data_9DW9
# 
_entry.id   9DW9 
# 
_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   9DW9         pdb_00009dw9 10.2210/pdb9dw9/pdb 
WWPDB D_1000288912 ?            ?                   
EMDB  EMD-47239    ?            ?                   
# 
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 2024-11-13 
2 'Structure model' 1 1 2024-11-20 
3 'Structure model' 1 2 2024-11-27 
# 
_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 2 'Structure model' 'Database references' 
3 3 'Structure model' 'Data collection'     
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
3 2 'Structure model' em_admin        
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' '_citation.country'                 
2  2 'Structure model' '_citation.journal_abbrev'          
3  2 'Structure model' '_citation.journal_id_ASTM'         
4  2 'Structure model' '_citation.journal_id_CSD'          
5  2 'Structure model' '_citation.journal_id_ISSN'         
6  2 'Structure model' '_citation.journal_volume'          
7  2 'Structure model' '_citation.page_first'              
8  2 'Structure model' '_citation.page_last'               
9  2 'Structure model' '_citation.pdbx_database_id_DOI'    
10 2 'Structure model' '_citation.pdbx_database_id_PubMed' 
11 2 'Structure model' '_citation.title'                   
12 2 'Structure model' '_citation.year'                    
13 2 'Structure model' '_citation_author.identifier_ORCID' 
14 2 'Structure model' '_em_admin.last_update'             
15 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                        9DW9 
_pdbx_database_status.recvd_initial_deposition_date   2024-10-08 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_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        'Phosphorylated (E1371Q)CFTR in complex with PKA-C' 
_pdbx_database_related.db_id          EMD-47239 
_pdbx_database_related.content_type   'associated EM volume' 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              juechen@rockefeller.edu 
_pdbx_contact_author.name_first         Jue 
_pdbx_contact_author.name_last          Chen 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-2075-4283 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Fiedorczuk, K.' 1 ? 
'Chen, J.'       2 ? 
'Csanady, L.'    3 ? 
# 
_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                e2409049121 
_citation.page_last                 e2409049121 
_citation.title                     
'The structures of protein kinase A in complex with CFTR: Mechanisms of phosphorylation and noncatalytic activation.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1073/pnas.2409049121 
_citation.pdbx_database_id_PubMed   39495916 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Fiedorczuk, K.' 1 ?                   
primary 'Iordanov, I.'   2 ?                   
primary 'Mihalyi, C.'    3 0000-0001-7536-3066 
primary 'Szollosi, A.'   4 0000-0002-5570-4609 
primary 'Csanady, L.'    5 0000-0002-6547-5889 
primary 'Chen, J.'       6 0000-0003-2075-4283 
# 
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 'Cystic fibrosis transmembrane conductance regulator'   168414.453 1 5.6.1.6   E1371Q ? 
'phosphorylated (E1371Q)CFTR' 
2 polymer     man 'cAMP-dependent protein kinase catalytic subunit alpha' 40757.633  1 2.7.11.11 ?      ? PKA-C 
3 non-polymer syn CHOLESTEROL                                             386.654    1 ?         ?      ? ? 
4 non-polymer syn DECANE                                                  142.282    4 ?         ?      ? ? 
5 non-polymer syn 'MAGNESIUM ION'                                         24.305     4 ?         ?      ? ? 
6 non-polymer syn "ADENOSINE-5'-TRIPHOSPHATE"                             507.181    3 ?         ?      ? ? 
7 non-polymer syn 'CHLORIDE ION'                                          35.453     4 ?         ?      ? ? 
8 non-polymer syn UNDECANE                                                156.308    3 ?         ?      ? ? 
9 water       nat water                                                   18.015     3 ?         ?      ? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 'CFTR,ATP-binding cassette sub-family C member 7,Channel conductance-controlling ATPase,cAMP-dependent chloride channel' 
2 'PKA C-alpha'                                                                                                            
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no yes 
;MQRSPLEKASVVSKLFFSWTRPILRKGYRQRLELSDIYQIPSVDSADNLSEKLEREWDRELASKKNPKLINALRRCFFWR
FMFYGIFLYLGEVTKAVQPLLLGRIIASYDPDNKEERSIAIYLGIGLCLLFIVRTLLLHPAIFGLHHIGMQMRIAMFSLI
YKKTLKLSSRVLDKISIGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVALLMGLIWELLQASAFCGLGFLIVLALFQAGL
GRMMMKYRDQRAGKISERLVITSEMIENIQSVKAYCWEEAMEKMIENLRQTELKLTRKAAYVRYFNSSAFFFSGFFVVFL
SVLPYALIKGIILRKIFTTISFCIVLRMAVTRQFPWAVQTWYDSLGAINKIQDFLQKQEYKTLEYNLTTTEVVMENVTAF
WEEGFGELFEKAKQNNNNRKTSNGDDSLFFSNFSLLGTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEG
KIKHSGRISFCSQFSWIMPGTIKENIIFGVSYDEYRYRSVIKACQLEEDISKFAEKDNIVLGEGGITLSGGQRARISLAR
AVYKDADLYLLDSPFGYLDVLTEKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQNLQPDF
SSKLMGCDSFDQFSAERRNSILTETLHRFSLEGDAPVSWTETKKQSFKQTGEFGEKRKNSILNPINSIRKFSIVQKTPLQ
MNGIEEDSDEPLERRLSLVPDSEQGEAILPRISVISTGPTLQARRRQSVLNLMTHSVNQGQNIHRKTTASTRKVSLAPQA
NLTELDIYSRRL(SEP)QETGLEISEEINEEDLKECFFDDMESIPAVTTWNTYLRYITVHKSLIFVLIWCLVIFLAEVAA
SLVVLWLLGNTPLQDKGNSTHSRNNSYAVIITSTSSYYVFYIYVGVADTLLAMGFFRGLPLVHTLITVSKILHHKMLHSV
LQAPMSTLNTLKAGGILNRFSKDIAILDDLLPLTIFDFIQLLLIVIGAIAVVAVLQPYIFVATVPVIVAFIMLRAYFLQT
SQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFGRQPYFETLFHKALNLHTANWFLYLSTLRWFQMRIEMIFVIFFIAVTF
ISILTTGEGEGRVGIILTLAMNIMSTLQWAVNSSIDVDSLMRSVSRVFKFIDMPTEGKPTKSTKPYKNGQLSKVMIIENS
HVKKDDIWPSGGQMTVKDLTAKYTEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGEIQIDGVSWDS
ITLQQWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCL
ARSVLSKAKILLLDQPSAHLDPVTYQIIRRTLKQAFADCTVILCEHRIEAMLECQQFLVIEENKVRQYDSIQKLLNERSL
FRQAISPSDRVKLFPHRNSSKCKSKPQIAALKEETEEEVQDTRL
;
;MQRSPLEKASVVSKLFFSWTRPILRKGYRQRLELSDIYQIPSVDSADNLSEKLEREWDRELASKKNPKLINALRRCFFWR
FMFYGIFLYLGEVTKAVQPLLLGRIIASYDPDNKEERSIAIYLGIGLCLLFIVRTLLLHPAIFGLHHIGMQMRIAMFSLI
YKKTLKLSSRVLDKISIGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVALLMGLIWELLQASAFCGLGFLIVLALFQAGL
GRMMMKYRDQRAGKISERLVITSEMIENIQSVKAYCWEEAMEKMIENLRQTELKLTRKAAYVRYFNSSAFFFSGFFVVFL
SVLPYALIKGIILRKIFTTISFCIVLRMAVTRQFPWAVQTWYDSLGAINKIQDFLQKQEYKTLEYNLTTTEVVMENVTAF
WEEGFGELFEKAKQNNNNRKTSNGDDSLFFSNFSLLGTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEG
KIKHSGRISFCSQFSWIMPGTIKENIIFGVSYDEYRYRSVIKACQLEEDISKFAEKDNIVLGEGGITLSGGQRARISLAR
AVYKDADLYLLDSPFGYLDVLTEKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQNLQPDF
SSKLMGCDSFDQFSAERRNSILTETLHRFSLEGDAPVSWTETKKQSFKQTGEFGEKRKNSILNPINSIRKFSIVQKTPLQ
MNGIEEDSDEPLERRLSLVPDSEQGEAILPRISVISTGPTLQARRRQSVLNLMTHSVNQGQNIHRKTTASTRKVSLAPQA
NLTELDIYSRRLSQETGLEISEEINEEDLKECFFDDMESIPAVTTWNTYLRYITVHKSLIFVLIWCLVIFLAEVAASLVV
LWLLGNTPLQDKGNSTHSRNNSYAVIITSTSSYYVFYIYVGVADTLLAMGFFRGLPLVHTLITVSKILHHKMLHSVLQAP
MSTLNTLKAGGILNRFSKDIAILDDLLPLTIFDFIQLLLIVIGAIAVVAVLQPYIFVATVPVIVAFIMLRAYFLQTSQQL
KQLESEGRSPIFTHLVTSLKGLWTLRAFGRQPYFETLFHKALNLHTANWFLYLSTLRWFQMRIEMIFVIFFIAVTFISIL
TTGEGEGRVGIILTLAMNIMSTLQWAVNSSIDVDSLMRSVSRVFKFIDMPTEGKPTKSTKPYKNGQLSKVMIIENSHVKK
DDIWPSGGQMTVKDLTAKYTEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGEIQIDGVSWDSITLQ
QWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSV
LSKAKILLLDQPSAHLDPVTYQIIRRTLKQAFADCTVILCEHRIEAMLECQQFLVIEENKVRQYDSIQKLLNERSLFRQA
ISPSDRVKLFPHRNSSKCKSKPQIAALKEETEEEVQDTRL
;
A ? 
2 'polypeptide(L)' no yes 
;MGNAAAAKKGSEQESVKEFLAKAKEDFLKKWENPAQNTAHLDQFERIKTLGTGSFGRVMLVKHMETGNHYAMKILDKQKV
VKLKQIEHTLNEKRILQAVNFPFLVKLEFSFKDNSNLYMVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHS
LDLIYRDLKPENLLIDQQGYIQVTDFGFAKRVKGRTW(TPO)LCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGY
PPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVNDIKNHKWFATTDWIAIYQRKVEAPFI
PKFKGPGDTSNFDDYEEEEIRVSINEKCGKEFSEF
;
;MGNAAAAKKGSEQESVKEFLAKAKEDFLKKWENPAQNTAHLDQFERIKTLGTGSFGRVMLVKHMETGNHYAMKILDKQKV
VKLKQIEHTLNEKRILQAVNFPFLVKLEFSFKDNSNLYMVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHS
LDLIYRDLKPENLLIDQQGYIQVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFF
ADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVNDIKNHKWFATTDWIAIYQRKVEAPFIPKFK
GPGDTSNFDDYEEEEIRVSINEKCGKEFSEF
;
G ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 CHOLESTEROL                 CLR 
4 DECANE                      D10 
5 'MAGNESIUM ION'             MG  
6 "ADENOSINE-5'-TRIPHOSPHATE" ATP 
7 'CHLORIDE ION'              CL  
8 UNDECANE                    UND 
9 water                       HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1    MET n 
1 2    GLN n 
1 3    ARG n 
1 4    SER n 
1 5    PRO n 
1 6    LEU n 
1 7    GLU n 
1 8    LYS n 
1 9    ALA n 
1 10   SER n 
1 11   VAL n 
1 12   VAL n 
1 13   SER n 
1 14   LYS n 
1 15   LEU n 
1 16   PHE n 
1 17   PHE n 
1 18   SER n 
1 19   TRP n 
1 20   THR n 
1 21   ARG n 
1 22   PRO n 
1 23   ILE n 
1 24   LEU n 
1 25   ARG n 
1 26   LYS n 
1 27   GLY n 
1 28   TYR n 
1 29   ARG n 
1 30   GLN n 
1 31   ARG n 
1 32   LEU n 
1 33   GLU n 
1 34   LEU n 
1 35   SER n 
1 36   ASP n 
1 37   ILE n 
1 38   TYR n 
1 39   GLN n 
1 40   ILE n 
1 41   PRO n 
1 42   SER n 
1 43   VAL n 
1 44   ASP n 
1 45   SER n 
1 46   ALA n 
1 47   ASP n 
1 48   ASN n 
1 49   LEU n 
1 50   SER n 
1 51   GLU n 
1 52   LYS n 
1 53   LEU n 
1 54   GLU n 
1 55   ARG n 
1 56   GLU n 
1 57   TRP n 
1 58   ASP n 
1 59   ARG n 
1 60   GLU n 
1 61   LEU n 
1 62   ALA n 
1 63   SER n 
1 64   LYS n 
1 65   LYS n 
1 66   ASN n 
1 67   PRO n 
1 68   LYS n 
1 69   LEU n 
1 70   ILE n 
1 71   ASN n 
1 72   ALA n 
1 73   LEU n 
1 74   ARG n 
1 75   ARG n 
1 76   CYS n 
1 77   PHE n 
1 78   PHE n 
1 79   TRP n 
1 80   ARG n 
1 81   PHE n 
1 82   MET n 
1 83   PHE n 
1 84   TYR n 
1 85   GLY n 
1 86   ILE n 
1 87   PHE n 
1 88   LEU n 
1 89   TYR n 
1 90   LEU n 
1 91   GLY n 
1 92   GLU n 
1 93   VAL n 
1 94   THR n 
1 95   LYS n 
1 96   ALA n 
1 97   VAL n 
1 98   GLN n 
1 99   PRO n 
1 100  LEU n 
1 101  LEU n 
1 102  LEU n 
1 103  GLY n 
1 104  ARG n 
1 105  ILE n 
1 106  ILE n 
1 107  ALA n 
1 108  SER n 
1 109  TYR n 
1 110  ASP n 
1 111  PRO n 
1 112  ASP n 
1 113  ASN n 
1 114  LYS n 
1 115  GLU n 
1 116  GLU n 
1 117  ARG n 
1 118  SER n 
1 119  ILE n 
1 120  ALA n 
1 121  ILE n 
1 122  TYR n 
1 123  LEU n 
1 124  GLY n 
1 125  ILE n 
1 126  GLY n 
1 127  LEU n 
1 128  CYS n 
1 129  LEU n 
1 130  LEU n 
1 131  PHE n 
1 132  ILE n 
1 133  VAL n 
1 134  ARG n 
1 135  THR n 
1 136  LEU n 
1 137  LEU n 
1 138  LEU n 
1 139  HIS n 
1 140  PRO n 
1 141  ALA n 
1 142  ILE n 
1 143  PHE n 
1 144  GLY n 
1 145  LEU n 
1 146  HIS n 
1 147  HIS n 
1 148  ILE n 
1 149  GLY n 
1 150  MET n 
1 151  GLN n 
1 152  MET n 
1 153  ARG n 
1 154  ILE n 
1 155  ALA n 
1 156  MET n 
1 157  PHE n 
1 158  SER n 
1 159  LEU n 
1 160  ILE n 
1 161  TYR n 
1 162  LYS n 
1 163  LYS n 
1 164  THR n 
1 165  LEU n 
1 166  LYS n 
1 167  LEU n 
1 168  SER n 
1 169  SER n 
1 170  ARG n 
1 171  VAL n 
1 172  LEU n 
1 173  ASP n 
1 174  LYS n 
1 175  ILE n 
1 176  SER n 
1 177  ILE n 
1 178  GLY n 
1 179  GLN n 
1 180  LEU n 
1 181  VAL n 
1 182  SER n 
1 183  LEU n 
1 184  LEU n 
1 185  SER n 
1 186  ASN n 
1 187  ASN n 
1 188  LEU n 
1 189  ASN n 
1 190  LYS n 
1 191  PHE n 
1 192  ASP n 
1 193  GLU n 
1 194  GLY n 
1 195  LEU n 
1 196  ALA n 
1 197  LEU n 
1 198  ALA n 
1 199  HIS n 
1 200  PHE n 
1 201  VAL n 
1 202  TRP n 
1 203  ILE n 
1 204  ALA n 
1 205  PRO n 
1 206  LEU n 
1 207  GLN n 
1 208  VAL n 
1 209  ALA n 
1 210  LEU n 
1 211  LEU n 
1 212  MET n 
1 213  GLY n 
1 214  LEU n 
1 215  ILE n 
1 216  TRP n 
1 217  GLU n 
1 218  LEU n 
1 219  LEU n 
1 220  GLN n 
1 221  ALA n 
1 222  SER n 
1 223  ALA n 
1 224  PHE n 
1 225  CYS n 
1 226  GLY n 
1 227  LEU n 
1 228  GLY n 
1 229  PHE n 
1 230  LEU n 
1 231  ILE n 
1 232  VAL n 
1 233  LEU n 
1 234  ALA n 
1 235  LEU n 
1 236  PHE n 
1 237  GLN n 
1 238  ALA n 
1 239  GLY n 
1 240  LEU n 
1 241  GLY n 
1 242  ARG n 
1 243  MET n 
1 244  MET n 
1 245  MET n 
1 246  LYS n 
1 247  TYR n 
1 248  ARG n 
1 249  ASP n 
1 250  GLN n 
1 251  ARG n 
1 252  ALA n 
1 253  GLY n 
1 254  LYS n 
1 255  ILE n 
1 256  SER n 
1 257  GLU n 
1 258  ARG n 
1 259  LEU n 
1 260  VAL n 
1 261  ILE n 
1 262  THR n 
1 263  SER n 
1 264  GLU n 
1 265  MET n 
1 266  ILE n 
1 267  GLU n 
1 268  ASN n 
1 269  ILE n 
1 270  GLN n 
1 271  SER n 
1 272  VAL n 
1 273  LYS n 
1 274  ALA n 
1 275  TYR n 
1 276  CYS n 
1 277  TRP n 
1 278  GLU n 
1 279  GLU n 
1 280  ALA n 
1 281  MET n 
1 282  GLU n 
1 283  LYS n 
1 284  MET n 
1 285  ILE n 
1 286  GLU n 
1 287  ASN n 
1 288  LEU n 
1 289  ARG n 
1 290  GLN n 
1 291  THR n 
1 292  GLU n 
1 293  LEU n 
1 294  LYS n 
1 295  LEU n 
1 296  THR n 
1 297  ARG n 
1 298  LYS n 
1 299  ALA n 
1 300  ALA n 
1 301  TYR n 
1 302  VAL n 
1 303  ARG n 
1 304  TYR n 
1 305  PHE n 
1 306  ASN n 
1 307  SER n 
1 308  SER n 
1 309  ALA n 
1 310  PHE n 
1 311  PHE n 
1 312  PHE n 
1 313  SER n 
1 314  GLY n 
1 315  PHE n 
1 316  PHE n 
1 317  VAL n 
1 318  VAL n 
1 319  PHE n 
1 320  LEU n 
1 321  SER n 
1 322  VAL n 
1 323  LEU n 
1 324  PRO n 
1 325  TYR n 
1 326  ALA n 
1 327  LEU n 
1 328  ILE n 
1 329  LYS n 
1 330  GLY n 
1 331  ILE n 
1 332  ILE n 
1 333  LEU n 
1 334  ARG n 
1 335  LYS n 
1 336  ILE n 
1 337  PHE n 
1 338  THR n 
1 339  THR n 
1 340  ILE n 
1 341  SER n 
1 342  PHE n 
1 343  CYS n 
1 344  ILE n 
1 345  VAL n 
1 346  LEU n 
1 347  ARG n 
1 348  MET n 
1 349  ALA n 
1 350  VAL n 
1 351  THR n 
1 352  ARG n 
1 353  GLN n 
1 354  PHE n 
1 355  PRO n 
1 356  TRP n 
1 357  ALA n 
1 358  VAL n 
1 359  GLN n 
1 360  THR n 
1 361  TRP n 
1 362  TYR n 
1 363  ASP n 
1 364  SER n 
1 365  LEU n 
1 366  GLY n 
1 367  ALA n 
1 368  ILE n 
1 369  ASN n 
1 370  LYS n 
1 371  ILE n 
1 372  GLN n 
1 373  ASP n 
1 374  PHE n 
1 375  LEU n 
1 376  GLN n 
1 377  LYS n 
1 378  GLN n 
1 379  GLU n 
1 380  TYR n 
1 381  LYS n 
1 382  THR n 
1 383  LEU n 
1 384  GLU n 
1 385  TYR n 
1 386  ASN n 
1 387  LEU n 
1 388  THR n 
1 389  THR n 
1 390  THR n 
1 391  GLU n 
1 392  VAL n 
1 393  VAL n 
1 394  MET n 
1 395  GLU n 
1 396  ASN n 
1 397  VAL n 
1 398  THR n 
1 399  ALA n 
1 400  PHE n 
1 401  TRP n 
1 402  GLU n 
1 403  GLU n 
1 404  GLY n 
1 405  PHE n 
1 406  GLY n 
1 407  GLU n 
1 408  LEU n 
1 409  PHE n 
1 410  GLU n 
1 411  LYS n 
1 412  ALA n 
1 413  LYS n 
1 414  GLN n 
1 415  ASN n 
1 416  ASN n 
1 417  ASN n 
1 418  ASN n 
1 419  ARG n 
1 420  LYS n 
1 421  THR n 
1 422  SER n 
1 423  ASN n 
1 424  GLY n 
1 425  ASP n 
1 426  ASP n 
1 427  SER n 
1 428  LEU n 
1 429  PHE n 
1 430  PHE n 
1 431  SER n 
1 432  ASN n 
1 433  PHE n 
1 434  SER n 
1 435  LEU n 
1 436  LEU n 
1 437  GLY n 
1 438  THR n 
1 439  PRO n 
1 440  VAL n 
1 441  LEU n 
1 442  LYS n 
1 443  ASP n 
1 444  ILE n 
1 445  ASN n 
1 446  PHE n 
1 447  LYS n 
1 448  ILE n 
1 449  GLU n 
1 450  ARG n 
1 451  GLY n 
1 452  GLN n 
1 453  LEU n 
1 454  LEU n 
1 455  ALA n 
1 456  VAL n 
1 457  ALA n 
1 458  GLY n 
1 459  SER n 
1 460  THR n 
1 461  GLY n 
1 462  ALA n 
1 463  GLY n 
1 464  LYS n 
1 465  THR n 
1 466  SER n 
1 467  LEU n 
1 468  LEU n 
1 469  MET n 
1 470  VAL n 
1 471  ILE n 
1 472  MET n 
1 473  GLY n 
1 474  GLU n 
1 475  LEU n 
1 476  GLU n 
1 477  PRO n 
1 478  SER n 
1 479  GLU n 
1 480  GLY n 
1 481  LYS n 
1 482  ILE n 
1 483  LYS n 
1 484  HIS n 
1 485  SER n 
1 486  GLY n 
1 487  ARG n 
1 488  ILE n 
1 489  SER n 
1 490  PHE n 
1 491  CYS n 
1 492  SER n 
1 493  GLN n 
1 494  PHE n 
1 495  SER n 
1 496  TRP n 
1 497  ILE n 
1 498  MET n 
1 499  PRO n 
1 500  GLY n 
1 501  THR n 
1 502  ILE n 
1 503  LYS n 
1 504  GLU n 
1 505  ASN n 
1 506  ILE n 
1 507  ILE n 
1 508  PHE n 
1 509  GLY n 
1 510  VAL n 
1 511  SER n 
1 512  TYR n 
1 513  ASP n 
1 514  GLU n 
1 515  TYR n 
1 516  ARG n 
1 517  TYR n 
1 518  ARG n 
1 519  SER n 
1 520  VAL n 
1 521  ILE n 
1 522  LYS n 
1 523  ALA n 
1 524  CYS n 
1 525  GLN n 
1 526  LEU n 
1 527  GLU n 
1 528  GLU n 
1 529  ASP n 
1 530  ILE n 
1 531  SER n 
1 532  LYS n 
1 533  PHE n 
1 534  ALA n 
1 535  GLU n 
1 536  LYS n 
1 537  ASP n 
1 538  ASN n 
1 539  ILE n 
1 540  VAL n 
1 541  LEU n 
1 542  GLY n 
1 543  GLU n 
1 544  GLY n 
1 545  GLY n 
1 546  ILE n 
1 547  THR n 
1 548  LEU n 
1 549  SER n 
1 550  GLY n 
1 551  GLY n 
1 552  GLN n 
1 553  ARG n 
1 554  ALA n 
1 555  ARG n 
1 556  ILE n 
1 557  SER n 
1 558  LEU n 
1 559  ALA n 
1 560  ARG n 
1 561  ALA n 
1 562  VAL n 
1 563  TYR n 
1 564  LYS n 
1 565  ASP n 
1 566  ALA n 
1 567  ASP n 
1 568  LEU n 
1 569  TYR n 
1 570  LEU n 
1 571  LEU n 
1 572  ASP n 
1 573  SER n 
1 574  PRO n 
1 575  PHE n 
1 576  GLY n 
1 577  TYR n 
1 578  LEU n 
1 579  ASP n 
1 580  VAL n 
1 581  LEU n 
1 582  THR n 
1 583  GLU n 
1 584  LYS n 
1 585  GLU n 
1 586  ILE n 
1 587  PHE n 
1 588  GLU n 
1 589  SER n 
1 590  CYS n 
1 591  VAL n 
1 592  CYS n 
1 593  LYS n 
1 594  LEU n 
1 595  MET n 
1 596  ALA n 
1 597  ASN n 
1 598  LYS n 
1 599  THR n 
1 600  ARG n 
1 601  ILE n 
1 602  LEU n 
1 603  VAL n 
1 604  THR n 
1 605  SER n 
1 606  LYS n 
1 607  MET n 
1 608  GLU n 
1 609  HIS n 
1 610  LEU n 
1 611  LYS n 
1 612  LYS n 
1 613  ALA n 
1 614  ASP n 
1 615  LYS n 
1 616  ILE n 
1 617  LEU n 
1 618  ILE n 
1 619  LEU n 
1 620  HIS n 
1 621  GLU n 
1 622  GLY n 
1 623  SER n 
1 624  SER n 
1 625  TYR n 
1 626  PHE n 
1 627  TYR n 
1 628  GLY n 
1 629  THR n 
1 630  PHE n 
1 631  SER n 
1 632  GLU n 
1 633  LEU n 
1 634  GLN n 
1 635  ASN n 
1 636  LEU n 
1 637  GLN n 
1 638  PRO n 
1 639  ASP n 
1 640  PHE n 
1 641  SER n 
1 642  SER n 
1 643  LYS n 
1 644  LEU n 
1 645  MET n 
1 646  GLY n 
1 647  CYS n 
1 648  ASP n 
1 649  SER n 
1 650  PHE n 
1 651  ASP n 
1 652  GLN n 
1 653  PHE n 
1 654  SER n 
1 655  ALA n 
1 656  GLU n 
1 657  ARG n 
1 658  ARG n 
1 659  ASN n 
1 660  SER n 
1 661  ILE n 
1 662  LEU n 
1 663  THR n 
1 664  GLU n 
1 665  THR n 
1 666  LEU n 
1 667  HIS n 
1 668  ARG n 
1 669  PHE n 
1 670  SER n 
1 671  LEU n 
1 672  GLU n 
1 673  GLY n 
1 674  ASP n 
1 675  ALA n 
1 676  PRO n 
1 677  VAL n 
1 678  SER n 
1 679  TRP n 
1 680  THR n 
1 681  GLU n 
1 682  THR n 
1 683  LYS n 
1 684  LYS n 
1 685  GLN n 
1 686  SER n 
1 687  PHE n 
1 688  LYS n 
1 689  GLN n 
1 690  THR n 
1 691  GLY n 
1 692  GLU n 
1 693  PHE n 
1 694  GLY n 
1 695  GLU n 
1 696  LYS n 
1 697  ARG n 
1 698  LYS n 
1 699  ASN n 
1 700  SER n 
1 701  ILE n 
1 702  LEU n 
1 703  ASN n 
1 704  PRO n 
1 705  ILE n 
1 706  ASN n 
1 707  SER n 
1 708  ILE n 
1 709  ARG n 
1 710  LYS n 
1 711  PHE n 
1 712  SER n 
1 713  ILE n 
1 714  VAL n 
1 715  GLN n 
1 716  LYS n 
1 717  THR n 
1 718  PRO n 
1 719  LEU n 
1 720  GLN n 
1 721  MET n 
1 722  ASN n 
1 723  GLY n 
1 724  ILE n 
1 725  GLU n 
1 726  GLU n 
1 727  ASP n 
1 728  SER n 
1 729  ASP n 
1 730  GLU n 
1 731  PRO n 
1 732  LEU n 
1 733  GLU n 
1 734  ARG n 
1 735  ARG n 
1 736  LEU n 
1 737  SER n 
1 738  LEU n 
1 739  VAL n 
1 740  PRO n 
1 741  ASP n 
1 742  SER n 
1 743  GLU n 
1 744  GLN n 
1 745  GLY n 
1 746  GLU n 
1 747  ALA n 
1 748  ILE n 
1 749  LEU n 
1 750  PRO n 
1 751  ARG n 
1 752  ILE n 
1 753  SER n 
1 754  VAL n 
1 755  ILE n 
1 756  SER n 
1 757  THR n 
1 758  GLY n 
1 759  PRO n 
1 760  THR n 
1 761  LEU n 
1 762  GLN n 
1 763  ALA n 
1 764  ARG n 
1 765  ARG n 
1 766  ARG n 
1 767  GLN n 
1 768  SER n 
1 769  VAL n 
1 770  LEU n 
1 771  ASN n 
1 772  LEU n 
1 773  MET n 
1 774  THR n 
1 775  HIS n 
1 776  SER n 
1 777  VAL n 
1 778  ASN n 
1 779  GLN n 
1 780  GLY n 
1 781  GLN n 
1 782  ASN n 
1 783  ILE n 
1 784  HIS n 
1 785  ARG n 
1 786  LYS n 
1 787  THR n 
1 788  THR n 
1 789  ALA n 
1 790  SER n 
1 791  THR n 
1 792  ARG n 
1 793  LYS n 
1 794  VAL n 
1 795  SER n 
1 796  LEU n 
1 797  ALA n 
1 798  PRO n 
1 799  GLN n 
1 800  ALA n 
1 801  ASN n 
1 802  LEU n 
1 803  THR n 
1 804  GLU n 
1 805  LEU n 
1 806  ASP n 
1 807  ILE n 
1 808  TYR n 
1 809  SER n 
1 810  ARG n 
1 811  ARG n 
1 812  LEU n 
1 813  SEP n 
1 814  GLN n 
1 815  GLU n 
1 816  THR n 
1 817  GLY n 
1 818  LEU n 
1 819  GLU n 
1 820  ILE n 
1 821  SER n 
1 822  GLU n 
1 823  GLU n 
1 824  ILE n 
1 825  ASN n 
1 826  GLU n 
1 827  GLU n 
1 828  ASP n 
1 829  LEU n 
1 830  LYS n 
1 831  GLU n 
1 832  CYS n 
1 833  PHE n 
1 834  PHE n 
1 835  ASP n 
1 836  ASP n 
1 837  MET n 
1 838  GLU n 
1 839  SER n 
1 840  ILE n 
1 841  PRO n 
1 842  ALA n 
1 843  VAL n 
1 844  THR n 
1 845  THR n 
1 846  TRP n 
1 847  ASN n 
1 848  THR n 
1 849  TYR n 
1 850  LEU n 
1 851  ARG n 
1 852  TYR n 
1 853  ILE n 
1 854  THR n 
1 855  VAL n 
1 856  HIS n 
1 857  LYS n 
1 858  SER n 
1 859  LEU n 
1 860  ILE n 
1 861  PHE n 
1 862  VAL n 
1 863  LEU n 
1 864  ILE n 
1 865  TRP n 
1 866  CYS n 
1 867  LEU n 
1 868  VAL n 
1 869  ILE n 
1 870  PHE n 
1 871  LEU n 
1 872  ALA n 
1 873  GLU n 
1 874  VAL n 
1 875  ALA n 
1 876  ALA n 
1 877  SER n 
1 878  LEU n 
1 879  VAL n 
1 880  VAL n 
1 881  LEU n 
1 882  TRP n 
1 883  LEU n 
1 884  LEU n 
1 885  GLY n 
1 886  ASN n 
1 887  THR n 
1 888  PRO n 
1 889  LEU n 
1 890  GLN n 
1 891  ASP n 
1 892  LYS n 
1 893  GLY n 
1 894  ASN n 
1 895  SER n 
1 896  THR n 
1 897  HIS n 
1 898  SER n 
1 899  ARG n 
1 900  ASN n 
1 901  ASN n 
1 902  SER n 
1 903  TYR n 
1 904  ALA n 
1 905  VAL n 
1 906  ILE n 
1 907  ILE n 
1 908  THR n 
1 909  SER n 
1 910  THR n 
1 911  SER n 
1 912  SER n 
1 913  TYR n 
1 914  TYR n 
1 915  VAL n 
1 916  PHE n 
1 917  TYR n 
1 918  ILE n 
1 919  TYR n 
1 920  VAL n 
1 921  GLY n 
1 922  VAL n 
1 923  ALA n 
1 924  ASP n 
1 925  THR n 
1 926  LEU n 
1 927  LEU n 
1 928  ALA n 
1 929  MET n 
1 930  GLY n 
1 931  PHE n 
1 932  PHE n 
1 933  ARG n 
1 934  GLY n 
1 935  LEU n 
1 936  PRO n 
1 937  LEU n 
1 938  VAL n 
1 939  HIS n 
1 940  THR n 
1 941  LEU n 
1 942  ILE n 
1 943  THR n 
1 944  VAL n 
1 945  SER n 
1 946  LYS n 
1 947  ILE n 
1 948  LEU n 
1 949  HIS n 
1 950  HIS n 
1 951  LYS n 
1 952  MET n 
1 953  LEU n 
1 954  HIS n 
1 955  SER n 
1 956  VAL n 
1 957  LEU n 
1 958  GLN n 
1 959  ALA n 
1 960  PRO n 
1 961  MET n 
1 962  SER n 
1 963  THR n 
1 964  LEU n 
1 965  ASN n 
1 966  THR n 
1 967  LEU n 
1 968  LYS n 
1 969  ALA n 
1 970  GLY n 
1 971  GLY n 
1 972  ILE n 
1 973  LEU n 
1 974  ASN n 
1 975  ARG n 
1 976  PHE n 
1 977  SER n 
1 978  LYS n 
1 979  ASP n 
1 980  ILE n 
1 981  ALA n 
1 982  ILE n 
1 983  LEU n 
1 984  ASP n 
1 985  ASP n 
1 986  LEU n 
1 987  LEU n 
1 988  PRO n 
1 989  LEU n 
1 990  THR n 
1 991  ILE n 
1 992  PHE n 
1 993  ASP n 
1 994  PHE n 
1 995  ILE n 
1 996  GLN n 
1 997  LEU n 
1 998  LEU n 
1 999  LEU n 
1 1000 ILE n 
1 1001 VAL n 
1 1002 ILE n 
1 1003 GLY n 
1 1004 ALA n 
1 1005 ILE n 
1 1006 ALA n 
1 1007 VAL n 
1 1008 VAL n 
1 1009 ALA n 
1 1010 VAL n 
1 1011 LEU n 
1 1012 GLN n 
1 1013 PRO n 
1 1014 TYR n 
1 1015 ILE n 
1 1016 PHE n 
1 1017 VAL n 
1 1018 ALA n 
1 1019 THR n 
1 1020 VAL n 
1 1021 PRO n 
1 1022 VAL n 
1 1023 ILE n 
1 1024 VAL n 
1 1025 ALA n 
1 1026 PHE n 
1 1027 ILE n 
1 1028 MET n 
1 1029 LEU n 
1 1030 ARG n 
1 1031 ALA n 
1 1032 TYR n 
1 1033 PHE n 
1 1034 LEU n 
1 1035 GLN n 
1 1036 THR n 
1 1037 SER n 
1 1038 GLN n 
1 1039 GLN n 
1 1040 LEU n 
1 1041 LYS n 
1 1042 GLN n 
1 1043 LEU n 
1 1044 GLU n 
1 1045 SER n 
1 1046 GLU n 
1 1047 GLY n 
1 1048 ARG n 
1 1049 SER n 
1 1050 PRO n 
1 1051 ILE n 
1 1052 PHE n 
1 1053 THR n 
1 1054 HIS n 
1 1055 LEU n 
1 1056 VAL n 
1 1057 THR n 
1 1058 SER n 
1 1059 LEU n 
1 1060 LYS n 
1 1061 GLY n 
1 1062 LEU n 
1 1063 TRP n 
1 1064 THR n 
1 1065 LEU n 
1 1066 ARG n 
1 1067 ALA n 
1 1068 PHE n 
1 1069 GLY n 
1 1070 ARG n 
1 1071 GLN n 
1 1072 PRO n 
1 1073 TYR n 
1 1074 PHE n 
1 1075 GLU n 
1 1076 THR n 
1 1077 LEU n 
1 1078 PHE n 
1 1079 HIS n 
1 1080 LYS n 
1 1081 ALA n 
1 1082 LEU n 
1 1083 ASN n 
1 1084 LEU n 
1 1085 HIS n 
1 1086 THR n 
1 1087 ALA n 
1 1088 ASN n 
1 1089 TRP n 
1 1090 PHE n 
1 1091 LEU n 
1 1092 TYR n 
1 1093 LEU n 
1 1094 SER n 
1 1095 THR n 
1 1096 LEU n 
1 1097 ARG n 
1 1098 TRP n 
1 1099 PHE n 
1 1100 GLN n 
1 1101 MET n 
1 1102 ARG n 
1 1103 ILE n 
1 1104 GLU n 
1 1105 MET n 
1 1106 ILE n 
1 1107 PHE n 
1 1108 VAL n 
1 1109 ILE n 
1 1110 PHE n 
1 1111 PHE n 
1 1112 ILE n 
1 1113 ALA n 
1 1114 VAL n 
1 1115 THR n 
1 1116 PHE n 
1 1117 ILE n 
1 1118 SER n 
1 1119 ILE n 
1 1120 LEU n 
1 1121 THR n 
1 1122 THR n 
1 1123 GLY n 
1 1124 GLU n 
1 1125 GLY n 
1 1126 GLU n 
1 1127 GLY n 
1 1128 ARG n 
1 1129 VAL n 
1 1130 GLY n 
1 1131 ILE n 
1 1132 ILE n 
1 1133 LEU n 
1 1134 THR n 
1 1135 LEU n 
1 1136 ALA n 
1 1137 MET n 
1 1138 ASN n 
1 1139 ILE n 
1 1140 MET n 
1 1141 SER n 
1 1142 THR n 
1 1143 LEU n 
1 1144 GLN n 
1 1145 TRP n 
1 1146 ALA n 
1 1147 VAL n 
1 1148 ASN n 
1 1149 SER n 
1 1150 SER n 
1 1151 ILE n 
1 1152 ASP n 
1 1153 VAL n 
1 1154 ASP n 
1 1155 SER n 
1 1156 LEU n 
1 1157 MET n 
1 1158 ARG n 
1 1159 SER n 
1 1160 VAL n 
1 1161 SER n 
1 1162 ARG n 
1 1163 VAL n 
1 1164 PHE n 
1 1165 LYS n 
1 1166 PHE n 
1 1167 ILE n 
1 1168 ASP n 
1 1169 MET n 
1 1170 PRO n 
1 1171 THR n 
1 1172 GLU n 
1 1173 GLY n 
1 1174 LYS n 
1 1175 PRO n 
1 1176 THR n 
1 1177 LYS n 
1 1178 SER n 
1 1179 THR n 
1 1180 LYS n 
1 1181 PRO n 
1 1182 TYR n 
1 1183 LYS n 
1 1184 ASN n 
1 1185 GLY n 
1 1186 GLN n 
1 1187 LEU n 
1 1188 SER n 
1 1189 LYS n 
1 1190 VAL n 
1 1191 MET n 
1 1192 ILE n 
1 1193 ILE n 
1 1194 GLU n 
1 1195 ASN n 
1 1196 SER n 
1 1197 HIS n 
1 1198 VAL n 
1 1199 LYS n 
1 1200 LYS n 
1 1201 ASP n 
1 1202 ASP n 
1 1203 ILE n 
1 1204 TRP n 
1 1205 PRO n 
1 1206 SER n 
1 1207 GLY n 
1 1208 GLY n 
1 1209 GLN n 
1 1210 MET n 
1 1211 THR n 
1 1212 VAL n 
1 1213 LYS n 
1 1214 ASP n 
1 1215 LEU n 
1 1216 THR n 
1 1217 ALA n 
1 1218 LYS n 
1 1219 TYR n 
1 1220 THR n 
1 1221 GLU n 
1 1222 GLY n 
1 1223 GLY n 
1 1224 ASN n 
1 1225 ALA n 
1 1226 ILE n 
1 1227 LEU n 
1 1228 GLU n 
1 1229 ASN n 
1 1230 ILE n 
1 1231 SER n 
1 1232 PHE n 
1 1233 SER n 
1 1234 ILE n 
1 1235 SER n 
1 1236 PRO n 
1 1237 GLY n 
1 1238 GLN n 
1 1239 ARG n 
1 1240 VAL n 
1 1241 GLY n 
1 1242 LEU n 
1 1243 LEU n 
1 1244 GLY n 
1 1245 ARG n 
1 1246 THR n 
1 1247 GLY n 
1 1248 SER n 
1 1249 GLY n 
1 1250 LYS n 
1 1251 SER n 
1 1252 THR n 
1 1253 LEU n 
1 1254 LEU n 
1 1255 SER n 
1 1256 ALA n 
1 1257 PHE n 
1 1258 LEU n 
1 1259 ARG n 
1 1260 LEU n 
1 1261 LEU n 
1 1262 ASN n 
1 1263 THR n 
1 1264 GLU n 
1 1265 GLY n 
1 1266 GLU n 
1 1267 ILE n 
1 1268 GLN n 
1 1269 ILE n 
1 1270 ASP n 
1 1271 GLY n 
1 1272 VAL n 
1 1273 SER n 
1 1274 TRP n 
1 1275 ASP n 
1 1276 SER n 
1 1277 ILE n 
1 1278 THR n 
1 1279 LEU n 
1 1280 GLN n 
1 1281 GLN n 
1 1282 TRP n 
1 1283 ARG n 
1 1284 LYS n 
1 1285 ALA n 
1 1286 PHE n 
1 1287 GLY n 
1 1288 VAL n 
1 1289 ILE n 
1 1290 PRO n 
1 1291 GLN n 
1 1292 LYS n 
1 1293 VAL n 
1 1294 PHE n 
1 1295 ILE n 
1 1296 PHE n 
1 1297 SER n 
1 1298 GLY n 
1 1299 THR n 
1 1300 PHE n 
1 1301 ARG n 
1 1302 LYS n 
1 1303 ASN n 
1 1304 LEU n 
1 1305 ASP n 
1 1306 PRO n 
1 1307 TYR n 
1 1308 GLU n 
1 1309 GLN n 
1 1310 TRP n 
1 1311 SER n 
1 1312 ASP n 
1 1313 GLN n 
1 1314 GLU n 
1 1315 ILE n 
1 1316 TRP n 
1 1317 LYS n 
1 1318 VAL n 
1 1319 ALA n 
1 1320 ASP n 
1 1321 GLU n 
1 1322 VAL n 
1 1323 GLY n 
1 1324 LEU n 
1 1325 ARG n 
1 1326 SER n 
1 1327 VAL n 
1 1328 ILE n 
1 1329 GLU n 
1 1330 GLN n 
1 1331 PHE n 
1 1332 PRO n 
1 1333 GLY n 
1 1334 LYS n 
1 1335 LEU n 
1 1336 ASP n 
1 1337 PHE n 
1 1338 VAL n 
1 1339 LEU n 
1 1340 VAL n 
1 1341 ASP n 
1 1342 GLY n 
1 1343 GLY n 
1 1344 CYS n 
1 1345 VAL n 
1 1346 LEU n 
1 1347 SER n 
1 1348 HIS n 
1 1349 GLY n 
1 1350 HIS n 
1 1351 LYS n 
1 1352 GLN n 
1 1353 LEU n 
1 1354 MET n 
1 1355 CYS n 
1 1356 LEU n 
1 1357 ALA n 
1 1358 ARG n 
1 1359 SER n 
1 1360 VAL n 
1 1361 LEU n 
1 1362 SER n 
1 1363 LYS n 
1 1364 ALA n 
1 1365 LYS n 
1 1366 ILE n 
1 1367 LEU n 
1 1368 LEU n 
1 1369 LEU n 
1 1370 ASP n 
1 1371 GLN n 
1 1372 PRO n 
1 1373 SER n 
1 1374 ALA n 
1 1375 HIS n 
1 1376 LEU n 
1 1377 ASP n 
1 1378 PRO n 
1 1379 VAL n 
1 1380 THR n 
1 1381 TYR n 
1 1382 GLN n 
1 1383 ILE n 
1 1384 ILE n 
1 1385 ARG n 
1 1386 ARG n 
1 1387 THR n 
1 1388 LEU n 
1 1389 LYS n 
1 1390 GLN n 
1 1391 ALA n 
1 1392 PHE n 
1 1393 ALA n 
1 1394 ASP n 
1 1395 CYS n 
1 1396 THR n 
1 1397 VAL n 
1 1398 ILE n 
1 1399 LEU n 
1 1400 CYS n 
1 1401 GLU n 
1 1402 HIS n 
1 1403 ARG n 
1 1404 ILE n 
1 1405 GLU n 
1 1406 ALA n 
1 1407 MET n 
1 1408 LEU n 
1 1409 GLU n 
1 1410 CYS n 
1 1411 GLN n 
1 1412 GLN n 
1 1413 PHE n 
1 1414 LEU n 
1 1415 VAL n 
1 1416 ILE n 
1 1417 GLU n 
1 1418 GLU n 
1 1419 ASN n 
1 1420 LYS n 
1 1421 VAL n 
1 1422 ARG n 
1 1423 GLN n 
1 1424 TYR n 
1 1425 ASP n 
1 1426 SER n 
1 1427 ILE n 
1 1428 GLN n 
1 1429 LYS n 
1 1430 LEU n 
1 1431 LEU n 
1 1432 ASN n 
1 1433 GLU n 
1 1434 ARG n 
1 1435 SER n 
1 1436 LEU n 
1 1437 PHE n 
1 1438 ARG n 
1 1439 GLN n 
1 1440 ALA n 
1 1441 ILE n 
1 1442 SER n 
1 1443 PRO n 
1 1444 SER n 
1 1445 ASP n 
1 1446 ARG n 
1 1447 VAL n 
1 1448 LYS n 
1 1449 LEU n 
1 1450 PHE n 
1 1451 PRO n 
1 1452 HIS n 
1 1453 ARG n 
1 1454 ASN n 
1 1455 SER n 
1 1456 SER n 
1 1457 LYS n 
1 1458 CYS n 
1 1459 LYS n 
1 1460 SER n 
1 1461 LYS n 
1 1462 PRO n 
1 1463 GLN n 
1 1464 ILE n 
1 1465 ALA n 
1 1466 ALA n 
1 1467 LEU n 
1 1468 LYS n 
1 1469 GLU n 
1 1470 GLU n 
1 1471 THR n 
1 1472 GLU n 
1 1473 GLU n 
1 1474 GLU n 
1 1475 VAL n 
1 1476 GLN n 
1 1477 ASP n 
1 1478 THR n 
1 1479 ARG n 
1 1480 LEU n 
2 1    MET n 
2 2    GLY n 
2 3    ASN n 
2 4    ALA n 
2 5    ALA n 
2 6    ALA n 
2 7    ALA n 
2 8    LYS n 
2 9    LYS n 
2 10   GLY n 
2 11   SER n 
2 12   GLU n 
2 13   GLN n 
2 14   GLU n 
2 15   SER n 
2 16   VAL n 
2 17   LYS n 
2 18   GLU n 
2 19   PHE n 
2 20   LEU n 
2 21   ALA n 
2 22   LYS n 
2 23   ALA n 
2 24   LYS n 
2 25   GLU n 
2 26   ASP n 
2 27   PHE n 
2 28   LEU n 
2 29   LYS n 
2 30   LYS n 
2 31   TRP n 
2 32   GLU n 
2 33   ASN n 
2 34   PRO n 
2 35   ALA n 
2 36   GLN n 
2 37   ASN n 
2 38   THR n 
2 39   ALA n 
2 40   HIS n 
2 41   LEU n 
2 42   ASP n 
2 43   GLN n 
2 44   PHE n 
2 45   GLU n 
2 46   ARG n 
2 47   ILE n 
2 48   LYS n 
2 49   THR n 
2 50   LEU n 
2 51   GLY n 
2 52   THR n 
2 53   GLY n 
2 54   SER n 
2 55   PHE n 
2 56   GLY n 
2 57   ARG n 
2 58   VAL n 
2 59   MET n 
2 60   LEU n 
2 61   VAL n 
2 62   LYS n 
2 63   HIS n 
2 64   MET n 
2 65   GLU n 
2 66   THR n 
2 67   GLY n 
2 68   ASN n 
2 69   HIS n 
2 70   TYR n 
2 71   ALA n 
2 72   MET n 
2 73   LYS n 
2 74   ILE n 
2 75   LEU n 
2 76   ASP n 
2 77   LYS n 
2 78   GLN n 
2 79   LYS n 
2 80   VAL n 
2 81   VAL n 
2 82   LYS n 
2 83   LEU n 
2 84   LYS n 
2 85   GLN n 
2 86   ILE n 
2 87   GLU n 
2 88   HIS n 
2 89   THR n 
2 90   LEU n 
2 91   ASN n 
2 92   GLU n 
2 93   LYS n 
2 94   ARG n 
2 95   ILE n 
2 96   LEU n 
2 97   GLN n 
2 98   ALA n 
2 99   VAL n 
2 100  ASN n 
2 101  PHE n 
2 102  PRO n 
2 103  PHE n 
2 104  LEU n 
2 105  VAL n 
2 106  LYS n 
2 107  LEU n 
2 108  GLU n 
2 109  PHE n 
2 110  SER n 
2 111  PHE n 
2 112  LYS n 
2 113  ASP n 
2 114  ASN n 
2 115  SER n 
2 116  ASN n 
2 117  LEU n 
2 118  TYR n 
2 119  MET n 
2 120  VAL n 
2 121  MET n 
2 122  GLU n 
2 123  TYR n 
2 124  VAL n 
2 125  PRO n 
2 126  GLY n 
2 127  GLY n 
2 128  GLU n 
2 129  MET n 
2 130  PHE n 
2 131  SER n 
2 132  HIS n 
2 133  LEU n 
2 134  ARG n 
2 135  ARG n 
2 136  ILE n 
2 137  GLY n 
2 138  ARG n 
2 139  PHE n 
2 140  SER n 
2 141  GLU n 
2 142  PRO n 
2 143  HIS n 
2 144  ALA n 
2 145  ARG n 
2 146  PHE n 
2 147  TYR n 
2 148  ALA n 
2 149  ALA n 
2 150  GLN n 
2 151  ILE n 
2 152  VAL n 
2 153  LEU n 
2 154  THR n 
2 155  PHE n 
2 156  GLU n 
2 157  TYR n 
2 158  LEU n 
2 159  HIS n 
2 160  SER n 
2 161  LEU n 
2 162  ASP n 
2 163  LEU n 
2 164  ILE n 
2 165  TYR n 
2 166  ARG n 
2 167  ASP n 
2 168  LEU n 
2 169  LYS n 
2 170  PRO n 
2 171  GLU n 
2 172  ASN n 
2 173  LEU n 
2 174  LEU n 
2 175  ILE n 
2 176  ASP n 
2 177  GLN n 
2 178  GLN n 
2 179  GLY n 
2 180  TYR n 
2 181  ILE n 
2 182  GLN n 
2 183  VAL n 
2 184  THR n 
2 185  ASP n 
2 186  PHE n 
2 187  GLY n 
2 188  PHE n 
2 189  ALA n 
2 190  LYS n 
2 191  ARG n 
2 192  VAL n 
2 193  LYS n 
2 194  GLY n 
2 195  ARG n 
2 196  THR n 
2 197  TRP n 
2 198  TPO n 
2 199  LEU n 
2 200  CYS n 
2 201  GLY n 
2 202  THR n 
2 203  PRO n 
2 204  GLU n 
2 205  TYR n 
2 206  LEU n 
2 207  ALA n 
2 208  PRO n 
2 209  GLU n 
2 210  ILE n 
2 211  ILE n 
2 212  LEU n 
2 213  SER n 
2 214  LYS n 
2 215  GLY n 
2 216  TYR n 
2 217  ASN n 
2 218  LYS n 
2 219  ALA n 
2 220  VAL n 
2 221  ASP n 
2 222  TRP n 
2 223  TRP n 
2 224  ALA n 
2 225  LEU n 
2 226  GLY n 
2 227  VAL n 
2 228  LEU n 
2 229  ILE n 
2 230  TYR n 
2 231  GLU n 
2 232  MET n 
2 233  ALA n 
2 234  ALA n 
2 235  GLY n 
2 236  TYR n 
2 237  PRO n 
2 238  PRO n 
2 239  PHE n 
2 240  PHE n 
2 241  ALA n 
2 242  ASP n 
2 243  GLN n 
2 244  PRO n 
2 245  ILE n 
2 246  GLN n 
2 247  ILE n 
2 248  TYR n 
2 249  GLU n 
2 250  LYS n 
2 251  ILE n 
2 252  VAL n 
2 253  SER n 
2 254  GLY n 
2 255  LYS n 
2 256  VAL n 
2 257  ARG n 
2 258  PHE n 
2 259  PRO n 
2 260  SER n 
2 261  HIS n 
2 262  PHE n 
2 263  SER n 
2 264  SER n 
2 265  ASP n 
2 266  LEU n 
2 267  LYS n 
2 268  ASP n 
2 269  LEU n 
2 270  LEU n 
2 271  ARG n 
2 272  ASN n 
2 273  LEU n 
2 274  LEU n 
2 275  GLN n 
2 276  VAL n 
2 277  ASP n 
2 278  LEU n 
2 279  THR n 
2 280  LYS n 
2 281  ARG n 
2 282  PHE n 
2 283  GLY n 
2 284  ASN n 
2 285  LEU n 
2 286  LYS n 
2 287  ASN n 
2 288  GLY n 
2 289  VAL n 
2 290  ASN n 
2 291  ASP n 
2 292  ILE n 
2 293  LYS n 
2 294  ASN n 
2 295  HIS n 
2 296  LYS n 
2 297  TRP n 
2 298  PHE n 
2 299  ALA n 
2 300  THR n 
2 301  THR n 
2 302  ASP n 
2 303  TRP n 
2 304  ILE n 
2 305  ALA n 
2 306  ILE n 
2 307  TYR n 
2 308  GLN n 
2 309  ARG n 
2 310  LYS n 
2 311  VAL n 
2 312  GLU n 
2 313  ALA n 
2 314  PRO n 
2 315  PHE n 
2 316  ILE n 
2 317  PRO n 
2 318  LYS n 
2 319  PHE n 
2 320  LYS n 
2 321  GLY n 
2 322  PRO n 
2 323  GLY n 
2 324  ASP n 
2 325  THR n 
2 326  SER n 
2 327  ASN n 
2 328  PHE n 
2 329  ASP n 
2 330  ASP n 
2 331  TYR n 
2 332  GLU n 
2 333  GLU n 
2 334  GLU n 
2 335  GLU n 
2 336  ILE n 
2 337  ARG n 
2 338  VAL n 
2 339  SER n 
2 340  ILE n 
2 341  ASN n 
2 342  GLU n 
2 343  LYS n 
2 344  CYS n 
2 345  GLY n 
2 346  LYS n 
2 347  GLU n 
2 348  PHE n 
2 349  SER n 
2 350  GLU n 
2 351  PHE n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_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 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_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 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_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 
1 1 sample 'Biological sequence' 1 1480 human             ? 'CFTR, ABCC7' ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? human 
'Homo sapiens' 9606 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 351  'domestic cattle' ? PRKACA        ? ? ? ? ? ? 'Bos taurus'   9913 ? ? ? ? ? ? ? ?     
'Bos taurus'   9913 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                     ?                  'C3 H7 N O2'        89.093  
ARG 'L-peptide linking' y ARGININE                    ?                  'C6 H15 N4 O2 1'    175.209 
ASN 'L-peptide linking' y ASPARAGINE                  ?                  'C4 H8 N2 O3'       132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'             ?                  'C4 H7 N O4'        133.103 
ATP non-polymer         . "ADENOSINE-5'-TRIPHOSPHATE" ?                  'C10 H16 N5 O13 P3' 507.181 
CL  non-polymer         . 'CHLORIDE ION'              ?                  'Cl -1'             35.453  
CLR non-polymer         . CHOLESTEROL                 ?                  'C27 H46 O'         386.654 
CYS 'L-peptide linking' y CYSTEINE                    ?                  'C3 H7 N O2 S'      121.158 
D10 non-polymer         . DECANE                      ?                  'C10 H22'           142.282 
GLN 'L-peptide linking' y GLUTAMINE                   ?                  'C5 H10 N2 O3'      146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'             ?                  'C5 H9 N O4'        147.129 
GLY 'peptide linking'   y GLYCINE                     ?                  'C2 H5 N O2'        75.067  
HIS 'L-peptide linking' y HISTIDINE                   ?                  'C6 H10 N3 O2 1'    156.162 
HOH non-polymer         . WATER                       ?                  'H2 O'              18.015  
ILE 'L-peptide linking' y ISOLEUCINE                  ?                  'C6 H13 N O2'       131.173 
LEU 'L-peptide linking' y LEUCINE                     ?                  'C6 H13 N O2'       131.173 
LYS 'L-peptide linking' y LYSINE                      ?                  'C6 H15 N2 O2 1'    147.195 
MET 'L-peptide linking' y METHIONINE                  ?                  'C5 H11 N O2 S'     149.211 
MG  non-polymer         . 'MAGNESIUM ION'             ?                  'Mg 2'              24.305  
PHE 'L-peptide linking' y PHENYLALANINE               ?                  'C9 H11 N O2'       165.189 
PRO 'L-peptide linking' y PROLINE                     ?                  'C5 H9 N O2'        115.130 
SEP 'L-peptide linking' n PHOSPHOSERINE               PHOSPHONOSERINE    'C3 H8 N O6 P'      185.072 
SER 'L-peptide linking' y SERINE                      ?                  'C3 H7 N O3'        105.093 
THR 'L-peptide linking' y THREONINE                   ?                  'C4 H9 N O3'        119.119 
TPO 'L-peptide linking' n PHOSPHOTHREONINE            PHOSPHONOTHREONINE 'C4 H10 N O6 P'     199.099 
TRP 'L-peptide linking' y TRYPTOPHAN                  ?                  'C11 H12 N2 O2'     204.225 
TYR 'L-peptide linking' y TYROSINE                    ?                  'C9 H11 N O3'       181.189 
UND non-polymer         . UNDECANE                    'LIPID FRAGMENT'   'C11 H24'           156.308 
VAL 'L-peptide linking' y VALINE                      ?                  'C5 H11 N O2'       117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1    MET 1    1    1    MET MET A . n 
A 1 2    GLN 2    2    2    GLN GLN A . n 
A 1 3    ARG 3    3    3    ARG ARG A . n 
A 1 4    SER 4    4    4    SER SER A . n 
A 1 5    PRO 5    5    5    PRO PRO A . n 
A 1 6    LEU 6    6    6    LEU LEU A . n 
A 1 7    GLU 7    7    7    GLU GLU A . n 
A 1 8    LYS 8    8    8    LYS LYS A . n 
A 1 9    ALA 9    9    9    ALA ALA A . n 
A 1 10   SER 10   10   10   SER SER A . n 
A 1 11   VAL 11   11   11   VAL VAL A . n 
A 1 12   VAL 12   12   12   VAL VAL A . n 
A 1 13   SER 13   13   13   SER SER A . n 
A 1 14   LYS 14   14   14   LYS LYS A . n 
A 1 15   LEU 15   15   15   LEU LEU A . n 
A 1 16   PHE 16   16   16   PHE PHE A . n 
A 1 17   PHE 17   17   17   PHE PHE A . n 
A 1 18   SER 18   18   18   SER SER A . n 
A 1 19   TRP 19   19   19   TRP TRP A . n 
A 1 20   THR 20   20   20   THR THR A . n 
A 1 21   ARG 21   21   21   ARG ARG A . n 
A 1 22   PRO 22   22   22   PRO PRO A . n 
A 1 23   ILE 23   23   23   ILE ILE A . n 
A 1 24   LEU 24   24   24   LEU LEU A . n 
A 1 25   ARG 25   25   25   ARG ARG A . n 
A 1 26   LYS 26   26   26   LYS LYS A . n 
A 1 27   GLY 27   27   27   GLY GLY A . n 
A 1 28   TYR 28   28   28   TYR TYR A . n 
A 1 29   ARG 29   29   29   ARG ARG A . n 
A 1 30   GLN 30   30   30   GLN GLN A . n 
A 1 31   ARG 31   31   31   ARG ARG A . n 
A 1 32   LEU 32   32   32   LEU LEU A . n 
A 1 33   GLU 33   33   33   GLU GLU A . n 
A 1 34   LEU 34   34   34   LEU LEU A . n 
A 1 35   SER 35   35   35   SER SER A . n 
A 1 36   ASP 36   36   36   ASP ASP A . n 
A 1 37   ILE 37   37   37   ILE ILE A . n 
A 1 38   TYR 38   38   38   TYR TYR A . n 
A 1 39   GLN 39   39   39   GLN GLN A . n 
A 1 40   ILE 40   40   40   ILE ILE A . n 
A 1 41   PRO 41   41   41   PRO PRO A . n 
A 1 42   SER 42   42   42   SER SER A . n 
A 1 43   VAL 43   43   43   VAL VAL A . n 
A 1 44   ASP 44   44   44   ASP ASP A . n 
A 1 45   SER 45   45   45   SER SER A . n 
A 1 46   ALA 46   46   46   ALA ALA A . n 
A 1 47   ASP 47   47   47   ASP ASP A . n 
A 1 48   ASN 48   48   48   ASN ASN A . n 
A 1 49   LEU 49   49   49   LEU LEU A . n 
A 1 50   SER 50   50   50   SER SER A . n 
A 1 51   GLU 51   51   51   GLU GLU A . n 
A 1 52   LYS 52   52   52   LYS LYS A . n 
A 1 53   LEU 53   53   53   LEU LEU A . n 
A 1 54   GLU 54   54   54   GLU GLU A . n 
A 1 55   ARG 55   55   55   ARG ARG A . n 
A 1 56   GLU 56   56   56   GLU GLU A . n 
A 1 57   TRP 57   57   57   TRP TRP A . n 
A 1 58   ASP 58   58   58   ASP ASP A . n 
A 1 59   ARG 59   59   59   ARG ARG A . n 
A 1 60   GLU 60   60   60   GLU GLU A . n 
A 1 61   LEU 61   61   61   LEU LEU A . n 
A 1 62   ALA 62   62   62   ALA ALA A . n 
A 1 63   SER 63   63   63   SER SER A . n 
A 1 64   LYS 64   64   64   LYS LYS A . n 
A 1 65   LYS 65   65   65   LYS LYS A . n 
A 1 66   ASN 66   66   66   ASN ASN A . n 
A 1 67   PRO 67   67   67   PRO PRO A . n 
A 1 68   LYS 68   68   68   LYS LYS A . n 
A 1 69   LEU 69   69   69   LEU LEU A . n 
A 1 70   ILE 70   70   70   ILE ILE A . n 
A 1 71   ASN 71   71   71   ASN ASN A . n 
A 1 72   ALA 72   72   72   ALA ALA A . n 
A 1 73   LEU 73   73   73   LEU LEU A . n 
A 1 74   ARG 74   74   74   ARG ARG A . n 
A 1 75   ARG 75   75   75   ARG ARG A . n 
A 1 76   CYS 76   76   76   CYS CYS A . n 
A 1 77   PHE 77   77   77   PHE PHE A . n 
A 1 78   PHE 78   78   78   PHE PHE A . n 
A 1 79   TRP 79   79   79   TRP TRP A . n 
A 1 80   ARG 80   80   80   ARG ARG A . n 
A 1 81   PHE 81   81   81   PHE PHE A . n 
A 1 82   MET 82   82   82   MET MET A . n 
A 1 83   PHE 83   83   83   PHE PHE A . n 
A 1 84   TYR 84   84   84   TYR TYR A . n 
A 1 85   GLY 85   85   85   GLY GLY A . n 
A 1 86   ILE 86   86   86   ILE ILE A . n 
A 1 87   PHE 87   87   87   PHE PHE A . n 
A 1 88   LEU 88   88   88   LEU LEU A . n 
A 1 89   TYR 89   89   89   TYR TYR A . n 
A 1 90   LEU 90   90   90   LEU LEU A . n 
A 1 91   GLY 91   91   91   GLY GLY A . n 
A 1 92   GLU 92   92   92   GLU GLU A . n 
A 1 93   VAL 93   93   93   VAL VAL A . n 
A 1 94   THR 94   94   94   THR THR A . n 
A 1 95   LYS 95   95   95   LYS LYS A . n 
A 1 96   ALA 96   96   96   ALA ALA A . n 
A 1 97   VAL 97   97   97   VAL VAL A . n 
A 1 98   GLN 98   98   98   GLN GLN A . n 
A 1 99   PRO 99   99   99   PRO PRO A . n 
A 1 100  LEU 100  100  100  LEU LEU A . n 
A 1 101  LEU 101  101  101  LEU LEU A . n 
A 1 102  LEU 102  102  102  LEU LEU A . n 
A 1 103  GLY 103  103  103  GLY GLY A . n 
A 1 104  ARG 104  104  104  ARG ARG A . n 
A 1 105  ILE 105  105  105  ILE ILE A . n 
A 1 106  ILE 106  106  106  ILE ILE A . n 
A 1 107  ALA 107  107  107  ALA ALA A . n 
A 1 108  SER 108  108  108  SER SER A . n 
A 1 109  TYR 109  109  109  TYR TYR A . n 
A 1 110  ASP 110  110  110  ASP ASP A . n 
A 1 111  PRO 111  111  111  PRO PRO A . n 
A 1 112  ASP 112  112  112  ASP ASP A . n 
A 1 113  ASN 113  113  113  ASN ASN A . n 
A 1 114  LYS 114  114  114  LYS LYS A . n 
A 1 115  GLU 115  115  115  GLU GLU A . n 
A 1 116  GLU 116  116  116  GLU GLU A . n 
A 1 117  ARG 117  117  117  ARG ARG A . n 
A 1 118  SER 118  118  118  SER SER A . n 
A 1 119  ILE 119  119  119  ILE ILE A . n 
A 1 120  ALA 120  120  120  ALA ALA A . n 
A 1 121  ILE 121  121  121  ILE ILE A . n 
A 1 122  TYR 122  122  122  TYR TYR A . n 
A 1 123  LEU 123  123  123  LEU LEU A . n 
A 1 124  GLY 124  124  124  GLY GLY A . n 
A 1 125  ILE 125  125  125  ILE ILE A . n 
A 1 126  GLY 126  126  126  GLY GLY A . n 
A 1 127  LEU 127  127  127  LEU LEU A . n 
A 1 128  CYS 128  128  128  CYS CYS A . n 
A 1 129  LEU 129  129  129  LEU LEU A . n 
A 1 130  LEU 130  130  130  LEU LEU A . n 
A 1 131  PHE 131  131  131  PHE PHE A . n 
A 1 132  ILE 132  132  132  ILE ILE A . n 
A 1 133  VAL 133  133  133  VAL VAL A . n 
A 1 134  ARG 134  134  134  ARG ARG A . n 
A 1 135  THR 135  135  135  THR THR A . n 
A 1 136  LEU 136  136  136  LEU LEU A . n 
A 1 137  LEU 137  137  137  LEU LEU A . n 
A 1 138  LEU 138  138  138  LEU LEU A . n 
A 1 139  HIS 139  139  139  HIS HIS A . n 
A 1 140  PRO 140  140  140  PRO PRO A . n 
A 1 141  ALA 141  141  141  ALA ALA A . n 
A 1 142  ILE 142  142  142  ILE ILE A . n 
A 1 143  PHE 143  143  143  PHE PHE A . n 
A 1 144  GLY 144  144  144  GLY GLY A . n 
A 1 145  LEU 145  145  145  LEU LEU A . n 
A 1 146  HIS 146  146  146  HIS HIS A . n 
A 1 147  HIS 147  147  147  HIS HIS A . n 
A 1 148  ILE 148  148  148  ILE ILE A . n 
A 1 149  GLY 149  149  149  GLY GLY A . n 
A 1 150  MET 150  150  150  MET MET A . n 
A 1 151  GLN 151  151  151  GLN GLN A . n 
A 1 152  MET 152  152  152  MET MET A . n 
A 1 153  ARG 153  153  153  ARG ARG A . n 
A 1 154  ILE 154  154  154  ILE ILE A . n 
A 1 155  ALA 155  155  155  ALA ALA A . n 
A 1 156  MET 156  156  156  MET MET A . n 
A 1 157  PHE 157  157  157  PHE PHE A . n 
A 1 158  SER 158  158  158  SER SER A . n 
A 1 159  LEU 159  159  159  LEU LEU A . n 
A 1 160  ILE 160  160  160  ILE ILE A . n 
A 1 161  TYR 161  161  161  TYR TYR A . n 
A 1 162  LYS 162  162  162  LYS LYS A . n 
A 1 163  LYS 163  163  163  LYS LYS A . n 
A 1 164  THR 164  164  164  THR THR A . n 
A 1 165  LEU 165  165  165  LEU LEU A . n 
A 1 166  LYS 166  166  166  LYS LYS A . n 
A 1 167  LEU 167  167  167  LEU LEU A . n 
A 1 168  SER 168  168  168  SER SER A . n 
A 1 169  SER 169  169  169  SER SER A . n 
A 1 170  ARG 170  170  170  ARG ARG A . n 
A 1 171  VAL 171  171  171  VAL VAL A . n 
A 1 172  LEU 172  172  172  LEU LEU A . n 
A 1 173  ASP 173  173  173  ASP ASP A . n 
A 1 174  LYS 174  174  174  LYS LYS A . n 
A 1 175  ILE 175  175  175  ILE ILE A . n 
A 1 176  SER 176  176  176  SER SER A . n 
A 1 177  ILE 177  177  177  ILE ILE A . n 
A 1 178  GLY 178  178  178  GLY GLY A . n 
A 1 179  GLN 179  179  179  GLN GLN A . n 
A 1 180  LEU 180  180  180  LEU LEU A . n 
A 1 181  VAL 181  181  181  VAL VAL A . n 
A 1 182  SER 182  182  182  SER SER A . n 
A 1 183  LEU 183  183  183  LEU LEU A . n 
A 1 184  LEU 184  184  184  LEU LEU A . n 
A 1 185  SER 185  185  185  SER SER A . n 
A 1 186  ASN 186  186  186  ASN ASN A . n 
A 1 187  ASN 187  187  187  ASN ASN A . n 
A 1 188  LEU 188  188  188  LEU LEU A . n 
A 1 189  ASN 189  189  189  ASN ASN A . n 
A 1 190  LYS 190  190  190  LYS LYS A . n 
A 1 191  PHE 191  191  191  PHE PHE A . n 
A 1 192  ASP 192  192  192  ASP ASP A . n 
A 1 193  GLU 193  193  193  GLU GLU A . n 
A 1 194  GLY 194  194  194  GLY GLY A . n 
A 1 195  LEU 195  195  195  LEU LEU A . n 
A 1 196  ALA 196  196  196  ALA ALA A . n 
A 1 197  LEU 197  197  197  LEU LEU A . n 
A 1 198  ALA 198  198  198  ALA ALA A . n 
A 1 199  HIS 199  199  199  HIS HIS A . n 
A 1 200  PHE 200  200  200  PHE PHE A . n 
A 1 201  VAL 201  201  201  VAL VAL A . n 
A 1 202  TRP 202  202  202  TRP TRP A . n 
A 1 203  ILE 203  203  203  ILE ILE A . n 
A 1 204  ALA 204  204  204  ALA ALA A . n 
A 1 205  PRO 205  205  205  PRO PRO A . n 
A 1 206  LEU 206  206  206  LEU LEU A . n 
A 1 207  GLN 207  207  207  GLN GLN A . n 
A 1 208  VAL 208  208  208  VAL VAL A . n 
A 1 209  ALA 209  209  209  ALA ALA A . n 
A 1 210  LEU 210  210  210  LEU LEU A . n 
A 1 211  LEU 211  211  211  LEU LEU A . n 
A 1 212  MET 212  212  212  MET MET A . n 
A 1 213  GLY 213  213  213  GLY GLY A . n 
A 1 214  LEU 214  214  214  LEU LEU A . n 
A 1 215  ILE 215  215  215  ILE ILE A . n 
A 1 216  TRP 216  216  216  TRP TRP A . n 
A 1 217  GLU 217  217  217  GLU GLU A . n 
A 1 218  LEU 218  218  218  LEU LEU A . n 
A 1 219  LEU 219  219  219  LEU LEU A . n 
A 1 220  GLN 220  220  220  GLN GLN A . n 
A 1 221  ALA 221  221  221  ALA ALA A . n 
A 1 222  SER 222  222  222  SER SER A . n 
A 1 223  ALA 223  223  223  ALA ALA A . n 
A 1 224  PHE 224  224  224  PHE PHE A . n 
A 1 225  CYS 225  225  225  CYS CYS A . n 
A 1 226  GLY 226  226  226  GLY GLY A . n 
A 1 227  LEU 227  227  227  LEU LEU A . n 
A 1 228  GLY 228  228  228  GLY GLY A . n 
A 1 229  PHE 229  229  229  PHE PHE A . n 
A 1 230  LEU 230  230  230  LEU LEU A . n 
A 1 231  ILE 231  231  231  ILE ILE A . n 
A 1 232  VAL 232  232  232  VAL VAL A . n 
A 1 233  LEU 233  233  233  LEU LEU A . n 
A 1 234  ALA 234  234  234  ALA ALA A . n 
A 1 235  LEU 235  235  235  LEU LEU A . n 
A 1 236  PHE 236  236  236  PHE PHE A . n 
A 1 237  GLN 237  237  237  GLN GLN A . n 
A 1 238  ALA 238  238  238  ALA ALA A . n 
A 1 239  GLY 239  239  239  GLY GLY A . n 
A 1 240  LEU 240  240  240  LEU LEU A . n 
A 1 241  GLY 241  241  241  GLY GLY A . n 
A 1 242  ARG 242  242  242  ARG ARG A . n 
A 1 243  MET 243  243  243  MET MET A . n 
A 1 244  MET 244  244  244  MET MET A . n 
A 1 245  MET 245  245  245  MET MET A . n 
A 1 246  LYS 246  246  246  LYS LYS A . n 
A 1 247  TYR 247  247  247  TYR TYR A . n 
A 1 248  ARG 248  248  248  ARG ARG A . n 
A 1 249  ASP 249  249  249  ASP ASP A . n 
A 1 250  GLN 250  250  250  GLN GLN A . n 
A 1 251  ARG 251  251  251  ARG ARG A . n 
A 1 252  ALA 252  252  252  ALA ALA A . n 
A 1 253  GLY 253  253  253  GLY GLY A . n 
A 1 254  LYS 254  254  254  LYS LYS A . n 
A 1 255  ILE 255  255  255  ILE ILE A . n 
A 1 256  SER 256  256  256  SER SER A . n 
A 1 257  GLU 257  257  257  GLU GLU A . n 
A 1 258  ARG 258  258  258  ARG ARG A . n 
A 1 259  LEU 259  259  259  LEU LEU A . n 
A 1 260  VAL 260  260  260  VAL VAL A . n 
A 1 261  ILE 261  261  261  ILE ILE A . n 
A 1 262  THR 262  262  262  THR THR A . n 
A 1 263  SER 263  263  263  SER SER A . n 
A 1 264  GLU 264  264  264  GLU GLU A . n 
A 1 265  MET 265  265  265  MET MET A . n 
A 1 266  ILE 266  266  266  ILE ILE A . n 
A 1 267  GLU 267  267  267  GLU GLU A . n 
A 1 268  ASN 268  268  268  ASN ASN A . n 
A 1 269  ILE 269  269  269  ILE ILE A . n 
A 1 270  GLN 270  270  270  GLN GLN A . n 
A 1 271  SER 271  271  271  SER SER A . n 
A 1 272  VAL 272  272  272  VAL VAL A . n 
A 1 273  LYS 273  273  273  LYS LYS A . n 
A 1 274  ALA 274  274  274  ALA ALA A . n 
A 1 275  TYR 275  275  275  TYR TYR A . n 
A 1 276  CYS 276  276  276  CYS CYS A . n 
A 1 277  TRP 277  277  277  TRP TRP A . n 
A 1 278  GLU 278  278  278  GLU GLU A . n 
A 1 279  GLU 279  279  279  GLU GLU A . n 
A 1 280  ALA 280  280  280  ALA ALA A . n 
A 1 281  MET 281  281  281  MET MET A . n 
A 1 282  GLU 282  282  282  GLU GLU A . n 
A 1 283  LYS 283  283  283  LYS LYS A . n 
A 1 284  MET 284  284  284  MET MET A . n 
A 1 285  ILE 285  285  285  ILE ILE A . n 
A 1 286  GLU 286  286  286  GLU GLU A . n 
A 1 287  ASN 287  287  287  ASN ASN A . n 
A 1 288  LEU 288  288  288  LEU LEU A . n 
A 1 289  ARG 289  289  289  ARG ARG A . n 
A 1 290  GLN 290  290  290  GLN GLN A . n 
A 1 291  THR 291  291  291  THR THR A . n 
A 1 292  GLU 292  292  292  GLU GLU A . n 
A 1 293  LEU 293  293  293  LEU LEU A . n 
A 1 294  LYS 294  294  294  LYS LYS A . n 
A 1 295  LEU 295  295  295  LEU LEU A . n 
A 1 296  THR 296  296  296  THR THR A . n 
A 1 297  ARG 297  297  297  ARG ARG A . n 
A 1 298  LYS 298  298  298  LYS LYS A . n 
A 1 299  ALA 299  299  299  ALA ALA A . n 
A 1 300  ALA 300  300  300  ALA ALA A . n 
A 1 301  TYR 301  301  301  TYR TYR A . n 
A 1 302  VAL 302  302  302  VAL VAL A . n 
A 1 303  ARG 303  303  303  ARG ARG A . n 
A 1 304  TYR 304  304  304  TYR TYR A . n 
A 1 305  PHE 305  305  305  PHE PHE A . n 
A 1 306  ASN 306  306  306  ASN ASN A . n 
A 1 307  SER 307  307  307  SER SER A . n 
A 1 308  SER 308  308  308  SER SER A . n 
A 1 309  ALA 309  309  309  ALA ALA A . n 
A 1 310  PHE 310  310  310  PHE PHE A . n 
A 1 311  PHE 311  311  311  PHE PHE A . n 
A 1 312  PHE 312  312  312  PHE PHE A . n 
A 1 313  SER 313  313  313  SER SER A . n 
A 1 314  GLY 314  314  314  GLY GLY A . n 
A 1 315  PHE 315  315  315  PHE PHE A . n 
A 1 316  PHE 316  316  316  PHE PHE A . n 
A 1 317  VAL 317  317  317  VAL VAL A . n 
A 1 318  VAL 318  318  318  VAL VAL A . n 
A 1 319  PHE 319  319  319  PHE PHE A . n 
A 1 320  LEU 320  320  320  LEU LEU A . n 
A 1 321  SER 321  321  321  SER SER A . n 
A 1 322  VAL 322  322  322  VAL VAL A . n 
A 1 323  LEU 323  323  323  LEU LEU A . n 
A 1 324  PRO 324  324  324  PRO PRO A . n 
A 1 325  TYR 325  325  325  TYR TYR A . n 
A 1 326  ALA 326  326  326  ALA ALA A . n 
A 1 327  LEU 327  327  327  LEU LEU A . n 
A 1 328  ILE 328  328  328  ILE ILE A . n 
A 1 329  LYS 329  329  329  LYS LYS A . n 
A 1 330  GLY 330  330  330  GLY GLY A . n 
A 1 331  ILE 331  331  331  ILE ILE A . n 
A 1 332  ILE 332  332  332  ILE ILE A . n 
A 1 333  LEU 333  333  333  LEU LEU A . n 
A 1 334  ARG 334  334  334  ARG ARG A . n 
A 1 335  LYS 335  335  335  LYS LYS A . n 
A 1 336  ILE 336  336  336  ILE ILE A . n 
A 1 337  PHE 337  337  337  PHE PHE A . n 
A 1 338  THR 338  338  338  THR THR A . n 
A 1 339  THR 339  339  339  THR THR A . n 
A 1 340  ILE 340  340  340  ILE ILE A . n 
A 1 341  SER 341  341  341  SER SER A . n 
A 1 342  PHE 342  342  342  PHE PHE A . n 
A 1 343  CYS 343  343  343  CYS CYS A . n 
A 1 344  ILE 344  344  344  ILE ILE A . n 
A 1 345  VAL 345  345  345  VAL VAL A . n 
A 1 346  LEU 346  346  346  LEU LEU A . n 
A 1 347  ARG 347  347  347  ARG ARG A . n 
A 1 348  MET 348  348  348  MET MET A . n 
A 1 349  ALA 349  349  349  ALA ALA A . n 
A 1 350  VAL 350  350  350  VAL VAL A . n 
A 1 351  THR 351  351  351  THR THR A . n 
A 1 352  ARG 352  352  352  ARG ARG A . n 
A 1 353  GLN 353  353  353  GLN GLN A . n 
A 1 354  PHE 354  354  354  PHE PHE A . n 
A 1 355  PRO 355  355  355  PRO PRO A . n 
A 1 356  TRP 356  356  356  TRP TRP A . n 
A 1 357  ALA 357  357  357  ALA ALA A . n 
A 1 358  VAL 358  358  358  VAL VAL A . n 
A 1 359  GLN 359  359  359  GLN GLN A . n 
A 1 360  THR 360  360  360  THR THR A . n 
A 1 361  TRP 361  361  361  TRP TRP A . n 
A 1 362  TYR 362  362  362  TYR TYR A . n 
A 1 363  ASP 363  363  363  ASP ASP A . n 
A 1 364  SER 364  364  364  SER SER A . n 
A 1 365  LEU 365  365  365  LEU LEU A . n 
A 1 366  GLY 366  366  366  GLY GLY A . n 
A 1 367  ALA 367  367  367  ALA ALA A . n 
A 1 368  ILE 368  368  368  ILE ILE A . n 
A 1 369  ASN 369  369  369  ASN ASN A . n 
A 1 370  LYS 370  370  370  LYS LYS A . n 
A 1 371  ILE 371  371  371  ILE ILE A . n 
A 1 372  GLN 372  372  372  GLN GLN A . n 
A 1 373  ASP 373  373  373  ASP ASP A . n 
A 1 374  PHE 374  374  374  PHE PHE A . n 
A 1 375  LEU 375  375  375  LEU LEU A . n 
A 1 376  GLN 376  376  376  GLN GLN A . n 
A 1 377  LYS 377  377  377  LYS LYS A . n 
A 1 378  GLN 378  378  378  GLN GLN A . n 
A 1 379  GLU 379  379  379  GLU GLU A . n 
A 1 380  TYR 380  380  380  TYR TYR A . n 
A 1 381  LYS 381  381  381  LYS LYS A . n 
A 1 382  THR 382  382  382  THR THR A . n 
A 1 383  LEU 383  383  383  LEU LEU A . n 
A 1 384  GLU 384  384  384  GLU GLU A . n 
A 1 385  TYR 385  385  385  TYR TYR A . n 
A 1 386  ASN 386  386  386  ASN ASN A . n 
A 1 387  LEU 387  387  387  LEU LEU A . n 
A 1 388  THR 388  388  388  THR THR A . n 
A 1 389  THR 389  389  389  THR THR A . n 
A 1 390  THR 390  390  390  THR THR A . n 
A 1 391  GLU 391  391  391  GLU GLU A . n 
A 1 392  VAL 392  392  392  VAL VAL A . n 
A 1 393  VAL 393  393  393  VAL VAL A . n 
A 1 394  MET 394  394  394  MET MET A . n 
A 1 395  GLU 395  395  395  GLU GLU A . n 
A 1 396  ASN 396  396  396  ASN ASN A . n 
A 1 397  VAL 397  397  397  VAL VAL A . n 
A 1 398  THR 398  398  398  THR THR A . n 
A 1 399  ALA 399  399  399  ALA ALA A . n 
A 1 400  PHE 400  400  400  PHE PHE A . n 
A 1 401  TRP 401  401  401  TRP TRP A . n 
A 1 402  GLU 402  402  402  GLU GLU A . n 
A 1 403  GLU 403  403  ?    ?   ?   A . n 
A 1 404  GLY 404  404  ?    ?   ?   A . n 
A 1 405  PHE 405  405  ?    ?   ?   A . n 
A 1 406  GLY 406  406  ?    ?   ?   A . n 
A 1 407  GLU 407  407  ?    ?   ?   A . n 
A 1 408  LEU 408  408  ?    ?   ?   A . n 
A 1 409  PHE 409  409  ?    ?   ?   A . n 
A 1 410  GLU 410  410  ?    ?   ?   A . n 
A 1 411  LYS 411  411  ?    ?   ?   A . n 
A 1 412  ALA 412  412  ?    ?   ?   A . n 
A 1 413  LYS 413  413  ?    ?   ?   A . n 
A 1 414  GLN 414  414  ?    ?   ?   A . n 
A 1 415  ASN 415  415  ?    ?   ?   A . n 
A 1 416  ASN 416  416  ?    ?   ?   A . n 
A 1 417  ASN 417  417  ?    ?   ?   A . n 
A 1 418  ASN 418  418  ?    ?   ?   A . n 
A 1 419  ARG 419  419  ?    ?   ?   A . n 
A 1 420  LYS 420  420  ?    ?   ?   A . n 
A 1 421  THR 421  421  ?    ?   ?   A . n 
A 1 422  SER 422  422  ?    ?   ?   A . n 
A 1 423  ASN 423  423  ?    ?   ?   A . n 
A 1 424  GLY 424  424  ?    ?   ?   A . n 
A 1 425  ASP 425  425  ?    ?   ?   A . n 
A 1 426  ASP 426  426  ?    ?   ?   A . n 
A 1 427  SER 427  427  ?    ?   ?   A . n 
A 1 428  LEU 428  428  ?    ?   ?   A . n 
A 1 429  PHE 429  429  ?    ?   ?   A . n 
A 1 430  PHE 430  430  ?    ?   ?   A . n 
A 1 431  SER 431  431  ?    ?   ?   A . n 
A 1 432  ASN 432  432  ?    ?   ?   A . n 
A 1 433  PHE 433  433  ?    ?   ?   A . n 
A 1 434  SER 434  434  ?    ?   ?   A . n 
A 1 435  LEU 435  435  ?    ?   ?   A . n 
A 1 436  LEU 436  436  ?    ?   ?   A . n 
A 1 437  GLY 437  437  437  GLY GLY A . n 
A 1 438  THR 438  438  438  THR THR A . n 
A 1 439  PRO 439  439  439  PRO PRO A . n 
A 1 440  VAL 440  440  440  VAL VAL A . n 
A 1 441  LEU 441  441  441  LEU LEU A . n 
A 1 442  LYS 442  442  442  LYS LYS A . n 
A 1 443  ASP 443  443  443  ASP ASP A . n 
A 1 444  ILE 444  444  444  ILE ILE A . n 
A 1 445  ASN 445  445  445  ASN ASN A . n 
A 1 446  PHE 446  446  446  PHE PHE A . n 
A 1 447  LYS 447  447  447  LYS LYS A . n 
A 1 448  ILE 448  448  448  ILE ILE A . n 
A 1 449  GLU 449  449  449  GLU GLU A . n 
A 1 450  ARG 450  450  450  ARG ARG A . n 
A 1 451  GLY 451  451  451  GLY GLY A . n 
A 1 452  GLN 452  452  452  GLN GLN A . n 
A 1 453  LEU 453  453  453  LEU LEU A . n 
A 1 454  LEU 454  454  454  LEU LEU A . n 
A 1 455  ALA 455  455  455  ALA ALA A . n 
A 1 456  VAL 456  456  456  VAL VAL A . n 
A 1 457  ALA 457  457  457  ALA ALA A . n 
A 1 458  GLY 458  458  458  GLY GLY A . n 
A 1 459  SER 459  459  459  SER SER A . n 
A 1 460  THR 460  460  460  THR THR A . n 
A 1 461  GLY 461  461  461  GLY GLY A . n 
A 1 462  ALA 462  462  462  ALA ALA A . n 
A 1 463  GLY 463  463  463  GLY GLY A . n 
A 1 464  LYS 464  464  464  LYS LYS A . n 
A 1 465  THR 465  465  465  THR THR A . n 
A 1 466  SER 466  466  466  SER SER A . n 
A 1 467  LEU 467  467  467  LEU LEU A . n 
A 1 468  LEU 468  468  468  LEU LEU A . n 
A 1 469  MET 469  469  469  MET MET A . n 
A 1 470  VAL 470  470  470  VAL VAL A . n 
A 1 471  ILE 471  471  471  ILE ILE A . n 
A 1 472  MET 472  472  472  MET MET A . n 
A 1 473  GLY 473  473  473  GLY GLY A . n 
A 1 474  GLU 474  474  474  GLU GLU A . n 
A 1 475  LEU 475  475  475  LEU LEU A . n 
A 1 476  GLU 476  476  476  GLU GLU A . n 
A 1 477  PRO 477  477  477  PRO PRO A . n 
A 1 478  SER 478  478  478  SER SER A . n 
A 1 479  GLU 479  479  479  GLU GLU A . n 
A 1 480  GLY 480  480  480  GLY GLY A . n 
A 1 481  LYS 481  481  481  LYS LYS A . n 
A 1 482  ILE 482  482  482  ILE ILE A . n 
A 1 483  LYS 483  483  483  LYS LYS A . n 
A 1 484  HIS 484  484  484  HIS HIS A . n 
A 1 485  SER 485  485  485  SER SER A . n 
A 1 486  GLY 486  486  486  GLY GLY A . n 
A 1 487  ARG 487  487  487  ARG ARG A . n 
A 1 488  ILE 488  488  488  ILE ILE A . n 
A 1 489  SER 489  489  489  SER SER A . n 
A 1 490  PHE 490  490  490  PHE PHE A . n 
A 1 491  CYS 491  491  491  CYS CYS A . n 
A 1 492  SER 492  492  492  SER SER A . n 
A 1 493  GLN 493  493  493  GLN GLN A . n 
A 1 494  PHE 494  494  494  PHE PHE A . n 
A 1 495  SER 495  495  495  SER SER A . n 
A 1 496  TRP 496  496  496  TRP TRP A . n 
A 1 497  ILE 497  497  497  ILE ILE A . n 
A 1 498  MET 498  498  498  MET MET A . n 
A 1 499  PRO 499  499  499  PRO PRO A . n 
A 1 500  GLY 500  500  500  GLY GLY A . n 
A 1 501  THR 501  501  501  THR THR A . n 
A 1 502  ILE 502  502  502  ILE ILE A . n 
A 1 503  LYS 503  503  503  LYS LYS A . n 
A 1 504  GLU 504  504  504  GLU GLU A . n 
A 1 505  ASN 505  505  505  ASN ASN A . n 
A 1 506  ILE 506  506  506  ILE ILE A . n 
A 1 507  ILE 507  507  507  ILE ILE A . n 
A 1 508  PHE 508  508  508  PHE PHE A . n 
A 1 509  GLY 509  509  509  GLY GLY A . n 
A 1 510  VAL 510  510  510  VAL VAL A . n 
A 1 511  SER 511  511  511  SER SER A . n 
A 1 512  TYR 512  512  512  TYR TYR A . n 
A 1 513  ASP 513  513  513  ASP ASP A . n 
A 1 514  GLU 514  514  514  GLU GLU A . n 
A 1 515  TYR 515  515  515  TYR TYR A . n 
A 1 516  ARG 516  516  516  ARG ARG A . n 
A 1 517  TYR 517  517  517  TYR TYR A . n 
A 1 518  ARG 518  518  518  ARG ARG A . n 
A 1 519  SER 519  519  519  SER SER A . n 
A 1 520  VAL 520  520  520  VAL VAL A . n 
A 1 521  ILE 521  521  521  ILE ILE A . n 
A 1 522  LYS 522  522  522  LYS LYS A . n 
A 1 523  ALA 523  523  523  ALA ALA A . n 
A 1 524  CYS 524  524  524  CYS CYS A . n 
A 1 525  GLN 525  525  525  GLN GLN A . n 
A 1 526  LEU 526  526  526  LEU LEU 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  ASP 529  529  529  ASP ASP A . n 
A 1 530  ILE 530  530  530  ILE ILE A . n 
A 1 531  SER 531  531  531  SER SER A . n 
A 1 532  LYS 532  532  532  LYS LYS A . n 
A 1 533  PHE 533  533  533  PHE PHE A . n 
