.71 ? 336  PHE A CE1    1 
ATOM   1573 C  CE2    . PHE A 1 336  ? 151.124 163.191 233.831 1.00 65.71 ? 336  PHE A CE2    1 
ATOM   1574 C  CZ     . PHE A 1 336  ? 151.551 164.410 233.343 1.00 65.71 ? 336  PHE A CZ     1 
ATOM   1575 N  N      . ALA A 1 337  ? 153.947 158.638 232.238 1.00 62.71 ? 337  ALA A N      1 
ATOM   1576 C  CA     . ALA A 1 337  ? 154.631 158.156 233.419 1.00 62.71 ? 337  ALA A CA     1 
ATOM   1577 C  C      . ALA A 1 337  ? 156.047 157.682 233.124 1.00 62.71 ? 337  ALA A C      1 
ATOM   1578 O  O      . ALA A 1 337  ? 156.763 157.319 234.060 1.00 62.71 ? 337  ALA A O      1 
ATOM   1579 C  CB     . ALA A 1 337  ? 153.820 157.040 234.077 1.00 62.71 ? 337  ALA A CB     1 
ATOM   1580 N  N      . TYR A 1 338  ? 156.485 157.704 231.863 1.00 61.64 ? 338  TYR A N      1 
ATOM   1581 C  CA     . TYR A 1 338  ? 157.804 157.149 231.562 1.00 61.64 ? 338  TYR A CA     1 
ATOM   1582 C  C      . TYR A 1 338  ? 158.901 158.208 231.594 1.00 61.64 ? 338  TYR A C      1 
ATOM   1583 O  O      . TYR A 1 338  ? 159.818 158.138 232.417 1.00 61.64 ? 338  TYR A O      1 
ATOM   1584 C  CB     . TYR A 1 338  ? 157.794 156.451 230.198 1.00 61.64 ? 338  TYR A CB     1 
ATOM   1585 C  CG     . TYR A 1 338  ? 159.140 155.896 229.792 1.00 61.64 ? 338  TYR A CG     1 
ATOM   1586 C  CD1    . TYR A 1 338  ? 159.653 154.758 230.397 1.00 61.64 ? 338  TYR A CD1    1 
ATOM   1587 C  CD2    . TYR A 1 338  ? 159.895 156.508 228.797 1.00 61.64 ? 338  TYR A CD2    1 
ATOM   1588 C  CE1    . TYR A 1 338  ? 160.886 154.249 230.031 1.00 61.64 ? 338  TYR A CE1    1 
ATOM   1589 C  CE2    . TYR A 1 338  ? 161.125 156.004 228.420 1.00 61.64 ? 338  TYR A CE2    1 
ATOM   1590 C  CZ     . TYR A 1 338  ? 161.615 154.874 229.041 1.00 61.64 ? 338  TYR A CZ     1 
ATOM   1591 O  OH     . TYR A 1 338  ? 162.839 154.366 228.674 1.00 61.64 ? 338  TYR A OH     1 
ATOM   1592 N  N      . ASN A 1 339  ? 158.819 159.193 230.704 1.00 68.55 ? 339  ASN A N      1 
ATOM   1593 C  CA     . ASN A 1 339  ? 159.849 160.216 230.611 1.00 68.55 ? 339  ASN A CA     1 
ATOM   1594 C  C      . ASN A 1 339  ? 159.502 161.483 231.375 1.00 68.55 ? 339  ASN A C      1 
ATOM   1595 O  O      . ASN A 1 339  ? 160.397 162.287 231.658 1.00 68.55 ? 339  ASN A O      1 
ATOM   1596 C  CB     . ASN A 1 339  ? 160.137 160.543 229.137 1.00 68.55 ? 339  ASN A CB     1 
ATOM   1597 C  CG     . ASN A 1 339  ? 158.883 160.905 228.349 1.00 68.55 ? 339  ASN A CG     1 
ATOM   1598 O  OD1    . ASN A 1 339  ? 157.785 161.012 228.896 1.00 68.55 ? 339  ASN A OD1    1 
ATOM   1599 N  ND2    . ASN A 1 339  ? 159.049 161.086 227.044 1.00 68.55 ? 339  ASN A ND2    1 
ATOM   1600 N  N      . HIS A 1 340  ? 158.230 161.669 231.718 1.00 72.29 ? 340  HIS A N      1 
ATOM   1601 C  CA     . HIS A 1 340  ? 157.831 162.825 232.505 1.00 72.29 ? 340  HIS A CA     1 
ATOM   1602 C  C      . HIS A 1 340  ? 158.108 162.621 233.987 1.00 72.29 ? 340  HIS A C      1 
ATOM   1603 O  O      . HIS A 1 340  ? 158.352 163.595 234.707 1.00 72.29 ? 340  HIS A O      1 
ATOM   1604 C  CB     . HIS A 1 340  ? 156.350 163.114 232.272 1.00 72.29 ? 340  HIS A CB     1 
ATOM   1605 C  CG     . HIS A 1 340  ? 155.840 164.304 233.017 1.00 72.29 ? 340  HIS A CG     1 
ATOM   1606 N  ND1    . HIS A 1 340  ? 156.127 165.598 232.640 1.00 72.29 ? 340  HIS A ND1    1 
ATOM   1607 C  CD2    . HIS A 1 340  ? 155.061 164.397 234.120 1.00 72.29 ? 340  HIS A CD2    1 
ATOM   1608 C  CE1    . HIS A 1 340  ? 155.546 166.438 233.477 1.00 72.29 ? 340  HIS A CE1    1 
ATOM   1609 N  NE2    . HIS A 1 340  ? 154.892 165.734 234.384 1.00 72.29 ? 340  HIS A NE2    1 
ATOM   1610 N  N      . THR A 1 341  ? 158.090 161.376 234.456 1.00 71.57 ? 341  THR A N      1 
ATOM   1611 C  CA     . THR A 1 341  ? 158.276 161.045 235.865 1.00 71.57 ? 341  THR A CA     1 
ATOM   1612 C  C      . THR A 1 341  ? 159.399 160.032 236.037 1.00 71.57 ? 341  THR A C      1 
ATOM   1613 O  O      . THR A 1 341  ? 159.257 159.026 236.736 1.00 71.57 ? 341  THR A O      1 
ATOM   1614 C  CB     . THR A 1 341  ? 157.006 160.481 236.489 1.00 71.57 ? 341  THR A CB     1 
ATOM   1615 O  OG1    . THR A 1 341  ? 156.668 159.262 235.820 1.00 71.57 ? 341  THR A OG1    1 
ATOM   1616 C  CG2    . THR A 1 341  ? 155.845 161.464 236.380 1.00 71.57 ? 341  THR A CG2    1 
ATOM   1617 N  N      . ILE A 1 342  ? 160.535 160.276 235.398 1.00 73.31 ? 342  ILE A N      1 
ATOM   1618 C  CA     . ILE A 1 342  ? 161.682 159.386 235.543 1.00 73.31 ? 342  ILE A CA     1 
ATOM   1619 C  C      . ILE A 1 342  ? 162.405 159.709 236.849 1.00 73.31 ? 342  ILE A C      1 
ATOM   1620 O  O      . ILE A 1 342  ? 162.599 160.881 237.197 1.00 73.31 ? 342  ILE A O      1 
ATOM   1621 C  CB     . ILE A 1 342  ? 162.606 159.482 234.311 1.00 73.31 ? 342  ILE A CB     1 
ATOM   1622 C  CG1    . ILE A 1 342  ? 163.727 158.441 234.377 1.00 73.31 ? 342  ILE A CG1    1 
ATOM   1623 C  CG2    . ILE A 1 342  ? 163.114 160.910 234.045 1.00 73.31 ? 342  ILE A CG2    1 
ATOM   1624 C  CD1    . ILE A 1 342  ? 163.236 157.026 234.237 1.00 73.31 ? 342  ILE A CD1    1 
ATOM   1625 N  N      . LYS A 1 343  ? 162.759 158.664 237.600 1.00 77.05 ? 343  LYS A N      1 
ATOM   1626 C  CA     . LYS A 1 343  ? 163.410 158.807 238.897 1.00 77.05 ? 343  LYS A CA     1 
ATOM   1627 C  C      . LYS A 1 343  ? 164.007 157.460 239.286 1.00 77.05 ? 343  LYS A C      1 
ATOM   1628 O  O      . LYS A 1 343  ? 163.445 156.407 238.978 1.00 77.05 ? 343  LYS A O      1 
ATOM   1629 C  CB     . LYS A 1 343  ? 162.426 159.290 239.975 1.00 77.05 ? 343  LYS A CB     1 
ATOM   1630 C  CG     . LYS A 1 343  ? 163.057 159.692 241.298 1.00 77.05 ? 343  LYS A CG     1 
ATOM   1631 C  CD     . LYS A 1 343  ? 162.045 160.337 242.228 1.00 77.05 ? 343  LYS A CD     1 
ATOM   1632 C  CE     . LYS A 1 343  ? 161.082 159.312 242.791 1.00 77.05 ? 343  LYS A CE     1 
ATOM   1633 N  NZ     . LYS A 1 343  ? 161.776 158.368 243.711 1.00 77.05 ? 343  LYS A NZ     1 
ATOM   1634 N  N      . ARG A 1 344  ? 165.159 157.506 239.956 1.00 79.87 ? 344  ARG A N      1 
ATOM   1635 C  CA     . ARG A 1 344  ? 165.859 156.315 240.439 1.00 79.87 ? 344  ARG A CA     1 
ATOM   1636 C  C      . ARG A 1 344  ? 166.288 156.587 241.878 1.00 79.87 ? 344  ARG A C      1 
ATOM   1637 O  O      . ARG A 1 344  ? 167.248 157.329 242.110 1.00 79.87 ? 344  ARG A O      1 
ATOM   1638 C  CB     . ARG A 1 344  ? 167.063 155.996 239.559 1.00 79.87 ? 344  ARG A CB     1 
ATOM   1639 C  CG     . ARG A 1 344  ? 166.724 155.562 238.147 1.00 79.87 ? 344  ARG A CG     1 
ATOM   1640 C  CD     . ARG A 1 344  ? 167.978 155.364 237.322 1.00 79.87 ? 344  ARG A CD     1 
ATOM   1641 N  NE     . ARG A 1 344  ? 167.677 154.943 235.958 1.00 79.87 ? 344  ARG A NE     1 
ATOM   1642 C  CZ     . ARG A 1 344  ? 168.596 154.767 235.015 1.00 79.87 ? 344  ARG A CZ     1 
ATOM   1643 N  NH1    . ARG A 1 344  ? 169.876 154.978 235.287 1.00 79.87 ? 344  ARG A NH1    1 
ATOM   1644 N  NH2    . ARG A 1 344  ? 168.235 154.382 233.798 1.00 79.87 ? 344  ARG A NH2    1 
ATOM   1645 N  N      . ASN A 1 345  ? 165.585 156.003 242.846 1.00 81.55 ? 345  ASN A N      1 
ATOM   1646 C  CA     . ASN A 1 345  ? 165.855 156.284 244.256 1.00 81.55 ? 345  ASN A CA     1 
ATOM   1647 C  C      . ASN A 1 345  ? 165.786 154.997 245.080 1.00 81.55 ? 345  ASN A C      1 
ATOM   1648 O  O      . ASN A 1 345  ? 165.161 154.941 246.140 1.00 81.55 ? 345  ASN A O      1 
ATOM   1649 C  CB     . ASN A 1 345  ? 164.888 157.347 244.782 1.00 81.55 ? 345  ASN A CB     1 
ATOM   1650 C  CG     . ASN A 1 345  ? 165.364 157.993 246.077 1.00 81.55 ? 345  ASN A CG     1 
ATOM   1651 O  OD1    . ASN A 1 345  ? 166.420 157.647 246.608 1.00 81.55 ? 345  ASN A OD1    1 
ATOM   1652 N  ND2    . ASN A 1 345  ? 164.580 158.933 246.591 1.00 81.55 ? 345  ASN A ND2    1 
ATOM   1653 N  N      . VAL A 1 346  ? 166.428 153.931 244.598 1.00 78.80 ? 346  VAL A N      1 
ATOM   1654 C  CA     . VAL A 1 346  ? 166.406 152.652 245.298 1.00 78.80 ? 346  VAL A CA     1 
ATOM   1655 C  C      . VAL A 1 346  ? 167.673 151.878 244.947 1.00 78.80 ? 346  VAL A C      1 
ATOM   1656 O  O      . VAL A 1 346  ? 168.369 152.186 243.976 1.00 78.80 ? 346  VAL A O      1 
ATOM   1657 C  CB     . VAL A 1 346  ? 165.133 151.837 244.939 1.00 78.80 ? 346  VAL A CB     1 
ATOM   1658 C  CG1    . VAL A 1 346  ? 165.298 151.130 243.606 1.00 78.80 ? 346  VAL A CG1    1 
ATOM   1659 C  CG2    . VAL A 1 346  ? 164.703 150.889 246.068 1.00 78.80 ? 346  VAL A CG2    1 
ATOM   1660 N  N      . ASP A 1 347  ? 167.993 150.893 245.780 1.00 78.24 ? 347  ASP A N      1 
ATOM   1661 C  CA     . ASP A 1 347  ? 168.947 149.844 245.465 1.00 78.24 ? 347  ASP A CA     1 
ATOM   1662 C  C      . ASP A 1 347  ? 168.162 148.598 245.057 1.00 78.24 ? 347  ASP A C      1 
ATOM   1663 O  O      . ASP A 1 347  ? 166.951 148.508 245.266 1.00 78.24 ? 347  ASP A O      1 
ATOM   1664 C  CB     . ASP A 1 347  ? 169.854 149.573 246.675 1.00 78.24 ? 347  ASP A CB     1 
ATOM   1665 C  CG     . ASP A 1 347  ? 171.110 148.792 246.319 1.00 78.24 ? 347  ASP A CG     1 
ATOM   1666 O  OD1    . ASP A 1 347  ? 171.284 148.435 245.134 1.00 78.24 ? 347  ASP A OD1    1 
ATOM   1667 O  OD2    . ASP A 1 347  ? 171.925 148.537 247.230 1.00 78.24 ? 347  ASP A OD2    1 
ATOM   1668 N  N      . GLY A 1 348  ? 168.858 147.625 244.476 1.00 76.87 ? 348  GLY A N      1 
ATOM   1669 C  CA     . GLY A 1 348  ? 168.149 146.475 243.953 1.00 76.87 ? 348  GLY A CA     1 
ATOM   1670 C  C      . GLY A 1 348  ? 167.826 146.609 242.481 1.00 76.87 ? 348  GLY A C      1 
ATOM   1671 O  O      . GLY A 1 348  ? 166.652 146.610 242.095 1.00 76.87 ? 348  GLY A O      1 
ATOM   1672 N  N      . GLN A 1 349  ? 168.876 146.785 241.672 1.00 76.02 ? 349  GLN A N      1 
ATOM   1673 C  CA     . GLN A 1 349  ? 168.890 146.927 240.212 1.00 76.02 ? 349  GLN A CA     1 
ATOM   1674 C  C      . GLN A 1 349  ? 168.279 148.235 239.724 1.00 76.02 ? 349  GLN A C      1 
ATOM   1675 O  O      . GLN A 1 349  ? 168.045 148.370 238.513 1.00 76.02 ? 349  GLN A O      1 
ATOM   1676 C  CB     . GLN A 1 349  ? 168.224 145.749 239.480 1.00 76.02 ? 349  GLN A CB     1 
ATOM   1677 C  CG     . GLN A 1 349  ? 168.985 144.433 239.576 1.00 76.02 ? 349  GLN A CG     1 
ATOM   1678 C  CD     . GLN A 1 349  ? 168.593 143.597 240.782 1.00 76.02 ? 349  GLN A CD     1 
ATOM   1679 O  OE1    . GLN A 1 349  ? 167.508 143.758 241.340 1.00 76.02 ? 349  GLN A OE1    1 
ATOM   1680 N  NE2    . GLN A 1 349  ? 169.480 142.696 241.190 1.00 76.02 ? 349  GLN A NE2    1 
ATOM   1681 N  N      . THR A 1 350  ? 168.029 149.191 240.628 1.00 74.43 ? 350  THR A N      1 
ATOM   1682 C  CA     . THR A 1 350  ? 167.775 150.608 240.333 1.00 74.43 ? 350  THR A CA     1 
ATOM   1683 C  C      . THR A 1 350  ? 166.536 150.782 239.442 1.00 74.43 ? 350  THR A C      1 
ATOM   1684 O  O      . THR A 1 350  ? 166.611 151.133 238.261 1.00 74.43 ? 350  THR A O      1 
ATOM   1685 C  CB     . THR A 1 350  ? 169.028 151.253 239.722 1.00 74.43 ? 350  THR A CB     1 
ATOM   1686 O  OG1    . THR A 1 350  ? 170.173 150.866 240.490 1.00 74.43 ? 350  THR A OG1    1 
ATOM   1687 C  CG2    . THR A 1 350  ? 168.942 152.766 239.795 1.00 74.43 ? 350  THR A CG2    1 
ATOM   1688 N  N      . ILE A 1 351  ? 165.385 150.463 240.033 1.00 71.14 ? 351  ILE A N      1 
ATOM   1689 C  CA     . ILE A 1 351  ? 164.114 150.471 239.315 1.00 71.14 ? 351  ILE A CA     1 
ATOM   1690 C  C      . ILE A 1 351  ? 163.670 151.902 239.041 1.00 71.14 ? 351  ILE A C      1 
ATOM   1691 O  O      . ILE A 1 351  ? 164.214 152.856 239.607 1.00 71.14 ? 351  ILE A O      1 
ATOM   1692 C  CB     . ILE A 1 351  ? 163.029 149.710 240.097 1.00 71.14 ? 351  ILE A CB     1 
ATOM   1693 C  CG1    . ILE A 1 351  ? 162.539 150.532 241.287 1.00 71.14 ? 351  ILE A CG1    1 
ATOM   1694 C  CG2    . ILE A 1 351  ? 163.581 148.388 240.596 1.00 71.14 ? 351  ILE A CG2    1 
ATOM   1695 C  CD1    . ILE A 1 351  ? 161.340 149.932 241.980 1.00 71.14 ? 351  ILE A CD1    1 
ATOM   1696 N  N      . ASN A 1 352  ? 162.678 152.064 238.172 1.00 68.92 ? 352  ASN A N      1 
ATOM   1697 C  CA     . ASN A 1 352  ? 162.098 153.365 237.872 1.00 68.92 ? 352  ASN A CA     1 
ATOM   1698 C  C      . ASN A 1 352  ? 160.721 153.464 238.507 1.00 68.92 ? 352  ASN A C      1 
ATOM   1699 O  O      . ASN A 1 352  ? 159.879 152.583 238.312 1.00 68.92 ? 352  ASN A O      1 
ATOM   1700 C  CB     . ASN A 1 352  ? 161.992 153.595 236.366 1.00 68.92 ? 352  ASN A CB     1 
ATOM   1701 C  CG     . ASN A 1 352  ? 163.332 153.833 235.723 1.00 68.92 ? 352  ASN A CG     1 
ATOM   1702 O  OD1    . ASN A 1 352  ? 164.186 154.517 236.279 1.00 68.92 ? 352  ASN A OD1    1 
ATOM   1703 N  ND2    . ASN A 1 352  ? 163.516 153.292 234.532 1.00 68.92 ? 352  ASN A ND2    1 
ATOM   1704 N  N      . VAL A 1 353  ? 160.496 154.535 239.262 1.00 71.55 ? 353  VAL A N      1 
ATOM   1705 C  CA     . VAL A 1 353  ? 159.232 154.755 239.944 1.00 71.55 ? 353  VAL A CA     1 
ATOM   1706 C  C      . VAL A 1 353  ? 158.641 156.083 239.489 1.00 71.55 ? 353  VAL A C      1 
ATOM   1707 O  O      . VAL A 1 353  ? 159.274 156.870 238.786 1.00 71.55 ? 353  VAL A O      1 
ATOM   1708 C  CB     . VAL A 1 353  ? 159.378 154.722 241.477 1.00 71.55 ? 353  VAL A CB     1 
ATOM   1709 C  CG1    . VAL A 1 353  ? 159.785 153.340 241.942 1.00 71.55 ? 353  VAL A CG1    1 
ATOM   1710 C  CG2    . VAL A 1 353  ? 160.399 155.741 241.927 1.00 71.55 ? 353  VAL A CG2    1 
ATOM   1711 N  N      . ILE A 1 354  ? 157.393 156.311 239.902 1.00 74.46 ? 354  ILE A N      1 
ATOM   1712 C  CA     . ILE A 1 354  ? 156.713 157.569 239.630 1.00 74.46 ? 354  ILE A CA     1 
ATOM   1713 C  C      . ILE A 1 354  ? 157.334 158.678 240.481 1.00 74.46 ? 354  ILE A C      1 
ATOM   1714 O  O      . ILE A 1 354  ? 158.000 158.429 241.493 1.00 74.46 ? 354  ILE A O      1 
ATOM   1715 C  CB     . ILE A 1 354  ? 155.206 157.399 239.910 1.00 74.46 ? 354  ILE A CB     1 
ATOM   1716 C  CG1    . ILE A 1 354  ? 154.344 158.431 239.173 1.00 74.46 ? 354  ILE A CG1    1 
ATOM   1717 C  CG2    . ILE A 1 354  ? 154.910 157.420 241.408 1.00 74.46 ? 354  ILE A CG2    1 
ATOM   1718 C  CD1    . ILE A 1 354  ? 154.227 158.182 237.696 1.00 74.46 ? 354  ILE A CD1    1 
ATOM   1719 N  N      . ASP A 1 355  ? 157.155 159.924 240.036 1.00 76.31 ? 355  ASP A N      1 
ATOM   1720 C  CA     . ASP A 1 355  ? 157.559 161.025 240.895 1.00 76.31 ? 355  ASP A CA     1 
ATOM   1721 C  C      . ASP A 1 355  ? 156.490 161.305 241.947 1.00 76.31 ? 355  ASP A C      1 
ATOM   1722 O  O      . ASP A 1 355  ? 155.294 161.164 241.680 1.00 76.31 ? 355  ASP A O      1 
ATOM   1723 C  CB     . ASP A 1 355  ? 157.811 162.293 240.084 1.00 76.31 ? 355  ASP A CB     1 
ATOM   1724 C  CG     . ASP A 1 355  ? 159.134 162.268 239.354 1.00 76.31 ? 355  ASP A CG     1 
ATOM   1725 O  OD1    . ASP A 1 355  ? 160.045 161.549 239.807 1.00 76.31 ? 355  ASP A OD1    1 
ATOM   1726 O  OD2    . ASP A 1 355  ? 159.277 162.997 238.353 1.00 76.31 ? 355  ASP A OD2    1 
ATOM   1727 N  N      . PRO A 1 356  ? 156.897 161.700 243.158 1.00 78.50 ? 356  PRO A N      1 
ATOM   1728 C  CA     . PRO A 1 356  ? 155.905 162.146 244.147 1.00 78.50 ? 356  PRO A CA     1 
ATOM   1729 C  C      . PRO A 1 356  ? 155.281 163.485 243.805 1.00 78.50 ? 356  PRO A C      1 
ATOM   1730 O  O      . PRO A 1 356  ? 154.194 163.789 244.312 1.00 78.50 ? 356  PRO A O      1 
ATOM   1731 C  CB     . PRO A 1 356  ? 156.715 162.222 245.447 1.00 78.50 ? 356  PRO A CB     1 
ATOM   1732 C  CG     . PRO A 1 356  ? 158.114 162.460 244.996 1.00 78.50 ? 356  PRO A CG     1 
ATOM   1733 C  CD     . PRO A 1 356  ? 158.264 161.704 243.706 1.00 78.50 ? 356  PRO A CD     1 
ATOM   1734 N  N      . GLN A 1 357  ? 155.933 164.294 242.966 1.00 79.38 ? 357  GLN A N      1 
ATOM   1735 C  CA     . GLN A 1 357  ? 155.346 165.563 242.548 1.00 79.38 ? 357  GLN A CA     1 
ATOM   1736 C  C      . GLN A 1 357  ? 154.178 165.343 241.596 1.00 79.38 ? 357  GLN A C      1 
ATOM   1737 O  O      . GLN A 1 357  ? 153.169 166.054 241.666 1.00 79.38 ? 357  GLN A O      1 
ATOM   1738 C  CB     . GLN A 1 357  ? 156.419 166.441 241.901 1.00 79.38 ? 357  GLN A CB     1 
ATOM   1739 C  CG     . GLN A 1 357  ? 155.946 167.820 241.452 1.00 79.38 ? 357  GLN A CG     1 
ATOM   1740 C  CD     . GLN A 1 357  ? 155.442 168.678 242.599 1.00 79.38 ? 357  GLN A CD     1 
ATOM   1741 O  OE1    . GLN A 1 357  ? 154.237 168.885 242.752 1.00 79.38 ? 357  GLN A OE1    1 
ATOM   1742 N  NE2    . GLN A 1 357  ? 156.363 169.183 243.410 1.00 79.38 ? 357  GLN A NE2    1 
ATOM   1743 N  N      . TYR A 1 358  ? 154.280 164.348 240.715 1.00 78.94 ? 358  TYR A N      1 
ATOM   1744 C  CA     . TYR A 1 358  ? 153.264 164.117 239.698 1.00 78.94 ? 358  TYR A CA     1 
ATOM   1745 C  C      . TYR A 1 358  ? 152.416 162.881 239.968 1.00 78.94 ? 358  TYR A C      1 
ATOM   1746 O  O      . TYR A 1 358  ? 151.675 162.450 239.075 1.00 78.94 ? 358  TYR A O      1 
ATOM   1747 C  CB     . TYR A 1 358  ? 153.915 164.015 238.319 1.00 78.94 ? 358  TYR A CB     1 
ATOM   1748 C  CG     . TYR A 1 358  ? 154.585 165.293 237.883 1.00 78.94 ? 358  TYR A CG     1 
ATOM   1749 C  CD1    . TYR A 1 358  ? 153.834 166.373 237.436 1.00 78.94 ? 358  TYR A CD1    1 
ATOM   1750 C  CD2    . TYR A 1 358  ? 155.969 165.420 237.914 1.00 78.94 ? 358  TYR A CD2    1 
ATOM   1751 C  CE1    . TYR A 1 358  ? 154.440 167.551 237.041 1.00 78.94 ? 358  TYR A CE1    1 
ATOM   1752 C  CE2    . TYR A 1 358  ? 156.588 166.592 237.517 1.00 78.94 ? 358  TYR A CE2    1 
ATOM   1753 C  CZ     . TYR A 1 358  ? 155.818 167.653 237.079 1.00 78.94 ? 358  TYR A CZ     1 
ATOM   1754 O  OH     . TYR A 1 358  ? 156.426 168.822 236.682 1.00 78.94 ? 358  TYR A OH     1 
ATOM   1755 N  N      . GLU A 1 359  ? 152.492 162.308 241.176 1.00 78.49 ? 359  GLU A N      1 
ATOM   1756 C  CA     . GLU A 1 359  ? 151.677 161.136 241.479 1.00 78.49 ? 359  GLU A CA     1 
ATOM   1757 C  C      . GLU A 1 359  ? 150.197 161.490 241.577 1.00 78.49 ? 359  GLU A C      1 
ATOM   1758 O  O      . GLU A 1 359  ? 149.348 160.692 241.166 1.00 78.49 ? 359  GLU A O      1 
ATOM   1759 C  CB     . GLU A 1 359  ? 152.172 160.444 242.756 1.00 78.49 ? 359  GLU A CB     1 
ATOM   1760 C  CG     . GLU A 1 359  ? 152.067 161.249 244.044 1.00 78.49 ? 359  GLU A CG     1 
ATOM   1761 C  CD     . GLU A 1 359  ? 152.616 160.503 245.244 1.00 78.49 ? 359  GLU A CD     1 
ATOM   1762 O  OE1    . GLU A 1 359  ? 153.094 159.362 245.070 1.00 78.49 ? 359  GLU A OE1    1 
ATOM   1763 O  OE2    . GLU A 1 359  ? 152.572 161.058 246.362 1.00 78.49 ? 359  GLU A OE2    1 
ATOM   1764 N  N      . ASP A 1 360  ? 149.875 162.701 242.045 1.00 78.29 ? 360  ASP A N      1 
ATOM   1765 C  CA     . ASP A 1 360  ? 148.487 163.151 242.081 1.00 78.29 ? 360  ASP A CA     1 
ATOM   1766 C  C      . ASP A 1 360  ? 147.943 163.345 240.671 1.00 78.29 ? 360  ASP A C      1 
ATOM   1767 O  O      . ASP A 1 360  ? 146.798 162.972 240.383 1.00 78.29 ? 360  ASP A O      1 
ATOM   1768 C  CB     . ASP A 1 360  ? 148.388 164.451 242.883 1.00 78.29 ? 360  ASP A CB     1 
ATOM   1769 C  CG     . ASP A 1 360  ? 146.959 164.804 243.277 1.00 78.29 ? 360  ASP A CG     1 
ATOM   1770 O  OD1    . ASP A 1 360  ? 146.027 164.024 242.986 1.00 78.29 ? 360  ASP A OD1    1 
ATOM   1771 O  OD2    . ASP A 1 360  ? 146.768 165.882 243.880 1.00 78.29 ? 360  ASP A OD2    1 
ATOM   1772 N  N      . GLU A 1 361  ? 148.769 163.882 239.770 1.00 76.66 ? 361  GLU A N      1 
ATOM   1773 C  CA     . GLU A 1 361  ? 148.326 164.113 238.400 1.00 76.66 ? 361  GLU A CA     1 
ATOM   1774 C  C      . GLU A 1 361  ? 148.158 162.805 237.639 1.00 76.66 ? 361  GLU A C      1 
ATOM   1775 O  O      . GLU A 1 361  ? 147.177 162.637 236.904 1.00 76.66 ? 361  GLU A O      1 
ATOM   1776 C  CB     . GLU A 1 361  ? 149.308 165.034 237.678 1.00 76.66 ? 361  GLU A CB     1 
ATOM   1777 C  CG     . GLU A 1 361  ? 148.883 165.391 236.266 1.00 76.66 ? 361  GLU A CG     1 
ATOM   1778 C  CD     . GLU A 1 361  ? 149.816 166.379 235.611 1.00 76.66 ? 361  GLU A CD     1 
ATOM   1779 O  OE1    . GLU A 1 361  ? 150.798 166.790 236.263 1.00 76.66 ? 361  GLU A OE1    1 
ATOM   1780 O  OE2    . GLU A 1 361  ? 149.569 166.744 234.444 1.00 76.66 ? 361  GLU A OE2    1 
ATOM   1781 N  N      . VAL A 1 362  ? 149.081 161.853 237.818 1.00 74.96 ? 362  VAL A N      1 
ATOM   1782 C  CA     . VAL A 1 362  ? 148.918 160.582 237.118 1.00 74.96 ? 362  VAL A CA     1 
ATOM   1783 C  C      . VAL A 1 362  ? 147.801 159.757 237.746 1.00 74.96 ? 362  VAL A C      1 
ATOM   1784 O  O      . VAL A 1 362  ? 147.156 158.964 237.053 1.00 74.96 ? 362  VAL A O      1 
ATOM   1785 C  CB     . VAL A 1 362  ? 150.238 159.783 237.043 1.00 74.96 ? 362  VAL A CB     1 
ATOM   1786 C  CG1    . VAL A 1 362  ? 151.307 160.581 236.329 1.00 74.96 ? 362  VAL A CG1    1 
ATOM   1787 C  CG2    . VAL A 1 362  ? 150.713 159.345 238.404 1.00 74.96 ? 362  VAL A CG2    1 
ATOM   1788 N  N      . ARG A 1 363  ? 147.502 159.961 239.037 1.00 73.04 ? 363  ARG A N      1 
ATOM   1789 C  CA     . ARG A 1 363  ? 146.372 159.261 239.638 1.00 73.04 ? 363  ARG A CA     1 
ATOM   1790 C  C      . ARG A 1 363  ? 145.053 159.837 239.139 1.00 73.04 ? 363  ARG A C      1 
ATOM   1791 O  O      . ARG A 1 363  ? 144.105 159.090 238.873 1.00 73.04 ? 363  ARG A O      1 
ATOM   1792 C  CB     . ARG A 1 363  ? 146.455 159.336 241.163 1.00 73.04 ? 363  ARG A CB     1 
ATOM   1793 C  CG     . ARG A 1 363  ? 145.394 158.528 241.899 1.00 73.04 ? 363  ARG A CG     1 
ATOM   1794 C  CD     . ARG A 1 363  ? 145.631 157.033 241.727 1.00 73.04 ? 363  ARG A CD     1 
ATOM   1795 N  NE     . ARG A 1 363  ? 144.674 156.224 242.477 1.00 73.04 ? 363  ARG A NE     1 
ATOM   1796 C  CZ     . ARG A 1 363  ? 143.491 155.833 242.010 1.00 73.04 ? 363  ARG A CZ     1 
ATOM   1797 N  NH1    . ARG A 1 363  ? 143.108 156.171 240.785 1.00 73.04 ? 363  ARG A NH1    1 
ATOM   1798 N  NH2    . ARG A 1 363  ? 142.688 155.099 242.769 1.00 73.04 ? 363  ARG A NH2    1 
ATOM   1799 N  N      . ALA A 1 364  ? 144.992 161.162 238.966 1.00 73.48 ? 364  ALA A N      1 
ATOM   1800 C  CA     . ALA A 1 364  ? 143.813 161.783 238.370 1.00 73.48 ? 364  ALA A CA     1 
ATOM   1801 C  C      . ALA A 1 364  ? 143.640 161.358 236.917 1.00 73.48 ? 364  ALA A C      1 
ATOM   1802 O  O      . ALA A 1 364  ? 142.515 161.111 236.464 1.00 73.48 ? 364  ALA A O      1 
ATOM   1803 C  CB     . ALA A 1 364  ? 143.910 163.305 238.475 1.00 73.48 ? 364  ALA A CB     1 
ATOM   1804 N  N      . LYS A 1 365  ? 144.749 161.221 236.189 1.00 71.80 ? 365  LYS A N      1 
ATOM   1805 C  CA     . LYS A 1 365  ? 144.677 160.824 234.788 1.00 71.80 ? 365  LYS A CA     1 
ATOM   1806 C  C      . LYS A 1 365  ? 144.279 159.357 234.646 1.00 71.80 ? 365  LYS A C      1 
ATOM   1807 O  O      . LYS A 1 365  ? 143.501 159.006 233.752 1.00 71.80 ? 365  LYS A O      1 
ATOM   1808 C  CB     . LYS A 1 365  ? 146.019 161.113 234.113 1.00 71.80 ? 365  LYS A CB     1 
ATOM   1809 C  CG     . LYS A 1 365  ? 146.024 160.971 232.609 1.00 71.80 ? 365  LYS A CG     1 
ATOM   1810 C  CD     . LYS A 1 365  ? 147.356 161.411 232.036 1.00 71.80 ? 365  LYS A CD     1 
ATOM   1811 C  CE     . LYS A 1 365  ? 147.486 162.924 232.108 1.00 71.80 ? 365  LYS A CE     1 
ATOM   1812 N  NZ     . LYS A 1 365  ? 148.699 163.439 231.420 1.00 71.80 ? 365  LYS A NZ     1 
ATOM   1813 N  N      . VAL A 1 366  ? 144.752 158.496 235.549 1.00 71.50 ? 366  VAL A N      1 
ATOM   1814 C  CA     . VAL A 1 366  ? 144.379 157.089 235.491 1.00 71.50 ? 366  VAL A CA     1 
ATOM   1815 C  C      . VAL A 1 366  ? 142.985 156.851 236.071 1.00 71.50 ? 366  VAL A C      1 
ATOM   1816 O  O      . VAL A 1 366  ? 142.381 155.808 235.798 1.00 71.50 ? 366  VAL A O      1 
ATOM   1817 C  CB     . VAL A 1 366  ? 145.443 156.225 236.202 1.00 71.50 ? 366  VAL A CB     1 
ATOM   1818 C  CG1    . VAL A 1 366  ? 145.291 156.266 237.707 1.00 71.50 ? 366  VAL A CG1    1 
ATOM   1819 C  CG2    . VAL A 1 366  ? 145.449 154.797 235.694 1.00 71.50 ? 366  VAL A CG2    1 
ATOM   1820 N  N      . VAL A 1 367  ? 142.436 157.788 236.850 1.00 72.27 ? 367  VAL A N      1 
ATOM   1821 C  CA     . VAL A 1 367  ? 141.083 157.603 237.364 1.00 72.27 ? 367  VAL A CA     1 
ATOM   1822 C  C      . VAL A 1 367  ? 140.040 158.283 236.477 1.00 72.27 ? 367  VAL A C      1 
ATOM   1823 O  O      . VAL A 1 367  ? 138.854 157.922 236.547 1.00 72.27 ? 367  VAL A O      1 
ATOM   1824 C  CB     . VAL A 1 367  ? 140.967 158.091 238.829 1.00 72.27 ? 367  VAL A CB     1 
ATOM   1825 C  CG1    . VAL A 1 367  ? 140.833 159.608 238.921 1.00 72.27 ? 367  VAL A CG1    1 
ATOM   1826 C  CG2    . VAL A 1 367  ? 139.847 157.370 239.581 1.00 72.27 ? 367  VAL A CG2    1 
ATOM   1827 N  N      . GLU A 1 368  ? 140.442 159.226 235.624 1.00 72.80 ? 368  GLU A N      1 
ATOM   1828 C  CA     . GLU A 1 368  ? 139.490 159.902 234.755 1.00 72.80 ? 368  GLU A CA     1 
ATOM   1829 C  C      . GLU A 1 368  ? 139.562 159.433 233.310 1.00 72.80 ? 368  GLU A C      1 
ATOM   1830 O  O      . GLU A 1 368  ? 138.518 159.259 232.675 1.00 72.80 ? 368  GLU A O      1 
ATOM   1831 C  CB     . GLU A 1 368  ? 139.712 161.421 234.818 1.00 72.80 ? 368  GLU A CB     1 
ATOM   1832 C  CG     . GLU A 1 368  ? 138.599 162.282 234.200 1.00 72.80 ? 368  GLU A CG     1 
ATOM   1833 C  CD     . GLU A 1 368  ? 138.801 162.563 232.719 1.00 72.80 ? 368  GLU A CD     1 
ATOM   1834 O  OE1    . GLU A 1 368  ? 139.967 162.606 232.273 1.00 72.80 ? 368  GLU A OE1    1 
ATOM   1835 O  OE2    . GLU A 1 368  ? 137.793 162.730 232.002 1.00 72.80 ? 368  GLU A OE2    1 
ATOM   1836 N  N      . VAL A 1 369  ? 140.762 159.229 232.771 1.00 72.74 ? 369  VAL A N      1 
ATOM   1837 C  CA     . VAL A 1 369  ? 140.914 159.055 231.329 1.00 72.74 ? 369  VAL A CA     1 
ATOM   1838 C  C      . VAL A 1 369  ? 140.467 157.662 230.894 1.00 72.74 ? 369  VAL A C      1 
ATOM   1839 O  O      . VAL A 1 369  ? 139.629 157.519 229.996 1.00 72.74 ? 369  VAL A O      1 
ATOM   1840 C  CB     . VAL A 1 369  ? 142.360 159.363 230.908 1.00 72.74 ? 369  VAL A CB     1 
ATOM   1841 C  CG1    . VAL A 1 369  ? 142.568 159.021 229.463 1.00 72.74 ? 369  VAL A CG1    1 
ATOM   1842 C  CG2    . VAL A 1 369  ? 142.641 160.839 231.118 1.00 72.74 ? 369  VAL A CG2    1 
ATOM   1843 N  N      . PHE A 1 370  ? 141.005 156.617 231.519 1.00 67.75 ? 370  PHE A N      1 
ATOM   1844 C  CA     . PHE A 1 370  ? 140.523 155.264 231.275 1.00 67.75 ? 370  PHE A CA     1 
ATOM   1845 C  C      . PHE A 1 370  ? 140.240 154.596 232.613 1.00 67.75 ? 370  PHE A C      1 
ATOM   1846 O  O      . PHE A 1 370  ? 141.047 154.690 233.541 1.00 67.75 ? 370  PHE A O      1 
ATOM   1847 C  CB     . PHE A 1 370  ? 141.518 154.445 230.425 1.00 67.75 ? 370  PHE A CB     1 
ATOM   1848 C  CG     . PHE A 1 370  ? 142.820 154.116 231.116 1.00 67.75 ? 370  PHE A CG     1 
ATOM   1849 C  CD1    . PHE A 1 370  ? 143.866 155.024 231.128 1.00 67.75 ? 370  PHE A CD1    1 
ATOM   1850 C  CD2    . PHE A 1 370  ? 143.011 152.873 231.706 1.00 67.75 ? 370  PHE A CD2    1 
ATOM   1851 C  CE1    . PHE A 1 370  ? 145.063 154.715 231.751 1.00 67.75 ? 370  PHE A CE1    1 
ATOM   1852 C  CE2    . PHE A 1 370  ? 144.204 152.563 232.330 1.00 67.75 ? 370  PHE A CE2    1 
ATOM   1853 C  CZ     . PHE A 1 370  ? 145.232 153.482 232.346 1.00 67.75 ? 370  PHE A CZ     1 
ATOM   1854 N  N      . GLY A 1 371  ? 139.085 153.947 232.720 1.00 67.09 ? 371  GLY A N      1 
ATOM   1855 C  CA     . GLY A 1 371  ? 138.696 153.317 233.966 1.00 67.09 ? 371  GLY A CA     1 
ATOM   1856 C  C      . GLY A 1 371  ? 137.973 154.264 234.900 1.00 67.09 ? 371  GLY A C      1 
ATOM   1857 O  O      . GLY A 1 371  ? 138.466 155.358 235.187 1.00 67.09 ? 371  GLY A O      1 
ATOM   1858 N  N      . ALA A 1 372  ? 136.794 153.861 235.375 1.00 67.05 ? 372  ALA A N      1 
ATOM   1859 C  CA     . ALA A 1 372  ? 136.000 154.679 236.286 1.00 67.05 ? 372  ALA A CA     1 
ATOM   1860 C  C      . ALA A 1 372  ? 136.131 154.214 237.732 1.00 67.05 ? 372  ALA A C      1 
ATOM   1861 O  O      . ALA A 1 372  ? 136.523 154.992 238.607 1.00 67.05 ? 372  ALA A O      1 
ATOM   1862 C  CB     . ALA A 1 372  ? 134.528 154.671 235.851 1.00 67.05 ? 372  ALA A CB     1 
ATOM   1863 N  N      . LYS A 1 373  ? 135.813 152.951 237.997 1.00 66.20 ? 373  LYS A N      1 
ATOM   1864 C  CA     . LYS A 1 373  ? 135.883 152.380 239.333 1.00 66.20 ? 373  LYS A CA     1 
ATOM   1865 C  C      . LYS A 1 373  ? 136.950 151.296 239.375 1.00 66.20 ? 373  LYS A C      1 
ATOM   1866 O  O      . LYS A 1 373  ? 137.145 150.567 238.398 1.00 66.20 ? 373  LYS A O      1 
ATOM   1867 C  CB     . LYS A 1 373  ? 134.533 151.794 239.756 1.00 66.20 ? 373  LYS A CB     1 
ATOM   1868 C  CG     . LYS A 1 373  ? 133.454 152.831 240.005 1.00 66.20 ? 373  LYS A CG     1 
ATOM   1869 C  CD     . LYS A 1 373  ? 132.119 152.169 240.307 1.00 66.20 ? 373  LYS A CD     1 
ATOM   1870 C  CE     . LYS A 1 373  ? 132.135 151.504 241.674 1.00 66.20 ? 373  LYS A CE     1 
ATOM   1871 N  NZ     . LYS A 1 373  ? 130.802 150.950 242.037 1.00 66.20 ? 373  LYS A NZ     1 
ATOM   1872 N  N      . GLY A 1 374  ? 137.631 151.192 240.510 1.00 68.58 ? 374  GLY A N      1 
ATOM   1873 C  CA     . GLY A 1 374  ? 138.679 150.199 240.660 1.00 68.58 ? 374  GLY A CA     1 
ATOM   1874 C  C      . GLY A 1 374  ? 139.944 150.518 239.894 1.00 68.58 ? 374  GLY A C      1 
ATOM   1875 O  O      . GLY A 1 374  ? 140.590 149.606 239.363 1.00 68.58 ? 374  GLY A O      1 
ATOM   1876 N  N      . ALA A 1 375  ? 140.318 151.794 239.824 1.00 69.40 ? 375  ALA A N      1 
ATOM   1877 C  CA     . ALA A 1 375  ? 141.518 152.199 239.107 1.00 69.40 ? 375  ALA A CA     1 
ATOM   1878 C  C      . ALA A 1 375  ? 142.783 152.069 239.944 1.00 69.40 ? 375  ALA A C      1 
ATOM   1879 O  O      . ALA A 1 375  ? 143.873 152.355 239.437 1.00 69.40 ? 375  ALA A O      1 
ATOM   1880 C  CB     . ALA A 1 375  ? 141.375 153.638 238.608 1.00 69.40 ? 375  ALA A CB     1 
ATOM   1881 N  N      . ASP A 1 376  ? 142.665 151.642 241.203 1.00 70.46 ? 376  ASP A N      1 
ATOM   1882 C  CA     . ASP A 1 376  ? 143.843 151.469 242.046 1.00 70.46 ? 376  ASP A CA     1 
ATOM   1883 C  C      . ASP A 1 376  ? 144.686 150.292 241.569 1.00 70.46 ? 376  ASP A C      1 
ATOM   1884 O  O      . ASP A 1 376  ? 145.922 150.368 241.570 1.00 70.46 ? 376  ASP A O      1 
ATOM   1885 C  CB     . ASP A 1 376  ? 143.414 151.277 243.503 1.00 70.46 ? 376  ASP A CB     1 
ATOM   1886 C  CG     . ASP A 1 376  ? 144.555 151.482 244.495 1.00 70.46 ? 376  ASP A CG     1 
ATOM   1887 O  OD1    . ASP A 1 376  ? 145.688 151.802 244.076 1.00 70.46 ? 376  ASP A OD1    1 
ATOM   1888 O  OD2    . ASP A 1 376  ? 144.312 151.321 245.709 1.00 70.46 ? 376  ASP A OD2    1 
ATOM   1889 N  N      . LYS A 1 377  ? 144.040 149.207 241.130 1.00 68.03 ? 377  LYS A N      1 
ATOM   1890 C  CA     . LYS A 1 377  ? 144.800 148.045 240.683 1.00 68.03 ? 377  LYS A CA     1 
ATOM   1891 C  C      . LYS A 1 377  ? 145.465 148.299 239.333 1.00 68.03 ? 377  LYS A C      1 
ATOM   1892 O  O      . LYS A 1 377  ? 146.605 147.876 239.116 1.00 68.03 ? 377  LYS A O      1 
ATOM   1893 C  CB     . LYS A 1 377  ? 143.912 146.795 240.654 1.00 68.03 ? 377  LYS A CB     1 
ATOM   1894 C  CG     . LYS A 1 377  ? 142.759 146.790 239.663 1.00 68.03 ? 377  LYS A CG     1 
ATOM   1895 C  CD     . LYS A 1 377  ? 141.920 145.531 239.819 1.00 68.03 ? 377  LYS A CD     1 
ATOM   1896 C  CE     . LYS A 1 377  ? 142.674 144.303 239.330 1.00 68.03 ? 377  LYS A CE     1 
ATOM   1897 N  NZ     . LYS A 1 377  ? 141.841 143.072 239.397 1.00 68.03 ? 377  LYS A NZ     1 
ATOM   1898 N  N      . THR A 1 378  ? 144.814 149.046 238.438 1.00 66.64 ? 378  THR A N      1 
ATOM   1899 C  CA     . THR A 1 378  ? 145.486 149.389 237.192 1.00 66.64 ? 378  THR A CA     1 
ATOM   1900 C  C      . THR A 1 378  ? 146.510 150.500 237.378 1.00 66.64 ? 378  THR A C      1 
ATOM   1901 O  O      . THR A 1 378  ? 147.441 150.596 236.578 1.00 66.64 ? 378  THR A O      1 
ATOM   1902 C  CB     . THR A 1 378  ? 144.478 149.767 236.098 1.00 66.64 ? 378  THR A CB     1 
ATOM   1903 O  OG1    . THR A 1 378  ? 145.167 149.919 234.853 1.00 66.64 ? 378  THR A OG1    1 
ATOM   1904 C  CG2    . THR A 1 378  ? 143.775 151.058 236.407 1.00 66.64 ? 378  THR A CG2    1 
ATOM   1905 N  N      . TYR A 1 379  ? 146.413 151.291 238.450 1.00 68.05 ? 379  TYR A N      1 
ATOM   1906 C  CA     . TYR A 1 379  ? 147.476 152.245 238.743 1.00 68.05 ? 379  TYR A CA     1 
ATOM   1907 C  C      . TYR A 1 379  ? 148.706 151.547 239.311 1.00 68.05 ? 379  TYR A C      1 
ATOM   1908 O  O      . TYR A 1 379  ? 149.839 151.868 238.930 1.00 68.05 ? 379  TYR A O      1 
ATOM   1909 C  CB     . TYR A 1 379  ? 146.968 153.319 239.700 1.00 68.05 ? 379  TYR A CB     1 
ATOM   1910 C  CG     . TYR A 1 379  ? 148.028 154.317 240.085 1.00 68.05 ? 379  TYR A CG     1 
ATOM   1911 C  CD1    . TYR A 1 379  ? 148.514 155.229 239.159 1.00 68.05 ? 379  TYR A CD1    1 
ATOM   1912 C  CD2    . TYR A 1 379  ? 148.532 154.357 241.379 1.00 68.05 ? 379  TYR A CD2    1 
ATOM   1913 C  CE1    . TYR A 1 379  ? 149.482 156.144 239.507 1.00 68.05 ? 379  TYR A CE1    1 
ATOM   1914 C  CE2    . TYR A 1 379  ? 149.495 155.276 241.738 1.00 68.05 ? 379  TYR A CE2    1 
ATOM   1915 C  CZ     . TYR A 1 379  ? 149.971 156.163 240.797 1.00 68.05 ? 379  TYR A CZ     1 
ATOM   1916 O  OH     . TYR A 1 379  ? 150.934 157.077 241.151 1.00 68.05 ? 379  TYR A OH     1 
ATOM   1917 N  N      . SER A 1 380  ? 148.501 150.581 240.213 1.00 66.85 ? 380  SER A N      1 
ATOM   1918 C  CA     . SER A 1 380  ? 149.603 149.748 240.690 1.00 66.85 ? 380  SER A CA     1 
ATOM   1919 C  C      . SER A 1 380  ? 150.218 148.945 239.551 1.00 66.85 ? 380  SER A C      1 
ATOM   1920 O  O      . SER A 1 380  ? 151.441 148.767 239.488 1.00 66.85 ? 380  SER A O      1 
ATOM   1921 C  CB     . SER A 1 380  ? 149.107 148.814 241.793 1.00 66.85 ? 380  SER A CB     1 
ATOM   1922 O  OG     . SER A 1 380  ? 150.132 147.935 242.220 1.00 66.85 ? 380  SER A OG     1 
ATOM   1923 N  N      . MET A 1 381  ? 149.380 148.502 238.616 1.00 63.17 ? 381  MET A N      1 
ATOM   1924 C  CA     . MET A 1 381  ? 149.840 147.759 237.452 1.00 63.17 ? 381  MET A CA     1 
ATOM   1925 C  C      . MET A 1 381  ? 150.647 148.642 236.507 1.00 63.17 ? 381  MET A C      1 
ATOM   1926 O  O      . MET A 1 381  ? 151.705 148.231 236.015 1.00 63.17 ? 381  MET A O      1 
ATOM   1927 C  CB     . MET A 1 381  ? 148.618 147.168 236.759 1.00 63.17 ? 381  MET A CB     1 
ATOM   1928 C  CG     . MET A 1 381  ? 148.888 146.212 235.653 1.00 63.17 ? 381  MET A CG     1 
ATOM   1929 S  SD     . MET A 1 381  ? 147.332 145.542 235.059 1.00 63.17 ? 381  MET A SD     1 
ATOM   1930 C  CE     . MET A 1 381  ? 146.885 144.476 236.424 1.00 63.17 ? 381  MET A CE     1 
ATOM   1931 N  N      . ILE A 1 382  ? 150.187 149.872 236.273 1.00 63.54 ? 382  ILE A N      1 
ATOM   1932 C  CA     . ILE A 1 382  ? 150.878 150.775 235.364 1.00 63.54 ? 382  ILE A CA     1 
ATOM   1933 C  C      . ILE A 1 382  ? 152.130 151.360 236.010 1.00 63.54 ? 382  ILE A C      1 
ATOM   1934 O  O      . ILE A 1 382  ? 153.004 151.871 235.301 1.00 63.54 ? 382  ILE A O      1 
ATOM   1935 C  CB     . ILE A 1 382  ? 149.884 151.853 234.891 1.00 63.54 ? 382  ILE A CB     1 
ATOM   1936 C  CG1    . ILE A 1 382  ? 150.280 152.443 233.547 1.00 63.54 ? 382  ILE A CG1    1 
ATOM   1937 C  CG2    . ILE A 1 382  ? 149.789 153.001 235.870 1.00 63.54 ? 382  ILE A CG2    1 
ATOM   1938 C  CD1    . ILE A 1 382  ? 149.152 153.245 232.947 1.00 63.54 ? 382  ILE A CD1    1 
ATOM   1939 N  N      . LYS A 1 383  ? 152.250 151.289 237.341 1.00 64.84 ? 383  LYS A N      1 
ATOM   1940 C  CA     . LYS A 1 383  ? 153.533 151.586 237.969 1.00 64.84 ? 383  LYS A CA     1 
ATOM   1941 C  C      . LYS A 1 383  ? 154.491 150.407 237.866 1.00 64.84 ? 383  LYS A C      1 
ATOM   1942 O  O      . LYS A 1 383  ? 155.674 150.594 237.564 1.00 64.84 ? 383  LYS A O      1 
ATOM   1943 C  CB     . LYS A 1 383  ? 153.354 151.964 239.438 1.00 64.84 ? 383  LYS A CB     1 
ATOM   1944 C  CG     . LYS A 1 383  ? 152.710 153.302 239.689 1.00 64.84 ? 383  LYS A CG     1 
ATOM   1945 C  CD     . LYS A 1 383  ? 152.829 153.663 241.155 1.00 64.84 ? 383  LYS A CD     1 
ATOM   1946 C  CE     . LYS A 1 383  ? 151.974 152.752 242.013 1.00 64.84 ? 383  LYS A CE     1 
ATOM   1947 N  NZ     . LYS A 1 383  ? 151.981 153.187 243.435 1.00 64.84 ? 383  LYS A NZ     1 
ATOM   1948 N  N      . ASP A 1 384  ? 154.007 149.187 238.119 1.00 63.40 ? 384  ASP A N      1 
ATOM   1949 C  CA     . ASP A 1 384  ? 154.886 148.024 238.090 1.00 63.40 ? 384  ASP A CA     1 
ATOM   1950 C  C      . ASP A 1 384  ? 155.286 147.607 236.680 1.00 63.40 ? 384  ASP A C      1 
ATOM   1951 O  O      . ASP A 1 384  ? 156.176 146.760 236.540 1.00 63.40 ? 384  ASP A O      1 
ATOM   1952 C  CB     . ASP A 1 384  ? 154.231 146.848 238.817 1.00 63.40 ? 384  ASP A CB     1 
ATOM   1953 C  CG     . ASP A 1 384  ? 154.212 147.034 240.323 1.00 63.40 ? 384  ASP A CG     1 
ATOM   1954 O  OD1    . ASP A 1 384  ? 155.116 147.715 240.849 1.00 63.40 ? 384  ASP A OD1    1 
ATOM   1955 O  OD2    . ASP A 1 384  ? 153.300 146.495 240.983 1.00 63.40 ? 384  ASP A OD2    1 
ATOM   1956 N  N      . VAL A 1 385  ? 154.636 148.149 235.646 1.00 59.19 ? 385  VAL A N      1 
ATOM   1957 C  CA     . VAL A 1 385  ? 155.157 148.012 234.285 1.00 59.19 ? 385  VAL A CA     1 
ATOM   1958 C  C      . VAL A 1 385  ? 156.528 148.668 234.172 1.00 59.19 ? 385  VAL A C      1 
ATOM   1959 O  O      . VAL A 1 385  ? 157.494 148.060 233.692 1.00 59.19 ? 385  VAL A O      1 
ATOM   1960 C  CB     . VAL A 1 385  ? 154.169 148.601 233.263 1.00 59.19 ? 385  VAL A CB     1 
ATOM   1961 C  CG1    . VAL A 1 385  ? 154.847 148.782 231.936 1.00 59.19 ? 385  VAL A CG1    1 
ATOM   1962 C  CG2    . VAL A 1 385  ? 152.991 147.673 233.079 1.00 59.19 ? 385  VAL A CG2    1 
ATOM   1963 N  N      . LEU A 1 386  ? 156.646 149.900 234.662 1.00 60.85 ? 386  LEU A N      1 
ATOM   1964 C  CA     . LEU A 1 386  ? 157.840 150.725 234.512 1.00 60.85 ? 386  LEU A CA     1 
ATOM   1965 C  C      . LEU A 1 386  ? 158.961 150.365 235.481 1.00 60.85 ? 386  LEU A C      1 
ATOM   1966 O  O      . LEU A 1 386  ? 159.892 151.160 235.630 1.00 60.85 ? 386  LEU A O      1 
ATOM   1967 C  CB     . LEU A 1 386  ? 157.470 152.193 234.701 1.00 60.85 ? 386  LEU A CB     1 
ATOM   1968 C  CG     . LEU A 1 386  ? 156.507 152.758 233.667 1.00 60.85 ? 386  LEU A CG     1 
ATOM   1969 C  CD1    . LEU A 1 386  ? 156.054 154.104 234.122 1.00 60.85 ? 386  LEU A CD1    1 
ATOM   1970 C  CD2    . LEU A 1 386  ? 157.186 152.857 232.322 1.00 60.85 ? 386  LEU A CD2    1 
ATOM   1971 N  N      . GLU A 1 387  ? 158.887 149.208 236.141 1.00 60.88 ? 387  GLU A N      1 
ATOM   1972 C  CA     . GLU A 1 387  ? 159.907 148.809 237.105 1.00 60.88 ? 387  GLU A CA     1 
ATOM   1973 C  C      . GLU A 1 387  ? 161.247 148.538 236.430 1.00 60.88 ? 387  GLU A C      1 
ATOM   1974 O  O      . GLU A 1 387  ? 162.302 148.861 236.985 1.00 60.88 ? 387  GLU A O      1 
ATOM   1975 C  CB     . GLU A 1 387  ? 159.409 147.584 237.880 1.00 60.88 ? 387  GLU A CB     1 
ATOM   1976 C  CG     . GLU A 1 387  ? 160.316 147.045 238.980 1.00 60.88 ? 387  GLU A CG     1 
ATOM   1977 C  CD     . GLU A 1 387  ? 161.222 145.933 238.488 1.00 60.88 ? 387  GLU A CD     1 
ATOM   1978 O  OE1    . GLU A 1 387  ? 160.842 145.251 237.517 1.00 60.88 ? 387  GLU A OE1    1 
ATOM   1979 O  OE2    . GLU A 1 387  ? 162.302 145.728 239.075 1.00 60.88 ? 387  GLU A OE2    1 
ATOM   1980 N  N      . ASP A 1 388  ? 161.234 147.963 235.233 1.00 57.30 ? 388  ASP A N      1 
ATOM   1981 C  CA     . ASP A 1 388  ? 162.458 147.624 234.521 1.00 57.30 ? 388  ASP A CA     1 
ATOM   1982 C  C      . ASP A 1 388  ? 162.619 148.572 233.341 1.00 57.30 ? 388  ASP A C      1 
ATOM   1983 O  O      . ASP A 1 388  ? 161.713 148.694 232.512 1.00 57.30 ? 388  ASP A O      1 
ATOM   1984 C  CB     . ASP A 1 388  ? 162.429 146.169 234.048 1.00 57.30 ? 388  ASP A CB     1 
ATOM   1985 C  CG     . ASP A 1 388  ? 163.804 145.647 233.664 1.00 57.30 ? 388  ASP A CG     1 
ATOM   1986 O  OD1    . ASP A 1 388  ? 164.793 146.404 233.777 1.00 57.30 ? 388  ASP A OD1    1 
ATOM   1987 O  OD2    . ASP A 1 388  ? 163.894 144.471 233.253 1.00 57.30 ? 388  ASP A OD2    1 
ATOM   1988 N  N      . GLU A 1 389  ? 163.772 149.239 233.271 1.00 57.61 ? 389  GLU A N      1 
ATOM   1989 C  CA     . GLU A 1 389  ? 163.997 150.223 232.220 1.00 57.61 ? 389  GLU A CA     1 
ATOM   1990 C  C      . GLU A 1 389  ? 164.260 149.582 230.867 1.00 57.61 ? 389  GLU A C      1 
ATOM   1991 O  O      . GLU A 1 389  ? 163.998 150.212 229.839 1.00 57.61 ? 389  GLU A O      1 
ATOM   1992 C  CB     . GLU A 1 389  ? 165.165 151.146 232.596 1.00 57.61 ? 389  GLU A CB     1 
ATOM   1993 C  CG     . GLU A 1 389  ? 166.557 150.511 232.581 1.00 57.61 ? 389  GLU A CG     1 
ATOM   1994 C  CD     . GLU A 1 389  ? 166.932 149.836 233.890 1.00 57.61 ? 389  GLU A CD     1 
ATOM   1995 O  OE1    . GLU A 1 389  ? 166.041 149.599 234.733 1.00 57.61 ? 389  GLU A OE1    1 
ATOM   1996 O  OE2    . GLU A 1 389  ? 168.129 149.537 234.074 1.00 57.61 ? 389  GLU A OE2    1 
ATOM   1997 N  N      . LYS A 1 390  ? 164.751 148.346 230.839 1.00 52.53 ? 390  LYS A N      1 
ATOM   1998 C  CA     . LYS A 1 390  ? 165.114 147.702 229.588 1.00 52.53 ? 390  LYS A CA     1 
ATOM   1999 C  C      . LYS A 1 390  ? 163.945 146.995 228.918 1.00 52.53 ? 390  LYS A C      1 
ATOM   2000 O  O      . LYS A 1 390  ? 164.055 146.627 227.744 1.00 52.53 ? 390  LYS A O      1 
ATOM   2001 C  CB     . LYS A 1 390  ? 166.251 146.704 229.819 1.00 52.53 ? 390  LYS A CB     1 
ATOM   2002 C  CG     . LYS A 1 390  ? 165.899 145.551 230.730 1.00 52.53 ? 390  LYS A CG     1 
ATOM   2003 C  CD     . LYS A 1 390  ? 167.053 144.571 230.826 1.00 52.53 ? 390  LYS A CD     1 
ATOM   2004 C  CE     . LYS A 1 390  ? 168.206 145.149 231.624 1.00 52.53 ? 390  LYS A CE     1 
ATOM   2005 N  NZ     . LYS A 1 390  ? 169.286 144.144 231.832 1.00 52.53 ? 390  LYS A NZ     1 
ATOM   2006 N  N      . MET A 1 391  ? 162.833 146.804 229.621 1.00 49.20 ? 391  MET A N      1 
ATOM   2007 C  CA     . MET A 1 391  ? 161.684 146.133 229.042 1.00 49.20 ? 391  MET A CA     1 
ATOM   2008 C  C      . MET A 1 391  ? 160.610 147.095 228.569 1.00 49.20 ? 391  MET A C      1 
ATOM   2009 O  O      . MET A 1 391  ? 159.679 146.670 227.883 1.00 49.20 ? 391  MET A O      1 
ATOM   2010 C  CB     . MET A 1 391  ? 161.085 145.150 230.049 1.00 49.20 ? 391  MET A CB     1 
ATOM   2011 C  CG     . MET A 1 391  ? 162.072 144.094 230.461 1.00 49.20 ? 391  MET A CG     1 
ATOM   2012 S  SD     . MET A 1 391  ? 162.672 143.165 229.045 1.00 49.20 ? 391  MET A SD     1 
ATOM   2013 C  CE     . MET A 1 391  ? 164.061 142.322 229.792 1.00 49.20 ? 391  MET A CE     1 
ATOM   2014 N  N      . ILE A 1 392  ? 160.720 148.373 228.895 1.00 48.45 ? 392  ILE A N      1 
ATOM   2015 C  CA     . ILE A 1 392  ? 159.753 149.367 228.461 1.00 48.45 ? 392  ILE A CA     1 
ATOM   2016 C  C      . ILE A 1 392  ? 160.476 150.388 227.593 1.00 48.45 ? 392  ILE A C      1 
ATOM   2017 O  O      . ILE A 1 392  ? 161.649 150.705 227.822 1.00 48.45 ? 392  ILE A O      1 
ATOM   2018 C  CB     . ILE A 1 392  ? 159.031 150.013 229.670 1.00 48.45 ? 392  ILE A CB     1 
ATOM   2019 C  CG1    . ILE A 1 392  ? 157.816 150.829 229.223 1.00 48.45 ? 392  ILE A CG1    1 
ATOM   2020 C  CG2    . ILE A 1 392  ? 159.980 150.798 230.576 1.00 48.45 ? 392  ILE A CG2    1 
ATOM   2021 C  CD1    . ILE A 1 392  ? 156.700 149.976 228.716 1.00 48.45 ? 392  ILE A CD1    1 
ATOM   2022 N  N      . SER A 1 393  ? 159.797 150.839 226.545 1.00 46.75 ? 393  SER A N      1 
ATOM   2023 C  CA     . SER A 1 393  ? 160.325 151.836 225.633 1.00 46.75 ? 393  SER A CA     1 
ATOM   2024 C  C      . SER A 1 393  ? 159.144 152.627 225.107 1.00 46.75 ? 393  SER A C      1 
ATOM   2025 O  O      . SER A 1 393  ? 158.055 152.083 224.927 1.00 46.75 ? 393  SER A O      1 
ATOM   2026 C  CB     . SER A 1 393  ? 161.105 151.191 224.483 1.00 46.75 ? 393  SER A CB     1 
ATOM   2027 O  OG     . SER A 1 393  ? 161.552 152.157 223.551 1.00 46.75 ? 393  SER A OG     1 
ATOM   2028 N  N      . VAL A 1 394  ? 159.351 153.918 224.886 1.00 52.59 ? 394  VAL A N      1 
ATOM   2029 C  CA     . VAL A 1 394  ? 158.266 154.822 224.525 1.00 52.59 ? 394  VAL A CA     1 
ATOM   2030 C  C      . VAL A 1 394  ? 158.646 155.548 223.246 1.00 52.59 ? 394  VAL A C      1 
ATOM   2031 O  O      . VAL A 1 394  ? 159.661 156.253 223.202 1.00 52.59 ? 394  VAL A O      1 
ATOM   2032 C  CB     . VAL A 1 394  ? 157.947 155.813 225.654 1.00 52.59 ? 394  VAL A CB     1 
ATOM   2033 C  CG1    . VAL A 1 394  ? 157.053 156.899 225.155 1.00 52.59 ? 394  VAL A CG1    1 
ATOM   2034 C  CG2    . VAL A 1 394  ? 157.247 155.091 226.786 1.00 52.59 ? 394  VAL A CG2    1 
ATOM   2035 N  N      . TYR A 1 395  ? 157.838 155.365 222.205 1.00 60.36 ? 395  TYR A N      1 
ATOM   2036 C  CA     . TYR A 1 395  ? 158.063 155.962 220.893 1.00 60.36 ? 395  TYR A CA     1 
ATOM   2037 C  C      . TYR A 1 395  ? 156.780 156.678 220.484 1.00 60.36 ? 395  TYR A C      1 
ATOM   2038 O  O      . TYR A 1 395  ? 155.803 156.034 220.096 1.00 60.36 ? 395  TYR A O      1 
ATOM   2039 C  CB     . TYR A 1 395  ? 158.458 154.896 219.881 1.00 60.36 ? 395  TYR A CB     1 
ATOM   2040 C  CG     . TYR A 1 395  ? 158.624 155.424 218.485 1.00 60.36 ? 395  TYR A CG     1 
ATOM   2041 C  CD1    . TYR A 1 395  ? 159.729 156.191 218.144 1.00 60.36 ? 395  TYR A CD1    1 
ATOM   2042 C  CD2    . TYR A 1 395  ? 157.674 155.158 217.506 1.00 60.36 ? 395  TYR A CD2    1 
ATOM   2043 C  CE1    . TYR A 1 395  ? 159.884 156.681 216.869 1.00 60.36 ? 395  TYR A CE1    1 
ATOM   2044 C  CE2    . TYR A 1 395  ? 157.821 155.643 216.228 1.00 60.36 ? 395  TYR A CE2    1 
ATOM   2045 C  CZ     . TYR A 1 395  ? 158.927 156.404 215.918 1.00 60.36 ? 395  TYR A CZ     1 
ATOM   2046 O  OH     . TYR A 1 395  ? 159.082 156.896 214.650 1.00 60.36 ? 395  TYR A OH     1 
ATOM   2047 N  N      . SER A 1 396  ? 156.784 158.005 220.565 1.00 66.69 ? 396  SER A N      1 
ATOM   2048 C  CA     . SER A 1 396  ? 155.590 158.789 220.289 1.00 66.69 ? 396  SER A CA     1 
ATOM   2049 C  C      . SER A 1 396  ? 155.441 159.037 218.790 1.00 66.69 ? 396  SER A C      1 
ATOM   2050 O  O      . SER A 1 396  ? 156.222 158.553 217.966 1.00 66.69 ? 396  SER A O      1 
ATOM   2051 C  CB     . SER A 1 396  ? 155.637 160.111 221.049 1.00 66.69 ? 396  SER A CB     1 
ATOM   2052 O  OG     . SER A 1 396  ? 156.684 160.934 220.570 1.00 66.69 ? 396  SER A OG     1 
ATOM   2053 N  N      . LEU A 1 397  ? 154.410 159.802 218.432 1.00 73.95 ? 397  LEU A N      1 
ATOM   2054 C  CA     . LEU A 1 397  ? 154.236 160.257 217.058 1.00 73.95 ? 397  LEU A CA     1 
ATOM   2055 C  C      . LEU A 1 397  ? 154.901 161.608 216.828 1.00 73.95 ? 397  LEU A C      1 
ATOM   2056 O  O      . LEU A 1 397  ? 155.708 161.759 215.906 1.00 73.95 ? 397  LEU A O      1 
ATOM   2057 C  CB     . LEU A 1 397  ? 152.751 160.350 216.702 1.00 73.95 ? 397  LEU A CB     1 
ATOM   2058 C  CG     . LEU A 1 397  ? 152.521 160.806 215.255 1.00 73.95 ? 397  LEU A CG     1 
ATOM   2059 C  CD1    . LEU A 1 397  ? 153.039 159.763 214.272 1.00 73.95 ? 397  LEU A CD1    1 
ATOM   2060 C  CD2    . LEU A 1 397  ? 151.065 161.156 214.971 1.00 73.95 ? 397  LEU A CD2    1 
ATOM   2061 N  N      . ASP A 1 398  ? 154.582 162.593 217.669 1.00 79.47 ? 398  ASP A N      1 
ATOM   2062 C  CA     . ASP A 1 398  ? 155.100 163.943 217.497 1.00 79.47 ? 398  ASP A CA     1 
ATOM   2063 C  C      . ASP A 1 398  ? 156.573 164.067 217.867 1.00 79.47 ? 398  ASP A C      1 
ATOM   2064 O  O      . ASP A 1 398  ? 157.207 165.061 217.494 1.00 79.47 ? 398  ASP A O      1 
ATOM   2065 C  CB     . ASP A 1 398  ? 154.269 164.927 218.323 1.00 79.47 ? 398  ASP A CB     1 
ATOM   2066 C  CG     . ASP A 1 398  ? 152.855 165.078 217.796 1.00 79.47 ? 398  ASP A CG     1 
ATOM   2067 O  OD1    . ASP A 1 398  ? 152.653 164.891 216.578 1.00 79.47 ? 398  ASP A OD1    1 
ATOM   2068 O  OD2    . ASP A 1 398  ? 151.947 165.385 218.598 1.00 79.47 ? 398  ASP A OD2    1 
ATOM   2069 N  N      . GLY A 1 399  ? 157.128 163.095 218.592 1.00 77.77 ? 399  GLY A N      1 
ATOM   2070 C  CA     . GLY A 1 399  ? 158.553 163.129 218.882 1.00 77.77 ? 399  GLY A CA     1 
ATOM   2071 C  C      . GLY A 1 399  ? 159.399 162.816 217.661 1.00 77.77 ? 399  GLY A C      1 
ATOM   2072 O  O      . GLY A 1 399  ? 160.267 163.603 217.274 1.00 77.77 ? 399  GLY A O      1 
ATOM   2073 N  N      . GLU A 1 400  ? 159.155 161.665 217.035 1.00 75.46 ? 400  GLU A N      1 
ATOM   2074 C  CA     . GLU A 1 400  ? 159.842 161.265 215.810 1.00 75.46 ? 400  GLU A CA     1 
ATOM   2075 C  C      . GLU A 1 400  ? 158.783 160.877 214.786 1.00 75.46 ? 400  GLU A C      1 
ATOM   2076 O  O      . GLU A 1 400  ? 158.256 159.762 214.828 1.00 75.46 ? 400  GLU A O      1 
ATOM   2077 C  CB     . GLU A 1 400  ? 160.807 160.107 216.070 1.00 75.46 ? 400  GLU A CB     1 
ATOM   2078 C  CG     . GLU A 1 400  ? 161.963 160.451 217.000 1.00 75.46 ? 400  GLU A CG     1 
ATOM   2079 C  CD     . GLU A 1 400  ? 162.932 161.452 216.393 1.00 75.46 ? 400  GLU A CD     1 
ATOM   2080 O  OE1    . GLU A 1 400  ? 163.120 161.434 215.158 1.00 75.46 ? 400  GLU A OE1    1 
ATOM   2081 O  OE2    . GLU A 1 400  ? 163.506 162.259 217.155 1.00 75.46 ? 400  GLU A OE2    1 
ATOM   2082 N  N      . ILE A 1 401  ? 158.472 161.797 213.872 1.00 76.34 ? 401  ILE A N      1 
ATOM   2083 C  CA     . ILE A 1 401  ? 157.326 161.651 212.981 1.00 76.34 ? 401  ILE A CA     1 
ATOM   2084 C  C      . ILE A 1 401  ? 157.619 160.675 211.848 1.00 76.34 ? 401  ILE A C      1 
ATOM   2085 O  O      . ILE A 1 401  ? 156.954 159.641 211.719 1.00 76.34 ? 401  ILE A O      1 
ATOM   2086 C  CB     . ILE A 1 401  ? 156.902 163.020 212.417 1.00 76.34 ? 401  ILE A CB     1 
ATOM   2087 C  CG1    . ILE A 1 401  ? 156.518 163.970 213.552 1.00 76.34 ? 401  ILE A CG1    1 
ATOM   2088 C  CG2    . ILE A 1 401  ? 155.747 162.856 211.452 1.00 76.34 ? 401  ILE A CG2    1 
ATOM   2089 C  CD1    . ILE A 1 401  ? 156.332 165.405 213.119 1.00 76.34 ? 401  ILE A CD1    1 
ATOM   2090 N  N      . SER A 1 402  ? 158.615 161.000 211.018 1.00 72.23 ? 402  SER A N      1 
ATOM   2091 C  CA     . SER A 1 402  ? 158.869 160.237 209.800 1.00 72.23 ? 402  SER A CA     1 
ATOM   2092 C  C      . SER A 1 402  ? 159.650 158.953 210.050 1.00 72.23 ? 402  SER A C      1 
ATOM   2093 O  O      . SER A 1 402  ? 159.698 158.095 209.160 1.00 72.23 ? 402  SER A O      1 
ATOM   2094 C  CB     . SER A 1 402  ? 159.616 161.102 208.783 1.00 72.23 ? 402  SER A CB     1 
ATOM   2095 O  OG     . SER A 1 402  ? 160.908 161.421 209.257 1.00 72.23 ? 402  SER A OG     1 
ATOM   2096 N  N      . GLN A 1 403  ? 160.269 158.817 211.222 1.00 66.79 ? 403  GLN A N      1 
ATOM   2097 C  CA     . GLN A 1 403  ? 160.966 157.591 211.586 1.00 66.79 ? 403  GLN A CA     1 
ATOM   2098 C  C      . GLN A 1 403  ? 159.987 156.431 211.726 1.00 66.79 ? 403  GLN A C      1 
ATOM   2099 O  O      . GLN A 1 403  ? 158.941 156.554 212.368 1.00 66.79 ? 403  GLN A O      1 
ATOM   2100 C  CB     . GLN A 1 403  ? 161.729 157.805 212.895 1.00 66.79 ? 403  GLN A CB     1 
ATOM   2101 C  CG     . GLN A 1 403  ? 162.435 156.578 213.446 1.00 66.79 ? 403  GLN A CG     1 
ATOM   2102 C  CD     . GLN A 1 403  ? 163.182 156.879 214.731 1.00 66.79 ? 403  GLN A CD     1 
ATOM   2103 O  OE1    . GLN A 1 403  ? 163.219 158.019 215.180 1.00 66.79 ? 403  GLN A OE1    1 
ATOM   2104 N  NE2    . GLN A 1 403  ? 163.753 155.851 215.344 1.00 66.79 ? 403  GLN A NE2    1 
ATOM   2105 N  N      . ASP A 1 404  ? 160.329 155.305 211.110 1.00 59.43 ? 404  ASP A N      1 
ATOM   2106 C  CA     . ASP A 1 404  ? 159.469 154.132 211.147 1.00 59.43 ? 404  ASP A CA     1 
ATOM   2107 C  C      . ASP A 1 404  ? 159.544 153.436 212.503 1.00 59.43 ? 404  ASP A C      1 
ATOM   2108 O  O      . ASP A 1 404  ? 160.506 153.589 213.258 1.00 59.43 ? 404  ASP A O      1 
ATOM   2109 C  CB     . ASP A 1 404  ? 159.846 153.165 210.027 1.00 59.43 ? 404  ASP A CB     1 
ATOM   2110 C  CG     . ASP A 1 404  ? 159.494 153.698 208.656 1.00 59.43 ? 404  ASP A CG     1 
ATOM   2111 O  OD1    . ASP A 1 404  ? 158.507 154.456 208.558 1.00 59.43 ? 404  ASP A OD1    1 
ATOM   2112 O  OD2    . ASP A 1 404  ? 160.202 153.359 207.681 1.00 59.43 ? 404  ASP A OD2    1 
ATOM   2113 N  N      . ILE A 1 405  ? 158.491 152.679 212.811 1.00 52.15 ? 405  ILE A N      1 
ATOM   2114 C  CA     . ILE A 1 405  ? 158.335 151.970 214.078 1.00 52.15 ? 405  ILE A CA     1 
ATOM   2115 C  C      . ILE A 1 405  ? 159.286 150.775 214.183 1.00 52.15 ? 405  ILE A C      1 
ATOM   2116 O  O      . ILE A 1 405  ? 159.489 150.221 215.273 1.00 52.15 ? 405  ILE A O      1 
ATOM   2117 C  CB     . ILE A 1 405  ? 156.860 151.542 214.233 1.00 52.15 ? 405  ILE A CB     1 
ATOM   2118 C  CG1    . ILE A 1 405  ? 156.496 151.259 215.688 1.00 52.15 ? 405  ILE A CG1    1 
ATOM   2119 C  CG2    . ILE A 1 405  ? 156.558 150.323 213.379 1.00 52.15 ? 405  ILE A CG2    1 
ATOM   2120 C  CD1    . ILE A 1 405  ? 155.016 151.146 215.916 1.00 52.15 ? 405  ILE A CD1    1 
ATOM   2121 N  N      . ASP A 1 406  ? 159.943 150.408 213.080 1.00 46.94 ? 406  ASP A N      1 
ATOM   2122 C  CA     . ASP A 1 406  ? 160.819 149.245 213.110 1.00 46.94 ? 406  ASP A CA     1 
ATOM   2123 C  C      . ASP A 1 406  ? 162.138 149.529 213.809 1.00 46.94 ? 406  ASP A C      1 
ATOM   2124 O  O      . ASP A 1 406  ? 162.688 148.637 214.461 1.00 46.94 ? 406  ASP A O      1 
ATOM   2125 C  CB     . ASP A 1 406  ? 161.072 148.722 211.689 1.00 46.94 ? 406  ASP A CB     1 
ATOM   2126 C  CG     . ASP A 1 406  ? 161.691 149.758 210.756 1.00 46.94 ? 406  ASP A CG     1 
ATOM   2127 O  OD1    . ASP A 1 406  ? 161.904 150.922 211.147 1.00 46.94 ? 406  ASP A OD1    1 
ATOM   2128 O  OD2    . ASP A 1 406  ? 161.955 149.397 209.592 1.00 46.94 ? 406  ASP A OD2    1 
ATOM   2129 N  N      . LEU A 1 407  ? 162.636 150.763 213.715 1.00 46.16 ? 407  LEU A N      1 
ATOM   2130 C  CA     . LEU A 1 407  ? 163.813 151.134 214.487 1.00 46.16 ? 407  LEU A CA     1 
ATOM   2131 C  C      . LEU A 1 407  ? 163.487 151.234 215.970 1.00 46.16 ? 407  LEU A C      1 
ATOM   2132 O  O      . LEU A 1 407  ? 164.344 150.938 216.805 1.00 46.16 ? 407  LEU A O      1 
ATOM   2133 C  CB     . LEU A 1 407  ? 164.407 152.437 213.952 1.00 46.16 ? 407  LEU A CB     1 
ATOM   2134 C  CG     . LEU A 1 407  ? 165.712 152.944 214.565 1.00 46.16 ? 407  LEU A CG     1 
ATOM   2135 C  CD1    . LEU A 1 407  ? 166.773 151.870 214.509 1.00 46.16 ? 407  LEU A CD1    1 
ATOM   2136 C  CD2    . LEU A 1 407  ? 166.197 154.159 213.796 1.00 46.16 ? 407  LEU A CD2    1 
ATOM   2137 N  N      . ALA A 1 408  ? 162.253 151.615 216.316 1.00 44.92 ? 408  ALA A N      1 
ATOM   2138 C  CA     . ALA A 1 408  ? 161.826 151.587 217.714 1.00 44.92 ? 408  ALA A CA     1 
ATOM   2139 C  C      . ALA A 1 408  ? 161.777 150.162 218.249 1.00 44.92 ? 408  ALA A C      1 
ATOM   2140 O  O      . ALA A 1 408  ? 162.203 149.903 219.383 1.00 44.92 ? 408  ALA A O      1 
ATOM   2141 C  CB     . ALA A 1 408  ? 160.463 152.259 217.863 1.00 44.92 ? 408  ALA A CB     1 
ATOM   2142 N  N      . ILE A 1 409  ? 161.299 149.224 217.427 1.00 42.58 ? 409  ILE A N      1 
ATOM   2143 C  CA     . ILE A 1 409  ? 161.306 147.811 217.803 1.00 42.58 ? 409  ILE A CA     1 
ATOM   2144 C  C      . ILE A 1 409  ? 162.734 147.294 217.945 1.00 42.58 ? 409  ILE A C      1 
ATOM   2145 O  O      . ILE A 1 409  ? 163.056 146.564 218.893 1.00 42.58 ? 409  ILE A O      1 
ATOM   2146 C  CB     . ILE A 1 409  ? 160.499 147.000 216.773 1.00 42.58 ? 409  ILE A CB     1 
ATOM   2147 C  CG1    . ILE A 1 409  ? 159.017 147.359 216.854 1.00 42.58 ? 409  ILE A CG1    1 
ATOM   2148 C  CG2    . ILE A 1 409  ? 160.704 145.517 216.952 1.00 42.58 ? 409  ILE A CG2    1 
ATOM   2149 C  CD1    . ILE A 1 409  ? 158.196 146.767 215.742 1.00 42.58 ? 409  ILE A CD1    1 
ATOM   2150 N  N      . LEU A 1 410  ? 163.617 147.696 217.030 1.00 42.51 ? 410  LEU A N      1 
ATOM   2151 C  CA     . LEU A 1 410  ? 165.003 147.242 217.067 1.00 42.51 ? 410  LEU A CA     1 
ATOM   2152 C  C      . LEU A 1 410  ? 165.742 147.811 218.271 1.00 42.51 ? 410  LEU A C      1 
ATOM   2153 O  O      . LEU A 1 410  ? 166.535 147.110 218.902 1.00 42.51 ? 410  LEU A O      1 
ATOM   2154 C  CB     . LEU A 1 410  ? 165.704 147.632 215.768 1.00 42.51 ? 410  LEU A CB     1 
ATOM   2155 C  CG     . LEU A 1 410  ? 167.075 147.028 215.489 1.00 42.51 ? 410  LEU A CG     1 
ATOM   2156 C  CD1    . LEU A 1 410  ? 166.954 145.528 215.382 1.00 42.51 ? 410  LEU A CD1    1 
ATOM   2157 C  CD2    . LEU A 1 410  ? 167.633 147.606 214.207 1.00 42.51 ? 410  LEU A CD2    1 
ATOM   2158 N  N      . LYS A 1 411  ? 165.469 149.069 218.623 1.00 43.01 ? 411  LYS A N      1 
ATOM   2159 C  CA     . LYS A 1 411  ? 166.040 149.648 219.831 1.00 43.01 ? 411  LYS A CA     1 
ATOM   2160 C  C      . LYS A 1 411  ? 165.506 148.983 221.088 1.00 43.01 ? 411  LYS A C      1 
ATOM   2161 O  O      . LYS A 1 411  ? 166.262 148.804 222.044 1.00 43.01 ? 411  LYS A O      1 
ATOM   2162 C  CB     . LYS A 1 411  ? 165.779 151.152 219.878 1.00 43.01 ? 411  LYS A CB     1 
ATOM   2163 C  CG     . LYS A 1 411  ? 166.632 151.960 218.921 1.00 43.01 ? 411  LYS A CG     1 
ATOM   2164 C  CD     . LYS A 1 411  ? 166.404 153.444 219.112 1.00 43.01 ? 411  LYS A CD     1 
ATOM   2165 C  CE     . LYS A 1 411  ? 165.059 153.858 218.543 1.00 43.01 ? 411  LYS A CE     1 
ATOM   2166 N  NZ     . LYS A 1 411  ? 164.833 155.325 218.617 1.00 43.01 ? 411  LYS A NZ     1 
ATOM   2167 N  N      . ALA A 1 412  ? 164.231 148.579 221.098 1.00 41.61 ? 412  ALA A N      1 
ATOM   2168 C  CA     . ALA A 1 412  ? 163.698 147.847 222.246 1.00 41.61 ? 412  ALA A CA     1 
ATOM   2169 C  C      . ALA A 1 412  ? 164.350 146.478 222.393 1.00 41.61 ? 412  ALA A C      1 
ATOM   2170 O  O      . ALA A 1 412  ? 164.636 146.035 223.511 1.00 41.61 ? 412  ALA A O      1 
ATOM   2171 C  CB     . ALA A 1 412  ? 162.188 147.696 222.114 1.00 41.61 ? 412  ALA A CB     1 
ATOM   2172 N  N      . LEU A 1 413  ? 164.604 145.802 221.273 1.00 41.79 ? 413  LEU A N      1 
ATOM   2173 C  CA     . LEU A 1 413  ? 165.199 144.470 221.330 1.00 41.79 ? 413  LEU A CA     1 
ATOM   2174 C  C      . LEU A 1 413  ? 166.679 144.531 221.684 1.00 41.79 ? 413  LEU A C      1 
ATOM   2175 O  O      . LEU A 1 413  ? 167.183 143.664 222.406 1.00 41.79 ? 413  LEU A O      1 
ATOM   2176 C  CB     . LEU A 1 413  ? 164.983 143.755 220.001 1.00 41.79 ? 413  LEU A CB     1 
ATOM   2177 C  CG     . LEU A 1 413  ? 163.518 143.399 219.772 1.00 41.79 ? 413  LEU A CG     1 
ATOM   2178 C  CD1    . LEU A 1 413  ? 163.287 142.948 218.359 1.00 41.79 ? 413  LEU A CD1    1 
ATOM   2179 C  CD2    . LEU A 1 413  ? 163.106 142.315 220.739 1.00 41.79 ? 413  LEU A CD2    1 
ATOM   2180 N  N      . LEU A 1 414  ? 167.390 145.547 221.194 1.00 43.63 ? 414  LEU A N      1 
ATOM   2181 C  CA     . LEU A 1 414  ? 168.784 145.757 221.566 1.00 43.63 ? 414  LEU A CA     1 
ATOM   2182 C  C      . LEU A 1 414  ? 168.932 146.385 222.943 1.00 43.63 ? 414  LEU A C      1 
ATOM   2183 O  O      . LEU A 1 414  ? 170.031 146.371 223.506 1.00 43.63 ? 414  LEU A O      1 
ATOM   2184 C  CB     . LEU A 1 414  ? 169.481 146.631 220.520 1.00 43.63 ? 414  LEU A CB     1 
ATOM   2185 C  CG     . LEU A 1 414  ? 170.141 145.991 219.294 1.00 43.63 ? 414  LEU A CG     1 
ATOM   2186 C  CD1    . LEU A 1 414  ? 169.175 145.318 218.374 1.00 43.63 ? 414  LEU A CD1    1 
ATOM   2187 C  CD2    . LEU A 1 414  ? 170.843 147.064 218.520 1.00 43.63 ? 414  LEU A CD2    1 
ATOM   2188 N  N      . LYS A 1 415  ? 167.851 146.931 223.490 1.00 45.83 ? 415  LYS A N      1 
ATOM   2189 C  CA     . LYS A 1 415  ? 167.818 147.489 224.830 1.00 45.83 ? 415  LYS A CA     1 
ATOM   2190 C  C      . LYS A 1 415  ? 167.498 146.442 225.883 1.00 45.83 ? 415  LYS A C      1 
ATOM   2191 O  O      . LYS A 1 415  ? 168.020 146.520 227.001 1.00 45.83 ? 415  LYS A O      1 
ATOM   2192 C  CB     . LYS A 1 415  ? 166.778 148.611 224.866 1.00 45.83 ? 415  LYS A CB     1 
ATOM   2193 C  CG     . LYS A 1 415  ? 166.684 149.418 226.136 1.00 45.83 ? 415  LYS A CG     1 
ATOM   2194 C  CD     . LYS A 1 415  ? 165.652 150.510 225.942 1.00 45.83 ? 415  LYS A CD     1 
ATOM   2195 C  CE     . LYS A 1 415  ? 165.501 151.378 227.168 1.00 45.83 ? 415  LYS A CE     1 
ATOM   2196 N  NZ     . LYS A 1 415  ? 164.462 152.427 226.966 1.00 45.83 ? 415  LYS A NZ     1 
ATOM   2197 N  N      . ALA A 1 416  ? 166.653 145.463 225.547 1.00 47.48 ? 416  ALA A N      1 
ATOM   2198 C  CA     . ALA A 1 416  ? 166.333 144.390 226.483 1.00 47.48 ? 416  ALA A CA     1 
ATOM   2199 C  C      . ALA A 1 416  ? 167.525 143.472 226.717 1.00 47.48 ? 416  ALA A C      1 
ATOM   2200 O  O      . ALA A 1 416  ? 167.639 142.884 227.800 1.00 47.48 ? 416  ALA A O      1 
ATOM   2201 C  CB     . ALA A 1 416  ? 165.141 143.584 225.971 1.00 47.48 ? 416  ALA A CB     1 
ATOM   2202 N  N      . ASN A 1 417  ? 168.397 143.337 225.708 1.00 49.20 ? 417  ASN A N      1 
ATOM   2203 C  CA     . ASN A 1 417  ? 169.670 142.606 225.778 1.00 49.20 ? 417  ASN A CA     1 
ATOM   2204 C  C      . ASN A 1 417  ? 169.444 141.128 226.110 1.00 49.20 ? 417  ASN A C      1 
ATOM   2205 O  O      . ASN A 1 417  ? 170.117 140.541 226.959 1.00 49.20 ? 417  ASN A O      1 
ATOM   2206 C  CB     . ASN A 1 417  ? 170.637 143.274 226.767 1.00 49.20 ? 417  ASN A CB     1 
ATOM   2207 C  CG     . ASN A 1 417  ? 172.083 142.864 226.553 1.00 49.20 ? 417  ASN A CG     1 
ATOM   2208 O  OD1    . ASN A 1 417  ? 172.395 142.079 225.660 1.00 49.20 ? 417  ASN A OD1    1 
ATOM   2209 N  ND2    . ASN A 1 417  ? 172.972 143.396 227.380 1.00 49.20 ? 417  ASN A ND2    1 
ATOM   2210 N  N      . ARG A 1 418  ? 168.466 140.529 225.433 1.00 50.46 ? 418  ARG A N      1 
ATOM   2211 C  CA     . ARG A 1 418  ? 168.157 139.119 225.604 1.00 50.46 ? 418  ARG A CA     1 
ATOM   2212 C  C      . ARG A 1 418  ? 168.281 138.309 224.325 1.00 50.46 ? 418  ARG A C      1 
ATOM   2213 O  O      . ARG A 1 418  ? 168.289 137.076 224.398 1.00 50.46 ? 418  ARG A O      1 
ATOM   2214 C  CB     . ARG A 1 418  ? 166.735 138.938 226.156 1.00 50.46 ? 418  ARG A CB     1 
ATOM   2215 C  CG     . ARG A 1 418  ? 166.533 139.426 227.576 1.00 50.46 ? 418  ARG A CG     1 
ATOM   2216 C  CD     . ARG A 1 418  ? 165.082 139.254 227.993 1.00 50.46 ? 418  ARG A CD     1 
ATOM   2217 N  NE     . ARG A 1 418  ? 164.688 137.851 228.059 1.00 50.46 ? 418  ARG A NE     1 
ATOM   2218 C  CZ     . ARG A 1 418  ? 164.803 137.094 229.145 1.00 50.46 ? 418  ARG A CZ     1 
ATOM   2219 N  NH1    . ARG A 1 418  ? 165.298 137.607 230.263 1.00 50.46 ? 418  ARG A NH1    1 
ATOM   2220 N  NH2    . ARG A 1 418  ? 164.420 135.825 229.113 1.00 50.46 ? 418  ARG A NH2    1 
ATOM   2221 N  N      . SER A 1 419  ? 168.386 138.953 223.169 1.00 49.75 ? 419  SER A N      1 
ATOM   2222 C  CA     . SER A 1 419  ? 168.376 138.250 221.898 1.00 49.75 ? 419  SER A CA     1 
ATOM   2223 C  C      . SER A 1 419  ? 169.783 137.836 221.486 1.00 49.75 ? 419  SER A C      1 
ATOM   2224 O  O      . SER A 1 419  ? 170.786 138.281 222.046 1.00 49.75 ? 419  SER A O      1 
ATOM   2225 C  CB     . SER A 1 419  ? 167.743 139.121 220.815 1.00 49.75 ? 419  SER A CB     1 
ATOM   2226 O  OG     . SER A 1 419  ? 166.380 139.365 221.099 1.00 49.75 ? 419  SER A OG     1 
ATOM   2227 N  N      . SER A 1 420  ? 169.839 136.959 220.487 1.00 50.90 ? 420  SER A N      1 
ATOM   2228 C  CA     . SER A 1 420  ? 171.095 136.551 219.895 1.00 50.90 ? 420  SER A CA     1 
ATOM   2229 C  C      . SER A 1 420  ? 171.703 137.714 219.115 1.00 50.90 ? 420  SER A C      1 
ATOM   2230 O  O      . SER A 1 420  ? 170.991 138.632 218.705 1.00 50.90 ? 420  SER A O      1 
ATOM   2231 C  CB     . SER A 1 420  ? 170.872 135.358 218.968 1.00 50.90 ? 420  SER A CB     1 
ATOM   2232 O  OG     . SER A 1 420  ? 170.381 134.238 219.682 1.00 50.90 ? 420  SER A OG     1 
ATOM   2233 N  N      . PRO A 1 421  ? 173.025 137.713 218.919 1.00 51.51 ? 421  PRO A N      1 
ATOM   2234 C  CA     . PRO A 1 421  ? 173.614 138.709 218.012 1.00 51.51 ? 421  PRO A CA     1 
ATOM   2235 C  C      . PRO A 1 421  ? 173.179 138.532 216.568 1.00 51.51 ? 421  PRO A C      1 
ATOM   2236 O  O      . PRO A 1 421  ? 173.027 139.532 215.856 1.00 51.51 ? 421  PRO A O      1 
ATOM   2237 C  CB     . PRO A 1 421  ? 175.124 138.489 218.183 1.00 51.51 ? 421  PRO A CB     1 
ATOM   2238 C  CG     . PRO A 1 421  ? 175.264 137.870 219.526 1.00 51.51 ? 421  PRO A CG     1 
ATOM   2239 C  CD     . PRO A 1 421  ? 174.058 136.995 219.686 1.00 51.51 ? 421  PRO A CD     1 
ATOM   2240 N  N      . VAL A 1 422  ? 172.937 137.299 216.123 1.00 47.77 ? 422  VAL A N      1 
ATOM   2241 C  CA     . VAL A 1 422  ? 172.493 137.098 214.748 1.00 47.77 ? 422  VAL A CA     1 
ATOM   2242 C  C      . VAL A 1 422  ? 171.014 137.436 214.577 1.00 47.77 ? 422  VAL A C      1 
ATOM   2243 O  O      . VAL A 1 422  ? 170.591 137.811 213.480 1.00 47.77 ? 422  VAL A O      1 
ATOM   2244 C  CB     . VAL A 1 422  ? 172.806 135.667 214.278 1.00 47.77 ? 422  VAL A CB     1 
ATOM   2245 C  CG1    . VAL A 1 422  ? 174.306 135.457 214.218 1.00 47.77 ? 422  VAL A CG1    1 
ATOM   2246 C  CG2    . VAL A 1 422  ? 172.172 134.643 215.203 1.00 47.77 ? 422  VAL A CG2    1 
ATOM   2247 N  N      . ALA A 1 423  ? 170.213 137.351 215.642 1.00 45.83 ? 423  ALA A N      1 
ATOM   2248 C  CA     . ALA A 1 423  ? 168.809 137.743 215.541 1.00 45.83 ? 423  ALA A CA     1 
ATOM   2249 C  C      . ALA A 1 423  ? 168.674 139.256 215.426 1.00 45.83 ? 423  ALA A C      1 
ATOM   2250 O  O      . ALA A 1 423  ? 167.923 139.766 214.584 1.00 45.83 ? 423  ALA A O      1 
ATOM   2251 C  CB     . ALA A 1 423  ? 168.032 137.221 216.748 1.00 45.83 ? 423  ALA A CB     1 
ATOM   2252 N  N      . GLN A 1 424  ? 169.414 139.987 216.261 1.00 45.05 ? 424  GLN A N      1 
ATOM   2253 C  CA     . GLN A 1 424  ? 169.503 141.437 216.131 1.00 45.05 ? 424  GLN A CA     1 
ATOM   2254 C  C      . GLN A 1 424  ? 170.095 141.825 214.785 1.00 45.05 ? 424  GLN A C      1 
ATOM   2255 O  O      . GLN A 1 424  ? 169.655 142.796 214.152 1.00 45.05 ? 424  GLN A O      1 
ATOM   2256 C  CB     . GLN A 1 424  ? 170.360 141.988 217.264 1.00 45.05 ? 424  GLN A CB     1 
ATOM   2257 C  CG     . GLN A 1 424  ? 169.816 141.695 218.645 1.00 45.05 ? 424  GLN A CG     1 
ATOM   2258 C  CD     . GLN A 1 424  ? 170.759 142.147 219.734 1.00 45.05 ? 424  GLN A CD     1 
ATOM   2259 O  OE1    . GLN A 1 424  ? 171.852 142.638 219.457 1.00 45.05 ? 424  GLN A OE1    1 
ATOM   2260 N  NE2    . GLN A 1 424  ? 170.348 141.969 220.982 1.00 45.05 ? 424  GLN A NE2    1 
ATOM   2261 N  N      . LEU A 1 425  ? 171.055 141.029 214.310 1.00 43.91 ? 425  LEU A N      1 
ATOM   2262 C  CA     . LEU A 1 425  ? 171.734 141.304 213.054 1.00 43.91 ? 425  LEU A CA     1 
ATOM   2263 C  C      . LEU A 1 425  ? 170.803 141.158 211.858 1.00 43.91 ? 425  LEU A C      1 
ATOM   2264 O  O      . LEU A 1 425  ? 170.773 142.027 210.980 1.00 43.91 ? 425  LEU A O      1 
ATOM   2265 C  CB     . LEU A 1 425  ? 172.935 140.378 212.918 1.00 43.91 ? 425  LEU A CB     1 
ATOM   2266 C  CG     . LEU A 1 425  ? 173.775 140.597 211.673 1.00 43.91 ? 425  LEU A CG     1 
ATOM   2267 C  CD1    . LEU A 1 425  ? 174.278 142.013 211.648 1.00 43.91 ? 425  LEU A CD1    1 
ATOM   2268 C  CD2    . LEU A 1 425  ? 174.921 139.638 211.704 1.00 43.91 ? 425  LEU A CD2    1 
ATOM   2269 N  N      . ASN A 1 426  ? 170.029 140.074 211.794 1.00 41.74 ? 426  ASN A N      1 
ATOM   2270 C  CA     . ASN A 1 426  ? 169.182 139.933 210.620 1.00 41.74 ? 426  ASN A CA     1 
ATOM   2271 C  C      . ASN A 1 426  ? 167.887 140.730 210.737 1.00 41.74 ? 426  ASN A C      1 
ATOM   2272 O  O      . ASN A 1 426  ? 167.271 141.018 209.707 1.00 41.74 ? 426  ASN A O      1 
ATOM   2273 C  CB     . ASN A 1 426  ? 168.944 138.448 210.268 1.00 41.74 ? 426  ASN A CB     1 
ATOM   2274 C  CG     . ASN A 1 426  ? 168.237 137.646 211.349 1.00 41.74 ? 426  ASN A CG     1 
ATOM   2275 O  OD1    . ASN A 1 426  ? 167.739 138.172 212.327 1.00 41.74 ? 426  ASN A OD1    1 
ATOM   2276 N  ND2    . ASN A 1 426  ? 168.201 136.334 211.157 1.00 41.74 ? 426  ASN A ND2    1 
ATOM   2277 N  N      . LEU A 1 427  ? 167.511 141.183 211.939 1.00 39.23 ? 427  LEU A N      1 
ATOM   2278 C  CA     . LEU A 1 427  ? 166.484 142.221 212.009 1.00 39.23 ? 427  LEU A CA     1 
ATOM   2279 C  C      . LEU A 1 427  ? 166.994 143.553 211.468 1.00 39.23 ? 427  LEU A C      1 
ATOM   2280 O  O      . LEU A 1 427  ? 166.266 144.254 210.752 1.00 39.23 ? 427  LEU A O      1 
ATOM   2281 C  CB     . LEU A 1 427  ? 165.981 142.382 213.438 1.00 39.23 ? 427  LEU A CB     1 
ATOM   2282 C  CG     . LEU A 1 427  ? 165.071 141.260 213.917 1.00 39.23 ? 427  LEU A CG     1 
ATOM   2283 C  CD1    . LEU A 1 427  ? 164.818 141.414 215.381 1.00 39.23 ? 427  LEU A CD1    1 
ATOM   2284 C  CD2    . LEU A 1 427  ? 163.781 141.307 213.156 1.00 39.23 ? 427  LEU A CD2    1 
ATOM   2285 N  N      . ALA A 1 428  ? 168.244 143.914 211.785 1.00 39.39 ? 428  ALA A N      1 
ATOM   2286 C  CA     . ALA A 1 428  ? 168.830 145.122 211.205 1.00 39.39 ? 428  ALA A CA     1 
ATOM   2287 C  C      . ALA A 1 428  ? 169.038 144.988 209.699 1.00 39.39 ? 428  ALA A C      1 
ATOM   2288 O  O      . ALA A 1 428  ? 168.965 145.987 208.977 1.00 39.39 ? 428  ALA A O      1 
ATOM   2289 C  CB     . ALA A 1 428  ? 170.151 145.451 211.894 1.00 39.39 ? 428  ALA A CB     1 
ATOM   2290 N  N      . LEU A 1 429  ? 169.300 143.772 209.215 1.00 38.93 ? 429  LEU A N      1 
ATOM   2291 C  CA     . LEU A 1 429  ? 169.343 143.521 207.777 1.00 38.93 ? 429  LEU A CA     1 
ATOM   2292 C  C      . LEU A 1 429  ? 167.978 143.710 207.135 1.00 38.93 ? 429  LEU A C      1 
ATOM   2293 O  O      . LEU A 1 429  ? 167.863 144.335 206.075 1.00 38.93 ? 429  LEU A O      1 
ATOM   2294 C  CB     . LEU A 1 429  ? 169.839 142.109 207.497 1.00 38.93 ? 429  LEU A CB     1 
ATOM   2295 C  CG     . LEU A 1 429  ? 171.313 141.792 207.607 1.00 38.93 ? 429  LEU A CG     1 
ATOM   2296 C  CD1    . LEU A 1 429  ? 171.447 140.312 207.522 1.00 38.93 ? 429  LEU A CD1    1 
ATOM   2297 C  CD2    . LEU A 1 429  ? 172.005 142.433 206.444 1.00 38.93 ? 429  LEU A CD2    1 
ATOM   2298 N  N      . ALA A 1 430  ? 166.937 143.149 207.753 1.00 38.73 ? 430  ALA A N      1 
ATOM   2299 C  CA     . ALA A 1 430  ? 165.594 143.237 207.198 1.00 38.73 ? 430  ALA A CA     1 
ATOM   2300 C  C      . ALA A 1 430  ? 165.061 144.661 207.224 1.00 38.73 ? 430  ALA A C      1 
ATOM   2301 O  O      . ALA A 1 430  ? 164.226 145.022 206.389 1.00 38.73 ? 430  ALA A O      1 
ATOM   2302 C  CB     . ALA A 1 430  ? 164.658 142.307 207.964 1.00 38.73 ? 430  ALA A CB     1 
ATOM   2303 N  N      . TRP A 1 431  ? 165.543 145.484 208.148 1.00 40.44 ? 431  TRP A N      1 
ATOM   2304 C  CA     . TRP A 1 431  ? 165.065 146.850 208.286 1.00 40.44 ? 431  TRP A CA     1 
ATOM   2305 C  C      . TRP A 1 431  ? 166.023 147.882 207.722 1.00 40.44 ? 431  TRP A C      1 
ATOM   2306 O  O      . TRP A 1 431  ? 165.715 149.078 207.786 1.00 40.44 ? 431  TRP A O      1 
ATOM   2307 C  CB     . TRP A 1 431  ? 164.795 147.138 209.753 1.00 40.44 ? 431  TRP A CB     1 
ATOM   2308 C  CG     . TRP A 1 431  ? 163.629 146.395 210.221 1.00 40.44 ? 431  TRP A CG     1 
ATOM   2309 C  CD1    . TRP A 1 431  ? 162.623 145.895 209.454 1.00 40.44 ? 431  TRP A CD1    1 
ATOM   2310 C  CD2    . TRP A 1 431  ? 163.381 145.950 211.547 1.00 40.44 ? 431  TRP A CD2    1 
ATOM   2311 N  NE1    . TRP A 1 431  ? 161.728 145.220 210.231 1.00 40.44 ? 431  TRP A NE1    1 
ATOM   2312 C  CE2    . TRP A 1 431  ? 162.176 145.236 211.524 1.00 40.44 ? 431  TRP A CE2    1 
ATOM   2313 C  CE3    . TRP A 1 431  ? 164.047 146.110 212.762 1.00 40.44 ? 431  TRP A CE3    1 
ATOM   2314 C  CZ2    . TRP A 1 431  ? 161.625 144.685 212.658 1.00 40.44 ? 431  TRP A CZ2    1 
ATOM   2315 C  CZ3    . TRP A 1 431  ? 163.501 145.550 213.886 1.00 40.44 ? 431  TRP A CZ3    1 
ATOM   2316 C  CH2    . TRP A 1 431  ? 162.300 144.851 213.830 1.00 40.44 ? 431  TRP A CH2    1 
ATOM   2317 N  N      . ASN A 1 432  ? 167.171 147.439 207.190 1.00 41.52 ? 432  ASN A N      1 
ATOM   2318 C  CA     . ASN A 1 432  ? 168.179 148.282 206.536 1.00 41.52 ? 432  ASN A CA     1 
ATOM   2319 C  C      . ASN A 1 432  ? 168.718 149.338 207.505 1.00 41.52 ? 432  ASN A C      1 
ATOM   2320 O  O      . ASN A 1 432  ? 168.974 150.485 207.137 1.00 41.52 ? 432  ASN A O      1 
ATOM   2321 C  CB     . ASN A 1 432  ? 167.626 148.910 205.248 1.00 41.52 ? 432  ASN A CB     1 
ATOM   2322 C  CG     . ASN A 1 432  ? 168.712 149.373 204.298 1.00 41.52 ? 432  ASN A CG     1 
ATOM   2323 O  OD1    . ASN A 1 432  ? 169.899 149.231 204.576 1.00 41.52 ? 432  ASN A OD1    1 
ATOM   2324 N  ND2    . ASN A 1 432  ? 168.305 149.935 203.168 1.00 41.52 ? 432  ASN A ND2    1 
ATOM   2325 N  N      . ARG A 1 433  ? 168.884 148.942 208.766 1.00 44.53 ? 433  ARG A N      1 
ATOM   2326 C  CA     . ARG A 1 433  ? 169.306 149.854 209.825 1.00 44.53 ? 433  ARG A CA     1 
ATOM   2327 C  C      . ARG A 1 433  ? 170.803 149.673 210.045 1.00 44.53 ? 433  ARG A C      1 
ATOM   2328 O  O      . ARG A 1 433  ? 171.251 148.905 210.893 1.00 44.53 ? 433  ARG A O      1 
ATOM   2329 C  CB     . ARG A 1 433  ? 168.508 149.605 211.098 1.00 44.53 ? 433  ARG A CB     1 
ATOM   2330 C  CG     . ARG A 1 433  ? 167.030 149.874 210.949 1.00 44.53 ? 433  ARG A CG     1 
ATOM   2331 C  CD     . ARG A 1 433  ? 166.782 151.351 210.749 1.00 44.53 ? 433  ARG A CD     1 
ATOM   2332 N  NE     . ARG A 1 433  ? 165.362 151.661 210.642 1.00 44.53 ? 433  ARG A NE     1 
ATOM   2333 C  CZ     . ARG A 1 433  ? 164.886 152.874 210.389 1.00 44.53 ? 433  ARG A CZ     1 
ATOM   2334 N  NH1    . ARG A 1 433  ? 165.720 153.888 210.217 1.00 44.53 ? 433  ARG A NH1    1 
ATOM   2335 N  NH2    . ARG A 1 433  ? 163.579 153.074 210.307 1.00 44.53 ? 433  ARG A NH2    1 
ATOM   2336 N  N      . ILE A 1 434  ? 171.585 150.402 209.251 1.00 46.68 ? 434  ILE A N      1 
ATOM   2337 C  CA     . ILE A 1 434  ? 173.033 150.240 209.283 1.00 46.68 ? 434  ILE A CA     1 
ATOM   2338 C  C      . ILE A 1 434  ? 173.653 151.006 210.451 1.00 46.68 ? 434  ILE A C      1 
ATOM   2339 O  O      . ILE A 1 434  ? 174.661 150.564 211.016 1.00 46.68 ? 434  ILE A O      1 
ATOM   2340 C  CB     . ILE A 1 434  ? 173.621 150.645 207.913 1.00 46.68 ? 434  ILE A CB     1 
ATOM   2341 C  CG1    . ILE A 1 434  ? 175.104 150.281 207.805 1.00 46.68 ? 434  ILE A CG1    1 
ATOM   2342 C  CG2    . ILE A 1 434  ? 173.353 152.112 207.579 1.00 46.68 ? 434  ILE A CG2    1 
ATOM   2343 C  CD1    . ILE A 1 434  ? 175.366 148.811 207.750 1.00 46.68 ? 434  ILE A CD1    1 
ATOM   2344 N  N      . ASP A 1 435  ? 173.043 152.117 210.875 1.00 49.25 ? 435  ASP A N      1 
ATOM   2345 C  CA     . ASP A 1 435  ? 173.650 152.949 211.908 1.00 49.25 ? 435  ASP A CA     1 
ATOM   2346 C  C      . ASP A 1 435  ? 173.562 152.299 213.286 1.00 49.25 ? 435  ASP A C      1 
ATOM   2347 O  O      . ASP A 1 435  ? 174.554 152.264 214.024 1.00 49.25 ? 435  ASP A O      1 
ATOM   2348 C  CB     . ASP A 1 435  ? 173.013 154.342 211.899 1.00 49.25 ? 435  ASP A CB     1 
ATOM   2349 C  CG     . ASP A 1 435  ? 171.494 154.306 211.999 1.00 49.25 ? 435  ASP A CG     1 
ATOM   2350 O  OD1    . ASP A 1 435  ? 170.905 153.203 211.996 1.00 49.25 ? 435  ASP A OD1    1 
ATOM   2351 O  OD2    . ASP A 1 435  ? 170.884 155.393 212.078 1.00 49.25 ? 435  ASP A OD2    1 
ATOM   2352 N  N      . LEU A 1 436  ? 172.400 151.738 213.633 1.00 50.18 ? 436  LEU A N      1 
ATOM   2353 C  CA     . LEU A 1 436  ? 172.278 151.047 214.910 1.00 50.18 ? 436  LEU A CA     1 
ATOM   2354 C  C      . LEU A 1 436  ? 173.048 149.732 214.897 1.00 50.18 ? 436  LEU A C      1 
ATOM   2355 O  O      . LEU A 1 436  ? 173.507 149.273 215.949 1.00 50.18 ? 436  LEU A O      1 
ATOM   2356 C  CB     . LEU A 1 436  ? 170.803 150.816 215.242 1.00 50.18 ? 436  LEU A CB     1 
ATOM   2357 C  CG     . LEU A 1 436  ? 170.506 150.348 216.669 1.00 50.18 ? 436  LEU A CG     1 
ATOM   2358 C  CD1    . LEU A 1 436  ? 170.902 151.432 217.663 1.00 50.18 ? 436  LEU A CD1    1 
ATOM   2359 C  CD2    . LEU A 1 436  ? 169.059 149.952 216.851 1.00 50.18 ? 436  LEU A CD2    1 
ATOM   2360 N  N      . ALA A 1 437  ? 173.225 149.133 213.717 1.00 50.64 ? 437  ALA A N      1 
ATOM   2361 C  CA     . ALA A 1 437  ? 174.038 147.927 213.606 1.00 50.64 ? 437  ALA A CA     1 
ATOM   2362 C  C      . ALA A 1 437  ? 175.511 148.228 213.844 1.00 50.64 ? 437  ALA A C      1 
ATOM   2363 O  O      . ALA A 1 437  ? 176.204 147.451 214.510 1.00 50.64 ? 437  ALA A O      1 
ATOM   2364 C  CB     . ALA A 1 437  ? 173.838 147.281 212.238 1.00 50.64 ? 437  ALA A CB     1 
ATOM   2365 N  N      . LYS A 1 438  ? 176.012 149.346 213.307 1.00 50.80 ? 438  LYS A N      1 
ATOM   2366 C  CA     . LYS A 1 438  ? 177.376 149.758 213.625 1.00 50.80 ? 438  LYS A CA     1 
ATOM   2367 C  C      . LYS A 1 438  ? 177.509 150.169 215.084 1.00 50.80 ? 438  LYS A C      1 
ATOM   2368 O  O      . LYS A 1 438  ? 178.567 149.968 215.689 1.00 50.80 ? 438  LYS A O      1 
ATOM   2369 C  CB     . LYS A 1 438  ? 177.823 150.915 212.729 1.00 50.80 ? 438  LYS A CB     1 
ATOM   2370 C  CG     . LYS A 1 438  ? 177.920 150.593 211.253 1.00 50.80 ? 438  LYS A CG     1 
ATOM   2371 C  CD     . LYS A 1 438  ? 178.573 151.734 210.491 1.00 50.80 ? 438  LYS A CD     1 
ATOM   2372 C  CE     . LYS A 1 438  ? 177.701 152.978 210.472 1.00 50.80 ? 438  LYS A CE     1 
ATOM   2373 N  NZ     . LYS A 1 438  ? 176.456 152.798 209.685 1.00 50.80 ? 438  LYS A NZ     1 
ATOM   2374 N  N      . SER A 1 439  ? 176.449 150.737 215.662 1.00 51.97 ? 439  SER A N      1 
ATOM   2375 C  CA     . SER A 1 439  ? 176.518 151.231 217.032 1.00 51.97 ? 439  SER A CA     1 
ATOM   2376 C  C      . SER A 1 439  ? 176.540 150.089 218.043 1.00 51.97 ? 439  SER A C      1 
ATOM   2377 O  O      . SER A 1 439  ? 177.499 149.941 218.807 1.00 51.97 ? 439  SER A O      1 
ATOM   2378 C  CB     . SER A 1 439  ? 175.338 152.163 217.302 1.00 51.97 ? 439  SER A CB     1 
ATOM   2379 O  OG     . SER A 1 439  ? 175.385 153.292 216.451 1.00 51.97 ? 439  SER A OG     1 
ATOM   2380 N  N      . ASP A 1 440  ? 175.492 149.261 218.058 1.00 52.95 ? 440  ASP A N      1 
ATOM   2381 C  CA     . ASP A 1 440  ? 175.278 148.338 219.162 1.00 52.95 ? 440  ASP A CA     1 
ATOM   2382 C  C      . ASP A 1 440  ? 175.379 146.864 218.796 1.00 52.95 ? 440  ASP A C      1 
ATOM   2383 O  O      . ASP A 1 440  ? 175.533 146.038 219.700 1.00 52.95 ? 440  ASP A O      1 
ATOM   2384 C  CB     . ASP A 1 440  ? 173.906 148.594 219.800 1.00 52.95 ? 440  ASP A CB     1 
ATOM   2385 C  CG     . ASP A 1 440  ? 173.822 149.947 220.480 1.00 52.95 ? 440  ASP A CG     1 
ATOM   2386 O  OD1    . ASP A 1 440  ? 174.866 150.446 220.951 1.00 52.95 ? 440  ASP A OD1    1 
ATOM   2387 O  OD2    . ASP A 1 440  ? 172.710 150.512 220.541 1.00 52.95 ? 440  ASP A OD2    1 
ATOM   2388 N  N      . ILE A 1 441  ? 175.297 146.506 217.519 1.00 51.44 ? 441  ILE A N      1 
ATOM   2389 C  CA     . ILE A 1 441  ? 175.436 145.105 217.131 1.00 51.44 ? 441  ILE A CA     1 
ATOM   2390 C  C      . ILE A 1 441  ? 176.897 144.748 216.881 1.00 51.44 ? 441  ILE A C      1 
ATOM   2391 O  O      . ILE A 1 441  ? 177.352 143.660 217.243 1.00 51.44 ? 441  ILE A O      1 
ATOM   2392 C  CB     . ILE A 1 441  ? 174.549 144.814 215.901 1.00 51.44 ? 441  ILE A CB     1 
ATOM   2393 C  CG1    . ILE A 1 441  ? 173.082 145.056 216.246 1.00 51.44 ? 441  ILE A CG1    1 
ATOM   2394 C  CG2    . ILE A 1 441  ? 174.705 143.384 215.410 1.00 51.44 ? 441  ILE A CG2    1 
ATOM   2395 C  CD1    . ILE A 1 441  ? 172.165 145.006 215.059 1.00 51.44 ? 441  ILE A CD1    1 
ATOM   2396 N  N      . PHE A 1 442  ? 177.664 145.683 216.329 1.00 51.47 ? 442  PHE A N      1 
ATOM   2397 C  CA     . PHE A 1 442  ? 179.068 145.478 215.992 1.00 51.47 ? 442  PHE A CA     1 
ATOM   2398 C  C      . PHE A 1 442  ? 179.995 146.221 216.948 1.00 51.47 ? 442  PHE A C      1 
ATOM   2399 O  O      . PHE A 1 442  ? 180.959 146.867 216.533 1.00 51.47 ? 442  PHE A O      1 
ATOM   2400 C  CB     . PHE A 1 442  ? 179.340 145.880 214.547 1.00 51.47 ? 442  PHE A CB     1 
ATOM   2401 C  CG     . PHE A 1 442  ? 178.830 144.891 213.550 1.00 51.47 ? 442  PHE A CG     1 
ATOM   2402 C  CD1    . PHE A 1 442  ? 179.588 143.788 213.212 1.00 51.47 ? 442  PHE A CD1    1 
ATOM   2403 C  CD2    . PHE A 1 442  ? 177.586 145.042 212.978 1.00 51.47 ? 442  PHE A CD2    1 
ATOM   2404 C  CE1    . PHE A 1 442  ? 179.122 142.863 212.310 1.00 51.47 ? 442  PHE A CE1    1 
ATOM   2405 C  CE2    . PHE A 1 442  ? 177.119 144.127 212.072 1.00 51.47 ? 442  PHE A CE2    1 
ATOM   2406 C  CZ     . PHE A 1 442  ? 177.888 143.035 211.741 1.00 51.47 ? 442  PHE A CZ     1 
ATOM   2407 N  N      . THR A 1 443  ? 179.686 146.151 218.241 1.00 63.89 ? 443  THR A N      1 
ATOM   2408 C  CA     . THR A 1 443  ? 180.574 146.658 219.276 1.00 63.89 ? 443  THR A CA     1 
ATOM   2409 C  C      . THR A 1 443  ? 181.877 145.860 219.314 1.00 63.89 ? 443  THR A C      1 
ATOM   2410 O  O      . THR A 1 443  ? 181.965 144.731 218.824 1.00 63.89 ? 443  THR A O      1 
ATOM   2411 C  CB     . THR A 1 443  ? 179.895 146.586 220.642 1.00 63.89 ? 443  THR A CB     1 
ATOM   2412 O  OG1    . THR A 1 443  ? 179.608 145.218 220.957 1.00 63.89 ? 443  THR A OG1    1 
ATOM   2413 C  CG2    . THR A 1 443  ? 178.603 147.371 220.632 1.00 63.89 ? 443  THR A CG2    1 
ATOM   2414 N  N      . GLU A 1 444  ? 182.898 146.468 219.925 1.00 71.73 ? 444  GLU A N      1 
ATOM   2415 C  CA     . GLU A 1 444  ? 184.216 145.845 219.984 1.00 71.73 ? 444  GLU A CA     1 
ATOM   2416 C  C      . GLU A 1 444  ? 184.237 144.653 220.934 1.00 71.73 ? 444  GLU A C      1 
ATOM   2417 O  O      . GLU A 1 444  ? 184.978 143.690 220.704 1.00 71.73 ? 444  GLU A O      1 
ATOM   2418 C  CB     . GLU A 1 444  ? 185.258 146.891 220.394 1.00 71.73 ? 444  GLU A CB     1 
ATOM   2419 C  CG     . GLU A 1 444  ? 186.706 146.419 220.371 1.00 71.73 ? 444  GLU A CG     1 
ATOM   2420 C  CD     . GLU A 1 444  ? 187.690 147.529 220.691 1.00 71.73 ? 444  GLU A CD     1 
ATOM   2421 O  OE1    . GLU A 1 444  ? 187.246 148.672 220.926 1.00 71.73 ? 444  GLU A OE1    1 
ATOM   2422 O  OE2    . GLU A 1 444  ? 188.909 147.258 220.712 1.00 71.73 ? 444  GLU A OE2    1 
ATOM   2423 N  N      . GLU A 1 445  ? 183.408 144.679 221.979 1.00 72.94 ? 445  GLU A N      1 
ATOM   2424 C  CA     . GLU A 1 445  ? 183.422 143.614 222.976 1.00 72.94 ? 445  GLU A CA     1 
ATOM   2425 C  C      . GLU A 1 445  ? 182.801 142.318 222.468 1.00 72.94 ? 445  GLU A C      1 
ATOM   2426 O  O      . GLU A 1 445  ? 183.009 141.267 223.083 1.00 72.94 ? 445  GLU A O      1 
ATOM   2427 C  CB     . GLU A 1 445  ? 182.699 144.077 224.241 1.00 72.94 ? 445  GLU A CB     1 
ATOM   2428 C  CG     . GLU A 1 445  ? 181.216 144.335 224.046 1.00 72.94 ? 445  GLU A CG     1 
ATOM   2429 C  CD     . GLU A 1 445  ? 180.550 144.879 225.294 1.00 72.94 ? 445  GLU A CD     1 
ATOM   2430 O  OE1    . GLU A 1 445  ? 181.257 145.092 226.302 1.00 72.94 ? 445  GLU A OE1    1 
ATOM   2431 O  OE2    . GLU A 1 445  ? 179.319 145.091 225.268 1.00 72.94 ? 445  GLU A OE2    1 
ATOM   2432 N  N      . GLN A 1 446  ? 182.056 142.363 221.369 1.00 64.91 ? 446  GLN A N      1 
ATOM   2433 C  CA     . GLN A 1 446  ? 181.408 141.184 220.798 1.00 64.91 ? 446  GLN A CA     1 
ATOM   2434 C  C      . GLN A 1 446  ? 181.997 140.972 219.406 1.00 64.91 ? 446  GLN A C      1 
ATOM   2435 O  O      . GLN A 1 446  ? 181.653 141.689 218.462 1.00 64.91 ? 446  GLN A O      1 
ATOM   2436 C  CB     . GLN A 1 446  ? 179.890 141.365 220.776 1.00 64.91 ? 446  GLN A CB     1 
ATOM   2437 C  CG     . GLN A 1 446  ? 179.071 140.114 220.476 1.00 64.91 ? 446  GLN A CG     1 
ATOM   2438 C  CD     . GLN A 1 446  ? 178.922 139.847 218.996 1.00 64.91 ? 446  GLN A CD     1 
ATOM   2439 O  OE1    . GLN A 1 446  ? 179.189 138.745 218.518 1.00 64.91 ? 446  GLN A OE1    1 
ATOM   2440 N  NE2    . GLN A 1 446  ? 178.497 140.864 218.258 1.00 64.91 ? 446  GLN A NE2    1 
ATOM   2441 N  N      . GLN A 1 447  ? 182.887 139.992 219.285 1.00 62.43 ? 447  GLN A N      1 
ATOM   2442 C  CA     . GLN A 1 447  ? 183.584 139.719 218.039 1.00 62.43 ? 447  GLN A CA     1 
ATOM   2443 C  C      . GLN A 1 447  ? 182.773 138.772 217.160 1.00 62.43 ? 447  GLN A C      1 
ATOM   2444 O  O      . GLN A 1 447  ? 181.897 138.041 217.628 1.00 62.43 ? 447  GLN A O      1 
ATOM   2445 C  CB     . GLN A 1 447  ? 184.966 139.127 218.316 1.00 62.43 ? 447  GLN A CB     1 
ATOM   2446 C  CG     . GLN A 1 447  ? 185.905 140.066 219.063 1.00 62.43 ? 447  GLN A CG     1 
ATOM   2447 C  CD     . GLN A 1 447  ? 186.298 141.278 218.240 1.00 62.43 ? 447  GLN A CD     1 
ATOM   2448 O  OE1    . GLN A 1 447  ? 186.531 141.176 217.036 1.00 62.43 ? 447  GLN A OE1    1 
ATOM   2449 N  NE2    . GLN A 1 447  ? 186.373 142.435 218.888 1.00 62.43 ? 447  GLN A NE2    1 
ATOM   2450 N  N      . TRP A 1 448  ? 183.083 138.791 215.867 1.00 52.40 ? 448  TRP A N      1 
ATOM   2451 C  CA     . TRP A 1 448  ? 182.342 138.041 214.867 1.00 52.40 ? 448  TRP A CA     1 
ATOM   2452 C  C      . TRP A 1 448  ? 183.245 137.044 214.154 1.00 52.40 ? 448  TRP A C      1 
ATOM   2453 O  O      . TRP A 1 448  ? 184.473 137.135 214.202 1.00 52.40 ? 448  TRP A O      1 
ATOM   2454 C  CB     . TRP A 1 448  ? 181.700 138.977 213.846 1.00 52.40 ? 448  TRP A CB     1 
ATOM   2455 C  CG     . TRP A 1 448  ? 180.557 139.739 214.398 1.00 52.40 ? 448  TRP A CG     1 
ATOM   2456 C  CD1    . TRP A 1 448  ? 180.588 140.988 214.934 1.00 52.40 ? 448  TRP A CD1    1 
ATOM   2457 C  CD2    . TRP A 1 448  ? 179.196 139.305 214.467 1.00 52.40 ? 448  TRP A CD2    1 
ATOM   2458 N  NE1    . TRP A 1 448  ? 179.331 141.359 215.339 1.00 52.40 ? 448  TRP A NE1    1 
ATOM   2459 C  CE2    . TRP A 1 448  ? 178.458 140.343 215.061 1.00 52.40 ? 448  TRP A CE2    1 
ATOM   2460 C  CE3    . TRP A 1 448  ? 178.531 138.136 214.090 1.00 52.40 ? 448  TRP A CE3    1 
ATOM   2461 C  CZ2    . TRP A 1 448  ? 177.092 140.252 215.278 1.00 52.40 ? 448  TRP A CZ2    1 
ATOM   2462 C  CZ3    . TRP A 1 448  ? 177.175 138.049 214.304 1.00 52.40 ? 448  TRP A CZ3    1 
ATOM   2463 C  CH2    . TRP A 1 448  ? 176.471 139.098 214.899 1.00 52.40 ? 448  TRP A CH2    1 
ATOM   2464 N  N      . THR A 1 449  ? 182.608 136.089 213.485 1.00 49.38 ? 449  THR A N      1 
ATOM   2465 C  CA     . THR A 1 449  ? 183.290 134.989 212.826 1.00 49.38 ? 449  THR A CA     1 
ATOM   2466 C  C      . THR A 1 449  ? 182.681 134.855 211.431 1.00 49.38 ? 449  THR A C      1 
ATOM   2467 O  O      . THR A 1 449  ? 181.712 135.541 211.096 1.00 49.38 ? 449  THR A O      1 
ATOM   2468 C  CB     . THR A 1 449  ? 183.152 133.698 213.660 1.00 49.38 ? 449  THR A CB     1 
ATOM   2469 O  OG1    . THR A 1 449  ? 183.247 134.029 215.049 1.00 49.38 ? 449  THR A OG1    1 
ATOM   2470 C  CG2    . THR A 1 449  ? 184.312 132.740 213.399 1.00 49.38 ? 449  THR A CG2    1 
ATOM   2471 N  N      . THR A 1 450  ? 183.270 133.997 210.595 1.00 47.14 ? 450  THR A N      1 
ATOM   2472 C  CA     . THR A 1 450  ? 182.730 133.752 209.262 1.00 47.14 ? 450  THR A CA     1 
ATOM   2473 C  C      . THR A 1 450  ? 181.388 133.034 209.323 1.00 47.14 ? 450  THR A C      1 
ATOM   2474 O  O      . THR A 1 450  ? 180.417 133.462 208.689 1.00 47.14 ? 450  THR A O      1 
ATOM   2475 C  CB     . THR A 1 450  ? 183.735 132.949 208.433 1.00 47.14 ? 450  THR A CB     1 
ATOM   2476 O  OG1    . THR A 1 450  ? 184.900 133.747 208.189 1.00 47.14 ? 450  THR A OG1    1 
ATOM   2477 C  CG2    . THR A 1 450  ? 183.130 132.500 207.114 1.00 47.14 ? 450  THR A CG2    1 
ATOM   2478 N  N      . GLU A 1 451  ? 181.312 131.942 210.089 1.00 48.91 ? 451  GLU A N      1 
ATOM   2479 C  CA     . GLU A 1 451  ? 180.084 131.157 210.156 1.00 48.91 ? 451  GLU A CA     1 
ATOM   2480 C  C      . GLU A 1 451  ? 178.969 131.874 210.906 1.00 48.91 ? 451  GLU A C      1 
ATOM   2481 O  O      . GLU A 1 451  ? 177.795 131.562 210.686 1.00 48.91 ? 451  GLU A O      1 
ATOM   2482 C  CB     . GLU A 1 451  ? 180.359 129.796 210.801 1.00 48.91 ? 451  GLU A CB     1 
ATOM   2483 C  CG     . GLU A 1 451  ? 180.739 129.846 212.274 1.00 48.91 ? 451  GLU A CG     1 
ATOM   2484 C  CD     . GLU A 1 451  ? 182.232 129.992 212.498 1.00 48.91 ? 451  GLU A CD     1 
ATOM   2485 O  OE1    . GLU A 1 451  ? 182.962 130.298 211.531 1.00 48.91 ? 451  GLU A OE1    1 
ATOM   2486 O  OE2    . GLU A 1 451  ? 182.678 129.807 213.650 1.00 48.91 ? 451  GLU A OE2    1 
ATOM   2487 N  N      . THR A 1 452  ? 179.300 132.828 211.772 1.00 47.35 ? 452  THR A N      1 
ATOM   2488 C  CA     . THR A 1 452  ? 178.291 133.636 212.437 1.00 47.35 ? 452  THR A CA     1 
ATOM   2489 C  C      . THR A 1 452  ? 177.923 134.880 211.642 1.00 47.35 ? 452  THR A C      1 
ATOM   2490 O  O      . THR A 1 452  ? 177.088 135.666 212.096 1.00 47.35 ? 452  THR A O      1 
ATOM   2491 C  CB     . THR A 1 452  ? 178.764 134.031 213.836 1.00 47.35 ? 452  THR A CB     1 
ATOM   2492 O  OG1    . THR A 1 452  ? 179.964 134.806 213.739 1.00 47.35 ? 452  THR A OG1    1 
ATOM   2493 C  CG2    . THR A 1 452  ? 179.032 132.792 214.666 1.00 47.35 ? 452  THR A CG2    1 
ATOM   2494 N  N      . LEU A 1 453  ? 178.529 135.075 210.472 1.00 43.81 ? 453  LEU A N      1 
ATOM   2495 C  CA     . LEU A 1 453  ? 178.142 136.129 209.550 1.00 43.81 ? 453  LEU A CA     1 
ATOM   2496 C  C      . LEU A 1 453  ? 177.773 135.615 208.169 1.00 43.81 ? 453  LEU A C      1 
ATOM   2497 O  O      . LEU A 1 453  ? 177.490 136.429 207.291 1.00 43.81 ? 453  LEU A O      1 
ATOM   2498 C  CB     . LEU A 1 453  ? 179.266 137.164 209.398 1.00 43.81 ? 453  LEU A CB     1 
ATOM   2499 C  CG     . LEU A 1 453  ? 179.583 138.153 210.514 1.00 43.81 ? 453  LEU A CG     1 
ATOM   2500 C  CD1    . LEU A 1 453  ? 180.852 138.900 210.185 1.00 43.81 ? 453  LEU A CD1    1 
ATOM   2501 C  CD2    . LEU A 1 453  ? 178.448 139.130 210.644 1.00 43.81 ? 453  LEU A CD2    1 
ATOM   2502 N  N      . SER A 1 454  ? 177.748 134.299 207.951 1.00 40.34 ? 454  SER A N      1 
ATOM   2503 C  CA     . SER A 1 454  ? 177.605 133.767 206.598 1.00 40.34 ? 454  SER A CA     1 
ATOM   2504 C  C      . SER A 1 454  ? 176.180 133.907 206.073 1.00 40.34 ? 454  SER A C      1 
ATOM   2505 O  O      . SER A 1 454  ? 175.976 134.332 204.931 1.00 40.34 ? 454  SER A O      1 
ATOM   2506 C  CB     . SER A 1 454  ? 178.043 132.305 206.561 1.00 40.34 ? 454  SER A CB     1 
ATOM   2507 O  OG     . SER A 1 454  ? 177.869 131.761 205.266 1.00 40.34 ? 454  SER A OG     1 
ATOM   2508 N  N      . ALA A 1 455  ? 175.181 133.553 206.886 1.00 37.35 ? 455  ALA A N      1 
ATOM   2509 C  CA     . ALA A 1 455  ? 173.792 133.721 206.470 1.00 37.35 ? 455  ALA A CA     1 
ATOM   2510 C  C      . ALA A 1 455  ? 173.419 135.192 206.361 1.00 37.35 ? 455  ALA A C      1 
ATOM   2511 O  O      . ALA A 1 455  ? 172.651 135.575 205.468 1.00 37.35 ? 455  ALA A O      1 
ATOM   2512 C  CB     . ALA A 1 455  ? 172.861 133.006 207.446 1.00 37.35 ? 455  ALA A CB     1 
ATOM   2513 N  N      . ALA A 1 456  ? 173.985 136.027 207.234 1.00 37.15 ? 456  ALA A N      1 
ATOM   2514 C  CA     . ALA A 1 456  ? 173.780 137.466 207.147 1.00 37.15 ? 456  ALA A CA     1 
ATOM   2515 C  C      . ALA A 1 456  ? 174.412 138.044 205.889 1.00 37.15 ? 456  ALA A C      1 
ATOM   2516 O  O      . ALA A 1 456  ? 173.846 138.944 205.263 1.00 37.15 ? 456  ALA A O      1 
ATOM   2517 C  CB     . ALA A 1 456  ? 174.354 138.144 208.384 1.00 37.15 ? 456  ALA A CB     1 
ATOM   2518 N  N      . MET A 1 457  ? 175.577 137.526 205.499 1.00 37.40 ? 457  MET A N      1 
ATOM   2519 C  CA     . MET A 1 457  ? 176.229 137.961 204.273 1.00 37.40 ? 457  MET A CA     1 
ATOM   2520 C  C      . MET A 1 457  ? 175.446 137.523 203.050 1.00 37.40 ? 457  MET A C      1 
ATOM   2521 O  O      . MET A 1 457  ? 175.363 138.263 202.066 1.00 37.40 ? 457  MET A O      1 
ATOM   2522 C  CB     . MET A 1 457  ? 177.638 137.394 204.211 1.00 37.40 ? 457  MET A CB     1 
ATOM   2523 C  CG     . MET A 1 457  ? 178.465 137.966 203.090 1.00 37.40 ? 457  MET A CG     1 
ATOM   2524 S  SD     . MET A 1 457  ? 178.747 139.710 203.387 1.00 37.40 ? 457  MET A SD     1 
ATOM   2525 C  CE     . MET A 1 457  ? 179.107 140.249 201.739 1.00 37.40 ? 457  MET A CE     1 
ATOM   2526 N  N      . LEU A 1 458  ? 174.883 136.316 203.093 1.00 34.94 ? 458  LEU A N      1 
ATOM   2527 C  CA     . LEU A 1 458  ? 174.028 135.848 202.009 1.00 34.94 ? 458  LEU A CA     1 
ATOM   2528 C  C      . LEU A 1 458  ? 172.785 136.719 201.869 1.00 34.94 ? 458  LEU A C      1 
ATOM   2529 O  O      . LEU A 1 458  ? 172.379 137.058 200.750 1.00 34.94 ? 458  LEU A O      1 
ATOM   2530 C  CB     . LEU A 1 458  ? 173.638 134.396 202.256 1.00 34.94 ? 458  LEU A CB     1 
ATOM   2531 C  CG     . LEU A 1 458  ? 172.774 133.750 201.182 1.00 34.94 ? 458  LEU A CG     1 
ATOM   2532 C  CD1    . LEU A 1 458  ? 173.548 133.592 199.886 1.00 34.94 ? 458  LEU A CD1    1 
ATOM   2533 C  CD2    . LEU A 1 458  ? 172.229 132.428 201.683 1.00 34.94 ? 458  LEU A CD2    1 
ATOM   2534 N  N      . THR A 1 459  ? 172.189 137.113 202.997 1.00 34.56 ? 459  THR A N      1 
ATOM   2535 C  CA     . THR A 1 459  ? 171.035 138.007 202.965 1.00 34.56 ? 459  THR A CA     1 
ATOM   2536 C  C      . THR A 1 459  ? 171.421 139.396 202.461 1.00 34.56 ? 459  THR A C      1 
ATOM   2537 O  O      . THR A 1 459  ? 170.675 140.012 201.693 1.00 34.56 ? 459  THR A O      1 
ATOM   2538 C  CB     . THR A 1 459  ? 170.405 138.078 204.359 1.00 34.56 ? 459  THR A CB     1 
ATOM   2539 O  OG1    . THR A 1 459  ? 170.041 136.758 204.780 1.00 34.56 ? 459  THR A OG1    1 
ATOM   2540 C  CG2    . THR A 1 459  ? 169.160 138.949 204.368 1.00 34.56 ? 459  THR A CG2    1 
ATOM   2541 N  N      . ALA A 1 460  ? 172.600 139.888 202.850 1.00 33.86 ? 460  ALA A N      1 
ATOM   2542 C  CA     . ALA A 1 460  ? 173.041 141.211 202.419 1.00 33.86 ? 460  ALA A CA     1 
ATOM   2543 C  C      . ALA A 1 460  ? 173.409 141.239 200.942 1.00 33.86 ? 460  ALA A C      1 
ATOM   2544 O  O      . ALA A 1 460  ? 173.212 142.261 200.276 1.00 33.86 ? 460  ALA A O      1 
ATOM   2545 C  CB     . ALA A 1 460  ? 174.225 141.671 203.267 1.00 33.86 ? 460  ALA A CB     1 
ATOM   2546 N  N      . LEU A 1 461  ? 173.947 140.139 200.415 1.00 32.53 ? 461  LEU A N      1 
ATOM   2547 C  CA     . LEU A 1 461  ? 174.250 140.074 198.991 1.00 32.53 ? 461  LEU A CA     1 
ATOM   2548 C  C      . LEU A 1 461  ? 172.982 139.932 198.164 1.00 32.53 ? 461  LEU A C      1 
ATOM   2549 O  O      . LEU A 1 461  ? 172.797 140.647 197.174 1.00 32.53 ? 461  LEU A O      1 
ATOM   2550 C  CB     . LEU A 1 461  ? 175.204 138.917 198.702 1.00 32.53 ? 461  LEU A CB     1 
ATOM   2551 C  CG     . LEU A 1 461  ? 176.652 139.070 199.154 1.00 32.53 ? 461  LEU A CG     1 
ATOM   2552 C  CD1    . LEU A 1 461  ? 177.418 137.780 198.937 1.00 32.53 ? 461  LEU A CD1    1 
ATOM   2553 C  CD2    . LEU A 1 461  ? 177.311 140.214 198.422 1.00 32.53 ? 461  LEU A CD2    1 
ATOM   2554 N  N      . LEU A 1 462  ? 172.091 139.017 198.558 1.00 33.88 ? 462  LEU A N      1 
ATOM   2555 C  CA     . LEU A 1 462  ? 170.919 138.736 197.737 1.00 33.88 ? 462  LEU A CA     1 
ATOM   2556 C  C      . LEU A 1 462  ? 169.879 139.848 197.773 1.00 33.88 ? 462  LEU A C      1 
ATOM   2557 O  O      . LEU A 1 462  ? 169.111 139.983 196.816 1.00 33.88 ? 462  LEU A O      1 
ATOM   2558 C  CB     . LEU A 1 462  ? 170.268 137.421 198.165 1.00 33.88 ? 462  LEU A CB     1 
ATOM   2559 C  CG     . LEU A 1 462  ? 171.027 136.130 197.866 1.00 33.88 ? 462  LEU A CG     1 
ATOM   2560 C  CD1    . LEU A 1 462  ? 170.291 134.945 198.460 1.00 33.88 ? 462  LEU A CD1    1 
ATOM   2561 C  CD2    . LEU A 1 462  ? 171.204 135.959 196.374 1.00 33.88 ? 462  LEU A CD2    1 
ATOM   2562 N  N      . ASP A 1 463  ? 169.832 140.650 198.834 1.00 37.50 ? 463  ASP A N      1 
ATOM   2563 C  CA     . ASP A 1 463  ? 168.809 141.679 198.960 1.00 37.50 ? 463  ASP A CA     1 
ATOM   2564 C  C      . ASP A 1 463  ? 169.334 143.077 198.673 1.00 37.50 ? 463  ASP A C      1 
ATOM   2565 O  O      . ASP A 1 463  ? 168.641 144.052 198.984 1.00 37.50 ? 463  ASP A O      1 
ATOM   2566 C  CB     . ASP A 1 463  ? 168.179 141.635 200.353 1.00 37.50 ? 463  ASP A CB     1 
ATOM   2567 C  CG     . ASP A 1 463  ? 167.357 140.383 200.580 1.00 37.50 ? 463  ASP A CG     1 
ATOM   2568 O  OD1    . ASP A 1 463  ? 166.819 139.836 199.595 1.00 37.50 ? 463  ASP A OD1    1 
ATOM   2569 O  OD2    . ASP A 1 463  ? 167.246 139.946 201.743 1.00 37.50 ? 463  ASP A OD2    1 
ATOM   2570 N  N      . ASP A 1 464  ? 170.528 143.184 198.076 1.00 37.44 ? 464  ASP A N      1 
ATOM   2571 C  CA     . ASP A 1 464  ? 171.198 144.444 197.728 1.00 37.44 ? 464  ASP A CA     1 
ATOM   2572 C  C      . ASP A 1 464  ? 171.366 145.336 198.963 1.00 37.44 ? 464  ASP A C      1 
ATOM   2573 O  O      . ASP A 1 464  ? 170.822 146.438 199.064 1.00 37.44 ? 464  ASP A O      1 
ATOM   2574 C  CB     . ASP A 1 464  ? 170.462 145.162 196.585 1.00 37.44 ? 464  ASP A CB     1 
ATOM   2575 C  CG     . ASP A 1 464  ? 171.219 146.370 196.056 1.00 37.44 ? 464  ASP A CG     1 
ATOM   2576 O  OD1    . ASP A 1 464  ? 172.256 146.190 195.387 1.00 37.44 ? 464  ASP A OD1    1 
ATOM   2577 O  OD2    . ASP A 1 464  ? 170.764 147.506 196.307 1.00 37.44 ? 464  ASP A OD2    1 
ATOM   2578 N  N      . LYS A 1 465  ? 172.109 144.813 199.932 1.00 38.04 ? 465  LYS A N      1 
ATOM   2579 C  CA     . LYS A 1 465  ? 172.448 145.547 201.147 1.00 38.04 ? 465  LYS A CA     1 
ATOM   2580 C  C      . LYS A 1 465  ? 173.956 145.729 201.116 1.00 38.04 ? 465  LYS A C      1 
ATOM   2581 O  O      . LYS A 1 465  ? 174.705 144.958 201.715 1.00 38.04 ? 465  LYS A O      1 
ATOM   2582 C  CB     . LYS A 1 465  ? 171.985 144.803 202.388 1.00 38.04 ? 465  LYS A CB     1 
ATOM   2583 C  CG     . LYS A 1 465  ? 170.503 144.487 202.398 1.00 38.04 ? 465  LYS A CG     1 
ATOM   2584 C  CD     . LYS A 1 465  ? 169.672 145.740 202.538 1.00 38.04 ? 465  LYS A CD     1 
ATOM   2585 C  CE     . LYS A 1 465  ? 168.192 145.417 202.493 1.00 38.04 ? 465  LYS A CE     1 
ATOM   2586 N  NZ     . LYS A 1 465  ? 167.771 144.620 203.670 1.00 38.04 ? 465  LYS A NZ     1 
ATOM   2587 N  N      . ALA A 1 466  ? 174.398 146.770 200.414 1.00 36.96 ? 466  ALA A N      1 
ATOM   2588 C  CA     . ALA A 1 466  ? 175.817 146.933 200.136 1.00 36.96 ? 466  ALA A CA     1 
ATOM   2589 C  C      . ALA A 1 466  ? 176.577 147.504 201.321 1.00 36.96 ? 466  ALA A C      1 
ATOM   2590 O  O      . ALA A 1 466  ? 177.751 147.176 201.510 1.00 36.96 ? 466  ALA A O      1 
ATOM   2591 C  CB     . ALA A 1 466  ? 176.009 147.828 198.918 1.00 36.96 ? 466  ALA A CB     1 
ATOM   2592 N  N      . GLU A 1 467  ? 175.936 148.354 202.122 1.00 39.71 ? 467  GLU A N      1 
ATOM   2593 C  CA     . GLU A 1 467  ? 176.590 148.856 203.322 1.00 39.71 ? 467  GLU A CA     1 
ATOM   2594 C  C      . GLU A 1 467  ? 176.678 147.782 204.399 1.00 39.71 ? 467  GLU A C      1 
ATOM   2595 O  O      . GLU A 1 467  ? 177.673 147.724 205.131 1.00 39.71 ? 467  GLU A O      1 
ATOM   2596 C  CB     . GLU A 1 467  ? 175.873 150.116 203.821 1.00 39.71 ? 467  GLU A CB     1 
ATOM   2597 C  CG     . GLU A 1 467  ? 174.406 149.944 204.197 1.00 39.71 ? 467  GLU A CG     1 
ATOM   2598 C  CD     . GLU A 1 467  ? 173.459 150.139 203.024 1.00 39.71 ? 467  GLU A CD     1 
ATOM   2599 O  OE1    . GLU A 1 467  ? 173.916 150.110 201.861 1.00 39.71 ? 467  GLU A OE1    1 
ATOM   2600 O  OE2    . GLU A 1 467  ? 172.250 150.326 203.268 1.00 39.71 ? 467  GLU A OE2    1 
ATOM   2601 N  N      . PHE A 1 468  ? 175.690 146.886 204.472 1.00 39.95 ? 468  PHE A N      1 
ATOM   2602 C  CA     . PHE A 1 468  ? 175.810 145.735 205.360 1.00 39.95 ? 468  PHE A CA     1 
ATOM   2603 C  C      . PHE A 1 468  ? 176.863 144.762 204.862 1.00 39.95 ? 468  PHE A C      1 
ATOM   2604 O  O      . PHE A 1 468  ? 177.589 144.175 205.665 1.00 39.95 ? 468  PHE A O      1 
ATOM   2605 C  CB     . PHE A 1 468  ? 174.467 145.031 205.503 1.00 39.95 ? 468  PHE A CB     1 
ATOM   2606 C  CG     . PHE A 1 468  ? 173.486 145.782 206.329 1.00 39.95 ? 468  PHE A CG     1 
ATOM   2607 C  CD1    . PHE A 1 468  ? 173.494 145.668 207.709 1.00 39.95 ? 468  PHE A CD1    1 
ATOM   2608 C  CD2    . PHE A 1 468  ? 172.574 146.629 205.731 1.00 39.95 ? 468  PHE A CD2    1 
ATOM   2609 C  CE1    . PHE A 1 468  ? 172.595 146.374 208.471 1.00 39.95 ? 468  PHE A CE1    1 
ATOM   2610 C  CE2    . PHE A 1 468  ? 171.680 147.335 206.486 1.00 39.95 ? 468  PHE A CE2    1 
ATOM   2611 C  CZ     . PHE A 1 468  ? 171.689 147.206 207.855 1.00 39.95 ? 468  PHE A CZ     1 
ATOM   2612 N  N      . ALA A 1 469  ? 176.965 144.594 203.542 1.00 38.92 ? 469  ALA A N      1 
ATOM   2613 C  CA     . ALA A 1 469  ? 178.012 143.760 202.957 1.00 38.92 ? 469  ALA A CA     1 
ATOM   2614 C  C      . ALA A 1 469  ? 179.399 144.312 203.263 1.00 38.92 ? 469  ALA A C      1 
ATOM   2615 O  O      . ALA A 1 469  ? 180.306 143.560 203.641 1.00 38.92 ? 469  ALA A O      1 
ATOM   2616 C  CB     . ALA A 1 469  ? 177.796 143.654 201.448 1.00 38.92 ? 469  ALA A CB     1 
ATOM   2617 N  N      . GLU A 1 470  ? 179.566 145.631 203.128 1.00 39.26 ? 470  GLU A N      1 
ATOM   2618 C  CA     . GLU A 1 470  ? 180.825 146.290 203.459 1.00 39.26 ? 470  GLU A CA     1 
ATOM   2619 C  C      . GLU A 1 470  ? 181.149 146.157 204.939 1.00 39.26 ? 470  GLU A C      1 
ATOM   2620 O  O      . GLU A 1 470  ? 182.301 145.897 205.305 1.00 39.26 ? 470  GLU A O      1 
ATOM   2621 C  CB     . GLU A 1 470  ? 180.751 147.761 203.062 1.00 39.26 ? 470  GLU A CB     1 
ATOM   2622 C  CG     . GLU A 1 470  ? 182.021 148.542 203.291 1.00 39.26 ? 470  GLU A CG     1 
ATOM   2623 C  CD     . GLU A 1 470  ? 181.894 149.978 202.837 1.00 39.26 ? 470  GLU A CD     1 
ATOM   2624 O  OE1    . GLU A 1 470  ? 180.801 150.351 202.363 1.00 39.26 ? 470  GLU A OE1    1 
ATOM   2625 O  OE2    . GLU A 1 470  ? 182.883 150.732 202.953 1.00 39.26 ? 470  GLU A OE2    1 
ATOM   2626 N  N      . LEU A 1 471  ? 180.136 146.301 205.800 1.00 42.79 ? 471  LEU A N      1 
ATOM   2627 C  CA     . LEU A 1 471  ? 180.335 146.178 207.239 1.00 42.79 ? 471  LEU A CA     1 
ATOM   2628 C  C      . LEU A 1 471  ? 180.726 144.758 207.631 1.00 42.79 ? 471  LEU A C      1 
ATOM   2629 O  O      . LEU A 1 471  ? 181.595 144.562 208.491 1.00 42.79 ? 471  LEU A O      1 
ATOM   2630 C  CB     . LEU A 1 471  ? 179.060 146.604 207.960 1.00 42.79 ? 471  LEU A CB     1 
ATOM   2631 C  CG     . LEU A 1 471  ? 179.114 146.761 209.471 1.00 42.79 ? 471  LEU A CG     1 
ATOM   2632 C  CD1    . LEU A 1 471  ? 180.062 147.894 209.818 1.00 42.79 ? 471  LEU A CD1    1 
ATOM   2633 C  CD2    . LEU A 1 471  ? 177.731 147.045 209.992 1.00 42.79 ? 471  LEU A CD2    1 
ATOM   2634 N  N      . PHE A 1 472  ? 180.107 143.759 206.994 1.00 41.03 ? 472  PHE A N      1 
ATOM   2635 C  CA     . PHE A 1 472  ? 180.440 142.366 207.276 1.00 41.03 ? 472  PHE A CA     1 
ATOM   2636 C  C      . PHE A 1 472  ? 181.854 142.048 206.822 1.00 41.03 ? 472  PHE A C      1 
ATOM   2637 O  O      . PHE A 1 472  ? 182.605 141.387 207.547 1.00 41.03 ? 472  PHE A O      1 
ATOM   2638 C  CB     . PHE A 1 472  ? 179.456 141.420 206.581 1.00 41.03 ? 472  PHE A CB     1 
ATOM   2639 C  CG     . PHE A 1 472  ? 178.038 141.513 207.078 1.00 41.03 ? 472  PHE A CG     1 
ATOM   2640 C  CD1    . PHE A 1 472  ? 177.731 142.077 208.306 1.00 41.03 ? 472  PHE A CD1    1 
ATOM   2641 C  CD2    . PHE A 1 472  ? 177.001 141.068 206.279 1.00 41.03 ? 472  PHE A CD2    1 
ATOM   2642 C  CE1    . PHE A 1 472  ? 176.423 142.172 208.725 1.00 41.03 ? 472  PHE A CE1    1 
ATOM   2643 C  CE2    . PHE A 1 472  ? 175.696 141.163 206.696 1.00 41.03 ? 472  PHE A CE2    1 
ATOM   2644 C  CZ     . PHE A 1 472  ? 175.407 141.711 207.922 1.00 41.03 ? 472  PHE A CZ     1 
ATOM   2645 N  N      . LEU A 1 473  ? 182.237 142.526 205.632 1.00 39.94 ? 473  LEU A N      1 
ATOM   2646 C  CA     . LEU A 1 473  ? 183.596 142.317 205.142 1.00 39.94 ? 473  LEU A CA     1 
ATOM   2647 C  C      . LEU A 1 473  ? 184.633 143.027 206.001 1.00 39.94 ? 473  LEU A C      1 
ATOM   2648 O  O      . LEU A 1 473  ? 185.752 142.526 206.147 1.00 39.94 ? 473  LEU A O      1 
ATOM   2649 C  CB     . LEU A 1 473  ? 183.721 142.790 203.694 1.00 39.94 ? 473  LEU A CB     1 
ATOM   2650 C  CG     . LEU A 1 473  ? 183.014 141.991 202.604 1.00 39.94 ? 473  LEU A CG     1 
ATOM   2651 C  CD1    . LEU A 1 473  ? 183.104 142.719 201.281 1.00 39.94 ? 473  LEU A CD1    1 
ATOM   2652 C  CD2    . LEU A 1 473  ? 183.623 140.616 202.492 1.00 39.94 ? 473  LEU A CD2    1 
ATOM   2653 N  N      . GLN A 1 474  ? 184.291 144.174 206.584 1.00 42.77 ? 474  GLN A N      1 
ATOM   2654 C  CA     . GLN A 1 474  ? 185.296 144.918 207.326 1.00 42.77 ? 474  GLN A CA     1 
ATOM   2655 C  C      . GLN A 1 474  ? 185.302 144.620 208.818 1.00 42.77 ? 474  GLN A C      1 
ATOM   2656 O  O      . GLN A 1 474  ? 186.201 145.099 209.515 1.00 42.77 ? 474  GLN A O      1 
ATOM   2657 C  CB     . GLN A 1 474  ? 185.122 146.425 207.114 1.00 42.77 ? 474  GLN A CB     1 
ATOM   2658 C  CG     . GLN A 1 474  ? 183.961 147.049 207.845 1.00 42.77 ? 474  GLN A CG     1 
ATOM   2659 C  CD     . GLN A 1 474  ? 183.756 148.494 207.451 1.00 42.77 ? 474  GLN A CD     1 
ATOM   2660 O  OE1    . GLN A 1 474  ? 184.486 149.028 206.618 1.00 42.77 ? 474  GLN A OE1    1 
ATOM   2661 N  NE2    . GLN A 1 474  ? 182.765 149.139 208.053 1.00 42.77 ? 474  GLN A NE2    1 
ATOM   2662 N  N      . ASN A 1 475  ? 184.345 143.850 209.340 1.00 45.23 ? 475  ASN A N      1 
ATOM   2663 C  CA     . ASN A 1 475  ? 184.418 143.459 210.755 1.00 45.23 ? 475  ASN A CA     1 
ATOM   2664 C  C      . ASN A 1 475  ? 185.115 142.118 210.972 1.00 45.23 ? 475  ASN A C      1 
ATOM   2665 O  O      . ASN A 1 475  ? 186.173 142.061 211.604 1.00 45.23 ? 475  ASN A O      1 
ATOM   2666 C  CB     . ASN A 1 475  ? 183.026 143.452 211.387 1.00 45.23 ? 475  ASN A CB     1 
ATOM   2667 C  CG     . ASN A 1 475  ? 182.571 144.831 211.786 1.00 45.23 ? 475  ASN A CG     1 
ATOM   2668 O  OD1    . ASN A 1 475  ? 181.627 145.374 211.229 1.00 45.23 ? 475  ASN A OD1    1 
ATOM   2669 N  ND2    . ASN A 1 475  ? 183.237 145.404 212.778 1.00 45.23 ? 475  ASN A ND2    1 
ATOM   2670 N  N      . GLY A 1 476  ? 184.544 141.037 210.454 1.00 45.25 ? 476  GLY A N      1 
ATOM   2671 C  CA     . GLY A 1 476  ? 185.079 139.738 210.813 1.00 45.25 ? 476  GLY A CA     1 
ATOM   2672 C  C      . GLY A 1 476  ? 184.991 138.648 209.769 1.00 45.25 ? 476  GLY A C      1 
ATOM   2673 O  O      . GLY A 1 476  ? 185.269 137.484 210.065 1.00 45.25 ? 476  GLY A O      1 
ATOM   2674 N  N      . LEU A 1 477  ? 184.610 138.999 208.549 1.00 42.67 ? 477  LEU A N      1 
ATOM   2675 C  CA     . LEU A 1 477  ? 184.281 138.019 207.527 1.00 42.67 ? 477  LEU A CA     1 
ATOM   2676 C  C      . LEU A 1 477  ? 185.239 138.115 206.350 1.00 42.67 ? 477  LEU A C      1 
ATOM   2677 O  O      . LEU A 1 477  ? 185.686 139.206 205.985 1.00 42.67 ? 477  LEU A O      1 
ATOM   2678 C  CB     . LEU A 1 477  ? 182.849 138.222 207.055 1.00 42.67 ? 477  LEU A CB     1 
ATOM   2679 C  CG     . LEU A 1 477  ? 182.190 137.398 205.967 1.00 42.67 ? 477  LEU A CG     1 
ATOM   2680 C  CD1    . LEU A 1 477  ? 182.108 135.963 206.347 1.00 42.67 ? 477  LEU A CD1    1 
ATOM   2681 C  CD2    . LEU A 1 477  ? 180.835 137.959 205.859 1.00 42.67 ? 477  LEU A CD2    1 
ATOM   2682 N  N      . SER A 1 478  ? 185.547 136.965 205.763 1.00 41.60 ? 478  SER A N      1 
ATOM   2683 C  CA     . SER A 1 478  ? 186.398 136.873 204.589 1.00 41.60 ? 478  SER A CA     1 
ATOM   2684 C  C      . SER A 1 478  ? 185.662 136.123 203.492 1.00 41.60 ? 478  SER A C      1 
ATOM   2685 O  O      . SER A 1 478  ? 185.017 135.105 203.756 1.00 41.60 ? 478  SER A O      1 
ATOM   2686 C  CB     . SER A 1 478  ? 187.711 136.165 204.920 1.00 41.60 ? 478  SER A CB     1 
ATOM   2687 O  OG     . SER A 1 478  ? 187.476 134.824 205.302 1.00 41.60 ? 478  SER A OG     1 
ATOM   2688 N  N      . MET A 1 479  ? 185.762 136.636 202.262 1.00 37.87 ? 479  MET A N      1 
ATOM   2689 C  CA     . MET A 1 479  ? 185.160 135.970 201.110 1.00 37.87 ? 479  MET A CA     1 
ATOM   2690 C  C      . MET A 1 479  ? 185.802 134.623 200.822 1.00 37.87 ? 479  MET A C      1 
ATOM   2691 O  O      . MET A 1 479  ? 185.162 133.753 200.221 1.00 37.87 ? 479  MET A O      1 
ATOM   2692 C  CB     . MET A 1 479  ? 185.266 136.853 199.870 1.00 37.87 ? 479  MET A CB     1 
ATOM   2693 C  CG     . MET A 1 479  ? 184.273 137.976 199.781 1.00 37.87 ? 479  MET A CG     1 
ATOM   2694 S  SD     . MET A 1 479  ? 182.615 137.350 199.489 1.00 37.87 ? 479  MET A SD     1 
ATOM   2695 C  CE     . MET A 1 479  ? 181.702 138.878 199.550 1.00 37.87 ? 479  MET A CE     1 
ATOM   2696 N  N      . ARG A 1 480  ? 187.066 134.443 201.210 1.00 41.58 ? 480  ARG A N      1 
ATOM   2697 C  CA     . ARG A 1 480  ? 187.744 133.173 200.984 1.00 41.58 ? 480  ARG A CA     1 
ATOM   2698 C  C      . ARG A 1 480  ? 187.128 132.064 201.825 1.00 41.58 ? 480  ARG A C      1 
ATOM   2699 O  O      . ARG A 1 480  ? 187.010 130.921 201.368 1.00 41.58 ? 480  ARG A O      1 
ATOM   2700 C  CB     . ARG A 1 480  ? 189.234 133.324 201.285 1.00 41.58 ? 480  ARG A CB     1 
ATOM   2701 C  CG     . ARG A 1 480  ? 190.070 132.098 200.974 1.00 41.58 ? 480  ARG A CG     1 
ATOM   2702 C  CD     . ARG A 1 480  ? 191.537 132.351 201.267 1.00 41.58 ? 480  ARG A CD     1 
ATOM   2703 N  NE     . ARG A 1 480  ? 192.365 131.196 200.935 1.00 41.58 ? 480  ARG A NE     1 
ATOM   2704 C  CZ     . ARG A 1 480  ? 192.639 130.206 201.778 1.00 41.58 ? 480  ARG A CZ     1 
ATOM   2705 N  NH1    . ARG A 1 480  ? 192.148 130.226 203.009 1.00 41.58 ? 480  ARG A NH1    1 
ATOM   2706 N  NH2    . ARG A 1 480  ? 193.403 129.194 201.389 1.00 41.58 ? 480  ARG A NH2    1 
ATOM   2707 N  N      . GLU A 1 481  ? 186.704 132.386 203.044 1.00 42.26 ? 481  GLU A N      1 
ATOM   2708 C  CA     . GLU A 1 481  ? 186.028 131.407 203.883 1.00 42.26 ? 481  GLU A CA     1 
ATOM   2709 C  C      . GLU A 1 481  ? 184.527 131.374 203.630 1.00 42.26 ? 481  GLU A C      1 
ATOM   2710 O  O      . GLU A 1 481  ? 183.915 130.303 203.698 1.00 42.26 ? 481  GLU A O      1 
ATOM   2711 C  CB     . GLU A 1 481  ? 186.300 131.699 205.359 1.00 42.26 ? 481  GLU A CB     1 
ATOM   2712 C  CG     . GLU A 1 481  ? 187.750 131.537 205.780 1.00 42.26 ? 481  GLU A CG     1 
ATOM   2713 C  CD     . GLU A 1 481  ? 188.220 130.095 205.750 1.00 42.26 ? 481  GLU A CD     1 
ATOM   2714 O  OE1    . GLU A 1 481  ? 187.397 129.191 206.008 1.00 42.26 ? 481  GLU A OE1    1 
ATOM   2715 O  OE2    . GLU A 1 481  ? 189.416 129.867 205.469 1.00 42.26 ? 481  GLU A OE2    1 
ATOM   2716 N  N      . PHE A 1 482  ? 183.922 132.528 203.342 1.00 37.65 ? 482  PHE A N      1 
ATOM   2717 C  CA     . PHE A 1 482  ? 182.484 132.588 203.099 1.00 37.65 ? 482  PHE A CA     1 
ATOM   2718 C  C      . PHE A 1 482  ? 182.102 131.917 201.788 1.00 37.65 ? 482  PHE A C      1 
ATOM   2719 O  O      . PHE A 1 482  ? 181.348 130.939 201.775 1.00 37.65 ? 482  PHE A O      1 
ATOM   2720 C  CB     . PHE A 1 482  ? 182.005 134.040 203.107 1.00 37.65 ? 482  PHE A CB     1 
ATOM   2721 C  CG     . PHE A 1 482  ? 180.628 134.226 202.541 1.00 37.65 ? 482  PHE A CG     1 
ATOM   2722 C  CD1    . PHE A 1 482  ? 179.514 133.770 203.218 1.00 37.65 ? 482  PHE A CD1    1 
ATOM   2723 C  CD2    . PHE A 1 482  ? 180.449 134.877 201.332 1.00 37.65 ? 482  PHE A CD2    1 
ATOM   2724 C  CE1    . PHE A 1 482  ? 178.254 133.942 202.686 1.00 37.65 ? 482  PHE A CE1    1 
ATOM   2725 C  CE2    . PHE A 1 482  ? 179.190 135.052 200.805 1.00 37.65 ? 482  PHE A CE2    1 
ATOM   2726 C  CZ     . PHE A 1 482  ? 178.094 134.589 201.483 1.00 37.65 ? 482  PHE A CZ     1 
ATOM   2727 N  N      . LEU A 1 483  ? 182.608 132.434 200.673 1.00 36.35 ? 483  LEU A N      1 
ATOM   2728 C  CA     . LEU A 1 483  ? 182.076 132.071 199.370 1.00 36.35 ? 483  LEU A CA     1 
ATOM   2729 C  C      . LEU A 1 483  ? 182.559 130.694 198.946 1.00 36.35 ? 483  LEU A C      1 
ATOM   2730 O  O      . LEU A 1 483  ? 183.762 130.425 198.910 1.00 36.35 ? 483  LEU A O      1 
ATOM   2731 C  CB     . LEU A 1 483  ? 182.474 133.108 198.325 1.00 36.35 ? 483  LEU A CB     1 
ATOM   2732 C  CG     . LEU A 1 483  ? 181.842 132.875 196.958 1.00 36.35 ? 483  LEU A CG     1 
ATOM   2733 C  CD1    . LEU A 1 483  ? 180.338 132.990 197.060 1.00 36.35 ? 483  LEU A CD1    1 
ATOM   2734 C  CD2    . LEU A 1 483  ? 182.376 133.866 195.966 1.00 36.35 ? 483  LEU A CD2    1 
ATOM   2735 N  N      . SER A 1 484  ? 181.613 129.825 198.634 1.00 36.36 ? 484  SER A N      1 
ATOM   2736 C  CA     . SER A 1 484  ? 181.867 128.512 198.076 1.00 36.36 ? 484  SER A CA     1 
ATOM   2737 C  C      . SER A 1 484  ? 181.170 128.410 196.725 1.00 36.36 ? 484  SER A C      1 
ATOM   2738 O  O      . SER A 1 484  ? 180.583 129.374 196.233 1.00 36.36 ? 484  SER A O      1 
ATOM   2739 C  CB     . SER A 1 484  ? 181.404 127.419 199.040 1.00 36.36 ? 484  SER A CB     1 
ATOM   2740 O  OG     . SER A 1 484  ? 180.011 127.498 199.257 1.00 36.36 ? 484  SER A OG     1 
ATOM   2741 N  N      . LEU A 1 485  ? 181.262 127.230 196.113 1.00 36.61 ? 485  LEU A N      1 
ATOM   2742 C  CA     . LEU A 1 485  ? 180.673 127.035 194.793 1.00 36.61 ? 485  LEU A CA     1 
ATOM   2743 C  C      . LEU A 1 485  ? 179.153 127.011 194.859 1.00 36.61 ? 485  LEU A C      1 
ATOM   2744 O  O      . LEU A 1 485  ? 178.480 127.611 194.013 1.00 36.61 ? 485  LEU A O      1 
ATOM   2745 C  CB     . LEU A 1 485  ? 181.202 125.744 194.175 1.00 36.61 ? 485  LEU A CB     1 
ATOM   2746 C  CG     . LEU A 1 485  ? 180.626 125.372 192.813 1.00 36.61 ? 485  LEU A CG     1 
ATOM   2747 C  CD1    . LEU A 1 485  ? 180.941 126.444 191.803 1.00 36.61 ? 485  LEU A CD1    1 
ATOM   2748 C  CD2    . LEU A 1 485  ? 181.151 124.026 192.367 1.00 36.61 ? 485  LEU A CD2    1 
ATOM   2749 N  N      . ASP A 1 486  ? 178.596 126.325 195.858 1.00 36.08 ? 486  ASP A N      1 
ATOM   2750 C  CA     . ASP A 1 486  ? 177.147 126.258 195.992 1.00 36.08 ? 486  ASP A CA     1 
ATOM   2751 C  C      . ASP A 1 486  ? 176.550 127.596 196.407 1.00 36.08 ? 486  ASP A C      1 
ATOM   2752 O  O      . ASP A 1 486  ? 175.457 127.946 195.949 1.00 36.08 ? 486  ASP A O      1 
ATOM   2753 C  CB     . ASP A 1 486  ? 176.770 125.148 196.976 1.00 36.08 ? 486  ASP A CB     1 
ATOM   2754 C  CG     . ASP A 1 486  ? 177.494 125.267 198.304 1.00 36.08 ? 486  ASP A CG     1 
ATOM   2755 O  OD1    . ASP A 1 486  ? 178.360 126.152 198.442 1.00 36.08 ? 486  ASP A OD1    1 
ATOM   2756 O  OD2    . ASP A 1 486  ? 177.199 124.467 199.217 1.00 36.08 ? 486  ASP A OD2    1 
ATOM   2757 N  N      . ILE A 1 487  ? 177.265 128.369 197.230 1.00 35.44 ? 487  ILE A N      1 
ATOM   2758 C  CA     . ILE A 1 487  ? 176.812 129.708 197.599 1.00 35.44 ? 487  ILE A CA     1 
ATOM   2759 C  C      . ILE A 1 487  ? 176.828 130.634 196.386 1.00 35.44 ? 487  ILE A C      1 
ATOM   2760 O  O      . ILE A 1 487  ? 175.923 131.450 196.203 1.00 35.44 ? 487  ILE A O      1 
ATOM   2761 C  CB     . ILE A 1 487  ? 177.668 130.246 198.764 1.00 35.44 ? 487  ILE A CB     1 
ATOM   2762 C  CG1    . ILE A 1 487  ? 177.408 129.422 200.023 1.00 35.44 ? 487  ILE A CG1    1 
ATOM   2763 C  CG2    . ILE A 1 487  ? 177.399 131.710 199.055 1.00 35.44 ? 487  ILE A CG2    1 
ATOM   2764 C  CD1    . ILE A 1 487  ? 178.321 129.746 201.170 1.00 35.44 ? 487  ILE A CD1    1 
ATOM   2765 N  N      . LEU A 1 488  ? 177.804 130.465 195.496 1.00 33.39 ? 488  LEU A N      1 
ATOM   2766 C  CA     . LEU A 1 488  ? 177.880 131.298 194.299 1.00 33.39 ? 488  LEU A CA     1 
ATOM   2767 C  C      . LEU A 1 488  ? 176.835 130.903 193.256 1.00 33.39 ? 488  LEU A C      1 
ATOM   2768 O  O      . LEU A 1 488  ? 176.276 131.771 192.573 1.00 33.39 ? 488  LEU A O      1 
ATOM   2769 C  CB     . LEU A 1 488  ? 179.288 131.211 193.718 1.00 33.39 ? 488  LEU A CB     1 
ATOM   2770 C  CG     . LEU A 1 488  ? 179.671 132.071 192.521 1.00 33.39 ? 488  LEU A CG     1 
ATOM   2771 C  CD1    . LEU A 1 488  ? 179.625 133.546 192.860 1.00 33.39 ? 488  LEU A CD1    1 
ATOM   2772 C  CD2    . LEU A 1 488  ? 181.047 131.675 192.082 1.00 33.39 ? 488  LEU A CD2    1 
ATOM   2773 N  N      . CYS A 1 489  ? 176.552 129.605 193.121 1.00 36.04 ? 489  CYS A N      1 
ATOM   2774 C  CA     . CYS A 1 489  ? 175.482 129.170 192.226 1.00 36.04 ? 489  CYS A CA     1 
ATOM   2775 C  C      . CYS A 1 489  ? 174.116 129.582 192.759 1.00 36.04 ? 489  CYS A C      1 
ATOM   2776 O  O      . CYS A 1 489  ? 173.220 129.935 191.985 1.00 36.04 ? 489  CYS A O      1 
ATOM   2777 C  CB     . CYS A 1 489  ? 175.541 127.658 192.026 1.00 36.04 ? 489  CYS A CB     1 
ATOM   2778 S  SG     . CYS A 1 489  ? 176.993 127.072 191.135 1.00 36.04 ? 489  CYS A SG     1 
ATOM   2779 N  N      . LYS A 1 490  ? 173.944 129.552 194.080 1.00 34.90 ? 490  LYS A N      1 
ATOM   2780 C  CA     . LYS A 1 490  ? 172.752 130.101 194.710 1.00 34.90 ? 490  LYS A CA     1 
ATOM   2781 C  C      . LYS A 1 490  ? 172.672 131.610 194.536 1.00 34.90 ? 490  LYS A C      1 
ATOM   2782 O  O      . LYS A 1 490  ? 171.581 132.164 194.382 1.00 34.90 ? 490  LYS A O      1 
ATOM   2783 C  CB     . LYS A 1 490  ? 172.767 129.706 196.184 1.00 34.90 ? 490  LYS A CB     1 
ATOM   2784 C  CG     . LYS A 1 490  ? 171.679 130.264 197.059 1.00 34.90 ? 490  LYS A CG     1 
ATOM   2785 C  CD     . LYS A 1 490  ? 171.726 129.556 198.398 1.00 34.90 ? 490  LYS A CD     1 
ATOM   2786 C  CE     . LYS A 1 490  ? 173.013 129.872 199.140 1.00 34.90 ? 490  LYS A CE     1 
ATOM   2787 N  NZ     . LYS A 1 490  ? 173.042 129.270 200.502 1.00 34.90 ? 490  LYS A NZ     1 
ATOM   2788 N  N      . LEU A 1 491  ? 173.820 132.277 194.519 1.00 31.28 ? 491  LEU A N      1 
ATOM   2789 C  CA     . LEU A 1 491  ? 173.867 133.721 194.351 1.00 31.28 ? 491  LEU A CA     1 
ATOM   2790 C  C      . LEU A 1 491  ? 173.454 134.118 192.940 1.00 31.28 ? 491  LEU A C      1 
ATOM   2791 O  O      . LEU A 1 491  ? 172.800 135.147 192.742 1.00 31.28 ? 491  LEU A O      1 
ATOM   2792 C  CB     . LEU A 1 491  ? 175.282 134.188 194.678 1.00 31.28 ? 491  LEU A CB     1 
ATOM   2793 C  CG     . LEU A 1 491  ? 175.639 135.635 194.938 1.00 31.28 ? 491  LEU A CG     1 
ATOM   2794 C  CD1    . LEU A 1 491  ? 174.971 136.093 196.206 1.00 31.28 ? 491  LEU A CD1    1 
ATOM   2795 C  CD2    . LEU A 1 491  ? 177.136 135.768 195.040 1.00 31.28 ? 491  LEU A CD2    1 
ATOM   2796 N  N      . TYR A 1 492  ? 173.819 133.308 191.949 1.00 32.08 ? 492  TYR A N      1 
ATOM   2797 C  CA     . TYR A 1 492  ? 173.287 133.472 190.600 1.00 32.08 ? 492  TYR A CA     1 
ATOM   2798 C  C      . TYR A 1 492  ? 171.912 132.841 190.414 1.00 32.08 ? 492  TYR A C      1 
ATOM   2799 O  O      . TYR A 1 492  ? 171.315 133.008 189.346 1.00 32.08 ? 492  TYR A O      1 
ATOM   2800 C  CB     . TYR A 1 492  ? 174.246 132.886 189.563 1.00 32.08 ? 492  TYR A CB     1 
ATOM   2801 C  CG     . TYR A 1 492  ? 175.433 133.756 189.227 1.00 32.08 ? 492  TYR A CG     1 
ATOM   2802 C  CD1    . TYR A 1 492  ? 175.324 134.778 188.293 1.00 32.08 ? 492  TYR A CD1    1 
ATOM   2803 C  CD2    . TYR A 1 492  ? 176.662 133.550 189.829 1.00 32.08 ? 492  TYR A CD2    1 
ATOM   2804 C  CE1    . TYR A 1 492  ? 176.407 135.570 187.974 1.00 32.08 ? 492  TYR A CE1    1 
ATOM   2805 C  CE2    . TYR A 1 492  ? 177.749 134.330 189.515 1.00 32.08 ? 492  TYR A CE2    1 
ATOM   2806 C  CZ     . TYR A 1 492  ? 177.616 135.340 188.592 1.00 32.08 ? 492  TYR A CZ     1 
ATOM   2807 O  OH     . TYR A 1 492  ? 178.707 136.109 188.284 1.00 32.08 ? 492  TYR A OH     1 
ATOM   2808 N  N      . ALA A 1 493  ? 171.399 132.116 191.408 1.00 37.31 ? 493  ALA A N      1 
ATOM   2809 C  CA     . ALA A 1 493  ? 170.068 131.533 191.280 1.00 37.31 ? 493  ALA A CA     1 
ATOM   2810 C  C      . ALA A 1 493  ? 168.974 132.537 191.622 1.00 37.31 ? 493  ALA A C      1 
ATOM   2811 O  O      . ALA A 1 493  ? 167.984 132.648 190.891 1.00 37.31 ? 493  ALA A O      1 
ATOM   2812 C  CB     . ALA A 1 493  ? 169.946 130.298 192.168 1.00 37.31 ? 493  ALA A CB     1 
ATOM   2813 N  N      . GLU A 1 494  ? 169.135 133.284 192.711 1.00 41.03 ? 494  GLU A N      1 
ATOM   2814 C  CA     . GLU A 1 494  ? 168.115 134.225 193.170 1.00 41.03 ? 494  GLU A CA     1 
ATOM   2815 C  C      . GLU A 1 494  ? 168.388 135.650 192.711 1.00 41.03 ? 494  GLU A C      1 
ATOM   2816 O  O      . GLU A 1 494  ? 168.215 136.599 193.482 1.00 41.03 ? 494  GLU A O      1 
ATOM   2817 C  CB     . GLU A 1 494  ? 167.947 134.175 194.688 1.00 41.03 ? 494  GLU A CB     1 
ATOM   2818 C  CG     . GLU A 1 494  ? 167.110 133.003 195.189 1.00 41.03 ? 494  GLU A CG     1 
ATOM   2819 C  CD     . GLU A 1 494  ? 167.930 131.813 195.627 1.00 41.03 ? 494  GLU A CD     1 
ATOM   2820 O  OE1    . GLU A 1 494  ? 169.151 131.966 195.777 1.00 41.03 ? 494  GLU A OE1    1 
ATOM   2821 O  OE2    . GLU A 1 494  ? 167.353 130.722 195.811 1.00 41.03 ? 494  GLU A OE2    1 
ATOM   2822 N  N      . VAL A 1 495  ? 168.844 135.822 191.473 1.00 43.28 ? 495  VAL A N      1 
ATOM   2823 C  CA     . VAL A 1 495  ? 168.825 137.120 190.798 1.00 43.28 ? 495  VAL A CA     1 
ATOM   2824 C  C      . VAL A 1 495  ? 167.369 137.577 190.699 1.00 43.28 ? 495  VAL A C      1 
ATOM   2825 O  O      . VAL A 1 495  ? 166.471 136.732 190.578 1.00 43.28 ? 495  VAL A O      1 
ATOM   2826 C  CB     . VAL A 1 495  ? 169.521 137.044 189.426 1.00 43.28 ? 495  VAL A CB     1 
ATOM   2827 C  CG1    . VAL A 1 495  ? 171.004 136.816 189.605 1.00 43.28 ? 495  VAL A CG1    1 
ATOM   2828 C  CG2    . VAL A 1 495  ? 168.942 135.925 188.583 1.00 43.28 ? 495  VAL A CG2    1 
ATOM   2829 N  N      . PRO A 1 496  ? 167.074 138.891 190.800 1.00 47.34 ? 496  PRO A N      1 
ATOM   2830 C  CA     . PRO A 1 496  ? 165.676 139.324 190.967 1.00 47.34 ? 496  PRO A CA     1 
ATOM   2831 C  C      . PRO A 1 496  ? 164.760 139.112 189.767 1.00 47.34 ? 496  PRO A C      1 
ATOM   2832 O  O      . PRO A 1 496  ? 163.670 138.553 189.925 1.00 47.34 ? 496  PRO A O      1 
ATOM   2833 C  CB     . PRO A 1 496  ? 165.814 140.816 191.302 1.00 47.34 ? 496  PRO A CB     1 
ATOM   2834 C  CG     . PRO A 1 496  ? 167.132 141.213 190.765 1.00 47.34 ? 496  PRO A CG     1 
ATOM   2835 C  CD     . PRO A 1 496  ? 168.015 140.021 190.912 1.00 47.34 ? 496  PRO A CD     1 
ATOM   2836 N  N      . GLY A 1 497  ? 165.164 139.540 188.575 1.00 48.56 ? 497  GLY A N      1 
ATOM   2837 C  CA     . GLY A 1 497  ? 164.308 139.367 187.418 1.00 48.56 ? 497  GLY A CA     1 
ATOM   2838 C  C      . GLY A 1 497  ? 164.144 140.618 186.583 1.00 48.56 ? 497  GLY A C      1 
ATOM   2839 O  O      . GLY A 1 497  ? 163.891 140.542 185.378 1.00 48.56 ? 497  GLY A O      1 
ATOM   2840 N  N      . ASN A 1 498  ? 164.283 141.779 187.217 1.00 49.66 ? 498  ASN A N      1 
ATOM   2841 C  CA     . ASN A 1 498  ? 164.286 143.049 186.507 1.00 49.66 ? 498  ASN A CA     1 
ATOM   2842 C  C      . ASN A 1 498  ? 165.643 143.387 185.896 1.00 49.66 ? 498  ASN A C      1 
ATOM   2843 O  O      . ASN A 1 498  ? 165.784 144.451 185.283 1.00 49.66 ? 498  ASN A O      1 
ATOM   2844 C  CB     . ASN A 1 498  ? 163.820 144.169 187.445 1.00 49.66 ? 498  ASN A CB     1 
ATOM   2845 C  CG     . ASN A 1 498  ? 164.616 144.231 188.741 1.00 49.66 ? 498  ASN A CG     1 
ATOM   2846 O  OD1    . ASN A 1 498  ? 165.570 143.484 188.942 1.00 49.66 ? 498  ASN A OD1    1 
ATOM   2847 N  ND2    . ASN A 1 498  ? 164.215 145.129 189.631 1.00 49.66 ? 498  ASN A ND2    1 
ATOM   2848 N  N      . THR A 1 499  ? 166.630 142.511 186.047 1.00 44.51 ? 499  THR A N      1 
ATOM   2849 C  CA     . THR A 1 499  ? 167.961 142.702 185.500 1.00 44.51 ? 499  THR A CA     1 
ATOM   2850 C  C      . THR A 1 499  ? 168.065 142.062 184.118 1.00 44.51 ? 499  THR A C      1 
ATOM   2851 O  O      . THR A 1 499  ? 167.165 141.359 183.664 1.00 44.51 ? 499  THR A O      1 
ATOM   2852 C  CB     . THR A 1 499  ? 169.006 142.111 186.444 1.00 44.51 ? 499  THR A CB     1 
ATOM   2853 O  OG1    . THR A 1 499  ? 168.782 140.704 186.577 1.00 44.51 ? 499  THR A OG1    1 
ATOM   2854 C  CG2    . THR A 1 499  ? 168.896 142.748 187.813 1.00 44.51 ? 499  THR A CG2    1 
ATOM   2855 N  N      . THR A 1 500  ? 169.184 142.332 183.444 1.00 40.53 ? 500  THR A N      1 
ATOM   2856 C  CA     . THR A 1 500  ? 169.482 141.737 182.143 1.00 40.53 ? 500  THR A CA     1 
ATOM   2857 C  C      . THR A 1 500  ? 170.010 140.313 182.299 1.00 40.53 ? 500  THR A C      1 
ATOM   2858 O  O      . THR A 1 500  ? 169.812 139.458 181.416 1.00 40.53 ? 500  THR A O      1 
ATOM   2859 C  CB     . THR A 1 500  ? 170.495 142.637 181.419 1.00 40.53 ? 500  THR A CB     1 
ATOM   2860 O  OG1    . THR A 1 500  ? 169.975 143.969 181.344 1.00 40.53 ? 500  THR A OG1    1 
ATOM   2861 C  CG2    . THR A 1 500  ? 170.808 142.163 180.002 1.00 40.53 ? 500  THR A CG2    1 
ATOM   2862 N  N      . ILE A 1 501  ? 170.625 140.033 183.449 1.00 38.32 ? 501  ILE A N      1 
ATOM   2863 C  CA     . ILE A 1 501  ? 171.344 138.782 183.629 1.00 38.32 ? 501  ILE A CA     1 
ATOM   2864 C  C      . ILE A 1 501  ? 170.384 137.605 183.778 1.00 38.32 ? 501  ILE A C      1 
ATOM   2865 O  O      . ILE A 1 501  ? 170.730 136.483 183.404 1.00 38.32 ? 501  ILE A O      1 
ATOM   2866 C  CB     . ILE A 1 501  ? 172.330 138.909 184.813 1.00 38.32 ? 501  ILE A CB     1 
ATOM   2867 C  CG1    . ILE A 1 501  ? 173.344 137.767 184.808 1.00 38.32 ? 501  ILE A CG1    1 
ATOM   2868 C  CG2    . ILE A 1 501  ? 171.612 138.995 186.152 1.00 38.32 ? 501  ILE A CG2    1 
ATOM   2869 C  CD1    . ILE A 1 501  ? 174.218 137.754 183.582 1.00 38.32 ? 501  ILE A CD1    1 
ATOM   2870 N  N      . LYS A 1 502  ? 169.151 137.832 184.246 1.00 42.57 ? 502  LYS A N      1 
ATOM   2871 C  CA     . LYS A 1 502  ? 168.233 136.695 184.305 1.00 42.57 ? 502  LYS A CA     1 
ATOM   2872 C  C      . LYS A 1 502  ? 167.728 136.276 182.917 1.00 42.57 ? 502  LYS A C      1 
ATOM   2873 O  O      . LYS A 1 502  ? 167.728 135.068 182.652 1.00 42.57 ? 502  LYS A O      1 
ATOM   2874 C  CB     . LYS A 1 502  ? 167.062 136.938 185.272 1.00 42.57 ? 502  LYS A CB     1 
ATOM   2875 C  CG     . LYS A 1 502  ? 166.117 135.736 185.343 1.00 42.57 ? 502  LYS A CG     1 
ATOM   2876 C  CD     . LYS A 1 502  ? 164.925 135.926 186.247 1.00 42.57 ? 502  LYS A CD     1 
ATOM   2877 C  CE     . LYS A 1 502  ? 165.327 135.814 187.692 1.00 42.57 ? 502  LYS A CE     1 
ATOM   2878 N  NZ     . LYS A 1 502  ? 165.799 134.446 188.035 1.00 42.57 ? 502  LYS A NZ     1 
ATOM   2879 N  N      . PRO A 1 503  ? 167.313 137.176 181.999 1.00 41.02 ? 503  PRO A N      1 
ATOM   2880 C  CA     . PRO A 1 503  ? 167.075 136.709 180.622 1.00 41.02 ? 503  PRO A CA     1 
ATOM   2881 C  C      . PRO A 1 503  ? 168.300 136.148 179.924 1.00 41.02 ? 503  PRO A C      1 
ATOM   2882 O  O      . PRO A 1 503  ? 168.147 135.212 179.133 1.00 41.02 ? 503  PRO A O      1 
ATOM   2883 C  CB     . PRO A 1 503  ? 166.558 137.963 179.909 1.00 41.02 ? 503  PRO A CB     1 
ATOM   2884 C  CG     . PRO A 1 503  ? 165.934 138.736 180.946 1.00 41.02 ? 503  PRO A CG     1 
ATOM   2885 C  CD     . PRO A 1 503  ? 166.779 138.546 182.146 1.00 41.02 ? 503  PRO A CD     1 
ATOM   2886 N  N      . LEU A 1 504  ? 169.509 136.645 180.221 1.00 40.74 ? 504  LEU A N      1 
ATOM   2887 C  CA     . LEU A 1 504  ? 170.704 136.059 179.608 1.00 40.74 ? 504  LEU A CA     1 
ATOM   2888 C  C      . LEU A 1 504  ? 170.953 134.631 180.098 1.00 40.74 ? 504  LEU A C      1 
ATOM   2889 O  O      . LEU A 1 504  ? 171.171 133.714 179.292 1.00 40.74 ? 504  LEU A O      1 
ATOM   2890 C  CB     . LEU A 1 504  ? 171.917 136.943 179.880 1.00 40.74 ? 504  LEU A CB     1 
ATOM   2891 C  CG     . LEU A 1 504  ? 171.895 138.289 179.164 1.00 40.74 ? 504  LEU A CG     1 
ATOM   2892 C  CD1    . LEU A 1 504  ? 173.064 139.143 179.610 1.00 40.74 ? 504  LEU A CD1    1 
ATOM   2893 C  CD2    . LEU A 1 504  ? 171.906 138.090 177.668 1.00 40.74 ? 504  LEU A CD2    1 
ATOM   2894 N  N      . LEU A 1 505  ? 170.889 134.418 181.416 1.00 42.16 ? 505  LEU A N      1 
ATOM   2895 C  CA     . LEU A 1 505  ? 171.075 133.083 181.977 1.00 42.16 ? 505  LEU A CA     1 
ATOM   2896 C  C      . LEU A 1 505  ? 169.950 132.137 181.574 1.00 42.16 ? 505  LEU A C      1 
ATOM   2897 O  O      . LEU A 1 505  ? 170.201 130.963 181.293 1.00 42.16 ? 505  LEU A O      1 
ATOM   2898 C  CB     . LEU A 1 505  ? 171.181 133.159 183.501 1.00 42.16 ? 505  LEU A CB     1 
ATOM   2899 C  CG     . LEU A 1 505  ? 172.430 133.792 184.113 1.00 42.16 ? 505  LEU A CG     1 
ATOM   2900 C  CD1    . LEU A 1 505  ? 172.267 133.939 185.611 1.00 42.16 ? 505  LEU A CD1    1 
ATOM   2901 C  CD2    . LEU A 1 505  ? 173.657 132.973 183.797 1.00 42.16 ? 505  LEU A CD2    1 
ATOM   2902 N  N      . GLN A 1 506  ? 168.708 132.625 181.506 1.00 45.82 ? 506  GLN A N      1 
ATOM   2903 C  CA     . GLN A 1 506  ? 167.605 131.752 181.118 1.00 45.82 ? 506  GLN A CA     1 
ATOM   2904 C  C      . GLN A 1 506  ? 167.626 131.429 179.630 1.00 45.82 ? 506  GLN A C      1 
ATOM   2905 O  O      . GLN A 1 506  ? 167.224 130.329 179.238 1.00 45.82 ? 506  GLN A O      1 
ATOM   2906 C  CB     . GLN A 1 506  ? 166.271 132.379 181.519 1.00 45.82 ? 506  GLN A CB     1 
ATOM   2907 C  CG     . GLN A 1 506  ? 166.000 132.309 183.013 1.00 45.82 ? 506  GLN A CG     1 
ATOM   2908 C  CD     . GLN A 1 506  ? 164.719 133.013 183.411 1.00 45.82 ? 506  GLN A CD     1 
ATOM   2909 O  OE1    . GLN A 1 506  ? 164.069 133.659 182.589 1.00 45.82 ? 506  GLN A OE1    1 
ATOM   2910 N  NE2    . GLN A 1 506  ? 164.344 132.885 184.678 1.00 45.82 ? 506  GLN A NE2    1 
ATOM   2911 N  N      . LYS A 1 507  ? 168.117 132.343 178.789 1.00 48.35 ? 507  LYS A N      1 
ATOM   2912 C  CA     . LYS A 1 507  ? 168.325 132.003 177.388 1.00 48.35 ? 507  LYS A CA     1 
ATOM   2913 C  C      . LYS A 1 507  ? 169.449 130.989 177.227 1.00 48.35 ? 507  LYS A C      1 
ATOM   2914 O  O      . LYS A 1 507  ? 169.377 130.116 176.352 1.00 48.35 ? 507  LYS A O      1 
ATOM   2915 C  CB     . LYS A 1 507  ? 168.619 133.269 176.583 1.00 48.35 ? 507  LYS A CB     1 
ATOM   2916 C  CG     . LYS A 1 507  ? 168.721 133.056 175.083 1.00 48.35 ? 507  LYS A CG     1 
ATOM   2917 C  CD     . LYS A 1 507  ? 168.976 134.360 174.354 1.00 48.35 ? 507  LYS A CD     1 
ATOM   2918 C  CE     . LYS A 1 507  ? 168.985 134.154 172.850 1.00 48.35 ? 507  LYS A CE     1 
ATOM   2919 N  NZ     . LYS A 1 507  ? 170.139 133.320 172.413 1.00 48.35 ? 507  LYS A NZ     1 
ATOM   2920 N  N      . GLU A 1 508  ? 170.473 131.055 178.083 1.00 49.31 ? 508  GLU A N      1 
ATOM   2921 C  CA     . GLU A 1 508  ? 171.521 130.040 178.023 1.00 49.31 ? 508  GLU A CA     1 
ATOM   2922 C  C      . GLU A 1 508  ? 171.025 128.685 178.532 1.00 49.31 ? 508  GLU A C      1 
ATOM   2923 O  O      . GLU A 1 508  ? 171.412 127.640 177.996 1.00 49.31 ? 508  GLU A O      1 
ATOM   2924 C  CB     . GLU A 1 508  ? 172.757 130.508 178.794 1.00 49.31 ? 508  GLU A CB     1 
ATOM   2925 C  CG     . GLU A 1 508  ? 173.916 129.531 178.722 1.00 49.31 ? 508  GLU A CG     1 
ATOM   2926 C  CD     . GLU A 1 508  ? 174.416 129.316 177.310 1.00 49.31 ? 508  GLU A CD     1 
ATOM   2927 O  OE1    . GLU A 1 508  ? 174.437 130.279 176.515 1.00 49.31 ? 508  GLU A OE1    1 
ATOM   2928 O  OE2    . GLU A 1 508  ? 174.734 128.159 176.977 1.00 49.31 ? 508  GLU A OE2    1 
ATOM   2929 N  N      . MET A 1 509  ? 170.149 128.677 179.545 1.00 51.45 ? 509  MET A N      1 
ATOM   2930 C  CA     . MET A 1 509  ? 169.490 127.429 179.937 1.00 51.45 ? 509  MET A CA     1 
ATOM   2931 C  C      . MET A 1 509  ? 168.579 126.892 178.837 1.00 51.45 ? 509  MET A C      1 
ATOM   2932 O  O      . MET A 1 509  ? 168.450 125.673 178.684 1.00 51.45 ? 509  MET A O      1 
ATOM   2933 C  CB     . MET A 1 509  ? 168.676 127.597 181.223 1.00 51.45 ? 509  MET A CB     1 
ATOM   2934 C  CG     . MET A 1 509  ? 169.396 127.259 182.525 1.00 51.45 ? 509  MET A CG     1 
ATOM   2935 S  SD     . MET A 1 509  ? 170.362 128.527 183.337 1.00 51.45 ? 509  MET A SD     1 
ATOM   2936 C  CE     . MET A 1 509  ? 169.065 129.489 184.105 1.00 51.45 ? 509  MET A CE     1 
ATOM   2937 N  N      . GLY A 1 510  ? 167.930 127.778 178.079 1.00 54.45 ? 510  GLY A N      1 
ATOM   2938 C  CA     . GLY A 1 510  ? 167.120 127.331 176.959 1.00 54.45 ? 510  GLY A CA     1 
ATOM   2939 C  C      . GLY A 1 510  ? 167.944 126.749 175.830 1.00 54.45 ? 510  GLY A C      1 
ATOM   2940 O  O      . GLY A 1 510  ? 167.512 125.804 175.164 1.00 54.45 ? 510  GLY A O      1 
ATOM   2941 N  N      . LYS A 1 511  ? 169.137 127.298 175.599 1.00 54.85 ? 511  LYS A N      1 
ATOM   2942 C  CA     . LYS A 1 511  ? 170.082 126.695 174.667 1.00 54.85 ? 511  LYS A CA     1 
ATOM   2943 C  C      . LYS A 1 511  ? 170.771 125.461 175.235 1.00 54.85 ? 511  LYS A C      1 
ATOM   2944 O  O      . LYS A 1 511  ? 171.385 124.709 174.472 1.00 54.85 ? 511  LYS A O      1 
ATOM   2945 C  CB     . LYS A 1 511  ? 171.144 127.716 174.251 1.00 54.85 ? 511  LYS A CB     1 
ATOM   2946 C  CG     . LYS A 1 511  ? 170.605 128.891 173.458 1.00 54.85 ? 511  LYS A CG     1 
ATOM   2947 C  CD     . LYS A 1 511  ? 170.123 128.448 172.083 1.00 54.85 ? 511  LYS A CD     1 
ATOM   2948 C  CE     . LYS A 1 511  ? 169.664 129.631 171.247 1.00 54.85 ? 511  LYS A CE     1 
ATOM   2949 N  NZ     . LYS A 1 511  ? 169.153 129.206 169.916 1.00 54.85 ? 511  LYS A NZ     1 
ATOM   2950 N  N      . ARG A 1 512  ? 170.678 125.234 176.544 1.00 53.82 ? 512  ARG A N      1 
ATOM   2951 C  CA     . ARG A 1 512  ? 171.397 124.165 177.223 1.00 53.82 ? 512  ARG A CA     1 
ATOM   2952 C  C      . ARG A 1 512  ? 170.515 122.981 177.599 1.00 53.82 ? 512  ARG A C      1 
ATOM   2953 O  O      . ARG A 1 512  ? 171.010 121.850 177.633 1.00 53.82 ? 512  ARG A O      1 
ATOM   2954 C  CB     . ARG A 1 512  ? 172.066 124.727 178.489 1.00 53.82 ? 512  ARG A CB     1 
ATOM   2955 C  CG     . ARG A 1 512  ? 173.009 123.796 179.220 1.00 53.82 ? 512  ARG A CG     1 
ATOM   2956 C  CD     . ARG A 1 512  ? 174.274 123.561 178.429 1.00 53.82 ? 512  ARG A CD     1 
ATOM   2957 N  NE     . ARG A 1 512  ? 175.030 124.796 178.265 1.00 53.82 ? 512  ARG A NE     1 
ATOM   2958 C  CZ     . ARG A 1 512  ? 175.900 125.259 179.156 1.00 53.82 ? 512  ARG A CZ     1 
ATOM   2959 N  NH1    . ARG A 1 512  ? 176.135 124.585 180.273 1.00 53.82 ? 512  ARG A NH1    1 
ATOM   2960 N  NH2    . ARG A 1 512  ? 176.542 126.393 178.929 1.00 53.82 ? 512  ARG A NH2    1 
ATOM   2961 N  N      . GLN A 1 513  ? 169.221 123.222 177.836 1.00 59.38 ? 513  GLN A N      1 
ATOM   2962 C  CA     . GLN A 1 513  ? 168.252 122.253 178.367 1.00 59.38 ? 513  GLN A CA     1 
ATOM   2963 C  C      . GLN A 1 513  ? 168.731 121.649 179.690 1.00 59.38 ? 513  GLN A C      1 
ATOM   2964 O  O      . GLN A 1 513  ? 168.912 120.439 179.834 1.00 59.38 ? 513  GLN A O      1 
ATOM   2965 C  CB     . GLN A 1 513  ? 167.910 121.156 177.349 1.00 59.38 ? 513  GLN A CB     1 
ATOM   2966 C  CG     . GLN A 1 513  ? 167.090 121.623 176.152 1.00 59.38 ? 513  GLN A CG     1 
ATOM   2967 C  CD     . GLN A 1 513  ? 167.943 122.143 175.013 1.00 59.38 ? 513  GLN A CD     1 
ATOM   2968 O  OE1    . GLN A 1 513  ? 169.143 121.877 174.947 1.00 59.38 ? 513  GLN A OE1    1 
ATOM   2969 N  NE2    . GLN A 1 513  ? 167.323 122.883 174.101 1.00 59.38 ? 513  GLN A NE2    1 
ATOM   2970 N  N      . VAL A 1 514  ? 168.940 122.534 180.663 1.00 61.34 ? 514  VAL A N      1 
ATOM   2971 C  CA     . VAL A 1 514  ? 169.256 122.177 182.043 1.00 61.34 ? 514  VAL A CA     1 
ATOM   2972 C  C      . VAL A 1 514  ? 168.359 123.017 182.943 1.00 61.34 ? 514  VAL A C      1 
ATOM   2973 O  O      . VAL A 1 514  ? 168.215 124.223 182.724 1.00 61.34 ? 514  VAL A O      1 
ATOM   2974 C  CB     . VAL A 1 514  ? 170.751 122.403 182.367 1.00 61.34 ? 514  VAL A CB     1 
ATOM   2975 C  CG1    . VAL A 1 514  ? 171.027 122.287 183.851 1.00 61.34 ? 514  VAL A CG1    1 
ATOM   2976 C  CG2    . VAL A 1 514  ? 171.617 121.386 181.637 1.00 61.34 ? 514  VAL A CG2    1 
ATOM   2977 N  N      . LYS A 1 515  ? 167.726 122.380 183.932 1.00 63.76 ? 515  LYS A N      1 
ATOM   2978 C  CA     . LYS A 1 515  ? 166.783 123.096 184.783 1.00 63.76 ? 515  LYS A CA     1 
ATOM   2979 C  C      . LYS A 1 515  ? 167.461 123.956 185.842 1.00 63.76 ? 515  LYS A C      1 
ATOM   2980 O  O      . LYS A 1 515  ? 166.835 124.892 186.350 1.00 63.76 ? 515  LYS A O      1 
ATOM   2981 C  CB     . LYS A 1 515  ? 165.825 122.111 185.461 1.00 63.76 ? 515  LYS A CB     1 
ATOM   2982 C  CG     . LYS A 1 515  ? 166.488 121.174 186.457 1.00 63.76 ? 515  LYS A CG     1 
ATOM   2983 C  CD     . LYS A 1 515  ? 165.485 120.220 187.079 1.00 63.76 ? 515  LYS A CD     1 
ATOM   2984 C  CE     . LYS A 1 515  ? 166.156 119.309 188.093 1.00 63.76 ? 515  LYS A CE     1 
ATOM   2985 N  NZ     . LYS A 1 515  ? 165.191 118.354 188.706 1.00 63.76 ? 515  LYS A NZ     1 
ATOM   2986 N  N      . THR A 1 516  ? 168.714 123.675 186.183 1.00 58.16 ? 516  THR A N      1 
ATOM   2987 C  CA     . THR A 1 516  ? 169.394 124.353 187.276 1.00 58.16 ? 516  THR A CA     1 
ATOM   2988 C  C      . THR A 1 516  ? 170.485 125.274 186.744 1.00 58.16 ? 516  THR A C      1 
ATOM   2989 O  O      . THR A 1 516  ? 170.796 125.296 185.551 1.00 58.16 ? 516  THR A O      1 
ATOM   2990 C  CB     . THR A 1 516  ? 169.994 123.342 188.259 1.00 58.16 ? 516  THR A CB     1 
ATOM   2991 O  OG1    . THR A 1 516  ? 170.500 124.034 189.406 1.00 58.16 ? 516  THR A OG1    1 
ATOM   2992 C  CG2    . THR A 1 516  ? 171.126 122.574 187.602 1.00 58.16 ? 516  THR A CG2    1 
ATOM   2993 N  N      . ILE A 1 517  ? 171.070 126.037 187.662 1.00 48.00 ? 517  ILE A N      1 
ATOM   2994 C  CA     . ILE A 1 517  ? 172.121 126.997 187.354 1.00 48.00 ? 517  ILE A CA     1 
ATOM   2995 C  C      . ILE A 1 517  ? 173.444 126.461 187.891 1.00 48.00 ? 517  ILE A C      1 
ATOM   2996 O  O      . ILE A 1 517  ? 173.492 125.822 188.950 1.00 48.00 ? 517  ILE A O      1 
ATOM   2997 C  CB     . ILE A 1 517  ? 171.772 128.394 187.922 1.00 48.00 ? 517  ILE A CB     1 
ATOM   2998 C  CG1    . ILE A 1 517  ? 172.753 129.472 187.452 1.00 48.00 ? 517  ILE A CG1    1 
ATOM   2999 C  CG2    . ILE A 1 517  ? 171.618 128.383 189.441 1.00 48.00 ? 517  ILE A CG2    1 
ATOM   3000 C  CD1    . ILE A 1 517  ? 172.665 129.780 185.988 1.00 48.00 ? 517  ILE A CD1    1 
ATOM   3001 N  N      . ASP A 1 518  ? 174.507 126.662 187.119 1.00 42.29 ? 518  ASP A N      1 
ATOM   3002 C  CA     . ASP A 1 518  ? 175.859 126.351 187.551 1.00 42.29 ? 518  ASP A CA     1 
ATOM   3003 C  C      . ASP A 1 518  ? 176.803 127.351 186.899 1.00 42.29 ? 518  ASP A C      1 
ATOM   3004 O  O      . ASP A 1 518  ? 176.377 128.256 186.179 1.00 42.29 ? 518  ASP A O      1 
ATOM   3005 C  CB     . ASP A 1 518  ? 176.230 124.894 187.243 1.00 42.29 ? 518  ASP A CB     1 
ATOM   3006 C  CG     . ASP A 1 518  ? 176.029 124.521 185.785 1.00 42.29 ? 518  ASP A CG     1 
ATOM   3007 O  OD1    . ASP A 1 518  ? 175.486 125.333 185.008 1.00 42.29 ? 518  ASP A OD1    1 
ATOM   3008 O  OD2    . ASP A 1 518  ? 176.421 123.396 185.413 1.00 42.29 ? 518  ASP A OD2    1 
ATOM   3009 N  N      . MET A 1 519  ? 178.097 127.188 187.158 1.00 38.12 ? 519  MET A N      1 
ATOM   3010 C  CA     . MET A 1 519  ? 179.058 128.164 186.672 1.00 38.12 ? 519  MET A CA     1 
ATOM   3011 C  C      . MET A 1 519  ? 179.395 127.995 185.203 1.00 38.12 ? 519  MET A C      1 
ATOM   3012 O  O      . MET A 1 519  ? 179.960 128.914 184.618 1.00 38.12 ? 519  MET A O      1 
ATOM   3013 C  CB     . MET A 1 519  ? 180.337 128.114 187.503 1.00 38.12 ? 519  MET A CB     1 
ATOM   3014 C  CG     . MET A 1 519  ? 180.179 128.636 188.912 1.00 38.12 ? 519  MET A CG     1 
ATOM   3015 S  SD     . MET A 1 519  ? 179.689 130.369 188.968 1.00 38.12 ? 519  MET A SD     1 
ATOM   3016 C  CE     . MET A 1 519  ? 177.989 130.242 189.505 1.00 38.12 ? 519  MET A CE     1 
ATOM   3017 N  N      . ASP A 1 520  ? 179.059 126.861 184.589 1.00 39.66 ? 520  ASP A N      1 
ATOM   3018 C  CA     . ASP A 1 520  ? 179.280 126.723 183.154 1.00 39.66 ? 520  ASP A CA     1 
ATOM   3019 C  C      . ASP A 1 520  ? 178.346 127.640 182.374 1.00 39.66 ? 520  ASP A C      1 
ATOM   3020 O  O      . ASP A 1 520  ? 178.763 128.287 181.405 1.00 39.66 ? 520  ASP A O      1 
ATOM   3021 C  CB     . ASP A 1 520  ? 179.085 125.268 182.736 1.00 39.66 ? 520  ASP A CB     1 
ATOM   3022 C  CG     . ASP A 1 520  ? 179.583 124.995 181.336 1.00 39.66 ? 520  ASP A CG     1 
ATOM   3023 O  OD1    . ASP A 1 520  ? 180.811 124.875 181.159 1.00 39.66 ? 520  ASP A OD1    1 
ATOM   3024 O  OD2    . ASP A 1 520  ? 178.751 124.907 180.412 1.00 39.66 ? 520  ASP A OD2    1 
ATOM   3025 N  N      . VAL A 1 521  ? 177.095 127.747 182.827 1.00 40.08 ? 521  VAL A N      1 
ATOM   3026 C  CA     . VAL A 1 521  ? 176.128 128.664 182.233 1.00 40.08 ? 521  VAL A CA     1 
ATOM   3027 C  C      . VAL A 1 521  ? 176.557 130.111 182.437 1.00 40.08 ? 521  VAL A C      1 
ATOM   3028 O  O      . VAL A 1 521  ? 176.520 130.921 181.502 1.00 40.08 ? 521  VAL A O      1 
ATOM   3029 C  CB     . VAL A 1 521  ? 174.734 128.393 182.826 1.00 40.08 ? 521  VAL A CB     1 
ATOM   3030 C  CG1    . VAL A 1 521  ? 173.748 129.457 182.400 1.00 40.08 ? 521  VAL A CG1    1 
ATOM   3031 C  CG2    . VAL A 1 521  ? 174.247 127.023 182.402 1.00 40.08 ? 521  VAL A CG2    1 
ATOM   3032 N  N      . VAL A 1 522  ? 176.996 130.446 183.652 1.00 37.20 ? 522  VAL A N      1 
ATOM   3033 C  CA     . VAL A 1 522  ? 177.433 131.801 183.976 1.00 37.20 ? 522  VAL A CA     1 
ATOM   3034 C  C      . VAL A 1 522  ? 178.680 132.173 183.185 1.00 37.20 ? 522  VAL A C      1 
ATOM   3035 O  O      . VAL A 1 522  ? 178.788 133.284 182.654 1.00 37.20 ? 522  VAL A O      1 
ATOM   3036 C  CB     . VAL A 1 522  ? 177.662 131.911 185.493 1.00 37.20 ? 522  VAL A CB     1 
ATOM   3037 C  CG1    . VAL A 1 522  ? 178.249 133.253 185.861 1.00 37.20 ? 522  VAL A CG1    1 
ATOM   3038 C  CG2    . VAL A 1 522  ? 176.364 131.676 186.230 1.00 37.20 ? 522  VAL A CG2    1 
ATOM   3039 N  N      . GLY A 1 523  ? 179.619 131.236 183.062 1.00 35.84 ? 523  GLY A N      1 
ATOM   3040 C  CA     . GLY A 1 523  ? 180.819 131.473 182.289 1.00 35.84 ? 523  GLY A CA     1 
ATOM   3041 C  C      . GLY A 1 523  ? 180.559 131.615 180.809 1.00 35.84 ? 523  GLY A C      1 
ATOM   3042 O  O      . GLY A 1 523  ? 181.206 132.422 180.148 1.00 35.84 ? 523  GLY A O      1 
ATOM   3043 N  N      . GLU A 1 524  ? 179.583 130.878 180.274 1.00 39.40 ? 524  GLU A N      1 
ATOM   3044 C  CA     . GLU A 1 524  ? 179.264 131.052 178.862 1.00 39.40 ? 524  GLU A CA     1 
ATOM   3045 C  C      . GLU A 1 524  ? 178.515 132.357 178.613 1.00 39.40 ? 524  GLU A C      1 
ATOM   3046 O  O      . GLU A 1 524  ? 178.725 132.991 177.572 1.00 39.40 ? 524  GLU A O      1 
ATOM   3047 C  CB     . GLU A 1 524  ? 178.481 129.845 178.345 1.00 39.40 ? 524  GLU A CB     1 
ATOM   3048 C  CG     . GLU A 1 524  ? 178.290 129.827 176.834 1.00 39.40 ? 524  GLU A CG     1 
ATOM   3049 C  CD     . GLU A 1 524  ? 177.757 128.504 176.325 1.00 39.40 ? 524  GLU A CD     1 
ATOM   3050 O  OE1    . GLU A 1 524  ? 177.569 127.584 177.144 1.00 39.40 ? 524  GLU A OE1    1 
ATOM   3051 O  OE2    . GLU A 1 524  ? 177.518 128.379 175.106 1.00 39.40 ? 524  GLU A OE2    1 
ATOM   3052 N  N      . VAL A 1 525  ? 177.677 132.792 179.562 1.00 36.63 ? 525  VAL A N      1 
ATOM   3053 C  CA     . VAL A 1 525  ? 177.051 134.112 179.461 1.00 36.63 ? 525  VAL A CA     1 
ATOM   3054 C  C      . VAL A 1 525  ? 178.110 135.210 179.507 1.00 36.63 ? 525  VAL A C      1 
ATOM   3055 O  O      . VAL A 1 525  ? 178.070 136.161 178.717 1.00 36.63 ? 525  VAL A O      1 
ATOM   3056 C  CB     . VAL A 1 525  ? 175.982 134.287 180.559 1.00 36.63 ? 525  VAL A CB     1 
ATOM   3057 C  CG1    . VAL A 1 525  ? 175.503 135.725 180.639 1.00 36.63 ? 525  VAL A CG1    1 
ATOM   3058 C  CG2    . VAL A 1 525  ? 174.796 133.405 180.261 1.00 36.63 ? 525  VAL A CG2    1 
ATOM   3059 N  N      . ILE A 1 526  ? 179.110 135.056 180.376 1.00 34.73 ? 526  ILE A N      1 
ATOM   3060 C  CA     . ILE A 1 526  ? 180.212 136.015 180.445 1.00 34.73 ? 526  ILE A CA     1 
ATOM   3061 C  C      . ILE A 1 526  ? 181.076 135.966 179.185 1.00 34.73 ? 526  ILE A C      1 
ATOM   3062 O  O      . ILE A 1 526  ? 181.570 137.003 178.728 1.00 34.73 ? 526  ILE A O      1 
ATOM   3063 C  CB     . ILE A 1 526  ? 181.009 135.772 181.746 1.00 34.73 ? 526  ILE A CB     1 
ATOM   3064 C  CG1    . ILE A 1 526  ? 180.189 136.248 182.942 1.00 34.73 ? 526  ILE A CG1    1 
ATOM   3065 C  CG2    . ILE A 1 526  ? 182.370 136.446 181.758 1.00 34.73 ? 526  ILE A CG2    1 
ATOM   3066 C  CD1    . ILE A 1 526  ? 180.793 135.917 184.260 1.00 34.73 ? 526  ILE A CD1    1 
ATOM   3067 N  N      . GLU A 1 527  ? 181.223 134.792 178.566 1.00 35.12 ? 527  GLU A N      1 
ATOM   3068 C  CA     . GLU A 1 527  ? 181.998 134.700 177.332 1.00 35.12 ? 527  GLU A CA     1 
ATOM   3069 C  C      . GLU A 1 527  ? 181.291 135.368 176.161 1.00 35.12 ? 527  GLU A C      1 
ATOM   3070 O  O      . GLU A 1 527  ? 181.927 136.096 175.393 1.00 35.12 ? 527  GLU A O      1 
ATOM   3071 C  CB     . GLU A 1 527  ? 182.309 133.245 176.990 1.00 35.12 ? 527  GLU A CB     1 
ATOM   3072 C  CG     . GLU A 1 527  ? 183.411 132.629 177.813 1.00 35.12 ? 527  GLU A CG     1 
ATOM   3073 C  CD     . GLU A 1 527  ? 183.669 131.185 177.447 1.00 35.12 ? 527  GLU A CD     1 
ATOM   3074 O  OE1    . GLU A 1 527  ? 182.901 130.635 176.632 1.00 35.12 ? 527  GLU A OE1    1 
ATOM   3075 O  OE2    . GLU A 1 527  ? 184.639 130.598 177.967 1.00 35.12 ? 527  GLU A OE2    1 
ATOM   3076 N  N      . GLU A 1 528  ? 179.987 135.134 175.989 1.00 37.45 ? 528  GLU A N      1 
ATOM   3077 C  CA     . GLU A 1 528  ? 179.294 135.876 174.939 1.00 37.45 ? 528  GLU A CA     1 
ATOM   3078 C  C      . GLU A 1 528  ? 178.988 137.317 175.323 1.00 37.45 ? 528  GLU A C      1 
ATOM   3079 O  O      . GLU A 1 528  ? 178.538 138.082 174.465 1.00 37.45 ? 528  GLU A O      1 
ATOM   3080 C  CB     . GLU A 1 528  ? 177.984 135.205 174.488 1.00 37.45 ? 528  GLU A CB     1 
ATOM   3081 C  CG     . GLU A 1 528  ? 178.153 134.036 173.510 1.00 37.45 ? 528  GLU A CG     1 
ATOM   3082 C  CD     . GLU A 1 528  ? 177.905 132.674 174.114 1.00 37.45 ? 528  GLU A CD     1 
ATOM   3083 O  OE1    . GLU A 1 528  ? 177.307 132.606 175.197 1.00 37.45 ? 528  GLU A OE1    1 