A 1 534  ALA 534  534  534  ALA ALA A . n 
A 1 535  GLU 535  535  535  GLU GLU A . n 
A 1 536  LYS 536  536  536  LYS LYS A . n 
A 1 537  ASP 537  537  537  ASP ASP A . n 
A 1 538  ASN 538  538  538  ASN ASN A . n 
A 1 539  ILE 539  539  539  ILE ILE A . n 
A 1 540  VAL 540  540  540  VAL VAL A . n 
A 1 541  LEU 541  541  541  LEU LEU A . n 
A 1 542  GLY 542  542  542  GLY GLY A . n 
A 1 543  GLU 543  543  543  GLU GLU A . n 
A 1 544  GLY 544  544  544  GLY GLY A . n 
A 1 545  GLY 545  545  545  GLY GLY A . n 
A 1 546  ILE 546  546  546  ILE ILE A . n 
A 1 547  THR 547  547  547  THR THR A . n 
A 1 548  LEU 548  548  548  LEU LEU A . n 
A 1 549  SER 549  549  549  SER SER A . n 
A 1 550  GLY 550  550  550  GLY GLY A . n 
A 1 551  GLY 551  551  551  GLY GLY A . n 
A 1 552  GLN 552  552  552  GLN GLN A . n 
A 1 553  ARG 553  553  553  ARG ARG A . n 
A 1 554  ALA 554  554  554  ALA ALA A . n 
A 1 555  ARG 555  555  555  ARG ARG A . n 
A 1 556  ILE 556  556  556  ILE ILE A . n 
A 1 557  SER 557  557  557  SER SER A . n 
A 1 558  LEU 558  558  558  LEU LEU A . n 
A 1 559  ALA 559  559  559  ALA ALA A . n 
A 1 560  ARG 560  560  560  ARG ARG A . n 
A 1 561  ALA 561  561  561  ALA ALA A . n 
A 1 562  VAL 562  562  562  VAL VAL A . n 
A 1 563  TYR 563  563  563  TYR TYR A . n 
A 1 564  LYS 564  564  564  LYS LYS A . n 
A 1 565  ASP 565  565  565  ASP ASP A . n 
A 1 566  ALA 566  566  566  ALA ALA A . n 
A 1 567  ASP 567  567  567  ASP ASP A . n 
A 1 568  LEU 568  568  568  LEU LEU A . n 
A 1 569  TYR 569  569  569  TYR TYR A . n 
A 1 570  LEU 570  570  570  LEU LEU A . n 
A 1 571  LEU 571  571  571  LEU LEU A . n 
A 1 572  ASP 572  572  572  ASP ASP A . n 
A 1 573  SER 573  573  573  SER SER A . n 
A 1 574  PRO 574  574  574  PRO PRO A . n 
A 1 575  PHE 575  575  575  PHE PHE A . n 
A 1 576  GLY 576  576  576  GLY GLY A . n 
A 1 577  TYR 577  577  577  TYR TYR A . n 
A 1 578  LEU 578  578  578  LEU LEU A . n 
A 1 579  ASP 579  579  579  ASP ASP A . n 
A 1 580  VAL 580  580  580  VAL VAL A . n 
A 1 581  LEU 581  581  581  LEU LEU A . n 
A 1 582  THR 582  582  582  THR THR A . n 
A 1 583  GLU 583  583  583  GLU GLU A . n 
A 1 584  LYS 584  584  584  LYS LYS A . n 
A 1 585  GLU 585  585  585  GLU GLU A . n 
A 1 586  ILE 586  586  586  ILE ILE A . n 
A 1 587  PHE 587  587  587  PHE PHE A . n 
A 1 588  GLU 588  588  588  GLU GLU A . n 
A 1 589  SER 589  589  589  SER SER A . n 
A 1 590  CYS 590  590  590  CYS CYS A . n 
A 1 591  VAL 591  591  591  VAL VAL A . n 
A 1 592  CYS 592  592  592  CYS CYS A . n 
A 1 593  LYS 593  593  593  LYS LYS A . n 
A 1 594  LEU 594  594  594  LEU LEU A . n 
A 1 595  MET 595  595  595  MET MET A . n 
A 1 596  ALA 596  596  596  ALA ALA A . n 
A 1 597  ASN 597  597  597  ASN ASN A . n 
A 1 598  LYS 598  598  598  LYS LYS A . n 
A 1 599  THR 599  599  599  THR THR A . n 
A 1 600  ARG 600  600  600  ARG ARG A . n 
A 1 601  ILE 601  601  601  ILE ILE A . n 
A 1 602  LEU 602  602  602  LEU LEU A . n 
A 1 603  VAL 603  603  603  VAL VAL A . n 
A 1 604  THR 604  604  604  THR THR A . n 
A 1 605  SER 605  605  605  SER SER A . n 
A 1 606  LYS 606  606  606  LYS LYS A . n 
A 1 607  MET 607  607  607  MET MET A . n 
A 1 608  GLU 608  608  608  GLU GLU A . n 
A 1 609  HIS 609  609  609  HIS HIS A . n 
A 1 610  LEU 610  610  610  LEU LEU A . n 
A 1 611  LYS 611  611  611  LYS LYS A . n 
A 1 612  LYS 612  612  612  LYS LYS A . n 
A 1 613  ALA 613  613  613  ALA ALA A . n 
A 1 614  ASP 614  614  614  ASP ASP A . n 
A 1 615  LYS 615  615  615  LYS LYS A . n 
A 1 616  ILE 616  616  616  ILE ILE A . n 
A 1 617  LEU 617  617  617  LEU LEU A . n 
A 1 618  ILE 618  618  618  ILE ILE A . n 
A 1 619  LEU 619  619  619  LEU LEU A . n 
A 1 620  HIS 620  620  620  HIS HIS A . n 
A 1 621  GLU 621  621  621  GLU GLU A . n 
A 1 622  GLY 622  622  622  GLY GLY A . n 
A 1 623  SER 623  623  623  SER SER A . n 
A 1 624  SER 624  624  624  SER SER A . n 
A 1 625  TYR 625  625  625  TYR TYR A . n 
A 1 626  PHE 626  626  626  PHE PHE A . n 
A 1 627  TYR 627  627  627  TYR TYR A . n 
A 1 628  GLY 628  628  628  GLY GLY A . n 
A 1 629  THR 629  629  629  THR THR A . n 
A 1 630  PHE 630  630  630  PHE PHE A . n 
A 1 631  SER 631  631  631  SER SER A . n 
A 1 632  GLU 632  632  632  GLU GLU A . n 
A 1 633  LEU 633  633  633  LEU LEU A . n 
A 1 634  GLN 634  634  634  GLN GLN A . n 
A 1 635  ASN 635  635  635  ASN ASN A . n 
A 1 636  LEU 636  636  ?    ?   ?   A . n 
A 1 637  GLN 637  637  ?    ?   ?   A . n 
A 1 638  PRO 638  638  ?    ?   ?   A . n 
A 1 639  ASP 639  639  ?    ?   ?   A . n 
A 1 640  PHE 640  640  ?    ?   ?   A . n 
A 1 641  SER 641  641  ?    ?   ?   A . n 
A 1 642  SER 642  642  ?    ?   ?   A . n 
A 1 643  LYS 643  643  ?    ?   ?   A . n 
A 1 644  LEU 644  644  ?    ?   ?   A . n 
A 1 645  MET 645  645  ?    ?   ?   A . n 
A 1 646  GLY 646  646  ?    ?   ?   A . n 
A 1 647  CYS 647  647  ?    ?   ?   A . n 
A 1 648  ASP 648  648  ?    ?   ?   A . n 
A 1 649  SER 649  649  ?    ?   ?   A . n 
A 1 650  PHE 650  650  ?    ?   ?   A . n 
A 1 651  ASP 651  651  ?    ?   ?   A . n 
A 1 652  GLN 652  652  ?    ?   ?   A . n 
A 1 653  PHE 653  653  ?    ?   ?   A . n 
A 1 654  SER 654  654  ?    ?   ?   A . n 
A 1 655  ALA 655  655  ?    ?   ?   A . n 
A 1 656  GLU 656  656  ?    ?   ?   A . n 
A 1 657  ARG 657  657  ?    ?   ?   A . n 
A 1 658  ARG 658  658  ?    ?   ?   A . n 
A 1 659  ASN 659  659  ?    ?   ?   A . n 
A 1 660  SER 660  660  ?    ?   ?   A . n 
A 1 661  ILE 661  661  ?    ?   ?   A . n 
A 1 662  LEU 662  662  ?    ?   ?   A . n 
A 1 663  THR 663  663  ?    ?   ?   A . n 
A 1 664  GLU 664  664  ?    ?   ?   A . n 
A 1 665  THR 665  665  ?    ?   ?   A . n 
A 1 666  LEU 666  666  ?    ?   ?   A . n 
A 1 667  HIS 667  667  ?    ?   ?   A . n 
A 1 668  ARG 668  668  ?    ?   ?   A . n 
A 1 669  PHE 669  669  ?    ?   ?   A . n 
A 1 670  SER 670  670  ?    ?   ?   A . n 
A 1 671  LEU 671  671  ?    ?   ?   A . n 
A 1 672  GLU 672  672  ?    ?   ?   A . n 
A 1 673  GLY 673  673  ?    ?   ?   A . n 
A 1 674  ASP 674  674  ?    ?   ?   A . n 
A 1 675  ALA 675  675  ?    ?   ?   A . n 
A 1 676  PRO 676  676  ?    ?   ?   A . n 
A 1 677  VAL 677  677  ?    ?   ?   A . n 
A 1 678  SER 678  678  ?    ?   ?   A . n 
A 1 679  TRP 679  679  ?    ?   ?   A . n 
A 1 680  THR 680  680  ?    ?   ?   A . n 
A 1 681  GLU 681  681  ?    ?   ?   A . n 
A 1 682  THR 682  682  ?    ?   ?   A . n 
A 1 683  LYS 683  683  ?    ?   ?   A . n 
A 1 684  LYS 684  684  ?    ?   ?   A . n 
A 1 685  GLN 685  685  ?    ?   ?   A . n 
A 1 686  SER 686  686  ?    ?   ?   A . n 
A 1 687  PHE 687  687  ?    ?   ?   A . n 
A 1 688  LYS 688  688  ?    ?   ?   A . n 
A 1 689  GLN 689  689  ?    ?   ?   A . n 
A 1 690  THR 690  690  ?    ?   ?   A . n 
A 1 691  GLY 691  691  ?    ?   ?   A . n 
A 1 692  GLU 692  692  ?    ?   ?   A . n 
A 1 693  PHE 693  693  ?    ?   ?   A . n 
A 1 694  GLY 694  694  ?    ?   ?   A . n 
A 1 695  GLU 695  695  ?    ?   ?   A . n 
A 1 696  LYS 696  696  ?    ?   ?   A . n 
A 1 697  ARG 697  697  ?    ?   ?   A . n 
A 1 698  LYS 698  698  ?    ?   ?   A . n 
A 1 699  ASN 699  699  ?    ?   ?   A . n 
A 1 700  SER 700  700  ?    ?   ?   A . n 
A 1 701  ILE 701  701  ?    ?   ?   A . n 
A 1 702  LEU 702  702  ?    ?   ?   A . n 
A 1 703  ASN 703  703  ?    ?   ?   A . n 
A 1 704  PRO 704  704  ?    ?   ?   A . n 
A 1 705  ILE 705  705  ?    ?   ?   A . n 
A 1 706  ASN 706  706  ?    ?   ?   A . n 
A 1 707  SER 707  707  ?    ?   ?   A . n 
A 1 708  ILE 708  708  ?    ?   ?   A . n 
A 1 709  ARG 709  709  ?    ?   ?   A . n 
A 1 710  LYS 710  710  ?    ?   ?   A . n 
A 1 711  PHE 711  711  ?    ?   ?   A . n 
A 1 712  SER 712  712  ?    ?   ?   A . n 
A 1 713  ILE 713  713  ?    ?   ?   A . n 
A 1 714  VAL 714  714  ?    ?   ?   A . n 
A 1 715  GLN 715  715  ?    ?   ?   A . n 
A 1 716  LYS 716  716  ?    ?   ?   A . n 
A 1 717  THR 717  717  ?    ?   ?   A . n 
A 1 718  PRO 718  718  ?    ?   ?   A . n 
A 1 719  LEU 719  719  ?    ?   ?   A . n 
A 1 720  GLN 720  720  ?    ?   ?   A . n 
A 1 721  MET 721  721  ?    ?   ?   A . n 
A 1 722  ASN 722  722  ?    ?   ?   A . n 
A 1 723  GLY 723  723  ?    ?   ?   A . n 
A 1 724  ILE 724  724  ?    ?   ?   A . n 
A 1 725  GLU 725  725  ?    ?   ?   A . n 
A 1 726  GLU 726  726  ?    ?   ?   A . n 
A 1 727  ASP 727  727  ?    ?   ?   A . n 
A 1 728  SER 728  728  ?    ?   ?   A . n 
A 1 729  ASP 729  729  ?    ?   ?   A . n 
A 1 730  GLU 730  730  ?    ?   ?   A . n 
A 1 731  PRO 731  731  ?    ?   ?   A . n 
A 1 732  LEU 732  732  ?    ?   ?   A . n 
A 1 733  GLU 733  733  ?    ?   ?   A . n 
A 1 734  ARG 734  734  ?    ?   ?   A . n 
A 1 735  ARG 735  735  ?    ?   ?   A . n 
A 1 736  LEU 736  736  ?    ?   ?   A . n 
A 1 737  SER 737  737  ?    ?   ?   A . n 
A 1 738  LEU 738  738  ?    ?   ?   A . n 
A 1 739  VAL 739  739  ?    ?   ?   A . n 
A 1 740  PRO 740  740  ?    ?   ?   A . n 
A 1 741  ASP 741  741  ?    ?   ?   A . n 
A 1 742  SER 742  742  ?    ?   ?   A . n 
A 1 743  GLU 743  743  ?    ?   ?   A . n 
A 1 744  GLN 744  744  ?    ?   ?   A . n 
A 1 745  GLY 745  745  ?    ?   ?   A . n 
A 1 746  GLU 746  746  ?    ?   ?   A . n 
A 1 747  ALA 747  747  ?    ?   ?   A . n 
A 1 748  ILE 748  748  ?    ?   ?   A . n 
A 1 749  LEU 749  749  ?    ?   ?   A . n 
A 1 750  PRO 750  750  ?    ?   ?   A . n 
A 1 751  ARG 751  751  ?    ?   ?   A . n 
A 1 752  ILE 752  752  ?    ?   ?   A . n 
A 1 753  SER 753  753  ?    ?   ?   A . n 
A 1 754  VAL 754  754  ?    ?   ?   A . n 
A 1 755  ILE 755  755  ?    ?   ?   A . n 
A 1 756  SER 756  756  ?    ?   ?   A . n 
A 1 757  THR 757  757  ?    ?   ?   A . n 
A 1 758  GLY 758  758  ?    ?   ?   A . n 
A 1 759  PRO 759  759  ?    ?   ?   A . n 
A 1 760  THR 760  760  ?    ?   ?   A . n 
A 1 761  LEU 761  761  ?    ?   ?   A . n 
A 1 762  GLN 762  762  ?    ?   ?   A . n 
A 1 763  ALA 763  763  ?    ?   ?   A . n 
A 1 764  ARG 764  764  ?    ?   ?   A . n 
A 1 765  ARG 765  765  ?    ?   ?   A . n 
A 1 766  ARG 766  766  ?    ?   ?   A . n 
A 1 767  GLN 767  767  ?    ?   ?   A . n 
A 1 768  SER 768  768  ?    ?   ?   A . n 
A 1 769  VAL 769  769  ?    ?   ?   A . n 
A 1 770  LEU 770  770  ?    ?   ?   A . n 
A 1 771  ASN 771  771  ?    ?   ?   A . n 
A 1 772  LEU 772  772  ?    ?   ?   A . n 
A 1 773  MET 773  773  ?    ?   ?   A . n 
A 1 774  THR 774  774  ?    ?   ?   A . n 
A 1 775  HIS 775  775  ?    ?   ?   A . n 
A 1 776  SER 776  776  ?    ?   ?   A . n 
A 1 777  VAL 777  777  ?    ?   ?   A . n 
A 1 778  ASN 778  778  ?    ?   ?   A . n 
A 1 779  GLN 779  779  ?    ?   ?   A . n 
A 1 780  GLY 780  780  ?    ?   ?   A . n 
A 1 781  GLN 781  781  ?    ?   ?   A . n 
A 1 782  ASN 782  782  ?    ?   ?   A . n 
A 1 783  ILE 783  783  ?    ?   ?   A . n 
A 1 784  HIS 784  784  ?    ?   ?   A . n 
A 1 785  ARG 785  785  ?    ?   ?   A . n 
A 1 786  LYS 786  786  ?    ?   ?   A . n 
A 1 787  THR 787  787  ?    ?   ?   A . n 
A 1 788  THR 788  788  ?    ?   ?   A . n 
A 1 789  ALA 789  789  ?    ?   ?   A . n 
A 1 790  SER 790  790  ?    ?   ?   A . n 
A 1 791  THR 791  791  ?    ?   ?   A . n 
A 1 792  ARG 792  792  ?    ?   ?   A . n 
A 1 793  LYS 793  793  ?    ?   ?   A . n 
A 1 794  VAL 794  794  ?    ?   ?   A . n 
A 1 795  SER 795  795  ?    ?   ?   A . n 
A 1 796  LEU 796  796  ?    ?   ?   A . n 
A 1 797  ALA 797  797  ?    ?   ?   A . n 
A 1 798  PRO 798  798  ?    ?   ?   A . n 
A 1 799  GLN 799  799  ?    ?   ?   A . n 
A 1 800  ALA 800  800  ?    ?   ?   A . n 
A 1 801  ASN 801  801  ?    ?   ?   A . n 
A 1 802  LEU 802  802  ?    ?   ?   A . n 
A 1 803  THR 803  803  ?    ?   ?   A . n 
A 1 804  GLU 804  804  ?    ?   ?   A . n 
A 1 805  LEU 805  805  ?    ?   ?   A . n 
A 1 806  ASP 806  806  806  ASP ASP A . n 
A 1 807  ILE 807  807  807  ILE ILE A . n 
A 1 808  TYR 808  808  808  TYR TYR A . n 
A 1 809  SER 809  809  809  SER SER A . n 
A 1 810  ARG 810  810  810  ARG ARG A . n 
A 1 811  ARG 811  811  811  ARG ARG A . n 
A 1 812  LEU 812  812  812  LEU LEU A . n 
A 1 813  SEP 813  813  813  SEP SEP A . n 
A 1 814  GLN 814  814  814  GLN GLN A . n 
A 1 815  GLU 815  815  ?    ?   ?   A . n 
A 1 816  THR 816  816  ?    ?   ?   A . n 
A 1 817  GLY 817  817  ?    ?   ?   A . n 
A 1 818  LEU 818  818  ?    ?   ?   A . n 
A 1 819  GLU 819  819  ?    ?   ?   A . n 
A 1 820  ILE 820  820  820  ILE ILE A . n 
A 1 821  SER 821  821  821  SER SER A . n 
A 1 822  GLU 822  822  822  GLU GLU A . n 
A 1 823  GLU 823  823  823  GLU GLU A . n 
A 1 824  ILE 824  824  824  ILE ILE A . n 
A 1 825  ASN 825  825  825  ASN ASN A . n 
A 1 826  GLU 826  826  826  GLU GLU A . n 
A 1 827  GLU 827  827  827  GLU GLU A . n 
A 1 828  ASP 828  828  828  ASP ASP A . n 
A 1 829  LEU 829  829  829  LEU LEU A . n 
A 1 830  LYS 830  830  830  LYS LYS A . n 
A 1 831  GLU 831  831  831  GLU GLU A . n 
A 1 832  CYS 832  832  832  CYS CYS A . n 
A 1 833  PHE 833  833  833  PHE PHE A . n 
A 1 834  PHE 834  834  ?    ?   ?   A . n 
A 1 835  ASP 835  835  ?    ?   ?   A . n 
A 1 836  ASP 836  836  ?    ?   ?   A . n 
A 1 837  MET 837  837  ?    ?   ?   A . n 
A 1 838  GLU 838  838  ?    ?   ?   A . n 
A 1 839  SER 839  839  ?    ?   ?   A . n 
A 1 840  ILE 840  840  ?    ?   ?   A . n 
A 1 841  PRO 841  841  ?    ?   ?   A . n 
A 1 842  ALA 842  842  ?    ?   ?   A . n 
A 1 843  VAL 843  843  ?    ?   ?   A . n 
A 1 844  THR 844  844  ?    ?   ?   A . n 
A 1 845  THR 845  845  ?    ?   ?   A . n 
A 1 846  TRP 846  846  846  TRP TRP A . n 
A 1 847  ASN 847  847  847  ASN ASN A . n 
A 1 848  THR 848  848  848  THR THR A . n 
A 1 849  TYR 849  849  849  TYR TYR A . n 
A 1 850  LEU 850  850  850  LEU LEU A . n 
A 1 851  ARG 851  851  851  ARG ARG A . n 
A 1 852  TYR 852  852  852  TYR TYR A . n 
A 1 853  ILE 853  853  853  ILE ILE A . n 
A 1 854  THR 854  854  854  THR THR A . n 
A 1 855  VAL 855  855  855  VAL VAL A . n 
A 1 856  HIS 856  856  856  HIS HIS A . n 
A 1 857  LYS 857  857  857  LYS LYS A . n 
A 1 858  SER 858  858  858  SER SER A . n 
A 1 859  LEU 859  859  859  LEU LEU A . n 
A 1 860  ILE 860  860  860  ILE ILE A . n 
A 1 861  PHE 861  861  861  PHE PHE A . n 
A 1 862  VAL 862  862  862  VAL VAL A . n 
A 1 863  LEU 863  863  863  LEU LEU A . n 
A 1 864  ILE 864  864  864  ILE ILE A . n 
A 1 865  TRP 865  865  865  TRP TRP A . n 
A 1 866  CYS 866  866  866  CYS CYS A . n 
A 1 867  LEU 867  867  867  LEU LEU A . n 
A 1 868  VAL 868  868  868  VAL VAL A . n 
A 1 869  ILE 869  869  869  ILE ILE A . n 
A 1 870  PHE 870  870  870  PHE PHE A . n 
A 1 871  LEU 871  871  871  LEU LEU A . n 
A 1 872  ALA 872  872  872  ALA ALA A . n 
A 1 873  GLU 873  873  873  GLU GLU A . n 
A 1 874  VAL 874  874  874  VAL VAL A . n 
A 1 875  ALA 875  875  875  ALA ALA A . n 
A 1 876  ALA 876  876  876  ALA ALA A . n 
A 1 877  SER 877  877  877  SER SER A . n 
A 1 878  LEU 878  878  878  LEU LEU A . n 
A 1 879  VAL 879  879  879  VAL VAL A . n 
A 1 880  VAL 880  880  880  VAL VAL A . n 
A 1 881  LEU 881  881  881  LEU LEU A . n 
A 1 882  TRP 882  882  882  TRP TRP A . n 
A 1 883  LEU 883  883  883  LEU LEU A . n 
A 1 884  LEU 884  884  884  LEU LEU A . n 
A 1 885  GLY 885  885  ?    ?   ?   A . n 
A 1 886  ASN 886  886  ?    ?   ?   A . n 
A 1 887  THR 887  887  ?    ?   ?   A . n 
A 1 888  PRO 888  888  ?    ?   ?   A . n 
A 1 889  LEU 889  889  ?    ?   ?   A . n 
A 1 890  GLN 890  890  ?    ?   ?   A . n 
A 1 891  ASP 891  891  ?    ?   ?   A . n 
A 1 892  LYS 892  892  ?    ?   ?   A . n 
A 1 893  GLY 893  893  ?    ?   ?   A . n 
A 1 894  ASN 894  894  ?    ?   ?   A . n 
A 1 895  SER 895  895  ?    ?   ?   A . n 
A 1 896  THR 896  896  ?    ?   ?   A . n 
A 1 897  HIS 897  897  ?    ?   ?   A . n 
A 1 898  SER 898  898  ?    ?   ?   A . n 
A 1 899  ARG 899  899  ?    ?   ?   A . n 
A 1 900  ASN 900  900  ?    ?   ?   A . n 
A 1 901  ASN 901  901  ?    ?   ?   A . n 
A 1 902  SER 902  902  ?    ?   ?   A . n 
A 1 903  TYR 903  903  903  TYR TYR A . n 
A 1 904  ALA 904  904  904  ALA ALA A . n 
A 1 905  VAL 905  905  905  VAL VAL A . n 
A 1 906  ILE 906  906  906  ILE ILE A . n 
A 1 907  ILE 907  907  907  ILE ILE A . n 
A 1 908  THR 908  908  908  THR THR A . n 
A 1 909  SER 909  909  909  SER SER A . n 
A 1 910  THR 910  910  910  THR THR A . n 
A 1 911  SER 911  911  911  SER SER A . n 
A 1 912  SER 912  912  912  SER SER A . n 
A 1 913  TYR 913  913  913  TYR TYR A . n 
A 1 914  TYR 914  914  914  TYR TYR A . n 
A 1 915  VAL 915  915  915  VAL VAL A . n 
A 1 916  PHE 916  916  916  PHE PHE A . n 
A 1 917  TYR 917  917  917  TYR TYR A . n 
A 1 918  ILE 918  918  918  ILE ILE A . n 
A 1 919  TYR 919  919  919  TYR TYR A . n 
A 1 920  VAL 920  920  920  VAL VAL A . n 
A 1 921  GLY 921  921  921  GLY GLY A . n 
A 1 922  VAL 922  922  922  VAL VAL A . n 
A 1 923  ALA 923  923  923  ALA ALA A . n 
A 1 924  ASP 924  924  924  ASP ASP A . n 
A 1 925  THR 925  925  925  THR THR A . n 
A 1 926  LEU 926  926  926  LEU LEU A . n 
A 1 927  LEU 927  927  927  LEU LEU A . n 
A 1 928  ALA 928  928  928  ALA ALA A . n 
A 1 929  MET 929  929  929  MET MET A . n 
A 1 930  GLY 930  930  930  GLY GLY A . n 
A 1 931  PHE 931  931  931  PHE PHE A . n 
A 1 932  PHE 932  932  932  PHE PHE A . n 
A 1 933  ARG 933  933  933  ARG ARG A . n 
A 1 934  GLY 934  934  934  GLY GLY A . n 
A 1 935  LEU 935  935  935  LEU LEU A . n 
A 1 936  PRO 936  936  936  PRO PRO A . n 
A 1 937  LEU 937  937  937  LEU LEU A . n 
A 1 938  VAL 938  938  938  VAL VAL A . n 
A 1 939  HIS 939  939  939  HIS HIS A . n 
A 1 940  THR 940  940  940  THR THR A . n 
A 1 941  LEU 941  941  941  LEU LEU A . n 
A 1 942  ILE 942  942  942  ILE ILE A . n 
A 1 943  THR 943  943  943  THR THR A . n 
A 1 944  VAL 944  944  944  VAL VAL A . n 
A 1 945  SER 945  945  945  SER SER A . n 
A 1 946  LYS 946  946  946  LYS LYS A . n 
A 1 947  ILE 947  947  947  ILE ILE A . n 
A 1 948  LEU 948  948  948  LEU LEU A . n 
A 1 949  HIS 949  949  949  HIS HIS A . n 
A 1 950  HIS 950  950  950  HIS HIS A . n 
A 1 951  LYS 951  951  951  LYS LYS A . n 
A 1 952  MET 952  952  952  MET MET A . n 
A 1 953  LEU 953  953  953  LEU LEU A . n 
A 1 954  HIS 954  954  954  HIS HIS A . n 
A 1 955  SER 955  955  955  SER SER A . n 
A 1 956  VAL 956  956  956  VAL VAL A . n 
A 1 957  LEU 957  957  957  LEU LEU A . n 
A 1 958  GLN 958  958  958  GLN GLN A . n 
A 1 959  ALA 959  959  959  ALA ALA A . n 
A 1 960  PRO 960  960  960  PRO PRO A . n 
A 1 961  MET 961  961  961  MET MET A . n 
A 1 962  SER 962  962  962  SER SER A . n 
A 1 963  THR 963  963  963  THR THR A . n 
A 1 964  LEU 964  964  964  LEU LEU A . n 
A 1 965  ASN 965  965  965  ASN ASN A . n 
A 1 966  THR 966  966  966  THR THR A . n 
A 1 967  LEU 967  967  967  LEU LEU A . n 
A 1 968  LYS 968  968  968  LYS LYS A . n 
A 1 969  ALA 969  969  969  ALA ALA A . n 
A 1 970  GLY 970  970  970  GLY GLY A . n 
A 1 971  GLY 971  971  971  GLY GLY A . n 
A 1 972  ILE 972  972  972  ILE ILE A . n 
A 1 973  LEU 973  973  973  LEU LEU A . n 
A 1 974  ASN 974  974  974  ASN ASN A . n 
A 1 975  ARG 975  975  975  ARG ARG A . n 
A 1 976  PHE 976  976  976  PHE PHE A . n 
A 1 977  SER 977  977  977  SER SER A . n 
A 1 978  LYS 978  978  978  LYS LYS A . n 
A 1 979  ASP 979  979  979  ASP ASP A . n 
A 1 980  ILE 980  980  980  ILE ILE A . n 
A 1 981  ALA 981  981  981  ALA ALA A . n 
A 1 982  ILE 982  982  982  ILE ILE A . n 
A 1 983  LEU 983  983  983  LEU LEU A . n 
A 1 984  ASP 984  984  984  ASP ASP A . n 
A 1 985  ASP 985  985  985  ASP ASP A . n 
A 1 986  LEU 986  986  986  LEU LEU A . n 
A 1 987  LEU 987  987  987  LEU LEU A . n 
A 1 988  PRO 988  988  988  PRO PRO A . n 
A 1 989  LEU 989  989  989  LEU LEU A . n 
A 1 990  THR 990  990  990  THR THR A . n 
A 1 991  ILE 991  991  991  ILE ILE A . n 
A 1 992  PHE 992  992  992  PHE PHE A . n 
A 1 993  ASP 993  993  993  ASP ASP A . n 
A 1 994  PHE 994  994  994  PHE PHE A . n 
A 1 995  ILE 995  995  995  ILE ILE A . n 
A 1 996  GLN 996  996  996  GLN GLN A . n 
A 1 997  LEU 997  997  997  LEU LEU A . n 
A 1 998  LEU 998  998  998  LEU LEU A . n 
A 1 999  LEU 999  999  999  LEU LEU A . n 
A 1 1000 ILE 1000 1000 1000 ILE ILE A . n 
A 1 1001 VAL 1001 1001 1001 VAL VAL A . n 
A 1 1002 ILE 1002 1002 1002 ILE ILE A . n 
A 1 1003 GLY 1003 1003 1003 GLY GLY A . n 
A 1 1004 ALA 1004 1004 1004 ALA ALA A . n 
A 1 1005 ILE 1005 1005 1005 ILE ILE A . n 
A 1 1006 ALA 1006 1006 1006 ALA ALA A . n 
A 1 1007 VAL 1007 1007 1007 VAL VAL A . n 
A 1 1008 VAL 1008 1008 1008 VAL VAL A . n 
A 1 1009 ALA 1009 1009 1009 ALA ALA A . n 
A 1 1010 VAL 1010 1010 1010 VAL VAL A . n 
A 1 1011 LEU 1011 1011 1011 LEU LEU A . n 
A 1 1012 GLN 1012 1012 1012 GLN GLN A . n 
A 1 1013 PRO 1013 1013 1013 PRO PRO A . n 
A 1 1014 TYR 1014 1014 1014 TYR TYR A . n 
A 1 1015 ILE 1015 1015 1015 ILE ILE A . n 
A 1 1016 PHE 1016 1016 1016 PHE PHE A . n 
A 1 1017 VAL 1017 1017 1017 VAL VAL A . n 
A 1 1018 ALA 1018 1018 1018 ALA ALA A . n 
A 1 1019 THR 1019 1019 1019 THR THR A . n 
A 1 1020 VAL 1020 1020 1020 VAL VAL A . n 
A 1 1021 PRO 1021 1021 1021 PRO PRO A . n 
A 1 1022 VAL 1022 1022 1022 VAL VAL A . n 
A 1 1023 ILE 1023 1023 1023 ILE ILE A . n 
A 1 1024 VAL 1024 1024 1024 VAL VAL A . n 
A 1 1025 ALA 1025 1025 1025 ALA ALA A . n 
A 1 1026 PHE 1026 1026 1026 PHE PHE A . n 
A 1 1027 ILE 1027 1027 1027 ILE ILE A . n 
A 1 1028 MET 1028 1028 1028 MET MET A . n 
A 1 1029 LEU 1029 1029 1029 LEU LEU A . n 
A 1 1030 ARG 1030 1030 1030 ARG ARG A . n 
A 1 1031 ALA 1031 1031 1031 ALA ALA A . n 
A 1 1032 TYR 1032 1032 1032 TYR TYR A . n 
A 1 1033 PHE 1033 1033 1033 PHE PHE A . n 
A 1 1034 LEU 1034 1034 1034 LEU LEU A . n 
A 1 1035 GLN 1035 1035 1035 GLN GLN A . n 
A 1 1036 THR 1036 1036 1036 THR THR A . n 
A 1 1037 SER 1037 1037 1037 SER SER A . n 
A 1 1038 GLN 1038 1038 1038 GLN GLN A . n 
A 1 1039 GLN 1039 1039 1039 GLN GLN A . n 
A 1 1040 LEU 1040 1040 1040 LEU LEU A . n 
A 1 1041 LYS 1041 1041 1041 LYS LYS A . n 
A 1 1042 GLN 1042 1042 1042 GLN GLN A . n 
A 1 1043 LEU 1043 1043 1043 LEU LEU A . n 
A 1 1044 GLU 1044 1044 1044 GLU GLU A . n 
A 1 1045 SER 1045 1045 1045 SER SER A . n 
A 1 1046 GLU 1046 1046 1046 GLU GLU A . n 
A 1 1047 GLY 1047 1047 1047 GLY GLY A . n 
A 1 1048 ARG 1048 1048 1048 ARG ARG A . n 
A 1 1049 SER 1049 1049 1049 SER SER A . n 
A 1 1050 PRO 1050 1050 1050 PRO PRO A . n 
A 1 1051 ILE 1051 1051 1051 ILE ILE A . n 
A 1 1052 PHE 1052 1052 1052 PHE PHE A . n 
A 1 1053 THR 1053 1053 1053 THR THR A . n 
A 1 1054 HIS 1054 1054 1054 HIS HIS A . n 
A 1 1055 LEU 1055 1055 1055 LEU LEU A . n 
A 1 1056 VAL 1056 1056 1056 VAL VAL A . n 
A 1 1057 THR 1057 1057 1057 THR THR A . n 
A 1 1058 SER 1058 1058 1058 SER SER A . n 
A 1 1059 LEU 1059 1059 1059 LEU LEU A . n 
A 1 1060 LYS 1060 1060 1060 LYS LYS A . n 
A 1 1061 GLY 1061 1061 1061 GLY GLY A . n 
A 1 1062 LEU 1062 1062 1062 LEU LEU A . n 
A 1 1063 TRP 1063 1063 1063 TRP TRP A . n 
A 1 1064 THR 1064 1064 1064 THR THR A . n 
A 1 1065 LEU 1065 1065 1065 LEU LEU A . n 
A 1 1066 ARG 1066 1066 1066 ARG ARG A . n 
A 1 1067 ALA 1067 1067 1067 ALA ALA A . n 
A 1 1068 PHE 1068 1068 1068 PHE PHE A . n 
A 1 1069 GLY 1069 1069 1069 GLY GLY A . n 
A 1 1070 ARG 1070 1070 1070 ARG ARG A . n 
A 1 1071 GLN 1071 1071 1071 GLN GLN A . n 
A 1 1072 PRO 1072 1072 1072 PRO PRO A . n 
A 1 1073 TYR 1073 1073 1073 TYR TYR A . n 
A 1 1074 PHE 1074 1074 1074 PHE PHE A . n 
A 1 1075 GLU 1075 1075 1075 GLU GLU A . n 
A 1 1076 THR 1076 1076 1076 THR THR A . n 
A 1 1077 LEU 1077 1077 1077 LEU LEU A . n 
A 1 1078 PHE 1078 1078 1078 PHE PHE A . n 
A 1 1079 HIS 1079 1079 1079 HIS HIS A . n 
A 1 1080 LYS 1080 1080 1080 LYS LYS A . n 
A 1 1081 ALA 1081 1081 1081 ALA ALA A . n 
A 1 1082 LEU 1082 1082 1082 LEU LEU A . n 
A 1 1083 ASN 1083 1083 1083 ASN ASN A . n 
A 1 1084 LEU 1084 1084 1084 LEU LEU A . n 
A 1 1085 HIS 1085 1085 1085 HIS HIS A . n 
A 1 1086 THR 1086 1086 1086 THR THR A . n 
A 1 1087 ALA 1087 1087 1087 ALA ALA A . n 
A 1 1088 ASN 1088 1088 1088 ASN ASN A . n 
A 1 1089 TRP 1089 1089 1089 TRP TRP A . n 
A 1 1090 PHE 1090 1090 1090 PHE PHE A . n 
A 1 1091 LEU 1091 1091 1091 LEU LEU A . n 
A 1 1092 TYR 1092 1092 1092 TYR TYR A . n 
A 1 1093 LEU 1093 1093 1093 LEU LEU A . n 
A 1 1094 SER 1094 1094 1094 SER SER A . n 
A 1 1095 THR 1095 1095 1095 THR THR A . n 
A 1 1096 LEU 1096 1096 1096 LEU LEU A . n 
A 1 1097 ARG 1097 1097 1097 ARG ARG A . n 
A 1 1098 TRP 1098 1098 1098 TRP TRP A . n 
A 1 1099 PHE 1099 1099 1099 PHE PHE A . n 
A 1 1100 GLN 1100 1100 1100 GLN GLN A . n 
A 1 1101 MET 1101 1101 1101 MET MET A . n 
A 1 1102 ARG 1102 1102 1102 ARG ARG A . n 
A 1 1103 ILE 1103 1103 1103 ILE ILE A . n 
A 1 1104 GLU 1104 1104 1104 GLU GLU A . n 
A 1 1105 MET 1105 1105 1105 MET MET A . n 
A 1 1106 ILE 1106 1106 1106 ILE ILE A . n 
A 1 1107 PHE 1107 1107 1107 PHE PHE A . n 
A 1 1108 VAL 1108 1108 1108 VAL VAL A . n 
A 1 1109 ILE 1109 1109 1109 ILE ILE A . n 
A 1 1110 PHE 1110 1110 1110 PHE PHE A . n 
A 1 1111 PHE 1111 1111 1111 PHE PHE A . n 
A 1 1112 ILE 1112 1112 1112 ILE ILE A . n 
A 1 1113 ALA 1113 1113 1113 ALA ALA A . n 
A 1 1114 VAL 1114 1114 1114 VAL VAL A . n 
A 1 1115 THR 1115 1115 1115 THR THR A . n 
A 1 1116 PHE 1116 1116 1116 PHE PHE A . n 
A 1 1117 ILE 1117 1117 1117 ILE ILE A . n 
A 1 1118 SER 1118 1118 1118 SER SER A . n 
A 1 1119 ILE 1119 1119 1119 ILE ILE A . n 
A 1 1120 LEU 1120 1120 1120 LEU LEU A . n 
A 1 1121 THR 1121 1121 1121 THR THR A . n 
A 1 1122 THR 1122 1122 1122 THR THR A . n 
A 1 1123 GLY 1123 1123 1123 GLY GLY A . n 
A 1 1124 GLU 1124 1124 1124 GLU GLU A . n 
A 1 1125 GLY 1125 1125 1125 GLY GLY A . n 
A 1 1126 GLU 1126 1126 1126 GLU GLU A . n 
A 1 1127 GLY 1127 1127 1127 GLY GLY A . n 
A 1 1128 ARG 1128 1128 1128 ARG ARG A . n 
A 1 1129 VAL 1129 1129 1129 VAL VAL A . n 
A 1 1130 GLY 1130 1130 1130 GLY GLY A . n 
A 1 1131 ILE 1131 1131 1131 ILE ILE A . n 
A 1 1132 ILE 1132 1132 1132 ILE ILE A . n 
A 1 1133 LEU 1133 1133 1133 LEU LEU A . n 
A 1 1134 THR 1134 1134 1134 THR THR A . n 
A 1 1135 LEU 1135 1135 1135 LEU LEU A . n 
A 1 1136 ALA 1136 1136 1136 ALA ALA A . n 
A 1 1137 MET 1137 1137 1137 MET MET A . n 
A 1 1138 ASN 1138 1138 1138 ASN ASN A . n 
A 1 1139 ILE 1139 1139 1139 ILE ILE A . n 
A 1 1140 MET 1140 1140 1140 MET MET A . n 
A 1 1141 SER 1141 1141 1141 SER SER A . n 
A 1 1142 THR 1142 1142 1142 THR THR A . n 
A 1 1143 LEU 1143 1143 1143 LEU LEU A . n 
A 1 1144 GLN 1144 1144 1144 GLN GLN A . n 
A 1 1145 TRP 1145 1145 1145 TRP TRP A . n 
A 1 1146 ALA 1146 1146 1146 ALA ALA A . n 
A 1 1147 VAL 1147 1147 1147 VAL VAL A . n 
A 1 1148 ASN 1148 1148 1148 ASN ASN A . n 
A 1 1149 SER 1149 1149 1149 SER SER A . n 
A 1 1150 SER 1150 1150 1150 SER SER A . n 
A 1 1151 ILE 1151 1151 1151 ILE ILE A . n 
A 1 1152 ASP 1152 1152 1152 ASP ASP A . n 
A 1 1153 VAL 1153 1153 1153 VAL VAL A . n 
A 1 1154 ASP 1154 1154 1154 ASP ASP A . n 
A 1 1155 SER 1155 1155 1155 SER SER A . n 
A 1 1156 LEU 1156 1156 1156 LEU LEU A . n 
A 1 1157 MET 1157 1157 1157 MET MET A . n 
A 1 1158 ARG 1158 1158 1158 ARG ARG A . n 
A 1 1159 SER 1159 1159 1159 SER SER A . n 
A 1 1160 VAL 1160 1160 1160 VAL VAL A . n 
A 1 1161 SER 1161 1161 1161 SER SER A . n 
A 1 1162 ARG 1162 1162 1162 ARG ARG A . n 
A 1 1163 VAL 1163 1163 1163 VAL VAL A . n 
A 1 1164 PHE 1164 1164 1164 PHE PHE A . n 
A 1 1165 LYS 1165 1165 1165 LYS LYS A . n 
A 1 1166 PHE 1166 1166 1166 PHE PHE A . n 
A 1 1167 ILE 1167 1167 1167 ILE ILE A . n 
A 1 1168 ASP 1168 1168 1168 ASP ASP A . n 
A 1 1169 MET 1169 1169 1169 MET MET A . n 
A 1 1170 PRO 1170 1170 1170 PRO PRO A . n 
A 1 1171 THR 1171 1171 1171 THR THR A . n 
A 1 1172 GLU 1172 1172 1172 GLU GLU A . n 
A 1 1173 GLY 1173 1173 1173 GLY GLY A . n 
A 1 1174 LYS 1174 1174 ?    ?   ?   A . n 
A 1 1175 PRO 1175 1175 ?    ?   ?   A . n 
A 1 1176 THR 1176 1176 ?    ?   ?   A . n 
A 1 1177 LYS 1177 1177 ?    ?   ?   A . n 
A 1 1178 SER 1178 1178 ?    ?   ?   A . n 
A 1 1179 THR 1179 1179 ?    ?   ?   A . n 
A 1 1180 LYS 1180 1180 ?    ?   ?   A . n 
A 1 1181 PRO 1181 1181 ?    ?   ?   A . n 
A 1 1182 TYR 1182 1182 ?    ?   ?   A . n 
A 1 1183 LYS 1183 1183 ?    ?   ?   A . n 
A 1 1184 ASN 1184 1184 ?    ?   ?   A . n 
A 1 1185 GLY 1185 1185 ?    ?   ?   A . n 
A 1 1186 GLN 1186 1186 ?    ?   ?   A . n 
A 1 1187 LEU 1187 1187 ?    ?   ?   A . n 
A 1 1188 SER 1188 1188 ?    ?   ?   A . n 
A 1 1189 LYS 1189 1189 ?    ?   ?   A . n 
A 1 1190 VAL 1190 1190 ?    ?   ?   A . n 
A 1 1191 MET 1191 1191 ?    ?   ?   A . n 
A 1 1192 ILE 1192 1192 ?    ?   ?   A . n 
A 1 1193 ILE 1193 1193 ?    ?   ?   A . n 
A 1 1194 GLU 1194 1194 ?    ?   ?   A . n 
A 1 1195 ASN 1195 1195 ?    ?   ?   A . n 
A 1 1196 SER 1196 1196 ?    ?   ?   A . n 
A 1 1197 HIS 1197 1197 ?    ?   ?   A . n 
A 1 1198 VAL 1198 1198 ?    ?   ?   A . n 
A 1 1199 LYS 1199 1199 ?    ?   ?   A . n 
A 1 1200 LYS 1200 1200 ?    ?   ?   A . n 
A 1 1201 ASP 1201 1201 ?    ?   ?   A . n 
A 1 1202 ASP 1202 1202 ?    ?   ?   A . n 
A 1 1203 ILE 1203 1203 1203 ILE ILE A . n 
A 1 1204 TRP 1204 1204 1204 TRP TRP A . n 
A 1 1205 PRO 1205 1205 1205 PRO PRO A . n 
A 1 1206 SER 1206 1206 1206 SER SER A . n 
A 1 1207 GLY 1207 1207 1207 GLY GLY A . n 
A 1 1208 GLY 1208 1208 1208 GLY GLY A . n 
A 1 1209 GLN 1209 1209 1209 GLN GLN A . n 
A 1 1210 MET 1210 1210 1210 MET MET A . n 
A 1 1211 THR 1211 1211 1211 THR THR A . n 
A 1 1212 VAL 1212 1212 1212 VAL VAL A . n 
A 1 1213 LYS 1213 1213 1213 LYS LYS A . n 
A 1 1214 ASP 1214 1214 1214 ASP ASP A . n 
A 1 1215 LEU 1215 1215 1215 LEU LEU A . n 
A 1 1216 THR 1216 1216 1216 THR THR A . n 
A 1 1217 ALA 1217 1217 1217 ALA ALA A . n 
A 1 1218 LYS 1218 1218 1218 LYS LYS A . n 
A 1 1219 TYR 1219 1219 1219 TYR TYR A . n 
A 1 1220 THR 1220 1220 1220 THR THR A . n 
A 1 1221 GLU 1221 1221 1221 GLU GLU A . n 
A 1 1222 GLY 1222 1222 1222 GLY GLY A . n 
A 1 1223 GLY 1223 1223 1223 GLY GLY A . n 
A 1 1224 ASN 1224 1224 1224 ASN ASN A . n 
A 1 1225 ALA 1225 1225 1225 ALA ALA A . n 
A 1 1226 ILE 1226 1226 1226 ILE ILE A . n 
A 1 1227 LEU 1227 1227 1227 LEU LEU A . n 
A 1 1228 GLU 1228 1228 1228 GLU GLU A . n 
A 1 1229 ASN 1229 1229 1229 ASN ASN A . n 
A 1 1230 ILE 1230 1230 1230 ILE ILE A . n 
A 1 1231 SER 1231 1231 1231 SER SER A . n 
A 1 1232 PHE 1232 1232 1232 PHE PHE A . n 
A 1 1233 SER 1233 1233 1233 SER SER A . n 
A 1 1234 ILE 1234 1234 1234 ILE ILE A . n 
A 1 1235 SER 1235 1235 1235 SER SER A . n 
A 1 1236 PRO 1236 1236 1236 PRO PRO A . n 
A 1 1237 GLY 1237 1237 1237 GLY GLY A . n 
A 1 1238 GLN 1238 1238 1238 GLN GLN A . n 
A 1 1239 ARG 1239 1239 1239 ARG ARG A . n 
A 1 1240 VAL 1240 1240 1240 VAL VAL A . n 
A 1 1241 GLY 1241 1241 1241 GLY GLY A . n 
A 1 1242 LEU 1242 1242 1242 LEU LEU A . n 
A 1 1243 LEU 1243 1243 1243 LEU LEU A . n 
A 1 1244 GLY 1244 1244 1244 GLY GLY A . n 
A 1 1245 ARG 1245 1245 1245 ARG ARG A . n 
A 1 1246 THR 1246 1246 1246 THR THR A . n 
A 1 1247 GLY 1247 1247 1247 GLY GLY A . n 
A 1 1248 SER 1248 1248 1248 SER SER A . n 
A 1 1249 GLY 1249 1249 1249 GLY GLY A . n 
A 1 1250 LYS 1250 1250 1250 LYS LYS A . n 
A 1 1251 SER 1251 1251 1251 SER SER A . n 
A 1 1252 THR 1252 1252 1252 THR THR A . n 
A 1 1253 LEU 1253 1253 1253 LEU LEU A . n 
A 1 1254 LEU 1254 1254 1254 LEU LEU A . n 
A 1 1255 SER 1255 1255 1255 SER SER A . n 
A 1 1256 ALA 1256 1256 1256 ALA ALA A . n 
A 1 1257 PHE 1257 1257 1257 PHE PHE A . n 
A 1 1258 LEU 1258 1258 1258 LEU LEU A . n 
A 1 1259 ARG 1259 1259 1259 ARG ARG A . n 
A 1 1260 LEU 1260 1260 1260 LEU LEU A . n 
A 1 1261 LEU 1261 1261 1261 LEU LEU A . n 
A 1 1262 ASN 1262 1262 1262 ASN ASN A . n 
A 1 1263 THR 1263 1263 1263 THR THR A . n 
A 1 1264 GLU 1264 1264 1264 GLU GLU A . n 
A 1 1265 GLY 1265 1265 1265 GLY GLY A . n 
A 1 1266 GLU 1266 1266 1266 GLU GLU A . n 
A 1 1267 ILE 1267 1267 1267 ILE ILE A . n 
A 1 1268 GLN 1268 1268 1268 GLN GLN A . n 
A 1 1269 ILE 1269 1269 1269 ILE ILE A . n 
A 1 1270 ASP 1270 1270 1270 ASP ASP A . n 
A 1 1271 GLY 1271 1271 1271 GLY GLY A . n 
A 1 1272 VAL 1272 1272 1272 VAL VAL A . n 
A 1 1273 SER 1273 1273 1273 SER SER A . n 
A 1 1274 TRP 1274 1274 1274 TRP TRP A . n 
A 1 1275 ASP 1275 1275 1275 ASP ASP A . n 
A 1 1276 SER 1276 1276 1276 SER SER A . n 
A 1 1277 ILE 1277 1277 1277 ILE ILE A . n 
A 1 1278 THR 1278 1278 1278 THR THR A . n 
A 1 1279 LEU 1279 1279 1279 LEU LEU A . n 
A 1 1280 GLN 1280 1280 1280 GLN GLN A . n 
A 1 1281 GLN 1281 1281 1281 GLN GLN A . n 
A 1 1282 TRP 1282 1282 1282 TRP TRP A . n 
A 1 1283 ARG 1283 1283 1283 ARG ARG A . n 
A 1 1284 LYS 1284 1284 1284 LYS LYS A . n 
A 1 1285 ALA 1285 1285 1285 ALA ALA A . n 
A 1 1286 PHE 1286 1286 1286 PHE PHE A . n 
A 1 1287 GLY 1287 1287 1287 GLY GLY A . n 
A 1 1288 VAL 1288 1288 1288 VAL VAL A . n 
A 1 1289 ILE 1289 1289 1289 ILE ILE A . n 
A 1 1290 PRO 1290 1290 1290 PRO PRO A . n 
A 1 1291 GLN 1291 1291 1291 GLN GLN A . n 
A 1 1292 LYS 1292 1292 1292 LYS LYS A . n 
A 1 1293 VAL 1293 1293 1293 VAL VAL A . n 
A 1 1294 PHE 1294 1294 1294 PHE PHE A . n 
A 1 1295 ILE 1295 1295 1295 ILE ILE A . n 
A 1 1296 PHE 1296 1296 1296 PHE PHE A . n 
A 1 1297 SER 1297 1297 1297 SER SER A . n 
A 1 1298 GLY 1298 1298 1298 GLY GLY A . n 
A 1 1299 THR 1299 1299 1299 THR THR A . n 
A 1 1300 PHE 1300 1300 1300 PHE PHE A . n 
A 1 1301 ARG 1301 1301 1301 ARG ARG A . n 
A 1 1302 LYS 1302 1302 1302 LYS LYS A . n 
A 1 1303 ASN 1303 1303 1303 ASN ASN A . n 
A 1 1304 LEU 1304 1304 1304 LEU LEU A . n 
A 1 1305 ASP 1305 1305 1305 ASP ASP A . n 
A 1 1306 PRO 1306 1306 1306 PRO PRO A . n 
A 1 1307 TYR 1307 1307 1307 TYR TYR A . n 
A 1 1308 GLU 1308 1308 1308 GLU GLU A . n 
A 1 1309 GLN 1309 1309 1309 GLN GLN A . n 
A 1 1310 TRP 1310 1310 1310 TRP TRP A . n 
A 1 1311 SER 1311 1311 1311 SER SER A . n 
A 1 1312 ASP 1312 1312 1312 ASP ASP A . n 
A 1 1313 GLN 1313 1313 1313 GLN GLN A . n 
A 1 1314 GLU 1314 1314 1314 GLU GLU A . n 
A 1 1315 ILE 1315 1315 1315 ILE ILE A . n 
A 1 1316 TRP 1316 1316 1316 TRP TRP A . n 
A 1 1317 LYS 1317 1317 1317 LYS LYS A . n 
A 1 1318 VAL 1318 1318 1318 VAL VAL A . n 
A 1 1319 ALA 1319 1319 1319 ALA ALA A . n 
A 1 1320 ASP 1320 1320 1320 ASP ASP A . n 
A 1 1321 GLU 1321 1321 1321 GLU GLU A . n 
A 1 1322 VAL 1322 1322 1322 VAL VAL A . n 
A 1 1323 GLY 1323 1323 1323 GLY GLY A . n 
A 1 1324 LEU 1324 1324 1324 LEU LEU A . n 
A 1 1325 ARG 1325 1325 1325 ARG ARG A . n 
A 1 1326 SER 1326 1326 1326 SER SER A . n 
A 1 1327 VAL 1327 1327 1327 VAL VAL A . n 
A 1 1328 ILE 1328 1328 1328 ILE ILE A . n 
A 1 1329 GLU 1329 1329 1329 GLU GLU A . n 
A 1 1330 GLN 1330 1330 1330 GLN GLN A . n 
A 1 1331 PHE 1331 1331 1331 PHE PHE A . n 
A 1 1332 PRO 1332 1332 1332 PRO PRO A . n 
A 1 1333 GLY 1333 1333 1333 GLY GLY A . n 
A 1 1334 LYS 1334 1334 1334 LYS LYS A . n 
A 1 1335 LEU 1335 1335 1335 LEU LEU A . n 
A 1 1336 ASP 1336 1336 1336 ASP ASP A . n 
A 1 1337 PHE 1337 1337 1337 PHE PHE A . n 
A 1 1338 VAL 1338 1338 1338 VAL VAL A . n 
A 1 1339 LEU 1339 1339 1339 LEU LEU A . n 
A 1 1340 VAL 1340 1340 1340 VAL VAL A . n 
A 1 1341 ASP 1341 1341 1341 ASP ASP A . n 
A 1 1342 GLY 1342 1342 1342 GLY GLY A . n 
A 1 1343 GLY 1343 1343 1343 GLY GLY A . n 
A 1 1344 CYS 1344 1344 1344 CYS CYS A . n 
A 1 1345 VAL 1345 1345 1345 VAL VAL A . n 
A 1 1346 LEU 1346 1346 1346 LEU LEU A . n 
A 1 1347 SER 1347 1347 1347 SER SER A . n 
A 1 1348 HIS 1348 1348 1348 HIS HIS A . n 
A 1 1349 GLY 1349 1349 1349 GLY GLY A . n 
A 1 1350 HIS 1350 1350 1350 HIS HIS A . n 
A 1 1351 LYS 1351 1351 1351 LYS LYS A . n 
A 1 1352 GLN 1352 1352 1352 GLN GLN A . n 
A 1 1353 LEU 1353 1353 1353 LEU LEU A . n 
A 1 1354 MET 1354 1354 1354 MET MET A . n 
A 1 1355 CYS 1355 1355 1355 CYS CYS A . n 
A 1 1356 LEU 1356 1356 1356 LEU LEU A . n 
A 1 1357 ALA 1357 1357 1357 ALA ALA A . n 
A 1 1358 ARG 1358 1358 1358 ARG ARG A . n 
A 1 1359 SER 1359 1359 1359 SER SER A . n 
A 1 1360 VAL 1360 1360 1360 VAL VAL A . n 
A 1 1361 LEU 1361 1361 1361 LEU LEU A . n 
A 1 1362 SER 1362 1362 1362 SER SER A . n 
A 1 1363 LYS 1363 1363 1363 LYS LYS A . n 
A 1 1364 ALA 1364 1364 1364 ALA ALA A . n 
A 1 1365 LYS 1365 1365 1365 LYS LYS A . n 
A 1 1366 ILE 1366 1366 1366 ILE ILE A . n 
A 1 1367 LEU 1367 1367 1367 LEU LEU A . n 
A 1 1368 LEU 1368 1368 1368 LEU LEU A . n 
A 1 1369 LEU 1369 1369 1369 LEU LEU A . n 
A 1 1370 ASP 1370 1370 1370 ASP ASP A . n 
A 1 1371 GLN 1371 1371 1371 GLN GLN A . n 
A 1 1372 PRO 1372 1372 1372 PRO PRO A . n 
A 1 1373 SER 1373 1373 1373 SER SER A . n 
A 1 1374 ALA 1374 1374 1374 ALA ALA A . n 
A 1 1375 HIS 1375 1375 1375 HIS HIS A . n 
A 1 1376 LEU 1376 1376 1376 LEU LEU A . n 
A 1 1377 ASP 1377 1377 1377 ASP ASP A . n 
A 1 1378 PRO 1378 1378 1378 PRO PRO A . n 
A 1 1379 VAL 1379 1379 1379 VAL VAL A . n 
A 1 1380 THR 1380 1380 1380 THR THR A . n 
A 1 1381 TYR 1381 1381 1381 TYR TYR A . n 
A 1 1382 GLN 1382 1382 1382 GLN GLN A . n 
A 1 1383 ILE 1383 1383 1383 ILE ILE A . n 
A 1 1384 ILE 1384 1384 1384 ILE ILE A . n 
A 1 1385 ARG 1385 1385 1385 ARG ARG A . n 
A 1 1386 ARG 1386 1386 1386 ARG ARG A . n 
A 1 1387 THR 1387 1387 1387 THR THR A . n 
A 1 1388 LEU 1388 1388 1388 LEU LEU A . n 
A 1 1389 LYS 1389 1389 1389 LYS LYS A . n 
A 1 1390 GLN 1390 1390 1390 GLN GLN A . n 
A 1 1391 ALA 1391 1391 1391 ALA ALA A . n 
A 1 1392 PHE 1392 1392 1392 PHE PHE A . n 
A 1 1393 ALA 1393 1393 1393 ALA ALA A . n 
A 1 1394 ASP 1394 1394 1394 ASP ASP A . n 
A 1 1395 CYS 1395 1395 1395 CYS CYS A . n 
A 1 1396 THR 1396 1396 1396 THR THR A . n 
A 1 1397 VAL 1397 1397 1397 VAL VAL A . n 
A 1 1398 ILE 1398 1398 1398 ILE ILE A . n 
A 1 1399 LEU 1399 1399 1399 LEU LEU A . n 
A 1 1400 CYS 1400 1400 1400 CYS CYS A . n 
A 1 1401 GLU 1401 1401 1401 GLU GLU A . n 
A 1 1402 HIS 1402 1402 1402 HIS HIS A . n 
A 1 1403 ARG 1403 1403 1403 ARG ARG A . n 
A 1 1404 ILE 1404 1404 1404 ILE ILE A . n 
A 1 1405 GLU 1405 1405 1405 GLU GLU A . n 
A 1 1406 ALA 1406 1406 1406 ALA ALA A . n 
A 1 1407 MET 1407 1407 1407 MET MET A . n 
A 1 1408 LEU 1408 1408 1408 LEU LEU A . n 
A 1 1409 GLU 1409 1409 1409 GLU GLU A . n 
A 1 1410 CYS 1410 1410 1410 CYS CYS A . n 
A 1 1411 GLN 1411 1411 1411 GLN GLN A . n 
A 1 1412 GLN 1412 1412 1412 GLN GLN A . n 
A 1 1413 PHE 1413 1413 1413 PHE PHE A . n 
A 1 1414 LEU 1414 1414 1414 LEU LEU A . n 
A 1 1415 VAL 1415 1415 1415 VAL VAL A . n 
A 1 1416 ILE 1416 1416 1416 ILE ILE A . n 
A 1 1417 GLU 1417 1417 1417 GLU GLU A . n 
A 1 1418 GLU 1418 1418 1418 GLU GLU A . n 
A 1 1419 ASN 1419 1419 1419 ASN ASN A . n 
A 1 1420 LYS 1420 1420 1420 LYS LYS A . n 
A 1 1421 VAL 1421 1421 1421 VAL VAL A . n 
A 1 1422 ARG 1422 1422 1422 ARG ARG A . n 
A 1 1423 GLN 1423 1423 1423 GLN GLN A . n 
A 1 1424 TYR 1424 1424 1424 TYR TYR A . n 
A 1 1425 ASP 1425 1425 1425 ASP ASP A . n 
A 1 1426 SER 1426 1426 1426 SER SER A . n 
A 1 1427 ILE 1427 1427 1427 ILE ILE A . n 
A 1 1428 GLN 1428 1428 1428 GLN GLN A . n 
A 1 1429 LYS 1429 1429 1429 LYS LYS A . n 
A 1 1430 LEU 1430 1430 1430 LEU LEU A . n 
A 1 1431 LEU 1431 1431 1431 LEU LEU A . n 
A 1 1432 ASN 1432 1432 1432 ASN ASN A . n 
A 1 1433 GLU 1433 1433 1433 GLU GLU A . n 
A 1 1434 ARG 1434 1434 1434 ARG ARG A . n 
A 1 1435 SER 1435 1435 1435 SER SER A . n 
A 1 1436 LEU 1436 1436 1436 LEU LEU A . n 
A 1 1437 PHE 1437 1437 1437 PHE PHE A . n 
A 1 1438 ARG 1438 1438 1438 ARG ARG A . n 
A 1 1439 GLN 1439 1439 1439 GLN GLN A . n 
A 1 1440 ALA 1440 1440 1440 ALA ALA A . n 
A 1 1441 ILE 1441 1441 1441 ILE ILE A . n 
A 1 1442 SER 1442 1442 1442 SER SER A . n 
A 1 1443 PRO 1443 1443 1443 PRO PRO A . n 
A 1 1444 SER 1444 1444 1444 SER SER A . n 
A 1 1445 ASP 1445 1445 1445 ASP ASP A . n 
A 1 1446 ARG 1446 1446 1446 ARG ARG A . n 
A 1 1447 VAL 1447 1447 1447 VAL VAL A . n 
A 1 1448 LYS 1448 1448 1448 LYS LYS A . n 
A 1 1449 LEU 1449 1449 1449 LEU LEU A . n 
A 1 1450 PHE 1450 1450 1450 PHE PHE A . n 
A 1 1451 PRO 1451 1451 1451 PRO PRO A . n 
A 1 1452 HIS 1452 1452 ?    ?   ?   A . n 
A 1 1453 ARG 1453 1453 ?    ?   ?   A . n 
A 1 1454 ASN 1454 1454 ?    ?   ?   A . n 
A 1 1455 SER 1455 1455 ?    ?   ?   A . n 
A 1 1456 SER 1456 1456 ?    ?   ?   A . n 
A 1 1457 LYS 1457 1457 ?    ?   ?   A . n 
A 1 1458 CYS 1458 1458 ?    ?   ?   A . n 
A 1 1459 LYS 1459 1459 ?    ?   ?   A . n 
A 1 1460 SER 1460 1460 ?    ?   ?   A . n 
A 1 1461 LYS 1461 1461 ?    ?   ?   A . n 
A 1 1462 PRO 1462 1462 ?    ?   ?   A . n 
A 1 1463 GLN 1463 1463 ?    ?   ?   A . n 
A 1 1464 ILE 1464 1464 ?    ?   ?   A . n 
A 1 1465 ALA 1465 1465 ?    ?   ?   A . n 
A 1 1466 ALA 1466 1466 ?    ?   ?   A . n 
A 1 1467 LEU 1467 1467 ?    ?   ?   A . n 
A 1 1468 LYS 1468 1468 ?    ?   ?   A . n 
A 1 1469 GLU 1469 1469 ?    ?   ?   A . n 
A 1 1470 GLU 1470 1470 ?    ?   ?   A . n 
A 1 1471 THR 1471 1471 ?    ?   ?   A . n 
A 1 1472 GLU 1472 1472 ?    ?   ?   A . n 
A 1 1473 GLU 1473 1473 ?    ?   ?   A . n 
A 1 1474 GLU 1474 1474 ?    ?   ?   A . n 
A 1 1475 VAL 1475 1475 ?    ?   ?   A . n 
A 1 1476 GLN 1476 1476 ?    ?   ?   A . n 
A 1 1477 ASP 1477 1477 ?    ?   ?   A . n 
A 1 1478 THR 1478 1478 ?    ?   ?   A . n 
A 1 1479 ARG 1479 1479 ?    ?   ?   A . n 
A 1 1480 LEU 1480 1480 ?    ?   ?   A . n 
B 2 1    MET 1    1    ?    ?   ?   G . n 
B 2 2    GLY 2    2    ?    ?   ?   G . n 
B 2 3    ASN 3    3    ?    ?   ?   G . n 
B 2 4    ALA 4    4    ?    ?   ?   G . n 
B 2 5    ALA 5    5    ?    ?   ?   G . n 
B 2 6    ALA 6    6    ?    ?   ?   G . n 
B 2 7    ALA 7    7    ?    ?   ?   G . n 
B 2 8    LYS 8    8    ?    ?   ?   G . n 
B 2 9    LYS 9    9    ?    ?   ?   G . n 
B 2 10   GLY 10   10   ?    ?   ?   G . n 
B 2 11   SER 11   11   ?    ?   ?   G . n 
B 2 12   GLU 12   12   ?    ?   ?   G . n 
B 2 13   GLN 13   13   13   GLN GLN G . n 
B 2 14   GLU 14   14   14   GLU GLU G . n 
B 2 15   SER 15   15   15   SER SER G . n 
B 2 16   VAL 16   16   16   VAL VAL G . n 
B 2 17   LYS 17   17   17   LYS LYS G . n 
B 2 18   GLU 18   18   18   GLU GLU G . n 
B 2 19   PHE 19   19   19   PHE PHE G . n 
B 2 20   LEU 20   20   20   LEU LEU G . n 
B 2 21   ALA 21   21   21   ALA ALA G . n 
B 2 22   LYS 22   22   22   LYS LYS G . n 
B 2 23   ALA 23   23   23   ALA ALA G . n 
B 2 24   LYS 24   24   24   LYS LYS G . n 
B 2 25   GLU 25   25   25   GLU GLU G . n 
B 2 26   ASP 26   26   26   ASP ASP G . n 
B 2 27   PHE 27   27   27   PHE PHE G . n 
B 2 28   LEU 28   28   28   LEU LEU G . n 
B 2 29   LYS 29   29   29   LYS LYS G . n 
B 2 30   LYS 30   30   30   LYS LYS G . n 
B 2 31   TRP 31   31   31   TRP TRP G . n 
B 2 32   GLU 32   32   32   GLU GLU G . n 
B 2 33   ASN 33   33   33   ASN ASN G . n 
B 2 34   PRO 34   34   34   PRO PRO G . n 
B 2 35   ALA 35   35   35   ALA ALA G . n 
B 2 36   GLN 36   36   36   GLN GLN G . n 
B 2 37   ASN 37   37   37   ASN ASN G . n 
B 2 38   THR 38   38   38   THR THR G . n 
B 2 39   ALA 39   39   39   ALA ALA G . n 
B 2 40   HIS 40   40   40   HIS HIS G . n 
B 2 41   LEU 41   41   41   LEU LEU G . n 
B 2 42   ASP 42   42   42   ASP ASP G . n 
B 2 43   GLN 43   43   43   GLN GLN G . n 
B 2 44   PHE 44   44   44   PHE PHE G . n 
B 2 45   GLU 45   45   45   GLU GLU G . n 
B 2 46   ARG 46   46   46   ARG ARG G . n 
B 2 47   ILE 47   47   47   ILE ILE G . n 
B 2 48   LYS 48   48   48   LYS LYS G . n 
B 2 49   THR 49   49   49   THR THR G . n 
B 2 50   LEU 50   50   50   LEU LEU G . n 
B 2 51   GLY 51   51   51   GLY GLY G . n 
B 2 52   THR 52   52   52   THR THR G . n 
B 2 53   GLY 53   53   53   GLY GLY G . n 
B 2 54   SER 54   54   54   SER SER G . n 
B 2 55   PHE 55   55   55   PHE PHE G . n 
B 2 56   GLY 56   56   56   GLY GLY G . n 
B 2 57   ARG 57   57   57   ARG ARG G . n 
B 2 58   VAL 58   58   58   VAL VAL G . n 
B 2 59   MET 59   59   59   MET MET G . n 
B 2 60   LEU 60   60   60   LEU LEU G . n 
B 2 61   VAL 61   61   61   VAL VAL G . n 
B 2 62   LYS 62   62   62   LYS LYS G . n 
B 2 63   HIS 63   63   63   HIS HIS G . n 
B 2 64   MET 64   64   64   MET MET G . n 
B 2 65   GLU 65   65   65   GLU GLU G . n 
B 2 66   THR 66   66   66   THR THR G . n 
B 2 67   GLY 67   67   67   GLY GLY G . n 
B 2 68   ASN 68   68   68   ASN ASN G . n 
B 2 69   HIS 69   69   69   HIS HIS G . n 
B 2 70   TYR 70   70   70   TYR TYR G . n 
B 2 71   ALA 71   71   71   ALA ALA G . n 
B 2 72   MET 72   72   72   MET MET G . n 
B 2 73   LYS 73   73   73   LYS LYS G . n 
B 2 74   ILE 74   74   74   ILE ILE G . n 
B 2 75   LEU 75   75   75   LEU LEU G . n 
B 2 76   ASP 76   76   76   ASP ASP G . n 
B 2 77   LYS 77   77   77   LYS LYS G . n 
B 2 78   GLN 78   78   78   GLN GLN G . n 
B 2 79   LYS 79   79   79   LYS LYS G . n 
B 2 80   VAL 80   80   80   VAL VAL G . n 
B 2 81   VAL 81   81   81   VAL VAL G . n 
B 2 82   LYS 82   82   82   LYS LYS G . n 
B 2 83   LEU 83   83   83   LEU LEU G . n 
B 2 84   LYS 84   84   84   LYS LYS G . n 
B 2 85   GLN 85   85   85   GLN GLN G . n 
B 2 86   ILE 86   86   86   ILE ILE G . n 
B 2 87   GLU 87   87   87   GLU GLU G . n 
B 2 88   HIS 88   88   88   HIS HIS G . n 
B 2 89   THR 89   89   89   THR THR G . n 
B 2 90   LEU 90   90   90   LEU LEU G . n 
B 2 91   ASN 91   91   91   ASN ASN G . n 
B 2 92   GLU 92   92   92   GLU GLU G . n 
B 2 93   LYS 93   93   93   LYS LYS G . n 
B 2 94   ARG 94   94   94   ARG ARG G . n 
B 2 95   ILE 95   95   95   ILE ILE G . n 
B 2 96   LEU 96   96   96   LEU LEU G . n 
B 2 97   GLN 97   97   97   GLN GLN G . n 
B 2 98   ALA 98   98   98   ALA ALA G . n 
B 2 99   VAL 99   99   99   VAL VAL G . n 
B 2 100  ASN 100  100  100  ASN ASN G . n 
B 2 101  PHE 101  101  101  PHE PHE G . n 
B 2 102  PRO 102  102  102  PRO PRO G . n 
B 2 103  PHE 103  103  103  PHE PHE G . n 
B 2 104  LEU 104  104  104  LEU LEU G . n 
B 2 105  VAL 105  105  105  VAL VAL G . n 
B 2 106  LYS 106  106  106  LYS LYS G . n 
B 2 107  LEU 107  107  107  LEU LEU G . n 
B 2 108  GLU 108  108  108  GLU GLU G . n 
B 2 109  PHE 109  109  109  PHE PHE G . n 
B 2 110  SER 110  110  110  SER SER G . n 
B 2 111  PHE 111  111  111  PHE PHE G . n 
B 2 112  LYS 112  112  112  LYS LYS G . n 
B 2 113  ASP 113  113  113  ASP ASP G . n 
B 2 114  ASN 114  114  114  ASN ASN G . n 
B 2 115  SER 115  115  115  SER SER G . n 
B 2 116  ASN 116  116  116  ASN ASN G . n 
B 2 117  LEU 117  117  117  LEU LEU G . n 
B 2 118  TYR 118  118  118  TYR TYR G . n 
B 2 119  MET 119  119  119  MET MET G . n 
B 2 120  VAL 120  120  120  VAL VAL G . n 
B 2 121  MET 121  121  121  MET MET G . n 
B 2 122  GLU 122  122  122  GLU GLU G . n 
B 2 123  TYR 123  123  123  TYR TYR G . n 
B 2 124  VAL 124  124  124  VAL VAL G . n 
B 2 125  PRO 125  125  125  PRO PRO G . n 
B 2 126  GLY 126  126  126  GLY GLY G . n 
B 2 127  GLY 127  127  127  GLY GLY G . n 
B 2 128  GLU 128  128  128  GLU GLU G . n 
B 2 129  MET 129  129  129  MET MET G . n 
B 2 130  PHE 130  130  130  PHE PHE G . n 
B 2 131  SER 131  131  131  SER SER G . n 
B 2 132  HIS 132  132  132  HIS HIS G . n 
B 2 133  LEU 133  133  133  LEU LEU G . n 
B 2 134  ARG 134  134  134  ARG ARG G . n 
B 2 135  ARG 135  135  135  ARG ARG G . n 
B 2 136  ILE 136  136  136  ILE ILE G . n 
B 2 137  GLY 137  137  137  GLY GLY G . n 
B 2 138  ARG 138  138  138  ARG ARG G . n 
B 2 139  PHE 139  139  139  PHE PHE G . n 
B 2 140  SER 140  140  140  SER SER G . n 
B 2 141  GLU 141  141  141  GLU GLU G . n 
B 2 142  PRO 142  142  142  PRO PRO G . n 
B 2 143  HIS 143  143  143  HIS HIS G . n 
B 2 144  ALA 144  144  144  ALA ALA G . n 
B 2 145  ARG 145  145  145  ARG ARG G . n 
B 2 146  PHE 146  146  146  PHE PHE G . n 
B 2 147  TYR 147  147  147  TYR TYR G . n 
B 2 148  ALA 148  148  148  ALA ALA G . n 
B 2 149  ALA 149  149  149  ALA ALA G . n 
B 2 150  GLN 150  150  150  GLN GLN G . n 
B 2 151  ILE 151  151  151  ILE ILE G . n 
B 2 152  VAL 152  152  152  VAL VAL G . n 
B 2 153  LEU 153  153  153  LEU LEU G . n 
B 2 154  THR 154  154  154  THR THR G . n 
B 2 155  PHE 155  155  155  PHE PHE G . n 
B 2 156  GLU 156  156  156  GLU GLU G . n 
B 2 157  TYR 157  157  157  TYR TYR G . n 
B 2 158  LEU 158  158  158  LEU LEU G . n 
B 2 159  HIS 159  159  159  HIS HIS G . n 
B 2 160  SER 160  160  160  SER SER G . n 
B 2 161  LEU 161  161  161  LEU LEU G . n 
B 2 162  ASP 162  162  162  ASP ASP G . n 
B 2 163  LEU 163  163  163  LEU LEU G . n 
B 2 164  ILE 164  164  164  ILE ILE G . n 
B 2 165  TYR 165  165  165  TYR TYR G . n 
B 2 166  ARG 166  166  166  ARG ARG G . n 
B 2 167  ASP 167  167  167  ASP ASP G . n 
B 2 168  LEU 168  168  168  LEU LEU G . n 
B 2 169  LYS 169  169  169  LYS LYS G . n 
B 2 170  PRO 170  170  170  PRO PRO G . n 
B 2 171  GLU 171  171  171  GLU GLU G . n 
B 2 172  ASN 172  172  172  ASN ASN G . n 
B 2 173  LEU 173  173  173  LEU LEU G . n 
B 2 174  LEU 174  174  174  LEU LEU G . n 
B 2 175  ILE 175  175  175  ILE ILE G . n 
B 2 176  ASP 176  176  176  ASP ASP G . n 
B 2 177  GLN 177  177  177  GLN GLN G . n 
B 2 178  GLN 178  178  178  GLN GLN G . n 
B 2 179  GLY 179  179  179  GLY GLY G . n 
B 2 180  TYR 180  180  180  TYR TYR G . n 
B 2 181  ILE 181  181  181  ILE ILE G . n 
B 2 182  GLN 182  182  182  GLN GLN G . n 
B 2 183  VAL 183  183  183  VAL VAL G . n 
B 2 184  THR 184  184  184  THR THR G . n 
B 2 185  ASP 185  185  185  ASP ASP G . n 
B 2 186  PHE 186  186  186  PHE PHE G . n 
B 2 187  GLY 187  187  187  GLY GLY G . n 
B 2 188  PHE 188  188  188  PHE PHE G . n 
B 2 189  ALA 189  189  189  ALA ALA G . n 
B 2 190  LYS 190  190  190  LYS LYS G . n 
B 2 191  ARG 191  191  191  ARG ARG G . n 
B 2 192  VAL 192  192  192  VAL VAL G . n 
B 2 193  LYS 193  193  193  LYS LYS G . n 
B 2 194  GLY 194  194  194  GLY GLY G . n 
B 2 195  ARG 195  195  195  ARG ARG G . n 
B 2 196  THR 196  196  196  THR THR G . n 
B 2 197  TRP 197  197  197  TRP TRP G . n 
B 2 198  TPO 198  198  198  TPO TPO G . n 
B 2 199  LEU 199  199  199  LEU LEU G . n 
B 2 200  CYS 200  200  200  CYS CYS G . n 
B 2 201  GLY 201  201  201  GLY GLY G . n 
B 2 202  THR 202  202  202  THR THR G . n 
B 2 203  PRO 203  203  203  PRO PRO G . n 
B 2 204  GLU 204  204  204  GLU GLU G . n 
B 2 205  TYR 205  205  205  TYR TYR G . n 
B 2 206  LEU 206  206  206  LEU LEU G . n 
B 2 207  ALA 207  207  207  ALA ALA G . n 
B 2 208  PRO 208  208  208  PRO PRO G . n 
B 2 209  GLU 209  209  209  GLU GLU G . n 
B 2 210  ILE 210  210  210  ILE ILE G . n 
B 2 211  ILE 211  211  211  ILE ILE G . n 
B 2 212  LEU 212  212  212  LEU LEU G . n 
B 2 213  SER 213  213  213  SER SER G . n 
B 2 214  LYS 214  214  214  LYS LYS G . n 
B 2 215  GLY 215  215  215  GLY GLY G . n 
B 2 216  TYR 216  216  216  TYR TYR G . n 
B 2 217  ASN 217  217  217  ASN ASN G . n 
B 2 218  LYS 218  218  218  LYS LYS G . n 
B 2 219  ALA 219  219  219  ALA ALA G . n 
B 2 220  VAL 220  220  220  VAL VAL G . n 
B 2 221  ASP 221  221  221  ASP ASP G . n 
B 2 222  TRP 222  222  222  TRP TRP G . n 
B 2 223  TRP 223  223  223  TRP TRP G . n 
B 2 224  ALA 224  224  224  ALA ALA G . n 
B 2 225  LEU 225  225  225  LEU LEU G . n 
B 2 226  GLY 226  226  226  GLY GLY G . n 
B 2 227  VAL 227  227  227  VAL VAL G . n 
B 2 228  LEU 228  228  228  LEU LEU G . n 
B 2 229  ILE 229  229  229  ILE ILE G . n 
B 2 230  TYR 230  230  230  TYR TYR G . n 
B 2 231  GLU 231  231  231  GLU GLU G . n 
B 2 232  MET 232  232  232  MET MET G . n 
B 2 233  ALA 233  233  233  ALA ALA G . n 
B 2 234  ALA 234  234  234  ALA ALA G . n 
B 2 235  GLY 235  235  235  GLY GLY G . n 
B 2 236  TYR 236  236  236  TYR TYR G . n 
B 2 237  PRO 237  237  237  PRO PRO G . n 
B 2 238  PRO 238  238  238  PRO PRO G . n 
B 2 239  PHE 239  239  239  PHE PHE G . n 
B 2 240  PHE 240  240  240  PHE PHE G . n 
B 2 241  ALA 241  241  241  ALA ALA G . n 
B 2 242  ASP 242  242  242  ASP ASP G . n 
B 2 243  GLN 243  243  243  GLN GLN G . n 
B 2 244  PRO 244  244  244  PRO PRO G . n 
B 2 245  ILE 245  245  245  ILE ILE G . n 
B 2 246  GLN 246  246  246  GLN GLN G . n 
B 2 247  ILE 247  247  247  ILE ILE G . n 
B 2 248  TYR 248  248  248  TYR TYR G . n 
B 2 249  GLU 249  249  249  GLU GLU G . n 
B 2 250  LYS 250  250  250  LYS LYS G . n 
B 2 251  ILE 251  251  251  ILE ILE G . n 
B 2 252  VAL 252  252  252  VAL VAL G . n 
B 2 253  SER 253  253  253  SER SER G . n 
B 2 254  GLY 254  254  254  GLY GLY G . n 
B 2 255  LYS 255  255  255  LYS LYS G . n 
B 2 256  VAL 256  256  256  VAL VAL G . n 
B 2 257  ARG 257  257  257  ARG ARG G . n 
B 2 258  PHE 258  258  258  PHE PHE G . n 
B 2 259  PRO 259  259  259  PRO PRO G . n 
B 2 260  SER 260  260  260  SER SER G . n 
B 2 261  HIS 261  261  261  HIS HIS G . n 
B 2 262  PHE 262  262  262  PHE PHE G . n 
B 2 263  SER 263  263  263  SER SER G . n 
B 2 264  SER 264  264  264  SER SER G . n 
B 2 265  ASP 265  265  265  ASP ASP G . n 
B 2 266  LEU 266  266  266  LEU LEU G . n 
B 2 267  LYS 267  267  267  LYS LYS G . n 
B 2 268  ASP 268  268  268  ASP ASP G . n 
B 2 269  LEU 269  269  269  LEU LEU G . n 
B 2 270  LEU 270  270  270  LEU LEU G . n 
B 2 271  ARG 271  271  271  ARG ARG G . n 
B 2 272  ASN 272  272  272  ASN ASN G . n 
B 2 273  LEU 273  273  273  LEU LEU G . n 
B 2 274  LEU 274  274  274  LEU LEU G . n 
B 2 275  GLN 275  275  275  GLN GLN G . n 
B 2 276  VAL 276  276  276  VAL VAL G . n 
B 2 277  ASP 277  277  277  ASP ASP G . n 
B 2 278  LEU 278  278  278  LEU LEU G . n 
B 2 279  THR 279  279  279  THR THR G . n 
B 2 280  LYS 280  280  280  LYS LYS G . n 
B 2 281  ARG 281  281  281  ARG ARG G . n 
B 2 282  PHE 282  282  282  PHE PHE G . n 
B 2 283  GLY 283  283  283  GLY GLY G . n 
B 2 284  ASN 284  284  284  ASN ASN G . n 
B 2 285  LEU 285  285  285  LEU LEU G . n 
B 2 286  LYS 286  286  286  LYS LYS G . n 
B 2 287  ASN 287  287  287  ASN ASN G . n 
B 2 288  GLY 288  288  288  GLY GLY G . n 
B 2 289  VAL 289  289  289  VAL VAL G . n 
B 2 290  ASN 290  290  290  ASN ASN G . n 
B 2 291  ASP 291  291  291  ASP ASP G . n 
B 2 292  ILE 292  292  292  ILE ILE G . n 
B 2 293  LYS 293  293  293  LYS LYS G . n 
B 2 294  ASN 294  294  294  ASN ASN G . n 
B 2 295  HIS 295  295  295  HIS HIS G . n 
B 2 296  LYS 296  296  296  LYS LYS G . n 
B 2 297  TRP 297  297  297  TRP TRP G . n 
B 2 298  PHE 298  298  298  PHE PHE G . n 
B 2 299  ALA 299  299  299  ALA ALA G . n 
B 2 300  THR 300  300  300  THR THR G . n 
B 2 301  THR 301  301  301  THR THR G . n 
B 2 302  ASP 302  302  302  ASP ASP G . n 
B 2 303  TRP 303  303  303  TRP TRP G . n 
B 2 304  ILE 304  304  304  ILE ILE G . n 
B 2 305  ALA 305  305  305  ALA ALA G . n 
B 2 306  ILE 306  306  306  ILE ILE G . n 
B 2 307  TYR 307  307  307  TYR TYR G . n 
B 2 308  GLN 308  308  308  GLN GLN G . n 
B 2 309  ARG 309  309  309  ARG ARG G . n 
B 2 310  LYS 310  310  310  LYS LYS G . n 
B 2 311  VAL 311  311  311  VAL VAL G . n 
B 2 312  GLU 312  312  312  GLU GLU G . n 
B 2 313  ALA 313  313  313  ALA ALA G . n 
B 2 314  PRO 314  314  314  PRO PRO G . n 
B 2 315  PHE 315  315  315  PHE PHE G . n 
B 2 316  ILE 316  316  316  ILE ILE G . n 
B 2 317  PRO 317  317  317  PRO PRO G . n 
B 2 318  LYS 318  318  318  LYS LYS G . n 
B 2 319  PHE 319  319  319  PHE PHE G . n 
B 2 320  LYS 320  320  320  LYS LYS G . n 
B 2 321  GLY 321  321  321  GLY GLY G . n 
B 2 322  PRO 322  322  322  PRO PRO G . n 
B 2 323  GLY 323  323  323  GLY GLY G . n 
B 2 324  ASP 324  324  324  ASP ASP G . n 
B 2 325  THR 325  325  325  THR THR G . n 
B 2 326  SER 326  326  326  SER SER G . n 
B 2 327  ASN 327  327  327  ASN ASN G . n 
B 2 328  PHE 328  328  328  PHE PHE G . n 
B 2 329  ASP 329  329  329  ASP ASP G . n 
B 2 330  ASP 330  330  330  ASP ASP G . n 
B 2 331  TYR 331  331  331  TYR TYR G . n 
B 2 332  GLU 332  332  ?    ?   ?   G . n 
B 2 333  GLU 333  333  ?    ?   ?   G . n 
B 2 334  GLU 334  334  ?    ?   ?   G . n 
B 2 335  GLU 335  335  ?    ?   ?   G . n 
B 2 336  ILE 336  336  ?    ?   ?   G . n 
B 2 337  ARG 337  337  ?    ?   ?   G . n 
B 2 338  VAL 338  338  ?    ?   ?   G . n 
B 2 339  SER 339  339  ?    ?   ?   G . n 
B 2 340  ILE 340  340  ?    ?   ?   G . n 
B 2 341  ASN 341  341  ?    ?   ?   G . n 
B 2 342  GLU 342  342  ?    ?   ?   G . n 
B 2 343  LYS 343  343  343  LYS LYS G . n 
B 2 344  CYS 344  344  344  CYS CYS G . n 
B 2 345  GLY 345  345  345  GLY GLY G . n 
B 2 346  LYS 346  346  346  LYS LYS G . n 
B 2 347  GLU 347  347  347  GLU GLU G . n 
B 2 348  PHE 348  348  348  PHE PHE G . n 
B 2 349  SER 349  349  349  SER SER G . n 
B 2 350  GLU 350  350  350  GLU GLU G . n 
B 2 351  PHE 351  351  351  PHE PHE G . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        ATP 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   ATP 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 3 CLR 1 1501 1501 CLR CLR A . 
D 4 D10 1 1502 1701 D10 POV A . 
E 5 MG  1 1503 1    MG  MG  A . 
F 5 MG  1 1504 2    MG  MG  A . 
G 6 ATP 1 1505 3    ATP ATP A . 
H 6 ATP 1 1506 4    ATP ATP A . 
I 7 CL  1 1507 1    CL  CL  A . 
J 7 CL  1 1508 2    CL  CL  A . 
K 7 CL  1 1509 3    CL  CL  A . 
L 7 CL  1 1510 4    CL  CL  A . 
M 8 UND 1 1511 1509 UND POV A . 
N 8 UND 1 1512 1510 UND POV A . 
O 8 UND 1 1513 1511 UND POV A . 
P 4 D10 1 1514 1512 D10 POV A . 
Q 4 D10 1 1515 1513 D10 POV A . 
R 4 D10 1 1516 1514 D10 POV A . 
S 6 ATP 1 401  401  ATP ATP G . 
T 5 MG  1 402  1    MG  MG  G . 
U 5 MG  1 403  2    MG  MG  G . 
V 9 HOH 1 1601 2    HOH HOH A . 
V 9 HOH 2 1602 1    HOH HOH A . 
V 9 HOH 3 1603 1    HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A GLU 402 ? CG  ? A GLU 402 CG  
2  1 Y 1 A GLU 402 ? CD  ? A GLU 402 CD  
3  1 Y 1 A GLU 402 ? OE1 ? A GLU 402 OE1 
4  1 Y 1 A GLU 402 ? OE2 ? A GLU 402 OE2 
5  1 Y 1 A TYR 903 ? CG  ? A TYR 903 CG  
6  1 Y 1 A TYR 903 ? CD1 ? A TYR 903 CD1 
7  1 Y 1 A TYR 903 ? CD2 ? A TYR 903 CD2 
8  1 Y 1 A TYR 903 ? CE1 ? A TYR 903 CE1 
9  1 Y 1 A TYR 903 ? CE2 ? A TYR 903 CE2 
10 1 Y 1 A TYR 903 ? CZ  ? A TYR 903 CZ  
11 1 Y 1 A TYR 903 ? OH  ? A TYR 903 OH  
12 1 Y 1 G GLN 13  ? CG  ? B GLN 13  CG  
13 1 Y 1 G GLN 13  ? CD  ? B GLN 13  CD  
14 1 Y 1 G GLN 13  ? OE1 ? B GLN 13  OE1 
15 1 Y 1 G GLN 13  ? NE2 ? B GLN 13  NE2 
16 1 Y 1 G GLU 14  ? CG  ? B GLU 14  CG  
17 1 Y 1 G GLU 14  ? CD  ? B GLU 14  CD  
18 1 Y 1 G GLU 14  ? OE1 ? B GLU 14  OE1 
19 1 Y 1 G GLU 14  ? OE2 ? B GLU 14  OE2 
20 1 Y 1 G PRO 34  ? CG  ? B PRO 34  CG  
21 1 Y 1 G PRO 34  ? CD  ? B PRO 34  CD  
22 1 Y 1 G GLN 36  ? CG  ? B GLN 36  CG  
23 1 Y 1 G GLN 36  ? CD  ? B GLN 36  CD  
24 1 Y 1 G GLN 36  ? OE1 ? B GLN 36  OE1 
25 1 Y 1 G GLN 36  ? NE2 ? B GLN 36  NE2 
26 1 Y 1 G ASN 37  ? CG  ? B ASN 37  CG  
27 1 Y 1 G ASN 37  ? OD1 ? B ASN 37  OD1 
28 1 Y 1 G ASN 37  ? ND2 ? B ASN 37  ND2 
29 1 Y 1 G THR 38  ? OG1 ? B THR 38  OG1 
30 1 Y 1 G THR 38  ? CG2 ? B THR 38  CG2 
31 1 Y 1 G HIS 40  ? CG  ? B HIS 40  CG  
32 1 Y 1 G HIS 40  ? ND1 ? B HIS 40  ND1 
33 1 Y 1 G HIS 40  ? CD2 ? B HIS 40  CD2 
34 1 Y 1 G HIS 40  ? CE1 ? B HIS 40  CE1 
35 1 Y 1 G HIS 40  ? NE2 ? B HIS 40  NE2 
36 1 Y 1 G LEU 41  ? CG  ? B LEU 41  CG  
37 1 Y 1 G LEU 41  ? CD1 ? B LEU 41  CD1 
38 1 Y 1 G LEU 41  ? CD2 ? B LEU 41  CD2 
39 1 Y 1 G ASP 42  ? CG  ? B ASP 42  CG  
40 1 Y 1 G ASP 42  ? OD1 ? B ASP 42  OD1 
41 1 Y 1 G ASP 42  ? OD2 ? B ASP 42  OD2 
42 1 Y 1 G GLN 43  ? CG  ? B GLN 43  CG  
43 1 Y 1 G GLN 43  ? CD  ? B GLN 43  CD  
44 1 Y 1 G GLN 43  ? OE1 ? B GLN 43  OE1 
45 1 Y 1 G GLN 43  ? NE2 ? B GLN 43  NE2 
46 1 Y 1 G PHE 44  ? CG  ? B PHE 44  CG  
47 1 Y 1 G PHE 44  ? CD1 ? B PHE 44  CD1 
48 1 Y 1 G PHE 44  ? CD2 ? B PHE 44  CD2 
49 1 Y 1 G PHE 44  ? CE1 ? B PHE 44  CE1 
50 1 Y 1 G PHE 44  ? CE2 ? B PHE 44  CE2 
51 1 Y 1 G PHE 44  ? CZ  ? B PHE 44  CZ  
52 1 Y 1 G ASP 76  ? CG  ? B ASP 76  CG  
53 1 Y 1 G ASP 76  ? OD1 ? B ASP 76  OD1 
54 1 Y 1 G ASP 76  ? OD2 ? B ASP 76  OD2 
55 1 Y 1 G PHE 319 ? CG  ? B PHE 319 CG  
56 1 Y 1 G PHE 319 ? CD1 ? B PHE 319 CD1 
57 1 Y 1 G PHE 319 ? CD2 ? B PHE 319 CD2 
58 1 Y 1 G PHE 319 ? CE1 ? B PHE 319 CE1 
59 1 Y 1 G PHE 319 ? CE2 ? B PHE 319 CE2 
60 1 Y 1 G PHE 319 ? CZ  ? B PHE 319 CZ  
61 1 Y 1 G LYS 320 ? CG  ? B LYS 320 CG  
62 1 Y 1 G LYS 320 ? CD  ? B LYS 320 CD  
63 1 Y 1 G LYS 320 ? CE  ? B LYS 320 CE  
64 1 Y 1 G LYS 320 ? NZ  ? B LYS 320 NZ  
65 1 Y 1 G PRO 322 ? CG  ? B PRO 322 CG  
66 1 Y 1 G PRO 322 ? CD  ? B PRO 322 CD  
67 1 Y 1 G ASP 324 ? CG  ? B ASP 324 CG  
68 1 Y 1 G ASP 324 ? OD1 ? B ASP 324 OD1 
69 1 Y 1 G ASP 324 ? OD2 ? B ASP 324 OD2 
70 1 Y 1 G THR 325 ? OG1 ? B THR 325 OG1 
71 1 Y 1 G THR 325 ? CG2 ? B THR 325 CG2 
72 1 Y 1 G SER 326 ? OG  ? B SER 326 OG  
73 1 Y 1 G CYS 344 ? SG  ? B CYS 344 SG  
74 1 Y 1 G LYS 346 ? CG  ? B LYS 346 CG  
75 1 Y 1 G LYS 346 ? CD  ? B LYS 346 CD  
76 1 Y 1 G LYS 346 ? CE  ? B LYS 346 CE  
77 1 Y 1 G LYS 346 ? NZ  ? B LYS 346 NZ  
78 1 Y 1 G GLU 347 ? CG  ? B GLU 347 CG  
79 1 Y 1 G GLU 347 ? CD  ? B GLU 347 CD  
80 1 Y 1 G GLU 347 ? OE1 ? B GLU 347 OE1 
81 1 Y 1 G GLU 347 ? OE2 ? B GLU 347 OE2 
82 1 Y 1 G SER 349 ? OG  ? B SER 349 OG  
83 1 Y 1 G GLU 350 ? CG  ? B GLU 350 CG  
84 1 Y 1 G GLU 350 ? CD  ? B GLU 350 CD  
85 1 Y 1 G GLU 350 ? OE1 ? B GLU 350 OE1 
86 1 Y 1 G GLU 350 ? OE2 ? B GLU 350 OE2 
# 
_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                     9DW9 
_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                         9DW9 
_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                   9DW9 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_refine.pdbx_refine_id                           'ELECTRON MICROSCOPY' 
_refine.entry_id                                 9DW9 
_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' ? 0.003 ? 12498 ? f_bond_d           ? ? 
'ELECTRON MICROSCOPY' ? 0.559 ? 16908 ? f_angle_d          ? ? 
'ELECTRON MICROSCOPY' ? 8.361 ? 1770  ? f_dihedral_angle_d ? ? 
'ELECTRON MICROSCOPY' ? 0.041 ? 1915  ? f_chiral_restr     ? ? 
'ELECTRON MICROSCOPY' ? 0.003 ? 2077  ? f_plane_restr      ? ? 
# 
_struct.entry_id                     9DW9 
_struct.title                        'Phosphorylated (E1371Q)CFTR in complex with PKA-C' 
_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        9DW9 
_struct_keywords.text            'CFTR, PKA, complex, HYDROLASE' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
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 ? 
E N N 5 ? 
F N N 5 ? 
G N N 6 ? 
H N N 6 ? 
I N N 7 ? 
J N N 7 ? 
K N N 7 ? 
L N N 7 ? 
M N N 8 ? 
N N N 8 ? 
O N N 8 ? 
P N N 4 ? 
Q N N 4 ? 
R N N 4 ? 
S N N 6 ? 
T N N 5 ? 
U N N 5 ? 
V N N 9 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP CFTR_HUMAN  P13569 ? 1 
;MQRSPLEKASVVSKLFFSWTRPILRKGYRQRLELSDIYQIPSVDSADNLSEKLEREWDRELASKKNPKLINALRRCFFWR
FMFYGIFLYLGEVTKAVQPLLLGRIIASYDPDNKEERSIAIYLGIGLCLLFIVRTLLLHPAIFGLHHIGMQMRIAMFSLI
YKKTLKLSSRVLDKISIGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVALLMGLIWELLQASAFCGLGFLIVLALFQAGL
GRMMMKYRDQRAGKISERLVITSEMIENIQSVKAYCWEEAMEKMIENLRQTELKLTRKAAYVRYFNSSAFFFSGFFVVFL
SVLPYALIKGIILRKIFTTISFCIVLRMAVTRQFPWAVQTWYDSLGAINKIQDFLQKQEYKTLEYNLTTTEVVMENVTAF
WEEGFGELFEKAKQNNNNRKTSNGDDSLFFSNFSLLGTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEG
KIKHSGRISFCSQFSWIMPGTIKENIIFGVSYDEYRYRSVIKACQLEEDISKFAEKDNIVLGEGGITLSGGQRARISLAR
AVYKDADLYLLDSPFGYLDVLTEKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQNLQPDF
SSKLMGCDSFDQFSAERRNSILTETLHRFSLEGDAPVSWTETKKQSFKQTGEFGEKRKNSILNPINSIRKFSIVQKTPLQ
MNGIEEDSDEPLERRLSLVPDSEQGEAILPRISVISTGPTLQARRRQSVLNLMTHSVNQGQNIHRKTTASTRKVSLAPQA
NLTELDIYSRRLSQETGLEISEEINEEDLKECFFDDMESIPAVTTWNTYLRYITVHKSLIFVLIWCLVIFLAEVAASLVV
LWLLGNTPLQDKGNSTHSRNNSYAVIITSTSSYYVFYIYVGVADTLLAMGFFRGLPLVHTLITVSKILHHKMLHSVLQAP
MSTLNTLKAGGILNRFSKDIAILDDLLPLTIFDFIQLLLIVIGAIAVVAVLQPYIFVATVPVIVAFIMLRAYFLQTSQQL
KQLESEGRSPIFTHLVTSLKGLWTLRAFGRQPYFETLFHKALNLHTANWFLYLSTLRWFQMRIEMIFVIFFIAVTFISIL
TTGEGEGRVGIILTLAMNIMSTLQWAVNSSIDVDSLMRSVSRVFKFIDMPTEGKPTKSTKPYKNGQLSKVMIIENSHVKK
DDIWPSGGQMTVKDLTAKYTEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGEIQIDGVSWDSITLQ
QWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSV
LSKAKILLLDEPSAHLDPVTYQIIRRTLKQAFADCTVILCEHRIEAMLECQQFLVIEENKVRQYDSIQKLLNERSLFRQA
ISPSDRVKLFPHRNSSKCKSKPQIAALKEETEEEVQDTRL
;
1 
2 UNP KAPCA_BOVIN P00517 ? 2 
;MGNAAAAKKGSEQESVKEFLAKAKEDFLKKWENPAQNTAHLDQFERIKTLGTGSFGRVMLVKHMETGNHYAMKILDKQKV
VKLKQIEHTLNEKRILQAVNFPFLVKLEFSFKDNSNLYMVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHS
LDLIYRDLKPENLLIDQQGYIQVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFF
ADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVNDIKNHKWFATTDWIAIYQRKVEAPFIPKFK
GPGDTSNFDDYEEEEIRVSINEKCGKEFSEF
;
1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9DW9 A 1 ? 1480 ? P13569 1 ? 1480 ? 1 1480 
2 2 9DW9 G 1 ? 351  ? P00517 1 ? 351  ? 1 351  
# 
_struct_ref_seq_dif.align_id                     1 
_struct_ref_seq_dif.pdbx_pdb_id_code             9DW9 
_struct_ref_seq_dif.mon_id                       GLN 
_struct_ref_seq_dif.pdbx_pdb_strand_id           A 
_struct_ref_seq_dif.seq_num                      1371 
_struct_ref_seq_dif.pdbx_pdb_ins_code            ? 
_struct_ref_seq_dif.pdbx_seq_db_name             UNP 
_struct_ref_seq_dif.pdbx_seq_db_accession_code   P13569 
_struct_ref_seq_dif.db_mon_id                    GLU 
_struct_ref_seq_dif.pdbx_seq_db_seq_num          1371 
_struct_ref_seq_dif.details                      'engineered mutation' 
_struct_ref_seq_dif.pdbx_auth_seq_num            1371 
_struct_ref_seq_dif.pdbx_ordinal                 1 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
_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,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U,V 
# 
_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   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0 
_pdbx_struct_oper_list.matrix[1][2]         0.0 
_pdbx_struct_oper_list.matrix[1][3]         0.0 
_pdbx_struct_oper_list.vector[1]            0.0 
_pdbx_struct_oper_list.matrix[2][1]         0.0 
_pdbx_struct_oper_list.matrix[2][2]         1.0 
_pdbx_struct_oper_list.matrix[2][3]         0.0 
_pdbx_struct_oper_list.vector[2]            0.0 
_pdbx_struct_oper_list.matrix[3][1]         0.0 
_pdbx_struct_oper_list.matrix[3][2]         0.0 
_pdbx_struct_oper_list.matrix[3][3]         1.0 
_pdbx_struct_oper_list.vector[3]            0.0 
# 
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 SER A 10   ? PHE A 16   ? SER A 10   PHE A 16   1 ? 7  
HELX_P HELX_P2  AA2 PHE A 17   ? TRP A 19   ? PHE A 17   TRP A 19   5 ? 3  
HELX_P HELX_P3  AA3 THR A 20   ? GLN A 30   ? THR A 20   GLN A 30   1 ? 11 
HELX_P HELX_P4  AA4 GLU A 33   ? ILE A 37   ? GLU A 33   ILE A 37   5 ? 5  
HELX_P HELX_P5  AA5 PRO A 41   ? ASP A 44   ? PRO A 41   ASP A 44   5 ? 4  
HELX_P HELX_P6  AA6 SER A 45   ? LYS A 64   ? SER A 45   LYS A 64   1 ? 20 
HELX_P HELX_P7  AA7 LYS A 68   ? SER A 108  ? LYS A 68   SER A 108  1 ? 41 
HELX_P HELX_P8  AA8 ASN A 113  ? SER A 118  ? ASN A 113  SER A 118  1 ? 6  
HELX_P HELX_P9  AA9 ILE A 119  ? LEU A 165  ? ILE A 119  LEU A 165  1 ? 47 
HELX_P HELX_P10 AB1 SER A 168  ? ASP A 173  ? SER A 168  ASP A 173  1 ? 6  
HELX_P HELX_P11 AB2 SER A 176  ? ASN A 186  ? SER A 176  ASN A 186  1 ? 11 
HELX_P HELX_P12 AB3 ASN A 189  ? ALA A 198  ? ASN A 189  ALA A 198  1 ? 10 
HELX_P HELX_P13 AB4 HIS A 199  ? GLU A 217  ? HIS A 199  GLU A 217  1 ? 19 
HELX_P HELX_P14 AB5 SER A 222  ? ASN A 268  ? SER A 222  ASN A 268  1 ? 47 
HELX_P HELX_P15 AB6 ASN A 268  ? CYS A 276  ? ASN A 268  CYS A 276  1 ? 9  
HELX_P HELX_P16 AB7 TRP A 277  ? SER A 308  ? TRP A 277  SER A 308  1 ? 32 
HELX_P HELX_P17 AB8 ALA A 309  ? PHE A 312  ? ALA A 309  PHE A 312  5 ? 4  
HELX_P HELX_P18 AB9 SER A 313  ? LYS A 329  ? SER A 313  LYS A 329  1 ? 17 
HELX_P HELX_P19 AC1 LEU A 333  ? ARG A 352  ? LEU A 333  ARG A 352  1 ? 20 
HELX_P HELX_P20 AC2 ARG A 352  ? LEU A 375  ? ARG A 352  LEU A 375  1 ? 24 
HELX_P HELX_P21 AC3 GLY A 463  ? MET A 472  ? GLY A 463  MET A 472  1 ? 10 
HELX_P HELX_P22 AC4 ILE A 502  ? PHE A 508  ? ILE A 502  PHE A 508  1 ? 7  
HELX_P HELX_P23 AC5 ASP A 513  ? CYS A 524  ? ASP A 513  CYS A 524  1 ? 12 
HELX_P HELX_P24 AC6 LEU A 526  ? PHE A 533  ? LEU A 526  PHE A 533  1 ? 8  
HELX_P HELX_P25 AC7 GLU A 535  ? ASN A 538  ? GLU A 535  ASN A 538  5 ? 4  
HELX_P HELX_P26 AC8 SER A 549  ? LYS A 564  ? SER A 549  LYS A 564  1 ? 16 
HELX_P HELX_P27 AC9 ASP A 579  ? CYS A 590  ? ASP A 579  CYS A 590  1 ? 12 
HELX_P HELX_P28 AD1 LYS A 606  ? LYS A 612  ? LYS A 606  LYS A 612  1 ? 7  
HELX_P HELX_P29 AD2 THR A 629  ? GLN A 634  ? THR A 629  GLN A 634  1 ? 6  
HELX_P HELX_P30 AD3 ASN A 825  ? LYS A 830  ? ASN A 825  LYS A 830  1 ? 6  
HELX_P HELX_P31 AD4 THR A 848  ? THR A 854  ? THR A 848  THR A 854  1 ? 7  
HELX_P HELX_P32 AD5 HIS A 856  ? LEU A 884  ? HIS A 856  LEU A 884  1 ? 29 
HELX_P HELX_P33 AD6 THR A 908  ? SER A 912  ? THR A 908  SER A 912  5 ? 5  
HELX_P HELX_P34 AD7 TYR A 913  ? LEU A 927  ? TYR A 913  LEU A 927  1 ? 15 
HELX_P HELX_P35 AD8 GLY A 930  ? GLN A 958  ? GLY A 930  GLN A 958  1 ? 29 
HELX_P HELX_P36 AD9 PRO A 960  ? LEU A 967  ? PRO A 960  LEU A 967  1 ? 8  
HELX_P HELX_P37 AE1 LYS A 968  ? GLN A 1012 ? LYS A 968  GLN A 1012 1 ? 45 
HELX_P HELX_P38 AE2 PRO A 1013 ? GLY A 1047 ? PRO A 1013 GLY A 1047 1 ? 35 
HELX_P HELX_P39 AE3 ARG A 1048 ? GLY A 1061 ? ARG A 1048 GLY A 1061 1 ? 14 
HELX_P HELX_P40 AE4 GLY A 1061 ? GLY A 1069 ? GLY A 1061 GLY A 1069 1 ? 9  
HELX_P HELX_P41 AE5 ARG A 1070 ? THR A 1122 ? ARG A 1070 THR A 1122 1 ? 53 
HELX_P HELX_P42 AE6 GLY A 1127 ? ASP A 1168 ? GLY A 1127 ASP A 1168 1 ? 42 
HELX_P HELX_P43 AE7 GLY A 1249 ? LEU A 1258 ? GLY A 1249 LEU A 1258 1 ? 10 
HELX_P HELX_P44 AE8 THR A 1278 ? LYS A 1284 ? THR A 1278 LYS A 1284 1 ? 7  
HELX_P HELX_P45 AE9 PHE A 1300 ? ASP A 1305 ? PHE A 1300 ASP A 1305 1 ? 6  
HELX_P HELX_P46 AF1 SER A 1311 ? GLY A 1323 ? SER A 1311 GLY A 1323 1 ? 13 
HELX_P HELX_P47 AF2 LEU A 1324 ? GLU A 1329 ? LEU A 1324 GLU A 1329 1 ? 6  
HELX_P HELX_P48 AF3 SER A 1347 ? SER A 1362 ? SER A 1347 SER A 1362 1 ? 16 
HELX_P HELX_P49 AF4 ASP A 1377 ? ALA A 1391 ? ASP A 1377 ALA A 1391 1 ? 15 
HELX_P HELX_P50 AF5 ILE A 1404 ? CYS A 1410 ? ILE A 1404 CYS A 1410 5 ? 7  
HELX_P HELX_P51 AF6 SER A 1426 ? ARG A 1434 ? SER A 1426 ARG A 1434 1 ? 9  
HELX_P HELX_P52 AF7 ARG A 1434 ? ALA A 1440 ? ARG A 1434 ALA A 1440 1 ? 7  
HELX_P HELX_P53 AF8 SER A 1442 ? PHE A 1450 ? SER A 1442 PHE A 1450 1 ? 9  
HELX_P HELX_P54 AF9 GLU B 14   ? ASN B 33   ? GLU G 14   ASN G 33   1 ? 20 
HELX_P HELX_P55 AG1 LYS B 77   ? LEU B 83   ? LYS G 77   LEU G 83   1 ? 7  
HELX_P HELX_P56 AG2 ILE B 86   ? GLN B 97   ? ILE G 86   GLN G 97   1 ? 12 
HELX_P HELX_P57 AG3 GLU B 128  ? GLY B 137  ? GLU G 128  GLY G 137  1 ? 10 
HELX_P HELX_P58 AG4 SER B 140  ? LEU B 161  ? SER G 140  LEU G 161  1 ? 22 
HELX_P HELX_P59 AG5 LYS B 169  ? GLU B 171  ? LYS G 169  GLU G 171  5 ? 3  
HELX_P HELX_P60 AG6 THR B 202  ? LEU B 206  ? THR G 202  LEU G 206  5 ? 5  
HELX_P HELX_P61 AG7 ALA B 207  ? LEU B 212  ? ALA G 207  LEU G 212  1 ? 6  
HELX_P HELX_P62 AG8 ALA B 219  ? GLY B 235  ? ALA G 219  GLY G 235  1 ? 17 
HELX_P HELX_P63 AG9 GLN B 243  ? GLY B 254  ? GLN G 243  GLY G 254  1 ? 12 
HELX_P HELX_P64 AH1 SER B 263  ? LEU B 274  ? SER G 263  LEU G 274  1 ? 12 
HELX_P HELX_P65 AH2 HIS B 295  ? ALA B 299  ? HIS G 295  ALA G 299  5 ? 5  
HELX_P HELX_P66 AH3 ASP B 302  ? ARG B 309  ? ASP G 302  ARG G 309  1 ? 8  
# 
_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 both ? A LEU 812  C   ? ? ? 1_555 A SEP 813 N   ? ? A LEU 812  A SEP 813  1_555 ? ? ? ? ? ? ? 1.327 ? ? 
covale2  covale both ? A SEP 813  C   ? ? ? 1_555 A GLN 814 N   ? ? A SEP 813  A GLN 814  1_555 ? ? ? ? ? ? ? 1.331 ? ? 
covale3  covale both ? B TRP 197  C   ? ? ? 1_555 B TPO 198 N   ? ? G TRP 197  G TPO 198  1_555 ? ? ? ? ? ? ? 1.328 ? ? 
covale4  covale both ? B TPO 198  C   ? ? ? 1_555 B LEU 199 N   ? ? G TPO 198  G LEU 199  1_555 ? ? ? ? ? ? ? 1.329 ? ? 
metalc1  metalc ?    ? A THR 465  OG1 ? ? ? 1_555 E MG  .   MG  ? ? A THR 465  A MG  1503 1_555 ? ? ? ? ? ? ? 2.017 ? ? 
metalc2  metalc ?    ? A GLN 493  OE1 ? ? ? 1_555 E MG  .   MG  ? ? A GLN 493  A MG  1503 1_555 ? ? ? ? ? ? ? 2.442 ? ? 
metalc3  metalc ?    ? A SER 1251 OG  ? ? ? 1_555 F MG  .   MG  ? ? A SER 1251 A MG  1504 1_555 ? ? ? ? ? ? ? 2.193 ? ? 
metalc4  metalc ?    ? A GLN 1291 OE1 ? ? ? 1_555 F MG  .   MG  ? ? A GLN 1291 A MG  1504 1_555 ? ? ? ? ? ? ? 2.759 ? ? 
metalc5  metalc ?    ? E MG  .    MG  ? ? ? 1_555 G ATP .   O2B ? ? A MG  1503 A ATP 1505 1_555 ? ? ? ? ? ? ? 2.377 ? ? 
metalc6  metalc ?    ? E MG  .    MG  ? ? ? 1_555 G ATP .   O3G ? ? A MG  1503 A ATP 1505 1_555 ? ? ? ? ? ? ? 2.364 ? ? 
metalc7  metalc ?    ? E MG  .    MG  ? ? ? 1_555 V HOH .   O   ? ? A MG  1503 A HOH 1601 1_555 ? ? ? ? ? ? ? 1.931 ? ? 
metalc8  metalc ?    ? E MG  .    MG  ? ? ? 1_555 V HOH .   O   ? ? A MG  1503 A HOH 1602 1_555 ? ? ? ? ? ? ? 2.021 ? ? 
metalc9  metalc ?    ? F MG  .    MG  ? ? ? 1_555 H ATP .   O3G ? ? A MG  1504 A ATP 1506 1_555 ? ? ? ? ? ? ? 2.524 ? ? 
metalc10 metalc ?    ? F MG  .    MG  ? ? ? 1_555 H ATP .   O2B ? ? A MG  1504 A ATP 1506 1_555 ? ? ? ? ? ? ? 2.492 ? ? 
metalc11 metalc ?    ? B ASN 172  OD1 ? ? ? 1_555 U MG  .   MG  ? ? G ASN 172  G MG  403  1_555 ? ? ? ? ? ? ? 2.219 ? ? 
metalc12 metalc ?    ? B ASP 185  OD1 ? ? ? 1_555 T MG  .   MG  ? ? G ASP 185  G MG  402  1_555 ? ? ? ? ? ? ? 2.286 ? ? 
metalc13 metalc ?    ? B ASP 185  OD2 ? ? ? 1_555 T MG  .   MG  ? ? G ASP 185  G MG  402  1_555 ? ? ? ? ? ? ? 2.995 ? ? 
metalc14 metalc ?    ? B ASP 185  OD2 ? ? ? 1_555 U MG  .   MG  ? ? G ASP 185  G MG  403  1_555 ? ? ? ? ? ? ? 2.169 ? ? 
metalc15 metalc ?    ? S ATP .    O3G ? ? ? 1_555 T MG  .   MG  ? ? G ATP 401  G MG  402  1_555 ? ? ? ? ? ? ? 2.228 ? ? 
metalc16 metalc ?    ? S ATP .    O2B ? ? ? 1_555 T MG  .   MG  ? ? G ATP 401  G MG  402  1_555 ? ? ? ? ? ? ? 2.416 ? ? 
metalc17 metalc ?    ? S ATP .    O2G ? ? ? 1_555 U MG  .   MG  ? ? G ATP 401  G MG  403  1_555 ? ? ? ? ? ? ? 2.252 ? ? 
metalc18 metalc ?    ? S ATP .    O2A ? ? ? 1_555 U MG  .   MG  ? ? G ATP 401  G MG  403  1_555 ? ? ? ? ? ? ? 2.203 ? ? 
# 
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  OG1 ? A THR 465  ? A THR 465  ? 1_555 MG ? E MG . ? A MG 1503 ? 1_555 OE1 ? A GLN 493  ? A GLN 493  ? 1_555 110.6 ? 
2  OG1 ? A THR 465  ? A THR 465  ? 1_555 MG ? E MG . ? A MG 1503 ? 1_555 O2B ? G ATP .    ? A ATP 1505 ? 1_555 77.4  ? 
3  OE1 ? A GLN 493  ? A GLN 493  ? 1_555 MG ? E MG . ? A MG 1503 ? 1_555 O2B ? G ATP .    ? A ATP 1505 ? 1_555 162.1 ? 
4  OG1 ? A THR 465  ? A THR 465  ? 1_555 MG ? E MG . ? A MG 1503 ? 1_555 O3G ? G ATP .    ? A ATP 1505 ? 1_555 153.5 ? 
5  OE1 ? A GLN 493  ? A GLN 493  ? 1_555 MG ? E MG . ? A MG 1503 ? 1_555 O3G ? G ATP .    ? A ATP 1505 ? 1_555 85.7  ? 
6  O2B ? G ATP .    ? A ATP 1505 ? 1_555 MG ? E MG . ? A MG 1503 ? 1_555 O3G ? G ATP .    ? A ATP 1505 ? 1_555 81.6  ? 
7  OG1 ? A THR 465  ? A THR 465  ? 1_555 MG ? E MG . ? A MG 1503 ? 1_555 O   ? V HOH .    ? A HOH 1601 ? 1_555 83.5  ? 
8  OE1 ? A GLN 493  ? A GLN 493  ? 1_555 MG ? E MG . ? A MG 1503 ? 1_555 O   ? V HOH .    ? A HOH 1601 ? 1_555 82.9  ? 
9  O2B ? G ATP .    ? A ATP 1505 ? 1_555 MG ? E MG . ? A MG 1503 ? 1_555 O   ? V HOH .    ? A HOH 1601 ? 1_555 82.1  ? 
10 O3G ? G ATP .    ? A ATP 1505 ? 1_555 MG ? E MG . ? A MG 1503 ? 1_555 O   ? V HOH .    ? A HOH 1601 ? 1_555 77.7  ? 
11 OG1 ? A THR 465  ? A THR 465  ? 1_555 MG ? E MG . ? A MG 1503 ? 1_555 O   ? V HOH .    ? A HOH 1602 ? 1_555 102.6 ? 
12 OE1 ? A GLN 493  ? A GLN 493  ? 1_555 MG ? E MG . ? A MG 1503 ? 1_555 O   ? V HOH .    ? A HOH 1602 ? 1_555 92.3  ? 
13 O2B ? G ATP .    ? A ATP 1505 ? 1_555 MG ? E MG . ? A MG 1503 ? 1_555 O   ? V HOH .    ? A HOH 1602 ? 1_555 101.7 ? 
14 O3G ? G ATP .    ? A ATP 1505 ? 1_555 MG ? E MG . ? A MG 1503 ? 1_555 O   ? V HOH .    ? A HOH 1602 ? 1_555 97.3  ? 
15 O   ? V HOH .    ? A HOH 1601 ? 1_555 MG ? E MG . ? A MG 1503 ? 1_555 O   ? V HOH .    ? A HOH 1602 ? 1_555 173.3 ? 
16 OG  ? A SER 1251 ? A SER 1251 ? 1_555 MG ? F MG . ? A MG 1504 ? 1_555 OE1 ? A GLN 1291 ? A GLN 1291 ? 1_555 97.9  ? 
17 OG  ? A SER 1251 ? A SER 1251 ? 1_555 MG ? F MG . ? A MG 1504 ? 1_555 O3G ? H ATP .    ? A ATP 1506 ? 1_555 149.5 ? 
18 OE1 ? A GLN 1291 ? A GLN 1291 ? 1_555 MG ? F MG . ? A MG 1504 ? 1_555 O3G ? H ATP .    ? A ATP 1506 ? 1_555 81.2  ? 
19 OG  ? A SER 1251 ? A SER 1251 ? 1_555 MG ? F MG . ? A MG 1504 ? 1_555 O2B ? H ATP .    ? A ATP 1506 ? 1_555 84.7  ? 
20 OE1 ? A GLN 1291 ? A GLN 1291 ? 1_555 MG ? F MG . ? A MG 1504 ? 1_555 O2B ? H ATP .    ? A ATP 1506 ? 1_555 145.6 ? 
21 O3G ? H ATP .    ? A ATP 1506 ? 1_555 MG ? F MG . ? A MG 1504 ? 1_555 O2B ? H ATP .    ? A ATP 1506 ? 1_555 79.8  ? 
22 OD1 ? B ASN 172  ? G ASN 172  ? 1_555 MG ? U MG . ? G MG 403  ? 1_555 OD2 ? B ASP 185  ? G ASP 185  ? 1_555 89.4  ? 
23 OD1 ? B ASN 172  ? G ASN 172  ? 1_555 MG ? U MG . ? G MG 403  ? 1_555 O2G ? S ATP .    ? G ATP 401  ? 1_555 113.7 ? 
24 OD2 ? B ASP 185  ? G ASP 185  ? 1_555 MG ? U MG . ? G MG 403  ? 1_555 O2G ? S ATP .    ? G ATP 401  ? 1_555 73.2  ? 
25 OD1 ? B ASN 172  ? G ASN 172  ? 1_555 MG ? U MG . ? G MG 403  ? 1_555 O2A ? S ATP .    ? G ATP 401  ? 1_555 139.0 ? 
26 OD2 ? B ASP 185  ? G ASP 185  ? 1_555 MG ? U MG . ? G MG 403  ? 1_555 O2A ? S ATP .    ? G ATP 401  ? 1_555 93.4  ? 
27 O2G ? S ATP .    ? G ATP 401  ? 1_555 MG ? U MG . ? G MG 403  ? 1_555 O2A ? S ATP .    ? G ATP 401  ? 1_555 106.2 ? 
28 OD1 ? B ASP 185  ? G ASP 185  ? 1_555 MG ? T MG . ? G MG 402  ? 1_555 OD2 ? B ASP 185  ? G ASP 185  ? 1_555 46.7  ? 
29 OD1 ? B ASP 185  ? G ASP 185  ? 1_555 MG ? T MG . ? G MG 402  ? 1_555 O3G ? S ATP .    ? G ATP 401  ? 1_555 116.0 ? 
30 OD2 ? B ASP 185  ? G ASP 185  ? 1_555 MG ? T MG . ? G MG 402  ? 1_555 O3G ? S ATP .    ? G ATP 401  ? 1_555 75.8  ? 
31 OD1 ? B ASP 185  ? G ASP 185  ? 1_555 MG ? T MG . ? G MG 402  ? 1_555 O2B ? S ATP .    ? G ATP 401  ? 1_555 70.4  ? 
32 OD2 ? B ASP 185  ? G ASP 185  ? 1_555 MG ? T MG . ? G MG 402  ? 1_555 O2B ? S ATP .    ? G ATP 401  ? 1_555 71.9  ? 
33 O3G ? S ATP .    ? G ATP 401  ? 1_555 MG ? T MG . ? G MG 402  ? 1_555 O2B ? S ATP .    ? G ATP 401  ? 1_555 66.5  ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 SEP A 813 ? . . . . SEP A 813 ? 1_555 . . . . . . . SER 1 SEP Phosphorylation 'Named protein modification' 
2 TPO B 198 ? . . . . TPO G 198 ? 1_555 . . . . . . . THR 1 TPO Phosphorylation 'Named protein modification' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 3 ? 
AA3 ? 6 ? 
AA4 ? 2 ? 
AA5 ? 4 ? 
AA6 ? 6 ? 
AA7 ? 2 ? 
AA8 ? 4 ? 
AA9 ? 2 ? 
AB1 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA3 4 5 ? parallel      
AA3 5 6 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA6 1 2 ? parallel      
AA6 2 3 ? parallel      
AA6 3 4 ? parallel      
AA6 4 5 ? parallel      
AA6 5 6 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA8 2 3 ? anti-parallel 
AA8 3 4 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AB1 1 2 ? anti-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 ILE A 331  ? ILE A 332  ? ILE A 331  ILE A 332  
AA1 2 VAL A 905  ? ILE A 906  ? VAL A 905  ILE A 906  
AA2 1 LEU A 441  ? GLU A 449  ? LEU A 441  GLU A 449  
AA2 2 GLU A 391  ? ALA A 399  ? GLU A 391  ALA A 399  
AA2 3 GLU A 479  ? LYS A 483  ? GLU A 479  LYS A 483  
AA3 1 ILE A 488  ? CYS A 491  ? ILE A 488  CYS A 491  
AA3 2 LEU A 568  ? ASP A 572  ? LEU A 568  ASP A 572  
AA3 3 THR A 599  ? VAL A 603  ? THR A 599  VAL A 603  
AA3 4 LEU A 453  ? GLY A 458  ? LEU A 453  GLY A 458  
AA3 5 LYS A 615  ? HIS A 620  ? LYS A 615  HIS A 620  
AA3 6 SER A 623  ? GLY A 628  ? SER A 623  GLY A 628  
AA4 1 GLY A 500  ? THR A 501  ? GLY A 500  THR A 501  
AA4 2 VAL A 540  ? LEU A 541  ? VAL A 540  LEU A 541  
AA5 1 LEU A 1227 ? ILE A 1234 ? LEU A 1227 ILE A 1234 
AA5 2 MET A 1210 ? LYS A 1218 ? MET A 1210 LYS A 1218 
AA5 3 ASN A 1262 ? ILE A 1269 ? ASN A 1262 ILE A 1269 
AA5 4 VAL A 1272 ? SER A 1273 ? VAL A 1272 SER A 1273 
AA6 1 PHE A 1286 ? ILE A 1289 ? PHE A 1286 ILE A 1289 
AA6 2 ILE A 1366 ? ASP A 1370 ? ILE A 1366 ASP A 1370 
AA6 3 THR A 1396 ? CYS A 1400 ? THR A 1396 CYS A 1400 
AA6 4 ARG A 1239 ? GLY A 1244 ? ARG A 1239 GLY A 1244 
AA6 5 GLN A 1412 ? GLU A 1417 ? GLN A 1412 GLU A 1417 
AA6 6 LYS A 1420 ? TYR A 1424 ? LYS A 1420 TYR A 1424 
AA7 1 GLY A 1298 ? THR A 1299 ? GLY A 1298 THR A 1299 
AA7 2 VAL A 1338 ? LEU A 1339 ? VAL A 1338 LEU A 1339 
AA8 1 VAL B 58   ? LYS B 62   ? VAL G 58   LYS G 62   
AA8 2 HIS B 69   ? ASP B 76   ? HIS G 69   ASP G 76   
AA8 3 ASN B 116  ? GLU B 122  ? ASN G 116  GLU G 122  
AA8 4 LEU B 107  ? SER B 110  ? LEU G 107  SER G 110  
AA9 1 LEU B 163  ? ILE B 164  ? LEU G 163  ILE G 164  
AA9 2 LYS B 190  ? ARG B 191  ? LYS G 190  ARG G 191  
AB1 1 LEU B 173  ? ILE B 175  ? LEU G 173  ILE G 175  
AB1 2 ILE B 181  ? VAL B 183  ? ILE G 181  VAL G 183  
# 
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 331  ? N ILE A 331  O ILE A 906  ? O ILE A 906  
AA2 1 2 O PHE A 446  ? O PHE A 446  N MET A 394  ? N MET A 394  
AA2 2 3 N VAL A 393  ? N VAL A 393  O LYS A 483  ? O LYS A 483  
AA3 1 2 N SER A 489  ? N SER A 489  O LEU A 570  ? O LEU A 570  
AA3 2 3 N TYR A 569  ? N TYR A 569  O ILE A 601  ? O ILE A 601  
AA3 3 4 O LEU A 602  ? O LEU A 602  N LEU A 454  ? N LEU A 454  
AA3 4 5 N ALA A 455  ? N ALA A 455  O LEU A 617  ? O LEU A 617  
AA3 5 6 N ILE A 618  ? N ILE A 618  O PHE A 626  ? O PHE A 626  
AA4 1 2 N GLY A 500  ? N GLY A 500  O LEU A 541  ? O LEU A 541  
AA5 1 2 O PHE A 1232 ? O PHE A 1232 N VAL A 1212 ? N VAL A 1212 
AA5 2 3 N THR A 1216 ? N THR A 1216 O GLU A 1264 ? O GLU A 1264 
AA5 3 4 N ILE A 1269 ? N ILE A 1269 O VAL A 1272 ? O VAL A 1272 
AA6 1 2 N GLY A 1287 ? N GLY A 1287 O LEU A 1368 ? O LEU A 1368 
AA6 2 3 N LEU A 1367 ? N LEU A 1367 O THR A 1396 ? O THR A 1396 
AA6 3 4 O VAL A 1397 ? O VAL A 1397 N VAL A 1240 ? N VAL A 1240 
AA6 4 5 N GLY A 1241 ? N GLY A 1241 O GLN A 1412 ? O GLN A 1412 
AA6 5 6 N VAL A 1415 ? N VAL A 1415 O ARG A 1422 ? O ARG A 1422 
AA7 1 2 N GLY A 1298 ? N GLY A 1298 O LEU A 1339 ? O LEU A 1339 
AA8 1 2 N VAL B 61   ? N VAL G 61   O TYR B 70   ? O TYR G 70   
AA8 2 3 N LEU B 75   ? N LEU G 75   O LEU B 117  ? O LEU G 117  
AA8 3 4 O VAL B 120  ? O VAL G 120  N GLU B 108  ? N GLU G 108  
AA9 1 2 N ILE B 164  ? N ILE G 164  O LYS B 190  ? O LYS G 190  
AB1 1 2 N LEU B 174  ? N LEU G 174  O GLN B 182  ? O GLN G 182  
# 
_pdbx_entry_details.entry_id                   9DW9 
_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 ASP A 443  ? ? 58.99   70.53   
2  1 LYS A 536  ? ? 60.35   -121.79 
3  1 PHE A 575  ? ? -94.07  58.59   
4  1 GLU A 822  ? ? 71.44   -10.07  
5  1 SER A 977  ? ? -102.12 -60.14  
6  1 LEU A 1335 ? ? 73.97   -3.72   
7  1 ASP A 1394 ? ? -94.97  57.61   
8  1 GLU A 1409 ? ? -91.46  51.63   
9  1 ILE G 47   ? ? -98.23  -64.29  
10 1 THR G 52   ? ? -129.20 -94.47  
11 1 PHE G 186  ? ? -83.85  33.99   
12 1 ASN G 217  ? ? -127.51 -168.42 
# 
loop_
_pdbx_struct_mod_residue.id 
_pdbx_struct_mod_residue.label_asym_id 
_pdbx_struct_mod_residue.label_comp_id 
_pdbx_struct_mod_residue.label_seq_id 
_pdbx_struct_mod_residue.auth_asym_id 
_pdbx_struct_mod_residue.auth_comp_id 
_pdbx_struct_mod_residue.auth_seq_id 
_pdbx_struct_mod_residue.PDB_ins_code 
_pdbx_struct_mod_residue.parent_comp_id 
_pdbx_struct_mod_residue.details 
1 A SEP 813 A SEP 813 ? SER 'modified residue' 
2 B TPO 198 G TPO 198 ? THR 'modified residue' 
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9DW9 
_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                    9DW9 
_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                  2.8 
_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               47950 
_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            7.4 
# 
_em_entity_assembly.id                   1 
_em_entity_assembly.parent_id            0 
_em_entity_assembly.source               'MULTIPLE SOURCES' 
_em_entity_assembly.type                 COMPLEX 
_em_entity_assembly.name                 'Phosphorylated (E1371Q)CFTR in complex with PKA-C' 
_em_entity_assembly.details              ? 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       1,2 
# 
_em_imaging.entry_id                        9DW9 
_em_imaging.id                              1 
_em_imaging.astigmatism                     ? 
_em_imaging.electron_beam_tilt_params       ? 
_em_imaging.residual_tilt                   ? 
_em_imaging.microscope_model                'TFS 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             800 
_em_imaging.nominal_defocus_max             1800 
_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_sample_support.id               1 
_em_sample_support.film_material    ? 
_em_sample_support.method           ? 
_em_sample_support.grid_material    COPPER 
_em_sample_support.grid_mesh_size   ? 
_em_sample_support.grid_type        'Quantifoil R0.6/1' 
_em_sample_support.details          ? 
_em_sample_support.specimen_id      1 
_em_sample_support.citation_id      ? 
# 
_em_vitrification.entry_id              9DW9 
_em_vitrification.id                    1 
_em_vitrification.specimen_id           1 
_em_vitrification.cryogen_name          ETHANE 
_em_vitrification.humidity              100 
_em_vitrification.temp                  ? 
_em_vitrification.chamber_temperature   ? 
_em_vitrification.instrument            'FEI VITROBOT MARK IV' 
_em_vitrification.method                ? 
_em_vitrification.time_resolved_state   ? 
_em_vitrification.citation_id           ? 
_em_vitrification.details               ? 
# 
_em_experiment.entry_id                9DW9 
_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 GLU 403  ? A GLU 403  
2   1 Y 1 A GLY 404  ? A GLY 404  
3   1 Y 1 A PHE 405  ? A PHE 405  
4   1 Y 1 A GLY 406  ? A GLY 406  
5   1 Y 1 A GLU 407  ? A GLU 407  
6   1 Y 1 A LEU 408  ? A LEU 408  
7   1 Y 1 A PHE 409  ? A PHE 409  
8   1 Y 1 A GLU 410  ? A GLU 410  
9   1 Y 1 A LYS 411  ? A LYS 411  
10  1 Y 1 A ALA 412  ? A ALA 412  
11  1 Y 1 A LYS 413  ? A LYS 413  
12  1 Y 1 A GLN 414  ? A GLN 414  
13  1 Y 1 A ASN 415  ? A ASN 415  
14  1 Y 1 A ASN 416  ? A ASN 416  
15  1 Y 1 A ASN 417  ? A ASN 417  
16  1 Y 1 A ASN 418  ? A ASN 418  
17  1 Y 1 A ARG 419  ? A ARG 419  
18  1 Y 1 A LYS 420  ? A LYS 420  
19  1 Y 1 A THR 421  ? A THR 421  
20  1 Y 1 A SER 422  ? A SER 422  
21  1 Y 1 A ASN 423  ? A ASN 423  
22  1 Y 1 A GLY 424  ? A GLY 424  
23  1 Y 1 A ASP 425  ? A ASP 425  
24  1 Y 1 A ASP 426  ? A ASP 426  
25  1 Y 1 A SER 427  ? A SER 427  
26  1 Y 1 A LEU 428  ? A LEU 428  
27  1 Y 1 A PHE 429  ? A PHE 429  
28  1 Y 1 A PHE 430  ? A PHE 430  
29  1 Y 1 A SER 431  ? A SER 431  
30  1 Y 1 A ASN 432  ? A ASN 432  
31  1 Y 1 A PHE 433  ? A PHE 433  
32  1 Y 1 A SER 434  ? A SER 434  
33  1 Y 1 A LEU 435  ? A LEU 435  
34  1 Y 1 A LEU 436  ? A LEU 436  
35  1 Y 1 A LEU 636  ? A LEU 636  
36  1 Y 1 A GLN 637  ? A GLN 637  
37  1 Y 1 A PRO 638  ? A PRO 638  
38  1 Y 1 A ASP 639  ? A ASP 639  
39  1 Y 1 A PHE 640  ? A PHE 640  
40  1 Y 1 A SER 641  ? A SER 641  
41  1 Y 1 A SER 642  ? A SER 642  
42  1 Y 1 A LYS 643  ? A LYS 643  
43  1 Y 1 A LEU 644  ? A LEU 644  
44  1 Y 1 A MET 645  ? A MET 645  
45  1 Y 1 A GLY 646  ? A GLY 646  
46  1 Y 1 A CYS 647  ? A CYS 647  
47  1 Y 1 A ASP 648  ? A ASP 648  
48  1 Y 1 A SER 649  ? A SER 649  
49  1 Y 1 A PHE 650  ? A PHE 650  
50  1 Y 1 A ASP 651  ? A ASP 651  
51  1 Y 1 A GLN 652  ? A GLN 652  
52  1 Y 1 A PHE 653  ? A PHE 653  
53  1 Y 1 A SER 654  ? A SER 654  
54  1 Y 1 A ALA 655  ? A ALA 655  
55  1 Y 1 A GLU 656  ? A GLU 656  
56  1 Y 1 A ARG 657  ? A ARG 657  
57  1 Y 1 A ARG 658  ? A ARG 658  
58  1 Y 1 A ASN 659  ? A ASN 659  
59  1 Y 1 A SER 660  ? A SER 660  
60  1 Y 1 A ILE 661  ? A ILE 661  
61  1 Y 1 A LEU 662  ? A LEU 662  
62  1 Y 1 A THR 663  ? A THR 663  
63  1 Y 1 A GLU 664  ? A GLU 664  
64  1 Y 1 A THR 665  ? A THR 665  
65  1 Y 1 A LEU 666  ? A LEU 666  
66  1 Y 1 A HIS 667  ? A HIS 667  
67  1 Y 1 A ARG 668  ? A ARG 668  
68  1 Y 1 A PHE 669  ? A PHE 669  
69  1 Y 1 A SER 670  ? A SER 670  
70  1 Y 1 A LEU 671  ? A LEU 671  
71  1 Y 1 A GLU 672  ? A GLU 672  
72  1 Y 1 A GLY 673  ? A GLY 673  
73  1 Y 1 A ASP 674  ? A ASP 674  
74  1 Y 1 A ALA 675  ? A ALA 675  
75  1 Y 1 A PRO 676  ? A PRO 676  
76  1 Y 1 A VAL 677  ? A VAL 677  
77  1 Y 1 A SER 678  ? A SER 678  
78  1 Y 1 A TRP 679  ? A TRP 679  
79  1 Y 1 A THR 680  ? A THR 680  
80  1 Y 1 A GLU 681  ? A GLU 681  
81  1 Y 1 A THR 682  ? A THR 682  
82  1 Y 1 A LYS 683  ? A LYS 683  
83  1 Y 1 A LYS 684  ? A LYS 684  
84  1 Y 1 A GLN 685  ? A GLN 685  
85  1 Y 1 A SER 686  ? A SER 686  
86  1 Y 1 A PHE 687  ? A PHE 687  
87  1 Y 1 A LYS 688  ? A LYS 688  
88  1 Y 1 A GLN 689  ? A GLN 689  
89  1 Y 1 A THR 690  ? A THR 690  
90  1 Y 1 A GLY 691  ? A GLY 691  
91  1 Y 1 A GLU 692  ? A GLU 692  
92  1 Y 1 A PHE 693  ? A PHE 693  
93  1 Y 1 A GLY 694  ? A GLY 694  
94  1 Y 1 A GLU 695  ? A GLU 695  
95  1 Y 1 A LYS 696  ? A LYS 696  
96  1 Y 1 A ARG 697  ? A ARG 697  
97  1 Y 1 A LYS 698  ? A LYS 698  
98  1 Y 1 A ASN 699  ? A ASN 699  
99  1 Y 1 A SER 700  ? A SER 700  
100 1 Y 1 A ILE 701  ? A ILE 701  
101 1 Y 1 A LEU 702  ? A LEU 702  
102 1 Y 1 A ASN 703  ? A ASN 703  
103 1 Y 1 A PRO 704  ? A PRO 704  
104 1 Y 1 A ILE 705  ? A ILE 705  
105 1 Y 1 A ASN 706  ? A ASN 706  
106 1 Y 1 A SER 707  ? A SER 707  
107 1 Y 1 A ILE 708  ? A ILE 708  
108 1 Y 1 A ARG 709  ? A ARG 709  
109 1 Y 1 A LYS 710  ? A LYS 710  
110 1 Y 1 A PHE 711  ? A PHE 711  
111 1 Y 1 A SER 712  ? A SER 712  
112 1 Y 1 A ILE 713  ? A ILE 713  
113 1 Y 1 A VAL 714  ? A VAL 714  
114 1 Y 1 A GLN 715  ? A GLN 715  
115 1 Y 1 A LYS 716  ? A LYS 716  
116 1 Y 1 A THR 717  ? A THR 717  
117 1 Y 1 A PRO 718  ? A PRO 718  
118 1 Y 1 A LEU 719  ? A LEU 719  
119 1 Y 1 A GLN 720  ? A GLN 720  
120 1 Y 1 A MET 721  ? A MET 721  
121 1 Y 1 A ASN 722  ? A ASN 722  
122 1 Y 1 A GLY 723  ? A GLY 723  
123 1 Y 1 A ILE 724  ? A ILE 724  
124 1 Y 1 A GLU 725  ? A GLU 725  
125 1 Y 1 A GLU 726  ? A GLU 726  
126 1 Y 1 A ASP 727  ? A ASP 727  
127 1 Y 1 A SER 728  ? A SER 728  
128 1 Y 1 A ASP 729  ? A ASP 729  
129 1 Y 1 A GLU 730  ? A GLU 730  
130 1 Y 1 A PRO 731  ? A PRO 731  
131 1 Y 1 A LEU 732  ? A LEU 732  
132 1 Y 1 A GLU 733  ? A GLU 733  
133 1 Y 1 A ARG 734  ? A ARG 734  
134 1 Y 1 A ARG 735  ? A ARG 735  
135 1 Y 1 A LEU 736  ? A LEU 736  
136 1 Y 1 A SER 737  ? A SER 737  
137 1 Y 1 A LEU 738  ? A LEU 738  
138 1 Y 1 A VAL 739  ? A VAL 739  
139 1 Y 1 A PRO 740  ? A PRO 740  
140 1 Y 1 A ASP 741  ? A ASP 741  
141 1 Y 1 A SER 742  ? A SER 742  
142 1 Y 1 A GLU 743  ? A GLU 743  
143 1 Y 1 A GLN 744  ? A GLN 744  
144 1 Y 1 A GLY 745  ? A GLY 745  
145 1 Y 1 A GLU 746  ? A GLU 746  
146 1 Y 1 A ALA 747  ? A ALA 747  
147 1 Y 1 A ILE 748  ? A ILE 748  
148 1 Y 1 A LEU 749  ? A LEU 749  
149 1 Y 1 A PRO 750  ? A PRO 750  
150 1 Y 1 A ARG 751  ? A ARG 751  
151 1 Y 1 A ILE 752  ? A ILE 752  
152 1 Y 1 A SER 753  ? A SER 753  
153 1 Y 1 A VAL 754  ? A VAL 754  
154 1 Y 1 A ILE 755  ? A ILE 755  
155 1 Y 1 A SER 756  ? A SER 756  
156 1 Y 1 A THR 757  ? A THR 757  
157 1 Y 1 A GLY 758  ? A GLY 758  
158 1 Y 1 A PRO 759  ? A PRO 759  
159 1 Y 1 A THR 760  ? A THR 760  
160 1 Y 1 A LEU 761  ? A LEU 761  
161 1 Y 1 A GLN 762  ? A GLN 762  
162 1 Y 1 A ALA 763  ? A ALA 763  
163 1 Y 1 A ARG 764  ? A ARG 764  
164 1 Y 1 A ARG 765  ? A ARG 765  
165 1 Y 1 A ARG 766  ? A ARG 766  
166 1 Y 1 A GLN 767  ? A GLN 767  
167 1 Y 1 A SER 768  ? A SER 768  
168 1 Y 1 A VAL 769  ? A VAL 769  
169 1 Y 1 A LEU 770  ? A LEU 770  
170 1 Y 1 A ASN 771  ? A ASN 771  
171 1 Y 1 A LEU 772  ? A LEU 772  
172 1 Y 1 A MET 773  ? A MET 773  
173 1 Y 1 A THR 774  ? A THR 774  
174 1 Y 1 A HIS 775  ? A HIS 775  
175 1 Y 1 A SER 776  ? A SER 776  
176 1 Y 1 A VAL 777  ? A VAL 777  
177 1 Y 1 A ASN 778  ? A ASN 778  
178 1 Y 1 A GLN 779  ? A GLN 779  
179 1 Y 1 A GLY 780  ? A GLY 780  
180 1 Y 1 A GLN 781  ? A GLN 781  
181 1 Y 1 A ASN 782  ? A ASN 782  
182 1 Y 1 A ILE 783  ? A ILE 783  
183 1 Y 1 A HIS 784  ? A HIS 784  
184 1 Y 1 A ARG 785  ? A ARG 785  
185 1 Y 1 A LYS 786  ? A LYS 786  
186 1 Y 1 A THR 787  ? A THR 787  
187 1 Y 1 A THR 788  ? A THR 788  
188 1 Y 1 A ALA 789  ? A ALA 789  
189 1 Y 1 A SER 790  ? A SER 790  
190 1 Y 1 A THR 791  ? A THR 791  
191 1 Y 1 A ARG 792  ? A ARG 792  
192 1 Y 1 A LYS 793  ? A LYS 793  
193 1 Y 1 A VAL 794  ? A VAL 794  
194 1 Y 1 A SER 795  ? A SER 795  
195 1 Y 1 A LEU 796  ? A LEU 796  
196 1 Y 1 A ALA 797  ? A ALA 797  
197 1 Y 1 A PRO 798  ? A PRO 798  
198 1 Y 1 A GLN 799  ? A GLN 799  
199 1 Y 1 A ALA 800  ? A ALA 800  
200 1 Y 1 A ASN 801  ? A ASN 801  
201 1 Y 1 A LEU 802  ? A LEU 802  
202 1 Y 1 A THR 803  ? A THR 803  
203 1 Y 1 A GLU 804  ? A GLU 804  
204 1 Y 1 A LEU 805  ? A LEU 805  
205 1 Y 1 A GLU 815  ? A GLU 815  
206 1 Y 1 A THR 816  ? A THR 816  
207 1 Y 1 A GLY 817  ? A GLY 817  
208 1 Y 1 A LEU 818  ? A LEU 818  
209 1 Y 1 A GLU 819  ? A GLU 819  
210 1 Y 1 A PHE 834  ? A PHE 834  
211 1 Y 1 A ASP 835  ? A ASP 835  
212 1 Y 1 A ASP 836  ? A ASP 836  
213 1 Y 1 A MET 837  ? A MET 837  
214 1 Y 1 A GLU 838  ? A GLU 838  
215 1 Y 1 A SER 839  ? A SER 839  
216 1 Y 1 A ILE 840  ? A ILE 840  
217 1 Y 1 A PRO 841  ? A PRO 841  
218 1 Y 1 A ALA 842  ? A ALA 842  
219 1 Y 1 A VAL 843  ? A VAL 843  
220 1 Y 1 A THR 844  ? A THR 844  
221 1 Y 1 A THR 845  ? A THR 845  
222 1 Y 1 A GLY 885  ? A GLY 885  
223 1 Y 1 A ASN 886  ? A ASN 886  
224 1 Y 1 A THR 887  ? A THR 887  
225 1 Y 1 A PRO 888  ? A PRO 888  
226 1 Y 1 A LEU 889  ? A LEU 889  
227 1 Y 1 A GLN 890  ? A GLN 890  
228 1 Y 1 A ASP 891  ? A ASP 891  
229 1 Y 1 A LYS 892  ? A LYS 892  
230 1 Y 1 A GLY 893  ? A GLY 893  
231 1 Y 1 A ASN 894  ? A ASN 894  
232 1 Y 1 A SER 895  ? A SER 895  
233 1 Y 1 A THR 896  ? A THR 896  
234 1 Y 1 A HIS 897  ? A HIS 897  
235 1 Y 1 A SER 898  ? A SER 898  
236 1 Y 1 A ARG 899  ? A ARG 899  
237 1 Y 1 A ASN 900  ? A ASN 900  
238 1 Y 1 A ASN 901  ? A ASN 901  
239 1 Y 1 A SER 902  ? A SER 902  
240 1 Y 1 A LYS 1174 ? A LYS 1174 
241 1 Y 1 A PRO 1175 ? A PRO 1175 
242 1 Y 1 A THR 1176 ? A THR 1176 
243 1 Y 1 A LYS 1177 ? A LYS 1177 
244 1 Y 1 A SER 1178 ? A SER 1178 
245 1 Y 1 A THR 1179 ? A THR 1179 
246 1 Y 1 A LYS 1180 ? A LYS 1180 
247 1 Y 1 A PRO 1181 ? A PRO 1181 
248 1 Y 1 A TYR 1182 ? A TYR 1182 
249 1 Y 1 A LYS 1183 ? A LYS 1183 
250 1 Y 1 A ASN 1184 ? A ASN 1184 
251 1 Y 1 A GLY 1185 ? A GLY 1185 
252 1 Y 1 A GLN 1186 ? A GLN 1186 
253 1 Y 1 A LEU 1187 ? A LEU 1187 
254 1 Y 1 A SER 1188 ? A SER 1188 
255 1 Y 1 A LYS 1189 ? A LYS 1189 
256 1 Y 1 A VAL 1190 ? A VAL 1190 
257 1 Y 1 A MET 1191 ? A MET 1191 
258 1 Y 1 A ILE 1192 ? A ILE 1192 
259 1 Y 1 A ILE 1193 ? A ILE 1193 
260 1 Y 1 A GLU 1194 ? A GLU 1194 
261 1 Y 1 A ASN 1195 ? A ASN 1195 
262 1 Y 1 A SER 1196 ? A SER 1196 
263 1 Y 1 A HIS 1197 ? A HIS 1197 
264 1 Y 1 A VAL 1198 ? A VAL 1198 
265 1 Y 1 A LYS 1199 ? A LYS 1199 
266 1 Y 1 A LYS 1200 ? A LYS 1200 
267 1 Y 1 A ASP 1201 ? A ASP 1201 
268 1 Y 1 A ASP 1202 ? A ASP 1202 
269 1 Y 1 A HIS 1452 ? A HIS 1452 
270 1 Y 1 A ARG 1453 ? A ARG 1453 
271 1 Y 1 A ASN 1454 ? A ASN 1454 
272 1 Y 1 A SER 1455 ? A SER 1455 
273 1 Y 1 A SER 1456 ? A SER 1456 
274 1 Y 1 A LYS 1457 ? A LYS 1457 
275 1 Y 1 A CYS 1458 ? A CYS 1458 
276 1 Y 1 A LYS 1459 ? A LYS 1459 
277 1 Y 1 A SER 1460 ? A SER 1460 
278 1 Y 1 A LYS 1461 ? A LYS 1461 
279 1 Y 1 A PRO 1462 ? A PRO 1462 
280 1 Y 1 A GLN 1463 ? A GLN 1463 
281 1 Y 1 A ILE 1464 ? A ILE 1464 
282 1 Y 1 A ALA 1465 ? A ALA 1465 
283 1 Y 1 A ALA 1466 ? A ALA 1466 
284 1 Y 1 A LEU 1467 ? A LEU 1467 
285 1 Y 1 A LYS 1468 ? A LYS 1468 
286 1 Y 1 A GLU 1469 ? A GLU 1469 
287 1 Y 1 A GLU 1470 ? A GLU 1470 
288 1 Y 1 A THR 1471 ? A THR 1471 
289 1 Y 1 A GLU 1472 ? A GLU 1472 
290 1 Y 1 A GLU 1473 ? A GLU 1473 
291 1 Y 1 A GLU 1474 ? A GLU 1474 
292 1 Y 1 A VAL 1475 ? A VAL 1475 
293 1 Y 1 A GLN 1476 ? A GLN 1476 
294 1 Y 1 A ASP 1477 ? A ASP 1477 
295 1 Y 1 A THR 1478 ? A THR 1478 
296 1 Y 1 A ARG 1479 ? A ARG 1479 
297 1 Y 1 A LEU 1480 ? A LEU 1480 
298 1 Y 1 G MET 1    ? B MET 1    
299 1 Y 1 G GLY 2    ? B GLY 2    
300 1 Y 1 G ASN 3    ? B ASN 3    
301 1 Y 1 G ALA 4    ? B ALA 4    
302 1 Y 1 G ALA 5    ? B ALA 5    
303 1 Y 1 G ALA 6    ? B ALA 6    
304 1 Y 1 G ALA 7    ? B ALA 7    
305 1 Y 1 G LYS 8    ? B LYS 8    
306 1 Y 1 G LYS 9    ? B LYS 9    
307 1 Y 1 G GLY 10   ? B GLY 10   
308 1 Y 1 G SER 11   ? B SER 11   
309 1 Y 1 G GLU 12   ? B GLU 12   
310 1 Y 1 G GLU 332  ? B GLU 332  
311 1 Y 1 G GLU 333  ? B GLU 333  
312 1 Y 1 G GLU 334  ? B GLU 334  
313 1 Y 1 G GLU 335  ? B GLU 335  
314 1 Y 1 G ILE 336  ? B ILE 336  
315 1 Y 1 G ARG 337  ? B ARG 337  
316 1 Y 1 G VAL 338  ? B VAL 338  
317 1 Y 1 G SER 339  ? B SER 339  
318 1 Y 1 G ILE 340  ? B ILE 340  
319 1 Y 1 G ASN 341  ? B ASN 341  
320 1 Y 1 G GLU 342  ? B GLU 342  
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N      N  N N 1   
ALA CA     C  N S 2   
ALA C      C  N N 3   
ALA O      O  N N 4   
ALA CB     C  N N 5   
ALA OXT    O  N N 6   
ALA H      H  N N 7   
ALA H2     H  N N 8   
ALA HA     H  N N 9   
ALA HB1    H  N N 10  
ALA HB2    H  N N 11  
ALA HB3    H  N N 12  
ALA HXT    H  N N 13  
ARG N      N  N N 14  
ARG CA     C  N S 15  
ARG C      C  N N 16  
ARG O      O  N N 17  
ARG CB     C  N N 18  
ARG CG     C  N N 19  
ARG CD     C  N N 20  
ARG NE     N  N N 21  
ARG CZ     C  N N 22  
ARG NH1    N  N N 23  
ARG NH2    N  N N 24  
ARG OXT    O  N N 25  
ARG H      H  N N 26  
ARG H2     H  N N 27  
ARG HA     H  N N 28  
ARG HB2    H  N N 29  
ARG HB3    H  N N 30  
ARG HG2    H  N N 31  
ARG HG3    H  N N 32  
ARG HD2    H  N N 33  
ARG HD3    H  N N 34  
ARG HE     H  N N 35  
ARG HH11   H  N N 36  
ARG HH12   H  N N 37  
ARG HH21   H  N N 38  
ARG HH22   H  N N 39  
ARG HXT    H  N N 40  
ASN N      N  N N 41  
ASN CA     C  N S 42  
ASN C      C  N N 43  
ASN O      O  N N 44  
ASN CB     C  N N 45  
ASN CG     C  N N 46  
ASN OD1    O  N N 47  
ASN ND2    N  N N 48  
ASN OXT    O  N N 49  
ASN H      H  N N 50  
ASN H2     H  N N 51  
ASN HA     H  N N 52  
ASN HB2    H  N N 53  
ASN HB3    H  N N 54  
ASN HD21   H  N N 55  
ASN HD22   H  N N 56  
ASN HXT    H  N N 57  
ASP N      N  N N 58  
ASP CA     C  N S 59  
ASP C      C  N N 60  
ASP O      O  N N 61  
ASP CB     C  N N 62  
ASP CG     C  N N 63  
ASP OD1    O  N N 64  
ASP OD2    O  N N 65  
ASP OXT    O  N N 66  
ASP H      H  N N 67  
ASP H2     H  N N 68  
ASP HA     H  N N 69  
ASP HB2    H  N N 70  
ASP HB3    H  N N 71  
ASP HD2    H  N N 72  
ASP HXT    H  N N 73  
ATP PG     P  N N 74  
ATP O1G    O  N N 75  
ATP O2G    O  N N 76  
ATP O3G    O  N N 77  
ATP PB     P  N R 78  
ATP O1B    O  N N 79  
ATP O2B    O  N N 80  
ATP O3B    O  N N 81  
ATP PA     P  N R 82  
ATP O1A    O  N N 83  
ATP O2A    O  N N 84  
ATP O3A    O  N N 85  
ATP "O5'"  O  N N 86  
ATP "C5'"  C  N N 87  
ATP "C4'"  C  N R 88  
ATP "O4'"  O  N N 89  
ATP "C3'"  C  N S 90  
ATP "O3'"  O  N N 91  
ATP "C2'"  C  N R 92  
ATP "O2'"  O  N N 93  
ATP "C1'"  C  N R 94  
ATP N9     N  Y N 95  
ATP C8     C  Y N 96  
ATP N7     N  Y N 97  
ATP C5     C  Y N 98  
ATP C6     C  Y N 99  
ATP N6     N  N N 100 
ATP N1     N  Y N 101 
ATP C2     C  Y N 102 
ATP N3     N  Y N 103 
ATP C4     C  Y N 104 
ATP HOG2   H  N N 105 
ATP HOG3   H  N N 106 
ATP HOB2   H  N N 107 
ATP HOA2   H  N N 108 
ATP "H5'1" H  N N 109 
ATP "H5'2" H  N N 110 
ATP "H4'"  H  N N 111 
ATP "H3'"  H  N N 112 
ATP "HO3'" H  N N 113 
ATP "H2'"  H  N N 114 
ATP "HO2'" H  N N 115 
ATP "H1'"  H  N N 116 
ATP H8     H  N N 117 
ATP HN61   H  N N 118 
ATP HN62   H  N N 119 
ATP H2     H  N N 120 
CL  CL     CL N N 121 
CLR C1     C  N N 122 
CLR C2     C  N N 123 
CLR C3     C  N S 124 
CLR C4     C  N N 125 
CLR C5     C  N N 126 
CLR C6     C  N N 127 
CLR C7     C  N N 128 
CLR C8     C  N S 129 
CLR C9     C  N S 130 
CLR C10    C  N R 131 
CLR C11    C  N N 132 
CLR C12    C  N N 133 
CLR C13    C  N R 134 
CLR C14    C  N S 135 
CLR C15    C  N N 136 
CLR C16    C  N N 137 
CLR C17    C  N R 138 
CLR C18    C  N N 139 
CLR C19    C  N N 140 
CLR C20    C  N R 141 
CLR C21    C  N N 142 
CLR C22    C  N N 143 
CLR C23    C  N N 144 
CLR C24    C  N N 145 
CLR C25    C  N N 146 
CLR C26    C  N N 147 
CLR C27    C  N N 148 
CLR O1     O  N N 149 
CLR H11    H  N N 150 
CLR H12    H  N N 151 
CLR H21    H  N N 152 
CLR H22    H  N N 153 
CLR H3     H  N N 154 
CLR H41    H  N N 155 
CLR H42    H  N N 156 
CLR H6     H  N N 157 
CLR H71    H  N N 158 
CLR H72    H  N N 159 
CLR H8     H  N N 160 
CLR H9     H  N N 161 
CLR H111   H  N N 162 
CLR H112   H  N N 163 
CLR H121   H  N N 164 
CLR H122   H  N N 165 
CLR H14    H  N N 166 
CLR H151   H  N N 167 
CLR H152   H  N N 168 
CLR H161   H  N N 169 
CLR H162   H  N N 170 
CLR H17    H  N N 171 
CLR H181   H  N N 172 
CLR H182   H  N N 173 
CLR H183   H  N N 174 
CLR H191   H  N N 175 
CLR H192   H  N N 176 
CLR H193   H  N N 177 
CLR H20    H  N N 178 
CLR H211   H  N N 179 
CLR H212   H  N N 180 
CLR H213   H  N N 181 
CLR H221   H  N N 182 
CLR H222   H  N N 183 
CLR H231   H  N N 184 
CLR H232   H  N N 185 
CLR H241   H  N N 186 
CLR H242   H  N N 187 
CLR H25    H  N N 188 
CLR H261   H  N N 189 
CLR H262   H  N N 190 
CLR H263   H  N N 191 
CLR H271   H  N N 192 
CLR H272   H  N N 193 
CLR H273   H  N N 194 
CLR H1     H  N N 195 
CYS N      N  N N 196 
CYS CA     C  N R 197 
CYS C      C  N N 198 
CYS O      O  N N 199 
CYS CB     C  N N 200 
CYS SG     S  N N 201 
CYS OXT    O  N N 202 
CYS H      H  N N 203 
CYS H2     H  N N 204 
CYS HA     H  N N 205 
CYS HB2    H  N N 206 
CYS HB3    H  N N 207 
CYS HG     H  N N 208 
CYS HXT    H  N N 209 
D10 C1     C  N N 210 
D10 C2     C  N N 211 
D10 C3     C  N N 212 
D10 C4     C  N N 213 
D10 C5     C  N N 214 
D10 C6     C  N N 215 
D10 C7     C  N N 216 
D10 C8     C  N N 217 
D10 C9     C  N N 218 
D10 C10    C  N N 219 
D10 H11    H  N N 220 
D10 H12    H  N N 221 
D10 H13    H  N N 222 
D10 H21    H  N N 223 
D10 H22    H  N N 224 
D10 H31    H  N N 225 
D10 H32    H  N N 226 
D10 H41    H  N N 227 
D10 H42    H  N N 228 
D10 H51    H  N N 229 
D10 H52    H  N N 230 
D10 H61    H  N N 231 
D10 H62    H  N N 232 
D10 H71    H  N N 233 
D10 H72    H  N N 234 
D10 H81    H  N N 235 
D10 H82    H  N N 236 
D10 H91    H  N N 237 
D10 H92    H  N N 238 
D10 H101   H  N N 239 
D10 H102   H  N N 240 
D10 H103   H  N N 241 
GLN N      N  N N 242 
GLN CA     C  N S 243 
GLN C      C  N N 244 
GLN O      O  N N 245 
GLN CB     C  N N 246 
GLN CG     C  N N 247 
GLN CD     C  N N 248 
GLN OE1    O  N N 249 
GLN NE2    N  N N 250 
GLN OXT    O  N N 251 
GLN H      H  N N 252 
GLN H2     H  N N 253 
GLN HA     H  N N 254 
GLN HB2    H  N N 255 
GLN HB3    H  N N 256 
GLN HG2    H  N N 257 
GLN HG3    H  N N 258 
GLN HE21   H  N N 259 
GLN HE22   H  N N 260 
GLN HXT    H  N N 261 
GLU N      N  N N 262 
GLU CA     C  N S 263 
GLU C      C  N N 264 
GLU O      O  N N 265 
GLU CB     C  N N 266 
GLU CG     C  N N 267 
GLU CD     C  N N 268 
GLU OE1    O  N N 269 
GLU OE2    O  N N 270 
GLU OXT    O  N N 271 
GLU H      H  N N 272 
GLU H2     H  N N 273 
GLU HA     H  N N 274 
GLU HB2    H  N N 275 
GLU HB3    H  N N 276 
GLU HG2    H  N N 277 
GLU HG3    H  N N 278 
GLU HE2    H  N N 279 
GLU HXT    H  N N 280 
GLY N      N  N N 281 
GLY CA     C  N N 282 
GLY C      C  N N 283 
GLY O      O  N N 284 
GLY OXT    O  N N 285 
GLY H      H  N N 286 
GLY H2     H  N N 287 
GLY HA2    H  N N 288 
GLY HA3    H  N N 289 
GLY HXT    H  N N 290 
HIS N      N  N N 291 
HIS CA     C  N S 292 
HIS C      C  N N 293 
HIS O      O  N N 294 
HIS CB     C  N N 295 
HIS CG     C  Y N 296 
HIS ND1    N  Y N 297 
HIS CD2    C  Y N 298 
HIS CE1    C  Y N 299 
HIS NE2    N  Y N 300 
HIS OXT    O  N N 301 
HIS H      H  N N 302 
HIS H2     H  N N 303 
HIS HA     H  N N 304 
HIS HB2    H  N N 305 
HIS HB3    H  N N 306 
HIS HD1    H  N N 307 
HIS HD2    H  N N 308 
HIS HE1    H  N N 309 
HIS HE2    H  N N 310 
HIS HXT    H  N N 311 
HOH O      O  N N 312 
HOH H1     H  N N 313 
HOH H2     H  N N 314 
ILE N      N  N N 315 
ILE CA     C  N S 316 
ILE C      C  N N 317 
ILE O      O  N N 318 
ILE CB     C  N S 319 
ILE CG1    C  N N 320 
ILE CG2    C  N N 321 
ILE CD1    C  N N 322 
ILE OXT    O  N N 323 
ILE H      H  N N 324 
ILE H2     H  N N 325 
ILE HA     H  N N 326 
ILE HB     H  N N 327 
ILE HG12   H  N N 328 
ILE HG13   H  N N 329 
ILE HG21   H  N N 330 
ILE HG22   H  N N 331 
ILE HG23   H  N N 332 
ILE HD11   H  N N 333 
ILE HD12   H  N N 334 
ILE HD13   H  N N 335 
ILE HXT    H  N N 336 
LEU N      N  N N 337 
LEU CA     C  N S 338 
LEU C      C  N N 339 
LEU O      O  N N 340 
LEU CB     C  N N 341 
LEU CG     C  N N 342 
LEU CD1    C  N N 343 
LEU CD2    C  N N 344 
LEU OXT    O  N N 345 
LEU H      H  N N 346 
LEU H2     H  N N 347 
LEU HA     H  N N 348 
LEU HB2    H  N N 349 
LEU HB3    H  N N 350 
LEU HG     H  N N 351 
LEU HD11   H  N N 352 
LEU HD12   H  N N 353 
LEU HD13   H  N N 354 
LEU HD21   H  N N 355 
LEU HD22   H  N N 356 
LEU HD23   H  N N 357 
LEU HXT    H  N N 358 
LYS N      N  N N 359 
LYS CA     C  N S 360 
LYS C      C  N N 361 
LYS O      O  N N 362 
LYS CB     C  N N 363 
LYS CG     C  N N 364 
LYS CD     C  N N 365 
LYS CE     C  N N 366 
LYS NZ     N  N N 367 
LYS OXT    O  N N 368 
LYS H      H  N N 369 
LYS H2     H  N N 370 
LYS HA     H  N N 371 
LYS HB2    H  N N 372 
LYS HB3    H  N N 373 
LYS HG2    H  N N 374 
LYS HG3    H  N N 375 
LYS HD2    H  N N 376 
LYS HD3    H  N N 377 
LYS HE2    H  N N 378 
LYS HE3    H  N N 379 
LYS HZ1    H  N N 380 
LYS HZ2    H  N N 381 
LYS HZ3    H  N N 382 
LYS HXT    H  N N 383 
MET N      N  N N 384 
MET CA     C  N S 385 
MET C      C  N N 386 
MET O      O  N N 387 
MET CB     C  N N 388 
MET CG     C  N N 389 
MET SD     S  N N 390 
MET CE     C  N N 391 
MET OXT    O  N N 392 
MET H      H  N N 393 
MET H2     H  N N 394 
MET HA     H  N N 395 
MET HB2    H  N N 396 
MET HB3    H  N N 397 
MET HG2    H  N N 398 
MET HG3    H  N N 399 
MET HE1    H  N N 400 
MET HE2    H  N N 401 
MET HE3    H  N N 402 
MET HXT    H  N N 403 
MG  MG     MG N N 404 
PHE N      N  N N 405 
PHE CA     C  N S 406 
PHE C      C  N N 407 
PHE O      O  N N 408 
PHE CB     C  N N 409 
PHE CG     C  Y N 410 
PHE CD1    C  Y N 411 
PHE CD2    C  Y N 412 
PHE CE1    C  Y N 413 
PHE CE2    C  Y N 414 
PHE CZ     C  Y N 415 
PHE OXT    O  N N 416 
PHE H      H  N N 417 
PHE H2     H  N N 418 
PHE HA     H  N N 419 
PHE HB2    H  N N 420 
PHE HB3    H  N N 421 
PHE HD1    H  N N 422 
PHE HD2    H  N N 423 
PHE HE1    H  N N 424 
PHE HE2    H  N N 425 
PHE HZ     H  N N 426 
PHE HXT    H  N N 427 
PRO N      N  N N 428 
PRO CA     C  N S 429 
PRO C      C  N N 430 
PRO O      O  N N 431 
PRO CB     C  N N 432 
PRO CG     C  N N 433 
PRO CD     C  N N 434 
PRO OXT    O  N N 435 
PRO H      H  N N 436 
PRO HA     H  N N 437 
PRO HB2    H  N N 438 
PRO HB3    H  N N 439 
PRO HG2    H  N N 440 
PRO HG3    H  N N 441 
PRO HD2    H  N N 442 
PRO HD3    H  N N 443 
PRO HXT    H  N N 444 
SEP N      N  N N 445 
SEP CA     C  N S 446 
SEP CB     C  N N 447 
SEP OG     O  N N 448 
SEP C      C  N N 449 
SEP O      O  N N 450 
SEP OXT    O  N N 451 
SEP P      P  N N 452 
SEP O1P    O  N N 453 
SEP O2P    O  N N 454 
SEP O3P    O  N N 455 
SEP H      H  N N 456 
SEP H2     H  N N 457 
SEP HA     H  N N 458 
SEP HB2    H  N N 459 
SEP HB3    H  N N 460 
SEP HXT    H  N N 461 
SEP HOP2   H  N N 462 
SEP HOP3   H  N N 463 
SER N      N  N N 464 
SER CA     C  N S 465 
SER C      C  N N 466 
SER O      O  N N 467 
SER CB     C  N N 468 
SER OG     O  N N 469 
SER OXT    O  N N 470 
SER H      H  N N 471 
SER H2     H  N N 472 
SER HA     H  N N 473 
SER HB2    H  N N 474 
SER HB3    H  N N 475 
SER HG     H  N N 476 
SER HXT    H  N N 477 
THR N      N  N N 478 
THR CA     C  N S 479 
THR C      C  N N 480 
THR O      O  N N 481 
THR CB     C  N R 482 
THR OG1    O  N N 483 
THR CG2    C  N N 484 
THR OXT    O  N N 485 
THR H      H  N N 486 
THR H2     H  N N 487 
THR HA     H  N N 488 
THR HB     H  N N 489 
THR HG1    H  N N 490 
THR HG21   H  N N 491 
THR HG22   H  N N 492 
THR HG23   H  N N 493 
THR HXT    H  N N 494 
TPO N      N  N N 495 
TPO CA     C  N S 496 
TPO CB     C  N R 497 
TPO CG2    C  N N 498 
TPO OG1    O  N N 499 
TPO P      P  N N 500 
TPO O1P    O  N N 501 
TPO O2P    O  N N 502 
TPO O3P    O  N N 503 
TPO C      C  N N 504 
TPO O      O  N N 505 
TPO OXT    O  N N 506 
TPO H      H  N N 507 
TPO H2     H  N N 508 
TPO HA     H  N N 509 
TPO HB     H  N N 510 
TPO HG21   H  N N 511 
TPO HG22   H  N N 512 
TPO HG23   H  N N 513 
TPO HOP2   H  N N 514 
TPO HOP3   H  N N 515 
TPO HXT    H  N N 516 
TRP N      N  N N 517 
TRP CA     C  N S 518 
TRP C      C  N N 519 
TRP O      O  N N 520 
TRP CB     C  N N 521 
TRP CG     C  Y N 522 
TRP CD1    C  Y N 523 
TRP CD2    C  Y N 524 
TRP NE1    N  Y N 525 
TRP CE2    C  Y N 526 
TRP CE3    C  Y N 527 
TRP CZ2    C  Y N 528 
TRP CZ3    C  Y N 529 
TRP CH2    C  Y N 530 
TRP OXT    O  N N 531 
TRP H      H  N N 532 
TRP H2     H  N N 533 
TRP HA     H  N N 534 
TRP HB2    H  N N 535 
TRP HB3    H  N N 536 
TRP HD1    H  N N 537 
TRP HE1    H  N N 538 
TRP HE3    H  N N 539 
TRP HZ2    H  N N 540 
TRP HZ3    H  N N 541 
TRP HH2    H  N N 542 
TRP HXT    H  N N 543 
TYR N      N  N N 544 
TYR CA     C  N S 545 
TYR C      C  N N 546 
TYR O      O  N N 547 
TYR CB     C  N N 548 
TYR CG     C  Y N 549 
TYR CD1    C  Y N 550 
TYR CD2    C  Y N 551 
TYR CE1    C  Y N 552 
TYR CE2    C  Y N 553 
TYR CZ     C  Y N 554 
TYR OH     O  N N 555 
TYR OXT    O  N N 556 
TYR H      H  N N 557 
TYR H2     H  N N 558 
TYR HA     H  N N 559 
TYR HB2    H  N N 560 
TYR HB3    H  N N 561 
TYR HD1    H  N N 562 
TYR HD2    H  N N 563 
TYR HE1    H  N N 564 
TYR HE2    H  N N 565 
TYR HH     H  N N 566 
TYR HXT    H  N N 567 
UND C1     C  N N 568 
UND C2     C  N N 569 
UND C3     C  N N 570 
UND C4     C  N N 571 
UND C5     C  N N 572 
UND C6     C  N N 573 
UND C7     C  N N 574 
UND C8     C  N N 575 
UND C9     C  N N 576 
UND C10    C  N N 577 
UND C11    C  N N 578 
UND H11    H  N N 579 
UND H12    H  N N 580 
UND H13    H  N N 581 
UND H21    H  N N 582 
UND H22    H  N N 583 
UND H31    H  N N 584 
UND H32    H  N N 585 
UND H41    H  N N 586 
UND H42    H  N N 587 
UND H51    H  N N 588 
UND H52    H  N N 589 
UND H61    H  N N 590 
UND H62    H  N N 591 
UND H71    H  N N 592 
UND H72    H  N N 593 
UND H81    H  N N 594 
UND H82    H  N N 595 
UND H91    H  N N 596 
UND H92    H  N N 597 
UND H101   H  N N 598 
UND H102   H  N N 599 
UND H111   H  N N 600 
UND H112   H  N N 601 
UND H113   H  N N 602 
VAL N      N  N N 603 
VAL CA     C  N S 604 
VAL C      C  N N 605 
VAL O      O  N N 606 
VAL CB     C  N N 607 
VAL CG1    C  N N 608 
VAL CG2    C  N N 609 
VAL OXT    O  N N 610 
VAL H      H  N N 611 
VAL H2     H  N N 612 
VAL HA     H  N N 613 
VAL HB     H  N N 614 
VAL HG11   H  N N 615 
VAL HG12   H  N N 616 
VAL HG13   H  N N 617 
VAL HG21   H  N N 618 
VAL HG22   H  N N 619 
VAL HG23   H  N N 620 
VAL HXT    H  N N 621 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N     CA     sing N N 1   
ALA N     H      sing N N 2   
ALA N     H2     sing N N 3   
ALA CA    C      sing N N 4   
ALA CA    CB     sing N N 5   
ALA CA    HA     sing N N 6   
ALA C     O      doub N N 7   
ALA C     OXT    sing N N 8   
ALA CB    HB1    sing N N 9   
ALA CB    HB2    sing N N 10  
ALA CB    HB3    sing N N 11  
ALA OXT   HXT    sing N N 12  
ARG N     CA     sing N N 13  
ARG N     H      sing N N 14  
ARG N     H2     sing N N 15  
ARG CA    C      sing N N 16  
ARG CA    CB     sing N N 17  
ARG CA    HA     sing N N 18  
ARG C     O      doub N N 19  
ARG C     OXT    sing N N 20  
ARG CB    CG     sing N N 21  
ARG CB    HB2    sing N N 22  
ARG CB    HB3    sing N N 23  
ARG CG    CD     sing N N 24  
ARG CG    HG2    sing N N 25  
ARG CG    HG3    sing N N 26  
ARG CD    NE     sing N N 27  
ARG CD    HD2    sing N N 28  
ARG CD    HD3    sing N N 29  
ARG NE    CZ     sing N N 30  
ARG NE    HE     sing N N 31  
ARG CZ    NH1    sing N N 32  
ARG CZ    NH2    doub N N 33  
ARG NH1   HH11   sing N N 34  
ARG NH1   HH12   sing N N 35  
ARG NH2   HH21   sing N N 36  
ARG NH2   HH22   sing N N 37  
ARG OXT   HXT    sing N N 38  
ASN N     CA     sing N N 39  
ASN N     H      sing N N 40  
ASN N     H2     sing N N 41  
ASN CA    C      sing N N 42  
ASN CA    CB     sing N N 43  
ASN CA    HA     sing N N 44  
ASN C     O      doub N N 45  
ASN C     OXT    sing N N 46  
ASN CB    CG     sing N N 47  
ASN CB    HB2    sing N N 48  
ASN CB    HB3    sing N N 49  
ASN CG    OD1    doub N N 50  
ASN CG    ND2    sing N N 51  
ASN ND2   HD21   sing N N 52  
ASN ND2   HD22   sing N N 53  
ASN OXT   HXT    sing N N 54  
ASP N     CA     sing N N 55  
ASP N     H      sing N N 56  
ASP N     H2     sing N N 57  
ASP CA    C      sing N N 58  
ASP CA    CB     sing N N 59  
ASP CA    HA     sing N N 60  
ASP C     O      doub N N 61  
ASP C     OXT    sing N N 62  
ASP CB    CG     sing N N 63  
ASP CB    HB2    sing N N 64  
ASP CB    HB3    sing N N 65  
ASP CG    OD1    doub N N 66  
ASP CG    OD2    sing N N 67  
ASP OD2   HD2    sing N N 68  
ASP OXT   HXT    sing N N 69  
ATP PG    O1G    doub N N 70  
ATP PG    O2G    sing N N 71  
ATP PG    O3G    sing N N 72  
ATP PG    O3B    sing N N 73  
ATP O2G   HOG2   sing N N 74  
ATP O3G   HOG3   sing N N 75  
ATP PB    O1B    doub N N 76  
ATP PB    O2B    sing N N 77  
ATP PB    O3B    sing N N 78  
ATP PB    O3A    sing N N 79  
ATP O2B   HOB2   sing N N 80  
ATP PA    O1A    doub N N 81  
ATP PA    O2A    sing N N 82  
ATP PA    O3A    sing N N 83  
ATP PA    "O5'"  sing N N 84  
ATP O2A   HOA2   sing N N 85  
ATP "O5'" "C5'"  sing N N 86  
ATP "C5'" "C4'"  sing N N 87  
ATP "C5'" "H5'1" sing N N 88  
ATP "C5'" "H5'2" sing N N 89  
ATP "C4'" "O4'"  sing N N 90  
ATP "C4'" "C3'"  sing N N 91  
ATP "C4'" "H4'"  sing N N 92  
ATP "O4'" "C1'"  sing N N 93  
ATP "C3'" "O3'"  sing N N 94  
ATP "C3'" "C2'"  sing N N 95  
ATP "C3'" "H3'"  sing N N 96  
ATP "O3'" "HO3'" sing N N 97  
ATP "C2'" "O2'"  sing N N 98  
ATP "C2'" "C1'"  sing N N 99  
ATP "C2'" "H2'"  sing N N 100 
ATP "O2'" "HO2'" sing N N 101 
ATP "C1'" N9     sing N N 102 
ATP "C1'" "H1'"  sing N N 103 
ATP N9    C8     sing Y N 104 
ATP N9    C4     sing Y N 105 
ATP C8    N7     doub Y N 106 
ATP C8    H8     sing N N 107 
ATP N7    C5     sing Y N 108 
ATP C5    C6     sing Y N 109 
ATP C5    C4     doub Y N 110 
ATP C6    N6     sing N N 111 
ATP C6    N1     doub Y N 112 
ATP N6    HN61   sing N N 113 
ATP N6    HN62   sing N N 114 
ATP N1    C2     sing Y N 115 
ATP C2    N3     doub Y N 116 
ATP C2    H2     sing N N 117 
ATP N3    C4     sing Y N 118 
CLR C1    C2     sing N N 119 
CLR C1    C10    sing N N 120 
CLR C1    H11    sing N N 121 
CLR C1    H12    sing N N 122 
CLR C2    C3     sing N N 123 
CLR C2    H21    sing N N 124 
CLR C2    H22    sing N N 125 
CLR C3    C4     sing N N 126 
CLR C3    O1     sing N N 127 
CLR C3    H3     sing N N 128 
CLR C4    C5     sing N N 129 
CLR C4    H41    sing N N 130 
CLR C4    H42    sing N N 131 
CLR C5    C6     doub N N 132 
CLR C5    C10    sing N N 133 
CLR C6    C7     sing N N 134 
CLR C6    H6     sing N N 135 
CLR C7    C8     sing N N 136 
CLR C7    H71    sing N N 137 
CLR C7    H72    sing N N 138 
CLR C8    C9     sing N N 139 
CLR C8    C14    sing N N 140 
CLR C8    H8     sing N N 141 
CLR C9    C10    sing N N 142 
CLR C9    C11    sing N N 143 
CLR C9    H9     sing N N 144 
CLR C10   C19    sing N N 145 
CLR C11   C12    sing N N 146 
CLR C11   H111   sing N N 147 
CLR C11   H112   sing N N 148 
CLR C12   C13    sing N N 149 
CLR C12   H121   sing N N 150 
CLR C12   H122   sing N N 151 
CLR C13   C14    sing N N 152 
CLR C13   C17    sing N N 153 
CLR C13   C18    sing N N 154 
CLR C14   C15    sing N N 155 
CLR C14   H14    sing N N 156 
CLR C15   C16    sing N N 157 
CLR C15   H151   sing N N 158 
CLR C15   H152   sing N N 159 
CLR C16   C17    sing N N 160 
CLR C16   H161   sing N N 161 
CLR C16   H162   sing N N 162 
CLR C17   C20    sing N N 163 
CLR C17   H17    sing N N 164 
CLR C18   H181   sing N N 165 
CLR C18   H182   sing N N 166 
CLR C18   H183   sing N N 167 
CLR C19   H191   sing N N 168 
CLR C19   H192   sing N N 169 
CLR C19   H193   sing N N 170 
CLR C20   C21    sing N N 171 
CLR C20   C22    sing N N 172 
CLR C20   H20    sing N N 173 
CLR C21   H211   sing N N 174 
CLR C21   H212   sing N N 175 
CLR C21   H213   sing N N 176 
CLR C22   C23    sing N N 177 
CLR C22   H221   sing N N 178 
CLR C22   H222   sing N N 179 
CLR C23   C24    sing N N 180 
CLR C23   H231   sing N N 181 
CLR C23   H232   sing N N 182 
CLR C24   C25    sing N N 183 
CLR C24   H241   sing N N 184 
CLR C24   H242   sing N N 185 
CLR C25   C26    sing N N 186 
CLR C25   C27    sing N N 187 
CLR C25   H25    sing N N 188 
CLR C26   H261   sing N N 189 
CLR C26   H262   sing N N 190 
CLR C26   H263   sing N N 191 
CLR C27   H271   sing N N 192 
CLR C27   H272   sing N N 193 
CLR C27   H273   sing N N 194 
CLR O1    H1     sing N N 195 
CYS N     CA     sing N N 196 
CYS N     H      sing N N 197 
CYS N     H2     sing N N 198 
CYS CA    C      sing N N 199 
CYS CA    CB     sing N N 200 
CYS CA    HA     sing N N 201 
CYS C     O      doub N N 202 
CYS C     OXT    sing N N 203 
CYS CB    SG     sing N N 204 
CYS CB    HB2    sing N N 205 
CYS CB    HB3    sing N N 206 
CYS SG    HG     sing N N 207 
CYS OXT   HXT    sing N N 208 
D10 C1    C2     sing N N 209 
D10 C1    H11    sing N N 210 
D10 C1    H12    sing N N 211 
D10 C1    H13    sing N N 212 
D10 C2    C3     sing N N 213 
D10 C2    H21    sing N N 214 
D10 C2    H22    sing N N 215 
D10 C3    C4     sing N N 216 
D10 C3    H31    sing N N 217 
D10 C3    H32    sing N N 218 
D10 C4    C5     sing N N 219 
D10 C4    H41    sing N N 220 
D10 C4    H42    sing N N 221 
D10 C5    C6     sing N N 222 
D10 C5    H51    sing N N 223 
D10 C5    H52    sing N N 224 
D10 C6    C7     sing N N 225 
D10 C6    H61    sing N N 226 
D10 C6    H62    sing N N 227 
D10 C7    C8     sing N N 228 
D10 C7    H71    sing N N 229 
D10 C7    H72    sing N N 230 
D10 C8    C9     sing N N 231 
D10 C8    H81    sing N N 232 
D10 C8    H82    sing N N 233 
D10 C9    C10    sing N N 234 
D10 C9    H91    sing N N 235 
D10 C9    H92    sing N N 236 
D10 C10   H101   sing N N 237 
D10 C10   H102   sing N N 238 
D10 C10   H103   sing N N 239 
GLN N     CA     sing N N 240 
GLN N     H      sing N N 241 
GLN N     H2     sing N N 242 
GLN CA    C      sing N N 243 
GLN CA    CB     sing N N 244 
GLN CA    HA     sing N N 245 
GLN C     O      doub N N 246 
GLN C     OXT    sing N N 247 
GLN CB    CG     sing N N 248 
GLN CB    HB2    sing N N 249 
GLN CB    HB3    sing N N 250 
GLN CG    CD     sing N N 251 
GLN CG    HG2    sing N N 252 
GLN CG    HG3    sing N N 253 
GLN CD    OE1    doub N N 254 
GLN CD    NE2    sing N N 255 
GLN NE2   HE21   sing N N 256 
GLN NE2   HE22   sing N N 257 
GLN OXT   HXT    sing N N 258 
GLU N     CA     sing N N 259 
GLU N     H      sing N N 260 
GLU N     H2     sing N N 261 
GLU CA    C      sing N N 262 
GLU CA    CB     sing N N 263 
GLU CA    HA     sing N N 264 
GLU C     O      doub N N 265 
GLU C     OXT    sing N N 266 
GLU CB    CG     sing N N 267 
GLU CB    HB2    sing N N 268 
GLU CB    HB3    sing N N 269 
GLU CG    CD     sing N N 270 
GLU CG    HG2    sing N N 271 
GLU CG    HG3    sing N N 272 
GLU CD    OE1    doub N N 273 
GLU CD    OE2    sing N N 274 
GLU OE2   HE2    sing N N 275 
GLU OXT   HXT    sing N N 276 
GLY N     CA     sing N N 277 
GLY N     H      sing N N 278 
GLY N     H2     sing N N 279 
GLY CA    C      sing N N 280 
GLY CA    HA2    sing N N 281 
GLY CA    HA3    sing N N 282 
GLY C     O      doub N N 283 
GLY C     OXT    sing N N 284 
GLY OXT   HXT    sing N N 285 
HIS N     CA     sing N N 286 
HIS N     H      sing N N 287 
HIS N     H2     sing N N 288 
HIS CA    C      sing N N 289 
HIS CA    CB     sing N N 290 
HIS CA    HA     sing N N 291 
HIS C     O      doub N N 292 
HIS C     OXT    sing N N 293 
HIS CB    CG     sing N N 294 
HIS CB    HB2    sing N N 295 
HIS CB    HB3    sing N N 296 
HIS CG    ND1    sing Y N 297 
HIS CG    CD2    doub Y N 298 
HIS ND1   CE1    doub Y N 299 
HIS ND1   HD1    sing N N 300 
HIS CD2   NE2    sing Y N 301 
HIS CD2   HD2    sing N N 302 
HIS CE1   NE2    sing Y N 303 
HIS CE1   HE1    sing N N 304 
HIS NE2   HE2    sing N N 305 
HIS OXT   HXT    sing N N 306 
HOH O     H1     sing N N 307 
HOH O     H2     sing N N 308 
ILE N     CA     sing N N 309 
ILE N     H      sing N N 310 
ILE N     H2     sing N N 311 
ILE CA    C      sing N N 312 
ILE CA    CB     sing N N 313 
ILE CA    HA     sing N N 314 
ILE C     O      doub N N 315 
ILE C     OXT    sing N N 316 
ILE CB    CG1    sing N N 317 
ILE CB    CG2    sing N N 318 
ILE CB    HB     sing N N 319 
ILE CG1   CD1    sing N N 320 
ILE CG1   HG12   sing N N 321 
ILE CG1   HG13   sing N N 322 
ILE CG2   HG21   sing N N 323 
ILE CG2   HG22   sing N N 324 
ILE CG2   HG23   sing N N 325 
ILE CD1   HD11   sing N N 326 
ILE CD1   HD12   sing N N 327 
ILE CD1   HD13   sing N N 328 
ILE OXT   HXT    sing N N 329 
LEU N     CA     sing N N 330 
LEU N     H      sing N N 331 
LEU N     H2     sing N N 332 
LEU CA    C      sing N N 333 
LEU CA    CB     sing N N 334 
LEU CA    HA     sing N N 335 
LEU C     O      doub N N 336 
LEU C     OXT    sing N N 337 
LEU CB    CG     sing N N 338 
LEU CB    HB2    sing N N 339 
LEU CB    HB3    sing N N 340 
LEU CG    CD1    sing N N 341 
LEU CG    CD2    sing N N 342 
LEU CG    HG     sing N N 343 
LEU CD1   HD11   sing N N 344 
LEU CD1   HD12   sing N N 345 
LEU CD1   HD13   sing N N 346 
LEU CD2   HD21   sing N N 347 
LEU CD2   HD22   sing N N 348 
LEU CD2   HD23   sing N N 349 
LEU OXT   HXT    sing N N 350 
LYS N     CA     sing N N 351 
LYS N     H      sing N N 352 
LYS N     H2     sing N N 353 
LYS CA    C      sing N N 354 
LYS CA    CB     sing N N 355 
LYS CA    HA     sing N N 356 
LYS C     O      doub N N 357 
LYS C     OXT    sing N N 358 
LYS CB    CG     sing N N 359 
LYS CB    HB2    sing N N 360 
LYS CB    HB3    sing N N 361 
LYS CG    CD     sing N N 362 
LYS CG    HG2    sing N N 363 
LYS CG    HG3    sing N N 364 
LYS CD    CE     sing N N 365 
LYS CD    HD2    sing N N 366 
LYS CD    HD3    sing N N 367 
LYS CE    NZ     sing N N 368 
LYS CE    HE2    sing N N 369 
LYS CE    HE3    sing N N 370 
LYS NZ    HZ1    sing N N 371 
LYS NZ    HZ2    sing N N 372 
LYS NZ    HZ3    sing N N 373 
LYS OXT   HXT    sing N N 374 
MET N     CA     sing N N 375 
MET N     H      sing N N 376 
MET N     H2     sing N N 377 
MET CA    C      sing N N 378 
MET CA    CB     sing N N 379 
MET CA    HA     sing N N 380 
MET C     O      doub N N 381 
MET C     OXT    sing N N 382 
MET CB    CG     sing N N 383 
MET CB    HB2    sing N N 384 
MET CB    HB3    sing N N 385 
MET CG    SD     sing N N 386 
MET CG    HG2    sing N N 387 
MET CG    HG3    sing N N 388 
MET SD    CE     sing N N 389 
MET CE    HE1    sing N N 390 
MET CE    HE2    sing N N 391 
MET CE    HE3    sing N N 392 
MET OXT   HXT    sing N N 393 
PHE N     CA     sing N N 394 
PHE N     H      sing N N 395 
PHE N     H2     sing N N 396 
PHE CA    C      sing N N 397 
PHE CA    CB     sing N N 398 
PHE CA    HA     sing N N 399 
PHE C     O      doub N N 400 
PHE C     OXT    sing N N 401 
PHE CB    CG     sing N N 402 
PHE CB    HB2    sing N N 403 
PHE CB    HB3    sing N N 404 
PHE CG    CD1    doub Y N 405 
PHE CG    CD2    sing Y N 406 
PHE CD1   CE1    sing Y N 407 
PHE CD1   HD1    sing N N 408 
PHE CD2   CE2    doub Y N 409 
PHE CD2   HD2    sing N N 410 
PHE CE1   CZ     doub Y N 411 
PHE CE1   HE1    sing N N 412 
PHE CE2   CZ     sing Y N 413 
PHE CE2   HE2    sing N N 414 
PHE CZ    HZ     sing N N 415 
PHE OXT   HXT    sing N N 416 
PRO N     CA     sing N N 417 
PRO N     CD     sing N N 418 
PRO N     H      sing N N 419 
PRO CA    C      sing N N 420 
PRO CA    CB     sing N N 421 
PRO CA    HA     sing N N 422 
PRO C     O      doub N N 423 
PRO C     OXT    sing N N 424 
PRO CB    CG     sing N N 425 
PRO CB    HB2    sing N N 426 
PRO CB    HB3    sing N N 427 
PRO CG    CD     sing N N 428 
PRO CG    HG2    sing N N 429 
PRO CG    HG3    sing N N 430 
PRO CD    HD2    sing N N 431 
PRO CD    HD3    sing N N 432 
PRO OXT   HXT    sing N N 433 
SEP N     CA     sing N N 434 
SEP N     H      sing N N 435 
SEP N     H2     sing N N 436 
SEP CA    CB     sing N N 437 
SEP CA    C      sing N N 438 
SEP CA    HA     sing N N 439 
SEP CB    OG     sing N N 440 
SEP CB    HB2    sing N N 441 
SEP CB    HB3    sing N N 442 
SEP OG    P      sing N N 443 
SEP C     O      doub N N 444 
SEP C     OXT    sing N N 445 
SEP OXT   HXT    sing N N 446 
SEP P     O1P    doub N N 447 
SEP P     O2P    sing N N 448 
SEP P     O3P    sing N N 449 
SEP O2P   HOP2   sing N N 450 
SEP O3P   HOP3   sing N N 451 
SER N     CA     sing N N 452 
SER N     H      sing N N 453 
SER N     H2     sing N N 454 
SER CA    C      sing N N 455 
SER CA    CB     sing N N 456 
SER CA    HA     sing N N 457 
SER C     O      doub N N 458 
SER C     OXT    sing N N 459 
SER CB    OG     sing N N 460 
SER CB    HB2    sing N N 461 
SER CB    HB3    sing N N 462 
SER OG    HG     sing N N 463 
SER OXT   HXT    sing N N 464 
THR N     CA     sing N N 465 
THR N     H      sing N N 466 
THR N     H2     sing N N 467 
THR CA    C      sing N N 468 
THR CA    CB     sing N N 469 
THR CA    HA     sing N N 470 
THR C     O      doub N N 471 
THR C     OXT    sing N N 472 
THR CB    OG1    sing N N 473 
THR CB    CG2    sing N N 474 
THR CB    HB     sing N N 475 
THR OG1   HG1    sing N N 476 
THR CG2   HG21   sing N N 477 
THR CG2   HG22   sing N N 478 
THR CG2   HG23   sing N N 479 
THR OXT   HXT    sing N N 480 
TPO N     CA     sing N N 481 
TPO N     H      sing N N 482 
TPO N     H2     sing N N 483 
TPO CA    CB     sing N N 484 
TPO CA    C      sing N N 485 
TPO CA    HA     sing N N 486 
TPO CB    CG2    sing N N 487 
TPO CB    OG1    sing N N 488 
TPO CB    HB     sing N N 489 
TPO CG2   HG21   sing N N 490 
TPO CG2   HG22   sing N N 491 
TPO CG2   HG23   sing N N 492 
TPO OG1   P      sing N N 493 
TPO P     O1P    doub N N 494 
TPO P     O2P    sing N N 495 
TPO P     O3P    sing N N 496 
TPO O2P   HOP2   sing N N 497 
TPO O3P   HOP3   sing N N 498 
TPO C     O      doub N N 499 
TPO C     OXT    sing N N 500 
TPO OXT   HXT    sing N N 501 
TRP N     CA     sing N N 502 
TRP N     H      sing N N 503 
TRP N     H2     sing N N 504 
TRP CA    C      sing N N 505 
TRP CA    CB     sing N N 506 
TRP CA    HA     sing N N 507 
TRP C     O      doub N N 508 
TRP C     OXT    sing N N 509 
TRP CB    CG     sing N N 510 
TRP CB    HB2    sing N N 511 
TRP CB    HB3    sing N N 512 
TRP CG    CD1    doub Y N 513 
TRP CG    CD2    sing Y N 514 
TRP CD1   NE1    sing Y N 515 
TRP CD1   HD1    sing N N 516 
TRP CD2   CE2    doub Y N 517 
TRP CD2   CE3    sing Y N 518 
TRP NE1   CE2    sing Y N 519 
TRP NE1   HE1    sing N N 520 
TRP CE2   CZ2    sing Y N 521 
TRP CE3   CZ3    doub Y N 522 
TRP CE3   HE3    sing N N 523 
TRP CZ2   CH2    doub Y N 524 
TRP CZ2   HZ2    sing N N 525 
TRP CZ3   CH2    sing Y N 526 
TRP CZ3   HZ3    sing N N 527 
TRP CH2   HH2    sing N N 528 
TRP OXT   HXT    sing N N 529 
TYR N     CA     sing N N 530 
TYR N     H      sing N N 531 
TYR N     H2     sing N N 532 
TYR CA    C      sing N N 533 
TYR CA    CB     sing N N 534 
TYR CA    HA     sing N N 535 
TYR C     O      doub N N 536 
TYR C     OXT    sing N N 537 
TYR CB    CG     sing N N 538 
TYR CB    HB2    sing N N 539 
TYR CB    HB3    sing N N 540 
TYR CG    CD1    doub Y N 541 
TYR CG    CD2    sing Y N 542 
TYR CD1   CE1    sing Y N 543 
TYR CD1   HD1    sing N N 544 
TYR CD2   CE2    doub Y N 545 
TYR CD2   HD2    sing N N 546 
TYR CE1   CZ     doub Y N 547 
TYR CE1   HE1    sing N N 548 
TYR CE2   CZ     sing Y N 549 
TYR CE2   HE2    sing N N 550 
TYR CZ    OH     sing N N 551 
TYR OH    HH     sing N N 552 
TYR OXT   HXT    sing N N 553 
UND C1    C2     sing N N 554 
UND C1    H11    sing N N 555 
UND C1    H12    sing N N 556 
UND C1    H13    sing N N 557 
UND C2    C3     sing N N 558 
UND C2    H21    sing N N 559 
UND C2    H22    sing N N 560 
UND C3    C4     sing N N 561 
UND C3    H31    sing N N 562 
UND C3    H32    sing N N 563 
UND C4    C5     sing N N 564 
UND C4    H41    sing N N 565 
UND C4    H42    sing N N 566 
UND C5    C6     sing N N 567 
UND C5    H51    sing N N 568 
UND C5    H52    sing N N 569 
UND C6    C7     sing N N 570 
UND C6    H61    sing N N 571 
UND C6    H62    sing N N 572 
UND C7    C8     sing N N 573 
UND C7    H71    sing N N 574 
UND C7    H72    sing N N 575 
UND C8    C9     sing N N 576 
UND C8    H81    sing N N 577 
UND C8    H82    sing N N 578 
UND C9    C10    sing N N 579 
UND C9    H91    sing N N 580 
UND C9    H92    sing N N 581 
UND C10   C11    sing N N 582 
UND C10   H101   sing N N 583 
UND C10   H102   sing N N 584 
UND C11   H111   sing N N 585 
UND C11   H112   sing N N 586 
UND C11   H113   sing N N 587 
VAL N     CA     sing N N 588 
VAL N     H      sing N N 589 
VAL N     H2     sing N N 590 
VAL CA    C      sing N N 591 
VAL CA    CB     sing N N 592 
VAL CA    HA     sing N N 593 
VAL C     O      doub N N 594 
VAL C     OXT    sing N N 595 
VAL CB    CG1    sing N N 596 
VAL CB    CG2    sing N N 597 
VAL CB    HB     sing N N 598 
VAL CG1   HG11   sing N N 599 
VAL CG1   HG12   sing N N 600 
VAL CG1   HG13   sing N N 601 
VAL CG2   HG21   sing N N 602 
VAL CG2   HG22   sing N N 603 
VAL CG2   HG23   sing N N 604 
VAL OXT   HXT    sing N N 605 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2024-10-08 
_em_admin.deposition_site    RCSB 
_em_admin.entry_id           9DW9 
_em_admin.last_update        2024-11-27 
_em_admin.map_release_date   2024-11-13 
_em_admin.title              'Phosphorylated (E1371Q)CFTR in complex with PKA-C' 
# 
_em_ctf_correction.details                  ? 