ATOM   3084 O  OE2    . GLU A 1 528  ? 178.306 131.666 173.501 1.00 37.45 ? 528  GLU A OE2    1 
ATOM   3085 N  N      . LEU A 1 529  ? 179.234 137.714 176.567 1.00 31.84 ? 529  LEU A N      1 
ATOM   3086 C  CA     . LEU A 1 529  ? 178.989 139.074 177.009 1.00 31.84 ? 529  LEU A CA     1 
ATOM   3087 C  C      . LEU A 1 529  ? 180.278 139.870 177.180 1.00 31.84 ? 529  LEU A C      1 
ATOM   3088 O  O      . LEU A 1 529  ? 180.230 141.048 177.541 1.00 31.84 ? 529  LEU A O      1 
ATOM   3089 C  CB     . LEU A 1 529  ? 178.194 139.014 178.313 1.00 31.84 ? 529  LEU A CB     1 
ATOM   3090 C  CG     . LEU A 1 529  ? 177.399 140.175 178.871 1.00 31.84 ? 529  LEU A CG     1 
ATOM   3091 C  CD1    . LEU A 1 529  ? 176.350 140.567 177.864 1.00 31.84 ? 529  LEU A CD1    1 
ATOM   3092 C  CD2    . LEU A 1 529  ? 176.757 139.653 180.106 1.00 31.84 ? 529  LEU A CD2    1 
ATOM   3093 N  N      . MET A 1 530  ? 181.429 139.243 176.966 1.00 29.57 ? 530  MET A N      1 
ATOM   3094 C  CA     . MET A 1 530  ? 182.707 139.918 176.784 1.00 29.57 ? 530  MET A CA     1 
ATOM   3095 C  C      . MET A 1 530  ? 183.100 140.014 175.323 1.00 29.57 ? 530  MET A C      1 
ATOM   3096 O  O      . MET A 1 530  ? 183.677 141.021 174.903 1.00 29.57 ? 530  MET A O      1 
ATOM   3097 C  CB     . MET A 1 530  ? 183.819 139.183 177.536 1.00 29.57 ? 530  MET A CB     1 
ATOM   3098 C  CG     . MET A 1 530  ? 183.964 139.424 179.020 1.00 29.57 ? 530  MET A CG     1 
ATOM   3099 S  SD     . MET A 1 530  ? 184.600 141.064 179.404 1.00 29.57 ? 530  MET A SD     1 
ATOM   3100 C  CE     . MET A 1 530  ? 186.240 141.033 178.699 1.00 29.57 ? 530  MET A CE     1 
ATOM   3101 N  N      . GLY A 1 531  ? 182.820 138.972 174.547 1.00 32.10 ? 531  GLY A N      1 
ATOM   3102 C  CA     . GLY A 1 531  ? 183.191 138.935 173.149 1.00 32.10 ? 531  GLY A CA     1 
ATOM   3103 C  C      . GLY A 1 531  ? 184.690 138.782 172.970 1.00 32.10 ? 531  GLY A C      1 
ATOM   3104 O  O      . GLY A 1 531  ? 185.452 138.611 173.920 1.00 32.10 ? 531  GLY A O      1 
ATOM   3105 N  N      . ASP A 1 532  ? 185.097 138.812 171.694 1.00 34.16 ? 532  ASP A N      1 
ATOM   3106 C  CA     . ASP A 1 532  ? 186.498 138.928 171.268 1.00 34.16 ? 532  ASP A CA     1 
ATOM   3107 C  C      . ASP A 1 532  ? 187.349 137.754 171.755 1.00 34.16 ? 532  ASP A C      1 
ATOM   3108 O  O      . ASP A 1 532  ? 188.482 137.941 172.207 1.00 34.16 ? 532  ASP A O      1 
ATOM   3109 C  CB     . ASP A 1 532  ? 187.097 140.265 171.716 1.00 34.16 ? 532  ASP A CB     1 
ATOM   3110 C  CG     . ASP A 1 532  ? 186.399 141.454 171.084 1.00 34.16 ? 532  ASP A CG     1 
ATOM   3111 O  OD1    . ASP A 1 532  ? 185.888 141.313 169.953 1.00 34.16 ? 532  ASP A OD1    1 
ATOM   3112 O  OD2    . ASP A 1 532  ? 186.351 142.528 171.721 1.00 34.16 ? 532  ASP A OD2    1 
ATOM   3113 N  N      . MET A 1 533  ? 186.775 136.544 171.671 1.00 36.14 ? 533  MET A N      1 
ATOM   3114 C  CA     . MET A 1 533  ? 187.410 135.279 172.072 1.00 36.14 ? 533  MET A CA     1 
ATOM   3115 C  C      . MET A 1 533  ? 187.822 135.273 173.543 1.00 36.14 ? 533  MET A C      1 
ATOM   3116 O  O      . MET A 1 533  ? 188.893 134.785 173.907 1.00 36.14 ? 533  MET A O      1 
ATOM   3117 C  CB     . MET A 1 533  ? 188.598 134.926 171.173 1.00 36.14 ? 533  MET A CB     1 
ATOM   3118 C  CG     . MET A 1 533  ? 188.195 134.455 169.796 1.00 36.14 ? 533  MET A CG     1 
ATOM   3119 S  SD     . MET A 1 533  ? 187.166 132.985 169.933 1.00 36.14 ? 533  MET A SD     1 
ATOM   3120 C  CE     . MET A 1 533  ? 188.338 131.831 170.647 1.00 36.14 ? 533  MET A CE     1 
ATOM   3121 N  N      . PHE A 1 534  ? 186.955 135.802 174.395 1.00 31.88 ? 534  PHE A N      1 
ATOM   3122 C  CA     . PHE A 1 534  ? 187.155 135.731 175.831 1.00 31.88 ? 534  PHE A CA     1 
ATOM   3123 C  C      . PHE A 1 534  ? 186.870 134.319 176.322 1.00 31.88 ? 534  PHE A C      1 
ATOM   3124 O  O      . PHE A 1 534  ? 185.989 133.627 175.806 1.00 31.88 ? 534  PHE A O      1 
ATOM   3125 C  CB     . PHE A 1 534  ? 186.237 136.721 176.539 1.00 31.88 ? 534  PHE A CB     1 
ATOM   3126 C  CG     . PHE A 1 534  ? 186.478 136.840 178.015 1.00 31.88 ? 534  PHE A CG     1 
ATOM   3127 C  CD1    . PHE A 1 534  ? 187.514 137.620 178.494 1.00 31.88 ? 534  PHE A CD1    1 
ATOM   3128 C  CD2    . PHE A 1 534  ? 185.670 136.174 178.923 1.00 31.88 ? 534  PHE A CD2    1 
ATOM   3129 C  CE1    . PHE A 1 534  ? 187.742 137.737 179.847 1.00 31.88 ? 534  PHE A CE1    1 
ATOM   3130 C  CE2    . PHE A 1 534  ? 185.899 136.282 180.277 1.00 31.88 ? 534  PHE A CE2    1 
ATOM   3131 C  CZ     . PHE A 1 534  ? 186.939 137.064 180.738 1.00 31.88 ? 534  PHE A CZ     1 
ATOM   3132 N  N      . GLU A 1 535  ? 187.625 133.892 177.328 1.00 32.25 ? 535  GLU A N      1 
ATOM   3133 C  CA     . GLU A 1 535  ? 187.473 132.564 177.910 1.00 32.25 ? 535  GLU A CA     1 
ATOM   3134 C  C      . GLU A 1 535  ? 187.296 132.725 179.410 1.00 32.25 ? 535  GLU A C      1 
ATOM   3135 O  O      . GLU A 1 535  ? 188.256 133.032 180.122 1.00 32.25 ? 535  GLU A O      1 
ATOM   3136 C  CB     . GLU A 1 535  ? 188.678 131.680 177.596 1.00 32.25 ? 535  GLU A CB     1 
ATOM   3137 C  CG     . GLU A 1 535  ? 188.842 131.368 176.122 1.00 32.25 ? 535  GLU A CG     1 
ATOM   3138 C  CD     . GLU A 1 535  ? 190.065 130.522 175.835 1.00 32.25 ? 535  GLU A CD     1 
ATOM   3139 O  OE1    . GLU A 1 535  ? 190.836 130.250 176.778 1.00 32.25 ? 535  GLU A OE1    1 
ATOM   3140 O  OE2    . GLU A 1 535  ? 190.262 130.138 174.664 1.00 32.25 ? 535  GLU A OE2    1 
ATOM   3141 N  N      . SER A 1 536  ? 186.074 132.519 179.887 1.00 33.02 ? 536  SER A N      1 
ATOM   3142 C  CA     . SER A 1 536  ? 185.797 132.663 181.306 1.00 33.02 ? 536  SER A CA     1 
ATOM   3143 C  C      . SER A 1 536  ? 186.388 131.493 182.079 1.00 33.02 ? 536  SER A C      1 
ATOM   3144 O  O      . SER A 1 536  ? 186.374 130.351 181.615 1.00 33.02 ? 536  SER A O      1 
ATOM   3145 C  CB     . SER A 1 536  ? 184.294 132.751 181.544 1.00 33.02 ? 536  SER A CB     1 
ATOM   3146 O  OG     . SER A 1 536  ? 184.028 132.926 182.915 1.00 33.02 ? 536  SER A OG     1 
ATOM   3147 N  N      . TYR A 1 537  ? 186.915 131.783 183.267 1.00 33.72 ? 537  TYR A N      1 
ATOM   3148 C  CA     . TYR A 1 537  ? 187.598 130.764 184.051 1.00 33.72 ? 537  TYR A CA     1 
ATOM   3149 C  C      . TYR A 1 537  ? 186.646 129.811 184.759 1.00 33.72 ? 537  TYR A C      1 
ATOM   3150 O  O      . TYR A 1 537  ? 187.113 128.836 185.354 1.00 33.72 ? 537  TYR A O      1 
ATOM   3151 C  CB     . TYR A 1 537  ? 188.550 131.418 185.064 1.00 33.72 ? 537  TYR A CB     1 
ATOM   3152 C  CG     . TYR A 1 537  ? 187.908 132.329 186.090 1.00 33.72 ? 537  TYR A CG     1 
ATOM   3153 C  CD1    . TYR A 1 537  ? 187.735 133.682 185.830 1.00 33.72 ? 537  TYR A CD1    1 
ATOM   3154 C  CD2    . TYR A 1 537  ? 187.506 131.845 187.329 1.00 33.72 ? 537  TYR A CD2    1 
ATOM   3155 C  CE1    . TYR A 1 537  ? 187.161 134.518 186.760 1.00 33.72 ? 537  TYR A CE1    1 
ATOM   3156 C  CE2    . TYR A 1 537  ? 186.933 132.675 188.265 1.00 33.72 ? 537  TYR A CE2    1 
ATOM   3157 C  CZ     . TYR A 1 537  ? 186.764 134.010 187.974 1.00 33.72 ? 537  TYR A CZ     1 
ATOM   3158 O  OH     . TYR A 1 537  ? 186.192 134.844 188.903 1.00 33.72 ? 537  TYR A OH     1 
ATOM   3159 N  N      . TYR A 1 538  ? 185.336 130.058 184.715 1.00 35.65 ? 538  TYR A N      1 
ATOM   3160 C  CA     . TYR A 1 538  ? 184.404 129.056 185.211 1.00 35.65 ? 538  TYR A CA     1 
ATOM   3161 C  C      . TYR A 1 538  ? 184.331 127.871 184.263 1.00 35.65 ? 538  TYR A C      1 
ATOM   3162 O  O      . TYR A 1 538  ? 184.093 126.740 184.698 1.00 35.65 ? 538  TYR A O      1 
ATOM   3163 C  CB     . TYR A 1 538  ? 183.005 129.626 185.360 1.00 35.65 ? 538  TYR A CB     1 
ATOM   3164 C  CG     . TYR A 1 538  ? 182.867 130.917 186.110 1.00 35.65 ? 538  TYR A CG     1 
ATOM   3165 C  CD1    . TYR A 1 538  ? 183.097 131.002 187.477 1.00 35.65 ? 538  TYR A CD1    1 
ATOM   3166 C  CD2    . TYR A 1 538  ? 182.403 132.040 185.455 1.00 35.65 ? 538  TYR A CD2    1 
ATOM   3167 C  CE1    . TYR A 1 538  ? 182.930 132.206 188.146 1.00 35.65 ? 538  TYR A CE1    1 
ATOM   3168 C  CE2    . TYR A 1 538  ? 182.234 133.220 186.102 1.00 35.65 ? 538  TYR A CE2    1 
ATOM   3169 C  CZ     . TYR A 1 538  ? 182.493 133.306 187.437 1.00 35.65 ? 538  TYR A CZ     1 
ATOM   3170 O  OH     . TYR A 1 538  ? 182.290 134.525 188.023 1.00 35.65 ? 538  TYR A OH     1 
ATOM   3171 N  N      . ARG A 1 539  ? 184.516 128.121 182.966 1.00 36.28 ? 539  ARG A N      1 
ATOM   3172 C  CA     . ARG A 1 539  ? 184.537 127.050 181.980 1.00 36.28 ? 539  ARG A CA     1 
ATOM   3173 C  C      . ARG A 1 539  ? 185.798 126.208 182.102 1.00 36.28 ? 539  ARG A C      1 
ATOM   3174 O  O      . ARG A 1 539  ? 185.794 125.027 181.739 1.00 36.28 ? 539  ARG A O      1 
ATOM   3175 C  CB     . ARG A 1 539  ? 184.455 127.639 180.573 1.00 36.28 ? 539  ARG A CB     1 
ATOM   3176 C  CG     . ARG A 1 539  ? 183.271 128.557 180.318 1.00 36.28 ? 539  ARG A CG     1 
ATOM   3177 C  CD     . ARG A 1 539  ? 181.952 127.824 180.309 1.00 36.28 ? 539  ARG A CD     1 
ATOM   3178 N  NE     . ARG A 1 539  ? 181.903 126.778 179.294 1.00 36.28 ? 539  ARG A NE     1 
ATOM   3179 C  CZ     . ARG A 1 539  ? 181.581 126.979 178.021 1.00 36.28 ? 539  ARG A CZ     1 
ATOM   3180 N  NH1    . ARG A 1 539  ? 181.292 128.197 177.590 1.00 36.28 ? 539  ARG A NH1    1 
ATOM   3181 N  NH2    . ARG A 1 539  ? 181.559 125.961 177.173 1.00 36.28 ? 539  ARG A NH2    1 
ATOM   3182 N  N      . LYS A 1 540  ? 186.879 126.795 182.613 1.00 36.73 ? 540  LYS A N      1 
ATOM   3183 C  CA     . LYS A 1 540  ? 188.196 126.174 182.631 1.00 36.73 ? 540  LYS A CA     1 
ATOM   3184 C  C      . LYS A 1 540  ? 188.538 125.540 183.970 1.00 36.73 ? 540  LYS A C      1 
ATOM   3185 O  O      . LYS A 1 540  ? 188.910 124.365 184.018 1.00 36.73 ? 540  LYS A O      1 
ATOM   3186 C  CB     . LYS A 1 540  ? 189.266 127.213 182.272 1.00 36.73 ? 540  LYS A CB     1 
ATOM   3187 C  CG     . LYS A 1 540  ? 189.193 127.733 180.849 1.00 36.73 ? 540  LYS A CG     1 
ATOM   3188 C  CD     . LYS A 1 540  ? 190.360 128.661 180.542 1.00 36.73 ? 540  LYS A CD     1 
ATOM   3189 C  CE     . LYS A 1 540  ? 190.190 130.009 181.230 1.00 36.73 ? 540  LYS A CE     1 
ATOM   3190 N  NZ     . LYS A 1 540  ? 191.238 130.988 180.836 1.00 36.73 ? 540  LYS A NZ     1 
ATOM   3191 N  N      . ASP A 1 541  ? 188.431 126.296 185.059 1.00 39.86 ? 541  ASP A N      1 
ATOM   3192 C  CA     . ASP A 1 541  ? 188.985 125.867 186.334 1.00 39.86 ? 541  ASP A CA     1 
ATOM   3193 C  C      . ASP A 1 541  ? 188.095 124.814 186.978 1.00 39.86 ? 541  ASP A C      1 
ATOM   3194 O  O      . ASP A 1 541  ? 186.866 124.887 186.907 1.00 39.86 ? 541  ASP A O      1 
ATOM   3195 C  CB     . ASP A 1 541  ? 189.153 127.061 187.275 1.00 39.86 ? 541  ASP A CB     1 
ATOM   3196 C  CG     . ASP A 1 541  ? 190.068 126.762 188.451 1.00 39.86 ? 541  ASP A CG     1 
ATOM   3197 O  OD1    . ASP A 1 541  ? 190.606 125.638 188.540 1.00 39.86 ? 541  ASP A OD1    1 
ATOM   3198 O  OD2    . ASP A 1 541  ? 190.255 127.660 189.293 1.00 39.86 ? 541  ASP A OD2    1 
ATOM   3199 N  N      . GLY A 1 542  ? 188.733 123.831 187.613 1.00 41.04 ? 542  GLY A N      1 
ATOM   3200 C  CA     . GLY A 1 542  ? 188.029 122.746 188.265 1.00 41.04 ? 542  GLY A CA     1 
ATOM   3201 C  C      . GLY A 1 542  ? 187.369 123.098 189.576 1.00 41.04 ? 542  GLY A C      1 
ATOM   3202 O  O      . GLY A 1 542  ? 186.577 122.302 190.088 1.00 41.04 ? 542  GLY A O      1 
ATOM   3203 N  N      . HIS A 1 543  ? 187.668 124.273 190.131 1.00 39.64 ? 543  HIS A N      1 
ATOM   3204 C  CA     . HIS A 1 543  ? 187.013 124.733 191.348 1.00 39.64 ? 543  HIS A CA     1 
ATOM   3205 C  C      . HIS A 1 543  ? 185.578 125.179 191.116 1.00 39.64 ? 543  HIS A C      1 
ATOM   3206 O  O      . HIS A 1 543  ? 184.855 125.404 192.091 1.00 39.64 ? 543  HIS A O      1 
ATOM   3207 C  CB     . HIS A 1 543  ? 187.802 125.887 191.961 1.00 39.64 ? 543  HIS A CB     1 
ATOM   3208 C  CG     . HIS A 1 543  ? 189.136 125.488 192.507 1.00 39.64 ? 543  HIS A CG     1 
ATOM   3209 N  ND1    . HIS A 1 543  ? 190.270 125.426 191.728 1.00 39.64 ? 543  HIS A ND1    1 
ATOM   3210 C  CD2    . HIS A 1 543  ? 189.520 125.150 193.760 1.00 39.64 ? 543  HIS A CD2    1 
ATOM   3211 C  CE1    . HIS A 1 543  ? 191.295 125.057 192.475 1.00 39.64 ? 543  HIS A CE1    1 
ATOM   3212 N  NE2    . HIS A 1 543  ? 190.866 124.884 193.713 1.00 39.64 ? 543  HIS A NE2    1 
ATOM   3213 N  N      . TYR A 1 544  ? 185.148 125.306 189.860 1.00 37.12 ? 544  TYR A N      1 
ATOM   3214 C  CA     . TYR A 1 544  ? 183.848 125.871 189.528 1.00 37.12 ? 544  TYR A CA     1 
ATOM   3215 C  C      . TYR A 1 544  ? 182.939 124.866 188.833 1.00 37.12 ? 544  TYR A C      1 
ATOM   3216 O  O      . TYR A 1 544  ? 181.987 125.263 188.156 1.00 37.12 ? 544  TYR A O      1 
ATOM   3217 C  CB     . TYR A 1 544  ? 184.028 127.118 188.663 1.00 37.12 ? 544  TYR A CB     1 
ATOM   3218 C  CG     . TYR A 1 544  ? 184.703 128.245 189.400 1.00 37.12 ? 544  TYR A CG     1 
ATOM   3219 C  CD1    . TYR A 1 544  ? 183.981 129.061 190.257 1.00 37.12 ? 544  TYR A CD1    1 
ATOM   3220 C  CD2    . TYR A 1 544  ? 186.064 128.477 189.261 1.00 37.12 ? 544  TYR A CD2    1 
ATOM   3221 C  CE1    . TYR A 1 544  ? 184.586 130.080 190.938 1.00 37.12 ? 544  TYR A CE1    1 
ATOM   3222 C  CE2    . TYR A 1 544  ? 186.682 129.501 189.945 1.00 37.12 ? 544  TYR A CE2    1 
ATOM   3223 C  CZ     . TYR A 1 544  ? 185.936 130.299 190.782 1.00 37.12 ? 544  TYR A CZ     1 
ATOM   3224 O  OH     . TYR A 1 544  ? 186.531 131.328 191.472 1.00 37.12 ? 544  TYR A OH     1 
ATOM   3225 N  N      . PHE A 1 545  ? 183.203 123.574 188.990 1.00 41.41 ? 545  PHE A N      1 
ATOM   3226 C  CA     . PHE A 1 545  ? 182.412 122.555 188.309 1.00 41.41 ? 545  PHE A CA     1 
ATOM   3227 C  C      . PHE A 1 545  ? 181.319 122.015 189.223 1.00 41.41 ? 545  PHE A C      1 
ATOM   3228 O  O      . PHE A 1 545  ? 181.605 121.426 190.264 1.00 41.41 ? 545  PHE A O      1 
ATOM   3229 C  CB     . PHE A 1 545  ? 183.303 121.408 187.825 1.00 41.41 ? 545  PHE A CB     1 
ATOM   3230 C  CG     . PHE A 1 545  ? 184.216 121.773 186.684 1.00 41.41 ? 545  PHE A CG     1 
ATOM   3231 C  CD1    . PHE A 1 545  ? 183.996 122.912 185.921 1.00 41.41 ? 545  PHE A CD1    1 
ATOM   3232 C  CD2    . PHE A 1 545  ? 185.303 120.968 186.376 1.00 41.41 ? 545  PHE A CD2    1 
ATOM   3233 C  CE1    . PHE A 1 545  ? 184.843 123.239 184.876 1.00 41.41 ? 545  PHE A CE1    1 
ATOM   3234 C  CE2    . PHE A 1 545  ? 186.152 121.289 185.330 1.00 41.41 ? 545  PHE A CE2    1 
ATOM   3235 C  CZ     . PHE A 1 545  ? 185.921 122.426 184.581 1.00 41.41 ? 545  PHE A CZ     1 
ATOM   3236 N  N      . PRO A 1 575  ? 188.685 126.162 199.054 1.00 39.23 ? 575  PRO A N      1 
ATOM   3237 C  CA     . PRO A 1 575  ? 187.936 127.382 198.736 1.00 39.23 ? 575  PRO A CA     1 
ATOM   3238 C  C      . PRO A 1 575  ? 188.107 127.815 197.284 1.00 39.23 ? 575  PRO A C      1 
ATOM   3239 O  O      . PRO A 1 575  ? 188.871 127.198 196.547 1.00 39.23 ? 575  PRO A O      1 
ATOM   3240 C  CB     . PRO A 1 575  ? 188.539 128.417 199.687 1.00 39.23 ? 575  PRO A CB     1 
ATOM   3241 C  CG     . PRO A 1 575  ? 189.911 127.924 199.953 1.00 39.23 ? 575  PRO A CG     1 
ATOM   3242 C  CD     . PRO A 1 575  ? 189.820 126.429 199.953 1.00 39.23 ? 575  PRO A CD     1 
ATOM   3243 N  N      . LEU A 1 576  ? 187.393 128.861 196.883 1.00 36.74 ? 576  LEU A N      1 
ATOM   3244 C  CA     . LEU A 1 576  ? 187.490 129.352 195.520 1.00 36.74 ? 576  LEU A CA     1 
ATOM   3245 C  C      . LEU A 1 576  ? 188.773 130.161 195.335 1.00 36.74 ? 576  LEU A C      1 
ATOM   3246 O  O      . LEU A 1 576  ? 189.291 130.735 196.296 1.00 36.74 ? 576  LEU A O      1 
ATOM   3247 C  CB     . LEU A 1 576  ? 186.273 130.207 195.176 1.00 36.74 ? 576  LEU A CB     1 
ATOM   3248 C  CG     . LEU A 1 576  ? 184.944 129.451 195.125 1.00 36.74 ? 576  LEU A CG     1 
ATOM   3249 C  CD1    . LEU A 1 576  ? 183.801 130.392 194.800 1.00 36.74 ? 576  LEU A CD1    1 
ATOM   3250 C  CD2    . LEU A 1 576  ? 185.006 128.306 194.136 1.00 36.74 ? 576  LEU A CD2    1 
ATOM   3251 N  N      . PRO A 1 577  ? 189.330 130.192 194.105 1.00 36.28 ? 577  PRO A N      1 
ATOM   3252 C  CA     . PRO A 1 577  ? 190.572 130.944 193.873 1.00 36.28 ? 577  PRO A CA     1 
ATOM   3253 C  C      . PRO A 1 577  ? 190.426 132.448 194.035 1.00 36.28 ? 577  PRO A C      1 
ATOM   3254 O  O      . PRO A 1 577  ? 191.208 133.076 194.755 1.00 36.28 ? 577  PRO A O      1 
ATOM   3255 C  CB     . PRO A 1 577  ? 190.929 130.582 192.428 1.00 36.28 ? 577  PRO A CB     1 
ATOM   3256 C  CG     . PRO A 1 577  ? 190.275 129.288 192.194 1.00 36.28 ? 577  PRO A CG     1 
ATOM   3257 C  CD     . PRO A 1 577  ? 188.995 129.343 192.948 1.00 36.28 ? 577  PRO A CD     1 
ATOM   3258 N  N      . THR A 1 578  ? 189.434 133.038 193.368 1.00 32.07 ? 578  THR A N      1 
ATOM   3259 C  CA     . THR A 1 578  ? 189.167 134.475 193.436 1.00 32.07 ? 578  THR A CA     1 
ATOM   3260 C  C      . THR A 1 578  ? 187.735 134.706 193.896 1.00 32.07 ? 578  THR A C      1 
ATOM   3261 O  O      . THR A 1 578  ? 186.830 134.870 193.065 1.00 32.07 ? 578  THR A O      1 
ATOM   3262 C  CB     . THR A 1 578  ? 189.412 135.144 192.087 1.00 32.07 ? 578  THR A CB     1 
ATOM   3263 O  OG1    . THR A 1 578  ? 188.627 134.496 191.078 1.00 32.07 ? 578  THR A OG1    1 
ATOM   3264 C  CG2    . THR A 1 578  ? 190.880 135.094 191.719 1.00 32.07 ? 578  THR A CG2    1 
ATOM   3265 N  N      . PRO A 1 579  ? 187.481 134.725 195.208 1.00 31.54 ? 579  PRO A N      1 
ATOM   3266 C  CA     . PRO A 1 579  ? 186.102 134.944 195.672 1.00 31.54 ? 579  PRO A CA     1 
ATOM   3267 C  C      . PRO A 1 579  ? 185.635 136.378 195.508 1.00 31.54 ? 579  PRO A C      1 
ATOM   3268 O  O      . PRO A 1 579  ? 184.457 136.615 195.207 1.00 31.54 ? 579  PRO A O      1 
ATOM   3269 C  CB     . PRO A 1 579  ? 186.166 134.536 197.147 1.00 31.54 ? 579  PRO A CB     1 
ATOM   3270 C  CG     . PRO A 1 579  ? 187.378 133.692 197.261 1.00 31.54 ? 579  PRO A CG     1 
ATOM   3271 C  CD     . PRO A 1 579  ? 188.353 134.279 196.304 1.00 31.54 ? 579  PRO A CD     1 
ATOM   3272 N  N      . TYR A 1 580  ? 186.533 137.346 195.702 1.00 28.74 ? 580  TYR A N      1 
ATOM   3273 C  CA     . TYR A 1 580  ? 186.173 138.745 195.515 1.00 28.74 ? 580  TYR A CA     1 
ATOM   3274 C  C      . TYR A 1 580  ? 185.848 139.038 194.060 1.00 28.74 ? 580  TYR A C      1 
ATOM   3275 O  O      . TYR A 1 580  ? 184.910 139.785 193.772 1.00 28.74 ? 580  TYR A O      1 
ATOM   3276 C  CB     . TYR A 1 580  ? 187.302 139.644 195.998 1.00 28.74 ? 580  TYR A CB     1 
ATOM   3277 C  CG     . TYR A 1 580  ? 187.530 139.610 197.486 1.00 28.74 ? 580  TYR A CG     1 
ATOM   3278 C  CD1    . TYR A 1 580  ? 186.762 140.382 198.343 1.00 28.74 ? 580  TYR A CD1    1 
ATOM   3279 C  CD2    . TYR A 1 580  ? 188.520 138.808 198.034 1.00 28.74 ? 580  TYR A CD2    1 
ATOM   3280 C  CE1    . TYR A 1 580  ? 186.975 140.360 199.707 1.00 28.74 ? 580  TYR A CE1    1 
ATOM   3281 C  CE2    . TYR A 1 580  ? 188.739 138.775 199.394 1.00 28.74 ? 580  TYR A CE2    1 
ATOM   3282 C  CZ     . TYR A 1 580  ? 187.962 139.553 200.226 1.00 28.74 ? 580  TYR A CZ     1 
ATOM   3283 O  OH     . TYR A 1 580  ? 188.176 139.522 201.586 1.00 28.74 ? 580  TYR A OH     1 
ATOM   3284 N  N      . LEU A 1 581  ? 186.556 138.391 193.133 1.00 26.51 ? 581  LEU A N      1 
ATOM   3285 C  CA     . LEU A 1 581  ? 186.346 138.666 191.717 1.00 26.51 ? 581  LEU A CA     1 
ATOM   3286 C  C      . LEU A 1 581  ? 185.023 138.107 191.224 1.00 26.51 ? 581  LEU A C      1 
ATOM   3287 O  O      . LEU A 1 581  ? 184.308 138.779 190.479 1.00 26.51 ? 581  LEU A O      1 
ATOM   3288 C  CB     . LEU A 1 581  ? 187.497 138.107 190.885 1.00 26.51 ? 581  LEU A CB     1 
ATOM   3289 C  CG     . LEU A 1 581  ? 187.368 138.351 189.378 1.00 26.51 ? 581  LEU A CG     1 
ATOM   3290 C  CD1    . LEU A 1 581  ? 187.264 139.834 189.094 1.00 26.51 ? 581  LEU A CD1    1 
ATOM   3291 C  CD2    . LEU A 1 581  ? 188.539 137.754 188.635 1.00 26.51 ? 581  LEU A CD2    1 
ATOM   3292 N  N      . ASP A 1 582  ? 184.661 136.893 191.624 1.00 28.51 ? 582  ASP A N      1 
ATOM   3293 C  CA     . ASP A 1 582  ? 183.420 136.366 191.076 1.00 28.51 ? 582  ASP A CA     1 
ATOM   3294 C  C      . ASP A 1 582  ? 182.185 136.856 191.830 1.00 28.51 ? 582  ASP A C      1 
ATOM   3295 O  O      . ASP A 1 582  ? 181.123 136.981 191.208 1.00 28.51 ? 582  ASP A O      1 
ATOM   3296 C  CB     . ASP A 1 582  ? 183.497 134.834 190.945 1.00 28.51 ? 582  ASP A CB     1 
ATOM   3297 C  CG     . ASP A 1 582  ? 183.846 134.140 192.213 1.00 28.51 ? 582  ASP A CG     1 
ATOM   3298 O  OD1    . ASP A 1 582  ? 183.928 134.795 193.240 1.00 28.51 ? 582  ASP A OD1    1 
ATOM   3299 O  OD2    . ASP A 1 582  ? 184.091 132.927 192.178 1.00 28.51 ? 582  ASP A OD2    1 
ATOM   3300 N  N      . VAL A 1 583  ? 182.304 137.247 193.107 1.00 25.43 ? 583  VAL A N      1 
ATOM   3301 C  CA     . VAL A 1 583  ? 181.168 137.967 193.685 1.00 25.43 ? 583  VAL A CA     1 
ATOM   3302 C  C      . VAL A 1 583  ? 181.094 139.390 193.118 1.00 25.43 ? 583  VAL A C      1 
ATOM   3303 O  O      . VAL A 1 583  ? 180.002 139.955 192.992 1.00 25.43 ? 583  VAL A O      1 
ATOM   3304 C  CB     . VAL A 1 583  ? 181.210 137.939 195.230 1.00 25.43 ? 583  VAL A CB     1 
ATOM   3305 C  CG1    . VAL A 1 583  ? 182.260 138.868 195.801 1.00 25.43 ? 583  VAL A CG1    1 
ATOM   3306 C  CG2    . VAL A 1 583  ? 179.843 138.247 195.816 1.00 25.43 ? 583  VAL A CG2    1 
ATOM   3307 N  N      . PHE A 1 584  ? 182.229 139.960 192.689 1.00 22.63 ? 584  PHE A N      1 
ATOM   3308 C  CA     . PHE A 1 584  ? 182.218 141.250 192.012 1.00 22.63 ? 584  PHE A CA     1 
ATOM   3309 C  C      . PHE A 1 584  ? 181.572 141.162 190.641 1.00 22.63 ? 584  PHE A C      1 
ATOM   3310 O  O      . PHE A 1 584  ? 180.802 142.045 190.262 1.00 22.63 ? 584  PHE A O      1 
ATOM   3311 C  CB     . PHE A 1 584  ? 183.644 141.779 191.887 1.00 22.63 ? 584  PHE A CB     1 
ATOM   3312 C  CG     . PHE A 1 584  ? 183.769 142.952 190.972 1.00 22.63 ? 584  PHE A CG     1 
ATOM   3313 C  CD1    . PHE A 1 584  ? 183.264 144.184 191.332 1.00 22.63 ? 584  PHE A CD1    1 
ATOM   3314 C  CD2    . PHE A 1 584  ? 184.385 142.818 189.738 1.00 22.63 ? 584  PHE A CD2    1 
ATOM   3315 C  CE1    . PHE A 1 584  ? 183.367 145.251 190.477 1.00 22.63 ? 584  PHE A CE1    1 
ATOM   3316 C  CE2    . PHE A 1 584  ? 184.491 143.888 188.892 1.00 22.63 ? 584  PHE A CE2    1 
ATOM   3317 C  CZ     . PHE A 1 584  ? 183.994 145.107 189.265 1.00 22.63 ? 584  PHE A CZ     1 
ATOM   3318 N  N      . LEU A 1 585  ? 181.894 140.120 189.879 1.00 24.10 ? 585  LEU A N      1 
ATOM   3319 C  CA     . LEU A 1 585  ? 181.272 139.928 188.578 1.00 24.10 ? 585  LEU A CA     1 
ATOM   3320 C  C      . LEU A 1 585  ? 179.794 139.628 188.715 1.00 24.10 ? 585  LEU A C      1 
ATOM   3321 O  O      . LEU A 1 585  ? 179.010 140.043 187.861 1.00 24.10 ? 585  LEU A O      1 
ATOM   3322 C  CB     . LEU A 1 585  ? 181.963 138.808 187.806 1.00 24.10 ? 585  LEU A CB     1 
ATOM   3323 C  CG     . LEU A 1 585  ? 183.376 139.092 187.308 1.00 24.10 ? 585  LEU A CG     1 
ATOM   3324 C  CD1    . LEU A 1 585  ? 183.961 137.862 186.646 1.00 24.10 ? 585  LEU A CD1    1 
ATOM   3325 C  CD2    . LEU A 1 585  ? 183.375 140.277 186.360 1.00 24.10 ? 585  LEU A CD2    1 
ATOM   3326 N  N      . TRP A 1 586  ? 179.397 138.939 189.787 1.00 25.59 ? 586  TRP A N      1 
ATOM   3327 C  CA     . TRP A 1 586  ? 177.979 138.780 190.085 1.00 25.59 ? 586  TRP A CA     1 
ATOM   3328 C  C      . TRP A 1 586  ? 177.313 140.122 190.350 1.00 25.59 ? 586  TRP A C      1 
ATOM   3329 O  O      . TRP A 1 586  ? 176.230 140.398 189.828 1.00 25.59 ? 586  TRP A O      1 
ATOM   3330 C  CB     . TRP A 1 586  ? 177.795 137.858 191.282 1.00 25.59 ? 586  TRP A CB     1 
ATOM   3331 C  CG     . TRP A 1 586  ? 176.375 137.704 191.625 1.00 25.59 ? 586  TRP A CG     1 
ATOM   3332 C  CD1    . TRP A 1 586  ? 175.442 137.004 190.939 1.00 25.59 ? 586  TRP A CD1    1 
ATOM   3333 C  CD2    . TRP A 1 586  ? 175.695 138.333 192.705 1.00 25.59 ? 586  TRP A CD2    1 
ATOM   3334 N  NE1    . TRP A 1 586  ? 174.223 137.117 191.547 1.00 25.59 ? 586  TRP A NE1    1 
ATOM   3335 C  CE2    . TRP A 1 586  ? 174.351 137.938 192.634 1.00 25.59 ? 586  TRP A CE2    1 
ATOM   3336 C  CE3    . TRP A 1 586  ? 176.100 139.173 193.743 1.00 25.59 ? 586  TRP A CE3    1 
ATOM   3337 C  CZ2    . TRP A 1 586  ? 173.408 138.350 193.560 1.00 25.59 ? 586  TRP A CZ2    1 
ATOM   3338 C  CZ3    . TRP A 1 586  ? 175.168 139.585 194.652 1.00 25.59 ? 586  TRP A CZ3    1 
ATOM   3339 C  CH2    . TRP A 1 586  ? 173.835 139.174 194.559 1.00 25.59 ? 586  TRP A CH2    1 
ATOM   3340 N  N      . ALA A 1 587  ? 177.950 140.970 191.160 1.00 22.87 ? 587  ALA A N      1 
ATOM   3341 C  CA     . ALA A 1 587  ? 177.394 142.283 191.472 1.00 22.87 ? 587  ALA A CA     1 
ATOM   3342 C  C      . ALA A 1 587  ? 177.351 143.198 190.252 1.00 22.87 ? 587  ALA A C      1 
ATOM   3343 O  O      . ALA A 1 587  ? 176.482 144.071 190.166 1.00 22.87 ? 587  ALA A O      1 
ATOM   3344 C  CB     . ALA A 1 587  ? 178.200 142.928 192.594 1.00 22.87 ? 587  ALA A CB     1 
ATOM   3345 N  N      . VAL A 1 588  ? 178.265 143.010 189.305 1.00 23.11 ? 588  VAL A N      1 
ATOM   3346 C  CA     . VAL A 1 588  ? 178.260 143.774 188.062 1.00 23.11 ? 588  VAL A CA     1 
ATOM   3347 C  C      . VAL A 1 588  ? 177.168 143.283 187.122 1.00 23.11 ? 588  VAL A C      1 
ATOM   3348 O  O      . VAL A 1 588  ? 176.446 144.086 186.522 1.00 23.11 ? 588  VAL A O      1 
ATOM   3349 C  CB     . VAL A 1 588  ? 179.657 143.713 187.416 1.00 23.11 ? 588  VAL A CB     1 
ATOM   3350 C  CG1    . VAL A 1 588  ? 179.641 144.214 185.991 1.00 23.11 ? 588  VAL A CG1    1 
ATOM   3351 C  CG2    . VAL A 1 588  ? 180.600 144.559 188.211 1.00 23.11 ? 588  VAL A CG2    1 
ATOM   3352 N  N      . LEU A 1 589  ? 177.013 141.962 186.997 1.00 24.97 ? 589  LEU A N      1 
ATOM   3353 C  CA     . LEU A 1 589  ? 175.991 141.409 186.114 1.00 24.97 ? 589  LEU A CA     1 
ATOM   3354 C  C      . LEU A 1 589  ? 174.586 141.681 186.628 1.00 24.97 ? 589  LEU A C      1 
ATOM   3355 O  O      . LEU A 1 589  ? 173.642 141.755 185.838 1.00 24.97 ? 589  LEU A O      1 
ATOM   3356 C  CB     . LEU A 1 589  ? 176.205 139.908 185.937 1.00 24.97 ? 589  LEU A CB     1 
ATOM   3357 C  CG     . LEU A 1 589  ? 177.425 139.502 185.116 1.00 24.97 ? 589  LEU A CG     1 
ATOM   3358 C  CD1    . LEU A 1 589  ? 177.621 138.001 185.125 1.00 24.97 ? 589  LEU A CD1    1 
ATOM   3359 C  CD2    . LEU A 1 589  ? 177.282 140.024 183.725 1.00 24.97 ? 589  LEU A CD2    1 
ATOM   3360 N  N      . CYS A 1 590  ? 174.434 141.867 187.933 1.00 25.86 ? 590  CYS A N      1 
ATOM   3361 C  CA     . CYS A 1 590  ? 173.146 142.190 188.523 1.00 25.86 ? 590  CYS A CA     1 
ATOM   3362 C  C      . CYS A 1 590  ? 172.819 143.675 188.484 1.00 25.86 ? 590  CYS A C      1 
ATOM   3363 O  O      . CYS A 1 590  ? 171.752 144.052 188.983 1.00 25.86 ? 590  CYS A O      1 
ATOM   3364 C  CB     . CYS A 1 590  ? 173.097 141.688 189.964 1.00 25.86 ? 590  CYS A CB     1 
ATOM   3365 S  SG     . CYS A 1 590  ? 173.037 139.904 190.102 1.00 25.86 ? 590  CYS A SG     1 
ATOM   3366 N  N      . ASN A 1 591  ? 173.702 144.500 187.905 1.00 26.14 ? 591  ASN A N      1 
ATOM   3367 C  CA     . ASN A 1 591  ? 173.548 145.957 187.782 1.00 26.14 ? 591  ASN A CA     1 
ATOM   3368 C  C      . ASN A 1 591  ? 173.357 146.603 189.155 1.00 26.14 ? 591  ASN A C      1 
ATOM   3369 O  O      . ASN A 1 591  ? 172.446 147.402 189.381 1.00 26.14 ? 591  ASN A O      1 
ATOM   3370 C  CB     . ASN A 1 591  ? 172.409 146.324 186.824 1.00 26.14 ? 591  ASN A CB     1 
ATOM   3371 C  CG     . ASN A 1 591  ? 172.468 147.769 186.360 1.00 26.14 ? 591  ASN A CG     1 
ATOM   3372 O  OD1    . ASN A 1 591  ? 173.401 148.501 186.682 1.00 26.14 ? 591  ASN A OD1    1 
ATOM   3373 N  ND2    . ASN A 1 591  ? 171.447 148.195 185.630 1.00 26.14 ? 591  ASN A ND2    1 
ATOM   3374 N  N      . ARG A 1 592  ? 174.220 146.233 190.089 1.00 27.59 ? 592  ARG A N      1 
ATOM   3375 C  CA     . ARG A 1 592  ? 174.159 146.741 191.452 1.00 27.59 ? 592  ARG A CA     1 
ATOM   3376 C  C      . ARG A 1 592  ? 175.315 147.709 191.631 1.00 27.59 ? 592  ARG A C      1 
ATOM   3377 O  O      . ARG A 1 592  ? 176.472 147.292 191.622 1.00 27.59 ? 592  ARG A O      1 
ATOM   3378 C  CB     . ARG A 1 592  ? 174.206 145.596 192.458 1.00 27.59 ? 592  ARG A CB     1 
ATOM   3379 C  CG     . ARG A 1 592  ? 172.998 144.697 192.323 1.00 27.59 ? 592  ARG A CG     1 
ATOM   3380 C  CD     . ARG A 1 592  ? 172.895 143.657 193.398 1.00 27.59 ? 592  ARG A CD     1 
ATOM   3381 N  NE     . ARG A 1 592  ? 171.713 142.830 193.192 1.00 27.59 ? 592  ARG A NE     1 
ATOM   3382 C  CZ     . ARG A 1 592  ? 171.294 141.908 194.045 1.00 27.59 ? 592  ARG A CZ     1 
ATOM   3383 N  NH1    . ARG A 1 592  ? 171.943 141.722 195.181 1.00 27.59 ? 592  ARG A NH1    1 
ATOM   3384 N  NH2    . ARG A 1 592  ? 170.211 141.196 193.776 1.00 27.59 ? 592  ARG A NH2    1 
ATOM   3385 N  N      . ARG A 1 593  ? 174.994 148.997 191.773 1.00 27.07 ? 593  ARG A N      1 
ATOM   3386 C  CA     . ARG A 1 593  ? 176.010 150.046 191.815 1.00 27.07 ? 593  ARG A CA     1 
ATOM   3387 C  C      . ARG A 1 593  ? 176.902 149.915 193.043 1.00 27.07 ? 593  ARG A C      1 
ATOM   3388 O  O      . ARG A 1 593  ? 178.119 149.721 192.931 1.00 27.07 ? 593  ARG A O      1 
ATOM   3389 C  CB     . ARG A 1 593  ? 175.342 151.422 191.820 1.00 27.07 ? 593  ARG A CB     1 
ATOM   3390 C  CG     . ARG A 1 593  ? 174.452 151.748 190.645 1.00 27.07 ? 593  ARG A CG     1 
ATOM   3391 C  CD     . ARG A 1 593  ? 175.260 151.964 189.410 1.00 27.07 ? 593  ARG A CD     1 
ATOM   3392 N  NE     . ARG A 1 593  ? 174.437 152.354 188.274 1.00 27.07 ? 593  ARG A NE     1 
ATOM   3393 C  CZ     . ARG A 1 593  ? 174.250 153.610 187.893 1.00 27.07 ? 593  ARG A CZ     1 
ATOM   3394 N  NH1    . ARG A 1 593  ? 174.843 154.596 188.546 1.00 27.07 ? 593  ARG A NH1    1 
ATOM   3395 N  NH2    . ARG A 1 593  ? 173.484 153.878 186.849 1.00 27.07 ? 593  ARG A NH2    1 
ATOM   3396 N  N      . GLU A 1 594  ? 176.306 150.023 194.230 1.00 26.98 ? 594  GLU A N      1 
ATOM   3397 C  CA     . GLU A 1 594  ? 177.093 150.124 195.449 1.00 26.98 ? 594  GLU A CA     1 
ATOM   3398 C  C      . GLU A 1 594  ? 177.672 148.786 195.862 1.00 26.98 ? 594  GLU A C      1 
ATOM   3399 O  O      . GLU A 1 594  ? 178.755 148.746 196.450 1.00 26.98 ? 594  GLU A O      1 
ATOM   3400 C  CB     . GLU A 1 594  ? 176.243 150.706 196.579 1.00 26.98 ? 594  GLU A CB     1 
ATOM   3401 C  CG     . GLU A 1 594  ? 175.798 152.132 196.336 1.00 26.98 ? 594  GLU A CG     1 
ATOM   3402 C  CD     . GLU A 1 594  ? 176.954 153.112 196.324 1.00 26.98 ? 594  GLU A CD     1 
ATOM   3403 O  OE1    . GLU A 1 594  ? 177.924 152.906 197.081 1.00 26.98 ? 594  GLU A OE1    1 
ATOM   3404 O  OE2    . GLU A 1 594  ? 176.896 154.087 195.547 1.00 26.98 ? 594  GLU A OE2    1 
ATOM   3405 N  N      . LEU A 1 595  ? 176.993 147.690 195.534 1.00 25.92 ? 595  LEU A N      1 
ATOM   3406 C  CA     . LEU A 1 595  ? 177.544 146.375 195.828 1.00 25.92 ? 595  LEU A CA     1 
ATOM   3407 C  C      . LEU A 1 595  ? 178.760 146.082 194.961 1.00 25.92 ? 595  LEU A C      1 
ATOM   3408 O  O      . LEU A 1 595  ? 179.763 145.562 195.459 1.00 25.92 ? 595  LEU A O      1 
ATOM   3409 C  CB     . LEU A 1 595  ? 176.467 145.308 195.649 1.00 25.92 ? 595  LEU A CB     1 
ATOM   3410 C  CG     . LEU A 1 595  ? 176.847 143.890 196.056 1.00 25.92 ? 595  LEU A CG     1 
ATOM   3411 C  CD1    . LEU A 1 595  ? 177.228 143.858 197.518 1.00 25.92 ? 595  LEU A CD1    1 
ATOM   3412 C  CD2    . LEU A 1 595  ? 175.688 142.967 195.799 1.00 25.92 ? 595  LEU A CD2    1 
ATOM   3413 N  N      . ALA A 1 596  ? 178.711 146.445 193.674 1.00 23.68 ? 596  ALA A N      1 
ATOM   3414 C  CA     . ALA A 1 596  ? 179.887 146.272 192.827 1.00 23.68 ? 596  ALA A CA     1 
ATOM   3415 C  C      . ALA A 1 596  ? 181.001 147.227 193.211 1.00 23.68 ? 596  ALA A C      1 
ATOM   3416 O  O      . ALA A 1 596  ? 182.174 146.874 193.079 1.00 23.68 ? 596  ALA A O      1 
ATOM   3417 C  CB     . ALA A 1 596  ? 179.540 146.450 191.355 1.00 23.68 ? 596  ALA A CB     1 
ATOM   3418 N  N      . ARG A 1 597  ? 180.661 148.417 193.713 1.00 24.79 ? 597  ARG A N      1 
ATOM   3419 C  CA     . ARG A 1 597  ? 181.685 149.321 194.225 1.00 24.79 ? 597  ARG A CA     1 
ATOM   3420 C  C      . ARG A 1 597  ? 182.385 148.730 195.444 1.00 24.79 ? 597  ARG A C      1 
ATOM   3421 O  O      . ARG A 1 597  ? 183.615 148.752 195.530 1.00 24.79 ? 597  ARG A O      1 
ATOM   3422 C  CB     . ARG A 1 597  ? 181.069 150.671 194.574 1.00 24.79 ? 597  ARG A CB     1 
ATOM   3423 C  CG     . ARG A 1 597  ? 182.091 151.689 195.016 1.00 24.79 ? 597  ARG A CG     1 
ATOM   3424 C  CD     . ARG A 1 597  ? 181.430 152.950 195.522 1.00 24.79 ? 597  ARG A CD     1 
ATOM   3425 N  NE     . ARG A 1 597  ? 180.550 152.655 196.647 1.00 24.79 ? 597  ARG A NE     1 
ATOM   3426 C  CZ     . ARG A 1 597  ? 180.954 152.505 197.904 1.00 24.79 ? 597  ARG A CZ     1 
ATOM   3427 N  NH1    . ARG A 1 597  ? 182.234 152.628 198.220 1.00 24.79 ? 597  ARG A NH1    1 
ATOM   3428 N  NH2    . ARG A 1 597  ? 180.069 152.234 198.851 1.00 24.79 ? 597  ARG A NH2    1 
ATOM   3429 N  N      . VAL A 1 598  ? 181.612 148.178 196.385 1.00 25.23 ? 598  VAL A N      1 
ATOM   3430 C  CA     . VAL A 1 598  ? 182.179 147.574 197.592 1.00 25.23 ? 598  VAL A CA     1 
ATOM   3431 C  C      . VAL A 1 598  ? 183.033 146.357 197.246 1.00 25.23 ? 598  VAL A C      1 
ATOM   3432 O  O      . VAL A 1 598  ? 184.142 146.191 197.769 1.00 25.23 ? 598  VAL A O      1 
ATOM   3433 C  CB     . VAL A 1 598  ? 181.053 147.227 198.587 1.00 25.23 ? 598  VAL A CB     1 
ATOM   3434 C  CG1    . VAL A 1 598  ? 181.552 146.326 199.702 1.00 25.23 ? 598  VAL A CG1    1 
ATOM   3435 C  CG2    . VAL A 1 598  ? 180.494 148.494 199.191 1.00 25.23 ? 598  VAL A CG2    1 
ATOM   3436 N  N      . LEU A 1 599  ? 182.559 145.515 196.329 1.00 23.90 ? 599  LEU A N      1 
ATOM   3437 C  CA     . LEU A 1 599  ? 183.312 144.325 195.955 1.00 23.90 ? 599  LEU A CA     1 
ATOM   3438 C  C      . LEU A 1 599  ? 184.475 144.631 195.023 1.00 23.90 ? 599  LEU A C      1 
ATOM   3439 O  O      . LEU A 1 599  ? 185.366 143.790 194.870 1.00 23.90 ? 599  LEU A O      1 
ATOM   3440 C  CB     . LEU A 1 599  ? 182.373 143.306 195.319 1.00 23.90 ? 599  LEU A CB     1 
ATOM   3441 C  CG     . LEU A 1 599  ? 181.325 142.848 196.330 1.00 23.90 ? 599  LEU A CG     1 
ATOM   3442 C  CD1    . LEU A 1 599  ? 180.269 141.993 195.678 1.00 23.90 ? 599  LEU A CD1    1 
ATOM   3443 C  CD2    . LEU A 1 599  ? 181.969 142.148 197.512 1.00 23.90 ? 599  LEU A CD2    1 
ATOM   3444 N  N      . TRP A 1 600  ? 184.485 145.807 194.400 1.00 21.22 ? 600  TRP A N      1 
ATOM   3445 C  CA     . TRP A 1 600  ? 185.647 146.261 193.655 1.00 21.22 ? 600  TRP A CA     1 
ATOM   3446 C  C      . TRP A 1 600  ? 186.712 146.823 194.585 1.00 21.22 ? 600  TRP A C      1 
ATOM   3447 O  O      . TRP A 1 600  ? 187.908 146.618 194.358 1.00 21.22 ? 600  TRP A O      1 
ATOM   3448 C  CB     . TRP A 1 600  ? 185.221 147.315 192.640 1.00 21.22 ? 600  TRP A CB     1 
ATOM   3449 C  CG     . TRP A 1 600  ? 186.324 147.822 191.805 1.00 21.22 ? 600  TRP A CG     1 
ATOM   3450 C  CD1    . TRP A 1 600  ? 186.982 147.161 190.815 1.00 21.22 ? 600  TRP A CD1    1 
ATOM   3451 C  CD2    . TRP A 1 600  ? 186.936 149.100 191.913 1.00 21.22 ? 600  TRP A CD2    1 
ATOM   3452 N  NE1    . TRP A 1 600  ? 187.956 147.960 190.287 1.00 21.22 ? 600  TRP A NE1    1 
ATOM   3453 C  CE2    . TRP A 1 600  ? 187.949 149.159 190.947 1.00 21.22 ? 600  TRP A CE2    1 
ATOM   3454 C  CE3    . TRP A 1 600  ? 186.717 150.209 192.733 1.00 21.22 ? 600  TRP A CE3    1 
ATOM   3455 C  CZ2    . TRP A 1 600  ? 188.740 150.283 190.776 1.00 21.22 ? 600  TRP A CZ2    1 
ATOM   3456 C  CZ3    . TRP A 1 600  ? 187.501 151.315 192.567 1.00 21.22 ? 600  TRP A CZ3    1 
ATOM   3457 C  CH2    . TRP A 1 600  ? 188.500 151.348 191.597 1.00 21.22 ? 600  TRP A CH2    1 
ATOM   3458 N  N      . GLU A 1 601  ? 186.292 147.550 195.624 1.00 25.39 ? 601  GLU A N      1 
ATOM   3459 C  CA     . GLU A 1 601  ? 187.231 148.086 196.603 1.00 25.39 ? 601  GLU A CA     1 
ATOM   3460 C  C      . GLU A 1 601  ? 187.893 146.984 197.419 1.00 25.39 ? 601  GLU A C      1 
ATOM   3461 O  O      . GLU A 1 601  ? 189.022 147.155 197.889 1.00 25.39 ? 601  GLU A O      1 
ATOM   3462 C  CB     . GLU A 1 601  ? 186.510 149.059 197.537 1.00 25.39 ? 601  GLU A CB     1 
ATOM   3463 C  CG     . GLU A 1 601  ? 186.028 150.330 196.878 1.00 25.39 ? 601  GLU A CG     1 
ATOM   3464 C  CD     . GLU A 1 601  ? 185.253 151.221 197.817 1.00 25.39 ? 601  GLU A CD     1 
ATOM   3465 O  OE1    . GLU A 1 601  ? 184.987 150.795 198.958 1.00 25.39 ? 601  GLU A OE1    1 
ATOM   3466 O  OE2    . GLU A 1 601  ? 184.905 152.348 197.412 1.00 25.39 ? 601  GLU A OE2    1 
ATOM   3467 N  N      . ALA A 1 602  ? 187.214 145.854 197.592 1.00 26.45 ? 602  ALA A N      1 
ATOM   3468 C  CA     . ALA A 1 602  ? 187.692 144.787 198.456 1.00 26.45 ? 602  ALA A CA     1 
ATOM   3469 C  C      . ALA A 1 602  ? 188.655 143.837 197.764 1.00 26.45 ? 602  ALA A C      1 
ATOM   3470 O  O      . ALA A 1 602  ? 189.483 143.215 198.437 1.00 26.45 ? 602  ALA A O      1 
ATOM   3471 C  CB     . ALA A 1 602  ? 186.505 143.991 199.005 1.00 26.45 ? 602  ALA A CB     1 
ATOM   3472 N  N      . GLY A 1 603  ? 188.580 143.712 196.444 1.00 27.14 ? 603  GLY A N      1 
ATOM   3473 C  CA     . GLY A 1 603  ? 189.326 142.703 195.731 1.00 27.14 ? 603  GLY A CA     1 
ATOM   3474 C  C      . GLY A 1 603  ? 190.563 143.214 195.020 1.00 27.14 ? 603  GLY A C      1 
ATOM   3475 O  O      . GLY A 1 603  ? 190.709 144.403 194.753 1.00 27.14 ? 603  GLY A O      1 
ATOM   3476 N  N      . ARG A 1 604  ? 191.452 142.272 194.702 1.00 29.42 ? 604  ARG A N      1 
ATOM   3477 C  CA     . ARG A 1 604  ? 192.674 142.543 193.962 1.00 29.42 ? 604  ARG A CA     1 
ATOM   3478 C  C      . ARG A 1 604  ? 192.361 142.756 192.483 1.00 29.42 ? 604  ARG A C      1 
ATOM   3479 O  O      . ARG A 1 604  ? 191.204 142.717 192.057 1.00 29.42 ? 604  ARG A O      1 
ATOM   3480 C  CB     . ARG A 1 604  ? 193.673 141.402 194.137 1.00 29.42 ? 604  ARG A CB     1 
ATOM   3481 C  CG     . ARG A 1 604  ? 194.180 141.191 195.549 1.00 29.42 ? 604  ARG A CG     1 
ATOM   3482 C  CD     . ARG A 1 604  ? 195.010 142.369 196.013 1.00 29.42 ? 604  ARG A CD     1 
ATOM   3483 N  NE     . ARG A 1 604  ? 195.692 142.101 197.274 1.00 29.42 ? 604  ARG A NE     1 
ATOM   3484 C  CZ     . ARG A 1 604  ? 195.145 142.263 198.474 1.00 29.42 ? 604  ARG A CZ     1 
ATOM   3485 N  NH1    . ARG A 1 604  ? 193.889 142.671 198.589 1.00 29.42 ? 604  ARG A NH1    1 
ATOM   3486 N  NH2    . ARG A 1 604  ? 195.849 141.997 199.564 1.00 29.42 ? 604  ARG A NH2    1 
ATOM   3487 N  N      . GLU A 1 605  ? 193.437 142.918 191.683 1.00 26.58 ? 605  GLU A N      1 
ATOM   3488 C  CA     . GLU A 1 605  ? 193.502 143.349 190.279 1.00 26.58 ? 605  GLU A CA     1 
ATOM   3489 C  C      . GLU A 1 605  ? 192.430 144.386 189.918 1.00 26.58 ? 605  GLU A C      1 
ATOM   3490 O  O      . GLU A 1 605  ? 191.539 144.116 189.106 1.00 26.58 ? 605  GLU A O      1 
ATOM   3491 C  CB     . GLU A 1 605  ? 193.491 142.123 189.339 1.00 26.58 ? 605  GLU A CB     1 
ATOM   3492 C  CG     . GLU A 1 605  ? 192.349 141.088 189.468 1.00 26.58 ? 605  GLU A CG     1 
ATOM   3493 C  CD     . GLU A 1 605  ? 192.669 139.959 190.425 1.00 26.58 ? 605  GLU A CD     1 
ATOM   3494 O  OE1    . GLU A 1 605  ? 193.690 140.053 191.135 1.00 26.58 ? 605  GLU A OE1    1 
ATOM   3495 O  OE2    . GLU A 1 605  ? 191.889 138.985 190.477 1.00 26.58 ? 605  GLU A OE2    1 
ATOM   3496 N  N      . PRO A 1 606  ? 192.494 145.594 190.494 1.00 22.66 ? 606  PRO A N      1 
ATOM   3497 C  CA     . PRO A 1 606  ? 191.321 146.486 190.446 1.00 22.66 ? 606  PRO A CA     1 
ATOM   3498 C  C      . PRO A 1 606  ? 191.023 147.117 189.094 1.00 22.66 ? 606  PRO A C      1 
ATOM   3499 O  O      . PRO A 1 606  ? 189.845 147.194 188.726 1.00 22.66 ? 606  PRO A O      1 
ATOM   3500 C  CB     . PRO A 1 606  ? 191.663 147.547 191.496 1.00 22.66 ? 606  PRO A CB     1 
ATOM   3501 C  CG     . PRO A 1 606  ? 193.124 147.533 191.549 1.00 22.66 ? 606  PRO A CG     1 
ATOM   3502 C  CD     . PRO A 1 606  ? 193.554 146.149 191.350 1.00 22.66 ? 606  PRO A CD     1 
ATOM   3503 N  N      . MET A 1 607  ? 192.022 147.593 188.345 1.00 20.94 ? 607  MET A N      1 
ATOM   3504 C  CA     . MET A 1 607  ? 191.673 148.264 187.096 1.00 20.94 ? 607  MET A CA     1 
ATOM   3505 C  C      . MET A 1 607  ? 191.299 147.270 186.006 1.00 20.94 ? 607  MET A C      1 
ATOM   3506 O  O      . MET A 1 607  ? 190.487 147.598 185.137 1.00 20.94 ? 607  MET A O      1 
ATOM   3507 C  CB     . MET A 1 607  ? 192.796 149.190 186.605 1.00 20.94 ? 607  MET A CB     1 
ATOM   3508 C  CG     . MET A 1 607  ? 194.026 148.520 186.044 1.00 20.94 ? 607  MET A CG     1 
ATOM   3509 S  SD     . MET A 1 607  ? 195.212 149.675 185.333 1.00 20.94 ? 607  MET A SD     1 
ATOM   3510 C  CE     . MET A 1 607  ? 195.924 150.403 186.793 1.00 20.94 ? 607  MET A CE     1 
ATOM   3511 N  N      . ALA A 1 608  ? 191.823 146.044 186.066 1.00 19.64 ? 608  ALA A N      1 
ATOM   3512 C  CA     . ALA A 1 608  ? 191.370 144.997 185.158 1.00 19.64 ? 608  ALA A CA     1 
ATOM   3513 C  C      . ALA A 1 608  ? 189.932 144.610 185.453 1.00 19.64 ? 608  ALA A C      1 
ATOM   3514 O  O      . ALA A 1 608  ? 189.135 144.400 184.531 1.00 19.64 ? 608  ALA A O      1 
ATOM   3515 C  CB     . ALA A 1 608  ? 192.277 143.780 185.273 1.00 19.64 ? 608  ALA A CB     1 
ATOM   3516 N  N      . ALA A 1 609  ? 189.587 144.545 186.741 1.00 19.72 ? 609  ALA A N      1 
ATOM   3517 C  CA     . ALA A 1 609  ? 188.218 144.283 187.164 1.00 19.72 ? 609  ALA A CA     1 
ATOM   3518 C  C      . ALA A 1 609  ? 187.276 145.388 186.716 1.00 19.72 ? 609  ALA A C      1 
ATOM   3519 O  O      . ALA A 1 609  ? 186.162 145.113 186.266 1.00 19.72 ? 609  ALA A O      1 
ATOM   3520 C  CB     . ALA A 1 609  ? 188.169 144.126 188.680 1.00 19.72 ? 609  ALA A CB     1 
ATOM   3521 N  N      . ALA A 1 610  ? 187.721 146.640 186.796 1.00 18.21 ? 610  ALA A N      1 
ATOM   3522 C  CA     . ALA A 1 610  ? 186.862 147.749 186.406 1.00 18.21 ? 610  ALA A CA     1 
ATOM   3523 C  C      . ALA A 1 610  ? 186.693 147.829 184.894 1.00 18.21 ? 610  ALA A C      1 
ATOM   3524 O  O      . ALA A 1 610  ? 185.609 148.165 184.410 1.00 18.21 ? 610  ALA A O      1 
ATOM   3525 C  CB     . ALA A 1 610  ? 187.416 149.053 186.964 1.00 18.21 ? 610  ALA A CB     1 
ATOM   3526 N  N      . LEU A 1 611  ? 187.741 147.512 184.130 1.00 18.72 ? 611  LEU A N      1 
ATOM   3527 C  CA     . LEU A 1 611  ? 187.612 147.490 182.675 1.00 18.72 ? 611  LEU A CA     1 
ATOM   3528 C  C      . LEU A 1 611  ? 186.734 146.336 182.208 1.00 18.72 ? 611  LEU A C      1 
ATOM   3529 O  O      . LEU A 1 611  ? 185.927 146.499 181.282 1.00 18.72 ? 611  LEU A O      1 
ATOM   3530 C  CB     . LEU A 1 611  ? 188.994 147.419 182.028 1.00 18.72 ? 611  LEU A CB     1 
ATOM   3531 C  CG     . LEU A 1 611  ? 189.817 148.699 182.115 1.00 18.72 ? 611  LEU A CG     1 
ATOM   3532 C  CD1    . LEU A 1 611  ? 191.252 148.420 181.774 1.00 18.72 ? 611  LEU A CD1    1 
ATOM   3533 C  CD2    . LEU A 1 611  ? 189.249 149.758 181.199 1.00 18.72 ? 611  LEU A CD2    1 
ATOM   3534 N  N      . MET A 1 612  ? 186.850 145.171 182.857 1.00 21.91 ? 612  MET A N      1 
ATOM   3535 C  CA     . MET A 1 612  ? 185.956 144.061 182.543 1.00 21.91 ? 612  MET A CA     1 
ATOM   3536 C  C      . MET A 1 612  ? 184.518 144.376 182.939 1.00 21.91 ? 612  MET A C      1 
ATOM   3537 O  O      . MET A 1 612  ? 183.582 144.011 182.221 1.00 21.91 ? 612  MET A O      1 
ATOM   3538 C  CB     . MET A 1 612  ? 186.432 142.786 183.234 1.00 21.91 ? 612  MET A CB     1 
ATOM   3539 C  CG     . MET A 1 612  ? 185.595 141.575 182.904 1.00 21.91 ? 612  MET A CG     1 
ATOM   3540 S  SD     . MET A 1 612  ? 186.139 140.035 183.639 1.00 21.91 ? 612  MET A SD     1 
ATOM   3541 C  CE     . MET A 1 612  ? 184.838 138.954 183.073 1.00 21.91 ? 612  MET A CE     1 
ATOM   3542 N  N      . ALA A 1 613  ? 184.328 145.075 184.060 1.00 20.18 ? 613  ALA A N      1 
ATOM   3543 C  CA     . ALA A 1 613  ? 182.995 145.483 184.481 1.00 20.18 ? 613  ALA A CA     1 
ATOM   3544 C  C      . ALA A 1 613  ? 182.384 146.477 183.508 1.00 20.18 ? 613  ALA A C      1 
ATOM   3545 O  O      . ALA A 1 613  ? 181.195 146.386 183.198 1.00 20.18 ? 613  ALA A O      1 
ATOM   3546 C  CB     . ALA A 1 613  ? 183.055 146.082 185.880 1.00 20.18 ? 613  ALA A CB     1 
ATOM   3547 N  N      . SER A 1 614  ? 183.183 147.423 183.012 1.00 21.01 ? 614  SER A N      1 
ATOM   3548 C  CA     . SER A 1 614  ? 182.690 148.379 182.029 1.00 21.01 ? 614  SER A CA     1 
ATOM   3549 C  C      . SER A 1 614  ? 182.309 147.687 180.729 1.00 21.01 ? 614  SER A C      1 
ATOM   3550 O  O      . SER A 1 614  ? 181.278 148.016 180.132 1.00 21.01 ? 614  SER A O      1 
ATOM   3551 C  CB     . SER A 1 614  ? 183.736 149.459 181.781 1.00 21.01 ? 614  SER A CB     1 
ATOM   3552 O  OG     . SER A 1 614  ? 184.880 148.916 181.157 1.00 21.01 ? 614  SER A OG     1 
ATOM   3553 N  N      . ARG A 1 615  ? 183.102 146.694 180.308 1.00 23.12 ? 615  ARG A N      1 
ATOM   3554 C  CA     . ARG A 1 615  ? 182.768 145.904 179.124 1.00 23.12 ? 615  ARG A CA     1 
ATOM   3555 C  C      . ARG A 1 615  ? 181.470 145.122 179.309 1.00 23.12 ? 615  ARG A C      1 
ATOM   3556 O  O      . ARG A 1 615  ? 180.597 145.147 178.434 1.00 23.12 ? 615  ARG A O      1 
ATOM   3557 C  CB     . ARG A 1 615  ? 183.922 144.963 178.793 1.00 23.12 ? 615  ARG A CB     1 
ATOM   3558 C  CG     . ARG A 1 615  ? 183.654 144.006 177.657 1.00 23.12 ? 615  ARG A CG     1 
ATOM   3559 C  CD     . ARG A 1 615  ? 183.499 144.668 176.329 1.00 23.12 ? 615  ARG A CD     1 
ATOM   3560 N  NE     . ARG A 1 615  ? 183.351 143.677 175.273 1.00 23.12 ? 615  ARG A NE     1 
ATOM   3561 C  CZ     . ARG A 1 615  ? 183.038 143.970 174.020 1.00 23.12 ? 615  ARG A CZ     1 
ATOM   3562 N  NH1    . ARG A 1 615  ? 182.839 145.228 173.666 1.00 23.12 ? 615  ARG A NH1    1 
ATOM   3563 N  NH2    . ARG A 1 615  ? 182.928 143.006 173.123 1.00 23.12 ? 615  ARG A NH2    1 
ATOM   3564 N  N      . LEU A 1 616  ? 181.326 144.435 180.452 1.00 23.61 ? 616  LEU A N      1 
ATOM   3565 C  CA     . LEU A 1 616  ? 180.103 143.699 180.785 1.00 23.61 ? 616  LEU A CA     1 
ATOM   3566 C  C      . LEU A 1 616  ? 178.876 144.597 180.807 1.00 23.61 ? 616  LEU A C      1 
ATOM   3567 O  O      . LEU A 1 616  ? 177.835 144.251 180.244 1.00 23.61 ? 616  LEU A O      1 
ATOM   3568 C  CB     . LEU A 1 616  ? 180.262 143.013 182.143 1.00 23.61 ? 616  LEU A CB     1 
ATOM   3569 C  CG     . LEU A 1 616  ? 180.631 141.542 182.307 1.00 23.61 ? 616  LEU A CG     1 
ATOM   3570 C  CD1    . LEU A 1 616  ? 181.900 141.236 181.680 1.00 23.61 ? 616  LEU A CD1    1 
ATOM   3571 C  CD2    . LEU A 1 616  ? 180.766 141.258 183.787 1.00 23.61 ? 616  LEU A CD2    1 
ATOM   3572 N  N      . LEU A 1 617  ? 178.988 145.766 181.435 1.00 23.52 ? 617  LEU A N      1 
ATOM   3573 C  CA     . LEU A 1 617  ? 177.830 146.632 181.610 1.00 23.52 ? 617  LEU A CA     1 
ATOM   3574 C  C      . LEU A 1 617  ? 177.424 147.304 180.308 1.00 23.52 ? 617  LEU A C      1 
ATOM   3575 O  O      . LEU A 1 617  ? 176.232 147.358 179.991 1.00 23.52 ? 617  LEU A O      1 
ATOM   3576 C  CB     . LEU A 1 617  ? 178.122 147.660 182.694 1.00 23.52 ? 617  LEU A CB     1 
ATOM   3577 C  CG     . LEU A 1 617  ? 178.134 147.023 184.075 1.00 23.52 ? 617  LEU A CG     1 
ATOM   3578 C  CD1    . LEU A 1 617  ? 178.846 147.892 185.048 1.00 23.52 ? 617  LEU A CD1    1 
ATOM   3579 C  CD2    . LEU A 1 617  ? 176.721 146.781 184.539 1.00 23.52 ? 617  LEU A CD2    1 
ATOM   3580 N  N      . LYS A 1 618  ? 178.379 147.792 179.514 1.00 25.41 ? 618  LYS A N      1 
ATOM   3581 C  CA     . LYS A 1 618  ? 177.943 148.394 178.261 1.00 25.41 ? 618  LYS A CA     1 
ATOM   3582 C  C      . LYS A 1 618  ? 177.584 147.354 177.213 1.00 25.41 ? 618  LYS A C      1 
ATOM   3583 O  O      . LYS A 1 618  ? 176.804 147.655 176.303 1.00 25.41 ? 618  LYS A O      1 
ATOM   3584 C  CB     . LYS A 1 618  ? 178.987 149.354 177.701 1.00 25.41 ? 618  LYS A CB     1 
ATOM   3585 C  CG     . LYS A 1 618  ? 180.234 148.732 177.174 1.00 25.41 ? 618  LYS A CG     1 
ATOM   3586 C  CD     . LYS A 1 618  ? 181.104 149.817 176.609 1.00 25.41 ? 618  LYS A CD     1 
ATOM   3587 C  CE     . LYS A 1 618  ? 181.590 150.733 177.709 1.00 25.41 ? 618  LYS A CE     1 
ATOM   3588 N  NZ     . LYS A 1 618  ? 182.552 151.727 177.181 1.00 25.41 ? 618  LYS A NZ     1 
ATOM   3589 N  N      . ARG A 1 619  ? 178.045 146.117 177.354 1.00 27.36 ? 619  ARG A N      1 
ATOM   3590 C  CA     . ARG A 1 619  ? 177.606 145.120 176.397 1.00 27.36 ? 619  ARG A CA     1 
ATOM   3591 C  C      . ARG A 1 619  ? 176.261 144.519 176.786 1.00 27.36 ? 619  ARG A C      1 
ATOM   3592 O  O      . ARG A 1 619  ? 175.471 144.175 175.902 1.00 27.36 ? 619  ARG A O      1 
ATOM   3593 C  CB     . ARG A 1 619  ? 178.698 144.064 176.229 1.00 27.36 ? 619  ARG A CB     1 
ATOM   3594 C  CG     . ARG A 1 619  ? 178.509 143.167 175.032 1.00 27.36 ? 619  ARG A CG     1 
ATOM   3595 C  CD     . ARG A 1 619  ? 179.799 142.459 174.685 1.00 27.36 ? 619  ARG A CD     1 
ATOM   3596 N  NE     . ARG A 1 619  ? 179.617 141.389 173.711 1.00 27.36 ? 619  ARG A NE     1 
ATOM   3597 C  CZ     . ARG A 1 619  ? 179.621 141.561 172.399 1.00 27.36 ? 619  ARG A CZ     1 
ATOM   3598 N  NH1    . ARG A 1 619  ? 179.790 142.768 171.889 1.00 27.36 ? 619  ARG A NH1    1 
ATOM   3599 N  NH2    . ARG A 1 619  ? 179.451 140.523 171.599 1.00 27.36 ? 619  ARG A NH2    1 
ATOM   3600 N  N      . MET A 1 620  ? 175.940 144.467 178.085 1.00 29.28 ? 620  MET A N      1 
ATOM   3601 C  CA     . MET A 1 620  ? 174.553 144.268 178.500 1.00 29.28 ? 620  MET A CA     1 
ATOM   3602 C  C      . MET A 1 620  ? 173.666 145.426 178.084 1.00 29.28 ? 620  MET A C      1 
ATOM   3603 O  O      . MET A 1 620  ? 172.481 145.223 177.822 1.00 29.28 ? 620  MET A O      1 
ATOM   3604 C  CB     . MET A 1 620  ? 174.442 144.088 180.010 1.00 29.28 ? 620  MET A CB     1 
ATOM   3605 C  CG     . MET A 1 620  ? 174.867 142.747 180.511 1.00 29.28 ? 620  MET A CG     1 
ATOM   3606 S  SD     . MET A 1 620  ? 174.539 142.508 182.258 1.00 29.28 ? 620  MET A SD     1 
ATOM   3607 C  CE     . MET A 1 620  ? 175.834 143.505 182.965 1.00 29.28 ? 620  MET A CE     1 
ATOM   3608 N  N      . ALA A 1 621  ? 174.209 146.643 178.050 1.00 30.84 ? 621  ALA A N      1 
ATOM   3609 C  CA     . ALA A 1 621  ? 173.440 147.782 177.568 1.00 30.84 ? 621  ALA A CA     1 
ATOM   3610 C  C      . ALA A 1 621  ? 173.110 147.640 176.091 1.00 30.84 ? 621  ALA A C      1 
ATOM   3611 O  O      . ALA A 1 621  ? 171.969 147.882 175.682 1.00 30.84 ? 621  ALA A O      1 
ATOM   3612 C  CB     . ALA A 1 621  ? 174.212 149.070 177.825 1.00 30.84 ? 621  ALA A CB     1 
ATOM   3613 N  N      . SER A 1 622  ? 174.088 147.219 175.286 1.00 33.26 ? 622  SER A N      1 
ATOM   3614 C  CA     . SER A 1 622  ? 173.832 146.955 173.873 1.00 33.26 ? 622  SER A CA     1 
ATOM   3615 C  C      . SER A 1 622  ? 172.864 145.792 173.695 1.00 33.26 ? 622  SER A C      1 
ATOM   3616 O  O      . SER A 1 622  ? 172.005 145.824 172.808 1.00 33.26 ? 622  SER A O      1 
ATOM   3617 C  CB     . SER A 1 622  ? 175.141 146.669 173.144 1.00 33.26 ? 622  SER A CB     1 
ATOM   3618 O  OG     . SER A 1 622  ? 175.689 145.432 173.554 1.00 33.26 ? 622  SER A OG     1 
ATOM   3619 N  N      . ARG A 1 623  ? 172.965 144.779 174.559 1.00 37.34 ? 623  ARG A N      1 
ATOM   3620 C  CA     . ARG A 1 623  ? 172.086 143.618 174.475 1.00 37.34 ? 623  ARG A CA     1 
ATOM   3621 C  C      . ARG A 1 623  ? 170.649 143.972 174.843 1.00 37.34 ? 623  ARG A C      1 
ATOM   3622 O  O      . ARG A 1 623  ? 169.710 143.545 174.168 1.00 37.34 ? 623  ARG A O      1 
ATOM   3623 C  CB     . ARG A 1 623  ? 172.620 142.509 175.380 1.00 37.34 ? 623  ARG A CB     1 
ATOM   3624 C  CG     . ARG A 1 623  ? 171.843 141.225 175.318 1.00 37.34 ? 623  ARG A CG     1 
ATOM   3625 C  CD     . ARG A 1 623  ? 171.961 140.610 173.939 1.00 37.34 ? 623  ARG A CD     1 
ATOM   3626 N  NE     . ARG A 1 623  ? 171.222 139.357 173.833 1.00 37.34 ? 623  ARG A NE     1 
ATOM   3627 C  CZ     . ARG A 1 623  ? 171.751 138.164 174.072 1.00 37.34 ? 623  ARG A CZ     1 
ATOM   3628 N  NH1    . ARG A 1 623  ? 173.025 138.061 174.420 1.00 37.34 ? 623  ARG A NH1    1 
ATOM   3629 N  NH2    . ARG A 1 623  ? 171.009 137.073 173.954 1.00 37.34 ? 623  ARG A NH2    1 
ATOM   3630 N  N      . ALA A 1 624  ? 170.457 144.759 175.903 1.00 37.58 ? 624  ALA A N      1 
ATOM   3631 C  CA     . ALA A 1 624  ? 169.128 145.198 176.306 1.00 37.58 ? 624  ALA A CA     1 
ATOM   3632 C  C      . ALA A 1 624  ? 168.556 146.245 175.366 1.00 37.58 ? 624  ALA A C      1 
ATOM   3633 O  O      . ALA A 1 624  ? 167.334 146.408 175.311 1.00 37.58 ? 624  ALA A O      1 
ATOM   3634 C  CB     . ALA A 1 624  ? 169.167 145.755 177.727 1.00 37.58 ? 624  ALA A CB     1 
ATOM   3635 N  N      . GLN A 1 625  ? 169.408 146.963 174.637 1.00 38.47 ? 625  GLN A N      1 
ATOM   3636 C  CA     . GLN A 1 625  ? 168.923 147.914 173.649 1.00 38.47 ? 625  GLN A CA     1 
ATOM   3637 C  C      . GLN A 1 625  ? 168.507 147.214 172.361 1.00 38.47 ? 625  GLN A C      1 
ATOM   3638 O  O      . GLN A 1 625  ? 167.542 147.629 171.711 1.00 38.47 ? 625  GLN A O      1 
ATOM   3639 C  CB     . GLN A 1 625  ? 170.005 148.959 173.379 1.00 38.47 ? 625  GLN A CB     1 
ATOM   3640 C  CG     . GLN A 1 625  ? 169.594 150.106 172.486 1.00 38.47 ? 625  GLN A CG     1 
ATOM   3641 C  CD     . GLN A 1 625  ? 170.707 151.116 172.317 1.00 38.47 ? 625  GLN A CD     1 
ATOM   3642 O  OE1    . GLN A 1 625  ? 171.809 150.930 172.831 1.00 38.47 ? 625  GLN A OE1    1 
ATOM   3643 N  NE2    . GLN A 1 625  ? 170.424 152.197 171.599 1.00 38.47 ? 625  GLN A NE2    1 
ATOM   3644 N  N      . GLU A 1 626  ? 169.207 146.144 171.984 1.00 41.32 ? 626  GLU A N      1 
ATOM   3645 C  CA     . GLU A 1 626  ? 168.927 145.461 170.728 1.00 41.32 ? 626  GLU A CA     1 
ATOM   3646 C  C      . GLU A 1 626  ? 167.857 144.384 170.847 1.00 41.32 ? 626  GLU A C      1 
ATOM   3647 O  O      . GLU A 1 626  ? 167.429 143.850 169.819 1.00 41.32 ? 626  GLU A O      1 
ATOM   3648 C  CB     . GLU A 1 626  ? 170.202 144.821 170.171 1.00 41.32 ? 626  GLU A CB     1 
ATOM   3649 C  CG     . GLU A 1 626  ? 170.648 143.574 170.919 1.00 41.32 ? 626  GLU A CG     1 
ATOM   3650 C  CD     . GLU A 1 626  ? 172.012 143.086 170.472 1.00 41.32 ? 626  GLU A CD     1 
ATOM   3651 O  OE1    . GLU A 1 626  ? 172.629 143.750 169.614 1.00 41.32 ? 626  GLU A OE1    1 
ATOM   3652 O  OE2    . GLU A 1 626  ? 172.470 142.043 170.982 1.00 41.32 ? 626  GLU A OE2    1 
ATOM   3653 N  N      . ASP A 1 627  ? 167.417 144.047 172.055 1.00 43.53 ? 627  ASP A N      1 
ATOM   3654 C  CA     . ASP A 1 627  ? 166.501 142.935 172.268 1.00 43.53 ? 627  ASP A CA     1 
ATOM   3655 C  C      . ASP A 1 627  ? 165.225 143.424 172.937 1.00 43.53 ? 627  ASP A C      1 
ATOM   3656 O  O      . ASP A 1 627  ? 165.271 144.235 173.868 1.00 43.53 ? 627  ASP A O      1 
ATOM   3657 C  CB     . ASP A 1 627  ? 167.155 141.851 173.123 1.00 43.53 ? 627  ASP A CB     1 
ATOM   3658 C  CG     . ASP A 1 627  ? 166.336 140.591 173.192 1.00 43.53 ? 627  ASP A CG     1 
ATOM   3659 O  OD1    . ASP A 1 627  ? 166.315 139.840 172.195 1.00 43.53 ? 627  ASP A OD1    1 
ATOM   3660 O  OD2    . ASP A 1 627  ? 165.718 140.348 174.246 1.00 43.53 ? 627  ASP A OD2    1 
ATOM   3661 N  N      . ASN A 1 628  ? 164.084 142.924 172.460 1.00 45.25 ? 628  ASN A N      1 
ATOM   3662 C  CA     . ASN A 1 628  ? 162.792 143.308 173.012 1.00 45.25 ? 628  ASN A CA     1 
ATOM   3663 C  C      . ASN A 1 628  ? 162.375 142.465 174.206 1.00 45.25 ? 628  ASN A C      1 
ATOM   3664 O  O      . ASN A 1 628  ? 161.569 142.929 175.020 1.00 45.25 ? 628  ASN A O      1 
ATOM   3665 C  CB     . ASN A 1 628  ? 161.706 143.225 171.937 1.00 45.25 ? 628  ASN A CB     1 
ATOM   3666 C  CG     . ASN A 1 628  ? 161.830 144.319 170.904 1.00 45.25 ? 628  ASN A CG     1 
ATOM   3667 O  OD1    . ASN A 1 628  ? 162.095 145.473 171.235 1.00 45.25 ? 628  ASN A OD1    1 
ATOM   3668 N  ND2    . ASN A 1 628  ? 161.641 143.962 169.641 1.00 45.25 ? 628  ASN A ND2    1 
ATOM   3669 N  N      . THR A 1 629  ? 162.901 141.250 174.335 1.00 42.89 ? 629  THR A N      1 
ATOM   3670 C  CA     . THR A 1 629  ? 162.605 140.404 175.483 1.00 42.89 ? 629  THR A CA     1 
ATOM   3671 C  C      . THR A 1 629  ? 163.449 140.743 176.706 1.00 42.89 ? 629  THR A C      1 
ATOM   3672 O  O      . THR A 1 629  ? 163.315 140.074 177.734 1.00 42.89 ? 629  THR A O      1 
ATOM   3673 C  CB     . THR A 1 629  ? 162.797 138.931 175.115 1.00 42.89 ? 629  THR A CB     1 
ATOM   3674 O  OG1    . THR A 1 629  ? 164.158 138.708 174.731 1.00 42.89 ? 629  THR A OG1    1 
ATOM   3675 C  CG2    . THR A 1 629  ? 161.888 138.550 173.960 1.00 42.89 ? 629  THR A CG2    1 
ATOM   3676 N  N      . ILE A 1 630  ? 164.313 141.751 176.621 1.00 40.28 ? 630  ILE A N      1 
ATOM   3677 C  CA     . ILE A 1 630  ? 165.079 142.246 177.757 1.00 40.28 ? 630  ILE A CA     1 
ATOM   3678 C  C      . ILE A 1 630  ? 164.699 143.704 177.968 1.00 40.28 ? 630  ILE A C      1 
ATOM   3679 O  O      . ILE A 1 630  ? 164.676 144.485 177.010 1.00 40.28 ? 630  ILE A O      1 
ATOM   3680 C  CB     . ILE A 1 630  ? 166.595 142.093 177.533 1.00 40.28 ? 630  ILE A CB     1 
ATOM   3681 C  CG1    . ILE A 1 630  ? 166.957 140.622 177.351 1.00 40.28 ? 630  ILE A CG1    1 
ATOM   3682 C  CG2    . ILE A 1 630  ? 167.365 142.631 178.709 1.00 40.28 ? 630  ILE A CG2    1 
ATOM   3683 C  CD1    . ILE A 1 630  ? 168.368 140.397 176.884 1.00 40.28 ? 630  ILE A CD1    1 
ATOM   3684 N  N      . THR A 1 631  ? 164.381 144.056 179.216 1.00 37.82 ? 631  THR A N      1 
ATOM   3685 C  CA     . THR A 1 631  ? 163.930 145.401 179.556 1.00 37.82 ? 631  THR A CA     1 
ATOM   3686 C  C      . THR A 1 631  ? 165.045 146.415 179.330 1.00 37.82 ? 631  THR A C      1 
ATOM   3687 O  O      . THR A 1 631  ? 166.172 146.228 179.796 1.00 37.82 ? 631  THR A O      1 
ATOM   3688 C  CB     . THR A 1 631  ? 163.466 145.442 181.012 1.00 37.82 ? 631  THR A CB     1 
ATOM   3689 O  OG1    . THR A 1 631  ? 162.405 144.499 181.199 1.00 37.82 ? 631  THR A OG1    1 
ATOM   3690 C  CG2    . THR A 1 631  ? 162.966 146.828 181.390 1.00 37.82 ? 631  THR A CG2    1 
ATOM   3691 N  N      . ASP A 1 632  ? 164.730 147.487 178.605 1.00 36.64 ? 632  ASP A N      1 
ATOM   3692 C  CA     . ASP A 1 632  ? 165.734 148.479 178.247 1.00 36.64 ? 632  ASP A CA     1 
ATOM   3693 C  C      . ASP A 1 632  ? 166.119 149.332 179.446 1.00 36.64 ? 632  ASP A C      1 
ATOM   3694 O  O      . ASP A 1 632  ? 165.534 150.392 179.686 1.00 36.64 ? 632  ASP A O      1 
ATOM   3695 C  CB     . ASP A 1 632  ? 165.234 149.368 177.111 1.00 36.64 ? 632  ASP A CB     1 
ATOM   3696 C  CG     . ASP A 1 632  ? 166.306 150.300 176.593 1.00 36.64 ? 632  ASP A CG     1 
ATOM   3697 O  OD1    . ASP A 1 632  ? 167.207 149.825 175.873 1.00 36.64 ? 632  ASP A OD1    1 
ATOM   3698 O  OD2    . ASP A 1 632  ? 166.255 151.506 176.911 1.00 36.64 ? 632  ASP A OD2    1 
ATOM   3699 N  N      . ILE A 1 633  ? 167.116 148.871 180.194 1.00 35.19 ? 633  ILE A N      1 
ATOM   3700 C  CA     . ILE A 1 633  ? 167.697 149.613 181.305 1.00 35.19 ? 633  ILE A CA     1 
ATOM   3701 C  C      . ILE A 1 633  ? 169.060 150.117 180.854 1.00 35.19 ? 633  ILE A C      1 
ATOM   3702 O  O      . ILE A 1 633  ? 169.982 150.270 181.663 1.00 35.19 ? 633  ILE A O      1 
ATOM   3703 C  CB     . ILE A 1 633  ? 167.787 148.749 182.576 1.00 35.19 ? 633  ILE A CB     1 
ATOM   3704 C  CG1    . ILE A 1 633  ? 168.537 147.443 182.298 1.00 35.19 ? 633  ILE A CG1    1 
ATOM   3705 C  CG2    . ILE A 1 633  ? 166.401 148.466 183.120 1.00 35.19 ? 633  ILE A CG2    1 
ATOM   3706 C  CD1    . ILE A 1 633  ? 168.881 146.663 183.542 1.00 35.19 ? 633  ILE A CD1    1 
ATOM   3707 N  N      . SER A 1 634  ? 169.176 150.381 179.547 1.00 33.71 ? 634  SER A N      1 
ATOM   3708 C  CA     . SER A 1 634  ? 170.461 150.648 178.910 1.00 33.71 ? 634  SER A CA     1 
ATOM   3709 C  C      . SER A 1 634  ? 171.119 151.925 179.413 1.00 33.71 ? 634  SER A C      1 
ATOM   3710 O  O      . SER A 1 634  ? 172.348 152.006 179.441 1.00 33.71 ? 634  SER A O      1 
ATOM   3711 C  CB     . SER A 1 634  ? 170.280 150.723 177.397 1.00 33.71 ? 634  SER A CB     1 
ATOM   3712 O  OG     . SER A 1 634  ? 169.867 149.476 176.877 1.00 33.71 ? 634  SER A OG     1 
ATOM   3713 N  N      . SER A 1 635  ? 170.333 152.922 179.815 1.00 31.97 ? 635  SER A N      1 
ATOM   3714 C  CA     . SER A 1 635  ? 170.920 154.163 180.311 1.00 31.97 ? 635  SER A CA     1 
ATOM   3715 C  C      . SER A 1 635  ? 171.594 153.954 181.661 1.00 31.97 ? 635  SER A C      1 
ATOM   3716 O  O      . SER A 1 635  ? 172.699 154.459 181.895 1.00 31.97 ? 635  SER A O      1 
ATOM   3717 C  CB     . SER A 1 635  ? 169.846 155.245 180.405 1.00 31.97 ? 635  SER A CB     1 
ATOM   3718 O  OG     . SER A 1 635  ? 169.313 155.538 179.127 1.00 31.97 ? 635  SER A OG     1 
ATOM   3719 N  N      . ASP A 1 636  ? 170.956 153.181 182.545 1.00 30.48 ? 636  ASP A N      1 
ATOM   3720 C  CA     . ASP A 1 636  ? 171.557 152.829 183.827 1.00 30.48 ? 636  ASP A CA     1 
ATOM   3721 C  C      . ASP A 1 636  ? 172.793 151.960 183.635 1.00 30.48 ? 636  ASP A C      1 
ATOM   3722 O  O      . ASP A 1 636  ? 173.786 152.113 184.354 1.00 30.48 ? 636  ASP A O      1 
ATOM   3723 C  CB     . ASP A 1 636  ? 170.522 152.113 184.697 1.00 30.48 ? 636  ASP A CB     1 
ATOM   3724 C  CG     . ASP A 1 636  ? 171.007 151.874 186.112 1.00 30.48 ? 636  ASP A CG     1 
ATOM   3725 O  OD1    . ASP A 1 636  ? 171.048 152.841 186.901 1.00 30.48 ? 636  ASP A OD1    1 
ATOM   3726 O  OD2    . ASP A 1 636  ? 171.344 150.717 186.440 1.00 30.48 ? 636  ASP A OD2    1 
ATOM   3727 N  N      . LEU A 1 637  ? 172.763 151.075 182.636 1.00 29.00 ? 637  LEU A N      1 
ATOM   3728 C  CA     . LEU A 1 637  ? 173.903 150.206 182.365 1.00 29.00 ? 637  LEU A CA     1 
ATOM   3729 C  C      . LEU A 1 637  ? 175.083 150.983 181.790 1.00 29.00 ? 637  LEU A C      1 
ATOM   3730 O  O      . LEU A 1 637  ? 176.231 150.739 182.176 1.00 29.00 ? 637  LEU A O      1 
ATOM   3731 C  CB     . LEU A 1 637  ? 173.479 149.076 181.431 1.00 29.00 ? 637  LEU A CB     1 
ATOM   3732 C  CG     . LEU A 1 637  ? 172.562 147.999 182.009 1.00 29.00 ? 637  LEU A CG     1 
ATOM   3733 C  CD1    . LEU A 1 637  ? 172.019 147.100 180.931 1.00 29.00 ? 637  LEU A CD1    1 
ATOM   3734 C  CD2    . LEU A 1 637  ? 173.344 147.176 182.986 1.00 29.00 ? 637  LEU A CD2    1 
ATOM   3735 N  N      . TYR A 1 638  ? 174.829 151.939 180.890 1.00 29.31 ? 638  TYR A N      1 
ATOM   3736 C  CA     . TYR A 1 638  ? 175.923 152.771 180.396 1.00 29.31 ? 638  TYR A CA     1 
ATOM   3737 C  C      . TYR A 1 638  ? 176.445 153.724 181.461 1.00 29.31 ? 638  TYR A C      1 
ATOM   3738 O  O      . TYR A 1 638  ? 177.639 154.038 181.465 1.00 29.31 ? 638  TYR A O      1 
ATOM   3739 C  CB     . TYR A 1 638  ? 175.518 153.574 179.159 1.00 29.31 ? 638  TYR A CB     1 
ATOM   3740 C  CG     . TYR A 1 638  ? 175.440 152.790 177.872 1.00 29.31 ? 638  TYR A CG     1 
ATOM   3741 C  CD1    . TYR A 1 638  ? 176.568 152.171 177.351 1.00 29.31 ? 638  TYR A CD1    1 
ATOM   3742 C  CD2    . TYR A 1 638  ? 174.276 152.777 177.110 1.00 29.31 ? 638  TYR A CD2    1 
ATOM   3743 C  CE1    . TYR A 1 638  ? 176.513 151.478 176.161 1.00 29.31 ? 638  TYR A CE1    1 
ATOM   3744 C  CE2    . TYR A 1 638  ? 174.214 152.091 175.915 1.00 29.31 ? 638  TYR A CE2    1 
ATOM   3745 C  CZ     . TYR A 1 638  ? 175.337 151.444 175.446 1.00 29.31 ? 638  TYR A CZ     1 
ATOM   3746 O  OH     . TYR A 1 638  ? 175.288 150.759 174.254 1.00 29.31 ? 638  TYR A OH     1 
ATOM   3747 N  N      . ASP A 1 639  ? 175.583 154.187 182.369 1.00 27.24 ? 639  ASP A N      1 
ATOM   3748 C  CA     . ASP A 1 639  ? 176.056 155.023 183.467 1.00 27.24 ? 639  ASP A CA     1 
ATOM   3749 C  C      . ASP A 1 639  ? 176.939 154.227 184.421 1.00 27.24 ? 639  ASP A C      1 
ATOM   3750 O  O      . ASP A 1 639  ? 177.976 154.723 184.882 1.00 27.24 ? 639  ASP A O      1 
ATOM   3751 C  CB     . ASP A 1 639  ? 174.864 155.628 184.203 1.00 27.24 ? 639  ASP A CB     1 
ATOM   3752 C  CG     . ASP A 1 639  ? 175.276 156.642 185.244 1.00 27.24 ? 639  ASP A CG     1 
ATOM   3753 O  OD1    . ASP A 1 639  ? 175.687 157.756 184.858 1.00 27.24 ? 639  ASP A OD1    1 
ATOM   3754 O  OD2    . ASP A 1 639  ? 175.183 156.331 186.450 1.00 27.24 ? 639  ASP A OD2    1 
ATOM   3755 N  N      . HIS A 1 640  ? 176.568 152.972 184.680 1.00 24.51 ? 640  HIS A N      1 
ATOM   3756 C  CA     . HIS A 1 640  ? 177.370 152.096 185.526 1.00 24.51 ? 640  HIS A CA     1 
ATOM   3757 C  C      . HIS A 1 640  ? 178.697 151.748 184.857 1.00 24.51 ? 640  HIS A C      1 
ATOM   3758 O  O      . HIS A 1 640  ? 179.745 151.689 185.519 1.00 24.51 ? 640  HIS A O      1 
ATOM   3759 C  CB     . HIS A 1 640  ? 176.544 150.847 185.833 1.00 24.51 ? 640  HIS A CB     1 
ATOM   3760 C  CG     . HIS A 1 640  ? 177.004 150.074 187.026 1.00 24.51 ? 640  HIS A CG     1 
ATOM   3761 N  ND1    . HIS A 1 640  ? 176.473 148.848 187.354 1.00 24.51 ? 640  HIS A ND1    1 
ATOM   3762 C  CD2    . HIS A 1 640  ? 177.940 150.342 187.964 1.00 24.51 ? 640  HIS A CD2    1 
ATOM   3763 C  CE1    . HIS A 1 640  ? 177.056 148.396 188.447 1.00 24.51 ? 640  HIS A CE1    1 
ATOM   3764 N  NE2    . HIS A 1 640  ? 177.943 149.289 188.843 1.00 24.51 ? 640  HIS A NE2    1 
ATOM   3765 N  N      . ALA A 1 641  ? 178.674 151.548 183.536 1.00 23.71 ? 641  ALA A N      1 
ATOM   3766 C  CA     . ALA A 1 641  ? 179.896 151.249 182.798 1.00 23.71 ? 641  ALA A CA     1 
ATOM   3767 C  C      . ALA A 1 641  ? 180.831 152.448 182.756 1.00 23.71 ? 641  ALA A C      1 
ATOM   3768 O  O      . ALA A 1 641  ? 182.049 152.287 182.862 1.00 23.71 ? 641  ALA A O      1 
ATOM   3769 C  CB     . ALA A 1 641  ? 179.561 150.798 181.381 1.00 23.71 ? 641  ALA A CB     1 
ATOM   3770 N  N      . ARG A 1 642  ? 180.279 153.654 182.594 1.00 23.94 ? 642  ARG A N      1 
ATOM   3771 C  CA     . ARG A 1 642  ? 181.075 154.875 182.657 1.00 23.94 ? 642  ARG A CA     1 
ATOM   3772 C  C      . ARG A 1 642  ? 181.667 155.069 184.047 1.00 23.94 ? 642  ARG A C      1 
ATOM   3773 O  O      . ARG A 1 642  ? 182.791 155.572 184.185 1.00 23.94 ? 642  ARG A O      1 
ATOM   3774 C  CB     . ARG A 1 642  ? 180.189 156.059 182.245 1.00 23.94 ? 642  ARG A CB     1 
ATOM   3775 C  CG     . ARG A 1 642  ? 180.859 157.418 182.010 1.00 23.94 ? 642  ARG A CG     1 
ATOM   3776 C  CD     . ARG A 1 642  ? 180.816 158.271 183.271 1.00 23.94 ? 642  ARG A CD     1 
ATOM   3777 N  NE     . ARG A 1 642  ? 179.460 158.337 183.802 1.00 23.94 ? 642  ARG A NE     1 
ATOM   3778 C  CZ     . ARG A 1 642  ? 179.172 158.577 185.075 1.00 23.94 ? 642  ARG A CZ     1 
ATOM   3779 N  NH1    . ARG A 1 642  ? 180.148 158.762 185.951 1.00 23.94 ? 642  ARG A NH1    1 
ATOM   3780 N  NH2    . ARG A 1 642  ? 177.909 158.614 185.474 1.00 23.94 ? 642  ARG A NH2    1 
ATOM   3781 N  N      . LEU A 1 643  ? 180.926 154.660 185.078 1.00 21.72 ? 643  LEU A N      1 
ATOM   3782 C  CA     . LEU A 1 643  ? 181.426 154.717 186.445 1.00 21.72 ? 643  LEU A CA     1 
ATOM   3783 C  C      . LEU A 1 643  ? 182.624 153.792 186.644 1.00 21.72 ? 643  LEU A C      1 
ATOM   3784 O  O      . LEU A 1 643  ? 183.628 154.183 187.249 1.00 21.72 ? 643  LEU A O      1 
ATOM   3785 C  CB     . LEU A 1 643  ? 180.280 154.367 187.394 1.00 21.72 ? 643  LEU A CB     1 
ATOM   3786 C  CG     . LEU A 1 643  ? 180.396 154.511 188.903 1.00 21.72 ? 643  LEU A CG     1 
ATOM   3787 C  CD1    . LEU A 1 643  ? 180.669 155.952 189.267 1.00 21.72 ? 643  LEU A CD1    1 
ATOM   3788 C  CD2    . LEU A 1 643  ? 179.095 154.052 189.521 1.00 21.72 ? 643  LEU A CD2    1 
ATOM   3789 N  N      . PHE A 1 644  ? 182.559 152.571 186.110 1.00 19.85 ? 644  PHE A N      1 
ATOM   3790 C  CA     . PHE A 1 644  ? 183.730 151.698 186.215 1.00 19.85 ? 644  PHE A CA     1 
ATOM   3791 C  C      . PHE A 1 644  ? 184.866 152.113 185.291 1.00 19.85 ? 644  PHE A C      1 
ATOM   3792 O  O      . PHE A 1 644  ? 186.034 151.850 185.603 1.00 19.85 ? 644  PHE A O      1 
ATOM   3793 C  CB     . PHE A 1 644  ? 183.360 150.244 185.971 1.00 19.85 ? 644  PHE A CB     1 
ATOM   3794 C  CG     . PHE A 1 644  ? 182.864 149.563 187.187 1.00 19.85 ? 644  PHE A CG     1 
ATOM   3795 C  CD1    . PHE A 1 644  ? 183.749 149.208 188.186 1.00 19.85 ? 644  PHE A CD1    1 
ATOM   3796 C  CD2    . PHE A 1 644  ? 181.531 149.266 187.343 1.00 19.85 ? 644  PHE A CD2    1 
ATOM   3797 C  CE1    . PHE A 1 644  ? 183.310 148.591 189.319 1.00 19.85 ? 644  PHE A CE1    1 
ATOM   3798 C  CE2    . PHE A 1 644  ? 181.095 148.631 188.476 1.00 19.85 ? 644  PHE A CE2    1 
ATOM   3799 C  CZ     . PHE A 1 644  ? 181.986 148.303 189.463 1.00 19.85 ? 644  PHE A CZ     1 
ATOM   3800 N  N      . GLU A 1 645  ? 184.555 152.778 184.177 1.00 21.72 ? 645  GLU A N      1 
ATOM   3801 C  CA     . GLU A 1 645  ? 185.601 153.368 183.351 1.00 21.72 ? 645  GLU A CA     1 
ATOM   3802 C  C      . GLU A 1 645  ? 186.375 154.425 184.119 1.00 21.72 ? 645  GLU A C      1 
ATOM   3803 O  O      . GLU A 1 645  ? 187.608 154.418 184.114 1.00 21.72 ? 645  GLU A O      1 
ATOM   3804 C  CB     . GLU A 1 645  ? 185.015 153.969 182.076 1.00 21.72 ? 645  GLU A CB     1 
ATOM   3805 C  CG     . GLU A 1 645  ? 184.663 152.954 181.020 1.00 21.72 ? 645  GLU A CG     1 
ATOM   3806 C  CD     . GLU A 1 645  ? 184.069 153.584 179.784 1.00 21.72 ? 645  GLU A CD     1 
ATOM   3807 O  OE1    . GLU A 1 645  ? 183.784 154.798 179.806 1.00 21.72 ? 645  GLU A OE1    1 
ATOM   3808 O  OE2    . GLU A 1 645  ? 183.897 152.864 178.783 1.00 21.72 ? 645  GLU A OE2    1 
ATOM   3809 N  N      . GLU A 1 646  ? 185.672 155.322 184.816 1.00 20.93 ? 646  GLU A N      1 
ATOM   3810 C  CA     . GLU A 1 646  ? 186.387 156.367 185.541 1.00 20.93 ? 646  GLU A CA     1 
ATOM   3811 C  C      . GLU A 1 646  ? 187.078 155.819 186.785 1.00 20.93 ? 646  GLU A C      1 
ATOM   3812 O  O      . GLU A 1 646  ? 188.112 156.356 187.192 1.00 20.93 ? 646  GLU A O      1 
ATOM   3813 C  CB     . GLU A 1 646  ? 185.460 157.535 185.889 1.00 20.93 ? 646  GLU A CB     1 
ATOM   3814 C  CG     . GLU A 1 646  ? 184.423 157.290 186.954 1.00 20.93 ? 646  GLU A CG     1 
ATOM   3815 C  CD     . GLU A 1 646  ? 183.514 158.484 187.152 1.00 20.93 ? 646  GLU A CD     1 
ATOM   3816 O  OE1    . GLU A 1 646  ? 183.699 159.492 186.437 1.00 20.93 ? 646  GLU A OE1    1 
ATOM   3817 O  OE2    . GLU A 1 646  ? 182.613 158.417 188.013 1.00 20.93 ? 646  GLU A OE2    1 
ATOM   3818 N  N      . ARG A 1 647  ? 186.566 154.723 187.361 1.00 20.18 ? 647  ARG A N      1 
ATOM   3819 C  CA     . ARG A 1 647  ? 187.298 154.044 188.432 1.00 20.18 ? 647  ARG A CA     1 
ATOM   3820 C  C      . ARG A 1 647  ? 188.608 153.446 187.930 1.00 20.18 ? 647  ARG A C      1 
ATOM   3821 O  O      . ARG A 1 647  ? 189.645 153.574 188.593 1.00 20.18 ? 647  ARG A O      1 
ATOM   3822 C  CB     . ARG A 1 647  ? 186.424 152.963 189.066 1.00 20.18 ? 647  ARG A CB     1 
ATOM   3823 C  CG     . ARG A 1 647  ? 185.327 153.517 189.927 1.00 20.18 ? 647  ARG A CG     1 
ATOM   3824 C  CD     . ARG A 1 647  ? 184.350 152.459 190.356 1.00 20.18 ? 647  ARG A CD     1 
ATOM   3825 N  NE     . ARG A 1 647  ? 183.235 153.067 191.064 1.00 20.18 ? 647  ARG A NE     1 
ATOM   3826 C  CZ     . ARG A 1 647  ? 182.124 152.429 191.397 1.00 20.18 ? 647  ARG A CZ     1 
ATOM   3827 N  NH1    . ARG A 1 647  ? 181.967 151.160 191.070 1.00 20.18 ? 647  ARG A NH1    1 
ATOM   3828 N  NH2    . ARG A 1 647  ? 181.161 153.069 192.039 1.00 20.18 ? 647  ARG A NH2    1 
ATOM   3829 N  N      . ALA A 1 648  ? 188.586 152.820 186.748 1.00 18.76 ? 648  ALA A N      1 
ATOM   3830 C  CA     . ALA A 1 648  ? 189.811 152.266 186.174 1.00 18.76 ? 648  ALA A CA     1 
ATOM   3831 C  C      . ALA A 1 648  ? 190.800 153.360 185.794 1.00 18.76 ? 648  ALA A C      1 
ATOM   3832 O  O      . ALA A 1 648  ? 192.009 153.208 186.009 1.00 18.76 ? 648  ALA A O      1 
ATOM   3833 C  CB     . ALA A 1 648  ? 189.479 151.407 184.957 1.00 18.76 ? 648  ALA A CB     1 
ATOM   3834 N  N      . VAL A 1 649  ? 190.302 154.472 185.240 1.00 19.28 ? 649  VAL A N      1 
ATOM   3835 C  CA     . VAL A 1 649  ? 191.158 155.604 184.889 1.00 19.28 ? 649  VAL A CA     1 
ATOM   3836 C  C      . VAL A 1 649  ? 191.770 156.226 186.137 1.00 19.28 ? 649  VAL A C      1 
ATOM   3837 O  O      . VAL A 1 649  ? 192.941 156.612 186.136 1.00 19.28 ? 649  VAL A O      1 
ATOM   3838 C  CB     . VAL A 1 649  ? 190.362 156.638 184.068 1.00 19.28 ? 649  VAL A CB     1 
ATOM   3839 C  CG1    . VAL A 1 649  ? 191.161 157.903 183.824 1.00 19.28 ? 649  VAL A CG1    1 