_em_ctf_correction.em_image_processing_id   1 
_em_ctf_correction.id                       1 
_em_ctf_correction.type                     'PHASE FLIPPING AND AMPLITUDE CORRECTION' 
# 
_em_entity_assembly_molwt.entity_assembly_id   1 
_em_entity_assembly_molwt.experimental_flag    NO 
_em_entity_assembly_molwt.id                   1 
_em_entity_assembly_molwt.units                MEGADALTONS 
_em_entity_assembly_molwt.value                0.21 
# 
_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          9913 
_em_entity_assembly_naturalsource.organism             'Bos taurus' 
_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         52.5 
_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 
'PARTICLE SELECTION'       ? 1  1 ? ? ? ? 
'IMAGE ACQUISITION'        ? 2  ? ? 1 ? ? 
MASKING                    ? 3  ? ? ? ? ? 
'CTF CORRECTION'           ? 4  1 ? ? ? ? 
'LAYERLINE INDEXING'       ? 5  ? ? ? ? ? 
'DIFFRACTION INDEXING'     ? 6  ? ? ? ? ? 
'MODEL FITTING'            ? 7  ? ? ? ? ? 
'MODEL REFINEMENT'         ? 8  ? ? ? ? ? 
OTHER                      ? 9  ? ? ? ? ? 
'INITIAL EULER ASSIGNMENT' ? 10 1 ? ? ? ? 
'FINAL EULER ASSIGNMENT'   ? 11 1 ? ? ? ? 
CLASSIFICATION             ? 12 1 ? ? ? ? 
RECONSTRUCTION             ? 13 1 ? ? ? ? 
# 
_em_specimen.concentration           5 
_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 
'Howard Hughes Medical Institute (HHMI)' 'United States' ? 1 
'Cystic Fibrosis Foundation'             'United States' ? 2 
# 
_atom_sites.entry_id                    9DW9 
_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  
CL 
MG 
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     . MET A 1 1    ? 176.565 146.962 135.236 1.00 83.77  ? 1    MET A N     1 
ATOM   2     C  CA    . MET A 1 1    ? 175.367 146.532 135.945 1.00 83.31  ? 1    MET A CA    1 
ATOM   3     C  C     . MET A 1 1    ? 175.555 145.095 136.427 1.00 82.30  ? 1    MET A C     1 
ATOM   4     O  O     . MET A 1 1    ? 175.579 144.159 135.628 1.00 79.81  ? 1    MET A O     1 
ATOM   5     C  CB    . MET A 1 1    ? 174.137 146.656 135.044 1.00 75.85  ? 1    MET A CB    1 
ATOM   6     C  CG    . MET A 1 1    ? 172.904 147.188 135.756 1.00 74.39  ? 1    MET A CG    1 
ATOM   7     S  SD    . MET A 1 1    ? 171.397 147.088 134.772 1.00 79.06  ? 1    MET A SD    1 
ATOM   8     C  CE    . MET A 1 1    ? 170.217 147.835 135.891 1.00 60.02  ? 1    MET A CE    1 
ATOM   9     N  N     . GLN A 1 2    ? 175.698 144.933 137.739 1.00 77.80  ? 2    GLN A N     1 
ATOM   10    C  CA    . GLN A 1 2    ? 176.091 143.662 138.324 1.00 76.25  ? 2    GLN A CA    1 
ATOM   11    C  C     . GLN A 1 2    ? 174.910 142.700 138.426 1.00 77.01  ? 2    GLN A C     1 
ATOM   12    O  O     . GLN A 1 2    ? 173.744 143.079 138.295 1.00 77.79  ? 2    GLN A O     1 
ATOM   13    C  CB    . GLN A 1 2    ? 176.689 143.874 139.713 1.00 77.68  ? 2    GLN A CB    1 
ATOM   14    C  CG    . GLN A 1 2    ? 177.914 144.761 139.738 1.00 81.50  ? 2    GLN A CG    1 
ATOM   15    C  CD    . GLN A 1 2    ? 178.285 145.188 141.143 1.00 83.69  ? 2    GLN A CD    1 
ATOM   16    O  OE1   . GLN A 1 2    ? 178.756 144.381 141.944 1.00 79.77  ? 2    GLN A OE1   1 
ATOM   17    N  NE2   . GLN A 1 2    ? 178.068 146.461 141.453 1.00 76.10  ? 2    GLN A NE2   1 
ATOM   18    N  N     . ARG A 1 3    ? 175.240 141.433 138.655 1.00 73.97  ? 3    ARG A N     1 
ATOM   19    C  CA    . ARG A 1 3    ? 174.242 140.420 138.955 1.00 71.28  ? 3    ARG A CA    1 
ATOM   20    C  C     . ARG A 1 3    ? 173.660 140.642 140.347 1.00 70.00  ? 3    ARG A C     1 
ATOM   21    O  O     . ARG A 1 3    ? 174.327 141.160 141.246 1.00 69.61  ? 3    ARG A O     1 
ATOM   22    C  CB    . ARG A 1 3    ? 174.867 139.029 138.871 1.00 78.27  ? 3    ARG A CB    1 
ATOM   23    C  CG    . ARG A 1 3    ? 175.251 138.600 137.460 1.00 82.15  ? 3    ARG A CG    1 
ATOM   24    C  CD    . ARG A 1 3    ? 174.119 137.920 136.665 1.00 87.44  ? 3    ARG A CD    1 
ATOM   25    N  NE    . ARG A 1 3    ? 173.066 137.239 137.421 1.00 91.80  ? 3    ARG A NE    1 
ATOM   26    C  CZ    . ARG A 1 3    ? 173.246 136.348 138.391 1.00 87.24  ? 3    ARG A CZ    1 
ATOM   27    N  NH1   . ARG A 1 3    ? 174.450 135.909 138.722 1.00 83.60  ? 3    ARG A NH1   1 
ATOM   28    N  NH2   . ARG A 1 3    ? 172.185 135.859 139.024 1.00 84.65  ? 3    ARG A NH2   1 
ATOM   29    N  N     . SER A 1 4    ? 172.405 140.252 140.518 1.00 69.63  ? 4    SER A N     1 
ATOM   30    C  CA    . SER A 1 4    ? 171.770 140.335 141.827 1.00 69.07  ? 4    SER A CA    1 
ATOM   31    C  C     . SER A 1 4    ? 172.405 139.323 142.773 1.00 71.40  ? 4    SER A C     1 
ATOM   32    O  O     . SER A 1 4    ? 172.394 138.120 142.474 1.00 72.79  ? 4    SER A O     1 
ATOM   33    C  CB    . SER A 1 4    ? 170.270 140.078 141.723 1.00 64.33  ? 4    SER A CB    1 
ATOM   34    O  OG    . SER A 1 4    ? 170.006 138.818 141.134 1.00 68.09  ? 4    SER A OG    1 
ATOM   35    N  N     . PRO A 1 5    ? 172.956 139.750 143.915 1.00 69.50  ? 5    PRO A N     1 
ATOM   36    C  CA    . PRO A 1 5    ? 173.572 138.788 144.839 1.00 67.07  ? 5    PRO A CA    1 
ATOM   37    C  C     . PRO A 1 5    ? 172.579 137.847 145.497 1.00 61.14  ? 5    PRO A C     1 
ATOM   38    O  O     . PRO A 1 5    ? 173.004 136.854 146.099 1.00 63.29  ? 5    PRO A O     1 
ATOM   39    C  CB    . PRO A 1 5    ? 174.256 139.688 145.873 1.00 60.54  ? 5    PRO A CB    1 
ATOM   40    C  CG    . PRO A 1 5    ? 173.424 140.918 145.883 1.00 58.64  ? 5    PRO A CG    1 
ATOM   41    C  CD    . PRO A 1 5    ? 172.987 141.120 144.452 1.00 61.72  ? 5    PRO A CD    1 
ATOM   42    N  N     . LEU A 1 6    ? 171.279 138.134 145.414 1.00 58.45  ? 6    LEU A N     1 
ATOM   43    C  CA    . LEU A 1 6    ? 170.274 137.243 145.982 1.00 61.25  ? 6    LEU A CA    1 
ATOM   44    C  C     . LEU A 1 6    ? 170.295 135.870 145.323 1.00 70.11  ? 6    LEU A C     1 
ATOM   45    O  O     . LEU A 1 6    ? 169.933 134.871 145.955 1.00 71.18  ? 6    LEU A O     1 
ATOM   46    C  CB    . LEU A 1 6    ? 168.888 137.873 145.845 1.00 53.36  ? 6    LEU A CB    1 
ATOM   47    C  CG    . LEU A 1 6    ? 167.692 137.070 146.354 1.00 52.90  ? 6    LEU A CG    1 
ATOM   48    C  CD1   . LEU A 1 6    ? 167.797 136.846 147.846 1.00 49.79  ? 6    LEU A CD1   1 
ATOM   49    C  CD2   . LEU A 1 6    ? 166.390 137.764 146.006 1.00 55.03  ? 6    LEU A CD2   1 
ATOM   50    N  N     . GLU A 1 7    ? 170.707 135.798 144.057 1.00 72.63  ? 7    GLU A N     1 
ATOM   51    C  CA    . GLU A 1 7    ? 170.631 134.536 143.330 1.00 77.16  ? 7    GLU A CA    1 
ATOM   52    C  C     . GLU A 1 7    ? 171.633 133.516 143.857 1.00 75.37  ? 7    GLU A C     1 
ATOM   53    O  O     . GLU A 1 7    ? 171.329 132.319 143.919 1.00 77.82  ? 7    GLU A O     1 
ATOM   54    C  CB    . GLU A 1 7    ? 170.845 134.780 141.838 1.00 85.34  ? 7    GLU A CB    1 
ATOM   55    C  CG    . GLU A 1 7    ? 169.706 135.529 141.175 1.00 85.45  ? 7    GLU A CG    1 
ATOM   56    C  CD    . GLU A 1 7    ? 168.474 134.668 141.003 1.00 91.69  ? 7    GLU A CD    1 
ATOM   57    O  OE1   . GLU A 1 7    ? 168.608 133.425 140.999 1.00 97.71  ? 7    GLU A OE1   1 
ATOM   58    O  OE2   . GLU A 1 7    ? 167.369 135.232 140.879 1.00 86.45  ? 7    GLU A OE2   1 
ATOM   59    N  N     . LYS A 1 8    ? 172.829 133.961 144.241 1.00 72.86  ? 8    LYS A N     1 
ATOM   60    C  CA    . LYS A 1 8    ? 173.881 133.063 144.702 1.00 72.43  ? 8    LYS A CA    1 
ATOM   61    C  C     . LYS A 1 8    ? 174.193 133.272 146.181 1.00 71.19  ? 8    LYS A C     1 
ATOM   62    O  O     . LYS A 1 8    ? 175.330 133.079 146.617 1.00 69.58  ? 8    LYS A O     1 
ATOM   63    C  CB    . LYS A 1 8    ? 175.141 133.227 143.853 1.00 74.98  ? 8    LYS A CB    1 
ATOM   64    C  CG    . LYS A 1 8    ? 175.292 132.152 142.786 1.00 80.86  ? 8    LYS A CG    1 
ATOM   65    C  CD    . LYS A 1 8    ? 176.348 132.503 141.748 1.00 79.64  ? 8    LYS A CD    1 
ATOM   66    C  CE    . LYS A 1 8    ? 177.627 133.012 142.387 1.00 76.01  ? 8    LYS A CE    1 
ATOM   67    N  NZ    . LYS A 1 8    ? 178.408 133.840 141.428 1.00 78.87  ? 8    LYS A NZ    1 
ATOM   68    N  N     . ALA A 1 9    ? 173.192 133.670 146.959 1.00 69.95  ? 9    ALA A N     1 
ATOM   69    C  CA    . ALA A 1 9    ? 173.342 133.869 148.392 1.00 64.78  ? 9    ALA A CA    1 
ATOM   70    C  C     . ALA A 1 9    ? 173.015 132.592 149.157 1.00 63.13  ? 9    ALA A C     1 
ATOM   71    O  O     . ALA A 1 9    ? 172.261 131.736 148.688 1.00 61.77  ? 9    ALA A O     1 
ATOM   72    C  CB    . ALA A 1 9    ? 172.445 135.010 148.876 1.00 56.36  ? 9    ALA A CB    1 
ATOM   73    N  N     . SER A 1 10   ? 173.598 132.474 150.347 1.00 62.35  ? 10   SER A N     1 
ATOM   74    C  CA    . SER A 1 10   ? 173.356 131.333 151.218 1.00 59.12  ? 10   SER A CA    1 
ATOM   75    C  C     . SER A 1 10   ? 171.948 131.382 151.808 1.00 57.21  ? 10   SER A C     1 
ATOM   76    O  O     . SER A 1 10   ? 171.227 132.376 151.690 1.00 60.15  ? 10   SER A O     1 
ATOM   77    C  CB    . SER A 1 10   ? 174.389 131.295 152.342 1.00 54.28  ? 10   SER A CB    1 
ATOM   78    O  OG    . SER A 1 10   ? 175.686 131.066 151.827 1.00 59.98  ? 10   SER A OG    1 
ATOM   79    N  N     . VAL A 1 11   ? 171.553 130.271 152.435 1.00 55.44  ? 11   VAL A N     1 
ATOM   80    C  CA    . VAL A 1 11   ? 170.278 130.228 153.149 1.00 55.62  ? 11   VAL A CA    1 
ATOM   81    C  C     . VAL A 1 11   ? 170.289 131.206 154.318 1.00 52.93  ? 11   VAL A C     1 
ATOM   82    O  O     . VAL A 1 11   ? 169.333 131.961 154.530 1.00 51.48  ? 11   VAL A O     1 
ATOM   83    C  CB    . VAL A 1 11   ? 169.971 128.793 153.615 1.00 56.79  ? 11   VAL A CB    1 
ATOM   84    C  CG1   . VAL A 1 11   ? 168.872 128.795 154.662 1.00 47.08  ? 11   VAL A CG1   1 
ATOM   85    C  CG2   . VAL A 1 11   ? 169.573 127.928 152.434 1.00 59.30  ? 11   VAL A CG2   1 
ATOM   86    N  N     . VAL A 1 12   ? 171.375 131.210 155.092 1.00 50.46  ? 12   VAL A N     1 
ATOM   87    C  CA    . VAL A 1 12   ? 171.463 132.112 156.237 1.00 50.39  ? 12   VAL A CA    1 
ATOM   88    C  C     . VAL A 1 12   ? 171.562 133.559 155.771 1.00 48.60  ? 12   VAL A C     1 
ATOM   89    O  O     . VAL A 1 12   ? 171.011 134.467 156.404 1.00 47.54  ? 12   VAL A O     1 
ATOM   90    C  CB    . VAL A 1 12   ? 172.650 131.717 157.135 1.00 50.82  ? 12   VAL A CB    1 
ATOM   91    C  CG1   . VAL A 1 12   ? 172.713 132.608 158.366 1.00 46.71  ? 12   VAL A CG1   1 
ATOM   92    C  CG2   . VAL A 1 12   ? 172.541 130.261 157.541 1.00 50.93  ? 12   VAL A CG2   1 
ATOM   93    N  N     . SER A 1 13   ? 172.265 133.800 154.663 1.00 49.60  ? 13   SER A N     1 
ATOM   94    C  CA    . SER A 1 13   ? 172.365 135.157 154.134 1.00 46.89  ? 13   SER A CA    1 
ATOM   95    C  C     . SER A 1 13   ? 171.008 135.675 153.675 1.00 44.37  ? 13   SER A C     1 
ATOM   96    O  O     . SER A 1 13   ? 170.678 136.845 153.898 1.00 44.17  ? 13   SER A O     1 
ATOM   97    C  CB    . SER A 1 13   ? 173.372 135.196 152.986 1.00 51.32  ? 13   SER A CB    1 
ATOM   98    O  OG    . SER A 1 13   ? 173.608 136.524 152.558 1.00 49.27  ? 13   SER A OG    1 
ATOM   99    N  N     . LYS A 1 14   ? 170.209 134.823 153.030 1.00 45.49  ? 14   LYS A N     1 
ATOM   100   C  CA    . LYS A 1 14   ? 168.880 135.244 152.601 1.00 46.07  ? 14   LYS A CA    1 
ATOM   101   C  C     . LYS A 1 14   ? 167.935 135.410 153.783 1.00 44.56  ? 14   LYS A C     1 
ATOM   102   O  O     . LYS A 1 14   ? 167.088 136.311 153.785 1.00 41.02  ? 14   LYS A O     1 
ATOM   103   C  CB    . LYS A 1 14   ? 168.304 134.244 151.599 1.00 44.95  ? 14   LYS A CB    1 
ATOM   104   C  CG    . LYS A 1 14   ? 168.952 134.292 150.232 1.00 50.37  ? 14   LYS A CG    1 
ATOM   105   C  CD    . LYS A 1 14   ? 168.182 133.445 149.235 1.00 53.12  ? 14   LYS A CD    1 
ATOM   106   C  CE    . LYS A 1 14   ? 168.260 131.972 149.585 1.00 56.85  ? 14   LYS A CE    1 
ATOM   107   N  NZ    . LYS A 1 14   ? 167.561 131.136 148.577 1.00 52.89  ? 14   LYS A NZ    1 
ATOM   108   N  N     . LEU A 1 15   ? 168.054 134.544 154.791 1.00 46.81  ? 15   LEU A N     1 
ATOM   109   C  CA    . LEU A 1 15   ? 167.150 134.606 155.935 1.00 42.52  ? 15   LEU A CA    1 
ATOM   110   C  C     . LEU A 1 15   ? 167.279 135.929 156.677 1.00 40.11  ? 15   LEU A C     1 
ATOM   111   O  O     . LEU A 1 15   ? 166.273 136.520 157.083 1.00 41.77  ? 15   LEU A O     1 
ATOM   112   C  CB    . LEU A 1 15   ? 167.423 133.437 156.881 1.00 41.00  ? 15   LEU A CB    1 
ATOM   113   C  CG    . LEU A 1 15   ? 166.308 133.082 157.864 1.00 41.77  ? 15   LEU A CG    1 
ATOM   114   C  CD1   . LEU A 1 15   ? 165.136 132.448 157.135 1.00 41.38  ? 15   LEU A CD1   1 
ATOM   115   C  CD2   . LEU A 1 15   ? 166.824 132.165 158.959 1.00 42.57  ? 15   LEU A CD2   1 
ATOM   116   N  N     . PHE A 1 16   ? 168.505 136.405 156.870 1.00 38.99  ? 16   PHE A N     1 
ATOM   117   C  CA    . PHE A 1 16   ? 168.759 137.637 157.602 1.00 35.07  ? 16   PHE A CA    1 
ATOM   118   C  C     . PHE A 1 16   ? 168.973 138.843 156.698 1.00 37.37  ? 16   PHE A C     1 
ATOM   119   O  O     . PHE A 1 16   ? 169.256 139.931 157.207 1.00 38.11  ? 16   PHE A O     1 
ATOM   120   C  CB    . PHE A 1 16   ? 169.968 137.459 158.519 1.00 34.31  ? 16   PHE A CB    1 
ATOM   121   C  CG    . PHE A 1 16   ? 169.694 136.607 159.719 1.00 37.60  ? 16   PHE A CG    1 
ATOM   122   C  CD1   . PHE A 1 16   ? 169.814 135.230 159.650 1.00 41.53  ? 16   PHE A CD1   1 
ATOM   123   C  CD2   . PHE A 1 16   ? 169.310 137.183 160.914 1.00 37.67  ? 16   PHE A CD2   1 
ATOM   124   C  CE1   . PHE A 1 16   ? 169.557 134.445 160.753 1.00 41.16  ? 16   PHE A CE1   1 
ATOM   125   C  CE2   . PHE A 1 16   ? 169.052 136.404 162.020 1.00 37.78  ? 16   PHE A CE2   1 
ATOM   126   C  CZ    . PHE A 1 16   ? 169.176 135.033 161.940 1.00 40.23  ? 16   PHE A CZ    1 
ATOM   127   N  N     . PHE A 1 17   ? 168.861 138.674 155.380 1.00 38.37  ? 17   PHE A N     1 
ATOM   128   C  CA    . PHE A 1 17   ? 168.996 139.768 154.414 1.00 34.82  ? 17   PHE A CA    1 
ATOM   129   C  C     . PHE A 1 17   ? 170.381 140.403 154.457 1.00 33.86  ? 17   PHE A C     1 
ATOM   130   O  O     . PHE A 1 17   ? 170.537 141.595 154.192 1.00 36.76  ? 17   PHE A O     1 
ATOM   131   C  CB    . PHE A 1 17   ? 167.907 140.826 154.620 1.00 30.86  ? 17   PHE A CB    1 
ATOM   132   C  CG    . PHE A 1 17   ? 166.514 140.286 154.484 1.00 33.92  ? 17   PHE A CG    1 
ATOM   133   C  CD1   . PHE A 1 17   ? 165.849 139.763 155.580 1.00 35.47  ? 17   PHE A CD1   1 
ATOM   134   C  CD2   . PHE A 1 17   ? 165.875 140.285 153.257 1.00 35.09  ? 17   PHE A CD2   1 
ATOM   135   C  CE1   . PHE A 1 17   ? 164.574 139.252 155.455 1.00 30.73  ? 17   PHE A CE1   1 
ATOM   136   C  CE2   . PHE A 1 17   ? 164.602 139.778 153.127 1.00 33.57  ? 17   PHE A CE2   1 
ATOM   137   C  CZ    . PHE A 1 17   ? 163.951 139.259 154.227 1.00 32.07  ? 17   PHE A CZ    1 
ATOM   138   N  N     . SER A 1 18   ? 171.403 139.609 154.780 1.00 35.05  ? 18   SER A N     1 
ATOM   139   C  CA    . SER A 1 18   ? 172.771 140.109 154.835 1.00 35.42  ? 18   SER A CA    1 
ATOM   140   C  C     . SER A 1 18   ? 173.332 140.458 153.464 1.00 37.61  ? 18   SER A C     1 
ATOM   141   O  O     . SER A 1 18   ? 174.374 141.115 153.390 1.00 39.96  ? 18   SER A O     1 
ATOM   142   C  CB    . SER A 1 18   ? 173.679 139.077 155.504 1.00 35.85  ? 18   SER A CB    1 
ATOM   143   O  OG    . SER A 1 18   ? 173.375 138.939 156.878 1.00 39.25  ? 18   SER A OG    1 
ATOM   144   N  N     . TRP A 1 19   ? 172.686 140.022 152.384 1.00 39.04  ? 19   TRP A N     1 
ATOM   145   C  CA    . TRP A 1 19   ? 173.155 140.337 151.041 1.00 36.58  ? 19   TRP A CA    1 
ATOM   146   C  C     . TRP A 1 19   ? 172.912 141.789 150.644 1.00 38.81  ? 19   TRP A C     1 
ATOM   147   O  O     . TRP A 1 19   ? 173.393 142.209 149.588 1.00 38.12  ? 19   TRP A O     1 
ATOM   148   C  CB    . TRP A 1 19   ? 172.513 139.379 150.037 1.00 37.14  ? 19   TRP A CB    1 
ATOM   149   C  CG    . TRP A 1 19   ? 171.020 139.414 150.020 1.00 39.75  ? 19   TRP A CG    1 
ATOM   150   C  CD1   . TRP A 1 19   ? 170.179 138.639 150.760 1.00 40.73  ? 19   TRP A CD1   1 
ATOM   151   C  CD2   . TRP A 1 19   ? 170.189 140.255 149.218 1.00 41.73  ? 19   TRP A CD2   1 
ATOM   152   N  NE1   . TRP A 1 19   ? 168.874 138.949 150.475 1.00 39.18  ? 19   TRP A NE1   1 
ATOM   153   C  CE2   . TRP A 1 19   ? 168.854 139.939 149.529 1.00 42.01  ? 19   TRP A CE2   1 
ATOM   154   C  CE3   . TRP A 1 19   ? 170.442 141.246 148.268 1.00 41.10  ? 19   TRP A CE3   1 
ATOM   155   C  CZ2   . TRP A 1 19   ? 167.776 140.578 148.924 1.00 42.59  ? 19   TRP A CZ2   1 
ATOM   156   C  CZ3   . TRP A 1 19   ? 169.373 141.877 147.670 1.00 41.38  ? 19   TRP A CZ3   1 
ATOM   157   C  CH2   . TRP A 1 19   ? 168.058 141.542 147.999 1.00 41.40  ? 19   TRP A CH2   1 
ATOM   158   N  N     . THR A 1 20   ? 172.185 142.559 151.451 1.00 41.07  ? 20   THR A N     1 
ATOM   159   C  CA    . THR A 1 20   ? 171.989 143.982 151.212 1.00 36.63  ? 20   THR A CA    1 
ATOM   160   C  C     . THR A 1 20   ? 173.070 144.848 151.845 1.00 34.82  ? 20   THR A C     1 
ATOM   161   O  O     . THR A 1 20   ? 173.058 146.065 151.648 1.00 37.92  ? 20   THR A O     1 
ATOM   162   C  CB    . THR A 1 20   ? 170.620 144.428 151.735 1.00 32.56  ? 20   THR A CB    1 
ATOM   163   O  OG1   . THR A 1 20   ? 170.643 144.450 153.165 1.00 33.64  ? 20   THR A OG1   1 
ATOM   164   C  CG2   . THR A 1 20   ? 169.535 143.481 151.269 1.00 30.06  ? 20   THR A CG2   1 
ATOM   165   N  N     . ARG A 1 21   ? 173.996 144.255 152.596 1.00 35.21  ? 21   ARG A N     1 
ATOM   166   C  CA    . ARG A 1 21   ? 175.017 145.047 153.278 1.00 39.14  ? 21   ARG A CA    1 
ATOM   167   C  C     . ARG A 1 21   ? 175.922 145.848 152.347 1.00 43.53  ? 21   ARG A C     1 
ATOM   168   O  O     . ARG A 1 21   ? 176.229 147.003 152.690 1.00 45.31  ? 21   ARG A O     1 
ATOM   169   C  CB    . ARG A 1 21   ? 175.863 144.141 154.182 1.00 44.71  ? 21   ARG A CB    1 
ATOM   170   C  CG    . ARG A 1 21   ? 175.095 143.493 155.320 1.00 44.77  ? 21   ARG A CG    1 
ATOM   171   C  CD    . ARG A 1 21   ? 174.687 144.486 156.395 1.00 47.67  ? 21   ARG A CD    1 
ATOM   172   N  NE    . ARG A 1 21   ? 175.823 145.079 157.091 1.00 51.93  ? 21   ARG A NE    1 
ATOM   173   C  CZ    . ARG A 1 21   ? 176.328 146.275 156.826 1.00 51.46  ? 21   ARG A CZ    1 
ATOM   174   N  NH1   . ARG A 1 21   ? 175.819 147.045 155.879 1.00 45.22  ? 21   ARG A NH1   1 
ATOM   175   N  NH2   . ARG A 1 21   ? 177.361 146.715 157.537 1.00 50.35  ? 21   ARG A NH2   1 
ATOM   176   N  N     . PRO A 1 22   ? 176.413 145.320 151.216 1.00 42.14  ? 22   PRO A N     1 
ATOM   177   C  CA    . PRO A 1 22   ? 177.331 146.126 150.389 1.00 43.07  ? 22   PRO A CA    1 
ATOM   178   C  C     . PRO A 1 22   ? 176.746 147.437 149.891 1.00 42.78  ? 22   PRO A C     1 
ATOM   179   O  O     . PRO A 1 22   ? 177.461 148.445 149.868 1.00 45.77  ? 22   PRO A O     1 
ATOM   180   C  CB    . PRO A 1 22   ? 177.677 145.180 149.230 1.00 42.58  ? 22   PRO A CB    1 
ATOM   181   C  CG    . PRO A 1 22   ? 177.447 143.831 149.776 1.00 40.77  ? 22   PRO A CG    1 
ATOM   182   C  CD    . PRO A 1 22   ? 176.260 143.965 150.662 1.00 41.30  ? 22   PRO A CD    1 
ATOM   183   N  N     . ILE A 1 23   ? 175.470 147.469 149.498 1.00 38.32  ? 23   ILE A N     1 
ATOM   184   C  CA    . ILE A 1 23   ? 174.909 148.720 148.992 1.00 39.62  ? 23   ILE A CA    1 
ATOM   185   C  C     . ILE A 1 23   ? 174.700 149.719 150.124 1.00 40.64  ? 23   ILE A C     1 
ATOM   186   O  O     . ILE A 1 23   ? 174.872 150.928 149.930 1.00 46.70  ? 23   ILE A O     1 
ATOM   187   C  CB    . ILE A 1 23   ? 173.610 148.462 148.204 1.00 40.38  ? 23   ILE A CB    1 
ATOM   188   C  CG1   . ILE A 1 23   ? 173.153 149.739 147.497 1.00 41.52  ? 23   ILE A CG1   1 
ATOM   189   C  CG2   . ILE A 1 23   ? 172.513 147.934 149.105 1.00 35.05  ? 23   ILE A CG2   1 
ATOM   190   C  CD1   . ILE A 1 23   ? 172.171 149.498 146.380 1.00 39.51  ? 23   ILE A CD1   1 
ATOM   191   N  N     . LEU A 1 24   ? 174.338 149.243 151.317 1.00 36.84  ? 24   LEU A N     1 
ATOM   192   C  CA    . LEU A 1 24   ? 174.218 150.128 152.470 1.00 36.25  ? 24   LEU A CA    1 
ATOM   193   C  C     . LEU A 1 24   ? 175.573 150.692 152.869 1.00 40.30  ? 24   LEU A C     1 
ATOM   194   O  O     . LEU A 1 24   ? 175.675 151.853 153.281 1.00 43.72  ? 24   LEU A O     1 
ATOM   195   C  CB    . LEU A 1 24   ? 173.592 149.372 153.639 1.00 34.55  ? 24   LEU A CB    1 
ATOM   196   C  CG    . LEU A 1 24   ? 172.114 149.016 153.515 1.00 32.89  ? 24   LEU A CG    1 
ATOM   197   C  CD1   . LEU A 1 24   ? 171.740 147.991 154.557 1.00 27.47  ? 24   LEU A CD1   1 
ATOM   198   C  CD2   . LEU A 1 24   ? 171.262 150.262 153.663 1.00 37.12  ? 24   LEU A CD2   1 
ATOM   199   N  N     . ARG A 1 25   ? 176.618 149.872 152.776 1.00 40.87  ? 25   ARG A N     1 
ATOM   200   C  CA    . ARG A 1 25   ? 177.970 150.324 153.076 1.00 43.97  ? 25   ARG A CA    1 
ATOM   201   C  C     . ARG A 1 25   ? 178.452 151.333 152.042 1.00 49.56  ? 25   ARG A C     1 
ATOM   202   O  O     . ARG A 1 25   ? 179.134 152.306 152.383 1.00 52.23  ? 25   ARG A O     1 
ATOM   203   C  CB    . ARG A 1 25   ? 178.893 149.112 153.139 1.00 47.95  ? 25   ARG A CB    1 
ATOM   204   C  CG    . ARG A 1 25   ? 179.412 148.785 154.522 1.00 54.48  ? 25   ARG A CG    1 
ATOM   205   C  CD    . ARG A 1 25   ? 180.540 147.779 154.432 1.00 59.00  ? 25   ARG A CD    1 
ATOM   206   N  NE    . ARG A 1 25   ? 180.048 146.427 154.671 1.00 61.51  ? 25   ARG A NE    1 
ATOM   207   C  CZ    . ARG A 1 25   ? 179.967 145.482 153.744 1.00 60.41  ? 25   ARG A CZ    1 
ATOM   208   N  NH1   . ARG A 1 25   ? 180.335 145.708 152.493 1.00 55.25  ? 25   ARG A NH1   1 
ATOM   209   N  NH2   . ARG A 1 25   ? 179.498 144.284 154.077 1.00 55.74  ? 25   ARG A NH2   1 
ATOM   210   N  N     . LYS A 1 26   ? 178.112 151.109 150.772 1.00 50.53  ? 26   LYS A N     1 
ATOM   211   C  CA    . LYS A 1 26   ? 178.490 152.028 149.704 1.00 49.31  ? 26   LYS A CA    1 
ATOM   212   C  C     . LYS A 1 26   ? 177.778 153.369 149.839 1.00 49.84  ? 26   LYS A C     1 
ATOM   213   O  O     . LYS A 1 26   ? 178.406 154.428 149.734 1.00 53.64  ? 26   LYS A O     1 
ATOM   214   C  CB    . LYS A 1 26   ? 178.179 151.384 148.352 1.00 51.52  ? 26   LYS A CB    1 
ATOM   215   C  CG    . LYS A 1 26   ? 178.131 152.330 147.164 1.00 59.48  ? 26   LYS A CG    1 
ATOM   216   C  CD    . LYS A 1 26   ? 179.467 152.983 146.867 1.00 65.10  ? 26   LYS A CD    1 
ATOM   217   C  CE    . LYS A 1 26   ? 179.371 153.798 145.585 1.00 67.04  ? 26   LYS A CE    1 
ATOM   218   N  NZ    . LYS A 1 26   ? 180.654 154.429 145.193 1.00 70.06  ? 26   LYS A NZ    1 
ATOM   219   N  N     . GLY A 1 27   ? 176.463 153.345 150.066 1.00 47.12  ? 27   GLY A N     1 
ATOM   220   C  CA    . GLY A 1 27   ? 175.683 154.569 150.080 1.00 44.41  ? 27   GLY A CA    1 
ATOM   221   C  C     . GLY A 1 27   ? 175.836 155.416 151.323 1.00 47.20  ? 27   GLY A C     1 
ATOM   222   O  O     . GLY A 1 27   ? 175.556 156.617 151.275 1.00 47.89  ? 27   GLY A O     1 
ATOM   223   N  N     . TYR A 1 28   ? 176.266 154.822 152.436 1.00 51.71  ? 28   TYR A N     1 
ATOM   224   C  CA    . TYR A 1 28   ? 176.463 155.603 153.652 1.00 52.36  ? 28   TYR A CA    1 
ATOM   225   C  C     . TYR A 1 28   ? 177.612 156.587 153.496 1.00 52.26  ? 28   TYR A C     1 
ATOM   226   O  O     . TYR A 1 28   ? 177.560 157.701 154.027 1.00 52.19  ? 28   TYR A O     1 
ATOM   227   C  CB    . TYR A 1 28   ? 176.716 154.678 154.840 1.00 47.12  ? 28   TYR A CB    1 
ATOM   228   C  CG    . TYR A 1 28   ? 177.014 155.423 156.119 1.00 46.61  ? 28   TYR A CG    1 
ATOM   229   C  CD1   . TYR A 1 28   ? 176.029 156.160 156.758 1.00 45.34  ? 28   TYR A CD1   1 
ATOM   230   C  CD2   . TYR A 1 28   ? 178.281 155.394 156.683 1.00 50.06  ? 28   TYR A CD2   1 
ATOM   231   C  CE1   . TYR A 1 28   ? 176.296 156.844 157.925 1.00 45.88  ? 28   TYR A CE1   1 
ATOM   232   C  CE2   . TYR A 1 28   ? 178.557 156.075 157.851 1.00 51.19  ? 28   TYR A CE2   1 
ATOM   233   C  CZ    . TYR A 1 28   ? 177.562 156.799 158.467 1.00 50.96  ? 28   TYR A CZ    1 
ATOM   234   O  OH    . TYR A 1 28   ? 177.832 157.480 159.630 1.00 52.31  ? 28   TYR A OH    1 
ATOM   235   N  N     . ARG A 1 29   ? 178.658 156.192 152.777 1.00 56.30  ? 29   ARG A N     1 
ATOM   236   C  CA    . ARG A 1 29   ? 179.850 157.021 152.677 1.00 62.81  ? 29   ARG A CA    1 
ATOM   237   C  C     . ARG A 1 29   ? 179.745 158.064 151.572 1.00 63.38  ? 29   ARG A C     1 
ATOM   238   O  O     . ARG A 1 29   ? 180.198 159.199 151.751 1.00 64.33  ? 29   ARG A O     1 
ATOM   239   C  CB    . ARG A 1 29   ? 181.079 156.140 152.444 1.00 62.65  ? 29   ARG A CB    1 
ATOM   240   C  CG    . ARG A 1 29   ? 182.403 156.805 152.781 1.00 63.27  ? 29   ARG A CG    1 
ATOM   241   C  CD    . ARG A 1 29   ? 182.746 156.654 154.258 1.00 67.68  ? 29   ARG A CD    1 
ATOM   242   N  NE    . ARG A 1 29   ? 181.908 157.477 155.123 1.00 71.11  ? 29   ARG A NE    1 
ATOM   243   C  CZ    . ARG A 1 29   ? 181.821 157.332 156.437 1.00 72.92  ? 29   ARG A CZ    1 
ATOM   244   N  NH1   . ARG A 1 29   ? 182.510 156.401 157.077 1.00 75.34  ? 29   ARG A NH1   1 
ATOM   245   N  NH2   . ARG A 1 29   ? 181.025 158.142 157.128 1.00 69.18  ? 29   ARG A NH2   1 
ATOM   246   N  N     . GLN A 1 30   ? 179.158 157.709 150.433 1.00 60.96  ? 30   GLN A N     1 
ATOM   247   C  CA    . GLN A 1 30   ? 179.142 158.605 149.288 1.00 56.61  ? 30   GLN A CA    1 
ATOM   248   C  C     . GLN A 1 30   ? 177.933 158.314 148.411 1.00 59.02  ? 30   GLN A C     1 
ATOM   249   O  O     . GLN A 1 30   ? 177.196 157.349 148.624 1.00 62.51  ? 30   GLN A O     1 
ATOM   250   C  CB    . GLN A 1 30   ? 180.446 158.489 148.497 1.00 62.83  ? 30   GLN A CB    1 
ATOM   251   C  CG    . GLN A 1 30   ? 180.748 157.091 148.001 1.00 67.17  ? 30   GLN A CG    1 
ATOM   252   C  CD    . GLN A 1 30   ? 181.788 157.085 146.904 1.00 73.35  ? 30   GLN A CD    1 
ATOM   253   O  OE1   . GLN A 1 30   ? 182.449 156.074 146.665 1.00 73.93  ? 30   GLN A OE1   1 
ATOM   254   N  NE2   . GLN A 1 30   ? 181.913 158.204 146.203 1.00 71.01  ? 30   GLN A NE2   1 
ATOM   255   N  N     . ARG A 1 31   ? 177.745 159.175 147.413 1.00 60.24  ? 31   ARG A N     1 
ATOM   256   C  CA    . ARG A 1 31   ? 176.589 159.099 146.531 1.00 58.87  ? 31   ARG A CA    1 
ATOM   257   C  C     . ARG A 1 31   ? 176.603 157.819 145.704 1.00 59.56  ? 31   ARG A C     1 
ATOM   258   O  O     . ARG A 1 31   ? 177.646 157.395 145.200 1.00 64.07  ? 31   ARG A O     1 
ATOM   259   C  CB    . ARG A 1 31   ? 176.563 160.317 145.611 1.00 56.50  ? 31   ARG A CB    1 
ATOM   260   C  CG    . ARG A 1 31   ? 175.320 160.437 144.757 1.00 60.82  ? 31   ARG A CG    1 
ATOM   261   C  CD    . ARG A 1 31   ? 174.877 161.881 144.646 1.00 65.72  ? 31   ARG A CD    1 
ATOM   262   N  NE    . ARG A 1 31   ? 174.343 162.369 145.910 1.00 70.51  ? 31   ARG A NE    1 
ATOM   263   C  CZ    . ARG A 1 31   ? 173.079 162.234 146.287 1.00 69.31  ? 31   ARG A CZ    1 
ATOM   264   N  NH1   . ARG A 1 31   ? 172.188 161.632 145.515 1.00 64.99  ? 31   ARG A NH1   1 
ATOM   265   N  NH2   . ARG A 1 31   ? 172.699 162.714 147.467 1.00 65.04  ? 31   ARG A NH2   1 
ATOM   266   N  N     . LEU A 1 32   ? 175.429 157.207 145.563 1.00 55.31  ? 32   LEU A N     1 
ATOM   267   C  CA    . LEU A 1 32   ? 175.306 155.985 144.780 1.00 57.52  ? 32   LEU A CA    1 
ATOM   268   C  C     . LEU A 1 32   ? 175.581 156.256 143.306 1.00 65.56  ? 32   LEU A C     1 
ATOM   269   O  O     . LEU A 1 32   ? 175.207 157.302 142.768 1.00 67.18  ? 32   LEU A O     1 
ATOM   270   C  CB    . LEU A 1 32   ? 173.911 155.385 144.950 1.00 56.15  ? 32   LEU A CB    1 
ATOM   271   C  CG    . LEU A 1 32   ? 173.568 154.825 146.329 1.00 54.93  ? 32   LEU A CG    1 
ATOM   272   C  CD1   . LEU A 1 32   ? 172.101 154.439 146.399 1.00 47.21  ? 32   LEU A CD1   1 
ATOM   273   C  CD2   . LEU A 1 32   ? 174.456 153.641 146.660 1.00 52.08  ? 32   LEU A CD2   1 
ATOM   274   N  N     . GLU A 1 33   ? 176.248 155.308 142.657 1.00 69.64  ? 33   GLU A N     1 
ATOM   275   C  CA    . GLU A 1 33   ? 176.582 155.398 141.243 1.00 69.46  ? 33   GLU A CA    1 
ATOM   276   C  C     . GLU A 1 33   ? 175.695 154.475 140.412 1.00 68.92  ? 33   GLU A C     1 
ATOM   277   O  O     . GLU A 1 33   ? 174.888 153.702 140.931 1.00 68.25  ? 33   GLU A O     1 
ATOM   278   C  CB    . GLU A 1 33   ? 178.059 155.064 141.019 1.00 71.67  ? 33   GLU A CB    1 
ATOM   279   C  CG    . GLU A 1 33   ? 179.012 156.177 141.414 1.00 74.39  ? 33   GLU A CG    1 
ATOM   280   C  CD    . GLU A 1 33   ? 180.465 155.801 141.206 1.00 80.85  ? 33   GLU A CD    1 
ATOM   281   O  OE1   . GLU A 1 33   ? 180.767 154.590 141.170 1.00 76.42  ? 33   GLU A OE1   1 
ATOM   282   O  OE2   . GLU A 1 33   ? 181.307 156.715 141.080 1.00 85.10  ? 33   GLU A OE2   1 
ATOM   283   N  N     . LEU A 1 34   ? 175.861 154.575 139.092 1.00 68.56  ? 34   LEU A N     1 
ATOM   284   C  CA    . LEU A 1 34   ? 175.050 153.791 138.166 1.00 67.60  ? 34   LEU A CA    1 
ATOM   285   C  C     . LEU A 1 34   ? 175.361 152.302 138.268 1.00 67.11  ? 34   LEU A C     1 
ATOM   286   O  O     . LEU A 1 34   ? 174.467 151.464 138.107 1.00 65.62  ? 34   LEU A O     1 
ATOM   287   C  CB    . LEU A 1 34   ? 175.273 154.294 136.740 1.00 67.11  ? 34   LEU A CB    1 
ATOM   288   C  CG    . LEU A 1 34   ? 174.389 153.795 135.598 1.00 72.15  ? 34   LEU A CG    1 
ATOM   289   C  CD1   . LEU A 1 34   ? 174.254 154.889 134.559 1.00 76.19  ? 34   LEU A CD1   1 
ATOM   290   C  CD2   . LEU A 1 34   ? 174.971 152.541 134.963 1.00 70.97  ? 34   LEU A CD2   1 
ATOM   291   N  N     . SER A 1 35   ? 176.625 151.954 138.513 1.00 67.81  ? 35   SER A N     1 
ATOM   292   C  CA    . SER A 1 35   ? 177.025 150.553 138.566 1.00 66.13  ? 35   SER A CA    1 
ATOM   293   C  C     . SER A 1 35   ? 176.478 149.830 139.789 1.00 69.18  ? 35   SER A C     1 
ATOM   294   O  O     . SER A 1 35   ? 176.489 148.595 139.817 1.00 72.02  ? 35   SER A O     1 
ATOM   295   C  CB    . SER A 1 35   ? 178.549 150.443 138.535 1.00 66.75  ? 35   SER A CB    1 
ATOM   296   O  OG    . SER A 1 35   ? 179.124 150.991 139.708 1.00 67.84  ? 35   SER A OG    1 
ATOM   297   N  N     . ASP A 1 36   ? 176.007 150.563 140.799 1.00 67.32  ? 36   ASP A N     1 
ATOM   298   C  CA    . ASP A 1 36   ? 175.557 149.925 142.031 1.00 63.35  ? 36   ASP A CA    1 
ATOM   299   C  C     . ASP A 1 36   ? 174.231 149.194 141.851 1.00 60.18  ? 36   ASP A C     1 
ATOM   300   O  O     . ASP A 1 36   ? 173.938 148.258 142.601 1.00 61.31  ? 36   ASP A O     1 
ATOM   301   C  CB    . ASP A 1 36   ? 175.443 150.964 143.142 1.00 65.20  ? 36   ASP A CB    1 
ATOM   302   C  CG    . ASP A 1 36   ? 176.697 151.801 143.280 1.00 68.80  ? 36   ASP A CG    1 
ATOM   303   O  OD1   . ASP A 1 36   ? 177.677 151.524 142.558 1.00 68.36  ? 36   ASP A OD1   1 
ATOM   304   O  OD2   . ASP A 1 36   ? 176.708 152.731 144.112 1.00 69.52  ? 36   ASP A OD2   1 
ATOM   305   N  N     . ILE A 1 37   ? 173.421 149.603 140.881 1.00 58.86  ? 37   ILE A N     1 
ATOM   306   C  CA    . ILE A 1 37   ? 172.106 149.004 140.674 1.00 58.00  ? 37   ILE A CA    1 
ATOM   307   C  C     . ILE A 1 37   ? 172.282 147.648 140.001 1.00 57.41  ? 37   ILE A C     1 
ATOM   308   O  O     . ILE A 1 37   ? 172.961 147.537 138.976 1.00 62.71  ? 37   ILE A O     1 
ATOM   309   C  CB    . ILE A 1 37   ? 171.208 149.927 139.840 1.00 57.82  ? 37   ILE A CB    1 
ATOM   310   C  CG1   . ILE A 1 37   ? 171.284 151.363 140.365 1.00 56.04  ? 37   ILE A CG1   1 
ATOM   311   C  CG2   . ILE A 1 37   ? 169.774 149.431 139.858 1.00 49.01  ? 37   ILE A CG2   1 
ATOM   312   C  CD1   . ILE A 1 37   ? 170.877 151.514 141.808 1.00 50.92  ? 37   ILE A CD1   1 
ATOM   313   N  N     . TYR A 1 38   ? 171.675 146.615 140.580 1.00 56.14  ? 38   TYR A N     1 
ATOM   314   C  CA    . TYR A 1 38   ? 171.835 145.248 140.106 1.00 56.50  ? 38   TYR A CA    1 
ATOM   315   C  C     . TYR A 1 38   ? 170.782 144.885 139.065 1.00 58.96  ? 38   TYR A C     1 
ATOM   316   O  O     . TYR A 1 38   ? 169.682 145.442 139.042 1.00 60.04  ? 38   TYR A O     1 
ATOM   317   C  CB    . TYR A 1 38   ? 171.750 144.263 141.271 1.00 54.87  ? 38   TYR A CB    1 
ATOM   318   C  CG    . TYR A 1 38   ? 172.696 144.571 142.404 1.00 59.69  ? 38   TYR A CG    1 
ATOM   319   C  CD1   . TYR A 1 38   ? 174.046 144.278 142.304 1.00 64.03  ? 38   TYR A CD1   1 
ATOM   320   C  CD2   . TYR A 1 38   ? 172.237 145.151 143.576 1.00 54.72  ? 38   TYR A CD2   1 
ATOM   321   C  CE1   . TYR A 1 38   ? 174.913 144.556 143.338 1.00 63.44  ? 38   TYR A CE1   1 
ATOM   322   C  CE2   . TYR A 1 38   ? 173.098 145.432 144.615 1.00 55.10  ? 38   TYR A CE2   1 
ATOM   323   C  CZ    . TYR A 1 38   ? 174.435 145.134 144.490 1.00 58.76  ? 38   TYR A CZ    1 
ATOM   324   O  OH    . TYR A 1 38   ? 175.300 145.411 145.522 1.00 50.93  ? 38   TYR A OH    1 
ATOM   325   N  N     . GLN A 1 39   ? 171.137 143.939 138.200 1.00 60.04  ? 39   GLN A N     1 
ATOM   326   C  CA    . GLN A 1 39   ? 170.177 143.376 137.260 1.00 55.13  ? 39   GLN A CA    1 
ATOM   327   C  C     . GLN A 1 39   ? 169.116 142.586 138.017 1.00 57.07  ? 39   GLN A C     1 
ATOM   328   O  O     . GLN A 1 39   ? 169.424 141.874 138.976 1.00 59.83  ? 39   GLN A O     1 
ATOM   329   C  CB    . GLN A 1 39   ? 170.896 142.479 136.252 1.00 57.81  ? 39   GLN A CB    1 
ATOM   330   C  CG    . GLN A 1 39   ? 169.999 141.889 135.179 1.00 59.53  ? 39   GLN A CG    1 
ATOM   331   C  CD    . GLN A 1 39   ? 169.482 142.935 134.211 1.00 64.01  ? 39   GLN A CD    1 
ATOM   332   O  OE1   . GLN A 1 39   ? 168.277 143.172 134.123 1.00 56.53  ? 39   GLN A OE1   1 
ATOM   333   N  NE2   . GLN A 1 39   ? 170.390 143.561 133.474 1.00 68.10  ? 39   GLN A NE2   1 
ATOM   334   N  N     . ILE A 1 40   ? 167.865 142.717 137.588 1.00 57.25  ? 40   ILE A N     1 
ATOM   335   C  CA    . ILE A 1 40   ? 166.731 142.112 138.285 1.00 53.50  ? 40   ILE A CA    1 
ATOM   336   C  C     . ILE A 1 40   ? 166.793 140.591 138.202 1.00 55.43  ? 40   ILE A C     1 
ATOM   337   O  O     . ILE A 1 40   ? 167.379 140.043 137.257 1.00 54.30  ? 40   ILE A O     1 
ATOM   338   C  CB    . ILE A 1 40   ? 165.400 142.630 137.722 1.00 45.94  ? 40   ILE A CB    1 
ATOM   339   C  CG1   . ILE A 1 40   ? 165.276 142.296 136.237 1.00 45.83  ? 40   ILE A CG1   1 
ATOM   340   C  CG2   . ILE A 1 40   ? 165.308 144.122 137.906 1.00 43.70  ? 40   ILE A CG2   1 
ATOM   341   C  CD1   . ILE A 1 40   ? 163.911 142.590 135.668 1.00 37.40  ? 40   ILE A CD1   1 
ATOM   342   N  N     . PRO A 1 41   ? 166.222 139.875 139.172 1.00 56.85  ? 41   PRO A N     1 
ATOM   343   C  CA    . PRO A 1 41   ? 166.146 138.413 139.074 1.00 56.90  ? 41   PRO A CA    1 
ATOM   344   C  C     . PRO A 1 41   ? 165.325 137.965 137.870 1.00 50.52  ? 41   PRO A C     1 
ATOM   345   O  O     . PRO A 1 41   ? 164.436 138.674 137.396 1.00 49.14  ? 41   PRO A O     1 
ATOM   346   C  CB    . PRO A 1 41   ? 165.476 138.007 140.391 1.00 56.04  ? 41   PRO A CB    1 
ATOM   347   C  CG    . PRO A 1 41   ? 165.829 139.107 141.336 1.00 50.73  ? 41   PRO A CG    1 
ATOM   348   C  CD    . PRO A 1 41   ? 165.798 140.356 140.498 1.00 49.17  ? 41   PRO A CD    1 
ATOM   349   N  N     . SER A 1 42   ? 165.647 136.770 137.367 1.00 51.70  ? 42   SER A N     1 
ATOM   350   C  CA    . SER A 1 42   ? 164.954 136.235 136.199 1.00 54.50  ? 42   SER A CA    1 
ATOM   351   C  C     . SER A 1 42   ? 163.465 136.035 136.456 1.00 54.28  ? 42   SER A C     1 
ATOM   352   O  O     . SER A 1 42   ? 162.655 136.152 135.529 1.00 55.44  ? 42   SER A O     1 
ATOM   353   C  CB    . SER A 1 42   ? 165.595 134.916 135.770 1.00 54.15  ? 42   SER A CB    1 
ATOM   354   O  OG    . SER A 1 42   ? 166.896 135.122 135.250 1.00 56.63  ? 42   SER A OG    1 
ATOM   355   N  N     . VAL A 1 43   ? 163.084 135.721 137.697 1.00 53.04  ? 43   VAL A N     1 
ATOM   356   C  CA    . VAL A 1 43   ? 161.680 135.491 138.017 1.00 49.49  ? 43   VAL A CA    1 
ATOM   357   C  C     . VAL A 1 43   ? 160.857 136.767 137.877 1.00 49.04  ? 43   VAL A C     1 
ATOM   358   O  O     . VAL A 1 43   ? 159.659 136.703 137.576 1.00 49.53  ? 43   VAL A O     1 
ATOM   359   C  CB    . VAL A 1 43   ? 161.570 134.891 139.436 1.00 47.76  ? 43   VAL A CB    1 
ATOM   360   C  CG1   . VAL A 1 43   ? 162.433 135.670 140.420 1.00 45.67  ? 43   VAL A CG1   1 
ATOM   361   C  CG2   . VAL A 1 43   ? 160.125 134.822 139.908 1.00 46.23  ? 43   VAL A CG2   1 
ATOM   362   N  N     . ASP A 1 44   ? 161.478 137.930 138.044 1.00 46.89  ? 44   ASP A N     1 
ATOM   363   C  CA    . ASP A 1 44   ? 160.770 139.201 138.083 1.00 41.77  ? 44   ASP A CA    1 
ATOM   364   C  C     . ASP A 1 44   ? 160.709 139.911 136.736 1.00 44.41  ? 44   ASP A C     1 
ATOM   365   O  O     . ASP A 1 44   ? 160.234 141.048 136.680 1.00 48.37  ? 44   ASP A O     1 
ATOM   366   C  CB    . ASP A 1 44   ? 161.420 140.122 139.115 1.00 41.91  ? 44   ASP A CB    1 
ATOM   367   C  CG    . ASP A 1 44   ? 161.250 139.614 140.526 1.00 48.73  ? 44   ASP A CG    1 
ATOM   368   O  OD1   . ASP A 1 44   ? 160.111 139.640 141.035 1.00 48.31  ? 44   ASP A OD1   1 
ATOM   369   O  OD2   . ASP A 1 44   ? 162.256 139.187 141.127 1.00 52.57  ? 44   ASP A OD2   1 
ATOM   370   N  N     . SER A 1 45   ? 161.185 139.288 135.660 1.00 41.77  ? 45   SER A N     1 
ATOM   371   C  CA    . SER A 1 45   ? 161.132 139.918 134.346 1.00 40.61  ? 45   SER A CA    1 
ATOM   372   C  C     . SER A 1 45   ? 159.693 140.043 133.860 1.00 38.08  ? 45   SER A C     1 
ATOM   373   O  O     . SER A 1 45   ? 158.860 139.167 134.102 1.00 42.25  ? 45   SER A O     1 
ATOM   374   C  CB    . SER A 1 45   ? 161.958 139.126 133.338 1.00 46.23  ? 45   SER A CB    1 
ATOM   375   O  OG    . SER A 1 45   ? 163.338 139.393 133.500 1.00 49.88  ? 45   SER A OG    1 
ATOM   376   N  N     . ALA A 1 46   ? 159.408 141.153 133.175 1.00 34.94  ? 46   ALA A N     1 
ATOM   377   C  CA    . ALA A 1 46   ? 158.051 141.415 132.705 1.00 36.82  ? 46   ALA A CA    1 
ATOM   378   C  C     . ALA A 1 46   ? 157.612 140.392 131.666 1.00 41.46  ? 46   ALA A C     1 
ATOM   379   O  O     . ALA A 1 46   ? 156.433 140.026 131.607 1.00 42.77  ? 46   ALA A O     1 
ATOM   380   C  CB    . ALA A 1 46   ? 157.955 142.831 132.140 1.00 34.46  ? 46   ALA A CB    1 
ATOM   381   N  N     . ASP A 1 47   ? 158.543 139.929 130.828 1.00 40.97  ? 47   ASP A N     1 
ATOM   382   C  CA    . ASP A 1 47   ? 158.198 138.957 129.794 1.00 41.31  ? 47   ASP A CA    1 
ATOM   383   C  C     . ASP A 1 47   ? 157.693 137.651 130.401 1.00 41.81  ? 47   ASP A C     1 
ATOM   384   O  O     . ASP A 1 47   ? 156.638 137.134 130.006 1.00 45.76  ? 47   ASP A O     1 
ATOM   385   C  CB    . ASP A 1 47   ? 159.420 138.709 128.907 1.00 48.59  ? 47   ASP A CB    1 
ATOM   386   C  CG    . ASP A 1 47   ? 159.126 137.786 127.744 1.00 60.81  ? 47   ASP A CG    1 
ATOM   387   O  OD1   . ASP A 1 47   ? 158.386 138.197 126.823 1.00 64.44  ? 47   ASP A OD1   1 
ATOM   388   O  OD2   . ASP A 1 47   ? 159.648 136.651 127.747 1.00 59.33  ? 47   ASP A OD2   1 
ATOM   389   N  N     . ASN A 1 48   ? 158.408 137.132 131.400 1.00 39.99  ? 48   ASN A N     1 
ATOM   390   C  CA    . ASN A 1 48   ? 158.043 135.860 132.009 1.00 41.63  ? 48   ASN A CA    1 
ATOM   391   C  C     . ASN A 1 48   ? 156.725 135.962 132.762 1.00 39.35  ? 48   ASN A C     1 
ATOM   392   O  O     . ASN A 1 48   ? 155.870 135.076 132.650 1.00 46.45  ? 48   ASN A O     1 
ATOM   393   C  CB    . ASN A 1 48   ? 159.151 135.404 132.955 1.00 44.44  ? 48   ASN A CB    1 
ATOM   394   C  CG    . ASN A 1 48   ? 160.449 135.120 132.238 1.00 56.55  ? 48   ASN A CG    1 
ATOM   395   O  OD1   . ASN A 1 48   ? 160.460 134.791 131.053 1.00 58.27  ? 48   ASN A OD1   1 
ATOM   396   N  ND2   . ASN A 1 48   ? 161.556 135.256 132.953 1.00 56.20  ? 48   ASN A ND2   1 
ATOM   397   N  N     . LEU A 1 49   ? 156.537 137.049 133.510 1.00 34.55  ? 49   LEU A N     1 
ATOM   398   C  CA    . LEU A 1 49   ? 155.309 137.220 134.275 1.00 34.19  ? 49   LEU A CA    1 
ATOM   399   C  C     . LEU A 1 49   ? 154.115 137.424 133.353 1.00 33.47  ? 49   LEU A C     1 
ATOM   400   O  O     . LEU A 1 49   ? 153.020 136.906 133.615 1.00 33.98  ? 49   LEU A O     1 
ATOM   401   C  CB    . LEU A 1 49   ? 155.461 138.402 135.231 1.00 33.90  ? 49   LEU A CB    1 
ATOM   402   C  CG    . LEU A 1 49   ? 156.430 138.215 136.400 1.00 35.03  ? 49   LEU A CG    1 
ATOM   403   C  CD1   . LEU A 1 49   ? 156.650 139.526 137.128 1.00 31.72  ? 49   LEU A CD1   1 
ATOM   404   C  CD2   . LEU A 1 49   ? 155.940 137.146 137.355 1.00 35.11  ? 49   LEU A CD2   1 
ATOM   405   N  N     . SER A 1 50   ? 154.311 138.170 132.265 1.00 31.78  ? 50   SER A N     1 
ATOM   406   C  CA    . SER A 1 50   ? 153.240 138.363 131.298 1.00 33.55  ? 50   SER A CA    1 
ATOM   407   C  C     . SER A 1 50   ? 152.838 137.046 130.653 1.00 35.40  ? 50   SER A C     1 
ATOM   408   O  O     . SER A 1 50   ? 151.645 136.770 130.497 1.00 38.60  ? 50   SER A O     1 
ATOM   409   C  CB    . SER A 1 50   ? 153.667 139.371 130.236 1.00 36.59  ? 50   SER A CB    1 
ATOM   410   O  OG    . SER A 1 50   ? 152.601 139.639 129.345 1.00 43.21  ? 50   SER A OG    1 
ATOM   411   N  N     . GLU A 1 51   ? 153.814 136.211 130.286 1.00 35.34  ? 51   GLU A N     1 
ATOM   412   C  CA    . GLU A 1 51   ? 153.479 134.902 129.730 1.00 37.39  ? 51   GLU A CA    1 
ATOM   413   C  C     . GLU A 1 51   ? 152.714 134.067 130.753 1.00 37.22  ? 51   GLU A C     1 
ATOM   414   O  O     . GLU A 1 51   ? 151.677 133.464 130.432 1.00 38.84  ? 51   GLU A O     1 
ATOM   415   C  CB    . GLU A 1 51   ? 154.769 134.200 129.283 1.00 42.38  ? 51   GLU A CB    1 
ATOM   416   C  CG    . GLU A 1 51   ? 154.884 132.659 129.412 1.00 52.45  ? 51   GLU A CG    1 
ATOM   417   C  CD    . GLU A 1 51   ? 153.701 131.836 128.887 1.00 54.26  ? 51   GLU A CD    1 
ATOM   418   O  OE1   . GLU A 1 51   ? 152.777 132.385 128.251 1.00 46.04  ? 51   GLU A OE1   1 
ATOM   419   O  OE2   . GLU A 1 51   ? 153.699 130.611 129.127 1.00 54.05  ? 51   GLU A OE2   1 
ATOM   420   N  N     . LYS A 1 52   ? 153.194 134.058 132.000 1.00 36.84  ? 52   LYS A N     1 
ATOM   421   C  CA    . LYS A 1 52   ? 152.548 133.293 133.062 1.00 35.64  ? 52   LYS A CA    1 
ATOM   422   C  C     . LYS A 1 52   ? 151.081 133.672 133.210 1.00 36.05  ? 52   LYS A C     1 
ATOM   423   O  O     . LYS A 1 52   ? 150.203 132.804 133.233 1.00 33.74  ? 52   LYS A O     1 
ATOM   424   C  CB    . LYS A 1 52   ? 153.291 133.517 134.380 1.00 37.74  ? 52   LYS A CB    1 
ATOM   425   C  CG    . LYS A 1 52   ? 154.059 132.316 134.885 1.00 48.39  ? 52   LYS A CG    1 
ATOM   426   C  CD    . LYS A 1 52   ? 154.554 132.557 136.301 1.00 52.02  ? 52   LYS A CD    1 
ATOM   427   C  CE    . LYS A 1 52   ? 153.409 132.521 137.300 1.00 47.66  ? 52   LYS A CE    1 
ATOM   428   N  NZ    . LYS A 1 52   ? 153.888 132.665 138.701 1.00 45.93  ? 52   LYS A NZ    1 
ATOM   429   N  N     . LEU A 1 53   ? 150.794 134.971 133.305 1.00 35.55  ? 53   LEU A N     1 
ATOM   430   C  CA    . LEU A 1 53   ? 149.411 135.388 133.519 1.00 33.15  ? 53   LEU A CA    1 
ATOM   431   C  C     . LEU A 1 53   ? 148.563 135.201 132.265 1.00 33.48  ? 53   LEU A C     1 
ATOM   432   O  O     . LEU A 1 53   ? 147.383 134.837 132.358 1.00 37.58  ? 53   LEU A O     1 
ATOM   433   C  CB    . LEU A 1 53   ? 149.356 136.842 133.984 1.00 36.14  ? 53   LEU A CB    1 
ATOM   434   C  CG    . LEU A 1 53   ? 147.945 137.329 134.339 1.00 33.40  ? 53   LEU A CG    1 
ATOM   435   C  CD1   . LEU A 1 53   ? 147.335 136.484 135.442 1.00 31.85  ? 53   LEU A CD1   1 
ATOM   436   C  CD2   . LEU A 1 53   ? 147.931 138.799 134.718 1.00 31.00  ? 53   LEU A CD2   1 
ATOM   437   N  N     . GLU A 1 54   ? 149.139 135.453 131.087 1.00 32.06  ? 54   GLU A N     1 
ATOM   438   C  CA    . GLU A 1 54   ? 148.372 135.392 129.850 1.00 31.00  ? 54   GLU A CA    1 
ATOM   439   C  C     . GLU A 1 54   ? 147.916 133.973 129.549 1.00 31.59  ? 54   GLU A C     1 
ATOM   440   O  O     . GLU A 1 54   ? 146.811 133.769 129.035 1.00 31.17  ? 54   GLU A O     1 
ATOM   441   C  CB    . GLU A 1 54   ? 149.211 135.946 128.702 1.00 33.33  ? 54   GLU A CB    1 
ATOM   442   C  CG    . GLU A 1 54   ? 148.410 136.433 127.517 1.00 42.62  ? 54   GLU A CG    1 
ATOM   443   C  CD    . GLU A 1 54   ? 149.250 136.520 126.262 1.00 53.21  ? 54   GLU A CD    1 
ATOM   444   O  OE1   . GLU A 1 54   ? 148.702 136.321 125.156 1.00 55.82  ? 54   GLU A OE1   1 
ATOM   445   O  OE2   . GLU A 1 54   ? 150.465 136.786 126.384 1.00 47.62  ? 54   GLU A OE2   1 
ATOM   446   N  N     . ARG A 1 55   ? 148.753 132.981 129.858 1.00 31.54  ? 55   ARG A N     1 
ATOM   447   C  CA    . ARG A 1 55   ? 148.353 131.588 129.670 1.00 30.09  ? 55   ARG A CA    1 
ATOM   448   C  C     . ARG A 1 55   ? 147.060 131.283 130.423 1.00 33.25  ? 55   ARG A C     1 
ATOM   449   O  O     . ARG A 1 55   ? 146.087 130.764 129.852 1.00 35.40  ? 55   ARG A O     1 
ATOM   450   C  CB    . ARG A 1 55   ? 149.484 130.682 130.152 1.00 32.03  ? 55   ARG A CB    1 
ATOM   451   C  CG    . ARG A 1 55   ? 149.198 129.204 130.155 1.00 30.93  ? 55   ARG A CG    1 
ATOM   452   C  CD    . ARG A 1 55   ? 150.395 128.465 130.732 1.00 34.94  ? 55   ARG A CD    1 
ATOM   453   N  NE    . ARG A 1 55   ? 151.566 128.512 129.864 1.00 45.85  ? 55   ARG A NE    1 
ATOM   454   C  CZ    . ARG A 1 55   ? 151.897 127.579 128.982 1.00 48.22  ? 55   ARG A CZ    1 
ATOM   455   N  NH1   . ARG A 1 55   ? 151.161 126.493 128.815 1.00 46.65  ? 55   ARG A NH1   1 
ATOM   456   N  NH2   . ARG A 1 55   ? 152.996 127.738 128.250 1.00 42.68  ? 55   ARG A NH2   1 
ATOM   457   N  N     . GLU A 1 56   ? 147.023 131.637 131.710 1.00 36.95  ? 56   GLU A N     1 
ATOM   458   C  CA    . GLU A 1 56   ? 145.858 131.353 132.538 1.00 33.41  ? 56   GLU A CA    1 
ATOM   459   C  C     . GLU A 1 56   ? 144.651 132.183 132.127 1.00 32.09  ? 56   GLU A C     1 
ATOM   460   O  O     . GLU A 1 56   ? 143.522 131.687 132.174 1.00 35.49  ? 56   GLU A O     1 
ATOM   461   C  CB    . GLU A 1 56   ? 146.194 131.602 134.006 1.00 33.52  ? 56   GLU A CB    1 
ATOM   462   C  CG    . GLU A 1 56   ? 147.275 130.693 134.560 1.00 36.43  ? 56   GLU A CG    1 
ATOM   463   C  CD    . GLU A 1 56   ? 146.902 129.223 134.520 1.00 47.51  ? 56   GLU A CD    1 
ATOM   464   O  OE1   . GLU A 1 56   ? 145.700 128.907 134.416 1.00 50.88  ? 56   GLU A OE1   1 
ATOM   465   O  OE2   . GLU A 1 56   ? 147.817 128.379 134.583 1.00 50.10  ? 56   GLU A OE2   1 
ATOM   466   N  N     . TRP A 1 57   ? 144.858 133.437 131.724 1.00 30.38  ? 57   TRP A N     1 
ATOM   467   C  CA    . TRP A 1 57   ? 143.721 134.243 131.287 1.00 30.82  ? 57   TRP A CA    1 
ATOM   468   C  C     . TRP A 1 57   ? 143.106 133.695 130.005 1.00 33.65  ? 57   TRP A C     1 
ATOM   469   O  O     . TRP A 1 57   ? 141.876 133.670 129.862 1.00 34.68  ? 57   TRP A O     1 
ATOM   470   C  CB    . TRP A 1 57   ? 144.134 135.703 131.114 1.00 29.43  ? 57   TRP A CB    1 
ATOM   471   C  CG    . TRP A 1 57   ? 143.018 136.579 130.626 1.00 31.84  ? 57   TRP A CG    1 
ATOM   472   C  CD1   . TRP A 1 57   ? 143.005 137.326 129.485 1.00 31.69  ? 57   TRP A CD1   1 
ATOM   473   C  CD2   . TRP A 1 57   ? 141.730 136.749 131.229 1.00 34.49  ? 57   TRP A CD2   1 
ATOM   474   N  NE1   . TRP A 1 57   ? 141.805 137.978 129.360 1.00 30.67  ? 57   TRP A NE1   1 
ATOM   475   C  CE2   . TRP A 1 57   ? 141.003 137.637 130.415 1.00 34.98  ? 57   TRP A CE2   1 
ATOM   476   C  CE3   . TRP A 1 57   ? 141.125 136.249 132.385 1.00 32.42  ? 57   TRP A CE3   1 
ATOM   477   C  CZ2   . TRP A 1 57   ? 139.705 138.033 130.719 1.00 32.82  ? 57   TRP A CZ2   1 
ATOM   478   C  CZ3   . TRP A 1 57   ? 139.838 136.641 132.682 1.00 30.35  ? 57   TRP A CZ3   1 
ATOM   479   C  CH2   . TRP A 1 57   ? 139.142 137.524 131.855 1.00 28.93  ? 57   TRP A CH2   1 
ATOM   480   N  N     . ASP A 1 58   ? 143.937 133.249 129.062 1.00 31.96  ? 58   ASP A N     1 
ATOM   481   C  CA    . ASP A 1 58   ? 143.396 132.654 127.847 1.00 32.05  ? 58   ASP A CA    1 
ATOM   482   C  C     . ASP A 1 58   ? 142.660 131.357 128.140 1.00 34.69  ? 58   ASP A C     1 
ATOM   483   O  O     . ASP A 1 58   ? 141.605 131.101 127.548 1.00 35.05  ? 58   ASP A O     1 
ATOM   484   C  CB    . ASP A 1 58   ? 144.511 132.416 126.833 1.00 33.71  ? 58   ASP A CB    1 
ATOM   485   C  CG    . ASP A 1 58   ? 145.138 133.704 126.356 1.00 41.65  ? 58   ASP A CG    1 
ATOM   486   O  OD1   . ASP A 1 58   ? 144.684 134.779 126.796 1.00 45.02  ? 58   ASP A OD1   1 
ATOM   487   O  OD2   . ASP A 1 58   ? 146.083 133.641 125.544 1.00 39.94  ? 58   ASP A OD2   1 
ATOM   488   N  N     . ARG A 1 59   ? 143.178 130.534 129.058 1.00 36.94  ? 59   ARG A N     1 
ATOM   489   C  CA    . ARG A 1 59   ? 142.444 129.321 129.411 1.00 33.71  ? 59   ARG A CA    1 
ATOM   490   C  C     . ARG A 1 59   ? 141.117 129.659 130.076 1.00 36.55  ? 59   ARG A C     1 
ATOM   491   O  O     . ARG A 1 59   ? 140.104 128.994 129.830 1.00 38.57  ? 59   ARG A O     1 
ATOM   492   C  CB    . ARG A 1 59   ? 143.284 128.430 130.322 1.00 34.72  ? 59   ARG A CB    1 
ATOM   493   C  CG    . ARG A 1 59   ? 142.681 127.050 130.509 1.00 46.54  ? 59   ARG A CG    1 
ATOM   494   C  CD    . ARG A 1 59   ? 143.666 126.079 131.130 1.00 51.76  ? 59   ARG A CD    1 
ATOM   495   N  NE    . ARG A 1 59   ? 143.780 126.256 132.572 1.00 56.00  ? 59   ARG A NE    1 
ATOM   496   C  CZ    . ARG A 1 59   ? 143.065 125.587 133.465 1.00 57.46  ? 59   ARG A CZ    1 
ATOM   497   N  NH1   . ARG A 1 59   ? 142.163 124.691 133.099 1.00 53.88  ? 59   ARG A NH1   1 
ATOM   498   N  NH2   . ARG A 1 59   ? 143.259 125.821 134.759 1.00 55.64  ? 59   ARG A NH2   1 
ATOM   499   N  N     . GLU A 1 60   ? 141.108 130.693 130.919 1.00 38.32  ? 60   GLU A N     1 
ATOM   500   C  CA    . GLU A 1 60   ? 139.877 131.122 131.571 1.00 35.48  ? 60   GLU A CA    1 
ATOM   501   C  C     . GLU A 1 60   ? 138.839 131.568 130.551 1.00 35.47  ? 60   GLU A C     1 
ATOM   502   O  O     . GLU A 1 60   ? 137.662 131.211 130.657 1.00 39.09  ? 60   GLU A O     1 
ATOM   503   C  CB    . GLU A 1 60   ? 140.185 132.256 132.550 1.00 36.91  ? 60   GLU A CB    1 
ATOM   504   C  CG    . GLU A 1 60   ? 139.021 132.695 133.420 1.00 39.76  ? 60   GLU A CG    1 
ATOM   505   C  CD    . GLU A 1 60   ? 138.612 131.657 134.449 1.00 47.14  ? 60   GLU A CD    1 
ATOM   506   O  OE1   . GLU A 1 60   ? 139.284 130.611 134.557 1.00 52.27  ? 60   GLU A OE1   1 
ATOM   507   O  OE2   . GLU A 1 60   ? 137.613 131.892 135.157 1.00 46.28  ? 60   GLU A OE2   1 
ATOM   508   N  N     . LEU A 1 61   ? 139.256 132.355 129.558 1.00 37.12  ? 61   LEU A N     1 
ATOM   509   C  CA    . LEU A 1 61   ? 138.318 132.792 128.528 1.00 33.75  ? 61   LEU A CA    1 
ATOM   510   C  C     . LEU A 1 61   ? 137.830 131.625 127.681 1.00 36.43  ? 61   LEU A C     1 
ATOM   511   O  O     . LEU A 1 61   ? 136.664 131.595 127.273 1.00 36.21  ? 61   LEU A O     1 
ATOM   512   C  CB    . LEU A 1 61   ? 138.953 133.857 127.636 1.00 33.43  ? 61   LEU A CB    1 
ATOM   513   C  CG    . LEU A 1 61   ? 139.168 135.234 128.252 1.00 35.56  ? 61   LEU A CG    1 
ATOM   514   C  CD1   . LEU A 1 61   ? 140.045 136.077 127.351 1.00 35.23  ? 61   LEU A CD1   1 
ATOM   515   C  CD2   . LEU A 1 61   ? 137.833 135.911 128.486 1.00 36.93  ? 61   LEU A CD2   1 
ATOM   516   N  N     . ALA A 1 62   ? 138.705 130.662 127.393 1.00 40.30  ? 62   ALA A N     1 
ATOM   517   C  CA    . ALA A 1 62   ? 138.358 129.587 126.476 1.00 36.79  ? 62   ALA A CA    1 
ATOM   518   C  C     . ALA A 1 62   ? 137.614 128.429 127.128 1.00 39.33  ? 62   ALA A C     1 
ATOM   519   O  O     . ALA A 1 62   ? 137.043 127.605 126.407 1.00 44.75  ? 62   ALA A O     1 
ATOM   520   C  CB    . ALA A 1 62   ? 139.620 129.049 125.796 1.00 32.24  ? 62   ALA A CB    1 
ATOM   521   N  N     . SER A 1 63   ? 137.590 128.339 128.460 1.00 39.40  ? 63   SER A N     1 
ATOM   522   C  CA    . SER A 1 63   ? 136.990 127.179 129.107 1.00 41.00  ? 63   SER A CA    1 
ATOM   523   C  C     . SER A 1 63   ? 135.865 127.492 130.086 1.00 47.10  ? 63   SER A C     1 
ATOM   524   O  O     . SER A 1 63   ? 135.268 126.553 130.624 1.00 51.35  ? 63   SER A O     1 
ATOM   525   C  CB    . SER A 1 63   ? 138.067 126.363 129.838 1.00 39.47  ? 63   SER A CB    1 
ATOM   526   O  OG    . SER A 1 63   ? 138.416 126.963 131.072 1.00 46.59  ? 63   SER A OG    1 
ATOM   527   N  N     . LYS A 1 64   ? 135.545 128.760 130.326 1.00 47.06  ? 64   LYS A N     1 
ATOM   528   C  CA    . LYS A 1 64   ? 134.499 129.126 131.270 1.00 47.34  ? 64   LYS A CA    1 
ATOM   529   C  C     . LYS A 1 64   ? 133.418 129.953 130.589 1.00 50.89  ? 64   LYS A C     1 
ATOM   530   O  O     . LYS A 1 64   ? 133.652 130.615 129.575 1.00 53.18  ? 64   LYS A O     1 
ATOM   531   C  CB    . LYS A 1 64   ? 135.062 129.902 132.466 1.00 45.35  ? 64   LYS A CB    1 
ATOM   532   C  CG    . LYS A 1 64   ? 136.053 129.129 133.305 1.00 43.98  ? 64   LYS A CG    1 
ATOM   533   C  CD    . LYS A 1 64   ? 135.376 127.938 133.961 1.00 49.78  ? 64   LYS A CD    1 
ATOM   534   C  CE    . LYS A 1 64   ? 136.336 127.165 134.846 1.00 53.33  ? 64   LYS A CE    1 
ATOM   535   N  NZ    . LYS A 1 64   ? 136.796 127.984 136.001 1.00 52.08  ? 64   LYS A NZ    1 
ATOM   536   N  N     . LYS A 1 65   ? 132.218 129.898 131.167 1.00 54.23  ? 65   LYS A N     1 
ATOM   537   C  CA    . LYS A 1 65   ? 131.082 130.659 130.664 1.00 57.36  ? 65   LYS A CA    1 
ATOM   538   C  C     . LYS A 1 65   ? 131.015 132.056 131.261 1.00 58.12  ? 65   LYS A C     1 
ATOM   539   O  O     . LYS A 1 65   ? 130.472 132.968 130.627 1.00 57.59  ? 65   LYS A O     1 
ATOM   540   C  CB    . LYS A 1 65   ? 129.760 129.933 130.952 1.00 58.49  ? 65   LYS A CB    1 
ATOM   541   C  CG    . LYS A 1 65   ? 129.783 128.399 131.012 1.00 57.71  ? 65   LYS A CG    1 
ATOM   542   C  CD    . LYS A 1 65   ? 130.467 127.732 129.821 1.00 55.41  ? 65   LYS A CD    1 
ATOM   543   C  CE    . LYS A 1 65   ? 131.681 126.922 130.254 1.00 52.77  ? 65   LYS A CE    1 
ATOM   544   N  NZ    . LYS A 1 65   ? 132.401 126.321 129.098 1.00 55.84  ? 65   LYS A NZ    1 
ATOM   545   N  N     . ASN A 1 66   ? 131.540 132.237 132.471 1.00 55.57  ? 66   ASN A N     1 
ATOM   546   C  CA    . ASN A 1 66   ? 131.645 133.543 133.119 1.00 50.21  ? 66   ASN A CA    1 
ATOM   547   C  C     . ASN A 1 66   ? 133.077 133.702 133.603 1.00 49.47  ? 66   ASN A C     1 
ATOM   548   O  O     . ASN A 1 66   ? 133.371 133.489 134.786 1.00 51.51  ? 66   ASN A O     1 
ATOM   549   C  CB    . ASN A 1 66   ? 130.653 133.680 134.275 1.00 53.52  ? 66   ASN A CB    1 
ATOM   550   C  CG    . ASN A 1 66   ? 129.222 133.803 133.802 1.00 63.46  ? 66   ASN A CG    1 
ATOM   551   O  OD1   . ASN A 1 66   ? 128.461 132.836 133.826 1.00 66.61  ? 66   ASN A OD1   1 
ATOM   552   N  ND2   . ASN A 1 66   ? 128.845 135.000 133.368 1.00 60.51  ? 66   ASN A ND2   1 
ATOM   553   N  N     . PRO A 1 67   ? 133.998 134.068 132.712 1.00 47.51  ? 67   PRO A N     1 
ATOM   554   C  CA    . PRO A 1 67   ? 135.410 134.145 133.100 1.00 45.23  ? 67   PRO A CA    1 
ATOM   555   C  C     . PRO A 1 67   ? 135.654 135.195 134.173 1.00 40.64  ? 67   PRO A C     1 
ATOM   556   O  O     . PRO A 1 67   ? 135.036 136.261 134.182 1.00 37.69  ? 67   PRO A O     1 
ATOM   557   C  CB    . PRO A 1 67   ? 136.117 134.508 131.789 1.00 40.73  ? 67   PRO A CB    1 
ATOM   558   C  CG    . PRO A 1 67   ? 135.084 135.208 130.997 1.00 38.75  ? 67   PRO A CG    1 
ATOM   559   C  CD    . PRO A 1 67   ? 133.788 134.519 131.327 1.00 44.96  ? 67   PRO A CD    1 
ATOM   560   N  N     . LYS A 1 68   ? 136.564 134.874 135.089 1.00 38.77  ? 68   LYS A N     1 
ATOM   561   C  CA    . LYS A 1 68   ? 136.939 135.760 136.182 1.00 36.48  ? 68   LYS A CA    1 
ATOM   562   C  C     . LYS A 1 68   ? 138.453 135.892 136.216 1.00 37.05  ? 68   LYS A C     1 
ATOM   563   O  O     . LYS A 1 68   ? 139.167 134.887 136.155 1.00 44.05  ? 68   LYS A O     1 
ATOM   564   C  CB    . LYS A 1 68   ? 136.425 135.231 137.522 1.00 40.73  ? 68   LYS A CB    1 
ATOM   565   C  CG    . LYS A 1 68   ? 134.921 135.051 137.588 1.00 42.40  ? 68   LYS A CG    1 
ATOM   566   C  CD    . LYS A 1 68   ? 134.194 136.378 137.490 1.00 43.35  ? 68   LYS A CD    1 
ATOM   567   C  CE    . LYS A 1 68   ? 132.701 136.169 137.307 1.00 51.08  ? 68   LYS A CE    1 
ATOM   568   N  NZ    . LYS A 1 68   ? 132.090 135.479 138.476 1.00 57.09  ? 68   LYS A NZ    1 
ATOM   569   N  N     . LEU A 1 69   ? 138.940 137.128 136.309 1.00 30.80  ? 69   LEU A N     1 
ATOM   570   C  CA    . LEU A 1 69   ? 140.377 137.355 136.389 1.00 29.66  ? 69   LEU A CA    1 
ATOM   571   C  C     . LEU A 1 69   ? 140.960 136.886 137.716 1.00 36.91  ? 69   LEU A C     1 
ATOM   572   O  O     . LEU A 1 69   ? 142.145 136.531 137.777 1.00 42.86  ? 69   LEU A O     1 
ATOM   573   C  CB    . LEU A 1 69   ? 140.671 138.838 136.172 1.00 26.48  ? 69   LEU A CB    1 
ATOM   574   C  CG    . LEU A 1 69   ? 142.126 139.271 136.022 1.00 28.43  ? 69   LEU A CG    1 
ATOM   575   C  CD1   . LEU A 1 69   ? 142.800 138.511 134.898 1.00 29.47  ? 69   LEU A CD1   1 
ATOM   576   C  CD2   . LEU A 1 69   ? 142.197 140.763 135.783 1.00 25.66  ? 69   LEU A CD2   1 
ATOM   577   N  N     . ILE A 1 70   ? 140.151 136.861 138.776 1.00 41.44  ? 70   ILE A N     1 
ATOM   578   C  CA    . ILE A 1 70   ? 140.637 136.399 140.068 1.00 39.62  ? 70   ILE A CA    1 
ATOM   579   C  C     . ILE A 1 70   ? 140.960 134.911 140.021 1.00 37.80  ? 70   ILE A C     1 
ATOM   580   O  O     . ILE A 1 70   ? 141.860 134.443 140.727 1.00 39.04  ? 70   ILE A O     1 
ATOM   581   C  CB    . ILE A 1 70   ? 139.616 136.740 141.171 1.00 39.68  ? 70   ILE A CB    1 
ATOM   582   C  CG1   . ILE A 1 70   ? 140.234 136.532 142.552 1.00 46.34  ? 70   ILE A CG1   1 
ATOM   583   C  CG2   . ILE A 1 70   ? 138.343 135.925 141.012 1.00 35.89  ? 70   ILE A CG2   1 
ATOM   584   C  CD1   . ILE A 1 70   ? 141.487 137.342 142.779 1.00 44.59  ? 70   ILE A CD1   1 
ATOM   585   N  N     . ASN A 1 71   ? 140.249 134.145 139.189 1.00 38.37  ? 71   ASN A N     1 
ATOM   586   C  CA    . ASN A 1 71   ? 140.589 132.738 139.000 1.00 39.47  ? 71   ASN A CA    1 
ATOM   587   C  C     . ASN A 1 71   ? 141.917 132.584 138.273 1.00 39.49  ? 71   ASN A C     1 
ATOM   588   O  O     . ASN A 1 71   ? 142.702 131.683 138.588 1.00 41.87  ? 71   ASN A O     1 
ATOM   589   C  CB    . ASN A 1 71   ? 139.477 132.027 138.232 1.00 42.02  ? 71   ASN A CB    1 
ATOM   590   C  CG    . ASN A 1 71   ? 138.416 131.458 139.143 1.00 49.79  ? 71   ASN A CG    1 
ATOM   591   O  OD1   . ASN A 1 71   ? 137.387 132.086 139.384 1.00 48.92  ? 71   ASN A OD1   1 
ATOM   592   N  ND2   . ASN A 1 71   ? 138.662 130.262 139.659 1.00 53.11  ? 71   ASN A ND2   1 
ATOM   593   N  N     . ALA A 1 72   ? 142.179 133.444 137.287 1.00 36.74  ? 72   ALA A N     1 
ATOM   594   C  CA    . ALA A 1 72   ? 143.460 133.405 136.590 1.00 34.73  ? 72   ALA A CA    1 
ATOM   595   C  C     . ALA A 1 72   ? 144.606 133.745 137.531 1.00 38.76  ? 72   ALA A C     1 
ATOM   596   O  O     . ALA A 1 72   ? 145.673 133.123 137.469 1.00 37.49  ? 72   ALA A O     1 
ATOM   597   C  CB    . ALA A 1 72   ? 143.440 134.362 135.401 1.00 31.92  ? 72   ALA A CB    1 
ATOM   598   N  N     . LEU A 1 73   ? 144.409 134.734 138.406 1.00 39.95  ? 73   LEU A N     1 
ATOM   599   C  CA    . LEU A 1 73   ? 145.447 135.073 139.374 1.00 35.58  ? 73   LEU A CA    1 
ATOM   600   C  C     . LEU A 1 73   ? 145.608 133.993 140.436 1.00 35.53  ? 73   LEU A C     1 
ATOM   601   O  O     . LEU A 1 73   ? 146.716 133.780 140.938 1.00 35.65  ? 73   LEU A O     1 
ATOM   602   C  CB    . LEU A 1 73   ? 145.141 136.417 140.031 1.00 34.78  ? 73   LEU A CB    1 
ATOM   603   C  CG    . LEU A 1 73   ? 145.412 137.652 139.175 1.00 38.61  ? 73   LEU A CG    1 
ATOM   604   C  CD1   . LEU A 1 73   ? 144.695 138.867 139.740 1.00 37.92  ? 73   LEU A CD1   1 
ATOM   605   C  CD2   . LEU A 1 73   ? 146.909 137.900 139.082 1.00 41.36  ? 73   LEU A CD2   1 
ATOM   606   N  N     . ARG A 1 74   ? 144.519 133.312 140.795 1.00 36.78  ? 74   ARG A N     1 
ATOM   607   C  CA    . ARG A 1 74   ? 144.584 132.283 141.826 1.00 35.53  ? 74   ARG A CA    1 
ATOM   608   C  C     . ARG A 1 74   ? 145.384 131.072 141.363 1.00 39.44  ? 74   ARG A C     1 
ATOM   609   O  O     . ARG A 1 74   ? 146.106 130.461 142.155 1.00 43.54  ? 74   ARG A O     1 
ATOM   610   C  CB    . ARG A 1 74   ? 143.170 131.882 142.239 1.00 37.24  ? 74   ARG A CB    1 
ATOM   611   C  CG    . ARG A 1 74   ? 143.097 130.953 143.427 1.00 44.26  ? 74   ARG A CG    1 
ATOM   612   C  CD    . ARG A 1 74   ? 141.683 130.423 143.602 1.00 45.03  ? 74   ARG A CD    1 
ATOM   613   N  NE    . ARG A 1 74   ? 141.174 129.739 142.419 1.00 48.16  ? 74   ARG A NE    1 
ATOM   614   C  CZ    . ARG A 1 74   ? 141.651 128.601 141.932 1.00 52.57  ? 74   ARG A CZ    1 
ATOM   615   N  NH1   . ARG A 1 74   ? 142.666 127.973 142.504 1.00 49.32  ? 74   ARG A NH1   1 
ATOM   616   N  NH2   . ARG A 1 74   ? 141.090 128.075 140.847 1.00 54.55  ? 74   ARG A NH2   1 
ATOM   617   N  N     . ARG A 1 75   ? 145.272 130.707 140.090 1.00 42.32  ? 75   ARG A N     1 
ATOM   618   C  CA    . ARG A 1 75   ? 146.040 129.590 139.556 1.00 39.34  ? 75   ARG A CA    1 
ATOM   619   C  C     . ARG A 1 75   ? 147.495 129.942 139.276 1.00 38.69  ? 75   ARG A C     1 
ATOM   620   O  O     . ARG A 1 75   ? 148.206 129.133 138.673 1.00 40.18  ? 75   ARG A O     1 
ATOM   621   C  CB    . ARG A 1 75   ? 145.367 129.056 138.291 1.00 36.81  ? 75   ARG A CB    1 
ATOM   622   C  CG    . ARG A 1 75   ? 143.972 128.534 138.551 1.00 42.58  ? 75   ARG A CG    1 
ATOM   623   C  CD    . ARG A 1 75   ? 143.434 127.745 137.379 1.00 48.75  ? 75   ARG A CD    1 
ATOM   624   N  NE    . ARG A 1 75   ? 143.407 128.537 136.157 1.00 53.40  ? 75   ARG A NE    1 
ATOM   625   C  CZ    . ARG A 1 75   ? 142.297 128.942 135.554 1.00 51.40  ? 75   ARG A CZ    1 
ATOM   626   N  NH1   . ARG A 1 75   ? 141.102 128.635 136.029 1.00 51.59  ? 75   ARG A NH1   1 
ATOM   627   N  NH2   . ARG A 1 75   ? 142.390 129.668 134.444 1.00 41.72  ? 75   ARG A NH2   1 
ATOM   628   N  N     . CYS A 1 76   ? 147.954 131.115 139.697 1.00 40.77  ? 76   CYS A N     1 
ATOM   629   C  CA    . CYS A 1 76   ? 149.338 131.538 139.533 1.00 39.64  ? 76   CYS A CA    1 
ATOM   630   C  C     . CYS A 1 76   ? 150.048 131.807 140.849 1.00 40.95  ? 76   CYS A C     1 
ATOM   631   O  O     . CYS A 1 76   ? 151.257 131.587 140.946 1.00 42.25  ? 76   CYS A O     1 
ATOM   632   C  CB    . CYS A 1 76   ? 149.404 132.804 138.665 1.00 36.97  ? 76   CYS A CB    1 
ATOM   633   S  SG    . CYS A 1 76   ? 149.145 132.546 136.904 1.00 55.48  ? 76   CYS A SG    1 
ATOM   634   N  N     . PHE A 1 77   ? 149.328 132.278 141.873 1.00 38.11  ? 77   PHE A N     1 
ATOM   635   C  CA    . PHE A 1 77   ? 149.972 132.796 143.074 1.00 38.82  ? 77   PHE A CA    1 
ATOM   636   C  C     . PHE A 1 77   ? 149.327 132.314 144.370 1.00 40.39  ? 77   PHE A C     1 
ATOM   637   O  O     . PHE A 1 77   ? 149.516 132.953 145.411 1.00 45.23  ? 77   PHE A O     1 
ATOM   638   C  CB    . PHE A 1 77   ? 149.958 134.329 143.068 1.00 37.46  ? 77   PHE A CB    1 
ATOM   639   C  CG    . PHE A 1 77   ? 150.652 134.944 141.889 1.00 34.16  ? 77   PHE A CG    1 
ATOM   640   C  CD1   . PHE A 1 77   ? 152.032 134.959 141.812 1.00 33.24  ? 77   PHE A CD1   1 
ATOM   641   C  CD2   . PHE A 1 77   ? 149.923 135.494 140.851 1.00 33.41  ? 77   PHE A CD2   1 
ATOM   642   C  CE1   . PHE A 1 77   ? 152.672 135.525 140.734 1.00 33.12  ? 77   PHE A CE1   1 
ATOM   643   C  CE2   . PHE A 1 77   ? 150.556 136.059 139.767 1.00 35.42  ? 77   PHE A CE2   1 
ATOM   644   C  CZ    . PHE A 1 77   ? 151.933 136.075 139.708 1.00 35.59  ? 77   PHE A CZ    1 
ATOM   645   N  N     . PHE A 1 78   ? 148.572 131.216 144.350 1.00 38.91  ? 78   PHE A N     1 
ATOM   646   C  CA    . PHE A 1 78   ? 147.802 130.850 145.534 1.00 42.66  ? 78   PHE A CA    1 
ATOM   647   C  C     . PHE A 1 78   ? 148.646 130.106 146.563 1.00 45.92  ? 78   PHE A C     1 
ATOM   648   O  O     . PHE A 1 78   ? 148.660 130.472 147.743 1.00 42.96  ? 78   PHE A O     1 
ATOM   649   C  CB    . PHE A 1 78   ? 146.593 130.004 145.137 1.00 41.87  ? 78   PHE A CB    1 
ATOM   650   C  CG    . PHE A 1 78   ? 145.726 129.614 146.293 1.00 44.36  ? 78   PHE A CG    1 
ATOM   651   C  CD1   . PHE A 1 78   ? 144.916 130.548 146.910 1.00 45.66  ? 78   PHE A CD1   1 
ATOM   652   C  CD2   . PHE A 1 78   ? 145.719 128.314 146.763 1.00 50.23  ? 78   PHE A CD2   1 
ATOM   653   C  CE1   . PHE A 1 78   ? 144.116 130.197 147.972 1.00 49.69  ? 78   PHE A CE1   1 
ATOM   654   C  CE2   . PHE A 1 78   ? 144.920 127.955 147.828 1.00 50.69  ? 78   PHE A CE2   1 
ATOM   655   C  CZ    . PHE A 1 78   ? 144.117 128.898 148.433 1.00 48.69  ? 78   PHE A CZ    1 
ATOM   656   N  N     . TRP A 1 79   ? 149.362 129.064 146.138 1.00 47.87  ? 79   TRP A N     1 
ATOM   657   C  CA    . TRP A 1 79   ? 150.038 128.200 147.099 1.00 46.62  ? 79   TRP A CA    1 
ATOM   658   C  C     . TRP A 1 79   ? 151.259 128.850 147.736 1.00 44.53  ? 79   TRP A C     1 
ATOM   659   O  O     . TRP A 1 79   ? 151.662 128.430 148.824 1.00 49.21  ? 79   TRP A O     1 
ATOM   660   C  CB    . TRP A 1 79   ? 150.420 126.874 146.443 1.00 53.65  ? 79   TRP A CB    1 
ATOM   661   C  CG    . TRP A 1 79   ? 149.226 126.075 146.046 1.00 57.61  ? 79   TRP A CG    1 
ATOM   662   C  CD1   . TRP A 1 79   ? 148.801 125.800 144.782 1.00 60.64  ? 79   TRP A CD1   1 
ATOM   663   C  CD2   . TRP A 1 79   ? 148.289 125.454 146.931 1.00 62.48  ? 79   TRP A CD2   1 
ATOM   664   N  NE1   . TRP A 1 79   ? 147.656 125.040 144.824 1.00 61.88  ? 79   TRP A NE1   1 
ATOM   665   C  CE2   . TRP A 1 79   ? 147.322 124.816 146.134 1.00 63.35  ? 79   TRP A CE2   1 
ATOM   666   C  CE3   . TRP A 1 79   ? 148.174 125.376 148.322 1.00 66.86  ? 79   TRP A CE3   1 
ATOM   667   C  CZ2   . TRP A 1 79   ? 146.255 124.106 146.680 1.00 66.04  ? 79   TRP A CZ2   1 
ATOM   668   C  CZ3   . TRP A 1 79   ? 147.116 124.673 148.862 1.00 68.55  ? 79   TRP A CZ3   1 
ATOM   669   C  CH2   . TRP A 1 79   ? 146.170 124.048 148.044 1.00 68.39  ? 79   TRP A CH2   1 
ATOM   670   N  N     . ARG A 1 80   ? 151.863 129.850 147.097 1.00 41.39  ? 80   ARG A N     1 
ATOM   671   C  CA    . ARG A 1 80   ? 152.900 130.612 147.783 1.00 39.38  ? 80   ARG A CA    1 
ATOM   672   C  C     . ARG A 1 80   ? 152.302 131.608 148.769 1.00 38.87  ? 80   ARG A C     1 
ATOM   673   O  O     . ARG A 1 80   ? 152.919 131.908 149.796 1.00 40.77  ? 80   ARG A O     1 
ATOM   674   C  CB    . ARG A 1 80   ? 153.790 131.330 146.769 1.00 42.41  ? 80   ARG A CB    1 
ATOM   675   C  CG    . ARG A 1 80   ? 154.728 130.398 146.025 1.00 48.24  ? 80   ARG A CG    1 
ATOM   676   C  CD    . ARG A 1 80   ? 155.656 131.149 145.088 1.00 52.61  ? 80   ARG A CD    1 
ATOM   677   N  NE    . ARG A 1 80   ? 156.406 132.193 145.777 1.00 57.23  ? 80   ARG A NE    1 
ATOM   678   C  CZ    . ARG A 1 80   ? 156.534 133.439 145.343 1.00 58.02  ? 80   ARG A CZ    1 
ATOM   679   N  NH1   . ARG A 1 80   ? 155.967 133.842 144.217 1.00 49.59  ? 80   ARG A NH1   1 
ATOM   680   N  NH2   . ARG A 1 80   ? 157.253 134.302 146.054 1.00 53.85  ? 80   ARG A NH2   1 
ATOM   681   N  N     . PHE A 1 81   ? 151.116 132.132 148.463 1.00 38.10  ? 81   PHE A N     1 
ATOM   682   C  CA    . PHE A 1 81   ? 150.415 133.041 149.365 1.00 34.54  ? 81   PHE A CA    1 
ATOM   683   C  C     . PHE A 1 81   ? 149.995 132.319 150.644 1.00 33.83  ? 81   PHE A C     1 
ATOM   684   O  O     . PHE A 1 81   ? 150.289 132.768 151.765 1.00 32.57  ? 81   PHE A O     1 
ATOM   685   C  CB    . PHE A 1 81   ? 149.218 133.624 148.602 1.00 31.89  ? 81   PHE A CB    1 
ATOM   686   C  CG    . PHE A 1 81   ? 148.305 134.494 149.415 1.00 31.76  ? 81   PHE A CG    1 
ATOM   687   C  CD1   . PHE A 1 81   ? 148.693 135.768 149.793 1.00 31.00  ? 81   PHE A CD1   1 
ATOM   688   C  CD2   . PHE A 1 81   ? 147.026 134.067 149.731 1.00 33.07  ? 81   PHE A CD2   1 
ATOM   689   C  CE1   . PHE A 1 81   ? 147.844 136.579 150.515 1.00 32.31  ? 81   PHE A CE1   1 
ATOM   690   C  CE2   . PHE A 1 81   ? 146.173 134.875 150.452 1.00 29.63  ? 81   PHE A CE2   1 
ATOM   691   C  CZ    . PHE A 1 81   ? 146.583 136.133 150.843 1.00 29.59  ? 81   PHE A CZ    1 
ATOM   692   N  N     . MET A 1 82   ? 149.355 131.159 150.491 1.00 35.81  ? 82   MET A N     1 
ATOM   693   C  CA    . MET A 1 82   ? 148.957 130.352 151.634 1.00 36.26  ? 82   MET A CA    1 
ATOM   694   C  C     . MET A 1 82   ? 150.156 129.789 152.383 1.00 35.57  ? 82   MET A C     1 
ATOM   695   O  O     . MET A 1 82   ? 150.037 129.475 153.570 1.00 37.41  ? 82   MET A O     1 
ATOM   696   C  CB    . MET A 1 82   ? 148.053 129.211 151.170 1.00 38.08  ? 82   MET A CB    1 
ATOM   697   C  CG    . MET A 1 82   ? 146.952 128.852 152.146 1.00 43.94  ? 82   MET A CG    1 
ATOM   698   S  SD    . MET A 1 82   ? 146.056 130.305 152.727 1.00 50.12  ? 82   MET A SD    1 
ATOM   699   C  CE    . MET A 1 82   ? 146.115 130.051 154.496 1.00 38.93  ? 82   MET A CE    1 
ATOM   700   N  N     . PHE A 1 83   ? 151.299 129.648 151.713 1.00 37.56  ? 83   PHE A N     1 
ATOM   701   C  CA    . PHE A 1 83   ? 152.496 129.132 152.368 1.00 33.94  ? 83   PHE A CA    1 
ATOM   702   C  C     . PHE A 1 83   ? 153.035 130.125 153.389 1.00 34.89  ? 83   PHE A C     1 
ATOM   703   O  O     . PHE A 1 83   ? 153.379 129.749 154.514 1.00 39.71  ? 83   PHE A O     1 
ATOM   704   C  CB    . PHE A 1 83   ? 153.551 128.798 151.312 1.00 34.49  ? 83   PHE A CB    1 
ATOM   705   C  CG    . PHE A 1 83   ? 154.913 128.514 151.872 1.00 37.12  ? 83   PHE A CG    1 
ATOM   706   C  CD1   . PHE A 1 83   ? 155.225 127.256 152.352 1.00 37.21  ? 83   PHE A CD1   1 
ATOM   707   C  CD2   . PHE A 1 83   ? 155.893 129.492 151.883 1.00 36.51  ? 83   PHE A CD2   1 
ATOM   708   C  CE1   . PHE A 1 83   ? 156.477 126.983 152.857 1.00 35.38  ? 83   PHE A CE1   1 
ATOM   709   C  CE2   . PHE A 1 83   ? 157.150 129.224 152.387 1.00 36.17  ? 83   PHE A CE2   1 
ATOM   710   C  CZ    . PHE A 1 83   ? 157.442 127.967 152.874 1.00 33.02  ? 83   PHE A CZ    1 
ATOM   711   N  N     . TYR A 1 84   ? 153.113 131.402 153.015 1.00 34.09  ? 84   TYR A N     1 
ATOM   712   C  CA    . TYR A 1 84   ? 153.570 132.437 153.932 1.00 30.08  ? 84   TYR A CA    1 
ATOM   713   C  C     . TYR A 1 84   ? 152.516 132.817 154.961 1.00 31.89  ? 84   TYR A C     1 
ATOM   714   O  O     . TYR A 1 84   ? 152.871 133.313 156.042 1.00 34.76  ? 84   TYR A O     1 
ATOM   715   C  CB    . TYR A 1 84   ? 153.989 133.679 153.149 1.00 27.94  ? 84   TYR A CB    1 
ATOM   716   C  CG    . TYR A 1 84   ? 155.235 133.486 152.322 1.00 29.37  ? 84   TYR A CG    1 
ATOM   717   C  CD1   . TYR A 1 84   ? 156.414 133.038 152.899 1.00 33.95  ? 84   TYR A CD1   1 
ATOM   718   C  CD2   . TYR A 1 84   ? 155.230 133.746 150.962 1.00 30.58  ? 84   TYR A CD2   1 
ATOM   719   C  CE1   . TYR A 1 84   ? 157.556 132.860 152.144 1.00 36.04  ? 84   TYR A CE1   1 
ATOM   720   C  CE2   . TYR A 1 84   ? 156.366 133.569 150.199 1.00 36.42  ? 84   TYR A CE2   1 
ATOM   721   C  CZ    . TYR A 1 84   ? 157.525 133.126 150.795 1.00 39.85  ? 84   TYR A CZ    1 
ATOM   722   O  OH    . TYR A 1 84   ? 158.659 132.951 150.040 1.00 42.05  ? 84   TYR A OH    1 
ATOM   723   N  N     . GLY A 1 85   ? 151.235 132.593 154.656 1.00 34.11  ? 85   GLY A N     1 
ATOM   724   C  CA    . GLY A 1 85   ? 150.208 132.852 155.649 1.00 34.25  ? 85   GLY A CA    1 
ATOM   725   C  C     . GLY A 1 85   ? 150.371 132.025 156.909 1.00 34.89  ? 85   GLY A C     1 
ATOM   726   O  O     . GLY A 1 85   ? 150.120 132.517 158.013 1.00 34.50  ? 85   GLY A O     1 
ATOM   727   N  N     . ILE A 1 86   ? 150.819 130.775 156.769 1.00 35.75  ? 86   ILE A N     1 
ATOM   728   C  CA    . ILE A 1 86   ? 150.981 129.900 157.928 1.00 37.55  ? 86   ILE A CA    1 
ATOM   729   C  C     . ILE A 1 86   ? 152.070 130.423 158.855 1.00 35.69  ? 86   ILE A C     1 
ATOM   730   O  O     . ILE A 1 86   ? 151.906 130.434 160.081 1.00 35.68  ? 86   ILE A O     1 
ATOM   731   C  CB    . ILE A 1 86   ? 151.267 128.456 157.475 1.00 36.39  ? 86   ILE A CB    1 
ATOM   732   C  CG1   . ILE A 1 86   ? 149.966 127.658 157.377 1.00 39.01  ? 86   ILE A CG1   1 
ATOM   733   C  CG2   . ILE A 1 86   ? 152.218 127.763 158.437 1.00 35.48  ? 86   ILE A CG2   1 
ATOM   734   C  CD1   . ILE A 1 86   ? 148.988 128.183 156.364 1.00 39.73  ? 86   ILE A CD1   1 
ATOM   735   N  N     . PHE A 1 87   ? 153.197 130.862 158.296 1.00 34.66  ? 87   PHE A N     1 
ATOM   736   C  CA    . PHE A 1 87   ? 154.275 131.355 159.144 1.00 31.80  ? 87   PHE A CA    1 
ATOM   737   C  C     . PHE A 1 87   ? 153.933 132.711 159.745 1.00 32.44  ? 87   PHE A C     1 
ATOM   738   O  O     . PHE A 1 87   ? 154.323 132.998 160.883 1.00 37.05  ? 87   PHE A O     1 
ATOM   739   C  CB    . PHE A 1 87   ? 155.577 131.415 158.350 1.00 32.88  ? 87   PHE A CB    1 
ATOM   740   C  CG    . PHE A 1 87   ? 156.071 130.068 157.917 1.00 37.10  ? 87   PHE A CG    1 
ATOM   741   C  CD1   . PHE A 1 87   ? 156.467 129.127 158.851 1.00 37.19  ? 87   PHE A CD1   1 
ATOM   742   C  CD2   . PHE A 1 87   ? 156.128 129.737 156.577 1.00 35.57  ? 87   PHE A CD2   1 
ATOM   743   C  CE1   . PHE A 1 87   ? 156.912 127.883 158.454 1.00 33.20  ? 87   PHE A CE1   1 
ATOM   744   C  CE2   . PHE A 1 87   ? 156.575 128.498 156.175 1.00 35.75  ? 87   PHE A CE2   1 
ATOM   745   C  CZ    . PHE A 1 87   ? 156.967 127.569 157.112 1.00 33.89  ? 87   PHE A CZ    1 
ATOM   746   N  N     . LEU A 1 88   ? 153.178 133.541 159.023 1.00 33.16  ? 88   LEU A N     1 
ATOM   747   C  CA    . LEU A 1 88   ? 152.689 134.775 159.628 1.00 34.16  ? 88   LEU A CA    1 
ATOM   748   C  C     . LEU A 1 88   ? 151.774 134.473 160.813 1.00 34.88  ? 88   LEU A C     1 
ATOM   749   O  O     . LEU A 1 88   ? 151.883 135.101 161.876 1.00 36.57  ? 88   LEU A O     1 
ATOM   750   C  CB    . LEU A 1 88   ? 151.966 135.613 158.573 1.00 35.99  ? 88   LEU A CB    1 
ATOM   751   C  CG    . LEU A 1 88   ? 151.552 137.036 158.936 1.00 39.36  ? 88   LEU A CG    1 
ATOM   752   C  CD1   . LEU A 1 88   ? 152.775 137.931 159.015 1.00 39.85  ? 88   LEU A CD1   1 
ATOM   753   C  CD2   . LEU A 1 88   ? 150.560 137.571 157.923 1.00 37.10  ? 88   LEU A CD2   1 
ATOM   754   N  N     . TYR A 1 89   ? 150.888 133.486 160.661 1.00 32.90  ? 89   TYR A N     1 
ATOM   755   C  CA    . TYR A 1 89   ? 150.008 133.099 161.758 1.00 32.44  ? 89   TYR A CA    1 
ATOM   756   C  C     . TYR A 1 89   ? 150.790 132.542 162.943 1.00 34.59  ? 89   TYR A C     1 
ATOM   757   O  O     . TYR A 1 89   ? 150.451 132.819 164.098 1.00 37.35  ? 89   TYR A O     1 
ATOM   758   C  CB    . TYR A 1 89   ? 148.987 132.075 161.274 1.00 33.64  ? 89   TYR A CB    1 
ATOM   759   C  CG    . TYR A 1 89   ? 148.139 131.517 162.385 1.00 34.59  ? 89   TYR A CG    1 
ATOM   760   C  CD1   . TYR A 1 89   ? 147.271 132.333 163.090 1.00 36.35  ? 89   TYR A CD1   1 
ATOM   761   C  CD2   . TYR A 1 89   ? 148.210 130.178 162.733 1.00 33.76  ? 89   TYR A CD2   1 
ATOM   762   C  CE1   . TYR A 1 89   ? 146.493 131.834 164.107 1.00 35.07  ? 89   TYR A CE1   1 
ATOM   763   C  CE2   . TYR A 1 89   ? 147.434 129.669 163.751 1.00 35.51  ? 89   TYR A CE2   1 
ATOM   764   C  CZ    . TYR A 1 89   ? 146.577 130.501 164.433 1.00 37.19  ? 89   TYR A CZ    1 
ATOM   765   O  OH    . TYR A 1 89   ? 145.800 130.002 165.449 1.00 40.05  ? 89   TYR A OH    1 
ATOM   766   N  N     . LEU A 1 90   ? 151.809 131.720 162.682 1.00 36.16  ? 90   LEU A N     1 
ATOM   767   C  CA    . LEU A 1 90   ? 152.595 131.161 163.777 1.00 31.98  ? 90   LEU A CA    1 
ATOM   768   C  C     . LEU A 1 90   ? 153.417 132.226 164.485 1.00 37.06  ? 90   LEU A C     1 
ATOM   769   O  O     . LEU A 1 90   ? 153.677 132.106 165.687 1.00 40.25  ? 90   LEU A O     1 
ATOM   770   C  CB    . LEU A 1 90   ? 153.508 130.044 163.274 1.00 32.57  ? 90   LEU A CB    1 
ATOM   771   C  CG    . LEU A 1 90   ? 152.832 128.716 162.941 1.00 34.74  ? 90   LEU A CG    1 
ATOM   772   C  CD1   . LEU A 1 90   ? 153.817 127.758 162.291 1.00 35.95  ? 90   LEU A CD1   1 
ATOM   773   C  CD2   . LEU A 1 90   ? 152.235 128.109 164.194 1.00 31.36  ? 90   LEU A CD2   1 
ATOM   774   N  N     . GLY A 1 91   ? 153.848 133.264 163.767 1.00 38.74  ? 91   GLY A N     1 
ATOM   775   C  CA    . GLY A 1 91   ? 154.490 134.379 164.438 1.00 37.70  ? 91   GLY A CA    1 
ATOM   776   C  C     . GLY A 1 91   ? 153.537 135.256 165.216 1.00 38.50  ? 91   GLY A C     1 
ATOM   777   O  O     . GLY A 1 91   ? 153.957 135.907 166.177 1.00 38.40  ? 91   GLY A O     1 
ATOM   778   N  N     . GLU A 1 92   ? 152.262 135.285 164.825 1.00 42.65  ? 92   GLU A N     1 
ATOM   779   C  CA    . GLU A 1 92   ? 151.269 136.016 165.608 1.00 39.17  ? 92   GLU A CA    1 
ATOM   780   C  C     . GLU A 1 92   ? 150.825 135.241 166.846 1.00 39.45  ? 92   GLU A C     1 
ATOM   781   O  O     . GLU A 1 92   ? 150.539 135.845 167.884 1.00 41.72  ? 92   GLU A O     1 
ATOM   782   C  CB    . GLU A 1 92   ? 150.063 136.365 164.738 1.00 34.45  ? 92   GLU A CB    1 
ATOM   783   C  CG    . GLU A 1 92   ? 150.358 137.405 163.681 1.00 38.22  ? 92   GLU A CG    1 
ATOM   784   C  CD    . GLU A 1 92   ? 150.582 138.777 164.280 1.00 46.69  ? 92   GLU A CD    1 
ATOM   785   O  OE1   . GLU A 1 92   ? 150.117 139.009 165.414 1.00 47.75  ? 92   GLU A OE1   1 
ATOM   786   O  OE2   . GLU A 1 92   ? 151.226 139.620 163.625 1.00 49.51  ? 92   GLU A OE2   1 
ATOM   787   N  N     . VAL A 1 93   ? 150.751 133.912 166.754 1.00 37.59  ? 93   VAL A N     1 
ATOM   788   C  CA    . VAL A 1 93   ? 150.346 133.107 167.906 1.00 35.32  ? 93   VAL A CA    1 
ATOM   789   C  C     . VAL A 1 93   ? 151.332 133.290 169.053 1.00 39.04  ? 93   VAL A C     1 
ATOM   790   O  O     . VAL A 1 93   ? 150.947 133.323 170.228 1.00 39.57  ? 93   VAL A O     1 
ATOM   791   C  CB    . VAL A 1 93   ? 150.211 131.627 167.504 1.00 37.90  ? 93   VAL A CB    1 
ATOM   792   C  CG1   . VAL A 1 93   ? 150.198 130.737 168.731 1.00 33.49  ? 93   VAL A CG1   1 
ATOM   793   C  CG2   . VAL A 1 93   ? 148.954 131.420 166.693 1.00 42.21  ? 93   VAL A CG2   1 
ATOM   794   N  N     . THR A 1 94   ? 152.618 133.414 168.725 1.00 42.77  ? 94   THR A N     1 
ATOM   795   C  CA    . THR A 1 94   ? 153.640 133.683 169.730 1.00 37.69  ? 94   THR A CA    1 
ATOM   796   C  C     . THR A 1 94   ? 153.344 134.955 170.511 1.00 37.94  ? 94   THR A C     1 
ATOM   797   O  O     . THR A 1 94   ? 153.646 135.039 171.707 1.00 39.34  ? 94   THR A O     1 
ATOM   798   C  CB    . THR A 1 94   ? 155.005 133.779 169.043 1.00 39.77  ? 94   THR A CB    1 
ATOM   799   O  OG1   . THR A 1 94   ? 155.386 132.491 168.540 1.00 40.59  ? 94   THR A OG1   1 
ATOM   800   C  CG2   . THR A 1 94   ? 156.063 134.303 169.982 1.00 41.40  ? 94   THR A CG2   1 
ATOM   801   N  N     . LYS A 1 95   ? 152.725 135.940 169.864 1.00 41.72  ? 95   LYS A N     1 
ATOM   802   C  CA    . LYS A 1 95   ? 152.505 137.235 170.494 1.00 42.11  ? 95   LYS A CA    1 
ATOM   803   C  C     . LYS A 1 95   ? 151.442 137.168 171.583 1.00 41.25  ? 95   LYS A C     1 
ATOM   804   O  O     . LYS A 1 95   ? 151.481 137.958 172.532 1.00 40.88  ? 95   LYS A O     1 
ATOM   805   C  CB    . LYS A 1 95   ? 152.124 138.250 169.419 1.00 41.16  ? 95   LYS A CB    1 
ATOM   806   C  CG    . LYS A 1 95   ? 152.335 139.695 169.786 1.00 41.47  ? 95   LYS A CG    1 
ATOM   807   C  CD    . LYS A 1 95   ? 152.020 140.561 168.586 1.00 47.20  ? 95   LYS A CD    1 
ATOM   808   C  CE    . LYS A 1 95   ? 152.992 140.262 167.454 1.00 42.89  ? 95   LYS A CE    1 
ATOM   809   N  NZ    . LYS A 1 95   ? 152.762 141.128 166.269 1.00 41.44  ? 95   LYS A NZ    1 
ATOM   810   N  N     . ALA A 1 96   ? 150.488 136.244 171.462 1.00 40.86  ? 96   ALA A N     1 
ATOM   811   C  CA    . ALA A 1 96   ? 149.400 136.144 172.428 1.00 36.30  ? 96   ALA A CA    1 
ATOM   812   C  C     . ALA A 1 96   ? 149.815 135.450 173.718 1.00 38.34  ? 96   ALA A C     1 
ATOM   813   O  O     . ALA A 1 96   ? 149.250 135.742 174.777 1.00 41.56  ? 96   ALA A O     1 
ATOM   814   C  CB    . ALA A 1 96   ? 148.215 135.407 171.805 1.00 35.62  ? 96   ALA A CB    1 
ATOM   815   N  N     . VAL A 1 97   ? 150.788 134.538 173.663 1.00 38.34  ? 97   VAL A N     1 
ATOM   816   C  CA    . VAL A 1 97   ? 151.139 133.722 174.820 1.00 36.76  ? 97   VAL A CA    1 
ATOM   817   C  C     . VAL A 1 97   ? 152.292 134.303 175.620 1.00 39.41  ? 97   VAL A C     1 
ATOM   818   O  O     . VAL A 1 97   ? 152.691 133.712 176.632 1.00 42.16  ? 97   VAL A O     1 
ATOM   819   C  CB    . VAL A 1 97   ? 151.468 132.276 174.398 1.00 32.78  ? 97   VAL A CB    1 
ATOM   820   C  CG1   . VAL A 1 97   ? 150.266 131.631 173.733 1.00 34.94  ? 97   VAL A CG1   1 
ATOM   821   C  CG2   . VAL A 1 97   ? 152.675 132.250 173.480 1.00 32.10  ? 97   VAL A CG2   1 
ATOM   822   N  N     . GLN A 1 98   ? 152.847 135.435 175.196 1.00 39.10  ? 98   GLN A N     1 
ATOM   823   C  CA    . GLN A 1 98   ? 153.921 136.065 175.959 1.00 38.69  ? 98   GLN A CA    1 
ATOM   824   C  C     . GLN A 1 98   ? 153.508 136.485 177.368 1.00 39.18  ? 98   GLN A C     1 
ATOM   825   O  O     . GLN A 1 98   ? 154.313 136.286 178.294 1.00 41.81  ? 98   GLN A O     1 
ATOM   826   C  CB    . GLN A 1 98   ? 154.478 137.257 175.172 1.00 37.94  ? 98   GLN A CB    1 
ATOM   827   C  CG    . GLN A 1 98   ? 155.405 138.147 175.970 1.00 42.41  ? 98   GLN A CG    1 
ATOM   828   C  CD    . GLN A 1 98   ? 156.103 139.170 175.106 1.00 48.47  ? 98   GLN A CD    1 
ATOM   829   O  OE1   . GLN A 1 98   ? 156.648 138.842 174.055 1.00 51.39  ? 98   GLN A OE1   1 
ATOM   830   N  NE2   . GLN A 1 98   ? 156.087 140.422 175.544 1.00 49.80  ? 98   GLN A NE2   1 
ATOM   831   N  N     . PRO A 1 99   ? 152.323 137.065 177.610 1.00 40.04  ? 99   PRO A N     1 
ATOM   832   C  CA    . PRO A 1 99   ? 151.972 137.441 178.991 1.00 36.81  ? 99   PRO A CA    1 
ATOM   833   C  C     . PRO A 1 99   ? 151.909 136.273 179.962 1.00 37.21  ? 99   PRO A C     1 
ATOM   834   O  O     . PRO A 1 99   ? 152.027 136.491 181.173 1.00 38.41  ? 99   PRO A O     1 
ATOM   835   C  CB    . PRO A 1 99   ? 150.602 138.117 178.833 1.00 33.28  ? 99   PRO A CB    1 
ATOM   836   C  CG    . PRO A 1 99   ? 150.591 138.608 177.448 1.00 32.72  ? 99   PRO A CG    1 
ATOM   837   C  CD    . PRO A 1 99   ? 151.310 137.560 176.661 1.00 39.00  ? 99   PRO A CD    1 
ATOM   838   N  N     . LEU A 1 100  ? 151.704 135.045 179.480 1.00 37.53  ? 100  LEU A N     1 
ATOM   839   C  CA    . LEU A 1 100  ? 151.750 133.894 180.377 1.00 40.97  ? 100  LEU A CA    1 
ATOM   840   C  C     . LEU A 1 100  ? 153.139 133.697 180.966 1.00 41.97  ? 100  LEU A C     1 
ATOM   841   O  O     . LEU A 1 100  ? 153.271 133.262 182.115 1.00 45.23  ? 100  LEU A O     1 
ATOM   842   C  CB    . LEU A 1 100  ? 151.311 132.623 179.649 1.00 39.15  ? 100  LEU A CB    1 
ATOM   843   C  CG    . LEU A 1 100  ? 149.847 132.512 179.233 1.00 40.45  ? 100  LEU A CG    1 
ATOM   844   C  CD1   . LEU A 1 100  ? 149.639 131.282 178.371 1.00 40.53  ? 100  LEU A CD1   1 
ATOM   845   C  CD2   . LEU A 1 100  ? 148.956 132.459 180.458 1.00 39.77  ? 100  LEU A CD2   1 
ATOM   846   N  N     . LEU A 1 101  ? 154.181 134.003 180.198 1.00 42.84  ? 101  LEU A N     1 
ATOM   847   C  CA    . LEU A 1 101  ? 155.550 133.819 180.658 1.00 42.13  ? 101  LEU A CA    1 
ATOM   848   C  C     . LEU A 1 101  ? 156.095 135.049 181.371 1.00 36.90  ? 101  LEU A C     1 
ATOM   849   O  O     . LEU A 1 101  ? 156.787 134.916 182.384 1.00 40.23  ? 101  LEU A O     1 
ATOM   850   C  CB    . LEU A 1 101  ? 156.453 133.458 179.476 1.00 44.46  ? 101  LEU A CB    1 
ATOM   851   C  CG    . LEU A 1 101  ? 156.209 132.092 178.829 1.00 46.68  ? 101  LEU A CG    1 
ATOM   852   C  CD1   . LEU A 1 101  ? 156.952 131.976 177.512 1.00 46.30  ? 101  LEU A CD1   1 
ATOM   853   C  CD2   . LEU A 1 101  ? 156.622 130.976 179.772 1.00 50.97  ? 101  LEU A CD2   1 
ATOM   854   N  N     . LEU A 1 102  ? 155.800 136.246 180.865 1.00 35.74  ? 102  LEU A N     1 
ATOM   855   C  CA    . LEU A 1 102  ? 156.353 137.462 181.453 1.00 37.78  ? 102  LEU A CA    1 
ATOM   856   C  C     . LEU A 1 102  ? 155.612 137.884 182.716 1.00 38.62  ? 102  LEU A C     1 
ATOM   857   O  O     . LEU A 1 102  ? 156.215 138.492 183.609 1.00 39.67  ? 102  LEU A O     1 
ATOM   858   C  CB    . LEU A 1 102  ? 156.332 138.591 180.421 1.00 38.00  ? 102  LEU A CB    1 
ATOM   859   C  CG    . LEU A 1 102  ? 157.000 139.915 180.791 1.00 36.60  ? 102  LEU A CG    1 
ATOM   860   C  CD1   . LEU A 1 102  ? 158.425 139.681 181.238 1.00 35.17  ? 102  LEU A CD1   1 
ATOM   861   C  CD2   . LEU A 1 102  ? 156.964 140.868 179.615 1.00 38.06  ? 102  LEU A CD2   1 
ATOM   862   N  N     . GLY A 1 103  ? 154.320 137.569 182.812 1.00 39.08  ? 103  GLY A N     1 
ATOM   863   C  CA    . GLY A 1 103  ? 153.572 137.916 184.009 1.00 34.15  ? 103  GLY A CA    1 
ATOM   864   C  C     . GLY A 1 103  ? 154.056 137.172 185.238 1.00 38.91  ? 103  GLY A C     1 
ATOM   865   O  O     . GLY A 1 103  ? 154.142 137.745 186.327 1.00 41.01  ? 103  GLY A O     1 
ATOM   866   N  N     . ARG A 1 104  ? 154.372 135.885 185.085 1.00 41.30  ? 104  ARG A N     1 
ATOM   867   C  CA    . ARG A 1 104  ? 154.918 135.121 186.201 1.00 43.15  ? 104  ARG A CA    1 
ATOM   868   C  C     . ARG A 1 104  ? 156.324 135.578 186.568 1.00 41.23  ? 104  ARG A C     1 
ATOM   869   O  O     . ARG A 1 104  ? 156.751 135.396 187.713 1.00 45.94  ? 104  ARG A O     1 
ATOM   870   C  CB    . ARG A 1 104  ? 154.908 133.632 185.871 1.00 45.89  ? 104  ARG A CB    1 
ATOM   871   C  CG    . ARG A 1 104  ? 153.518 133.054 185.744 1.00 44.22  ? 104  ARG A CG    1 
ATOM   872   C  CD    . ARG A 1 104  ? 153.552 131.557 185.509 1.00 49.27  ? 104  ARG A CD    1 
ATOM   873   N  NE    . ARG A 1 104  ? 152.233 130.957 185.670 1.00 52.53  ? 104  ARG A NE    1 
ATOM   874   C  CZ    . ARG A 1 104  ? 151.255 131.048 184.780 1.00 51.68  ? 104  ARG A CZ    1 
ATOM   875   N  NH1   . ARG A 1 104  ? 151.414 131.701 183.642 1.00 50.51  ? 104  ARG A NH1   1 
ATOM   876   N  NH2   . ARG A 1 104  ? 150.088 130.467 185.039 1.00 49.89  ? 104  ARG A NH2   1 
ATOM   877   N  N     . ILE A 1 105  ? 157.064 136.146 185.617 1.00 37.38  ? 105  ILE A N     1 
ATOM   878   C  CA    . ILE A 1 105  ? 158.377 136.694 185.936 1.00 34.90  ? 105  ILE A CA    1 
ATOM   879   C  C     . ILE A 1 105  ? 158.243 137.992 186.722 1.00 35.04  ? 105  ILE A C     1 
ATOM   880   O  O     . ILE A 1 105  ? 158.949 138.204 187.714 1.00 37.17  ? 105  ILE A O     1 
ATOM   881   C  CB    . ILE A 1 105  ? 159.205 136.890 184.654 1.00 38.41  ? 105  ILE A CB    1 
ATOM   882   C  CG1   . ILE A 1 105  ? 159.644 135.540 184.087 1.00 41.57  ? 105  ILE A CG1   1 
ATOM   883   C  CG2   . ILE A 1 105  ? 160.417 137.763 184.922 1.00 38.38  ? 105  ILE A CG2   1 
ATOM   884   C  CD1   . ILE A 1 105  ? 160.122 135.611 182.655 1.00 43.38  ? 105  ILE A CD1   1 
ATOM   885   N  N     . ILE A 1 106  ? 157.332 138.875 186.305 1.00 35.66  ? 106  ILE A N     1 
ATOM   886   C  CA    . ILE A 1 106  ? 157.149 140.138 187.016 1.00 35.98  ? 106  ILE A CA    1 
ATOM   887   C  C     . ILE A 1 106  ? 156.615 139.887 188.422 1.00 38.31  ? 106  ILE A C     1 
ATOM   888   O  O     . ILE A 1 106  ? 156.998 140.570 189.378 1.00 38.08  ? 106  ILE A O     1 
ATOM   889   C  CB    . ILE A 1 106  ? 156.228 141.076 186.214 1.00 34.67  ? 106  ILE A CB    1 
ATOM   890   C  CG1   . ILE A 1 106  ? 156.947 141.596 184.972 1.00 34.37  ? 106  ILE A CG1   1 
ATOM   891   C  CG2   . ILE A 1 106  ? 155.778 142.250 187.060 1.00 35.65  ? 106  ILE A CG2   1 
ATOM   892   C  CD1   . ILE A 1 106  ? 156.014 142.127 183.910 1.00 36.66  ? 106  ILE A CD1   1 
ATOM   893   N  N     . ALA A 1 107  ? 155.735 138.897 188.574 1.00 39.23  ? 107  ALA A N     1 
ATOM   894   C  CA    . ALA A 1 107  ? 155.187 138.577 189.887 1.00 39.12  ? 107  ALA A CA    1 
ATOM   895   C  C     . ALA A 1 107  ? 156.240 138.048 190.852 1.00 46.14  ? 107  ALA A C     1 
ATOM   896   O  O     . ALA A 1 107  ? 156.041 138.133 192.067 1.00 51.90  ? 107  ALA A O     1 
ATOM   897   C  CB    . ALA A 1 107  ? 154.057 137.559 189.748 1.00 41.34  ? 107  ALA A CB    1 
ATOM   898   N  N     . SER A 1 108  ? 157.348 137.504 190.344 1.00 43.65  ? 108  SER A N     1 
ATOM   899   C  CA    . SER A 1 108  ? 158.386 136.935 191.197 1.00 40.05  ? 108  SER A CA    1 
ATOM   900   C  C     . SER A 1 108  ? 159.169 137.986 191.971 1.00 42.20  ? 108  SER A C     1 
ATOM   901   O  O     . SER A 1 108  ? 159.904 137.622 192.894 1.00 49.14  ? 108  SER A O     1 
ATOM   902   C  CB    . SER A 1 108  ? 159.347 136.092 190.357 1.00 39.92  ? 108  SER A CB    1 
ATOM   903   O  OG    . SER A 1 108  ? 160.350 136.891 189.758 1.00 39.23  ? 108  SER A OG    1 
ATOM   904   N  N     . TYR A 1 109  ? 159.041 139.268 191.622 1.00 40.33  ? 109  TYR A N     1 
ATOM   905   C  CA    . TYR A 1 109  ? 159.710 140.312 192.391 1.00 40.81  ? 109  TYR A CA    1 
ATOM   906   C  C     . TYR A 1 109  ? 159.068 140.490 193.758 1.00 48.44  ? 109  TYR A C     1 
ATOM   907   O  O     . TYR A 1 109  ? 159.735 140.915 194.708 1.00 55.53  ? 109  TYR A O     1 
ATOM   908   C  CB    . TYR A 1 109  ? 159.690 141.631 191.621 1.00 39.02  ? 109  TYR A CB    1 
ATOM   909   C  CG    . TYR A 1 109  ? 160.249 141.542 190.221 1.00 36.26  ? 109  TYR A CG    1 
ATOM   910   C  CD1   . TYR A 1 109  ? 161.297 140.686 189.924 1.00 34.72  ? 109  TYR A CD1   1 
ATOM   911   C  CD2   . TYR A 1 109  ? 159.718 142.306 189.194 1.00 36.78  ? 109  TYR A CD2   1 
ATOM   912   C  CE1   . TYR A 1 109  ? 161.805 140.599 188.648 1.00 34.41  ? 109  TYR A CE1   1 
ATOM   913   C  CE2   . TYR A 1 109  ? 160.219 142.225 187.915 1.00 36.95  ? 109  TYR A CE2   1 
ATOM   914   C  CZ    . TYR A 1 109  ? 161.262 141.369 187.647 1.00 37.14  ? 109  TYR A CZ    1 
ATOM   915   O  OH    . TYR A 1 109  ? 161.770 141.281 186.374 1.00 39.37  ? 109  TYR A OH    1 
ATOM   916   N  N     . ASP A 1 110  ? 157.784 140.197 193.867 1.00 52.25  ? 110  ASP A N     1 
ATOM   917   C  CA    . ASP A 1 110  ? 157.075 140.262 195.137 1.00 53.51  ? 110  ASP A CA    1 
ATOM   918   C  C     . ASP A 1 110  ? 157.446 139.050 195.984 1.00 54.33  ? 110  ASP A C     1 
ATOM   919   O  O     . ASP A 1 110  ? 157.283 137.914 195.521 1.00 55.50  ? 110  ASP A O     1 
ATOM   920   C  CB    . ASP A 1 110  ? 155.571 140.307 194.872 1.00 54.68  ? 110  ASP A CB    1 
ATOM   921   C  CG    . ASP A 1 110  ? 154.751 140.517 196.131 1.00 59.00  ? 110  ASP A CG    1 
ATOM   922   O  OD1   . ASP A 1 110  ? 155.332 140.776 197.202 1.00 62.86  ? 110  ASP A OD1   1 
ATOM   923   O  OD2   . ASP A 1 110  ? 153.510 140.427 196.043 1.00 58.74  ? 110  ASP A OD2   1 
ATOM   924   N  N     . PRO A 1 111  ? 157.956 139.233 197.205 1.00 58.44  ? 111  PRO A N     1 
ATOM   925   C  CA    . PRO A 1 111  ? 158.303 138.071 198.038 1.00 58.99  ? 111  PRO A CA    1 
ATOM   926   C  C     . PRO A 1 111  ? 157.132 137.156 198.347 1.00 60.93  ? 111  PRO A C     1 
ATOM   927   O  O     . PRO A 1 111  ? 157.357 135.987 198.685 1.00 60.06  ? 111  PRO A O     1 
ATOM   928   C  CB    . PRO A 1 111  ? 158.859 138.712 199.319 1.00 56.44  ? 111  PRO A CB    1 
ATOM   929   C  CG    . PRO A 1 111  ? 159.347 140.048 198.881 1.00 59.85  ? 111  PRO A CG    1 
ATOM   930   C  CD    . PRO A 1 111  ? 158.360 140.496 197.842 1.00 61.10  ? 111  PRO A CD    1 
ATOM   931   N  N     . ASP A 1 112  ? 155.896 137.649 198.265 1.00 63.01  ? 112  ASP A N     1 
ATOM   932   C  CA    . ASP A 1 112  ? 154.738 136.810 198.553 1.00 64.16  ? 112  ASP A CA    1 
ATOM   933   C  C     . ASP A 1 112  ? 154.649 135.627 197.597 1.00 67.33  ? 112  ASP A C     1 
ATOM   934   O  O     . ASP A 1 112  ? 154.404 134.491 198.017 1.00 69.20  ? 112  ASP A O     1 
ATOM   935   C  CB    . ASP A 1 112  ? 153.458 137.641 198.485 1.00 63.71  ? 112  ASP A CB    1 
ATOM   936   C  CG    . ASP A 1 112  ? 152.214 136.787 198.558 1.00 72.55  ? 112  ASP A CG    1 
ATOM   937   O  OD1   . ASP A 1 112  ? 151.896 136.283 199.656 1.00 82.83  ? 112  ASP A OD1   1 
ATOM   938   O  OD2   . ASP A 1 112  ? 151.558 136.615 197.510 1.00 65.72  ? 112  ASP A OD2   1 
ATOM   939   N  N     . ASN A 1 113  ? 154.855 135.874 196.303 1.00 65.97  ? 113  ASN A N     1 
ATOM   940   C  CA    . ASN A 1 113  ? 154.644 134.857 195.274 1.00 63.42  ? 113  ASN A CA    1 
ATOM   941   C  C     . ASN A 1 113  ? 155.802 133.858 195.251 1.00 62.48  ? 113  ASN A C     1 
ATOM   942   O  O     . ASN A 1 113  ? 156.490 133.681 194.248 1.00 63.47  ? 113  ASN A O     1 
ATOM   943   C  CB    . ASN A 1 113  ? 154.466 135.514 193.912 1.00 60.42  ? 113  ASN A CB    1 
ATOM   944   C  CG    . ASN A 1 113  ? 153.283 136.451 193.865 1.00 62.01  ? 113  ASN A CG    1 
ATOM   945   O  OD1   . ASN A 1 113  ? 152.163 136.069 194.192 1.00 66.09  ? 113  ASN A OD1   1 
ATOM   946   N  ND2   . ASN A 1 113  ? 153.524 137.685 193.447 1.00 56.22  ? 113  ASN A ND2   1 
ATOM   947   N  N     . LYS A 1 114  ? 155.998 133.191 196.392 1.00 61.06  ? 114  LYS A N     1 
ATOM   948   C  CA    . LYS A 1 114  ? 157.135 132.289 196.545 1.00 63.55  ? 114  LYS A CA    1 
ATOM   949   C  C     . LYS A 1 114  ? 157.106 131.142 195.541 1.00 68.05  ? 114  LYS A C     1 
ATOM   950   O  O     . LYS A 1 114  ? 158.156 130.568 195.233 1.00 65.73  ? 114  LYS A O     1 
ATOM   951   C  CB    . LYS A 1 114  ? 157.183 131.743 197.972 1.00 64.45  ? 114  LYS A CB    1 
ATOM   952   C  CG    . LYS A 1 114  ? 155.899 131.083 198.431 1.00 65.32  ? 114  LYS A CG    1 
ATOM   953   C  CD    . LYS A 1 114  ? 156.119 130.283 199.704 1.00 64.46  ? 114  LYS A CD    1 
ATOM   954   C  CE    . LYS A 1 114  ? 156.921 131.069 200.727 1.00 65.80  ? 114  LYS A CE    1 
ATOM   955   N  NZ    . LYS A 1 114  ? 156.041 131.813 201.669 1.00 61.43  ? 114  LYS A NZ    1 
ATOM   956   N  N     . GLU A 1 115  ? 155.928 130.783 195.028 1.00 68.91  ? 115  GLU A N     1 
ATOM   957   C  CA    . GLU A 1 115  ? 155.867 129.710 194.040 1.00 68.08  ? 115  GLU A CA    1 
ATOM   958   C  C     . GLU A 1 115  ? 156.487 130.137 192.715 1.00 67.31  ? 115  GLU A C     1 
ATOM   959   O  O     . GLU A 1 115  ? 157.195 129.351 192.074 1.00 65.57  ? 115  GLU A O     1 
ATOM   960   C  CB    . GLU A 1 115  ? 154.423 129.258 193.836 1.00 72.40  ? 115  GLU A CB    1 
ATOM   961   C  CG    . GLU A 1 115  ? 154.242 128.337 192.643 1.00 80.23  ? 115  GLU A CG    1 
ATOM   962   C  CD    . GLU A 1 115  ? 152.869 127.702 192.594 1.00 87.99  ? 115  GLU A CD    1 
ATOM   963   O  OE1   . GLU A 1 115  ? 152.321 127.383 193.669 1.00 93.78  ? 115  GLU A OE1   1 
ATOM   964   O  OE2   . GLU A 1 115  ? 152.339 127.519 191.479 1.00 90.51  ? 115  GLU A OE2   1 
ATOM   965   N  N     . GLU A 1 116  ? 156.230 131.374 192.283 1.00 64.80  ? 116  GLU A N     1 
ATOM   966   C  CA    . GLU A 1 116  ? 156.781 131.839 191.014 1.00 60.09  ? 116  GLU A CA    1 
ATOM   967   C  C     . GLU A 1 116  ? 158.295 131.974 191.073 1.00 60.47  ? 116  GLU A C     1 
ATOM   968   O  O     . GLU A 1 116  ? 158.966 131.866 190.042 1.00 62.24  ? 116  GLU A O     1 
ATOM   969   C  CB    . GLU A 1 116  ? 156.152 133.175 190.619 1.00 56.72  ? 116  GLU A CB    1 
ATOM   970   C  CG    . GLU A 1 116  ? 154.903 133.051 189.770 1.00 62.04  ? 116  GLU A CG    1 
ATOM   971   C  CD    . GLU A 1 116  ? 153.713 132.537 190.551 1.00 71.42  ? 116  GLU A CD    1 
ATOM   972   O  OE1   . GLU A 1 116  ? 153.624 132.829 191.761 1.00 70.08  ? 116  GLU A OE1   1 
ATOM   973   O  OE2   . GLU A 1 116  ? 152.863 131.845 189.954 1.00 72.84  ? 116  GLU A OE2   1 
ATOM   974   N  N     . ARG A 1 117  ? 158.853 132.209 192.261 1.00 60.30  ? 117  ARG A N     1 
ATOM   975   C  CA    . ARG A 1 117  ? 160.294 132.391 192.379 1.00 60.51  ? 117  ARG A CA    1 
ATOM   976   C  C     . ARG A 1 117  ? 161.046 131.073 192.270 1.00 63.91  ? 117  ARG A C     1 
ATOM   977   O  O     . ARG A 1 117  ? 162.256 131.075 192.019 1.00 64.83  ? 117  ARG A O     1 
ATOM   978   C  CB    . ARG A 1 117  ? 160.630 133.078 193.702 1.00 57.55  ? 117  ARG A CB    1 
ATOM   979   C  CG    . ARG A 1 117  ? 159.550 134.022 194.181 1.00 57.91  ? 117  ARG A CG    1 
ATOM   980   C  CD    . ARG A 1 117  ? 159.947 134.753 195.448 1.00 61.39  ? 117  ARG A CD    1 
ATOM   981   N  NE    . ARG A 1 117  ? 160.780 135.914 195.170 1.00 59.76  ? 117  ARG A NE    1 
ATOM   982   C  CZ    . ARG A 1 117  ? 161.507 136.547 196.079 1.00 60.54  ? 117  ARG A CZ    1 
ATOM   983   N  NH1   . ARG A 1 117  ? 161.543 136.144 197.338 1.00 65.05  ? 117  ARG A NH1   1 
ATOM   984   N  NH2   . ARG A 1 117  ? 162.216 137.611 195.716 1.00 59.86  ? 117  ARG A NH2   1 
ATOM   985   N  N     . SER A 1 118  ? 160.359 129.947 192.467 1.00 63.26  ? 118  SER A N     1 
ATOM   986   C  CA    . SER A 1 118  ? 161.006 128.645 192.366 1.00 59.91  ? 118  SER A CA    1 
ATOM   987   C  C     . SER A 1 118  ? 161.270 128.225 190.923 1.00 63.45  ? 118  SER A C     1 
ATOM   988   O  O     . SER A 1 118  ? 162.085 127.324 190.698 1.00 63.95  ? 118  SER A O     1 
ATOM   989   C  CB    . SER A 1 118  ? 160.159 127.582 193.068 1.00 52.32  ? 118  SER A CB    1 
ATOM   990   O  OG    . SER A 1 118  ? 160.256 127.698 194.475 1.00 55.25  ? 118  SER A OG    1 
ATOM   991   N  N     . ILE A 1 119  ? 160.609 128.845 189.944 1.00 58.05  ? 119  ILE A N     1 
ATOM   992   C  CA    . ILE A 1 119  ? 160.711 128.402 188.556 1.00 55.82  ? 119  ILE A CA    1 
ATOM   993   C  C     . ILE A 1 119  ? 161.046 129.562 187.626 1.00 59.14  ? 119  ILE A C     1 
ATOM   994   O  O     . ILE A 1 119  ? 160.875 129.457 186.407 1.00 59.58  ? 119  ILE A O     1 
ATOM   995   C  CB    . ILE A 1 119  ? 159.414 127.705 188.105 1.00 52.05  ? 119  ILE A CB    1 
ATOM   996   C  CG1   . ILE A 1 119  ? 158.219 128.644 188.266 1.00 51.45  ? 119  ILE A CG1   1 
ATOM   997   C  CG2   . ILE A 1 119  ? 159.203 126.417 188.879 1.00 52.26  ? 119  ILE A CG2   1 
ATOM   998   C  CD1   . ILE A 1 119  ? 157.085 128.357 187.313 1.00 47.98  ? 119  ILE A CD1   1 
ATOM   999   N  N     . ALA A 1 120  ? 161.520 130.675 188.192 1.00 59.00  ? 120  ALA A N     1 
ATOM   1000  C  CA    . ALA A 1 120  ? 161.762 131.874 187.393 1.00 54.57  ? 120  ALA A CA    1 
ATOM   1001  C  C     . ALA A 1 120  ? 162.821 131.653 186.318 1.00 57.45  ? 120  ALA A C     1 
ATOM   1002  O  O     . ALA A 1 120  ? 162.730 132.236 185.230 1.00 60.30  ? 120  ALA A O     1 
ATOM   1003  C  CB    . ALA A 1 120  ? 162.169 133.031 188.304 1.00 49.28  ? 120  ALA A CB    1 
ATOM   1004  N  N     . ILE A 1 121  ? 163.831 130.829 186.600 1.00 55.71  ? 121  ILE A N     1 
ATOM   1005  C  CA    . ILE A 1 121  ? 164.926 130.627 185.653 1.00 57.66  ? 121  ILE A CA    1 
ATOM   1006  C  C     . ILE A 1 121  ? 164.413 129.974 184.375 1.00 60.29  ? 121  ILE A C     1 
ATOM   1007  O  O     . ILE A 1 121  ? 164.768 130.381 183.258 1.00 60.92  ? 121  ILE A O     1 
ATOM   1008  C  CB    . ILE A 1 121  ? 166.061 129.794 186.288 1.00 55.71  ? 121  ILE A CB    1 
ATOM   1009  C  CG1   . ILE A 1 121  ? 166.628 130.423 187.577 1.00 59.75  ? 121  ILE A CG1   1 
ATOM   1010  C  CG2   . ILE A 1 121  ? 167.176 129.566 185.284 1.00 51.98  ? 121  ILE A CG2   1 
ATOM   1011  C  CD1   . ILE A 1 121  ? 165.740 130.380 188.823 1.00 59.52  ? 121  ILE A CD1   1 
ATOM   1012  N  N     . TYR A 1 122  ? 163.558 128.965 184.519 1.00 59.08  ? 122  TYR A N     1 
ATOM   1013  C  CA    . TYR A 1 122  ? 163.046 128.250 183.361 1.00 55.28  ? 122  TYR A CA    1 
ATOM   1014  C  C     . TYR A 1 122  ? 162.093 129.123 182.560 1.00 56.93  ? 122  TYR A C     1 
ATOM   1015  O  O     . TYR A 1 122  ? 162.067 129.046 181.325 1.00 58.05  ? 122  TYR A O     1 
ATOM   1016  C  CB    . TYR A 1 122  ? 162.346 126.977 183.827 1.00 53.39  ? 122  TYR A CB    1 
ATOM   1017  C  CG    . TYR A 1 122  ? 163.154 126.200 184.844 1.00 58.66  ? 122  TYR A CG    1 
ATOM   1018  C  CD1   . TYR A 1 122  ? 164.490 125.897 184.625 1.00 58.76  ? 122  TYR A CD1   1 
ATOM   1019  C  CD2   . TYR A 1 122  ? 162.579 125.792 186.039 1.00 60.54  ? 122  TYR A CD2   1 
ATOM   1020  C  CE1   . TYR A 1 122  ? 165.226 125.197 185.567 1.00 58.74  ? 122  TYR A CE1   1 
ATOM   1021  C  CE2   . TYR A 1 122  ? 163.303 125.094 186.981 1.00 58.80  ? 122  TYR A CE2   1 
ATOM   1022  C  CZ    . TYR A 1 122  ? 164.625 124.799 186.743 1.00 60.60  ? 122  TYR A CZ    1 
ATOM   1023  O  OH    . TYR A 1 122  ? 165.344 124.101 187.686 1.00 60.85  ? 122  TYR A OH    1 
ATOM   1024  N  N     . LEU A 1 123  ? 161.347 129.993 183.245 1.00 54.66  ? 123  LEU A N     1 
ATOM   1025  C  CA    . LEU A 1 123  ? 160.495 130.957 182.558 1.00 55.54  ? 123  LEU A CA    1 
ATOM   1026  C  C     . LEU A 1 123  ? 161.329 131.950 181.761 1.00 54.48  ? 123  LEU A C     1 
ATOM   1027  O  O     . LEU A 1 123  ? 160.959 132.328 180.643 1.00 55.14  ? 123  LEU A O     1 
ATOM   1028  C  CB    . LEU A 1 123  ? 159.623 131.697 183.572 1.00 54.38  ? 123  LEU A CB    1 
ATOM   1029  C  CG    . LEU A 1 123  ? 158.537 130.911 184.302 1.00 51.96  ? 123  LEU A CG    1 
ATOM   1030  C  CD1   . LEU A 1 123  ? 158.064 131.693 185.514 1.00 50.48  ? 123  LEU A CD1   1 
ATOM   1031  C  CD2   . LEU A 1 123  ? 157.379 130.603 183.378 1.00 48.99  ? 123  LEU A CD2   1 
ATOM   1032  N  N     . GLY A 1 124  ? 162.459 132.383 182.322 1.00 51.02  ? 124  GLY A N     1 
ATOM   1033  C  CA    . GLY A 1 124  ? 163.346 133.262 181.580 1.00 49.65  ? 124  GLY A CA    1 
ATOM   1034  C  C     . GLY A 1 124  ? 163.911 132.595 180.341 1.00 55.31  ? 124  GLY A C     1 
ATOM   1035  O  O     . GLY A 1 124  ? 163.970 133.205 179.268 1.00 59.90  ? 124  GLY A O     1 
ATOM   1036  N  N     . ILE A 1 125  ? 164.318 131.329 180.467 1.00 53.14  ? 125  ILE A N     1 
ATOM   1037  C  CA    . ILE A 1 125  ? 164.818 130.597 179.304 1.00 50.74  ? 125  ILE A CA    1 
ATOM   1038  C  C     . ILE A 1 125  ? 163.734 130.486 178.235 1.00 49.78  ? 125  ILE A C     1 
ATOM   1039  O  O     . ILE A 1 125  ? 163.990 130.691 177.038 1.00 50.18  ? 125  ILE A O     1 
ATOM   1040  C  CB    . ILE A 1 125  ? 165.338 129.212 179.727 1.00 52.25  ? 125  ILE A CB    1 
ATOM   1041  C  CG1   . ILE A 1 125  ? 166.561 129.349 180.637 1.00 54.60  ? 125  ILE A CG1   1 
ATOM   1042  C  CG2   . ILE A 1 125  ? 165.672 128.372 178.506 1.00 50.13  ? 125  ILE A CG2   1 
ATOM   1043  C  CD1   . ILE A 1 125  ? 166.908 128.077 181.378 1.00 54.48  ? 125  ILE A CD1   1 
ATOM   1044  N  N     . GLY A 1 126  ? 162.503 130.180 178.650 1.00 48.44  ? 126  GLY A N     1 
ATOM   1045  C  CA    . GLY A 1 126  ? 161.411 130.085 177.695 1.00 47.26  ? 126  GLY A CA    1 
ATOM   1046  C  C     . GLY A 1 126  ? 161.125 131.397 176.986 1.00 47.29  ? 126  GLY A C     1 
ATOM   1047  O  O     . GLY A 1 126  ? 160.882 131.416 175.778 1.00 46.98  ? 126  GLY A O     1 
ATOM   1048  N  N     . LEU A 1 127  ? 161.147 132.510 177.723 1.00 47.51  ? 127  LEU A N     1 
ATOM   1049  C  CA    . LEU A 1 127  ? 160.910 133.808 177.096 1.00 46.82  ? 127  LEU A CA    1 
ATOM   1050  C  C     . LEU A 1 127  ? 162.022 134.157 176.113 1.00 45.81  ? 127  LEU A C     1 
ATOM   1051  O  O     . LEU A 1 127  ? 161.763 134.714 175.033 1.00 47.13  ? 127  LEU A O     1 
ATOM   1052  C  CB    . LEU A 1 127  ? 160.782 134.890 178.166 1.00 45.47  ? 127  LEU A CB    1 
ATOM   1053  C  CG    . LEU A 1 127  ? 160.280 136.257 177.702 1.00 43.14  ? 127  LEU A CG    1 
ATOM   1054  C  CD1   . LEU A 1 127  ? 158.840 136.162 177.245 1.00 45.61  ? 127  LEU A CD1   1 
ATOM   1055  C  CD2   . LEU A 1 127  ? 160.421 137.288 178.805 1.00 40.95  ? 127  LEU A CD2   1 
ATOM   1056  N  N     . CYS A 1 128  ? 163.268 133.836 176.471 1.00 46.48  ? 128  CYS A N     1 
ATOM   1057  C  CA    . CYS A 1 128  ? 164.384 134.106 175.572 1.00 50.37  ? 128  CYS A CA    1 
ATOM   1058  C  C     . CYS A 1 128  ? 164.260 133.303 174.285 1.00 47.87  ? 128  CYS A C     1 
ATOM   1059  O  O     . CYS A 1 128  ? 164.582 133.806 173.203 1.00 49.03  ? 128  CYS A O     1 
ATOM   1060  C  CB    . CYS A 1 128  ? 165.709 133.809 176.271 1.00 52.20  ? 128  CYS A CB    1 
ATOM   1061  S  SG    . CYS A 1 128  ? 166.078 134.905 177.659 1.00 59.24  ? 128  CYS A SG    1 
ATOM   1062  N  N     . LEU A 1 129  ? 163.797 132.055 174.379 1.00 46.75  ? 129  LEU A N     1 
ATOM   1063  C  CA    . LEU A 1 129  ? 163.566 131.280 173.161 1.00 47.37  ? 129  LEU A CA    1 
ATOM   1064  C  C     . LEU A 1 129  ? 162.373 131.806 172.370 1.00 44.71  ? 129  LEU A C     1 
ATOM   1065  O  O     . LEU A 1 129  ? 162.375 131.761 171.131 1.00 46.02  ? 129  LEU A O     1 
ATOM   1066  C  CB    . LEU A 1 129  ? 163.360 129.807 173.502 1.00 46.49  ? 129  LEU A CB    1 
ATOM   1067  C  CG    . LEU A 1 129  ? 164.619 129.006 173.822 1.00 47.14  ? 129  LEU A CG    1 
ATOM   1068  C  CD1   . LEU A 1 129  ? 164.246 127.611 174.293 1.00 45.25  ? 129  LEU A CD1   1 
ATOM   1069  C  CD2   . LEU A 1 129  ? 165.527 128.942 172.607 1.00 41.40  ? 129  LEU A CD2   1 
ATOM   1070  N  N     . LEU A 1 130  ? 161.349 132.301 173.067 1.00 43.34  ? 130  LEU A N     1 
ATOM   1071  C  CA    . LEU A 1 130  ? 160.150 132.792 172.399 1.00 43.24  ? 130  LEU A CA    1 
ATOM   1072  C  C     . LEU A 1 130  ? 160.454 134.027 171.558 1.00 40.77  ? 130  LEU A C     1 
ATOM   1073  O  O     . LEU A 1 130  ? 159.945 134.164 170.439 1.00 38.98  ? 130  LEU A O     1 
ATOM   1074  C  CB    . LEU A 1 130  ? 159.075 133.085 173.445 1.00 46.22  ? 130  LEU A CB    1 
ATOM   1075  C  CG    . LEU A 1 130  ? 157.628 133.287 173.003 1.00 42.76  ? 130  LEU A CG    1 
ATOM   1076  C  CD1   . LEU A 1 130  ? 157.055 131.977 172.501 1.00 39.83  ? 130  LEU A CD1   1 
ATOM   1077  C  CD2   . LEU A 1 130  ? 156.791 133.829 174.147 1.00 40.26  ? 130  LEU A CD2   1 
ATOM   1078  N  N     . PHE A 1 131  ? 161.300 134.927 172.069 1.00 43.41  ? 131  PHE A N     1 
ATOM   1079  C  CA    . PHE A 1 131  ? 161.692 136.095 171.277 1.00 44.25  ? 131  PHE A CA    1 
ATOM   1080  C  C     . PHE A 1 131  ? 162.408 135.684 169.994 1.00 46.48  ? 131  PHE A C     1 
ATOM   1081  O  O     . PHE A 1 131  ? 162.126 136.219 168.910 1.00 45.97  ? 131  PHE A O     1 
ATOM   1082  C  CB    . PHE A 1 131  ? 162.597 137.020 172.087 1.00 45.10  ? 131  PHE A CB    1 
ATOM   1083  C  CG    . PHE A 1 131  ? 161.902 137.747 173.193 1.00 48.54  ? 131  PHE A CG    1 
ATOM   1084  C  CD1   . PHE A 1 131  ? 160.631 138.254 173.013 1.00 46.56  ? 131  PHE A CD1   1 
ATOM   1085  C  CD2   . PHE A 1 131  ? 162.538 137.953 174.405 1.00 47.10  ? 131  PHE A CD2   1 
ATOM   1086  C  CE1   . PHE A 1 131  ? 159.994 138.934 174.027 1.00 46.93  ? 131  PHE A CE1   1 
ATOM   1087  C  CE2   . PHE A 1 131  ? 161.907 138.634 175.423 1.00 48.99  ? 131  PHE A CE2   1 
ATOM   1088  C  CZ    . PHE A 1 131  ? 160.632 139.125 175.233 1.00 51.04  ? 131  PHE A CZ    1 
ATOM   1089  N  N     . ILE A 1 132  ? 163.345 134.740 170.105 1.00 46.50  ? 132  ILE A N     1 
ATOM   1090  C  CA    . ILE A 1 132  ? 164.121 134.307 168.950 1.00 43.21  ? 132  ILE A CA    1 
ATOM   1091  C  C     . ILE A 1 132  ? 163.219 133.659 167.912 1.00 43.18  ? 132  ILE A C     1 
ATOM   1092  O  O     . ILE A 1 132  ? 163.363 133.903 166.709 1.00 43.90  ? 132  ILE A O     1 
ATOM   1093  C  CB    . ILE A 1 132  ? 165.248 133.356 169.391 1.00 44.19  ? 132  ILE A CB    1 
ATOM   1094  C  CG1   . ILE A 1 132  ? 166.315 134.111 170.180 1.00 47.05  ? 132  ILE A CG1   1 
ATOM   1095  C  CG2   . ILE A 1 132  ? 165.870 132.668 168.192 1.00 40.77  ? 132  ILE A CG2   1 
ATOM   1096  C  CD1   . ILE A 1 132  ? 167.243 133.204 170.958 1.00 46.92  ? 132  ILE A CD1   1 
ATOM   1097  N  N     . VAL A 1 133  ? 162.280 132.817 168.349 1.00 42.53  ? 133  VAL A N     1 
ATOM   1098  C  CA    . VAL A 1 133  ? 161.418 132.179 167.360 1.00 37.04  ? 133  VAL A CA    1 
ATOM   1099  C  C     . VAL A 1 133  ? 160.468 133.194 166.734 1.00 44.69  ? 133  VAL A C     1 
ATOM   1100  O  O     . VAL A 1 133  ? 160.122 133.072 165.554 1.00 49.88  ? 133  VAL A O     1 
ATOM   1101  C  CB    . VAL A 1 133  ? 160.660 130.978 167.956 1.00 38.38  ? 133  VAL A CB    1 
ATOM   1102  C  CG1   . VAL A 1 133  ? 161.638 129.914 168.422 1.00 41.00  ? 133  VAL A CG1   1 
ATOM   1103  C  CG2   . VAL A 1 133  ? 159.744 131.405 169.076 1.00 46.96  ? 133  VAL A CG2   1 
ATOM   1104  N  N     . ARG A 1 134  ? 160.037 134.212 167.486 1.00 44.28  ? 134  ARG A N     1 
ATOM   1105  C  CA    . ARG A 1 134  ? 159.149 135.206 166.890 1.00 41.42  ? 134  ARG A CA    1 
ATOM   1106  C  C     . ARG A 1 134  ? 159.863 136.024 165.822 1.00 44.04  ? 134  ARG A C     1 
ATOM   1107  O  O     . ARG A 1 134  ? 159.311 136.261 164.743 1.00 44.17  ? 134  ARG A O     1 
ATOM   1108  C  CB    . ARG A 1 134  ? 158.562 136.133 167.953 1.00 40.11  ? 134  ARG A CB    1 
ATOM   1109  C  CG    . ARG A 1 134  ? 157.509 137.057 167.358 1.00 42.08  ? 134  ARG A CG    1 
ATOM   1110  C  CD    . ARG A 1 134  ? 156.661 137.777 168.386 1.00 45.33  ? 134  ARG A CD    1 
ATOM   1111  N  NE    . ARG A 1 134  ? 157.449 138.625 169.269 1.00 48.13  ? 134  ARG A NE    1 
ATOM   1112  C  CZ    . ARG A 1 134  ? 157.369 138.599 170.591 1.00 47.67  ? 134  ARG A CZ    1 
ATOM   1113  N  NH1   . ARG A 1 134  ? 156.528 137.793 171.216 1.00 43.37  ? 134  ARG A NH1   1 
ATOM   1114  N  NH2   . ARG A 1 134  ? 158.142 139.413 171.303 1.00 50.71  ? 134  ARG A NH2   1 
ATOM   1115  N  N     . THR A 1 135  ? 161.088 136.478 166.105 1.00 45.37  ? 135  THR A N     1 
ATOM   1116  C  CA    . THR A 1 135  ? 161.744 137.379 165.158 1.00 43.78  ? 135  THR A CA    1 
ATOM   1117  C  C     . THR A 1 135  ? 162.066 136.705 163.827 1.00 44.00  ? 135  THR A C     1 
ATOM   1118  O  O     . THR A 1 135  ? 162.216 137.401 162.818 1.00 46.33  ? 135  THR A O     1 
ATOM   1119  C  CB    . THR A 1 135  ? 163.023 137.969 165.758 1.00 43.06  ? 135  THR A CB    1 
ATOM   1120  O  OG1   . THR A 1 135  ? 163.547 138.971 164.878 1.00 39.22  ? 135  THR A OG1   1 
ATOM   1121  C  CG2   . THR A 1 135  ? 164.073 136.898 165.952 1.00 43.59  ? 135  THR A CG2   1 
ATOM   1122  N  N     . LEU A 1 136  ? 162.159 135.376 163.793 1.00 42.43  ? 136  LEU A N     1 
ATOM   1123  C  CA    . LEU A 1 136  ? 162.522 134.660 162.577 1.00 40.12  ? 136  LEU A CA    1 
ATOM   1124  C  C     . LEU A 1 136  ? 161.323 134.236 161.741 1.00 41.88  ? 136  LEU A C     1 
ATOM   1125  O  O     . LEU A 1 136  ? 161.503 133.842 160.584 1.00 43.68  ? 136  LEU A O     1 
ATOM   1126  C  CB    . LEU A 1 136  ? 163.350 133.420 162.920 1.00 37.91  ? 136  LEU A CB    1 
ATOM   1127  C  CG    . LEU A 1 136  ? 164.838 133.648 163.173 1.00 41.76  ? 136  LEU A CG    1 
ATOM   1128  C  CD1   . LEU A 1 136  ? 165.483 132.377 163.687 1.00 39.63  ? 136  LEU A CD1   1 
ATOM   1129  C  CD2   . LEU A 1 136  ? 165.522 134.120 161.904 1.00 42.96  ? 136  LEU A CD2   1 
ATOM   1130  N  N     . LEU A 1 137  ? 160.118 134.283 162.300 1.00 43.22  ? 137  LEU A N     1 
ATOM   1131  C  CA    . LEU A 1 137  ? 158.931 133.816 161.597 1.00 42.30  ? 137  LEU A CA    1 
ATOM   1132  C  C     . LEU A 1 137  ? 158.211 134.919 160.834 1.00 38.62  ? 137  LEU A C     1 
ATOM   1133  O  O     . LEU A 1 137  ? 157.494 134.626 159.872 1.00 40.88  ? 137  LEU A O     1 
ATOM   1134  C  CB    . LEU A 1 137  ? 157.957 133.174 162.589 1.00 43.47  ? 137  LEU A CB    1 
ATOM   1135  C  CG    . LEU A 1 137  ? 158.251 131.742 163.028 1.00 39.87  ? 137  LEU A CG    1 
ATOM   1136  C  CD1   . LEU A 1 137  ? 157.369 131.361 164.202 1.00 38.04  ? 137  LEU A CD1   1 
ATOM   1137  C  CD2   . LEU A 1 137  ? 158.054 130.786 161.877 1.00 37.21  ? 137  LEU A CD2   1 
ATOM   1138  N  N     . LEU A 1 138  ? 158.388 136.177 161.232 1.00 34.93  ? 138  LEU A N     1 
ATOM   1139  C  CA    . LEU A 1 138  ? 157.556 137.267 160.727 1.00 34.99  ? 138  LEU A CA    1 
ATOM   1140  C  C     . LEU A 1 138  ? 158.128 137.903 159.462 1.00 37.14  ? 138  LEU A C     1 
ATOM   1141  O  O     . LEU A 1 138  ? 157.455 137.959 158.429 1.00 35.23  ? 138  LEU A O     1 
ATOM   1142  C  CB    . LEU A 1 138  ? 157.382 138.330 161.817 1.00 35.94  ? 138  LEU A CB    1 
ATOM   1143  C  CG    . LEU A 1 138  ? 156.427 138.005 162.964 1.00 39.69  ? 138  LEU A CG    1 
ATOM   1144  C  CD1   . LEU A 1 138  ? 156.505 139.090 164.022 1.00 43.01  ? 138  LEU A CD1   1 
ATOM   1145  C  CD2   . LEU A 1 138  ? 155.006 137.838 162.466 1.00 37.41  ? 138  LEU A CD2   1 
ATOM   1146  N  N     . HIS A 1 139  ? 159.359 138.400 159.540 1.00 34.68  ? 139  HIS A N     1 
ATOM   1147  C  CA    . HIS A 1 139  ? 159.901 139.224 158.463 1.00 31.95  ? 139  HIS A CA    1 
ATOM   1148  C  C     . HIS A 1 139  ? 160.069 138.494 157.132 1.00 33.58  ? 139  HIS A C     1 
ATOM   1149  O  O     . HIS A 1 139  ? 159.721 139.087 156.093 1.00 34.71  ? 139  HIS A O     1 
ATOM   1150  C  CB    . HIS A 1 139  ? 161.218 139.845 158.936 1.00 32.06  ? 139  HIS A CB    1 
ATOM   1151  C  CG    . HIS A 1 139  ? 161.050 140.760 160.106 1.00 36.67  ? 139  HIS A CG    1 
ATOM   1152  N  ND1   . HIS A 1 139  ? 160.526 142.028 159.989 1.00 34.55  ? 139  HIS A ND1   1 
ATOM   1153  C  CD2   . HIS A 1 139  ? 161.301 140.577 161.424 1.00 36.20  ? 139  HIS A CD2   1 
ATOM   1154  C  CE1   . HIS A 1 139  ? 160.479 142.594 161.181 1.00 31.16  ? 139  HIS A CE1   1 
ATOM   1155  N  NE2   . HIS A 1 139  ? 160.943 141.735 162.069 1.00 35.41  ? 139  HIS A NE2   1 
ATOM   1156  N  N     . PRO A 1 140  ? 160.595 137.262 157.068 1.00 33.07  ? 140  PRO A N     1 
ATOM   1157  C  CA    . PRO A 1 140  ? 160.640 136.572 155.766 1.00 30.56  ? 140  PRO A CA    1 
ATOM   1158  C  C     . PRO A 1 140  ? 159.272 136.363 155.136 1.00 32.45  ? 140  PRO A C     1 
ATOM   1159  O  O     . PRO A 1 140  ? 159.139 136.482 153.911 1.00 36.30  ? 140  PRO A O     1 
ATOM   1160  C  CB    . PRO A 1 140  ? 161.332 135.241 156.102 1.00 29.77  ? 140  PRO A CB    1 
ATOM   1161  C  CG    . PRO A 1 140  ? 162.078 135.511 157.360 1.00 28.02  ? 140  PRO A CG    1 
ATOM   1162  C  CD    . PRO A 1 140  ? 161.212 136.445 158.125 1.00 32.13  ? 140  PRO A CD    1 
ATOM   1163  N  N     . ALA A 1 141  ? 158.240 136.081 155.936 1.00 28.39  ? 141  ALA A N     1 
ATOM   1164  C  CA    . ALA A 1 141  ? 156.899 135.924 155.379 1.00 26.27  ? 141  ALA A CA    1 
ATOM   1165  C  C     . ALA A 1 141  ? 156.384 137.232 154.793 1.00 30.80  ? 141  ALA A C     1 
ATOM   1166  O  O     . ALA A 1 141  ? 155.785 137.244 153.709 1.00 33.00  ? 141  ALA A O     1 
ATOM   1167  C  CB    . ALA A 1 141  ? 155.942 135.401 156.448 1.00 26.98  ? 141  ALA A CB    1 
ATOM   1168  N  N     . ILE A 1 142  ? 156.612 138.344 155.493 1.00 29.44  ? 142  ILE A N     1 
ATOM   1169  C  CA    . ILE A 1 142  ? 156.177 139.641 154.991 1.00 30.51  ? 142  ILE A CA    1 
ATOM   1170  C  C     . ILE A 1 142  ? 156.906 139.985 153.699 1.00 32.55  ? 142  ILE A C     1 
ATOM   1171  O  O     . ILE A 1 142  ? 156.302 140.494 152.745 1.00 35.97  ? 142  ILE A O     1 
ATOM   1172  C  CB    . ILE A 1 142  ? 156.384 140.725 156.063 1.00 32.59  ? 142  ILE A CB    1 
ATOM   1173  C  CG1   . ILE A 1 142  ? 155.524 140.434 157.291 1.00 33.96  ? 142  ILE A CG1   1 
ATOM   1174  C  CG2   . ILE A 1 142  ? 156.053 142.092 155.505 1.00 33.24  ? 142  ILE A CG2   1 
ATOM   1175  C  CD1   . ILE A 1 142  ? 155.968 141.172 158.528 1.00 35.17  ? 142  ILE A CD1   1 
ATOM   1176  N  N     . PHE A 1 143  ? 158.210 139.707 153.640 1.00 29.60  ? 143  PHE A N     1 
ATOM   1177  C  CA    . PHE A 1 143  ? 158.953 139.974 152.413 1.00 29.23  ? 143  PHE A CA    1 
ATOM   1178  C  C     . PHE A 1 143  ? 158.448 139.118 151.257 1.00 30.35  ? 143  PHE A C     1 
ATOM   1179  O  O     . PHE A 1 143  ? 158.317 139.607 150.128 1.00 33.41  ? 143  PHE A O     1 
ATOM   1180  C  CB    . PHE A 1 143  ? 160.443 139.747 152.637 1.00 28.14  ? 143  PHE A CB    1 
ATOM   1181  C  CG    . PHE A 1 143  ? 161.288 140.119 151.459 1.00 32.26  ? 143  PHE A CG    1 
ATOM   1182  C  CD1   . PHE A 1 143  ? 161.544 141.447 151.174 1.00 32.10  ? 143  PHE A CD1   1 
ATOM   1183  C  CD2   . PHE A 1 143  ? 161.822 139.146 150.632 1.00 31.08  ? 143  PHE A CD2   1 
ATOM   1184  C  CE1   . PHE A 1 143  ? 162.315 141.800 150.093 1.00 33.54  ? 143  PHE A CE1   1 
ATOM   1185  C  CE2   . PHE A 1 143  ? 162.598 139.494 149.546 1.00 30.36  ? 143  PHE A CE2   1 
ATOM   1186  C  CZ    . PHE A 1 143  ? 162.844 140.824 149.277 1.00 33.12  ? 143  PHE A CZ    1 
ATOM   1187  N  N     . GLY A 1 144  ? 158.148 137.846 151.517 1.00 27.53  ? 144  GLY A N     1 
ATOM   1188  C  CA    . GLY A 1 144  ? 157.614 137.000 150.464 1.00 26.46  ? 144  GLY A CA    1 
ATOM   1189  C  C     . GLY A 1 144  ? 156.268 137.482 149.956 1.00 31.98  ? 144  GLY A C     1 
ATOM   1190  O  O     . GLY A 1 144  ? 155.996 137.443 148.751 1.00 38.13  ? 144  GLY A O     1 
ATOM   1191  N  N     . LEU A 1 145  ? 155.414 137.959 150.863 1.00 29.47  ? 145  LEU A N     1 
ATOM   1192  C  CA    . LEU A 1 145  ? 154.116 138.481 150.446 1.00 27.57  ? 145  LEU A CA    1 
ATOM   1193  C  C     . LEU A 1 145  ? 154.272 139.752 149.612 1.00 30.67  ? 145  LEU A C     1 
ATOM   1194  O  O     . LEU A 1 145  ? 153.570 139.933 148.605 1.00 34.52  ? 145  LEU A O     1 
ATOM   1195  C  CB    . LEU A 1 145  ? 153.244 138.727 151.675 1.00 28.53  ? 145  LEU A CB    1 
ATOM   1196  C  CG    . LEU A 1 145  ? 152.682 137.458 152.326 1.00 28.43  ? 145  LEU A CG    1 
ATOM   1197  C  CD1   . LEU A 1 145  ? 152.108 137.752 153.703 1.00 29.80  ? 145  LEU A CD1   1 
ATOM   1198  C  CD2   . LEU A 1 145  ? 151.644 136.806 151.435 1.00 27.09  ? 145  LEU A CD2   1 
ATOM   1199  N  N     . HIS A 1 146  ? 155.202 140.635 150.002 1.00 30.89  ? 146  HIS A N     1 
ATOM   1200  C  CA    . HIS A 1 146  ? 155.487 141.817 149.187 1.00 31.55  ? 146  HIS A CA    1 
ATOM   1201  C  C     . HIS A 1 146  ? 155.964 141.430 147.795 1.00 31.30  ? 146  HIS A C     1 
ATOM   1202  O  O     . HIS A 1 146  ? 155.555 142.036 146.794 1.00 34.59  ? 146  HIS A O     1 
ATOM   1203  C  CB    . HIS A 1 146  ? 156.540 142.702 149.859 1.00 31.56  ? 146  HIS A CB    1 
ATOM   1204  C  CG    . HIS A 1 146  ? 156.048 143.440 151.063 1.00 37.31  ? 146  HIS A CG    1 
ATOM   1205  N  ND1   . HIS A 1 146  ? 154.717 143.722 151.273 1.00 42.32  ? 146  HIS A ND1   1 
ATOM   1206  C  CD2   . HIS A 1 146  ? 156.718 143.996 152.100 1.00 36.57  ? 146  HIS A CD2   1 
ATOM   1207  C  CE1   . HIS A 1 146  ? 154.585 144.398 152.400 1.00 43.47  ? 146  HIS A CE1   1 
ATOM   1208  N  NE2   . HIS A 1 146  ? 155.784 144.579 152.920 1.00 40.27  ? 146  HIS A NE2   1 
ATOM   1209  N  N     . HIS A 1 147  ? 156.837 140.426 147.714 1.00 29.15  ? 147  HIS A N     1 
ATOM   1210  C  CA    . HIS A 1 147  ? 157.365 139.991 146.427 1.00 29.07  ? 147  HIS A CA    1 
ATOM   1211  C  C     . HIS A 1 147  ? 156.261 139.421 145.538 1.00 32.99  ? 147  HIS A C     1 
ATOM   1212  O  O     . HIS A 1 147  ? 156.204 139.728 144.335 1.00 38.60  ? 147  HIS A O     1 
ATOM   1213  C  CB    . HIS A 1 147  ? 158.474 138.971 146.685 1.00 29.84  ? 147  HIS A CB    1 
ATOM   1214  C  CG    . HIS A 1 147  ? 159.259 138.584 145.473 1.00 39.28  ? 147  HIS A CG    1 
ATOM   1215  N  ND1   . HIS A 1 147  ? 159.737 137.307 145.280 1.00 42.67  ? 147  HIS A ND1   1 
ATOM   1216  C  CD2   . HIS A 1 147  ? 159.675 139.308 144.408 1.00 43.17  ? 147  HIS A CD2   1 
ATOM   1217  C  CE1   . HIS A 1 147  ? 160.405 137.257 144.143 1.00 43.32  ? 147  HIS A CE1   1 
ATOM   1218  N  NE2   . HIS A 1 147  ? 160.381 138.457 143.592 1.00 43.48  ? 147  HIS A NE2   1 
ATOM   1219  N  N     . ILE A 1 148  ? 155.345 138.642 146.121 1.00 29.93  ? 148  ILE A N     1 
ATOM   1220  C  CA    . ILE A 1 148  ? 154.220 138.107 145.357 1.00 29.07  ? 148  ILE A CA    1 
ATOM   1221  C  C     . ILE A 1 148  ? 153.353 139.239 144.815 1.00 29.64  ? 148  ILE A C     1 
ATOM   1222  O  O     . ILE A 1 148  ? 152.944 139.229 143.644 1.00 32.94  ? 148  ILE A O     1 
ATOM   1223  C  CB    . ILE A 1 148  ? 153.391 137.142 146.222 1.00 34.26  ? 148  ILE A CB    1 
ATOM   1224  C  CG1   . ILE A 1 148  ? 154.135 135.833 146.466 1.00 38.49  ? 148  ILE A CG1   1 
ATOM   1225  C  CG2   . ILE A 1 148  ? 152.053 136.854 145.569 1.00 32.01  ? 148  ILE A CG2   1 
ATOM   1226  C  CD1   . ILE A 1 148  ? 153.575 135.050 147.631 1.00 37.04  ? 148  ILE A CD1   1 
ATOM   1227  N  N     . GLY A 1 149  ? 153.047 140.227 145.660 1.00 29.74  ? 149  GLY A N     1 
ATOM   1228  C  CA    . GLY A 1 149  ? 152.213 141.330 145.206 1.00 32.08  ? 149  GLY A CA    1 
ATOM   1229  C  C     . GLY A 1 149  ? 152.853 142.145 144.101 1.00 33.31  ? 149  GLY A C     1 
ATOM   1230  O  O     . GLY A 1 149  ? 152.177 142.552 143.147 1.00 34.88  ? 149  GLY A O     1 
ATOM   1231  N  N     . MET A 1 150  ? 154.164 142.374 144.198 1.00 31.53  ? 150  MET A N     1 
ATOM   1232  C  CA    . MET A 1 150  ? 154.863 143.095 143.141 1.00 30.79  ? 150  MET A CA    1 
ATOM   1233  C  C     . MET A 1 150  ? 154.799 142.336 141.821 1.00 29.33  ? 150  MET A C     1 
ATOM   1234  O  O     . MET A 1 150  ? 154.556 142.934 140.762 1.00 28.01  ? 150  MET A O     1 
ATOM   1235  C  CB    . MET A 1 150  ? 156.310 143.347 143.563 1.00 32.07  ? 150  MET A CB    1 
ATOM   1236  C  CG    . MET A 1 150  ? 157.190 143.947 142.488 1.00 37.43  ? 150  MET A CG    1 
ATOM   1237  S  SD    . MET A 1 150  ? 158.913 144.048 143.002 1.00 46.18  ? 150  MET A SD    1 
ATOM   1238  C  CE    . MET A 1 150  ? 159.499 142.425 142.533 1.00 40.33  ? 150  MET A CE    1 