ATOM   3840 C  CG2    . VAL A 1 649  ? 189.997 156.070 182.757 1.00 19.28 ? 649  VAL A CG2    1 
ATOM   3841 N  N      . GLY A 1 650  ? 191.011 156.295 187.231 1.00 19.90 ? 650  GLY A N      1 
ATOM   3842 C  CA     . GLY A 1 650  ? 191.551 156.867 188.449 1.00 19.90 ? 650  GLY A CA     1 
ATOM   3843 C  C      . GLY A 1 650  ? 192.593 155.987 189.107 1.00 19.90 ? 650  GLY A C      1 
ATOM   3844 O  O      . GLY A 1 650  ? 193.588 156.486 189.643 1.00 19.90 ? 650  GLY A O      1 
ATOM   3845 N  N      . VAL A 1 651  ? 192.391 154.666 189.057 1.00 19.89 ? 651  VAL A N      1 
ATOM   3846 C  CA     . VAL A 1 651  ? 193.425 153.738 189.515 1.00 19.89 ? 651  VAL A CA     1 
ATOM   3847 C  C      . VAL A 1 651  ? 194.680 153.865 188.659 1.00 19.89 ? 651  VAL A C      1 
ATOM   3848 O  O      . VAL A 1 651  ? 195.793 153.925 189.188 1.00 19.89 ? 651  VAL A O      1 
ATOM   3849 C  CB     . VAL A 1 651  ? 192.884 152.296 189.537 1.00 19.89 ? 651  VAL A CB     1 
ATOM   3850 C  CG1    . VAL A 1 651  ? 193.985 151.306 189.836 1.00 19.89 ? 651  VAL A CG1    1 
ATOM   3851 C  CG2    . VAL A 1 651  ? 191.844 152.170 190.596 1.00 19.89 ? 651  VAL A CG2    1 
ATOM   3852 N  N      . LEU A 1 652  ? 194.518 153.949 187.333 1.00 19.17 ? 652  LEU A N      1 
ATOM   3853 C  CA     . LEU A 1 652  ? 195.663 154.122 186.440 1.00 19.17 ? 652  LEU A CA     1 
ATOM   3854 C  C      . LEU A 1 652  ? 196.358 155.458 186.660 1.00 19.17 ? 652  LEU A C      1 
ATOM   3855 O  O      . LEU A 1 652  ? 197.582 155.551 186.542 1.00 19.17 ? 652  LEU A O      1 
ATOM   3856 C  CB     . LEU A 1 652  ? 195.212 153.996 184.985 1.00 19.17 ? 652  LEU A CB     1 
ATOM   3857 C  CG     . LEU A 1 652  ? 196.307 154.099 183.926 1.00 19.17 ? 652  LEU A CG     1 
ATOM   3858 C  CD1    . LEU A 1 652  ? 197.309 152.982 184.094 1.00 19.17 ? 652  LEU A CD1    1 
ATOM   3859 C  CD2    . LEU A 1 652  ? 195.732 154.100 182.539 1.00 19.17 ? 652  LEU A CD2    1 
ATOM   3860 N  N      . ASP A 1 653  ? 195.604 156.483 187.042 1.00 22.43 ? 653  ASP A N      1 
ATOM   3861 C  CA     . ASP A 1 653  ? 196.188 157.791 187.284 1.00 22.43 ? 653  ASP A CA     1 
ATOM   3862 C  C      . ASP A 1 653  ? 196.992 157.793 188.573 1.00 22.43 ? 653  ASP A C      1 
ATOM   3863 O  O      . ASP A 1 653  ? 198.078 158.379 188.630 1.00 22.43 ? 653  ASP A O      1 
ATOM   3864 C  CB     . ASP A 1 653  ? 195.084 158.843 187.325 1.00 22.43 ? 653  ASP A CB     1 
ATOM   3865 C  CG     . ASP A 1 653  ? 195.606 160.250 187.130 1.00 22.43 ? 653  ASP A CG     1 
ATOM   3866 O  OD1    . ASP A 1 653  ? 196.826 160.424 186.920 1.00 22.43 ? 653  ASP A OD1    1 
ATOM   3867 O  OD2    . ASP A 1 653  ? 194.789 161.191 187.186 1.00 22.43 ? 653  ASP A OD2    1 
ATOM   3868 N  N      . GLU A 1 654  ? 196.485 157.125 189.609 1.00 25.79 ? 654  GLU A N      1 
ATOM   3869 C  CA     . GLU A 1 654  ? 197.256 156.995 190.838 1.00 25.79 ? 654  GLU A CA     1 
ATOM   3870 C  C      . GLU A 1 654  ? 198.462 156.082 190.643 1.00 25.79 ? 654  GLU A C      1 
ATOM   3871 O  O      . GLU A 1 654  ? 199.497 156.279 191.284 1.00 25.79 ? 654  GLU A O      1 
ATOM   3872 C  CB     . GLU A 1 654  ? 196.363 156.480 191.966 1.00 25.79 ? 654  GLU A CB     1 
ATOM   3873 C  CG     . GLU A 1 654  ? 197.009 156.529 193.341 1.00 25.79 ? 654  GLU A CG     1 
ATOM   3874 C  CD     . GLU A 1 654  ? 197.221 157.940 193.851 1.00 25.79 ? 654  GLU A CD     1 
ATOM   3875 O  OE1    . GLU A 1 654  ? 196.440 158.838 193.474 1.00 25.79 ? 654  GLU A OE1    1 
ATOM   3876 O  OE2    . GLU A 1 654  ? 198.174 158.153 194.631 1.00 25.79 ? 654  GLU A OE2    1 
ATOM   3877 N  N      . CYS A 1 655  ? 198.353 155.090 189.756 1.00 25.36 ? 655  CYS A N      1 
ATOM   3878 C  CA     . CYS A 1 655  ? 199.510 154.281 189.390 1.00 25.36 ? 655  CYS A CA     1 
ATOM   3879 C  C      . CYS A 1 655  ? 200.527 155.083 188.595 1.00 25.36 ? 655  CYS A C      1 
ATOM   3880 O  O      . CYS A 1 655  ? 201.713 154.760 188.610 1.00 25.36 ? 655  CYS A O      1 
ATOM   3881 C  CB     . CYS A 1 655  ? 199.081 153.067 188.566 1.00 25.36 ? 655  CYS A CB     1 
ATOM   3882 S  SG     . CYS A 1 655  ? 198.163 151.799 189.436 1.00 25.36 ? 655  CYS A SG     1 
ATOM   3883 N  N      . PHE A 1 656  ? 200.084 156.079 187.847 1.00 24.47 ? 656  PHE A N      1 
ATOM   3884 C  CA     . PHE A 1 656  ? 200.987 156.875 187.035 1.00 24.47 ? 656  PHE A CA     1 
ATOM   3885 C  C      . PHE A 1 656  ? 201.622 158.017 187.810 1.00 24.47 ? 656  PHE A C      1 
ATOM   3886 O  O      . PHE A 1 656  ? 202.696 158.487 187.419 1.00 24.47 ? 656  PHE A O      1 
ATOM   3887 C  CB     . PHE A 1 656  ? 200.219 157.412 185.828 1.00 24.47 ? 656  PHE A CB     1 
ATOM   3888 C  CG     . PHE A 1 656  ? 201.058 158.167 184.844 1.00 24.47 ? 656  PHE A CG     1 
ATOM   3889 C  CD1    . PHE A 1 656  ? 201.887 157.498 183.962 1.00 24.47 ? 656  PHE A CD1    1 
ATOM   3890 C  CD2    . PHE A 1 656  ? 201.002 159.546 184.788 1.00 24.47 ? 656  PHE A CD2    1 
ATOM   3891 C  CE1    . PHE A 1 656  ? 202.635 158.189 183.041 1.00 24.47 ? 656  PHE A CE1    1 
ATOM   3892 C  CE2    . PHE A 1 656  ? 201.764 160.242 183.885 1.00 24.47 ? 656  PHE A CE2    1 
ATOM   3893 C  CZ     . PHE A 1 656  ? 202.580 159.561 183.011 1.00 24.47 ? 656  PHE A CZ     1 
ATOM   3894 N  N      . ASN A 1 657  ? 200.991 158.459 188.904 1.00 28.58 ? 657  ASN A N      1 
ATOM   3895 C  CA     . ASN A 1 657  ? 201.522 159.575 189.680 1.00 28.58 ? 657  ASN A CA     1 
ATOM   3896 C  C      . ASN A 1 657  ? 202.835 159.230 190.371 1.00 28.58 ? 657  ASN A C      1 
ATOM   3897 O  O      . ASN A 1 657  ? 203.646 160.125 190.628 1.00 28.58 ? 657  ASN A O      1 
ATOM   3898 C  CB     . ASN A 1 657  ? 200.503 160.041 190.714 1.00 28.58 ? 657  ASN A CB     1 
ATOM   3899 C  CG     . ASN A 1 657  ? 199.350 160.798 190.096 1.00 28.58 ? 657  ASN A CG     1 
ATOM   3900 O  OD1    . ASN A 1 657  ? 199.532 161.569 189.155 1.00 28.58 ? 657  ASN A OD1    1 
ATOM   3901 N  ND2    . ASN A 1 657  ? 198.154 160.598 190.638 1.00 28.58 ? 657  ASN A ND2    1 
ATOM   3902 N  N      . GLU A 1 658  ? 203.070 157.958 190.680 1.00 31.49 ? 658  GLU A N      1 
ATOM   3903 C  CA     . GLU A 1 658  ? 204.377 157.519 191.147 1.00 31.49 ? 658  GLU A CA     1 
ATOM   3904 C  C      . GLU A 1 658  ? 204.795 156.297 190.344 1.00 31.49 ? 658  GLU A C      1 
ATOM   3905 O  O      . GLU A 1 658  ? 203.983 155.397 190.111 1.00 31.49 ? 658  GLU A O      1 
ATOM   3906 C  CB     . GLU A 1 658  ? 204.378 157.245 192.668 1.00 31.49 ? 658  GLU A CB     1 
ATOM   3907 C  CG     . GLU A 1 658  ? 203.629 156.010 193.162 1.00 31.49 ? 658  GLU A CG     1 
ATOM   3908 C  CD     . GLU A 1 658  ? 202.149 156.238 193.346 1.00 31.49 ? 658  GLU A CD     1 
ATOM   3909 O  OE1    . GLU A 1 658  ? 201.637 157.298 192.932 1.00 31.49 ? 658  GLU A OE1    1 
ATOM   3910 O  OE2    . GLU A 1 658  ? 201.489 155.330 193.883 1.00 31.49 ? 658  GLU A OE2    1 
ATOM   3911 N  N      . ASN A 1 659  ? 206.042 156.313 189.867 1.00 30.21 ? 659  ASN A N      1 
ATOM   3912 C  CA     . ASN A 1 659  ? 206.694 155.196 189.179 1.00 30.21 ? 659  ASN A CA     1 
ATOM   3913 C  C      . ASN A 1 659  ? 205.913 154.779 187.926 1.00 30.21 ? 659  ASN A C      1 
ATOM   3914 O  O      . ASN A 1 659  ? 205.223 153.761 187.888 1.00 30.21 ? 659  ASN A O      1 
ATOM   3915 C  CB     . ASN A 1 659  ? 206.928 154.026 190.139 1.00 30.21 ? 659  ASN A CB     1 
ATOM   3916 C  CG     . ASN A 1 659  ? 208.018 153.087 189.661 1.00 30.21 ? 659  ASN A CG     1 
ATOM   3917 O  OD1    . ASN A 1 659  ? 208.470 153.160 188.519 1.00 30.21 ? 659  ASN A OD1    1 
ATOM   3918 N  ND2    . ASN A 1 659  ? 208.513 152.260 190.571 1.00 30.21 ? 659  ASN A ND2    1 
ATOM   3919 N  N      . GLU A 1 660  ? 205.999 155.661 186.923 1.00 28.62 ? 660  GLU A N      1 
ATOM   3920 C  CA     . GLU A 1 660  ? 205.370 155.457 185.618 1.00 28.62 ? 660  GLU A CA     1 
ATOM   3921 C  C      . GLU A 1 660  ? 205.845 154.182 184.920 1.00 28.62 ? 660  GLU A C      1 
ATOM   3922 O  O      . GLU A 1 660  ? 205.122 153.623 184.080 1.00 28.62 ? 660  GLU A O      1 
ATOM   3923 C  CB     . GLU A 1 660  ? 205.679 156.662 184.740 1.00 28.62 ? 660  GLU A CB     1 
ATOM   3924 C  CG     . GLU A 1 660  ? 205.292 157.982 185.359 1.00 28.62 ? 660  GLU A CG     1 
ATOM   3925 C  CD     . GLU A 1 660  ? 205.693 159.159 184.496 1.00 28.62 ? 660  GLU A CD     1 
ATOM   3926 O  OE1    . GLU A 1 660  ? 206.391 158.942 183.483 1.00 28.62 ? 660  GLU A OE1    1 
ATOM   3927 O  OE2    . GLU A 1 660  ? 205.314 160.301 184.827 1.00 28.62 ? 660  GLU A OE2    1 
ATOM   3928 N  N      . THR A 1 661  ? 207.065 153.729 185.229 1.00 27.80 ? 661  THR A N      1 
ATOM   3929 C  CA     . THR A 1 661  ? 207.576 152.478 184.678 1.00 27.80 ? 661  THR A CA     1 
ATOM   3930 C  C      . THR A 1 661  ? 206.741 151.287 185.137 1.00 27.80 ? 661  THR A C      1 
ATOM   3931 O  O      . THR A 1 661  ? 206.427 150.395 184.339 1.00 27.80 ? 661  THR A O      1 
ATOM   3932 C  CB     . THR A 1 661  ? 209.042 152.301 185.080 1.00 27.80 ? 661  THR A CB     1 
ATOM   3933 O  OG1    . THR A 1 661  ? 209.796 153.433 184.628 1.00 27.80 ? 661  THR A OG1    1 
ATOM   3934 C  CG2    . THR A 1 661  ? 209.630 151.041 184.466 1.00 27.80 ? 661  THR A CG2    1 
ATOM   3935 N  N      . LEU A 1 662  ? 206.344 151.271 186.412 1.00 27.82 ? 662  LEU A N      1 
ATOM   3936 C  CA     . LEU A 1 662  ? 205.469 150.205 186.884 1.00 27.82 ? 662  LEU A CA     1 
ATOM   3937 C  C      . LEU A 1 662  ? 204.071 150.316 186.294 1.00 27.82 ? 662  LEU A C      1 
ATOM   3938 O  O      . LEU A 1 662  ? 203.389 149.300 186.149 1.00 27.82 ? 662  LEU A O      1 
ATOM   3939 C  CB     . LEU A 1 662  ? 205.391 150.187 188.407 1.00 27.82 ? 662  LEU A CB     1 
ATOM   3940 C  CG     . LEU A 1 662  ? 206.628 149.752 189.180 1.00 27.82 ? 662  LEU A CG     1 
ATOM   3941 C  CD1    . LEU A 1 662  ? 206.331 149.731 190.664 1.00 27.82 ? 662  LEU A CD1    1 
ATOM   3942 C  CD2    . LEU A 1 662  ? 207.108 148.400 188.709 1.00 27.82 ? 662  LEU A CD2    1 
ATOM   3943 N  N      . SER A 1 663  ? 203.642 151.521 185.921 1.00 25.38 ? 663  SER A N      1 
ATOM   3944 C  CA     . SER A 1 663  ? 202.378 151.673 185.206 1.00 25.38 ? 663  SER A CA     1 
ATOM   3945 C  C      . SER A 1 663  ? 202.440 151.025 183.830 1.00 25.38 ? 663  SER A C      1 
ATOM   3946 O  O      . SER A 1 663  ? 201.505 150.320 183.425 1.00 25.38 ? 663  SER A O      1 
ATOM   3947 C  CB     . SER A 1 663  ? 202.042 153.147 185.066 1.00 25.38 ? 663  SER A CB     1 
ATOM   3948 O  OG     . SER A 1 663  ? 202.039 153.753 186.329 1.00 25.38 ? 663  SER A OG     1 
ATOM   3949 N  N      . GLN A 1 664  ? 203.535 151.263 183.100 1.00 24.10 ? 664  GLN A N      1 
ATOM   3950 C  CA     . GLN A 1 664  ? 203.704 150.627 181.797 1.00 24.10 ? 664  GLN A CA     1 
ATOM   3951 C  C      . GLN A 1 664  ? 203.829 149.116 181.917 1.00 24.10 ? 664  GLN A C      1 
ATOM   3952 O  O      . GLN A 1 664  ? 203.266 148.382 181.101 1.00 24.10 ? 664  GLN A O      1 
ATOM   3953 C  CB     . GLN A 1 664  ? 204.912 151.203 181.058 1.00 24.10 ? 664  GLN A CB     1 
ATOM   3954 C  CG     . GLN A 1 664  ? 204.585 152.404 180.191 1.00 24.10 ? 664  GLN A CG     1 
ATOM   3955 C  CD     . GLN A 1 664  ? 204.259 153.629 180.990 1.00 24.10 ? 664  GLN A CD     1 
ATOM   3956 O  OE1    . GLN A 1 664  ? 203.125 154.094 180.988 1.00 24.10 ? 664  GLN A OE1    1 
ATOM   3957 N  NE2    . GLN A 1 664  ? 205.258 154.182 181.660 1.00 24.10 ? 664  GLN A NE2    1 
ATOM   3958 N  N      . THR A 1 665  ? 204.538 148.628 182.933 1.00 26.70 ? 665  THR A N      1 
ATOM   3959 C  CA     . THR A 1 665  ? 204.641 147.183 183.100 1.00 26.70 ? 665  THR A CA     1 
ATOM   3960 C  C      . THR A 1 665  ? 203.410 146.572 183.754 1.00 26.70 ? 665  THR A C      1 
ATOM   3961 O  O      . THR A 1 665  ? 203.323 145.346 183.842 1.00 26.70 ? 665  THR A O      1 
ATOM   3962 C  CB     . THR A 1 665  ? 205.874 146.814 183.921 1.00 26.70 ? 665  THR A CB     1 
ATOM   3963 O  OG1    . THR A 1 665  ? 205.749 147.353 185.238 1.00 26.70 ? 665  THR A OG1    1 
ATOM   3964 C  CG2    . THR A 1 665  ? 207.128 147.362 183.266 1.00 26.70 ? 665  THR A CG2    1 
ATOM   3965 N  N      . LEU A 1 666  ? 202.482 147.392 184.229 1.00 26.63 ? 666  LEU A N      1 
ATOM   3966 C  CA     . LEU A 1 666  ? 201.208 146.940 184.761 1.00 26.63 ? 666  LEU A CA     1 
ATOM   3967 C  C      . LEU A 1 666  ? 200.126 146.879 183.697 1.00 26.63 ? 666  LEU A C      1 
ATOM   3968 O  O      . LEU A 1 666  ? 199.184 146.090 183.822 1.00 26.63 ? 666  LEU A O      1 
ATOM   3969 C  CB     . LEU A 1 666  ? 200.780 147.887 185.881 1.00 26.63 ? 666  LEU A CB     1 
ATOM   3970 C  CG     . LEU A 1 666  ? 199.493 147.708 186.674 1.00 26.63 ? 666  LEU A CG     1 
ATOM   3971 C  CD1    . LEU A 1 666  ? 199.537 146.477 187.524 1.00 26.63 ? 666  LEU A CD1    1 
ATOM   3972 C  CD2    . LEU A 1 666  ? 199.280 148.916 187.522 1.00 26.63 ? 666  LEU A CD2    1 
ATOM   3973 N  N      . LEU A 1 667  ? 200.236 147.699 182.652 1.00 23.90 ? 667  LEU A N      1 
ATOM   3974 C  CA     . LEU A 1 667  ? 199.248 147.685 181.582 1.00 23.90 ? 667  LEU A CA     1 
ATOM   3975 C  C      . LEU A 1 667  ? 199.441 146.559 180.576 1.00 23.90 ? 667  LEU A C      1 
ATOM   3976 O  O      . LEU A 1 667  ? 198.590 146.393 179.699 1.00 23.90 ? 667  LEU A O      1 
ATOM   3977 C  CB     . LEU A 1 667  ? 199.267 149.013 180.835 1.00 23.90 ? 667  LEU A CB     1 
ATOM   3978 C  CG     . LEU A 1 667  ? 198.728 150.198 181.615 1.00 23.90 ? 667  LEU A CG     1 
ATOM   3979 C  CD1    . LEU A 1 667  ? 199.031 151.464 180.866 1.00 23.90 ? 667  LEU A CD1    1 
ATOM   3980 C  CD2    . LEU A 1 667  ? 197.243 150.015 181.796 1.00 23.90 ? 667  LEU A CD2    1 
ATOM   3981 N  N      . VAL A 1 668  ? 200.531 145.800 180.655 1.00 28.87 ? 668  VAL A N      1 
ATOM   3982 C  CA     . VAL A 1 668  ? 200.833 144.764 179.675 1.00 28.87 ? 668  VAL A CA     1 
ATOM   3983 C  C      . VAL A 1 668  ? 201.019 143.399 180.335 1.00 28.87 ? 668  VAL A C      1 
ATOM   3984 O  O      . VAL A 1 668  ? 201.654 142.524 179.771 1.00 28.87 ? 668  VAL A O      1 
ATOM   3985 C  CB     . VAL A 1 668  ? 202.063 145.141 178.825 1.00 28.87 ? 668  VAL A CB     1 
ATOM   3986 C  CG1    . VAL A 1 668  ? 201.771 146.339 177.944 1.00 28.87 ? 668  VAL A CG1    1 
ATOM   3987 C  CG2    . VAL A 1 668  ? 203.257 145.420 179.711 1.00 28.87 ? 668  VAL A CG2    1 
ATOM   3988 N  N      . ARG A 1 669  ? 200.420 143.195 181.504 1.00 34.23 ? 669  ARG A N      1 
ATOM   3989 C  CA     . ARG A 1 669  ? 200.688 142.019 182.316 1.00 34.23 ? 669  ARG A CA     1 
ATOM   3990 C  C      . ARG A 1 669  ? 200.007 140.768 181.768 1.00 34.23 ? 669  ARG A C      1 
ATOM   3991 O  O      . ARG A 1 669  ? 199.247 140.793 180.799 1.00 34.23 ? 669  ARG A O      1 
ATOM   3992 C  CB     . ARG A 1 669  ? 200.209 142.231 183.742 1.00 34.23 ? 669  ARG A CB     1 
ATOM   3993 C  CG     . ARG A 1 669  ? 201.008 143.180 184.549 1.00 34.23 ? 669  ARG A CG     1 
ATOM   3994 C  CD     . ARG A 1 669  ? 200.370 143.301 185.897 1.00 34.23 ? 669  ARG A CD     1 
ATOM   3995 N  NE     . ARG A 1 669  ? 200.426 142.048 186.633 1.00 34.23 ? 669  ARG A NE     1 
ATOM   3996 C  CZ     . ARG A 1 669  ? 199.768 141.824 187.763 1.00 34.23 ? 669  ARG A CZ     1 
ATOM   3997 N  NH1    . ARG A 1 669  ? 198.998 142.774 188.278 1.00 34.23 ? 669  ARG A NH1    1 
ATOM   3998 N  NH2    . ARG A 1 669  ? 199.873 140.652 188.373 1.00 34.23 ? 669  ARG A NH2    1 
ATOM   3999 N  N      . GLU A 1 670  ? 200.279 139.660 182.448 1.00 39.06 ? 670  GLU A N      1 
ATOM   4000 C  CA     . GLU A 1 670  ? 199.663 138.361 182.198 1.00 39.06 ? 670  GLU A CA     1 
ATOM   4001 C  C      . GLU A 1 670  ? 198.547 138.208 183.226 1.00 39.06 ? 670  GLU A C      1 
ATOM   4002 O  O      . GLU A 1 670  ? 198.772 137.756 184.348 1.00 39.06 ? 670  GLU A O      1 
ATOM   4003 C  CB     . GLU A 1 670  ? 200.711 137.258 182.322 1.00 39.06 ? 670  GLU A CB     1 
ATOM   4004 C  CG     . GLU A 1 670  ? 200.257 135.837 182.007 1.00 39.06 ? 670  GLU A CG     1 
ATOM   4005 C  CD     . GLU A 1 670  ? 200.005 135.604 180.532 1.00 39.06 ? 670  GLU A CD     1 
ATOM   4006 O  OE1    . GLU A 1 670  ? 200.549 136.357 179.698 1.00 39.06 ? 670  GLU A OE1    1 
ATOM   4007 O  OE2    . GLU A 1 670  ? 199.291 134.638 180.203 1.00 39.06 ? 670  GLU A OE2    1 
ATOM   4008 N  N      . LEU A 1 671  ? 197.337 138.613 182.846 1.00 33.37 ? 671  LEU A N      1 
ATOM   4009 C  CA     . LEU A 1 671  ? 196.179 138.546 183.737 1.00 33.37 ? 671  LEU A CA     1 
ATOM   4010 C  C      . LEU A 1 671  ? 195.510 137.193 183.549 1.00 33.37 ? 671  LEU A C      1 
ATOM   4011 O  O      . LEU A 1 671  ? 194.679 137.021 182.658 1.00 33.37 ? 671  LEU A O      1 
ATOM   4012 C  CB     . LEU A 1 671  ? 195.215 139.688 183.449 1.00 33.37 ? 671  LEU A CB     1 
ATOM   4013 C  CG     . LEU A 1 671  ? 195.750 141.088 183.736 1.00 33.37 ? 671  LEU A CG     1 
ATOM   4014 C  CD1    . LEU A 1 671  ? 194.796 142.118 183.189 1.00 33.37 ? 671  LEU A CD1    1 
ATOM   4015 C  CD2    . LEU A 1 671  ? 195.963 141.286 185.217 1.00 33.37 ? 671  LEU A CD2    1 
ATOM   4016 N  N      . ASP A 1 672  ? 195.859 136.233 184.409 1.00 35.65 ? 672  ASP A N      1 
ATOM   4017 C  CA     . ASP A 1 672  ? 195.403 134.858 184.236 1.00 35.65 ? 672  ASP A CA     1 
ATOM   4018 C  C      . ASP A 1 672  ? 193.917 134.682 184.517 1.00 35.65 ? 672  ASP A C      1 
ATOM   4019 O  O      . ASP A 1 672  ? 193.310 133.747 183.985 1.00 35.65 ? 672  ASP A O      1 
ATOM   4020 C  CB     . ASP A 1 672  ? 196.213 133.921 185.131 1.00 35.65 ? 672  ASP A CB     1 
ATOM   4021 C  CG     . ASP A 1 672  ? 197.647 133.759 184.660 1.00 35.65 ? 672  ASP A CG     1 
ATOM   4022 O  OD1    . ASP A 1 672  ? 197.894 133.889 183.443 1.00 35.65 ? 672  ASP A OD1    1 
ATOM   4023 O  OD2    . ASP A 1 672  ? 198.526 133.493 185.506 1.00 35.65 ? 672  ASP A OD2    1 
ATOM   4024 N  N      . HIS A 1 673  ? 193.315 135.550 185.327 1.00 31.54 ? 673  HIS A N      1 
ATOM   4025 C  CA     . HIS A 1 673  ? 191.888 135.477 185.602 1.00 31.54 ? 673  HIS A CA     1 
ATOM   4026 C  C      . HIS A 1 673  ? 191.071 136.320 184.643 1.00 31.54 ? 673  HIS A C      1 
ATOM   4027 O  O      . HIS A 1 673  ? 189.902 136.605 184.920 1.00 31.54 ? 673  HIS A O      1 
ATOM   4028 C  CB     . HIS A 1 673  ? 191.601 135.893 187.042 1.00 31.54 ? 673  HIS A CB     1 
ATOM   4029 C  CG     . HIS A 1 673  ? 192.232 134.997 188.058 1.00 31.54 ? 673  HIS A CG     1 
ATOM   4030 N  ND1    . HIS A 1 673  ? 193.458 135.265 188.624 1.00 31.54 ? 673  HIS A ND1    1 
ATOM   4031 C  CD2    . HIS A 1 673  ? 191.829 133.813 188.573 1.00 31.54 ? 673  HIS A CD2    1 
ATOM   4032 C  CE1    . HIS A 1 673  ? 193.770 134.299 189.469 1.00 31.54 ? 673  HIS A CE1    1 
ATOM   4033 N  NE2    . HIS A 1 673  ? 192.799 133.405 189.455 1.00 31.54 ? 673  HIS A NE2    1 
ATOM   4034 N  N      . TYR A 1 674  ? 191.663 136.732 183.528 1.00 27.76 ? 674  TYR A N      1 
ATOM   4035 C  CA     . TYR A 1 674  ? 190.985 137.523 182.515 1.00 27.76 ? 674  TYR A CA     1 
ATOM   4036 C  C      . TYR A 1 674  ? 191.258 136.962 181.130 1.00 27.76 ? 674  TYR A C      1 
ATOM   4037 O  O      . TYR A 1 674  ? 191.279 137.710 180.160 1.00 27.76 ? 674  TYR A O      1 
ATOM   4038 C  CB     . TYR A 1 674  ? 191.407 138.988 182.603 1.00 27.76 ? 674  TYR A CB     1 
ATOM   4039 C  CG     . TYR A 1 674  ? 190.955 139.638 183.885 1.00 27.76 ? 674  TYR A CG     1 
ATOM   4040 C  CD1    . TYR A 1 674  ? 189.683 140.176 184.004 1.00 27.76 ? 674  TYR A CD1    1 
ATOM   4041 C  CD2    . TYR A 1 674  ? 191.784 139.670 184.991 1.00 27.76 ? 674  TYR A CD2    1 
ATOM   4042 C  CE1    . TYR A 1 674  ? 189.265 140.752 185.181 1.00 27.76 ? 674  TYR A CE1    1 
ATOM   4043 C  CE2    . TYR A 1 674  ? 191.374 140.234 186.165 1.00 27.76 ? 674  TYR A CE2    1 
ATOM   4044 C  CZ     . TYR A 1 674  ? 190.115 140.774 186.257 1.00 27.76 ? 674  TYR A CZ     1 
ATOM   4045 O  OH     . TYR A 1 674  ? 189.713 141.341 187.437 1.00 27.76 ? 674  TYR A OH     1 
ATOM   4046 N  N      . SER A 1 675  ? 191.439 135.639 181.040 1.00 30.92 ? 675  SER A N      1 
ATOM   4047 C  CA     . SER A 1 675  ? 191.775 134.911 179.807 1.00 30.92 ? 675  SER A CA     1 
ATOM   4048 C  C      . SER A 1 675  ? 193.045 135.455 179.160 1.00 30.92 ? 675  SER A C      1 
ATOM   4049 O  O      . SER A 1 675  ? 193.099 135.669 177.947 1.00 30.92 ? 675  SER A O      1 
ATOM   4050 C  CB     . SER A 1 675  ? 190.615 134.895 178.805 1.00 30.92 ? 675  SER A CB     1 
ATOM   4051 O  OG     . SER A 1 675  ? 190.382 136.173 178.259 1.00 30.92 ? 675  SER A OG     1 
ATOM   4052 N  N      . ARG A 1 676  ? 194.053 135.716 179.996 1.00 33.00 ? 676  ARG A N      1 
ATOM   4053 C  CA     . ARG A 1 676  ? 195.434 136.007 179.608 1.00 33.00 ? 676  ARG A CA     1 
ATOM   4054 C  C      . ARG A 1 676  ? 195.567 137.273 178.766 1.00 33.00 ? 676  ARG A C      1 
ATOM   4055 O  O      . ARG A 1 676  ? 196.534 137.421 178.016 1.00 33.00 ? 676  ARG A O      1 
ATOM   4056 C  CB     . ARG A 1 676  ? 196.067 134.816 178.880 1.00 33.00 ? 676  ARG A CB     1 
ATOM   4057 C  CG     . ARG A 1 676  ? 196.233 133.578 179.743 1.00 33.00 ? 676  ARG A CG     1 
ATOM   4058 C  CD     . ARG A 1 676  ? 196.910 132.461 178.963 1.00 33.00 ? 676  ARG A CD     1 
ATOM   4059 N  NE     . ARG A 1 676  ? 197.146 131.270 179.776 1.00 33.00 ? 676  ARG A NE     1 
ATOM   4060 C  CZ     . ARG A 1 676  ? 196.300 130.250 179.873 1.00 33.00 ? 676  ARG A CZ     1 
ATOM   4061 N  NH1    . ARG A 1 676  ? 195.154 130.270 179.208 1.00 33.00 ? 676  ARG A NH1    1 
ATOM   4062 N  NH2    . ARG A 1 676  ? 196.601 129.208 180.637 1.00 33.00 ? 676  ARG A NH2    1 
ATOM   4063 N  N      . MET A 1 677  ? 194.621 138.197 178.876 1.00 28.10 ? 677  MET A N      1 
ATOM   4064 C  CA     . MET A 1 677  ? 194.661 139.439 178.126 1.00 28.10 ? 677  MET A CA     1 
ATOM   4065 C  C      . MET A 1 677  ? 195.061 140.565 179.067 1.00 28.10 ? 677  MET A C      1 
ATOM   4066 O  O      . MET A 1 677  ? 194.832 140.493 180.275 1.00 28.10 ? 677  MET A O      1 
ATOM   4067 C  CB     . MET A 1 677  ? 193.311 139.723 177.454 1.00 28.10 ? 677  MET A CB     1 
ATOM   4068 C  CG     . MET A 1 677  ? 192.202 140.166 178.364 1.00 28.10 ? 677  MET A CG     1 
ATOM   4069 S  SD     . MET A 1 677  ? 190.581 140.013 177.592 1.00 28.10 ? 677  MET A SD     1 
ATOM   4070 C  CE     . MET A 1 677  ? 190.615 141.323 176.389 1.00 28.10 ? 677  MET A CE     1 
ATOM   4071 N  N      . THR A 1 678  ? 195.692 141.591 178.508 1.00 24.90 ? 678  THR A N      1 
ATOM   4072 C  CA     . THR A 1 678  ? 196.288 142.647 179.306 1.00 24.90 ? 678  THR A CA     1 
ATOM   4073 C  C      . THR A 1 678  ? 195.230 143.659 179.729 1.00 24.90 ? 678  THR A C      1 
ATOM   4074 O  O      . THR A 1 678  ? 194.040 143.515 179.445 1.00 24.90 ? 678  THR A O      1 
ATOM   4075 C  CB     . THR A 1 678  ? 197.402 143.332 178.525 1.00 24.90 ? 678  THR A CB     1 
ATOM   4076 O  OG1    . THR A 1 678  ? 196.843 144.010 177.397 1.00 24.90 ? 678  THR A OG1    1 
ATOM   4077 C  CG2    . THR A 1 678  ? 198.380 142.311 178.018 1.00 24.90 ? 678  THR A CG2    1 
ATOM   4078 N  N      . ALA A 1 679  ? 195.674 144.707 180.422 1.00 21.76 ? 679  ALA A N      1 
ATOM   4079 C  CA     . ALA A 1 679  ? 194.768 145.796 180.765 1.00 21.76 ? 679  ALA A CA     1 
ATOM   4080 C  C      . ALA A 1 679  ? 194.441 146.657 179.552 1.00 21.76 ? 679  ALA A C      1 
ATOM   4081 O  O      . ALA A 1 679  ? 193.333 147.200 179.467 1.00 21.76 ? 679  ALA A O      1 
ATOM   4082 C  CB     . ALA A 1 679  ? 195.367 146.647 181.880 1.00 21.76 ? 679  ALA A CB     1 
ATOM   4083 N  N      . LEU A 1 680  ? 195.379 146.786 178.604 1.00 21.25 ? 680  LEU A N      1 
ATOM   4084 C  CA     . LEU A 1 680  ? 195.088 147.487 177.356 1.00 21.25 ? 680  LEU A CA     1 
ATOM   4085 C  C      . LEU A 1 680  ? 194.032 146.765 176.538 1.00 21.25 ? 680  LEU A C      1 
ATOM   4086 O  O      . LEU A 1 680  ? 193.200 147.403 175.891 1.00 21.25 ? 680  LEU A O      1 
ATOM   4087 C  CB     . LEU A 1 680  ? 196.340 147.634 176.498 1.00 21.25 ? 680  LEU A CB     1 
ATOM   4088 C  CG     . LEU A 1 680  ? 197.460 148.618 176.761 1.00 21.25 ? 680  LEU A CG     1 
ATOM   4089 C  CD1    . LEU A 1 680  ? 198.498 148.369 175.701 1.00 21.25 ? 680  LEU A CD1    1 
ATOM   4090 C  CD2    . LEU A 1 680  ? 196.931 150.020 176.665 1.00 21.25 ? 680  LEU A CD2    1 
ATOM   4091 N  N      . GLU A 1 681  ? 194.063 145.439 176.533 1.00 23.48 ? 681  GLU A N      1 
ATOM   4092 C  CA     . GLU A 1 681  ? 193.103 144.696 175.733 1.00 23.48 ? 681  GLU A CA     1 
ATOM   4093 C  C      . GLU A 1 681  ? 191.726 144.679 176.382 1.00 23.48 ? 681  GLU A C      1 
ATOM   4094 O  O      . GLU A 1 681  ? 190.712 144.741 175.676 1.00 23.48 ? 681  GLU A O      1 
ATOM   4095 C  CB     . GLU A 1 681  ? 193.643 143.294 175.489 1.00 23.48 ? 681  GLU A CB     1 
ATOM   4096 C  CG     . GLU A 1 681  ? 194.910 143.347 174.667 1.00 23.48 ? 681  GLU A CG     1 
ATOM   4097 C  CD     . GLU A 1 681  ? 195.548 142.003 174.449 1.00 23.48 ? 681  GLU A CD     1 
ATOM   4098 O  OE1    . GLU A 1 681  ? 195.073 141.009 175.027 1.00 23.48 ? 681  GLU A OE1    1 
ATOM   4099 O  OE2    . GLU A 1 681  ? 196.540 141.947 173.696 1.00 23.48 ? 681  GLU A OE2    1 
ATOM   4100 N  N      . LEU A 1 682  ? 191.673 144.648 177.717 1.00 22.05 ? 682  LEU A N      1 
ATOM   4101 C  CA     . LEU A 1 682  ? 190.425 144.881 178.435 1.00 22.05 ? 682  LEU A CA     1 
ATOM   4102 C  C      . LEU A 1 682  ? 189.922 146.306 178.276 1.00 22.05 ? 682  LEU A C      1 
ATOM   4103 O  O      . LEU A 1 682  ? 188.726 146.550 178.455 1.00 22.05 ? 682  LEU A O      1 
ATOM   4104 C  CB     . LEU A 1 682  ? 190.602 144.577 179.920 1.00 22.05 ? 682  LEU A CB     1 
ATOM   4105 C  CG     . LEU A 1 682  ? 190.773 143.122 180.323 1.00 22.05 ? 682  LEU A CG     1 
ATOM   4106 C  CD1    . LEU A 1 682  ? 191.226 143.043 181.757 1.00 22.05 ? 682  LEU A CD1    1 
ATOM   4107 C  CD2    . LEU A 1 682  ? 189.456 142.402 180.150 1.00 22.05 ? 682  LEU A CD2    1 
ATOM   4108 N  N      . ALA A 1 683  ? 190.804 147.250 177.966 1.00 21.49 ? 683  ALA A N      1 
ATOM   4109 C  CA     . ALA A 1 683  ? 190.396 148.630 177.761 1.00 21.49 ? 683  ALA A CA     1 
ATOM   4110 C  C      . ALA A 1 683  ? 189.927 148.910 176.347 1.00 21.49 ? 683  ALA A C      1 
ATOM   4111 O  O      . ALA A 1 683  ? 189.058 149.764 176.152 1.00 21.49 ? 683  ALA A O      1 
ATOM   4112 C  CB     . ALA A 1 683  ? 191.550 149.563 178.092 1.00 21.49 ? 683  ALA A CB     1 
ATOM   4113 N  N      . VAL A 1 684  ? 190.501 148.237 175.355 1.00 21.43 ? 684  VAL A N      1 
ATOM   4114 C  CA     . VAL A 1 684  ? 190.071 148.447 173.981 1.00 21.43 ? 684  VAL A CA     1 
ATOM   4115 C  C      . VAL A 1 684  ? 188.931 147.518 173.584 1.00 21.43 ? 684  VAL A C      1 
ATOM   4116 O  O      . VAL A 1 684  ? 188.236 147.803 172.599 1.00 21.43 ? 684  VAL A O      1 
ATOM   4117 C  CB     . VAL A 1 684  ? 191.238 148.297 172.989 1.00 21.43 ? 684  VAL A CB     1 
ATOM   4118 C  CG1    . VAL A 1 684  ? 192.345 149.270 173.330 1.00 21.43 ? 684  VAL A CG1    1 
ATOM   4119 C  CG2    . VAL A 1 684  ? 191.743 146.876 172.951 1.00 21.43 ? 684  VAL A CG2    1 
ATOM   4120 N  N      . SER A 1 685  ? 188.711 146.419 174.315 1.00 22.55 ? 685  SER A N      1 
ATOM   4121 C  CA     . SER A 1 685  ? 187.496 145.647 174.091 1.00 22.55 ? 685  SER A CA     1 
ATOM   4122 C  C      . SER A 1 685  ? 186.293 146.382 174.654 1.00 22.55 ? 685  SER A C      1 
ATOM   4123 O  O      . SER A 1 685  ? 185.215 146.383 174.051 1.00 22.55 ? 685  SER A O      1 
ATOM   4124 C  CB     . SER A 1 685  ? 187.615 144.261 174.718 1.00 22.55 ? 685  SER A CB     1 
ATOM   4125 O  OG     . SER A 1 685  ? 187.613 144.347 176.128 1.00 22.55 ? 685  SER A OG     1 
ATOM   4126 N  N      . ALA A 1 686  ? 186.476 147.041 175.792 1.00 22.83 ? 686  ALA A N      1 
ATOM   4127 C  CA     . ALA A 1 686  ? 185.451 147.849 176.430 1.00 22.83 ? 686  ALA A CA     1 
ATOM   4128 C  C      . ALA A 1 686  ? 185.253 149.200 175.764 1.00 22.83 ? 686  ALA A C      1 
ATOM   4129 O  O      . ALA A 1 686  ? 184.387 149.949 176.224 1.00 22.83 ? 686  ALA A O      1 
ATOM   4130 C  CB     . ALA A 1 686  ? 185.802 148.061 177.901 1.00 22.83 ? 686  ALA A CB     1 
ATOM   4131 N  N      . GLU A 1 687  ? 186.015 149.495 174.702 1.00 23.16 ? 687  GLU A N      1 
ATOM   4132 C  CA     . GLU A 1 687  ? 186.146 150.805 174.039 1.00 23.16 ? 687  GLU A CA     1 
ATOM   4133 C  C      . GLU A 1 687  ? 186.216 151.961 175.040 1.00 23.16 ? 687  GLU A C      1 
ATOM   4134 O  O      . GLU A 1 687  ? 185.571 153.002 174.901 1.00 23.16 ? 687  GLU A O      1 
ATOM   4135 C  CB     . GLU A 1 687  ? 185.065 151.019 172.956 1.00 23.16 ? 687  GLU A CB     1 
ATOM   4136 C  CG     . GLU A 1 687  ? 183.574 151.052 173.332 1.00 23.16 ? 687  GLU A CG     1 
ATOM   4137 C  CD     . GLU A 1 687  ? 182.904 149.697 173.218 1.00 23.16 ? 687  GLU A CD     1 
ATOM   4138 O  OE1    . GLU A 1 687  ? 183.620 148.684 173.082 1.00 23.16 ? 687  GLU A OE1    1 
ATOM   4139 O  OE2    . GLU A 1 687  ? 181.657 149.644 173.264 1.00 23.16 ? 687  GLU A OE2    1 
ATOM   4140 N  N      . SER A 1 688  ? 187.053 151.770 176.055 1.00 22.18 ? 688  SER A N      1 
ATOM   4141 C  CA     . SER A 1 688  ? 187.244 152.762 177.106 1.00 22.18 ? 688  SER A CA     1 
ATOM   4142 C  C      . SER A 1 688  ? 188.220 153.805 176.585 1.00 22.18 ? 688  SER A C      1 
ATOM   4143 O  O      . SER A 1 688  ? 189.435 153.624 176.655 1.00 22.18 ? 688  SER A O      1 
ATOM   4144 C  CB     . SER A 1 688  ? 187.749 152.095 178.378 1.00 22.18 ? 688  SER A CB     1 
ATOM   4145 O  OG     . SER A 1 688  ? 187.905 153.041 179.416 1.00 22.18 ? 688  SER A OG     1 
ATOM   4146 N  N      . GLN A 1 689  ? 187.683 154.899 176.042 1.00 21.53 ? 689  GLN A N      1 
ATOM   4147 C  CA     . GLN A 1 689  ? 188.535 155.910 175.430 1.00 21.53 ? 689  GLN A CA     1 
ATOM   4148 C  C      . GLN A 1 689  ? 189.266 156.743 176.468 1.00 21.53 ? 689  GLN A C      1 
ATOM   4149 O  O      . GLN A 1 689  ? 190.394 157.173 176.220 1.00 21.53 ? 689  GLN A O      1 
ATOM   4150 C  CB     . GLN A 1 689  ? 187.719 156.817 174.515 1.00 21.53 ? 689  GLN A CB     1 
ATOM   4151 C  CG     . GLN A 1 689  ? 187.248 156.148 173.251 1.00 21.53 ? 689  GLN A CG     1 
ATOM   4152 C  CD     . GLN A 1 689  ? 186.510 157.103 172.346 1.00 21.53 ? 689  GLN A CD     1 
ATOM   4153 O  OE1    . GLN A 1 689  ? 186.281 158.259 172.701 1.00 21.53 ? 689  GLN A OE1    1 
ATOM   4154 N  NE2    . GLN A 1 689  ? 186.136 156.627 171.165 1.00 21.53 ? 689  GLN A NE2    1 
ATOM   4155 N  N      . ASP A 1 690  ? 188.649 156.982 177.627 1.00 21.41 ? 690  ASP A N      1 
ATOM   4156 C  CA     . ASP A 1 690  ? 189.313 157.742 178.678 1.00 21.41 ? 690  ASP A CA     1 
ATOM   4157 C  C      . ASP A 1 690  ? 190.472 156.981 179.305 1.00 21.41 ? 690  ASP A C      1 
ATOM   4158 O  O      . ASP A 1 690  ? 191.362 157.604 179.891 1.00 21.41 ? 690  ASP A O      1 
ATOM   4159 C  CB     . ASP A 1 690  ? 188.301 158.158 179.750 1.00 21.41 ? 690  ASP A CB     1 
ATOM   4160 C  CG     . ASP A 1 690  ? 187.522 156.980 180.323 1.00 21.41 ? 690  ASP A CG     1 
ATOM   4161 O  OD1    . ASP A 1 690  ? 187.652 155.847 179.811 1.00 21.41 ? 690  ASP A OD1    1 
ATOM   4162 O  OD2    . ASP A 1 690  ? 186.775 157.191 181.304 1.00 21.41 ? 690  ASP A OD2    1 
ATOM   4163 N  N      . PHE A 1 691  ? 190.486 155.655 179.180 1.00 17.45 ? 691  PHE A N      1 
ATOM   4164 C  CA     . PHE A 1 691  ? 191.593 154.861 179.691 1.00 17.45 ? 691  PHE A CA     1 
ATOM   4165 C  C      . PHE A 1 691  ? 192.768 154.889 178.730 1.00 17.45 ? 691  PHE A C      1 
ATOM   4166 O  O      . PHE A 1 691  ? 193.914 155.036 179.155 1.00 17.45 ? 691  PHE A O      1 
ATOM   4167 C  CB     . PHE A 1 691  ? 191.134 153.424 179.917 1.00 17.45 ? 691  PHE A CB     1 
ATOM   4168 C  CG     . PHE A 1 691  ? 192.032 152.623 180.809 1.00 17.45 ? 691  PHE A CG     1 
ATOM   4169 C  CD1    . PHE A 1 691  ? 191.882 152.677 182.178 1.00 17.45 ? 691  PHE A CD1    1 
ATOM   4170 C  CD2    . PHE A 1 691  ? 193.035 151.834 180.284 1.00 17.45 ? 691  PHE A CD2    1 
ATOM   4171 C  CE1    . PHE A 1 691  ? 192.696 151.933 182.999 1.00 17.45 ? 691  PHE A CE1    1 
ATOM   4172 C  CE2    . PHE A 1 691  ? 193.846 151.085 181.096 1.00 17.45 ? 691  PHE A CE2    1 
ATOM   4173 C  CZ     . PHE A 1 691  ? 193.680 151.139 182.454 1.00 17.45 ? 691  PHE A CZ     1 
ATOM   4174 N  N      . ILE A 1 692  ? 192.499 154.733 177.434 1.00 17.79 ? 692  ILE A N      1 
ATOM   4175 C  CA     . ILE A 1 692  ? 193.556 154.725 176.432 1.00 17.79 ? 692  ILE A CA     1 
ATOM   4176 C  C      . ILE A 1 692  ? 194.133 156.122 176.251 1.00 17.79 ? 692  ILE A C      1 
ATOM   4177 O  O      . ILE A 1 692  ? 195.328 156.279 175.982 1.00 17.79 ? 692  ILE A O      1 
ATOM   4178 C  CB     . ILE A 1 692  ? 192.997 154.133 175.124 1.00 17.79 ? 692  ILE A CB     1 
ATOM   4179 C  CG1    . ILE A 1 692  ? 192.469 152.725 175.385 1.00 17.79 ? 692  ILE A CG1    1 
ATOM   4180 C  CG2    . ILE A 1 692  ? 194.049 154.052 174.037 1.00 17.79 ? 692  ILE A CG2    1 
ATOM   4181 C  CD1    . ILE A 1 692  ? 193.537 151.766 175.848 1.00 17.79 ? 692  ILE A CD1    1 
ATOM   4182 N  N      . ALA A 1 693  ? 193.325 157.158 176.455 1.00 17.47 ? 693  ALA A N      1 
ATOM   4183 C  CA     . ALA A 1 693  ? 193.806 158.528 176.362 1.00 17.47 ? 693  ALA A CA     1 
ATOM   4184 C  C      . ALA A 1 693  ? 194.589 158.975 177.582 1.00 17.47 ? 693  ALA A C      1 
ATOM   4185 O  O      . ALA A 1 693  ? 195.046 160.120 177.610 1.00 17.47 ? 693  ALA A O      1 
ATOM   4186 C  CB     . ALA A 1 693  ? 192.646 159.494 176.139 1.00 17.47 ? 693  ALA A CB     1 
ATOM   4187 N  N      . HIS A 1 694  ? 194.729 158.122 178.588 1.00 17.24 ? 694  HIS A N      1 
ATOM   4188 C  CA     . HIS A 1 694  ? 195.568 158.435 179.728 1.00 17.24 ? 694  HIS A CA     1 
ATOM   4189 C  C      . HIS A 1 694  ? 197.025 158.480 179.295 1.00 17.24 ? 694  HIS A C      1 
ATOM   4190 O  O      . HIS A 1 694  ? 197.420 157.841 178.321 1.00 17.24 ? 694  HIS A O      1 
ATOM   4191 C  CB     . HIS A 1 694  ? 195.363 157.406 180.836 1.00 17.24 ? 694  HIS A CB     1 
ATOM   4192 C  CG     . HIS A 1 694  ? 195.996 157.790 182.129 1.00 17.24 ? 694  HIS A CG     1 
ATOM   4193 N  ND1    . HIS A 1 694  ? 197.280 157.425 182.465 1.00 17.24 ? 694  HIS A ND1    1 
ATOM   4194 C  CD2    . HIS A 1 694  ? 195.542 158.551 183.148 1.00 17.24 ? 694  HIS A CD2    1 
ATOM   4195 C  CE1    . HIS A 1 694  ? 197.583 157.930 183.644 1.00 17.24 ? 694  HIS A CE1    1 
ATOM   4196 N  NE2    . HIS A 1 694  ? 196.546 158.619 184.079 1.00 17.24 ? 694  HIS A NE2    1 
ATOM   4197 N  N      . THR A 1 695  ? 197.816 159.273 180.023 1.00 17.37 ? 695  THR A N      1 
ATOM   4198 C  CA     . THR A 1 695  ? 199.209 159.519 179.667 1.00 17.37 ? 695  THR A CA     1 
ATOM   4199 C  C      . THR A 1 695  ? 200.038 158.242 179.718 1.00 17.37 ? 695  THR A C      1 
ATOM   4200 O  O      . THR A 1 695  ? 200.957 158.071 178.912 1.00 17.37 ? 695  THR A O      1 
ATOM   4201 C  CB     . THR A 1 695  ? 199.791 160.578 180.605 1.00 17.37 ? 695  THR A CB     1 
ATOM   4202 O  OG1    . THR A 1 695  ? 198.894 161.690 180.665 1.00 17.37 ? 695  THR A OG1    1 
ATOM   4203 C  CG2    . THR A 1 695  ? 201.121 161.093 180.086 1.00 17.37 ? 695  THR A CG2    1 
ATOM   4204 N  N      . SER A 1 696  ? 199.687 157.317 180.615 1.00 18.39 ? 696  SER A N      1 
ATOM   4205 C  CA     . SER A 1 696  ? 200.395 156.047 180.732 1.00 18.39 ? 696  SER A CA     1 
ATOM   4206 C  C      . SER A 1 696  ? 200.189 155.176 179.499 1.00 18.39 ? 696  SER A C      1 
ATOM   4207 O  O      . SER A 1 696  ? 201.157 154.659 178.926 1.00 18.39 ? 696  SER A O      1 
ATOM   4208 C  CB     . SER A 1 696  ? 199.932 155.308 181.984 1.00 18.39 ? 696  SER A CB     1 
ATOM   4209 O  OG     . SER A 1 696  ? 200.639 154.096 182.148 1.00 18.39 ? 696  SER A OG     1 
ATOM   4210 N  N      . CYS A 1 697  ? 198.932 155.010 179.071 1.00 17.77 ? 697  CYS A N      1 
ATOM   4211 C  CA     . CYS A 1 697  ? 198.642 154.225 177.874 1.00 17.77 ? 697  CYS A CA     1 
ATOM   4212 C  C      . CYS A 1 697  ? 199.227 154.863 176.626 1.00 17.77 ? 697  CYS A C      1 
ATOM   4213 O  O      . CYS A 1 697  ? 199.665 154.152 175.718 1.00 17.77 ? 697  CYS A O      1 
ATOM   4214 C  CB     . CYS A 1 697  ? 197.136 154.043 177.702 1.00 17.77 ? 697  CYS A CB     1 
ATOM   4215 S  SG     . CYS A 1 697  ? 196.359 152.966 178.903 1.00 17.77 ? 697  CYS A SG     1 
ATOM   4216 N  N      . GLN A 1 698  ? 199.313 156.188 176.589 1.00 16.27 ? 698  GLN A N      1 
ATOM   4217 C  CA     . GLN A 1 698  ? 199.838 156.833 175.398 1.00 16.27 ? 698  GLN A CA     1 
ATOM   4218 C  C      . GLN A 1 698  ? 201.359 156.796 175.337 1.00 16.27 ? 698  GLN A C      1 
ATOM   4219 O  O      . GLN A 1 698  ? 201.919 156.627 174.250 1.00 16.27 ? 698  GLN A O      1 
ATOM   4220 C  CB     . GLN A 1 698  ? 199.304 158.256 175.304 1.00 16.27 ? 698  GLN A CB     1 
ATOM   4221 C  CG     . GLN A 1 698  ? 197.825 158.246 175.070 1.00 16.27 ? 698  GLN A CG     1 
ATOM   4222 C  CD     . GLN A 1 698  ? 197.460 157.534 173.781 1.00 16.27 ? 698  GLN A CD     1 
ATOM   4223 O  OE1    . GLN A 1 698  ? 198.084 157.744 172.746 1.00 16.27 ? 698  GLN A OE1    1 
ATOM   4224 N  NE2    . GLN A 1 698  ? 196.468 156.666 173.847 1.00 16.27 ? 698  GLN A NE2    1 
ATOM   4225 N  N      . VAL A 1 699  ? 202.055 156.906 176.474 1.00 16.98 ? 699  VAL A N      1 
ATOM   4226 C  CA     . VAL A 1 699  ? 203.505 156.731 176.408 1.00 16.98 ? 699  VAL A CA     1 
ATOM   4227 C  C      . VAL A 1 699  ? 203.854 155.263 176.208 1.00 16.98 ? 699  VAL A C      1 
ATOM   4228 O  O      . VAL A 1 699  ? 204.887 154.945 175.610 1.00 16.98 ? 699  VAL A O      1 
ATOM   4229 C  CB     . VAL A 1 699  ? 204.226 157.326 177.636 1.00 16.98 ? 699  VAL A CB     1 
ATOM   4230 C  CG1    . VAL A 1 699  ? 203.955 158.814 177.745 1.00 16.98 ? 699  VAL A CG1    1 
ATOM   4231 C  CG2    . VAL A 1 699  ? 203.869 156.603 178.915 1.00 16.98 ? 699  VAL A CG2    1 
ATOM   4232 N  N      . LEU A 1 700  ? 202.976 154.351 176.627 1.00 16.94 ? 700  LEU A N      1 
ATOM   4233 C  CA     . LEU A 1 700  ? 203.170 152.939 176.324 1.00 16.94 ? 700  LEU A CA     1 
ATOM   4234 C  C      . LEU A 1 700  ? 203.016 152.664 174.834 1.00 16.94 ? 700  LEU A C      1 
ATOM   4235 O  O      . LEU A 1 700  ? 203.828 151.946 174.243 1.00 16.94 ? 700  LEU A O      1 
ATOM   4236 C  CB     . LEU A 1 700  ? 202.180 152.105 177.127 1.00 16.94 ? 700  LEU A CB     1 
ATOM   4237 C  CG     . LEU A 1 700  ? 202.232 150.600 176.925 1.00 16.94 ? 700  LEU A CG     1 
ATOM   4238 C  CD1    . LEU A 1 700  ? 203.569 150.046 177.361 1.00 16.94 ? 700  LEU A CD1    1 
ATOM   4239 C  CD2    . LEU A 1 700  ? 201.127 149.989 177.726 1.00 16.94 ? 700  LEU A CD2    1 
ATOM   4240 N  N      . LEU A 1 701  ? 201.975 153.225 174.211 1.00 16.00 ? 701  LEU A N      1 
ATOM   4241 C  CA     . LEU A 1 701  ? 201.794 153.082 172.770 1.00 16.00 ? 701  LEU A CA     1 
ATOM   4242 C  C      . LEU A 1 701  ? 202.879 153.795 171.983 1.00 16.00 ? 701  LEU A C      1 
ATOM   4243 O  O      . LEU A 1 701  ? 203.193 153.382 170.866 1.00 16.00 ? 701  LEU A O      1 
ATOM   4244 C  CB     . LEU A 1 701  ? 200.432 153.618 172.338 1.00 16.00 ? 701  LEU A CB     1 
ATOM   4245 C  CG     . LEU A 1 701  ? 199.189 152.844 172.752 1.00 16.00 ? 701  LEU A CG     1 
ATOM   4246 C  CD1    . LEU A 1 701  ? 197.950 153.589 172.311 1.00 16.00 ? 701  LEU A CD1    1 
ATOM   4247 C  CD2    . LEU A 1 701  ? 199.230 151.453 172.175 1.00 16.00 ? 701  LEU A CD2    1 
ATOM   4248 N  N      . THR A 1 702  ? 203.458 154.859 172.530 1.00 16.79 ? 702  THR A N      1 
ATOM   4249 C  CA     . THR A 1 702  ? 204.546 155.522 171.831 1.00 16.79 ? 702  THR A CA     1 
ATOM   4250 C  C      . THR A 1 702  ? 205.852 154.744 171.958 1.00 16.79 ? 702  THR A C      1 
ATOM   4251 O  O      . THR A 1 702  ? 206.641 154.723 171.013 1.00 16.79 ? 702  THR A O      1 
ATOM   4252 C  CB     . THR A 1 702  ? 204.699 156.953 172.348 1.00 16.79 ? 702  THR A CB     1 
ATOM   4253 O  OG1    . THR A 1 702  ? 203.421 157.593 172.334 1.00 16.79 ? 702  THR A OG1    1 
ATOM   4254 C  CG2    . THR A 1 702  ? 205.608 157.759 171.439 1.00 16.79 ? 702  THR A CG2    1 
ATOM   4255 N  N      . ARG A 1 703  ? 206.091 154.069 173.086 1.00 18.03 ? 703  ARG A N      1 
ATOM   4256 C  CA     . ARG A 1 703  ? 207.263 153.201 173.170 1.00 18.03 ? 703  ARG A CA     1 
ATOM   4257 C  C      . ARG A 1 703  ? 207.087 151.939 172.339 1.00 18.03 ? 703  ARG A C      1 
ATOM   4258 O  O      . ARG A 1 703  ? 208.065 151.417 171.798 1.00 18.03 ? 703  ARG A O      1 
ATOM   4259 C  CB     . ARG A 1 703  ? 207.562 152.833 174.620 1.00 18.03 ? 703  ARG A CB     1 
ATOM   4260 C  CG     . ARG A 1 703  ? 208.010 153.997 175.460 1.00 18.03 ? 703  ARG A CG     1 
ATOM   4261 C  CD     . ARG A 1 703  ? 208.392 153.586 176.865 1.00 18.03 ? 703  ARG A CD     1 
ATOM   4262 N  NE     . ARG A 1 703  ? 208.643 154.756 177.699 1.00 18.03 ? 703  ARG A NE     1 
ATOM   4263 C  CZ     . ARG A 1 703  ? 209.813 155.378 177.785 1.00 18.03 ? 703  ARG A CZ     1 
ATOM   4264 N  NH1    . ARG A 1 703  ? 210.853 154.946 177.084 1.00 18.03 ? 703  ARG A NH1    1 
ATOM   4265 N  NH2    . ARG A 1 703  ? 209.942 156.438 178.571 1.00 18.03 ? 703  ARG A NH2    1 
ATOM   4266 N  N      . LEU A 1 704  ? 205.861 151.427 172.238 1.00 16.81 ? 704  LEU A N      1 
ATOM   4267 C  CA     . LEU A 1 704  ? 205.599 150.309 171.340 1.00 16.81 ? 704  LEU A CA     1 
ATOM   4268 C  C      . LEU A 1 704  ? 205.680 150.735 169.887 1.00 16.81 ? 704  LEU A C      1 
ATOM   4269 O  O      . LEU A 1 704  ? 206.051 149.933 169.028 1.00 16.81 ? 704  LEU A O      1 
ATOM   4270 C  CB     . LEU A 1 704  ? 204.227 149.707 171.629 1.00 16.81 ? 704  LEU A CB     1 
ATOM   4271 C  CG     . LEU A 1 704  ? 204.079 148.914 172.920 1.00 16.81 ? 704  LEU A CG     1 
ATOM   4272 C  CD1    . LEU A 1 704  ? 202.619 148.616 173.173 1.00 16.81 ? 704  LEU A CD1    1 
ATOM   4273 C  CD2    . LEU A 1 704  ? 204.874 147.630 172.823 1.00 16.81 ? 704  LEU A CD2    1 
ATOM   4274 N  N      . TRP A 1 705  ? 205.348 151.988 169.605 1.00 12.95 ? 705  TRP A N      1 
ATOM   4275 C  CA     . TRP A 1 705  ? 205.375 152.536 168.260 1.00 12.95 ? 705  TRP A CA     1 
ATOM   4276 C  C      . TRP A 1 705  ? 206.785 152.888 167.823 1.00 12.95 ? 705  TRP A C      1 
ATOM   4277 O  O      . TRP A 1 705  ? 207.076 152.875 166.628 1.00 12.95 ? 705  TRP A O      1 
ATOM   4278 C  CB     . TRP A 1 705  ? 204.455 153.751 168.231 1.00 12.95 ? 705  TRP A CB     1 
ATOM   4279 C  CG     . TRP A 1 705  ? 204.312 154.445 166.952 1.00 12.95 ? 705  TRP A CG     1 
ATOM   4280 C  CD1    . TRP A 1 705  ? 204.775 155.679 166.644 1.00 12.95 ? 705  TRP A CD1    1 
ATOM   4281 C  CD2    . TRP A 1 705  ? 203.638 153.964 165.792 1.00 12.95 ? 705  TRP A CD2    1 
ATOM   4282 N  NE1    . TRP A 1 705  ? 204.430 156.005 165.363 1.00 12.95 ? 705  TRP A NE1    1 
ATOM   4283 C  CE2    . TRP A 1 705  ? 203.735 154.961 164.814 1.00 12.95 ? 705  TRP A CE2    1 
ATOM   4284 C  CE3    . TRP A 1 705  ? 202.970 152.779 165.481 1.00 12.95 ? 705  TRP A CE3    1 
ATOM   4285 C  CZ2    . TRP A 1 705  ? 203.187 154.814 163.553 1.00 12.95 ? 705  TRP A CZ2    1 
ATOM   4286 C  CZ3    . TRP A 1 705  ? 202.422 152.640 164.237 1.00 12.95 ? 705  TRP A CZ3    1 
ATOM   4287 C  CH2    . TRP A 1 705  ? 202.530 153.646 163.289 1.00 12.95 ? 705  TRP A CH2    1 
ATOM   4288 N  N      . MET A 1 706  ? 207.671 153.180 168.763 1.00 20.25 ? 706  MET A N      1 
ATOM   4289 C  CA     . MET A 1 706  ? 209.071 153.469 168.481 1.00 20.25 ? 706  MET A CA     1 
ATOM   4290 C  C      . MET A 1 706  ? 209.848 152.325 169.125 1.00 20.25 ? 706  MET A C      1 
ATOM   4291 O  O      . MET A 1 706  ? 210.313 152.429 170.260 1.00 20.25 ? 706  MET A O      1 
ATOM   4292 C  CB     . MET A 1 706  ? 209.476 154.821 169.057 1.00 20.25 ? 706  MET A CB     1 
ATOM   4293 C  CG     . MET A 1 706  ? 208.539 155.964 168.698 1.00 20.25 ? 706  MET A CG     1 
ATOM   4294 S  SD     . MET A 1 706  ? 208.395 156.371 166.964 1.00 20.25 ? 706  MET A SD     1 
ATOM   4295 C  CE     . MET A 1 706  ? 209.916 157.253 166.758 1.00 20.25 ? 706  MET A CE     1 
ATOM   4296 N  N      . GLY A 1 707  ? 209.981 151.225 168.404 1.00 27.00 ? 707  GLY A N      1 
ATOM   4297 C  CA     . GLY A 1 707  ? 210.539 150.038 169.013 1.00 27.00 ? 707  GLY A CA     1 
ATOM   4298 C  C      . GLY A 1 707  ? 212.048 150.038 169.095 1.00 27.00 ? 707  GLY A C      1 
ATOM   4299 O  O      . GLY A 1 707  ? 212.724 149.774 168.093 1.00 27.00 ? 707  GLY A O      1 
ATOM   4300 N  N      . THR A 1 708  ? 212.563 150.290 170.306 1.00 34.00 ? 708  THR A N      1 
ATOM   4301 C  CA     . THR A 1 708  ? 213.992 150.424 170.615 1.00 34.00 ? 708  THR A CA     1 
ATOM   4302 C  C      . THR A 1 708  ? 214.614 151.490 169.709 1.00 34.00 ? 708  THR A C      1 
ATOM   4303 O  O      . THR A 1 708  ? 215.472 151.230 168.864 1.00 34.00 ? 708  THR A O      1 
ATOM   4304 C  CB     . THR A 1 708  ? 214.724 149.073 170.526 1.00 34.00 ? 708  THR A CB     1 
ATOM   4305 O  OG1    . THR A 1 708  ? 213.963 148.081 171.224 1.00 34.00 ? 708  THR A OG1    1 
ATOM   4306 C  CG2    . THR A 1 708  ? 216.086 149.141 171.211 1.00 34.00 ? 708  THR A CG2    1 
ATOM   4307 N  N      . MET A 1 709  ? 214.094 152.699 169.867 1.00 32.17 ? 709  MET A N      1 
ATOM   4308 C  CA     . MET A 1 709  ? 214.402 153.863 169.051 1.00 32.17 ? 709  MET A CA     1 
ATOM   4309 C  C      . MET A 1 709  ? 213.853 155.057 169.806 1.00 32.17 ? 709  MET A C      1 
ATOM   4310 O  O      . MET A 1 709  ? 212.857 154.928 170.524 1.00 32.17 ? 709  MET A O      1 
ATOM   4311 C  CB     . MET A 1 709  ? 213.790 153.742 167.646 1.00 32.17 ? 709  MET A CB     1 
ATOM   4312 C  CG     . MET A 1 709  ? 214.162 154.822 166.652 1.00 32.17 ? 709  MET A CG     1 
ATOM   4313 S  SD     . MET A 1 709  ? 213.679 154.406 164.960 1.00 32.17 ? 709  MET A SD     1 
ATOM   4314 C  CE     . MET A 1 709  ? 211.900 154.573 164.985 1.00 32.17 ? 709  MET A CE     1 
ATOM   4315 N  N      . ALA A 1 710  ? 214.537 156.195 169.683 1.00 29.85 ? 710  ALA A N      1 
ATOM   4316 C  CA     . ALA A 1 710  ? 214.180 157.374 170.459 1.00 29.85 ? 710  ALA A CA     1 
ATOM   4317 C  C      . ALA A 1 710  ? 212.796 157.873 170.075 1.00 29.85 ? 710  ALA A C      1 
ATOM   4318 O  O      . ALA A 1 710  ? 212.449 157.951 168.895 1.00 29.85 ? 710  ALA A O      1 
ATOM   4319 C  CB     . ALA A 1 710  ? 215.211 158.480 170.259 1.00 29.85 ? 710  ALA A CB     1 
ATOM   4320 N  N      . MET A 1 711  ? 212.002 158.212 171.093 1.00 26.39 ? 711  MET A N      1 
ATOM   4321 C  CA     . MET A 1 711  ? 210.568 158.446 170.957 1.00 26.39 ? 711  MET A CA     1 
ATOM   4322 C  C      . MET A 1 711  ? 210.227 159.721 170.204 1.00 26.39 ? 711  MET A C      1 
ATOM   4323 O  O      . MET A 1 711  ? 209.040 159.999 170.014 1.00 26.39 ? 711  MET A O      1 
ATOM   4324 C  CB     . MET A 1 711  ? 209.919 158.483 172.339 1.00 26.39 ? 711  MET A CB     1 
ATOM   4325 C  CG     . MET A 1 711  ? 209.931 157.154 173.067 1.00 26.39 ? 711  MET A CG     1 
ATOM   4326 S  SD     . MET A 1 711  ? 209.379 157.303 174.775 1.00 26.39 ? 711  MET A SD     1 
ATOM   4327 C  CE     . MET A 1 711  ? 207.639 157.614 174.554 1.00 26.39 ? 711  MET A CE     1 
ATOM   4328 N  N      . ASN A 1 712  ? 211.218 160.500 169.774 1.00 27.29 ? 712  ASN A N      1 
ATOM   4329 C  CA     . ASN A 1 712  ? 210.978 161.742 169.054 1.00 27.29 ? 712  ASN A CA     1 
ATOM   4330 C  C      . ASN A 1 712  ? 211.766 161.822 167.750 1.00 27.29 ? 712  ASN A C      1 
ATOM   4331 O  O      . ASN A 1 712  ? 212.002 162.926 167.250 1.00 27.29 ? 712  ASN A O      1 
ATOM   4332 C  CB     . ASN A 1 712  ? 211.289 162.944 169.953 1.00 27.29 ? 712  ASN A CB     1 
ATOM   4333 C  CG     . ASN A 1 712  ? 212.696 162.907 170.539 1.00 27.29 ? 712  ASN A CG     1 
ATOM   4334 O  OD1    . ASN A 1 712  ? 213.501 162.028 170.233 1.00 27.29 ? 712  ASN A OD1    1 
ATOM   4335 N  ND2    . ASN A 1 712  ? 212.993 163.875 171.394 1.00 27.29 ? 712  ASN A ND2    1 
ATOM   4336 N  N      . THR A 1 713  ? 212.192 160.690 167.194 1.00 27.18 ? 713  THR A N      1 
ATOM   4337 C  CA     . THR A 1 713  ? 212.819 160.724 165.880 1.00 27.18 ? 713  THR A CA     1 
ATOM   4338 C  C      . THR A 1 713  ? 211.743 160.936 164.828 1.00 27.18 ? 713  THR A C      1 
ATOM   4339 O  O      . THR A 1 713  ? 210.691 160.293 164.858 1.00 27.18 ? 713  THR A O      1 
ATOM   4340 C  CB     . THR A 1 713  ? 213.604 159.444 165.591 1.00 27.18 ? 713  THR A CB     1 
ATOM   4341 O  OG1    . THR A 1 713  ? 212.720 158.328 165.538 1.00 27.18 ? 713  THR A OG1    1 
ATOM   4342 C  CG2    . THR A 1 713  ? 214.647 159.199 166.659 1.00 27.18 ? 713  THR A CG2    1 
ATOM   4343 N  N      . ARG A 1 714  ? 211.995 161.862 163.913 1.00 27.97 ? 714  ARG A N      1 
ATOM   4344 C  CA     . ARG A 1 714  ? 210.974 162.284 162.976 1.00 27.97 ? 714  ARG A CA     1 
ATOM   4345 C  C      . ARG A 1 714  ? 210.902 161.316 161.803 1.00 27.97 ? 714  ARG A C      1 
ATOM   4346 O  O      . ARG A 1 714  ? 211.759 160.448 161.628 1.00 27.97 ? 714  ARG A O      1 
ATOM   4347 C  CB     . ARG A 1 714  ? 211.258 163.705 162.506 1.00 27.97 ? 714  ARG A CB     1 
ATOM   4348 C  CG     . ARG A 1 714  ? 211.244 164.726 163.627 1.00 27.97 ? 714  ARG A CG     1 
ATOM   4349 C  CD     . ARG A 1 714  ? 209.846 164.905 164.178 1.00 27.97 ? 714  ARG A CD     1 
ATOM   4350 N  NE     . ARG A 1 714  ? 208.922 165.366 163.147 1.00 27.97 ? 714  ARG A NE     1 
ATOM   4351 C  CZ     . ARG A 1 714  ? 208.739 166.640 162.821 1.00 27.97 ? 714  ARG A CZ     1 
ATOM   4352 N  NH1    . ARG A 1 714  ? 209.415 167.594 163.447 1.00 27.97 ? 714  ARG A NH1    1 
ATOM   4353 N  NH2    . ARG A 1 714  ? 207.878 166.962 161.868 1.00 27.97 ? 714  ARG A NH2    1 
ATOM   4354 N  N      . TRP A 1 715  ? 209.849 161.471 160.997 1.00 28.84 ? 715  TRP A N      1 
ATOM   4355 C  CA     . TRP A 1 715  ? 209.573 160.520 159.926 1.00 28.84 ? 715  TRP A CA     1 
ATOM   4356 C  C      . TRP A 1 715  ? 210.605 160.597 158.812 1.00 28.84 ? 715  TRP A C      1 
ATOM   4357 O  O      . TRP A 1 715  ? 210.856 159.594 158.138 1.00 28.84 ? 715  TRP A O      1 
ATOM   4358 C  CB     . TRP A 1 715  ? 208.176 160.765 159.359 1.00 28.84 ? 715  TRP A CB     1 
ATOM   4359 C  CG     . TRP A 1 715  ? 208.018 162.130 158.760 1.00 28.84 ? 715  TRP A CG     1 
ATOM   4360 C  CD1    . TRP A 1 715  ? 207.628 163.264 159.404 1.00 28.84 ? 715  TRP A CD1    1 
ATOM   4361 C  CD2    . TRP A 1 715  ? 208.264 162.507 157.400 1.00 28.84 ? 715  TRP A CD2    1 
ATOM   4362 N  NE1    . TRP A 1 715  ? 207.612 164.321 158.532 1.00 28.84 ? 715  TRP A NE1    1 
ATOM   4363 C  CE2    . TRP A 1 715  ? 207.999 163.882 157.294 1.00 28.84 ? 715  TRP A CE2    1 
ATOM   4364 C  CE3    . TRP A 1 715  ? 208.681 161.811 156.261 1.00 28.84 ? 715  TRP A CE3    1 
ATOM   4365 C  CZ2    . TRP A 1 715  ? 208.137 164.576 156.098 1.00 28.84 ? 715  TRP A CZ2    1 
ATOM   4366 C  CZ3    . TRP A 1 715  ? 208.819 162.501 155.079 1.00 28.84 ? 715  TRP A CZ3    1 
ATOM   4367 C  CH2    . TRP A 1 715  ? 208.547 163.869 155.004 1.00 28.84 ? 715  TRP A CH2    1 
ATOM   4368 N  N      . TRP A 1 716  ? 211.207 161.768 158.602 1.00 30.32 ? 716  TRP A N      1 
ATOM   4369 C  CA     . TRP A 1 716  ? 212.148 161.927 157.502 1.00 30.32 ? 716  TRP A CA     1 
ATOM   4370 C  C      . TRP A 1 716  ? 213.484 161.263 157.804 1.00 30.32 ? 716  TRP A C      1 
ATOM   4371 O  O      . TRP A 1 716  ? 214.133 160.754 156.886 1.00 30.32 ? 716  TRP A O      1 
ATOM   4372 C  CB     . TRP A 1 716  ? 212.326 163.409 157.174 1.00 30.32 ? 716  TRP A CB     1 
ATOM   4373 C  CG     . TRP A 1 716  ? 212.814 164.247 158.308 1.00 30.32 ? 716  TRP A CG     1 
ATOM   4374 C  CD1    . TRP A 1 716  ? 212.055 164.877 159.248 1.00 30.32 ? 716  TRP A CD1    1 
ATOM   4375 C  CD2    . TRP A 1 716  ? 214.173 164.567 158.609 1.00 30.32 ? 716  TRP A CD2    1 
ATOM   4376 N  NE1    . TRP A 1 716  ? 212.859 165.562 160.123 1.00 30.32 ? 716  TRP A NE1    1 
ATOM   4377 C  CE2    . TRP A 1 716  ? 214.165 165.383 159.754 1.00 30.32 ? 716  TRP A CE2    1 
ATOM   4378 C  CE3    . TRP A 1 716  ? 215.399 164.232 158.028 1.00 30.32 ? 716  TRP A CE3    1 
ATOM   4379 C  CZ2    . TRP A 1 716  ? 215.334 165.874 160.327 1.00 30.32 ? 716  TRP A CZ2    1 
ATOM   4380 C  CZ3    . TRP A 1 716  ? 216.555 164.717 158.595 1.00 30.32 ? 716  TRP A CZ3    1 
ATOM   4381 C  CH2    . TRP A 1 716  ? 216.517 165.530 159.734 1.00 30.32 ? 716  TRP A CH2    1 
ATOM   4382 N  N      . LYS A 1 717  ? 213.892 161.223 159.076 1.00 32.32 ? 717  LYS A N      1 
ATOM   4383 C  CA     . LYS A 1 717  ? 215.077 160.458 159.456 1.00 32.32 ? 717  LYS A CA     1 
ATOM   4384 C  C      . LYS A 1 717  ? 214.849 158.966 159.265 1.00 32.32 ? 717  LYS A C      1 
ATOM   4385 O  O      . LYS A 1 717  ? 215.737 158.252 158.783 1.00 32.32 ? 717  LYS A O      1 
ATOM   4386 C  CB     . LYS A 1 717  ? 215.452 160.747 160.906 1.00 32.32 ? 717  LYS A CB     1 
ATOM   4387 C  CG     . LYS A 1 717  ? 215.982 162.141 161.160 1.00 32.32 ? 717  LYS A CG     1 
ATOM   4388 C  CD     . LYS A 1 717  ? 216.351 162.316 162.621 1.00 32.32 ? 717  LYS A CD     1 
ATOM   4389 C  CE     . LYS A 1 717  ? 216.867 163.712 162.903 1.00 32.32 ? 717  LYS A CE     1 
ATOM   4390 N  NZ     . LYS A 1 717  ? 217.213 163.888 164.338 1.00 32.32 ? 717  LYS A NZ     1 
ATOM   4391 N  N      . VAL A 1 718  ? 213.650 158.494 159.612 1.00 31.31 ? 718  VAL A N      1 
ATOM   4392 C  CA     . VAL A 1 718  ? 213.283 157.095 159.416 1.00 31.31 ? 718  VAL A CA     1 
ATOM   4393 C  C      . VAL A 1 718  ? 213.245 156.761 157.932 1.00 31.31 ? 718  VAL A C      1 
ATOM   4394 O  O      . VAL A 1 718  ? 213.680 155.684 157.510 1.00 31.31 ? 718  VAL A O      1 
ATOM   4395 C  CB     . VAL A 1 718  ? 211.935 156.812 160.107 1.00 31.31 ? 718  VAL A CB     1 
ATOM   4396 C  CG1    . VAL A 1 718  ? 211.481 155.385 159.879 1.00 31.31 ? 718  VAL A CG1    1 
ATOM   4397 C  CG2    . VAL A 1 718  ? 212.043 157.104 161.588 1.00 31.31 ? 718  VAL A CG2    1 
ATOM   4398 N  N      . LEU A 1 719  ? 212.789 157.705 157.113 1.00 33.55 ? 719  LEU A N      1 
ATOM   4399 C  CA     . LEU A 1 719  ? 212.728 157.489 155.673 1.00 33.55 ? 719  LEU A CA     1 
ATOM   4400 C  C      . LEU A 1 719  ? 214.115 157.466 155.038 1.00 33.55 ? 719  LEU A C      1 
ATOM   4401 O  O      . LEU A 1 719  ? 214.400 156.596 154.207 1.00 33.55 ? 719  LEU A O      1 
ATOM   4402 C  CB     . LEU A 1 719  ? 211.855 158.564 155.034 1.00 33.55 ? 719  LEU A CB     1 
ATOM   4403 C  CG     . LEU A 1 719  ? 211.736 158.546 153.516 1.00 33.55 ? 719  LEU A CG     1 
ATOM   4404 C  CD1    . LEU A 1 719  ? 211.231 157.212 153.043 1.00 33.55 ? 719  LEU A CD1    1 
ATOM   4405 C  CD2    . LEU A 1 719  ? 210.800 159.648 153.075 1.00 33.55 ? 719  LEU A CD2    1 
ATOM   4406 N  N      . VAL A 1 720  ? 214.989 158.407 155.401 1.00 36.91 ? 720  VAL A N      1 
ATOM   4407 C  CA     . VAL A 1 720  ? 216.319 158.411 154.802 1.00 36.91 ? 720  VAL A CA     1 
ATOM   4408 C  C      . VAL A 1 720  ? 217.218 157.321 155.372 1.00 36.91 ? 720  VAL A C      1 
ATOM   4409 O  O      . VAL A 1 720  ? 218.232 156.990 154.750 1.00 36.91 ? 720  VAL A O      1 
ATOM   4410 C  CB     . VAL A 1 720  ? 217.020 159.774 154.941 1.00 36.91 ? 720  VAL A CB     1 
ATOM   4411 C  CG1    . VAL A 1 720  ? 216.202 160.862 154.266 1.00 36.91 ? 720  VAL A CG1    1 
ATOM   4412 C  CG2    . VAL A 1 720  ? 217.306 160.107 156.393 1.00 36.91 ? 720  VAL A CG2    1 
ATOM   4413 N  N      . CYS A 1 721  ? 216.887 156.753 156.532 1.00 40.11 ? 721  CYS A N      1 
ATOM   4414 C  CA     . CYS A 1 721  ? 217.608 155.602 157.057 1.00 40.11 ? 721  CYS A CA     1 
ATOM   4415 C  C      . CYS A 1 721  ? 216.894 154.294 156.776 1.00 40.11 ? 721  CYS A C      1 
ATOM   4416 O  O      . CYS A 1 721  ? 217.359 153.238 157.207 1.00 40.11 ? 721  CYS A O      1 
ATOM   4417 C  CB     . CYS A 1 721  ? 217.820 155.762 158.558 1.00 40.11 ? 721  CYS A CB     1 
ATOM   4418 S  SG     . CYS A 1 721  ? 218.806 157.192 158.957 1.00 40.11 ? 721  CYS A SG     1 
ATOM   4419 N  N      . LEU A 1 722  ? 215.771 154.348 156.073 1.00 37.54 ? 722  LEU A N      1 
ATOM   4420 C  CA     . LEU A 1 722  ? 214.938 153.193 155.787 1.00 37.54 ? 722  LEU A CA     1 
ATOM   4421 C  C      . LEU A 1 722  ? 215.305 152.560 154.455 1.00 37.54 ? 722  LEU A C      1 
ATOM   4422 O  O      . LEU A 1 722  ? 215.262 151.334 154.317 1.00 37.54 ? 722  LEU A O      1 
ATOM   4423 C  CB     . LEU A 1 722  ? 213.473 153.627 155.793 1.00 37.54 ? 722  LEU A CB     1 
ATOM   4424 C  CG     . LEU A 1 722  ? 212.322 152.638 155.740 1.00 37.54 ? 722  LEU A CG     1 
ATOM   4425 C  CD1    . LEU A 1 722  ? 212.296 151.799 156.992 1.00 37.54 ? 722  LEU A CD1    1 
ATOM   4426 C  CD2    . LEU A 1 722  ? 211.052 153.422 155.609 1.00 37.54 ? 722  LEU A CD2    1 
ATOM   4427 N  N      . TYR A 1 723  ? 215.673 153.381 153.477 1.00 42.83 ? 723  TYR A N      1 
ATOM   4428 C  CA     . TYR A 1 723  ? 216.172 152.910 152.195 1.00 42.83 ? 723  TYR A CA     1 
ATOM   4429 C  C      . TYR A 1 723  ? 217.680 153.051 152.073 1.00 42.83 ? 723  TYR A C      1 
ATOM   4430 O  O      . TYR A 1 723  ? 218.250 152.636 151.061 1.00 42.83 ? 723  TYR A O      1 
ATOM   4431 C  CB     . TYR A 1 723  ? 215.470 153.656 151.058 1.00 42.83 ? 723  TYR A CB     1 
ATOM   4432 C  CG     . TYR A 1 723  ? 213.996 153.344 151.005 1.00 42.83 ? 723  TYR A CG     1 
ATOM   4433 C  CD1    . TYR A 1 723  ? 213.540 152.166 150.430 1.00 42.83 ? 723  TYR A CD1    1 
ATOM   4434 C  CD2    . TYR A 1 723  ? 213.063 154.209 151.560 1.00 42.83 ? 723  TYR A CD2    1 
ATOM   4435 C  CE1    . TYR A 1 723  ? 212.195 151.867 150.393 1.00 42.83 ? 723  TYR A CE1    1 
ATOM   4436 C  CE2    . TYR A 1 723  ? 211.716 153.918 151.529 1.00 42.83 ? 723  TYR A CE2    1 
ATOM   4437 C  CZ     . TYR A 1 723  ? 211.289 152.746 150.942 1.00 42.83 ? 723  TYR A CZ     1 
ATOM   4438 O  OH     . TYR A 1 723  ? 209.948 152.445 150.904 1.00 42.83 ? 723  TYR A OH     1 
ATOM   4439 N  N      . LEU A 1 724  ? 218.338 153.624 153.080 1.00 47.28 ? 724  LEU A N      1 
ATOM   4440 C  CA     . LEU A 1 724  ? 219.796 153.674 153.161 1.00 47.28 ? 724  LEU A CA     1 
ATOM   4441 C  C      . LEU A 1 724  ? 220.221 153.062 154.489 1.00 47.28 ? 724  LEU A C      1 
ATOM   4442 O  O      . LEU A 1 724  ? 220.302 153.759 155.509 1.00 47.28 ? 724  LEU A O      1 
ATOM   4443 C  CB     . LEU A 1 724  ? 220.324 155.101 153.024 1.00 47.28 ? 724  LEU A CB     1 
ATOM   4444 C  CG     . LEU A 1 724  ? 220.516 155.720 151.636 1.00 47.28 ? 724  LEU A CG     1 
ATOM   4445 C  CD1    . LEU A 1 724  ? 219.204 156.113 150.975 1.00 47.28 ? 724  LEU A CD1    1 
ATOM   4446 C  CD2    . LEU A 1 724  ? 221.444 156.919 151.732 1.00 47.28 ? 724  LEU A CD2    1 
ATOM   4447 N  N      . PRO A 1 725  ? 220.508 151.756 154.518 1.00 50.91 ? 725  PRO A N      1 
ATOM   4448 C  CA     . PRO A 1 725  ? 220.967 151.127 155.766 1.00 50.91 ? 725  PRO A CA     1 
ATOM   4449 C  C      . PRO A 1 725  ? 222.453 151.320 156.058 1.00 50.91 ? 725  PRO A C      1 
ATOM   4450 O  O      . PRO A 1 725  ? 223.029 150.559 156.842 1.00 50.91 ? 725  PRO A O      1 
ATOM   4451 C  CB     . PRO A 1 725  ? 220.643 149.643 155.548 1.00 50.91 ? 725  PRO A CB     1 
ATOM   4452 C  CG     . PRO A 1 725  ? 219.632 149.621 154.450 1.00 50.91 ? 725  PRO A CG     1 
ATOM   4453 C  CD     . PRO A 1 725  ? 220.024 150.753 153.558 1.00 50.91 ? 725  PRO A CD     1 
ATOM   4454 N  N      . VAL A 1 726  ? 223.098 152.284 155.401 1.00 53.64 ? 726  VAL A N      1 
ATOM   4455 C  CA     . VAL A 1 726  ? 224.433 152.714 155.779 1.00 53.64 ? 726  VAL A CA     1 
ATOM   4456 C  C      . VAL A 1 726  ? 224.420 154.083 156.462 1.00 53.64 ? 726  VAL A C      1 
ATOM   4457 O  O      . VAL A 1 726  ? 225.283 154.351 157.307 1.00 53.64 ? 726  VAL A O      1 
ATOM   4458 C  CB     . VAL A 1 726  ? 225.373 152.705 154.546 1.00 53.64 ? 726  VAL A CB     1 
ATOM   4459 C  CG1    . VAL A 1 726  ? 224.986 153.767 153.510 1.00 53.64 ? 726  VAL A CG1    1 
ATOM   4460 C  CG2    . VAL A 1 726  ? 226.849 152.808 154.944 1.00 53.64 ? 726  VAL A CG2    1 
ATOM   4461 N  N      . LEU A 1 727  ? 223.399 154.887 156.181 1.00 50.61 ? 727  LEU A N      1 
ATOM   4462 C  CA     . LEU A 1 727  ? 223.253 156.196 156.810 1.00 50.61 ? 727  LEU A CA     1 
ATOM   4463 C  C      . LEU A 1 727  ? 222.335 156.095 158.034 1.00 50.61 ? 727  LEU A C      1 
ATOM   4464 O  O      . LEU A 1 727  ? 221.832 157.103 158.532 1.00 50.61 ? 727  LEU A O      1 
ATOM   4465 C  CB     . LEU A 1 727  ? 222.696 157.213 155.813 1.00 50.61 ? 727  LEU A CB     1 
ATOM   4466 C  CG     . LEU A 1 727  ? 222.464 158.628 156.348 1.00 50.61 ? 727  LEU A CG     1 
ATOM   4467 C  CD1    . LEU A 1 727  ? 223.767 159.237 156.843 1.00 50.61 ? 727  LEU A CD1    1 
ATOM   4468 C  CD2    . LEU A 1 727  ? 221.827 159.508 155.284 1.00 50.61 ? 727  LEU A CD2    1 
ATOM   4469 N  N      . ILE A 1 728  ? 222.127 154.869 158.508 1.00 49.79 ? 728  ILE A N      1 
ATOM   4470 C  CA     . ILE A 1 728  ? 221.281 154.588 159.659 1.00 49.79 ? 728  ILE A CA     1 
ATOM   4471 C  C      . ILE A 1 728  ? 222.019 154.818 160.976 1.00 49.79 ? 728  ILE A C      1 
ATOM   4472 O  O      . ILE A 1 728  ? 221.401 155.166 161.987 1.00 49.79 ? 728  ILE A O      1 
ATOM   4473 C  CB     . ILE A 1 728  ? 220.765 153.146 159.507 1.00 49.79 ? 728  ILE A CB     1 
ATOM   4474 C  CG1    . ILE A 1 728  ? 219.729 152.773 160.554 1.00 49.79 ? 728  ILE A CG1    1 
ATOM   4475 C  CG2    . ILE A 1 728  ? 221.911 152.140 159.479 1.00 49.79 ? 728  ILE A CG2    1 
ATOM   4476 C  CD1    . ILE A 1 728  ? 219.142 151.449 160.236 1.00 49.79 ? 728  ILE A CD1    1 
ATOM   4477 N  N      . PHE A 1 729  ? 223.338 154.659 160.981 1.00 52.50 ? 729  PHE A N      1 
ATOM   4478 C  CA     . PHE A 1 729  ? 224.195 154.753 162.156 1.00 52.50 ? 729  PHE A CA     1 
ATOM   4479 C  C      . PHE A 1 729  ? 224.387 156.168 162.718 1.00 52.50 ? 729  PHE A C      1 
ATOM   4480 O  O      . PHE A 1 729  ? 224.400 156.300 163.948 1.00 52.50 ? 729  PHE A O      1 
ATOM   4481 C  CB     . PHE A 1 729  ? 225.556 154.112 161.848 1.00 52.50 ? 729  PHE A CB     1 
ATOM   4482 C  CG     . PHE A 1 729  ? 225.514 152.610 161.726 1.00 52.50 ? 729  PHE A CG     1 
ATOM   4483 C  CD1    . PHE A 1 729  ? 224.473 151.878 162.277 1.00 52.50 ? 729  PHE A CD1    1 
ATOM   4484 C  CD2    . PHE A 1 729  ? 226.515 151.933 161.043 1.00 52.50 ? 729  PHE A CD2    1 
ATOM   4485 C  CE1    . PHE A 1 729  ? 224.437 150.496 162.159 1.00 52.50 ? 729  PHE A CE1    1 
ATOM   4486 C  CE2    . PHE A 1 729  ? 226.485 150.551 160.919 1.00 52.50 ? 729  PHE A CE2    1 
ATOM   4487 C  CZ     . PHE A 1 729  ? 225.445 149.833 161.477 1.00 52.50 ? 729  PHE A CZ     1 
ATOM   4488 N  N      . PRO A 1 730  ? 224.560 157.244 161.923 1.00 49.98 ? 730  PRO A N      1 
ATOM   4489 C  CA     . PRO A 1 730  ? 224.735 158.550 162.584 1.00 49.98 ? 730  PRO A CA     1 
ATOM   4490 C  C      . PRO A 1 730  ? 223.471 159.137 163.190 1.00 49.98 ? 730  PRO A C      1 
ATOM   4491 O  O      . PRO A 1 730  ? 223.532 159.679 164.300 1.00 49.98 ? 730  PRO A O      1 
ATOM   4492 C  CB     . PRO A 1 730  ? 225.275 159.446 161.460 1.00 49.98 ? 730  PRO A CB     1 
ATOM   4493 C  CG     . PRO A 1 730  ? 225.837 158.530 160.475 1.00 49.98 ? 730  PRO A CG     1 
ATOM   4494 C  CD     . PRO A 1 730  ? 224.927 157.368 160.495 1.00 49.98 ? 730  PRO A CD     1 
ATOM   4495 N  N      . ILE A 1 731  ? 222.329 159.066 162.508 1.00 45.14 ? 731  ILE A N      1 
ATOM   4496 C  CA     . ILE A 1 731  ? 221.254 160.002 162.809 1.00 45.14 ? 731  ILE A CA     1 
ATOM   4497 C  C      . ILE A 1 731  ? 219.992 159.319 163.339 1.00 45.14 ? 731  ILE A C      1 
ATOM   4498 O  O      . ILE A 1 731  ? 218.938 159.939 163.373 1.00 45.14 ? 731  ILE A O      1 
ATOM   4499 C  CB     . ILE A 1 731  ? 220.926 160.880 161.587 1.00 45.14 ? 731  ILE A CB     1 
ATOM   4500 C  CG1    . ILE A 1 731  ? 220.484 160.011 160.416 1.00 45.14 ? 731  ILE A CG1    1 
ATOM   4501 C  CG2    . ILE A 1 731  ? 222.118 161.747 161.207 1.00 45.14 ? 731  ILE A CG2    1 
ATOM   4502 C  CD1    . ILE A 1 731  ? 219.863 160.791 159.293 1.00 45.14 ? 731  ILE A CD1    1 
ATOM   4503 N  N      . ILE A 1 732  ? 220.068 158.064 163.770 1.00 40.92 ? 732  ILE A N      1 
ATOM   4504 C  CA     . ILE A 1 732  ? 218.964 157.433 164.490 1.00 40.92 ? 732  ILE A CA     1 
ATOM   4505 C  C      . ILE A 1 732  ? 219.465 157.054 165.874 1.00 40.92 ? 732  ILE A C      1 
ATOM   4506 O  O      . ILE A 1 732  ? 220.401 156.256 166.007 1.00 40.92 ? 732  ILE A O      1 
ATOM   4507 C  CB     . ILE A 1 732  ? 218.396 156.208 163.756 1.00 40.92 ? 732  ILE A CB     1 
ATOM   4508 C  CG1    . ILE A 1 732  ? 217.817 156.601 162.402 1.00 40.92 ? 732  ILE A CG1    1 
ATOM   4509 C  CG2    . ILE A 1 732  ? 217.288 155.586 164.570 1.00 40.92 ? 732  ILE A CG2    1 
ATOM   4510 C  CD1    . ILE A 1 732  ? 216.635 157.539 162.485 1.00 40.92 ? 732  ILE A CD1    1 
ATOM   4511 N  N      . TYR A 1 733  ? 218.842 157.621 166.899 1.00 40.83 ? 733  TYR A N      1 
ATOM   4512 C  CA     . TYR A 1 733  ? 219.238 157.402 168.280 1.00 40.83 ? 733  TYR A CA     1 
ATOM   4513 C  C      . TYR A 1 733  ? 218.371 156.320 168.906 1.00 40.83 ? 733  TYR A C      1 
ATOM   4514 O  O      . TYR A 1 733  ? 217.155 156.288 168.705 1.00 40.83 ? 733  TYR A O      1 
ATOM   4515 C  CB     . TYR A 1 733  ? 219.130 158.695 169.088 1.00 40.83 ? 733  TYR A CB     1 
ATOM   4516 C  CG     . TYR A 1 733  ? 220.123 159.749 168.663 1.00 40.83 ? 733  TYR A CG     1 
ATOM   4517 C  CD1    . TYR A 1 733  ? 221.430 159.730 169.134 1.00 40.83 ? 733  TYR A CD1    1 
ATOM   4518 C  CD2    . TYR A 1 733  ? 219.759 160.752 167.775 1.00 40.83 ? 733  TYR A CD2    1 
ATOM   4519 C  CE1    . TYR A 1 733  ? 222.345 160.689 168.741 1.00 40.83 ? 733  TYR A CE1    1 
ATOM   4520 C  CE2    . TYR A 1 733  ? 220.665 161.716 167.373 1.00 40.83 ? 733  TYR A CE2    1 
ATOM   4521 C  CZ     . TYR A 1 733  ? 221.957 161.680 167.859 1.00 40.83 ? 733  TYR A CZ     1 
ATOM   4522 O  OH     . TYR A 1 733  ? 222.861 162.638 167.462 1.00 40.83 ? 733  TYR A OH     1 
ATOM   4523 N  N      . PHE A 1 734  ? 219.006 155.434 169.659 1.00 39.87 ? 734  PHE A N      1 
ATOM   4524 C  CA     . PHE A 1 734  ? 218.330 154.319 170.298 1.00 39.87 ? 734  PHE A CA     1 
ATOM   4525 C  C      . PHE A 1 734  ? 218.276 154.545 171.799 1.00 39.87 ? 734  PHE A C      1 
ATOM   4526 O  O      . PHE A 1 734  ? 219.200 155.122 172.380 1.00 39.87 ? 734  PHE A O      1 
ATOM   4527 C  CB     . PHE A 1 734  ? 219.039 153.006 169.982 1.00 39.87 ? 734  PHE A CB     1 
ATOM   4528 C  CG     . PHE A 1 734  ? 218.854 152.545 168.568 1.00 39.87 ? 734  PHE A CG     1 
ATOM   4529 C  CD1    . PHE A 1 734  ? 217.840 153.058 167.780 1.00 39.87 ? 734  PHE A CD1    1 
ATOM   4530 C  CD2    . PHE A 1 734  ? 219.694 151.601 168.024 1.00 39.87 ? 734  PHE A CD2    1 
ATOM   4531 C  CE1    . PHE A 1 734  ? 217.662 152.628 166.488 1.00 39.87 ? 734  PHE A CE1    1 
ATOM   4532 C  CE2    . PHE A 1 734  ? 219.521 151.180 166.728 1.00 39.87 ? 734  PHE A CE2    1 
ATOM   4533 C  CZ     . PHE A 1 734  ? 218.505 151.697 165.960 1.00 39.87 ? 734  PHE A CZ     1 
ATOM   4534 N  N      . VAL A 1 735  ? 217.180 154.116 172.414 1.00 39.16 ? 735  VAL A N      1 
ATOM   4535 C  CA     . VAL A 1 735  ? 216.988 154.249 173.857 1.00 39.16 ? 735  VAL A CA     1 
ATOM   4536 C  C      . VAL A 1 735  ? 217.998 153.452 174.689 1.00 39.16 ? 735  VAL A C      1 
ATOM   4537 O  O      . VAL A 1 735  ? 218.181 153.797 175.867 1.00 39.16 ? 735  VAL A O      1 
ATOM   4538 C  CB     . VAL A 1 735  ? 215.532 153.934 174.253 1.00 39.16 ? 735  VAL A CB     1 
ATOM   4539 C  CG1    . VAL A 1 735  ? 214.626 155.051 173.775 1.00 39.16 ? 735  VAL A CG1    1 
ATOM   4540 C  CG2    . VAL A 1 735  ? 215.045 152.636 173.649 1.00 39.16 ? 735  VAL A CG2    1 
ATOM   4541 N  N      . PRO A 1 736  ? 218.670 152.386 174.175 1.00 39.12 ? 736  PRO A N      1 
ATOM   4542 C  CA     . PRO A 1 736  ? 219.877 152.102 174.963 1.00 39.12 ? 736  PRO A CA     1 
ATOM   4543 C  C      . PRO A 1 736  ? 221.010 153.078 174.656 1.00 39.12 ? 736  PRO A C      1 
ATOM   4544 O  O      . PRO A 1 736  ? 221.527 153.064 173.538 1.00 39.12 ? 736  PRO A O      1 
ATOM   4545 C  CB     . PRO A 1 736  ? 220.260 150.683 174.534 1.00 39.12 ? 736  PRO A CB     1 
ATOM   4546 C  CG     . PRO A 1 736  ? 219.021 150.098 174.001 1.00 39.12 ? 736  PRO A CG     1 
ATOM   4547 C  CD     . PRO A 1 736  ? 218.333 151.228 173.322 1.00 39.12 ? 736  PRO A CD     1 
ATOM   4548 N  N      . PHE A 1 826  ? 226.860 146.201 162.978 1.00 67.96 ? 826  PHE A N      1 
ATOM   4549 C  CA     . PHE A 1 826  ? 226.729 144.943 162.258 1.00 67.96 ? 826  PHE A CA     1 
ATOM   4550 C  C      . PHE A 1 826  ? 225.298 144.815 161.737 1.00 67.96 ? 826  PHE A C      1 
ATOM   4551 O  O      . PHE A 1 826  ? 224.988 145.285 160.641 1.00 67.96 ? 826  PHE A O      1 
ATOM   4552 C  CB     . PHE A 1 826  ? 227.107 143.763 163.163 1.00 67.96 ? 826  PHE A CB     1 
ATOM   4553 C  CG     . PHE A 1 826  ? 227.162 142.433 162.454 1.00 67.96 ? 826  PHE A CG     1 
ATOM   4554 C  CD1    . PHE A 1 826  ? 228.192 142.146 161.569 1.00 67.96 ? 826  PHE A CD1    1 
ATOM   4555 C  CD2    . PHE A 1 826  ? 226.206 141.456 162.702 1.00 67.96 ? 826  PHE A CD2    1 
ATOM   4556 C  CE1    . PHE A 1 826  ? 228.251 140.922 160.922 1.00 67.96 ? 826  PHE A CE1    1 
ATOM   4557 C  CE2    . PHE A 1 826  ? 226.261 140.230 162.059 1.00 67.96 ? 826  PHE A CE2    1 
ATOM   4558 C  CZ     . PHE A 1 826  ? 227.286 139.963 161.170 1.00 67.96 ? 826  PHE A CZ     1 
ATOM   4559 N  N      . CYS A 1 827  ? 224.426 144.184 162.525 1.00 61.20 ? 827  CYS A N      1 
ATOM   4560 C  CA     . CYS A 1 827  ? 223.022 144.063 162.161 1.00 61.20 ? 827  CYS A CA     1 
ATOM   4561 C  C      . CYS A 1 827  ? 222.066 144.281 163.325 1.00 61.20 ? 827  CYS A C      1 
ATOM   4562 O  O      . CYS A 1 827  ? 220.852 144.228 163.111 1.00 61.20 ? 827  CYS A O      1 
ATOM   4563 C  CB     . CYS A 1 827  ? 222.739 142.685 161.533 1.00 61.20 ? 827  CYS A CB     1 
ATOM   4564 S  SG     . CYS A 1 827  ? 223.475 142.418 159.901 1.00 61.20 ? 827  CYS A SG     1 
ATOM   4565 N  N      . ASP A 1 828  ? 222.567 144.522 164.539 1.00 51.39 ? 828  ASP A N      1 
ATOM   4566 C  CA     . ASP A 1 828  ? 221.687 144.696 165.692 1.00 51.39 ? 828  ASP A CA     1 
ATOM   4567 C  C      . ASP A 1 828  ? 220.937 146.021 165.621 1.00 51.39 ? 828  ASP A C      1 
ATOM   4568 O  O      . ASP A 1 828  ? 219.724 146.071 165.866 1.00 51.39 ? 828  ASP A O      1 
ATOM   4569 C  CB     . ASP A 1 828  ? 222.503 144.604 166.979 1.00 51.39 ? 828  ASP A CB     1 
ATOM   4570 C  CG     . ASP A 1 828  ? 221.638 144.565 168.214 1.00 51.39 ? 828  ASP A CG     1 
ATOM   4571 O  OD1    . ASP A 1 828  ? 221.038 143.503 168.483 1.00 51.39 ? 828  ASP A OD1    1 
ATOM   4572 O  OD2    . ASP A 1 828  ? 221.557 145.594 168.917 1.00 51.39 ? 828  ASP A OD2    1 
ATOM   4573 N  N      . ARG A 1 829  ? 221.639 147.100 165.261 1.00 48.26 ? 829  ARG A N      1 
ATOM   4574 C  CA     . ARG A 1 829  ? 220.980 148.380 165.025 1.00 48.26 ? 829  ARG A CA     1 
ATOM   4575 C  C      . ARG A 1 829  ? 220.043 148.317 163.829 1.00 48.26 ? 829  ARG A C      1 
ATOM   4576 O  O      . ARG A 1 829  ? 218.990 148.965 163.837 1.00 48.26 ? 829  ARG A O      1 
ATOM   4577 C  CB     . ARG A 1 829  ? 222.022 149.478 164.824 1.00 48.26 ? 829  ARG A CB     1 
ATOM   4578 C  CG     . ARG A 1 829  ? 222.814 149.801 166.075 1.00 48.26 ? 829  ARG A CG     1 
ATOM   4579 C  CD     . ARG A 1 829  ? 223.803 150.925 165.841 1.00 48.26 ? 829  ARG A CD     1 
ATOM   4580 N  NE     . ARG A 1 829  ? 224.635 151.166 167.016 1.00 48.26 ? 829  ARG A NE     1 
ATOM   4581 C  CZ     . ARG A 1 829  ? 224.313 151.997 168.002 1.00 48.26 ? 829  ARG A CZ     1 
ATOM   4582 N  NH1    . ARG A 1 829  ? 223.175 152.675 167.957 1.00 48.26 ? 829  ARG A NH1    1 
ATOM   4583 N  NH2    . ARG A 1 829  ? 225.131 152.153 169.033 1.00 48.26 ? 829  ARG A NH2    1 
ATOM   4584 N  N      . ILE A 1 830  ? 220.392 147.509 162.823 1.00 47.95 ? 830  ILE A N      1 
ATOM   4585 C  CA     . ILE A 1 830  ? 219.545 147.330 161.646 1.00 47.95 ? 830  ILE A CA     1 
ATOM   4586 C  C      . ILE A 1 830  ? 218.225 146.674 162.033 1.00 47.95 ? 830  ILE A C      1 
ATOM   4587 O  O      . ILE A 1 830  ? 217.144 147.152 161.670 1.00 47.95 ? 830  ILE A O      1 
ATOM   4588 C  CB     . ILE A 1 830  ? 220.286 146.499 160.583 1.00 47.95 ? 830  ILE A CB     1 
ATOM   4589 C  CG1    . ILE A 1 830  ? 221.603 147.165 160.199 1.00 47.95 ? 830  ILE A CG1    1 
ATOM   4590 C  CG2    . ILE A 1 830  ? 219.414 146.296 159.354 1.00 47.95 ? 830  ILE A CG2    1 
ATOM   4591 C  CD1    . ILE A 1 830  ? 221.429 148.494 159.561 1.00 47.95 ? 830  ILE A CD1    1 
ATOM   4592 N  N      . MET A 1 831  ? 218.294 145.577 162.788 1.00 44.66 ? 831  MET A N      1 
ATOM   4593 C  CA     . MET A 1 831  ? 217.073 144.864 163.137 1.00 44.66 ? 831  MET A CA     1 
ATOM   4594 C  C      . MET A 1 831  ? 216.262 145.619 164.181 1.00 44.66 ? 831  MET A C      1 
ATOM   4595 O  O      . MET A 1 831  ? 215.033 145.502 164.200 1.00 44.66 ? 831  MET A O      1 