ATOM   1239  N  N     . GLN A 1 151  ? 154.995 141.014 141.867 1.00 30.21  ? 151  GLN A N     1 
ATOM   1240  C  CA    . GLN A 1 151  ? 154.905 140.220 140.643 1.00 27.25  ? 151  GLN A CA    1 
ATOM   1241  C  C     . GLN A 1 151  ? 153.512 140.305 140.028 1.00 27.65  ? 151  GLN A C     1 
ATOM   1242  O  O     . GLN A 1 151  ? 153.368 140.445 138.802 1.00 30.87  ? 151  GLN A O     1 
ATOM   1243  C  CB    . GLN A 1 151  ? 155.271 138.768 140.937 1.00 28.37  ? 151  GLN A CB    1 
ATOM   1244  C  CG    . GLN A 1 151  ? 156.748 138.536 141.135 1.00 31.32  ? 151  GLN A CG    1 
ATOM   1245  C  CD    . GLN A 1 151  ? 157.067 137.101 141.480 1.00 36.10  ? 151  GLN A CD    1 
ATOM   1246  O  OE1   . GLN A 1 151  ? 156.210 136.223 141.404 1.00 34.56  ? 151  GLN A OE1   1 
ATOM   1247  N  NE2   . GLN A 1 151  ? 158.308 136.853 141.869 1.00 42.17  ? 151  GLN A NE2   1 
ATOM   1248  N  N     . MET A 1 152  ? 152.475 140.223 140.867 1.00 28.98  ? 152  MET A N     1 
ATOM   1249  C  CA    . MET A 1 152  ? 151.103 140.302 140.370 1.00 27.64  ? 152  MET A CA    1 
ATOM   1250  C  C     . MET A 1 152  ? 150.843 141.636 139.681 1.00 30.37  ? 152  MET A C     1 
ATOM   1251  O  O     . MET A 1 152  ? 150.234 141.685 138.600 1.00 31.88  ? 152  MET A O     1 
ATOM   1252  C  CB    . MET A 1 152  ? 150.123 140.096 141.525 1.00 31.22  ? 152  MET A CB    1 
ATOM   1253  C  CG    . MET A 1 152  ? 150.085 138.671 142.036 1.00 36.29  ? 152  MET A CG    1 
ATOM   1254  S  SD    . MET A 1 152  ? 148.713 138.246 143.129 1.00 45.20  ? 152  MET A SD    1 
ATOM   1255  C  CE    . MET A 1 152  ? 147.818 139.787 143.194 1.00 32.21  ? 152  MET A CE    1 
ATOM   1256  N  N     . ARG A 1 153  ? 151.307 142.731 140.291 1.00 29.53  ? 153  ARG A N     1 
ATOM   1257  C  CA    . ARG A 1 153  ? 151.098 144.050 139.700 1.00 27.77  ? 153  ARG A CA    1 
ATOM   1258  C  C     . ARG A 1 153  ? 151.805 144.172 138.355 1.00 27.83  ? 153  ARG A C     1 
ATOM   1259  O  O     . ARG A 1 153  ? 151.243 144.726 137.400 1.00 31.26  ? 153  ARG A O     1 
ATOM   1260  C  CB    . ARG A 1 153  ? 151.567 145.137 140.666 1.00 32.25  ? 153  ARG A CB    1 
ATOM   1261  C  CG    . ARG A 1 153  ? 151.071 146.529 140.322 1.00 33.79  ? 153  ARG A CG    1 
ATOM   1262  C  CD    . ARG A 1 153  ? 152.114 147.597 140.604 1.00 35.87  ? 153  ARG A CD    1 
ATOM   1263  N  NE    . ARG A 1 153  ? 153.304 147.466 139.773 1.00 35.00  ? 153  ARG A NE    1 
ATOM   1264  C  CZ    . ARG A 1 153  ? 154.528 147.278 140.243 1.00 36.41  ? 153  ARG A CZ    1 
ATOM   1265  N  NH1   . ARG A 1 153  ? 154.765 147.189 141.540 1.00 36.97  ? 153  ARG A NH1   1 
ATOM   1266  N  NH2   . ARG A 1 153  ? 155.540 147.175 139.388 1.00 32.53  ? 153  ARG A NH2   1 
ATOM   1267  N  N     . ILE A 1 154  ? 153.032 143.648 138.254 1.00 27.17  ? 154  ILE A N     1 
ATOM   1268  C  CA    . ILE A 1 154  ? 153.752 143.713 136.982 1.00 27.80  ? 154  ILE A CA    1 
ATOM   1269  C  C     . ILE A 1 154  ? 153.000 142.954 135.892 1.00 29.71  ? 154  ILE A C     1 
ATOM   1270  O  O     . ILE A 1 154  ? 152.843 143.445 134.761 1.00 30.06  ? 154  ILE A O     1 
ATOM   1271  C  CB    . ILE A 1 154  ? 155.186 143.181 137.150 1.00 26.73  ? 154  ILE A CB    1 
ATOM   1272  C  CG1   . ILE A 1 154  ? 156.010 144.122 138.027 1.00 30.10  ? 154  ILE A CG1   1 
ATOM   1273  C  CG2   . ILE A 1 154  ? 155.849 143.014 135.800 1.00 26.46  ? 154  ILE A CG2   1 
ATOM   1274  C  CD1   . ILE A 1 154  ? 157.232 143.474 138.634 1.00 31.16  ? 154  ILE A CD1   1 
ATOM   1275  N  N     . ALA A 1 155  ? 152.516 141.749 136.213 1.00 28.45  ? 155  ALA A N     1 
ATOM   1276  C  CA    . ALA A 1 155  ? 151.800 140.963 135.211 1.00 25.36  ? 155  ALA A CA    1 
ATOM   1277  C  C     . ALA A 1 155  ? 150.535 141.676 134.740 1.00 29.28  ? 155  ALA A C     1 
ATOM   1278  O  O     . ALA A 1 155  ? 150.236 141.708 133.534 1.00 29.38  ? 155  ALA A O     1 
ATOM   1279  C  CB    . ALA A 1 155  ? 151.460 139.583 135.771 1.00 22.47  ? 155  ALA A CB    1 
ATOM   1280  N  N     . MET A 1 156  ? 149.780 142.262 135.675 1.00 31.45  ? 156  MET A N     1 
ATOM   1281  C  CA    . MET A 1 156  ? 148.555 142.949 135.272 1.00 27.82  ? 156  MET A CA    1 
ATOM   1282  C  C     . MET A 1 156  ? 148.854 144.177 134.419 1.00 27.81  ? 156  MET A C     1 
ATOM   1283  O  O     . MET A 1 156  ? 148.121 144.465 133.463 1.00 30.70  ? 156  MET A O     1 
ATOM   1284  C  CB    . MET A 1 156  ? 147.717 143.321 136.495 1.00 29.15  ? 156  MET A CB    1 
ATOM   1285  C  CG    . MET A 1 156  ? 146.977 142.135 137.104 1.00 33.43  ? 156  MET A CG    1 
ATOM   1286  S  SD    . MET A 1 156  ? 145.971 142.547 138.541 1.00 58.77  ? 156  MET A SD    1 
ATOM   1287  C  CE    . MET A 1 156  ? 147.150 143.428 139.552 1.00 32.37  ? 156  MET A CE    1 
ATOM   1288  N  N     . PHE A 1 157  ? 149.924 144.911 134.738 1.00 28.27  ? 157  PHE A N     1 
ATOM   1289  C  CA    . PHE A 1 157  ? 150.289 146.062 133.915 1.00 26.79  ? 157  PHE A CA    1 
ATOM   1290  C  C     . PHE A 1 157  ? 150.635 145.639 132.492 1.00 27.65  ? 157  PHE A C     1 
ATOM   1291  O  O     . PHE A 1 157  ? 150.232 146.299 131.521 1.00 27.05  ? 157  PHE A O     1 
ATOM   1292  C  CB    . PHE A 1 157  ? 151.462 146.810 134.547 1.00 27.60  ? 157  PHE A CB    1 
ATOM   1293  C  CG    . PHE A 1 157  ? 151.062 147.778 135.621 1.00 34.04  ? 157  PHE A CG    1 
ATOM   1294  C  CD1   . PHE A 1 157  ? 149.926 147.565 136.383 1.00 32.69  ? 157  PHE A CD1   1 
ATOM   1295  C  CD2   . PHE A 1 157  ? 151.843 148.885 135.890 1.00 36.43  ? 157  PHE A CD2   1 
ATOM   1296  C  CE1   . PHE A 1 157  ? 149.565 148.453 137.370 1.00 32.59  ? 157  PHE A CE1   1 
ATOM   1297  C  CE2   . PHE A 1 157  ? 151.489 149.773 136.881 1.00 39.19  ? 157  PHE A CE2   1 
ATOM   1298  C  CZ    . PHE A 1 157  ? 150.349 149.556 137.622 1.00 38.91  ? 157  PHE A CZ    1 
ATOM   1299  N  N     . SER A 1 158  ? 151.372 144.533 132.348 1.00 28.79  ? 158  SER A N     1 
ATOM   1300  C  CA    . SER A 1 158  ? 151.707 144.053 131.010 1.00 27.31  ? 158  SER A CA    1 
ATOM   1301  C  C     . SER A 1 158  ? 150.454 143.684 130.226 1.00 28.47  ? 158  SER A C     1 
ATOM   1302  O  O     . SER A 1 158  ? 150.336 144.011 129.036 1.00 28.37  ? 158  SER A O     1 
ATOM   1303  C  CB    . SER A 1 158  ? 152.650 142.855 131.094 1.00 30.33  ? 158  SER A CB    1 
ATOM   1304  O  OG    . SER A 1 158  ? 153.921 143.249 131.569 1.00 39.21  ? 158  SER A OG    1 
ATOM   1305  N  N     . LEU A 1 159  ? 149.499 143.014 130.879 1.00 29.93  ? 159  LEU A N     1 
ATOM   1306  C  CA    . LEU A 1 159  ? 148.267 142.651 130.179 1.00 28.30  ? 159  LEU A CA    1 
ATOM   1307  C  C     . LEU A 1 159  ? 147.467 143.885 129.766 1.00 26.16  ? 159  LEU A C     1 
ATOM   1308  O  O     . LEU A 1 159  ? 146.914 143.928 128.659 1.00 25.78  ? 159  LEU A O     1 
ATOM   1309  C  CB    . LEU A 1 159  ? 147.422 141.716 131.041 1.00 29.89  ? 159  LEU A CB    1 
ATOM   1310  C  CG    . LEU A 1 159  ? 147.443 140.263 130.562 1.00 31.71  ? 159  LEU A CG    1 
ATOM   1311  C  CD1   . LEU A 1 159  ? 148.830 139.675 130.707 1.00 31.96  ? 159  LEU A CD1   1 
ATOM   1312  C  CD2   . LEU A 1 159  ? 146.422 139.422 131.306 1.00 29.37  ? 159  LEU A CD2   1 
ATOM   1313  N  N     . ILE A 1 160  ? 147.403 144.900 130.632 1.00 27.23  ? 160  ILE A N     1 
ATOM   1314  C  CA    . ILE A 1 160  ? 146.681 146.124 130.282 1.00 26.48  ? 160  ILE A CA    1 
ATOM   1315  C  C     . ILE A 1 160  ? 147.309 146.792 129.064 1.00 27.56  ? 160  ILE A C     1 
ATOM   1316  O  O     . ILE A 1 160  ? 146.603 147.216 128.137 1.00 28.19  ? 160  ILE A O     1 
ATOM   1317  C  CB    . ILE A 1 160  ? 146.626 147.090 131.482 1.00 25.76  ? 160  ILE A CB    1 
ATOM   1318  C  CG1   . ILE A 1 160  ? 145.681 146.571 132.563 1.00 24.69  ? 160  ILE A CG1   1 
ATOM   1319  C  CG2   . ILE A 1 160  ? 146.190 148.468 131.040 1.00 25.16  ? 160  ILE A CG2   1 
ATOM   1320  C  CD1   . ILE A 1 160  ? 145.910 147.207 133.911 1.00 26.18  ? 160  ILE A CD1   1 
ATOM   1321  N  N     . TYR A 1 161  ? 148.642 146.898 129.038 1.00 27.12  ? 161  TYR A N     1 
ATOM   1322  C  CA    . TYR A 1 161  ? 149.269 147.533 127.882 1.00 25.79  ? 161  TYR A CA    1 
ATOM   1323  C  C     . TYR A 1 161  ? 149.030 146.733 126.610 1.00 26.94  ? 161  TYR A C     1 
ATOM   1324  O  O     . TYR A 1 161  ? 148.768 147.314 125.551 1.00 26.76  ? 161  TYR A O     1 
ATOM   1325  C  CB    . TYR A 1 161  ? 150.768 147.727 128.091 1.00 28.99  ? 161  TYR A CB    1 
ATOM   1326  C  CG    . TYR A 1 161  ? 151.410 148.469 126.934 1.00 29.78  ? 161  TYR A CG    1 
ATOM   1327  C  CD1   . TYR A 1 161  ? 151.310 149.847 126.829 1.00 27.17  ? 161  TYR A CD1   1 
ATOM   1328  C  CD2   . TYR A 1 161  ? 152.084 147.786 125.932 1.00 28.01  ? 161  TYR A CD2   1 
ATOM   1329  C  CE1   . TYR A 1 161  ? 151.880 150.522 125.775 1.00 26.11  ? 161  TYR A CE1   1 
ATOM   1330  C  CE2   . TYR A 1 161  ? 152.654 148.455 124.874 1.00 28.08  ? 161  TYR A CE2   1 
ATOM   1331  C  CZ    . TYR A 1 161  ? 152.548 149.822 124.799 1.00 29.63  ? 161  TYR A CZ    1 
ATOM   1332  O  OH    . TYR A 1 161  ? 153.119 150.496 123.748 1.00 33.50  ? 161  TYR A OH    1 
ATOM   1333  N  N     . LYS A 1 162  ? 149.126 145.403 126.682 1.00 29.56  ? 162  LYS A N     1 
ATOM   1334  C  CA    . LYS A 1 162  ? 148.888 144.609 125.481 1.00 27.52  ? 162  LYS A CA    1 
ATOM   1335  C  C     . LYS A 1 162  ? 147.445 144.726 125.006 1.00 26.35  ? 162  LYS A C     1 
ATOM   1336  O  O     . LYS A 1 162  ? 147.176 144.594 123.808 1.00 27.34  ? 162  LYS A O     1 
ATOM   1337  C  CB    . LYS A 1 162  ? 149.260 143.150 125.729 1.00 31.32  ? 162  LYS A CB    1 
ATOM   1338  C  CG    . LYS A 1 162  ? 150.756 142.916 125.741 1.00 34.11  ? 162  LYS A CG    1 
ATOM   1339  C  CD    . LYS A 1 162  ? 151.100 141.467 126.005 1.00 39.80  ? 162  LYS A CD    1 
ATOM   1340  C  CE    . LYS A 1 162  ? 152.588 141.227 125.834 1.00 48.13  ? 162  LYS A CE    1 
ATOM   1341  N  NZ    . LYS A 1 162  ? 152.941 139.805 126.078 1.00 44.65  ? 162  LYS A NZ    1 
ATOM   1342  N  N     . LYS A 1 163  ? 146.507 144.976 125.919 1.00 29.11  ? 163  LYS A N     1 
ATOM   1343  C  CA    . LYS A 1 163  ? 145.131 145.226 125.496 1.00 28.40  ? 163  LYS A CA    1 
ATOM   1344  C  C     . LYS A 1 163  ? 144.976 146.599 124.853 1.00 29.05  ? 163  LYS A C     1 
ATOM   1345  O  O     . LYS A 1 163  ? 144.164 146.770 123.937 1.00 29.53  ? 163  LYS A O     1 
ATOM   1346  C  CB    . LYS A 1 163  ? 144.175 145.083 126.677 1.00 31.80  ? 163  LYS A CB    1 
ATOM   1347  C  CG    . LYS A 1 163  ? 142.724 145.340 126.315 1.00 30.97  ? 163  LYS A CG    1 
ATOM   1348  C  CD    . LYS A 1 163  ? 142.139 144.222 125.486 1.00 27.08  ? 163  LYS A CD    1 
ATOM   1349  C  CE    . LYS A 1 163  ? 140.788 144.624 124.931 1.00 30.37  ? 163  LYS A CE    1 
ATOM   1350  N  NZ    . LYS A 1 163  ? 140.066 143.466 124.347 1.00 33.17  ? 163  LYS A NZ    1 
ATOM   1351  N  N     . THR A 1 164  ? 145.735 147.591 125.323 1.00 29.24  ? 164  THR A N     1 
ATOM   1352  C  CA    . THR A 1 164  ? 145.551 148.957 124.833 1.00 30.39  ? 164  THR A CA    1 
ATOM   1353  C  C     . THR A 1 164  ? 145.770 149.061 123.326 1.00 32.38  ? 164  THR A C     1 
ATOM   1354  O  O     . THR A 1 164  ? 145.043 149.784 122.636 1.00 31.58  ? 164  THR A O     1 
ATOM   1355  C  CB    . THR A 1 164  ? 146.486 149.909 125.577 1.00 31.68  ? 164  THR A CB    1 
ATOM   1356  O  OG1   . THR A 1 164  ? 146.104 149.971 126.955 1.00 38.06  ? 164  THR A OG1   1 
ATOM   1357  C  CG2   . THR A 1 164  ? 146.422 151.295 124.983 1.00 26.83  ? 164  THR A CG2   1 
ATOM   1358  N  N     . LEU A 1 165  ? 146.759 148.342 122.792 1.00 30.51  ? 165  LEU A N     1 
ATOM   1359  C  CA    . LEU A 1 165  ? 147.072 148.437 121.371 1.00 26.55  ? 165  LEU A CA    1 
ATOM   1360  C  C     . LEU A 1 165  ? 146.025 147.788 120.476 1.00 29.92  ? 165  LEU A C     1 
ATOM   1361  O  O     . LEU A 1 165  ? 146.107 147.940 119.253 1.00 29.84  ? 165  LEU A O     1 
ATOM   1362  C  CB    . LEU A 1 165  ? 148.439 147.818 121.086 1.00 25.59  ? 165  LEU A CB    1 
ATOM   1363  C  CG    . LEU A 1 165  ? 149.653 148.503 121.712 1.00 29.73  ? 165  LEU A CG    1 
ATOM   1364  C  CD1   . LEU A 1 165  ? 150.935 147.815 121.289 1.00 27.27  ? 165  LEU A CD1   1 
ATOM   1365  C  CD2   . LEU A 1 165  ? 149.690 149.970 121.334 1.00 30.87  ? 165  LEU A CD2   1 
ATOM   1366  N  N     . LYS A 1 166  ? 145.059 147.067 121.041 1.00 33.77  ? 166  LYS A N     1 
ATOM   1367  C  CA    . LYS A 1 166  ? 144.046 146.368 120.264 1.00 30.57  ? 166  LYS A CA    1 
ATOM   1368  C  C     . LYS A 1 166  ? 142.689 147.054 120.279 1.00 32.10  ? 166  LYS A C     1 
ATOM   1369  O  O     . LYS A 1 166  ? 141.778 146.592 119.588 1.00 35.63  ? 166  LYS A O     1 
ATOM   1370  C  CB    . LYS A 1 166  ? 143.881 144.935 120.781 1.00 32.51  ? 166  LYS A CB    1 
ATOM   1371  C  CG    . LYS A 1 166  ? 145.062 144.034 120.502 1.00 35.04  ? 166  LYS A CG    1 
ATOM   1372  C  CD    . LYS A 1 166  ? 144.803 142.629 121.005 1.00 36.73  ? 166  LYS A CD    1 
ATOM   1373  C  CE    . LYS A 1 166  ? 145.865 141.670 120.510 1.00 43.31  ? 166  LYS A CE    1 
ATOM   1374  N  NZ    . LYS A 1 166  ? 147.203 141.982 121.080 1.00 42.75  ? 166  LYS A NZ    1 
ATOM   1375  N  N     . LEU A 1 167  ? 142.529 148.127 121.050 1.00 35.19  ? 167  LEU A N     1 
ATOM   1376  C  CA    . LEU A 1 167  ? 141.221 148.747 121.223 1.00 36.52  ? 167  LEU A CA    1 
ATOM   1377  C  C     . LEU A 1 167  ? 140.679 149.291 119.908 1.00 41.20  ? 167  LEU A C     1 
ATOM   1378  O  O     . LEU A 1 167  ? 141.415 149.877 119.111 1.00 41.20  ? 167  LEU A O     1 
ATOM   1379  C  CB    . LEU A 1 167  ? 141.303 149.862 122.263 1.00 35.62  ? 167  LEU A CB    1 
ATOM   1380  C  CG    . LEU A 1 167  ? 141.509 149.398 123.703 1.00 33.31  ? 167  LEU A CG    1 
ATOM   1381  C  CD1   . LEU A 1 167  ? 141.679 150.586 124.629 1.00 34.53  ? 167  LEU A CD1   1 
ATOM   1382  C  CD2   . LEU A 1 167  ? 140.344 148.538 124.145 1.00 29.51  ? 167  LEU A CD2   1 
ATOM   1383  N  N     . SER A 1 168  ? 139.383 149.086 119.689 1.00 39.83  ? 168  SER A N     1 
ATOM   1384  C  CA    . SER A 1 168  ? 138.727 149.553 118.476 1.00 40.16  ? 168  SER A CA    1 
ATOM   1385  C  C     . SER A 1 168  ? 138.722 151.074 118.411 1.00 43.74  ? 168  SER A C     1 
ATOM   1386  O  O     . SER A 1 168  ? 138.889 151.765 119.418 1.00 47.56  ? 168  SER A O     1 
ATOM   1387  C  CB    . SER A 1 168  ? 137.295 149.026 118.411 1.00 44.07  ? 168  SER A CB    1 
ATOM   1388  O  OG    . SER A 1 168  ? 136.718 149.275 117.145 1.00 49.87  ? 168  SER A OG    1 
ATOM   1389  N  N     . SER A 1 169  ? 138.545 151.597 117.197 1.00 48.40  ? 169  SER A N     1 
ATOM   1390  C  CA    . SER A 1 169  ? 138.483 153.040 117.006 1.00 48.57  ? 169  SER A CA    1 
ATOM   1391  C  C     . SER A 1 169  ? 137.206 153.650 117.569 1.00 51.86  ? 169  SER A C     1 
ATOM   1392  O  O     . SER A 1 169  ? 137.196 154.840 117.896 1.00 54.96  ? 169  SER A O     1 
ATOM   1393  C  CB    . SER A 1 169  ? 138.605 153.372 115.520 1.00 45.92  ? 169  SER A CB    1 
ATOM   1394  O  OG    . SER A 1 169  ? 138.777 154.763 115.324 1.00 47.88  ? 169  SER A OG    1 
ATOM   1395  N  N     . ARG A 1 170  ? 136.132 152.867 117.688 1.00 54.14  ? 170  ARG A N     1 
ATOM   1396  C  CA    . ARG A 1 170  ? 134.883 153.399 118.219 1.00 55.03  ? 170  ARG A CA    1 
ATOM   1397  C  C     . ARG A 1 170  ? 134.896 153.505 119.736 1.00 56.76  ? 170  ARG A C     1 
ATOM   1398  O  O     . ARG A 1 170  ? 134.270 154.412 120.294 1.00 62.25  ? 170  ARG A O     1 
ATOM   1399  C  CB    . ARG A 1 170  ? 133.707 152.536 117.765 1.00 55.03  ? 170  ARG A CB    1 
ATOM   1400  C  CG    . ARG A 1 170  ? 133.521 152.506 116.264 1.00 59.64  ? 170  ARG A CG    1 
ATOM   1401  C  CD    . ARG A 1 170  ? 132.101 152.093 115.893 1.00 63.37  ? 170  ARG A CD    1 
ATOM   1402  N  NE    . ARG A 1 170  ? 131.792 152.209 114.469 1.00 73.91  ? 170  ARG A NE    1 
ATOM   1403  C  CZ    . ARG A 1 170  ? 132.014 153.275 113.707 1.00 67.11  ? 170  ARG A CZ    1 
ATOM   1404  N  NH1   . ARG A 1 170  ? 132.478 154.409 114.207 1.00 66.33  ? 170  ARG A NH1   1 
ATOM   1405  N  NH2   . ARG A 1 170  ? 131.732 153.210 112.409 1.00 60.25  ? 170  ARG A NH2   1 
ATOM   1406  N  N     . VAL A 1 171  ? 135.595 152.600 120.418 1.00 56.18  ? 171  VAL A N     1 
ATOM   1407  C  CA    . VAL A 1 171  ? 135.660 152.644 121.873 1.00 57.56  ? 171  VAL A CA    1 
ATOM   1408  C  C     . VAL A 1 171  ? 136.763 153.574 122.369 1.00 59.81  ? 171  VAL A C     1 
ATOM   1409  O  O     . VAL A 1 171  ? 136.769 153.939 123.553 1.00 63.15  ? 171  VAL A O     1 
ATOM   1410  C  CB    . VAL A 1 171  ? 135.846 151.223 122.440 1.00 48.35  ? 171  VAL A CB    1 
ATOM   1411  C  CG1   . VAL A 1 171  ? 137.279 150.754 122.269 1.00 44.47  ? 171  VAL A CG1   1 
ATOM   1412  C  CG2   . VAL A 1 171  ? 135.413 151.155 123.893 1.00 53.93  ? 171  VAL A CG2   1 
ATOM   1413  N  N     . LEU A 1 172  ? 137.688 153.978 121.496 1.00 57.08  ? 172  LEU A N     1 
ATOM   1414  C  CA    . LEU A 1 172  ? 138.798 154.825 121.919 1.00 59.83  ? 172  LEU A CA    1 
ATOM   1415  C  C     . LEU A 1 172  ? 138.346 156.237 122.272 1.00 63.82  ? 172  LEU A C     1 
ATOM   1416  O  O     . LEU A 1 172  ? 138.984 156.897 123.099 1.00 64.51  ? 172  LEU A O     1 
ATOM   1417  C  CB    . LEU A 1 172  ? 139.864 154.868 120.829 1.00 59.08  ? 172  LEU A CB    1 
ATOM   1418  C  CG    . LEU A 1 172  ? 140.941 153.791 120.938 1.00 54.38  ? 172  LEU A CG    1 
ATOM   1419  C  CD1   . LEU A 1 172  ? 141.742 153.722 119.654 1.00 50.72  ? 172  LEU A CD1   1 
ATOM   1420  C  CD2   . LEU A 1 172  ? 141.844 154.063 122.126 1.00 52.74  ? 172  LEU A CD2   1 
ATOM   1421  N  N     . ASP A 1 173  ? 137.263 156.722 121.660 1.00 64.93  ? 173  ASP A N     1 
ATOM   1422  C  CA    . ASP A 1 173  ? 136.795 158.075 121.940 1.00 68.20  ? 173  ASP A CA    1 
ATOM   1423  C  C     . ASP A 1 173  ? 136.356 158.248 123.387 1.00 68.27  ? 173  ASP A C     1 
ATOM   1424  O  O     . ASP A 1 173  ? 136.337 159.377 123.887 1.00 70.75  ? 173  ASP A O     1 
ATOM   1425  C  CB    . ASP A 1 173  ? 135.636 158.437 121.012 1.00 70.83  ? 173  ASP A CB    1 
ATOM   1426  C  CG    . ASP A 1 173  ? 135.977 158.248 119.553 1.00 75.91  ? 173  ASP A CG    1 
ATOM   1427  O  OD1   . ASP A 1 173  ? 137.062 157.701 119.262 1.00 75.43  ? 173  ASP A OD1   1 
ATOM   1428  O  OD2   . ASP A 1 173  ? 135.166 158.653 118.696 1.00 74.82  ? 173  ASP A OD2   1 
ATOM   1429  N  N     . LYS A 1 174  ? 136.005 157.158 124.061 1.00 67.75  ? 174  LYS A N     1 
ATOM   1430  C  CA    . LYS A 1 174  ? 135.511 157.185 125.429 1.00 67.78  ? 174  LYS A CA    1 
ATOM   1431  C  C     . LYS A 1 174  ? 136.610 157.022 126.469 1.00 63.52  ? 174  LYS A C     1 
ATOM   1432  O  O     . LYS A 1 174  ? 136.323 157.110 127.667 1.00 65.33  ? 174  LYS A O     1 
ATOM   1433  C  CB    . LYS A 1 174  ? 134.469 156.080 125.611 1.00 69.82  ? 174  LYS A CB    1 
ATOM   1434  C  CG    . LYS A 1 174  ? 133.227 156.268 124.763 1.00 72.91  ? 174  LYS A CG    1 
ATOM   1435  C  CD    . LYS A 1 174  ? 132.678 154.927 124.305 1.00 81.74  ? 174  LYS A CD    1 
ATOM   1436  C  CE    . LYS A 1 174  ? 132.348 154.020 125.475 1.00 87.39  ? 174  LYS A CE    1 
ATOM   1437  N  NZ    . LYS A 1 174  ? 131.814 152.710 125.005 1.00 84.43  ? 174  LYS A NZ    1 
ATOM   1438  N  N     . ILE A 1 175  ? 137.847 156.779 126.047 1.00 59.32  ? 175  ILE A N     1 
ATOM   1439  C  CA    . ILE A 1 175  ? 138.964 156.521 126.950 1.00 60.54  ? 175  ILE A CA    1 
ATOM   1440  C  C     . ILE A 1 175  ? 139.992 157.628 126.765 1.00 60.33  ? 175  ILE A C     1 
ATOM   1441  O  O     . ILE A 1 175  ? 140.514 157.821 125.661 1.00 62.36  ? 175  ILE A O     1 
ATOM   1442  C  CB    . ILE A 1 175  ? 139.592 155.144 126.690 1.00 59.83  ? 175  ILE A CB    1 
ATOM   1443  C  CG1   . ILE A 1 175  ? 138.540 154.044 126.833 1.00 56.82  ? 175  ILE A CG1   1 
ATOM   1444  C  CG2   . ILE A 1 175  ? 140.751 154.899 127.639 1.00 54.87  ? 175  ILE A CG2   1 
ATOM   1445  C  CD1   . ILE A 1 175  ? 138.971 152.720 126.254 1.00 50.68  ? 175  ILE A CD1   1 
ATOM   1446  N  N     . SER A 1 176  ? 140.285 158.348 127.841 1.00 57.24  ? 176  SER A N     1 
ATOM   1447  C  CA    . SER A 1 176  ? 141.256 159.431 127.814 1.00 55.72  ? 176  SER A CA    1 
ATOM   1448  C  C     . SER A 1 176  ? 142.580 158.984 128.425 1.00 50.43  ? 176  SER A C     1 
ATOM   1449  O  O     . SER A 1 176  ? 142.697 157.904 129.009 1.00 52.05  ? 176  SER A O     1 
ATOM   1450  C  CB    . SER A 1 176  ? 140.711 160.660 128.552 1.00 57.85  ? 176  SER A CB    1 
ATOM   1451  O  OG    . SER A 1 176  ? 140.702 160.465 129.956 1.00 54.76  ? 176  SER A OG    1 
ATOM   1452  N  N     . ILE A 1 177  ? 143.595 159.838 128.271 1.00 45.36  ? 177  ILE A N     1 
ATOM   1453  C  CA    . ILE A 1 177  ? 144.890 159.573 128.890 1.00 46.98  ? 177  ILE A CA    1 
ATOM   1454  C  C     . ILE A 1 177  ? 144.780 159.622 130.407 1.00 47.54  ? 177  ILE A C     1 
ATOM   1455  O  O     . ILE A 1 177  ? 145.469 158.875 131.114 1.00 46.04  ? 177  ILE A O     1 
ATOM   1456  C  CB    . ILE A 1 177  ? 145.954 160.559 128.357 1.00 44.58  ? 177  ILE A CB    1 
ATOM   1457  C  CG1   . ILE A 1 177  ? 147.346 160.183 128.870 1.00 39.98  ? 177  ILE A CG1   1 
ATOM   1458  C  CG2   . ILE A 1 177  ? 145.616 161.992 128.729 1.00 38.97  ? 177  ILE A CG2   1 
ATOM   1459  C  CD1   . ILE A 1 177  ? 147.802 158.809 128.456 1.00 37.18  ? 177  ILE A CD1   1 
ATOM   1460  N  N     . GLY A 1 178  ? 143.908 160.487 130.933 1.00 44.73  ? 178  GLY A N     1 
ATOM   1461  C  CA    . GLY A 1 178  ? 143.761 160.597 132.372 1.00 42.79  ? 178  GLY A CA    1 
ATOM   1462  C  C     . GLY A 1 178  ? 143.190 159.350 133.009 1.00 45.60  ? 178  GLY A C     1 
ATOM   1463  O  O     . GLY A 1 178  ? 143.620 158.956 134.094 1.00 48.53  ? 178  GLY A O     1 
ATOM   1464  N  N     . GLN A 1 179  ? 142.239 158.696 132.339 1.00 41.74  ? 179  GLN A N     1 
ATOM   1465  C  CA    . GLN A 1 179  ? 141.656 157.473 132.881 1.00 45.45  ? 179  GLN A CA    1 
ATOM   1466  C  C     . GLN A 1 179  ? 142.686 156.355 132.964 1.00 45.49  ? 179  GLN A C     1 
ATOM   1467  O  O     . GLN A 1 179  ? 142.760 155.645 133.971 1.00 43.90  ? 179  GLN A O     1 
ATOM   1468  C  CB    . GLN A 1 179  ? 140.468 157.042 132.026 1.00 51.88  ? 179  GLN A CB    1 
ATOM   1469  C  CG    . GLN A 1 179  ? 139.246 157.923 132.183 1.00 56.65  ? 179  GLN A CG    1 
ATOM   1470  C  CD    . GLN A 1 179  ? 138.128 157.533 131.242 1.00 58.38  ? 179  GLN A CD    1 
ATOM   1471  O  OE1   . GLN A 1 179  ? 137.618 156.415 131.296 1.00 60.39  ? 179  GLN A OE1   1 
ATOM   1472  N  NE2   . GLN A 1 179  ? 137.732 158.460 130.378 1.00 55.29  ? 179  GLN A NE2   1 
ATOM   1473  N  N     . LEU A 1 180  ? 143.509 156.202 131.928 1.00 46.50  ? 180  LEU A N     1 
ATOM   1474  C  CA    . LEU A 1 180  ? 144.523 155.155 131.933 1.00 46.01  ? 180  LEU A CA    1 
ATOM   1475  C  C     . LEU A 1 180  ? 145.627 155.461 132.937 1.00 43.73  ? 180  LEU A C     1 
ATOM   1476  O  O     . LEU A 1 180  ? 146.103 154.564 133.649 1.00 44.80  ? 180  LEU A O     1 
ATOM   1477  C  CB    . LEU A 1 180  ? 145.101 155.001 130.529 1.00 43.32  ? 180  LEU A CB    1 
ATOM   1478  C  CG    . LEU A 1 180  ? 145.405 153.598 130.013 1.00 46.14  ? 180  LEU A CG    1 
ATOM   1479  C  CD1   . LEU A 1 180  ? 144.124 152.796 129.892 1.00 47.39  ? 180  LEU A CD1   1 
ATOM   1480  C  CD2   . LEU A 1 180  ? 146.112 153.685 128.674 1.00 43.57  ? 180  LEU A CD2   1 
ATOM   1481  N  N     . VAL A 1 181  ? 146.043 156.726 133.010 1.00 41.06  ? 181  VAL A N     1 
ATOM   1482  C  CA    . VAL A 1 181  ? 147.075 157.117 133.961 1.00 42.55  ? 181  VAL A CA    1 
ATOM   1483  C  C     . VAL A 1 181  ? 146.575 156.944 135.390 1.00 42.64  ? 181  VAL A C     1 
ATOM   1484  O  O     . VAL A 1 181  ? 147.343 156.593 136.291 1.00 45.20  ? 181  VAL A O     1 
ATOM   1485  C  CB    . VAL A 1 181  ? 147.539 158.556 133.672 1.00 41.13  ? 181  VAL A CB    1 
ATOM   1486  C  CG1   . VAL A 1 181  ? 148.262 159.146 134.864 1.00 36.89  ? 181  VAL A CG1   1 
ATOM   1487  C  CG2   . VAL A 1 181  ? 148.439 158.572 132.449 1.00 39.07  ? 181  VAL A CG2   1 
ATOM   1488  N  N     . SER A 1 182  ? 145.282 157.183 135.624 1.00 39.17  ? 182  SER A N     1 
ATOM   1489  C  CA    . SER A 1 182  ? 144.695 156.890 136.927 1.00 41.56  ? 182  SER A CA    1 
ATOM   1490  C  C     . SER A 1 182  ? 144.643 155.391 137.192 1.00 45.28  ? 182  SER A C     1 
ATOM   1491  O  O     . SER A 1 182  ? 144.886 154.947 138.319 1.00 44.56  ? 182  SER A O     1 
ATOM   1492  C  CB    . SER A 1 182  ? 143.293 157.492 137.016 1.00 42.47  ? 182  SER A CB    1 
ATOM   1493  O  OG    . SER A 1 182  ? 143.345 158.888 137.233 1.00 44.13  ? 182  SER A OG    1 
ATOM   1494  N  N     . LEU A 1 183  ? 144.310 154.596 136.173 1.00 44.96  ? 183  LEU A N     1 
ATOM   1495  C  CA    . LEU A 1 183  ? 144.246 153.149 136.347 1.00 44.86  ? 183  LEU A CA    1 
ATOM   1496  C  C     . LEU A 1 183  ? 145.604 152.565 136.710 1.00 44.32  ? 183  LEU A C     1 
ATOM   1497  O  O     . LEU A 1 183  ? 145.677 151.565 137.434 1.00 45.59  ? 183  LEU A O     1 
ATOM   1498  C  CB    . LEU A 1 183  ? 143.707 152.490 135.076 1.00 43.56  ? 183  LEU A CB    1 
ATOM   1499  C  CG    . LEU A 1 183  ? 143.548 150.968 135.074 1.00 42.46  ? 183  LEU A CG    1 
ATOM   1500  C  CD1   . LEU A 1 183  ? 142.547 150.533 136.123 1.00 40.59  ? 183  LEU A CD1   1 
ATOM   1501  C  CD2   . LEU A 1 183  ? 143.129 150.465 133.702 1.00 38.15  ? 183  LEU A CD2   1 
ATOM   1502  N  N     . LEU A 1 184  ? 146.684 153.162 136.213 1.00 44.58  ? 184  LEU A N     1 
ATOM   1503  C  CA    . LEU A 1 184  ? 148.014 152.662 136.555 1.00 42.45  ? 184  LEU A CA    1 
ATOM   1504  C  C     . LEU A 1 184  ? 148.583 153.288 137.825 1.00 41.07  ? 184  LEU A C     1 
ATOM   1505  O  O     . LEU A 1 184  ? 149.261 152.605 138.597 1.00 41.13  ? 184  LEU A O     1 
ATOM   1506  C  CB    . LEU A 1 184  ? 148.988 152.883 135.395 1.00 45.07  ? 184  LEU A CB    1 
ATOM   1507  C  CG    . LEU A 1 184  ? 149.204 151.697 134.449 1.00 44.88  ? 184  LEU A CG    1 
ATOM   1508  C  CD1   . LEU A 1 184  ? 147.943 151.341 133.684 1.00 40.30  ? 184  LEU A CD1   1 
ATOM   1509  C  CD2   . LEU A 1 184  ? 150.349 151.985 133.501 1.00 46.87  ? 184  LEU A CD2   1 
ATOM   1510  N  N     . SER A 1 185  ? 148.321 154.573 138.062 1.00 43.63  ? 185  SER A N     1 
ATOM   1511  C  CA    . SER A 1 185  ? 148.959 155.275 139.170 1.00 43.78  ? 185  SER A CA    1 
ATOM   1512  C  C     . SER A 1 185  ? 148.419 154.817 140.521 1.00 44.67  ? 185  SER A C     1 
ATOM   1513  O  O     . SER A 1 185  ? 149.159 154.784 141.510 1.00 42.60  ? 185  SER A O     1 
ATOM   1514  C  CB    . SER A 1 185  ? 148.769 156.781 139.000 1.00 39.04  ? 185  SER A CB    1 
ATOM   1515  O  OG    . SER A 1 185  ? 149.491 157.497 139.981 1.00 43.31  ? 185  SER A OG    1 
ATOM   1516  N  N     . ASN A 1 186  ? 147.130 154.479 140.589 1.00 47.12  ? 186  ASN A N     1 
ATOM   1517  C  CA    . ASN A 1 186  ? 146.520 154.140 141.872 1.00 46.84  ? 186  ASN A CA    1 
ATOM   1518  C  C     . ASN A 1 186  ? 147.067 152.832 142.432 1.00 48.57  ? 186  ASN A C     1 
ATOM   1519  O  O     . ASN A 1 186  ? 147.284 152.714 143.643 1.00 50.90  ? 186  ASN A O     1 
ATOM   1520  C  CB    . ASN A 1 186  ? 145.000 154.067 141.728 1.00 47.62  ? 186  ASN A CB    1 
ATOM   1521  C  CG    . ASN A 1 186  ? 144.369 155.427 141.508 1.00 53.60  ? 186  ASN A CG    1 
ATOM   1522  O  OD1   . ASN A 1 186  ? 145.019 156.460 141.663 1.00 53.41  ? 186  ASN A OD1   1 
ATOM   1523  N  ND2   . ASN A 1 186  ? 143.093 155.433 141.146 1.00 58.34  ? 186  ASN A ND2   1 
ATOM   1524  N  N     . ASN A 1 187  ? 147.298 151.845 141.573 1.00 44.85  ? 187  ASN A N     1 
ATOM   1525  C  CA    . ASN A 1 187  ? 147.678 150.504 141.996 1.00 41.26  ? 187  ASN A CA    1 
ATOM   1526  C  C     . ASN A 1 187  ? 149.185 150.302 142.068 1.00 42.83  ? 187  ASN A C     1 
ATOM   1527  O  O     . ASN A 1 187  ? 149.636 149.161 142.193 1.00 47.01  ? 187  ASN A O     1 
ATOM   1528  C  CB    . ASN A 1 187  ? 147.079 149.469 141.044 1.00 38.91  ? 187  ASN A CB    1 
ATOM   1529  C  CG    . ASN A 1 187  ? 145.576 149.570 140.949 1.00 46.90  ? 187  ASN A CG    1 
ATOM   1530  O  OD1   . ASN A 1 187  ? 145.030 149.878 139.890 1.00 47.67  ? 187  ASN A OD1   1 
ATOM   1531  N  ND2   . ASN A 1 187  ? 144.895 149.300 142.053 1.00 49.59  ? 187  ASN A ND2   1 
ATOM   1532  N  N     . LEU A 1 188  ? 149.972 151.374 141.994 1.00 40.90  ? 188  LEU A N     1 
ATOM   1533  C  CA    . LEU A 1 188  ? 151.398 151.223 141.729 1.00 43.59  ? 188  LEU A CA    1 
ATOM   1534  C  C     . LEU A 1 188  ? 152.154 150.700 142.948 1.00 48.54  ? 188  LEU A C     1 
ATOM   1535  O  O     . LEU A 1 188  ? 152.909 149.726 142.847 1.00 54.04  ? 188  LEU A O     1 
ATOM   1536  C  CB    . LEU A 1 188  ? 151.971 152.554 141.247 1.00 45.49  ? 188  LEU A CB    1 
ATOM   1537  C  CG    . LEU A 1 188  ? 153.406 152.577 140.731 1.00 43.38  ? 188  LEU A CG    1 
ATOM   1538  C  CD1   . LEU A 1 188  ? 153.677 151.403 139.816 1.00 34.15  ? 188  LEU A CD1   1 
ATOM   1539  C  CD2   . LEU A 1 188  ? 153.598 153.862 139.971 1.00 38.55  ? 188  LEU A CD2   1 
ATOM   1540  N  N     . ASN A 1 189  ? 151.974 151.325 144.107 1.00 44.08  ? 189  ASN A N     1 
ATOM   1541  C  CA    . ASN A 1 189  ? 152.700 150.920 145.307 1.00 44.62  ? 189  ASN A CA    1 
ATOM   1542  C  C     . ASN A 1 189  ? 151.826 150.262 146.360 1.00 45.48  ? 189  ASN A C     1 
ATOM   1543  O  O     . ASN A 1 189  ? 152.273 149.327 147.027 1.00 46.07  ? 189  ASN A O     1 
ATOM   1544  C  CB    . ASN A 1 189  ? 153.411 152.123 145.935 1.00 45.98  ? 189  ASN A CB    1 
ATOM   1545  C  CG    . ASN A 1 189  ? 154.602 152.585 145.126 1.00 52.28  ? 189  ASN A CG    1 
ATOM   1546  O  OD1   . ASN A 1 189  ? 154.931 152.003 144.094 1.00 50.52  ? 189  ASN A OD1   1 
ATOM   1547  N  ND2   . ASN A 1 189  ? 155.263 153.635 145.596 1.00 49.77  ? 189  ASN A ND2   1 
ATOM   1548  N  N     . LYS A 1 190  ? 150.591 150.732 146.530 1.00 47.39  ? 190  LYS A N     1 
ATOM   1549  C  CA    . LYS A 1 190  ? 149.720 150.193 147.569 1.00 45.67  ? 190  LYS A CA    1 
ATOM   1550  C  C     . LYS A 1 190  ? 149.350 148.737 147.309 1.00 43.03  ? 190  LYS A C     1 
ATOM   1551  O  O     . LYS A 1 190  ? 149.115 147.980 148.262 1.00 44.31  ? 190  LYS A O     1 
ATOM   1552  C  CB    . LYS A 1 190  ? 148.468 151.062 147.688 1.00 47.86  ? 190  LYS A CB    1 
ATOM   1553  C  CG    . LYS A 1 190  ? 147.352 150.704 146.726 1.00 48.55  ? 190  LYS A CG    1 
ATOM   1554  C  CD    . LYS A 1 190  ? 146.204 151.690 146.832 1.00 54.42  ? 190  LYS A CD    1 
ATOM   1555  C  CE    . LYS A 1 190  ? 145.622 151.720 148.230 1.00 57.70  ? 190  LYS A CE    1 
ATOM   1556  N  NZ    . LYS A 1 190  ? 144.412 152.583 148.296 1.00 59.41  ? 190  LYS A NZ    1 
ATOM   1557  N  N     . PHE A 1 191  ? 149.302 148.321 146.041 1.00 41.65  ? 191  PHE A N     1 
ATOM   1558  C  CA    . PHE A 1 191  ? 148.867 146.963 145.734 1.00 39.15  ? 191  PHE A CA    1 
ATOM   1559  C  C     . PHE A 1 191  ? 149.875 145.936 146.234 1.00 39.13  ? 191  PHE A C     1 
ATOM   1560  O  O     . PHE A 1 191  ? 149.496 144.843 146.669 1.00 41.44  ? 191  PHE A O     1 
ATOM   1561  C  CB    . PHE A 1 191  ? 148.635 146.810 144.231 1.00 35.86  ? 191  PHE A CB    1 
ATOM   1562  C  CG    . PHE A 1 191  ? 147.940 145.534 143.859 1.00 37.04  ? 191  PHE A CG    1 
ATOM   1563  C  CD1   . PHE A 1 191  ? 148.657 144.369 143.650 1.00 34.98  ? 191  PHE A CD1   1 
ATOM   1564  C  CD2   . PHE A 1 191  ? 146.563 145.498 143.729 1.00 34.36  ? 191  PHE A CD2   1 
ATOM   1565  C  CE1   . PHE A 1 191  ? 148.017 143.200 143.320 1.00 33.16  ? 191  PHE A CE1   1 
ATOM   1566  C  CE2   . PHE A 1 191  ? 145.917 144.330 143.396 1.00 33.69  ? 191  PHE A CE2   1 
ATOM   1567  C  CZ    . PHE A 1 191  ? 146.645 143.178 143.193 1.00 35.55  ? 191  PHE A CZ    1 
ATOM   1568  N  N     . ASP A 1 192  ? 151.166 146.267 146.173 1.00 40.71  ? 192  ASP A N     1 
ATOM   1569  C  CA    . ASP A 1 192  ? 152.191 145.362 146.682 1.00 39.69  ? 192  ASP A CA    1 
ATOM   1570  C  C     . ASP A 1 192  ? 152.127 145.256 148.199 1.00 41.14  ? 192  ASP A C     1 
ATOM   1571  O  O     . ASP A 1 192  ? 152.303 144.169 148.760 1.00 41.58  ? 192  ASP A O     1 
ATOM   1572  C  CB    . ASP A 1 192  ? 153.572 145.846 146.244 1.00 41.68  ? 192  ASP A CB    1 
ATOM   1573  C  CG    . ASP A 1 192  ? 153.599 146.294 144.799 1.00 45.37  ? 192  ASP A CG    1 
ATOM   1574  O  OD1   . ASP A 1 192  ? 152.575 146.147 144.105 1.00 43.65  ? 192  ASP A OD1   1 
ATOM   1575  O  OD2   . ASP A 1 192  ? 154.653 146.793 144.357 1.00 47.28  ? 192  ASP A OD2   1 
ATOM   1576  N  N     . GLU A 1 193  ? 151.878 146.378 148.877 1.00 42.74  ? 193  GLU A N     1 
ATOM   1577  C  CA    . GLU A 1 193  ? 151.822 146.377 150.333 1.00 39.90  ? 193  GLU A CA    1 
ATOM   1578  C  C     . GLU A 1 193  ? 150.570 145.687 150.849 1.00 42.33  ? 193  GLU A C     1 
ATOM   1579  O  O     . GLU A 1 193  ? 150.567 145.173 151.973 1.00 38.63  ? 193  GLU A O     1 
ATOM   1580  C  CB    . GLU A 1 193  ? 151.883 147.811 150.853 1.00 44.25  ? 193  GLU A CB    1 
ATOM   1581  C  CG    . GLU A 1 193  ? 153.002 148.638 150.252 1.00 47.15  ? 193  GLU A CG    1 
ATOM   1582  C  CD    . GLU A 1 193  ? 154.341 147.939 150.322 1.00 51.79  ? 193  GLU A CD    1 
ATOM   1583  O  OE1   . GLU A 1 193  ? 154.961 147.951 151.405 1.00 53.99  ? 193  GLU A OE1   1 
ATOM   1584  O  OE2   . GLU A 1 193  ? 154.776 147.377 149.297 1.00 51.20  ? 193  GLU A OE2   1 
ATOM   1585  N  N     . GLY A 1 194  ? 149.501 145.665 150.052 1.00 43.41  ? 194  GLY A N     1 
ATOM   1586  C  CA    . GLY A 1 194  ? 148.259 145.075 150.516 1.00 34.90  ? 194  GLY A CA    1 
ATOM   1587  C  C     . GLY A 1 194  ? 148.325 143.575 150.717 1.00 35.71  ? 194  GLY A C     1 
ATOM   1588  O  O     . GLY A 1 194  ? 147.556 143.020 151.505 1.00 38.56  ? 194  GLY A O     1 
ATOM   1589  N  N     . LEU A 1 195  ? 149.232 142.894 150.012 1.00 34.41  ? 195  LEU A N     1 
ATOM   1590  C  CA    . LEU A 1 195  ? 149.295 141.437 150.108 1.00 31.19  ? 195  LEU A CA    1 
ATOM   1591  C  C     . LEU A 1 195  ? 149.690 140.973 151.502 1.00 32.39  ? 195  LEU A C     1 
ATOM   1592  O  O     . LEU A 1 195  ? 149.305 139.876 151.921 1.00 34.99  ? 195  LEU A O     1 
ATOM   1593  C  CB    . LEU A 1 195  ? 150.268 140.880 149.071 1.00 32.23  ? 195  LEU A CB    1 
ATOM   1594  C  CG    . LEU A 1 195  ? 149.667 140.356 147.765 1.00 29.68  ? 195  LEU A CG    1 
ATOM   1595  C  CD1   . LEU A 1 195  ? 148.883 139.082 148.012 1.00 28.28  ? 195  LEU A CD1   1 
ATOM   1596  C  CD2   . LEU A 1 195  ? 148.781 141.399 147.119 1.00 30.53  ? 195  LEU A CD2   1 
ATOM   1597  N  N     . ALA A 1 196  ? 150.456 141.782 152.231 1.00 32.56  ? 196  ALA A N     1 
ATOM   1598  C  CA    . ALA A 1 196  ? 150.838 141.411 153.587 1.00 31.14  ? 196  ALA A CA    1 
ATOM   1599  C  C     . ALA A 1 196  ? 149.686 141.576 154.569 1.00 33.54  ? 196  ALA A C     1 
ATOM   1600  O  O     . ALA A 1 196  ? 149.596 140.823 155.544 1.00 34.87  ? 196  ALA A O     1 
ATOM   1601  C  CB    . ALA A 1 196  ? 152.041 142.239 154.037 1.00 32.30  ? 196  ALA A CB    1 
ATOM   1602  N  N     . LEU A 1 197  ? 148.802 142.543 154.329 1.00 32.85  ? 197  LEU A N     1 
ATOM   1603  C  CA    . LEU A 1 197  ? 147.692 142.804 155.237 1.00 31.06  ? 197  LEU A CA    1 
ATOM   1604  C  C     . LEU A 1 197  ? 146.541 141.825 155.051 1.00 29.70  ? 197  LEU A C     1 
ATOM   1605  O  O     . LEU A 1 197  ? 145.717 141.671 155.957 1.00 35.38  ? 197  LEU A O     1 
ATOM   1606  C  CB    . LEU A 1 197  ? 147.182 144.230 155.034 1.00 31.68  ? 197  LEU A CB    1 
ATOM   1607  C  CG    . LEU A 1 197  ? 147.910 145.358 155.757 1.00 31.44  ? 197  LEU A CG    1 
ATOM   1608  C  CD1   . LEU A 1 197  ? 147.457 146.695 155.205 1.00 29.77  ? 197  LEU A CD1   1 
ATOM   1609  C  CD2   . LEU A 1 197  ? 147.650 145.277 157.242 1.00 33.07  ? 197  LEU A CD2   1 
ATOM   1610  N  N     . ALA A 1 198  ? 146.460 141.170 153.892 1.00 29.04  ? 198  ALA A N     1 
ATOM   1611  C  CA    . ALA A 1 198  ? 145.262 140.414 153.536 1.00 30.52  ? 198  ALA A CA    1 
ATOM   1612  C  C     . ALA A 1 198  ? 145.015 139.226 154.458 1.00 31.09  ? 198  ALA A C     1 
ATOM   1613  O  O     . ALA A 1 198  ? 143.860 138.850 154.677 1.00 31.32  ? 198  ALA A O     1 
ATOM   1614  C  CB    . ALA A 1 198  ? 145.360 139.940 152.087 1.00 32.52  ? 198  ALA A CB    1 
ATOM   1615  N  N     . HIS A 1 199  ? 146.069 138.619 155.004 1.00 33.24  ? 199  HIS A N     1 
ATOM   1616  C  CA    . HIS A 1 199  ? 145.899 137.369 155.739 1.00 32.10  ? 199  HIS A CA    1 
ATOM   1617  C  C     . HIS A 1 199  ? 145.208 137.542 157.086 1.00 32.81  ? 199  HIS A C     1 
ATOM   1618  O  O     . HIS A 1 199  ? 144.710 136.556 157.636 1.00 35.48  ? 199  HIS A O     1 
ATOM   1619  C  CB    . HIS A 1 199  ? 147.249 136.684 155.953 1.00 31.33  ? 199  HIS A CB    1 
ATOM   1620  C  CG    . HIS A 1 199  ? 147.619 135.720 154.870 1.00 33.70  ? 199  HIS A CG    1 
ATOM   1621  N  ND1   . HIS A 1 199  ? 146.813 134.663 154.510 1.00 32.00  ? 199  HIS A ND1   1 
ATOM   1622  C  CD2   . HIS A 1 199  ? 148.713 135.645 154.077 1.00 33.51  ? 199  HIS A CD2   1 
ATOM   1623  C  CE1   . HIS A 1 199  ? 147.391 133.981 153.539 1.00 28.65  ? 199  HIS A CE1   1 
ATOM   1624  N  NE2   . HIS A 1 199  ? 148.546 134.556 153.257 1.00 29.00  ? 199  HIS A NE2   1 
ATOM   1625  N  N     . PHE A 1 200  ? 145.155 138.754 157.632 1.00 30.74  ? 200  PHE A N     1 
ATOM   1626  C  CA    . PHE A 1 200  ? 144.590 138.900 158.968 1.00 29.94  ? 200  PHE A CA    1 
ATOM   1627  C  C     . PHE A 1 200  ? 143.076 138.749 159.003 1.00 30.86  ? 200  PHE A C     1 
ATOM   1628  O  O     . PHE A 1 200  ? 142.521 138.651 160.103 1.00 33.00  ? 200  PHE A O     1 
ATOM   1629  C  CB    . PHE A 1 200  ? 144.981 140.248 159.567 1.00 28.79  ? 200  PHE A CB    1 
ATOM   1630  C  CG    . PHE A 1 200  ? 146.415 140.329 159.983 1.00 29.92  ? 200  PHE A CG    1 
ATOM   1631  C  CD1   . PHE A 1 200  ? 146.836 139.754 161.167 1.00 30.82  ? 200  PHE A CD1   1 
ATOM   1632  C  CD2   . PHE A 1 200  ? 147.341 140.992 159.200 1.00 34.24  ? 200  PHE A CD2   1 
ATOM   1633  C  CE1   . PHE A 1 200  ? 148.153 139.828 161.554 1.00 33.44  ? 200  PHE A CE1   1 
ATOM   1634  C  CE2   . PHE A 1 200  ? 148.660 141.071 159.585 1.00 36.81  ? 200  PHE A CE2   1 
ATOM   1635  C  CZ    . PHE A 1 200  ? 149.067 140.488 160.764 1.00 36.70  ? 200  PHE A CZ    1 
ATOM   1636  N  N     . VAL A 1 201  ? 142.409 138.686 157.847 1.00 29.32  ? 201  VAL A N     1 
ATOM   1637  C  CA    . VAL A 1 201  ? 140.960 138.535 157.813 1.00 29.31  ? 201  VAL A CA    1 
ATOM   1638  C  C     . VAL A 1 201  ? 140.532 137.196 158.400 1.00 32.75  ? 201  VAL A C     1 
ATOM   1639  O  O     . VAL A 1 201  ? 139.368 137.027 158.778 1.00 33.05  ? 201  VAL A O     1 
ATOM   1640  C  CB    . VAL A 1 201  ? 140.444 138.703 156.369 1.00 28.03  ? 201  VAL A CB    1 
ATOM   1641  C  CG1   . VAL A 1 201  ? 140.695 137.447 155.553 1.00 30.52  ? 201  VAL A CG1   1 
ATOM   1642  C  CG2   . VAL A 1 201  ? 138.976 139.074 156.357 1.00 24.56  ? 201  VAL A CG2   1 
ATOM   1643  N  N     . TRP A 1 202  ? 141.450 136.234 158.485 1.00 32.87  ? 202  TRP A N     1 
ATOM   1644  C  CA    . TRP A 1 202  ? 141.216 134.985 159.189 1.00 29.35  ? 202  TRP A CA    1 
ATOM   1645  C  C     . TRP A 1 202  ? 142.137 134.776 160.379 1.00 30.14  ? 202  TRP A C     1 
ATOM   1646  O  O     . TRP A 1 202  ? 141.809 133.965 161.249 1.00 31.48  ? 202  TRP A O     1 
ATOM   1647  C  CB    . TRP A 1 202  ? 141.353 133.790 158.231 1.00 27.99  ? 202  TRP A CB    1 
ATOM   1648  C  CG    . TRP A 1 202  ? 142.750 133.547 157.726 1.00 30.81  ? 202  TRP A CG    1 
ATOM   1649  C  CD1   . TRP A 1 202  ? 143.300 134.035 156.576 1.00 30.13  ? 202  TRP A CD1   1 
ATOM   1650  C  CD2   . TRP A 1 202  ? 143.764 132.745 158.343 1.00 35.11  ? 202  TRP A CD2   1 
ATOM   1651  N  NE1   . TRP A 1 202  ? 144.592 133.591 156.443 1.00 29.93  ? 202  TRP A NE1   1 
ATOM   1652  C  CE2   . TRP A 1 202  ? 144.901 132.799 157.516 1.00 33.83  ? 202  TRP A CE2   1 
ATOM   1653  C  CE3   . TRP A 1 202  ? 143.824 131.991 159.519 1.00 31.60  ? 202  TRP A CE3   1 
ATOM   1654  C  CZ2   . TRP A 1 202  ? 146.083 132.129 157.825 1.00 34.16  ? 202  TRP A CZ2   1 
ATOM   1655  C  CZ3   . TRP A 1 202  ? 144.997 131.328 159.824 1.00 30.26  ? 202  TRP A CZ3   1 
ATOM   1656  C  CH2   . TRP A 1 202  ? 146.109 131.401 158.981 1.00 34.48  ? 202  TRP A CH2   1 
ATOM   1657  N  N     . ILE A 1 203  ? 143.271 135.474 160.442 1.00 29.82  ? 203  ILE A N     1 
ATOM   1658  C  CA    . ILE A 1 203  ? 144.148 135.371 161.603 1.00 29.10  ? 203  ILE A CA    1 
ATOM   1659  C  C     . ILE A 1 203  ? 143.503 136.025 162.819 1.00 31.33  ? 203  ILE A C     1 
ATOM   1660  O  O     . ILE A 1 203  ? 143.546 135.482 163.928 1.00 33.54  ? 203  ILE A O     1 
ATOM   1661  C  CB    . ILE A 1 203  ? 145.527 135.985 161.296 1.00 27.57  ? 203  ILE A CB    1 
ATOM   1662  C  CG1   . ILE A 1 203  ? 146.288 135.133 160.280 1.00 28.20  ? 203  ILE A CG1   1 
ATOM   1663  C  CG2   . ILE A 1 203  ? 146.343 136.142 162.564 1.00 25.74  ? 203  ILE A CG2   1 
ATOM   1664  C  CD1   . ILE A 1 203  ? 147.534 135.796 159.743 1.00 29.35  ? 203  ILE A CD1   1 
ATOM   1665  N  N     . ALA A 1 204  ? 142.901 137.202 162.631 1.00 29.80  ? 204  ALA A N     1 
ATOM   1666  C  CA    . ALA A 1 204  ? 142.361 137.942 163.769 1.00 28.72  ? 204  ALA A CA    1 
ATOM   1667  C  C     . ALA A 1 204  ? 141.238 137.214 164.505 1.00 33.35  ? 204  ALA A C     1 
ATOM   1668  O  O     . ALA A 1 204  ? 141.255 137.223 165.750 1.00 35.51  ? 204  ALA A O     1 
ATOM   1669  C  CB    . ALA A 1 204  ? 141.912 139.336 163.311 1.00 26.01  ? 204  ALA A CB    1 
ATOM   1670  N  N     . PRO A 1 205  ? 140.243 136.601 163.841 1.00 34.41  ? 205  PRO A N     1 
ATOM   1671  C  CA    . PRO A 1 205  ? 139.242 135.826 164.597 1.00 32.00  ? 205  PRO A CA    1 
ATOM   1672  C  C     . PRO A 1 205  ? 139.836 134.722 165.456 1.00 33.30  ? 205  PRO A C     1 
ATOM   1673  O  O     . PRO A 1 205  ? 139.369 134.495 166.578 1.00 35.40  ? 205  PRO A O     1 
ATOM   1674  C  CB    . PRO A 1 205  ? 138.344 135.260 163.492 1.00 25.33  ? 205  PRO A CB    1 
ATOM   1675  C  CG    . PRO A 1 205  ? 138.414 136.269 162.427 1.00 24.41  ? 205  PRO A CG    1 
ATOM   1676  C  CD    . PRO A 1 205  ? 139.828 136.774 162.437 1.00 29.44  ? 205  PRO A CD    1 
ATOM   1677  N  N     . LEU A 1 206  ? 140.872 134.040 164.968 1.00 31.31  ? 206  LEU A N     1 
ATOM   1678  C  CA    . LEU A 1 206  ? 141.499 132.984 165.751 1.00 31.22  ? 206  LEU A CA    1 
ATOM   1679  C  C     . LEU A 1 206  ? 142.266 133.541 166.942 1.00 33.96  ? 206  LEU A C     1 
ATOM   1680  O  O     . LEU A 1 206  ? 142.249 132.941 168.025 1.00 35.14  ? 206  LEU A O     1 
ATOM   1681  C  CB    . LEU A 1 206  ? 142.433 132.162 164.865 1.00 33.80  ? 206  LEU A CB    1 
ATOM   1682  C  CG    . LEU A 1 206  ? 141.755 131.175 163.919 1.00 33.44  ? 206  LEU A CG    1 
ATOM   1683  C  CD1   . LEU A 1 206  ? 142.774 130.575 162.973 1.00 34.87  ? 206  LEU A CD1   1 
ATOM   1684  C  CD2   . LEU A 1 206  ? 141.040 130.090 164.701 1.00 35.26  ? 206  LEU A CD2   1 
ATOM   1685  N  N     . GLN A 1 207  ? 142.918 134.692 166.770 1.00 33.83  ? 207  GLN A N     1 
ATOM   1686  C  CA    . GLN A 1 207  ? 143.588 135.336 167.893 1.00 33.92  ? 207  GLN A CA    1 
ATOM   1687  C  C     . GLN A 1 207  ? 142.583 135.767 168.951 1.00 35.94  ? 207  GLN A C     1 
ATOM   1688  O  O     . GLN A 1 207  ? 142.847 135.643 170.151 1.00 37.68  ? 207  GLN A O     1 
ATOM   1689  C  CB    . GLN A 1 207  ? 144.402 136.532 167.401 1.00 33.82  ? 207  GLN A CB    1 
ATOM   1690  C  CG    . GLN A 1 207  ? 145.678 136.154 166.679 1.00 36.04  ? 207  GLN A CG    1 
ATOM   1691  C  CD    . GLN A 1 207  ? 146.694 135.515 167.594 1.00 41.52  ? 207  GLN A CD    1 
ATOM   1692  O  OE1   . GLN A 1 207  ? 146.808 134.294 167.652 1.00 48.12  ? 207  GLN A OE1   1 
ATOM   1693  N  NE2   . GLN A 1 207  ? 147.451 136.339 168.305 1.00 38.27  ? 207  GLN A NE2   1 
ATOM   1694  N  N     . VAL A 1 208  ? 141.421 136.265 168.525 1.00 36.24  ? 208  VAL A N     1 
ATOM   1695  C  CA    . VAL A 1 208  ? 140.380 136.631 169.479 1.00 37.38  ? 208  VAL A CA    1 
ATOM   1696  C  C     . VAL A 1 208  ? 139.849 135.396 170.198 1.00 37.40  ? 208  VAL A C     1 
ATOM   1697  O  O     . VAL A 1 208  ? 139.617 135.422 171.411 1.00 40.90  ? 208  VAL A O     1 
ATOM   1698  C  CB    . VAL A 1 208  ? 139.260 137.411 168.771 1.00 35.92  ? 208  VAL A CB    1 
ATOM   1699  C  CG1   . VAL A 1 208  ? 138.055 137.549 169.676 1.00 37.29  ? 208  VAL A CG1   1 
ATOM   1700  C  CG2   . VAL A 1 208  ? 139.765 138.778 168.357 1.00 34.73  ? 208  VAL A CG2   1 
ATOM   1701  N  N     . ALA A 1 209  ? 139.645 134.297 169.468 1.00 34.40  ? 209  ALA A N     1 
ATOM   1702  C  CA    . ALA A 1 209  ? 139.164 133.070 170.097 1.00 35.41  ? 209  ALA A CA    1 
ATOM   1703  C  C     . ALA A 1 209  ? 140.151 132.534 171.127 1.00 35.67  ? 209  ALA A C     1 
ATOM   1704  O  O     . ALA A 1 209  ? 139.739 131.987 172.153 1.00 35.60  ? 209  ALA A O     1 
ATOM   1705  C  CB    . ALA A 1 209  ? 138.886 132.008 169.035 1.00 32.95  ? 209  ALA A CB    1 
ATOM   1706  N  N     . LEU A 1 210  ? 141.452 132.660 170.863 1.00 38.29  ? 210  LEU A N     1 
ATOM   1707  C  CA    . LEU A 1 210  ? 142.451 132.233 171.841 1.00 35.05  ? 210  LEU A CA    1 
ATOM   1708  C  C     . LEU A 1 210  ? 142.490 133.172 173.045 1.00 36.77  ? 210  LEU A C     1 
ATOM   1709  O  O     . LEU A 1 210  ? 142.493 132.728 174.203 1.00 40.47  ? 210  LEU A O     1 
ATOM   1710  C  CB    . LEU A 1 210  ? 143.823 132.157 171.171 1.00 34.93  ? 210  LEU A CB    1 
ATOM   1711  C  CG    . LEU A 1 210  ? 145.040 131.775 172.014 1.00 38.41  ? 210  LEU A CG    1 
ATOM   1712  C  CD1   . LEU A 1 210  ? 144.898 130.375 172.570 1.00 38.46  ? 210  LEU A CD1   1 
ATOM   1713  C  CD2   . LEU A 1 210  ? 146.315 131.897 171.197 1.00 38.18  ? 210  LEU A CD2   1 
ATOM   1714  N  N     . LEU A 1 211  ? 142.516 134.481 172.789 1.00 37.20  ? 211  LEU A N     1 
ATOM   1715  C  CA    . LEU A 1 211  ? 142.681 135.453 173.861 1.00 36.77  ? 211  LEU A CA    1 
ATOM   1716  C  C     . LEU A 1 211  ? 141.459 135.523 174.765 1.00 36.39  ? 211  LEU A C     1 
ATOM   1717  O  O     . LEU A 1 211  ? 141.598 135.783 175.963 1.00 39.19  ? 211  LEU A O     1 
ATOM   1718  C  CB    . LEU A 1 211  ? 142.985 136.824 173.263 1.00 38.55  ? 211  LEU A CB    1 
ATOM   1719  C  CG    . LEU A 1 211  ? 144.428 136.981 172.791 1.00 34.51  ? 211  LEU A CG    1 
ATOM   1720  C  CD1   . LEU A 1 211  ? 144.545 138.147 171.834 1.00 33.41  ? 211  LEU A CD1   1 
ATOM   1721  C  CD2   . LEU A 1 211  ? 145.352 137.164 173.978 1.00 32.22  ? 211  LEU A CD2   1 
ATOM   1722  N  N     . MET A 1 212  ? 140.259 135.313 174.219 1.00 36.42  ? 212  MET A N     1 
ATOM   1723  C  CA    . MET A 1 212  ? 139.068 135.307 175.058 1.00 38.57  ? 212  MET A CA    1 
ATOM   1724  C  C     . MET A 1 212  ? 139.050 134.107 175.992 1.00 41.21  ? 212  MET A C     1 
ATOM   1725  O  O     . MET A 1 212  ? 138.547 134.206 177.116 1.00 43.98  ? 212  MET A O     1 
ATOM   1726  C  CB    . MET A 1 212  ? 137.808 135.325 174.193 1.00 38.98  ? 212  MET A CB    1 
ATOM   1727  C  CG    . MET A 1 212  ? 137.418 136.708 173.693 1.00 45.47  ? 212  MET A CG    1 
ATOM   1728  S  SD    . MET A 1 212  ? 137.827 138.041 174.838 1.00 63.67  ? 212  MET A SD    1 
ATOM   1729  C  CE    . MET A 1 212  ? 136.608 137.776 176.118 1.00 50.31  ? 212  MET A CE    1 
ATOM   1730  N  N     . GLY A 1 213  ? 139.579 132.968 175.543 1.00 38.47  ? 213  GLY A N     1 
ATOM   1731  C  CA    . GLY A 1 213  ? 139.710 131.826 176.427 1.00 34.32  ? 213  GLY A CA    1 
ATOM   1732  C  C     . GLY A 1 213  ? 140.798 132.007 177.463 1.00 36.47  ? 213  GLY A C     1 
ATOM   1733  O  O     . GLY A 1 213  ? 140.696 131.477 178.572 1.00 39.91  ? 213  GLY A O     1 
ATOM   1734  N  N     . LEU A 1 214  ? 141.850 132.753 177.125 1.00 36.84  ? 214  LEU A N     1 
ATOM   1735  C  CA    . LEU A 1 214  ? 142.882 133.024 178.124 1.00 34.92  ? 214  LEU A CA    1 
ATOM   1736  C  C     . LEU A 1 214  ? 142.417 134.035 179.167 1.00 38.38  ? 214  LEU A C     1 
ATOM   1737  O  O     . LEU A 1 214  ? 142.759 133.909 180.347 1.00 44.01  ? 214  LEU A O     1 
ATOM   1738  C  CB    . LEU A 1 214  ? 144.170 133.502 177.457 1.00 35.04  ? 214  LEU A CB    1 
ATOM   1739  C  CG    . LEU A 1 214  ? 144.965 132.460 176.673 1.00 37.24  ? 214  LEU A CG    1 
ATOM   1740  C  CD1   . LEU A 1 214  ? 146.150 133.106 175.979 1.00 36.95  ? 214  LEU A CD1   1 
ATOM   1741  C  CD2   . LEU A 1 214  ? 145.427 131.355 177.604 1.00 34.15  ? 214  LEU A CD2   1 
ATOM   1742  N  N     . ILE A 1 215  ? 141.652 135.048 178.757 1.00 39.14  ? 215  ILE A N     1 
ATOM   1743  C  CA    . ILE A 1 215  ? 141.135 136.022 179.714 1.00 40.40  ? 215  ILE A CA    1 
ATOM   1744  C  C     . ILE A 1 215  ? 140.024 135.409 180.559 1.00 43.55  ? 215  ILE A C     1 
ATOM   1745  O  O     . ILE A 1 215  ? 139.819 135.808 181.713 1.00 45.33  ? 215  ILE A O     1 
ATOM   1746  C  CB    . ILE A 1 215  ? 140.663 137.292 178.978 1.00 41.27  ? 215  ILE A CB    1 
ATOM   1747  C  CG1   . ILE A 1 215  ? 141.851 138.019 178.351 1.00 34.73  ? 215  ILE A CG1   1 
ATOM   1748  C  CG2   . ILE A 1 215  ? 139.945 138.237 179.917 1.00 43.94  ? 215  ILE A CG2   1 
ATOM   1749  C  CD1   . ILE A 1 215  ? 141.470 138.982 177.259 1.00 32.54  ? 215  ILE A CD1   1 
ATOM   1750  N  N     . TRP A 1 216  ? 139.313 134.415 180.020 1.00 46.29  ? 216  TRP A N     1 
ATOM   1751  C  CA    . TRP A 1 216  ? 138.194 133.809 180.736 1.00 45.09  ? 216  TRP A CA    1 
ATOM   1752  C  C     . TRP A 1 216  ? 138.640 133.171 182.045 1.00 47.03  ? 216  TRP A C     1 
ATOM   1753  O  O     . TRP A 1 216  ? 137.900 133.190 183.034 1.00 49.15  ? 216  TRP A O     1 
ATOM   1754  C  CB    . TRP A 1 216  ? 137.506 132.777 179.840 1.00 46.71  ? 216  TRP A CB    1 
ATOM   1755  C  CG    . TRP A 1 216  ? 136.215 132.232 180.383 1.00 54.04  ? 216  TRP A CG    1 
ATOM   1756  C  CD1   . TRP A 1 216  ? 134.953 132.611 180.028 1.00 55.77  ? 216  TRP A CD1   1 
ATOM   1757  C  CD2   . TRP A 1 216  ? 136.061 131.168 181.330 1.00 54.28  ? 216  TRP A CD2   1 
ATOM   1758  N  NE1   . TRP A 1 216  ? 134.025 131.872 180.721 1.00 54.31  ? 216  TRP A NE1   1 
ATOM   1759  C  CE2   . TRP A 1 216  ? 134.681 130.978 181.523 1.00 52.64  ? 216  TRP A CE2   1 
ATOM   1760  C  CE3   . TRP A 1 216  ? 136.957 130.366 182.041 1.00 52.26  ? 216  TRP A CE3   1 
ATOM   1761  C  CZ2   . TRP A 1 216  ? 134.176 130.025 182.398 1.00 51.69  ? 216  TRP A CZ2   1 
ATOM   1762  C  CZ3   . TRP A 1 216  ? 136.454 129.423 182.910 1.00 53.74  ? 216  TRP A CZ3   1 
ATOM   1763  C  CH2   . TRP A 1 216  ? 135.078 129.260 183.081 1.00 57.66  ? 216  TRP A CH2   1 
ATOM   1764  N  N     . GLU A 1 217  ? 139.841 132.594 182.076 1.00 46.85  ? 217  GLU A N     1 
ATOM   1765  C  CA    . GLU A 1 217  ? 140.294 131.930 183.291 1.00 49.61  ? 217  GLU A CA    1 
ATOM   1766  C  C     . GLU A 1 217  ? 140.730 132.916 184.370 1.00 53.53  ? 217  GLU A C     1 
ATOM   1767  O  O     . GLU A 1 217  ? 140.816 132.533 185.542 1.00 58.11  ? 217  GLU A O     1 
ATOM   1768  C  CB    . GLU A 1 217  ? 141.421 130.951 182.971 1.00 50.86  ? 217  GLU A CB    1 
ATOM   1769  C  CG    . GLU A 1 217  ? 142.814 131.494 183.161 1.00 57.37  ? 217  GLU A CG    1 
ATOM   1770  C  CD    . GLU A 1 217  ? 143.815 130.394 183.438 1.00 67.59  ? 217  GLU A CD    1 
ATOM   1771  O  OE1   . GLU A 1 217  ? 143.794 129.848 184.560 1.00 67.82  ? 217  GLU A OE1   1 
ATOM   1772  O  OE2   . GLU A 1 217  ? 144.614 130.068 182.537 1.00 71.21  ? 217  GLU A OE2   1 
ATOM   1773  N  N     . LEU A 1 218  ? 141.030 134.165 184.006 1.00 52.33  ? 218  LEU A N     1 
ATOM   1774  C  CA    . LEU A 1 218  ? 141.214 135.207 185.011 1.00 50.56  ? 218  LEU A CA    1 
ATOM   1775  C  C     . LEU A 1 218  ? 139.874 135.722 185.519 1.00 48.75  ? 218  LEU A C     1 
ATOM   1776  O  O     . LEU A 1 218  ? 139.633 135.768 186.729 1.00 48.44  ? 218  LEU A O     1 
ATOM   1777  C  CB    . LEU A 1 218  ? 142.029 136.367 184.436 1.00 48.59  ? 218  LEU A CB    1 
ATOM   1778  C  CG    . LEU A 1 218  ? 143.518 136.185 184.165 1.00 49.74  ? 218  LEU A CG    1 
ATOM   1779  C  CD1   . LEU A 1 218  ? 143.999 137.301 183.258 1.00 43.39  ? 218  LEU A CD1   1 
ATOM   1780  C  CD2   . LEU A 1 218  ? 144.299 136.177 185.466 1.00 48.59  ? 218  LEU A CD2   1 
ATOM   1781  N  N     . LEU A 1 219  ? 138.996 136.110 184.601 1.00 50.59  ? 219  LEU A N     1 
ATOM   1782  C  CA    . LEU A 1 219  ? 137.694 136.697 184.910 1.00 50.64  ? 219  LEU A CA    1 
ATOM   1783  C  C     . LEU A 1 219  ? 136.646 135.751 184.337 1.00 51.03  ? 219  LEU A C     1 
ATOM   1784  O  O     . LEU A 1 219  ? 136.495 135.651 183.117 1.00 56.78  ? 219  LEU A O     1 
ATOM   1785  C  CB    . LEU A 1 219  ? 137.575 138.093 184.313 1.00 49.92  ? 219  LEU A CB    1 
ATOM   1786  C  CG    . LEU A 1 219  ? 138.747 139.040 184.567 1.00 45.40  ? 219  LEU A CG    1 
ATOM   1787  C  CD1   . LEU A 1 219  ? 138.566 140.313 183.770 1.00 46.84  ? 219  LEU A CD1   1 
ATOM   1788  C  CD2   . LEU A 1 219  ? 138.890 139.344 186.045 1.00 46.13  ? 219  LEU A CD2   1 
ATOM   1789  N  N     . GLN A 1 220  ? 135.924 135.058 185.214 1.00 49.72  ? 220  GLN A N     1 
ATOM   1790  C  CA    . GLN A 1 220  ? 135.113 133.919 184.803 1.00 53.82  ? 220  GLN A CA    1 
ATOM   1791  C  C     . GLN A 1 220  ? 134.083 134.279 183.738 1.00 56.19  ? 220  GLN A C     1 
ATOM   1792  O  O     . GLN A 1 220  ? 134.157 133.784 182.610 1.00 58.93  ? 220  GLN A O     1 
ATOM   1793  C  CB    . GLN A 1 220  ? 134.414 133.313 186.020 1.00 57.50  ? 220  GLN A CB    1 
ATOM   1794  C  CG    . GLN A 1 220  ? 135.328 133.113 187.218 1.00 57.63  ? 220  GLN A CG    1 
ATOM   1795  C  CD    . GLN A 1 220  ? 136.644 132.470 186.848 1.00 58.04  ? 220  GLN A CD    1 
ATOM   1796  O  OE1   . GLN A 1 220  ? 136.678 131.434 186.187 1.00 56.30  ? 220  GLN A OE1   1 
ATOM   1797  N  NE2   . GLN A 1 220  ? 137.740 133.080 187.281 1.00 54.72  ? 220  GLN A NE2   1 
ATOM   1798  N  N     . ALA A 1 221  ? 133.125 135.139 184.074 1.00 54.00  ? 221  ALA A N     1 
ATOM   1799  C  CA    . ALA A 1 221  ? 132.086 135.534 183.133 1.00 49.85  ? 221  ALA A CA    1 
ATOM   1800  C  C     . ALA A 1 221  ? 132.147 137.004 182.744 1.00 52.31  ? 221  ALA A C     1 
ATOM   1801  O  O     . ALA A 1 221  ? 131.390 137.424 181.863 1.00 50.90  ? 221  ALA A O     1 
ATOM   1802  C  CB    . ALA A 1 221  ? 130.702 135.221 183.709 1.00 46.47  ? 221  ALA A CB    1 
ATOM   1803  N  N     . SER A 1 222  ? 133.013 137.793 183.379 1.00 54.75  ? 222  SER A N     1 
ATOM   1804  C  CA    . SER A 1 222  ? 133.031 139.238 183.192 1.00 53.97  ? 222  SER A CA    1 
ATOM   1805  C  C     . SER A 1 222  ? 133.767 139.685 181.934 1.00 56.79  ? 222  SER A C     1 
ATOM   1806  O  O     . SER A 1 222  ? 133.651 140.856 181.557 1.00 58.59  ? 222  SER A O     1 
ATOM   1807  C  CB    . SER A 1 222  ? 133.658 139.906 184.415 1.00 53.78  ? 222  SER A CB    1 
ATOM   1808  O  OG    . SER A 1 222  ? 133.531 141.313 184.351 1.00 59.96  ? 222  SER A OG    1 
ATOM   1809  N  N     . ALA A 1 223  ? 134.521 138.796 181.283 1.00 53.42  ? 223  ALA A N     1 
ATOM   1810  C  CA    . ALA A 1 223  ? 135.260 139.178 180.081 1.00 51.72  ? 223  ALA A CA    1 
ATOM   1811  C  C     . ALA A 1 223  ? 134.329 139.550 178.932 1.00 55.35  ? 223  ALA A C     1 
ATOM   1812  O  O     . ALA A 1 223  ? 134.668 140.404 178.097 1.00 59.56  ? 223  ALA A O     1 
ATOM   1813  C  CB    . ALA A 1 223  ? 136.195 138.043 179.665 1.00 48.34  ? 223  ALA A CB    1 
ATOM   1814  N  N     . PHE A 1 224  ? 133.156 138.921 178.864 1.00 54.35  ? 224  PHE A N     1 
ATOM   1815  C  CA    . PHE A 1 224  ? 132.234 139.209 177.776 1.00 52.65  ? 224  PHE A CA    1 
ATOM   1816  C  C     . PHE A 1 224  ? 131.719 140.639 177.835 1.00 55.44  ? 224  PHE A C     1 
ATOM   1817  O  O     . PHE A 1 224  ? 131.275 141.170 176.811 1.00 58.34  ? 224  PHE A O     1 
ATOM   1818  C  CB    . PHE A 1 224  ? 131.074 138.217 177.810 1.00 51.98  ? 224  PHE A CB    1 
ATOM   1819  C  CG    . PHE A 1 224  ? 131.509 136.785 177.708 1.00 53.97  ? 224  PHE A CG    1 
ATOM   1820  C  CD1   . PHE A 1 224  ? 132.238 136.343 176.618 1.00 52.51  ? 224  PHE A CD1   1 
ATOM   1821  C  CD2   . PHE A 1 224  ? 131.198 135.885 178.710 1.00 52.79  ? 224  PHE A CD2   1 
ATOM   1822  C  CE1   . PHE A 1 224  ? 132.644 135.028 176.529 1.00 47.07  ? 224  PHE A CE1   1 
ATOM   1823  C  CE2   . PHE A 1 224  ? 131.599 134.570 178.627 1.00 54.68  ? 224  PHE A CE2   1 
ATOM   1824  C  CZ    . PHE A 1 224  ? 132.323 134.139 177.535 1.00 51.67  ? 224  PHE A CZ    1 
ATOM   1825  N  N     . CYS A 1 225  ? 131.815 141.284 178.999 1.00 55.67  ? 225  CYS A N     1 
ATOM   1826  C  CA    . CYS A 1 225  ? 131.416 142.681 179.110 1.00 57.93  ? 225  CYS A CA    1 
ATOM   1827  C  C     . CYS A 1 225  ? 132.295 143.571 178.242 1.00 57.98  ? 225  CYS A C     1 
ATOM   1828  O  O     . CYS A 1 225  ? 131.808 144.535 177.641 1.00 59.69  ? 225  CYS A O     1 
ATOM   1829  C  CB    . CYS A 1 225  ? 131.476 143.125 180.571 1.00 58.43  ? 225  CYS A CB    1 
ATOM   1830  S  SG    . CYS A 1 225  ? 130.412 142.181 181.689 1.00 71.75  ? 225  CYS A SG    1 
ATOM   1831  N  N     . GLY A 1 226  ? 133.595 143.271 178.169 1.00 58.44  ? 226  GLY A N     1 
ATOM   1832  C  CA    . GLY A 1 226  ? 134.463 143.978 177.244 1.00 56.20  ? 226  GLY A CA    1 
ATOM   1833  C  C     . GLY A 1 226  ? 134.424 143.421 175.838 1.00 55.24  ? 226  GLY A C     1 
ATOM   1834  O  O     . GLY A 1 226  ? 134.652 144.157 174.868 1.00 55.16  ? 226  GLY A O     1 
ATOM   1835  N  N     . LEU A 1 227  ? 134.111 142.129 175.698 1.00 54.33  ? 227  LEU A N     1 
ATOM   1836  C  CA    . LEU A 1 227  ? 133.979 141.563 174.359 1.00 53.66  ? 227  LEU A CA    1 
ATOM   1837  C  C     . LEU A 1 227  ? 132.842 142.224 173.585 1.00 56.63  ? 227  LEU A C     1 
ATOM   1838  O  O     . LEU A 1 227  ? 132.984 142.513 172.390 1.00 58.55  ? 227  LEU A O     1 
ATOM   1839  C  CB    . LEU A 1 227  ? 133.767 140.051 174.439 1.00 53.42  ? 227  LEU A CB    1 
ATOM   1840  C  CG    . LEU A 1 227  ? 133.692 139.335 173.089 1.00 52.26  ? 227  LEU A CG    1 
ATOM   1841  C  CD1   . LEU A 1 227  ? 135.011 139.451 172.352 1.00 52.29  ? 227  LEU A CD1   1 
ATOM   1842  C  CD2   . LEU A 1 227  ? 133.303 137.879 173.263 1.00 49.81  ? 227  LEU A CD2   1 
ATOM   1843  N  N     . GLY A 1 228  ? 131.709 142.480 174.246 1.00 55.00  ? 228  GLY A N     1 
ATOM   1844  C  CA    . GLY A 1 228  ? 130.620 143.181 173.584 1.00 53.32  ? 228  GLY A CA    1 
ATOM   1845  C  C     . GLY A 1 228  ? 130.969 144.604 173.191 1.00 54.11  ? 228  GLY A C     1 
ATOM   1846  O  O     . GLY A 1 228  ? 130.550 145.082 172.130 1.00 54.41  ? 228  GLY A O     1 
ATOM   1847  N  N     . PHE A 1 229  ? 131.753 145.293 174.023 1.00 50.47  ? 229  PHE A N     1 
ATOM   1848  C  CA    . PHE A 1 229  ? 132.214 146.633 173.676 1.00 51.00  ? 229  PHE A CA    1 
ATOM   1849  C  C     . PHE A 1 229  ? 133.079 146.603 172.423 1.00 52.82  ? 229  PHE A C     1 
ATOM   1850  O  O     . PHE A 1 229  ? 132.914 147.431 171.516 1.00 52.10  ? 229  PHE A O     1 
ATOM   1851  C  CB    . PHE A 1 229  ? 132.980 147.236 174.854 1.00 50.88  ? 229  PHE A CB    1 
ATOM   1852  C  CG    . PHE A 1 229  ? 133.546 148.599 174.580 1.00 55.18  ? 229  PHE A CG    1 
ATOM   1853  C  CD1   . PHE A 1 229  ? 132.733 149.717 174.584 1.00 52.93  ? 229  PHE A CD1   1 
ATOM   1854  C  CD2   . PHE A 1 229  ? 134.899 148.759 174.326 1.00 54.09  ? 229  PHE A CD2   1 
ATOM   1855  C  CE1   . PHE A 1 229  ? 133.254 150.967 174.336 1.00 54.91  ? 229  PHE A CE1   1 
ATOM   1856  C  CE2   . PHE A 1 229  ? 135.427 150.006 174.077 1.00 56.12  ? 229  PHE A CE2   1 
ATOM   1857  C  CZ    . PHE A 1 229  ? 134.602 151.114 174.082 1.00 61.57  ? 229  PHE A CZ    1 
ATOM   1858  N  N     . LEU A 1 230  ? 133.996 145.636 172.345 1.00 51.74  ? 230  LEU A N     1 
ATOM   1859  C  CA    . LEU A 1 230  ? 134.815 145.519 171.142 1.00 47.14  ? 230  LEU A CA    1 
ATOM   1860  C  C     . LEU A 1 230  ? 133.980 145.141 169.922 1.00 47.58  ? 230  LEU A C     1 
ATOM   1861  O  O     . LEU A 1 230  ? 134.278 145.588 168.809 1.00 49.89  ? 230  LEU A O     1 
ATOM   1862  C  CB    . LEU A 1 230  ? 135.933 144.502 171.357 1.00 47.58  ? 230  LEU A CB    1 
ATOM   1863  C  CG    . LEU A 1 230  ? 137.158 145.042 172.091 1.00 44.50  ? 230  LEU A CG    1 
ATOM   1864  C  CD1   . LEU A 1 230  ? 138.145 143.930 172.352 1.00 36.57  ? 230  LEU A CD1   1 
ATOM   1865  C  CD2   . LEU A 1 230  ? 137.805 146.158 171.300 1.00 42.20  ? 230  LEU A CD2   1 
ATOM   1866  N  N     . ILE A 1 231  ? 132.931 144.336 170.106 1.00 46.26  ? 231  ILE A N     1 
ATOM   1867  C  CA    . ILE A 1 231  ? 132.055 143.992 168.987 1.00 49.07  ? 231  ILE A CA    1 
ATOM   1868  C  C     . ILE A 1 231  ? 131.349 145.234 168.450 1.00 50.13  ? 231  ILE A C     1 
ATOM   1869  O  O     . ILE A 1 231  ? 131.272 145.454 167.229 1.00 51.88  ? 231  ILE A O     1 
ATOM   1870  C  CB    . ILE A 1 231  ? 131.044 142.913 169.417 1.00 51.46  ? 231  ILE A CB    1 
ATOM   1871  C  CG1   . ILE A 1 231  ? 131.725 141.545 169.512 1.00 52.83  ? 231  ILE A CG1   1 
ATOM   1872  C  CG2   . ILE A 1 231  ? 129.864 142.875 168.461 1.00 47.61  ? 231  ILE A CG2   1 
ATOM   1873  C  CD1   . ILE A 1 231  ? 130.766 140.371 169.448 1.00 54.08  ? 231  ILE A CD1   1 
ATOM   1874  N  N     . VAL A 1 232  ? 130.829 146.069 169.352 1.00 47.40  ? 232  VAL A N     1 
ATOM   1875  C  CA    . VAL A 1 232  ? 130.153 147.290 168.925 1.00 45.11  ? 232  VAL A CA    1 
ATOM   1876  C  C     . VAL A 1 232  ? 131.135 148.224 168.223 1.00 44.64  ? 232  VAL A C     1 
ATOM   1877  O  O     . VAL A 1 232  ? 130.802 148.859 167.213 1.00 46.82  ? 232  VAL A O     1 
ATOM   1878  C  CB    . VAL A 1 232  ? 129.473 147.963 170.131 1.00 46.23  ? 232  VAL A CB    1 
ATOM   1879  C  CG1   . VAL A 1 232  ? 129.115 149.404 169.819 1.00 44.56  ? 232  VAL A CG1   1 
ATOM   1880  C  CG2   . VAL A 1 232  ? 128.239 147.175 170.538 1.00 45.77  ? 232  VAL A CG2   1 
ATOM   1881  N  N     . LEU A 1 233  ? 132.370 148.298 168.725 1.00 43.29  ? 233  LEU A N     1 
ATOM   1882  C  CA    . LEU A 1 233  ? 133.375 149.132 168.070 1.00 44.63  ? 233  LEU A CA    1 
ATOM   1883  C  C     . LEU A 1 233  ? 133.726 148.610 166.678 1.00 44.63  ? 233  LEU A C     1 
ATOM   1884  O  O     . LEU A 1 233  ? 133.955 149.405 165.752 1.00 45.40  ? 233  LEU A O     1 
ATOM   1885  C  CB    . LEU A 1 233  ? 134.622 149.209 168.950 1.00 44.87  ? 233  LEU A CB    1 
ATOM   1886  C  CG    . LEU A 1 233  ? 135.277 150.577 169.110 1.00 39.70  ? 233  LEU A CG    1 
ATOM   1887  C  CD1   . LEU A 1 233  ? 136.167 150.862 167.932 1.00 42.21  ? 233  LEU A CD1   1 
ATOM   1888  C  CD2   . LEU A 1 233  ? 134.218 151.649 169.241 1.00 43.47  ? 233  LEU A CD2   1 
ATOM   1889  N  N     . ALA A 1 234  ? 133.745 147.287 166.502 1.00 42.66  ? 234  ALA A N     1 
ATOM   1890  C  CA    . ALA A 1 234  ? 134.010 146.725 165.182 1.00 43.29  ? 234  ALA A CA    1 
ATOM   1891  C  C     . ALA A 1 234  ? 132.891 147.061 164.203 1.00 44.44  ? 234  ALA A C     1 
ATOM   1892  O  O     . ALA A 1 234  ? 133.154 147.404 163.043 1.00 42.94  ? 234  ALA A O     1 
ATOM   1893  C  CB    . ALA A 1 234  ? 134.200 145.212 165.284 1.00 44.19  ? 234  ALA A CB    1 
ATOM   1894  N  N     . LEU A 1 235  ? 131.636 146.979 164.654 1.00 43.80  ? 235  LEU A N     1 
ATOM   1895  C  CA    . LEU A 1 235  ? 130.532 147.395 163.789 1.00 42.39  ? 235  LEU A CA    1 
ATOM   1896  C  C     . LEU A 1 235  ? 130.627 148.877 163.433 1.00 43.38  ? 235  LEU A C     1 
ATOM   1897  O  O     . LEU A 1 235  ? 130.334 149.266 162.293 1.00 42.48  ? 235  LEU A O     1 
ATOM   1898  C  CB    . LEU A 1 235  ? 129.189 147.095 164.453 1.00 45.27  ? 235  LEU A CB    1 
ATOM   1899  C  CG    . LEU A 1 235  ? 128.596 145.705 164.218 1.00 54.17  ? 235  LEU A CG    1 
ATOM   1900  C  CD1   . LEU A 1 235  ? 127.502 145.414 165.229 1.00 55.62  ? 235  LEU A CD1   1 
ATOM   1901  C  CD2   . LEU A 1 235  ? 128.056 145.600 162.802 1.00 55.69  ? 235  LEU A CD2   1 
ATOM   1902  N  N     . PHE A 1 236  ? 131.056 149.708 164.383 1.00 42.84  ? 236  PHE A N     1 
ATOM   1903  C  CA    . PHE A 1 236  ? 131.228 151.134 164.111 1.00 41.43  ? 236  PHE A CA    1 
ATOM   1904  C  C     . PHE A 1 236  ? 132.264 151.370 163.011 1.00 43.28  ? 236  PHE A C     1 
ATOM   1905  O  O     . PHE A 1 236  ? 132.044 152.164 162.084 1.00 42.87  ? 236  PHE A O     1 
ATOM   1906  C  CB    . PHE A 1 236  ? 131.617 151.843 165.410 1.00 42.46  ? 236  PHE A CB    1 
ATOM   1907  C  CG    . PHE A 1 236  ? 131.974 153.290 165.245 1.00 46.37  ? 236  PHE A CG    1 
ATOM   1908  C  CD1   . PHE A 1 236  ? 133.260 153.731 165.521 1.00 46.55  ? 236  PHE A CD1   1 
ATOM   1909  C  CD2   . PHE A 1 236  ? 131.028 154.211 164.833 1.00 44.98  ? 236  PHE A CD2   1 
ATOM   1910  C  CE1   . PHE A 1 236  ? 133.597 155.064 165.387 1.00 44.12  ? 236  PHE A CE1   1 
ATOM   1911  C  CE2   . PHE A 1 236  ? 131.359 155.546 164.691 1.00 46.42  ? 236  PHE A CE2   1 
ATOM   1912  C  CZ    . PHE A 1 236  ? 132.645 155.974 164.969 1.00 45.84  ? 236  PHE A CZ    1 
ATOM   1913  N  N     . GLN A 1 237  ? 133.402 150.675 163.090 1.00 41.20  ? 237  GLN A N     1 
ATOM   1914  C  CA    . GLN A 1 237  ? 134.418 150.830 162.048 1.00 36.09  ? 237  GLN A CA    1 
ATOM   1915  C  C     . GLN A 1 237  ? 133.939 150.304 160.698 1.00 39.18  ? 237  GLN A C     1 
ATOM   1916  O  O     . GLN A 1 237  ? 134.249 150.898 159.649 1.00 41.53  ? 237  GLN A O     1 
ATOM   1917  C  CB    . GLN A 1 237  ? 135.706 150.126 162.461 1.00 34.24  ? 237  GLN A CB    1 
ATOM   1918  C  CG    . GLN A 1 237  ? 136.458 150.841 163.555 1.00 35.20  ? 237  GLN A CG    1 
ATOM   1919  C  CD    . GLN A 1 237  ? 137.685 150.089 164.002 1.00 33.66  ? 237  GLN A CD    1 
ATOM   1920  O  OE1   . GLN A 1 237  ? 137.594 148.966 164.490 1.00 39.26  ? 237  GLN A OE1   1 
ATOM   1921  N  NE2   . GLN A 1 237  ? 138.848 150.699 163.822 1.00 32.84  ? 237  GLN A NE2   1 
ATOM   1922  N  N     . ALA A 1 238  ? 133.196 149.192 160.702 1.00 41.62  ? 238  ALA A N     1 
ATOM   1923  C  CA    . ALA A 1 238  ? 132.639 148.670 159.458 1.00 40.11  ? 238  ALA A CA    1 
ATOM   1924  C  C     . ALA A 1 238  ? 131.665 149.653 158.832 1.00 41.23  ? 238  ALA A C     1 
ATOM   1925  O  O     . ALA A 1 238  ? 131.512 149.678 157.606 1.00 39.57  ? 238  ALA A O     1 
ATOM   1926  C  CB    . ALA A 1 238  ? 131.946 147.330 159.703 1.00 36.87  ? 238  ALA A CB    1 
ATOM   1927  N  N     . GLY A 1 239  ? 130.995 150.466 159.652 1.00 44.92  ? 239  GLY A N     1 
ATOM   1928  C  CA    . GLY A 1 239  ? 130.165 151.525 159.106 1.00 39.84  ? 239  GLY A CA    1 
ATOM   1929  C  C     . GLY A 1 239  ? 130.947 152.708 158.572 1.00 41.57  ? 239  GLY A C     1 
ATOM   1930  O  O     . GLY A 1 239  ? 130.540 153.321 157.582 1.00 43.02  ? 239  GLY A O     1 
ATOM   1931  N  N     . LEU A 1 240  ? 132.065 153.053 159.214 1.00 42.28  ? 240  LEU A N     1 
ATOM   1932  C  CA    . LEU A 1 240  ? 132.869 154.183 158.737 1.00 40.50  ? 240  LEU A CA    1 
ATOM   1933  C  C     . LEU A 1 240  ? 133.513 153.895 157.380 1.00 40.84  ? 240  LEU A C     1 
ATOM   1934  O  O     . LEU A 1 240  ? 133.600 154.786 156.513 1.00 47.63  ? 240  LEU A O     1 
ATOM   1935  C  CB    . LEU A 1 240  ? 133.943 154.533 159.764 1.00 39.34  ? 240  LEU A CB    1 
ATOM   1936  C  CG    . LEU A 1 240  ? 133.518 155.278 161.027 1.00 37.63  ? 240  LEU A CG    1 
ATOM   1937  C  CD1   . LEU A 1 240  ? 134.664 155.296 162.019 1.00 36.51  ? 240  LEU A CD1   1 
ATOM   1938  C  CD2   . LEU A 1 240  ? 133.078 156.686 160.694 1.00 34.86  ? 240  LEU A CD2   1 
ATOM   1939  N  N     . GLY A 1 241  ? 133.991 152.663 157.187 1.00 38.24  ? 241  GLY A N     1 
ATOM   1940  C  CA    . GLY A 1 241  ? 134.683 152.342 155.948 1.00 35.72  ? 241  GLY A CA    1 
ATOM   1941  C  C     . GLY A 1 241  ? 133.819 152.518 154.715 1.00 41.81  ? 241  GLY A C     1 
ATOM   1942  O  O     . GLY A 1 241  ? 134.315 152.905 153.650 1.00 44.36  ? 241  GLY A O     1 
ATOM   1943  N  N     . ARG A 1 242  ? 132.518 152.261 154.844 1.00 45.53  ? 242  ARG A N     1 
ATOM   1944  C  CA    . ARG A 1 242  ? 131.611 152.362 153.706 1.00 43.79  ? 242  ARG A CA    1 
ATOM   1945  C  C     . ARG A 1 242  ? 131.419 153.812 153.275 1.00 41.55  ? 242  ARG A C     1 
ATOM   1946  O  O     . ARG A 1 242  ? 131.374 154.109 152.074 1.00 46.75  ? 242  ARG A O     1 
ATOM   1947  C  CB    . ARG A 1 242  ? 130.284 151.705 154.073 1.00 47.11  ? 242  ARG A CB    1 
ATOM   1948  C  CG    . ARG A 1 242  ? 129.921 150.511 153.216 1.00 54.36  ? 242  ARG A CG    1 
ATOM   1949  C  CD    . ARG A 1 242  ? 128.544 149.990 153.575 1.00 57.75  ? 242  ARG A CD    1 
ATOM   1950  N  NE    . ARG A 1 242  ? 128.570 149.356 154.888 1.00 70.38  ? 242  ARG A NE    1 
ATOM   1951  C  CZ    . ARG A 1 242  ? 127.525 148.791 155.478 1.00 77.70  ? 242  ARG A CZ    1 
ATOM   1952  N  NH1   . ARG A 1 242  ? 126.339 148.753 154.895 1.00 82.49  ? 242  ARG A NH1   1 
ATOM   1953  N  NH2   . ARG A 1 242  ? 127.677 148.245 156.682 1.00 63.97  ? 242  ARG A NH2   1 
ATOM   1954  N  N     . MET A 1 243  ? 131.329 154.733 154.237 1.00 39.37  ? 243  MET A N     1 
ATOM   1955  C  CA    . MET A 1 243  ? 131.278 156.153 153.901 1.00 37.95  ? 243  MET A CA    1 
ATOM   1956  C  C     . MET A 1 243  ? 132.563 156.596 153.218 1.00 39.05  ? 243  MET A C     1 
ATOM   1957  O  O     . MET A 1 243  ? 132.529 157.371 152.250 1.00 40.31  ? 243  MET A O     1 
ATOM   1958  C  CB    . MET A 1 243  ? 131.044 156.984 155.160 1.00 40.50  ? 243  MET A CB    1 
ATOM   1959  C  CG    . MET A 1 243  ? 129.704 156.769 155.829 1.00 48.26  ? 243  MET A CG    1 
ATOM   1960  S  SD    . MET A 1 243  ? 129.591 157.677 157.382 1.00 69.51  ? 243  MET A SD    1 
ATOM   1961  C  CE    . MET A 1 243  ? 129.608 159.369 156.797 1.00 52.86  ? 243  MET A CE    1 
ATOM   1962  N  N     . MET A 1 244  ? 133.707 156.119 153.716 1.00 40.81  ? 244  MET A N     1 
ATOM   1963  C  CA    . MET A 1 244  ? 134.968 156.470 153.068 1.00 39.92  ? 244  MET A CA    1 
ATOM   1964  C  C     . MET A 1 244  ? 134.981 156.010 151.614 1.00 42.36  ? 244  MET A C     1 
ATOM   1965  O  O     . MET A 1 244  ? 135.369 156.770 150.713 1.00 41.80  ? 244  MET A O     1 
ATOM   1966  C  CB    . MET A 1 244  ? 136.139 155.877 153.858 1.00 37.46  ? 244  MET A CB    1 
ATOM   1967  C  CG    . MET A 1 244  ? 137.511 155.879 153.175 1.00 43.05  ? 244  MET A CG    1 
ATOM   1968  S  SD    . MET A 1 244  ? 137.770 154.650 151.870 1.00 70.68  ? 244  MET A SD    1 
ATOM   1969  C  CE    . MET A 1 244  ? 139.531 154.368 151.998 1.00 60.78  ? 244  MET A CE    1 
ATOM   1970  N  N     . MET A 1 245  ? 134.546 154.771 151.367 1.00 43.15  ? 245  MET A N     1 
ATOM   1971  C  CA    . MET A 1 245  ? 134.529 154.248 150.003 1.00 41.61  ? 245  MET A CA    1 
ATOM   1972  C  C     . MET A 1 245  ? 133.582 155.044 149.117 1.00 43.72  ? 245  MET A C     1 
ATOM   1973  O  O     . MET A 1 245  ? 133.884 155.297 147.945 1.00 49.24  ? 245  MET A O     1 
ATOM   1974  C  CB    . MET A 1 245  ? 134.139 152.773 150.005 1.00 43.47  ? 245  MET A CB    1 
ATOM   1975  C  CG    . MET A 1 245  ? 135.317 151.828 150.108 1.00 46.19  ? 245  MET A CG    1 
ATOM   1976  S  SD    . MET A 1 245  ? 134.862 150.197 150.719 1.00 55.29  ? 245  MET A SD    1 
ATOM   1977  C  CE    . MET A 1 245  ? 133.190 150.045 150.104 1.00 47.21  ? 245  MET A CE    1 
ATOM   1978  N  N     . LYS A 1 246  ? 132.422 155.429 149.654 1.00 42.39  ? 246  LYS A N     1 
ATOM   1979  C  CA    . LYS A 1 246  ? 131.471 156.222 148.880 1.00 40.82  ? 246  LYS A CA    1 
ATOM   1980  C  C     . LYS A 1 246  ? 132.077 157.555 148.449 1.00 40.74  ? 246  LYS A C     1 
ATOM   1981  O  O     . LYS A 1 246  ? 131.978 157.943 147.275 1.00 41.99  ? 246  LYS A O     1 
ATOM   1982  C  CB    . LYS A 1 246  ? 130.204 156.437 149.707 1.00 40.99  ? 246  LYS A CB    1 
ATOM   1983  C  CG    . LYS A 1 246  ? 129.024 156.999 148.949 1.00 46.38  ? 246  LYS A CG    1 
ATOM   1984  C  CD    . LYS A 1 246  ? 128.292 158.018 149.800 1.00 50.64  ? 246  LYS A CD    1 
ATOM   1985  C  CE    . LYS A 1 246  ? 127.050 158.541 149.103 1.00 57.88  ? 246  LYS A CE    1 
ATOM   1986  N  NZ    . LYS A 1 246  ? 126.428 159.666 149.852 1.00 60.57  ? 246  LYS A NZ    1 
ATOM   1987  N  N     . TYR A 1 247  ? 132.733 158.258 149.378 1.00 41.69  ? 247  TYR A N     1 
ATOM   1988  C  CA    . TYR A 1 247  ? 133.358 159.529 149.014 1.00 38.14  ? 247  TYR A CA    1 
ATOM   1989  C  C     . TYR A 1 247  ? 134.453 159.332 147.976 1.00 40.40  ? 247  TYR A C     1 
ATOM   1990  O  O     . TYR A 1 247  ? 134.577 160.130 147.039 1.00 41.67  ? 247  TYR A O     1 
ATOM   1991  C  CB    . TYR A 1 247  ? 133.934 160.227 150.243 1.00 36.90  ? 247  TYR A CB    1 
ATOM   1992  C  CG    . TYR A 1 247  ? 132.913 160.609 151.277 1.00 38.39  ? 247  TYR A CG    1 
ATOM   1993  C  CD1   . TYR A 1 247  ? 131.648 161.037 150.906 1.00 38.47  ? 247  TYR A CD1   1 
ATOM   1994  C  CD2   . TYR A 1 247  ? 133.220 160.560 152.625 1.00 37.36  ? 247  TYR A CD2   1 
ATOM   1995  C  CE1   . TYR A 1 247  ? 130.715 161.391 151.854 1.00 38.93  ? 247  TYR A CE1   1 
ATOM   1996  C  CE2   . TYR A 1 247  ? 132.296 160.915 153.578 1.00 36.17  ? 247  TYR A CE2   1 
ATOM   1997  C  CZ    . TYR A 1 247  ? 131.046 161.330 153.189 1.00 39.29  ? 247  TYR A CZ    1 
ATOM   1998  O  OH    . TYR A 1 247  ? 130.123 161.683 154.141 1.00 44.36  ? 247  TYR A OH    1 
ATOM   1999  N  N     . ARG A 1 248  ? 135.260 158.281 148.128 1.00 42.73  ? 248  ARG A N     1 
ATOM   2000  C  CA    . ARG A 1 248  ? 136.339 158.043 147.174 1.00 41.52  ? 248  ARG A CA    1 
ATOM   2001  C  C     . ARG A 1 248  ? 135.793 157.759 145.778 1.00 41.86  ? 248  ARG A C     1 
ATOM   2002  O  O     . ARG A 1 248  ? 136.315 158.279 144.781 1.00 42.43  ? 248  ARG A O     1 
ATOM   2003  C  CB    . ARG A 1 248  ? 137.208 156.890 147.669 1.00 42.91  ? 248  ARG A CB    1 
ATOM   2004  C  CG    . ARG A 1 248  ? 138.020 156.186 146.608 1.00 48.16  ? 248  ARG A CG    1 
ATOM   2005  C  CD    . ARG A 1 248  ? 138.879 155.120 147.252 1.00 53.18  ? 248  ARG A CD    1 
ATOM   2006  N  NE    . ARG A 1 248  ? 138.180 153.841 147.272 1.00 58.88  ? 248  ARG A NE    1 
ATOM   2007  C  CZ    . ARG A 1 248  ? 138.582 152.772 147.945 1.00 58.09  ? 248  ARG A CZ    1 
ATOM   2008  N  NH1   . ARG A 1 248  ? 139.678 152.793 148.686 1.00 54.05  ? 248  ARG A NH1   1 
ATOM   2009  N  NH2   . ARG A 1 248  ? 137.862 151.656 147.877 1.00 52.22  ? 248  ARG A NH2   1 
ATOM   2010  N  N     . ASP A 1 249  ? 134.735 156.948 145.687 1.00 44.48  ? 249  ASP A N     1 
ATOM   2011  C  CA    . ASP A 1 249  ? 134.142 156.657 144.385 1.00 44.17  ? 249  ASP A CA    1 
ATOM   2012  C  C     . ASP A 1 249  ? 133.569 157.912 143.744 1.00 46.51  ? 249  ASP A C     1 
ATOM   2013  O  O     . ASP A 1 249  ? 133.698 158.106 142.531 1.00 47.74  ? 249  ASP A O     1 
ATOM   2014  C  CB    . ASP A 1 249  ? 133.064 155.581 144.514 1.00 46.42  ? 249  ASP A CB    1 
ATOM   2015  C  CG    . ASP A 1 249  ? 133.579 154.316 145.168 1.00 58.06  ? 249  ASP A CG    1 
ATOM   2016  O  OD1   . ASP A 1 249  ? 134.814 154.172 145.294 1.00 55.17  ? 249  ASP A OD1   1 
ATOM   2017  O  OD2   . ASP A 1 249  ? 132.751 153.469 145.563 1.00 61.17  ? 249  ASP A OD2   1 
ATOM   2018  N  N     . GLN A 1 250  ? 132.925 158.776 144.533 1.00 44.73  ? 250  GLN A N     1 
ATOM   2019  C  CA    . GLN A 1 250  ? 132.438 160.026 143.953 1.00 40.60  ? 250  GLN A CA    1 
ATOM   2020  C  C     . GLN A 1 250  ? 133.590 160.899 143.468 1.00 43.81  ? 250  GLN A C     1 
ATOM   2021  O  O     . GLN A 1 250  ? 133.501 161.520 142.403 1.00 44.74  ? 250  GLN A O     1 
ATOM   2022  C  CB    . GLN A 1 250  ? 131.574 160.794 144.949 1.00 40.12  ? 250  GLN A CB    1 
ATOM   2023  C  CG    . GLN A 1 250  ? 130.193 160.215 145.161 1.00 47.76  ? 250  GLN A CG    1 
ATOM   2024  C  CD    . GLN A 1 250  ? 129.457 160.892 146.297 1.00 51.82  ? 250  GLN A CD    1 
ATOM   2025  O  OE1   . GLN A 1 250  ? 128.800 160.236 147.101 1.00 50.31  ? 250  GLN A OE1   1 
ATOM   2026  N  NE2   . GLN A 1 250  ? 129.566 162.214 146.370 1.00 45.04  ? 250  GLN A NE2   1 
ATOM   2027  N  N     . ARG A 1 251  ? 134.683 160.959 144.232 1.00 47.53  ? 251  ARG A N     1 
ATOM   2028  C  CA    . ARG A 1 251  ? 135.797 161.830 143.865 1.00 42.92  ? 251  ARG A CA    1 
ATOM   2029  C  C     . ARG A 1 251  ? 136.554 161.326 142.643 1.00 43.13  ? 251  ARG A C     1 
ATOM   2030  O  O     . ARG A 1 251  ? 137.189 162.122 141.943 1.00 44.43  ? 251  ARG A O     1 
ATOM   2031  C  CB    . ARG A 1 251  ? 136.762 161.972 145.040 1.00 41.21  ? 251  ARG A CB    1 
ATOM   2032  C  CG    . ARG A 1 251  ? 137.867 162.982 144.816 1.00 40.07  ? 251  ARG A CG    1 
ATOM   2033  C  CD    . ARG A 1 251  ? 138.825 162.985 145.980 1.00 41.55  ? 251  ARG A CD    1 
ATOM   2034  N  NE    . ARG A 1 251  ? 139.395 161.659 146.181 1.00 46.66  ? 251  ARG A NE    1 
ATOM   2035  C  CZ    . ARG A 1 251  ? 140.632 161.427 146.592 1.00 51.85  ? 251  ARG A CZ    1 
ATOM   2036  N  NH1   . ARG A 1 251  ? 141.474 162.416 146.843 1.00 52.22  ? 251  ARG A NH1   1 
ATOM   2037  N  NH2   . ARG A 1 251  ? 141.039 160.171 146.744 1.00 53.27  ? 251  ARG A NH2   1 
ATOM   2038  N  N     . ALA A 1 252  ? 136.503 160.018 142.374 1.00 43.42  ? 252  ALA A N     1 
ATOM   2039  C  CA    . ALA A 1 252  ? 137.388 159.426 141.371 1.00 40.58  ? 252  ALA A CA    1 
ATOM   2040  C  C     . ALA A 1 252  ? 137.283 160.091 139.999 1.00 40.27  ? 252  ALA A C     1 
ATOM   2041  O  O     . ALA A 1 252  ? 138.260 160.094 139.243 1.00 39.16  ? 252  ALA A O     1 
ATOM   2042  C  CB    . ALA A 1 252  ? 137.102 157.931 141.244 1.00 42.81  ? 252  ALA A CB    1 
ATOM   2043  N  N     . GLY A 1 253  ? 136.122 160.655 139.651 1.00 41.76  ? 253  GLY A N     1 
ATOM   2044  C  CA    . GLY A 1 253  ? 135.891 161.085 138.279 1.00 36.39  ? 253  GLY A CA    1 
ATOM   2045  C  C     . GLY A 1 253  ? 136.498 162.417 137.882 1.00 40.42  ? 253  GLY A C     1 
ATOM   2046  O  O     . GLY A 1 253  ? 136.743 162.637 136.692 1.00 39.23  ? 253  GLY A O     1 
ATOM   2047  N  N     . LYS A 1 254  ? 136.740 163.316 138.838 1.00 45.08  ? 254  LYS A N     1 
ATOM   2048  C  CA    . LYS A 1 254  ? 137.203 164.662 138.506 1.00 42.53  ? 254  LYS A CA    1 
ATOM   2049  C  C     . LYS A 1 254  ? 138.700 164.708 138.231 1.00 39.20  ? 254  LYS A C     1 
ATOM   2050  O  O     . LYS A 1 254  ? 139.177 165.595 137.504 1.00 42.85  ? 254  LYS A O     1 
ATOM   2051  C  CB    . LYS A 1 254  ? 136.866 165.625 139.643 1.00 44.00  ? 254  LYS A CB    1 
ATOM   2052  C  CG    . LYS A 1 254  ? 135.386 165.881 139.833 1.00 48.18  ? 254  LYS A CG    1 
ATOM   2053  C  CD    . LYS A 1 254  ? 134.817 164.924 140.870 1.00 48.77  ? 254  LYS A CD    1 
ATOM   2054  C  CE    . LYS A 1 254  ? 133.406 165.300 141.274 1.00 50.01  ? 254  LYS A CE    1 
ATOM   2055  N  NZ    . LYS A 1 254  ? 132.447 165.193 140.142 1.00 57.39  ? 254  LYS A NZ    1 
ATOM   2056  N  N     . ILE A 1 255  ? 139.447 163.766 138.805 1.00 36.79  ? 255  ILE A N     1 
ATOM   2057  C  CA    . ILE A 1 255  ? 140.899 163.797 138.712 1.00 43.10  ? 255  ILE A CA    1 
ATOM   2058  C  C     . ILE A 1 255  ? 141.345 163.551 137.278 1.00 42.06  ? 255  ILE A C     1 
ATOM   2059  O  O     . ILE A 1 255  ? 142.312 164.156 136.803 1.00 44.97  ? 255  ILE A O     1 
ATOM   2060  C  CB    . ILE A 1 255  ? 141.505 162.773 139.690 1.00 42.71  ? 255  ILE A CB    1 
ATOM   2061  C  CG1   . ILE A 1 255  ? 141.264 163.218 141.132 1.00 38.93  ? 255  ILE A CG1   1 
ATOM   2062  C  CG2   . ILE A 1 255  ? 142.994 162.597 139.445 1.00 36.98  ? 255  ILE A CG2   1 
ATOM   2063  C  CD1   . ILE A 1 255  ? 141.257 162.085 142.122 1.00 38.61  ? 255  ILE A CD1   1 
ATOM   2064  N  N     . SER A 1 256  ? 140.642 162.669 136.563 1.00 35.51  ? 256  SER A N     1 
ATOM   2065  C  CA    . SER A 1 256  ? 140.982 162.396 135.170 1.00 38.42  ? 256  SER A CA    1 
ATOM   2066  C  C     . SER A 1 256  ? 140.826 163.641 134.305 1.00 42.16  ? 256  SER A C     1 
ATOM   2067  O  O     . SER A 1 256  ? 141.689 163.940 133.469 1.00 48.70  ? 256  SER A O     1 
ATOM   2068  C  CB    . SER A 1 256  ? 140.109 161.264 134.636 1.00 45.53  ? 256  SER A CB    1 
ATOM   2069  O  OG    . SER A 1 256  ? 140.509 160.016 135.171 1.00 55.95  ? 256  SER A OG    1 
ATOM   2070  N  N     . GLU A 1 257  ? 139.732 164.383 134.495 1.00 39.96  ? 257  GLU A N     1 
ATOM   2071  C  CA    . GLU A 1 257  ? 139.518 165.595 133.714 1.00 40.12  ? 257  GLU A CA    1 
ATOM   2072  C  C     . GLU A 1 257  ? 140.561 166.651 134.049 1.00 38.45  ? 257  GLU A C     1 
ATOM   2073  O  O     . GLU A 1 257  ? 141.088 167.323 133.147 1.00 40.52  ? 257  GLU A O     1 
ATOM   2074  C  CB    . GLU A 1 257  ? 138.111 166.136 133.976 1.00 40.32  ? 257  GLU A CB    1 
ATOM   2075  C  CG    . GLU A 1 257  ? 137.592 167.207 133.007 1.00 49.80  ? 257  GLU A CG    1 
ATOM   2076  C  CD    . GLU A 1 257  ? 138.214 167.151 131.618 1.00 56.89  ? 257  GLU A CD    1 
ATOM   2077  O  OE1   . GLU A 1 257  ? 138.566 168.222 131.084 1.00 54.05  ? 257  GLU A OE1   1 
ATOM   2078  O  OE2   . GLU A 1 257  ? 138.284 166.051 131.027 1.00 56.20  ? 257  GLU A OE2   1 
ATOM   2079  N  N     . ARG A 1 258  ? 140.905 166.779 135.331 1.00 36.00  ? 258  ARG A N     1 
ATOM   2080  C  CA    . ARG A 1 258  ? 141.958 167.711 135.719 1.00 36.37  ? 258  ARG A CA    1 
ATOM   2081  C  C     . ARG A 1 258  ? 143.282 167.345 135.059 1.00 37.68  ? 258  ARG A C     1 
ATOM   2082  O  O     . ARG A 1 258  ? 143.997 168.215 134.545 1.00 40.24  ? 258  ARG A O     1 
ATOM   2083  C  CB    . ARG A 1 258  ? 142.100 167.723 137.239 1.00 36.53  ? 258  ARG A CB    1 
ATOM   2084  C  CG    . ARG A 1 258  ? 143.210 168.605 137.752 1.00 39.03  ? 258  ARG A CG    1 
ATOM   2085  C  CD    . ARG A 1 258  ? 143.270 168.566 139.263 1.00 41.10  ? 258  ARG A CD    1 
ATOM   2086  N  NE    . ARG A 1 258  ? 143.688 167.259 139.757 1.00 47.39  ? 258  ARG A NE    1 
ATOM   2087  C  CZ    . ARG A 1 258  ? 144.946 166.843 139.812 1.00 46.91  ? 258  ARG A CZ    1 
ATOM   2088  N  NH1   . ARG A 1 258  ? 145.946 167.607 139.404 1.00 42.10  ? 258  ARG A NH1   1 
ATOM   2089  N  NH2   . ARG A 1 258  ? 145.208 165.631 140.290 1.00 41.67  ? 258  ARG A NH2   1 
ATOM   2090  N  N     . LEU A 1 259  ? 143.618 166.052 135.056 1.00 38.17  ? 259  LEU A N     1 
ATOM   2091  C  CA    . LEU A 1 259  ? 144.885 165.601 134.491 1.00 39.64  ? 259  LEU A CA    1 
ATOM   2092  C  C     . LEU A 1 259  ? 144.950 165.847 132.990 1.00 40.52  ? 259  LEU A C     1 
ATOM   2093  O  O     . LEU A 1 259  ? 145.982 166.299 132.473 1.00 41.34  ? 259  LEU A O     1 
ATOM   2094  C  CB    . LEU A 1 259  ? 145.095 164.119 134.797 1.00 37.81  ? 259  LEU A CB    1 
ATOM   2095  C  CG    . LEU A 1 259  ? 145.489 163.775 136.233 1.00 36.43  ? 259  LEU A CG    1 
ATOM   2096  C  CD1   . LEU A 1 259  ? 145.534 162.272 136.437 1.00 35.54  ? 259  LEU A CD1   1 
ATOM   2097  C  CD2   . LEU A 1 259  ? 146.827 164.404 136.577 1.00 39.29  ? 259  LEU A CD2   1 
ATOM   2098  N  N     . VAL A 1 260  ? 143.863 165.560 132.269 1.00 40.79  ? 260  VAL A N     1 
ATOM   2099  C  CA    . VAL A 1 260  ? 143.901 165.764 130.824 1.00 38.67  ? 260  VAL A CA    1 
ATOM   2100  C  C     . VAL A 1 260  ? 144.014 167.249 130.496 1.00 38.53  ? 260  VAL A C     1 
ATOM   2101  O  O     . VAL A 1 260  ? 144.771 167.637 129.594 1.00 39.61  ? 260  VAL A O     1 
ATOM   2102  C  CB    . VAL A 1 260  ? 142.693 165.104 130.126 1.00 35.52  ? 260  VAL A CB    1 
ATOM   2103  C  CG1   . VAL A 1 260  ? 142.663 163.619 130.411 1.00 41.05  ? 260  VAL A CG1   1 
ATOM   2104  C  CG2   . VAL A 1 260  ? 141.391 165.745 130.528 1.00 38.74  ? 260  VAL A CG2   1 
ATOM   2105  N  N     . ILE A 1 261  ? 143.306 168.110 131.237 1.00 38.85  ? 261  ILE A N     1 
ATOM   2106  C  CA    . ILE A 1 261  ? 143.420 169.541 130.965 1.00 37.47  ? 261  ILE A CA    1 
ATOM   2107  C  C     . ILE A 1 261  ? 144.835 170.031 131.248 1.00 36.82  ? 261  ILE A C     1 
ATOM   2108  O  O     . ILE A 1 261  ? 145.403 170.811 130.472 1.00 37.40  ? 261  ILE A O     1 
ATOM   2109  C  CB    . ILE A 1 261  ? 142.380 170.335 131.772 1.00 39.37  ? 261  ILE A CB    1 
ATOM   2110  C  CG1   . ILE A 1 261  ? 140.988 170.128 131.184 1.00 42.20  ? 261  ILE A CG1   1 
ATOM   2111  C  CG2   . ILE A 1 261  ? 142.730 171.813 131.780 1.00 42.68  ? 261  ILE A CG2   1 
ATOM   2112  C  CD1   . ILE A 1 261  ? 140.578 171.182 130.181 1.00 46.09  ? 261  ILE A CD1   1 
ATOM   2113  N  N     . THR A 1 262  ? 145.429 169.579 132.355 1.00 35.89  ? 262  THR A N     1 
ATOM   2114  C  CA    . THR A 1 262  ? 146.773 170.023 132.708 1.00 32.63  ? 262  THR A CA    1 
ATOM   2115  C  C     . THR A 1 262  ? 147.793 169.594 131.661 1.00 34.70  ? 262  THR A C     1 
ATOM   2116  O  O     . THR A 1 262  ? 148.636 170.397 131.239 1.00 32.36  ? 262  THR A O     1 
ATOM   2117  C  CB    . THR A 1 262  ? 147.156 169.472 134.078 1.00 34.41  ? 262  THR A CB    1 
ATOM   2118  O  OG1   . THR A 1 262  ? 146.195 169.901 135.046 1.00 38.86  ? 262  THR A OG1   1 
ATOM   2119  C  CG2   . THR A 1 262  ? 148.521 169.976 134.489 1.00 34.76  ? 262  THR A CG2   1 
ATOM   2120  N  N     . SER A 1 263  ? 147.722 168.336 131.217 1.00 36.40  ? 263  SER A N     1 
ATOM   2121  C  CA    . SER A 1 263  ? 148.674 167.863 130.218 1.00 35.92  ? 263  SER A CA    1 
ATOM   2122  C  C     . SER A 1 263  ? 148.501 168.608 128.900 1.00 39.89  ? 263  SER A C     1 
ATOM   2123  O  O     . SER A 1 263  ? 149.493 168.999 128.267 1.00 40.80  ? 263  SER A O     1 
ATOM   2124  C  CB    . SER A 1 263  ? 148.519 166.358 130.010 1.00 37.17  ? 263  SER A CB    1 
ATOM   2125  O  OG    . SER A 1 263  ? 147.350 166.057 129.272 1.00 42.35  ? 263  SER A OG    1 
ATOM   2126  N  N     . GLU A 1 264  ? 147.251 168.834 128.480 1.00 40.80  ? 264  GLU A N     1 
ATOM   2127  C  CA    . GLU A 1 264  ? 147.009 169.569 127.244 1.00 36.40  ? 264  GLU A CA    1 
ATOM   2128  C  C     . GLU A 1 264  ? 147.575 170.980 127.323 1.00 32.92  ? 264  GLU A C     1 
ATOM   2129  O  O     . GLU A 1 264  ? 148.210 171.459 126.378 1.00 35.02  ? 264  GLU A O     1 
ATOM   2130  C  CB    . GLU A 1 264  ? 145.512 169.615 126.941 1.00 39.50  ? 264  GLU A CB    1 
ATOM   2131  C  CG    . GLU A 1 264  ? 144.958 168.346 126.336 1.00 47.97  ? 264  GLU A CG    1 
ATOM   2132  C  CD    . GLU A 1 264  ? 143.451 168.390 126.172 1.00 57.41  ? 264  GLU A CD    1 
ATOM   2133  O  OE1   . GLU A 1 264  ? 142.811 169.279 126.773 1.00 57.10  ? 264  GLU A OE1   1 
ATOM   2134  O  OE2   . GLU A 1 264  ? 142.908 167.535 125.443 1.00 56.36  ? 264  GLU A OE2   1 
ATOM   2135  N  N     . MET A 1 265  ? 147.352 171.666 128.445 1.00 35.50  ? 265  MET A N     1 
ATOM   2136  C  CA    . MET A 1 265  ? 147.814 173.046 128.549 1.00 33.93  ? 265  MET A CA    1 
ATOM   2137  C  C     . MET A 1 265  ? 149.330 173.130 128.654 1.00 31.76  ? 265  MET A C     1 
ATOM   2138  O  O     . MET A 1 265  ? 149.922 174.117 128.208 1.00 30.39  ? 265  MET A O     1 
ATOM   2139  C  CB    . MET A 1 265  ? 147.158 173.744 129.740 1.00 33.83  ? 265  MET A CB    1 
ATOM   2140  C  CG    . MET A 1 265  ? 147.948 173.674 131.031 1.00 36.13  ? 265  MET A CG    1 
ATOM   2141  S  SD    . MET A 1 265  ? 147.295 174.785 132.278 1.00 44.94  ? 265  MET A SD    1 
ATOM   2142  C  CE    . MET A 1 265  ? 145.637 174.142 132.427 1.00 40.58  ? 265  MET A CE    1 
ATOM   2143  N  N     . ILE A 1 266  ? 149.977 172.123 129.241 1.00 35.41  ? 266  ILE A N     1 
ATOM   2144  C  CA    . ILE A 1 266  ? 151.428 172.208 129.362 1.00 35.56  ? 266  ILE A CA    1 
ATOM   2145  C  C     . ILE A 1 266  ? 152.116 171.842 128.054 1.00 35.64  ? 266  ILE A C     1 
ATOM   2146  O  O     . ILE A 1 266  ? 153.142 172.438 127.706 1.00 35.20  ? 266  ILE A O     1 
ATOM   2147  C  CB    . ILE A 1 266  ? 151.930 171.341 130.528 1.00 37.32  ? 266  ILE A CB    1 
ATOM   2148  C  CG1   . ILE A 1 266  ? 151.458 171.924 131.859 1.00 37.50  ? 266  ILE A CG1   1 
ATOM   2149  C  CG2   . ILE A 1 266  ? 153.440 171.252 130.514 1.00 33.32  ? 266  ILE A CG2   1 
ATOM   2150  C  CD1   . ILE A 1 266  ? 151.631 170.992 133.021 1.00 32.45  ? 266  ILE A CD1   1 
ATOM   2151  N  N     . GLU A 1 267  ? 151.576 170.888 127.292 1.00 37.27  ? 267  GLU A N     1 
ATOM   2152  C  CA    . GLU A 1 267  ? 152.233 170.537 126.036 1.00 35.84  ? 267  GLU A CA    1 
ATOM   2153  C  C     . GLU A 1 267  ? 152.068 171.607 124.963 1.00 36.00  ? 267  GLU A C     1 
ATOM   2154  O  O     . GLU A 1 267  ? 152.837 171.618 123.998 1.00 34.98  ? 267  GLU A O     1 
ATOM   2155  C  CB    . GLU A 1 267  ? 151.711 169.203 125.508 1.00 36.60  ? 267  GLU A CB    1 
ATOM   2156  C  CG    . GLU A 1 267  ? 150.346 169.279 124.868 1.00 43.75  ? 267  GLU A CG    1 
ATOM   2157  C  CD    . GLU A 1 267  ? 150.195 168.293 123.732 1.00 51.30  ? 267  GLU A CD    1 
ATOM   2158  O  OE1   . GLU A 1 267  ? 151.164 168.133 122.960 1.00 52.22  ? 267  GLU A OE1   1 
ATOM   2159  O  OE2   . GLU A 1 267  ? 149.114 167.676 123.616 1.00 49.70  ? 267  GLU A OE2   1 
ATOM   2160  N  N     . ASN A 1 268  ? 151.088 172.499 125.107 1.00 33.90  ? 268  ASN A N     1 
ATOM   2161  C  CA    . ASN A 1 268  ? 150.881 173.621 124.198 1.00 29.32  ? 268  ASN A CA    1 
ATOM   2162  C  C     . ASN A 1 268  ? 151.215 174.949 124.866 1.00 31.59  ? 268  ASN A C     1 
ATOM   2163  O  O     . ASN A 1 268  ? 150.521 175.945 124.659 1.00 30.39  ? 268  ASN A O     1 
ATOM   2164  C  CB    . ASN A 1 268  ? 149.443 173.643 123.684 1.00 27.94  ? 268  ASN A CB    1 
ATOM   2165  C  CG    . ASN A 1 268  ? 149.129 172.479 122.771 1.00 38.03  ? 268  ASN A CG    1 
ATOM   2166  O  OD1   . ASN A 1 268  ? 149.597 172.422 121.636 1.00 48.15  ? 268  ASN A OD1   1 
ATOM   2167  N  ND2   . ASN A 1 268  ? 148.332 171.541 123.263 1.00 36.34  ? 268  ASN A ND2   1 
ATOM   2168  N  N     . ILE A 1 269  ? 152.270 174.968 125.683 1.00 32.60  ? 269  ILE A N     1 
ATOM   2169  C  CA    . ILE A 1 269  ? 152.569 176.131 126.513 1.00 30.69  ? 269  ILE A CA    1 
ATOM   2170  C  C     . ILE A 1 269  ? 152.911 177.356 125.673 1.00 32.08  ? 269  ILE A C     1 
ATOM   2171  O  O     . ILE A 1 269  ? 152.659 178.491 126.093 1.00 31.54  ? 269  ILE A O     1 
ATOM   2172  C  CB    . ILE A 1 269  ? 153.694 175.783 127.510 1.00 32.00  ? 269  ILE A CB    1 
ATOM   2173  C  CG1   . ILE A 1 269  ? 153.928 176.931 128.494 1.00 29.77  ? 269  ILE A CG1   1 
ATOM   2174  C  CG2   . ILE A 1 269  ? 154.967 175.411 126.778 1.00 34.19  ? 269  ILE A CG2   1 
ATOM   2175  C  CD1   . ILE A 1 269  ? 152.690 177.367 129.229 1.00 30.68  ? 269  ILE A CD1   1 
ATOM   2176  N  N     . GLN A 1 270  ? 153.489 177.161 124.487 1.00 31.88  ? 270  GLN A N     1 
ATOM   2177  C  CA    . GLN A 1 270  ? 153.889 178.309 123.678 1.00 30.88  ? 270  GLN A CA    1 
ATOM   2178  C  C     . GLN A 1 270  ? 152.675 179.062 123.149 1.00 31.53  ? 270  GLN A C     1 
ATOM   2179  O  O     . GLN A 1 270  ? 152.667 180.299 123.121 1.00 33.04  ? 270  GLN A O     1 
ATOM   2180  C  CB    . GLN A 1 270  ? 154.792 177.853 122.533 1.00 35.21  ? 270  GLN A CB    1 
ATOM   2181  C  CG    . GLN A 1 270  ? 155.454 178.987 121.772 1.00 41.39  ? 270  GLN A CG    1 
ATOM   2182  C  CD    . GLN A 1 270  ? 156.479 178.491 120.773 1.00 43.95  ? 270  GLN A CD    1 
ATOM   2183  O  OE1   . GLN A 1 270  ? 156.406 177.356 120.303 1.00 45.87  ? 270  GLN A OE1   1 
ATOM   2184  N  NE2   . GLN A 1 270  ? 157.447 179.338 120.449 1.00 41.33  ? 270  GLN A NE2   1 
ATOM   2185  N  N     . SER A 1 271  ? 151.627 178.336 122.752 1.00 31.15  ? 271  SER A N     1 
ATOM   2186  C  CA    . SER A 1 271  ? 150.386 178.984 122.338 1.00 24.55  ? 271  SER A CA    1 
ATOM   2187  C  C     . SER A 1 271  ? 149.723 179.701 123.505 1.00 26.15  ? 271  SER A C     1 
ATOM   2188  O  O     . SER A 1 271  ? 149.163 180.789 123.334 1.00 26.54  ? 271  SER A O     1 
ATOM   2189  C  CB    . SER A 1 271  ? 149.432 177.954 121.735 1.00 25.74  ? 271  SER A CB    1 
ATOM   2190  O  OG    . SER A 1 271  ? 149.831 177.587 120.429 1.00 36.97  ? 271  SER A OG    1 
ATOM   2191  N  N     . VAL A 1 272  ? 149.766 179.101 124.696 1.00 26.94  ? 272  VAL A N     1 
ATOM   2192  C  CA    . VAL A 1 272  ? 149.186 179.729 125.880 1.00 25.64  ? 272  VAL A CA    1 
ATOM   2193  C  C     . VAL A 1 272  ? 149.914 181.027 126.201 1.00 28.83  ? 272  VAL A C     1 
ATOM   2194  O  O     . VAL A 1 272  ? 149.291 182.039 126.545 1.00 31.38  ? 272  VAL A O     1 
ATOM   2195  C  CB    . VAL A 1 272  ? 149.220 178.747 127.066 1.00 27.19  ? 272  VAL A CB    1 
ATOM   2196  C  CG1   . VAL A 1 272  ? 148.895 179.458 128.368 1.00 32.15  ? 272  VAL A CG1   1 
ATOM   2197  C  CG2   . VAL A 1 272  ? 148.260 177.593 126.827 1.00 25.85  ? 272  VAL A CG2   1 
ATOM   2198  N  N     . LYS A 1 273  ? 151.243 181.017 126.098 1.00 28.22  ? 273  LYS A N     1 
ATOM   2199  C  CA    . LYS A 1 273  ? 152.021 182.229 126.330 1.00 26.35  ? 273  LYS A CA    1 
ATOM   2200  C  C     . LYS A 1 273  ? 151.728 183.287 125.274 1.00 30.11  ? 273  LYS A C     1 
ATOM   2201  O  O     . LYS A 1 273  ? 151.603 184.473 125.597 1.00 34.82  ? 273  LYS A O     1 
ATOM   2202  C  CB    . LYS A 1 273  ? 153.512 181.896 126.355 1.00 29.64  ? 273  LYS A CB    1 
ATOM   2203  C  CG    . LYS A 1 273  ? 153.995 181.245 127.637 1.00 34.67  ? 273  LYS A CG    1 
ATOM   2204  C  CD    . LYS A 1 273  ? 155.482 180.952 127.566 1.00 38.45  ? 273  LYS A CD    1 
ATOM   2205  C  CE    . LYS A 1 273  ? 155.988 180.326 128.851 1.00 35.86  ? 273  LYS A CE    1 
ATOM   2206  N  NZ    . LYS A 1 273  ? 155.847 181.245 130.008 1.00 39.12  ? 273  LYS A NZ    1 
ATOM   2207  N  N     . ALA A 1 274  ? 151.619 182.882 124.006 1.00 28.47  ? 274  ALA A N     1 
ATOM   2208  C  CA    . ALA A 1 274  ? 151.358 183.847 122.941 1.00 25.89  ? 274  ALA A CA    1 
ATOM   2209  C  C     . ALA A 1 274  ? 149.981 184.481 123.085 1.00 32.54  ? 274  ALA A C     1 
ATOM   2210  O  O     . ALA A 1 274  ? 149.822 185.686 122.863 1.00 34.93  ? 274  ALA A O     1 
ATOM   2211  C  CB    . ALA A 1 274  ? 151.496 183.175 121.577 1.00 27.53  ? 274  ALA A CB    1 
ATOM   2212  N  N     . TYR A 1 275  ? 148.973 183.688 123.453 1.00 32.83  ? 275  TYR A N     1 
ATOM   2213  C  CA    . TYR A 1 275  ? 147.630 184.214 123.657 1.00 26.04  ? 275  TYR A CA    1 
ATOM   2214  C  C     . TYR A 1 275  ? 147.472 184.972 124.968 1.00 30.55  ? 275  TYR A C     1 
ATOM   2215  O  O     . TYR A 1 275  ? 146.495 185.713 125.115 1.00 34.08  ? 275  TYR A O     1 
ATOM   2216  C  CB    . TYR A 1 275  ? 146.600 183.085 123.633 1.00 27.51  ? 275  TYR A CB    1 
ATOM   2217  C  CG    . TYR A 1 275  ? 146.304 182.486 122.279 1.00 29.96  ? 275  TYR A CG    1 
ATOM   2218  C  CD1   . TYR A 1 275  ? 146.088 183.292 121.174 1.00 30.86  ? 275  TYR A CD1   1 
ATOM   2219  C  CD2   . TYR A 1 275  ? 146.193 181.114 122.119 1.00 29.47  ? 275  TYR A CD2   1 
ATOM   2220  C  CE1   . TYR A 1 275  ? 145.798 182.747 119.942 1.00 28.39  ? 275  TYR A CE1   1 
ATOM   2221  C  CE2   . TYR A 1 275  ? 145.903 180.562 120.891 1.00 29.21  ? 275  TYR A CE2   1 
ATOM   2222  C  CZ    . TYR A 1 275  ? 145.706 181.383 119.807 1.00 33.98  ? 275  TYR A CZ    1 
ATOM   2223  O  OH    . TYR A 1 275  ? 145.414 180.840 118.579 1.00 42.48  ? 275  TYR A OH    1 
ATOM   2224  N  N     . CYS A 1 276  ? 148.397 184.798 125.915 1.00 31.52  ? 276  CYS A N     1 
ATOM   2225  C  CA    . CYS A 1 276  ? 148.265 185.337 127.272 1.00 33.07  ? 276  CYS A CA    1 
ATOM   2226  C  C     . CYS A 1 276  ? 147.024 184.767 127.960 1.00 37.27  ? 276  CYS A C     1 
ATOM   2227  O  O     . CYS A 1 276  ? 146.151 185.499 128.429 1.00 41.25  ? 276  CYS A O     1 
ATOM   2228  C  CB    . CYS A 1 276  ? 148.241 186.868 127.268 1.00 37.70  ? 276  CYS A CB    1 
ATOM   2229  S  SG    . CYS A 1 276  ? 149.756 187.653 126.673 1.00 45.29  ? 276  CYS A SG    1 
ATOM   2230  N  N     . TRP A 1 277  ? 146.948 183.436 128.004 1.00 34.03  ? 277  TRP A N     1 
ATOM   2231  C  CA    . TRP A 1 277  ? 145.813 182.716 128.569 1.00 34.85  ? 277  TRP A CA    1 
ATOM   2232  C  C     . TRP A 1 277  ? 146.110 182.062 129.910 1.00 38.60  ? 277  TRP A C     1 
ATOM   2233  O  O     . TRP A 1 277  ? 145.272 181.303 130.405 1.00 45.64  ? 277  TRP A O     1 
ATOM   2234  C  CB    . TRP A 1 277  ? 145.328 181.641 127.594 1.00 30.24  ? 277  TRP A CB    1 
ATOM   2235  C  CG    . TRP A 1 277  ? 144.484 182.151 126.487 1.00 30.06  ? 277  TRP A CG    1 
ATOM   2236  C  CD1   . TRP A 1 277  ? 144.157 183.447 126.235 1.00 31.46  ? 277  TRP A CD1   1 
ATOM   2237  C  CD2   . TRP A 1 277  ? 143.842 181.369 125.479 1.00 32.46  ? 277  TRP A CD2   1 
ATOM   2238  N  NE1   . TRP A 1 277  ? 143.353 183.523 125.125 1.00 30.62  ? 277  TRP A NE1   1 
ATOM   2239  C  CE2   . TRP A 1 277  ? 143.145 182.259 124.643 1.00 32.13  ? 277  TRP A CE2   1 
ATOM   2240  C  CE3   . TRP A 1 277  ? 143.790 180.001 125.200 1.00 32.60  ? 277  TRP A CE3   1 
ATOM   2241  C  CZ2   . TRP A 1 277  ? 142.405 181.827 123.549 1.00 29.14  ? 277  TRP A CZ2   1 
ATOM   2242  C  CZ3   . TRP A 1 277  ? 143.054 179.573 124.115 1.00 32.03  ? 277  TRP A CZ3   1 
ATOM   2243  C  CH2   . TRP A 1 277  ? 142.371 180.482 123.304 1.00 29.86  ? 277  TRP A CH2   1 
ATOM   2244  N  N     . GLU A 1 278  ? 147.273 182.329 130.503 1.00 39.08  ? 278  GLU A N     1 
ATOM   2245  C  CA    . GLU A 1 278  ? 147.717 181.582 131.677 1.00 38.79  ? 278  GLU A CA    1 
ATOM   2246  C  C     . GLU A 1 278  ? 146.718 181.675 132.828 1.00 38.77  ? 278  GLU A C     1 
ATOM   2247  O  O     . GLU A 1 278  ? 146.402 180.670 133.478 1.00 41.00  ? 278  GLU A O     1 
ATOM   2248  C  CB    . GLU A 1 278  ? 149.095 182.092 132.098 1.00 38.69  ? 278  GLU A CB    1 
ATOM   2249  C  CG    . GLU A 1 278  ? 150.156 181.860 131.032 1.00 41.45  ? 278  GLU A CG    1 
ATOM   2250  C  CD    . GLU A 1 278  ? 151.224 182.932 131.016 1.00 49.93  ? 278  GLU A CD    1 
ATOM   2251  O  OE1   . GLU A 1 278  ? 150.954 184.027 130.479 1.00 49.76  ? 278  GLU A OE1   1 
ATOM   2252  O  OE2   . GLU A 1 278  ? 152.332 182.681 131.531 1.00 50.33  ? 278  GLU A OE2   1 
ATOM   2253  N  N     . GLU A 1 279  ? 146.204 182.880 133.087 1.00 39.64  ? 279  GLU A N     1 
ATOM   2254  C  CA    . GLU A 1 279  ? 145.298 183.080 134.214 1.00 38.63  ? 279  GLU A CA    1 
ATOM   2255  C  C     . GLU A 1 279  ? 143.989 182.322 134.027 1.00 40.76  ? 279  GLU A C     1 
ATOM   2256  O  O     . GLU A 1 279  ? 143.449 181.760 134.986 1.00 43.66  ? 279  GLU A O     1 
ATOM   2257  C  CB    . GLU A 1 279  ? 145.040 184.572 134.412 1.00 40.11  ? 279  GLU A CB    1 
ATOM   2258  C  CG    . GLU A 1 279  ? 146.293 185.427 134.303 1.00 46.66  ? 279  GLU A CG    1 
ATOM   2259  C  CD    . GLU A 1 279  ? 146.458 186.068 132.936 1.00 54.95  ? 279  GLU A CD    1 
ATOM   2260  O  OE1   . GLU A 1 279  ? 145.587 186.875 132.548 1.00 55.00  ? 279  GLU A OE1   1 
ATOM   2261  O  OE2   . GLU A 1 279  ? 147.461 185.771 132.252 1.00 55.19  ? 279  GLU A OE2   1 
ATOM   2262  N  N     . ALA A 1 280  ? 143.468 182.284 132.799 1.00 41.50  ? 280  ALA A N     1 
ATOM   2263  C  CA    . ALA A 1 280  ? 142.225 181.563 132.543 1.00 36.33  ? 280  ALA A CA    1 
ATOM   2264  C  C     . ALA A 1 280  ? 142.398 180.068 132.781 1.00 36.19  ? 280  ALA A C     1 
ATOM   2265  O  O     . ALA A 1 280  ? 141.534 179.418 133.383 1.00 41.80  ? 280  ALA A O     1 
ATOM   2266  C  CB    . ALA A 1 280  ? 141.752 181.829 131.115 1.00 35.98  ? 280  ALA A CB    1 
ATOM   2267  N  N     . MET A 1 281  ? 143.514 179.506 132.313 1.00 32.95  ? 281  MET A N     1 
ATOM   2268  C  CA    . MET A 1 281  ? 143.777 178.087 132.520 1.00 37.01  ? 281  MET A CA    1 
ATOM   2269  C  C     . MET A 1 281  ? 143.934 177.775 134.002 1.00 38.75  ? 281  MET A C     1 
ATOM   2270  O  O     . MET A 1 281  ? 143.435 176.748 134.488 1.00 38.07  ? 281  MET A O     1 
ATOM   2271  C  CB    . MET A 1 281  ? 145.026 177.669 131.743 1.00 35.07  ? 281  MET A CB    1 
ATOM   2272  C  CG    . MET A 1 281  ? 145.050 178.127 130.290 1.00 35.26  ? 281  MET A CG    1 
ATOM   2273  S  SD    . MET A 1 281  ? 143.646 177.598 129.291 1.00 55.17  ? 281  MET A SD    1 
ATOM   2274  C  CE    . MET A 1 281  ? 143.899 175.829 129.245 1.00 39.62  ? 281  MET A CE    1 
ATOM   2275  N  N     . GLU A 1 282  ? 144.616 178.658 134.738 1.00 39.80  ? 282  GLU A N     1 
ATOM   2276  C  CA    . GLU A 1 282  ? 144.718 178.486 136.183 1.00 38.45  ? 282  GLU A CA    1 
ATOM   2277  C  C     . GLU A 1 282  ? 143.346 178.518 136.840 1.00 37.93  ? 282  GLU A C     1 
ATOM   2278  O  O     . GLU A 1 282  ? 143.079 177.748 137.768 1.00 39.98  ? 282  GLU A O     1 
ATOM   2279  C  CB    . GLU A 1 282  ? 145.620 179.560 136.786 1.00 37.47  ? 282  GLU A CB    1 
ATOM   2280  C  CG    . GLU A 1 282  ? 147.089 179.364 136.497 1.00 41.10  ? 282  GLU A CG    1 
ATOM   2281  C  CD    . GLU A 1 282  ? 147.962 180.313 137.286 1.00 48.21  ? 282  GLU A CD    1 
ATOM   2282  O  OE1   . GLU A 1 282  ? 148.131 180.084 138.501 1.00 47.55  ? 282  GLU A OE1   1 
ATOM   2283  O  OE2   . GLU A 1 282  ? 148.487 181.279 136.696 1.00 49.79  ? 282  GLU A OE2   1 
ATOM   2284  N  N     . LYS A 1 283  ? 142.465 179.405 136.374 1.00 38.32  ? 283  LYS A N     1 
ATOM   2285  C  CA    . LYS A 1 283  ? 141.117 179.475 136.927 1.00 38.90  ? 283  LYS A CA    1 
ATOM   2286  C  C     . LYS A 1 283  ? 140.345 178.182 136.695 1.00 40.81  ? 283  LYS A C     1 
ATOM   2287  O  O     . LYS A 1 283  ? 139.662 177.692 137.602 1.00 42.74  ? 283  LYS A O     1 
ATOM   2288  C  CB    . LYS A 1 283  ? 140.368 180.661 136.325 1.00 37.77  ? 283  LYS A CB    1 
ATOM   2289  C  CG    . LYS A 1 283  ? 139.101 181.028 137.066 1.00 44.06  ? 283  LYS A CG    1 
ATOM   2290  C  CD    . LYS A 1 283  ? 139.402 181.805 138.327 1.00 49.58  ? 283  LYS A CD    1 
ATOM   2291  C  CE    . LYS A 1 283  ? 138.257 181.677 139.319 1.00 48.66  ? 283  LYS A CE    1 
ATOM   2292  N  NZ    . LYS A 1 283  ? 138.347 180.418 140.105 1.00 43.88  ? 283  LYS A NZ    1 
ATOM   2293  N  N     . MET A 1 284  ? 140.450 177.606 135.495 1.00 39.85  ? 284  MET A N     1 
ATOM   2294  C  CA    . MET A 1 284  ? 139.780 176.329 135.244 1.00 38.53  ? 284  MET A CA    1 
ATOM   2295  C  C     . MET A 1 284  ? 140.332 175.221 136.137 1.00 39.98  ? 284  MET A C     1 
ATOM   2296  O  O     . MET A 1 284  ? 139.565 174.433 136.716 1.00 43.17  ? 284  MET A O     1 
ATOM   2297  C  CB    . MET A 1 284  ? 139.910 175.935 133.772 1.00 39.05  ? 284  MET A CB    1 
ATOM   2298  C  CG    . MET A 1 284  ? 139.787 177.077 132.787 1.00 45.60  ? 284  MET A CG    1 
ATOM   2299  S  SD    . MET A 1 284  ? 139.744 176.544 131.065 1.00 55.28  ? 284  MET A SD    1 
ATOM   2300  C  CE    . MET A 1 284  ? 140.743 175.063 131.150 1.00 47.12  ? 284  MET A CE    1 
ATOM   2301  N  N     . ILE A 1 285  ? 141.657 175.155 136.280 1.00 40.68  ? 285  ILE A N     1 
ATOM   2302  C  CA    . ILE A 1 285  ? 142.242 174.088 137.085 1.00 38.32  ? 285  ILE A CA    1 
ATOM   2303  C  C     . ILE A 1 285  ? 141.856 174.242 138.549 1.00 37.31  ? 285  ILE A C     1 
ATOM   2304  O  O     . ILE A 1 285  ? 141.554 173.256 139.230 1.00 41.13  ? 285  ILE A O     1 
ATOM   2305  C  CB    . ILE A 1 285  ? 143.768 174.038 136.898 1.00 36.33  ? 285  ILE A CB    1 
ATOM   2306  C  CG1   . ILE A 1 285  ? 144.096 173.583 135.484 1.00 40.51  ? 285  ILE A CG1   1 
ATOM   2307  C  CG2   . ILE A 1 285  ? 144.389 173.070 137.880 1.00 32.42  ? 285  ILE A CG2   1 
ATOM   2308  C  CD1   . ILE A 1 285  ? 143.617 172.186 135.199 1.00 39.39  ? 285  ILE A CD1   1 
ATOM   2309  N  N     . GLU A 1 286  ? 141.839 175.473 139.059 1.00 36.40  ? 286  GLU A N     1 
ATOM   2310  C  CA    . GLU A 1 286  ? 141.457 175.655 140.452 1.00 38.75  ? 286  GLU A CA    1 
ATOM   2311  C  C     . GLU A 1 286  ? 139.965 175.441 140.677 1.00 41.52  ? 286  GLU A C     1 
ATOM   2312  O  O     . GLU A 1 286  ? 139.578 174.990 141.761 1.00 45.33  ? 286  GLU A O     1 
ATOM   2313  C  CB    . GLU A 1 286  ? 141.899 177.031 140.948 1.00 43.28  ? 286  GLU A CB    1 
ATOM   2314  C  CG    . GLU A 1 286  ? 140.894 178.146 140.791 1.00 46.33  ? 286  GLU A CG    1 
ATOM   2315  C  CD    . GLU A 1 286  ? 141.427 179.466 141.310 1.00 52.98  ? 286  GLU A CD    1 
ATOM   2316  O  OE1   . GLU A 1 286  ? 142.369 180.015 140.700 1.00 49.26  ? 286  GLU A OE1   1 
ATOM   2317  O  OE2   . GLU A 1 286  ? 140.911 179.948 142.338 1.00 58.36  ? 286  GLU A OE2   1 
ATOM   2318  N  N     . ASN A 1 287  ? 139.123 175.691 139.669 1.00 41.61  ? 287  ASN A N     1 
ATOM   2319  C  CA    . ASN A 1 287  ? 137.720 175.305 139.792 1.00 39.42  ? 287  ASN A CA    1 
ATOM   2320  C  C     . ASN A 1 287  ? 137.580 173.795 139.903 1.00 39.68  ? 287  ASN A C     1 
ATOM   2321  O  O     . ASN A 1 287  ? 136.763 173.299 140.686 1.00 40.67  ? 287  ASN A O     1 
ATOM   2322  C  CB    . ASN A 1 287  ? 136.908 175.820 138.604 1.00 37.79  ? 287  ASN A CB    1 
ATOM   2323  C  CG    . ASN A 1 287  ? 136.590 177.294 138.705 1.00 44.61  ? 287  ASN A CG    1 
ATOM   2324  O  OD1   . ASN A 1 287  ? 136.734 177.903 139.764 1.00 48.49  ? 287  ASN A OD1   1 
ATOM   2325  N  ND2   . ASN A 1 287  ? 136.144 177.877 137.601 1.00 45.73  ? 287  ASN A ND2   1 
ATOM   2326  N  N     . LEU A 1 288  ? 138.362 173.048 139.124 1.00 40.32  ? 288  LEU A N     1 
ATOM   2327  C  CA    . LEU A 1 288  ? 138.320 171.592 139.254 1.00 37.95  ? 288  LEU A CA    1 
ATOM   2328  C  C     . LEU A 1 288  ? 138.838 171.133 140.616 1.00 40.66  ? 288  LEU A C     1 
ATOM   2329  O  O     . LEU A 1 288  ? 138.277 170.212 141.218 1.00 39.50  ? 288  LEU A O     1 
ATOM   2330  C  CB    . LEU A 1 288  ? 139.104 170.936 138.121 1.00 34.99  ? 288  LEU A CB    1 
ATOM   2331  C  CG    . LEU A 1 288  ? 138.353 170.880 136.791 1.00 35.88  ? 288  LEU A CG    1 
ATOM   2332  C  CD1   . LEU A 1 288  ? 139.305 170.613 135.643 1.00 39.95  ? 288  LEU A CD1   1 
ATOM   2333  C  CD2   . LEU A 1 288  ? 137.267 169.818 136.845 1.00 31.78  ? 288  LEU A CD2   1 
ATOM   2334  N  N     . ARG A 1 289  ? 139.911 171.757 141.111 1.00 40.24  ? 289  ARG A N     1 
ATOM   2335  C  CA    . ARG A 1 289  ? 140.481 171.372 142.403 1.00 35.92  ? 289  ARG A CA    1 
ATOM   2336  C  C     . ARG A 1 289  ? 139.500 171.613 143.546 1.00 40.60  ? 289  ARG A C     1 
ATOM   2337  O  O     . ARG A 1 289  ? 139.410 170.807 144.488 1.00 44.28  ? 289  ARG A O     1 
ATOM   2338  C  CB    . ARG A 1 289  ? 141.774 172.150 142.647 1.00 32.88  ? 289  ARG A CB    1 
ATOM   2339  C  CG    . ARG A 1 289  ? 142.964 171.657 141.857 1.00 36.88  ? 289  ARG A CG    1 
ATOM   2340  C  CD    . ARG A 1 289  ? 143.454 170.312 142.355 1.00 38.70  ? 289  ARG A CD    1 
ATOM   2341  N  NE    . ARG A 1 289  ? 144.051 170.404 143.681 1.00 39.69  ? 289  ARG A NE    1 
ATOM   2342  C  CZ    . ARG A 1 289  ? 144.325 169.363 144.454 1.00 39.78  ? 289  ARG A CZ    1 
ATOM   2343  N  NH1   . ARG A 1 289  ? 144.063 168.127 144.066 1.00 39.87  ? 289  ARG A NH1   1 
ATOM   2344  N  NH2   . ARG A 1 289  ? 144.880 169.568 145.644 1.00 35.68  ? 289  ARG A NH2   1 
ATOM   2345  N  N     . GLN A 1 290  ? 138.791 172.744 143.496 1.00 40.21  ? 290  GLN A N     1 
ATOM   2346  C  CA    . GLN A 1 290  ? 137.916 173.140 144.593 1.00 40.22  ? 290  GLN A CA    1 
ATOM   2347  C  C     . GLN A 1 290  ? 136.811 172.118 144.827 1.00 40.72  ? 290  GLN A C     1 
ATOM   2348  O  O     . GLN A 1 290  ? 136.384 171.907 145.967 1.00 41.72  ? 290  GLN A O     1 
ATOM   2349  C  CB    . GLN A 1 290  ? 137.344 174.527 144.298 1.00 41.50  ? 290  GLN A CB    1 
ATOM   2350  C  CG    . GLN A 1 290  ? 136.204 174.967 145.185 1.00 47.24  ? 290  GLN A CG    1 
ATOM   2351  C  CD    . GLN A 1 290  ? 134.891 175.050 144.438 1.00 56.55  ? 290  GLN A CD    1 
ATOM   2352  O  OE1   . GLN A 1 290  ? 134.845 175.482 143.286 1.00 57.00  ? 290  GLN A OE1   1 
ATOM   2353  N  NE2   . GLN A 1 290  ? 133.813 174.638 145.090 1.00 60.72  ? 290  GLN A NE2   1 
ATOM   2354  N  N     . THR A 1 291  ? 136.337 171.469 143.763 1.00 43.81  ? 291  THR A N     1 
ATOM   2355  C  CA    . THR A 1 291  ? 135.260 170.495 143.911 1.00 45.07  ? 291  THR A CA    1 
ATOM   2356  C  C     . THR A 1 291  ? 135.740 169.235 144.624 1.00 44.72  ? 291  THR A C     1 
ATOM   2357  O  O     . THR A 1 291  ? 135.088 168.750 145.555 1.00 45.62  ? 291  THR A O     1 
ATOM   2358  C  CB    . THR A 1 291  ? 134.675 170.145 142.544 1.00 43.23  ? 291  THR A CB    1 
ATOM   2359  O  OG1   . THR A 1 291  ? 134.081 171.311 141.962 1.00 49.09  ? 291  THR A OG1   1 
ATOM   2360  C  CG2   . THR A 1 291  ? 133.618 169.068 142.681 1.00 44.02  ? 291  THR A CG2   1 
ATOM   2361  N  N     . GLU A 1 292  ? 136.883 168.691 144.204 1.00 42.56  ? 292  GLU A N     1 
ATOM   2362  C  CA    . GLU A 1 292  ? 137.348 167.422 144.752 1.00 39.49  ? 292  GLU A CA    1 
ATOM   2363  C  C     . GLU A 1 292  ? 137.938 167.568 146.149 1.00 39.79  ? 292  GLU A C     1 
ATOM   2364  O  O     . GLU A 1 292  ? 137.956 166.592 146.917 1.00 40.22  ? 292  GLU A O     1 
ATOM   2365  C  CB    . GLU A 1 292  ? 138.373 166.790 143.812 1.00 40.56  ? 292  GLU A CB    1 
ATOM   2366  C  CG    . GLU A 1 292  ? 139.606 167.634 143.570 1.00 46.81  ? 292  GLU A CG    1 
ATOM   2367  C  CD    . GLU A 1 292  ? 140.705 166.867 142.868 1.00 52.54  ? 292  GLU A CD    1 
ATOM   2368  O  OE1   . GLU A 1 292  ? 141.365 166.040 143.530 1.00 52.25  ? 292  GLU A OE1   1 
ATOM   2369  O  OE2   . GLU A 1 292  ? 140.907 167.087 141.656 1.00 50.71  ? 292  GLU A OE2   1 
ATOM   2370  N  N     . LEU A 1 293  ? 138.425 168.761 146.506 1.00 39.67  ? 293  LEU A N     1 
ATOM   2371  C  CA    . LEU A 1 293  ? 138.995 168.906 147.841 1.00 38.90  ? 293  LEU A CA    1 
ATOM   2372  C  C     . LEU A 1 293  ? 137.956 168.759 148.949 1.00 39.37  ? 293  LEU A C     1 
ATOM   2373  O  O     . LEU A 1 293  ? 138.311 168.355 150.062 1.00 41.53  ? 293  LEU A O     1 
ATOM   2374  C  CB    . LEU A 1 293  ? 139.701 170.249 147.978 1.00 38.64  ? 293  LEU A CB    1 
ATOM   2375  C  CG    . LEU A 1 293  ? 141.198 170.227 147.679 1.00 40.15  ? 293  LEU A CG    1 
ATOM   2376  C  CD1   . LEU A 1 293  ? 141.854 171.358 148.414 1.00 36.96  ? 293  LEU A CD1   1 
ATOM   2377  C  CD2   . LEU A 1 293  ? 141.833 168.905 148.062 1.00 38.48  ? 293  LEU A CD2   1 
ATOM   2378  N  N     . LYS A 1 294  ? 136.683 169.045 148.670 1.00 35.97  ? 294  LYS A N     1 
ATOM   2379  C  CA    . LYS A 1 294  ? 135.654 168.853 149.686 1.00 37.81  ? 294  LYS A CA    1 
ATOM   2380  C  C     . LYS A 1 294  ? 135.469 167.375 150.001 1.00 39.91  ? 294  LYS A C     1 
ATOM   2381  O  O     . LYS A 1 294  ? 135.373 166.985 151.173 1.00 42.26  ? 294  LYS A O     1 
ATOM   2382  C  CB    . LYS A 1 294  ? 134.336 169.465 149.220 1.00 38.67  ? 294  LYS A CB    1 
ATOM   2383  C  CG    . LYS A 1 294  ? 134.373 170.969 149.045 1.00 44.90  ? 294  LYS A CG    1 
ATOM   2384  C  CD    . LYS A 1 294  ? 133.033 171.483 148.549 1.00 50.35  ? 294  LYS A CD    1 
ATOM   2385  C  CE    . LYS A 1 294  ? 133.158 172.855 147.914 1.00 53.96  ? 294  LYS A CE    1 
ATOM   2386  N  NZ    . LYS A 1 294  ? 131.879 173.297 147.293 1.00 54.08  ? 294  LYS A NZ    1 
ATOM   2387  N  N     . LEU A 1 295  ? 135.426 166.541 148.962 1.00 36.16  ? 295  LEU A N     1 
ATOM   2388  C  CA    . LEU A 1 295  ? 135.344 165.101 149.159 1.00 31.93  ? 295  LEU A CA    1 
ATOM   2389  C  C     . LEU A 1 295  ? 136.584 164.576 149.863 1.00 33.55  ? 295  LEU A C     1 
ATOM   2390  O  O     . LEU A 1 295  ? 136.487 163.676 150.708 1.00 37.80  ? 295  LEU A O     1 
ATOM   2391  C  CB    . LEU A 1 295  ? 135.162 164.412 147.808 1.00 34.88  ? 295  LEU A CB    1 
ATOM   2392  C  CG    . LEU A 1 295  ? 133.795 164.579 147.142 1.00 36.12  ? 295  LEU A CG    1 
ATOM   2393  C  CD1   . LEU A 1 295  ? 133.895 164.315 145.658 1.00 36.85  ? 295  LEU A CD1   1 
ATOM   2394  C  CD2   . LEU A 1 295  ? 132.769 163.657 147.768 1.00 42.98  ? 295  LEU A CD2   1 
ATOM   2395  N  N     . THR A 1 296  ? 137.753 165.140 149.548 1.00 32.81  ? 296  THR A N     1 
ATOM   2396  C  CA    . THR A 1 296  ? 138.972 164.728 150.240 1.00 32.38  ? 296  THR A CA    1 
ATOM   2397  C  C     . THR A 1 296  ? 138.905 165.050 151.731 1.00 32.89  ? 296  THR A C     1 
ATOM   2398  O  O     . THR A 1 296  ? 139.265 164.212 152.569 1.00 35.34  ? 296  THR A O     1 
ATOM   2399  C  CB    . THR A 1 296  ? 140.191 165.391 149.601 1.00 34.68  ? 296  THR A CB    1 
ATOM   2400  O  OG1   . THR A 1 296  ? 140.255 165.030 148.218 1.00 40.33  ? 296  THR A OG1   1 
ATOM   2401  C  CG2   . THR A 1 296  ? 141.462 164.944 150.289 1.00 35.86  ? 296  THR A CG2   1 
ATOM   2402  N  N     . ARG A 1 297  ? 138.435 166.251 152.083 1.00 32.13  ? 297  ARG A N     1 
ATOM   2403  C  CA    . ARG A 1 297  ? 138.300 166.607 153.493 1.00 33.01  ? 297  ARG A CA    1 
ATOM   2404  C  C     . ARG A 1 297  ? 137.301 165.705 154.206 1.00 33.49  ? 297  ARG A C     1 
ATOM   2405  O  O     . ARG A 1 297  ? 137.529 165.301 155.351 1.00 36.91  ? 297  ARG A O     1 
ATOM   2406  C  CB    . ARG A 1 297  ? 137.885 168.070 153.653 1.00 33.35  ? 297  ARG A CB    1 
ATOM   2407  C  CG    . ARG A 1 297  ? 138.943 169.087 153.282 1.00 35.38  ? 297  ARG A CG    1 
ATOM   2408  C  CD    . ARG A 1 297  ? 138.384 170.498 153.363 1.00 34.66  ? 297  ARG A CD    1 
ATOM   2409  N  NE    . ARG A 1 297  ? 139.232 171.481 152.700 1.00 36.22  ? 297  ARG A NE    1 
ATOM   2410  C  CZ    . ARG A 1 297  ? 140.353 171.972 153.210 1.00 34.09  ? 297  ARG A CZ    1 
ATOM   2411  N  NH1   . ARG A 1 297  ? 140.805 171.581 154.389 1.00 32.11  ? 297  ARG A NH1   1 
ATOM   2412  N  NH2   . ARG A 1 297  ? 141.038 172.876 152.518 1.00 33.42  ? 297  ARG A NH2   1 
ATOM   2413  N  N     . LYS A 1 298  ? 136.172 165.405 153.563 1.00 31.42  ? 298  LYS A N     1 
ATOM   2414  C  CA    . LYS A 1 298  ? 135.169 164.558 154.204 1.00 29.14  ? 298  LYS A CA    1 
ATOM   2415  C  C     . LYS A 1 298  ? 135.700 163.147 154.444 1.00 31.53  ? 298  LYS A C     1 
ATOM   2416  O  O     . LYS A 1 298  ? 135.500 162.566 155.525 1.00 36.59  ? 298  LYS A O     1 
ATOM   2417  C  CB    . LYS A 1 298  ? 133.901 164.544 153.353 1.00 32.48  ? 298  LYS A CB    1 
ATOM   2418  C  CG    . LYS A 1 298  ? 133.048 165.783 153.564 1.00 36.33  ? 298  LYS A CG    1 
ATOM   2419  C  CD    . LYS A 1 298  ? 132.084 166.024 152.421 1.00 35.60  ? 298  LYS A CD    1 
ATOM   2420  C  CE    . LYS A 1 298  ? 131.274 164.798 152.090 1.00 43.91  ? 298  LYS A CE    1 
ATOM   2421  N  NZ    . LYS A 1 298  ? 130.328 165.084 150.979 1.00 50.19  ? 298  LYS A NZ    1 
ATOM   2422  N  N     . ALA A 1 299  ? 136.411 162.590 153.461 1.00 32.01  ? 299  ALA A N     1 
ATOM   2423  C  CA    . ALA A 1 299  ? 137.002 161.270 153.647 1.00 29.46  ? 299  ALA A CA    1 
ATOM   2424  C  C     . ALA A 1 299  ? 138.065 161.292 154.738 1.00 31.25  ? 299  ALA A C     1 
ATOM   2425  O  O     . ALA A 1 299  ? 138.198 160.328 155.500 1.00 31.62  ? 299  ALA A O     1 
ATOM   2426  C  CB    . ALA A 1 299  ? 137.588 160.764 152.332 1.00 28.00  ? 299  ALA A CB    1 
ATOM   2427  N  N     . ALA A 1 300  ? 138.820 162.390 154.844 1.00 31.28  ? 300  ALA A N     1 
ATOM   2428  C  CA    . ALA A 1 300  ? 139.808 162.496 155.913 1.00 30.62  ? 300  ALA A CA    1 
ATOM   2429  C  C     . ALA A 1 300  ? 139.154 162.594 157.287 1.00 32.17  ? 300  ALA A C     1 
ATOM   2430  O  O     . ALA A 1 300  ? 139.673 162.030 158.259 1.00 36.13  ? 300  ALA A O     1 
ATOM   2431  C  CB    . ALA A 1 300  ? 140.713 163.700 155.671 1.00 30.70  ? 300  ALA A CB    1 
ATOM   2432  N  N     . TYR A 1 301  ? 138.016 163.287 157.389 1.00 31.90  ? 301  TYR A N     1 
ATOM   2433  C  CA    . TYR A 1 301  ? 137.290 163.316 158.657 1.00 29.87  ? 301  TYR A CA    1 
ATOM   2434  C  C     . TYR A 1 301  ? 136.831 161.921 159.057 1.00 31.19  ? 301  TYR A C     1 
ATOM   2435  O  O     . TYR A 1 301  ? 136.936 161.543 160.229 1.00 31.37  ? 301  TYR A O     1 
ATOM   2436  C  CB    . TYR A 1 301  ? 136.084 164.254 158.586 1.00 25.78  ? 301  TYR A CB    1 
ATOM   2437  C  CG    . TYR A 1 301  ? 136.396 165.694 158.256 1.00 31.17  ? 301  TYR A CG    1 
ATOM   2438  C  CD1   . TYR A 1 301  ? 137.637 166.242 158.537 1.00 34.18  ? 301  TYR A CD1   1 
ATOM   2439  C  CD2   . TYR A 1 301  ? 135.437 166.510 157.676 1.00 32.85  ? 301  TYR A CD2   1 
ATOM   2440  C  CE1   . TYR A 1 301  ? 137.919 167.562 158.236 1.00 36.39  ? 301  TYR A CE1   1 
ATOM   2441  C  CE2   . TYR A 1 301  ? 135.708 167.826 157.372 1.00 33.85  ? 301  TYR A CE2   1 
ATOM   2442  C  CZ    . TYR A 1 301  ? 136.950 168.348 157.654 1.00 36.33  ? 301  TYR A CZ    1 
ATOM   2443  O  OH    . TYR A 1 301  ? 137.226 169.661 157.354 1.00 36.39  ? 301  TYR A OH    1 
ATOM   2444  N  N     . VAL A 1 302  ? 136.315 161.144 158.102 1.00 31.44  ? 302  VAL A N     1 
ATOM   2445  C  CA    . VAL A 1 302  ? 135.896 159.778 158.427 1.00 31.78  ? 302  VAL A CA    1 
ATOM   2446  C  C     . VAL A 1 302  ? 137.096 158.929 158.845 1.00 32.92  ? 302  VAL A C     1 
ATOM   2447  O  O     . VAL A 1 302  ? 137.028 158.146 159.808 1.00 31.80  ? 302  VAL A O     1 
ATOM   2448  C  CB    . VAL A 1 302  ? 135.142 159.151 157.241 1.00 30.46  ? 302  VAL A CB    1 
ATOM   2449  C  CG1   . VAL A 1 302  ? 135.171 157.642 157.335 1.00 34.77  ? 302  VAL A CG1   1 
ATOM   2450  C  CG2   . VAL A 1 302  ? 133.715 159.639 157.219 1.00 31.03  ? 302  VAL A CG2   1 
ATOM   2451  N  N     . ARG A 1 303  ? 138.216 159.072 158.132 1.00 32.72  ? 303  ARG A N     1 
ATOM   2452  C  CA    . ARG A 1 303  ? 139.379 158.242 158.418 1.00 30.19  ? 303  ARG A CA    1 
ATOM   2453  C  C     . ARG A 1 303  ? 140.020 158.600 159.752 1.00 31.21  ? 303  ARG A C     1 
ATOM   2454  O  O     . ARG A 1 303  ? 140.649 157.740 160.377 1.00 33.20  ? 303  ARG A O     1 
ATOM   2455  C  CB    . ARG A 1 303  ? 140.390 158.346 157.278 1.00 33.95  ? 303  ARG A CB    1 
ATOM   2456  C  CG    . ARG A 1 303  ? 139.959 157.565 156.053 1.00 40.93  ? 303  ARG A CG    1 
ATOM   2457  C  CD    . ARG A 1 303  ? 141.089 157.344 155.070 1.00 41.13  ? 303  ARG A CD    1 
ATOM   2458  N  NE    . ARG A 1 303  ? 141.692 158.593 154.627 1.00 43.52  ? 303  ARG A NE    1 
ATOM   2459  C  CZ    . ARG A 1 303  ? 142.959 158.716 154.261 1.00 50.98  ? 303  ARG A CZ    1 
ATOM   2460  N  NH1   . ARG A 1 303  ? 143.778 157.677 154.245 1.00 48.15  ? 303  ARG A NH1   1 
ATOM   2461  N  NH2   . ARG A 1 303  ? 143.413 159.909 153.889 1.00 50.80  ? 303  ARG A NH2   1 
ATOM   2462  N  N     . TYR A 1 304  ? 139.874 159.845 160.213 1.00 32.45  ? 304  TYR A N     1 
ATOM   2463  C  CA    . TYR A 1 304  ? 140.345 160.174 161.556 1.00 29.69  ? 304  TYR A CA    1 
ATOM   2464  C  C     . TYR A 1 304  ? 139.623 159.342 162.609 1.00 29.80  ? 304  TYR A C     1 
ATOM   2465  O  O     . TYR A 1 304  ? 140.259 158.704 163.455 1.00 31.91  ? 304  TYR A O     1 
ATOM   2466  C  CB    . TYR A 1 304  ? 140.148 161.657 161.862 1.00 28.98  ? 304  TYR A CB    1 
ATOM   2467  C  CG    . TYR A 1 304  ? 140.179 161.919 163.350 1.00 33.89  ? 304  TYR A CG    1 
ATOM   2468  C  CD1   . TYR A 1 304  ? 141.369 161.858 164.057 1.00 36.13  ? 304  TYR A CD1   1 
ATOM   2469  C  CD2   . TYR A 1 304  ? 139.011 162.166 164.055 1.00 33.99  ? 304  TYR A CD2   1 
ATOM   2470  C  CE1   . TYR A 1 304  ? 141.397 162.073 165.419 1.00 35.75  ? 304  TYR A CE1   1 
ATOM   2471  C  CE2   . TYR A 1 304  ? 139.031 162.379 165.413 1.00 32.50  ? 304  TYR A CE2   1 
ATOM   2472  C  CZ    . TYR A 1 304  ? 140.222 162.330 166.090 1.00 35.55  ? 304  TYR A CZ    1 
ATOM   2473  O  OH    . TYR A 1 304  ? 140.236 162.544 167.444 1.00 41.69  ? 304  TYR A OH    1 
ATOM   2474  N  N     . PHE A 1 305  ? 138.287 159.352 162.583 1.00 30.74  ? 305  PHE A N     1 
ATOM   2475  C  CA    . PHE A 1 305  ? 137.529 158.568 163.549 1.00 26.02  ? 305  PHE A CA    1 
ATOM   2476  C  C     . PHE A 1 305  ? 137.820 157.086 163.416 1.00 30.45  ? 305  PHE A C     1 
ATOM   2477  O  O     . PHE A 1 305  ? 137.822 156.367 164.420 1.00 36.00  ? 305  PHE A O     1 
ATOM   2478  C  CB    . PHE A 1 305  ? 136.028 158.819 163.399 1.00 26.29  ? 305  PHE A CB    1 
ATOM   2479  C  CG    . PHE A 1 305  ? 135.569 160.133 163.956 1.00 28.68  ? 305  PHE A CG    1 
ATOM   2480  C  CD1   . PHE A 1 305  ? 135.586 160.364 165.321 1.00 29.81  ? 305  PHE A CD1   1 
ATOM   2481  C  CD2   . PHE A 1 305  ? 135.112 161.133 163.120 1.00 29.10  ? 305  PHE A CD2   1 
ATOM   2482  C  CE1   . PHE A 1 305  ? 135.157 161.569 165.837 1.00 31.74  ? 305  PHE A CE1   1 
ATOM   2483  C  CE2   . PHE A 1 305  ? 134.685 162.338 163.630 1.00 29.54  ? 305  PHE A CE2   1 
ATOM   2484  C  CZ    . PHE A 1 305  ? 134.707 162.557 164.989 1.00 28.71  ? 305  PHE A CZ    1 
ATOM   2485  N  N     . ASN A 1 306  ? 138.053 156.603 162.196 1.00 35.25  ? 306  ASN A N     1 
ATOM   2486  C  CA    . ASN A 1 306  ? 138.448 155.204 162.059 1.00 30.71  ? 306  ASN A CA    1 
ATOM   2487  C  C     . ASN A 1 306  ? 139.796 154.941 162.725 1.00 32.89  ? 306  ASN A C     1 
ATOM   2488  O  O     . ASN A 1 306  ? 139.976 153.915 163.389 1.00 30.80  ? 306  ASN A O     1 
ATOM   2489  C  CB    . ASN A 1 306  ? 138.485 154.802 160.586 1.00 29.73  ? 306  ASN A CB    1 
ATOM   2490  C  CG    . ASN A 1 306  ? 138.930 153.371 160.385 1.00 31.73  ? 306  ASN A CG    1 
ATOM   2491  O  OD1   . ASN A 1 306  ? 138.388 152.449 160.988 1.00 35.20  ? 306  ASN A OD1   1 
ATOM   2492  N  ND2   . ASN A 1 306  ? 139.924 153.178 159.530 1.00 33.35  ? 306  ASN A ND2   1 
ATOM   2493  N  N     . SER A 1 307  ? 140.749 155.864 162.574 1.00 34.99  ? 307  SER A N     1 