ATOM   4596 C  CB     . MET A 1 831  ? 217.401 143.439 163.599 1.00 44.66 ? 831  MET A CB     1 
ATOM   4597 C  CG     . MET A 1 831  ? 218.230 143.297 164.872 1.00 44.66 ? 831  MET A CG     1 
ATOM   4598 S  SD     . MET A 1 831  ? 217.271 143.201 166.396 1.00 44.66 ? 831  MET A SD     1 
ATOM   4599 C  CE     . MET A 1 831  ? 216.553 141.570 166.234 1.00 44.66 ? 831  MET A CE     1 
ATOM   4600 N  N      . HIS A 1 832  ? 216.910 146.425 165.029 1.00 42.15 ? 832  HIS A N      1 
ATOM   4601 C  CA     . HIS A 1 832  ? 216.138 147.246 165.955 1.00 42.15 ? 832  HIS A CA     1 
ATOM   4602 C  C      . HIS A 1 832  ? 215.475 148.423 165.260 1.00 42.15 ? 832  HIS A C      1 
ATOM   4603 O  O      . HIS A 1 832  ? 214.403 148.862 165.690 1.00 42.15 ? 832  HIS A O      1 
ATOM   4604 C  CB     . HIS A 1 832  ? 217.013 147.734 167.106 1.00 42.15 ? 832  HIS A CB     1 
ATOM   4605 C  CG     . HIS A 1 832  ? 217.301 146.681 168.125 1.00 42.15 ? 832  HIS A CG     1 
ATOM   4606 N  ND1    . HIS A 1 832  ? 218.431 145.895 168.091 1.00 42.15 ? 832  HIS A ND1    1 
ATOM   4607 C  CD2    . HIS A 1 832  ? 216.582 146.260 169.192 1.00 42.15 ? 832  HIS A CD2    1 
ATOM   4608 C  CE1    . HIS A 1 832  ? 218.407 145.052 169.108 1.00 42.15 ? 832  HIS A CE1    1 
ATOM   4609 N  NE2    . HIS A 1 832  ? 217.294 145.251 169.789 1.00 42.15 ? 832  HIS A NE2    1 
ATOM   4610 N  N      . PHE A 1 833  ? 216.083 148.946 164.198 1.00 35.84 ? 833  PHE A N      1 
ATOM   4611 C  CA     . PHE A 1 833  ? 215.434 150.011 163.446 1.00 35.84 ? 833  PHE A CA     1 
ATOM   4612 C  C      . PHE A 1 833  ? 214.264 149.472 162.640 1.00 35.84 ? 833  PHE A C      1 
ATOM   4613 O  O      . PHE A 1 833  ? 213.157 150.011 162.707 1.00 35.84 ? 833  PHE A O      1 
ATOM   4614 C  CB     . PHE A 1 833  ? 216.442 150.697 162.535 1.00 35.84 ? 833  PHE A CB     1 
ATOM   4615 C  CG     . PHE A 1 833  ? 215.863 151.813 161.717 1.00 35.84 ? 833  PHE A CG     1 
ATOM   4616 C  CD1    . PHE A 1 833  ? 215.591 153.036 162.294 1.00 35.84 ? 833  PHE A CD1    1 
ATOM   4617 C  CD2    . PHE A 1 833  ? 215.583 151.637 160.371 1.00 35.84 ? 833  PHE A CD2    1 
ATOM   4618 C  CE1    . PHE A 1 833  ? 215.058 154.064 161.547 1.00 35.84 ? 833  PHE A CE1    1 
ATOM   4619 C  CE2    . PHE A 1 833  ? 215.052 152.661 159.623 1.00 35.84 ? 833  PHE A CE2    1 
ATOM   4620 C  CZ     . PHE A 1 833  ? 214.792 153.873 160.215 1.00 35.84 ? 833  PHE A CZ     1 
ATOM   4621 N  N      . TYR A 1 834  ? 214.482 148.391 161.888 1.00 37.49 ? 834  TYR A N      1 
ATOM   4622 C  CA     . TYR A 1 834  ? 213.402 147.812 161.098 1.00 37.49 ? 834  TYR A CA     1 
ATOM   4623 C  C      . TYR A 1 834  ? 212.369 147.071 161.938 1.00 37.49 ? 834  TYR A C      1 
ATOM   4624 O  O      . TYR A 1 834  ? 211.301 146.744 161.415 1.00 37.49 ? 834  TYR A O      1 
ATOM   4625 C  CB     . TYR A 1 834  ? 213.975 146.887 160.021 1.00 37.49 ? 834  TYR A CB     1 
ATOM   4626 C  CG     . TYR A 1 834  ? 214.647 147.636 158.892 1.00 37.49 ? 834  TYR A CG     1 
ATOM   4627 C  CD1    . TYR A 1 834  ? 213.893 148.262 157.914 1.00 37.49 ? 834  TYR A CD1    1 
ATOM   4628 C  CD2    . TYR A 1 834  ? 216.028 147.710 158.798 1.00 37.49 ? 834  TYR A CD2    1 
ATOM   4629 C  CE1    . TYR A 1 834  ? 214.495 148.947 156.884 1.00 37.49 ? 834  TYR A CE1    1 
ATOM   4630 C  CE2    . TYR A 1 834  ? 216.639 148.398 157.775 1.00 37.49 ? 834  TYR A CE2    1 
ATOM   4631 C  CZ     . TYR A 1 834  ? 215.868 149.012 156.820 1.00 37.49 ? 834  TYR A CZ     1 
ATOM   4632 O  OH     . TYR A 1 834  ? 216.464 149.699 155.790 1.00 37.49 ? 834  TYR A OH     1 
ATOM   4633 N  N      . SER A 1 835  ? 212.648 146.798 163.213 1.00 32.08 ? 835  SER A N      1 
ATOM   4634 C  CA     . SER A 1 835  ? 211.643 146.244 164.107 1.00 32.08 ? 835  SER A CA     1 
ATOM   4635 C  C      . SER A 1 835  ? 210.615 147.265 164.553 1.00 32.08 ? 835  SER A C      1 
ATOM   4636 O  O      . SER A 1 835  ? 209.543 146.869 165.021 1.00 32.08 ? 835  SER A O      1 
ATOM   4637 C  CB     . SER A 1 835  ? 212.303 145.645 165.350 1.00 32.08 ? 835  SER A CB     1 
ATOM   4638 O  OG     . SER A 1 835  ? 213.099 144.521 165.040 1.00 32.08 ? 835  SER A OG     1 
ATOM   4639 N  N      . ALA A 1 836  ? 210.923 148.549 164.434 1.00 25.76 ? 836  ALA A N      1 
ATOM   4640 C  CA     . ALA A 1 836  ? 210.043 149.587 164.946 1.00 25.76 ? 836  ALA A CA     1 
ATOM   4641 C  C      . ALA A 1 836  ? 208.784 149.667 164.097 1.00 25.76 ? 836  ALA A C      1 
ATOM   4642 O  O      . ALA A 1 836  ? 208.877 149.698 162.867 1.00 25.76 ? 836  ALA A O      1 
ATOM   4643 C  CB     . ALA A 1 836  ? 210.760 150.930 164.959 1.00 25.76 ? 836  ALA A CB     1 
ATOM   4644 N  N      . PRO A 1 837  ? 207.598 149.662 164.707 1.00 20.10 ? 837  PRO A N      1 
ATOM   4645 C  CA     . PRO A 1 837  ? 206.366 149.820 163.926 1.00 20.10 ? 837  PRO A CA     1 
ATOM   4646 C  C      . PRO A 1 837  ? 206.236 151.162 163.249 1.00 20.10 ? 837  PRO A C      1 
ATOM   4647 O  O      . PRO A 1 837  ? 205.465 151.274 162.296 1.00 20.10 ? 837  PRO A O      1 
ATOM   4648 C  CB     . PRO A 1 837  ? 205.266 149.618 164.972 1.00 20.10 ? 837  PRO A CB     1 
ATOM   4649 C  CG     . PRO A 1 837  ? 205.891 148.759 165.979 1.00 20.10 ? 837  PRO A CG     1 
ATOM   4650 C  CD     . PRO A 1 837  ? 207.314 149.197 166.071 1.00 20.10 ? 837  PRO A CD     1 
ATOM   4651 N  N      . PHE A 1 838  ? 206.952 152.185 163.708 1.00 19.42 ? 838  PHE A N      1 
ATOM   4652 C  CA     . PHE A 1 838  ? 206.995 153.431 162.962 1.00 19.42 ? 838  PHE A CA     1 
ATOM   4653 C  C      . PHE A 1 838  ? 207.832 153.295 161.700 1.00 19.42 ? 838  PHE A C      1 
ATOM   4654 O  O      . PHE A 1 838  ? 207.512 153.918 160.686 1.00 19.42 ? 838  PHE A O      1 
ATOM   4655 C  CB     . PHE A 1 838  ? 207.519 154.547 163.861 1.00 19.42 ? 838  PHE A CB     1 
ATOM   4656 C  CG     . PHE A 1 838  ? 207.529 155.895 163.219 1.00 19.42 ? 838  PHE A CG     1 
ATOM   4657 C  CD1    . PHE A 1 838  ? 206.351 156.469 162.779 1.00 19.42 ? 838  PHE A CD1    1 
ATOM   4658 C  CD2    . PHE A 1 838  ? 208.697 156.627 163.132 1.00 19.42 ? 838  PHE A CD2    1 
ATOM   4659 C  CE1    . PHE A 1 838  ? 206.348 157.717 162.214 1.00 19.42 ? 838  PHE A CE1    1 
ATOM   4660 C  CE2    . PHE A 1 838  ? 208.694 157.881 162.576 1.00 19.42 ? 838  PHE A CE2    1 
ATOM   4661 C  CZ     . PHE A 1 838  ? 207.520 158.423 162.114 1.00 19.42 ? 838  PHE A CZ     1 
ATOM   4662 N  N      . SER A 1 839  ? 208.889 152.479 161.733 1.00 23.87 ? 839  SER A N      1 
ATOM   4663 C  CA     . SER A 1 839  ? 209.653 152.200 160.522 1.00 23.87 ? 839  SER A CA     1 
ATOM   4664 C  C      . SER A 1 839  ? 208.820 151.422 159.521 1.00 23.87 ? 839  SER A C      1 
ATOM   4665 O  O      . SER A 1 839  ? 208.830 151.725 158.324 1.00 23.87 ? 839  SER A O      1 
ATOM   4666 C  CB     . SER A 1 839  ? 210.909 151.414 160.861 1.00 23.87 ? 839  SER A CB     1 
ATOM   4667 O  OG     . SER A 1 839  ? 211.748 152.130 161.736 1.00 23.87 ? 839  SER A OG     1 
ATOM   4668 N  N      . LYS A 1 840  ? 208.092 150.420 160.010 1.00 24.24 ? 840  LYS A N      1 
ATOM   4669 C  CA     . LYS A 1 840  ? 207.171 149.656 159.185 1.00 24.24 ? 840  LYS A CA     1 
ATOM   4670 C  C      . LYS A 1 840  ? 206.043 150.527 158.659 1.00 24.24 ? 840  LYS A C      1 
ATOM   4671 O  O      . LYS A 1 840  ? 205.588 150.337 157.530 1.00 24.24 ? 840  LYS A O      1 
ATOM   4672 C  CB     . LYS A 1 840  ? 206.624 148.503 160.011 1.00 24.24 ? 840  LYS A CB     1 
ATOM   4673 C  CG     . LYS A 1 840  ? 207.710 147.558 160.459 1.00 24.24 ? 840  LYS A CG     1 
ATOM   4674 C  CD     . LYS A 1 840  ? 207.165 146.532 161.398 1.00 24.24 ? 840  LYS A CD     1 
ATOM   4675 C  CE     . LYS A 1 840  ? 208.209 145.567 161.844 1.00 24.24 ? 840  LYS A CE     1 
ATOM   4676 N  NZ     . LYS A 1 840  ? 207.618 144.586 162.779 1.00 24.24 ? 840  LYS A NZ     1 
ATOM   4677 N  N      . PHE A 1 841  ? 205.617 151.512 159.447 1.00 17.46 ? 841  PHE A N      1 
ATOM   4678 C  CA     . PHE A 1 841  ? 204.597 152.452 159.011 1.00 17.46 ? 841  PHE A CA     1 
ATOM   4679 C  C      . PHE A 1 841  ? 205.101 153.346 157.890 1.00 17.46 ? 841  PHE A C      1 
ATOM   4680 O  O      . PHE A 1 841  ? 204.407 153.537 156.891 1.00 17.46 ? 841  PHE A O      1 
ATOM   4681 C  CB     . PHE A 1 841  ? 204.144 153.299 160.187 1.00 17.46 ? 841  PHE A CB     1 
ATOM   4682 C  CG     . PHE A 1 841  ? 203.124 154.331 159.828 1.00 17.46 ? 841  PHE A CG     1 
ATOM   4683 C  CD1    . PHE A 1 841  ? 201.818 153.967 159.592 1.00 17.46 ? 841  PHE A CD1    1 
ATOM   4684 C  CD2    . PHE A 1 841  ? 203.469 155.669 159.728 1.00 17.46 ? 841  PHE A CD2    1 
ATOM   4685 C  CE1    . PHE A 1 841  ? 200.880 154.903 159.270 1.00 17.46 ? 841  PHE A CE1    1 
ATOM   4686 C  CE2    . PHE A 1 841  ? 202.530 156.605 159.396 1.00 17.46 ? 841  PHE A CE2    1 
ATOM   4687 C  CZ     . PHE A 1 841  ? 201.236 156.217 159.166 1.00 17.46 ? 841  PHE A CZ     1 
ATOM   4688 N  N      . VAL A 1 842  ? 206.287 153.939 158.061 1.00 21.68 ? 842  VAL A N      1 
ATOM   4689 C  CA     . VAL A 1 842  ? 206.847 154.828 157.044 1.00 21.68 ? 842  VAL A CA     1 
ATOM   4690 C  C      . VAL A 1 842  ? 207.154 154.050 155.770 1.00 21.68 ? 842  VAL A C      1 
ATOM   4691 O  O      . VAL A 1 842  ? 206.909 154.530 154.653 1.00 21.68 ? 842  VAL A O      1 
ATOM   4692 C  CB     . VAL A 1 842  ? 208.090 155.552 157.601 1.00 21.68 ? 842  VAL A CB     1 
ATOM   4693 C  CG1    . VAL A 1 842  ? 208.807 156.344 156.526 1.00 21.68 ? 842  VAL A CG1    1 
ATOM   4694 C  CG2    . VAL A 1 842  ? 207.684 156.491 158.710 1.00 21.68 ? 842  VAL A CG2    1 
ATOM   4695 N  N      . GLY A 1 843  ? 207.618 152.809 155.920 1.00 23.58 ? 843  GLY A N      1 
ATOM   4696 C  CA     . GLY A 1 843  ? 207.801 151.949 154.766 1.00 23.58 ? 843  GLY A CA     1 
ATOM   4697 C  C      . GLY A 1 843  ? 206.502 151.589 154.077 1.00 23.58 ? 843  GLY A C      1 
ATOM   4698 O  O      . GLY A 1 843  ? 206.447 151.525 152.849 1.00 23.58 ? 843  GLY A O      1 
ATOM   4699 N  N      . ASN A 1 844  ? 205.437 151.376 154.853 1.00 22.44 ? 844  ASN A N      1 
ATOM   4700 C  CA     . ASN A 1 844  ? 204.135 151.091 154.266 1.00 22.44 ? 844  ASN A CA     1 
ATOM   4701 C  C      . ASN A 1 844  ? 203.583 152.307 153.540 1.00 22.44 ? 844  ASN A C      1 
ATOM   4702 O  O      . ASN A 1 844  ? 202.985 152.164 152.476 1.00 22.44 ? 844  ASN A O      1 
ATOM   4703 C  CB     . ASN A 1 844  ? 203.159 150.640 155.349 1.00 22.44 ? 844  ASN A CB     1 
ATOM   4704 C  CG     . ASN A 1 844  ? 202.023 149.784 154.809 1.00 22.44 ? 844  ASN A CG     1 
ATOM   4705 O  OD1    . ASN A 1 844  ? 201.250 149.221 155.576 1.00 22.44 ? 844  ASN A OD1    1 
ATOM   4706 N  ND2    . ASN A 1 844  ? 201.942 149.649 153.493 1.00 22.44 ? 844  ASN A ND2    1 
ATOM   4707 N  N      . VAL A 1 845  ? 203.807 153.507 154.079 1.00 20.81 ? 845  VAL A N      1 
ATOM   4708 C  CA     . VAL A 1 845  ? 203.335 154.731 153.434 1.00 20.81 ? 845  VAL A CA     1 
ATOM   4709 C  C      . VAL A 1 845  ? 204.059 154.954 152.112 1.00 20.81 ? 845  VAL A C      1 
ATOM   4710 O  O      . VAL A 1 845  ? 203.429 155.220 151.083 1.00 20.81 ? 845  VAL A O      1 
ATOM   4711 C  CB     . VAL A 1 845  ? 203.500 155.938 154.377 1.00 20.81 ? 845  VAL A CB     1 
ATOM   4712 C  CG1    . VAL A 1 845  ? 203.216 157.235 153.652 1.00 20.81 ? 845  VAL A CG1    1 
ATOM   4713 C  CG2    . VAL A 1 845  ? 202.569 155.818 155.545 1.00 20.81 ? 845  VAL A CG2    1 
ATOM   4714 N  N      . VAL A 1 846  ? 205.381 154.785 152.104 1.00 22.33 ? 846  VAL A N      1 
ATOM   4715 C  CA     . VAL A 1 846  ? 206.149 155.030 150.887 1.00 22.33 ? 846  VAL A CA     1 
ATOM   4716 C  C      . VAL A 1 846  ? 205.901 153.941 149.848 1.00 22.33 ? 846  VAL A C      1 
ATOM   4717 O  O      . VAL A 1 846  ? 205.639 154.237 148.673 1.00 22.33 ? 846  VAL A O      1 
ATOM   4718 C  CB     . VAL A 1 846  ? 207.636 155.173 151.239 1.00 22.33 ? 846  VAL A CB     1 
ATOM   4719 C  CG1    . VAL A 1 846  ? 208.480 155.291 149.989 1.00 22.33 ? 846  VAL A CG1    1 
ATOM   4720 C  CG2    . VAL A 1 846  ? 207.806 156.390 152.097 1.00 22.33 ? 846  VAL A CG2    1 
ATOM   4721 N  N      . GLY A 1 847  ? 205.939 152.670 150.260 1.00 21.49 ? 847  GLY A N      1 
ATOM   4722 C  CA     . GLY A 1 847  ? 205.662 151.588 149.335 1.00 21.49 ? 847  GLY A CA     1 
ATOM   4723 C  C      . GLY A 1 847  ? 204.224 151.554 148.874 1.00 21.49 ? 847  GLY A C      1 
ATOM   4724 O  O      . GLY A 1 847  ? 203.936 151.113 147.759 1.00 21.49 ? 847  GLY A O      1 
ATOM   4725 N  N      . TYR A 1 848  ? 203.311 152.089 149.678 1.00 21.28 ? 848  TYR A N      1 
ATOM   4726 C  CA     . TYR A 1 848  ? 201.918 152.109 149.285 1.00 21.28 ? 848  TYR A CA     1 
ATOM   4727 C  C      . TYR A 1 848  ? 201.612 153.282 148.369 1.00 21.28 ? 848  TYR A C      1 
ATOM   4728 O  O      . TYR A 1 848  ? 200.759 153.154 147.495 1.00 21.28 ? 848  TYR A O      1 
ATOM   4729 C  CB     . TYR A 1 848  ? 201.034 152.163 150.524 1.00 21.28 ? 848  TYR A CB     1 
ATOM   4730 C  CG     . TYR A 1 848  ? 199.632 151.723 150.248 1.00 21.28 ? 848  TYR A CG     1 
ATOM   4731 C  CD1    . TYR A 1 848  ? 199.308 150.370 150.242 1.00 21.28 ? 848  TYR A CD1    1 
ATOM   4732 C  CD2    . TYR A 1 848  ? 198.641 152.638 149.936 1.00 21.28 ? 848  TYR A CD2    1 
ATOM   4733 C  CE1    . TYR A 1 848  ? 198.027 149.945 149.976 1.00 21.28 ? 848  TYR A CE1    1 
ATOM   4734 C  CE2    . TYR A 1 848  ? 197.361 152.217 149.657 1.00 21.28 ? 848  TYR A CE2    1 
ATOM   4735 C  CZ     . TYR A 1 848  ? 197.057 150.876 149.687 1.00 21.28 ? 848  TYR A CZ     1 
ATOM   4736 O  OH     . TYR A 1 848  ? 195.774 150.467 149.417 1.00 21.28 ? 848  TYR A OH     1 
ATOM   4737 N  N      . LEU A 1 849  ? 202.295 154.420 148.537 1.00 19.68 ? 849  LEU A N      1 
ATOM   4738 C  CA     . LEU A 1 849  ? 202.220 155.476 147.531 1.00 19.68 ? 849  LEU A CA     1 
ATOM   4739 C  C      . LEU A 1 849  ? 202.808 155.017 146.209 1.00 19.68 ? 849  LEU A C      1 
ATOM   4740 O  O      . LEU A 1 849  ? 202.281 155.351 145.140 1.00 19.68 ? 849  LEU A O      1 
ATOM   4741 C  CB     . LEU A 1 849  ? 202.943 156.734 148.004 1.00 19.68 ? 849  LEU A CB     1 
ATOM   4742 C  CG     . LEU A 1 849  ? 202.298 157.586 149.088 1.00 19.68 ? 849  LEU A CG     1 
ATOM   4743 C  CD1    . LEU A 1 849  ? 203.254 158.687 149.495 1.00 19.68 ? 849  LEU A CD1    1 
ATOM   4744 C  CD2    . LEU A 1 849  ? 200.986 158.165 148.597 1.00 19.68 ? 849  LEU A CD2    1 
ATOM   4745 N  N      . ALA A 1 850  ? 203.903 154.251 146.266 1.00 18.76 ? 850  ALA A N      1 
ATOM   4746 C  CA     . ALA A 1 850  ? 204.468 153.662 145.057 1.00 18.76 ? 850  ALA A CA     1 
ATOM   4747 C  C      . ALA A 1 850  ? 203.485 152.702 144.401 1.00 18.76 ? 850  ALA A C      1 
ATOM   4748 O  O      . ALA A 1 850  ? 203.343 152.688 143.173 1.00 18.76 ? 850  ALA A O      1 
ATOM   4749 C  CB     . ALA A 1 850  ? 205.773 152.947 145.391 1.00 18.76 ? 850  ALA A CB     1 
ATOM   4750 N  N      . PHE A 1 851  ? 202.772 151.923 145.215 1.00 19.79 ? 851  PHE A N      1 
ATOM   4751 C  CA     . PHE A 1 851  ? 201.745 151.020 144.712 1.00 19.79 ? 851  PHE A CA     1 
ATOM   4752 C  C      . PHE A 1 851  ? 200.571 151.760 144.084 1.00 19.79 ? 851  PHE A C      1 
ATOM   4753 O  O      . PHE A 1 851  ? 200.054 151.327 143.053 1.00 19.79 ? 851  PHE A O      1 
ATOM   4754 C  CB     . PHE A 1 851  ? 201.261 150.123 145.842 1.00 19.79 ? 851  PHE A CB     1 
ATOM   4755 C  CG     . PHE A 1 851  ? 200.008 149.385 145.525 1.00 19.79 ? 851  PHE A CG     1 
ATOM   4756 C  CD1    . PHE A 1 851  ? 199.985 148.416 144.545 1.00 19.79 ? 851  PHE A CD1    1 
ATOM   4757 C  CD2    . PHE A 1 851  ? 198.846 149.655 146.221 1.00 19.79 ? 851  PHE A CD2    1 
ATOM   4758 C  CE1    . PHE A 1 851  ? 198.838 147.740 144.269 1.00 19.79 ? 851  PHE A CE1    1 
ATOM   4759 C  CE2    . PHE A 1 851  ? 197.692 148.977 145.937 1.00 19.79 ? 851  PHE A CE2    1 
ATOM   4760 C  CZ     . PHE A 1 851  ? 197.690 148.018 144.958 1.00 19.79 ? 851  PHE A CZ     1 
ATOM   4761 N  N      . ILE A 1 852  ? 200.118 152.853 144.700 1.00 19.28 ? 852  ILE A N      1 
ATOM   4762 C  CA     . ILE A 1 852  ? 198.998 153.605 144.139 1.00 19.28 ? 852  ILE A CA     1 
ATOM   4763 C  C      . ILE A 1 852  ? 199.408 154.273 142.833 1.00 19.28 ? 852  ILE A C      1 
ATOM   4764 O  O      . ILE A 1 852  ? 198.639 154.285 141.868 1.00 19.28 ? 852  ILE A O      1 
ATOM   4765 C  CB     . ILE A 1 852  ? 198.451 154.616 145.166 1.00 19.28 ? 852  ILE A CB     1 
ATOM   4766 C  CG1    . ILE A 1 852  ? 197.853 153.889 146.368 1.00 19.28 ? 852  ILE A CG1    1 
ATOM   4767 C  CG2    . ILE A 1 852  ? 197.381 155.512 144.566 1.00 19.28 ? 852  ILE A CG2    1 
ATOM   4768 C  CD1    . ILE A 1 852  ? 196.721 152.950 146.022 1.00 19.28 ? 852  ILE A CD1    1 
ATOM   4769 N  N      . PHE A 1 853  ? 200.647 154.770 142.756 1.00 19.04 ? 853  PHE A N      1 
ATOM   4770 C  CA     . PHE A 1 853  ? 201.144 155.352 141.511 1.00 19.04 ? 853  PHE A CA     1 
ATOM   4771 C  C      . PHE A 1 853  ? 201.297 154.301 140.417 1.00 19.04 ? 853  PHE A C      1 
ATOM   4772 O  O      . PHE A 1 853  ? 201.018 154.575 139.247 1.00 19.04 ? 853  PHE A O      1 
ATOM   4773 C  CB     . PHE A 1 853  ? 202.479 156.053 141.754 1.00 19.04 ? 853  PHE A CB     1 
ATOM   4774 C  CG     . PHE A 1 853  ? 202.374 157.327 142.539 1.00 19.04 ? 853  PHE A CG     1 
ATOM   4775 C  CD1    . PHE A 1 853  ? 201.159 157.977 142.695 1.00 19.04 ? 853  PHE A CD1    1 
ATOM   4776 C  CD2    . PHE A 1 853  ? 203.502 157.880 143.123 1.00 19.04 ? 853  PHE A CD2    1 
ATOM   4777 C  CE1    . PHE A 1 853  ? 201.072 159.153 143.418 1.00 19.04 ? 853  PHE A CE1    1 
ATOM   4778 C  CE2    . PHE A 1 853  ? 203.422 159.057 143.848 1.00 19.04 ? 853  PHE A CE2    1 
ATOM   4779 C  CZ     . PHE A 1 853  ? 202.204 159.693 143.995 1.00 19.04 ? 853  PHE A CZ     1 
ATOM   4780 N  N      . LEU A 1 854  ? 201.716 153.089 140.778 1.00 18.71 ? 854  LEU A N      1 
ATOM   4781 C  CA     . LEU A 1 854  ? 201.852 152.038 139.776 1.00 18.71 ? 854  LEU A CA     1 
ATOM   4782 C  C      . LEU A 1 854  ? 200.490 151.542 139.303 1.00 18.71 ? 854  LEU A C      1 
ATOM   4783 O  O      . LEU A 1 854  ? 200.291 151.311 138.103 1.00 18.71 ? 854  LEU A O      1 
ATOM   4784 C  CB     . LEU A 1 854  ? 202.669 150.884 140.341 1.00 18.71 ? 854  LEU A CB     1 
ATOM   4785 C  CG     . LEU A 1 854  ? 203.044 149.799 139.343 1.00 18.71 ? 854  LEU A CG     1 
ATOM   4786 C  CD1    . LEU A 1 854  ? 204.048 150.334 138.349 1.00 18.71 ? 854  LEU A CD1    1 
ATOM   4787 C  CD2    . LEU A 1 854  ? 203.565 148.599 140.075 1.00 18.71 ? 854  LEU A CD2    1 
ATOM   4788 N  N      . TYR A 1 855  ? 199.545 151.381 140.238 1.00 18.92 ? 855  TYR A N      1 
ATOM   4789 C  CA     . TYR A 1 855  ? 198.176 151.007 139.904 1.00 18.92 ? 855  TYR A CA     1 
ATOM   4790 C  C      . TYR A 1 855  ? 197.541 152.066 139.014 1.00 18.92 ? 855  TYR A C      1 
ATOM   4791 O  O      . TYR A 1 855  ? 196.812 151.742 138.072 1.00 18.92 ? 855  TYR A O      1 
ATOM   4792 C  CB     . TYR A 1 855  ? 197.356 150.865 141.184 1.00 18.92 ? 855  TYR A CB     1 
ATOM   4793 C  CG     . TYR A 1 855  ? 196.123 149.974 141.124 1.00 18.92 ? 855  TYR A CG     1 
ATOM   4794 C  CD1    . TYR A 1 855  ? 196.108 148.757 141.777 1.00 18.92 ? 855  TYR A CD1    1 
ATOM   4795 C  CD2    . TYR A 1 855  ? 195.028 150.305 140.336 1.00 18.92 ? 855  TYR A CD2    1 
ATOM   4796 C  CE1    . TYR A 1 855  ? 194.995 147.945 141.736 1.00 18.92 ? 855  TYR A CE1    1 
ATOM   4797 C  CE2    . TYR A 1 855  ? 193.929 149.486 140.272 1.00 18.92 ? 855  TYR A CE2    1 
ATOM   4798 C  CZ     . TYR A 1 855  ? 193.914 148.315 140.977 1.00 18.92 ? 855  TYR A CZ     1 
ATOM   4799 O  OH     . TYR A 1 855  ? 192.811 147.507 140.912 1.00 18.92 ? 855  TYR A OH     1 
ATOM   4800 N  N      . ALA A 1 856  ? 197.828 153.340 139.290 1.00 16.28 ? 856  ALA A N      1 
ATOM   4801 C  CA     . ALA A 1 856  ? 197.275 154.430 138.504 1.00 16.28 ? 856  ALA A CA     1 
ATOM   4802 C  C      . ALA A 1 856  ? 197.915 154.517 137.131 1.00 16.28 ? 856  ALA A C      1 
ATOM   4803 O  O      . ALA A 1 856  ? 197.244 154.898 136.171 1.00 16.28 ? 856  ALA A O      1 
ATOM   4804 C  CB     . ALA A 1 856  ? 197.447 155.750 139.248 1.00 16.28 ? 856  ALA A CB     1 
ATOM   4805 N  N      . TYR A 1 857  ? 199.204 154.191 137.015 1.00 15.69 ? 857  TYR A N      1 
ATOM   4806 C  CA     . TYR A 1 857  ? 199.810 154.103 135.693 1.00 15.69 ? 857  TYR A CA     1 
ATOM   4807 C  C      . TYR A 1 857  ? 199.203 152.962 134.892 1.00 15.69 ? 857  TYR A C      1 
ATOM   4808 O  O      . TYR A 1 857  ? 199.028 153.076 133.675 1.00 15.69 ? 857  TYR A O      1 
ATOM   4809 C  CB     . TYR A 1 857  ? 201.328 153.927 135.790 1.00 15.69 ? 857  TYR A CB     1 
ATOM   4810 C  CG     . TYR A 1 857  ? 201.967 153.727 134.430 1.00 15.69 ? 857  TYR A CG     1 
ATOM   4811 C  CD1    . TYR A 1 857  ? 202.127 154.790 133.560 1.00 15.69 ? 857  TYR A CD1    1 
ATOM   4812 C  CD2    . TYR A 1 857  ? 202.366 152.465 134.003 1.00 15.69 ? 857  TYR A CD2    1 
ATOM   4813 C  CE1    . TYR A 1 857  ? 202.679 154.610 132.315 1.00 15.69 ? 857  TYR A CE1    1 
ATOM   4814 C  CE2    . TYR A 1 857  ? 202.913 152.277 132.760 1.00 15.69 ? 857  TYR A CE2    1 
ATOM   4815 C  CZ     . TYR A 1 857  ? 203.072 153.351 131.922 1.00 15.69 ? 857  TYR A CZ     1 
ATOM   4816 O  OH     . TYR A 1 857  ? 203.624 153.166 130.680 1.00 15.69 ? 857  TYR A OH     1 
ATOM   4817 N  N      . VAL A 1 858  ? 198.905 151.846 135.554 1.00 16.84 ? 858  VAL A N      1 
ATOM   4818 C  CA     . VAL A 1 858  ? 198.313 150.711 134.858 1.00 16.84 ? 858  VAL A CA     1 
ATOM   4819 C  C      . VAL A 1 858  ? 196.903 151.045 134.386 1.00 16.84 ? 858  VAL A C      1 
ATOM   4820 O  O      . VAL A 1 858  ? 196.573 150.855 133.213 1.00 16.84 ? 858  VAL A O      1 
ATOM   4821 C  CB     . VAL A 1 858  ? 198.347 149.458 135.750 1.00 16.84 ? 858  VAL A CB     1 
ATOM   4822 C  CG1    . VAL A 1 858  ? 197.512 148.358 135.151 1.00 16.84 ? 858  VAL A CG1    1 
ATOM   4823 C  CG2    . VAL A 1 858  ? 199.775 148.969 135.884 1.00 16.84 ? 858  VAL A CG2    1 
ATOM   4824 N  N      . VAL A 1 859  ? 196.072 151.613 135.259 1.00 15.62 ? 859  VAL A N      1 
ATOM   4825 C  CA     . VAL A 1 859  ? 194.691 151.853 134.851 1.00 15.62 ? 859  VAL A CA     1 
ATOM   4826 C  C      . VAL A 1 859  ? 194.536 153.092 133.975 1.00 15.62 ? 859  VAL A C      1 
ATOM   4827 O  O      . VAL A 1 859  ? 193.586 153.156 133.188 1.00 15.62 ? 859  VAL A O      1 
ATOM   4828 C  CB     . VAL A 1 859  ? 193.730 151.949 136.050 1.00 15.62 ? 859  VAL A CB     1 
ATOM   4829 C  CG1    . VAL A 1 859  ? 193.739 150.662 136.836 1.00 15.62 ? 859  VAL A CG1    1 
ATOM   4830 C  CG2    . VAL A 1 859  ? 194.044 153.138 136.942 1.00 15.62 ? 859  VAL A CG2    1 
ATOM   4831 N  N      . LEU A 1 860  ? 195.441 154.068 134.059 1.00 12.03 ? 860  LEU A N      1 
ATOM   4832 C  CA     . LEU A 1 860  ? 195.282 155.291 133.289 1.00 12.03 ? 860  LEU A CA     1 
ATOM   4833 C  C      . LEU A 1 860  ? 196.046 155.291 131.979 1.00 12.03 ? 860  LEU A C      1 
ATOM   4834 O  O      . LEU A 1 860  ? 195.672 156.034 131.068 1.00 12.03 ? 860  LEU A O      1 
ATOM   4835 C  CB     . LEU A 1 860  ? 195.728 156.511 134.102 1.00 12.03 ? 860  LEU A CB     1 
ATOM   4836 C  CG     . LEU A 1 860  ? 194.892 157.010 135.277 1.00 12.03 ? 860  LEU A CG     1 
ATOM   4837 C  CD1    . LEU A 1 860  ? 195.617 158.144 135.962 1.00 12.03 ? 860  LEU A CD1    1 
ATOM   4838 C  CD2    . LEU A 1 860  ? 193.530 157.440 134.813 1.00 12.03 ? 860  LEU A CD2    1 
ATOM   4839 N  N      . PHE A 1 861  ? 197.092 154.511 131.866 1.00 14.83 ? 861  PHE A N      1 
ATOM   4840 C  CA     . PHE A 1 861  ? 197.969 154.680 130.718 1.00 14.83 ? 861  PHE A CA     1 
ATOM   4841 C  C      . PHE A 1 861  ? 198.221 153.399 129.948 1.00 14.83 ? 861  PHE A C      1 
ATOM   4842 O  O      . PHE A 1 861  ? 198.317 153.444 128.721 1.00 14.83 ? 861  PHE A O      1 
ATOM   4843 C  CB     . PHE A 1 861  ? 199.301 155.270 131.179 1.00 14.83 ? 861  PHE A CB     1 
ATOM   4844 C  CG     . PHE A 1 861  ? 199.191 156.657 131.732 1.00 14.83 ? 861  PHE A CG     1 
ATOM   4845 C  CD1    . PHE A 1 861  ? 199.124 157.752 130.891 1.00 14.83 ? 861  PHE A CD1    1 
ATOM   4846 C  CD2    . PHE A 1 861  ? 199.165 156.867 133.097 1.00 14.83 ? 861  PHE A CD2    1 
ATOM   4847 C  CE1    . PHE A 1 861  ? 199.029 159.026 131.404 1.00 14.83 ? 861  PHE A CE1    1 
ATOM   4848 C  CE2    . PHE A 1 861  ? 199.067 158.138 133.613 1.00 14.83 ? 861  PHE A CE2    1 
ATOM   4849 C  CZ     . PHE A 1 861  ? 199.000 159.218 132.763 1.00 14.83 ? 861  PHE A CZ     1 
ATOM   4850 N  N      . ASN A 1 862  ? 198.346 152.262 130.625 1.00 18.92 ? 862  ASN A N      1 
ATOM   4851 C  CA     . ASN A 1 862  ? 198.775 151.056 129.919 1.00 18.92 ? 862  ASN A CA     1 
ATOM   4852 C  C      . ASN A 1 862  ? 198.127 149.847 130.594 1.00 18.92 ? 862  ASN A C      1 
ATOM   4853 O  O      . ASN A 1 862  ? 198.662 149.290 131.553 1.00 18.92 ? 862  ASN A O      1 
ATOM   4854 C  CB     . ASN A 1 862  ? 200.292 150.950 129.903 1.00 18.92 ? 862  ASN A CB     1 
ATOM   4855 C  CG     . ASN A 1 862  ? 200.797 149.973 128.871 1.00 18.92 ? 862  ASN A CG     1 
ATOM   4856 O  OD1    . ASN A 1 862  ? 200.025 149.299 128.198 1.00 18.92 ? 862  ASN A OD1    1 
ATOM   4857 N  ND2    . ASN A 1 862  ? 202.104 149.926 128.709 1.00 18.92 ? 862  ASN A ND2    1 
ATOM   4858 N  N      . PHE A 1 863  ? 196.984 149.441 130.061 1.00 22.56 ? 863  PHE A N      1 
ATOM   4859 C  CA     . PHE A 1 863  ? 196.323 148.200 130.458 1.00 22.56 ? 863  PHE A CA     1 
ATOM   4860 C  C      . PHE A 1 863  ? 195.733 147.593 129.200 1.00 22.56 ? 863  PHE A C      1 
ATOM   4861 O  O      . PHE A 1 863  ? 194.523 147.665 128.967 1.00 22.56 ? 863  PHE A O      1 
ATOM   4862 C  CB     . PHE A 1 863  ? 195.249 148.464 131.510 1.00 22.56 ? 863  PHE A CB     1 
ATOM   4863 C  CG     . PHE A 1 863  ? 194.670 147.230 132.113 1.00 22.56 ? 863  PHE A CG     1 
ATOM   4864 C  CD1    . PHE A 1 863  ? 195.433 146.434 132.940 1.00 22.56 ? 863  PHE A CD1    1 
ATOM   4865 C  CD2    . PHE A 1 863  ? 193.350 146.890 131.902 1.00 22.56 ? 863  PHE A CD2    1 
ATOM   4866 C  CE1    . PHE A 1 863  ? 194.901 145.310 133.514 1.00 22.56 ? 863  PHE A CE1    1 
ATOM   4867 C  CE2    . PHE A 1 863  ? 192.816 145.764 132.483 1.00 22.56 ? 863  PHE A CE2    1 
ATOM   4868 C  CZ     . PHE A 1 863  ? 193.587 144.987 133.294 1.00 22.56 ? 863  PHE A CZ     1 
ATOM   4869 N  N      . PRO A 1 864  ? 196.563 147.001 128.348 1.00 26.97 ? 864  PRO A N      1 
ATOM   4870 C  CA     . PRO A 1 864  ? 196.090 146.582 127.030 1.00 26.97 ? 864  PRO A CA     1 
ATOM   4871 C  C      . PRO A 1 864  ? 195.353 145.256 127.119 1.00 26.97 ? 864  PRO A C      1 
ATOM   4872 O  O      . PRO A 1 864  ? 195.299 144.613 128.162 1.00 26.97 ? 864  PRO A O      1 
ATOM   4873 C  CB     . PRO A 1 864  ? 197.385 146.443 126.231 1.00 26.97 ? 864  PRO A CB     1 
ATOM   4874 C  CG     . PRO A 1 864  ? 198.361 146.010 127.243 1.00 26.97 ? 864  PRO A CG     1 
ATOM   4875 C  CD     . PRO A 1 864  ? 197.991 146.683 128.528 1.00 26.97 ? 864  PRO A CD     1 
ATOM   4876 N  N      . ARG A 1 865  ? 194.780 144.853 125.991 1.00 34.40 ? 865  ARG A N      1 
ATOM   4877 C  CA     . ARG A 1 865  ? 194.151 143.548 125.925 1.00 34.40 ? 865  ARG A CA     1 
ATOM   4878 C  C      . ARG A 1 865  ? 195.210 142.456 125.904 1.00 34.40 ? 865  ARG A C      1 
ATOM   4879 O  O      . ARG A 1 865  ? 196.367 142.676 125.538 1.00 34.40 ? 865  ARG A O      1 
ATOM   4880 C  CB     . ARG A 1 865  ? 193.269 143.424 124.686 1.00 34.40 ? 865  ARG A CB     1 
ATOM   4881 C  CG     . ARG A 1 865  ? 192.084 144.350 124.672 1.00 34.40 ? 865  ARG A CG     1 
ATOM   4882 C  CD     . ARG A 1 865  ? 191.211 144.107 123.466 1.00 34.40 ? 865  ARG A CD     1 
ATOM   4883 N  NE     . ARG A 1 865  ? 190.588 142.790 123.517 1.00 34.40 ? 865  ARG A NE     1 
ATOM   4884 C  CZ     . ARG A 1 865  ? 189.902 142.252 122.516 1.00 34.40 ? 865  ARG A CZ     1 
ATOM   4885 N  NH1    . ARG A 1 865  ? 189.748 142.921 121.382 1.00 34.40 ? 865  ARG A NH1    1 
ATOM   4886 N  NH2    . ARG A 1 865  ? 189.372 141.046 122.647 1.00 34.40 ? 865  ARG A NH2    1 
ATOM   4887 N  N      . PHE A 1 866  ? 194.797 141.262 126.297 1.00 42.40 ? 866  PHE A N      1 
ATOM   4888 C  CA     . PHE A 1 866  ? 195.672 140.103 126.273 1.00 42.40 ? 866  PHE A CA     1 
ATOM   4889 C  C      . PHE A 1 866  ? 195.624 139.470 124.890 1.00 42.40 ? 866  PHE A C      1 
ATOM   4890 O  O      . PHE A 1 866  ? 194.541 139.228 124.350 1.00 42.40 ? 866  PHE A O      1 
ATOM   4891 C  CB     . PHE A 1 866  ? 195.248 139.097 127.342 1.00 42.40 ? 866  PHE A CB     1 
ATOM   4892 C  CG     . PHE A 1 866  ? 196.114 137.881 127.403 1.00 42.40 ? 866  PHE A CG     1 
ATOM   4893 C  CD1    . PHE A 1 866  ? 197.376 137.944 127.963 1.00 42.40 ? 866  PHE A CD1    1 
ATOM   4894 C  CD2    . PHE A 1 866  ? 195.664 136.672 126.904 1.00 42.40 ? 866  PHE A CD2    1 
ATOM   4895 C  CE1    . PHE A 1 866  ? 198.171 136.821 128.026 1.00 42.40 ? 866  PHE A CE1    1 
ATOM   4896 C  CE2    . PHE A 1 866  ? 196.460 135.549 126.958 1.00 42.40 ? 866  PHE A CE2    1 
ATOM   4897 C  CZ     . PHE A 1 866  ? 197.715 135.625 127.517 1.00 42.40 ? 866  PHE A CZ     1 
ATOM   4898 N  N      . ASP A 1 867  ? 196.799 139.212 124.315 1.00 52.79 ? 867  ASP A N      1 
ATOM   4899 C  CA     . ASP A 1 867  ? 196.858 138.533 123.037 1.00 52.79 ? 867  ASP A CA     1 
ATOM   4900 C  C      . ASP A 1 867  ? 198.091 137.644 122.931 1.00 52.79 ? 867  ASP A C      1 
ATOM   4901 O  O      . ASP A 1 867  ? 199.200 138.093 123.258 1.00 52.79 ? 867  ASP A O      1 
ATOM   4902 C  CB     . ASP A 1 867  ? 196.816 139.525 121.869 1.00 52.79 ? 867  ASP A CB     1 
ATOM   4903 C  CG     . ASP A 1 867  ? 197.815 140.656 122.012 1.00 52.79 ? 867  ASP A CG     1 
ATOM   4904 O  OD1    . ASP A 1 867  ? 198.427 140.797 123.089 1.00 52.79 ? 867  ASP A OD1    1 
ATOM   4905 O  OD2    . ASP A 1 867  ? 197.991 141.412 121.034 1.00 52.79 ? 867  ASP A OD2    1 
ATOM   4906 N  N      . PRO A 1 868  ? 197.937 136.394 122.494 1.00 57.43 ? 868  PRO A N      1 
ATOM   4907 C  CA     . PRO A 1 868  ? 199.088 135.492 122.364 1.00 57.43 ? 868  PRO A CA     1 
ATOM   4908 C  C      . PRO A 1 868  ? 199.972 135.746 121.152 1.00 57.43 ? 868  PRO A C      1 
ATOM   4909 O  O      . PRO A 1 868  ? 200.856 134.930 120.881 1.00 57.43 ? 868  PRO A O      1 
ATOM   4910 C  CB     . PRO A 1 868  ? 198.421 134.110 122.256 1.00 57.43 ? 868  PRO A CB     1 
ATOM   4911 C  CG     . PRO A 1 868  ? 197.055 134.288 122.832 1.00 57.43 ? 868  PRO A CG     1 
ATOM   4912 C  CD     . PRO A 1 868  ? 196.660 135.667 122.432 1.00 57.43 ? 868  PRO A CD     1 
ATOM   4913 N  N      . ALA A 1 869  ? 199.763 136.835 120.410 1.00 60.02 ? 869  ALA A N      1 
ATOM   4914 C  CA     . ALA A 1 869  ? 200.594 137.111 119.243 1.00 60.02 ? 869  ALA A CA     1 
ATOM   4915 C  C      . ALA A 1 869  ? 201.972 137.611 119.657 1.00 60.02 ? 869  ALA A C      1 
ATOM   4916 O  O      . ALA A 1 869  ? 202.992 136.979 119.363 1.00 60.02 ? 869  ALA A O      1 
ATOM   4917 C  CB     . ALA A 1 869  ? 199.897 138.127 118.336 1.00 60.02 ? 869  ALA A CB     1 
ATOM   4918 N  N      . LYS A 1 870  ? 202.020 138.744 120.349 1.00 58.15 ? 870  LYS A N      1 
ATOM   4919 C  CA     . LYS A 1 870  ? 203.286 139.295 120.798 1.00 58.15 ? 870  LYS A CA     1 
ATOM   4920 C  C      . LYS A 1 870  ? 203.726 138.622 122.095 1.00 58.15 ? 870  LYS A C      1 
ATOM   4921 O  O      . LYS A 1 870  ? 203.013 137.796 122.672 1.00 58.15 ? 870  LYS A O      1 
ATOM   4922 C  CB     . LYS A 1 870  ? 203.173 140.807 120.969 1.00 58.15 ? 870  LYS A CB     1 
ATOM   4923 C  CG     . LYS A 1 870  ? 202.187 141.241 122.028 1.00 58.15 ? 870  LYS A CG     1 
ATOM   4924 C  CD     . LYS A 1 870  ? 202.105 142.754 122.086 1.00 58.15 ? 870  LYS A CD     1 
ATOM   4925 C  CE     . LYS A 1 870  ? 201.376 143.300 120.872 1.00 58.15 ? 870  LYS A CE     1 
ATOM   4926 N  NZ     . LYS A 1 870  ? 199.951 142.871 120.851 1.00 58.15 ? 870  LYS A NZ     1 
ATOM   4927 N  N      . THR A 1 871  ? 204.927 138.977 122.547 1.00 53.61 ? 871  THR A N      1 
ATOM   4928 C  CA     . THR A 1 871  ? 205.505 138.321 123.710 1.00 53.61 ? 871  THR A CA     1 
ATOM   4929 C  C      . THR A 1 871  ? 204.809 138.765 124.990 1.00 53.61 ? 871  THR A C      1 
ATOM   4930 O  O      . THR A 1 871  ? 204.197 139.838 125.054 1.00 53.61 ? 871  THR A O      1 
ATOM   4931 C  CB     . THR A 1 871  ? 207.008 138.599 123.802 1.00 53.61 ? 871  THR A CB     1 
ATOM   4932 O  OG1    . THR A 1 871  ? 207.568 137.850 124.889 1.00 53.61 ? 871  THR A OG1    1 
ATOM   4933 C  CG2    . THR A 1 871  ? 207.290 140.083 124.010 1.00 53.61 ? 871  THR A CG2    1 
ATOM   4934 N  N      . LEU A 1 872  ? 204.917 137.919 126.011 1.00 48.05 ? 872  LEU A N      1 
ATOM   4935 C  CA     . LEU A 1 872  ? 204.339 138.176 127.326 1.00 48.05 ? 872  LEU A CA     1 
ATOM   4936 C  C      . LEU A 1 872  ? 202.881 138.620 127.275 1.00 48.05 ? 872  LEU A C      1 
ATOM   4937 O  O      . LEU A 1 872  ? 202.445 139.431 128.090 1.00 48.05 ? 872  LEU A O      1 
ATOM   4938 C  CB     . LEU A 1 872  ? 205.178 139.211 128.077 1.00 48.05 ? 872  LEU A CB     1 
ATOM   4939 C  CG     . LEU A 1 872  ? 204.851 139.405 129.558 1.00 48.05 ? 872  LEU A CG     1 
ATOM   4940 C  CD1    . LEU A 1 872  ? 205.041 138.102 130.317 1.00 48.05 ? 872  LEU A CD1    1 
ATOM   4941 C  CD2    . LEU A 1 872  ? 205.717 140.506 130.150 1.00 48.05 ? 872  LEU A CD2    1 
ATOM   4942 N  N      . GLY A 1 873  ? 202.126 138.081 126.326 1.00 45.93 ? 873  GLY A N      1 
ATOM   4943 C  CA     . GLY A 1 873  ? 200.731 138.432 126.193 1.00 45.93 ? 873  GLY A CA     1 
ATOM   4944 C  C      . GLY A 1 873  ? 200.446 139.897 125.972 1.00 45.93 ? 873  GLY A C      1 
ATOM   4945 O  O      . GLY A 1 873  ? 199.284 140.302 126.046 1.00 45.93 ? 873  GLY A O      1 
ATOM   4946 N  N      . GLY A 1 874  ? 201.464 140.710 125.695 1.00 41.53 ? 874  GLY A N      1 
ATOM   4947 C  CA     . GLY A 1 874  ? 201.280 142.142 125.623 1.00 41.53 ? 874  GLY A CA     1 
ATOM   4948 C  C      . GLY A 1 874  ? 201.232 142.846 126.960 1.00 41.53 ? 874  GLY A C      1 
ATOM   4949 O  O      . GLY A 1 874  ? 201.064 144.071 126.989 1.00 41.53 ? 874  GLY A O      1 
ATOM   4950 N  N      . ILE A 1 875  ? 201.377 142.113 128.063 1.00 36.13 ? 875  ILE A N      1 
ATOM   4951 C  CA     . ILE A 1 875  ? 201.336 142.702 129.395 1.00 36.13 ? 875  ILE A CA     1 
ATOM   4952 C  C      . ILE A 1 875  ? 202.605 143.512 129.616 1.00 36.13 ? 875  ILE A C      1 
ATOM   4953 O  O      . ILE A 1 875  ? 203.720 143.002 129.462 1.00 36.13 ? 875  ILE A O      1 
ATOM   4954 C  CB     . ILE A 1 875  ? 201.176 141.616 130.465 1.00 36.13 ? 875  ILE A CB     1 
ATOM   4955 C  CG1    . ILE A 1 875  ? 199.835 140.911 130.311 1.00 36.13 ? 875  ILE A CG1    1 
ATOM   4956 C  CG2    . ILE A 1 875  ? 201.293 142.199 131.858 1.00 36.13 ? 875  ILE A CG2    1 
ATOM   4957 C  CD1    . ILE A 1 875  ? 199.703 139.706 131.188 1.00 36.13 ? 875  ILE A CD1    1 
ATOM   4958 N  N      . HIS A 1 876  ? 202.435 144.782 129.961 1.00 29.57 ? 876  HIS A N      1 
ATOM   4959 C  CA     . HIS A 1 876  ? 203.566 145.632 130.283 1.00 29.57 ? 876  HIS A CA     1 
ATOM   4960 C  C      . HIS A 1 876  ? 204.160 145.186 131.618 1.00 29.57 ? 876  HIS A C      1 
ATOM   4961 O  O      . HIS A 1 876  ? 203.423 144.719 132.490 1.00 29.57 ? 876  HIS A O      1 
ATOM   4962 C  CB     . HIS A 1 876  ? 203.100 147.089 130.335 1.00 29.57 ? 876  HIS A CB     1 
ATOM   4963 C  CG     . HIS A 1 876  ? 204.206 148.096 130.310 1.00 29.57 ? 876  HIS A CG     1 
ATOM   4964 N  ND1    . HIS A 1 876  ? 204.719 148.671 131.451 1.00 29.57 ? 876  HIS A ND1    1 
ATOM   4965 C  CD2    . HIS A 1 876  ? 204.917 148.608 129.279 1.00 29.57 ? 876  HIS A CD2    1 
ATOM   4966 C  CE1    . HIS A 1 876  ? 205.681 149.514 131.120 1.00 29.57 ? 876  HIS A CE1    1 
ATOM   4967 N  NE2    . HIS A 1 876  ? 205.821 149.493 129.809 1.00 29.57 ? 876  HIS A NE2    1 
ATOM   4968 N  N      . PRO A 1 877  ? 205.486 145.261 131.791 1.00 29.65 ? 877  PRO A N      1 
ATOM   4969 C  CA     . PRO A 1 877  ? 206.086 144.764 133.042 1.00 29.65 ? 877  PRO A CA     1 
ATOM   4970 C  C      . PRO A 1 877  ? 205.729 145.572 134.279 1.00 29.65 ? 877  PRO A C      1 
ATOM   4971 O  O      . PRO A 1 877  ? 205.900 145.058 135.390 1.00 29.65 ? 877  PRO A O      1 
ATOM   4972 C  CB     . PRO A 1 877  ? 207.592 144.808 132.755 1.00 29.65 ? 877  PRO A CB     1 
ATOM   4973 C  CG     . PRO A 1 877  ? 207.745 145.757 131.639 1.00 29.65 ? 877  PRO A CG     1 
ATOM   4974 C  CD     . PRO A 1 877  ? 206.519 145.603 130.801 1.00 29.65 ? 877  PRO A CD     1 
ATOM   4975 N  N      . THR A 1 878  ? 205.223 146.799 134.129 1.00 27.50 ? 878  THR A N      1 
ATOM   4976 C  CA     . THR A 1 878  ? 204.646 147.502 135.271 1.00 27.50 ? 878  THR A CA     1 
ATOM   4977 C  C      . THR A 1 878  ? 203.410 146.789 135.797 1.00 27.50 ? 878  THR A C      1 
ATOM   4978 O  O      . THR A 1 878  ? 203.169 146.774 137.007 1.00 27.50 ? 878  THR A O      1 
ATOM   4979 C  CB     . THR A 1 878  ? 204.304 148.940 134.893 1.00 27.50 ? 878  THR A CB     1 
ATOM   4980 O  OG1    . THR A 1 878  ? 203.449 148.946 133.743 1.00 27.50 ? 878  THR A OG1    1 
ATOM   4981 C  CG2    . THR A 1 878  ? 205.563 149.735 134.613 1.00 27.50 ? 878  THR A CG2    1 
ATOM   4982 N  N      . GLU A 1 879  ? 202.641 146.158 134.912 1.00 29.03 ? 879  GLU A N      1 
ATOM   4983 C  CA     . GLU A 1 879  ? 201.512 145.352 135.356 1.00 29.03 ? 879  GLU A CA     1 
ATOM   4984 C  C      . GLU A 1 879  ? 201.974 144.068 136.045 1.00 29.03 ? 879  GLU A C      1 
ATOM   4985 O  O      . GLU A 1 879  ? 201.299 143.577 136.955 1.00 29.03 ? 879  GLU A O      1 
ATOM   4986 C  CB     . GLU A 1 879  ? 200.611 145.058 134.161 1.00 29.03 ? 879  GLU A CB     1 
ATOM   4987 C  CG     . GLU A 1 879  ? 199.328 144.358 134.484 1.00 29.03 ? 879  GLU A CG     1 
ATOM   4988 C  CD     . GLU A 1 879  ? 198.487 144.109 133.258 1.00 29.03 ? 879  GLU A CD     1 
ATOM   4989 O  OE1    . GLU A 1 879  ? 198.875 144.560 132.160 1.00 29.03 ? 879  GLU A OE1    1 
ATOM   4990 O  OE2    . GLU A 1 879  ? 197.454 143.425 133.387 1.00 29.03 ? 879  GLU A OE2    1 
ATOM   4991 N  N      . ILE A 1 880  ? 203.146 143.546 135.677 1.00 29.66 ? 880  ILE A N      1 
ATOM   4992 C  CA     . ILE A 1 880  ? 203.698 142.385 136.372 1.00 29.66 ? 880  ILE A CA     1 
ATOM   4993 C  C      . ILE A 1 880  ? 204.180 142.773 137.766 1.00 29.66 ? 880  ILE A C      1 
ATOM   4994 O  O      . ILE A 1 880  ? 203.986 142.027 138.735 1.00 29.66 ? 880  ILE A O      1 
ATOM   4995 C  CB     . ILE A 1 880  ? 204.825 141.757 135.533 1.00 29.66 ? 880  ILE A CB     1 
ATOM   4996 C  CG1    . ILE A 1 880  ? 204.288 141.306 134.184 1.00 29.66 ? 880  ILE A CG1    1 
ATOM   4997 C  CG2    . ILE A 1 880  ? 205.442 140.560 136.238 1.00 29.66 ? 880  ILE A CG2    1 
ATOM   4998 C  CD1    . ILE A 1 880  ? 205.368 140.902 133.240 1.00 29.66 ? 880  ILE A CD1    1 
ATOM   4999 N  N      . VAL A 1 881  ? 204.801 143.951 137.893 1.00 28.11 ? 881  VAL A N      1 
ATOM   5000 C  CA     . VAL A 1 881  ? 205.183 144.461 139.209 1.00 28.11 ? 881  VAL A CA     1 
ATOM   5001 C  C      . VAL A 1 881  ? 203.938 144.752 140.047 1.00 28.11 ? 881  VAL A C      1 
ATOM   5002 O  O      . VAL A 1 881  ? 203.935 144.541 141.268 1.00 28.11 ? 881  VAL A O      1 
ATOM   5003 C  CB     . VAL A 1 881  ? 206.090 145.700 139.045 1.00 28.11 ? 881  VAL A CB     1 
ATOM   5004 C  CG1    . VAL A 1 881  ? 206.477 146.307 140.386 1.00 28.11 ? 881  VAL A CG1    1 
ATOM   5005 C  CG2    . VAL A 1 881  ? 207.346 145.339 138.285 1.00 28.11 ? 881  VAL A CG2    1 
ATOM   5006 N  N      . LEU A 1 882  ? 202.849 145.180 139.399 1.00 26.87 ? 882  LEU A N      1 
ATOM   5007 C  CA     . LEU A 1 882  ? 201.577 145.369 140.091 1.00 26.87 ? 882  LEU A CA     1 
ATOM   5008 C  C      . LEU A 1 882  ? 201.011 144.045 140.591 1.00 26.87 ? 882  LEU A C      1 
ATOM   5009 O  O      . LEU A 1 882  ? 200.482 143.979 141.706 1.00 26.87 ? 882  LEU A O      1 
ATOM   5010 C  CB     . LEU A 1 882  ? 200.579 146.059 139.160 1.00 26.87 ? 882  LEU A CB     1 
ATOM   5011 C  CG     . LEU A 1 882  ? 199.237 146.484 139.758 1.00 26.87 ? 882  LEU A CG     1 
ATOM   5012 C  CD1    . LEU A 1 882  ? 199.453 147.588 140.755 1.00 26.87 ? 882  LEU A CD1    1 
ATOM   5013 C  CD2    . LEU A 1 882  ? 198.260 146.917 138.691 1.00 26.87 ? 882  LEU A CD2    1 
ATOM   5014 N  N      . TYR A 1 883  ? 201.120 142.982 139.784 1.00 29.61 ? 883  TYR A N      1 
ATOM   5015 C  CA     . TYR A 1 883  ? 200.681 141.652 140.216 1.00 29.61 ? 883  TYR A CA     1 
ATOM   5016 C  C      . TYR A 1 883  ? 201.501 141.169 141.398 1.00 29.61 ? 883  TYR A C      1 
ATOM   5017 O  O      . TYR A 1 883  ? 200.959 140.584 142.344 1.00 29.61 ? 883  TYR A O      1 
ATOM   5018 C  CB     . TYR A 1 883  ? 200.816 140.629 139.088 1.00 29.61 ? 883  TYR A CB     1 
ATOM   5019 C  CG     . TYR A 1 883  ? 199.940 140.832 137.882 1.00 29.61 ? 883  TYR A CG     1 
ATOM   5020 C  CD1    . TYR A 1 883  ? 198.878 141.719 137.902 1.00 29.61 ? 883  TYR A CD1    1 
ATOM   5021 C  CD2    . TYR A 1 883  ? 200.176 140.116 136.716 1.00 29.61 ? 883  TYR A CD2    1 
ATOM   5022 C  CE1    . TYR A 1 883  ? 198.100 141.908 136.794 1.00 29.61 ? 883  TYR A CE1    1 
ATOM   5023 C  CE2    . TYR A 1 883  ? 199.390 140.288 135.605 1.00 29.61 ? 883  TYR A CE2    1 
ATOM   5024 C  CZ     . TYR A 1 883  ? 198.350 141.182 135.652 1.00 29.61 ? 883  TYR A CZ     1 
ATOM   5025 O  OH     . TYR A 1 883  ? 197.565 141.360 134.542 1.00 29.61 ? 883  TYR A OH     1 
ATOM   5026 N  N      . PHE A 1 884  ? 202.814 141.409 141.345 1.00 32.30 ? 884  PHE A N      1 
ATOM   5027 C  CA     . PHE A 1 884  ? 203.716 141.051 142.434 1.00 32.30 ? 884  PHE A CA     1 
ATOM   5028 C  C      . PHE A 1 884  ? 203.350 141.774 143.722 1.00 32.30 ? 884  PHE A C      1 
ATOM   5029 O  O      . PHE A 1 884  ? 203.307 141.161 144.795 1.00 32.30 ? 884  PHE A O      1 
ATOM   5030 C  CB     . PHE A 1 884  ? 205.152 141.376 142.026 1.00 32.30 ? 884  PHE A CB     1 
ATOM   5031 C  CG     . PHE A 1 884  ? 206.184 141.002 143.049 1.00 32.30 ? 884  PHE A CG     1 
ATOM   5032 C  CD1    . PHE A 1 884  ? 206.600 139.689 143.182 1.00 32.30 ? 884  PHE A CD1    1 
ATOM   5033 C  CD2    . PHE A 1 884  ? 206.748 141.969 143.871 1.00 32.30 ? 884  PHE A CD2    1 
ATOM   5034 C  CE1    . PHE A 1 884  ? 207.560 139.343 144.113 1.00 32.30 ? 884  PHE A CE1    1 
ATOM   5035 C  CE2    . PHE A 1 884  ? 207.704 141.627 144.811 1.00 32.30 ? 884  PHE A CE2    1 
ATOM   5036 C  CZ     . PHE A 1 884  ? 208.108 140.312 144.932 1.00 32.30 ? 884  PHE A CZ     1 
ATOM   5037 N  N      . TRP A 1 885  ? 203.049 143.068 143.638 1.00 31.99 ? 885  TRP A N      1 
ATOM   5038 C  CA     . TRP A 1 885  ? 202.777 143.795 144.871 1.00 31.99 ? 885  TRP A CA     1 
ATOM   5039 C  C      . TRP A 1 885  ? 201.374 143.513 145.410 1.00 31.99 ? 885  TRP A C      1 
ATOM   5040 O  O      . TRP A 1 885  ? 201.171 143.536 146.629 1.00 31.99 ? 885  TRP A O      1 
ATOM   5041 C  CB     . TRP A 1 885  ? 202.997 145.298 144.678 1.00 31.99 ? 885  TRP A CB     1 
ATOM   5042 C  CG     . TRP A 1 885  ? 203.015 146.026 145.992 1.00 31.99 ? 885  TRP A CG     1 
ATOM   5043 C  CD1    . TRP A 1 885  ? 202.012 146.754 146.536 1.00 31.99 ? 885  TRP A CD1    1 
ATOM   5044 C  CD2    . TRP A 1 885  ? 204.082 146.045 146.949 1.00 31.99 ? 885  TRP A CD2    1 
ATOM   5045 N  NE1    . TRP A 1 885  ? 202.383 147.256 147.754 1.00 31.99 ? 885  TRP A NE1    1 
ATOM   5046 C  CE2    . TRP A 1 885  ? 203.652 146.829 148.037 1.00 31.99 ? 885  TRP A CE2    1 
ATOM   5047 C  CE3    . TRP A 1 885  ? 205.360 145.477 146.990 1.00 31.99 ? 885  TRP A CE3    1 
ATOM   5048 C  CZ2    . TRP A 1 885  ? 204.452 147.062 149.154 1.00 31.99 ? 885  TRP A CZ2    1 
ATOM   5049 C  CZ3    . TRP A 1 885  ? 206.154 145.711 148.099 1.00 31.99 ? 885  TRP A CZ3    1 
ATOM   5050 C  CH2    . TRP A 1 885  ? 205.695 146.497 149.166 1.00 31.99 ? 885  TRP A CH2    1 
ATOM   5051 N  N      . VAL A 1 886  ? 200.401 143.198 144.555 1.00 29.27 ? 886  VAL A N      1 
ATOM   5052 C  CA     . VAL A 1 886  ? 199.109 142.811 145.123 1.00 29.27 ? 886  VAL A CA     1 
ATOM   5053 C  C      . VAL A 1 886  ? 199.171 141.380 145.675 1.00 29.27 ? 886  VAL A C      1 
ATOM   5054 O  O      . VAL A 1 886  ? 198.505 141.065 146.668 1.00 29.27 ? 886  VAL A O      1 
ATOM   5055 C  CB     . VAL A 1 886  ? 197.973 142.996 144.101 1.00 29.27 ? 886  VAL A CB     1 
ATOM   5056 C  CG1    . VAL A 1 886  ? 196.643 142.706 144.726 1.00 29.27 ? 886  VAL A CG1    1 
ATOM   5057 C  CG2    . VAL A 1 886  ? 197.930 144.401 143.619 1.00 29.27 ? 886  VAL A CG2    1 
ATOM   5058 N  N      . PHE A 1 887  ? 200.014 140.513 145.104 1.00 32.21 ? 887  PHE A N      1 
ATOM   5059 C  CA     . PHE A 1 887  ? 200.276 139.222 145.735 1.00 32.21 ? 887  PHE A CA     1 
ATOM   5060 C  C      . PHE A 1 887  ? 200.980 139.389 147.077 1.00 32.21 ? 887  PHE A C      1 
ATOM   5061 O  O      . PHE A 1 887  ? 200.738 138.611 148.004 1.00 32.21 ? 887  PHE A O      1 
ATOM   5062 C  CB     . PHE A 1 887  ? 201.104 138.343 144.800 1.00 32.21 ? 887  PHE A CB     1 
ATOM   5063 C  CG     . PHE A 1 887  ? 201.432 136.996 145.369 1.00 32.21 ? 887  PHE A CG     1 
ATOM   5064 C  CD1    . PHE A 1 887  ? 200.461 136.015 145.469 1.00 32.21 ? 887  PHE A CD1    1 
ATOM   5065 C  CD2    . PHE A 1 887  ? 202.718 136.707 145.791 1.00 32.21 ? 887  PHE A CD2    1 
ATOM   5066 C  CE1    . PHE A 1 887  ? 200.764 134.773 145.991 1.00 32.21 ? 887  PHE A CE1    1 
ATOM   5067 C  CE2    . PHE A 1 887  ? 203.029 135.470 146.317 1.00 32.21 ? 887  PHE A CE2    1 
ATOM   5068 C  CZ     . PHE A 1 887  ? 202.051 134.501 146.414 1.00 32.21 ? 887  PHE A CZ     1 
ATOM   5069 N  N      . THR A 1 888  ? 201.826 140.413 147.202 1.00 33.47 ? 888  THR A N      1 
ATOM   5070 C  CA     . THR A 1 888  ? 202.412 140.770 148.491 1.00 33.47 ? 888  THR A CA     1 
ATOM   5071 C  C      . THR A 1 888  ? 201.344 141.203 149.495 1.00 33.47 ? 888  THR A C      1 
ATOM   5072 O  O      . THR A 1 888  ? 201.393 140.813 150.666 1.00 33.47 ? 888  THR A O      1 
ATOM   5073 C  CB     . THR A 1 888  ? 203.440 141.881 148.282 1.00 33.47 ? 888  THR A CB     1 
ATOM   5074 O  OG1    . THR A 1 888  ? 204.439 141.439 147.358 1.00 33.47 ? 888  THR A OG1    1 
ATOM   5075 C  CG2    . THR A 1 888  ? 204.096 142.268 149.570 1.00 33.47 ? 888  THR A CG2    1 
ATOM   5076 N  N      . ILE A 1 889  ? 200.366 141.999 149.047 1.00 30.30 ? 889  ILE A N      1 
ATOM   5077 C  CA     . ILE A 1 889  ? 199.249 142.400 149.910 1.00 30.30 ? 889  ILE A CA     1 
ATOM   5078 C  C      . ILE A 1 889  ? 198.418 141.184 150.326 1.00 30.30 ? 889  ILE A C      1 
ATOM   5079 O  O      . ILE A 1 889  ? 197.972 141.075 151.479 1.00 30.30 ? 889  ILE A O      1 
ATOM   5080 C  CB     . ILE A 1 889  ? 198.390 143.462 149.195 1.00 30.30 ? 889  ILE A CB     1 
ATOM   5081 C  CG1    . ILE A 1 889  ? 199.211 144.718 148.925 1.00 30.30 ? 889  ILE A CG1    1 
ATOM   5082 C  CG2    . ILE A 1 889  ? 197.181 143.850 150.020 1.00 30.30 ? 889  ILE A CG2    1 
ATOM   5083 C  CD1    . ILE A 1 889  ? 198.555 145.674 147.965 1.00 30.30 ? 889  ILE A CD1    1 
ATOM   5084 N  N      . LEU A 1 890  ? 198.237 140.237 149.404 1.00 30.17 ? 890  LEU A N      1 
ATOM   5085 C  CA     . LEU A 1 890  ? 197.495 139.011 149.684 1.00 30.17 ? 890  LEU A CA     1 
ATOM   5086 C  C      . LEU A 1 890  ? 198.194 138.155 150.731 1.00 30.17 ? 890  LEU A C      1 
ATOM   5087 O  O      . LEU A 1 890  ? 197.562 137.682 151.681 1.00 30.17 ? 890  LEU A O      1 
ATOM   5088 C  CB     . LEU A 1 890  ? 197.310 138.214 148.395 1.00 30.17 ? 890  LEU A CB     1 
ATOM   5089 C  CG     . LEU A 1 890  ? 196.579 136.880 148.531 1.00 30.17 ? 890  LEU A CG     1 
ATOM   5090 C  CD1    . LEU A 1 890  ? 195.130 137.086 148.919 1.00 30.17 ? 890  LEU A CD1    1 
ATOM   5091 C  CD2    . LEU A 1 890  ? 196.698 136.072 147.256 1.00 30.17 ? 890  LEU A CD2    1 
ATOM   5092 N  N      . ILE A 1 891  ? 199.502 137.939 150.564 1.00 32.02 ? 891  ILE A N      1 
ATOM   5093 C  CA     . ILE A 1 891  ? 200.277 137.162 151.528 1.00 32.02 ? 891  ILE A CA     1 
ATOM   5094 C  C      . ILE A 1 891  ? 200.358 137.889 152.866 1.00 32.02 ? 891  ILE A C      1 
ATOM   5095 O  O      . ILE A 1 891  ? 200.368 137.251 153.924 1.00 32.02 ? 891  ILE A O      1 
ATOM   5096 C  CB     . ILE A 1 891  ? 201.666 136.843 150.933 1.00 32.02 ? 891  ILE A CB     1 
ATOM   5097 C  CG1    . ILE A 1 891  ? 201.517 135.974 149.686 1.00 32.02 ? 891  ILE A CG1    1 
ATOM   5098 C  CG2    . ILE A 1 891  ? 202.574 136.115 151.910 1.00 32.02 ? 891  ILE A CG2    1 
ATOM   5099 C  CD1    . ILE A 1 891  ? 200.857 134.646 149.931 1.00 32.02 ? 891  ILE A CD1    1 
ATOM   5100 N  N      . GLU A 1 892  ? 200.352 139.225 152.847 1.00 33.38 ? 892  GLU A N      1 
ATOM   5101 C  CA     . GLU A 1 892  ? 200.277 140.001 154.081 1.00 33.38 ? 892  GLU A CA     1 
ATOM   5102 C  C      . GLU A 1 892  ? 198.973 139.752 154.829 1.00 33.38 ? 892  GLU A C      1 
ATOM   5103 O  O      . GLU A 1 892  ? 198.982 139.550 156.046 1.00 33.38 ? 892  GLU A O      1 
ATOM   5104 C  CB     . GLU A 1 892  ? 200.444 141.487 153.764 1.00 33.38 ? 892  GLU A CB     1 
ATOM   5105 C  CG     . GLU A 1 892  ? 200.169 142.409 154.931 1.00 33.38 ? 892  GLU A CG     1 
ATOM   5106 C  CD     . GLU A 1 892  ? 201.117 142.210 156.088 1.00 33.38 ? 892  GLU A CD     1 
ATOM   5107 O  OE1    . GLU A 1 892  ? 202.303 141.889 155.865 1.00 33.38 ? 892  GLU A OE1    1 
ATOM   5108 O  OE2    . GLU A 1 892  ? 200.654 142.337 157.238 1.00 33.38 ? 892  GLU A OE2    1 
ATOM   5109 N  N      . GLU A 1 893  ? 197.849 139.711 154.114 1.00 30.57 ? 893  GLU A N      1 
ATOM   5110 C  CA     . GLU A 1 893  ? 196.580 139.460 154.794 1.00 30.57 ? 893  GLU A CA     1 
ATOM   5111 C  C      . GLU A 1 893  ? 196.435 138.006 155.230 1.00 30.57 ? 893  GLU A C      1 
ATOM   5112 O  O      . GLU A 1 893  ? 195.809 137.734 156.262 1.00 30.57 ? 893  GLU A O      1 
ATOM   5113 C  CB     . GLU A 1 893  ? 195.418 139.883 153.903 1.00 30.57 ? 893  GLU A CB     1 
ATOM   5114 C  CG     . GLU A 1 893  ? 195.392 141.377 153.671 1.00 30.57 ? 893  GLU A CG     1 
ATOM   5115 C  CD     . GLU A 1 893  ? 195.143 142.163 154.945 1.00 30.57 ? 893  GLU A CD     1 
ATOM   5116 O  OE1    . GLU A 1 893  ? 194.326 141.725 155.777 1.00 30.57 ? 893  GLU A OE1    1 
ATOM   5117 O  OE2    . GLU A 1 893  ? 195.797 143.207 155.133 1.00 30.57 ? 893  GLU A OE2    1 
ATOM   5118 N  N      . ILE A 1 894  ? 197.025 137.069 154.483 1.00 30.50 ? 894  ILE A N      1 
ATOM   5119 C  CA     . ILE A 1 894  ? 197.072 135.672 154.917 1.00 30.50 ? 894  ILE A CA     1 
ATOM   5120 C  C      . ILE A 1 894  ? 197.915 135.530 156.182 1.00 30.50 ? 894  ILE A C      1 
ATOM   5121 O  O      . ILE A 1 894  ? 197.555 134.788 157.104 1.00 30.50 ? 894  ILE A O      1 
ATOM   5122 C  CB     . ILE A 1 894  ? 197.594 134.779 153.772 1.00 30.50 ? 894  ILE A CB     1 
ATOM   5123 C  CG1    . ILE A 1 894  ? 196.584 134.729 152.630 1.00 30.50 ? 894  ILE A CG1    1 
ATOM   5124 C  CG2    . ILE A 1 894  ? 197.887 133.360 154.235 1.00 30.50 ? 894  ILE A CG2    1 
ATOM   5125 C  CD1    . ILE A 1 894  ? 197.119 134.070 151.387 1.00 30.50 ? 894  ILE A CD1    1 
ATOM   5126 N  N      . ARG A 1 895  ? 199.026 136.265 156.259 1.00 32.21 ? 895  ARG A N      1 
ATOM   5127 C  CA     . ARG A 1 895  ? 199.855 136.268 157.459 1.00 32.21 ? 895  ARG A CA     1 
ATOM   5128 C  C      . ARG A 1 895  ? 199.117 136.901 158.633 1.00 32.21 ? 895  ARG A C      1 
ATOM   5129 O  O      . ARG A 1 895  ? 199.277 136.461 159.775 1.00 32.21 ? 895  ARG A O      1 
ATOM   5130 C  CB     . ARG A 1 895  ? 201.165 137.010 157.171 1.00 32.21 ? 895  ARG A CB     1 
ATOM   5131 C  CG     . ARG A 1 895  ? 202.332 136.787 158.145 1.00 32.21 ? 895  ARG A CG     1 
ATOM   5132 C  CD     . ARG A 1 895  ? 202.336 137.774 159.298 1.00 32.21 ? 895  ARG A CD     1 
ATOM   5133 N  NE     . ARG A 1 895  ? 202.308 139.153 158.833 1.00 32.21 ? 895  ARG A NE     1 
ATOM   5134 C  CZ     . ARG A 1 895  ? 201.855 140.165 159.561 1.00 32.21 ? 895  ARG A CZ     1 
ATOM   5135 N  NH1    . ARG A 1 895  ? 201.378 139.947 160.776 1.00 32.21 ? 895  ARG A NH1    1 
ATOM   5136 N  NH2    . ARG A 1 895  ? 201.860 141.391 159.072 1.00 32.21 ? 895  ARG A NH2    1 
ATOM   5137 N  N      . GLN A 1 896  ? 198.320 137.942 158.377 1.00 31.24 ? 896  GLN A N      1 
ATOM   5138 C  CA     . GLN A 1 896  ? 197.539 138.556 159.448 1.00 31.24 ? 896  GLN A CA     1 
ATOM   5139 C  C      . GLN A 1 896  ? 196.453 137.617 159.951 1.00 31.24 ? 896  GLN A C      1 
ATOM   5140 O  O      . GLN A 1 896  ? 196.128 137.621 161.142 1.00 31.24 ? 896  GLN A O      1 
ATOM   5141 C  CB     . GLN A 1 896  ? 196.908 139.865 158.979 1.00 31.24 ? 896  GLN A CB     1 
ATOM   5142 C  CG     . GLN A 1 896  ? 197.880 140.985 158.713 1.00 31.24 ? 896  GLN A CG     1 
ATOM   5143 C  CD     . GLN A 1 896  ? 197.183 142.236 158.241 1.00 31.24 ? 896  GLN A CD     1 
ATOM   5144 O  OE1    . GLN A 1 896  ? 195.960 142.274 158.139 1.00 31.24 ? 896  GLN A OE1    1 
ATOM   5145 N  NE2    . GLN A 1 896  ? 197.960 143.265 157.926 1.00 31.24 ? 896  GLN A NE2    1 
ATOM   5146 N  N      . LEU A 1 897  ? 195.869 136.821 159.055 1.00 32.65 ? 897  LEU A N      1 
ATOM   5147 C  CA     . LEU A 1 897  ? 194.894 135.817 159.470 1.00 32.65 ? 897  LEU A CA     1 
ATOM   5148 C  C      . LEU A 1 897  ? 195.553 134.706 160.277 1.00 32.65 ? 897  LEU A C      1 
ATOM   5149 O  O      . LEU A 1 897  ? 195.032 134.287 161.316 1.00 32.65 ? 897  LEU A O      1 
ATOM   5150 C  CB     . LEU A 1 897  ? 194.187 135.241 158.246 1.00 32.65 ? 897  LEU A CB     1 
ATOM   5151 C  CG     . LEU A 1 897  ? 193.174 134.129 158.506 1.00 32.65 ? 897  LEU A CG     1 
ATOM   5152 C  CD1    . LEU A 1 897  ? 192.063 134.623 159.392 1.00 32.65 ? 897  LEU A CD1    1 
ATOM   5153 C  CD2    . LEU A 1 897  ? 192.618 133.613 157.196 1.00 32.65 ? 897  LEU A CD2    1 
ATOM   5154 N  N      . ALA A 1 898  ? 196.704 134.219 159.811 1.00 31.72 ? 898  ALA A N      1 
ATOM   5155 C  CA     . ALA A 1 898  ? 197.383 133.117 160.481 1.00 31.72 ? 898  ALA A CA     1 
ATOM   5156 C  C      . ALA A 1 898  ? 198.002 133.545 161.804 1.00 31.72 ? 898  ALA A C      1 
ATOM   5157 O  O      . ALA A 1 898  ? 198.182 132.712 162.697 1.00 31.72 ? 898  ALA A O      1 
ATOM   5158 C  CB     . ALA A 1 898  ? 198.457 132.533 159.565 1.00 31.72 ? 898  ALA A CB     1 
ATOM   5159 N  N      . ALA A 1 899  ? 198.324 134.828 161.955 1.00 32.88 ? 899  ALA A N      1 
ATOM   5160 C  CA     . ALA A 1 899  ? 198.978 135.333 163.152 1.00 32.88 ? 899  ALA A CA     1 
ATOM   5161 C  C      . ALA A 1 899  ? 197.990 135.831 164.196 1.00 32.88 ? 899  ALA A C      1 
ATOM   5162 O  O      . ALA A 1 899  ? 198.373 136.612 165.074 1.00 32.88 ? 899  ALA A O      1 
ATOM   5163 C  CB     . ALA A 1 899  ? 199.959 136.447 162.786 1.00 32.88 ? 899  ALA A CB     1 
ATOM   5164 N  N      . LYS A 1 900  ? 196.743 135.406 164.125 1.00 34.87 ? 900  LYS A N      1 
ATOM   5165 C  CA     . LYS A 1 900  ? 195.795 135.775 165.156 1.00 34.87 ? 900  LYS A CA     1 
ATOM   5166 C  C      . LYS A 1 900  ? 195.994 134.907 166.399 1.00 34.87 ? 900  LYS A C      1 
ATOM   5167 O  O      . LYS A 1 900  ? 196.400 133.747 166.290 1.00 34.87 ? 900  LYS A O      1 
ATOM   5168 C  CB     . LYS A 1 900  ? 194.367 135.646 164.637 1.00 34.87 ? 900  LYS A CB     1 
ATOM   5169 C  CG     . LYS A 1 900  ? 194.056 136.628 163.532 1.00 34.87 ? 900  LYS A CG     1 
ATOM   5170 C  CD     . LYS A 1 900  ? 194.152 138.045 164.060 1.00 34.87 ? 900  LYS A CD     1 
ATOM   5171 C  CE     . LYS A 1 900  ? 193.817 139.076 163.010 1.00 34.87 ? 900  LYS A CE     1 
ATOM   5172 N  NZ     . LYS A 1 900  ? 193.935 140.452 163.550 1.00 34.87 ? 900  LYS A NZ     1 
ATOM   5173 N  N      . PRO A 1 901  ? 195.753 135.466 167.586 1.00 37.29 ? 901  PRO A N      1 
ATOM   5174 C  CA     . PRO A 1 901  ? 195.965 134.723 168.850 1.00 37.29 ? 901  PRO A CA     1 
ATOM   5175 C  C      . PRO A 1 901  ? 195.129 133.457 169.030 1.00 37.29 ? 901  PRO A C      1 
ATOM   5176 O  O      . PRO A 1 901  ? 195.600 132.560 169.745 1.00 37.29 ? 901  PRO A O      1 
ATOM   5177 C  CB     . PRO A 1 901  ? 195.630 135.767 169.926 1.00 37.29 ? 901  PRO A CB     1 
ATOM   5178 C  CG     . PRO A 1 901  ? 195.890 137.061 169.273 1.00 37.29 ? 901  PRO A CG     1 
ATOM   5179 C  CD     . PRO A 1 901  ? 195.485 136.894 167.848 1.00 37.29 ? 901  PRO A CD     1 
ATOM   5180 N  N      . PRO A 1 902  ? 193.909 133.308 168.473 1.00 39.50 ? 902  PRO A N      1 
ATOM   5181 C  CA     . PRO A 1 902  ? 193.249 131.996 168.577 1.00 39.50 ? 902  PRO A CA     1 
ATOM   5182 C  C      . PRO A 1 902  ? 193.959 130.901 167.794 1.00 39.50 ? 902  PRO A C      1 
ATOM   5183 O  O      . PRO A 1 902  ? 194.846 131.137 166.974 1.00 39.50 ? 902  PRO A O      1 
ATOM   5184 C  CB     . PRO A 1 902  ? 191.853 132.245 168.013 1.00 39.50 ? 902  PRO A CB     1 
ATOM   5185 C  CG     . PRO A 1 902  ? 191.597 133.604 168.288 1.00 39.50 ? 902  PRO A CG     1 
ATOM   5186 C  CD     . PRO A 1 902  ? 192.881 134.307 168.089 1.00 39.50 ? 902  PRO A CD     1 
ATOM   5187 N  N      . LYS A 1 903  ? 193.540 129.669 168.076 1.00 43.26 ? 903  LYS A N      1 
ATOM   5188 C  CA     . LYS A 1 903  ? 194.112 128.466 167.485 1.00 43.26 ? 903  LYS A CA     1 
ATOM   5189 C  C      . LYS A 1 903  ? 193.237 127.868 166.394 1.00 43.26 ? 903  LYS A C      1 
ATOM   5190 O  O      . LYS A 1 903  ? 193.760 127.374 165.392 1.00 43.26 ? 903  LYS A O      1 
ATOM   5191 C  CB     . LYS A 1 903  ? 194.360 127.403 168.563 1.00 43.26 ? 903  LYS A CB     1 
ATOM   5192 C  CG     . LYS A 1 903  ? 195.704 127.494 169.287 1.00 43.26 ? 903  LYS A CG     1 
ATOM   5193 C  CD     . LYS A 1 903  ? 195.742 128.610 170.318 1.00 43.26 ? 903  LYS A CD     1 
ATOM   5194 C  CE     . LYS A 1 903  ? 194.806 128.321 171.477 1.00 43.26 ? 903  LYS A CE     1 
ATOM   5195 N  NZ     . LYS A 1 903  ? 194.867 129.389 172.513 1.00 43.26 ? 903  LYS A NZ     1 
ATOM   5196 N  N      . TYR A 1 904  ? 191.920 127.886 166.570 1.00 44.22 ? 904  TYR A N      1 
ATOM   5197 C  CA     . TYR A 1 904  ? 191.016 127.373 165.554 1.00 44.22 ? 904  TYR A CA     1 
ATOM   5198 C  C      . TYR A 1 904  ? 190.918 128.354 164.395 1.00 44.22 ? 904  TYR A C      1 
ATOM   5199 O  O      . TYR A 1 904  ? 191.101 129.561 164.561 1.00 44.22 ? 904  TYR A O      1 
ATOM   5200 C  CB     . TYR A 1 904  ? 189.628 127.120 166.143 1.00 44.22 ? 904  TYR A CB     1 
ATOM   5201 C  CG     . TYR A 1 904  ? 189.588 126.002 167.158 1.00 44.22 ? 904  TYR A CG     1 
ATOM   5202 C  CD1    . TYR A 1 904  ? 189.555 124.671 166.755 1.00 44.22 ? 904  TYR A CD1    1 
ATOM   5203 C  CD2    . TYR A 1 904  ? 189.579 126.276 168.521 1.00 44.22 ? 904  TYR A CD2    1 
ATOM   5204 C  CE1    . TYR A 1 904  ? 189.517 123.644 167.680 1.00 44.22 ? 904  TYR A CE1    1 
ATOM   5205 C  CE2    . TYR A 1 904  ? 189.541 125.257 169.455 1.00 44.22 ? 904  TYR A CE2    1 
ATOM   5206 C  CZ     . TYR A 1 904  ? 189.510 123.943 169.029 1.00 44.22 ? 904  TYR A CZ     1 
ATOM   5207 O  OH     . TYR A 1 904  ? 189.472 122.927 169.956 1.00 44.22 ? 904  TYR A OH     1 
ATOM   5208 N  N      . ILE A 1 905  ? 190.614 127.819 163.210 1.00 41.72 ? 905  ILE A N      1 
ATOM   5209 C  CA     . ILE A 1 905  ? 190.613 128.634 162.000 1.00 41.72 ? 905  ILE A CA     1 
ATOM   5210 C  C      . ILE A 1 905  ? 189.407 129.566 161.982 1.00 41.72 ? 905  ILE A C      1 
ATOM   5211 O  O      . ILE A 1 905  ? 189.517 130.734 161.588 1.00 41.72 ? 905  ILE A O      1 
ATOM   5212 C  CB     . ILE A 1 905  ? 190.659 127.731 160.755 1.00 41.72 ? 905  ILE A CB     1 
ATOM   5213 C  CG1    . ILE A 1 905  ? 191.862 126.792 160.833 1.00 41.72 ? 905  ILE A CG1    1 
ATOM   5214 C  CG2    . ILE A 1 905  ? 190.750 128.555 159.486 1.00 41.72 ? 905  ILE A CG2    1 
ATOM   5215 C  CD1    . ILE A 1 905  ? 193.199 127.503 160.905 1.00 41.72 ? 905  ILE A CD1    1 
ATOM   5216 N  N      . LYS A 1 906  ? 188.248 129.075 162.432 1.00 40.95 ? 906  LYS A N      1 
ATOM   5217 C  CA     . LYS A 1 906  ? 187.044 129.899 162.476 1.00 40.95 ? 906  LYS A CA     1 
ATOM   5218 C  C      . LYS A 1 906  ? 187.183 131.023 163.493 1.00 40.95 ? 906  LYS A C      1 
ATOM   5219 O  O      . LYS A 1 906  ? 186.687 132.133 163.267 1.00 40.95 ? 906  LYS A O      1 
ATOM   5220 C  CB     . LYS A 1 906  ? 185.828 129.016 162.783 1.00 40.95 ? 906  LYS A CB     1 
ATOM   5221 C  CG     . LYS A 1 906  ? 184.458 129.702 162.749 1.00 40.95 ? 906  LYS A CG     1 
ATOM   5222 C  CD     . LYS A 1 906  ? 183.930 130.054 164.139 1.00 40.95 ? 906  LYS A CD     1 
ATOM   5223 C  CE     . LYS A 1 906  ? 183.533 128.812 164.918 1.00 40.95 ? 906  LYS A CE     1 
ATOM   5224 N  NZ     . LYS A 1 906  ? 183.008 129.151 166.270 1.00 40.95 ? 906  LYS A NZ     1 
ATOM   5225 N  N      . ASP A 1 907  ? 187.900 130.774 164.587 1.00 39.04 ? 907  ASP A N      1 
ATOM   5226 C  CA     . ASP A 1 907  ? 188.125 131.826 165.566 1.00 39.04 ? 907  ASP A CA     1 
ATOM   5227 C  C      . ASP A 1 907  ? 189.151 132.840 165.070 1.00 39.04 ? 907  ASP A C      1 
ATOM   5228 O  O      . ASP A 1 907  ? 189.036 134.030 165.384 1.00 39.04 ? 907  ASP A O      1 
ATOM   5229 C  CB     . ASP A 1 907  ? 188.551 131.206 166.892 1.00 39.04 ? 907  ASP A CB     1 
ATOM   5230 C  CG     . ASP A 1 907  ? 187.446 130.385 167.527 1.00 39.04 ? 907  ASP A CG     1 
ATOM   5231 O  OD1    . ASP A 1 907  ? 186.262 130.705 167.297 1.00 39.04 ? 907  ASP A OD1    1 
ATOM   5232 O  OD2    . ASP A 1 907  ? 187.763 129.423 168.257 1.00 39.04 ? 907  ASP A OD2    1 
ATOM   5233 N  N      . LYS A 1 908  ? 190.135 132.396 164.278 1.00 36.14 ? 908  LYS A N      1 
ATOM   5234 C  CA     . LYS A 1 908  ? 191.042 133.332 163.619 1.00 36.14 ? 908  LYS A CA     1 
ATOM   5235 C  C      . LYS A 1 908  ? 190.301 134.214 162.627 1.00 36.14 ? 908  LYS A C      1 
ATOM   5236 O  O      . LYS A 1 908  ? 190.588 135.407 162.523 1.00 36.14 ? 908  LYS A O      1 
ATOM   5237 C  CB     . LYS A 1 908  ? 192.166 132.591 162.899 1.00 36.14 ? 908  LYS A CB     1 
ATOM   5238 C  CG     . LYS A 1 908  ? 193.210 131.964 163.785 1.00 36.14 ? 908  LYS A CG     1 
ATOM   5239 C  CD     . LYS A 1 908  ? 194.315 131.386 162.930 1.00 36.14 ? 908  LYS A CD     1 
ATOM   5240 C  CE     . LYS A 1 908  ? 195.342 130.657 163.764 1.00 36.14 ? 908  LYS A CE     1 
ATOM   5241 N  NZ     . LYS A 1 908  ? 196.068 131.591 164.658 1.00 36.14 ? 908  LYS A NZ     1 
ATOM   5242 N  N      . VAL A 1 909  ? 189.338 133.645 161.898 1.00 34.49 ? 909  VAL A N      1 
ATOM   5243 C  CA     . VAL A 1 909  ? 188.524 134.431 160.972 1.00 34.49 ? 909  VAL A CA     1 
ATOM   5244 C  C      . VAL A 1 909  ? 187.637 135.416 161.732 1.00 34.49 ? 909  VAL A C      1 
ATOM   5245 O  O      . VAL A 1 909  ? 187.453 136.565 161.307 1.00 34.49 ? 909  VAL A O      1 
ATOM   5246 C  CB     . VAL A 1 909  ? 187.714 133.480 160.070 1.00 34.49 ? 909  VAL A CB     1 
ATOM   5247 C  CG1    . VAL A 1 909  ? 186.695 134.216 159.238 1.00 34.49 ? 909  VAL A CG1    1 
ATOM   5248 C  CG2    . VAL A 1 909  ? 188.647 132.727 159.151 1.00 34.49 ? 909  VAL A CG2    1 
ATOM   5249 N  N      . SER A 1 910  ? 187.120 134.999 162.891 1.00 33.18 ? 910  SER A N      1 
ATOM   5250 C  CA     . SER A 1 910  ? 186.288 135.882 163.705 1.00 33.18 ? 910  SER A CA     1 
ATOM   5251 C  C      . SER A 1 910  ? 187.087 137.051 164.272 1.00 33.18 ? 910  SER A C      1 
ATOM   5252 O  O      . SER A 1 910  ? 186.585 138.178 164.333 1.00 33.18 ? 910  SER A O      1 
ATOM   5253 C  CB     . SER A 1 910  ? 185.636 135.088 164.834 1.00 33.18 ? 910  SER A CB     1 
ATOM   5254 O  OG     . SER A 1 910  ? 184.856 135.929 165.664 1.00 33.18 ? 910  SER A OG     1 
ATOM   5255 N  N      . VAL A 1 911  ? 188.329 136.803 164.695 1.00 32.69 ? 911  VAL A N      1 
ATOM   5256 C  CA     . VAL A 1 911  ? 189.175 137.892 165.177 1.00 32.69 ? 911  VAL A CA     1 
ATOM   5257 C  C      . VAL A 1 911  ? 189.654 138.755 164.013 1.00 32.69 ? 911  VAL A C      1 
ATOM   5258 O  O      . VAL A 1 911  ? 189.770 139.981 164.143 1.00 32.69 ? 911  VAL A O      1 
ATOM   5259 C  CB     . VAL A 1 911  ? 190.336 137.307 166.006 1.00 32.69 ? 911  VAL A CB     1 
ATOM   5260 C  CG1    . VAL A 1 911  ? 191.327 138.373 166.433 1.00 32.69 ? 911  VAL A CG1    1 
ATOM   5261 C  CG2    . VAL A 1 911  ? 189.781 136.648 167.237 1.00 32.69 ? 911  VAL A CG2    1 
ATOM   5262 N  N      . TYR A 1 912  ? 189.879 138.142 162.849 1.00 30.84 ? 912  TYR A N      1 
ATOM   5263 C  CA     . TYR A 1 912  ? 190.370 138.856 161.677 1.00 30.84 ? 912  TYR A CA     1 
ATOM   5264 C  C      . TYR A 1 912  ? 189.342 139.838 161.142 1.00 30.84 ? 912  TYR A C      1 
ATOM   5265 O  O      . TYR A 1 912  ? 189.683 140.976 160.809 1.00 30.84 ? 912  TYR A O      1 
ATOM   5266 C  CB     . TYR A 1 912  ? 190.752 137.845 160.602 1.00 30.84 ? 912  TYR A CB     1 
ATOM   5267 C  CG     . TYR A 1 912  ? 191.287 138.443 159.335 1.00 30.84 ? 912  TYR A CG     1 
ATOM   5268 C  CD1    . TYR A 1 912  ? 192.586 138.923 159.265 1.00 30.84 ? 912  TYR A CD1    1 
ATOM   5269 C  CD2    . TYR A 1 912  ? 190.492 138.527 158.202 1.00 30.84 ? 912  TYR A CD2    1 
ATOM   5270 C  CE1    . TYR A 1 912  ? 193.075 139.466 158.104 1.00 30.84 ? 912  TYR A CE1    1 
ATOM   5271 C  CE2    . TYR A 1 912  ? 190.969 139.074 157.044 1.00 30.84 ? 912  TYR A CE2    1 
ATOM   5272 C  CZ     . TYR A 1 912  ? 192.259 139.539 156.998 1.00 30.84 ? 912  TYR A CZ     1 
ATOM   5273 O  OH     . TYR A 1 912  ? 192.727 140.083 155.831 1.00 30.84 ? 912  TYR A OH     1 
ATOM   5274 N  N      . PHE A 1 913  ? 188.078 139.431 161.064 1.00 30.16 ? 913  PHE A N      1 
ATOM   5275 C  CA     . PHE A 1 913  ? 187.032 140.321 160.580 1.00 30.16 ? 913  PHE A CA     1 
ATOM   5276 C  C      . PHE A 1 913  ? 186.386 141.131 161.696 1.00 30.16 ? 913  PHE A C      1 
ATOM   5277 O  O      . PHE A 1 913  ? 185.211 141.499 161.590 1.00 30.16 ? 913  PHE A O      1 
ATOM   5278 C  CB     . PHE A 1 913  ? 185.982 139.531 159.803 1.00 30.16 ? 913  PHE A CB     1 
ATOM   5279 C  CG     . PHE A 1 913  ? 186.479 139.010 158.490 1.00 30.16 ? 913  PHE A CG     1 
ATOM   5280 C  CD1    . PHE A 1 913  ? 186.611 139.854 157.400 1.00 30.16 ? 913  PHE A CD1    1 
ATOM   5281 C  CD2    . PHE A 1 913  ? 186.819 137.681 158.346 1.00 30.16 ? 913  PHE A CD2    1 
ATOM   5282 C  CE1    . PHE A 1 913  ? 187.075 139.375 156.191 1.00 30.16 ? 913  PHE A CE1    1 
ATOM   5283 C  CE2    . PHE A 1 913  ? 187.281 137.194 157.143 1.00 30.16 ? 913  PHE A CE2    1 
ATOM   5284 C  CZ     . PHE A 1 913  ? 187.408 138.042 156.063 1.00 30.16 ? 913  PHE A CZ     1 
ATOM   5285 N  N      . SER A 1 914  ? 187.124 141.410 162.771 1.00 29.43 ? 914  SER A N      1 
ATOM   5286 C  CA     . SER A 1 914  ? 186.635 142.320 163.798 1.00 29.43 ? 914  SER A CA     1 
ATOM   5287 C  C      . SER A 1 914  ? 186.751 143.770 163.353 1.00 29.43 ? 914  SER A C      1 
ATOM   5288 O  O      . SER A 1 914  ? 185.820 144.558 163.552 1.00 29.43 ? 914  SER A O      1 
ATOM   5289 C  CB     . SER A 1 914  ? 187.400 142.106 165.100 1.00 29.43 ? 914  SER A CB     1 
ATOM   5290 O  OG     . SER A 1 914  ? 187.167 140.809 165.610 1.00 29.43 ? 914  SER A OG     1 
ATOM   5291 N  N      . ASP A 1 915  ? 187.879 144.142 162.754 1.00 27.97 ? 915  ASP A N      1 
ATOM   5292 C  CA     . ASP A 1 915  ? 188.029 145.470 162.181 1.00 27.97 ? 915  ASP A CA     1 
ATOM   5293 C  C      . ASP A 1 915  ? 187.566 145.489 160.731 1.00 27.97 ? 915  ASP A C      1 
ATOM   5294 O  O      . ASP A 1 915  ? 187.655 144.492 160.011 1.00 27.97 ? 915  ASP A O      1 
ATOM   5295 C  CB     . ASP A 1 915  ? 189.474 145.964 162.283 1.00 27.97 ? 915  ASP A CB     1 
ATOM   5296 C  CG     . ASP A 1 915  ? 190.475 145.000 161.686 1.00 27.97 ? 915  ASP A CG     1 
ATOM   5297 O  OD1    . ASP A 1 915  ? 190.099 143.855 161.365 1.00 27.97 ? 915  ASP A OD1    1 
ATOM   5298 O  OD2    . ASP A 1 915  ? 191.648 145.398 161.526 1.00 27.97 ? 915  ASP A OD2    1 
ATOM   5299 N  N      . THR A 1 916  ? 187.057 146.642 160.312 1.00 26.69 ? 916  THR A N      1 
ATOM   5300 C  CA     . THR A 1 916  ? 186.554 146.797 158.958 1.00 26.69 ? 916  THR A CA     1 
ATOM   5301 C  C      . THR A 1 916  ? 187.664 146.981 157.936 1.00 26.69 ? 916  THR A C      1 
ATOM   5302 O  O      . THR A 1 916  ? 187.401 146.867 156.732 1.00 26.69 ? 916  THR A O      1 
ATOM   5303 C  CB     . THR A 1 916  ? 185.596 147.983 158.898 1.00 26.69 ? 916  THR A CB     1 
ATOM   5304 O  OG1    . THR A 1 916  ? 186.312 149.191 159.187 1.00 26.69 ? 916  THR A OG1    1 
ATOM   5305 C  CG2    . THR A 1 916  ? 184.496 147.810 159.926 1.00 26.69 ? 916  THR A CG2    1 
ATOM   5306 N  N      . TRP A 1 917  ? 188.890 147.264 158.383 1.00 23.76 ? 917  TRP A N      1 
ATOM   5307 C  CA     . TRP A 1 917  ? 189.998 147.393 157.448 1.00 23.76 ? 917  TRP A CA     1 
ATOM   5308 C  C      . TRP A 1 917  ? 190.347 146.057 156.815 1.00 23.76 ? 917  TRP A C      1 
ATOM   5309 O  O      . TRP A 1 917  ? 190.770 146.015 155.658 1.00 23.76 ? 917  TRP A O      1 
ATOM   5310 C  CB     . TRP A 1 917  ? 191.223 147.980 158.140 1.00 23.76 ? 917  TRP A CB     1 
ATOM   5311 C  CG     . TRP A 1 917  ? 191.027 149.358 158.669 1.00 23.76 ? 917  TRP A CG     1 
ATOM   5312 C  CD1    . TRP A 1 917  ? 190.975 149.725 159.975 1.00 23.76 ? 917  TRP A CD1    1 
ATOM   5313 C  CD2    . TRP A 1 917  ? 190.791 150.548 157.908 1.00 23.76 ? 917  TRP A CD2    1 
ATOM   5314 N  NE1    . TRP A 1 917  ? 190.765 151.075 160.081 1.00 23.76 ? 917  TRP A NE1    1 
ATOM   5315 C  CE2    . TRP A 1 917  ? 190.642 151.603 158.824 1.00 23.76 ? 917  TRP A CE2    1 
ATOM   5316 C  CE3    . TRP A 1 917  ? 190.706 150.827 156.542 1.00 23.76 ? 917  TRP A CE3    1 
ATOM   5317 C  CZ2    . TRP A 1 917  ? 190.418 152.913 158.419 1.00 23.76 ? 917  TRP A CZ2    1 
ATOM   5318 C  CZ3    . TRP A 1 917  ? 190.482 152.123 156.147 1.00 23.76 ? 917  TRP A CZ3    1 
ATOM   5319 C  CH2    . TRP A 1 917  ? 190.341 153.150 157.078 1.00 23.76 ? 917  TRP A CH2    1 
ATOM   5320 N  N      . ASN A 1 918  ? 190.146 144.958 157.543 1.00 27.59 ? 918  ASN A N      1 
ATOM   5321 C  CA     . ASN A 1 918  ? 190.290 143.642 156.938 1.00 27.59 ? 918  ASN A CA     1 
ATOM   5322 C  C      . ASN A 1 918  ? 189.178 143.358 155.941 1.00 27.59 ? 918  ASN A C      1 
ATOM   5323 O  O      . ASN A 1 918  ? 189.410 142.646 154.963 1.00 27.59 ? 918  ASN A O      1 
ATOM   5324 C  CB     . ASN A 1 918  ? 190.328 142.562 158.011 1.00 27.59 ? 918  ASN A CB     1 
ATOM   5325 C  CG     . ASN A 1 918  ? 191.615 142.568 158.783 1.00 27.59 ? 918  ASN A CG     1 
ATOM   5326 O  OD1    . ASN A 1 918  ? 192.684 142.776 158.219 1.00 27.59 ? 918  ASN A OD1    1 
ATOM   5327 N  ND2    . ASN A 1 918  ? 191.528 142.333 160.080 1.00 27.59 ? 918  ASN A ND2    1 
ATOM   5328 N  N      . PHE A 1 919  ? 187.978 143.910 156.156 1.00 27.12 ? 919  PHE A N      1 
ATOM   5329 C  CA     . PHE A 1 919  ? 186.929 143.805 155.143 1.00 27.12 ? 919  PHE A CA     1 
ATOM   5330 C  C      . PHE A 1 919  ? 187.312 144.545 153.872 1.00 27.12 ? 919  PHE A C      1 
ATOM   5331 O  O      . PHE A 1 919  ? 187.097 144.037 152.766 1.00 27.12 ? 919  PHE A O      1 
ATOM   5332 C  CB     . PHE A 1 919  ? 185.600 144.347 155.667 1.00 27.12 ? 919  PHE A CB     1 
ATOM   5333 C  CG     . PHE A 1 919  ? 184.896 143.435 156.620 1.00 27.12 ? 919  PHE A CG     1 
ATOM   5334 C  CD1    . PHE A 1 919  ? 184.170 142.354 156.150 1.00 27.12 ? 919  PHE A CD1    1 
ATOM   5335 C  CD2    . PHE A 1 919  ? 184.926 143.677 157.979 1.00 27.12 ? 919  PHE A CD2    1 
ATOM   5336 C  CE1    . PHE A 1 919  ? 183.506 141.518 157.023 1.00 27.12 ? 919  PHE A CE1    1 
ATOM   5337 C  CE2    . PHE A 1 919  ? 184.261 142.851 158.855 1.00 27.12 ? 919  PHE A CE2    1 
ATOM   5338 C  CZ     . PHE A 1 919  ? 183.551 141.768 158.376 1.00 27.12 ? 919  PHE A CZ     1 
ATOM   5339 N  N      . VAL A 1 920  ? 187.891 145.741 154.013 1.00 25.49 ? 920  VAL A N      1 
ATOM   5340 C  CA     . VAL A 1 920  ? 188.338 146.499 152.846 1.00 25.49 ? 920  VAL A CA     1 
ATOM   5341 C  C      . VAL A 1 920  ? 189.481 145.775 152.139 1.00 25.49 ? 920  VAL A C      1 
ATOM   5342 O  O      . VAL A 1 920  ? 189.520 145.710 150.903 1.00 25.49 ? 920  VAL A O      1 
ATOM   5343 C  CB     . VAL A 1 920  ? 188.729 147.929 153.266 1.00 25.49 ? 920  VAL A CB     1 
ATOM   5344 C  CG1    . VAL A 1 920  ? 189.237 148.732 152.081 1.00 25.49 ? 920  VAL A CG1    1 
ATOM   5345 C  CG2    . VAL A 1 920  ? 187.546 148.629 153.907 1.00 25.49 ? 920  VAL A CG2    1 
ATOM   5346 N  N      . ASP A 1 921  ? 190.394 145.177 152.916 1.00 26.55 ? 921  ASP A N      1 
ATOM   5347 C  CA     . ASP A 1 921  ? 191.489 144.377 152.367 1.00 26.55 ? 921  ASP A CA     1 
ATOM   5348 C  C      . ASP A 1 921  ? 190.983 143.184 151.569 1.00 26.55 ? 921  ASP A C      1 
ATOM   5349 O  O      . ASP A 1 921  ? 191.379 142.991 150.418 1.00 26.55 ? 921  ASP A O      1 
ATOM   5350 C  CB     . ASP A 1 921  ? 192.397 143.895 153.496 1.00 26.55 ? 921  ASP A CB     1 
ATOM   5351 C  CG     . ASP A 1 921  ? 193.335 144.963 153.987 1.00 26.55 ? 921  ASP A CG     1 
ATOM   5352 O  OD1    . ASP A 1 921  ? 193.831 145.740 153.151 1.00 26.55 ? 921  ASP A OD1    1 
ATOM   5353 O  OD2    . ASP A 1 921  ? 193.566 145.035 155.210 1.00 26.55 ? 921  ASP A OD2    1 
ATOM   5354 N  N      . ILE A 1 922  ? 190.107 142.372 152.167 1.00 27.05 ? 922  ILE A N      1 
ATOM   5355 C  CA     . ILE A 1 922  ? 189.621 141.164 151.505 1.00 27.05 ? 922  ILE A CA     1 
ATOM   5356 C  C      . ILE A 1 922  ? 188.740 141.506 150.310 1.00 27.05 ? 922  ILE A C      1 
ATOM   5357 O  O      . ILE A 1 922  ? 188.822 140.840 149.271 1.00 27.05 ? 922  ILE A O      1 
ATOM   5358 C  CB     . ILE A 1 922  ? 188.913 140.255 152.533 1.00 27.05 ? 922  ILE A CB     1 
ATOM   5359 C  CG1    . ILE A 1 922  ? 189.927 139.761 153.562 1.00 27.05 ? 922  ILE A CG1    1 
ATOM   5360 C  CG2    . ILE A 1 922  ? 188.238 139.059 151.884 1.00 27.05 ? 922  ILE A CG2    1 
ATOM   5361 C  CD1    . ILE A 1 922  ? 191.087 138.995 152.958 1.00 27.05 ? 922  ILE A CD1    1 
ATOM   5362 N  N      . PHE A 1 923  ? 187.959 142.589 150.392 1.00 25.56 ? 923  PHE A N      1 
ATOM   5363 C  CA     . PHE A 1 923  ? 187.151 143.004 149.251 1.00 25.56 ? 923  PHE A CA     1 
ATOM   5364 C  C      . PHE A 1 923  ? 188.021 143.481 148.095 1.00 25.56 ? 923  PHE A C      1 
ATOM   5365 O  O      . PHE A 1 923  ? 187.803 143.079 146.949 1.00 25.56 ? 923  PHE A O      1 
ATOM   5366 C  CB     . PHE A 1 923  ? 186.164 144.097 149.657 1.00 25.56 ? 923  PHE A CB     1 
ATOM   5367 C  CG     . PHE A 1 923  ? 185.279 144.551 148.531 1.00 25.56 ? 923  PHE A CG     1 
ATOM   5368 C  CD1    . PHE A 1 923  ? 184.223 143.763 148.102 1.00 25.56 ? 923  PHE A CD1    1 
ATOM   5369 C  CD2    . PHE A 1 923  ? 185.513 145.756 147.888 1.00 25.56 ? 923  PHE A CD2    1 
ATOM   5370 C  CE1    . PHE A 1 923  ? 183.414 144.174 147.060 1.00 25.56 ? 923  PHE A CE1    1 
ATOM   5371 C  CE2    . PHE A 1 923  ? 184.711 146.169 146.844 1.00 25.56 ? 923  PHE A CE2    1 
ATOM   5372 C  CZ     . PHE A 1 923  ? 183.661 145.379 146.431 1.00 25.56 ? 923  PHE A CZ     1 
ATOM   5373 N  N      . SER A 1 924  ? 189.020 144.323 148.375 1.00 24.52 ? 924  SER A N      1 
ATOM   5374 C  CA     . SER A 1 924  ? 189.863 144.840 147.302 1.00 24.52 ? 924  SER A CA     1 
ATOM   5375 C  C      . SER A 1 924  ? 190.734 143.747 146.697 1.00 24.52 ? 924  SER A C      1 
ATOM   5376 O  O      . SER A 1 924  ? 190.932 143.714 145.478 1.00 24.52 ? 924  SER A O      1 
ATOM   5377 C  CB     . SER A 1 924  ? 190.717 145.994 147.817 1.00 24.52 ? 924  SER A CB     1 
ATOM   5378 O  OG     . SER A 1 924  ? 191.642 145.551 148.789 1.00 24.52 ? 924  SER A OG     1 
ATOM   5379 N  N      . LEU A 1 925  ? 191.215 142.813 147.522 1.00 26.33 ? 925  LEU A N      1 
ATOM   5380 C  CA     . LEU A 1 925  ? 191.995 141.694 147.006 1.00 26.33 ? 925  LEU A CA     1 
ATOM   5381 C  C      . LEU A 1 925  ? 191.143 140.746 146.175 1.00 26.33 ? 925  LEU A C      1 
ATOM   5382 O  O      . LEU A 1 925  ? 191.585 140.288 145.119 1.00 26.33 ? 925  LEU A O      1 
ATOM   5383 C  CB     . LEU A 1 925  ? 192.661 140.943 148.155 1.00 26.33 ? 925  LEU A CB     1 
ATOM   5384 C  CG     . LEU A 1 925  ? 193.849 141.638 148.806 1.00 26.33 ? 925  LEU A CG     1 
ATOM   5385 C  CD1    . LEU A 1 925  ? 194.261 140.923 150.070 1.00 26.33 ? 925  LEU A CD1    1 
ATOM   5386 C  CD2    . LEU A 1 925  ? 194.984 141.666 147.836 1.00 26.33 ? 925  LEU A CD2    1 
ATOM   5387 N  N      . THR A 1 926  ? 189.914 140.457 146.616 1.00 25.67 ? 926  THR A N      1 
ATOM   5388 C  CA     . THR A 1 926  ? 189.039 139.566 145.861 1.00 25.67 ? 926  THR A CA     1 
ATOM   5389 C  C      . THR A 1 926  ? 188.621 140.193 144.538 1.00 25.67 ? 926  THR A C      1 
ATOM   5390 O  O      . THR A 1 926  ? 188.619 139.522 143.501 1.00 25.67 ? 926  THR A O      1 
ATOM   5391 C  CB     . THR A 1 926  ? 187.813 139.218 146.703 1.00 25.67 ? 926  THR A CB     1 
ATOM   5392 O  OG1    . THR A 1 926  ? 188.241 138.673 147.956 1.00 25.67 ? 926  THR A OG1    1 
ATOM   5393 C  CG2    . THR A 1 926  ? 186.950 138.192 145.999 1.00 25.67 ? 926  THR A CG2    1 
ATOM   5394 N  N      . VAL A 1 927  ? 188.311 141.490 144.550 1.00 24.70 ? 927  VAL A N      1 
ATOM   5395 C  CA     . VAL A 1 927  ? 187.950 142.205 143.332 1.00 24.70 ? 927  VAL A CA     1 
ATOM   5396 C  C      . VAL A 1 927  ? 189.143 142.317 142.381 1.00 24.70 ? 927  VAL A C      1 
ATOM   5397 O  O      . VAL A 1 927  ? 188.981 142.203 141.158 1.00 24.70 ? 927  VAL A O      1 
ATOM   5398 C  CB     . VAL A 1 927  ? 187.339 143.562 143.740 1.00 24.70 ? 927  VAL A CB     1 
ATOM   5399 C  CG1    . VAL A 1 927  ? 187.211 144.497 142.595 1.00 24.70 ? 927  VAL A CG1    1 
ATOM   5400 C  CG2    . VAL A 1 927  ? 185.952 143.339 144.315 1.00 24.70 ? 927  VAL A CG2    1 
ATOM   5401 N  N      . PHE A 1 928  ? 190.361 142.445 142.917 1.00 24.78 ? 928  PHE A N      1 
ATOM   5402 C  CA     . PHE A 1 928  ? 191.548 142.442 142.067 1.00 24.78 ? 928  PHE A CA     1 
ATOM   5403 C  C      . PHE A 1 928  ? 191.783 141.069 141.447 1.00 24.78 ? 928  PHE A C      1 
ATOM   5404 O  O      . PHE A 1 928  ? 192.181 140.976 140.282 1.00 24.78 ? 928  PHE A O      1 
ATOM   5405 C  CB     . PHE A 1 928  ? 192.774 142.867 142.876 1.00 24.78 ? 928  PHE A CB     1 
ATOM   5406 C  CG     . PHE A 1 928  ? 194.008 143.117 142.046 1.00 24.78 ? 928  PHE A CG     1 
ATOM   5407 C  CD1    . PHE A 1 928  ? 194.247 144.361 141.491 1.00 24.78 ? 928  PHE A CD1    1 
ATOM   5408 C  CD2    . PHE A 1 928  ? 194.910 142.097 141.784 1.00 24.78 ? 928  PHE A CD2    1 
ATOM   5409 C  CE1    . PHE A 1 928  ? 195.381 144.590 140.736 1.00 24.78 ? 928  PHE A CE1    1 
ATOM   5410 C  CE2    . PHE A 1 928  ? 196.041 142.324 141.044 1.00 24.78 ? 928  PHE A CE2    1 
ATOM   5411 C  CZ     . PHE A 1 928  ? 196.269 143.567 140.503 1.00 24.78 ? 928  PHE A CZ     1 
ATOM   5412 N  N      . ILE A 1 929  ? 191.579 139.997 142.220 1.00 25.98 ? 929  ILE A N      1 
ATOM   5413 C  CA     . ILE A 1 929  ? 191.767 138.649 141.689 1.00 25.98 ? 929  ILE A CA     1 
ATOM   5414 C  C      . ILE A 1 929  ? 190.729 138.345 140.615 1.00 25.98 ? 929  ILE A C      1 
ATOM   5415 O  O      . ILE A 1 929  ? 191.048 137.735 139.592 1.00 25.98 ? 929  ILE A O      1 
ATOM   5416 C  CB     . ILE A 1 929  ? 191.755 137.614 142.834 1.00 25.98 ? 929  ILE A CB     1 
ATOM   5417 C  CG1    . ILE A 1 929  ? 192.989 137.790 143.719 1.00 25.98 ? 929  ILE A CG1    1 
ATOM   5418 C  CG2    . ILE A 1 929  ? 191.712 136.182 142.323 1.00 25.98 ? 929  ILE A CG2    1 
ATOM   5419 C  CD1    . ILE A 1 929  ? 194.295 137.626 142.990 1.00 25.98 ? 929  ILE A CD1    1 
ATOM   5420 N  N      . ILE A 1 930  ? 189.494 138.826 140.797 1.00 26.12 ? 930  ILE A N      1 
ATOM   5421 C  CA     . ILE A 1 930  ? 188.471 138.689 139.759 1.00 26.12 ? 930  ILE A CA     1 
ATOM   5422 C  C      . ILE A 1 930  ? 188.868 139.459 138.503 1.00 26.12 ? 930  ILE A C      1 
ATOM   5423 O  O      . ILE A 1 930  ? 188.743 138.947 137.383 1.00 26.12 ? 930  ILE A O      1 
ATOM   5424 C  CB     . ILE A 1 930  ? 187.099 139.137 140.303 1.00 26.12 ? 930  ILE A CB     1 
ATOM   5425 C  CG1    . ILE A 1 930  ? 186.604 138.161 141.367 1.00 26.12 ? 930  ILE A CG1    1 
ATOM   5426 C  CG2    . ILE A 1 930  ? 186.065 139.237 139.199 1.00 26.12 ? 930  ILE A CG2    1 
ATOM   5427 C  CD1    . ILE A 1 930  ? 185.442 138.688 142.168 1.00 26.12 ? 930  ILE A CD1    1 
ATOM   5428 N  N      . ALA A 1 931  ? 189.415 140.669 138.676 1.00 25.93 ? 931  ALA A N      1 
ATOM   5429 C  CA     . ALA A 1 931  ? 189.844 141.482 137.540 1.00 25.93 ? 931  ALA A CA     1 
ATOM   5430 C  C      . ALA A 1 931  ? 190.988 140.836 136.772 1.00 25.93 ? 931  ALA A C      1 
ATOM   5431 O  O      . ALA A 1 931  ? 191.008 140.857 135.539 1.00 25.93 ? 931  ALA A O      1 
ATOM   5432 C  CB     . ALA A 1 931  ? 190.264 142.868 138.019 1.00 25.93 ? 931  ALA A CB     1 
ATOM   5433 N  N      . ILE A 1 932  ? 191.935 140.227 137.477 1.00 27.37 ? 932  ILE A N      1 
ATOM   5434 C  CA     . ILE A 1 932  ? 193.089 139.647 136.800 1.00 27.37 ? 932  ILE A CA     1 
ATOM   5435 C  C      . ILE A 1 932  ? 192.802 138.225 136.309 1.00 27.37 ? 932  ILE A C      1 
ATOM   5436 O  O      . ILE A 1 932  ? 193.494 137.731 135.411 1.00 27.37 ? 932  ILE A O      1 
ATOM   5437 C  CB     . ILE A 1 932  ? 194.311 139.793 137.732 1.00 27.37 ? 932  ILE A CB     1 
ATOM   5438 C  CG1    . ILE A 1 932  ? 194.495 141.275 138.059 1.00 27.37 ? 932  ILE A CG1    1 
ATOM   5439 C  CG2    . ILE A 1 932  ? 195.618 139.308 137.122 1.00 27.37 ? 932  ILE A CG2    1 
ATOM   5440 C  CD1    . ILE A 1 932  ? 194.595 142.194 136.857 1.00 27.37 ? 932  ILE A CD1    1 
ATOM   5441 N  N      . ILE A 1 933  ? 191.754 137.575 136.811 1.00 28.63 ? 933  ILE A N      1 
ATOM   5442 C  CA     . ILE A 1 933  ? 191.244 136.394 136.122 1.00 28.63 ? 933  ILE A CA     1 
ATOM   5443 C  C      . ILE A 1 933  ? 190.587 136.795 134.806 1.00 28.63 ? 933  ILE A C      1 
ATOM   5444 O  O      . ILE A 1 933  ? 190.876 136.217 133.753 1.00 28.63 ? 933  ILE A O      1 
ATOM   5445 C  CB     . ILE A 1 933  ? 190.289 135.601 137.032 1.00 28.63 ? 933  ILE A CB     1 
ATOM   5446 C  CG1    . ILE A 1 933  ? 191.081 134.871 138.116 1.00 28.63 ? 933  ILE A CG1    1 
ATOM   5447 C  CG2    . ILE A 1 933  ? 189.463 134.606 136.235 1.00 28.63 ? 933  ILE A CG2    1 
ATOM   5448 C  CD1    . ILE A 1 933  ? 190.228 134.336 139.229 1.00 28.63 ? 933  ILE A CD1    1 
ATOM   5449 N  N      . LEU A 1 934  ? 189.738 137.831 134.832 1.00 29.19 ? 934  LEU A N      1 
ATOM   5450 C  CA     . LEU A 1 934  ? 189.067 138.275 133.611 1.00 29.19 ? 934  LEU A CA     1 
ATOM   5451 C  C      . LEU A 1 934  ? 189.999 138.994 132.640 1.00 29.19 ? 934  LEU A C      1 
ATOM   5452 O  O      . LEU A 1 934  ? 189.587 139.265 131.508 1.00 29.19 ? 934  LEU A O      1 
ATOM   5453 C  CB     . LEU A 1 934  ? 187.902 139.197 133.950 1.00 29.19 ? 934  LEU A CB     1 
ATOM   5454 C  CG     . LEU A 1 934  ? 186.754 138.656 134.797 1.00 29.19 ? 934  LEU A CG     1 
ATOM   5455 C  CD1    . LEU A 1 934  ? 185.749 139.761 135.051 1.00 29.19 ? 934  LEU A CD1    1 
ATOM   5456 C  CD2    . LEU A 1 934  ? 186.098 137.444 134.169 1.00 29.19 ? 934  LEU A CD2    1 
ATOM   5457 N  N      . ARG A 1 935  ? 191.207 139.341 133.090 1.00 31.61 ? 935  ARG A N      1 
ATOM   5458 C  CA     . ARG A 1 935  ? 192.262 139.922 132.261 1.00 31.61 ? 935  ARG A CA     1 
ATOM   5459 C  C      . ARG A 1 935  ? 192.539 139.123 130.992 1.00 31.61 ? 935  ARG A C      1 
ATOM   5460 O  O      . ARG A 1 935  ? 192.729 139.700 129.916 1.00 31.61 ? 935  ARG A O      1 
ATOM   5461 C  CB     . ARG A 1 935  ? 193.532 140.000 133.107 1.00 31.61 ? 935  ARG A CB     1 
ATOM   5462 C  CG     . ARG A 1 935  ? 194.782 140.428 132.422 1.00 31.61 ? 935  ARG A CG     1 
ATOM   5463 C  CD     . ARG A 1 935  ? 194.726 141.881 132.189 1.00 31.61 ? 935  ARG A CD     1 
ATOM   5464 N  NE     . ARG A 1 935  ? 195.925 142.393 131.556 1.00 31.61 ? 935  ARG A NE     1 
ATOM   5465 C  CZ     . ARG A 1 935  ? 196.070 142.496 130.247 1.00 31.61 ? 935  ARG A CZ     1 
ATOM   5466 N  NH1    . ARG A 1 935  ? 195.081 142.137 129.446 1.00 31.61 ? 935  ARG A NH1    1 
ATOM   5467 N  NH2    . ARG A 1 935  ? 197.189 142.982 129.738 1.00 31.61 ? 935  ARG A NH2    1 
ATOM   5468 N  N      . PHE A 1 936  ? 192.553 137.795 131.094 1.00 34.72 ? 936  PHE A N      1 
ATOM   5469 C  CA     . PHE A 1 936  ? 193.178 136.941 130.095 1.00 34.72 ? 936  PHE A CA     1 
ATOM   5470 C  C      . PHE A 1 936  ? 192.209 136.330 129.096 1.00 34.72 ? 936  PHE A C      1 
ATOM   5471 O  O      . PHE A 1 936  ? 192.657 135.650 128.170 1.00 34.72 ? 936  PHE A O      1 
ATOM   5472 C  CB     . PHE A 1 936  ? 193.944 135.816 130.787 1.00 34.72 ? 936  PHE A CB     1 
ATOM   5473 C  CG     . PHE A 1 936  ? 195.104 136.287 131.601 1.00 34.72 ? 936  PHE A CG     1 
ATOM   5474 C  CD1    . PHE A 1 936  ? 196.306 136.594 130.998 1.00 34.72 ? 936  PHE A CD1    1 
ATOM   5475 C  CD2    . PHE A 1 936  ? 194.995 136.420 132.969 1.00 34.72 ? 936  PHE A CD2    1 
ATOM   5476 C  CE1    . PHE A 1 936  ? 197.376 137.025 131.743 1.00 34.72 ? 936  PHE A CE1    1 
ATOM   5477 C  CE2    . PHE A 1 936  ? 196.065 136.856 133.723 1.00 34.72 ? 936  PHE A CE2    1 
ATOM   5478 C  CZ     . PHE A 1 936  ? 197.256 137.158 133.107 1.00 34.72 ? 936  PHE A CZ     1 
ATOM   5479 N  N      . PHE A 1 937  ? 190.905 136.549 129.240 1.00 35.14 ? 937  PHE A N      1 
ATOM   5480 C  CA     . PHE A 1 937  ? 189.942 135.801 128.438 1.00 35.14 ? 937  PHE A CA     1 
ATOM   5481 C  C      . PHE A 1 937  ? 189.778 136.314 127.013 1.00 35.14 ? 937  PHE A C      1 
ATOM   5482 O  O      . PHE A 1 937  ? 188.945 135.757 126.288 1.00 35.14 ? 937  PHE A O      1 
ATOM   5483 C  CB     . PHE A 1 937  ? 188.574 135.785 129.117 1.00 35.14 ? 937  PHE A CB     1 
ATOM   5484 C  CG     . PHE A 1 937  ? 188.486 134.854 130.285 1.00 35.14 ? 937  PHE A CG     1 
ATOM   5485 C  CD1    . PHE A 1 937  ? 188.325 133.495 130.084 1.00 35.14 ? 937  PHE A CD1    1 
ATOM   5486 C  CD2    . PHE A 1 937  ? 188.539 135.333 131.577 1.00 35.14 ? 937  PHE A CD2    1 
ATOM   5487 C  CE1    . PHE A 1 937  ? 188.235 132.629 131.155 1.00 35.14 ? 937  PHE A CE1    1 
ATOM   5488 C  CE2    . PHE A 1 937  ? 188.443 134.472 132.654 1.00 35.14 ? 937  PHE A CE2    1 
ATOM   5489 C  CZ     . PHE A 1 937  ? 188.295 133.119 132.440 1.00 35.14 ? 937  PHE A CZ     1 
ATOM   5490 N  N      . THR A 1 938  ? 190.513 137.369 126.621 1.00 36.88 ? 938  THR A N      1 
ATOM   5491 C  CA     . THR A 1 938  ? 190.606 137.984 125.272 1.00 36.88 ? 938  THR A CA     1 
ATOM   5492 C  C      . THR A 1 938  ? 189.247 138.218 124.584 1.00 36.88 ? 938  THR A C      1 
ATOM   5493 O  O      . THR A 1 938  ? 189.173 138.350 123.358 1.00 36.88 ? 938  THR A O      1 
ATOM   5494 C  CB     . THR A 1 938  ? 191.579 137.226 124.335 1.00 36.88 ? 938  THR A CB     1 
ATOM   5495 O  OG1    . THR A 1 938  ? 191.803 138.010 123.158 1.00 36.88 ? 938  THR A OG1    1 
ATOM   5496 C  CG2    . THR A 1 938  ? 191.107 135.823 123.894 1.00 36.88 ? 938  THR A CG2    1 
ATOM   5497 N  N      . ASN A 1 939  ? 188.171 138.338 125.351 1.00 34.56 ? 939  ASN A N      1 
ATOM   5498 C  CA     . ASN A 1 939  ? 186.879 138.759 124.841 1.00 34.56 ? 939  ASN A CA     1 
ATOM   5499 C  C      . ASN A 1 939  ? 186.758 140.260 125.057 1.00 34.56 ? 939  ASN A C      1 
ATOM   5500 O  O      . ASN A 1 939  ? 187.420 140.826 125.928 1.00 34.56 ? 939  ASN A O      1 
ATOM   5501 C  CB     . ASN A 1 939  ? 185.743 138.018 125.549 1.00 34.56 ? 939  ASN A CB     1 
ATOM   5502 C  CG     . ASN A 1 939  ? 184.406 138.168 124.845 1.00 34.56 ? 939  ASN A CG     1 
ATOM   5503 O  OD1    . ASN A 1 939  ? 184.311 138.794 123.790 1.00 34.56 ? 939  ASN A OD1    1 
ATOM   5504 N  ND2    . ASN A 1 939  ? 183.362 137.606 125.436 1.00 34.56 ? 939  ASN A ND2    1 
ATOM   5505 N  N      . SER A 1 940  ? 185.927 140.906 124.239 1.00 33.09 ? 940  SER A N      1 
ATOM   5506 C  CA     . SER A 1 940  ? 185.758 142.350 124.350 1.00 33.09 ? 940  SER A CA     1 
ATOM   5507 C  C      . SER A 1 940  ? 185.032 142.721 125.637 1.00 33.09 ? 940  SER A C      1 
ATOM   5508 O  O      . SER A 1 940  ? 185.491 143.586 126.392 1.00 33.09 ? 940  SER A O      1 
ATOM   5509 C  CB     . SER A 1 940  ? 185.004 142.885 123.133 1.00 33.09 ? 940  SER A CB     1 
ATOM   5510 O  OG     . SER A 1 940  ? 183.666 142.414 123.112 1.00 33.09 ? 940  SER A OG     1 
ATOM   5511 N  N      . ARG A 1 941  ? 183.906 142.061 125.914 1.00 31.48 ? 941  ARG A N      1 
ATOM   5512 C  CA     . ARG A 1 941  ? 183.113 142.404 127.089 1.00 31.48 ? 941  ARG A CA     1 
ATOM   5513 C  C      . ARG A 1 941  ? 183.772 141.935 128.378 1.00 31.48 ? 941  ARG A C      1 
ATOM   5514 O  O      . ARG A 1 941  ? 183.671 142.616 129.404 1.00 31.48 ? 941  ARG A O      1 
ATOM   5515 C  CB     . ARG A 1 941  ? 181.710 141.813 126.968 1.00 31.48 ? 941  ARG A CB     1 
ATOM   5516 C  CG     . ARG A 1 941  ? 180.922 142.339 125.787 1.00 31.48 ? 941  ARG A CG     1 
ATOM   5517 C  CD     . ARG A 1 941  ? 180.674 143.830 125.926 1.00 31.48 ? 941  ARG A CD     1 
ATOM   5518 N  NE     . ARG A 1 941  ? 179.870 144.145 127.103 1.00 31.48 ? 941  ARG A NE     1 
ATOM   5519 C  CZ     . ARG A 1 941  ? 179.785 145.355 127.644 1.00 31.48 ? 941  ARG A CZ     1 
ATOM   5520 N  NH1    . ARG A 1 941  ? 180.457 146.368 127.114 1.00 31.48 ? 941  ARG A NH1    1 
ATOM   5521 N  NH2    . ARG A 1 941  ? 179.032 145.552 128.716 1.00 31.48 ? 941  ARG A NH2    1 
ATOM   5522 N  N      . ILE A 1 942  ? 184.465 140.795 128.341 1.00 30.31 ? 942  ILE A N      1 
ATOM   5523 C  CA     . ILE A 1 942  ? 185.114 140.283 129.544 1.00 30.31 ? 942  ILE A CA     1 
ATOM   5524 C  C      . ILE A 1 942  ? 186.303 141.157 129.925 1.00 30.31 ? 942  ILE A C      1 
ATOM   5525 O  O      . ILE A 1 942  ? 186.481 141.500 131.099 1.00 30.31 ? 942  ILE A O      1 
ATOM   5526 C  CB     . ILE A 1 942  ? 185.516 138.810 129.350 1.00 30.31 ? 942  ILE A CB     1 
ATOM   5527 C  CG1    . ILE A 1 942  ? 184.272 137.947 129.167 1.00 30.31 ? 942  ILE A CG1    1 
ATOM   5528 C  CG2    . ILE A 1 942  ? 186.287 138.301 130.539 1.00 30.31 ? 942  ILE A CG2    1 
ATOM   5529 C  CD1    . ILE A 1 942  ? 184.573 136.527 128.758 1.00 30.31 ? 942  ILE A CD1    1 
ATOM   5530 N  N      . PHE A 1 943  ? 187.109 141.572 128.943 1.00 28.44 ? 943  PHE A N      1 
ATOM   5531 C  CA     . PHE A 1 943  ? 188.197 142.498 129.240 1.00 28.44 ? 943  PHE A CA     1 
ATOM   5532 C  C      . PHE A 1 943  ? 187.684 143.887 129.600 1.00 28.44 ? 943  PHE A C      1 
ATOM   5533 O  O      . PHE A 1 943  ? 188.322 144.587 130.397 1.00 28.44 ? 943  PHE A O      1 
ATOM   5534 C  CB     . PHE A 1 943  ? 189.168 142.599 128.067 1.00 28.44 ? 943  PHE A CB     1 
ATOM   5535 C  CG     . PHE A 1 943  ? 190.272 143.589 128.294 1.00 28.44 ? 943  PHE A CG     1 
ATOM   5536 C  CD1    . PHE A 1 943  ? 191.309 143.298 129.163 1.00 28.44 ? 943  PHE A CD1    1 
ATOM   5537 C  CD2    . PHE A 1 943  ? 190.251 144.828 127.673 1.00 28.44 ? 943  PHE A CD2    1 
ATOM   5538 C  CE1    . PHE A 1 943  ? 192.310 144.213 129.388 1.00 28.44 ? 943  PHE A CE1    1 
ATOM   5539 C  CE2    . PHE A 1 943  ? 191.249 145.742 127.899 1.00 28.44 ? 943  PHE A CE2    1 
ATOM   5540 C  CZ     . PHE A 1 943  ? 192.275 145.434 128.754 1.00 28.44 ? 943  PHE A CZ     1 
ATOM   5541 N  N      . THR A 1 944  ? 186.565 144.312 129.009 1.00 26.87 ? 944  THR A N      1 
ATOM   5542 C  CA     . THR A 1 944  ? 185.958 145.580 129.397 1.00 26.87 ? 944  THR A CA     1 
ATOM   5543 C  C      . THR A 1 944  ? 185.535 145.555 130.858 1.00 26.87 ? 944  THR A C      1 
ATOM   5544 O  O      . THR A 1 944  ? 185.810 146.500 131.609 1.00 26.87 ? 944  THR A O      1 
ATOM   5545 C  CB     . THR A 1 944  ? 184.767 145.880 128.488 1.00 26.87 ? 944  THR A CB     1 
ATOM   5546 O  OG1    . THR A 1 944  ? 185.218 145.982 127.134 1.00 26.87 ? 944  THR A OG1    1 
ATOM   5547 C  CG2    . THR A 1 944  ? 184.096 147.179 128.881 1.00 26.87 ? 944  THR A CG2    1 
ATOM   5548 N  N      . ALA A 1 945  ? 184.928 144.449 131.292 1.00 24.64 ? 945  ALA A N      1 
ATOM   5549 C  CA     . ALA A 1 945  ? 184.593 144.278 132.700 1.00 24.64 ? 945  ALA A CA     1 
ATOM   5550 C  C      . ALA A 1 945  ? 185.843 144.199 133.566 1.00 24.64 ? 945  ALA A C      1 
ATOM   5551 O  O      . ALA A 1 945  ? 185.852 144.714 134.684 1.00 24.64 ? 945  ALA A O      1 
ATOM   5552 C  CB     . ALA A 1 945  ? 183.738 143.028 132.883 1.00 24.64 ? 945  ALA A CB     1 
ATOM   5553 N  N      . SER A 1 946  ? 186.908 143.579 133.050 1.00 25.34 ? 946  SER A N      1 
ATOM   5554 C  CA     . SER A 1 946  ? 188.163 143.459 133.792 1.00 25.34 ? 946  SER A CA     1 
ATOM   5555 C  C      . SER A 1 946  ? 188.787 144.824 134.062 1.00 25.34 ? 946  SER A C      1 
ATOM   5556 O  O      . SER A 1 946  ? 189.164 145.136 135.199 1.00 25.34 ? 946  SER A O      1 
ATOM   5557 C  CB     . SER A 1 946  ? 189.132 142.571 133.013 1.00 25.34 ? 946  SER A CB     1 
ATOM   5558 O  OG     . SER A 1 946  ? 190.365 142.446 133.690 1.00 25.34 ? 946  SER A OG     1 
ATOM   5559 N  N      . ARG A 1 947  ? 188.864 145.670 133.034 1.00 23.86 ? 947  ARG A N      1 
ATOM   5560 C  CA     . ARG A 1 947  ? 189.450 146.990 133.226 1.00 23.86 ? 947  ARG A CA     1 
ATOM   5561 C  C      . ARG A 1 947  ? 188.535 147.917 134.019 1.00 23.86 ? 947  ARG A C      1 
ATOM   5562 O  O      . ARG A 1 947  ? 189.035 148.765 134.762 1.00 23.86 ? 947  ARG A O      1 
ATOM   5563 C  CB     . ARG A 1 947  ? 189.828 147.619 131.885 1.00 23.86 ? 947  ARG A CB     1 
ATOM   5564 C  CG     . ARG A 1 947  ? 188.695 147.863 130.953 1.00 23.86 ? 947  ARG A CG     1 
ATOM   5565 C  CD     . ARG A 1 947  ? 189.125 148.645 129.742 1.00 23.86 ? 947  ARG A CD     1 
ATOM   5566 N  NE     . ARG A 1 947  ? 187.996 148.847 128.850 1.00 23.86 ? 947  ARG A NE     1 
ATOM   5567 C  CZ     . ARG A 1 947  ? 187.109 149.826 128.986 1.00 23.86 ? 947  ARG A CZ     1 
ATOM   5568 N  NH1    . ARG A 1 947  ? 187.217 150.698 129.978 1.00 23.86 ? 947  ARG A NH1    1 
ATOM   5569 N  NH2    . ARG A 1 947  ? 186.108 149.933 128.125 1.00 23.86 ? 947  ARG A NH2    1 
ATOM   5570 N  N      . ILE A 1 948  ? 187.212 147.751 133.931 1.00 22.70 ? 948  ILE A N      1 
ATOM   5571 C  CA     . ILE A 1 948  ? 186.324 148.589 134.737 1.00 22.70 ? 948  ILE A CA     1 
ATOM   5572 C  C      . ILE A 1 948  ? 186.393 148.191 136.209 1.00 22.70 ? 948  ILE A C      1 
ATOM   5573 O  O      . ILE A 1 948  ? 186.453 149.051 137.096 1.00 22.70 ? 948  ILE A O      1 
ATOM   5574 C  CB     . ILE A 1 948  ? 184.891 148.531 134.176 1.00 22.70 ? 948  ILE A CB     1 
ATOM   5575 C  CG1    . ILE A 1 948  ? 184.809 149.301 132.859 1.00 22.70 ? 948  ILE A CG1    1 
ATOM   5576 C  CG2    . ILE A 1 948  ? 183.866 149.052 135.167 1.00 22.70 ? 948  ILE A CG2    1 
ATOM   5577 C  CD1    . ILE A 1 948  ? 183.524 149.079 132.116 1.00 22.70 ? 948  ILE A CD1    1 
ATOM   5578 N  N      . ILE A 1 949  ? 186.443 146.888 136.487 1.00 22.27 ? 949  ILE A N      1 
ATOM   5579 C  CA     . ILE A 1 949  ? 186.589 146.388 137.852 1.00 22.27 ? 949  ILE A CA     1 
ATOM   5580 C  C      . ILE A 1 949  ? 187.938 146.797 138.447 1.00 22.27 ? 949  ILE A C      1 
ATOM   5581 O  O      . ILE A 1 949  ? 188.022 147.184 139.620 1.00 22.27 ? 949  ILE A O      1 
ATOM   5582 C  CB     . ILE A 1 949  ? 186.359 144.862 137.845 1.00 22.27 ? 949  ILE A CB     1 
ATOM   5583 C  CG1    . ILE A 1 949  ? 184.865 144.548 137.742 1.00 22.27 ? 949  ILE A CG1    1 
ATOM   5584 C  CG2    . ILE A 1 949  ? 186.957 144.174 139.018 1.00 22.27 ? 949  ILE A CG2    1 
ATOM   5585 C  CD1    . ILE A 1 949  ? 184.577 143.113 137.380 1.00 22.27 ? 949  ILE A CD1    1 
ATOM   5586 N  N      . LEU A 1 950  ? 188.992 146.825 137.628 1.00 20.46 ? 950  LEU A N      1 
ATOM   5587 C  CA     . LEU A 1 950  ? 190.301 147.269 138.110 1.00 20.46 ? 950  LEU A CA     1 
ATOM   5588 C  C      . LEU A 1 950  ? 190.315 148.776 138.390 1.00 20.46 ? 950  LEU A C      1 
ATOM   5589 O  O      . LEU A 1 950  ? 190.798 149.237 139.444 1.00 20.46 ? 950  LEU A O      1 
ATOM   5590 C  CB     . LEU A 1 950  ? 191.359 146.917 137.071 1.00 20.46 ? 950  LEU A CB     1 
ATOM   5591 C  CG     . LEU A 1 950  ? 192.785 146.812 137.584 1.00 20.46 ? 950  LEU A CG     1 
ATOM   5592 C  CD1    . LEU A 1 950  ? 192.901 145.508 138.319 1.00 20.46 ? 950  LEU A CD1    1 
ATOM   5593 C  CD2    . LEU A 1 950  ? 193.800 146.911 136.485 1.00 20.46 ? 950  LEU A CD2    1 
ATOM   5594 N  N      . SER A 1 951  ? 189.758 149.558 137.459 1.00 20.79 ? 951  SER A N      1 
ATOM   5595 C  CA     . SER A 1 951  ? 189.728 151.009 137.565 1.00 20.79 ? 951  SER A CA     1 
ATOM   5596 C  C      . SER A 1 951  ? 188.767 151.494 138.636 1.00 20.79 ? 951  SER A C      1 
ATOM   5597 O  O      . SER A 1 951  ? 188.809 152.668 139.002 1.00 20.79 ? 951  SER A O      1 
ATOM   5598 C  CB     . SER A 1 951  ? 189.349 151.612 136.212 1.00 20.79 ? 951  SER A CB     1 
ATOM   5599 O  OG     . SER A 1 951  ? 190.289 151.252 135.219 1.00 20.79 ? 951  SER A OG     1 
ATOM   5600 N  N      . LEU A 1 952  ? 187.873 150.637 139.110 1.00 21.56 ? 952  LEU A N      1 
ATOM   5601 C  CA     . LEU A 1 952  ? 187.052 150.948 140.268 1.00 21.56 ? 952  LEU A CA     1 
ATOM   5602 C  C      . LEU A 1 952  ? 187.574 150.324 141.553 1.00 21.56 ? 952  LEU A C      1 
ATOM   5603 O  O      . LEU A 1 952  ? 187.089 150.677 142.632 1.00 21.56 ? 952  LEU A O      1 
ATOM   5604 C  CB     . LEU A 1 952  ? 185.603 150.506 140.024 1.00 21.56 ? 952  LEU A CB     1 
ATOM   5605 C  CG     . LEU A 1 952  ? 184.644 151.507 139.367 1.00 21.56 ? 952  LEU A CG     1 
ATOM   5606 C  CD1    . LEU A 1 952  ? 185.000 151.880 137.937 1.00 21.56 ? 952  LEU A CD1    1 
ATOM   5607 C  CD2    . LEU A 1 952  ? 183.242 150.936 139.410 1.00 21.56 ? 952  LEU A CD2    1 
ATOM   5608 N  N      . ASP A 1 953  ? 188.542 149.413 141.466 1.00 22.24 ? 953  ASP A N      1 
ATOM   5609 C  CA     . ASP A 1 953  ? 189.155 148.828 142.651 1.00 22.24 ? 953  ASP A CA     1 
ATOM   5610 C  C      . ASP A 1 953  ? 190.347 149.631 143.170 1.00 22.24 ? 953  ASP A C      1 
ATOM   5611 O  O      . ASP A 1 953  ? 190.735 149.468 144.346 1.00 22.24 ? 953  ASP A O      1 
ATOM   5612 C  CB     . ASP A 1 953  ? 189.542 147.383 142.329 1.00 22.24 ? 953  ASP A CB     1 
ATOM   5613 C  CG     . ASP A 1 953  ? 189.961 146.603 143.540 1.00 22.24 ? 953  ASP A CG     1 
ATOM   5614 O  OD1    . ASP A 1 953  ? 189.139 146.421 144.456 1.00 22.24 ? 953  ASP A OD1    1 
ATOM   5615 O  OD2    . ASP A 1 953  ? 191.095 146.110 143.548 1.00 22.24 ? 953  ASP A OD2    1 
ATOM   5616 N  N      . ILE A 1 954  ? 190.910 150.511 142.330 1.00 21.09 ? 954  ILE A N      1 
ATOM   5617 C  CA     . ILE A 1 954  ? 191.841 151.530 142.846 1.00 21.09 ? 954  ILE A CA     1 
ATOM   5618 C  C      . ILE A 1 954  ? 191.188 152.395 143.935 1.00 21.09 ? 954  ILE A C      1 
ATOM   5619 O  O      . ILE A 1 954  ? 191.860 152.815 144.891 1.00 21.09 ? 954  ILE A O      1 
ATOM   5620 C  CB     . ILE A 1 954  ? 192.425 152.386 141.692 1.00 21.09 ? 954  ILE A CB     1 
ATOM   5621 C  CG1    . ILE A 1 954  ? 193.479 153.381 142.191 1.00 21.09 ? 954  ILE A CG1    1 
ATOM   5622 C  CG2    . ILE A 1 954  ? 191.357 153.160 140.953 1.00 21.09 ? 954  ILE A CG2    1 
ATOM   5623 C  CD1    . ILE A 1 954  ? 194.661 152.779 142.858 1.00 21.09 ? 954  ILE A CD1    1 
ATOM   5624 N  N      . ILE A 1 955  ? 189.871 152.622 143.841 1.00 21.57 ? 955  ILE A N      1 
ATOM   5625 C  CA     . ILE A 1 955  ? 189.132 153.368 144.854 1.00 21.57 ? 955  ILE A CA     1 
ATOM   5626 C  C      . ILE A 1 955  ? 189.197 152.657 146.197 1.00 21.57 ? 955  ILE A C      1 
ATOM   5627 O  O      . ILE A 1 955  ? 189.422 153.285 147.234 1.00 21.57 ? 955  ILE A O      1 
ATOM   5628 C  CB     . ILE A 1 955  ? 187.679 153.578 144.386 1.00 21.57 ? 955  ILE A CB     1 
ATOM   5629 C  CG1    . ILE A 1 955  ? 187.647 154.472 143.144 1.00 21.57 ? 955  ILE A CG1    1 
ATOM   5630 C  CG2    . ILE A 1 955  ? 186.820 154.168 145.488 1.00 21.57 ? 955  ILE A CG2    1 
ATOM   5631 C  CD1    . ILE A 1 955  ? 186.301 154.521 142.460 1.00 21.57 ? 955  ILE A CD1    1 
ATOM   5632 N  N      . PHE A 1 956  ? 189.069 151.333 146.194 1.00 23.06 ? 956  PHE A N      1 
ATOM   5633 C  CA     . PHE A 1 956  ? 189.053 150.597 147.451 1.00 23.06 ? 956  PHE A CA     1 
ATOM   5634 C  C      . PHE A 1 956  ? 190.445 150.432 148.036 1.00 23.06 ? 956  PHE A C      1 
ATOM   5635 O  O      . PHE A 1 956  ? 190.590 150.387 149.263 1.00 23.06 ? 956  PHE A O      1 
ATOM   5636 C  CB     . PHE A 1 956  ? 188.369 149.253 147.241 1.00 23.06 ? 956  PHE A CB     1 
ATOM   5637 C  CG     . PHE A 1 956  ? 186.913 149.384 146.915 1.00 23.06 ? 956  PHE A CG     1 
ATOM   5638 C  CD1    . PHE A 1 956  ? 185.987 149.588 147.923 1.00 23.06 ? 956  PHE A CD1    1 
ATOM   5639 C  CD2    . PHE A 1 956  ? 186.473 149.338 145.603 1.00 23.06 ? 956  PHE A CD2    1 
ATOM   5640 C  CE1    . PHE A 1 956  ? 184.649 149.723 147.634 1.00 23.06 ? 956  PHE A CE1    1 
ATOM   5641 C  CE2    . PHE A 1 956  ? 185.133 149.474 145.304 1.00 23.06 ? 956  PHE A CE2    1 
ATOM   5642 C  CZ     . PHE A 1 956  ? 184.219 149.666 146.322 1.00 23.06 ? 956  PHE A CZ     1 
ATOM   5643 N  N      . PHE A 1 957  ? 191.478 150.387 147.194 1.00 21.35 ? 957  PHE A N      1 
ATOM   5644 C  CA     . PHE A 1 957  ? 192.837 150.472 147.738 1.00 21.35 ? 957  PHE A CA     1 
ATOM   5645 C  C      . PHE A 1 957  ? 193.117 151.833 148.382 1.00 21.35 ? 957  PHE A C      1 
ATOM   5646 O  O      . PHE A 1 957  ? 193.761 151.910 149.439 1.00 21.35 ? 957  PHE A O      1 
ATOM   5647 C  CB     . PHE A 1 957  ? 193.874 150.175 146.662 1.00 21.35 ? 957  PHE A CB     1 
ATOM   5648 C  CG     . PHE A 1 957  ? 194.040 148.720 146.369 1.00 21.35 ? 957  PHE A CG     1 
ATOM   5649 C  CD1    . PHE A 1 957  ? 194.675 147.890 147.278 1.00 21.35 ? 957  PHE A CD1    1 
ATOM   5650 C  CD2    . PHE A 1 957  ? 193.614 148.186 145.171 1.00 21.35 ? 957  PHE A CD2    1 
ATOM   5651 C  CE1    . PHE A 1 957  ? 194.845 146.548 147.007 1.00 21.35 ? 957  PHE A CE1    1 
ATOM   5652 C  CE2    . PHE A 1 957  ? 193.796 146.846 144.900 1.00 21.35 ? 957  PHE A CE2    1 
ATOM   5653 C  CZ     . PHE A 1 957  ? 194.404 146.028 145.819 1.00 21.35 ? 957  PHE A CZ     1 
ATOM   5654 N  N      . ILE A 1 958  ? 192.613 152.914 147.786 1.00 20.76 ? 958  ILE A N      1 
ATOM   5655 C  CA     . ILE A 1 958  ? 192.815 154.226 148.395 1.00 20.76 ? 958  ILE A CA     1 
ATOM   5656 C  C      . ILE A 1 958  ? 191.980 154.379 149.672 1.00 20.76 ? 958  ILE A C      1 
ATOM   5657 O  O      . ILE A 1 958  ? 192.426 155.013 150.637 1.00 20.76 ? 958  ILE A O      1 
ATOM   5658 C  CB     . ILE A 1 958  ? 192.546 155.315 147.336 1.00 20.76 ? 958  ILE A CB     1 
ATOM   5659 C  CG1    . ILE A 1 958  ? 193.607 155.215 146.237 1.00 20.76 ? 958  ILE A CG1    1 
ATOM   5660 C  CG2    . ILE A 1 958  ? 192.586 156.712 147.916 1.00 20.76 ? 958  ILE A CG2    1 
ATOM   5661 C  CD1    . ILE A 1 958  ? 193.322 156.044 145.014 1.00 20.76 ? 958  ILE A CD1    1 
ATOM   5662 N  N      . VAL A 1 959  ? 190.791 153.770 149.719 1.00 21.26 ? 959  VAL A N      1 
ATOM   5663 C  CA     . VAL A 1 959  ? 190.003 153.708 150.953 1.00 21.26 ? 959  VAL A CA     1 
ATOM   5664 C  C      . VAL A 1 959  ? 190.743 152.923 152.033 1.00 21.26 ? 959  VAL A C      1 
ATOM   5665 O  O      . VAL A 1 959  ? 190.699 153.286 153.215 1.00 21.26 ? 959  VAL A O      1 
ATOM   5666 C  CB     . VAL A 1 959  ? 188.600 153.124 150.656 1.00 21.26 ? 959  VAL A CB     1 
ATOM   5667 C  CG1    . VAL A 1 959  ? 187.843 152.763 151.919 1.00 21.26 ? 959  VAL A CG1    1 
ATOM   5668 C  CG2    . VAL A 1 959  ? 187.771 154.136 149.890 1.00 21.26 ? 959  VAL A CG2    1 
ATOM   5669 N  N      . ARG A 1 960  ? 191.483 151.881 151.649 1.00 21.71 ? 960  ARG A N      1 
ATOM   5670 C  CA     . ARG A 1 960  ? 192.315 151.181 152.625 1.00 21.71 ? 960  ARG A CA     1 
ATOM   5671 C  C      . ARG A 1 960  ? 193.466 152.054 153.122 1.00 21.71 ? 960  ARG A C      1 
ATOM   5672 O  O      . ARG A 1 960  ? 193.851 151.963 154.294 1.00 21.71 ? 960  ARG A O      1 
ATOM   5673 C  CB     . ARG A 1 960  ? 192.838 149.875 152.026 1.00 21.71 ? 960  ARG A CB     1 
ATOM   5674 C  CG     . ARG A 1 960  ? 193.637 149.042 153.004 1.00 21.71 ? 960  ARG A CG     1 
ATOM   5675 C  CD     . ARG A 1 960  ? 192.763 148.672 154.184 1.00 21.71 ? 960  ARG A CD     1 
ATOM   5676 N  NE     . ARG A 1 960  ? 193.507 147.981 155.229 1.00 21.71 ? 960  ARG A NE     1 
ATOM   5677 C  CZ     . ARG A 1 960  ? 194.143 148.601 156.216 1.00 21.71 ? 960  ARG A CZ     1 
ATOM   5678 N  NH1    . ARG A 1 960  ? 194.119 149.921 156.291 1.00 21.71 ? 960  ARG A NH1    1 
ATOM   5679 N  NH2    . ARG A 1 960  ? 194.796 147.903 157.131 1.00 21.71 ? 960  ARG A NH2    1 
ATOM   5680 N  N      . SER A 1 961  ? 193.977 152.953 152.279 1.00 20.00 ? 961  SER A N      1 
ATOM   5681 C  CA     . SER A 1 961  ? 195.061 153.867 152.716 1.00 20.00 ? 961  SER A CA     1 
ATOM   5682 C  C      . SER A 1 961  ? 194.639 154.934 153.792 1.00 20.00 ? 961  SER A C      1 
ATOM   5683 O  O      . SER A 1 961  ? 195.469 155.802 154.040 1.00 20.00 ? 961  SER A O      1 
ATOM   5684 C  CB     . SER A 1 961  ? 195.639 154.611 151.517 1.00 20.00 ? 961  SER A CB     1 
ATOM   5685 O  OG     . SER A 1 961  ? 194.686 155.510 150.973 1.00 20.00 ? 961  SER A OG     1 
ATOM   5686 N  N      . LEU A 1 962  ? 193.463 154.961 154.420 1.00 18.85 ? 962  LEU A N      1 
ATOM   5687 C  CA     . LEU A 1 962  ? 193.104 156.031 155.345 1.00 18.85 ? 962  LEU A CA     1 
ATOM   5688 C  C      . LEU A 1 962  ? 193.607 155.774 156.762 1.00 18.85 ? 962  LEU A C      1 
ATOM   5689 O  O      . LEU A 1 962  ? 193.707 156.712 157.572 1.00 18.85 ? 962  LEU A O      1 
ATOM   5690 C  CB     . LEU A 1 962  ? 191.587 156.193 155.339 1.00 18.85 ? 962  LEU A CB     1 
ATOM   5691 C  CG     . LEU A 1 962  ? 191.027 156.487 153.946 1.00 18.85 ? 962  LEU A CG     1 
ATOM   5692 C  CD1    . LEU A 1 962  ? 189.513 156.395 153.935 1.00 18.85 ? 962  LEU A CD1    1 
ATOM   5693 C  CD2    . LEU A 1 962  ? 191.495 157.834 153.435 1.00 18.85 ? 962  LEU A CD2    1 
ATOM   5694 N  N      . GLN A 1 963  ? 193.954 154.526 157.075 1.00 19.63 ? 963  GLN A N      1 
ATOM   5695 C  CA     . GLN A 1 963  ? 194.590 154.231 158.350 1.00 19.63 ? 963  GLN A CA     1 
ATOM   5696 C  C      . GLN A 1 963  ? 195.986 154.837 158.428 1.00 19.63 ? 963  GLN A C      1 
ATOM   5697 O  O      . GLN A 1 963  ? 196.486 155.082 159.531 1.00 19.63 ? 963  GLN A O      1 
ATOM   5698 C  CB     . GLN A 1 963  ? 194.629 152.719 158.561 1.00 19.63 ? 963  GLN A CB     1 
ATOM   5699 C  CG     . GLN A 1 963  ? 194.901 152.304 159.987 1.00 19.63 ? 963  GLN A CG     1 
ATOM   5700 C  CD     . GLN A 1 963  ? 194.848 150.820 160.181 1.00 19.63 ? 963  GLN A CD     1 
ATOM   5701 O  OE1    . GLN A 1 963  ? 194.711 150.064 159.225 1.00 19.63 ? 963  GLN A OE1    1 
ATOM   5702 N  NE2    . GLN A 1 963  ? 194.931 150.388 161.429 1.00 19.63 ? 963  GLN A NE2    1 
ATOM   5703 N  N      . ILE A 1 964  ? 196.615 155.075 157.274 1.00 17.79 ? 964  ILE A N      1 
ATOM   5704 C  CA     . ILE A 1 964  ? 197.796 155.930 157.192 1.00 17.79 ? 964  ILE A CA     1 
ATOM   5705 C  C      . ILE A 1 964  ? 197.494 157.315 157.746 1.00 17.79 ? 964  ILE A C      1 
ATOM   5706 O  O      . ILE A 1 964  ? 198.250 157.850 158.561 1.00 17.79 ? 964  ILE A O      1 
ATOM   5707 C  CB     . ILE A 1 964  ? 198.290 155.996 155.736 1.00 17.79 ? 964  ILE A CB     1 
ATOM   5708 C  CG1    . ILE A 1 964  ? 198.938 154.669 155.332 1.00 17.79 ? 964  ILE A CG1    1 
ATOM   5709 C  CG2    . ILE A 1 964  ? 199.176 157.207 155.493 1.00 17.79 ? 964  ILE A CG2    1 
ATOM   5710 C  CD1    . ILE A 1 964  ? 199.174 154.530 153.855 1.00 17.79 ? 964  ILE A CD1    1 
ATOM   5711 N  N      . PHE A 1 965  ? 196.369 157.906 157.332 1.00 17.14 ? 965  PHE A N      1 
ATOM   5712 C  CA     . PHE A 1 965  ? 196.006 159.244 157.792 1.00 17.14 ? 965  PHE A CA     1 
ATOM   5713 C  C      . PHE A 1 965  ? 195.641 159.269 159.264 1.00 17.14 ? 965  PHE A C      1 
ATOM   5714 O  O      . PHE A 1 965  ? 195.725 160.325 159.894 1.00 17.14 ? 965  PHE A O      1 
ATOM   5715 C  CB     . PHE A 1 965  ? 194.846 159.802 156.966 1.00 17.14 ? 965  PHE A CB     1 
ATOM   5716 C  CG     . PHE A 1 965  ? 195.224 160.189 155.566 1.00 17.14 ? 965  PHE A CG     1 
ATOM   5717 C  CD1    . PHE A 1 965  ? 196.554 160.354 155.207 1.00 17.14 ? 965  PHE A CD1    1 
ATOM   5718 C  CD2    . PHE A 1 965  ? 194.246 160.392 154.609 1.00 17.14 ? 965  PHE A CD2    1 
ATOM   5719 C  CE1    . PHE A 1 965  ? 196.900 160.702 153.922 1.00 17.14 ? 965  PHE A CE1    1 
ATOM   5720 C  CE2    . PHE A 1 965  ? 194.586 160.746 153.319 1.00 17.14 ? 965  PHE A CE2    1 
ATOM   5721 C  CZ     . PHE A 1 965  ? 195.916 160.901 152.976 1.00 17.14 ? 965  PHE A CZ     1 
ATOM   5722 N  N      . SER A 1 966  ? 195.254 158.126 159.824 1.00 16.53 ? 966  SER A N      1 
ATOM   5723 C  CA     . SER A 1 966  ? 194.971 158.060 161.260 1.00 16.53 ? 966  SER A CA     1 
ATOM   5724 C  C      . SER A 1 966  ? 196.209 158.213 162.163 1.00 16.53 ? 966  SER A C      1 
ATOM   5725 O  O      . SER A 1 966  ? 196.041 158.188 163.384 1.00 16.53 ? 966  SER A O      1 
ATOM   5726 C  CB     . SER A 1 966  ? 194.266 156.748 161.603 1.00 16.53 ? 966  SER A CB     1 
ATOM   5727 O  OG     . SER A 1 966  ? 195.124 155.637 161.445 1.00 16.53 ? 966  SER A OG     1 
ATOM   5728 N  N      . VAL A 1 967  ? 197.427 158.365 161.629 1.00 16.02 ? 967  VAL A N      1 
ATOM   5729 C  CA     . VAL A 1 967  ? 198.591 158.641 162.471 1.00 16.02 ? 967  VAL A CA     1 
ATOM   5730 C  C      . VAL A 1 967  ? 198.571 160.075 162.986 1.00 16.02 ? 967  VAL A C      1 
ATOM   5731 O  O      . VAL A 1 967  ? 199.185 160.377 164.014 1.00 16.02 ? 967  VAL A O      1 
ATOM   5732 C  CB     . VAL A 1 967  ? 199.905 158.348 161.703 1.00 16.02 ? 967  VAL A CB     1 
ATOM   5733 C  CG1    . VAL A 1 967  ? 200.204 159.403 160.641 1.00 16.02 ? 967  VAL A CG1    1 
ATOM   5734 C  CG2    . VAL A 1 967  ? 201.101 158.181 162.635 1.00 16.02 ? 967  VAL A CG2    1 
ATOM   5735 N  N      . ASN A 1 968  ? 197.845 160.964 162.323 1.00 15.61 ? 968  ASN A N      1 
ATOM   5736 C  CA     . ASN A 1 968  ? 197.875 162.375 162.648 1.00 15.61 ? 968  ASN A CA     1 
ATOM   5737 C  C      . ASN A 1 968  ? 196.770 162.681 163.645 1.00 15.61 ? 968  ASN A C      1 
ATOM   5738 O  O      . ASN A 1 968  ? 195.671 162.129 163.558 1.00 15.61 ? 968  ASN A O      1 
ATOM   5739 C  CB     . ASN A 1 968  ? 197.712 163.205 161.376 1.00 15.61 ? 968  ASN A CB     1 
ATOM   5740 C  CG     . ASN A 1 968  ? 198.089 164.652 161.562 1.00 15.61 ? 968  ASN A CG     1 
ATOM   5741 O  OD1    . ASN A 1 968  ? 198.482 165.076 162.644 1.00 15.61 ? 968  ASN A OD1    1 
ATOM   5742 N  ND2    . ASN A 1 968  ? 197.984 165.420 160.494 1.00 15.61 ? 968  ASN A ND2    1 
ATOM   5743 N  N      . ARG A 1 969  ? 197.078 163.553 164.604 1.00 16.45 ? 969  ARG A N      1 
ATOM   5744 C  CA     . ARG A 1 969  ? 196.096 163.952 165.601 1.00 16.45 ? 969  ARG A CA     1 
ATOM   5745 C  C      . ARG A 1 969  ? 194.961 164.752 164.975 1.00 16.45 ? 969  ARG A C      1 
ATOM   5746 O  O      . ARG A 1 969  ? 193.821 164.689 165.447 1.00 16.45 ? 969  ARG A O      1 
ATOM   5747 C  CB     . ARG A 1 969  ? 196.795 164.754 166.697 1.00 16.45 ? 969  ARG A CB     1 
ATOM   5748 C  CG     . ARG A 1 969  ? 195.928 165.158 167.858 1.00 16.45 ? 969  ARG A CG     1 
ATOM   5749 C  CD     . ARG A 1 969  ? 196.734 165.975 168.835 1.00 16.45 ? 969  ARG A CD     1 
ATOM   5750 N  NE     . ARG A 1 969  ? 197.289 167.166 168.200 1.00 16.45 ? 969  ARG A NE     1 
ATOM   5751 C  CZ     . ARG A 1 969  ? 196.629 168.304 168.021 1.00 16.45 ? 969  ARG A CZ     1 
ATOM   5752 N  NH1    . ARG A 1 969  ? 195.374 168.427 168.430 1.00 16.45 ? 969  ARG A NH1    1 
ATOM   5753 N  NH2    . ARG A 1 969  ? 197.230 169.327 167.432 1.00 16.45 ? 969  ARG A NH2    1 
ATOM   5754 N  N      . LEU A 1 970  ? 195.246 165.489 163.903 1.00 15.11 ? 970  LEU A N      1 
ATOM   5755 C  CA     . LEU A 1 970  ? 194.200 166.235 163.220 1.00 15.11 ? 970  LEU A CA     1 
ATOM   5756 C  C      . LEU A 1 970  ? 193.436 165.355 162.240 1.00 15.11 ? 970  LEU A C      1 
ATOM   5757 O  O      . LEU A 1 970  ? 192.204 165.357 162.231 1.00 15.11 ? 970  LEU A O      1 
ATOM   5758 C  CB     . LEU A 1 970  ? 194.789 167.445 162.491 1.00 15.11 ? 970  LEU A CB     1 
ATOM   5759 C  CG     . LEU A 1 970  ? 194.959 168.768 163.247 1.00 15.11 ? 970  LEU A CG     1 
ATOM   5760 C  CD1    . LEU A 1 970  ? 193.627 169.212 163.828 1.00 15.11 ? 970  LEU A CD1    1 
ATOM   5761 C  CD2    . LEU A 1 970  ? 196.036 168.721 164.312 1.00 15.11 ? 970  LEU A CD2    1 
ATOM   5762 N  N      . LEU A 1 971  ? 194.149 164.582 161.423 1.00 14.65 ? 971  LEU A N      1 
ATOM   5763 C  CA     . LEU A 1 971  ? 193.520 163.897 160.300 1.00 14.65 ? 971  LEU A CA     1 
ATOM   5764 C  C      . LEU A 1 971  ? 192.726 162.665 160.708 1.00 14.65 ? 971  LEU A C      1 
ATOM   5765 O  O      . LEU A 1 971  ? 191.721 162.358 160.067 1.00 14.65 ? 971  LEU A O      1 
ATOM   5766 C  CB     . LEU A 1 971  ? 194.575 163.510 159.268 1.00 14.65 ? 971  LEU A CB     1 
ATOM   5767 C  CG     . LEU A 1 971  ? 195.169 164.668 158.480 1.00 14.65 ? 971  LEU A CG     1 
ATOM   5768 C  CD1    . LEU A 1 971  ? 196.298 164.171 157.607 1.00 14.65 ? 971  LEU A CD1    1 
ATOM   5769 C  CD2    . LEU A 1 971  ? 194.086 165.310 157.644 1.00 14.65 ? 971  LEU A CD2    1 
ATOM   5770 N  N      . GLY A 1 972  ? 193.155 161.951 161.744 1.00 14.16 ? 972  GLY A N      1 
ATOM   5771 C  CA     . GLY A 1 972  ? 192.499 160.743 162.200 1.00 14.16 ? 972  GLY A CA     1 
ATOM   5772 C  C      . GLY A 1 972  ? 191.037 160.851 162.618 1.00 14.16 ? 972  GLY A C      1 
ATOM   5773 O  O      . GLY A 1 972  ? 190.177 160.107 162.119 1.00 14.16 ? 972  GLY A O      1 
ATOM   5774 N  N      . PRO A 1 973  ? 190.722 161.749 163.563 1.00 14.29 ? 973  PRO A N      1 
ATOM   5775 C  CA     . PRO A 1 973  ? 189.308 161.979 163.898 1.00 14.29 ? 973  PRO A CA     1 
ATOM   5776 C  C      . PRO A 1 973  ? 188.478 162.526 162.755 1.00 14.29 ? 973  PRO A C      1 
ATOM   5777 O  O      . PRO A 1 973  ? 187.263 162.326 162.762 1.00 14.29 ? 973  PRO A O      1 
ATOM   5778 C  CB     . PRO A 1 973  ? 189.382 162.980 165.054 1.00 14.29 ? 973  PRO A CB     1 
ATOM   5779 C  CG     . PRO A 1 973  ? 190.675 162.744 165.651 1.00 14.29 ? 973  PRO A CG     1 
ATOM   5780 C  CD     . PRO A 1 973  ? 191.599 162.411 164.548 1.00 14.29 ? 973  PRO A CD     1 
ATOM   5781 N  N      . LYS A 1 974  ? 189.091 163.183 161.770 1.00 14.33 ? 974  LYS A N      1 
ATOM   5782 C  CA     . LYS A 1 974  ? 188.362 163.568 160.565 1.00 14.33 ? 974  LYS A CA     1 
ATOM   5783 C  C      . LYS A 1 974  ? 187.899 162.337 159.796 1.00 14.33 ? 974  LYS A C      1 
ATOM   5784 O  O      . LYS A 1 974  ? 186.783 162.309 159.272 1.00 14.33 ? 974  LYS A O      1 
ATOM   5785 C  CB     . LYS A 1 974  ? 189.236 164.457 159.681 1.00 14.33 ? 974  LYS A CB     1 
ATOM   5786 C  CG     . LYS A 1 974  ? 189.059 165.966 159.849 1.00 14.33 ? 974  LYS A CG     1 
ATOM   5787 C  CD     . LYS A 1 974  ? 189.312 166.439 161.268 1.00 14.33 ? 974  LYS A CD     1 
ATOM   5788 C  CE     . LYS A 1 974  ? 189.244 167.938 161.384 1.00 14.33 ? 974  LYS A CE     1 
ATOM   5789 N  NZ     . LYS A 1 974  ? 190.322 168.550 160.558 1.00 14.33 ? 974  LYS A NZ     1 
ATOM   5790 N  N      . LEU A 1 975  ? 188.720 161.286 159.769 1.00 14.28 ? 975  LEU A N      1 
ATOM   5791 C  CA     . LEU A 1 975  ? 188.309 160.041 159.133 1.00 14.28 ? 975  LEU A CA     1 
ATOM   5792 C  C      . LEU A 1 975  ? 187.272 159.292 159.962 1.00 14.28 ? 975  LEU A C      1 
ATOM   5793 O  O      . LEU A 1 975  ? 186.404 158.613 159.396 1.00 14.28 ? 975  LEU A O      1 
ATOM   5794 C  CB     . LEU A 1 975  ? 189.523 159.152 158.863 1.00 14.28 ? 975  LEU A CB     1 
ATOM   5795 C  CG     . LEU A 1 975  ? 190.271 159.328 157.532 1.00 14.28 ? 975  LEU A CG     1 
ATOM   5796 C  CD1    . LEU A 1 975  ? 189.301 159.174 156.379 1.00 14.28 ? 975  LEU A CD1    1 
ATOM   5797 C  CD2    . LEU A 1 975  ? 191.038 160.623 157.400 1.00 14.28 ? 975  LEU A CD2    1 
ATOM   5798 N  N      . VAL A 1 976  ? 187.338 159.404 161.292 1.00 14.93 ? 976  VAL A N      1 
ATOM   5799 C  CA     . VAL A 1 976  ? 186.272 158.858 162.139 1.00 14.93 ? 976  VAL A CA     1 
ATOM   5800 C  C      . VAL A 1 976  ? 184.951 159.576 161.865 1.00 14.93 ? 976  VAL A C      1 
ATOM   5801 O  O      . VAL A 1 976  ? 183.879 158.950 161.812 1.00 14.93 ? 976  VAL A O      1 
ATOM   5802 C  CB     . VAL A 1 976  ? 186.678 158.951 163.623 1.00 14.93 ? 976  VAL A CB     1 
ATOM   5803 C  CG1    . VAL A 1 976  ? 185.574 158.447 164.538 1.00 14.93 ? 976  VAL A CG1    1 
ATOM   5804 C  CG2    . VAL A 1 976  ? 187.942 158.174 163.864 1.00 14.93 ? 976  VAL A CG2    1 
ATOM   5805 N  N      . MET A 1 977  ? 185.018 160.896 161.663 1.00 15.63 ? 977  MET A N      1 
ATOM   5806 C  CA     . MET A 1 977  ? 183.853 161.679 161.260 1.00 15.63 ? 977  MET A CA     1 
ATOM   5807 C  C      . MET A 1 977  ? 183.307 161.217 159.920 1.00 15.63 ? 977  MET A C      1 
ATOM   5808 O  O      . MET A 1 977  ? 182.098 161.069 159.769 1.00 15.63 ? 977  MET A O      1 
ATOM   5809 C  CB     . MET A 1 977  ? 184.214 163.159 161.186 1.00 15.63 ? 977  MET A CB     1 
ATOM   5810 C  CG     . MET A 1 977  ? 184.422 163.816 162.504 1.00 15.63 ? 977  MET A CG     1 
ATOM   5811 S  SD     . MET A 1 977  ? 185.291 165.365 162.302 1.00 15.63 ? 977  MET A SD     1 
ATOM   5812 C  CE     . MET A 1 977  ? 185.586 165.794 164.006 1.00 15.63 ? 977  MET A CE     1 
ATOM   5813 N  N      . ILE A 1 978  ? 184.188 160.995 158.938 1.00 14.33 ? 978  ILE A N      1 
ATOM   5814 C  CA     . ILE A 1 978  ? 183.773 160.521 157.613 1.00 14.33 ? 978  ILE A CA     1 
ATOM   5815 C  C      . ILE A 1 978  ? 183.077 159.167 157.712 1.00 14.33 ? 978  ILE A C      1 
ATOM   5816 O  O      . ILE A 1 978  ? 182.048 158.933 157.069 1.00 14.33 ? 978  ILE A O      1 
ATOM   5817 C  CB     . ILE A 1 978  ? 184.989 160.475 156.664 1.00 14.33 ? 978  ILE A CB     1 
ATOM   5818 C  CG1    . ILE A 1 978  ? 185.461 161.887 156.341 1.00 14.33 ? 978  ILE A CG1    1 
ATOM   5819 C  CG2    . ILE A 1 978  ? 184.679 159.730 155.375 1.00 14.33 ? 978  ILE A CG2    1 
ATOM   5820 C  CD1    . ILE A 1 978  ? 186.805 161.941 155.686 1.00 14.33 ? 978  ILE A CD1    1 
ATOM   5821 N  N      . GLN A 1 979  ? 183.581 158.291 158.581 1.00 15.79 ? 979  GLN A N      1 
ATOM   5822 C  CA     . GLN A 1 979  ? 182.996 156.965 158.764 1.00 15.79 ? 979  GLN A CA     1 
ATOM   5823 C  C      . GLN A 1 979  ? 181.607 157.040 159.404 1.00 15.79 ? 979  GLN A C      1 
ATOM   5824 O  O      . GLN A 1 979  ? 180.650 156.401 158.931 1.00 15.79 ? 979  GLN A O      1 
ATOM   5825 C  CB     . GLN A 1 979  ? 183.971 156.129 159.595 1.00 15.79 ? 979  GLN A CB     1 
ATOM   5826 C  CG     . GLN A 1 979  ? 183.726 154.641 159.674 1.00 15.79 ? 979  GLN A CG     1 
ATOM   5827 C  CD     . GLN A 1 979  ? 183.003 154.231 160.930 1.00 15.79 ? 979  GLN A CD     1 
ATOM   5828 O  OE1    . GLN A 1 979  ? 183.083 154.906 161.955 1.00 15.79 ? 979  GLN A OE1    1 
ATOM   5829 N  NE2    . GLN A 1 979  ? 182.327 153.096 160.873 1.00 15.79 ? 979  GLN A NE2    1 
ATOM   5830 N  N      . LYS A 1 980  ? 181.458 157.854 160.451 1.00 16.00 ? 980  LYS A N      1 
ATOM   5831 C  CA     . LYS A 1 980  ? 180.148 157.976 161.088 1.00 16.00 ? 980  LYS A CA     1 
ATOM   5832 C  C      . LYS A 1 980  ? 179.159 158.757 160.226 1.00 16.00 ? 980  LYS A C      1 
ATOM   5833 O  O      . LYS A 1 980  ? 177.952 158.489 160.268 1.00 16.00 ? 980  LYS A O      1 
ATOM   5834 C  CB     . LYS A 1 980  ? 180.299 158.615 162.461 1.00 16.00 ? 980  LYS A CB     1 
ATOM   5835 C  CG     . LYS A 1 980  ? 181.014 157.747 163.462 1.00 16.00 ? 980  LYS A CG     1 
ATOM   5836 C  CD     . LYS A 1 980  ? 181.075 158.407 164.818 1.00 16.00 ? 980  LYS A CD     1 
ATOM   5837 C  CE     . LYS A 1 980  ? 181.866 157.559 165.793 1.00 16.00 ? 980  LYS A CE     1 
ATOM   5838 N  NZ     . LYS A 1 980  ? 181.161 156.287 166.099 1.00 16.00 ? 980  LYS A NZ     1 
ATOM   5839 N  N      . MET A 1 981  ? 179.651 159.688 159.406 1.00 15.20 ? 981  MET A N      1 
ATOM   5840 C  CA     . MET A 1 981  ? 178.799 160.370 158.439 1.00 15.20 ? 981  MET A CA     1 
ATOM   5841 C  C      . MET A 1 981  ? 178.368 159.445 157.314 1.00 15.20 ? 981  MET A C      1 
ATOM   5842 O  O      . MET A 1 981  ? 177.272 159.609 156.780 1.00 15.20 ? 981  MET A O      1 
ATOM   5843 C  CB     . MET A 1 981  ? 179.523 161.586 157.867 1.00 15.20 ? 981  MET A CB     1 
ATOM   5844 C  CG     . MET A 1 981  ? 179.616 162.767 158.799 1.00 15.20 ? 981  MET A CG     1 
ATOM   5845 S  SD     . MET A 1 981  ? 180.728 164.009 158.134 1.00 15.20 ? 981  MET A SD     1 
ATOM   5846 C  CE     . MET A 1 981  ? 180.848 165.121 159.521 1.00 15.20 ? 981  MET A CE     1 
ATOM   5847 N  N      . MET A 1 982  ? 179.200 158.475 156.932 1.00 17.18 ? 982  MET A N      1 
ATOM   5848 C  CA     . MET A 1 982  ? 178.745 157.485 155.962 1.00 17.18 ? 982  MET A CA     1 
ATOM   5849 C  C      . MET A 1 982  ? 177.685 156.573 156.554 1.00 17.18 ? 982  MET A C      1 
ATOM   5850 O  O      . MET A 1 982  ? 176.768 156.153 155.841 1.00 17.18 ? 982  MET A O      1 
ATOM   5851 C  CB     . MET A 1 982  ? 179.912 156.661 155.426 1.00 17.18 ? 982  MET A CB     1 
ATOM   5852 C  CG     . MET A 1 982  ? 180.799 157.399 154.449 1.00 17.18 ? 982  MET A CG     1 
ATOM   5853 S  SD     . MET A 1 982  ? 182.051 156.330 153.724 1.00 17.18 ? 982  MET A SD     1 
ATOM   5854 C  CE     . MET A 1 982  ? 183.187 156.148 155.092 1.00 17.18 ? 982  MET A CE     1 
ATOM   5855 N  N      . GLN A 1 983  ? 177.776 156.283 157.854 1.00 17.48 ? 983  GLN A N      1 
ATOM   5856 C  CA     . GLN A 1 983  ? 176.678 155.588 158.528 1.00 17.48 ? 983  GLN A CA     1 
ATOM   5857 C  C      . GLN A 1 983  ? 175.393 156.416 158.515 1.00 17.48 ? 983  GLN A C      1 
ATOM   5858 O  O      . GLN A 1 983  ? 174.304 155.886 158.252 1.00 17.48 ? 983  GLN A O      1 
ATOM   5859 C  CB     . GLN A 1 983  ? 177.074 155.247 159.960 1.00 17.48 ? 983  GLN A CB     1 
ATOM   5860 C  CG     . GLN A 1 983  ? 178.172 154.215 160.069 1.00 17.48 ? 983  GLN A CG     1 
ATOM   5861 C  CD     . GLN A 1 983  ? 178.554 153.942 161.502 1.00 17.48 ? 983  GLN A CD     1 
ATOM   5862 O  OE1    . GLN A 1 983  ? 178.065 154.594 162.422 1.00 17.48 ? 983  GLN A OE1    1 
ATOM   5863 N  NE2    . GLN A 1 983  ? 179.419 152.961 161.704 1.00 17.48 ? 983  GLN A NE2    1 
ATOM   5864 N  N      . ASP A 1 984  ? 175.505 157.724 158.778 1.00 17.56 ? 984  ASP A N      1 
ATOM   5865 C  CA     . ASP A 1 984  ? 174.338 158.609 158.734 1.00 17.56 ? 984  ASP A CA     1 
ATOM   5866 C  C      . ASP A 1 984  ? 173.745 158.700 157.333 1.00 17.56 ? 984  ASP A C      1 
ATOM   5867 O  O      . ASP A 1 984  ? 172.521 158.754 157.168 1.00 17.56 ? 984  ASP A O      1 
ATOM   5868 C  CB     . ASP A 1 984  ? 174.715 160.008 159.206 1.00 17.56 ? 984  ASP A CB     1 
ATOM   5869 C  CG     . ASP A 1 984  ? 175.055 160.060 160.665 1.00 17.56 ? 984  ASP A CG     1 
ATOM   5870 O  OD1    . ASP A 1 984  ? 174.540 159.224 161.435 1.00 17.56 ? 984  ASP A OD1    1 
ATOM   5871 O  OD2    . ASP A 1 984  ? 175.831 160.955 161.041 1.00 17.56 ? 984  ASP A OD2    1 
ATOM   5872 N  N      . LEU A 1 985  ? 174.603 158.734 156.317 1.00 18.11 ? 985  LEU A N      1 
ATOM   5873 C  CA     . LEU A 1 985  ? 174.141 158.801 154.938 1.00 18.11 ? 985  LEU A CA     1 
ATOM   5874 C  C      . LEU A 1 985  ? 173.473 157.498 154.525 1.00 18.11 ? 985  LEU A C      1 
ATOM   5875 O  O      . LEU A 1 985  ? 172.483 157.512 153.788 1.00 18.11 ? 985  LEU A O      1 
ATOM   5876 C  CB     . LEU A 1 985  ? 175.318 159.149 154.024 1.00 18.11 ? 985  LEU A CB     1 
ATOM   5877 C  CG     . LEU A 1 985  ? 175.109 159.495 152.551 1.00 18.11 ? 985  LEU A CG     1 
ATOM   5878 C  CD1    . LEU A 1 985  ? 176.107 160.555 152.153 1.00 18.11 ? 985  LEU A CD1    1 
ATOM   5879 C  CD2    . LEU A 1 985  ? 175.302 158.282 151.664 1.00 18.11 ? 985  LEU A CD2    1 
ATOM   5880 N  N      . ALA A 1 986  ? 173.983 156.366 155.016 1.00 18.63 ? 986  ALA A N      1 
ATOM   5881 C  CA     . ALA A 1 986  ? 173.335 155.086 154.765 1.00 18.63 ? 986  ALA A CA     1 
ATOM   5882 C  C      . ALA A 1 986  ? 171.986 154.994 155.461 1.00 18.63 ? 986  ALA A C      1 
ATOM   5883 O  O      . ALA A 1 986  ? 171.096 154.275 154.994 1.00 18.63 ? 986  ALA A O      1 
ATOM   5884 C  CB     . ALA A 1 986  ? 174.244 153.945 155.215 1.00 18.63 ? 986  ALA A CB     1 
ATOM   5885 N  N      . GLN A 1 987  ? 171.817 155.701 156.576 1.00 20.16 ? 987  GLN A N      1 
ATOM   5886 C  CA     . GLN A 1 987  ? 170.509 155.733 157.225 1.00 20.16 ? 987  GLN A CA     1 
ATOM   5887 C  C      . GLN A 1 987  ? 169.532 156.670 156.516 1.00 20.16 ? 987  GLN A C      1 
ATOM   5888 O  O      . GLN A 1 987  ? 168.334 156.380 156.452 1.00 20.16 ? 987  GLN A O      1 
ATOM   5889 C  CB     . GLN A 1 987  ? 170.678 156.130 158.686 1.00 20.16 ? 987  GLN A CB     1 
ATOM   5890 C  CG     . GLN A 1 987  ? 171.391 155.070 159.495 1.00 20.16 ? 987  GLN A CG     1 
ATOM   5891 C  CD     . GLN A 1 987  ? 171.754 155.541 160.880 1.00 20.16 ? 987  GLN A CD     1 
ATOM   5892 O  OE1    . GLN A 1 987  ? 171.524 156.695 161.235 1.00 20.16 ? 987  GLN A OE1    1 
ATOM   5893 N  NE2    . GLN A 1 987  ? 172.341 154.652 161.670 1.00 20.16 ? 987  GLN A NE2    1 
ATOM   5894 N  N      . PHE A 1 988  ? 170.016 157.787 155.977 1.00 19.20 ? 988  PHE A N      1 
ATOM   5895 C  CA     . PHE A 1 988  ? 169.156 158.803 155.373 1.00 19.20 ? 988  PHE A CA     1 
ATOM   5896 C  C      . PHE A 1 988  ? 168.896 158.562 153.885 1.00 19.20 ? 988  PHE A C      1 
ATOM   5897 O  O      . PHE A 1 988  ? 168.004 159.207 153.298 1.00 19.20 ? 988  PHE A O      1 
ATOM   5898 C  CB     . PHE A 1 988  ? 169.802 160.179 155.583 1.00 19.20 ? 988  PHE A CB     1 
ATOM   5899 C  CG     . PHE A 1 988  ? 168.881 161.340 155.353 1.00 19.20 ? 988  PHE A CG     1 
ATOM   5900 C  CD1    . PHE A 1 988  ? 167.933 161.675 156.303 1.00 19.20 ? 988  PHE A CD1    1 
ATOM   5901 C  CD2    . PHE A 1 988  ? 168.976 162.113 154.209 1.00 19.20 ? 988  PHE A CD2    1 
ATOM   5902 C  CE1    . PHE A 1 988  ? 167.088 162.745 156.110 1.00 19.20 ? 988  PHE A CE1    1 
ATOM   5903 C  CE2    . PHE A 1 988  ? 168.131 163.189 154.013 1.00 19.20 ? 988  PHE A CE2    1 
ATOM   5904 C  CZ     . PHE A 1 988  ? 167.185 163.501 154.964 1.00 19.20 ? 988  PHE A CZ     1 
ATOM   5905 N  N      . ILE A 1 989  ? 169.639 157.635 153.270 1.00 21.73 ? 989  ILE A N      1 
ATOM   5906 C  CA     . ILE A 1 989  ? 169.543 157.413 151.837 1.00 21.73 ? 989  ILE A CA     1 
ATOM   5907 C  C      . ILE A 1 989  ? 168.207 156.793 151.448 1.00 21.73 ? 989  ILE A C      1 
ATOM   5908 O  O      . ILE A 1 989  ? 167.771 156.959 150.311 1.00 21.73 ? 989  ILE A O      1 
ATOM   5909 C  CB     . ILE A 1 989  ? 170.752 156.566 151.375 1.00 21.73 ? 989  ILE A CB     1 
ATOM   5910 C  CG1    . ILE A 1 989  ? 170.986 156.706 149.871 1.00 21.73 ? 989  ILE A CG1    1 
ATOM   5911 C  CG2    . ILE A 1 989  ? 170.599 155.102 151.760 1.00 21.73 ? 989  ILE A CG2    1 
ATOM   5912 C  CD1    . ILE A 1 989  ? 171.415 158.091 149.465 1.00 21.73 ? 989  ILE A CD1    1 
ATOM   5913 N  N      . ILE A 1 990  ? 167.502 156.152 152.385 1.00 22.87 ? 990  ILE A N      1 
ATOM   5914 C  CA     . ILE A 1 990  ? 166.185 155.606 152.078 1.00 22.87 ? 990  ILE A CA     1 
ATOM   5915 C  C      . ILE A 1 990  ? 165.150 156.721 151.949 1.00 22.87 ? 990  ILE A C      1 
ATOM   5916 O  O      . ILE A 1 990  ? 164.291 156.678 151.065 1.00 22.87 ? 990  ILE A O      1 
ATOM   5917 C  CB     . ILE A 1 990  ? 165.794 154.539 153.125 1.00 22.87 ? 990  ILE A CB     1 
ATOM   5918 C  CG1    . ILE A 1 990  ? 164.437 153.908 152.800 1.00 22.87 ? 990  ILE A CG1    1 
ATOM   5919 C  CG2    . ILE A 1 990  ? 165.871 155.067 154.556 1.00 22.87 ? 990  ILE A CG2    1 
ATOM   5920 C  CD1    . ILE A 1 990  ? 164.423 153.104 151.525 1.00 22.87 ? 990  ILE A CD1    1 
ATOM   5921 N  N      . ILE A 1 991  ? 165.249 157.761 152.779 1.00 22.06 ? 991  ILE A N      1 
ATOM   5922 C  CA     . ILE A 1 991  ? 164.341 158.901 152.677 1.00 22.06 ? 991  ILE A CA     1 
ATOM   5923 C  C      . ILE A 1 991  ? 164.632 159.696 151.412 1.00 22.06 ? 991  ILE A C      1 
ATOM   5924 O  O      . ILE A 1 991  ? 163.706 160.117 150.690 1.00 22.06 ? 991  ILE A O      1 
ATOM   5925 C  CB     . ILE A 1 991  ? 164.458 159.765 153.946 1.00 22.06 ? 991  ILE A CB     1 
ATOM   5926 C  CG1    . ILE A 1 991  ? 164.019 158.963 155.169 1.00 22.06 ? 991  ILE A CG1    1 
ATOM   5927 C  CG2    . ILE A 1 991  ? 163.633 161.029 153.834 1.00 22.06 ? 991  ILE A CG2    1 
ATOM   5928 C  CD1    . ILE A 1 991  ? 164.348 159.628 156.480 1.00 22.06 ? 991  ILE A CD1    1 
ATOM   5929 N  N      . LEU A 1 992  ? 165.925 159.885 151.110 1.00 20.17 ? 992  LEU A N      1 
ATOM   5930 C  CA     . LEU A 1 992  ? 166.315 160.500 149.842 1.00 20.17 ? 992  LEU A CA     1 
ATOM   5931 C  C      . LEU A 1 992  ? 165.825 159.696 148.644 1.00 20.17 ? 992  LEU A C      1 
ATOM   5932 O  O      . LEU A 1 992  ? 165.343 160.272 147.665 1.00 20.17 ? 992  LEU A O      1 
ATOM   5933 C  CB     . LEU A 1 992  ? 167.829 160.663 149.773 1.00 20.17 ? 992  LEU A CB     1 
ATOM   5934 C  CG     . LEU A 1 992  ? 168.441 161.764 150.626 1.00 20.17 ? 992  LEU A CG     1 
ATOM   5935 C  CD1    . LEU A 1 992  ? 169.953 161.667 150.595 1.00 20.17 ? 992  LEU A CD1    1 
ATOM   5936 C  CD2    . LEU A 1 992  ? 167.981 163.112 150.105 1.00 20.17 ? 992  LEU A CD2    1 
ATOM   5937 N  N      . ALA A 1 993  ? 165.899 158.366 148.721 1.00 18.87 ? 993  ALA A N      1 
ATOM   5938 C  CA     . ALA A 1 993  ? 165.466 157.526 147.612 1.00 18.87 ? 993  ALA A CA     1 
ATOM   5939 C  C      . ALA A 1 993  ? 163.956 157.553 147.447 1.00 18.87 ? 993  ALA A C      1 
ATOM   5940 O  O      . ALA A 1 993  ? 163.465 157.556 146.317 1.00 18.87 ? 993  ALA A O      1 
ATOM   5941 C  CB     . ALA A 1 993  ? 165.955 156.095 147.814 1.00 18.87 ? 993  ALA A CB     1 
ATOM   5942 N  N      . VAL A 1 994  ? 163.208 157.602 148.553 1.00 18.59 ? 994  VAL A N      1 
ATOM   5943 C  CA     . VAL A 1 994  ? 161.748 157.659 148.474 1.00 18.59 ? 994  VAL A CA     1 
ATOM   5944 C  C      . VAL A 1 994  ? 161.294 158.949 147.803 1.00 18.59 ? 994  VAL A C      1 
ATOM   5945 O  O      . VAL A 1 994  ? 160.503 158.918 146.852 1.00 18.59 ? 994  VAL A O      1 
ATOM   5946 C  CB     . VAL A 1 994  ? 161.121 157.487 149.870 1.00 18.59 ? 994  VAL A CB     1 
ATOM   5947 C  CG1    . VAL A 1 994  ? 159.665 157.895 149.855 1.00 18.59 ? 994  VAL A CG1    1 
ATOM   5948 C  CG2    . VAL A 1 994  ? 161.205 156.039 150.291 1.00 18.59 ? 994  VAL A CG2    1 
ATOM   5949 N  N      . PHE A 1 995  ? 161.828 160.096 148.240 1.00 16.87 ? 995  PHE A N      1 
ATOM   5950 C  CA     . PHE A 1 995  ? 161.374 161.342 147.619 1.00 16.87 ? 995  PHE A CA     1 
ATOM   5951 C  C      . PHE A 1 995  ? 161.932 161.527 146.206 1.00 16.87 ? 995  PHE A C      1 
ATOM   5952 O  O      . PHE A 1 995  ? 161.237 162.078 145.342 1.00 16.87 ? 995  PHE A O      1 
ATOM   5953 C  CB     . PHE A 1 995  ? 161.701 162.540 148.506 1.00 16.87 ? 995  PHE A CB     1 
ATOM   5954 C  CG     . PHE A 1 995  ? 160.890 162.582 149.770 1.00 16.87 ? 995  PHE A CG     1 
ATOM   5955 C  CD1    . PHE A 1 995  ? 159.526 162.818 149.717 1.00 16.87 ? 995  PHE A CD1    1 
ATOM   5956 C  CD2    . PHE A 1 995  ? 161.488 162.422 151.007 1.00 16.87 ? 995  PHE A CD2    1 
ATOM   5957 C  CE1    . PHE A 1 995  ? 158.772 162.863 150.873 1.00 16.87 ? 995  PHE A CE1    1 
ATOM   5958 C  CE2    . PHE A 1 995  ? 160.739 162.474 152.165 1.00 16.87 ? 995  PHE A CE2    1 
ATOM   5959 C  CZ     . PHE A 1 995  ? 159.383 162.695 152.098 1.00 16.87 ? 995  PHE A CZ     1 
ATOM   5960 N  N      . THR A 1 996  ? 163.134 161.009 145.935 1.00 15.08 ? 996  THR A N      1 
ATOM   5961 C  CA     . THR A 1 996  ? 163.713 161.052 144.595 1.00 15.08 ? 996  THR A CA     1 
ATOM   5962 C  C      . THR A 1 996  ? 162.898 160.232 143.600 1.00 15.08 ? 996  THR A C      1 
ATOM   5963 O  O      . THR A 1 996  ? 162.554 160.717 142.518 1.00 15.08 ? 996  THR A O      1 
ATOM   5964 C  CB     . THR A 1 996  ? 165.160 160.554 144.669 1.00 15.08 ? 996  THR A CB     1 
ATOM   5965 O  OG1    . THR A 1 996  ? 165.948 161.488 145.416 1.00 15.08 ? 996  THR A OG1    1 
ATOM   5966 C  CG2    . THR A 1 996  ? 165.770 160.344 143.300 1.00 15.08 ? 996  THR A CG2    1 
ATOM   5967 N  N      . ILE A 1 997  ? 162.565 158.988 143.957 1.00 13.70 ? 997  ILE A N      1 
ATOM   5968 C  CA     . ILE A 1 997  ? 161.799 158.134 143.058 1.00 13.70 ? 997  ILE A CA     1 
ATOM   5969 C  C      . ILE A 1 997  ? 160.357 158.615 142.944 1.00 13.70 ? 997  ILE A C      1 
ATOM   5970 O  O      . ILE A 1 997  ? 159.766 158.551 141.858 1.00 13.70 ? 997  ILE A O      1 
ATOM   5971 C  CB     . ILE A 1 997  ? 161.913 156.664 143.520 1.00 13.70 ? 997  ILE A CB     1 
ATOM   5972 C  CG1    . ILE A 1 997  ? 163.366 156.199 143.429 1.00 13.70 ? 997  ILE A CG1    1 
ATOM   5973 C  CG2    . ILE A 1 997  ? 161.061 155.724 142.692 1.00 13.70 ? 997  ILE A CG2    1 
ATOM   5974 C  CD1    . ILE A 1 997  ? 163.945 156.301 142.058 1.00 13.70 ? 997  ILE A CD1    1 
ATOM   5975 N  N      . ALA A 1 998  ? 159.793 159.177 144.022 1.00 12.31 ? 998  ALA A N      1 
ATOM   5976 C  CA     . ALA A 1 998  ? 158.433 159.702 143.965 1.00 12.31 ? 998  ALA A CA     1 
ATOM   5977 C  C      . ALA A 1 998  ? 158.337 160.910 143.046 1.00 12.31 ? 998  ALA A C      1 
ATOM   5978 O  O      . ALA A 1 998  ? 157.353 161.059 142.314 1.00 12.31 ? 998  ALA A O      1 
ATOM   5979 C  CB     . ALA A 1 998  ? 157.953 160.067 145.367 1.00 12.31 ? 998  ALA A CB     1 
ATOM   5980 N  N      . TYR A 1 999  ? 159.351 161.776 143.056 1.00 9.40  ? 999  TYR A N      1 
ATOM   5981 C  CA     . TYR A 1 999  ? 159.361 162.886 142.113 1.00 9.40  ? 999  TYR A CA     1 
ATOM   5982 C  C      . TYR A 1 999  ? 159.663 162.427 140.691 1.00 9.40  ? 999  TYR A C      1 
ATOM   5983 O  O      . TYR A 1 999  ? 159.091 162.957 139.735 1.00 9.40  ? 999  TYR A O      1 
ATOM   5984 C  CB     . TYR A 1 999  ? 160.362 163.940 142.568 1.00 9.40  ? 999  TYR A CB     1 
ATOM   5985 C  CG     . TYR A 1 999  ? 160.688 164.964 141.518 1.00 9.40  ? 999  TYR A CG     1 
ATOM   5986 C  CD1    . TYR A 1 999  ? 159.763 165.910 141.110 1.00 9.40  ? 999  TYR A CD1    1 
ATOM   5987 C  CD2    . TYR A 1 999  ? 161.945 164.994 140.955 1.00 9.40  ? 999  TYR A CD2    1 
ATOM   5988 C  CE1    . TYR A 1 999  ? 160.090 166.839 140.142 1.00 9.40  ? 999  TYR A CE1    1 
ATOM   5989 C  CE2    . TYR A 1 999  ? 162.283 165.911 140.003 1.00 9.40  ? 999  TYR A CE2    1 
ATOM   5990 C  CZ     . TYR A 1 999  ? 161.356 166.837 139.599 1.00 9.40  ? 999  TYR A CZ     1 
ATOM   5991 O  OH     . TYR A 1 999  ? 161.691 167.758 138.640 1.00 9.40  ? 999  TYR A OH     1 
ATOM   5992 N  N      . GLY A 1 1000 ? 160.552 161.444 140.529 1.00 12.71 ? 1000 GLY A N      1 
ATOM   5993 C  CA     . GLY A 1 1000 ? 160.949 161.021 139.198 1.00 12.71 ? 1000 GLY A CA     1 
ATOM   5994 C  C      . GLY A 1 1000 ? 159.879 160.279 138.436 1.00 12.71 ? 1000 GLY A C      1 
ATOM   5995 O  O      . GLY A 1 1000 ? 159.789 160.420 137.215 1.00 12.71 ? 1000 GLY A O      1 
ATOM   5996 N  N      . ILE A 1 1001 ? 159.060 159.488 139.136 1.00 10.33 ? 1001 ILE A N      1 
ATOM   5997 C  CA     . ILE A 1 1001 ? 157.944 158.797 138.492 1.00 10.33 ? 1001 ILE A CA     1 
ATOM   5998 C  C      . ILE A 1 1001 ? 156.943 159.800 137.932 1.00 10.33 ? 1001 ILE A C      1 
ATOM   5999 O  O      . ILE A 1 1001 ? 156.535 159.708 136.769 1.00 10.33 ? 1001 ILE A O      1 
ATOM   6000 C  CB     . ILE A 1 1001 ? 157.277 157.818 139.475 1.00 10.33 ? 1001 ILE A CB     1 
ATOM   6001 C  CG1    . ILE A 1 1001 ? 158.203 156.641 139.776 1.00 10.33 ? 1001 ILE A CG1    1 
ATOM   6002 C  CG2    . ILE A 1 1001 ? 155.946 157.322 138.942 1.00 10.33 ? 1001 ILE A CG2    1 
ATOM   6003 C  CD1    . ILE A 1 1001 ? 157.743 155.816 140.938 1.00 10.33 ? 1001 ILE A CD1    1 
ATOM   6004 N  N      . ALA A 1 1002 ? 156.569 160.799 138.737 1.00 11.11 ? 1002 ALA A N      1 
ATOM   6005 C  CA     . ALA A 1 1002 ? 155.617 161.811 138.288 1.00 11.11 ? 1002 ALA A CA     1 
ATOM   6006 C  C      . ALA A 1 1002 ? 156.212 162.696 137.204 1.00 11.11 ? 1002 ALA A C      1 
ATOM   6007 O  O      . ALA A 1 1002 ? 155.516 163.075 136.254 1.00 11.11 ? 1002 ALA A O      1 
ATOM   6008 C  CB     . ALA A 1 1002 ? 155.159 162.657 139.472 1.00 11.11 ? 1002 ALA A CB     1 
ATOM   6009 N  N      . LEU A 1 1003 ? 157.507 162.999 137.314 1.00 12.38 ? 1003 LEU A N      1 
ATOM   6010 C  CA     . LEU A 1 1003 ? 158.194 163.821 136.327 1.00 12.38 ? 1003 LEU A CA     1 
ATOM   6011 C  C      . LEU A 1 1003 ? 158.258 163.127 134.973 1.00 12.38 ? 1003 LEU A C      1 
ATOM   6012 O  O      . LEU A 1 1003 ? 157.920 163.720 133.944 1.00 12.38 ? 1003 LEU A O      1 
ATOM   6013 C  CB     . LEU A 1 1003 ? 159.596 164.140 136.838 1.00 12.38 ? 1003 LEU A CB     1 
ATOM   6014 C  CG     . LEU A 1 1003 ? 160.494 165.023 135.983 1.00 12.38 ? 1003 LEU A CG     1 
ATOM   6015 C  CD1    . LEU A 1 1003 ? 159.962 166.442 135.905 1.00 12.38 ? 1003 LEU A CD1    1 
ATOM   6016 C  CD2    . LEU A 1 1003 ? 161.924 164.979 136.493 1.00 12.38 ? 1003 LEU A CD2    1 
ATOM   6017 N  N      . HIS A 1 1004 ? 158.659 161.856 134.958 1.00 10.72 ? 1004 HIS A N      1 
ATOM   6018 C  CA     . HIS A 1 1004 ? 158.737 161.126 133.705 1.00 10.72 ? 1004 HIS A CA     1 
ATOM   6019 C  C      . HIS A 1 1004 ? 157.362 160.763 133.175 1.00 10.72 ? 1004 HIS A C      1 
ATOM   6020 O  O      . HIS A 1 1004 ? 157.210 160.568 131.968 1.00 10.72 ? 1004 HIS A O      1 
ATOM   6021 C  CB     . HIS A 1 1004 ? 159.572 159.860 133.882 1.00 10.72 ? 1004 HIS A CB     1 
ATOM   6022 C  CG     . HIS A 1 1004 ? 160.002 159.243 132.591 1.00 10.72 ? 1004 HIS A CG     1 
ATOM   6023 N  ND1    . HIS A 1 1004 ? 159.165 158.464 131.823 1.00 10.72 ? 1004 HIS A ND1    1 
ATOM   6024 C  CD2    . HIS A 1 1004 ? 161.185 159.278 131.939 1.00 10.72 ? 1004 HIS A CD2    1 
ATOM   6025 C  CE1    . HIS A 1 1004 ? 159.805 158.073 130.738 1.00 10.72 ? 1004 HIS A CE1    1 
ATOM   6026 N  NE2    . HIS A 1 1004 ? 161.039 158.535 130.795 1.00 10.72 ? 1004 HIS A NE2    1 
ATOM   6027 N  N      . ALA A 1 1005 ? 156.358 160.675 134.047 1.00 12.33 ? 1005 ALA A N      1 
ATOM   6028 C  CA     . ALA A 1 1005 ? 155.003 160.417 133.588 1.00 12.33 ? 1005 ALA A CA     1 
ATOM   6029 C  C      . ALA A 1 1005 ? 154.406 161.638 132.905 1.00 12.33 ? 1005 ALA A C      1 
ATOM   6030 O  O      . ALA A 1 1005 ? 153.673 161.503 131.923 1.00 12.33 ? 1005 ALA A O      1 
ATOM   6031 C  CB     . ALA A 1 1005 ? 154.135 159.976 134.762 1.00 12.33 ? 1005 ALA A CB     1 
ATOM   6032 N  N      . VAL A 1 1006 ? 154.704 162.839 133.404 1.00 12.46 ? 1006 VAL A N      1 
ATOM   6033 C  CA     . VAL A 1 1006 ? 154.132 164.007 132.746 1.00 12.46 ? 1006 VAL A CA     1 
ATOM   6034 C  C      . VAL A 1 1006 ? 154.962 164.421 131.532 1.00 12.46 ? 1006 VAL A C      1 
ATOM   6035 O  O      . VAL A 1 1006 ? 154.407 164.930 130.555 1.00 12.46 ? 1006 VAL A O      1 
ATOM   6036 C  CB     . VAL A 1 1006 ? 153.927 165.171 133.736 1.00 12.46 ? 1006 VAL A CB     1 
ATOM   6037 C  CG1    . VAL A 1 1006 ? 152.999 164.740 134.860 1.00 12.46 ? 1006 VAL A CG1    1 
ATOM   6038 C  CG2    . VAL A 1 1006 ? 155.237 165.709 134.286 1.00 12.46 ? 1006 VAL A CG2    1 
ATOM   6039 N  N      . MET A 1 1007 ? 156.278 164.183 131.536 1.00 14.43 ? 1007 MET A N      1 
ATOM   6040 C  CA     . MET A 1 1007 ? 157.059 164.513 130.350 1.00 14.43 ? 1007 MET A CA     1 
ATOM   6041 C  C      . MET A 1 1007 ? 156.867 163.487 129.242 1.00 14.43 ? 1007 MET A C      1 
ATOM   6042 O  O      . MET A 1 1007 ? 156.724 163.856 128.073 1.00 14.43 ? 1007 MET A O      1 
ATOM   6043 C  CB     . MET A 1 1007 ? 158.544 164.617 130.675 1.00 14.43 ? 1007 MET A CB     1 
ATOM   6044 C  CG     . MET A 1 1007 ? 158.943 165.744 131.575 1.00 14.43 ? 1007 MET A CG     1 
ATOM   6045 S  SD     . MET A 1 1007 ? 160.727 165.889 131.590 1.00 14.43 ? 1007 MET A SD     1 
ATOM   6046 C  CE     . MET A 1 1007 ? 161.208 164.388 132.427 1.00 14.43 ? 1007 MET A CE     1 
ATOM   6047 N  N      . PHE A 1 1008 ? 156.871 162.196 129.578 1.00 13.62 ? 1008 PHE A N      1 
ATOM   6048 C  CA     . PHE A 1 1008 ? 156.858 161.125 128.583 1.00 13.62 ? 1008 PHE A CA     1 
ATOM   6049 C  C      . PHE A 1 1008 ? 155.746 160.136 128.910 1.00 13.62 ? 1008 PHE A C      1 
ATOM   6050 O  O      . PHE A 1 1008 ? 155.991 159.109 129.553 1.00 13.62 ? 1008 PHE A O      1 
ATOM   6051 C  CB     . PHE A 1 1008 ? 158.213 160.420 128.538 1.00 13.62 ? 1008 PHE A CB     1 
ATOM   6052 C  CG     . PHE A 1 1008 ? 159.370 161.355 128.377 1.00 13.62 ? 1008 PHE A CG     1 
ATOM   6053 C  CD1    . PHE A 1 1008 ? 159.627 161.953 127.162 1.00 13.62 ? 1008 PHE A CD1    1 
ATOM   6054 C  CD2    . PHE A 1 1008 ? 160.210 161.627 129.446 1.00 13.62 ? 1008 PHE A CD2    1 
ATOM   6055 C  CE1    . PHE A 1 1008 ? 160.687 162.814 127.020 1.00 13.62 ? 1008 PHE A CE1    1 
ATOM   6056 C  CE2    . PHE A 1 1008 ? 161.269 162.494 129.306 1.00 13.62 ? 1008 PHE A CE2    1 
ATOM   6057 C  CZ     . PHE A 1 1008 ? 161.511 163.078 128.089 1.00 13.62 ? 1008 PHE A CZ     1 
ATOM   6058 N  N      . PRO A 1 1009 ? 154.511 160.413 128.486 1.00 17.68 ? 1009 PRO A N      1 
ATOM   6059 C  CA     . PRO A 1 1009 ? 153.414 159.460 128.724 1.00 17.68 ? 1009 PRO A CA     1 
ATOM   6060 C  C      . PRO A 1 1009 ? 153.568 158.217 127.856 1.00 17.68 ? 1009 PRO A C      1 
ATOM   6061 O  O      . PRO A 1 1009 ? 153.773 158.314 126.646 1.00 17.68 ? 1009 PRO A O      1 
ATOM   6062 C  CB     . PRO A 1 1009 ? 152.164 160.260 128.345 1.00 17.68 ? 1009 PRO A CB     1 
ATOM   6063 C  CG     . PRO A 1 1009 ? 152.587 161.675 128.422 1.00 17.68 ? 1009 PRO A CG     1 
ATOM   6064 C  CD     . PRO A 1 1009 ? 154.002 161.696 127.983 1.00 17.68 ? 1009 PRO A CD     1 
ATOM   6065 N  N      . SER A 1 1010 ? 153.446 157.045 128.487 1.00 22.00 ? 1010 SER A N      1 
ATOM   6066 C  CA     . SER A 1 1010 ? 153.948 155.791 127.930 1.00 22.00 ? 1010 SER A CA     1 
ATOM   6067 C  C      . SER A 1 1010 ? 153.090 155.157 126.831 1.00 22.00 ? 1010 SER A C      1 
ATOM   6068 O  O      . SER A 1 1010 ? 153.657 154.513 125.940 1.00 22.00 ? 1010 SER A O      1 
ATOM   6069 C  CB     . SER A 1 1010 ? 154.195 154.785 129.057 1.00 22.00 ? 1010 SER A CB     1 
ATOM   6070 O  OG     . SER A 1 1010 ? 154.590 153.529 128.537 1.00 22.00 ? 1010 SER A OG     1 
ATOM   6071 N  N      . PRO A 1 1011 ? 151.745 155.221 126.855 1.00 23.71 ? 1011 PRO A N      1 
ATOM   6072 C  CA     . PRO A 1 1011 ? 151.079 154.807 125.596 1.00 23.71 ? 1011 PRO A CA     1 
ATOM   6073 C  C      . PRO A 1 1011 ? 150.821 155.983 124.656 1.00 23.71 ? 1011 PRO A C      1 
ATOM   6074 O  O      . PRO A 1 1011 ? 149.691 156.468 124.509 1.00 23.71 ? 1011 PRO A O      1 
ATOM   6075 C  CB     . PRO A 1 1011 ? 149.781 154.168 126.100 1.00 23.71 ? 1011 PRO A CB     1 
ATOM   6076 C  CG     . PRO A 1 1011 ? 149.977 153.938 127.541 1.00 23.71 ? 1011 PRO A CG     1 
ATOM   6077 C  CD     . PRO A 1 1011 ? 150.817 155.076 127.986 1.00 23.71 ? 1011 PRO A CD     1 
ATOM   6078 N  N      . GLY A 1 1012 ? 151.860 156.472 123.994 1.00 24.76 ? 1012 GLY A N      1 
ATOM   6079 C  CA     . GLY A 1 1012 ? 151.661 157.614 123.127 1.00 24.76 ? 1012 GLY A CA     1 
ATOM   6080 C  C      . GLY A 1 1012 ? 152.851 157.952 122.260 1.00 24.76 ? 1012 GLY A C      1 
ATOM   6081 O  O      . GLY A 1 1012 ? 153.776 157.156 122.102 1.00 24.76 ? 1012 GLY A O      1 
ATOM   6082 N  N      . ILE A 1 1013 ? 152.808 159.164 121.702 1.00 25.34 ? 1013 ILE A N      1 
ATOM   6083 C  CA     . ILE A 1 1013 ? 153.829 159.610 120.761 1.00 25.34 ? 1013 ILE A CA     1 
ATOM   6084 C  C      . ILE A 1 1013 ? 155.024 160.263 121.444 1.00 25.34 ? 1013 ILE A C      1 
ATOM   6085 O  O      . ILE A 1 1013 ? 156.080 160.411 120.813 1.00 25.34 ? 1013 ILE A O      1 
ATOM   6086 C  CB     . ILE A 1 1013 ? 153.237 160.581 119.723 1.00 25.34 ? 1013 ILE A CB     1 
ATOM   6087 C  CG1    . ILE A 1 1013 ? 152.744 161.855 120.389 1.00 25.34 ? 1013 ILE A CG1    1 
ATOM   6088 C  CG2    . ILE A 1 1013 ? 152.077 159.954 119.003 1.00 25.34 ? 1013 ILE A CG2    1 
ATOM   6089 C  CD1    . ILE A 1 1013 ? 152.343 162.930 119.412 1.00 25.34 ? 1013 ILE A CD1    1 
ATOM   6090 N  N      . TYR A 1 1014 ? 154.895 160.654 122.707 1.00 21.77 ? 1014 TYR A N      1 
ATOM   6091 C  CA     . TYR A 1 1014 ? 156.006 161.191 123.473 1.00 21.77 ? 1014 TYR A CA     1 
ATOM   6092 C  C      . TYR A 1 1014 ? 156.594 160.151 124.403 1.00 21.77 ? 1014 TYR A C      1 
ATOM   6093 O  O      . TYR A 1 1014 ? 157.369 160.493 125.297 1.00 21.77 ? 1014 TYR A O      1 
ATOM   6094 C  CB     . TYR A 1 1014 ? 155.560 162.422 124.261 1.00 21.77 ? 1014 TYR A CB     1 
ATOM   6095 C  CG     . TYR A 1 1014 ? 155.085 163.533 123.366 1.00 21.77 ? 1014 TYR A CG     1 
ATOM   6096 C  CD1    . TYR A 1 1014 ? 155.987 164.317 122.666 1.00 21.77 ? 1014 TYR A CD1    1 
ATOM   6097 C  CD2    . TYR A 1 1014 ? 153.734 163.791 123.217 1.00 21.77 ? 1014 TYR A CD2    1 
ATOM   6098 C  CE1    . TYR A 1 1014 ? 155.555 165.328 121.839 1.00 21.77 ? 1014 TYR A CE1    1 
ATOM   6099 C  CE2    . TYR A 1 1014 ? 153.290 164.793 122.392 1.00 21.77 ? 1014 TYR A CE2    1 
ATOM   6100 C  CZ     . TYR A 1 1014 ? 154.203 165.562 121.708 1.00 21.77 ? 1014 TYR A CZ     1 
ATOM   6101 O  OH     . TYR A 1 1014 ? 153.757 166.569 120.886 1.00 21.77 ? 1014 TYR A OH     1 
ATOM   6102 N  N      . ALA A 1 1015 ? 156.242 158.888 124.202 1.00 22.00 ? 1015 ALA A N      1 
ATOM   6103 C  CA     . ALA A 1 1015 ? 156.715 157.802 125.041 1.00 22.00 ? 1015 ALA A CA     1 
ATOM   6104 C  C      . ALA A 1 1015 ? 158.160 157.473 124.727 1.00 22.00 ? 1015 ALA A C      1 
ATOM   6105 O  O      . ALA A 1 1015 ? 158.541 157.366 123.560 1.00 22.00 ? 1015 ALA A O      1 
ATOM   6106 C  CB     . ALA A 1 1015 ? 155.864 156.564 124.816 1.00 22.00 ? 1015 ALA A CB     1 
ATOM   6107 N  N      . ARG A 1 1016 ? 158.962 157.305 125.767 1.00 19.63 ? 1016 ARG A N      1 
ATOM   6108 C  CA     . ARG A 1 1016 ? 160.262 156.673 125.614 1.00 19.63 ? 1016 ARG A CA     1 
ATOM   6109 C  C      . ARG A 1 1016 ? 160.032 155.177 125.488 1.00 19.63 ? 1016 ARG A C      1 
ATOM   6110 O  O      . ARG A 1 1016 ? 159.615 154.523 126.448 1.00 19.63 ? 1016 ARG A O      1 
ATOM   6111 C  CB     . ARG A 1 1016 ? 161.166 157.004 126.794 1.00 19.63 ? 1016 ARG A CB     1 
ATOM   6112 C  CG     . ARG A 1 1016 ? 161.641 158.425 126.774 1.00 19.63 ? 1016 ARG A CG     1 
ATOM   6113 C  CD     . ARG A 1 1016 ? 162.647 158.672 127.854 1.00 19.63 ? 1016 ARG A CD     1 
ATOM   6114 N  NE     . ARG A 1 1016 ? 163.245 159.990 127.712 1.00 19.63 ? 1016 ARG A NE     1 
ATOM   6115 C  CZ     . ARG A 1 1016 ? 164.164 160.468 128.534 1.00 19.63 ? 1016 ARG A CZ     1 
ATOM   6116 N  NH1    . ARG A 1 1016 ? 164.579 159.729 129.542 1.00 19.63 ? 1016 ARG A NH1    1 
ATOM   6117 N  NH2    . ARG A 1 1016 ? 164.676 161.673 128.347 1.00 19.63 ? 1016 ARG A NH2    1 
ATOM   6118 N  N      . ASN A 1 1017 ? 160.293 154.626 124.309 1.00 23.96 ? 1017 ASN A N      1 
ATOM   6119 C  CA     . ASN A 1 1017 ? 159.999 153.218 124.057 1.00 23.96 ? 1017 ASN A CA     1 
ATOM   6120 C  C      . ASN A 1 1017 ? 161.173 152.327 124.441 1.00 23.96 ? 1017 ASN A C      1 
ATOM   6121 O  O      . ASN A 1 1017 ? 161.661 151.503 123.673 1.00 23.96 ? 1017 ASN A O      1 
ATOM   6122 C  CB     . ASN A 1 1017 ? 159.609 153.037 122.601 1.00 23.96 ? 1017 ASN A CB     1 
ATOM   6123 C  CG     . ASN A 1 1017 ? 158.315 153.724 122.277 1.00 23.96 ? 1017 ASN A CG     1 
ATOM   6124 O  OD1    . ASN A 1 1017 ? 157.363 153.669 123.051 1.00 23.96 ? 1017 ASN A OD1    1 
ATOM   6125 N  ND2    . ASN A 1 1017 ? 158.268 154.385 121.141 1.00 23.96 ? 1017 ASN A ND2    1 
ATOM   6126 N  N      . ASN A 1 1018 ? 161.619 152.512 125.677 1.00 20.04 ? 1018 ASN A N      1 
ATOM   6127 C  CA     . ASN A 1 1018 ? 162.735 151.777 126.250 1.00 20.04 ? 1018 ASN A CA     1 
ATOM   6128 C  C      . ASN A 1 1018 ? 162.530 151.813 127.751 1.00 20.04 ? 1018 ASN A C      1 
ATOM   6129 O  O      . ASN A 1 1018 ? 162.463 152.897 128.335 1.00 20.04 ? 1018 ASN A O      1 
ATOM   6130 C  CB     . ASN A 1 1018 ? 164.070 152.402 125.853 1.00 20.04 ? 1018 ASN A CB     1 
ATOM   6131 C  CG     . ASN A 1 1018 ? 165.260 151.538 126.218 1.00 20.04 ? 1018 ASN A CG     1 
ATOM   6132 O  OD1    . ASN A 1 1018 ? 165.116 150.445 126.766 1.00 20.04 ? 1018 ASN A OD1    1 
ATOM   6133 N  ND2    . ASN A 1 1018 ? 166.450 152.029 125.912 1.00 20.04 ? 1018 ASN A ND2    1 
ATOM   6134 N  N      . THR A 1 1019 ? 162.393 150.635 128.360 1.00 17.08 ? 1019 THR A N      1 
ATOM   6135 C  CA     . THR A 1 1019 ? 162.161 150.540 129.795 1.00 17.08 ? 1019 THR A CA     1 
ATOM   6136 C  C      . THR A 1 1019 ? 163.374 151.025 130.578 1.00 17.08 ? 1019 THR A C      1 
ATOM   6137 O  O      . THR A 1 1019 ? 163.229 151.633 131.648 1.00 17.08 ? 1019 THR A O      1 
ATOM   6138 C  CB     . THR A 1 1019 ? 161.806 149.090 130.142 1.00 17.08 ? 1019 THR A CB     1 
ATOM   6139 O  OG1    . THR A 1 1019 ? 160.686 148.682 129.351 1.00 17.08 ? 1019 THR A OG1    1 
ATOM   6140 C  CG2    . THR A 1 1019 ? 161.438 148.928 131.598 1.00 17.08 ? 1019 THR A CG2    1 
ATOM   6141 N  N      . TRP A 1 1020 ? 164.567 150.842 130.015 1.00 17.74 ? 1020 TRP A N      1 
ATOM   6142 C  CA     . TRP A 1 1020 ? 165.786 151.191 130.728 1.00 17.74 ? 1020 TRP A CA     1 
ATOM   6143 C  C      . TRP A 1 1020 ? 165.996 152.698 130.793 1.00 17.74 ? 1020 TRP A C      1 
ATOM   6144 O  O      . TRP A 1 1020 ? 166.411 153.213 131.837 1.00 17.74 ? 1020 TRP A O      1 
ATOM   6145 C  CB     . TRP A 1 1020 ? 166.983 150.496 130.085 1.00 17.74 ? 1020 TRP A CB     1 
ATOM   6146 C  CG     . TRP A 1 1020 ? 168.271 150.756 130.786 1.00 17.74 ? 1020 TRP A CG     1 
ATOM   6147 C  CD1    . TRP A 1 1020 ? 169.324 151.479 130.319 1.00 17.74 ? 1020 TRP A CD1    1 
ATOM   6148 C  CD2    . TRP A 1 1020 ? 168.627 150.332 132.106 1.00 17.74 ? 1020 TRP A CD2    1 
ATOM   6149 N  NE1    . TRP A 1 1020 ? 170.328 151.509 131.254 1.00 17.74 ? 1020 TRP A NE1    1 
ATOM   6150 C  CE2    . TRP A 1 1020 ? 169.925 150.810 132.361 1.00 17.74 ? 1020 TRP A CE2    1 
ATOM   6151 C  CE3    . TRP A 1 1020 ? 167.978 149.584 133.094 1.00 17.74 ? 1020 TRP A CE3    1 
ATOM   6152 C  CZ2    . TRP A 1 1020 ? 170.584 150.572 133.563 1.00 17.74 ? 1020 TRP A CZ2    1 
ATOM   6153 C  CZ3    . TRP A 1 1020 ? 168.632 149.346 134.283 1.00 17.74 ? 1020 TRP A CZ3    1 
ATOM   6154 C  CH2    . TRP A 1 1020 ? 169.923 149.838 134.509 1.00 17.74 ? 1020 TRP A CH2    1 
ATOM   6155 N  N      . VAL A 1 1021 ? 165.702 153.431 129.713 1.00 16.73 ? 1021 VAL A N      1 
ATOM   6156 C  CA     . VAL A 1 1021 ? 165.874 154.879 129.793 1.00 16.73 ? 1021 VAL A CA     1 
ATOM   6157 C  C      . VAL A 1 1021 ? 164.783 155.501 130.655 1.00 16.73 ? 1021 VAL A C      1 
ATOM   6158 O  O      . VAL A 1 1021 ? 165.026 156.514 131.313 1.00 16.73 ? 1021 VAL A O      1 
ATOM   6159 C  CB     . VAL A 1 1021 ? 165.948 155.545 128.402 1.00 16.73 ? 1021 VAL A CB     1 
ATOM   6160 C  CG1    . VAL A 1 1021 ? 167.070 154.943 127.578 1.00 16.73 ? 1021 VAL A CG1    1 
ATOM   6161 C  CG2    . VAL A 1 1021 ? 164.627 155.505 127.668 1.00 16.73 ? 1021 VAL A CG2    1 
ATOM   6162 N  N      . THR A 1 1022 ? 163.609 154.868 130.744 1.00 14.71 ? 1022 THR A N      1 
ATOM   6163 C  CA     . THR A 1 1022 ? 162.571 155.334 131.657 1.00 14.71 ? 1022 THR A CA     1 
ATOM   6164 C  C      . THR A 1 1022 ? 162.994 155.164 133.109 1.00 14.71 ? 1022 THR A C      1 
ATOM   6165 O  O      . THR A 1 1022 ? 162.916 156.114 133.900 1.00 14.71 ? 1022 THR A O      1 
ATOM   6166 C  CB     . THR A 1 1022 ? 161.260 154.598 131.391 1.00 14.71 ? 1022 THR A CB     1 
ATOM   6167 O  OG1    . THR A 1 1022 ? 160.790 154.916 130.078 1.00 14.71 ? 1022 THR A OG1    1 
ATOM   6168 C  CG2    . THR A 1 1022 ? 160.206 154.993 132.408 1.00 14.71 ? 1022 THR A CG2    1 
ATOM   6169 N  N      . ILE A 1 1023 ? 163.483 153.973 133.466 1.00 15.71 ? 1023 ILE A N      1 
ATOM   6170 C  CA     . ILE A 1 1023 ? 163.855 153.702 134.852 1.00 15.71 ? 1023 ILE A CA     1 
ATOM   6171 C  C      . ILE A 1 1023 ? 165.078 154.519 135.256 1.00 15.71 ? 1023 ILE A C      1 
ATOM   6172 O  O      . ILE A 1 1023 ? 165.103 155.135 136.332 1.00 15.71 ? 1023 ILE A O      1 
ATOM   6173 C  CB     . ILE A 1 1023 ? 164.073 152.192 135.052 1.00 15.71 ? 1023 ILE A CB     1 
ATOM   6174 C  CG1    . ILE A 1 1023 ? 162.748 151.449 134.900 1.00 15.71 ? 1023 ILE A CG1    1 
ATOM   6175 C  CG2    . ILE A 1 1023 ? 164.688 151.896 136.404 1.00 15.71 ? 1023 ILE A CG2    1 
ATOM   6176 C  CD1    . ILE A 1 1023 ? 162.901 149.962 134.855 1.00 15.71 ? 1023 ILE A CD1    1 
ATOM   6177 N  N      . THR A 1 1024 ? 166.088 154.585 134.385 1.00 17.02 ? 1024 THR A N      1 
ATOM   6178 C  CA     . THR A 1 1024 ? 167.247 155.408 134.685 1.00 17.02 ? 1024 THR A CA     1 
ATOM   6179 C  C      . THR A 1 1024 ? 166.944 156.894 134.647 1.00 17.02 ? 1024 THR A C      1 
ATOM   6180 O  O      . THR A 1 1024 ? 167.631 157.644 135.327 1.00 17.02 ? 1024 THR A O      1 
ATOM   6181 C  CB     . THR A 1 1024 ? 168.397 155.109 133.732 1.00 17.02 ? 1024 THR A CB     1 
ATOM   6182 O  OG1    . THR A 1 1024 ? 167.958 155.252 132.379 1.00 17.02 ? 1024 THR A OG1    1 
ATOM   6183 C  CG2    . THR A 1 1024 ? 168.910 153.728 133.964 1.00 17.02 ? 1024 THR A CG2    1 
ATOM   6184 N  N      . SER A 1 1025 ? 165.921 157.339 133.915 1.00 16.35 ? 1025 SER A N      1 
ATOM   6185 C  CA     . SER A 1 1025 ? 165.549 158.745 133.977 1.00 16.35 ? 1025 SER A CA     1 
ATOM   6186 C  C      . SER A 1 1025 ? 164.894 159.079 135.306 1.00 16.35 ? 1025 SER A C      1 
ATOM   6187 O  O      . SER A 1 1025 ? 165.223 160.103 135.920 1.00 16.35 ? 1025 SER A O      1 
ATOM   6188 C  CB     . SER A 1 1025 ? 164.614 159.081 132.828 1.00 16.35 ? 1025 SER A CB     1 
ATOM   6189 O  OG     . SER A 1 1025 ? 165.256 158.839 131.597 1.00 16.35 ? 1025 SER A OG     1 
ATOM   6190 N  N      . VAL A 1 1026 ? 163.986 158.204 135.762 1.00 14.56 ? 1026 VAL A N      1 
ATOM   6191 C  CA     . VAL A 1 1026 ? 163.342 158.335 137.070 1.00 14.56 ? 1026 VAL A CA     1 
ATOM   6192 C  C      . VAL A 1 1026 ? 164.376 158.360 138.193 1.00 14.56 ? 1026 VAL A C      1 
ATOM   6193 O  O      . VAL A 1 1026 ? 164.256 159.133 139.150 1.00 14.56 ? 1026 VAL A O      1 
ATOM   6194 C  CB     . VAL A 1 1026 ? 162.316 157.198 137.256 1.00 14.56 ? 1026 VAL A CB     1 
ATOM   6195 C  CG1    . VAL A 1 1026 ? 161.771 157.152 138.669 1.00 14.56 ? 1026 VAL A CG1    1 
ATOM   6196 C  CG2    . VAL A 1 1026 ? 161.169 157.370 136.301 1.00 14.56 ? 1026 VAL A CG2    1 
ATOM   6197 N  N      . VAL A 1 1027 ? 165.425 157.550 138.078 1.00 16.65 ? 1027 VAL A N      1 
ATOM   6198 C  CA     . VAL A 1 1027 ? 166.459 157.568 139.111 1.00 16.65 ? 1027 VAL A CA     1 
ATOM   6199 C  C      . VAL A 1 1027 ? 167.404 158.757 138.923 1.00 16.65 ? 1027 VAL A C      1 
ATOM   6200 O  O      . VAL A 1 1027 ? 167.815 159.403 139.892 1.00 16.65 ? 1027 VAL A O      1 
ATOM   6201 C  CB     . VAL A 1 1027 ? 167.207 156.222 139.110 1.00 16.65 ? 1027 VAL A CB     1 
ATOM   6202 C  CG1    . VAL A 1 1027 ? 168.338 156.216 140.119 1.00 16.65 ? 1027 VAL A CG1    1 
ATOM   6203 C  CG2    . VAL A 1 1027 ? 166.246 155.090 139.404 1.00 16.65 ? 1027 VAL A CG2    1 
ATOM   6204 N  N      . GLN A 1 1028 ? 167.697 159.109 137.674 1.00 18.94 ? 1028 GLN A N      1 
ATOM   6205 C  CA     . GLN A 1 1028 ? 168.827 159.951 137.314 1.00 18.94 ? 1028 GLN A CA     1 
ATOM   6206 C  C      . GLN A 1 1028 ? 168.512 161.428 137.458 1.00 18.94 ? 1028 GLN A C      1 
ATOM   6207 O  O      . GLN A 1 1028 ? 169.232 162.159 138.144 1.00 18.94 ? 1028 GLN A O      1 
ATOM   6208 C  CB     . GLN A 1 1028 ? 169.223 159.638 135.872 1.00 18.94 ? 1028 GLN A CB     1 
ATOM   6209 C  CG     . GLN A 1 1028 ? 170.367 160.434 135.339 1.00 18.94 ? 1028 GLN A CG     1 
ATOM   6210 C  CD     . GLN A 1 1028 ? 170.658 160.101 133.904 1.00 18.94 ? 1028 GLN A CD     1 
ATOM   6211 O  OE1    . GLN A 1 1028 ? 169.942 159.320 133.285 1.00 18.94 ? 1028 GLN A OE1    1 
ATOM   6212 N  NE2    . GLN A 1 1028 ? 171.718 160.681 133.364 1.00 18.94 ? 1028 GLN A NE2    1 
ATOM   6213 N  N      . TYR A 1 1029 ? 167.455 161.886 136.794 1.00 19.94 ? 1029 TYR A N      1 
ATOM   6214 C  CA     . TYR A 1 1029 ? 167.152 163.311 136.693 1.00 19.94 ? 1029 TYR A CA     1 
ATOM   6215 C  C      . TYR A 1 1029 ? 166.791 163.974 138.025 1.00 19.94 ? 1029 TYR A C      1 
ATOM   6216 O  O      . TYR A 1 1029 ? 167.273 165.088 138.252 1.00 19.94 ? 1029 TYR A O      1 
ATOM   6217 C  CB     . TYR A 1 1029 ? 166.063 163.520 135.637 1.00 19.94 ? 1029 TYR A CB     1 
ATOM   6218 C  CG     . TYR A 1 1029 ? 166.542 163.188 134.248 1.00 19.94 ? 1029 TYR A CG     1 
ATOM   6219 C  CD1    . TYR A 1 1029 ? 167.876 163.350 133.898 1.00 19.94 ? 1029 TYR A CD1    1 
ATOM   6220 C  CD2    . TYR A 1 1029 ? 165.685 162.630 133.317 1.00 19.94 ? 1029 TYR A CD2    1 
ATOM   6221 C  CE1    . TYR A 1 1029 ? 168.325 163.024 132.642 1.00 19.94 ? 1029 TYR A CE1    1 
ATOM   6222 C  CE2    . TYR A 1 1029 ? 166.128 162.288 132.062 1.00 19.94 ? 1029 TYR A CE2    1 
ATOM   6223 C  CZ     . TYR A 1 1029 ? 167.447 162.493 131.727 1.00 19.94 ? 1029 TYR A CZ     1 
ATOM   6224 O  OH     . TYR A 1 1029 ? 167.896 162.159 130.470 1.00 19.94 ? 1029 TYR A OH     1 
ATOM   6225 N  N      . PRO A 1 1030 ? 165.995 163.372 138.934 1.00 17.20 ? 1030 PRO A N      1 
ATOM   6226 C  CA     . PRO A 1 1030 ? 165.887 163.960 140.280 1.00 17.20 ? 1030 PRO A CA     1 
ATOM   6227 C  C      . PRO A 1 1030 ? 167.193 164.030 141.036 1.00 17.20 ? 1030 PRO A C      1 
ATOM   6228 O  O      . PRO A 1 1030 ? 167.410 164.985 141.792 1.00 17.20 ? 1030 PRO A O      1 
ATOM   6229 C  CB     . PRO A 1 1030 ? 164.913 163.021 140.991 1.00 17.20 ? 1030 PRO A CB     1 
ATOM   6230 C  CG     . PRO A 1 1030 ? 164.163 162.450 139.972 1.00 17.20 ? 1030 PRO A CG     1 
ATOM   6231 C  CD     . PRO A 1 1030 ? 165.002 162.288 138.800 1.00 17.20 ? 1030 PRO A CD     1 
ATOM   6232 N  N      . TYR A 1 1031 ? 168.078 163.058 140.828 1.00 17.54 ? 1031 TYR A N      1 
ATOM   6233 C  CA     . TYR A 1 1031 ? 169.342 163.035 141.544 1.00 17.54 ? 1031 TYR A CA     1 
ATOM   6234 C  C      . TYR A 1 1031 ? 170.262 164.159 141.095 1.00 17.54 ? 1031 TYR A C      1 
ATOM   6235 O  O      . TYR A 1 1031 ? 170.940 164.776 141.922 1.00 17.54 ? 1031 TYR A O      1 
ATOM   6236 C  CB     . TYR A 1 1031 ? 170.023 161.684 141.360 1.00 17.54 ? 1031 TYR A CB     1 
ATOM   6237 C  CG     . TYR A 1 1031 ? 171.305 161.590 142.129 1.00 17.54 ? 1031 TYR A CG     1 
ATOM   6238 C  CD1    . TYR A 1 1031 ? 171.292 161.444 143.506 1.00 17.54 ? 1031 TYR A CD1    1 
ATOM   6239 C  CD2    . TYR A 1 1031 ? 172.526 161.661 141.485 1.00 17.54 ? 1031 TYR A CD2    1 
ATOM   6240 C  CE1    . TYR A 1 1031 ? 172.457 161.369 144.219 1.00 17.54 ? 1031 TYR A CE1    1 
ATOM   6241 C  CE2    . TYR A 1 1031 ? 173.696 161.590 142.189 1.00 17.54 ? 1031 TYR A CE2    1 
ATOM   6242 C  CZ     . TYR A 1 1031 ? 173.658 161.438 143.555 1.00 17.54 ? 1031 TYR A CZ     1 
ATOM   6243 O  OH     . TYR A 1 1031 ? 174.831 161.364 144.266 1.00 17.54 ? 1031 TYR A OH     1 
ATOM   6244 N  N      . TRP A 1 1032 ? 170.316 164.440 139.794 1.00 30.66 ? 1032 TRP A N      1 
ATOM   6245 C  CA     . TRP A 1 1032 ? 171.202 165.510 139.364 1.00 30.66 ? 1032 TRP A CA     1 
ATOM   6246 C  C      . TRP A 1 1032 ? 170.571 166.870 139.561 1.00 30.66 ? 1032 TRP A C      1 
ATOM   6247 O  O      . TRP A 1 1032 ? 171.285 167.829 139.862 1.00 30.66 ? 1032 TRP A O      1 
ATOM   6248 C  CB     . TRP A 1 1032 ? 171.634 165.343 137.909 1.00 30.66 ? 1032 TRP A CB     1 
ATOM   6249 C  CG     . TRP A 1 1032 ? 172.424 164.106 137.648 1.00 30.66 ? 1032 TRP A CG     1 
ATOM   6250 C  CD1    . TRP A 1 1032 ? 172.070 163.079 136.844 1.00 30.66 ? 1032 TRP A CD1    1 
ATOM   6251 C  CD2    . TRP A 1 1032 ? 173.661 163.721 138.267 1.00 30.66 ? 1032 TRP A CD2    1 
ATOM   6252 N  NE1    . TRP A 1 1032 ? 173.026 162.101 136.870 1.00 30.66 ? 1032 TRP A NE1    1 
ATOM   6253 C  CE2    . TRP A 1 1032 ? 174.010 162.467 137.746 1.00 30.66 ? 1032 TRP A CE2    1 
ATOM   6254 C  CE3    . TRP A 1 1032 ? 174.516 164.326 139.193 1.00 30.66 ? 1032 TRP A CE3    1 
ATOM   6255 C  CZ2    . TRP A 1 1032 ? 175.171 161.805 138.116 1.00 30.66 ? 1032 TRP A CZ2    1 
ATOM   6256 C  CZ3    . TRP A 1 1032 ? 175.659 163.668 139.561 1.00 30.66 ? 1032 TRP A CZ3    1 
ATOM   6257 C  CH2    . TRP A 1 1032 ? 175.979 162.422 139.025 1.00 30.66 ? 1032 TRP A CH2    1 
ATOM   6258 N  N      . GLN A 1 1033 ? 169.245 166.966 139.421 1.00 18.34 ? 1033 GLN A N      1 
ATOM   6259 C  CA     . GLN A 1 1033 ? 168.547 168.198 139.773 1.00 18.34 ? 1033 GLN A CA     1 
ATOM   6260 C  C      . GLN A 1 1033 ? 168.712 168.547 141.243 1.00 18.34 ? 1033 GLN A C      1 
ATOM   6261 O  O      . GLN A 1 1033 ? 168.751 169.727 141.592 1.00 18.34 ? 1033 GLN A O      1 
ATOM   6262 C  CB     . GLN A 1 1033 ? 167.071 168.079 139.405 1.00 18.34 ? 1033 GLN A CB     1 
ATOM   6263 C  CG     . GLN A 1 1033 ? 166.802 168.225 137.927 1.00 18.34 ? 1033 GLN A CG     1 
ATOM   6264 C  CD     . GLN A 1 1033 ? 165.392 167.859 137.565 1.00 18.34 ? 1033 GLN A CD     1 
ATOM   6265 O  OE1    . GLN A 1 1033 ? 164.641 167.377 138.403 1.00 18.34 ? 1033 GLN A OE1    1 
ATOM   6266 N  NE2    . GLN A 1 1033 ? 165.017 168.091 136.319 1.00 18.34 ? 1033 GLN A NE2    1 
ATOM   6267 N  N      . MET A 1 1034 ? 168.856 167.537 142.102 1.00 20.13 ? 1034 MET A N      1 
ATOM   6268 C  CA     . MET A 1 1034 ? 169.094 167.747 143.527 1.00 20.13 ? 1034 MET A CA     1 
ATOM   6269 C  C      . MET A 1 1034 ? 170.399 168.493 143.798 1.00 20.13 ? 1034 MET A C      1 
ATOM   6270 O  O      . MET A 1 1034 ? 170.497 169.239 144.777 1.00 20.13 ? 1034 MET A O      1 
ATOM   6271 C  CB     . MET A 1 1034 ? 169.100 166.385 144.212 1.00 20.13 ? 1034 MET A CB     1 
ATOM   6272 C  CG     . MET A 1 1034 ? 169.200 166.389 145.695 1.00 20.13 ? 1034 MET A CG     1 
ATOM   6273 S  SD     . MET A 1 1034 ? 169.213 164.694 146.293 1.00 20.13 ? 1034 MET A SD     1 
ATOM   6274 C  CE     . MET A 1 1034 ? 170.876 164.216 145.851 1.00 20.13 ? 1034 MET A CE     1 
ATOM   6275 N  N      . TYR A 1 1035 ? 171.398 168.325 142.937 1.00 21.79 ? 1035 TYR A N      1 
ATOM   6276 C  CA     . TYR A 1 1035 ? 172.672 169.023 143.031 1.00 21.79 ? 1035 TYR A CA     1 
ATOM   6277 C  C      . TYR A 1 1035 ? 172.672 170.355 142.299 1.00 21.79 ? 1035 TYR A C      1 
ATOM   6278 O  O      . TYR A 1 1035 ? 173.747 170.874 141.981 1.00 21.79 ? 1035 TYR A O      1 
ATOM   6279 C  CB     . TYR A 1 1035 ? 173.781 168.128 142.484 1.00 21.79 ? 1035 TYR A CB     1 
ATOM   6280 C  CG     . TYR A 1 1035 ? 174.087 166.972 143.389 1.00 21.79 ? 1035 TYR A CG     1 
ATOM   6281 C  CD1    . TYR A 1 1035 ? 173.963 167.095 144.764 1.00 21.79 ? 1035 TYR A CD1    1 
ATOM   6282 C  CD2    . TYR A 1 1035 ? 174.393 165.731 142.871 1.00 21.79 ? 1035 TYR A CD2    1 
ATOM   6283 C  CE1    . TYR A 1 1035 ? 174.214 166.031 145.599 1.00 21.79 ? 1035 TYR A CE1    1 
ATOM   6284 C  CE2    . TYR A 1 1035 ? 174.635 164.663 143.697 1.00 21.79 ? 1035 TYR A CE2    1 
ATOM   6285 C  CZ     . TYR A 1 1035 ? 174.540 164.817 145.059 1.00 21.79 ? 1035 TYR A CZ     1 
ATOM   6286 O  OH     . TYR A 1 1035 ? 174.782 163.750 145.885 1.00 21.79 ? 1035 TYR A OH     1 
ATOM   6287 N  N      . GLY A 1 1036 ? 171.499 170.915 142.015 1.00 20.46 ? 1036 GLY A N      1 
ATOM   6288 C  CA     . GLY A 1 1036 ? 171.403 172.164 141.302 1.00 20.46 ? 1036 GLY A CA     1 
ATOM   6289 C  C      . GLY A 1 1036 ? 171.527 172.067 139.801 1.00 20.46 ? 1036 GLY A C      1 
ATOM   6290 O  O      . GLY A 1 1036 ? 171.337 173.079 139.118 1.00 20.46 ? 1036 GLY A O      1 
ATOM   6291 N  N      . GLU A 1 1037 ? 171.840 170.891 139.252 1.00 21.04 ? 1037 GLU A N      1 
ATOM   6292 C  CA     . GLU A 1 1037 ? 171.892 170.698 137.802 1.00 21.04 ? 1037 GLU A CA     1 
ATOM   6293 C  C      . GLU A 1 1037 ? 170.455 170.638 137.293 1.00 21.04 ? 1037 GLU A C      1 
ATOM   6294 O  O      . GLU A 1 1037 ? 169.875 169.577 137.059 1.00 21.04 ? 1037 GLU A O      1 
ATOM   6295 C  CB     . GLU A 1 1037 ? 172.694 169.448 137.443 1.00 21.04 ? 1037 GLU A CB     1 
ATOM   6296 C  CG     . GLU A 1 1037 ? 172.852 169.149 135.949 1.00 21.04 ? 1037 GLU A CG     1 
ATOM   6297 C  CD     . GLU A 1 1037 ? 173.696 170.164 135.211 1.00 21.04 ? 1037 GLU A CD     1 
ATOM   6298 O  OE1    . GLU A 1 1037 ? 174.588 170.780 135.833 1.00 21.04 ? 1037 GLU A OE1    1 
ATOM   6299 O  OE2    . GLU A 1 1037 ? 173.464 170.346 133.999 1.00 21.04 ? 1037 GLU A OE2    1 
ATOM   6300 N  N      . LEU A 1 1038 ? 169.863 171.820 137.157 1.00 19.60 ? 1038 LEU A N      1 
ATOM   6301 C  CA     . LEU A 1 1038 ? 168.500 171.932 136.672 1.00 19.60 ? 1038 LEU A CA     1 
ATOM   6302 C  C      . LEU A 1 1038 ? 168.482 171.610 135.191 1.00 19.60 ? 1038 LEU A C      1 
ATOM   6303 O  O      . LEU A 1 1038 ? 169.276 172.154 134.418 1.00 19.60 ? 1038 LEU A O      1 
ATOM   6304 C  CB     . LEU A 1 1038 ? 167.970 173.345 136.897 1.00 19.60 ? 1038 LEU A CB     1 
ATOM   6305 C  CG     . LEU A 1 1038 ? 167.906 173.919 138.305 1.00 19.60 ? 1038 LEU A CG     1 
ATOM   6306 C  CD1    . LEU A 1 1038 ? 167.445 175.356 138.230 1.00 19.60 ? 1038 LEU A CD1    1 
ATOM   6307 C  CD2    . LEU A 1 1038 ? 166.989 173.109 139.175 1.00 19.60 ? 1038 LEU A CD2    1 
ATOM   6308 N  N      . PHE A 1 1039 ? 167.598 170.714 134.792 1.00 20.30 ? 1039 PHE A N      1 
ATOM   6309 C  CA     . PHE A 1 1039 ? 167.453 170.398 133.375 1.00 20.30 ? 1039 PHE A CA     1 
ATOM   6310 C  C      . PHE A 1 1039 ? 166.350 171.228 132.747 1.00 20.30 ? 1039 PHE A C      1 
ATOM   6311 O  O      . PHE A 1 1039 ? 165.485 170.694 132.073 1.00 20.30 ? 1039 PHE A O      1 
ATOM   6312 C  CB     . PHE A 1 1039 ? 167.195 168.911 133.201 1.00 20.30 ? 1039 PHE A CB     1 
ATOM   6313 C  CG     . PHE A 1 1039 ? 168.367 168.062 133.567 1.00 20.30 ? 1039 PHE A CG     1 
ATOM   6314 C  CD1    . PHE A 1 1039 ? 169.372 167.823 132.649 1.00 20.30 ? 1039 PHE A CD1    1 
ATOM   6315 C  CD2    . PHE A 1 1039 ? 168.486 167.538 134.838 1.00 20.30 ? 1039 PHE A CD2    1 
ATOM   6316 C  CE1    . PHE A 1 1039 ? 170.457 167.049 132.986 1.00 20.30 ? 1039 PHE A CE1    1 
ATOM   6317 C  CE2    . PHE A 1 1039 ? 169.571 166.773 135.183 1.00 20.30 ? 1039 PHE A CE2    1 
ATOM   6318 C  CZ     . PHE A 1 1039 ? 170.557 166.528 134.257 1.00 20.30 ? 1039 PHE A CZ     1 
ATOM   6319 N  N      . LEU A 1 1040 ? 166.413 172.550 132.940 1.00 20.15 ? 1040 LEU A N      1 
ATOM   6320 C  CA     . LEU A 1 1040 ? 165.303 173.435 132.593 1.00 20.15 ? 1040 LEU A CA     1 
ATOM   6321 C  C      . LEU A 1 1040 ? 165.078 173.498 131.094 1.00 20.15 ? 1040 LEU A C      1 
ATOM   6322 O  O      . LEU A 1 1040 ? 163.943 173.415 130.629 1.00 20.15 ? 1040 LEU A O      1 
ATOM   6323 C  CB     . LEU A 1 1040 ? 165.553 174.838 133.141 1.00 20.15 ? 1040 LEU A CB     1 
ATOM   6324 C  CG     . LEU A 1 1040 ? 165.351 175.105 134.623 1.00 20.15 ? 1040 LEU A CG     1 
ATOM   6325 C  CD1    . LEU A 1 1040 ? 165.858 176.483 134.940 1.00 20.15 ? 1040 LEU A CD1    1 
ATOM   6326 C  CD2    . LEU A 1 1040 ? 163.881 175.018 134.908 1.00 20.15 ? 1040 LEU A CD2    1 
ATOM   6327 N  N      . ASP A 1 1041 ? 166.148 173.640 130.317 1.00 24.07 ? 1041 ASP A N      1 
ATOM   6328 C  CA     . ASP A 1 1041 ? 165.983 173.653 128.870 1.00 24.07 ? 1041 ASP A CA     1 
ATOM   6329 C  C      . ASP A 1 1041 ? 165.616 172.268 128.361 1.00 24.07 ? 1041 ASP A C      1 
ATOM   6330 O  O      . ASP A 1 1041 ? 164.922 172.140 127.350 1.00 24.07 ? 1041 ASP A O      1 
ATOM   6331 C  CB     . ASP A 1 1041 ? 167.262 174.167 128.211 1.00 24.07 ? 1041 ASP A CB     1 
ATOM   6332 C  CG     . ASP A 1 1041 ? 167.056 174.565 126.765 1.00 24.07 ? 1041 ASP A CG     1 
ATOM   6333 O  OD1    . ASP A 1 1041 ? 166.453 175.631 126.524 1.00 24.07 ? 1041 ASP A OD1    1 
ATOM   6334 O  OD2    . ASP A 1 1041 ? 167.507 173.828 125.866 1.00 24.07 ? 1041 ASP A OD2    1 
ATOM   6335 N  N      . GLU A 1 1042 ? 166.029 171.230 129.085 1.00 22.84 ? 1042 GLU A N      1 
ATOM   6336 C  CA     . GLU A 1 1042 ? 165.693 169.861 128.723 1.00 22.84 ? 1042 GLU A CA     1 
ATOM   6337 C  C      . GLU A 1 1042 ? 164.232 169.541 129.022 1.00 22.84 ? 1042 GLU A C      1 
ATOM   6338 O  O      . GLU A 1 1042 ? 163.500 169.079 128.143 1.00 22.84 ? 1042 GLU A O      1 
ATOM   6339 C  CB     . GLU A 1 1042 ? 166.617 168.900 129.467 1.00 22.84 ? 1042 GLU A CB     1 
ATOM   6340 C  CG     . GLU A 1 1042 ? 168.058 168.852 128.974 1.00 22.84 ? 1042 GLU A CG     1 
ATOM   6341 C  CD     . GLU A 1 1042 ? 168.945 169.960 129.521 1.00 22.84 ? 1042 GLU A CD     1 
ATOM   6342 O  OE1    . GLU A 1 1042 ? 168.456 170.823 130.272 1.00 22.84 ? 1042 GLU A OE1    1 
ATOM   6343 O  OE2    . GLU A 1 1042 ? 170.153 169.955 129.215 1.00 22.84 ? 1042 GLU A OE2    1 
ATOM   6344 N  N      . ILE A 1 1043 ? 163.784 169.785 130.260 1.00 19.28 ? 1043 ILE A N      1 
ATOM   6345 C  CA     . ILE A 1 1043 ? 162.465 169.316 130.683 1.00 19.28 ? 1043 ILE A CA     1 
ATOM   6346 C  C      . ILE A 1 1043 ? 161.333 170.249 130.283 1.00 19.28 ? 1043 ILE A C      1 
ATOM   6347 O  O      . ILE A 1 1043 ? 160.167 169.930 130.543 1.00 19.28 ? 1043 ILE A O      1 
ATOM   6348 C  CB     . ILE A 1 1043 ? 162.377 169.101 132.209 1.00 19.28 ? 1043 ILE A CB     1 
ATOM   6349 C  CG1    . ILE A 1 1043 ? 162.410 170.429 132.963 1.00 19.28 ? 1043 ILE A CG1    1 
ATOM   6350 C  CG2    . ILE A 1 1043 ? 163.478 168.165 132.694 1.00 19.28 ? 1043 ILE A CG2    1 
ATOM   6351 C  CD1    . ILE A 1 1043 ? 162.117 170.295 134.424 1.00 19.28 ? 1043 ILE A CD1    1 
ATOM   6352 N  N      . GLN A 1 1044 ? 161.627 171.394 129.669 1.00 22.19 ? 1044 GLN A N      1 
ATOM   6353 C  CA     . GLN A 1 1044 ? 160.599 172.286 129.147 1.00 22.19 ? 1044 GLN A CA     1 
ATOM   6354 C  C      . GLN A 1 1044 ? 160.351 172.085 127.667 1.00 22.19 ? 1044 GLN A C      1 
ATOM   6355 O  O      . GLN A 1 1044 ? 159.728 172.940 127.031 1.00 22.19 ? 1044 GLN A O      1 
ATOM   6356 C  CB     . GLN A 1 1044 ? 160.969 173.742 129.398 1.00 22.19 ? 1044 GLN A CB     1 
ATOM   6357 C  CG     . GLN A 1 1044 ? 160.837 174.178 130.826 1.00 22.19 ? 1044 GLN A CG     1 
ATOM   6358 C  CD     . GLN A 1 1044 ? 161.455 175.532 131.065 1.00 22.19 ? 1044 GLN A CD     1 
ATOM   6359 O  OE1    . GLN A 1 1044 ? 162.055 176.115 130.167 1.00 22.19 ? 1044 GLN A OE1    1 
ATOM   6360 N  NE2    . GLN A 1 1044 ? 161.327 176.036 132.281 1.00 22.19 ? 1044 GLN A NE2    1 
ATOM   6361 N  N      . GLY A 1 1045 ? 160.828 170.989 127.102 1.00 23.57 ? 1045 GLY A N      1 
ATOM   6362 C  CA     . GLY A 1 1045 ? 160.525 170.629 125.746 1.00 23.57 ? 1045 GLY A CA     1 
ATOM   6363 C  C      . GLY A 1 1045 ? 161.625 170.909 124.752 1.00 23.57 ? 1045 GLY A C      1 
ATOM   6364 O  O      . GLY A 1 1045 ? 161.626 170.309 123.674 1.00 23.57 ? 1045 GLY A O      1 
ATOM   6365 N  N      . GLU A 1 1046 ? 162.554 171.801 125.075 1.00 26.33 ? 1046 GLU A N      1 
ATOM   6366 C  CA     . GLU A 1 1046 ? 163.695 172.003 124.200 1.00 26.33 ? 1046 GLU A CA     1 
ATOM   6367 C  C      . GLU A 1 1046 ? 164.708 170.890 124.437 1.00 26.33 ? 1046 GLU A C      1 
ATOM   6368 O  O      . GLU A 1 1046 ? 164.545 170.045 125.324 1.00 26.33 ? 1046 GLU A O      1 
ATOM   6369 C  CB     . GLU A 1 1046 ? 164.306 173.385 124.409 1.00 26.33 ? 1046 GLU A CB     1 
ATOM   6370 C  CG     . GLU A 1 1046 ? 163.394 174.519 123.996 1.00 26.33 ? 1046 GLU A CG     1 
ATOM   6371 C  CD     . GLU A 1 1046 ? 162.494 174.982 125.119 1.00 26.33 ? 1046 GLU A CD     1 
ATOM   6372 O  OE1    . GLU A 1 1046 ? 162.697 174.535 126.265 1.00 26.33 ? 1046 GLU A OE1    1 
ATOM   6373 O  OE2    . GLU A 1 1046 ? 161.571 175.776 124.851 1.00 26.33 ? 1046 GLU A OE2    1 
ATOM   6374 N  N      . LYS A 1 1047 ? 165.780 170.915 123.647 1.00 28.73 ? 1047 LYS A N      1 
ATOM   6375 C  CA     . LYS A 1 1047 ? 166.712 169.810 123.430 1.00 28.73 ? 1047 LYS A CA     1 
ATOM   6376 C  C      . LYS A 1 1047 ? 165.990 168.486 123.173 1.00 28.73 ? 1047 LYS A C      1 
ATOM   6377 O  O      . LYS A 1 1047 ? 166.087 167.577 124.004 1.00 28.73 ? 1047 LYS A O      1 
ATOM   6378 C  CB     . LYS A 1 1047 ? 167.654 169.666 124.629 1.00 28.73 ? 1047 LYS A CB     1 
ATOM   6379 C  CG     . LYS A 1 1047 ? 168.551 170.865 124.852 1.00 28.73 ? 1047 LYS A CG     1 
ATOM   6380 C  CD     . LYS A 1 1047 ? 169.458 170.656 126.040 1.00 28.73 ? 1047 LYS A CD     1 
ATOM   6381 C  CE     . LYS A 1 1047 ? 170.322 171.874 126.292 1.00 28.73 ? 1047 LYS A CE     1 
ATOM   6382 N  NZ     . LYS A 1 1047 ? 171.223 171.673 127.460 1.00 28.73 ? 1047 LYS A NZ     1 
ATOM   6383 N  N      . PRO A 1 1048 ? 165.258 168.319 122.063 1.00 31.13 ? 1048 PRO A N      1 
ATOM   6384 C  CA     . PRO A 1 1048 ? 164.532 167.061 121.862 1.00 31.13 ? 1048 PRO A CA     1 
ATOM   6385 C  C      . PRO A 1 1048 ? 165.403 165.919 121.376 1.00 31.13 ? 1048 PRO A C      1 
ATOM   6386 O  O      . PRO A 1 1048 ? 164.925 164.778 121.325 1.00 31.13 ? 1048 PRO A O      1 
ATOM   6387 C  CB     . PRO A 1 1048 ? 163.494 167.427 120.795 1.00 31.13 ? 1048 PRO A CB     1 
ATOM   6388 C  CG     . PRO A 1 1048 ? 163.475 168.913 120.746 1.00 31.13 ? 1048 PRO A CG     1 
ATOM   6389 C  CD     . PRO A 1 1048 ? 164.884 169.288 121.021 1.00 31.13 ? 1048 PRO A CD     1 
ATOM   6390 N  N      . LYS A 1 1049 ? 166.653 166.188 121.002 1.00 34.72 ? 1049 LYS A N      1 
ATOM   6391 C  CA     . LYS A 1 1049 ? 167.535 165.137 120.514 1.00 34.72 ? 1049 LYS A CA     1 
ATOM   6392 C  C      . LYS A 1 1049 ? 168.124 164.334 121.667 1.00 34.72 ? 1049 LYS A C      1 
ATOM   6393 O  O      . LYS A 1 1049 ? 167.928 163.118 121.754 1.00 34.72 ? 1049 LYS A O      1 
ATOM   6394 C  CB     . LYS A 1 1049 ? 168.649 165.745 119.660 1.00 34.72 ? 1049 LYS A CB     1 
ATOM   6395 C  CG     . LYS A 1 1049 ? 168.160 166.529 118.457 1.00 34.72 ? 1049 LYS A CG     1 
ATOM   6396 C  CD     . LYS A 1 1049 ? 167.457 165.635 117.450 1.00 34.72 ? 1049 LYS A CD     1 
ATOM   6397 C  CE     . LYS A 1 1049 ? 167.156 166.392 116.167 1.00 34.72 ? 1049 LYS A CE     1 
ATOM   6398 N  NZ     . LYS A 1 1049 ? 166.131 167.449 116.374 1.00 34.72 ? 1049 LYS A NZ     1 
ATOM   6399 N  N      . GLU A 1 1050 ? 168.848 164.999 122.564 1.00 32.52 ? 1050 GLU A N      1 
ATOM   6400 C  CA     . GLU A 1 1050 ? 169.563 164.310 123.627 1.00 32.52 ? 1050 GLU A CA     1 
ATOM   6401 C  C      . GLU A 1 1050 ? 168.748 164.139 124.900 1.00 32.52 ? 1050 GLU A C      1 
ATOM   6402 O  O      . GLU A 1 1050 ? 169.186 163.415 125.799 1.00 32.52 ? 1050 GLU A O      1 
ATOM   6403 C  CB     . GLU A 1 1050 ? 170.870 165.042 123.950 1.00 32.52 ? 1050 GLU A CB     1 
ATOM   6404 C  CG     . GLU A 1 1050 ? 170.706 166.450 124.492 1.00 32.52 ? 1050 GLU A CG     1 
ATOM   6405 C  CD     . GLU A 1 1050 ? 170.720 167.502 123.399 1.00 32.52 ? 1050 GLU A CD     1 
ATOM   6406 O  OE1    . GLU A 1 1050 ? 170.544 167.144 122.215 1.00 32.52 ? 1050 GLU A OE1    1 
ATOM   6407 O  OE2    . GLU A 1 1050 ? 170.923 168.690 123.726 1.00 32.52 ? 1050 GLU A OE2    1 
ATOM   6408 N  N      . PHE A 1 1051 ? 167.584 164.773 125.004 1.00 23.68 ? 1051 PHE A N      1 
ATOM   6409 C  CA     . PHE A 1 1051 ? 166.684 164.538 126.123 1.00 23.68 ? 1051 PHE A CA     1 
ATOM   6410 C  C      . PHE A 1 1051 ? 165.427 163.801 125.693 1.00 23.68 ? 1051 PHE A C      1 
ATOM   6411 O  O      . PHE A 1 1051 ? 165.102 162.750 126.250 1.00 23.68 ? 1051 PHE A O      1 
ATOM   6412 C  CB     . PHE A 1 1051 ? 166.309 165.864 126.792 1.00 23.68 ? 1051 PHE A CB     1 
ATOM   6413 C  CG     . PHE A 1 1051 ? 165.540 165.702 128.064 1.00 23.68 ? 1051 PHE A CG     1 
ATOM   6414 C  CD1    . PHE A 1 1051 ? 166.188 165.345 129.228 1.00 23.68 ? 1051 PHE A CD1    1 
ATOM   6415 C  CD2    . PHE A 1 1051 ? 164.172 165.904 128.101 1.00 23.68 ? 1051 PHE A CD2    1 
ATOM   6416 C  CE1    . PHE A 1 1051 ? 165.493 165.208 130.401 1.00 23.68 ? 1051 PHE A CE1    1 
ATOM   6417 C  CE2    . PHE A 1 1051 ? 163.476 165.758 129.275 1.00 23.68 ? 1051 PHE A CE2    1 
ATOM   6418 C  CZ     . PHE A 1 1051 ? 164.137 165.405 130.423 1.00 23.68 ? 1051 PHE A CZ     1 
ATOM   6419 N  N      . GLY A 1 1052 ? 164.720 164.320 124.708 1.00 22.37 ? 1052 GLY A N      1 
ATOM   6420 C  CA     . GLY A 1 1052 ? 163.541 163.672 124.169 1.00 22.37 ? 1052 GLY A CA     1 
ATOM   6421 C  C      . GLY A 1 1052 ? 162.429 164.673 123.935 1.00 22.37 ? 1052 GLY A C      1 
ATOM   6422 O  O      . GLY A 1 1052 ? 162.421 165.779 124.472 1.00 22.37 ? 1052 GLY A O      1 
ATOM   6423 N  N      . GLU A 1 1053 ? 161.477 164.277 123.094 1.00 21.17 ? 1053 GLU A N      1 
ATOM   6424 C  CA     . GLU A 1 1053 ? 160.265 165.057 122.877 1.00 21.17 ? 1053 GLU A CA     1 
ATOM   6425 C  C      . GLU A 1 1053 ? 159.398 164.993 124.127 1.00 21.17 ? 1053 GLU A C      1 
ATOM   6426 O  O      . GLU A 1 1053 ? 158.756 163.974 124.395 1.00 21.17 ? 1053 GLU A O      1 
ATOM   6427 C  CB     . GLU A 1 1053 ? 159.498 164.529 121.668 1.00 21.17 ? 1053 GLU A CB     1 
ATOM   6428 C  CG     . GLU A 1 1053 ? 160.128 164.778 120.308 1.00 21.17 ? 1053 GLU A CG     1 
ATOM   6429 C  CD     . GLU A 1 1053 ? 160.036 166.227 119.872 1.00 21.17 ? 1053 GLU A CD     1 
ATOM   6430 O  OE1    . GLU A 1 1053 ? 159.116 166.930 120.336 1.00 21.17 ? 1053 GLU A OE1    1 
ATOM   6431 O  OE2    . GLU A 1 1053 ? 160.852 166.652 119.028 1.00 21.17 ? 1053 GLU A OE2    1 
ATOM   6432 N  N      . VAL A 1 1054 ? 159.382 166.074 124.888 1.00 18.15 ? 1054 VAL A N      1 
ATOM   6433 C  CA     . VAL A 1 1054 ? 158.547 166.184 126.076 1.00 18.15 ? 1054 VAL A CA     1 
ATOM   6434 C  C      . VAL A 1 1054 ? 157.118 166.477 125.637 1.00 18.15 ? 1054 VAL A C      1 
ATOM   6435 O  O      . VAL A 1 1054 ? 156.896 167.162 124.633 1.00 18.15 ? 1054 VAL A O      1 
ATOM   6436 C  CB     . VAL A 1 1054 ? 159.120 167.272 127.008 1.00 18.15 ? 1054 VAL A CB     1 
ATOM   6437 C  CG1    . VAL A 1 1054 ? 158.291 167.473 128.261 1.00 18.15 ? 1054 VAL A CG1    1 
ATOM   6438 C  CG2    . VAL A 1 1054 ? 160.537 166.929 127.385 1.00 18.15 ? 1054 VAL A CG2    1 
ATOM   6439 N  N      . ASP A 1 1055 ? 156.151 165.886 126.338 1.00 19.81 ? 1055 ASP A N      1 
ATOM   6440 C  CA     . ASP A 1 1055 ? 154.743 166.177 126.109 1.00 19.81 ? 1055 ASP A CA     1 
ATOM   6441 C  C      . ASP A 1 1055 ? 154.466 167.659 126.353 1.00 19.81 ? 1055 ASP A C      1 
ATOM   6442 O  O      . ASP A 1 1055 ? 154.959 168.219 127.337 1.00 19.81 ? 1055 ASP A O      1 
ATOM   6443 C  CB     . ASP A 1 1055 ? 153.880 165.326 127.039 1.00 19.81 ? 1055 ASP A CB     1 
ATOM   6444 C  CG     . ASP A 1 1055 ? 152.406 165.447 126.745 1.00 19.81 ? 1055 ASP A CG     1 
ATOM   6445 O  OD1    . ASP A 1 1055 ? 151.959 164.914 125.712 1.00 19.81 ? 1055 ASP A OD1    1 
ATOM   6446 O  OD2    . ASP A 1 1055 ? 151.685 166.052 127.560 1.00 19.81 ? 1055 ASP A OD2    1 
ATOM   6447 N  N      . PRO A 1 1056 ? 153.702 168.322 125.473 1.00 20.37 ? 1056 PRO A N      1 
ATOM   6448 C  CA     . PRO A 1 1056 ? 153.513 169.774 125.611 1.00 20.37 ? 1056 PRO A CA     1 
ATOM   6449 C  C      . PRO A 1 1056 ? 152.723 170.179 126.837 1.00 20.37 ? 1056 PRO A C      1 
ATOM   6450 O  O      . PRO A 1 1056 ? 152.939 171.279 127.358 1.00 20.37 ? 1056 PRO A O      1 
ATOM   6451 C  CB     . PRO A 1 1056 ? 152.771 170.152 124.323 1.00 20.37 ? 1056 PRO A CB     1 
ATOM   6452 C  CG     . PRO A 1 1056 ? 153.057 169.058 123.383 1.00 20.37 ? 1056 PRO A CG     1 
ATOM   6453 C  CD     . PRO A 1 1056 ? 153.123 167.829 124.218 1.00 20.37 ? 1056 PRO A CD     1 
ATOM   6454 N  N      . ASP A 1 1057 ? 151.815 169.331 127.315 1.00 20.68 ? 1057 ASP A N      1 
ATOM   6455 C  CA     . ASP A 1 1057 ? 151.152 169.604 128.580 1.00 20.68 ? 1057 ASP A CA     1 
ATOM   6456 C  C      . ASP A 1 1057 ? 152.046 169.297 129.769 1.00 20.68 ? 1057 ASP A C      1 
ATOM   6457 O  O      . ASP A 1 1057 ? 151.778 169.778 130.872 1.00 20.68 ? 1057 ASP A O      1 
ATOM   6458 C  CB     . ASP A 1 1057 ? 149.848 168.814 128.674 1.00 20.68 ? 1057 ASP A CB     1 
ATOM   6459 C  CG     . ASP A 1 1057 ? 148.778 169.355 127.749 1.00 20.68 ? 1057 ASP A CG     1 
ATOM   6460 O  OD1    . ASP A 1 1057 ? 148.775 170.576 127.496 1.00 20.68 ? 1057 ASP A OD1    1 
ATOM   6461 O  OD2    . ASP A 1 1057 ? 147.944 168.564 127.265 1.00 20.68 ? 1057 ASP A OD2    1 
ATOM   6462 N  N      . GLY A 1 1058 ? 153.106 168.531 129.566 1.00 17.75 ? 1058 GLY A N      1 
ATOM   6463 C  CA     . GLY A 1 1058 ? 154.114 168.315 130.574 1.00 17.75 ? 1058 GLY A CA     1 
ATOM   6464 C  C      . GLY A 1 1058 ? 155.298 169.245 130.470 1.00 17.75 ? 1058 GLY A C      1 
ATOM   6465 O  O      . GLY A 1 1058 ? 156.274 169.056 131.198 1.00 17.75 ? 1058 GLY A O      1 
ATOM   6466 N  N      . ARG A 1 1059 ? 155.251 170.237 129.579 1.00 19.31 ? 1059 ARG A N      1 
ATOM   6467 C  CA     . ARG A 1 1059 ? 156.308 171.233 129.463 1.00 19.31 ? 1059 ARG A CA     1 
ATOM   6468 C  C      . ARG A 1 1059 ? 156.115 172.413 130.397 1.00 19.31 ? 1059 ARG A C      1 
ATOM   6469 O  O      . ARG A 1 1059 ? 157.083 173.129 130.676 1.00 19.31 ? 1059 ARG A O      1 
ATOM   6470 C  CB     . ARG A 1 1059 ? 156.402 171.751 128.027 1.00 19.31 ? 1059 ARG A CB     1 
ATOM   6471 C  CG     . ARG A 1 1059 ? 156.981 170.758 127.063 1.00 19.31 ? 1059 ARG A CG     1 
ATOM   6472 C  CD     . ARG A 1 1059 ? 156.923 171.253 125.644 1.00 19.31 ? 1059 ARG A CD     1 
ATOM   6473 N  NE     . ARG A 1 1059 ? 157.328 170.202 124.721 1.00 19.31 ? 1059 ARG A NE     1 
ATOM   6474 C  CZ     . ARG A 1 1059 ? 157.272 170.302 123.401 1.00 19.31 ? 1059 ARG A CZ     1 
ATOM   6475 N  NH1    . ARG A 1 1059 ? 156.821 171.412 122.842 1.00 19.31 ? 1059 ARG A NH1    1 
ATOM   6476 N  NH2    . ARG A 1 1059 ? 157.660 169.290 122.642 1.00 19.31 ? 1059 ARG A NH2    1 
ATOM   6477 N  N      . TRP A 1 1060 ? 154.893 172.647 130.865 1.00 16.85 ? 1060 TRP A N      1 
ATOM   6478 C  CA     . TRP A 1 1060 ? 154.644 173.655 131.882 1.00 16.85 ? 1060 TRP A CA     1 
ATOM   6479 C  C      . TRP A 1 1060 ? 154.547 173.075 133.281 1.00 16.85 ? 1060 TRP A C      1 
ATOM   6480 O  O      . TRP A 1 1060 ? 154.858 173.772 134.250 1.00 16.85 ? 1060 TRP A O      1 
ATOM   6481 C  CB     . TRP A 1 1060 ? 153.362 174.436 131.567 1.00 16.85 ? 1060 TRP A CB     1 
ATOM   6482 C  CG     . TRP A 1 1060 ? 152.129 173.593 131.443 1.00 16.85 ? 1060 TRP A CG     1 
ATOM   6483 C  CD1    . TRP A 1 1060 ? 151.632 173.052 130.303 1.00 16.85 ? 1060 TRP A CD1    1 
ATOM   6484 C  CD2    . TRP A 1 1060 ? 151.233 173.210 132.494 1.00 16.85 ? 1060 TRP A CD2    1 
ATOM   6485 N  NE1    . TRP A 1 1060 ? 150.489 172.345 130.572 1.00 16.85 ? 1060 TRP A NE1    1 
ATOM   6486 C  CE2    . TRP A 1 1060 ? 150.224 172.424 131.912 1.00 16.85 ? 1060 TRP A CE2    1 
ATOM   6487 C  CE3    . TRP A 1 1060 ? 151.194 173.444 133.870 1.00 16.85 ? 1060 TRP A CE3    1 
ATOM   6488 C  CZ2    . TRP A 1 1060 ? 149.185 171.876 132.656 1.00 16.85 ? 1060 TRP A CZ2    1 
ATOM   6489 C  CZ3    . TRP A 1 1060 ? 150.166 172.899 134.607 1.00 16.85 ? 1060 TRP A CZ3    1 
ATOM   6490 C  CH2    . TRP A 1 1060 ? 149.174 172.125 133.999 1.00 16.85 ? 1060 TRP A CH2    1 
ATOM   6491 N  N      . LEU A 1 1061 ? 154.130 171.818 133.411 1.00 14.56 ? 1061 LEU A N      1 
ATOM   6492 C  CA     . LEU A 1 1061 ? 154.032 171.184 134.716 1.00 14.56 ? 1061 LEU A CA     1 
ATOM   6493 C  C      . LEU A 1 1061 ? 155.382 170.700 135.219 1.00 14.56 ? 1061 LEU A C      1 
ATOM   6494 O  O      . LEU A 1 1061 ? 155.575 170.580 136.433 1.00 14.56 ? 1061 LEU A O      1 
ATOM   6495 C  CB     . LEU A 1 1061 ? 153.031 170.026 134.647 1.00 14.56 ? 1061 LEU A CB     1 
ATOM   6496 C  CG     . LEU A 1 1061 ? 152.640 169.285 135.924 1.00 14.56 ? 1061 LEU A CG     1 
ATOM   6497 C  CD1    . LEU A 1 1061 ? 152.011 170.249 136.908 1.00 14.56 ? 1061 LEU A CD1    1 
ATOM   6498 C  CD2    . LEU A 1 1061 ? 151.690 168.162 135.609 1.00 14.56 ? 1061 LEU A CD2    1 
ATOM   6499 N  N      . SER A 1 1062 ? 156.321 170.438 134.315 1.00 14.81 ? 1062 SER A N      1 
ATOM   6500 C  CA     . SER A 1 1062 ? 157.664 170.049 134.733 1.00 14.81 ? 1062 SER A CA     1 
ATOM   6501 C  C      . SER A 1 1062 ? 158.433 171.132 135.489 1.00 14.81 ? 1062 SER A C      1 
ATOM   6502 O  O      . SER A 1 1062 ? 159.115 170.768 136.461 1.00 14.81 ? 1062 SER A O      1 
ATOM   6503 C  CB     . SER A 1 1062 ? 158.462 169.563 133.519 1.00 14.81 ? 1062 SER A CB     1 
ATOM   6504 O  OG     . SER A 1 1062 ? 157.803 168.477 132.911 1.00 14.81 ? 1062 SER A OG     1 
ATOM   6505 N  N      . PRO A 1 1063 ? 158.396 172.435 135.132 1.00 13.62 ? 1063 PRO A N      1 
ATOM   6506 C  CA     . PRO A 1 1063 ? 159.004 173.417 136.040 1.00 13.62 ? 1063 PRO A CA     1 
ATOM   6507 C  C      . PRO A 1 1063 ? 158.303 173.541 137.374 1.00 13.62 ? 1063 PRO A C      1 
ATOM   6508 O  O      . PRO A 1 1063 ? 158.977 173.827 138.365 1.00 13.62 ? 1063 PRO A O      1 
ATOM   6509 C  CB     . PRO A 1 1063 ? 158.920 174.727 135.252 1.00 13.62 ? 1063 PRO A CB     1 
ATOM   6510 C  CG     . PRO A 1 1063 ? 158.878 174.331 133.894 1.00 13.62 ? 1063 PRO A CG     1 
ATOM   6511 C  CD     . PRO A 1 1063 ? 158.100 173.089 133.839 1.00 13.62 ? 1063 PRO A CD     1 
ATOM   6512 N  N      . LEU A 1 1064 ? 156.985 173.338 137.438 1.00 13.36 ? 1064 LEU A N      1 
ATOM   6513 C  CA     . LEU A 1 1064 ? 156.282 173.396 138.716 1.00 13.36 ? 1064 LEU A CA     1 
ATOM   6514 C  C      . LEU A 1 1064 ? 156.711 172.259 139.630 1.00 13.36 ? 1064 LEU A C      1 
ATOM   6515 O  O      . LEU A 1 1064 ? 157.030 172.477 140.810 1.00 13.36 ? 1064 LEU A O      1 
ATOM   6516 C  CB     . LEU A 1 1064 ? 154.775 173.353 138.487 1.00 13.36 ? 1064 LEU A CB     1 
ATOM   6517 C  CG     . LEU A 1 1064 ? 154.151 174.591 137.861 1.00 13.36 ? 1064 LEU A CG     1 
ATOM   6518 C  CD1    . LEU A 1 1064 ? 152.694 174.343 137.536 1.00 13.36 ? 1064 LEU A CD1    1 
ATOM   6519 C  CD2    . LEU A 1 1064 ? 154.289 175.761 138.812 1.00 13.36 ? 1064 LEU A CD2    1 
ATOM   6520 N  N      . LEU A 1 1065 ? 156.746 171.040 139.088 1.00 12.47 ? 1065 LEU A N      1 
ATOM   6521 C  CA     . LEU A 1 1065 ? 157.209 169.891 139.853 1.00 12.47 ? 1065 LEU A CA     1 
ATOM   6522 C  C      . LEU A 1 1065 ? 158.674 170.031 140.226 1.00 12.47 ? 1065 LEU A C      1 
ATOM   6523 O  O      . LEU A 1 1065 ? 159.072 169.661 141.337 1.00 12.47 ? 1065 LEU A O      1 
ATOM   6524 C  CB     . LEU A 1 1065 ? 156.988 168.611 139.054 1.00 12.47 ? 1065 LEU A CB     1 
ATOM   6525 C  CG     . LEU A 1 1065 ? 155.540 168.209 138.806 1.00 12.47 ? 1065 LEU A CG     1 
ATOM   6526 C  CD1    . LEU A 1 1065 ? 155.494 166.992 137.907 1.00 12.47 ? 1065 LEU A CD1    1 
ATOM   6527 C  CD2    . LEU A 1 1065 ? 154.852 167.946 140.127 1.00 12.47 ? 1065 LEU A CD2    1 
ATOM   6528 N  N      . LEU A 1 1066 ? 159.485 170.582 139.317 1.00 12.22 ? 1066 LEU A N      1 
ATOM   6529 C  CA     . LEU A 1 1066 ? 160.884 170.841 139.622 1.00 12.22 ? 1066 LEU A CA     1 
ATOM   6530 C  C      . LEU A 1 1066 ? 161.037 171.849 140.745 1.00 12.22 ? 1066 LEU A C      1 
ATOM   6531 O  O      . LEU A 1 1066 ? 161.851 171.643 141.635 1.00 12.22 ? 1066 LEU A O      1 
ATOM   6532 C  CB     . LEU A 1 1066 ? 161.624 171.312 138.370 1.00 12.22 ? 1066 LEU A CB     1 
ATOM   6533 C  CG     . LEU A 1 1066 ? 163.086 171.718 138.578 1.00 12.22 ? 1066 LEU A CG     1 
ATOM   6534 C  CD1    . LEU A 1 1066 ? 163.898 170.597 139.151 1.00 12.22 ? 1066 LEU A CD1    1 
ATOM   6535 C  CD2    . LEU A 1 1066 ? 163.696 172.188 137.288 1.00 12.22 ? 1066 LEU A CD2    1 
ATOM   6536 N  N      . ALA A 1 1067 ? 160.244 172.920 140.742 1.00 10.71 ? 1067 ALA A N      1 
ATOM   6537 C  CA     . ALA A 1 1067 ? 160.343 173.940 141.780 1.00 10.71 ? 1067 ALA A CA     1 
ATOM   6538 C  C      . ALA A 1 1067 ? 159.953 173.391 143.149 1.00 10.71 ? 1067 ALA A C      1 
ATOM   6539 O  O      . ALA A 1 1067 ? 160.623 173.674 144.155 1.00 10.71 ? 1067 ALA A O      1 
ATOM   6540 C  CB     . ALA A 1 1067 ? 159.464 175.130 141.406 1.00 10.71 ? 1067 ALA A CB     1 
ATOM   6541 N  N      . ILE A 1 1068 ? 158.898 172.573 143.195 1.00 9.46  ? 1068 ILE A N      1 
ATOM   6542 C  CA     . ILE A 1 1068 ? 158.493 171.940 144.450 1.00 9.46  ? 1068 ILE A CA     1 
ATOM   6543 C  C      . ILE A 1 1068 ? 159.562 170.965 144.933 1.00 9.46  ? 1068 ILE A C      1 
ATOM   6544 O  O      . ILE A 1 1068 ? 159.906 170.939 146.121 1.00 9.46  ? 1068 ILE A O      1 
ATOM   6545 C  CB     . ILE A 1 1068 ? 157.128 171.252 144.274 1.00 9.46  ? 1068 ILE A CB     1 
ATOM   6546 C  CG1    . ILE A 1 1068 ? 156.063 172.285 143.929 1.00 9.46  ? 1068 ILE A CG1    1 
ATOM   6547 C  CG2    . ILE A 1 1068 ? 156.719 170.501 145.529 1.00 9.46  ? 1068 ILE A CG2    1 
ATOM   6548 C  CD1    . ILE A 1 1068 ? 154.790 171.681 143.433 1.00 9.46  ? 1068 ILE A CD1    1 
ATOM   6549 N  N      . TYR A 1 1069 ? 160.137 170.185 144.016 1.00 8.30  ? 1069 TYR A N      1 
ATOM   6550 C  CA     . TYR A 1 1069 ? 161.204 169.257 144.371 1.00 8.30  ? 1069 TYR A CA     1 
ATOM   6551 C  C      . TYR A 1 1069 ? 162.477 169.972 144.800 1.00 8.30  ? 1069 TYR A C      1 
ATOM   6552 O  O      . TYR A 1 1069 ? 163.204 169.465 145.658 1.00 8.30  ? 1069 TYR A O      1 
ATOM   6553 C  CB     . TYR A 1 1069 ? 161.486 168.339 143.189 1.00 8.30  ? 1069 TYR A CB     1 
ATOM   6554 C  CG     . TYR A 1 1069 ? 162.649 167.402 143.371 1.00 8.30  ? 1069 TYR A CG     1 
ATOM   6555 C  CD1    . TYR A 1 1069 ? 162.550 166.288 144.193 1.00 8.30  ? 1069 TYR A CD1    1 
ATOM   6556 C  CD2    . TYR A 1 1069 ? 163.842 167.623 142.698 1.00 8.30  ? 1069 TYR A CD2    1 
ATOM   6557 C  CE1    . TYR A 1 1069 ? 163.608 165.430 144.345 1.00 8.30  ? 1069 TYR A CE1    1 
ATOM   6558 C  CE2    . TYR A 1 1069 ? 164.904 166.777 142.849 1.00 8.30  ? 1069 TYR A CE2    1 
ATOM   6559 C  CZ     . TYR A 1 1069 ? 164.781 165.678 143.669 1.00 8.30  ? 1069 TYR A CZ     1 
ATOM   6560 O  OH     . TYR A 1 1069 ? 165.841 164.821 143.826 1.00 8.30  ? 1069 TYR A OH     1 
ATOM   6561 N  N      . MET A 1 1070 ? 162.763 171.139 144.223 1.00 13.47 ? 1070 MET A N      1 
ATOM   6562 C  CA     . MET A 1 1070 ? 163.960 171.873 144.606 1.00 13.47 ? 1070 MET A CA     1 
ATOM   6563 C  C      . MET A 1 1070 ? 163.813 172.460 145.993 1.00 13.47 ? 1070 MET A C      1 
ATOM   6564 O  O      . MET A 1 1070 ? 164.763 172.436 146.780 1.00 13.47 ? 1070 MET A O      1 
ATOM   6565 C  CB     . MET A 1 1070 ? 164.286 172.985 143.607 1.00 13.47 ? 1070 MET A CB     1 
ATOM   6566 C  CG     . MET A 1 1070 ? 164.788 172.515 142.270 1.00 13.47 ? 1070 MET A CG     1 
ATOM   6567 S  SD     . MET A 1 1070 ? 166.157 171.384 142.383 1.00 13.47 ? 1070 MET A SD     1 
ATOM   6568 C  CE     . MET A 1 1070 ? 167.441 172.514 142.857 1.00 13.47 ? 1070 MET A CE     1 
ATOM   6569 N  N      . VAL A 1 1071 ? 162.633 172.993 146.316 1.00 12.80 ? 1071 VAL A N      1 
ATOM   6570 C  CA     . VAL A 1 1071 ? 162.476 173.543 147.652 1.00 12.80 ? 1071 VAL A CA     1 
ATOM   6571 C  C      . VAL A 1 1071 ? 162.329 172.431 148.688 1.00 12.80 ? 1071 VAL A C      1 
ATOM   6572 O  O      . VAL A 1 1071 ? 162.655 172.639 149.861 1.00 12.80 ? 1071 VAL A O      1 
ATOM   6573 C  CB     . VAL A 1 1071 ? 161.306 174.550 147.686 1.00 12.80 ? 1071 VAL A CB     1 
ATOM   6574 C  CG1    . VAL A 1 1071 ? 159.959 173.863 147.638 1.00 12.80 ? 1071 VAL A CG1    1 
ATOM   6575 C  CG2    . VAL A 1 1071 ? 161.417 175.486 148.879 1.00 12.80 ? 1071 VAL A CG2    1 
ATOM   6576 N  N      . PHE A 1 1072 ? 161.899 171.234 148.290 1.00 13.46 ? 1072 PHE A N      1 
ATOM   6577 C  CA     . PHE A 1 1072 ? 161.766 170.168 149.272 1.00 13.46 ? 1072 PHE A CA     1 
ATOM   6578 C  C      . PHE A 1 1072 ? 163.044 169.364 149.462 1.00 13.46 ? 1072 PHE A C      1 
ATOM   6579 O  O      . PHE A 1 1072 ? 163.266 168.823 150.544 1.00 13.46 ? 1072 PHE A O      1 
ATOM   6580 C  CB     . PHE A 1 1072 ? 160.628 169.219 148.887 1.00 13.46 ? 1072 PHE A CB     1 
ATOM   6581 C  CG     . PHE A 1 1072 ? 160.321 168.203 149.943 1.00 13.46 ? 1072 PHE A CG     1 
ATOM   6582 C  CD1    . PHE A 1 1072 ? 159.616 168.567 151.075 1.00 13.46 ? 1072 PHE A CD1    1 
ATOM   6583 C  CD2    . PHE A 1 1072 ? 160.763 166.894 149.826 1.00 13.46 ? 1072 PHE A CD2    1 
ATOM   6584 C  CE1    . PHE A 1 1072 ? 159.342 167.644 152.062 1.00 13.46 ? 1072 PHE A CE1    1 
ATOM   6585 C  CE2    . PHE A 1 1072 ? 160.500 165.971 150.814 1.00 13.46 ? 1072 PHE A CE2    1 
ATOM   6586 C  CZ     . PHE A 1 1072 ? 159.785 166.345 151.930 1.00 13.46 ? 1072 PHE A CZ     1 
ATOM   6587 N  N      . THR A 1 1073 ? 163.895 169.259 148.451 1.00 13.36 ? 1073 THR A N      1 
ATOM   6588 C  CA     . THR A 1 1073 ? 165.010 168.329 148.509 1.00 13.36 ? 1073 THR A CA     1 
ATOM   6589 C  C      . THR A 1 1073 ? 166.363 169.019 148.556 1.00 13.36 ? 1073 THR A C      1 
ATOM   6590 O  O      . THR A 1 1073 ? 167.203 168.661 149.382 1.00 13.36 ? 1073 THR A O      1 
ATOM   6591 C  CB     . THR A 1 1073 ? 164.943 167.372 147.315 1.00 13.36 ? 1073 THR A CB     1 
ATOM   6592 O  OG1    . THR A 1 1073 ? 163.650 166.763 147.281 1.00 13.36 ? 1073 THR A OG1    1 
ATOM   6593 C  CG2    . THR A 1 1073 ? 165.959 166.273 147.464 1.00 13.36 ? 1073 THR A CG2    1 
ATOM   6594 N  N      . ASN A 1 1074 ? 166.607 169.992 147.676 1.00 13.61 ? 1074 ASN A N      1 
ATOM   6595 C  CA     . ASN A 1 1074 ? 167.859 170.738 147.736 1.00 13.61 ? 1074 ASN A CA     1 
ATOM   6596 C  C      . ASN A 1 1074 ? 167.916 171.606 148.986 1.00 13.61 ? 1074 ASN A C      1 
ATOM   6597 O  O      . ASN A 1 1074 ? 168.969 171.723 149.621 1.00 13.61 ? 1074 ASN A O      1 
ATOM   6598 C  CB     . ASN A 1 1074 ? 168.018 171.602 146.486 1.00 13.61 ? 1074 ASN A CB     1 
ATOM   6599 C  CG     . ASN A 1 1074 ? 169.468 171.952 146.184 1.00 13.61 ? 1074 ASN A CG     1 
ATOM   6600 O  OD1    . ASN A 1 1074 ? 169.766 172.499 145.130 1.00 13.61 ? 1074 ASN A OD1    1 
ATOM   6601 N  ND2    . ASN A 1 1074 ? 170.377 171.603 147.083 1.00 13.61 ? 1074 ASN A ND2    1 
ATOM   6602 N  N      . ILE A 1 1075 ? 166.796 172.209 149.358 1.00 12.23 ? 1075 ILE A N      1 
ATOM   6603 C  CA     . ILE A 1 1075 ? 166.772 173.128 150.483 1.00 12.23 ? 1075 ILE A CA     1 
ATOM   6604 C  C      . ILE A 1 1075 ? 166.434 172.410 151.779 1.00 12.23 ? 1075 ILE A C      1 
ATOM   6605 O  O      . ILE A 1 1075 ? 167.109 172.593 152.792 1.00 12.23 ? 1075 ILE A O      1 
ATOM   6606 C  CB     . ILE A 1 1075 ? 165.788 174.280 150.191 1.00 12.23 ? 1075 ILE A CB     1 
ATOM   6607 C  CG1    . ILE A 1 1075 ? 166.253 175.073 148.973 1.00 12.23 ? 1075 ILE A CG1    1 
ATOM   6608 C  CG2    . ILE A 1 1075 ? 165.666 175.205 151.383 1.00 12.23 ? 1075 ILE A CG2    1 
ATOM   6609 C  CD1    . ILE A 1 1075 ? 165.233 176.049 148.476 1.00 12.23 ? 1075 ILE A CD1    1 
ATOM   6610 N  N      . LEU A 1 1076 ? 165.409 171.566 151.785 1.00 11.50 ? 1076 LEU A N      1 
ATOM   6611 C  CA     . LEU A 1 1076 ? 164.946 171.015 153.051 1.00 11.50 ? 1076 LEU A CA     1 
ATOM   6612 C  C      . LEU A 1 1076 ? 165.618 169.692 153.408 1.00 11.50 ? 1076 LEU A C      1 
ATOM   6613 O  O      . LEU A 1 1076 ? 166.069 169.522 154.543 1.00 11.50 ? 1076 LEU A O      1 
ATOM   6614 C  CB     . LEU A 1 1076 ? 163.423 170.862 153.025 1.00 11.50 ? 1076 LEU A CB     1 
ATOM   6615 C  CG     . LEU A 1 1076 ? 162.722 170.275 154.247 1.00 11.50 ? 1076 LEU A CG     1 
ATOM   6616 C  CD1    . LEU A 1 1076 ? 162.907 171.157 155.447 1.00 11.50 ? 1076 LEU A CD1    1 
ATOM   6617 C  CD2    . LEU A 1 1076 ? 161.257 170.104 153.967 1.00 11.50 ? 1076 LEU A CD2    1 
ATOM   6618 N  N      . LEU A 1 1077 ? 165.691 168.742 152.472 1.00 13.31 ? 1077 LEU A N      1 
ATOM   6619 C  CA     . LEU A 1 1077 ? 166.209 167.419 152.817 1.00 13.31 ? 1077 LEU A CA     1 
ATOM   6620 C  C      . LEU A 1 1077 ? 167.726 167.393 152.871 1.00 13.31 ? 1077 LEU A C      1 
ATOM   6621 O  O      . LEU A 1 1077 ? 168.303 166.732 153.741 1.00 13.31 ? 1077 LEU A O      1 
ATOM   6622 C  CB     . LEU A 1 1077 ? 165.726 166.367 151.825 1.00 13.31 ? 1077 LEU A CB     1 
ATOM   6623 C  CG     . LEU A 1 1077 ? 164.263 165.948 151.840 1.00 13.31 ? 1077 LEU A CG     1 
ATOM   6624 C  CD1    . LEU A 1 1077 ? 164.029 164.972 150.714 1.00 13.31 ? 1077 LEU A CD1    1 
ATOM   6625 C  CD2    . LEU A 1 1077 ? 163.891 165.341 153.173 1.00 13.31 ? 1077 LEU A CD2    1 
ATOM   6626 N  N      . LEU A 1 1078 ? 168.384 168.071 151.930 1.00 12.46 ? 1078 LEU A N      1 
ATOM   6627 C  CA     . LEU A 1 1078 ? 169.842 168.108 151.930 1.00 12.46 ? 1078 LEU A CA     1 
ATOM   6628 C  C      . LEU A 1 1078 ? 170.383 168.877 153.116 1.00 12.46 ? 1078 LEU A C      1 
ATOM   6629 O  O      . LEU A 1 1078 ? 171.408 168.497 153.679 1.00 12.46 ? 1078 LEU A O      1 
ATOM   6630 C  CB     . LEU A 1 1078 ? 170.370 168.691 150.624 1.00 12.46 ? 1078 LEU A CB     1 
ATOM   6631 C  CG     . LEU A 1 1078 ? 170.892 167.627 149.659 1.00 12.46 ? 1078 LEU A CG     1 
ATOM   6632 C  CD1    . LEU A 1 1078 ? 169.832 166.632 149.296 1.00 12.46 ? 1078 LEU A CD1    1 
ATOM   6633 C  CD2    . LEU A 1 1078 ? 171.429 168.302 148.409 1.00 12.46 ? 1078 LEU A CD2    1 
ATOM   6634 N  N      . ASN A 1 1079 ? 169.699 169.924 153.545 1.00 12.80 ? 1079 ASN A N      1 
ATOM   6635 C  CA     . ASN A 1 1079 ? 170.171 170.622 154.726 1.00 12.80 ? 1079 ASN A CA     1 
ATOM   6636 C  C      . ASN A 1 1079 ? 169.830 169.881 156.006 1.00 12.80 ? 1079 ASN A C      1 
ATOM   6637 O  O      . ASN A 1 1079 ? 170.535 170.046 156.998 1.00 12.80 ? 1079 ASN A O      1 
ATOM   6638 C  CB     . ASN A 1 1079 ? 169.615 172.036 154.744 1.00 12.80 ? 1079 ASN A CB     1 
ATOM   6639 C  CG     . ASN A 1 1079 ? 170.167 172.869 153.621 1.00 12.80 ? 1079 ASN A CG     1 
ATOM   6640 O  OD1    . ASN A 1 1079 ? 171.364 172.842 153.350 1.00 12.80 ? 1079 ASN A OD1    1 
ATOM   6641 N  ND2    . ASN A 1 1079 ? 169.297 173.585 152.932 1.00 12.80 ? 1079 ASN A ND2    1 
ATOM   6642 N  N      . LEU A 1 1080 ? 168.804 169.030 155.988 1.00 12.37 ? 1080 LEU A N      1 
ATOM   6643 C  CA     . LEU A 1 1080 ? 168.585 168.095 157.086 1.00 12.37 ? 1080 LEU A CA     1 
ATOM   6644 C  C      . LEU A 1 1080 ? 169.700 167.063 157.160 1.00 12.37 ? 1080 LEU A C      1 
ATOM   6645 O  O      . LEU A 1 1080 ? 170.163 166.720 158.251 1.00 12.37 ? 1080 LEU A O      1 
ATOM   6646 C  CB     . LEU A 1 1080 ? 167.235 167.405 156.918 1.00 12.37 ? 1080 LEU A CB     1 
ATOM   6647 C  CG     . LEU A 1 1080 ? 166.868 166.324 157.929 1.00 12.37 ? 1080 LEU A CG     1 
ATOM   6648 C  CD1    . LEU A 1 1080 ? 166.816 166.891 159.323 1.00 12.37 ? 1080 LEU A CD1    1 
ATOM   6649 C  CD2    . LEU A 1 1080 ? 165.543 165.716 157.546 1.00 12.37 ? 1080 LEU A CD2    1 
ATOM   6650 N  N      . LEU A 1 1081 ? 170.146 166.567 156.008 1.00 11.98 ? 1081 LEU A N      1 
ATOM   6651 C  CA     . LEU A 1 1081 ? 171.259 165.626 155.975 1.00 11.98 ? 1081 LEU A CA     1 
ATOM   6652 C  C      . LEU A 1 1081 ? 172.562 166.284 156.412 1.00 11.98 ? 1081 LEU A C      1 
ATOM   6653 O  O      . LEU A 1 1081 ? 173.362 165.674 157.128 1.00 11.98 ? 1081 LEU A O      1 
ATOM   6654 C  CB     . LEU A 1 1081 ? 171.384 165.037 154.572 1.00 11.98 ? 1081 LEU A CB     1 
ATOM   6655 C  CG     . LEU A 1 1081 ? 172.502 164.037 154.299 1.00 11.98 ? 1081 LEU A CG     1 
ATOM   6656 C  CD1    . LEU A 1 1081 ? 172.388 162.819 155.191 1.00 11.98 ? 1081 LEU A CD1    1 
ATOM   6657 C  CD2    . LEU A 1 1081 ? 172.470 163.642 152.845 1.00 11.98 ? 1081 LEU A CD2    1 
ATOM   6658 N  N      . ILE A 1 1082 ? 172.774 167.541 156.023 1.00 11.26 ? 1082 ILE A N      1 
ATOM   6659 C  CA     . ILE A 1 1082 ? 173.930 168.298 156.490 1.00 11.26 ? 1082 ILE A CA     1 
ATOM   6660 C  C      . ILE A 1 1082 ? 173.810 168.605 157.982 1.00 11.26 ? 1082 ILE A C      1 
ATOM   6661 O  O      . ILE A 1 1082 ? 174.814 168.614 158.692 1.00 11.26 ? 1082 ILE A O      1 
ATOM   6662 C  CB     . ILE A 1 1082 ? 174.100 169.562 155.619 1.00 11.26 ? 1082 ILE A CB     1 
ATOM   6663 C  CG1    . ILE A 1 1082 ? 174.488 169.165 154.200 1.00 11.26 ? 1082 ILE A CG1    1 
ATOM   6664 C  CG2    . ILE A 1 1082 ? 175.157 170.505 156.147 1.00 11.26 ? 1082 ILE A CG2    1 
ATOM   6665 C  CD1    . ILE A 1 1082 ? 174.364 170.278 153.213 1.00 11.26 ? 1082 ILE A CD1    1 
ATOM   6666 N  N      . ALA A 1 1083 ? 172.592 168.796 158.496 1.00 11.69 ? 1083 ALA A N      1 
ATOM   6667 C  CA     . ALA A 1 1083 ? 172.402 168.971 159.934 1.00 11.69 ? 1083 ALA A CA     1 
ATOM   6668 C  C      . ALA A 1 1083 ? 172.726 167.697 160.706 1.00 11.69 ? 1083 ALA A C      1 
ATOM   6669 O  O      . ALA A 1 1083 ? 173.303 167.760 161.796 1.00 11.69 ? 1083 ALA A O      1 
ATOM   6670 C  CB     . ALA A 1 1083 ? 170.974 169.416 160.224 1.00 11.69 ? 1083 ALA A CB     1 
ATOM   6671 N  N      . ILE A 1 1084 ? 172.366 166.537 160.154 1.00 12.30 ? 1084 ILE A N      1 
ATOM   6672 C  CA     . ILE A 1 1084 ? 172.749 165.253 160.743 1.00 12.30 ? 1084 ILE A CA     1 
ATOM   6673 C  C      . ILE A 1 1084 ? 174.265 165.074 160.706 1.00 12.30 ? 1084 ILE A C      1 
ATOM   6674 O  O      . ILE A 1 1084 ? 174.878 164.620 161.685 1.00 12.30 ? 1084 ILE A O      1 
ATOM   6675 C  CB     . ILE A 1 1084 ? 172.010 164.108 160.024 1.00 12.30 ? 1084 ILE A CB     1 
ATOM   6676 C  CG1    . ILE A 1 1084 ? 170.510 164.212 160.276 1.00 12.30 ? 1084 ILE A CG1    1 
ATOM   6677 C  CG2    . ILE A 1 1084 ? 172.483 162.754 160.492 1.00 12.30 ? 1084 ILE A CG2    1 
ATOM   6678 C  CD1    . ILE A 1 1084 ? 169.690 163.380 159.347 1.00 12.30 ? 1084 ILE A CD1    1 
ATOM   6679 N  N      . PHE A 1 1085 ? 174.892 165.472 159.593 1.00 11.18 ? 1085 PHE A N      1 
ATOM   6680 C  CA     . PHE A 1 1085 ? 176.349 165.460 159.481 1.00 11.18 ? 1085 PHE A CA     1 
ATOM   6681 C  C      . PHE A 1 1085 ? 177.004 166.373 160.506 1.00 11.18 ? 1085 PHE A C      1 
ATOM   6682 O  O      . PHE A 1 1085 ? 178.036 166.027 161.083 1.00 11.18 ? 1085 PHE A O      1 
ATOM   6683 C  CB     . PHE A 1 1085 ? 176.770 165.883 158.076 1.00 11.18 ? 1085 PHE A CB     1 
ATOM   6684 C  CG     . PHE A 1 1085 ? 176.566 164.834 157.029 1.00 11.18 ? 1085 PHE A CG     1 
ATOM   6685 C  CD1    . PHE A 1 1085 ? 176.337 163.517 157.374 1.00 11.18 ? 1085 PHE A CD1    1 
ATOM   6686 C  CD2    . PHE A 1 1085 ? 176.625 165.170 155.688 1.00 11.18 ? 1085 PHE A CD2    1 
ATOM   6687 C  CE1    . PHE A 1 1085 ? 176.155 162.563 156.405 1.00 11.18 ? 1085 PHE A CE1    1 
ATOM   6688 C  CE2    . PHE A 1 1085 ? 176.450 164.216 154.719 1.00 11.18 ? 1085 PHE A CE2    1 
ATOM   6689 C  CZ     . PHE A 1 1085 ? 176.217 162.910 155.078 1.00 11.18 ? 1085 PHE A CZ     1 
ATOM   6690 N  N      . ASN A 1 1086 ? 176.413 167.540 160.753 1.00 13.94 ? 1086 ASN A N      1 
ATOM   6691 C  CA     . ASN A 1 1086 ? 176.987 168.481 161.704 1.00 13.94 ? 1086 ASN A CA     1 
ATOM   6692 C  C      . ASN A 1 1086 ? 176.795 168.016 163.137 1.00 13.94 ? 1086 ASN A C      1 
ATOM   6693 O  O      . ASN A 1 1086 ? 177.660 168.263 163.980 1.00 13.94 ? 1086 ASN A O      1 
ATOM   6694 C  CB     . ASN A 1 1086 ? 176.377 169.866 161.524 1.00 13.94 ? 1086 ASN A CB     1 
ATOM   6695 C  CG     . ASN A 1 1086 ? 176.717 170.479 160.192 1.00 13.94 ? 1086 ASN A CG     1 
ATOM   6696 O  OD1    . ASN A 1 1086 ? 177.817 170.305 159.679 1.00 13.94 ? 1086 ASN A OD1    1 
ATOM   6697 N  ND2    . ASN A 1 1086 ? 175.770 171.211 159.621 1.00 13.94 ? 1086 ASN A ND2    1 
ATOM   6698 N  N      . TYR A 1 1087 ? 175.678 167.346 163.426 1.00 14.76 ? 1087 TYR A N      1 
ATOM   6699 C  CA     . TYR A 1 1087 ? 175.484 166.740 164.738 1.00 14.76 ? 1087 TYR A CA     1 
ATOM   6700 C  C      . TYR A 1 1087 ? 176.519 165.649 164.989 1.00 14.76 ? 1087 TYR A C      1 
ATOM   6701 O  O      . TYR A 1 1087 ? 177.090 165.554 166.088 1.00 14.76 ? 1087 TYR A O      1 
ATOM   6702 C  CB     . TYR A 1 1087 ? 174.061 166.189 164.828 1.00 14.76 ? 1087 TYR A CB     1 
ATOM   6703 C  CG     . TYR A 1 1087 ? 173.677 165.651 166.177 1.00 14.76 ? 1087 TYR A CG     1 
ATOM   6704 C  CD1    . TYR A 1 1087 ? 173.427 166.507 167.237 1.00 14.76 ? 1087 TYR A CD1    1 
ATOM   6705 C  CD2    . TYR A 1 1087 ? 173.548 164.287 166.389 1.00 14.76 ? 1087 TYR A CD2    1 
ATOM   6706 C  CE1    . TYR A 1 1087 ? 173.077 166.021 168.475 1.00 14.76 ? 1087 TYR A CE1    1 
ATOM   6707 C  CE2    . TYR A 1 1087 ? 173.194 163.790 167.622 1.00 14.76 ? 1087 TYR A CE2    1 
ATOM   6708 C  CZ     . TYR A 1 1087 ? 172.960 164.663 168.663 1.00 14.76 ? 1087 TYR A CZ     1 
ATOM   6709 O  OH     . TYR A 1 1087 ? 172.604 164.176 169.899 1.00 14.76 ? 1087 TYR A OH     1 
ATOM   6710 N  N      . THR A 1 1088 ? 176.803 164.848 163.958 1.00 15.60 ? 1088 THR A N      1 
ATOM   6711 C  CA     . THR A 1 1088 ? 177.866 163.849 164.026 1.00 15.60 ? 1088 THR A CA     1 
ATOM   6712 C  C      . THR A 1 1088 ? 179.237 164.493 164.225 1.00 15.60 ? 1088 THR A C      1 
ATOM   6713 O  O      . THR A 1 1088 ? 180.049 164.010 165.029 1.00 15.60 ? 1088 THR A O      1 
ATOM   6714 C  CB     . THR A 1 1088 ? 177.839 163.012 162.750 1.00 15.60 ? 1088 THR A CB     1 
ATOM   6715 O  OG1    . THR A 1 1088 ? 176.571 162.360 162.646 1.00 15.60 ? 1088 THR A OG1    1 
ATOM   6716 C  CG2    . THR A 1 1088 ? 178.925 161.981 162.750 1.00 15.60 ? 1088 THR A CG2    1 
ATOM   6717 N  N      . PHE A 1 1089 ? 179.502 165.588 163.502 1.00 15.35 ? 1089 PHE A N      1 
ATOM   6718 C  CA     . PHE A 1 1089 ? 180.739 166.347 163.659 1.00 15.35 ? 1089 PHE A CA     1 
ATOM   6719 C  C      . PHE A 1 1089 ? 180.911 166.859 165.078 1.00 15.35 ? 1089 PHE A C      1 
ATOM   6720 O  O      . PHE A 1 1089 ? 182.016 166.819 165.620 1.00 15.35 ? 1089 PHE A O      1 
ATOM   6721 C  CB     . PHE A 1 1089 ? 180.773 167.529 162.686 1.00 15.35 ? 1089 PHE A CB     1 
ATOM   6722 C  CG     . PHE A 1 1089 ? 181.935 168.461 162.913 1.00 15.35 ? 1089 PHE A CG     1 
ATOM   6723 C  CD1    . PHE A 1 1089 ? 183.192 168.122 162.486 1.00 15.35 ? 1089 PHE A CD1    1 
ATOM   6724 C  CD2    . PHE A 1 1089 ? 181.770 169.668 163.583 1.00 15.35 ? 1089 PHE A CD2    1 
ATOM   6725 C  CE1    . PHE A 1 1089 ? 184.262 168.958 162.705 1.00 15.35 ? 1089 PHE A CE1    1 
ATOM   6726 C  CE2    . PHE A 1 1089 ? 182.841 170.495 163.813 1.00 15.35 ? 1089 PHE A CE2    1 
ATOM   6727 C  CZ     . PHE A 1 1089 ? 184.083 170.141 163.376 1.00 15.35 ? 1089 PHE A CZ     1 
ATOM   6728 N  N      . GLU A 1 1090 ? 179.843 167.384 165.678 1.00 18.35 ? 1090 GLU A N      1 
ATOM   6729 C  CA     . GLU A 1 1090 ? 179.961 167.930 167.024 1.00 18.35 ? 1090 GLU A CA     1 
ATOM   6730 C  C      . GLU A 1 1090 ? 180.196 166.827 168.047 1.00 18.35 ? 1090 GLU A C      1 
ATOM   6731 O  O      . GLU A 1 1090 ? 181.028 166.987 168.952 1.00 18.35 ? 1090 GLU A O      1 
ATOM   6732 C  CB     . GLU A 1 1090 ? 178.723 168.750 167.378 1.00 18.35 ? 1090 GLU A CB     1 
ATOM   6733 C  CG     . GLU A 1 1090 ? 178.583 170.024 166.570 1.00 18.35 ? 1090 GLU A CG     1 
ATOM   6734 C  CD     . GLU A 1 1090 ? 179.682 171.030 166.845 1.00 18.35 ? 1090 GLU A CD     1 
ATOM   6735 O  OE1    . GLU A 1 1090 ? 180.160 171.106 167.997 1.00 18.35 ? 1090 GLU A OE1    1 
ATOM   6736 O  OE2    . GLU A 1 1090 ? 180.072 171.748 165.903 1.00 18.35 ? 1090 GLU A OE2    1 
ATOM   6737 N  N      . ARG A 1 1091 ? 179.520 165.682 167.882 1.00 19.44 ? 1091 ARG A N      1 
ATOM   6738 C  CA     . ARG A 1 1091 ? 179.736 164.555 168.786 1.00 19.44 ? 1091 ARG A CA     1 
ATOM   6739 C  C      . ARG A 1 1091 ? 181.143 163.980 168.678 1.00 19.44 ? 1091 ARG A C      1 
ATOM   6740 O  O      . ARG A 1 1091 ? 181.698 163.528 169.683 1.00 19.44 ? 1091 ARG A O      1 
ATOM   6741 C  CB     . ARG A 1 1091 ? 178.723 163.449 168.519 1.00 19.44 ? 1091 ARG A CB     1 
ATOM   6742 C  CG     . ARG A 1 1091 ? 177.313 163.757 168.948 1.00 19.44 ? 1091 ARG A CG     1 
ATOM   6743 C  CD     . ARG A 1 1091 ? 176.424 162.577 168.618 1.00 19.44 ? 1091 ARG A CD     1 
ATOM   6744 N  NE     . ARG A 1 1091 ? 176.305 162.395 167.175 1.00 19.44 ? 1091 ARG A NE     1 
ATOM   6745 C  CZ     . ARG A 1 1091 ? 175.731 161.348 166.595 1.00 19.44 ? 1091 ARG A CZ     1 
ATOM   6746 N  NH1    . ARG A 1 1091 ? 175.221 160.374 167.335 1.00 19.44 ? 1091 ARG A NH1    1 
ATOM   6747 N  NH2    . ARG A 1 1091 ? 175.670 161.273 165.274 1.00 19.44 ? 1091 ARG A NH2    1 
ATOM   6748 N  N      . VAL A 1 1092 ? 181.737 163.979 167.487 1.00 19.74 ? 1092 VAL A N      1 
ATOM   6749 C  CA     . VAL A 1 1092 ? 183.104 163.475 167.397 1.00 19.74 ? 1092 VAL A CA     1 
ATOM   6750 C  C      . VAL A 1 1092 ? 184.109 164.539 167.834 1.00 19.74 ? 1092 VAL A C      1 
ATOM   6751 O  O      . VAL A 1 1092 ? 185.053 164.236 168.564 1.00 19.74 ? 1092 VAL A O      1 
ATOM   6752 C  CB     . VAL A 1 1092 ? 183.398 162.943 165.982 1.00 19.74 ? 1092 VAL A CB     1 
ATOM   6753 C  CG1    . VAL A 1 1092 ? 184.839 162.456 165.875 1.00 19.74 ? 1092 VAL A CG1    1 
ATOM   6754 C  CG2    . VAL A 1 1092 ? 182.453 161.814 165.645 1.00 19.74 ? 1092 VAL A CG2    1 
ATOM   6755 N  N      . GLN A 1 1093 ? 183.901 165.798 167.441 1.00 22.08 ? 1093 GLN A N      1 
ATOM   6756 C  CA     . GLN A 1 1093 ? 184.843 166.877 167.722 1.00 22.08 ? 1093 GLN A CA     1 
ATOM   6757 C  C      . GLN A 1 1093 ? 184.908 167.214 169.208 1.00 22.08 ? 1093 GLN A C      1 
ATOM   6758 O  O      . GLN A 1 1093 ? 185.944 167.686 169.689 1.00 22.08 ? 1093 GLN A O      1 
ATOM   6759 C  CB     . GLN A 1 1093 ? 184.442 168.099 166.889 1.00 22.08 ? 1093 GLN A CB     1 
ATOM   6760 C  CG     . GLN A 1 1093 ? 185.321 169.329 166.999 1.00 22.08 ? 1093 GLN A CG     1 
ATOM   6761 C  CD     . GLN A 1 1093 ? 186.710 169.131 166.438 1.00 22.08 ? 1093 GLN A CD     1 
ATOM   6762 O  OE1    . GLN A 1 1093 ? 186.889 168.512 165.395 1.00 22.08 ? 1093 GLN A OE1    1 
ATOM   6763 N  NE2    . GLN A 1 1093 ? 187.704 169.674 167.124 1.00 22.08 ? 1093 GLN A NE2    1 
ATOM   6764 N  N      . GLU A 1 1094 ? 183.842 166.939 169.966 1.00 27.23 ? 1094 GLU A N      1 
ATOM   6765 C  CA     . GLU A 1 1094 ? 183.937 167.121 171.411 1.00 27.23 ? 1094 GLU A CA     1 
ATOM   6766 C  C      . GLU A 1 1094 ? 184.760 166.034 172.095 1.00 27.23 ? 1094 GLU A C      1 
ATOM   6767 O  O      . GLU A 1 1094 ? 185.032 166.152 173.294 1.00 27.23 ? 1094 GLU A O      1 
ATOM   6768 C  CB     . GLU A 1 1094 ? 182.541 167.170 172.028 1.00 27.23 ? 1094 GLU A CB     1 
ATOM   6769 C  CG     . GLU A 1 1094 ? 181.807 165.849 172.001 1.00 27.23 ? 1094 GLU A CG     1 
ATOM   6770 C  CD     . GLU A 1 1094 ? 180.359 165.976 172.425 1.00 27.23 ? 1094 GLU A CD     1 
ATOM   6771 O  OE1    . GLU A 1 1094 ? 179.916 167.112 172.696 1.00 27.23 ? 1094 GLU A OE1    1 
ATOM   6772 O  OE2    . GLU A 1 1094 ? 179.664 164.941 172.482 1.00 27.23 ? 1094 GLU A OE2    1 
ATOM   6773 N  N      . ASP A 1 1095 ? 185.169 164.995 171.366 1.00 26.04 ? 1095 ASP A N      1 
ATOM   6774 C  CA     . ASP A 1 1095 ? 185.896 163.869 171.930 1.00 26.04 ? 1095 ASP A CA     1 
ATOM   6775 C  C      . ASP A 1 1095 ? 187.080 163.486 171.046 1.00 26.04 ? 1095 ASP A C      1 
ATOM   6776 O  O      . ASP A 1 1095 ? 187.639 162.397 171.221 1.00 26.04 ? 1095 ASP A O      1 
ATOM   6777 C  CB     . ASP A 1 1095 ? 184.936 162.681 172.095 1.00 26.04 ? 1095 ASP A CB     1 
ATOM   6778 C  CG     . ASP A 1 1095 ? 185.369 161.713 173.173 1.00 26.04 ? 1095 ASP A CG     1 
ATOM   6779 O  OD1    . ASP A 1 1095 ? 186.377 161.990 173.848 1.00 26.04 ? 1095 ASP A OD1    1 
ATOM   6780 O  OD2    . ASP A 1 1095 ? 184.702 160.674 173.346 1.00 26.04 ? 1095 ASP A OD2    1 
ATOM   6781 N  N      . SER A 1 1096 ? 187.437 164.348 170.083 1.00 22.73 ? 1096 SER A N      1 
ATOM   6782 C  CA     . SER A 1 1096 ? 188.352 163.997 168.996 1.00 22.73 ? 1096 SER A CA     1 
ATOM   6783 C  C      . SER A 1 1096 ? 189.748 163.642 169.479 1.00 22.73 ? 1096 SER A C      1 
ATOM   6784 O  O      . SER A 1 1096 ? 190.393 162.760 168.898 1.00 22.73 ? 1096 SER A O      1 
ATOM   6785 C  CB     . SER A 1 1096 ? 188.431 165.144 167.990 1.00 22.73 ? 1096 SER A CB     1 
ATOM   6786 O  OG     . SER A 1 1096 ? 189.056 166.276 168.561 1.00 22.73 ? 1096 SER A OG     1 
ATOM   6787 N  N      . ASP A 1 1097 ? 190.211 164.288 170.550 1.00 21.92 ? 1097 ASP A N      1 
ATOM   6788 C  CA     . ASP A 1 1097 ? 191.512 163.954 171.119 1.00 21.92 ? 1097 ASP A CA     1 
ATOM   6789 C  C      . ASP A 1 1097 ? 191.526 162.516 171.618 1.00 21.92 ? 1097 ASP A C      1 
ATOM   6790 O  O      . ASP A 1 1097 ? 192.394 161.730 171.232 1.00 21.92 ? 1097 ASP A O      1 
ATOM   6791 C  CB     . ASP A 1 1097 ? 191.845 164.926 172.249 1.00 21.92 ? 1097 ASP A CB     1 
ATOM   6792 C  CG     . ASP A 1 1097 ? 193.322 164.962 172.573 1.00 21.92 ? 1097 ASP A CG     1 
ATOM   6793 O  OD1    . ASP A 1 1097 ? 194.102 164.280 171.877 1.00 21.92 ? 1097 ASP A OD1    1 
ATOM   6794 O  OD2    . ASP A 1 1097 ? 193.705 165.675 173.525 1.00 21.92 ? 1097 ASP A OD2    1 
ATOM   6795 N  N      . LYS A 1 1098 ? 190.505 162.131 172.391 1.00 21.65 ? 1098 LYS A N      1 
ATOM   6796 C  CA     . LYS A 1 1098 ? 190.428 160.774 172.922 1.00 21.65 ? 1098 LYS A CA     1 
ATOM   6797 C  C      . LYS A 1 1098 ? 190.158 159.741 171.841 1.00 21.65 ? 1098 LYS A C      1 
ATOM   6798 O  O      . LYS A 1 1098 ? 190.621 158.603 171.961 1.00 21.65 ? 1098 LYS A O      1 
ATOM   6799 C  CB     . LYS A 1 1098 ? 189.343 160.673 173.991 1.00 21.65 ? 1098 LYS A CB     1 
ATOM   6800 C  CG     . LYS A 1 1098 ? 189.616 161.458 175.249 1.00 21.65 ? 1098 LYS A CG     1 
ATOM   6801 C  CD     . LYS A 1 1098 ? 188.555 161.179 176.297 1.00 21.65 ? 1098 LYS A CD     1 
ATOM   6802 C  CE     . LYS A 1 1098 ? 188.801 161.992 177.556 1.00 21.65 ? 1098 LYS A CE     1 
ATOM   6803 N  NZ     . LYS A 1 1098 ? 190.046 161.568 178.251 1.00 21.65 ? 1098 LYS A NZ     1 
ATOM   6804 N  N      . VAL A 1 1099 ? 189.421 160.099 170.783 1.00 20.78 ? 1099 VAL A N      1 
ATOM   6805 C  CA     . VAL A 1 1099 ? 189.193 159.093 169.747 1.00 20.78 ? 1099 VAL A CA     1 
ATOM   6806 C  C      . VAL A 1 1099 ? 190.460 158.894 168.924 1.00 20.78 ? 1099 VAL A C      1 
ATOM   6807 O  O      . VAL A 1 1099 ? 190.720 157.782 168.443 1.00 20.78 ? 1099 VAL A O      1 
ATOM   6808 C  CB     . VAL A 1 1099 ? 187.969 159.406 168.850 1.00 20.78 ? 1099 VAL A CB     1 
ATOM   6809 C  CG1    . VAL A 1 1099 ? 186.723 159.652 169.680 1.00 20.78 ? 1099 VAL A CG1    1 
ATOM   6810 C  CG2    . VAL A 1 1099 ? 188.215 160.514 167.847 1.00 20.78 ? 1099 VAL A CG2    1 
ATOM   6811 N  N      . TRP A 1 1100 ? 191.304 159.928 168.808 1.00 14.68 ? 1100 TRP A N      1 
ATOM   6812 C  CA     . TRP A 1 1100 ? 192.594 159.733 168.160 1.00 14.68 ? 1100 TRP A CA     1 
ATOM   6813 C  C      . TRP A 1 1100 ? 193.527 158.900 169.027 1.00 14.68 ? 1100 TRP A C      1 
ATOM   6814 O  O      . TRP A 1 1100 ? 194.259 158.045 168.512 1.00 14.68 ? 1100 TRP A O      1 
ATOM   6815 C  CB     . TRP A 1 1100 ? 193.252 161.068 167.833 1.00 14.68 ? 1100 TRP A CB     1 
ATOM   6816 C  CG     . TRP A 1 1100 ? 194.563 160.832 167.192 1.00 14.68 ? 1100 TRP A CG     1 
ATOM   6817 C  CD1    . TRP A 1 1100 ? 194.779 160.276 165.976 1.00 14.68 ? 1100 TRP A CD1    1 
ATOM   6818 C  CD2    . TRP A 1 1100 ? 195.852 161.068 167.762 1.00 14.68 ? 1100 TRP A CD2    1 
ATOM   6819 N  NE1    . TRP A 1 1100 ? 196.119 160.173 165.735 1.00 14.68 ? 1100 TRP A NE1    1 
ATOM   6820 C  CE2    . TRP A 1 1100 ? 196.802 160.647 166.821 1.00 14.68 ? 1100 TRP A CE2    1 
ATOM   6821 C  CE3    . TRP A 1 1100 ? 196.294 161.602 168.974 1.00 14.68 ? 1100 TRP A CE3    1 
ATOM   6822 C  CZ2    . TRP A 1 1100 ? 198.163 160.753 167.043 1.00 14.68 ? 1100 TRP A CZ2    1 
ATOM   6823 C  CZ3    . TRP A 1 1100 ? 197.645 161.702 169.194 1.00 14.68 ? 1100 TRP A CZ3    1 
ATOM   6824 C  CH2    . TRP A 1 1100 ? 198.565 161.287 168.232 1.00 14.68 ? 1100 TRP A CH2    1 
ATOM   6825 N  N      . LYS A 1 1101 ? 193.506 159.136 170.345 1.00 18.76 ? 1101 LYS A N      1 
ATOM   6826 C  CA     . LYS A 1 1101 ? 194.276 158.308 171.271 1.00 18.76 ? 1101 LYS A CA     1 
ATOM   6827 C  C      . LYS A 1 1101 ? 193.831 156.852 171.214 1.00 18.76 ? 1101 LYS A C      1 
ATOM   6828 O  O      . LYS A 1 1101 ? 194.656 155.941 171.335 1.00 18.76 ? 1101 LYS A O      1 
ATOM   6829 C  CB     . LYS A 1 1101 ? 194.133 158.816 172.704 1.00 18.76 ? 1101 LYS A CB     1 
ATOM   6830 C  CG     . LYS A 1 1101 ? 194.526 160.251 172.996 1.00 18.76 ? 1101 LYS A CG     1 
ATOM   6831 C  CD     . LYS A 1 1101 ? 195.973 160.558 172.900 1.00 18.76 ? 1101 LYS A CD     1 
ATOM   6832 C  CE     . LYS A 1 1101 ? 196.176 162.019 173.205 1.00 18.76 ? 1101 LYS A CE     1 
ATOM   6833 N  NZ     . LYS A 1 1101 ? 195.753 162.342 174.589 1.00 18.76 ? 1101 LYS A NZ     1 
ATOM   6834 N  N      . PHE A 1 1102 ? 192.533 156.615 171.014 1.00 19.20 ? 1102 PHE A N      1 
ATOM   6835 C  CA     . PHE A 1 1102 ? 192.031 155.249 170.961 1.00 19.20 ? 1102 PHE A CA     1 
ATOM   6836 C  C      . PHE A 1 1102 ? 192.413 154.556 169.659 1.00 19.20 ? 1102 PHE A C      1 
ATOM   6837 O  O      . PHE A 1 1102 ? 192.806 153.386 169.674 1.00 19.20 ? 1102 PHE A O      1 
ATOM   6838 C  CB     . PHE A 1 1102 ? 190.516 155.236 171.143 1.00 19.20 ? 1102 PHE A CB     1 
ATOM   6839 C  CG     . PHE A 1 1102 ? 189.937 153.860 171.253 1.00 19.20 ? 1102 PHE A CG     1 
ATOM   6840 C  CD1    . PHE A 1 1102 ? 190.029 153.155 172.440 1.00 19.20 ? 1102 PHE A CD1    1 
ATOM   6841 C  CD2    . PHE A 1 1102 ? 189.312 153.263 170.171 1.00 19.20 ? 1102 PHE A CD2    1 
ATOM   6842 C  CE1    . PHE A 1 1102 ? 189.502 151.891 172.549 1.00 19.20 ? 1102 PHE A CE1    1 
ATOM   6843 C  CE2    . PHE A 1 1102 ? 188.788 151.994 170.275 1.00 19.20 ? 1102 PHE A CE2    1 
ATOM   6844 C  CZ     . PHE A 1 1102 ? 188.883 151.309 171.466 1.00 19.20 ? 1102 PHE A CZ     1 
ATOM   6845 N  N      . GLN A 1 1103 ? 192.286 155.239 168.518 1.00 18.86 ? 1103 GLN A N      1 
ATOM   6846 C  CA     . GLN A 1 1103 ? 192.637 154.591 167.256 1.00 18.86 ? 1103 GLN A CA     1 
ATOM   6847 C  C      . GLN A 1 1103 ? 194.140 154.510 167.034 1.00 18.86 ? 1103 GLN A C      1 
ATOM   6848 O  O      . GLN A 1 1103 ? 194.596 153.764 166.155 1.00 18.86 ? 1103 GLN A O      1 
ATOM   6849 C  CB     . GLN A 1 1103 ? 191.990 155.319 166.087 1.00 18.86 ? 1103 GLN A CB     1 
ATOM   6850 C  CG     . GLN A 1 1103 ? 192.501 156.704 165.917 1.00 18.86 ? 1103 GLN A CG     1 
ATOM   6851 C  CD     . GLN A 1 1103 ? 191.780 157.448 164.839 1.00 18.86 ? 1103 GLN A CD     1 
ATOM   6852 O  OE1    . GLN A 1 1103 ? 190.999 156.879 164.084 1.00 18.86 ? 1103 GLN A OE1    1 
ATOM   6853 N  NE2    . GLN A 1 1103 ? 192.002 158.741 164.787 1.00 18.86 ? 1103 GLN A NE2    1 
ATOM   6854 N  N      . ARG A 1 1104 ? 194.913 155.244 167.831 1.00 18.13 ? 1104 ARG A N      1 
ATOM   6855 C  CA     . ARG A 1 1104 ? 196.358 155.091 167.832 1.00 18.13 ? 1104 ARG A CA     1 
ATOM   6856 C  C      . ARG A 1 1104 ? 196.776 153.708 168.328 1.00 18.13 ? 1104 ARG A C      1 
ATOM   6857 O  O      . ARG A 1 1104 ? 197.814 153.187 167.905 1.00 18.13 ? 1104 ARG A O      1 
ATOM   6858 C  CB     . ARG A 1 1104 ? 196.938 156.218 168.678 1.00 18.13 ? 1104 ARG A CB     1 
ATOM   6859 C  CG     . ARG A 1 1104 ? 198.404 156.375 168.640 1.00 18.13 ? 1104 ARG A CG     1 
ATOM   6860 C  CD     . ARG A 1 1104 ? 198.764 157.694 169.260 1.00 18.13 ? 1104 ARG A CD     1 
ATOM   6861 N  NE     . ARG A 1 1104 ? 200.199 157.897 169.224 1.00 18.13 ? 1104 ARG A NE     1 
ATOM   6862 C  CZ     . ARG A 1 1104 ? 201.004 157.594 170.228 1.00 18.13 ? 1104 ARG A CZ     1 
ATOM   6863 N  NH1    . ARG A 1 1104 ? 200.502 157.116 171.355 1.00 18.13 ? 1104 ARG A NH1    1 
ATOM   6864 N  NH2    . ARG A 1 1104 ? 202.303 157.798 170.115 1.00 18.13 ? 1104 ARG A NH2    1 
ATOM   6865 N  N      . TYR A 1 1105 ? 195.949 153.078 169.174 1.00 18.90 ? 1105 TYR A N      1 
ATOM   6866 C  CA     . TYR A 1 1105 ? 196.169 151.687 169.568 1.00 18.90 ? 1105 TYR A CA     1 
ATOM   6867 C  C      . TYR A 1 1105 ? 196.082 150.749 168.374 1.00 18.90 ? 1105 TYR A C      1 
ATOM   6868 O  O      . TYR A 1 1105 ? 196.929 149.867 168.206 1.00 18.90 ? 1105 TYR A O      1 
ATOM   6869 C  CB     . TYR A 1 1105 ? 195.149 151.260 170.627 1.00 18.90 ? 1105 TYR A CB     1 
ATOM   6870 C  CG     . TYR A 1 1105 ? 195.318 149.825 171.101 1.00 18.90 ? 1105 TYR A CG     1 
ATOM   6871 C  CD1    . TYR A 1 1105 ? 196.260 149.503 172.062 1.00 18.90 ? 1105 TYR A CD1    1 
ATOM   6872 C  CD2    . TYR A 1 1105 ? 194.549 148.792 170.569 1.00 18.90 ? 1105 TYR A CD2    1 
ATOM   6873 C  CE1    . TYR A 1 1105 ? 196.431 148.207 172.491 1.00 18.90 ? 1105 TYR A CE1    1 
ATOM   6874 C  CE2    . TYR A 1 1105 ? 194.713 147.492 170.994 1.00 18.90 ? 1105 TYR A CE2    1 
ATOM   6875 C  CZ     . TYR A 1 1105 ? 195.656 147.206 171.957 1.00 18.90 ? 1105 TYR A CZ     1 
ATOM   6876 O  OH     . TYR A 1 1105 ? 195.823 145.912 172.385 1.00 18.90 ? 1105 TYR A OH     1 
ATOM   6877 N  N      . ASP A 1 1106 ? 195.030 150.891 167.564 1.00 19.23 ? 1106 ASP A N      1 
ATOM   6878 C  CA     . ASP A 1 1106 ? 194.862 150.035 166.396 1.00 19.23 ? 1106 ASP A CA     1 
ATOM   6879 C  C      . ASP A 1 1106 ? 195.950 150.290 165.369 1.00 19.23 ? 1106 ASP A C      1 
ATOM   6880 O  O      . ASP A 1 1106 ? 196.384 149.360 164.679 1.00 19.23 ? 1106 ASP A O      1 
ATOM   6881 C  CB     . ASP A 1 1106 ? 193.488 150.265 165.776 1.00 19.23 ? 1106 ASP A CB     1 
ATOM   6882 C  CG     . ASP A 1 1106 ? 192.360 149.803 166.671 1.00 19.23 ? 1106 ASP A CG     1 
ATOM   6883 O  OD1    . ASP A 1 1106 ? 192.558 148.836 167.435 1.00 19.23 ? 1106 ASP A OD1    1 
ATOM   6884 O  OD2    . ASP A 1 1106 ? 191.272 150.413 166.614 1.00 19.23 ? 1106 ASP A OD2    1 
ATOM   6885 N  N      . LEU A 1 1107 ? 196.416 151.537 165.283 1.00 17.98 ? 1107 LEU A N      1 
ATOM   6886 C  CA     . LEU A 1 1107 ? 197.566 151.858 164.445 1.00 17.98 ? 1107 LEU A CA     1 
ATOM   6887 C  C      . LEU A 1 1107 ? 198.830 151.143 164.915 1.00 17.98 ? 1107 LEU A C      1 
ATOM   6888 O  O      . LEU A 1 1107 ? 199.621 150.669 164.095 1.00 17.98 ? 1107 LEU A O      1 
ATOM   6889 C  CB     . LEU A 1 1107 ? 197.789 153.364 164.442 1.00 17.98 ? 1107 LEU A CB     1 
ATOM   6890 C  CG     . LEU A 1 1107 ? 198.893 153.884 163.535 1.00 17.98 ? 1107 LEU A CG     1 
ATOM   6891 C  CD1    . LEU A 1 1107 ? 198.513 153.754 162.074 1.00 17.98 ? 1107 LEU A CD1    1 
ATOM   6892 C  CD2    . LEU A 1 1107 ? 199.189 155.293 163.913 1.00 17.98 ? 1107 LEU A CD2    1 
ATOM   6893 N  N      . VAL A 1 1108 ? 199.052 151.085 166.229 1.00 18.68 ? 1108 VAL A N      1 
ATOM   6894 C  CA     . VAL A 1 1108 ? 200.224 150.385 166.753 1.00 18.68 ? 1108 VAL A CA     1 
ATOM   6895 C  C      . VAL A 1 1108 ? 200.093 148.881 166.539 1.00 18.68 ? 1108 VAL A C      1 
ATOM   6896 O  O      . VAL A 1 1108 ? 201.060 148.210 166.161 1.00 18.68 ? 1108 VAL A O      1 
ATOM   6897 C  CB     . VAL A 1 1108 ? 200.442 150.749 168.237 1.00 18.68 ? 1108 VAL A CB     1 
ATOM   6898 C  CG1    . VAL A 1 1108 ? 201.486 149.863 168.885 1.00 18.68 ? 1108 VAL A CG1    1 
ATOM   6899 C  CG2    . VAL A 1 1108 ? 200.892 152.181 168.359 1.00 18.68 ? 1108 VAL A CG2    1 
ATOM   6900 N  N      . GLN A 1 1109 ? 198.886 148.339 166.717 1.00 20.93 ? 1109 GLN A N      1 
ATOM   6901 C  CA     . GLN A 1 1109 ? 198.673 146.903 166.549 1.00 20.93 ? 1109 GLN A CA     1 
ATOM   6902 C  C      . GLN A 1 1109 ? 198.803 146.453 165.101 1.00 20.93 ? 1109 GLN A C      1 
ATOM   6903 O  O      . GLN A 1 1109 ? 199.251 145.331 164.848 1.00 20.93 ? 1109 GLN A O      1 
ATOM   6904 C  CB     . GLN A 1 1109 ? 197.302 146.497 167.079 1.00 20.93 ? 1109 GLN A CB     1 
ATOM   6905 C  CG     . GLN A 1 1109 ? 197.171 146.603 168.570 1.00 20.93 ? 1109 GLN A CG     1 
ATOM   6906 C  CD     . GLN A 1 1109 ? 198.191 145.765 169.298 1.00 20.93 ? 1109 GLN A CD     1 
ATOM   6907 O  OE1    . GLN A 1 1109 ? 199.094 146.294 169.948 1.00 20.93 ? 1109 GLN A OE1    1 
ATOM   6908 N  NE2    . GLN A 1 1109 ? 198.067 144.448 169.184 1.00 20.93 ? 1109 GLN A NE2    1 
ATOM   6909 N  N      . GLU A 1 1110 ? 198.413 147.287 164.139 1.00 22.96 ? 1110 GLU A N      1 
ATOM   6910 C  CA     . GLU A 1 1110 ? 198.508 146.854 162.752 1.00 22.96 ? 1110 GLU A CA     1 
ATOM   6911 C  C      . GLU A 1 1110 ? 199.915 146.929 162.186 1.00 22.96 ? 1110 GLU A C      1 
ATOM   6912 O  O      . GLU A 1 1110 ? 200.140 146.433 161.079 1.00 22.96 ? 1110 GLU A O      1 
ATOM   6913 C  CB     . GLU A 1 1110 ? 197.557 147.664 161.875 1.00 22.96 ? 1110 GLU A CB     1 
ATOM   6914 C  CG     . GLU A 1 1110 ? 196.102 147.293 162.108 1.00 22.96 ? 1110 GLU A CG     1 
ATOM   6915 C  CD     . GLU A 1 1110 ? 195.784 145.871 161.672 1.00 22.96 ? 1110 GLU A CD     1 
ATOM   6916 O  OE1    . GLU A 1 1110 ? 196.352 145.413 160.657 1.00 22.96 ? 1110 GLU A OE1    1 
ATOM   6917 O  OE2    . GLU A 1 1110 ? 194.981 145.203 162.359 1.00 22.96 ? 1110 GLU A OE2    1 
ATOM   6918 N  N      . TYR A 1 1111 ? 200.861 147.526 162.902 1.00 21.40 ? 1111 TYR A N      1 
ATOM   6919 C  CA     . TYR A 1 1111 ? 202.240 147.570 162.455 1.00 21.40 ? 1111 TYR A CA     1 
ATOM   6920 C  C      . TYR A 1 1111 ? 203.214 146.882 163.391 1.00 21.40 ? 1111 TYR A C      1 
ATOM   6921 O  O      . TYR A 1 1111 ? 204.384 146.739 163.033 1.00 21.40 ? 1111 TYR A O      1 
ATOM   6922 C  CB     . TYR A 1 1111 ? 202.680 149.021 162.227 1.00 21.40 ? 1111 TYR A CB     1 
ATOM   6923 C  CG     . TYR A 1 1111 ? 202.010 149.620 161.024 1.00 21.40 ? 1111 TYR A CG     1 
ATOM   6924 C  CD1    . TYR A 1 1111 ? 202.499 149.382 159.752 1.00 21.40 ? 1111 TYR A CD1    1 
ATOM   6925 C  CD2    . TYR A 1 1111 ? 200.861 150.379 161.154 1.00 21.40 ? 1111 TYR A CD2    1 
ATOM   6926 C  CE1    . TYR A 1 1111 ? 201.885 149.902 158.651 1.00 21.40 ? 1111 TYR A CE1    1 
ATOM   6927 C  CE2    . TYR A 1 1111 ? 200.232 150.903 160.056 1.00 21.40 ? 1111 TYR A CE2    1 
ATOM   6928 C  CZ     . TYR A 1 1111 ? 200.754 150.667 158.805 1.00 21.40 ? 1111 TYR A CZ     1 
ATOM   6929 O  OH     . TYR A 1 1111 ? 200.136 151.191 157.697 1.00 21.40 ? 1111 TYR A OH     1 
ATOM   6930 N  N      . HIS A 1 1112 ? 202.772 146.443 164.565 1.00 25.06 ? 1112 HIS A N      1 
ATOM   6931 C  CA     . HIS A 1 1112 ? 203.661 145.702 165.446 1.00 25.06 ? 1112 HIS A CA     1 
ATOM   6932 C  C      . HIS A 1 1112 ? 203.913 144.295 164.923 1.00 25.06 ? 1112 HIS A C      1 
ATOM   6933 O  O      . HIS A 1 1112 ? 204.987 143.730 165.154 1.00 25.06 ? 1112 HIS A O      1 
ATOM   6934 C  CB     . HIS A 1 1112 ? 203.073 145.665 166.853 1.00 25.06 ? 1112 HIS A CB     1 
ATOM   6935 C  CG     . HIS A 1 1112 ? 203.948 144.993 167.859 1.00 25.06 ? 1112 HIS A CG     1 
ATOM   6936 N  ND1    . HIS A 1 1112 ? 205.106 145.565 168.337 1.00 25.06 ? 1112 HIS A ND1    1 
ATOM   6937 C  CD2    . HIS A 1 1112 ? 203.831 143.799 168.485 1.00 25.06 ? 1112 HIS A CD2    1 
ATOM   6938 C  CE1    . HIS A 1 1112 ? 205.667 144.750 169.211 1.00 25.06 ? 1112 HIS A CE1    1 
ATOM   6939 N  NE2    . HIS A 1 1112 ? 204.914 143.671 169.318 1.00 25.06 ? 1112 HIS A NE2    1 
ATOM   6940 N  N      . SER A 1 1113 ? 202.954 143.729 164.197 1.00 29.01 ? 1113 SER A N      1 
ATOM   6941 C  CA     . SER A 1 1113 ? 203.036 142.359 163.716 1.00 29.01 ? 1113 SER A CA     1 
ATOM   6942 C  C      . SER A 1 1113 ? 203.609 142.238 162.310 1.00 29.01 ? 1113 SER A C      1 
ATOM   6943 O  O      . SER A 1 1113 ? 203.800 141.111 161.842 1.00 29.01 ? 1113 SER A O      1 
ATOM   6944 C  CB     . SER A 1 1113 ? 201.648 141.716 163.754 1.00 29.01 ? 1113 SER A CB     1 
ATOM   6945 O  OG     . SER A 1 1113 ? 200.766 142.373 162.861 1.00 29.01 ? 1113 SER A OG     1 
ATOM   6946 N  N      . ARG A 1 1114 ? 203.884 143.361 161.633 1.00 31.12 ? 1114 ARG A N      1 
ATOM   6947 C  CA     . ARG A 1 1114 ? 204.437 143.345 160.285 1.00 31.12 ? 1114 ARG A CA     1 
ATOM   6948 C  C      . ARG A 1 1114 ? 205.846 142.745 160.286 1.00 31.12 ? 1114 ARG A C      1 
ATOM   6949 O  O      . ARG A 1 1114 ? 206.519 142.733 161.319 1.00 31.12 ? 1114 ARG A O      1 
ATOM   6950 C  CB     . ARG A 1 1114 ? 204.475 144.763 159.715 1.00 31.12 ? 1114 ARG A CB     1 
ATOM   6951 C  CG     . ARG A 1 1114 ? 203.152 145.456 159.573 1.00 31.12 ? 1114 ARG A CG     1 
ATOM   6952 C  CD     . ARG A 1 1114 ? 202.305 144.808 158.531 1.00 31.12 ? 1114 ARG A CD     1 
ATOM   6953 N  NE     . ARG A 1 1114 ? 201.067 145.540 158.309 1.00 31.12 ? 1114 ARG A NE     1 
ATOM   6954 C  CZ     . ARG A 1 1114 ? 200.911 146.459 157.365 1.00 31.12 ? 1114 ARG A CZ     1 
ATOM   6955 N  NH1    . ARG A 1 1114 ? 201.913 146.741 156.548 1.00 31.12 ? 1114 ARG A NH1    1 
ATOM   6956 N  NH2    . ARG A 1 1114 ? 199.751 147.081 157.226 1.00 31.12 ? 1114 ARG A NH2    1 
ATOM   6957 N  N      . PRO A 1 1115 ? 206.306 142.218 159.144 1.00 41.67 ? 1115 PRO A N      1 
ATOM   6958 C  CA     . PRO A 1 1115 ? 207.644 141.612 159.105 1.00 41.67 ? 1115 PRO A CA     1 
ATOM   6959 C  C      . PRO A 1 1115 ? 208.772 142.624 159.253 1.00 41.67 ? 1115 PRO A C      1 
ATOM   6960 O  O      . PRO A 1 1115 ? 208.736 143.717 158.683 1.00 41.67 ? 1115 PRO A O      1 
ATOM   6961 C  CB     . PRO A 1 1115 ? 207.687 140.943 157.727 1.00 41.67 ? 1115 PRO A CB     1 
ATOM   6962 C  CG     . PRO A 1 1115 ? 206.279 140.684 157.398 1.00 41.67 ? 1115 PRO A CG     1 
ATOM   6963 C  CD     . PRO A 1 1115 ? 205.520 141.841 157.953 1.00 41.67 ? 1115 PRO A CD     1 
ATOM   6964 N  N      . VAL A 1 1116 ? 209.800 142.216 159.993 1.00 46.29 ? 1116 VAL A N      1 
ATOM   6965 C  CA     . VAL A 1 1116 ? 210.957 143.085 160.278 1.00 46.29 ? 1116 VAL A CA     1 
ATOM   6966 C  C      . VAL A 1 1116 ? 211.905 142.896 159.100 1.00 46.29 ? 1116 VAL A C      1 
ATOM   6967 O  O      . VAL A 1 1116 ? 212.896 142.160 159.147 1.00 46.29 ? 1116 VAL A O      1 
ATOM   6968 C  CB     . VAL A 1 1116 ? 211.600 142.735 161.631 1.00 46.29 ? 1116 VAL A CB     1 
ATOM   6969 C  CG1    . VAL A 1 1116 ? 212.840 143.579 161.936 1.00 46.29 ? 1116 VAL A CG1    1 
ATOM   6970 C  CG2    . VAL A 1 1116 ? 210.575 142.837 162.755 1.00 46.29 ? 1116 VAL A CG2    1 
ATOM   6971 N  N      . PHE A 1 1117 ? 211.585 143.570 158.001 1.00 56.26 ? 1117 PHE A N      1 
ATOM   6972 C  CA     . PHE A 1 1117 ? 212.281 143.368 156.734 1.00 56.26 ? 1117 PHE A CA     1 
ATOM   6973 C  C      . PHE A 1 1117 ? 212.165 144.653 155.920 1.00 56.26 ? 1117 PHE A C      1 
ATOM   6974 O  O      . PHE A 1 1117 ? 211.719 145.688 156.424 1.00 56.26 ? 1117 PHE A O      1 
ATOM   6975 C  CB     . PHE A 1 1117 ? 211.735 142.142 155.977 1.00 56.26 ? 1117 PHE A CB     1 
ATOM   6976 C  CG     . PHE A 1 1117 ? 212.145 140.810 156.577 1.00 56.26 ? 1117 PHE A CG     1 
ATOM   6977 C  CD1    . PHE A 1 1117 ? 213.408 140.291 156.338 1.00 56.26 ? 1117 PHE A CD1    1 
ATOM   6978 C  CD2    . PHE A 1 1117 ? 211.275 140.094 157.402 1.00 56.26 ? 1117 PHE A CD2    1 
ATOM   6979 C  CE1    . PHE A 1 1117 ? 213.796 139.081 156.895 1.00 56.26 ? 1117 PHE A CE1    1 
ATOM   6980 C  CE2    . PHE A 1 1117 ? 211.657 138.884 157.956 1.00 56.26 ? 1117 PHE A CE2    1 
ATOM   6981 C  CZ     . PHE A 1 1117 ? 212.919 138.377 157.701 1.00 56.26 ? 1117 PHE A CZ     1 
ATOM   6982 N  N      . ALA A 1 1118 ? 212.572 144.585 154.656 1.00 60.26 ? 1118 ALA A N      1 
ATOM   6983 C  CA     . ALA A 1 1118 ? 212.622 145.774 153.823 1.00 60.26 ? 1118 ALA A CA     1 
ATOM   6984 C  C      . ALA A 1 1118 ? 211.213 146.190 153.392 1.00 60.26 ? 1118 ALA A C      1 
ATOM   6985 O  O      . ALA A 1 1118 ? 210.311 145.354 153.302 1.00 60.26 ? 1118 ALA A O      1 
ATOM   6986 C  CB     . ALA A 1 1118 ? 213.498 145.527 152.598 1.00 60.26 ? 1118 ALA A CB     1 
ATOM   6987 N  N      . PRO A 1 1119 ? 210.992 147.481 153.157 1.00 55.16 ? 1119 PRO A N      1 
ATOM   6988 C  CA     . PRO A 1 1119 ? 209.660 147.945 152.732 1.00 55.16 ? 1119 PRO A CA     1 
ATOM   6989 C  C      . PRO A 1 1119 ? 209.300 147.568 151.298 1.00 55.16 ? 1119 PRO A C      1 
ATOM   6990 O  O      . PRO A 1 1119 ? 208.114 147.315 151.040 1.00 55.16 ? 1119 PRO A O      1 
ATOM   6991 C  CB     . PRO A 1 1119 ? 209.736 149.469 152.925 1.00 55.16 ? 1119 PRO A CB     1 
ATOM   6992 C  CG     . PRO A 1 1119 ? 210.778 149.654 153.965 1.00 55.16 ? 1119 PRO A CG     1 
ATOM   6993 C  CD     . PRO A 1 1119 ? 211.797 148.589 153.705 1.00 55.16 ? 1119 PRO A CD     1 
ATOM   6994 N  N      . PRO A 1 1120 ? 210.255 147.520 150.291 1.00 58.42 ? 1120 PRO A N      1 
ATOM   6995 C  CA     . PRO A 1 1120 ? 209.834 146.936 149.005 1.00 58.42 ? 1120 PRO A CA     1 
ATOM   6996 C  C      . PRO A 1 1120 ? 209.921 145.419 148.975 1.00 58.42 ? 1120 PRO A C      1 
ATOM   6997 O  O      . PRO A 1 1120 ? 209.261 144.772 148.155 1.00 58.42 ? 1120 PRO A O      1 
ATOM   6998 C  CB     . PRO A 1 1120 ? 210.805 147.556 147.989 1.00 58.42 ? 1120 PRO A CB     1 
ATOM   6999 C  CG     . PRO A 1 1120 ? 211.370 148.731 148.655 1.00 58.42 ? 1120 PRO A CG     1 
ATOM   7000 C  CD     . PRO A 1 1120 ? 211.488 148.308 150.074 1.00 58.42 ? 1120 PRO A CD     1 
ATOM   7001 N  N      . LEU A 1 1121 ? 210.733 144.839 149.855 1.00 60.84 ? 1121 LEU A N      1 
ATOM   7002 C  CA     . LEU A 1 1121 ? 210.978 143.398 149.875 1.00 60.84 ? 1121 LEU A CA     1 
ATOM   7003 C  C      . LEU A 1 1121 ? 210.238 142.708 151.012 1.00 60.84 ? 1121 LEU A C      1 
ATOM   7004 O  O      . LEU A 1 1121 ? 210.761 141.773 151.624 1.00 60.84 ? 1121 LEU A O      1 
ATOM   7005 C  CB     . LEU A 1 1121 ? 212.475 143.122 149.968 1.00 60.84 ? 1121 LEU A CB     1 
ATOM   7006 C  CG     . LEU A 1 1121 ? 213.355 143.549 148.792 1.00 60.84 ? 1121 LEU A CG     1 
ATOM   7007 C  CD1    . LEU A 1 1121 ? 214.819 143.365 149.144 1.00 60.84 ? 1121 LEU A CD1    1 
ATOM   7008 C  CD2    . LEU A 1 1121 ? 213.002 142.760 147.543 1.00 60.84 ? 1121 LEU A CD2    1 
ATOM   7009 N  N      . VAL A 1 1122 ? 209.020 143.149 151.325 1.00 57.67 ? 1122 VAL A N      1 
ATOM   7010 C  CA     . VAL A 1 1122 ? 208.295 142.572 152.452 1.00 57.67 ? 1122 VAL A CA     1 
ATOM   7011 C  C      . VAL A 1 1122 ? 207.655 141.228 152.090 1.00 57.67 ? 1122 VAL A C      1 
ATOM   7012 O  O      . VAL A 1 1122 ? 207.415 140.401 152.980 1.00 57.67 ? 1122 VAL A O      1 
ATOM   7013 C  CB     . VAL A 1 1122 ? 207.310 143.637 152.982 1.00 57.67 ? 1122 VAL A CB     1 
ATOM   7014 C  CG1    . VAL A 1 1122 ? 206.275 143.999 151.947 1.00 57.67 ? 1122 VAL A CG1    1 
ATOM   7015 C  CG2    . VAL A 1 1122 ? 206.666 143.234 154.315 1.00 57.67 ? 1122 VAL A CG2    1 
ATOM   7016 N  N      . LEU A 1 1123 ? 207.426 140.953 150.802 1.00 54.02 ? 1123 LEU A N      1 
ATOM   7017 C  CA     . LEU A 1 1123 ? 207.067 139.593 150.401 1.00 54.02 ? 1123 LEU A CA     1 
ATOM   7018 C  C      . LEU A 1 1123 ? 208.250 138.650 150.554 1.00 54.02 ? 1123 LEU A C      1 
ATOM   7019 O  O      . LEU A 1 1123 ? 208.090 137.502 150.990 1.00 54.02 ? 1123 LEU A O      1 
ATOM   7020 C  CB     . LEU A 1 1123 ? 206.570 139.572 148.960 1.00 54.02 ? 1123 LEU A CB     1 
ATOM   7021 C  CG     . LEU A 1 1123 ? 206.101 138.212 148.449 1.00 54.02 ? 1123 LEU A CG     1 
ATOM   7022 C  CD1    . LEU A 1 1123 ? 204.929 137.715 149.275 1.00 54.02 ? 1123 LEU A CD1    1 
ATOM   7023 C  CD2    . LEU A 1 1123 ? 205.720 138.307 146.995 1.00 54.02 ? 1123 LEU A CD2    1 
ATOM   7024 N  N      . LEU A 1 1124 ? 209.451 139.127 150.208 1.00 62.12 ? 1124 LEU A N      1 
ATOM   7025 C  CA     . LEU A 1 1124 ? 210.679 138.410 150.535 1.00 62.12 ? 1124 LEU A CA     1 
ATOM   7026 C  C      . LEU A 1 1124 ? 210.842 138.261 152.043 1.00 62.12 ? 1124 LEU A C      1 
ATOM   7027 O  O      . LEU A 1 1124 ? 211.413 137.272 152.516 1.00 62.12 ? 1124 LEU A O      1 
ATOM   7028 C  CB     . LEU A 1 1124 ? 211.869 139.146 149.907 1.00 62.12 ? 1124 LEU A CB     1 
ATOM   7029 C  CG     . LEU A 1 1124 ? 213.299 138.606 149.899 1.00 62.12 ? 1124 LEU A CG     1 
ATOM   7030 C  CD1    . LEU A 1 1124 ? 213.985 139.042 148.618 1.00 62.12 ? 1124 LEU A CD1    1 
ATOM   7031 C  CD2    . LEU A 1 1124 ? 214.088 139.125 151.086 1.00 62.12 ? 1124 LEU A CD2    1 
ATOM   7032 N  N      . GLY A 1 1125 ? 210.307 139.211 152.809 1.00 62.28 ? 1125 GLY A N      1 
ATOM   7033 C  CA     . GLY A 1 1125 ? 210.264 139.054 154.250 1.00 62.28 ? 1125 GLY A CA     1 
ATOM   7034 C  C      . GLY A 1 1125 ? 209.335 137.947 154.712 1.00 62.28 ? 1125 GLY A C      1 
ATOM   7035 O  O      . GLY A 1 1125 ? 209.654 137.215 155.653 1.00 62.28 ? 1125 GLY A O      1 
ATOM   7036 N  N      . HIS A 1 1126 ? 208.175 137.809 154.063 1.00 56.55 ? 1126 HIS A N      1 
ATOM   7037 C  CA     . HIS A 1 1126 ? 207.292 136.681 154.353 1.00 56.55 ? 1126 HIS A CA     1 
ATOM   7038 C  C      . HIS A 1 1126 ? 207.931 135.356 153.956 1.00 56.55 ? 1126 HIS A C      1 
ATOM   7039 O  O      . HIS A 1 1126 ? 207.709 134.335 154.621 1.00 56.55 ? 1126 HIS A O      1 
ATOM   7040 C  CB     . HIS A 1 1126 ? 205.959 136.851 153.627 1.00 56.55 ? 1126 HIS A CB     1 
ATOM   7041 C  CG     . HIS A 1 1126 ? 205.156 138.021 154.100 1.00 56.55 ? 1126 HIS A CG     1 
ATOM   7042 N  ND1    . HIS A 1 1126 ? 205.274 139.277 153.546 1.00 56.55 ? 1126 HIS A ND1    1 
ATOM   7043 C  CD2    . HIS A 1 1126 ? 204.219 138.125 155.071 1.00 56.55 ? 1126 HIS A CD2    1 
ATOM   7044 C  CE1    . HIS A 1 1126 ? 204.445 140.105 154.156 1.00 56.55 ? 1126 HIS A CE1    1 
ATOM   7045 N  NE2    . HIS A 1 1126 ? 203.794 139.431 155.087 1.00 56.55 ? 1126 HIS A NE2    1 
ATOM   7046 N  N      . ILE A 1 1127 ? 208.719 135.363 152.878 1.00 65.83 ? 1127 ILE A N      1 
ATOM   7047 C  CA     . ILE A 1 1127 ? 209.476 134.179 152.472 1.00 65.83 ? 1127 ILE A CA     1 
ATOM   7048 C  C      . ILE A 1 1127 ? 210.497 133.804 153.542 1.00 65.83 ? 1127 ILE A C      1 
ATOM   7049 O  O      . ILE A 1 1127 ? 210.616 132.635 153.932 1.00 65.83 ? 1127 ILE A O      1 
ATOM   7050 C  CB     . ILE A 1 1127 ? 210.143 134.418 151.104 1.00 65.83 ? 1127 ILE A CB     1 
ATOM   7051 C  CG1    . ILE A 1 1127 ? 209.083 134.531 150.005 1.00 65.83 ? 1127 ILE A CG1    1 
ATOM   7052 C  CG2    . ILE A 1 1127 ? 211.143 133.319 150.773 1.00 65.83 ? 1127 ILE A CG2    1 
ATOM   7053 C  CD1    . ILE A 1 1127 ? 209.623 135.015 148.679 1.00 65.83 ? 1127 ILE A CD1    1 
ATOM   7054 N  N      . LEU A 1 1128 ? 211.225 134.797 154.059 1.00 69.37 ? 1128 LEU A N      1 
ATOM   7055 C  CA     . LEU A 1 1128 ? 212.232 134.517 155.079 1.00 69.37 ? 1128 LEU A CA     1 
ATOM   7056 C  C      . LEU A 1 1128 ? 211.625 134.200 156.443 1.00 69.37 ? 1128 LEU A C      1 
ATOM   7057 O  O      . LEU A 1 1128 ? 212.302 133.586 157.274 1.00 69.37 ? 1128 LEU A O      1 
ATOM   7058 C  CB     . LEU A 1 1128 ? 213.213 135.685 155.192 1.00 69.37 ? 1128 LEU A CB     1 
ATOM   7059 C  CG     . LEU A 1 1128 ? 214.108 135.880 153.963 1.00 69.37 ? 1128 LEU A CG     1 
ATOM   7060 C  CD1    . LEU A 1 1128 ? 215.014 137.094 154.121 1.00 69.37 ? 1128 LEU A CD1    1 
ATOM   7061 C  CD2    . LEU A 1 1128 ? 214.923 134.627 153.680 1.00 69.37 ? 1128 LEU A CD2    1 
ATOM   7062 N  N      . ILE A 1 1129 ? 210.380 134.606 156.700 1.00 68.01 ? 1129 ILE A N      1 
ATOM   7063 C  CA     . ILE A 1 1129 ? 209.691 134.132 157.899 1.00 68.01 ? 1129 ILE A CA     1 
ATOM   7064 C  C      . ILE A 1 1129 ? 209.240 132.685 157.724 1.00 68.01 ? 1129 ILE A C      1 
ATOM   7065 O  O      . ILE A 1 1129 ? 209.425 131.854 158.623 1.00 68.01 ? 1129 ILE A O      1 
ATOM   7066 C  CB     . ILE A 1 1129 ? 208.514 135.063 158.258 1.00 68.01 ? 1129 ILE A CB     1 
ATOM   7067 C  CG1    . ILE A 1 1129 ? 209.028 136.412 158.763 1.00 68.01 ? 1129 ILE A CG1    1 
ATOM   7068 C  CG2    . ILE A 1 1129 ? 207.593 134.439 159.305 1.00 68.01 ? 1129 ILE A CG2    1 
ATOM   7069 C  CD1    . ILE A 1 1129 ? 207.934 137.432 158.966 1.00 68.01 ? 1129 ILE A CD1    1 
ATOM   7070 N  N      . PHE A 1 1130 ? 208.672 132.355 156.556 1.00 70.71 ? 1130 PHE A N      1 
ATOM   7071 C  CA     . PHE A 1 1130 ? 208.193 130.997 156.303 1.00 70.71 ? 1130 PHE A CA     1 
ATOM   7072 C  C      . PHE A 1 1130 ? 209.334 129.986 156.234 1.00 70.71 ? 1130 PHE A C      1 
ATOM   7073 O  O      . PHE A 1 1130 ? 209.141 128.813 156.574 1.00 70.71 ? 1130 PHE A O      1 
ATOM   7074 C  CB     . PHE A 1 1130 ? 207.379 130.970 155.009 1.00 70.71 ? 1130 PHE A CB     1 
ATOM   7075 C  CG     . PHE A 1 1130 ? 206.776 129.631 154.694 1.00 70.71 ? 1130 PHE A CG     1 
ATOM   7076 C  CD1    . PHE A 1 1130 ? 205.669 129.174 155.394 1.00 70.71 ? 1130 PHE A CD1    1 
ATOM   7077 C  CD2    . PHE A 1 1130 ? 207.309 128.833 153.692 1.00 70.71 ? 1130 PHE A CD2    1 
ATOM   7078 C  CE1    . PHE A 1 1130 ? 205.107 127.944 155.107 1.00 70.71 ? 1130 PHE A CE1    1 
ATOM   7079 C  CE2    . PHE A 1 1130 ? 206.752 127.600 153.399 1.00 70.71 ? 1130 PHE A CE2    1 
ATOM   7080 C  CZ     . PHE A 1 1130 ? 205.649 127.156 154.108 1.00 70.71 ? 1130 PHE A CZ     1 
ATOM   7081 N  N      . ILE A 1 1131 ? 210.522 130.415 155.817 1.00 70.81 ? 1131 ILE A N      1 
ATOM   7082 C  CA     . ILE A 1 1131 ? 211.685 129.537 155.787 1.00 70.81 ? 1131 ILE A CA     1 
ATOM   7083 C  C      . ILE A 1 1131 ? 212.727 130.002 156.795 1.00 70.81 ? 1131 ILE A C      1 
ATOM   7084 O  O      . ILE A 1 1131 ? 212.399 130.651 157.787 1.00 70.81 ? 1131 ILE A O      1 
ATOM   7085 C  CB     . ILE A 1 1131 ? 212.290 129.459 154.376 1.00 70.81 ? 1131 ILE A CB     1 
ATOM   7086 C  CG1    . ILE A 1 1131 ? 211.275 128.880 153.389 1.00 70.81 ? 1131 ILE A CG1    1 
ATOM   7087 C  CG2    . ILE A 1 1131 ? 213.566 128.632 154.390 1.00 70.81 ? 1131 ILE A CG2    1 
ATOM   7088 C  CD1    . ILE A 1 1131 ? 210.838 127.468 153.721 1.00 70.81 ? 1131 ILE A CD1    1 
ATOM   7089 N  N      . LYS A 1 1150 ? 201.622 142.353 176.259 1.00 38.95 ? 1150 LYS A N      1 
ATOM   7090 C  CA     . LYS A 1 1150 ? 201.648 140.967 176.706 1.00 38.95 ? 1150 LYS A CA     1 
ATOM   7091 C  C      . LYS A 1 1150 ? 203.020 140.562 177.222 1.00 38.95 ? 1150 LYS A C      1 
ATOM   7092 O  O      . LYS A 1 1150 ? 203.843 140.059 176.461 1.00 38.95 ? 1150 LYS A O      1 
ATOM   7093 C  CB     . LYS A 1 1150 ? 201.244 140.024 175.572 1.00 38.95 ? 1150 LYS A CB     1 
ATOM   7094 C  CG     . LYS A 1 1150 ? 199.783 140.073 175.161 1.00 38.95 ? 1150 LYS A CG     1 
ATOM   7095 C  CD     . LYS A 1 1150 ? 199.537 139.072 174.037 1.00 38.95 ? 1150 LYS A CD     1 
ATOM   7096 C  CE     . LYS A 1 1150 ? 198.096 139.072 173.567 1.00 38.95 ? 1150 LYS A CE     1 
ATOM   7097 N  NZ     . LYS A 1 1150 ? 197.883 138.117 172.444 1.00 38.95 ? 1150 LYS A NZ     1 
ATOM   7098 N  N      . ILE A 1 1151 ? 203.275 140.778 178.511 1.00 40.49 ? 1151 ILE A N      1 
ATOM   7099 C  CA     . ILE A 1 1151 ? 204.507 140.313 179.129 1.00 40.49 ? 1151 ILE A CA     1 
ATOM   7100 C  C      . ILE A 1 1151 ? 204.153 139.334 180.241 1.00 40.49 ? 1151 ILE A C      1 
ATOM   7101 O  O      . ILE A 1 1151 ? 203.032 139.308 180.755 1.00 40.49 ? 1151 ILE A O      1 
ATOM   7102 C  CB     . ILE A 1 1151 ? 205.380 141.464 179.677 1.00 40.49 ? 1151 ILE A CB     1 
ATOM   7103 C  CG1    . ILE A 1 1151 ? 204.711 142.143 180.871 1.00 40.49 ? 1151 ILE A CG1    1 
ATOM   7104 C  CG2    . ILE A 1 1151 ? 205.659 142.487 178.589 1.00 40.49 ? 1151 ILE A CG2    1 
ATOM   7105 C  CD1    . ILE A 1 1151 ? 205.602 143.132 181.586 1.00 40.49 ? 1151 ILE A CD1    1 
ATOM   7106 N  N      . GLY A 1 1152 ? 205.129 138.506 180.596 1.00 52.33 ? 1152 GLY A N      1 
ATOM   7107 C  CA     . GLY A 1 1152 ? 204.969 137.584 181.700 1.00 52.33 ? 1152 GLY A CA     1 
ATOM   7108 C  C      . GLY A 1 1152 ? 205.948 137.884 182.812 1.00 52.33 ? 1152 GLY A C      1 
ATOM   7109 O  O      . GLY A 1 1152 ? 207.143 138.058 182.561 1.00 52.33 ? 1152 GLY A O      1 
ATOM   7110 N  N      . LEU A 1 1153 ? 205.458 137.953 184.043 1.00 56.46 ? 1153 LEU A N      1 
ATOM   7111 C  CA     . LEU A 1 1153 ? 206.291 138.270 185.192 1.00 56.46 ? 1153 LEU A CA     1 
ATOM   7112 C  C      . LEU A 1 1153 ? 206.514 137.016 186.028 1.00 56.46 ? 1153 LEU A C      1 
ATOM   7113 O  O      . LEU A 1 1153 ? 205.865 135.984 185.837 1.00 56.46 ? 1153 LEU A O      1 
ATOM   7114 C  CB     . LEU A 1 1153 ? 205.654 139.374 186.051 1.00 56.46 ? 1153 LEU A CB     1 
ATOM   7115 C  CG     . LEU A 1 1153 ? 205.647 140.847 185.618 1.00 56.46 ? 1153 LEU A CG     1 
ATOM   7116 C  CD1    . LEU A 1 1153 ? 204.578 141.139 184.578 1.00 56.46 ? 1153 LEU A CD1    1 
ATOM   7117 C  CD2    . LEU A 1 1153 ? 205.470 141.760 186.821 1.00 56.46 ? 1153 LEU A CD2    1 
ATOM   7118 N  N      . SER A 1 1154 ? 207.452 137.120 186.966 1.00 58.78 ? 1154 SER A N      1 
ATOM   7119 C  CA     . SER A 1 1154 ? 207.638 136.084 187.964 1.00 58.78 ? 1154 SER A CA     1 
ATOM   7120 C  C      . SER A 1 1154 ? 206.436 136.065 188.907 1.00 58.78 ? 1154 SER A C      1 
ATOM   7121 O  O      . SER A 1 1154 ? 205.726 137.067 189.029 1.00 58.78 ? 1154 SER A O      1 
ATOM   7122 C  CB     . SER A 1 1154 ? 208.928 136.334 188.744 1.00 58.78 ? 1154 SER A CB     1 
ATOM   7123 O  OG     . SER A 1 1154 ? 210.059 136.267 187.894 1.00 58.78 ? 1154 SER A OG     1 
ATOM   7124 N  N      . PRO A 1 1155 ? 206.160 134.923 189.554 1.00 57.27 ? 1155 PRO A N      1 
ATOM   7125 C  CA     . PRO A 1 1155 ? 205.070 134.894 190.547 1.00 57.27 ? 1155 PRO A CA     1 
ATOM   7126 C  C      . PRO A 1 1155 ? 205.288 135.828 191.724 1.00 57.27 ? 1155 PRO A C      1 
ATOM   7127 O  O      . PRO A 1 1155 ? 204.320 136.426 192.212 1.00 57.27 ? 1155 PRO A O      1 
ATOM   7128 C  CB     . PRO A 1 1155 ? 205.038 133.424 190.985 1.00 57.27 ? 1155 PRO A CB     1 
ATOM   7129 C  CG     . PRO A 1 1155 ? 205.582 132.682 189.816 1.00 57.27 ? 1155 PRO A CG     1 
ATOM   7130 C  CD     . PRO A 1 1155 ? 206.647 133.566 189.243 1.00 57.27 ? 1155 PRO A CD     1 
ATOM   7131 N  N      . ALA A 1 1156 ? 206.534 135.995 192.173 1.00 55.48 ? 1156 ALA A N      1 
ATOM   7132 C  CA     . ALA A 1 1156 ? 206.830 137.033 193.153 1.00 55.48 ? 1156 ALA A CA     1 
ATOM   7133 C  C      . ALA A 1 1156 ? 206.644 138.419 192.551 1.00 55.48 ? 1156 ALA A C      1 
ATOM   7134 O  O      . ALA A 1 1156 ? 206.138 139.330 193.219 1.00 55.48 ? 1156 ALA A O      1 
ATOM   7135 C  CB     . ALA A 1 1156 ? 208.251 136.865 193.687 1.00 55.48 ? 1156 ALA A CB     1 
ATOM   7136 N  N      . GLU A 1 1157 ? 207.020 138.588 191.279 1.00 55.21 ? 1157 GLU A N      1 
ATOM   7137 C  CA     . GLU A 1 1157 ? 206.825 139.869 190.608 1.00 55.21 ? 1157 GLU A CA     1 
ATOM   7138 C  C      . GLU A 1 1157 ? 205.350 140.146 190.354 1.00 55.21 ? 1157 GLU A C      1 
ATOM   7139 O  O      . GLU A 1 1157 ? 204.904 141.289 190.496 1.00 55.21 ? 1157 GLU A O      1 
ATOM   7140 C  CB     . GLU A 1 1157 ? 207.610 139.910 189.300 1.00 55.21 ? 1157 GLU A CB     1 
ATOM   7141 C  CG     . GLU A 1 1157 ? 209.115 139.985 189.477 1.00 55.21 ? 1157 GLU A CG     1 
ATOM   7142 C  CD     . GLU A 1 1157 ? 209.854 139.986 188.155 1.00 55.21 ? 1157 GLU A CD     1 
ATOM   7143 O  OE1    . GLU A 1 1157 ? 209.201 139.802 187.106 1.00 55.21 ? 1157 GLU A OE1    1 
ATOM   7144 O  OE2    . GLU A 1 1157 ? 211.089 140.169 188.162 1.00 55.21 ? 1157 GLU A OE2    1 
ATOM   7145 N  N      . MET A 1 1158 ? 204.575 139.116 189.988 1.00 50.54 ? 1158 MET A N      1 
ATOM   7146 C  CA     . MET A 1 1158 ? 203.133 139.296 189.834 1.00 50.54 ? 1158 MET A CA     1 
ATOM   7147 C  C      . MET A 1 1158 ? 202.465 139.618 191.163 1.00 50.54 ? 1158 MET A C      1 
ATOM   7148 O  O      . MET A 1 1158 ? 201.538 140.433 191.209 1.00 50.54 ? 1158 MET A O      1 
ATOM   7149 C  CB     . MET A 1 1158 ? 202.487 138.058 189.214 1.00 50.54 ? 1158 MET A CB     1 
ATOM   7150 C  CG     . MET A 1 1158 ? 202.756 137.877 187.740 1.00 50.54 ? 1158 MET A CG     1 
ATOM   7151 S  SD     . MET A 1 1158 ? 201.814 136.523 187.020 1.00 50.54 ? 1158 MET A SD     1 
ATOM   7152 C  CE     . MET A 1 1158 ? 202.693 135.106 187.663 1.00 50.54 ? 1158 MET A CE     1 
ATOM   7153 N  N      . GLU A 1 1159 ? 202.942 139.016 192.256 1.00 44.86 ? 1159 GLU A N      1 
ATOM   7154 C  CA     . GLU A 1 1159 ? 202.376 139.310 193.569 1.00 44.86 ? 1159 GLU A CA     1 
ATOM   7155 C  C      . GLU A 1 1159 ? 202.706 140.731 194.015 1.00 44.86 ? 1159 GLU A C      1 
ATOM   7156 O  O      . GLU A 1 1159 ? 201.835 141.439 194.535 1.00 44.86 ? 1159 GLU A O      1 
ATOM   7157 C  CB     . GLU A 1 1159 ? 202.875 138.289 194.592 1.00 44.86 ? 1159 GLU A CB     1 
ATOM   7158 C  CG     . GLU A 1 1159 ? 202.320 138.473 195.997 1.00 44.86 ? 1159 GLU A CG     1 
ATOM   7159 C  CD     . GLU A 1 1159 ? 200.832 138.193 196.094 1.00 44.86 ? 1159 GLU A CD     1 
ATOM   7160 O  OE1    . GLU A 1 1159 ? 200.315 137.389 195.290 1.00 44.86 ? 1159 GLU A OE1    1 
ATOM   7161 O  OE2    . GLU A 1 1159 ? 200.175 138.781 196.979 1.00 44.86 ? 1159 GLU A OE2    1 
ATOM   7162 N  N      . GLN A 1 1160 ? 203.949 141.175 193.797 1.00 42.11 ? 1160 GLN A N      1 
ATOM   7163 C  CA     . GLN A 1 1160 ? 204.321 142.544 194.147 1.00 42.11 ? 1160 GLN A CA     1 
ATOM   7164 C  C      . GLN A 1 1160 ? 203.611 143.561 193.265 1.00 42.11 ? 1160 GLN A C      1 
ATOM   7165 O  O      . GLN A 1 1160 ? 203.243 144.643 193.731 1.00 42.11 ? 1160 GLN A O      1 
ATOM   7166 C  CB     . GLN A 1 1160 ? 205.833 142.728 194.048 1.00 42.11 ? 1160 GLN A CB     1 
ATOM   7167 C  CG     . GLN A 1 1160 ? 206.617 142.019 195.128 1.00 42.11 ? 1160 GLN A CG     1 
ATOM   7168 C  CD     . GLN A 1 1160 ? 208.107 142.227 194.984 1.00 42.11 ? 1160 GLN A CD     1 
ATOM   7169 O  OE1    . GLN A 1 1160 ? 208.569 142.840 194.022 1.00 42.11 ? 1160 GLN A OE1    1 
ATOM   7170 N  NE2    . GLN A 1 1160 ? 208.871 141.722 195.944 1.00 42.11 ? 1160 GLN A NE2    1 
ATOM   7171 N  N      . MET A 1 1161 ? 203.392 143.222 191.995 1.00 37.41 ? 1161 MET A N      1 
ATOM   7172 C  CA     . MET A 1 1161 ? 202.710 144.131 191.085 1.00 37.41 ? 1161 MET A CA     1 
ATOM   7173 C  C      . MET A 1 1161 ? 201.228 144.236 191.425 1.00 37.41 ? 1161 MET A C      1 
ATOM   7174 O  O      . MET A 1 1161 ? 200.647 145.324 191.349 1.00 37.41 ? 1161 MET A O      1 
ATOM   7175 C  CB     . MET A 1 1161 ? 202.919 143.644 189.654 1.00 37.41 ? 1161 MET A CB     1 
ATOM   7176 C  CG     . MET A 1 1161 ? 202.516 144.623 188.585 1.00 37.41 ? 1161 MET A CG     1 
ATOM   7177 S  SD     . MET A 1 1161 ? 203.554 146.089 188.552 1.00 37.41 ? 1161 MET A SD     1 
ATOM   7178 C  CE     . MET A 1 1161 ? 205.051 145.387 187.876 1.00 37.41 ? 1161 MET A CE     1 
ATOM   7179 N  N      . ASP A 1 1162 ? 200.611 143.116 191.824 1.00 35.93 ? 1162 ASP A N      1 
ATOM   7180 C  CA     . ASP A 1 1162 ? 199.239 143.134 192.325 1.00 35.93 ? 1162 ASP A CA     1 
ATOM   7181 C  C      . ASP A 1 1162 ? 199.122 143.940 193.608 1.00 35.93 ? 1162 ASP A C      1 
ATOM   7182 O  O      . ASP A 1 1162 ? 198.148 144.678 193.790 1.00 35.93 ? 1162 ASP A O      1 
ATOM   7183 C  CB     . ASP A 1 1162 ? 198.743 141.710 192.563 1.00 35.93 ? 1162 ASP A CB     1 
ATOM   7184 C  CG     . ASP A 1 1162 ? 198.383 140.991 191.284 1.00 35.93 ? 1162 ASP A CG     1 
ATOM   7185 O  OD1    . ASP A 1 1162 ? 197.965 141.660 190.319 1.00 35.93 ? 1162 ASP A OD1    1 
ATOM   7186 O  OD2    . ASP A 1 1162 ? 198.503 139.749 191.247 1.00 35.93 ? 1162 ASP A OD2    1 
ATOM   7187 N  N      . ASN A 1 1163 ? 200.103 143.808 194.507 1.00 34.22 ? 1163 ASN A N      1 
ATOM   7188 C  CA     . ASN A 1 1163 ? 200.092 144.584 195.744 1.00 34.22 ? 1163 ASN A CA     1 
ATOM   7189 C  C      . ASN A 1 1163 ? 200.233 146.072 195.465 1.00 34.22 ? 1163 ASN A C      1 
ATOM   7190 O  O      . ASN A 1 1163 ? 199.532 146.888 196.066 1.00 34.22 ? 1163 ASN A O      1 
ATOM   7191 C  CB     . ASN A 1 1163 ? 201.209 144.110 196.672 1.00 34.22 ? 1163 ASN A CB     1 
ATOM   7192 C  CG     . ASN A 1 1163 ? 200.938 142.744 197.256 1.00 34.22 ? 1163 ASN A CG     1 
ATOM   7193 O  OD1    . ASN A 1 1163 ? 199.822 142.447 197.676 1.00 34.22 ? 1163 ASN A OD1    1 
ATOM   7194 N  ND2    . ASN A 1 1163 ? 201.959 141.897 197.279 1.00 34.22 ? 1163 ASN A ND2    1 
ATOM   7195 N  N      . TRP A 1 1164 ? 201.110 146.436 194.528 1.00 28.84 ? 1164 TRP A N      1 
ATOM   7196 C  CA     . TRP A 1 1164 ? 201.317 147.836 194.174 1.00 28.84 ? 1164 TRP A CA     1 
ATOM   7197 C  C      . TRP A 1 1164 ? 200.084 148.437 193.509 1.00 28.84 ? 1164 TRP A C      1 
ATOM   7198 O  O      . TRP A 1 1164 ? 199.698 149.575 193.809 1.00 28.84 ? 1164 TRP A O      1 
ATOM   7199 C  CB     . TRP A 1 1164 ? 202.524 147.951 193.249 1.00 28.84 ? 1164 TRP A CB     1 
ATOM   7200 C  CG     . TRP A 1 1164 ? 202.862 149.346 192.895 1.00 28.84 ? 1164 TRP A CG     1 
ATOM   7201 C  CD1    . TRP A 1 1164 ? 203.431 150.275 193.702 1.00 28.84 ? 1164 TRP A CD1    1 
ATOM   7202 C  CD2    . TRP A 1 1164 ? 202.601 149.997 191.652 1.00 28.84 ? 1164 TRP A CD2    1 
ATOM   7203 N  NE1    . TRP A 1 1164 ? 203.572 151.461 193.031 1.00 28.84 ? 1164 TRP A NE1    1 
ATOM   7204 C  CE2    . TRP A 1 1164 ? 203.067 151.316 191.767 1.00 28.84 ? 1164 TRP A CE2    1 
ATOM   7205 C  CE3    . TRP A 1 1164 ? 202.033 149.586 190.445 1.00 28.84 ? 1164 TRP A CE3    1 
ATOM   7206 C  CZ2    . TRP A 1 1164 ? 202.981 152.229 190.724 1.00 28.84 ? 1164 TRP A CZ2    1 
ATOM   7207 C  CZ3    . TRP A 1 1164 ? 201.943 150.492 189.418 1.00 28.84 ? 1164 TRP A CZ3    1 
ATOM   7208 C  CH2    . TRP A 1 1164 ? 202.412 151.800 189.562 1.00 28.84 ? 1164 TRP A CH2    1 
ATOM   7209 N  N      . GLU A 1 1165 ? 199.457 147.681 192.603 1.00 28.20 ? 1165 GLU A N      1 
ATOM   7210 C  CA     . GLU A 1 1165 ? 198.231 148.125 191.952 1.00 28.20 ? 1165 GLU A CA     1 
ATOM   7211 C  C      . GLU A 1 1165 ? 197.091 148.269 192.952 1.00 28.20 ? 1165 GLU A C      1 
ATOM   7212 O  O      . GLU A 1 1165 ? 196.302 149.216 192.876 1.00 28.20 ? 1165 GLU A O      1 
ATOM   7213 C  CB     . GLU A 1 1165 ? 197.855 147.130 190.862 1.00 28.20 ? 1165 GLU A CB     1 
ATOM   7214 C  CG     . GLU A 1 1165 ? 196.673 147.520 190.020 1.00 28.20 ? 1165 GLU A CG     1 
ATOM   7215 C  CD     . GLU A 1 1165 ? 196.245 146.391 189.113 1.00 28.20 ? 1165 GLU A CD     1 
ATOM   7216 O  OE1    . GLU A 1 1165 ? 196.857 145.305 189.192 1.00 28.20 ? 1165 GLU A OE1    1 
ATOM   7217 O  OE2    . GLU A 1 1165 ? 195.287 146.571 188.339 1.00 28.20 ? 1165 GLU A OE2    1 
ATOM   7218 N  N      . PHE A 1 1166 ? 197.011 147.349 193.917 1.00 28.91 ? 1166 PHE A N      1 
ATOM   7219 C  CA     . PHE A 1 1166 ? 195.980 147.416 194.943 1.00 28.91 ? 1166 PHE A CA     1 
ATOM   7220 C  C      . PHE A 1 1166 ? 196.206 148.594 195.879 1.00 28.91 ? 1166 PHE A C      1 
ATOM   7221 O  O      . PHE A 1 1166 ? 195.248 149.226 196.324 1.00 28.91 ? 1166 PHE A O      1 
ATOM   7222 C  CB     . PHE A 1 1166 ? 195.956 146.101 195.720 1.00 28.91 ? 1166 PHE A CB     1 
ATOM   7223 C  CG     . PHE A 1 1166 ? 194.831 145.989 196.698 1.00 28.91 ? 1166 PHE A CG     1 
ATOM   7224 C  CD1    . PHE A 1 1166 ? 193.548 145.715 196.262 1.00 28.91 ? 1166 PHE A CD1    1 
ATOM   7225 C  CD2    . PHE A 1 1166 ? 195.054 146.147 198.054 1.00 28.91 ? 1166 PHE A CD2    1 
ATOM   7226 C  CE1    . PHE A 1 1166 ? 192.508 145.607 197.158 1.00 28.91 ? 1166 PHE A CE1    1 
ATOM   7227 C  CE2    . PHE A 1 1166 ? 194.017 146.037 198.953 1.00 28.91 ? 1166 PHE A CE2    1 
ATOM   7228 C  CZ     . PHE A 1 1166 ? 192.741 145.772 198.503 1.00 28.91 ? 1166 PHE A CZ     1 
ATOM   7229 N  N      . GLN A 1 1167 ? 197.467 148.925 196.166 1.00 28.52 ? 1167 GLN A N      1 
ATOM   7230 C  CA     . GLN A 1 1167 ? 197.758 150.066 197.031 1.00 28.52 ? 1167 GLN A CA     1 
ATOM   7231 C  C      . GLN A 1 1167 ? 197.480 151.390 196.331 1.00 28.52 ? 1167 GLN A C      1 
ATOM   7232 O  O      . GLN A 1 1167 ? 196.999 152.343 196.959 1.00 28.52 ? 1167 GLN A O      1 
ATOM   7233 C  CB     . GLN A 1 1167 ? 199.206 149.998 197.508 1.00 28.52 ? 1167 GLN A CB     1 
ATOM   7234 C  CG     . GLN A 1 1167 ? 199.454 148.935 198.558 1.00 28.52 ? 1167 GLN A CG     1 
ATOM   7235 C  CD     . GLN A 1 1167 ? 200.925 148.710 198.811 1.00 28.52 ? 1167 GLN A CD     1 
ATOM   7236 O  OE1    . GLN A 1 1167 ? 201.777 149.296 198.143 1.00 28.52 ? 1167 GLN A OE1    1 
ATOM   7237 N  NE2    . GLN A 1 1167 ? 201.236 147.842 199.764 1.00 28.52 ? 1167 GLN A NE2    1 
ATOM   7238 N  N      . ALA A 1 1168 ? 197.766 151.473 195.030 1.00 26.70 ? 1168 ALA A N      1 
ATOM   7239 C  CA     . ALA A 1 1168 ? 197.392 152.673 194.286 1.00 26.70 ? 1168 ALA A CA     1 
ATOM   7240 C  C      . ALA A 1 1168 ? 195.881 152.794 194.141 1.00 26.70 ? 1168 ALA A C      1 
ATOM   7241 O  O      . ALA A 1 1168 ? 195.342 153.906 194.165 1.00 26.70 ? 1168 ALA A O      1 
ATOM   7242 C  CB     . ALA A 1 1168 ? 198.063 152.676 192.921 1.00 26.70 ? 1168 ALA A CB     1 
ATOM   7243 N  N      . ALA A 1 1169 ? 195.177 151.669 194.035 1.00 26.36 ? 1169 ALA A N      1 
ATOM   7244 C  CA     . ALA A 1 1169 ? 193.722 151.720 194.092 1.00 26.36 ? 1169 ALA A CA     1 
ATOM   7245 C  C      . ALA A 1 1169 ? 193.228 152.153 195.462 1.00 26.36 ? 1169 ALA A C      1 
ATOM   7246 O  O      . ALA A 1 1169 ? 192.228 152.860 195.552 1.00 26.36 ? 1169 ALA A O      1 
ATOM   7247 C  CB     . ALA A 1 1169 ? 193.127 150.371 193.738 1.00 26.36 ? 1169 ALA A CB     1 
ATOM   7248 N  N      . GLU A 1 1170 ? 193.905 151.730 196.536 1.00 28.68 ? 1170 GLU A N      1 
ATOM   7249 C  CA     . GLU A 1 1170 ? 193.561 152.185 197.882 1.00 28.68 ? 1170 GLU A CA     1 
ATOM   7250 C  C      . GLU A 1 1170 ? 193.700 153.691 198.015 1.00 28.68 ? 1170 GLU A C      1 
ATOM   7251 O  O      . GLU A 1 1170 ? 192.831 154.352 198.597 1.00 28.68 ? 1170 GLU A O      1 
ATOM   7252 C  CB     . GLU A 1 1170 ? 194.446 151.511 198.926 1.00 28.68 ? 1170 GLU A CB     1 
ATOM   7253 C  CG     . GLU A 1 1170 ? 194.123 150.080 199.263 1.00 28.68 ? 1170 GLU A CG     1 
ATOM   7254 C  CD     . GLU A 1 1170 ? 195.091 149.535 200.285 1.00 28.68 ? 1170 GLU A CD     1 
ATOM   7255 O  OE1    . GLU A 1 1170 ? 196.095 150.219 200.567 1.00 28.68 ? 1170 GLU A OE1    1 
ATOM   7256 O  OE2    . GLU A 1 1170 ? 194.847 148.441 200.828 1.00 28.68 ? 1170 GLU A OE2    1 
ATOM   7257 N  N      . MET A 1 1171 ? 194.787 154.247 197.477 1.00 29.51 ? 1171 MET A N      1 
ATOM   7258 C  CA     . MET A 1 1171 ? 194.963 155.697 197.492 1.00 29.51 ? 1171 MET A CA     1 
ATOM   7259 C  C      . MET A 1 1171 ? 193.911 156.400 196.646 1.00 29.51 ? 1171 MET A C      1 
ATOM   7260 O  O      . MET A 1 1171 ? 193.420 157.467 197.027 1.00 29.51 ? 1171 MET A O      1 
ATOM   7261 C  CB     . MET A 1 1171 ? 196.369 156.068 197.029 1.00 29.51 ? 1171 MET A CB     1 
ATOM   7262 C  CG     . MET A 1 1171 ? 197.429 155.771 198.071 1.00 29.51 ? 1171 MET A CG     1 
ATOM   7263 S  SD     . MET A 1 1171 ? 199.083 156.276 197.586 1.00 29.51 ? 1171 MET A SD     1 
ATOM   7264 C  CE     . MET A 1 1171 ? 199.494 154.965 196.449 1.00 29.51 ? 1171 MET A CE     1 
ATOM   7265 N  N      . TYR A 1 1172 ? 193.527 155.805 195.515 1.00 25.70 ? 1172 TYR A N      1 
ATOM   7266 C  CA     . TYR A 1 1172 ? 192.466 156.383 194.693 1.00 25.70 ? 1172 TYR A CA     1 
ATOM   7267 C  C      . TYR A 1 1172 ? 191.116 156.366 195.403 1.00 25.70 ? 1172 TYR A C      1 
ATOM   7268 O  O      . TYR A 1 1172 ? 190.371 157.351 195.360 1.00 25.70 ? 1172 TYR A O      1 
ATOM   7269 C  CB     . TYR A 1 1172 ? 192.364 155.646 193.360 1.00 25.70 ? 1172 TYR A CB     1 
ATOM   7270 C  CG     . TYR A 1 1172 ? 191.126 156.040 192.601 1.00 25.70 ? 1172 TYR A CG     1 
ATOM   7271 C  CD1    . TYR A 1 1172 ? 190.994 157.315 192.073 1.00 25.70 ? 1172 TYR A CD1    1 
ATOM   7272 C  CD2    . TYR A 1 1172 ? 190.082 155.141 192.419 1.00 25.70 ? 1172 TYR A CD2    1 
ATOM   7273 C  CE1    . TYR A 1 1172 ? 189.861 157.689 191.401 1.00 25.70 ? 1172 TYR A CE1    1 
ATOM   7274 C  CE2    . TYR A 1 1172 ? 188.947 155.507 191.729 1.00 25.70 ? 1172 TYR A CE2    1 
ATOM   7275 C  CZ     . TYR A 1 1172 ? 188.849 156.782 191.220 1.00 25.70 ? 1172 TYR A CZ     1 
ATOM   7276 O  OH     . TYR A 1 1172 ? 187.726 157.170 190.532 1.00 25.70 ? 1172 TYR A OH     1 
ATOM   7277 N  N      . ILE A 1 1173 ? 190.777 155.244 196.032 1.00 28.13 ? 1173 ILE A N      1 
ATOM   7278 C  CA     . ILE A 1 1173 ? 189.510 155.104 196.742 1.00 28.13 ? 1173 ILE A CA     1 
ATOM   7279 C  C      . ILE A 1 1173 ? 189.462 156.045 197.939 1.00 28.13 ? 1173 ILE A C      1 
ATOM   7280 O  O      . ILE A 1 1173 ? 188.426 156.661 198.216 1.00 28.13 ? 1173 ILE A O      1 
ATOM   7281 C  CB     . ILE A 1 1173 ? 189.317 153.625 197.128 1.00 28.13 ? 1173 ILE A CB     1 
ATOM   7282 C  CG1    . ILE A 1 1173 ? 189.064 152.801 195.866 1.00 28.13 ? 1173 ILE A CG1    1 
ATOM   7283 C  CG2    . ILE A 1 1173 ? 188.181 153.433 198.108 1.00 28.13 ? 1173 ILE A CG2    1 
ATOM   7284 C  CD1    . ILE A 1 1173 ? 189.381 151.338 196.018 1.00 28.13 ? 1173 ILE A CD1    1 
ATOM   7285 N  N      . HIS A 1 1174 ? 190.602 156.237 198.610 1.00 31.85 ? 1174 HIS A N      1 
ATOM   7286 C  CA     . HIS A 1 1174 ? 190.681 157.213 199.691 1.00 31.85 ? 1174 HIS A CA     1 
ATOM   7287 C  C      . HIS A 1 1174 ? 190.511 158.640 199.184 1.00 31.85 ? 1174 HIS A C      1 
ATOM   7288 O  O      . HIS A 1 1174 ? 189.838 159.446 199.831 1.00 31.85 ? 1174 HIS A O      1 
ATOM   7289 C  CB     . HIS A 1 1174 ? 192.010 157.078 200.424 1.00 31.85 ? 1174 HIS A CB     1 
ATOM   7290 C  CG     . HIS A 1 1174 ? 192.168 158.039 201.559 1.00 31.85 ? 1174 HIS A CG     1 
ATOM   7291 N  ND1    . HIS A 1 1174 ? 191.514 157.882 202.761 1.00 31.85 ? 1174 HIS A ND1    1 
ATOM   7292 C  CD2    . HIS A 1 1174 ? 192.890 159.178 201.669 1.00 31.85 ? 1174 HIS A CD2    1 
ATOM   7293 C  CE1    . HIS A 1 1174 ? 191.835 158.878 203.566 1.00 31.85 ? 1174 HIS A CE1    1 
ATOM   7294 N  NE2    . HIS A 1 1174 ? 192.669 159.678 202.928 1.00 31.85 ? 1174 HIS A NE2    1 
ATOM   7295 N  N      . GLN A 1 1175 ? 191.115 158.976 198.039 1.00 32.21 ? 1175 GLN A N      1 
ATOM   7296 C  CA     . GLN A 1 1175 ? 190.926 160.307 197.468 1.00 32.21 ? 1175 GLN A CA     1 
ATOM   7297 C  C      . GLN A 1 1175 ? 189.491 160.534 197.011 1.00 32.21 ? 1175 GLN A C      1 
ATOM   7298 O  O      . GLN A 1 1175 ? 188.986 161.655 197.106 1.00 32.21 ? 1175 GLN A O      1 
ATOM   7299 C  CB     . GLN A 1 1175 ? 191.888 160.524 196.305 1.00 32.21 ? 1175 GLN A CB     1 
ATOM   7300 C  CG     . GLN A 1 1175 ? 193.336 160.691 196.719 1.00 32.21 ? 1175 GLN A CG     1 
ATOM   7301 C  CD     . GLN A 1 1175 ? 194.271 160.755 195.530 1.00 32.21 ? 1175 GLN A CD     1 
ATOM   7302 O  OE1    . GLN A 1 1175 ? 193.849 160.591 194.386 1.00 32.21 ? 1175 GLN A OE1    1 
ATOM   7303 N  NE2    . GLN A 1 1175 ? 195.550 160.990 195.795 1.00 32.21 ? 1175 GLN A NE2    1 
ATOM   7304 N  N      . GLN A 1 1176 ? 188.812 159.485 196.549 1.00 33.01 ? 1176 GLN A N      1 
ATOM   7305 C  CA     . GLN A 1 1176 ? 187.401 159.622 196.203 1.00 33.01 ? 1176 GLN A CA     1 
ATOM   7306 C  C      . GLN A 1 1176 ? 186.542 159.799 197.444 1.00 33.01 ? 1176 GLN A C      1 
ATOM   7307 O  O      . GLN A 1 1176 ? 185.559 160.542 197.418 1.00 33.01 ? 1176 GLN A O      1 
ATOM   7308 C  CB     . GLN A 1 1176 ? 186.928 158.418 195.396 1.00 33.01 ? 1176 GLN A CB     1 
ATOM   7309 C  CG     . GLN A 1 1176 ? 187.501 158.372 194.015 1.00 33.01 ? 1176 GLN A CG     1 
ATOM   7310 C  CD     . GLN A 1 1176 ? 187.105 159.569 193.181 1.00 33.01 ? 1176 GLN A CD     1 
ATOM   7311 O  OE1    . GLN A 1 1176 ? 187.926 160.436 192.888 1.00 33.01 ? 1176 GLN A OE1    1 
ATOM   7312 N  NE2    . GLN A 1 1176 ? 185.839 159.621 192.788 1.00 33.01 ? 1176 GLN A NE2    1 
ATOM   7313 N  N      . GLN A 1 1177 ? 186.908 159.143 198.545 1.00 36.11 ? 1177 GLN A N      1 
ATOM   7314 C  CA     . GLN A 1 1177 ? 186.191 159.350 199.800 1.00 36.11 ? 1177 GLN A CA     1 
ATOM   7315 C  C      . GLN A 1 1177 ? 186.432 160.748 200.356 1.00 36.11 ? 1177 GLN A C      1 
ATOM   7316 O  O      . GLN A 1 1177 ? 185.531 161.348 200.951 1.00 36.11 ? 1177 GLN A O      1 
ATOM   7317 C  CB     . GLN A 1 1177 ? 186.603 158.288 200.814 1.00 36.11 ? 1177 GLN A CB     1 
ATOM   7318 C  CG     . GLN A 1 1177 ? 186.103 156.900 200.475 1.00 36.11 ? 1177 GLN A CG     1 
ATOM   7319 C  CD     . GLN A 1 1177 ? 186.686 155.838 201.378 1.00 36.11 ? 1177 GLN A CD     1 
ATOM   7320 O  OE1    . GLN A 1 1177 ? 187.531 156.123 202.225 1.00 36.11 ? 1177 GLN A OE1    1 
ATOM   7321 N  NE2    . GLN A 1 1177 ? 186.243 154.601 201.197 1.00 36.11 ? 1177 GLN A NE2    1 
ATOM   7322 N  N      . GLN A 1 1178 ? 187.639 161.285 200.168 1.00 37.09 ? 1178 GLN A N      1 
ATOM   7323 C  CA     . GLN A 1 1178 ? 187.921 162.642 200.624 1.00 37.09 ? 1178 GLN A CA     1 
ATOM   7324 C  C      . GLN A 1 1178 ? 187.241 163.684 199.748 1.00 37.09 ? 1178 GLN A C      1 
ATOM   7325 O  O      . GLN A 1 1178 ? 186.864 164.751 200.242 1.00 37.09 ? 1178 GLN A O      1 
ATOM   7326 C  CB     . GLN A 1 1178 ? 189.428 162.893 200.668 1.00 37.09 ? 1178 GLN A CB     1 
ATOM   7327 C  CG     . GLN A 1 1178 ? 190.171 162.082 201.709 1.00 37.09 ? 1178 GLN A CG     1 
ATOM   7328 C  CD     . GLN A 1 1178 ? 189.759 162.426 203.123 1.00 37.09 ? 1178 GLN A CD     1 
ATOM   7329 O  OE1    . GLN A 1 1178 ? 189.534 163.590 203.452 1.00 37.09 ? 1178 GLN A OE1    1 
ATOM   7330 N  NE2    . GLN A 1 1178 ? 189.654 161.410 203.969 1.00 37.09 ? 1178 GLN A NE2    1 
ATOM   7331 N  N      . LYS A 1 1179 ? 187.088 163.406 198.452 1.00 40.14 ? 1179 LYS A N      1 
ATOM   7332 C  CA     . LYS A 1 1179 ? 186.285 164.280 197.604 1.00 40.14 ? 1179 LYS A CA     1 
ATOM   7333 C  C      . LYS A 1 1179 ? 184.803 164.169 197.927 1.00 40.14 ? 1179 LYS A C      1 
ATOM   7334 O  O      . LYS A 1 1179 ? 184.080 165.164 197.837 1.00 40.14 ? 1179 LYS A O      1 
ATOM   7335 C  CB     . LYS A 1 1179 ? 186.517 163.959 196.129 1.00 40.14 ? 1179 LYS A CB     1 
ATOM   7336 C  CG     . LYS A 1 1179 ? 187.886 164.343 195.605 1.00 40.14 ? 1179 LYS A CG     1 
ATOM   7337 C  CD     . LYS A 1 1179 ? 188.027 163.969 194.141 1.00 40.14 ? 1179 LYS A CD     1 
ATOM   7338 C  CE     . LYS A 1 1179 ? 189.373 164.397 193.589 1.00 40.14 ? 1179 LYS A CE     1 
ATOM   7339 N  NZ     . LYS A 1 1179 ? 190.488 163.636 194.215 1.00 40.14 ? 1179 LYS A NZ     1 
ATOM   7340 N  N      . ASN A 1 1180 ? 184.335 162.975 198.298 1.00 44.80 ? 1180 ASN A N      1 
ATOM   7341 C  CA     . ASN A 1 1180 ? 182.927 162.778 198.624 1.00 44.80 ? 1180 ASN A CA     1 
ATOM   7342 C  C      . ASN A 1 1180 ? 182.567 163.480 199.926 1.00 44.80 ? 1180 ASN A C      1 
ATOM   7343 O  O      . ASN A 1 1180 ? 181.558 164.191 200.000 1.00 44.80 ? 1180 ASN A O      1 
ATOM   7344 C  CB     . ASN A 1 1180 ? 182.628 161.281 198.716 1.00 44.80 ? 1180 ASN A CB     1 
ATOM   7345 C  CG     . ASN A 1 1180 ? 181.140 160.971 198.734 1.00 44.80 ? 1180 ASN A CG     1 
ATOM   7346 O  OD1    . ASN A 1 1180 ? 180.297 161.863 198.636 1.00 44.80 ? 1180 ASN A OD1    1 
ATOM   7347 N  ND2    . ASN A 1 1180 ? 180.813 159.692 198.867 1.00 44.80 ? 1180 ASN A ND2    1 
ATOM   7348 N  N      . SER A 1 1181 ? 183.386 163.302 200.962 1.00 45.75 ? 1181 SER A N      1 
ATOM   7349 C  CA     . SER A 1 1181 ? 183.146 163.950 202.244 1.00 45.75 ? 1181 SER A CA     1 
ATOM   7350 C  C      . SER A 1 1181 ? 183.457 165.439 202.223 1.00 45.75 ? 1181 SER A C      1 
ATOM   7351 O  O      . SER A 1 1181 ? 183.111 166.136 203.181 1.00 45.75 ? 1181 SER A O      1 
ATOM   7352 C  CB     . SER A 1 1181 ? 183.971 163.269 203.335 1.00 45.75 ? 1181 SER A CB     1 
ATOM   7353 O  OG     . SER A 1 1181 ? 183.561 161.926 203.516 1.00 45.75 ? 1181 SER A OG     1 
ATOM   7354 N  N      . GLY A 1 1182 ? 184.099 165.938 201.174 1.00 46.75 ? 1182 GLY A N      1 
ATOM   7355 C  CA     . GLY A 1 1182 ? 184.409 167.341 201.039 1.00 46.75 ? 1182 GLY A CA     1 
ATOM   7356 C  C      . GLY A 1 1182 ? 183.446 168.142 200.198 1.00 46.75 ? 1182 GLY A C      1 
ATOM   7357 O  O      . GLY A 1 1182 ? 183.648 169.349 200.042 1.00 46.75 ? 1182 GLY A O      1 
ATOM   7358 N  N      . THR A 1 1183 ? 182.411 167.516 199.642 1.00 50.30 ? 1183 THR A N      1 
ATOM   7359 C  CA     . THR A 1 1183 ? 181.397 168.266 198.919 1.00 50.30 ? 1183 THR A CA     1 
ATOM   7360 C  C      . THR A 1 1183 ? 180.530 169.052 199.892 1.00 50.30 ? 1183 THR A C      1 
ATOM   7361 O  O      . THR A 1 1183 ? 180.519 168.801 201.098 1.00 50.30 ? 1183 THR A O      1 
ATOM   7362 C  CB     . THR A 1 1183 ? 180.512 167.345 198.079 1.00 50.30 ? 1183 THR A CB     1 
ATOM   7363 O  OG1    . THR A 1 1183 ? 179.910 166.354 198.919 1.00 50.30 ? 1183 THR A OG1    1 
ATOM   7364 C  CG2    . THR A 1 1183 ? 181.312 166.682 196.977 1.00 50.30 ? 1183 THR A CG2    1 
ATOM   7365 N  N      . LEU A 1 1184 ? 179.784 170.012 199.341 1.00 52.46 ? 1184 LEU A N      1 
ATOM   7366 C  CA     . LEU A 1 1184 ? 178.989 170.912 200.168 1.00 52.46 ? 1184 LEU A CA     1 
ATOM   7367 C  C      . LEU A 1 1184 ? 177.834 170.180 200.836 1.00 52.46 ? 1184 LEU A C      1 
ATOM   7368 O  O      . LEU A 1 1184 ? 177.510 170.455 201.996 1.00 52.46 ? 1184 LEU A O      1 
ATOM   7369 C  CB     . LEU A 1 1184 ? 178.477 172.073 199.318 1.00 52.46 ? 1184 LEU A CB     1 
ATOM   7370 C  CG     . LEU A 1 1184 ? 177.710 173.183 200.030 1.00 52.46 ? 1184 LEU A CG     1 
ATOM   7371 C  CD1    . LEU A 1 1184 ? 178.601 173.862 201.050 1.00 52.46 ? 1184 LEU A CD1    1 
ATOM   7372 C  CD2    . LEU A 1 1184 ? 177.195 174.181 199.015 1.00 52.46 ? 1184 LEU A CD2    1 
ATOM   7373 N  N      . GLU A 1 1185 ? 177.232 169.216 200.137 1.00 53.89 ? 1185 GLU A N      1 
ATOM   7374 C  CA     . GLU A 1 1185 ? 176.089 168.497 200.689 1.00 53.89 ? 1185 GLU A CA     1 
ATOM   7375 C  C      . GLU A 1 1185 ? 176.504 167.585 201.837 1.00 53.89 ? 1185 GLU A C      1 
ATOM   7376 O  O      . GLU A 1 1185 ? 175.823 167.531 202.867 1.00 53.89 ? 1185 GLU A O      1 
ATOM   7377 C  CB     . GLU A 1 1185 ? 175.390 167.700 199.588 1.00 53.89 ? 1185 GLU A CB     1 
ATOM   7378 C  CG     . GLU A 1 1185 ? 174.651 168.559 198.567 1.00 53.89 ? 1185 GLU A CG     1 
ATOM   7379 C  CD     . GLU A 1 1185 ? 175.542 169.059 197.446 1.00 53.89 ? 1185 GLU A CD     1 
ATOM   7380 O  OE1    . GLU A 1 1185 ? 176.724 168.661 197.397 1.00 53.89 ? 1185 GLU A OE1    1 
ATOM   7381 O  OE2    . GLU A 1 1185 ? 175.063 169.861 196.619 1.00 53.89 ? 1185 GLU A OE2    1 
ATOM   7382 N  N      . GLU A 1 1186 ? 177.638 166.895 201.699 1.00 52.96 ? 1186 GLU A N      1 
ATOM   7383 C  CA     . GLU A 1 1186 ? 178.106 166.040 202.784 1.00 52.96 ? 1186 GLU A CA     1 
ATOM   7384 C  C      . GLU A 1 1186 ? 178.671 166.849 203.945 1.00 52.96 ? 1186 GLU A C      1 
ATOM   7385 O  O      . GLU A 1 1186 ? 178.559 166.417 205.097 1.00 52.96 ? 1186 GLU A O      1 
ATOM   7386 C  CB     . GLU A 1 1186 ? 179.139 165.044 202.264 1.00 52.96 ? 1186 GLU A CB     1 
ATOM   7387 C  CG     . GLU A 1 1186 ? 178.548 163.987 201.346 1.00 52.96 ? 1186 GLU A CG     1 
ATOM   7388 C  CD     . GLU A 1 1186 ? 177.607 163.038 202.068 1.00 52.96 ? 1186 GLU A CD     1 
ATOM   7389 O  OE1    . GLU A 1 1186 ? 177.844 162.744 203.258 1.00 52.96 ? 1186 GLU A OE1    1 
ATOM   7390 O  OE2    . GLU A 1 1186 ? 176.624 162.587 201.444 1.00 52.96 ? 1186 GLU A OE2    1 
ATOM   7391 N  N      . ARG A 1 1187 ? 179.253 168.024 203.677 1.00 52.10 ? 1187 ARG A N      1 
ATOM   7392 C  CA     . ARG A 1 1187 ? 179.682 168.891 204.772 1.00 52.10 ? 1187 ARG A CA     1 
ATOM   7393 C  C      . ARG A 1 1187 ? 178.492 169.439 205.548 1.00 52.10 ? 1187 ARG A C      1 
ATOM   7394 O  O      . ARG A 1 1187 ? 178.538 169.509 206.779 1.00 52.10 ? 1187 ARG A O      1 
ATOM   7395 C  CB     . ARG A 1 1187 ? 180.546 170.042 204.259 1.00 52.10 ? 1187 ARG A CB     1 
ATOM   7396 C  CG     . ARG A 1 1187 ? 181.959 169.660 203.864 1.00 52.10 ? 1187 ARG A CG     1 
ATOM   7397 C  CD     . ARG A 1 1187 ? 182.737 170.887 203.423 1.00 52.10 ? 1187 ARG A CD     1 
ATOM   7398 N  NE     . ARG A 1 1187 ? 184.049 170.549 202.886 1.00 52.10 ? 1187 ARG A NE     1 
ATOM   7399 C  CZ     . ARG A 1 1187 ? 185.149 170.419 203.620 1.00 52.10 ? 1187 ARG A CZ     1 
ATOM   7400 N  NH1    . ARG A 1 1187 ? 185.098 170.593 204.932 1.00 52.10 ? 1187 ARG A NH1    1 
ATOM   7401 N  NH2    . ARG A 1 1187 ? 186.300 170.110 203.041 1.00 52.10 ? 1187 ARG A NH2    1 
ATOM   7402 N  N      . VAL A 1 1188 ? 177.413 169.810 204.854 1.00 53.89 ? 1188 VAL A N      1 
ATOM   7403 C  CA     . VAL A 1 1188 ? 176.213 170.284 205.541 1.00 53.89 ? 1188 VAL A CA     1 
ATOM   7404 C  C      . VAL A 1 1188 ? 175.538 169.141 206.299 1.00 53.89 ? 1188 VAL A C      1 
ATOM   7405 O  O      . VAL A 1 1188 ? 175.037 169.332 207.413 1.00 53.89 ? 1188 VAL A O      1 
ATOM   7406 C  CB     . VAL A 1 1188 ? 175.270 170.975 204.533 1.00 53.89 ? 1188 VAL A CB     1 
ATOM   7407 C  CG1    . VAL A 1 1188 ? 173.905 171.248 205.126 1.00 53.89 ? 1188 VAL A CG1    1 
ATOM   7408 C  CG2    . VAL A 1 1188 ? 175.865 172.299 204.104 1.00 53.89 ? 1188 VAL A CG2    1 
ATOM   7409 N  N      . ARG A 1 1189 ? 175.576 167.926 205.743 1.00 56.24 ? 1189 ARG A N      1 
ATOM   7410 C  CA     . ARG A 1 1189 ? 175.014 166.761 206.425 1.00 56.24 ? 1189 ARG A CA     1 
ATOM   7411 C  C      . ARG A 1 1189 ? 175.789 166.424 207.698 1.00 56.24 ? 1189 ARG A C      1 
ATOM   7412 O  O      . ARG A 1 1189 ? 175.193 166.182 208.758 1.00 56.24 ? 1189 ARG A O      1 
ATOM   7413 C  CB     . ARG A 1 1189 ? 175.003 165.574 205.466 1.00 56.24 ? 1189 ARG A CB     1 
ATOM   7414 C  CG     . ARG A 1 1189 ? 174.356 164.320 206.001 1.00 56.24 ? 1189 ARG A CG     1 
ATOM   7415 C  CD     . ARG A 1 1189 ? 174.354 163.249 204.928 1.00 56.24 ? 1189 ARG A CD     1 
ATOM   7416 N  NE     . ARG A 1 1189 ? 173.764 161.998 205.388 1.00 56.24 ? 1189 ARG A NE     1 
ATOM   7417 C  CZ     . ARG A 1 1189 ? 173.643 160.914 204.630 1.00 56.24 ? 1189 ARG A CZ     1 
ATOM   7418 N  NH1    . ARG A 1 1189 ? 173.094 159.813 205.123 1.00 56.24 ? 1189 ARG A NH1    1 
ATOM   7419 N  NH2    . ARG A 1 1189 ? 174.074 160.931 203.377 1.00 56.24 ? 1189 ARG A NH2    1 
ATOM   7420 N  N      . ALA A 1 1190 ? 177.122 166.432 207.619 1.00 58.38 ? 1190 ALA A N      1 
ATOM   7421 C  CA     . ALA A 1 1190 ? 177.939 166.183 208.801 1.00 58.38 ? 1190 ALA A CA     1 
ATOM   7422 C  C      . ALA A 1 1190 ? 177.833 167.315 209.812 1.00 58.38 ? 1190 ALA A C      1 
ATOM   7423 O  O      . ALA A 1 1190 ? 177.881 167.066 211.021 1.00 58.38 ? 1190 ALA A O      1 
ATOM   7424 C  CB     . ALA A 1 1190 ? 179.396 165.971 208.398 1.00 58.38 ? 1190 ALA A CB     1 
ATOM   7425 N  N      . LEU A 1 1191 ? 177.668 168.556 209.346 1.00 58.59 ? 1191 LEU A N      1 
ATOM   7426 C  CA     . LEU A 1 1191 ? 177.488 169.677 210.261 1.00 58.59 ? 1191 LEU A CA     1 
ATOM   7427 C  C      . LEU A 1 1191 ? 176.146 169.592 210.971 1.00 58.59 ? 1191 LEU A C      1 
ATOM   7428 O  O      . LEU A 1 1191 ? 176.044 169.927 212.154 1.00 58.59 ? 1191 LEU A O      1 
ATOM   7429 C  CB     . LEU A 1 1191 ? 177.614 170.996 209.502 1.00 58.59 ? 1191 LEU A CB     1 
ATOM   7430 C  CG     . LEU A 1 1191 ? 177.565 172.273 210.338 1.00 58.59 ? 1191 LEU A CG     1 
ATOM   7431 C  CD1    . LEU A 1 1191 ? 178.735 172.309 211.299 1.00 58.59 ? 1191 LEU A CD1    1 
ATOM   7432 C  CD2    . LEU A 1 1191 ? 177.559 173.501 209.446 1.00 58.59 ? 1191 LEU A CD2    1 
ATOM   7433 N  N      . GLY A 1 1192 ? 175.109 169.129 210.270 1.00 60.49 ? 1192 GLY A N      1 
ATOM   7434 C  CA     . GLY A 1 1192 ? 173.834 168.885 210.916 1.00 60.49 ? 1192 GLY A CA     1 
ATOM   7435 C  C      . GLY A 1 1192 ? 173.898 167.757 211.923 1.00 60.49 ? 1192 GLY A C      1 
ATOM   7436 O  O      . GLY A 1 1192 ? 173.239 167.813 212.964 1.00 60.49 ? 1192 GLY A O      1 
ATOM   7437 N  N      . ASP A 1 1193 ? 174.712 166.735 211.644 1.00 63.40 ? 1193 ASP A N      1 
ATOM   7438 C  CA     . ASP A 1 1193 ? 174.946 165.688 212.636 1.00 63.40 ? 1193 ASP A CA     1 
ATOM   7439 C  C      . ASP A 1 1193 ? 175.703 166.225 213.850 1.00 63.40 ? 1193 ASP A C      1 
ATOM   7440 O  O      . ASP A 1 1193 ? 175.436 165.814 214.985 1.00 63.40 ? 1193 ASP A O      1 
ATOM   7441 C  CB     . ASP A 1 1193 ? 175.705 164.527 211.998 1.00 63.40 ? 1193 ASP A CB     1 
ATOM   7442 C  CG     . ASP A 1 1193 ? 174.888 163.809 210.943 1.00 63.40 ? 1193 ASP A CG     1 
ATOM   7443 O  OD1    . ASP A 1 1193 ? 173.643 163.833 211.035 1.00 63.40 ? 1193 ASP A OD1    1 
ATOM   7444 O  OD2    . ASP A 1 1193 ? 175.490 163.214 210.025 1.00 63.40 ? 1193 ASP A OD2    1 
ATOM   7445 N  N      . ARG A 1 1194 ? 176.635 167.160 213.631 1.00 63.50 ? 1194 ARG A N      1 
ATOM   7446 C  CA     . ARG A 1 1194 ? 177.324 167.809 214.747 1.00 63.50 ? 1194 ARG A CA     1 
ATOM   7447 C  C      . ARG A 1 1194 ? 176.367 168.662 215.572 1.00 63.50 ? 1194 ARG A C      1 
ATOM   7448 O  O      . ARG A 1 1194 ? 176.474 168.706 216.801 1.00 63.50 ? 1194 ARG A O      1 
ATOM   7449 C  CB     . ARG A 1 1194 ? 178.476 168.677 214.244 1.00 63.50 ? 1194 ARG A CB     1 
ATOM   7450 C  CG     . ARG A 1 1194 ? 179.656 167.938 213.650 1.00 63.50 ? 1194 ARG A CG     1 
ATOM   7451 C  CD     . ARG A 1 1194 ? 180.739 168.937 213.262 1.00 63.50 ? 1194 ARG A CD     1 
ATOM   7452 N  NE     . ARG A 1 1194 ? 181.896 168.310 212.630 1.00 63.50 ? 1194 ARG A NE     1 
ATOM   7453 C  CZ     . ARG A 1 1194 ? 182.050 168.182 211.316 1.00 63.50 ? 1194 ARG A CZ     1 
ATOM   7454 N  NH1    . ARG A 1 1194 ? 183.135 167.599 210.827 1.00 63.50 ? 1194 ARG A NH1    1 
ATOM   7455 N  NH2    . ARG A 1 1194 ? 181.123 168.645 210.490 1.00 63.50 ? 1194 ARG A NH2    1 
ATOM   7456 N  N      . VAL A 1 1195 ? 175.432 169.351 214.911 1.00 65.56 ? 1195 VAL A N      1 
ATOM   7457 C  CA     . VAL A 1 1195 ? 174.426 170.142 215.619 1.00 65.56 ? 1195 VAL A CA     1 
ATOM   7458 C  C      . VAL A 1 1195 ? 173.488 169.230 216.405 1.00 65.56 ? 1195 VAL A C      1 
ATOM   7459 O  O      . VAL A 1 1195 ? 173.081 169.554 217.527 1.00 65.56 ? 1195 VAL A O      1 
ATOM   7460 C  CB     . VAL A 1 1195 ? 173.674 171.052 214.625 1.00 65.56 ? 1195 VAL A CB     1 
ATOM   7461 C  CG1    . VAL A 1 1195 ? 172.482 171.740 215.266 1.00 65.56 ? 1195 VAL A CG1    1 
ATOM   7462 C  CG2    . VAL A 1 1195 ? 174.609 172.117 214.090 1.00 65.56 ? 1195 VAL A CG2    1 
ATOM   7463 N  N      . ASP A 1 1196 ? 173.183 168.049 215.859 1.00 66.69 ? 1196 ASP A N      1 
ATOM   7464 C  CA     . ASP A 1 1196 ? 172.387 167.069 216.597 1.00 66.69 ? 1196 ASP A CA     1 
ATOM   7465 C  C      . ASP A 1 1196 ? 173.145 166.527 217.806 1.00 66.69 ? 1196 ASP A C      1 
ATOM   7466 O  O      . ASP A 1 1196 ? 172.545 166.270 218.855 1.00 66.69 ? 1196 ASP A O      1 
ATOM   7467 C  CB     . ASP A 1 1196 ? 171.971 165.928 215.672 1.00 66.69 ? 1196 ASP A CB     1 
ATOM   7468 C  CG     . ASP A 1 1196 ? 170.992 166.372 214.606 1.00 66.69 ? 1196 ASP A CG     1 
ATOM   7469 O  OD1    . ASP A 1 1196 ? 170.235 167.333 214.856 1.00 66.69 ? 1196 ASP A OD1    1 
ATOM   7470 O  OD2    . ASP A 1 1196 ? 170.983 165.763 213.516 1.00 66.69 ? 1196 ASP A OD2    1 
ATOM   7471 N  N      . CYS A 1 1197 ? 174.466 166.369 217.686 1.00 69.67 ? 1197 CYS A N      1 
ATOM   7472 C  CA     . CYS A 1 1197 ? 175.262 165.939 218.835 1.00 69.67 ? 1197 CYS A CA     1 
ATOM   7473 C  C      . CYS A 1 1197 ? 175.353 167.033 219.896 1.00 69.67 ? 1197 CYS A C      1 
ATOM   7474 O  O      . CYS A 1 1197 ? 175.339 166.738 221.097 1.00 69.67 ? 1197 CYS A O      1 
ATOM   7475 C  CB     . CYS A 1 1197 ? 176.657 165.511 218.382 1.00 69.67 ? 1197 CYS A CB     1 
ATOM   7476 S  SG     . CYS A 1 1197 ? 176.686 163.993 217.400 1.00 69.67 ? 1197 CYS A SG     1 
ATOM   7477 N  N      . ILE A 1 1198 ? 175.440 168.298 219.471 1.00 70.07 ? 1198 ILE A N      1 
ATOM   7478 C  CA     . ILE A 1 1198 ? 175.395 169.426 220.403 1.00 70.07 ? 1198 ILE A CA     1 
ATOM   7479 C  C      . ILE A 1 1198 ? 174.044 169.486 221.109 1.00 70.07 ? 1198 ILE A C      1 
ATOM   7480 O  O      . ILE A 1 1198 ? 173.968 169.738 222.318 1.00 70.07 ? 1198 ILE A O      1 
ATOM   7481 C  CB     . ILE A 1 1198 ? 175.721 170.740 219.659 1.00 70.07 ? 1198 ILE A CB     1 
ATOM   7482 C  CG1    . ILE A 1 1198 ? 177.184 170.756 219.213 1.00 70.07 ? 1198 ILE A CG1    1 
ATOM   7483 C  CG2    . ILE A 1 1198 ? 175.424 171.977 220.504 1.00 70.07 ? 1198 ILE A CG2    1 
ATOM   7484 C  CD1    . ILE A 1 1198 ? 178.175 170.691 220.357 1.00 70.07 ? 1198 ILE A CD1    1 
ATOM   7485 N  N      . ASN A 1 1199 ? 172.964 169.206 220.375 1.00 72.06 ? 1199 ASN A N      1 
ATOM   7486 C  CA     . ASN A 1 1199 ? 171.626 169.220 220.961 1.00 72.06 ? 1199 ASN A CA     1 
ATOM   7487 C  C      . ASN A 1 1199 ? 171.446 168.071 221.950 1.00 72.06 ? 1199 ASN A C      1 
ATOM   7488 O  O      . ASN A 1 1199 ? 170.839 168.250 223.012 1.00 72.06 ? 1199 ASN A O      1 
ATOM   7489 C  CB     . ASN A 1 1199 ? 170.579 169.150 219.848 1.00 72.06 ? 1199 ASN A CB     1 
ATOM   7490 C  CG     . ASN A 1 1199 ? 169.186 169.528 220.318 1.00 72.06 ? 1199 ASN A CG     1 
ATOM   7491 O  OD1    . ASN A 1 1199 ? 168.977 169.887 221.476 1.00 72.06 ? 1199 ASN A OD1    1 
ATOM   7492 N  ND2    . ASN A 1 1199 ? 168.220 169.443 219.412 1.00 72.06 ? 1199 ASN A ND2    1 
ATOM   7493 N  N      . SER A 1 1200 ? 171.995 166.896 221.631 1.00 73.54 ? 1200 SER A N      1 
ATOM   7494 C  CA     . SER A 1 1200 ? 171.944 165.768 222.557 1.00 73.54 ? 1200 SER A CA     1 
ATOM   7495 C  C      . SER A 1 1200 ? 172.783 166.028 223.804 1.00 73.54 ? 1200 SER A C      1 
ATOM   7496 O  O      . SER A 1 1200 ? 172.376 165.670 224.915 1.00 73.54 ? 1200 SER A O      1 
ATOM   7497 C  CB     . SER A 1 1200 ? 172.411 164.495 221.855 1.00 73.54 ? 1200 SER A CB     1 
ATOM   7498 O  OG     . SER A 1 1200 ? 171.536 164.152 220.795 1.00 73.54 ? 1200 SER A OG     1 
ATOM   7499 N  N      . GLN A 1 1201 ? 173.948 166.665 223.640 1.00 73.04 ? 1201 GLN A N      1 
ATOM   7500 C  CA     . GLN A 1 1201 ? 174.776 167.028 224.788 1.00 73.04 ? 1201 GLN A CA     1 
ATOM   7501 C  C      . GLN A 1 1201 ? 174.084 168.058 225.672 1.00 73.04 ? 1201 GLN A C      1 
ATOM   7502 O  O      . GLN A 1 1201 ? 174.139 167.962 226.904 1.00 73.04 ? 1201 GLN A O      1 
ATOM   7503 C  CB     . GLN A 1 1201 ? 176.129 167.556 224.308 1.00 73.04 ? 1201 GLN A CB     1 
ATOM   7504 C  CG     . GLN A 1 1201 ? 177.085 167.948 225.421 1.00 73.04 ? 1201 GLN A CG     1 
ATOM   7505 C  CD     . GLN A 1 1201 ? 178.432 168.404 224.898 1.00 73.04 ? 1201 GLN A CD     1 
ATOM   7506 O  OE1    . GLN A 1 1201 ? 178.663 168.433 223.689 1.00 73.04 ? 1201 GLN A OE1    1 
ATOM   7507 N  NE2    . GLN A 1 1201 ? 179.327 168.771 225.808 1.00 73.04 ? 1201 GLN A NE2    1 
ATOM   7508 N  N      . LEU A 1 1202 ? 173.404 169.033 225.064 1.00 72.80 ? 1202 LEU A N      1 
ATOM   7509 C  CA     . LEU A 1 1202 ? 172.692 170.036 225.847 1.00 72.80 ? 1202 LEU A CA     1 
ATOM   7510 C  C      . LEU A 1 1202 ? 171.447 169.447 226.503 1.00 72.80 ? 1202 LEU A C      1 
ATOM   7511 O  O      . LEU A 1 1202 ? 171.014 169.936 227.552 1.00 72.80 ? 1202 LEU A O      1 
ATOM   7512 C  CB     . LEU A 1 1202 ? 172.344 171.232 224.956 1.00 72.80 ? 1202 LEU A CB     1 
ATOM   7513 C  CG     . LEU A 1 1202 ? 171.855 172.551 225.567 1.00 72.80 ? 1202 LEU A CG     1 
ATOM   7514 C  CD1    . LEU A 1 1202 ? 172.378 173.700 224.729 1.00 72.80 ? 1202 LEU A CD1    1 
ATOM   7515 C  CD2    . LEU A 1 1202 ? 170.335 172.634 225.644 1.00 72.80 ? 1202 LEU A CD2    1 
ATOM   7516 N  N      . ASN A 1 1203 ? 170.860 168.405 225.908 1.00 72.97 ? 1203 ASN A N      1 
ATOM   7517 C  CA     . ASN A 1 1203 ? 169.789 167.686 226.589 1.00 72.97 ? 1203 ASN A CA     1 
ATOM   7518 C  C      . ASN A 1 1203 ? 170.322 166.865 227.758 1.00 72.97 ? 1203 ASN A C      1 
ATOM   7519 O  O      . ASN A 1 1203 ? 169.631 166.713 228.772 1.00 72.97 ? 1203 ASN A O      1 
ATOM   7520 C  CB     . ASN A 1 1203 ? 169.042 166.784 225.605 1.00 72.97 ? 1203 ASN A CB     1 
ATOM   7521 C  CG     . ASN A 1 1203 ? 168.184 167.568 224.630 1.00 72.97 ? 1203 ASN A CG     1 
ATOM   7522 O  OD1    . ASN A 1 1203 ? 167.543 168.551 225.002 1.00 72.97 ? 1203 ASN A OD1    1 
ATOM   7523 N  ND2    . ASN A 1 1203 ? 168.158 167.129 223.377 1.00 72.97 ? 1203 ASN A ND2    1 
ATOM   7524 N  N      . ARG A 1 1204 ? 171.538 166.327 227.633 1.00 73.47 ? 1204 ARG A N      1 
ATOM   7525 C  CA     . ARG A 1 1204 ? 172.149 165.611 228.750 1.00 73.47 ? 1204 ARG A CA     1 
ATOM   7526 C  C      . ARG A 1 1204 ? 172.540 166.554 229.882 1.00 73.47 ? 1204 ARG A C      1 
ATOM   7527 O  O      . ARG A 1 1204 ? 172.473 166.169 231.055 1.00 73.47 ? 1204 ARG A O      1 
ATOM   7528 C  CB     . ARG A 1 1204 ? 173.373 164.827 228.276 1.00 73.47 ? 1204 ARG A CB     1 
ATOM   7529 C  CG     . ARG A 1 1204 ? 173.061 163.637 227.385 1.00 73.47 ? 1204 ARG A CG     1 
ATOM   7530 C  CD     . ARG A 1 1204 ? 174.339 162.951 226.933 1.00 73.47 ? 1204 ARG A CD     1 
ATOM   7531 N  NE     . ARG A 1 1204 ? 174.079 161.842 226.020 1.00 73.47 ? 1204 ARG A NE     1 
ATOM   7532 C  CZ     . ARG A 1 1204 ? 175.030 161.127 225.427 1.00 73.47 ? 1204 ARG A CZ     1 
ATOM   7533 N  NH1    . ARG A 1 1204 ? 176.307 161.405 225.651 1.00 73.47 ? 1204 ARG A NH1    1 
ATOM   7534 N  NH2    . ARG A 1 1204 ? 174.704 160.133 224.611 1.00 73.47 ? 1204 ARG A NH2    1 
ATOM   7535 N  N      . VAL A 1 1205 ? 172.958 167.779 229.555 1.00 72.35 ? 1205 VAL A N      1 
ATOM   7536 C  CA     . VAL A 1 1205 ? 173.272 168.758 230.592 1.00 72.35 ? 1205 VAL A CA     1 
ATOM   7537 C  C      . VAL A 1 1205 ? 171.995 169.238 231.273 1.00 72.35 ? 1205 VAL A C      1 
ATOM   7538 O  O      . VAL A 1 1205 ? 171.884 169.223 232.505 1.00 72.35 ? 1205 VAL A O      1 
ATOM   7539 C  CB     . VAL A 1 1205 ? 174.077 169.932 230.002 1.00 72.35 ? 1205 VAL A CB     1 
ATOM   7540 C  CG1    . VAL A 1 1205 ? 174.239 171.040 231.032 1.00 72.35 ? 1205 VAL A CG1    1 
ATOM   7541 C  CG2    . VAL A 1 1205 ? 175.442 169.457 229.536 1.00 72.35 ? 1205 VAL A CG2    1 
ATOM   7542 N  N      . LEU A 1 1206 ? 171.010 169.656 230.484 1.00 71.53 ? 1206 LEU A N      1 
ATOM   7543 C  CA     . LEU A 1 1206 ? 169.736 170.111 231.027 1.00 71.53 ? 1206 LEU A CA     1 
ATOM   7544 C  C      . LEU A 1 1206 ? 168.891 168.906 231.430 1.00 71.53 ? 1206 LEU A C      1 
ATOM   7545 O  O      . LEU A 1 1206 ? 168.061 168.991 232.335 1.00 71.53 ? 1206 LEU A O      1 
ATOM   7546 C  CB     . LEU A 1 1206 ? 169.001 170.988 230.003 1.00 71.53 ? 1206 LEU A CB     1 
ATOM   7547 C  CG     . LEU A 1 1206 ? 167.765 171.808 230.392 1.00 71.53 ? 1206 LEU A CG     1 
ATOM   7548 C  CD1    . LEU A 1 1206 ? 167.748 173.095 229.585 1.00 71.53 ? 1206 LEU A CD1    1 
ATOM   7549 C  CD2    . LEU A 1 1206 ? 166.461 171.053 230.160 1.00 71.53 ? 1206 LEU A CD2    1 
HETATM 7550 C  C1     . NAG B 2 .    ? 157.048 155.055 120.803 1.00 28.94 ? 1    NAG B C1     1 
HETATM 7551 C  C2     . NAG B 2 .    ? 157.257 156.193 119.804 1.00 28.94 ? 1    NAG B C2     1 
HETATM 7552 C  C3     . NAG B 2 .    ? 155.914 156.814 119.412 1.00 28.94 ? 1    NAG B C3     1 
HETATM 7553 C  C4     . NAG B 2 .    ? 154.902 155.754 118.985 1.00 28.94 ? 1    NAG B C4     1 
HETATM 7554 C  C5     . NAG B 2 .    ? 154.819 154.652 120.035 1.00 28.94 ? 1    NAG B C5     1 
HETATM 7555 C  C6     . NAG B 2 .    ? 153.931 153.500 119.627 1.00 28.94 ? 1    NAG B C6     1 
HETATM 7556 C  C7     . NAG B 2 .    ? 159.468 157.192 120.205 1.00 28.94 ? 1    NAG B C7     1 
HETATM 7557 C  C8     . NAG B 2 .    ? 160.216 158.320 120.846 1.00 28.94 ? 1    NAG B C8     1 
HETATM 7558 N  N2     . NAG B 2 .    ? 158.140 157.209 120.356 1.00 28.94 ? 1    NAG B N2     1 
HETATM 7559 O  O3     . NAG B 2 .    ? 156.133 157.744 118.358 1.00 28.94 ? 1    NAG B O3     1 
HETATM 7560 O  O4     . NAG B 2 .    ? 153.605 156.331 118.884 1.00 28.94 ? 1    NAG B O4     1 
HETATM 7561 O  O5     . NAG B 2 .    ? 156.125 154.110 120.268 1.00 28.94 ? 1    NAG B O5     1 
HETATM 7562 O  O6     . NAG B 2 .    ? 153.988 153.271 118.226 1.00 28.94 ? 1    NAG B O6     1 
HETATM 7563 O  O7     . NAG B 2 .    ? 160.039 156.302 119.586 1.00 28.94 ? 1    NAG B O7     1 
HETATM 7564 C  C1     . NAG B 2 .    ? 153.197 156.512 117.520 1.00 32.32 ? 2    NAG B C1     1 
HETATM 7565 C  C2     . NAG B 2 .    ? 151.677 156.621 117.465 1.00 32.32 ? 2    NAG B C2     1 
HETATM 7566 C  C3     . NAG B 2 .    ? 151.218 156.913 116.038 1.00 32.32 ? 2    NAG B C3     1 
HETATM 7567 C  C4     . NAG B 2 .    ? 151.920 158.151 115.495 1.00 32.32 ? 2    NAG B C4     1 
HETATM 7568 C  C5     . NAG B 2 .    ? 153.434 157.993 115.616 1.00 32.32 ? 2    NAG B C5     1 
HETATM 7569 C  C6     . NAG B 2 .    ? 154.190 159.244 115.236 1.00 32.32 ? 2    NAG B C6     1 
HETATM 7570 C  C7     . NAG B 2 .    ? 150.435 155.372 119.171 1.00 32.32 ? 2    NAG B C7     1 
HETATM 7571 C  C8     . NAG B 2 .    ? 149.822 154.057 119.546 1.00 32.32 ? 2    NAG B C8     1 
HETATM 7572 N  N2     . NAG B 2 .    ? 151.037 155.420 117.978 1.00 32.32 ? 2    NAG B N2     1 
HETATM 7573 O  O3     . NAG B 2 .    ? 149.809 157.111 116.029 1.00 32.32 ? 2    NAG B O3     1 
HETATM 7574 O  O4     . NAG B 2 .    ? 151.576 158.349 114.129 1.00 32.32 ? 2    NAG B O4     1 
HETATM 7575 O  O5     . NAG B 2 .    ? 153.787 157.701 116.978 1.00 32.32 ? 2    NAG B O5     1 
HETATM 7576 O  O6     . NAG B 2 .    ? 155.220 159.529 116.172 1.00 32.32 ? 2    NAG B O6     1 
HETATM 7577 O  O7     . NAG B 2 .    ? 150.387 156.346 119.913 1.00 32.32 ? 2    NAG B O7     1 
HETATM 7578 CA CA     . CA  C 3 .    ? 194.611 144.247 157.366 1.00 28.25 ? 4000 CA  A CA     1 
HETATM 7579 O  OP3    . A2R D 4 .    ? 131.632 145.779 224.752 1.00 57.72 ? 4001 A2R A OP3    1 
HETATM 7580 P  "P2'"  . A2R D 4 .    ? 131.765 145.038 226.068 1.00 57.72 ? 4001 A2R A "P2'"  1 
HETATM 7581 O  OP1    . A2R D 4 .    ? 132.230 143.625 225.805 1.00 57.72 ? 4001 A2R A OP1    1 
HETATM 7582 O  OP2    . A2R D 4 .    ? 130.399 144.984 226.742 1.00 57.72 ? 4001 A2R A OP2    1 
HETATM 7583 O  "O2'"  . A2R D 4 .    ? 132.813 145.839 227.069 1.00 57.72 ? 4001 A2R A "O2'"  1 
HETATM 7584 C  "C2'"  . A2R D 4 .    ? 134.293 145.638 227.044 1.00 57.72 ? 4001 A2R A "C2'"  1 
HETATM 7585 C  "C1'"  . A2R D 4 .    ? 134.894 145.626 225.528 1.00 57.72 ? 4001 A2R A "C1'"  1 
HETATM 7586 N  N9     . A2R D 4 .    ? 136.044 144.760 225.351 1.00 57.72 ? 4001 A2R A N9     1 
HETATM 7587 C  C4     . A2R D 4 .    ? 136.275 144.028 224.268 1.00 57.72 ? 4001 A2R A C4     1 
HETATM 7588 N  N3     . A2R D 4 .    ? 135.551 143.883 223.137 1.00 57.72 ? 4001 A2R A N3     1 
HETATM 7589 C  C2     . A2R D 4 .    ? 135.986 143.001 222.041 1.00 57.72 ? 4001 A2R A C2     1 
HETATM 7590 N  N1     . A2R D 4 .    ? 137.221 142.257 222.162 1.00 57.72 ? 4001 A2R A N1     1 
HETATM 7591 C  C6     . A2R D 4 .    ? 137.985 142.407 223.359 1.00 57.72 ? 4001 A2R A C6     1 
HETATM 7592 N  N6     . A2R D 4 .    ? 139.192 141.710 223.529 1.00 57.72 ? 4001 A2R A N6     1 
HETATM 7593 C  C5     . A2R D 4 .    ? 137.459 143.344 224.451 1.00 57.72 ? 4001 A2R A C5     1 
HETATM 7594 N  N7     . A2R D 4 .    ? 137.942 143.675 225.631 1.00 57.72 ? 4001 A2R A N7     1 
HETATM 7595 C  C8     . A2R D 4 .    ? 137.078 144.558 226.198 1.00 57.72 ? 4001 A2R A C8     1 
HETATM 7596 O  "O4'"  . A2R D 4 .    ? 135.219 146.848 225.187 1.00 57.72 ? 4001 A2R A "O4'"  1 
HETATM 7597 C  "C3'"  . A2R D 4 .    ? 134.911 146.889 227.642 1.00 57.72 ? 4001 A2R A "C3'"  1 
HETATM 7598 O  "O3'"  . A2R D 4 .    ? 133.973 147.517 228.608 1.00 57.72 ? 4001 A2R A "O3'"  1 
HETATM 7599 C  "C4'"  . A2R D 4 .    ? 135.058 147.783 226.351 1.00 57.72 ? 4001 A2R A "C4'"  1 
HETATM 7600 C  "C5'"  . A2R D 4 .    ? 136.204 148.604 226.446 1.00 57.72 ? 4001 A2R A "C5'"  1 
HETATM 7601 O  "O5'"  . A2R D 4 .    ? 137.076 148.301 225.342 1.00 57.72 ? 4001 A2R A "O5'"  1 
HETATM 7602 P  P      . A2R D 4 .    ? 138.745 148.573 225.556 1.00 57.72 ? 4001 A2R A P      1 
HETATM 7603 O  O1     . A2R D 4 .    ? 138.986 149.076 226.954 1.00 57.72 ? 4001 A2R A O1     1 
HETATM 7604 O  O2     . A2R D 4 .    ? 139.219 149.613 224.580 1.00 57.72 ? 4001 A2R A O2     1 
HETATM 7605 O  O3     . A2R D 4 .    ? 139.587 147.150 225.296 1.00 57.72 ? 4001 A2R A O3     1 
HETATM 7606 P  P1     . A2R D 4 .    ? 141.003 146.723 226.138 1.00 57.72 ? 4001 A2R A P1     1 
HETATM 7607 O  O11    . A2R D 4 .    ? 142.086 147.725 225.805 1.00 57.72 ? 4001 A2R A O11    1 
HETATM 7608 O  O12    . A2R D 4 .    ? 140.696 146.760 227.612 1.00 57.72 ? 4001 A2R A O12    1 
HETATM 7609 O  "O15'" . A2R D 4 .    ? 141.486 145.182 225.690 1.00 57.72 ? 4001 A2R A "O15'" 1 
HETATM 7610 C  "C15'" . A2R D 4 .    ? 141.493 144.852 224.288 1.00 57.72 ? 4001 A2R A "C15'" 1 
HETATM 7611 C  "C14'" . A2R D 4 .    ? 142.135 143.620 224.057 1.00 57.72 ? 4001 A2R A "C14'" 1 
HETATM 7612 C  "C13'" . A2R D 4 .    ? 143.412 143.490 224.921 1.00 57.72 ? 4001 A2R A "C13'" 1 
HETATM 7613 O  "O13'" . A2R D 4 .    ? 143.259 142.352 225.865 1.00 57.72 ? 4001 A2R A "O13'" 1 
HETATM 7614 C  "C12'" . A2R D 4 .    ? 144.387 143.223 224.089 1.00 57.72 ? 4001 A2R A "C12'" 1 
HETATM 7615 O  "O12'" . A2R D 4 .    ? 144.646 141.782 224.066 1.00 57.72 ? 4001 A2R A "O12'" 1 
HETATM 7616 C  "C11'" . A2R D 4 .    ? 143.910 143.715 222.628 1.00 57.72 ? 4001 A2R A "C11'" 1 
HETATM 7617 O  "O14'" . A2R D 4 .    ? 142.608 143.544 222.592 1.00 57.72 ? 4001 A2R A "O14'" 1 
HETATM 7618 O  "O11'" . A2R D 4 .    ? 144.228 145.050 222.452 1.00 57.72 ? 4001 A2R A "O11'" 1 
# 