ATOM   2494  C  CA    . SER A 1 307  ? 142.114 155.633 163.037 1.00 32.64  ? 307  SER A CA    1 
ATOM   2495  C  C     . SER A 1 307  ? 142.277 155.801 164.542 1.00 34.67  ? 307  SER A C     1 
ATOM   2496  O  O     . SER A 1 307  ? 143.210 155.235 165.120 1.00 40.23  ? 307  SER A O     1 
ATOM   2497  C  CB    . SER A 1 307  ? 143.078 156.574 162.316 1.00 33.22  ? 307  SER A CB    1 
ATOM   2498  O  OG    . SER A 1 307  ? 144.422 156.272 162.644 1.00 38.08  ? 307  SER A OG    1 
ATOM   2499  N  N     . SER A 1 308  ? 141.409 156.571 165.191 1.00 34.14  ? 308  SER A N     1 
ATOM   2500  C  CA    . SER A 1 308  ? 141.560 156.869 166.610 1.00 32.48  ? 308  SER A CA    1 
ATOM   2501  C  C     . SER A 1 308  ? 140.869 155.854 167.508 1.00 36.10  ? 308  SER A C     1 
ATOM   2502  O  O     . SER A 1 308  ? 140.809 156.065 168.723 1.00 40.21  ? 308  SER A O     1 
ATOM   2503  C  CB    . SER A 1 308  ? 141.019 158.266 166.919 1.00 31.68  ? 308  SER A CB    1 
ATOM   2504  O  OG    . SER A 1 308  ? 139.604 158.271 166.916 1.00 32.51  ? 308  SER A OG    1 
ATOM   2505  N  N     . ALA A 1 309  ? 140.334 154.773 166.943 1.00 34.45  ? 309  ALA A N     1 
ATOM   2506  C  CA    . ALA A 1 309  ? 139.605 153.799 167.746 1.00 30.39  ? 309  ALA A CA    1 
ATOM   2507  C  C     . ALA A 1 309  ? 140.531 153.030 168.679 1.00 35.28  ? 309  ALA A C     1 
ATOM   2508  O  O     . ALA A 1 309  ? 140.141 152.682 169.797 1.00 39.59  ? 309  ALA A O     1 
ATOM   2509  C  CB    . ALA A 1 309  ? 138.849 152.838 166.834 1.00 32.53  ? 309  ALA A CB    1 
ATOM   2510  N  N     . PHE A 1 310  ? 141.756 152.746 168.235 1.00 33.48  ? 310  PHE A N     1 
ATOM   2511  C  CA    . PHE A 1 310  ? 142.667 151.935 169.037 1.00 30.12  ? 310  PHE A CA    1 
ATOM   2512  C  C     . PHE A 1 310  ? 143.031 152.634 170.340 1.00 34.77  ? 310  PHE A C     1 
ATOM   2513  O  O     . PHE A 1 310  ? 143.084 152.004 171.402 1.00 39.54  ? 310  PHE A O     1 
ATOM   2514  C  CB    . PHE A 1 310  ? 143.926 151.608 168.234 1.00 32.12  ? 310  PHE A CB    1 
ATOM   2515  C  CG    . PHE A 1 310  ? 144.963 150.847 169.012 1.00 31.59  ? 310  PHE A CG    1 
ATOM   2516  C  CD1   . PHE A 1 310  ? 144.798 149.500 169.276 1.00 32.63  ? 310  PHE A CD1   1 
ATOM   2517  C  CD2   . PHE A 1 310  ? 146.100 151.480 169.481 1.00 33.33  ? 310  PHE A CD2   1 
ATOM   2518  C  CE1   . PHE A 1 310  ? 145.744 148.800 169.991 1.00 31.90  ? 310  PHE A CE1   1 
ATOM   2519  C  CE2   . PHE A 1 310  ? 147.051 150.783 170.197 1.00 31.65  ? 310  PHE A CE2   1 
ATOM   2520  C  CZ    . PHE A 1 310  ? 146.872 149.441 170.451 1.00 31.38  ? 310  PHE A CZ    1 
ATOM   2521  N  N     . PHE A 1 311  ? 143.298 153.938 170.277 1.00 36.67  ? 311  PHE A N     1 
ATOM   2522  C  CA    . PHE A 1 311  ? 143.772 154.652 171.457 1.00 37.78  ? 311  PHE A CA    1 
ATOM   2523  C  C     . PHE A 1 311  ? 142.652 154.899 172.461 1.00 39.72  ? 311  PHE A C     1 
ATOM   2524  O  O     . PHE A 1 311  ? 142.878 154.843 173.675 1.00 42.73  ? 311  PHE A O     1 
ATOM   2525  C  CB    . PHE A 1 311  ? 144.432 155.960 171.033 1.00 35.19  ? 311  PHE A CB    1 
ATOM   2526  C  CG    . PHE A 1 311  ? 145.491 155.781 169.989 1.00 38.64  ? 311  PHE A CG    1 
ATOM   2527  C  CD1   . PHE A 1 311  ? 146.692 155.171 170.306 1.00 41.00  ? 311  PHE A CD1   1 
ATOM   2528  C  CD2   . PHE A 1 311  ? 145.284 156.203 168.689 1.00 39.78  ? 311  PHE A CD2   1 
ATOM   2529  C  CE1   . PHE A 1 311  ? 147.668 154.992 169.352 1.00 37.70  ? 311  PHE A CE1   1 
ATOM   2530  C  CE2   . PHE A 1 311  ? 146.259 156.031 167.728 1.00 42.27  ? 311  PHE A CE2   1 
ATOM   2531  C  CZ    . PHE A 1 311  ? 147.453 155.423 168.060 1.00 41.71  ? 311  PHE A CZ    1 
ATOM   2532  N  N     . PHE A 1 312  ? 141.442 155.175 171.982 1.00 36.91  ? 312  PHE A N     1 
ATOM   2533  C  CA    . PHE A 1 312  ? 140.310 155.458 172.855 1.00 39.97  ? 312  PHE A CA    1 
ATOM   2534  C  C     . PHE A 1 312  ? 139.566 154.211 173.300 1.00 46.76  ? 312  PHE A C     1 
ATOM   2535  O  O     . PHE A 1 312  ? 138.369 154.293 173.595 1.00 53.84  ? 312  PHE A O     1 
ATOM   2536  C  CB    . PHE A 1 312  ? 139.342 156.428 172.176 1.00 40.78  ? 312  PHE A CB    1 
ATOM   2537  C  CG    . PHE A 1 312  ? 139.680 157.873 172.403 1.00 46.46  ? 312  PHE A CG    1 
ATOM   2538  C  CD1   . PHE A 1 312  ? 139.370 158.485 173.606 1.00 46.39  ? 312  PHE A CD1   1 
ATOM   2539  C  CD2   . PHE A 1 312  ? 140.305 158.618 171.420 1.00 47.16  ? 312  PHE A CD2   1 
ATOM   2540  C  CE1   . PHE A 1 312  ? 139.675 159.811 173.822 1.00 48.47  ? 312  PHE A CE1   1 
ATOM   2541  C  CE2   . PHE A 1 312  ? 140.613 159.945 171.629 1.00 46.77  ? 312  PHE A CE2   1 
ATOM   2542  C  CZ    . PHE A 1 312  ? 140.298 160.544 172.832 1.00 50.46  ? 312  PHE A CZ    1 
ATOM   2543  N  N     . SER A 1 313  ? 140.232 153.060 173.345 1.00 45.99  ? 313  SER A N     1 
ATOM   2544  C  CA    . SER A 1 313  ? 139.633 151.849 173.878 1.00 42.12  ? 313  SER A CA    1 
ATOM   2545  C  C     . SER A 1 313  ? 140.495 151.172 174.933 1.00 42.15  ? 313  SER A C     1 
ATOM   2546  O  O     . SER A 1 313  ? 140.077 150.149 175.483 1.00 44.23  ? 313  SER A O     1 
ATOM   2547  C  CB    . SER A 1 313  ? 139.339 150.851 172.748 1.00 42.06  ? 313  SER A CB    1 
ATOM   2548  O  OG    . SER A 1 313  ? 140.536 150.349 172.180 1.00 38.76  ? 313  SER A OG    1 
ATOM   2549  N  N     . GLY A 1 314  ? 141.679 151.709 175.232 1.00 43.93  ? 314  GLY A N     1 
ATOM   2550  C  CA    . GLY A 1 314  ? 142.580 151.038 176.153 1.00 44.15  ? 314  GLY A CA    1 
ATOM   2551  C  C     . GLY A 1 314  ? 142.062 150.971 177.574 1.00 48.25  ? 314  GLY A C     1 
ATOM   2552  O  O     . GLY A 1 314  ? 142.305 149.989 178.280 1.00 49.63  ? 314  GLY A O     1 
ATOM   2553  N  N     . PHE A 1 315  ? 141.342 152.002 178.012 1.00 49.11  ? 315  PHE A N     1 
ATOM   2554  C  CA    . PHE A 1 315  ? 140.850 152.072 179.381 1.00 48.92  ? 315  PHE A CA    1 
ATOM   2555  C  C     . PHE A 1 315  ? 139.505 151.385 179.560 1.00 49.72  ? 315  PHE A C     1 
ATOM   2556  O  O     . PHE A 1 315  ? 139.279 150.732 180.583 1.00 52.80  ? 315  PHE A O     1 
ATOM   2557  C  CB    . PHE A 1 315  ? 140.733 153.532 179.824 1.00 52.22  ? 315  PHE A CB    1 
ATOM   2558  C  CG    . PHE A 1 315  ? 140.386 153.698 181.276 1.00 59.38  ? 315  PHE A CG    1 
ATOM   2559  C  CD1   . PHE A 1 315  ? 141.364 153.607 182.249 1.00 58.38  ? 315  PHE A CD1   1 
ATOM   2560  C  CD2   . PHE A 1 315  ? 139.081 153.949 181.666 1.00 57.69  ? 315  PHE A CD2   1 
ATOM   2561  C  CE1   . PHE A 1 315  ? 141.049 153.757 183.581 1.00 58.08  ? 315  PHE A CE1   1 
ATOM   2562  C  CE2   . PHE A 1 315  ? 138.759 154.101 182.998 1.00 57.74  ? 315  PHE A CE2   1 
ATOM   2563  C  CZ    . PHE A 1 315  ? 139.745 154.006 183.957 1.00 59.65  ? 315  PHE A CZ    1 
ATOM   2564  N  N     . PHE A 1 316  ? 138.603 151.522 178.592 1.00 49.69  ? 316  PHE A N     1 
ATOM   2565  C  CA    . PHE A 1 316  ? 137.236 151.057 178.788 1.00 50.41  ? 316  PHE A CA    1 
ATOM   2566  C  C     . PHE A 1 316  ? 137.116 149.543 178.664 1.00 50.49  ? 316  PHE A C     1 
ATOM   2567  O  O     . PHE A 1 316  ? 136.268 148.938 179.329 1.00 52.23  ? 316  PHE A O     1 
ATOM   2568  C  CB    . PHE A 1 316  ? 136.315 151.755 177.790 1.00 52.87  ? 316  PHE A CB    1 
ATOM   2569  C  CG    . PHE A 1 316  ? 136.324 153.248 177.920 1.00 62.23  ? 316  PHE A CG    1 
ATOM   2570  C  CD1   . PHE A 1 316  ? 135.666 153.872 178.965 1.00 61.46  ? 316  PHE A CD1   1 
ATOM   2571  C  CD2   . PHE A 1 316  ? 137.014 154.027 177.009 1.00 60.08  ? 316  PHE A CD2   1 
ATOM   2572  C  CE1   . PHE A 1 316  ? 135.685 155.245 179.089 1.00 59.69  ? 316  PHE A CE1   1 
ATOM   2573  C  CE2   . PHE A 1 316  ? 137.036 155.400 177.126 1.00 59.85  ? 316  PHE A CE2   1 
ATOM   2574  C  CZ    . PHE A 1 316  ? 136.371 156.011 178.167 1.00 60.19  ? 316  PHE A CZ    1 
ATOM   2575  N  N     . VAL A 1 317  ? 137.963 148.919 177.846 1.00 51.11  ? 317  VAL A N     1 
ATOM   2576  C  CA    . VAL A 1 317  ? 137.902 147.472 177.669 1.00 48.16  ? 317  VAL A CA    1 
ATOM   2577  C  C     . VAL A 1 317  ? 138.238 146.759 178.972 1.00 49.91  ? 317  VAL A C     1 
ATOM   2578  O  O     . VAL A 1 317  ? 137.570 145.793 179.359 1.00 49.71  ? 317  VAL A O     1 
ATOM   2579  C  CB    . VAL A 1 317  ? 138.839 147.041 176.526 1.00 42.62  ? 317  VAL A CB    1 
ATOM   2580  C  CG1   . VAL A 1 317  ? 139.058 145.542 176.551 1.00 41.20  ? 317  VAL A CG1   1 
ATOM   2581  C  CG2   . VAL A 1 317  ? 138.272 147.469 175.189 1.00 43.38  ? 317  VAL A CG2   1 
ATOM   2582  N  N     . VAL A 1 318  ? 139.280 147.218 179.666 1.00 49.77  ? 318  VAL A N     1 
ATOM   2583  C  CA    . VAL A 1 318  ? 139.648 146.605 180.936 1.00 47.70  ? 318  VAL A CA    1 
ATOM   2584  C  C     . VAL A 1 318  ? 138.715 147.051 182.056 1.00 51.25  ? 318  VAL A C     1 
ATOM   2585  O  O     . VAL A 1 318  ? 138.402 146.262 182.952 1.00 58.52  ? 318  VAL A O     1 
ATOM   2586  C  CB    . VAL A 1 318  ? 141.117 146.906 181.271 1.00 43.33  ? 318  VAL A CB    1 
ATOM   2587  C  CG1   . VAL A 1 318  ? 142.027 146.243 180.265 1.00 44.46  ? 318  VAL A CG1   1 
ATOM   2588  C  CG2   . VAL A 1 318  ? 141.363 148.399 181.280 1.00 46.30  ? 318  VAL A CG2   1 
ATOM   2589  N  N     . PHE A 1 319  ? 138.252 148.301 182.026 1.00 49.75  ? 319  PHE A N     1 
ATOM   2590  C  CA    . PHE A 1 319  ? 137.386 148.801 183.088 1.00 47.92  ? 319  PHE A CA    1 
ATOM   2591  C  C     . PHE A 1 319  ? 136.052 148.065 183.101 1.00 50.87  ? 319  PHE A C     1 
ATOM   2592  O  O     . PHE A 1 319  ? 135.593 147.608 184.155 1.00 53.00  ? 319  PHE A O     1 
ATOM   2593  C  CB    . PHE A 1 319  ? 137.175 150.305 182.907 1.00 49.41  ? 319  PHE A CB    1 
ATOM   2594  C  CG    . PHE A 1 319  ? 136.406 150.956 184.019 1.00 54.32  ? 319  PHE A CG    1 
ATOM   2595  C  CD1   . PHE A 1 319  ? 137.046 151.343 185.182 1.00 55.45  ? 319  PHE A CD1   1 
ATOM   2596  C  CD2   . PHE A 1 319  ? 135.049 151.202 183.892 1.00 54.93  ? 319  PHE A CD2   1 
ATOM   2597  C  CE1   . PHE A 1 319  ? 136.351 151.950 186.204 1.00 54.75  ? 319  PHE A CE1   1 
ATOM   2598  C  CE2   . PHE A 1 319  ? 134.346 151.810 184.913 1.00 54.69  ? 319  PHE A CE2   1 
ATOM   2599  C  CZ    . PHE A 1 319  ? 134.999 152.185 186.070 1.00 55.79  ? 319  PHE A CZ    1 
ATOM   2600  N  N     . LEU A 1 320  ? 135.424 147.922 181.932 1.00 51.95  ? 320  LEU A N     1 
ATOM   2601  C  CA    . LEU A 1 320  ? 134.119 147.278 181.857 1.00 50.72  ? 320  LEU A CA    1 
ATOM   2602  C  C     . LEU A 1 320  ? 134.179 145.794 182.181 1.00 56.55  ? 320  LEU A C     1 
ATOM   2603  O  O     . LEU A 1 320  ? 133.149 145.210 182.530 1.00 60.46  ? 320  LEU A O     1 
ATOM   2604  C  CB    . LEU A 1 320  ? 133.513 147.467 180.468 1.00 50.15  ? 320  LEU A CB    1 
ATOM   2605  C  CG    . LEU A 1 320  ? 132.954 148.845 180.121 1.00 54.57  ? 320  LEU A CG    1 
ATOM   2606  C  CD1   . LEU A 1 320  ? 131.860 148.708 179.080 1.00 54.04  ? 320  LEU A CD1   1 
ATOM   2607  C  CD2   . LEU A 1 320  ? 132.429 149.551 181.361 1.00 55.74  ? 320  LEU A CD2   1 
ATOM   2608  N  N     . SER A 1 321  ? 135.347 145.167 182.057 1.00 55.19  ? 321  SER A N     1 
ATOM   2609  C  CA    . SER A 1 321  ? 135.480 143.752 182.363 1.00 52.54  ? 321  SER A CA    1 
ATOM   2610  C  C     . SER A 1 321  ? 136.022 143.492 183.759 1.00 52.51  ? 321  SER A C     1 
ATOM   2611  O  O     . SER A 1 321  ? 135.879 142.374 184.263 1.00 54.83  ? 321  SER A O     1 
ATOM   2612  C  CB    . SER A 1 321  ? 136.390 143.067 181.338 1.00 53.26  ? 321  SER A CB    1 
ATOM   2613  O  OG    . SER A 1 321  ? 137.732 143.488 181.485 1.00 56.30  ? 321  SER A OG    1 
ATOM   2614  N  N     . VAL A 1 322  ? 136.628 144.488 184.395 1.00 50.95  ? 322  VAL A N     1 
ATOM   2615  C  CA    . VAL A 1 322  ? 137.165 144.336 185.738 1.00 49.34  ? 322  VAL A CA    1 
ATOM   2616  C  C     . VAL A 1 322  ? 136.177 144.806 186.797 1.00 54.65  ? 322  VAL A C     1 
ATOM   2617  O  O     . VAL A 1 322  ? 136.093 144.211 187.872 1.00 56.27  ? 322  VAL A O     1 
ATOM   2618  C  CB    . VAL A 1 322  ? 138.511 145.084 185.849 1.00 49.37  ? 322  VAL A CB    1 
ATOM   2619  C  CG1   . VAL A 1 322  ? 138.764 145.544 187.269 1.00 47.96  ? 322  VAL A CG1   1 
ATOM   2620  C  CG2   . VAL A 1 322  ? 139.646 144.196 185.368 1.00 46.47  ? 322  VAL A CG2   1 
ATOM   2621  N  N     . LEU A 1 323  ? 135.404 145.856 186.510 1.00 57.82  ? 323  LEU A N     1 
ATOM   2622  C  CA    . LEU A 1 323  ? 134.469 146.376 187.506 1.00 54.40  ? 323  LEU A CA    1 
ATOM   2623  C  C     . LEU A 1 323  ? 133.426 145.356 187.952 1.00 56.97  ? 323  LEU A C     1 
ATOM   2624  O  O     . LEU A 1 323  ? 133.203 145.235 189.169 1.00 55.27  ? 323  LEU A O     1 
ATOM   2625  C  CB    . LEU A 1 323  ? 133.815 147.656 186.972 1.00 53.03  ? 323  LEU A CB    1 
ATOM   2626  C  CG    . LEU A 1 323  ? 132.704 148.287 187.813 1.00 58.30  ? 323  LEU A CG    1 
ATOM   2627  C  CD1   . LEU A 1 323  ? 132.829 149.797 187.779 1.00 58.21  ? 323  LEU A CD1   1 
ATOM   2628  C  CD2   . LEU A 1 323  ? 131.329 147.866 187.313 1.00 56.00  ? 323  LEU A CD2   1 
ATOM   2629  N  N     . PRO A 1 324  ? 132.748 144.612 187.066 1.00 57.23  ? 324  PRO A N     1 
ATOM   2630  C  CA    . PRO A 1 324  ? 131.793 143.604 187.557 1.00 54.58  ? 324  PRO A CA    1 
ATOM   2631  C  C     . PRO A 1 324  ? 132.448 142.483 188.341 1.00 56.35  ? 324  PRO A C     1 
ATOM   2632  O  O     . PRO A 1 324  ? 131.759 141.805 189.113 1.00 58.73  ? 324  PRO A O     1 
ATOM   2633  C  CB    . PRO A 1 324  ? 131.135 143.074 186.274 1.00 54.53  ? 324  PRO A CB    1 
ATOM   2634  C  CG    . PRO A 1 324  ? 131.456 144.073 185.223 1.00 56.17  ? 324  PRO A CG    1 
ATOM   2635  C  CD    . PRO A 1 324  ? 132.785 144.633 185.596 1.00 55.52  ? 324  PRO A CD    1 
ATOM   2636  N  N     . TYR A 1 325  ? 133.751 142.264 188.169 1.00 56.51  ? 325  TYR A N     1 
ATOM   2637  C  CA    . TYR A 1 325  ? 134.450 141.250 188.947 1.00 56.82  ? 325  TYR A CA    1 
ATOM   2638  C  C     . TYR A 1 325  ? 134.870 141.788 190.308 1.00 56.88  ? 325  TYR A C     1 
ATOM   2639  O  O     . TYR A 1 325  ? 134.775 141.078 191.315 1.00 58.96  ? 325  TYR A O     1 
ATOM   2640  C  CB    . TYR A 1 325  ? 135.669 140.748 188.169 1.00 57.19  ? 325  TYR A CB    1 
ATOM   2641  C  CG    . TYR A 1 325  ? 136.454 139.648 188.856 1.00 56.08  ? 325  TYR A CG    1 
ATOM   2642  C  CD1   . TYR A 1 325  ? 137.431 139.945 189.797 1.00 52.48  ? 325  TYR A CD1   1 
ATOM   2643  C  CD2   . TYR A 1 325  ? 136.226 138.315 188.551 1.00 54.02  ? 325  TYR A CD2   1 
ATOM   2644  C  CE1   . TYR A 1 325  ? 138.147 138.947 190.420 1.00 48.65  ? 325  TYR A CE1   1 
ATOM   2645  C  CE2   . TYR A 1 325  ? 136.942 137.312 189.168 1.00 51.50  ? 325  TYR A CE2   1 
ATOM   2646  C  CZ    . TYR A 1 325  ? 137.899 137.633 190.101 1.00 48.92  ? 325  TYR A CZ    1 
ATOM   2647  O  OH    . TYR A 1 325  ? 138.614 136.638 190.720 1.00 51.97  ? 325  TYR A OH    1 
ATOM   2648  N  N     . ALA A 1 326  ? 135.341 143.034 190.356 1.00 56.45  ? 326  ALA A N     1 
ATOM   2649  C  CA    . ALA A 1 326  ? 135.866 143.595 191.594 1.00 56.96  ? 326  ALA A CA    1 
ATOM   2650  C  C     . ALA A 1 326  ? 134.785 143.851 192.635 1.00 60.48  ? 326  ALA A C     1 
ATOM   2651  O  O     . ALA A 1 326  ? 135.099 143.903 193.828 1.00 61.86  ? 326  ALA A O     1 
ATOM   2652  C  CB    . ALA A 1 326  ? 136.618 144.893 191.304 1.00 51.55  ? 326  ALA A CB    1 
ATOM   2653  N  N     . LEU A 1 327  ? 133.527 144.016 192.223 1.00 61.63  ? 327  LEU A N     1 
ATOM   2654  C  CA    . LEU A 1 327  ? 132.481 144.341 193.187 1.00 62.80  ? 327  LEU A CA    1 
ATOM   2655  C  C     . LEU A 1 327  ? 132.047 143.115 193.981 1.00 63.65  ? 327  LEU A C     1 
ATOM   2656  O  O     . LEU A 1 327  ? 131.934 143.174 195.210 1.00 67.03  ? 327  LEU A O     1 
ATOM   2657  C  CB    . LEU A 1 327  ? 131.281 144.967 192.474 1.00 59.74  ? 327  LEU A CB    1 
ATOM   2658  C  CG    . LEU A 1 327  ? 131.496 146.369 191.908 1.00 62.31  ? 327  LEU A CG    1 
ATOM   2659  C  CD1   . LEU A 1 327  ? 130.291 146.808 191.097 1.00 59.30  ? 327  LEU A CD1   1 
ATOM   2660  C  CD2   . LEU A 1 327  ? 131.781 147.357 193.026 1.00 59.68  ? 327  LEU A CD2   1 
ATOM   2661  N  N     . ILE A 1 328  ? 131.804 141.993 193.299 1.00 62.13  ? 328  ILE A N     1 
ATOM   2662  C  CA    . ILE A 1 328  ? 131.353 140.799 194.003 1.00 66.46  ? 328  ILE A CA    1 
ATOM   2663  C  C     . ILE A 1 328  ? 132.462 140.190 194.854 1.00 68.63  ? 328  ILE A C     1 
ATOM   2664  O  O     . ILE A 1 328  ? 132.168 139.474 195.818 1.00 71.87  ? 328  ILE A O     1 
ATOM   2665  C  CB    . ILE A 1 328  ? 130.775 139.772 193.008 1.00 67.37  ? 328  ILE A CB    1 
ATOM   2666  C  CG1   . ILE A 1 328  ? 131.789 139.435 191.919 1.00 68.61  ? 328  ILE A CG1   1 
ATOM   2667  C  CG2   . ILE A 1 328  ? 129.493 140.296 192.387 1.00 65.98  ? 328  ILE A CG2   1 
ATOM   2668  C  CD1   . ILE A 1 328  ? 131.435 138.201 191.116 1.00 67.00  ? 328  ILE A CD1   1 
ATOM   2669  N  N     . LYS A 1 329  ? 133.726 140.460 194.534 1.00 66.65  ? 329  LYS A N     1 
ATOM   2670  C  CA    . LYS A 1 329  ? 134.839 140.089 195.399 1.00 65.39  ? 329  LYS A CA    1 
ATOM   2671  C  C     . LYS A 1 329  ? 136.058 140.911 195.007 1.00 64.30  ? 329  LYS A C     1 
ATOM   2672  O  O     . LYS A 1 329  ? 136.192 141.335 193.858 1.00 60.69  ? 329  LYS A O     1 
ATOM   2673  C  CB    . LYS A 1 329  ? 135.157 138.587 195.338 1.00 62.83  ? 329  LYS A CB    1 
ATOM   2674  C  CG    . LYS A 1 329  ? 135.737 138.084 194.028 1.00 61.69  ? 329  LYS A CG    1 
ATOM   2675  C  CD    . LYS A 1 329  ? 134.652 137.838 193.002 1.00 59.34  ? 329  LYS A CD    1 
ATOM   2676  C  CE    . LYS A 1 329  ? 135.035 136.741 192.029 1.00 59.11  ? 329  LYS A CE    1 
ATOM   2677  N  NZ    . LYS A 1 329  ? 135.080 135.416 192.701 1.00 59.46  ? 329  LYS A NZ    1 
ATOM   2678  N  N     . GLY A 1 330  ? 136.946 141.122 195.978 1.00 63.53  ? 330  GLY A N     1 
ATOM   2679  C  CA    . GLY A 1 330  ? 138.083 141.997 195.755 1.00 61.79  ? 330  GLY A CA    1 
ATOM   2680  C  C     . GLY A 1 330  ? 139.039 141.450 194.712 1.00 59.63  ? 330  GLY A C     1 
ATOM   2681  O  O     . GLY A 1 330  ? 139.066 140.253 194.424 1.00 64.29  ? 330  GLY A O     1 
ATOM   2682  N  N     . ILE A 1 331  ? 139.826 142.353 194.131 1.00 49.89  ? 331  ILE A N     1 
ATOM   2683  C  CA    . ILE A 1 331  ? 140.782 142.012 193.086 1.00 49.34  ? 331  ILE A CA    1 
ATOM   2684  C  C     . ILE A 1 331  ? 142.147 142.577 193.460 1.00 53.29  ? 331  ILE A C     1 
ATOM   2685  O  O     . ILE A 1 331  ? 142.246 143.681 194.006 1.00 57.14  ? 331  ILE A O     1 
ATOM   2686  C  CB    . ILE A 1 331  ? 140.319 142.530 191.706 1.00 48.64  ? 331  ILE A CB    1 
ATOM   2687  C  CG1   . ILE A 1 331  ? 141.213 141.988 190.590 1.00 42.43  ? 331  ILE A CG1   1 
ATOM   2688  C  CG2   . ILE A 1 331  ? 140.273 144.051 191.678 1.00 49.91  ? 331  ILE A CG2   1 
ATOM   2689  C  CD1   . ILE A 1 331  ? 140.596 142.101 189.220 1.00 40.23  ? 331  ILE A CD1   1 
ATOM   2690  N  N     . ILE A 1 332  ? 143.197 141.802 193.197 1.00 49.43  ? 332  ILE A N     1 
ATOM   2691  C  CA    . ILE A 1 332  ? 144.570 142.225 193.445 1.00 42.97  ? 332  ILE A CA    1 
ATOM   2692  C  C     . ILE A 1 332  ? 145.128 142.878 192.188 1.00 44.06  ? 332  ILE A C     1 
ATOM   2693  O  O     . ILE A 1 332  ? 144.614 142.689 191.082 1.00 44.24  ? 332  ILE A O     1 
ATOM   2694  C  CB    . ILE A 1 332  ? 145.441 141.039 193.908 1.00 43.72  ? 332  ILE A CB    1 
ATOM   2695  C  CG1   . ILE A 1 332  ? 145.399 139.903 192.887 1.00 45.57  ? 332  ILE A CG1   1 
ATOM   2696  C  CG2   . ILE A 1 332  ? 144.976 140.542 195.260 1.00 45.29  ? 332  ILE A CG2   1 
ATOM   2697  C  CD1   . ILE A 1 332  ? 146.377 138.792 193.179 1.00 41.42  ? 332  ILE A CD1   1 
ATOM   2698  N  N     . LEU A 1 333  ? 146.196 143.664 192.362 1.00 41.94  ? 333  LEU A N     1 
ATOM   2699  C  CA    . LEU A 1 333  ? 146.763 144.422 191.249 1.00 38.22  ? 333  LEU A CA    1 
ATOM   2700  C  C     . LEU A 1 333  ? 147.360 143.515 190.176 1.00 35.04  ? 333  LEU A C     1 
ATOM   2701  O  O     . LEU A 1 333  ? 147.375 143.880 188.992 1.00 35.16  ? 333  LEU A O     1 
ATOM   2702  C  CB    . LEU A 1 333  ? 147.822 145.390 191.773 1.00 37.66  ? 333  LEU A CB    1 
ATOM   2703  C  CG    . LEU A 1 333  ? 147.336 146.494 192.715 1.00 39.35  ? 333  LEU A CG    1 
ATOM   2704  C  CD1   . LEU A 1 333  ? 148.487 147.390 193.143 1.00 38.59  ? 333  LEU A CD1   1 
ATOM   2705  C  CD2   . LEU A 1 333  ? 146.247 147.312 192.056 1.00 40.13  ? 333  LEU A CD2   1 
ATOM   2706  N  N     . ARG A 1 334  ? 147.860 142.343 190.568 1.00 34.18  ? 334  ARG A N     1 
ATOM   2707  C  CA    . ARG A 1 334  ? 148.468 141.423 189.612 1.00 37.94  ? 334  ARG A CA    1 
ATOM   2708  C  C     . ARG A 1 334  ? 147.472 141.005 188.537 1.00 39.35  ? 334  ARG A C     1 
ATOM   2709  O  O     . ARG A 1 334  ? 147.797 140.976 187.342 1.00 41.18  ? 334  ARG A O     1 
ATOM   2710  C  CB    . ARG A 1 334  ? 149.003 140.196 190.346 1.00 36.15  ? 334  ARG A CB    1 
ATOM   2711  C  CG    . ARG A 1 334  ? 149.735 139.224 189.454 1.00 37.52  ? 334  ARG A CG    1 
ATOM   2712  C  CD    . ARG A 1 334  ? 150.083 137.955 190.197 1.00 45.89  ? 334  ARG A CD    1 
ATOM   2713  N  NE    . ARG A 1 334  ? 150.579 136.926 189.292 1.00 54.53  ? 334  ARG A NE    1 
ATOM   2714  C  CZ    . ARG A 1 334  ? 151.003 135.731 189.676 1.00 53.91  ? 334  ARG A CZ    1 
ATOM   2715  N  NH1   . ARG A 1 334  ? 150.998 135.372 190.949 1.00 52.68  ? 334  ARG A NH1   1 
ATOM   2716  N  NH2   . ARG A 1 334  ? 151.431 134.869 188.759 1.00 49.82  ? 334  ARG A NH2   1 
ATOM   2717  N  N     . LYS A 1 335  ? 146.251 140.665 188.953 1.00 37.54  ? 335  LYS A N     1 
ATOM   2718  C  CA    . LYS A 1 335  ? 145.227 140.237 188.010 1.00 36.45  ? 335  LYS A CA    1 
ATOM   2719  C  C     . LYS A 1 335  ? 144.835 141.364 187.062 1.00 36.11  ? 335  LYS A C     1 
ATOM   2720  O  O     . LYS A 1 335  ? 144.601 141.123 185.871 1.00 38.28  ? 335  LYS A O     1 
ATOM   2721  C  CB    . LYS A 1 335  ? 144.017 139.723 188.789 1.00 37.93  ? 335  LYS A CB    1 
ATOM   2722  C  CG    . LYS A 1 335  ? 142.928 139.098 187.952 1.00 42.06  ? 335  LYS A CG    1 
ATOM   2723  C  CD    . LYS A 1 335  ? 141.832 138.558 188.849 1.00 44.07  ? 335  LYS A CD    1 
ATOM   2724  C  CE    . LYS A 1 335  ? 142.308 137.338 189.625 1.00 41.05  ? 335  LYS A CE    1 
ATOM   2725  N  NZ    . LYS A 1 335  ? 142.386 136.117 188.782 1.00 38.72  ? 335  LYS A NZ    1 
ATOM   2726  N  N     . ILE A 1 336  ? 144.803 142.601 187.559 1.00 33.57  ? 336  ILE A N     1 
ATOM   2727  C  CA    . ILE A 1 336  ? 144.498 143.745 186.707 1.00 32.92  ? 336  ILE A CA    1 
ATOM   2728  C  C     . ILE A 1 336  ? 145.593 143.947 185.666 1.00 32.52  ? 336  ILE A C     1 
ATOM   2729  O  O     . ILE A 1 336  ? 145.312 144.212 184.489 1.00 34.89  ? 336  ILE A O     1 
ATOM   2730  C  CB    . ILE A 1 336  ? 144.300 145.006 187.566 1.00 34.39  ? 336  ILE A CB    1 
ATOM   2731  C  CG1   . ILE A 1 336  ? 143.144 144.814 188.545 1.00 34.65  ? 336  ILE A CG1   1 
ATOM   2732  C  CG2   . ILE A 1 336  ? 144.038 146.212 186.687 1.00 32.66  ? 336  ILE A CG2   1 
ATOM   2733  C  CD1   . ILE A 1 336  ? 143.122 145.835 189.656 1.00 37.13  ? 336  ILE A CD1   1 
ATOM   2734  N  N     . PHE A 1 337  ? 146.857 143.825 186.075 1.00 31.97  ? 337  PHE A N     1 
ATOM   2735  C  CA    . PHE A 1 337  ? 147.942 144.021 185.120 1.00 33.70  ? 337  PHE A CA    1 
ATOM   2736  C  C     . PHE A 1 337  ? 147.959 142.914 184.069 1.00 32.30  ? 337  PHE A C     1 
ATOM   2737  O  O     . PHE A 1 337  ? 148.213 143.176 182.887 1.00 32.82  ? 337  PHE A O     1 
ATOM   2738  C  CB    . PHE A 1 337  ? 149.281 144.108 185.852 1.00 34.06  ? 337  PHE A CB    1 
ATOM   2739  C  CG    . PHE A 1 337  ? 150.452 144.303 184.937 1.00 33.20  ? 337  PHE A CG    1 
ATOM   2740  C  CD1   . PHE A 1 337  ? 150.618 145.500 184.270 1.00 36.40  ? 337  PHE A CD1   1 
ATOM   2741  C  CD2   . PHE A 1 337  ? 151.387 143.302 184.750 1.00 33.89  ? 337  PHE A CD2   1 
ATOM   2742  C  CE1   . PHE A 1 337  ? 151.680 145.696 183.427 1.00 34.47  ? 337  PHE A CE1   1 
ATOM   2743  C  CE2   . PHE A 1 337  ? 152.457 143.496 183.906 1.00 35.54  ? 337  PHE A CE2   1 
ATOM   2744  C  CZ    . PHE A 1 337  ? 152.604 144.696 183.246 1.00 35.75  ? 337  PHE A CZ    1 
ATOM   2745  N  N     . THR A 1 338  ? 147.674 141.674 184.472 1.00 32.62  ? 338  THR A N     1 
ATOM   2746  C  CA    . THR A 1 338  ? 147.583 140.592 183.494 1.00 33.20  ? 338  THR A CA    1 
ATOM   2747  C  C     . THR A 1 338  ? 146.424 140.806 182.526 1.00 33.70  ? 338  THR A C     1 
ATOM   2748  O  O     . THR A 1 338  ? 146.548 140.518 181.322 1.00 38.95  ? 338  THR A O     1 
ATOM   2749  C  CB    . THR A 1 338  ? 147.433 139.251 184.209 1.00 35.58  ? 338  THR A CB    1 
ATOM   2750  O  OG1   . THR A 1 338  ? 148.431 139.142 185.229 1.00 38.67  ? 338  THR A OG1   1 
ATOM   2751  C  CG2   . THR A 1 338  ? 147.605 138.106 183.234 1.00 32.95  ? 338  THR A CG2   1 
ATOM   2752  N  N     . THR A 1 339  ? 145.299 141.319 183.029 1.00 33.38  ? 339  THR A N     1 
ATOM   2753  C  CA    . THR A 1 339  ? 144.177 141.638 182.157 1.00 33.32  ? 339  THR A CA    1 
ATOM   2754  C  C     . THR A 1 339  ? 144.567 142.696 181.136 1.00 33.97  ? 339  THR A C     1 
ATOM   2755  O  O     . THR A 1 339  ? 144.223 142.581 179.956 1.00 35.13  ? 339  THR A O     1 
ATOM   2756  C  CB    . THR A 1 339  ? 142.987 142.111 182.989 1.00 30.75  ? 339  THR A CB    1 
ATOM   2757  O  OG1   . THR A 1 339  ? 142.610 141.081 183.908 1.00 34.90  ? 339  THR A OG1   1 
ATOM   2758  C  CG2   . THR A 1 339  ? 141.810 142.433 182.091 1.00 31.76  ? 339  THR A CG2   1 
ATOM   2759  N  N     . ILE A 1 340  ? 145.294 143.726 181.572 1.00 34.73  ? 340  ILE A N     1 
ATOM   2760  C  CA    . ILE A 1 340  ? 145.775 144.748 180.645 1.00 32.51  ? 340  ILE A CA    1 
ATOM   2761  C  C     . ILE A 1 340  ? 146.699 144.132 179.599 1.00 32.20  ? 340  ILE A C     1 
ATOM   2762  O  O     . ILE A 1 340  ? 146.638 144.475 178.408 1.00 33.80  ? 340  ILE A O     1 
ATOM   2763  C  CB    . ILE A 1 340  ? 146.477 145.879 181.417 1.00 30.99  ? 340  ILE A CB    1 
ATOM   2764  C  CG1   . ILE A 1 340  ? 145.465 146.688 182.228 1.00 30.83  ? 340  ILE A CG1   1 
ATOM   2765  C  CG2   . ILE A 1 340  ? 147.244 146.779 180.472 1.00 28.39  ? 340  ILE A CG2   1 
ATOM   2766  C  CD1   . ILE A 1 340  ? 146.095 147.512 183.327 1.00 33.82  ? 340  ILE A CD1   1 
ATOM   2767  N  N     . SER A 1 341  ? 147.575 143.220 180.029 1.00 35.20  ? 341  SER A N     1 
ATOM   2768  C  CA    . SER A 1 341  ? 148.531 142.613 179.108 1.00 31.07  ? 341  SER A CA    1 
ATOM   2769  C  C     . SER A 1 341  ? 147.827 141.833 178.005 1.00 31.25  ? 341  SER A C     1 
ATOM   2770  O  O     . SER A 1 341  ? 148.226 141.903 176.838 1.00 31.45  ? 341  SER A O     1 
ATOM   2771  C  CB    . SER A 1 341  ? 149.494 141.710 179.875 1.00 31.80  ? 341  SER A CB    1 
ATOM   2772  O  OG    . SER A 1 341  ? 150.340 142.478 180.708 1.00 35.67  ? 341  SER A OG    1 
ATOM   2773  N  N     . PHE A 1 342  ? 146.782 141.079 178.350 1.00 30.31  ? 342  PHE A N     1 
ATOM   2774  C  CA    . PHE A 1 342  ? 146.033 140.388 177.297 1.00 29.75  ? 342  PHE A CA    1 
ATOM   2775  C  C     . PHE A 1 342  ? 145.180 141.349 176.469 1.00 34.14  ? 342  PHE A C     1 
ATOM   2776  O  O     . PHE A 1 342  ? 145.014 141.157 175.254 1.00 33.97  ? 342  PHE A O     1 
ATOM   2777  C  CB    . PHE A 1 342  ? 145.160 139.281 177.887 1.00 32.27  ? 342  PHE A CB    1 
ATOM   2778  C  CG    . PHE A 1 342  ? 145.927 138.080 178.359 1.00 34.02  ? 342  PHE A CG    1 
ATOM   2779  C  CD1   . PHE A 1 342  ? 146.777 137.410 177.500 1.00 35.17  ? 342  PHE A CD1   1 
ATOM   2780  C  CD2   . PHE A 1 342  ? 145.782 137.607 179.649 1.00 32.60  ? 342  PHE A CD2   1 
ATOM   2781  C  CE1   . PHE A 1 342  ? 147.478 136.300 177.921 1.00 36.11  ? 342  PHE A CE1   1 
ATOM   2782  C  CE2   . PHE A 1 342  ? 146.481 136.497 180.075 1.00 33.48  ? 342  PHE A CE2   1 
ATOM   2783  C  CZ    . PHE A 1 342  ? 147.329 135.843 179.209 1.00 36.67  ? 342  PHE A CZ    1 
ATOM   2784  N  N     . CYS A 1 343  ? 144.630 142.386 177.103 1.00 35.85  ? 343  CYS A N     1 
ATOM   2785  C  CA    . CYS A 1 343  ? 143.735 143.285 176.390 1.00 29.71  ? 343  CYS A CA    1 
ATOM   2786  C  C     . CYS A 1 343  ? 144.472 144.131 175.366 1.00 30.83  ? 343  CYS A C     1 
ATOM   2787  O  O     . CYS A 1 343  ? 143.864 144.564 174.385 1.00 35.58  ? 343  CYS A O     1 
ATOM   2788  C  CB    . CYS A 1 343  ? 142.983 144.174 177.376 1.00 32.14  ? 343  CYS A CB    1 
ATOM   2789  S  SG    . CYS A 1 343  ? 141.710 143.295 178.304 1.00 51.45  ? 343  CYS A SG    1 
ATOM   2790  N  N     . ILE A 1 344  ? 145.769 144.378 175.562 1.00 30.44  ? 344  ILE A N     1 
ATOM   2791  C  CA    . ILE A 1 344  ? 146.533 145.087 174.534 1.00 28.77  ? 344  ILE A CA    1 
ATOM   2792  C  C     . ILE A 1 344  ? 146.488 144.322 173.216 1.00 29.77  ? 344  ILE A C     1 
ATOM   2793  O  O     . ILE A 1 344  ? 146.160 144.879 172.159 1.00 28.15  ? 344  ILE A O     1 
ATOM   2794  C  CB    . ILE A 1 344  ? 147.983 145.317 174.993 1.00 27.24  ? 344  ILE A CB    1 
ATOM   2795  C  CG1   . ILE A 1 344  ? 148.048 146.411 176.054 1.00 31.49  ? 344  ILE A CG1   1 
ATOM   2796  C  CG2   . ILE A 1 344  ? 148.860 145.680 173.812 1.00 25.25  ? 344  ILE A CG2   1 
ATOM   2797  C  CD1   . ILE A 1 344  ? 149.283 146.341 176.911 1.00 31.08  ? 344  ILE A CD1   1 
ATOM   2798  N  N     . VAL A 1 345  ? 146.793 143.023 173.267 1.00 31.88  ? 345  VAL A N     1 
ATOM   2799  C  CA    . VAL A 1 345  ? 146.805 142.207 172.058 1.00 29.59  ? 345  VAL A CA    1 
ATOM   2800  C  C     . VAL A 1 345  ? 145.395 142.047 171.508 1.00 31.08  ? 345  VAL A C     1 
ATOM   2801  O  O     . VAL A 1 345  ? 145.189 142.035 170.289 1.00 31.83  ? 345  VAL A O     1 
ATOM   2802  C  CB    . VAL A 1 345  ? 147.464 140.845 172.340 1.00 29.24  ? 345  VAL A CB    1 
ATOM   2803  C  CG1   . VAL A 1 345  ? 147.589 140.032 171.060 1.00 31.88  ? 345  VAL A CG1   1 
ATOM   2804  C  CG2   . VAL A 1 345  ? 148.821 141.040 172.980 1.00 26.43  ? 345  VAL A CG2   1 
ATOM   2805  N  N     . LEU A 1 346  ? 144.401 141.930 172.391 1.00 32.87  ? 346  LEU A N     1 
ATOM   2806  C  CA    . LEU A 1 346  ? 143.022 141.822 171.918 1.00 33.03  ? 346  LEU A CA    1 
ATOM   2807  C  C     . LEU A 1 346  ? 142.594 143.076 171.156 1.00 31.17  ? 346  LEU A C     1 
ATOM   2808  O  O     . LEU A 1 346  ? 142.000 142.989 170.074 1.00 31.19  ? 346  LEU A O     1 
ATOM   2809  C  CB    . LEU A 1 346  ? 142.089 141.549 173.097 1.00 35.71  ? 346  LEU A CB    1 
ATOM   2810  C  CG    . LEU A 1 346  ? 140.621 141.252 172.800 1.00 38.02  ? 346  LEU A CG    1 
ATOM   2811  C  CD1   . LEU A 1 346  ? 140.477 139.886 172.179 1.00 37.87  ? 346  LEU A CD1   1 
ATOM   2812  C  CD2   . LEU A 1 346  ? 139.824 141.320 174.084 1.00 41.14  ? 346  LEU A CD2   1 
ATOM   2813  N  N     . ARG A 1 347  ? 142.902 144.257 171.703 1.00 30.60  ? 347  ARG A N     1 
ATOM   2814  C  CA    . ARG A 1 347  ? 142.555 145.505 171.033 1.00 30.02  ? 347  ARG A CA    1 
ATOM   2815  C  C     . ARG A 1 347  ? 143.296 145.645 169.712 1.00 30.70  ? 347  ARG A C     1 
ATOM   2816  O  O     . ARG A 1 347  ? 142.718 146.090 168.713 1.00 30.95  ? 347  ARG A O     1 
ATOM   2817  C  CB    . ARG A 1 347  ? 142.863 146.698 171.937 1.00 29.54  ? 347  ARG A CB    1 
ATOM   2818  C  CG    . ARG A 1 347  ? 141.959 146.821 173.143 1.00 29.82  ? 347  ARG A CG    1 
ATOM   2819  C  CD    . ARG A 1 347  ? 142.316 148.039 173.981 1.00 35.27  ? 347  ARG A CD    1 
ATOM   2820  N  NE    . ARG A 1 347  ? 143.726 148.081 174.349 1.00 38.11  ? 347  ARG A NE    1 
ATOM   2821  C  CZ    . ARG A 1 347  ? 144.574 149.021 173.956 1.00 34.89  ? 347  ARG A CZ    1 
ATOM   2822  N  NH1   . ARG A 1 347  ? 144.182 150.036 173.205 1.00 32.61  ? 347  ARG A NH1   1 
ATOM   2823  N  NH2   . ARG A 1 347  ? 145.847 148.943 174.329 1.00 30.89  ? 347  ARG A NH2   1 
ATOM   2824  N  N     . MET A 1 348  ? 144.580 145.280 169.686 1.00 32.71  ? 348  MET A N     1 
ATOM   2825  C  CA    . MET A 1 348  ? 145.330 145.374 168.438 1.00 30.74  ? 348  MET A CA    1 
ATOM   2826  C  C     . MET A 1 348  ? 144.739 144.460 167.373 1.00 30.98  ? 348  MET A C     1 
ATOM   2827  O  O     . MET A 1 348  ? 144.652 144.841 166.202 1.00 27.42  ? 348  MET A O     1 
ATOM   2828  C  CB    . MET A 1 348  ? 146.801 145.040 168.677 1.00 29.53  ? 348  MET A CB    1 
ATOM   2829  C  CG    . MET A 1 348  ? 147.714 145.397 167.517 1.00 30.15  ? 348  MET A CG    1 
ATOM   2830  S  SD    . MET A 1 348  ? 147.872 147.169 167.258 1.00 43.28  ? 348  MET A SD    1 
ATOM   2831  C  CE    . MET A 1 348  ? 148.669 147.198 165.659 1.00 36.66  ? 348  MET A CE    1 
ATOM   2832  N  N     . ALA A 1 349  ? 144.319 143.254 167.761 1.00 34.19  ? 349  ALA A N     1 
ATOM   2833  C  CA    . ALA A 1 349  ? 143.703 142.346 166.799 1.00 27.40  ? 349  ALA A CA    1 
ATOM   2834  C  C     . ALA A 1 349  ? 142.369 142.880 166.296 1.00 27.14  ? 349  ALA A C     1 
ATOM   2835  O  O     . ALA A 1 349  ? 142.070 142.784 165.102 1.00 28.42  ? 349  ALA A O     1 
ATOM   2836  C  CB    . ALA A 1 349  ? 143.519 140.964 167.423 1.00 29.48  ? 349  ALA A CB    1 
ATOM   2837  N  N     . VAL A 1 350  ? 141.554 143.448 167.184 1.00 31.65  ? 350  VAL A N     1 
ATOM   2838  C  CA    . VAL A 1 350  ? 140.185 143.782 166.799 1.00 29.38  ? 350  VAL A CA    1 
ATOM   2839  C  C     . VAL A 1 350  ? 140.126 145.107 166.048 1.00 31.20  ? 350  VAL A C     1 
ATOM   2840  O  O     . VAL A 1 350  ? 139.556 145.186 164.954 1.00 37.01  ? 350  VAL A O     1 
ATOM   2841  C  CB    . VAL A 1 350  ? 139.266 143.789 168.032 1.00 29.40  ? 350  VAL A CB    1 
ATOM   2842  C  CG1   . VAL A 1 350  ? 137.906 144.350 167.666 1.00 31.48  ? 350  VAL A CG1   1 
ATOM   2843  C  CG2   . VAL A 1 350  ? 139.121 142.387 168.584 1.00 29.05  ? 350  VAL A CG2   1 
ATOM   2844  N  N     . THR A 1 351  ? 140.698 146.170 166.609 1.00 29.78  ? 351  THR A N     1 
ATOM   2845  C  CA    . THR A 1 351  ? 140.472 147.510 166.081 1.00 29.46  ? 351  THR A CA    1 
ATOM   2846  C  C     . THR A 1 351  ? 141.527 147.972 165.085 1.00 29.56  ? 351  THR A C     1 
ATOM   2847  O  O     . THR A 1 351  ? 141.380 149.058 164.519 1.00 31.48  ? 351  THR A O     1 
ATOM   2848  C  CB    . THR A 1 351  ? 140.384 148.523 167.229 1.00 29.95  ? 351  THR A CB    1 
ATOM   2849  O  OG1   . THR A 1 351  ? 141.690 148.756 167.766 1.00 29.64  ? 351  THR A OG1   1 
ATOM   2850  C  CG2   . THR A 1 351  ? 139.480 148.006 168.328 1.00 28.87  ? 351  THR A CG2   1 
ATOM   2851  N  N     . ARG A 1 352  ? 142.585 147.196 164.855 1.00 29.35  ? 352  ARG A N     1 
ATOM   2852  C  CA    . ARG A 1 352  ? 143.629 147.635 163.934 1.00 28.50  ? 352  ARG A CA    1 
ATOM   2853  C  C     . ARG A 1 352  ? 143.822 146.691 162.753 1.00 27.67  ? 352  ARG A C     1 
ATOM   2854  O  O     . ARG A 1 352  ? 143.896 147.133 161.604 1.00 30.26  ? 352  ARG A O     1 
ATOM   2855  C  CB    . ARG A 1 352  ? 144.953 147.802 164.678 1.00 29.59  ? 352  ARG A CB    1 
ATOM   2856  C  CG    . ARG A 1 352  ? 145.323 149.238 164.980 1.00 27.55  ? 352  ARG A CG    1 
ATOM   2857  C  CD    . ARG A 1 352  ? 145.485 150.027 163.699 1.00 32.28  ? 352  ARG A CD    1 
ATOM   2858  N  NE    . ARG A 1 352  ? 146.138 151.313 163.909 1.00 36.23  ? 352  ARG A NE    1 
ATOM   2859  C  CZ    . ARG A 1 352  ? 145.541 152.389 164.400 1.00 36.89  ? 352  ARG A CZ    1 
ATOM   2860  N  NH1   . ARG A 1 352  ? 144.268 152.371 164.753 1.00 37.63  ? 352  ARG A NH1   1 
ATOM   2861  N  NH2   . ARG A 1 352  ? 146.240 153.510 164.538 1.00 35.42  ? 352  ARG A NH2   1 
ATOM   2862  N  N     . GLN A 1 353  ? 143.913 145.391 163.025 1.00 29.36  ? 353  GLN A N     1 
ATOM   2863  C  CA    . GLN A 1 353  ? 144.332 144.442 162.000 1.00 24.43  ? 353  GLN A CA    1 
ATOM   2864  C  C     . GLN A 1 353  ? 143.167 143.980 161.132 1.00 27.27  ? 353  GLN A C     1 
ATOM   2865  O  O     . GLN A 1 353  ? 143.329 143.806 159.920 1.00 35.66  ? 353  GLN A O     1 
ATOM   2866  C  CB    . GLN A 1 353  ? 145.022 143.252 162.661 1.00 26.88  ? 353  GLN A CB    1 
ATOM   2867  C  CG    . GLN A 1 353  ? 146.383 143.600 163.235 1.00 30.98  ? 353  GLN A CG    1 
ATOM   2868  C  CD    . GLN A 1 353  ? 147.035 142.438 163.943 1.00 36.89  ? 353  GLN A CD    1 
ATOM   2869  O  OE1   . GLN A 1 353  ? 146.416 141.395 164.144 1.00 38.65  ? 353  GLN A OE1   1 
ATOM   2870  N  NE2   . GLN A 1 353  ? 148.295 142.605 164.318 1.00 35.28  ? 353  GLN A NE2   1 
ATOM   2871  N  N     . PHE A 1 354  ? 141.992 143.772 161.730 1.00 22.98  ? 354  PHE A N     1 
ATOM   2872  C  CA    . PHE A 1 354  ? 140.863 143.244 160.965 1.00 24.99  ? 354  PHE A CA    1 
ATOM   2873  C  C     . PHE A 1 354  ? 140.294 144.265 159.981 1.00 28.25  ? 354  PHE A C     1 
ATOM   2874  O  O     . PHE A 1 354  ? 140.144 143.925 158.791 1.00 29.90  ? 354  PHE A O     1 
ATOM   2875  C  CB    . PHE A 1 354  ? 139.800 142.709 161.931 1.00 27.51  ? 354  PHE A CB    1 
ATOM   2876  C  CG    . PHE A 1 354  ? 138.661 141.999 161.262 1.00 26.59  ? 354  PHE A CG    1 
ATOM   2877  C  CD1   . PHE A 1 354  ? 138.826 140.721 160.760 1.00 25.29  ? 354  PHE A CD1   1 
ATOM   2878  C  CD2   . PHE A 1 354  ? 137.422 142.601 161.152 1.00 26.16  ? 354  PHE A CD2   1 
ATOM   2879  C  CE1   . PHE A 1 354  ? 137.783 140.064 160.152 1.00 27.33  ? 354  PHE A CE1   1 
ATOM   2880  C  CE2   . PHE A 1 354  ? 136.373 141.947 160.545 1.00 26.63  ? 354  PHE A CE2   1 
ATOM   2881  C  CZ    . PHE A 1 354  ? 136.554 140.676 160.044 1.00 28.48  ? 354  PHE A CZ    1 
ATOM   2882  N  N     . PRO A 1 355  ? 139.945 145.496 160.383 1.00 28.19  ? 355  PRO A N     1 
ATOM   2883  C  CA    . PRO A 1 355  ? 139.403 146.446 159.397 1.00 28.73  ? 355  PRO A CA    1 
ATOM   2884  C  C     . PRO A 1 355  ? 140.365 146.781 158.273 1.00 29.84  ? 355  PRO A C     1 
ATOM   2885  O  O     . PRO A 1 355  ? 139.922 146.978 157.134 1.00 32.43  ? 355  PRO A O     1 
ATOM   2886  C  CB    . PRO A 1 355  ? 139.071 147.686 160.242 1.00 27.42  ? 355  PRO A CB    1 
ATOM   2887  C  CG    . PRO A 1 355  ? 139.827 147.531 161.494 1.00 26.75  ? 355  PRO A CG    1 
ATOM   2888  C  CD    . PRO A 1 355  ? 139.942 146.072 161.739 1.00 25.92  ? 355  PRO A CD    1 
ATOM   2889  N  N     . TRP A 1 356  ? 141.668 146.838 158.551 1.00 26.44  ? 356  TRP A N     1 
ATOM   2890  C  CA    . TRP A 1 356  ? 142.637 147.084 157.489 1.00 26.49  ? 356  TRP A CA    1 
ATOM   2891  C  C     . TRP A 1 356  ? 142.626 145.959 156.461 1.00 27.95  ? 356  TRP A C     1 
ATOM   2892  O  O     . TRP A 1 356  ? 142.682 146.216 155.254 1.00 29.60  ? 356  TRP A O     1 
ATOM   2893  C  CB    . TRP A 1 356  ? 144.034 147.259 158.085 1.00 27.33  ? 356  TRP A CB    1 
ATOM   2894  C  CG    . TRP A 1 356  ? 144.410 148.670 158.473 1.00 33.99  ? 356  TRP A CG    1 
ATOM   2895  C  CD1   . TRP A 1 356  ? 145.484 149.374 158.016 1.00 37.14  ? 356  TRP A CD1   1 
ATOM   2896  C  CD2   . TRP A 1 356  ? 143.720 149.543 159.380 1.00 38.54  ? 356  TRP A CD2   1 
ATOM   2897  N  NE1   . TRP A 1 356  ? 145.515 150.621 158.585 1.00 40.19  ? 356  TRP A NE1   1 
ATOM   2898  C  CE2   . TRP A 1 356  ? 144.442 150.751 159.424 1.00 39.92  ? 356  TRP A CE2   1 
ATOM   2899  C  CE3   . TRP A 1 356  ? 142.566 149.423 160.158 1.00 37.53  ? 356  TRP A CE3   1 
ATOM   2900  C  CZ2   . TRP A 1 356  ? 144.050 151.828 160.214 1.00 35.87  ? 356  TRP A CZ2   1 
ATOM   2901  C  CZ3   . TRP A 1 356  ? 142.180 150.493 160.942 1.00 33.85  ? 356  TRP A CZ3   1 
ATOM   2902  C  CH2   . TRP A 1 356  ? 142.919 151.678 160.964 1.00 34.24  ? 356  TRP A CH2   1 
ATOM   2903  N  N     . ALA A 1 357  ? 142.539 144.709 156.920 1.00 26.24  ? 357  ALA A N     1 
ATOM   2904  C  CA    . ALA A 1 357  ? 142.466 143.576 156.004 1.00 24.29  ? 357  ALA A CA    1 
ATOM   2905  C  C     . ALA A 1 357  ? 141.190 143.618 155.170 1.00 30.70  ? 357  ALA A C     1 
ATOM   2906  O  O     . ALA A 1 357  ? 141.211 143.335 153.964 1.00 32.07  ? 357  ALA A O     1 
ATOM   2907  C  CB    . ALA A 1 357  ? 142.558 142.267 156.785 1.00 22.33  ? 357  ALA A CB    1 
ATOM   2908  N  N     . VAL A 1 358  ? 140.061 143.951 155.800 1.00 28.69  ? 358  VAL A N     1 
ATOM   2909  C  CA    . VAL A 1 358  ? 138.802 144.021 155.058 1.00 26.63  ? 358  VAL A CA    1 
ATOM   2910  C  C     . VAL A 1 358  ? 138.869 145.109 153.990 1.00 27.38  ? 358  VAL A C     1 
ATOM   2911  O  O     . VAL A 1 358  ? 138.442 144.910 152.841 1.00 28.22  ? 358  VAL A O     1 
ATOM   2912  C  CB    . VAL A 1 358  ? 137.622 144.237 156.025 1.00 26.58  ? 358  VAL A CB    1 
ATOM   2913  C  CG1   . VAL A 1 358  ? 136.371 144.616 155.262 1.00 29.94  ? 358  VAL A CG1   1 
ATOM   2914  C  CG2   . VAL A 1 358  ? 137.379 142.991 156.844 1.00 24.48  ? 358  VAL A CG2   1 
ATOM   2915  N  N     . GLN A 1 359  ? 139.417 146.273 154.345 1.00 26.66  ? 359  GLN A N     1 
ATOM   2916  C  CA    . GLN A 1 359  ? 139.547 147.357 153.379 1.00 28.40  ? 359  GLN A CA    1 
ATOM   2917  C  C     . GLN A 1 359  ? 140.500 146.979 152.251 1.00 30.12  ? 359  GLN A C     1 
ATOM   2918  O  O     . GLN A 1 359  ? 140.280 147.347 151.090 1.00 33.53  ? 359  GLN A O     1 
ATOM   2919  C  CB    . GLN A 1 359  ? 140.024 148.625 154.086 1.00 29.86  ? 359  GLN A CB    1 
ATOM   2920  C  CG    . GLN A 1 359  ? 139.972 149.873 153.232 1.00 37.15  ? 359  GLN A CG    1 
ATOM   2921  C  CD    . GLN A 1 359  ? 138.558 150.247 152.844 1.00 44.34  ? 359  GLN A CD    1 
ATOM   2922  O  OE1   . GLN A 1 359  ? 137.750 150.623 153.691 1.00 48.07  ? 359  GLN A OE1   1 
ATOM   2923  N  NE2   . GLN A 1 359  ? 138.246 150.126 151.563 1.00 42.86  ? 359  GLN A NE2   1 
ATOM   2924  N  N     . THR A 1 360  ? 141.569 146.250 152.576 1.00 27.84  ? 360  THR A N     1 
ATOM   2925  C  CA    . THR A 1 360  ? 142.503 145.802 151.551 1.00 25.90  ? 360  THR A CA    1 
ATOM   2926  C  C     . THR A 1 360  ? 141.829 144.854 150.572 1.00 26.06  ? 360  THR A C     1 
ATOM   2927  O  O     . THR A 1 360  ? 142.054 144.944 149.360 1.00 29.55  ? 360  THR A O     1 
ATOM   2928  C  CB    . THR A 1 360  ? 143.711 145.129 152.205 1.00 27.46  ? 360  THR A CB    1 
ATOM   2929  O  OG1   . THR A 1 360  ? 144.412 146.087 153.005 1.00 32.96  ? 360  THR A OG1   1 
ATOM   2930  C  CG2   . THR A 1 360  ? 144.653 144.577 151.159 1.00 26.31  ? 360  THR A CG2   1 
ATOM   2931  N  N     . TRP A 1 361  ? 140.998 143.940 151.076 1.00 27.72  ? 361  TRP A N     1 
ATOM   2932  C  CA    . TRP A 1 361  ? 140.256 143.056 150.180 1.00 26.93  ? 361  TRP A CA    1 
ATOM   2933  C  C     . TRP A 1 361  ? 139.312 143.844 149.283 1.00 27.76  ? 361  TRP A C     1 
ATOM   2934  O  O     . TRP A 1 361  ? 139.218 143.571 148.078 1.00 31.71  ? 361  TRP A O     1 
ATOM   2935  C  CB    . TRP A 1 361  ? 139.492 142.005 150.981 1.00 26.41  ? 361  TRP A CB    1 
ATOM   2936  C  CG    . TRP A 1 361  ? 140.333 140.838 151.375 1.00 28.39  ? 361  TRP A CG    1 
ATOM   2937  C  CD1   . TRP A 1 361  ? 140.836 140.569 152.611 1.00 29.09  ? 361  TRP A CD1   1 
ATOM   2938  C  CD2   . TRP A 1 361  ? 140.743 139.757 150.531 1.00 30.37  ? 361  TRP A CD2   1 
ATOM   2939  N  NE1   . TRP A 1 361  ? 141.552 139.399 152.586 1.00 31.58  ? 361  TRP A NE1   1 
ATOM   2940  C  CE2   . TRP A 1 361  ? 141.506 138.879 151.320 1.00 32.47  ? 361  TRP A CE2   1 
ATOM   2941  C  CE3   . TRP A 1 361  ? 140.544 139.451 149.182 1.00 34.01  ? 361  TRP A CE3   1 
ATOM   2942  C  CZ2   . TRP A 1 361  ? 142.072 137.715 150.807 1.00 33.04  ? 361  TRP A CZ2   1 
ATOM   2943  C  CZ3   . TRP A 1 361  ? 141.105 138.295 148.674 1.00 32.50  ? 361  TRP A CZ3   1 
ATOM   2944  C  CH2   . TRP A 1 361  ? 141.859 137.442 149.485 1.00 29.98  ? 361  TRP A CH2   1 
ATOM   2945  N  N     . TYR A 1 362  ? 138.618 144.837 149.846 1.00 29.88  ? 362  TYR A N     1 
ATOM   2946  C  CA    . TYR A 1 362  ? 137.759 145.688 149.025 1.00 28.09  ? 362  TYR A CA    1 
ATOM   2947  C  C     . TYR A 1 362  ? 138.541 146.345 147.895 1.00 29.32  ? 362  TYR A C     1 
ATOM   2948  O  O     . TYR A 1 362  ? 138.144 146.273 146.724 1.00 30.40  ? 362  TYR A O     1 
ATOM   2949  C  CB    . TYR A 1 362  ? 137.090 146.756 149.888 1.00 27.82  ? 362  TYR A CB    1 
ATOM   2950  C  CG    . TYR A 1 362  ? 135.752 146.363 150.462 1.00 30.44  ? 362  TYR A CG    1 
ATOM   2951  C  CD1   . TYR A 1 362  ? 134.666 146.125 149.634 1.00 33.38  ? 362  TYR A CD1   1 
ATOM   2952  C  CD2   . TYR A 1 362  ? 135.567 146.249 151.830 1.00 33.05  ? 362  TYR A CD2   1 
ATOM   2953  C  CE1   . TYR A 1 362  ? 133.439 145.779 150.153 1.00 39.46  ? 362  TYR A CE1   1 
ATOM   2954  C  CE2   . TYR A 1 362  ? 134.343 145.901 152.357 1.00 35.45  ? 362  TYR A CE2   1 
ATOM   2955  C  CZ    . TYR A 1 362  ? 133.284 145.667 151.515 1.00 40.72  ? 362  TYR A CZ    1 
ATOM   2956  O  OH    . TYR A 1 362  ? 132.062 145.320 152.035 1.00 41.00  ? 362  TYR A OH    1 
ATOM   2957  N  N     . ASP A 1 363  ? 139.668 146.979 148.227 1.00 29.47  ? 363  ASP A N     1 
ATOM   2958  C  CA    . ASP A 1 363  ? 140.437 147.700 147.218 1.00 28.98  ? 363  ASP A CA    1 
ATOM   2959  C  C     . ASP A 1 363  ? 140.981 146.759 146.151 1.00 28.22  ? 363  ASP A C     1 
ATOM   2960  O  O     . ASP A 1 363  ? 140.902 147.056 144.951 1.00 27.65  ? 363  ASP A O     1 
ATOM   2961  C  CB    . ASP A 1 363  ? 141.578 148.466 147.881 1.00 31.21  ? 363  ASP A CB    1 
ATOM   2962  C  CG    . ASP A 1 363  ? 141.090 149.451 148.914 1.00 40.81  ? 363  ASP A CG    1 
ATOM   2963  O  OD1   . ASP A 1 363  ? 139.862 149.525 149.129 1.00 40.06  ? 363  ASP A OD1   1 
ATOM   2964  O  OD2   . ASP A 1 363  ? 141.935 150.143 149.519 1.00 45.80  ? 363  ASP A OD2   1 
ATOM   2965  N  N     . SER A 1 364  ? 141.518 145.610 146.568 1.00 28.68  ? 364  SER A N     1 
ATOM   2966  C  CA    . SER A 1 364  ? 142.108 144.675 145.619 1.00 26.11  ? 364  SER A CA    1 
ATOM   2967  C  C     . SER A 1 364  ? 141.060 144.124 144.663 1.00 28.43  ? 364  SER A C     1 
ATOM   2968  O  O     . SER A 1 364  ? 141.274 144.096 143.444 1.00 34.44  ? 364  SER A O     1 
ATOM   2969  C  CB    . SER A 1 364  ? 142.802 143.540 146.369 1.00 29.50  ? 364  SER A CB    1 
ATOM   2970  O  OG    . SER A 1 364  ? 144.002 143.992 146.967 1.00 30.47  ? 364  SER A OG    1 
ATOM   2971  N  N     . LEU A 1 365  ? 139.911 143.694 145.192 1.00 29.52  ? 365  LEU A N     1 
ATOM   2972  C  CA    . LEU A 1 365  ? 138.894 143.123 144.318 1.00 29.31  ? 365  LEU A CA    1 
ATOM   2973  C  C     . LEU A 1 365  ? 138.270 144.176 143.415 1.00 30.14  ? 365  LEU A C     1 
ATOM   2974  O  O     . LEU A 1 365  ? 137.939 143.877 142.262 1.00 31.65  ? 365  LEU A O     1 
ATOM   2975  C  CB    . LEU A 1 365  ? 137.823 142.412 145.140 1.00 30.32  ? 365  LEU A CB    1 
ATOM   2976  C  CG    . LEU A 1 365  ? 138.296 141.111 145.792 1.00 32.18  ? 365  LEU A CG    1 
ATOM   2977  C  CD1   . LEU A 1 365  ? 137.260 140.584 146.768 1.00 35.65  ? 365  LEU A CD1   1 
ATOM   2978  C  CD2   . LEU A 1 365  ? 138.623 140.070 144.732 1.00 34.04  ? 365  LEU A CD2   1 
ATOM   2979  N  N     . GLY A 1 366  ? 138.135 145.416 143.892 1.00 32.66  ? 366  GLY A N     1 
ATOM   2980  C  CA    . GLY A 1 366  ? 137.638 146.468 143.022 1.00 31.87  ? 366  GLY A CA    1 
ATOM   2981  C  C     . GLY A 1 366  ? 138.586 146.773 141.880 1.00 33.30  ? 366  GLY A C     1 
ATOM   2982  O  O     . GLY A 1 366  ? 138.161 146.914 140.727 1.00 38.02  ? 366  GLY A O     1 
ATOM   2983  N  N     . ALA A 1 367  ? 139.887 146.856 142.175 1.00 32.37  ? 367  ALA A N     1 
ATOM   2984  C  CA    . ALA A 1 367  ? 140.867 147.089 141.120 1.00 34.20  ? 367  ALA A CA    1 
ATOM   2985  C  C     . ALA A 1 367  ? 140.876 145.947 140.113 1.00 31.75  ? 367  ALA A C     1 
ATOM   2986  O  O     . ALA A 1 367  ? 140.949 146.182 138.900 1.00 34.59  ? 367  ALA A O     1 
ATOM   2987  C  CB    . ALA A 1 367  ? 142.257 147.278 141.722 1.00 33.00  ? 367  ALA A CB    1 
ATOM   2988  N  N     . ILE A 1 368  ? 140.805 144.705 140.594 1.00 31.19  ? 368  ILE A N     1 
ATOM   2989  C  CA    . ILE A 1 368  ? 140.816 143.564 139.684 1.00 29.67  ? 368  ILE A CA    1 
ATOM   2990  C  C     . ILE A 1 368  ? 139.579 143.572 138.794 1.00 29.66  ? 368  ILE A C     1 
ATOM   2991  O  O     . ILE A 1 368  ? 139.664 143.295 137.593 1.00 31.61  ? 368  ILE A O     1 
ATOM   2992  C  CB    . ILE A 1 368  ? 140.952 142.248 140.472 1.00 31.25  ? 368  ILE A CB    1 
ATOM   2993  C  CG1   . ILE A 1 368  ? 142.376 142.103 141.010 1.00 28.78  ? 368  ILE A CG1   1 
ATOM   2994  C  CG2   . ILE A 1 368  ? 140.593 141.062 139.605 1.00 33.99  ? 368  ILE A CG2   1 
ATOM   2995  C  CD1   . ILE A 1 368  ? 142.510 141.101 142.127 1.00 30.85  ? 368  ILE A CD1   1 
ATOM   2996  N  N     . ASN A 1 369  ? 138.413 143.899 139.359 1.00 31.46  ? 369  ASN A N     1 
ATOM   2997  C  CA    . ASN A 1 369  ? 137.200 143.945 138.545 1.00 31.49  ? 369  ASN A CA    1 
ATOM   2998  C  C     . ASN A 1 369  ? 137.268 145.053 137.502 1.00 34.94  ? 369  ASN A C     1 
ATOM   2999  O  O     . ASN A 1 369  ? 136.820 144.870 136.364 1.00 34.71  ? 369  ASN A O     1 
ATOM   3000  C  CB    . ASN A 1 369  ? 135.976 144.123 139.439 1.00 31.06  ? 369  ASN A CB    1 
ATOM   3001  C  CG    . ASN A 1 369  ? 135.657 142.880 140.233 1.00 37.64  ? 369  ASN A CG    1 
ATOM   3002  O  OD1   . ASN A 1 369  ? 136.126 141.789 139.914 1.00 37.96  ? 369  ASN A OD1   1 
ATOM   3003  N  ND2   . ASN A 1 369  ? 134.857 143.037 141.278 1.00 35.88  ? 369  ASN A ND2   1 
ATOM   3004  N  N     . LYS A 1 370  ? 137.828 146.208 137.867 1.00 34.83  ? 370  LYS A N     1 
ATOM   3005  C  CA    . LYS A 1 370  ? 137.954 147.294 136.901 1.00 32.28  ? 370  LYS A CA    1 
ATOM   3006  C  C     . LYS A 1 370  ? 138.911 146.924 135.772 1.00 35.57  ? 370  LYS A C     1 
ATOM   3007  O  O     . LYS A 1 370  ? 138.635 147.198 134.594 1.00 39.17  ? 370  LYS A O     1 
ATOM   3008  C  CB    . LYS A 1 370  ? 138.412 148.562 137.616 1.00 35.24  ? 370  LYS A CB    1 
ATOM   3009  C  CG    . LYS A 1 370  ? 138.197 149.835 136.836 1.00 43.73  ? 370  LYS A CG    1 
ATOM   3010  C  CD    . LYS A 1 370  ? 138.750 151.017 137.602 1.00 46.33  ? 370  LYS A CD    1 
ATOM   3011  C  CE    . LYS A 1 370  ? 138.122 151.094 138.982 1.00 43.39  ? 370  LYS A CE    1 
ATOM   3012  N  NZ    . LYS A 1 370  ? 138.504 152.334 139.704 1.00 56.87  ? 370  LYS A NZ    1 
ATOM   3013  N  N     . ILE A 1 371  ? 140.026 146.272 136.107 1.00 33.14  ? 371  ILE A N     1 
ATOM   3014  C  CA    . ILE A 1 371  ? 140.963 145.836 135.077 1.00 27.09  ? 371  ILE A CA    1 
ATOM   3015  C  C     . ILE A 1 371  ? 140.317 144.787 134.181 1.00 28.00  ? 371  ILE A C     1 
ATOM   3016  O  O     . ILE A 1 371  ? 140.516 144.787 132.961 1.00 32.41  ? 371  ILE A O     1 
ATOM   3017  C  CB    . ILE A 1 371  ? 142.263 145.320 135.718 1.00 27.58  ? 371  ILE A CB    1 
ATOM   3018  C  CG1   . ILE A 1 371  ? 143.030 146.473 136.364 1.00 30.81  ? 371  ILE A CG1   1 
ATOM   3019  C  CG2   . ILE A 1 371  ? 143.135 144.633 134.689 1.00 25.38  ? 371  ILE A CG2   1 
ATOM   3020  C  CD1   . ILE A 1 371  ? 144.099 146.026 137.325 1.00 28.00  ? 371  ILE A CD1   1 
ATOM   3021  N  N     . GLN A 1 372  ? 139.523 143.886 134.763 1.00 29.54  ? 372  GLN A N     1 
ATOM   3022  C  CA    . GLN A 1 372  ? 138.817 142.895 133.958 1.00 27.93  ? 372  GLN A CA    1 
ATOM   3023  C  C     . GLN A 1 372  ? 137.833 143.560 133.007 1.00 33.39  ? 372  GLN A C     1 
ATOM   3024  O  O     . GLN A 1 372  ? 137.675 143.121 131.863 1.00 36.41  ? 372  GLN A O     1 
ATOM   3025  C  CB    . GLN A 1 372  ? 138.090 141.897 134.854 1.00 26.76  ? 372  GLN A CB    1 
ATOM   3026  C  CG    . GLN A 1 372  ? 137.415 140.787 134.080 1.00 30.19  ? 372  GLN A CG    1 
ATOM   3027  C  CD    . GLN A 1 372  ? 136.640 139.847 134.967 1.00 38.41  ? 372  GLN A CD    1 
ATOM   3028  O  OE1   . GLN A 1 372  ? 136.964 139.673 136.140 1.00 40.96  ? 372  GLN A OE1   1 
ATOM   3029  N  NE2   . GLN A 1 372  ? 135.612 139.224 134.409 1.00 39.44  ? 372  GLN A NE2   1 
ATOM   3030  N  N     . ASP A 1 373  ? 137.148 144.609 133.469 1.00 36.94  ? 373  ASP A N     1 
ATOM   3031  C  CA    . ASP A 1 373  ? 136.263 145.351 132.576 1.00 34.36  ? 373  ASP A CA    1 
ATOM   3032  C  C     . ASP A 1 373  ? 137.043 145.998 131.440 1.00 34.80  ? 373  ASP A C     1 
ATOM   3033  O  O     . ASP A 1 373  ? 136.555 146.068 130.307 1.00 34.37  ? 373  ASP A O     1 
ATOM   3034  C  CB    . ASP A 1 373  ? 135.473 146.404 133.351 1.00 38.38  ? 373  ASP A CB    1 
ATOM   3035  C  CG    . ASP A 1 373  ? 134.445 145.793 134.281 1.00 53.37  ? 373  ASP A CG    1 
ATOM   3036  O  OD1   . ASP A 1 373  ? 134.071 144.619 134.069 1.00 54.69  ? 373  ASP A OD1   1 
ATOM   3037  O  OD2   . ASP A 1 373  ? 133.997 146.497 135.210 1.00 59.22  ? 373  ASP A OD2   1 
ATOM   3038  N  N     . PHE A 1 374  ? 138.258 146.476 131.718 1.00 33.66  ? 374  PHE A N     1 
ATOM   3039  C  CA    . PHE A 1 374  ? 139.067 147.044 130.642 1.00 30.61  ? 374  PHE A CA    1 
ATOM   3040  C  C     . PHE A 1 374  ? 139.460 145.987 129.616 1.00 30.44  ? 374  PHE A C     1 
ATOM   3041  O  O     . PHE A 1 374  ? 139.478 146.261 128.411 1.00 31.77  ? 374  PHE A O     1 
ATOM   3042  C  CB    . PHE A 1 374  ? 140.318 147.712 131.205 1.00 33.19  ? 374  PHE A CB    1 
ATOM   3043  C  CG    . PHE A 1 374  ? 141.139 148.420 130.166 1.00 34.81  ? 374  PHE A CG    1 
ATOM   3044  C  CD1   . PHE A 1 374  ? 140.807 149.700 129.757 1.00 36.74  ? 374  PHE A CD1   1 
ATOM   3045  C  CD2   . PHE A 1 374  ? 142.229 147.798 129.583 1.00 33.50  ? 374  PHE A CD2   1 
ATOM   3046  C  CE1   . PHE A 1 374  ? 141.555 150.350 128.803 1.00 31.36  ? 374  PHE A CE1   1 
ATOM   3047  C  CE2   . PHE A 1 374  ? 142.977 148.444 128.624 1.00 31.54  ? 374  PHE A CE2   1 
ATOM   3048  C  CZ    . PHE A 1 374  ? 142.640 149.721 128.235 1.00 29.27  ? 374  PHE A CZ    1 
ATOM   3049  N  N     . LEU A 1 375  ? 139.784 144.776 130.071 1.00 32.43  ? 375  LEU A N     1 
ATOM   3050  C  CA    . LEU A 1 375  ? 140.326 143.743 129.196 1.00 30.59  ? 375  LEU A CA    1 
ATOM   3051  C  C     . LEU A 1 375  ? 139.294 143.140 128.254 1.00 31.49  ? 375  LEU A C     1 
ATOM   3052  O  O     . LEU A 1 375  ? 139.669 142.329 127.402 1.00 34.37  ? 375  LEU A O     1 
ATOM   3053  C  CB    . LEU A 1 375  ? 140.957 142.629 130.028 1.00 27.87  ? 375  LEU A CB    1 
ATOM   3054  C  CG    . LEU A 1 375  ? 142.272 142.949 130.736 1.00 27.93  ? 375  LEU A CG    1 
ATOM   3055  C  CD1   . LEU A 1 375  ? 142.728 141.762 131.562 1.00 27.74  ? 375  LEU A CD1   1 
ATOM   3056  C  CD2   . LEU A 1 375  ? 143.335 143.348 129.740 1.00 29.06  ? 375  LEU A CD2   1 
ATOM   3057  N  N     . GLN A 1 376  ? 138.015 143.492 128.384 1.00 33.61  ? 376  GLN A N     1 
ATOM   3058  C  CA    . GLN A 1 376  ? 136.966 142.892 127.566 1.00 34.19  ? 376  GLN A CA    1 
ATOM   3059  C  C     . GLN A 1 376  ? 136.284 143.907 126.653 1.00 36.93  ? 376  GLN A C     1 
ATOM   3060  O  O     . GLN A 1 376  ? 135.152 143.680 126.220 1.00 38.98  ? 376  GLN A O     1 
ATOM   3061  C  CB    . GLN A 1 376  ? 135.936 142.190 128.451 1.00 32.01  ? 376  GLN A CB    1 
ATOM   3062  C  CG    . GLN A 1 376  ? 136.470 140.945 129.142 1.00 32.83  ? 376  GLN A CG    1 
ATOM   3063  C  CD    . GLN A 1 376  ? 135.394 140.168 129.871 1.00 39.09  ? 376  GLN A CD    1 
ATOM   3064  O  OE1   . GLN A 1 376  ? 135.321 138.945 129.771 1.00 41.69  ? 376  GLN A OE1   1 
ATOM   3065  N  NE2   . GLN A 1 376  ? 134.557 140.875 130.616 1.00 38.62  ? 376  GLN A NE2   1 
ATOM   3066  N  N     . LYS A 1 377  ? 136.946 145.022 126.357 1.00 36.07  ? 377  LYS A N     1 
ATOM   3067  C  CA    . LYS A 1 377  ? 136.397 146.017 125.449 1.00 37.34  ? 377  LYS A CA    1 
ATOM   3068  C  C     . LYS A 1 377  ? 136.522 145.565 123.995 1.00 40.10  ? 377  LYS A C     1 
ATOM   3069  O  O     . LYS A 1 377  ? 137.249 144.624 123.665 1.00 39.21  ? 377  LYS A O     1 
ATOM   3070  C  CB    . LYS A 1 377  ? 137.093 147.361 125.650 1.00 37.68  ? 377  LYS A CB    1 
ATOM   3071  C  CG    . LYS A 1 377  ? 136.533 148.167 126.807 1.00 33.81  ? 377  LYS A CG    1 
ATOM   3072  C  CD    . LYS A 1 377  ? 137.332 149.432 127.049 1.00 38.20  ? 377  LYS A CD    1 
ATOM   3073  C  CE    . LYS A 1 377  ? 136.506 150.462 127.795 1.00 41.28  ? 377  LYS A CE    1 
ATOM   3074  N  NZ    . LYS A 1 377  ? 135.972 149.921 129.073 1.00 46.39  ? 377  LYS A NZ    1 
ATOM   3075  N  N     . GLN A 1 378  ? 135.788 146.254 123.121 1.00 41.21  ? 378  GLN A N     1 
ATOM   3076  C  CA    . GLN A 1 378  ? 135.735 145.898 121.708 1.00 43.76  ? 378  GLN A CA    1 
ATOM   3077  C  C     . GLN A 1 378  ? 137.077 146.141 121.023 1.00 45.41  ? 378  GLN A C     1 
ATOM   3078  O  O     . GLN A 1 378  ? 137.763 147.128 121.298 1.00 47.44  ? 378  GLN A O     1 
ATOM   3079  C  CB    . GLN A 1 378  ? 134.637 146.699 121.013 1.00 44.53  ? 378  GLN A CB    1 
ATOM   3080  C  CG    . GLN A 1 378  ? 133.810 145.894 120.037 1.00 51.56  ? 378  GLN A CG    1 
ATOM   3081  C  CD    . GLN A 1 378  ? 133.216 146.747 118.939 1.00 60.99  ? 378  GLN A CD    1 
ATOM   3082  O  OE1   . GLN A 1 378  ? 132.825 147.892 119.168 1.00 63.87  ? 378  GLN A OE1   1 
ATOM   3083  N  NE2   . GLN A 1 378  ? 133.143 146.193 117.734 1.00 61.33  ? 378  GLN A NE2   1 
ATOM   3084  N  N     . GLU A 1 379  ? 137.447 145.233 120.121 1.00 41.72  ? 379  GLU A N     1 
ATOM   3085  C  CA    . GLU A 1 379  ? 138.768 145.232 119.507 1.00 38.59  ? 379  GLU A CA    1 
ATOM   3086  C  C     . GLU A 1 379  ? 138.739 145.587 118.022 1.00 42.75  ? 379  GLU A C     1 
ATOM   3087  O  O     . GLU A 1 379  ? 137.720 145.474 117.338 1.00 46.06  ? 379  GLU A O     1 
ATOM   3088  C  CB    . GLU A 1 379  ? 139.443 143.872 119.678 1.00 38.71  ? 379  GLU A CB    1 
ATOM   3089  C  CG    . GLU A 1 379  ? 139.798 143.521 121.099 1.00 44.26  ? 379  GLU A CG    1 
ATOM   3090  C  CD    . GLU A 1 379  ? 140.627 142.262 121.181 1.00 50.49  ? 379  GLU A CD    1 
ATOM   3091  O  OE1   . GLU A 1 379  ? 140.925 141.682 120.116 1.00 49.54  ? 379  GLU A OE1   1 
ATOM   3092  O  OE2   . GLU A 1 379  ? 140.988 141.857 122.304 1.00 53.21  ? 379  GLU A OE2   1 
ATOM   3093  N  N     . TYR A 1 380  ? 139.904 146.022 117.544 1.00 43.43  ? 380  TYR A N     1 
ATOM   3094  C  CA    . TYR A 1 380  ? 140.145 146.281 116.130 1.00 39.18  ? 380  TYR A CA    1 
ATOM   3095  C  C     . TYR A 1 380  ? 140.176 144.982 115.330 1.00 42.00  ? 380  TYR A C     1 
ATOM   3096  O  O     . TYR A 1 380  ? 140.760 143.985 115.765 1.00 47.52  ? 380  TYR A O     1 
ATOM   3097  C  CB    . TYR A 1 380  ? 141.468 147.034 115.987 1.00 36.72  ? 380  TYR A CB    1 
ATOM   3098  C  CG    . TYR A 1 380  ? 142.024 147.162 114.588 1.00 40.96  ? 380  TYR A CG    1 
ATOM   3099  C  CD1   . TYR A 1 380  ? 141.535 148.114 113.707 1.00 45.07  ? 380  TYR A CD1   1 
ATOM   3100  C  CD2   . TYR A 1 380  ? 143.071 146.357 114.165 1.00 40.46  ? 380  TYR A CD2   1 
ATOM   3101  C  CE1   . TYR A 1 380  ? 142.056 148.241 112.436 1.00 42.65  ? 380  TYR A CE1   1 
ATOM   3102  C  CE2   . TYR A 1 380  ? 143.596 146.479 112.897 1.00 41.19  ? 380  TYR A CE2   1 
ATOM   3103  C  CZ    . TYR A 1 380  ? 143.085 147.423 112.037 1.00 40.92  ? 380  TYR A CZ    1 
ATOM   3104  O  OH    . TYR A 1 380  ? 143.605 147.546 110.771 1.00 43.59  ? 380  TYR A OH    1 
ATOM   3105  N  N     . LYS A 1 381  ? 139.533 144.990 114.163 1.00 43.47  ? 381  LYS A N     1 
ATOM   3106  C  CA    . LYS A 1 381  ? 139.560 143.845 113.261 1.00 46.10  ? 381  LYS A CA    1 
ATOM   3107  C  C     . LYS A 1 381  ? 140.757 143.923 112.320 1.00 49.28  ? 381  LYS A C     1 
ATOM   3108  O  O     . LYS A 1 381  ? 140.971 144.942 111.658 1.00 50.97  ? 381  LYS A O     1 
ATOM   3109  C  CB    . LYS A 1 381  ? 138.272 143.772 112.446 1.00 48.17  ? 381  LYS A CB    1 
ATOM   3110  C  CG    . LYS A 1 381  ? 137.100 143.145 113.165 1.00 49.27  ? 381  LYS A CG    1 
ATOM   3111  C  CD    . LYS A 1 381  ? 135.891 143.107 112.251 1.00 55.75  ? 381  LYS A CD    1 
ATOM   3112  C  CE    . LYS A 1 381  ? 136.126 142.157 111.088 1.00 60.35  ? 381  LYS A CE    1 
ATOM   3113  N  NZ    . LYS A 1 381  ? 135.077 142.282 110.040 1.00 59.90  ? 381  LYS A NZ    1 
ATOM   3114  N  N     . THR A 1 382  ? 141.527 142.840 112.254 1.00 47.83  ? 382  THR A N     1 
ATOM   3115  C  CA    . THR A 1 382  ? 142.686 142.789 111.374 1.00 48.64  ? 382  THR A CA    1 
ATOM   3116  C  C     . THR A 1 382  ? 142.259 142.578 109.925 1.00 48.77  ? 382  THR A C     1 
ATOM   3117  O  O     . THR A 1 382  ? 141.320 141.832 109.639 1.00 51.78  ? 382  THR A O     1 
ATOM   3118  C  CB    . THR A 1 382  ? 143.631 141.672 111.814 1.00 49.09  ? 382  THR A CB    1 
ATOM   3119  O  OG1   . THR A 1 382  ? 143.884 141.792 113.218 1.00 50.76  ? 382  THR A OG1   1 
ATOM   3120  C  CG2   . THR A 1 382  ? 144.953 141.772 111.073 1.00 46.87  ? 382  THR A CG2   1 
ATOM   3121  N  N     . LEU A 1 383  ? 142.956 143.245 109.009 1.00 47.20  ? 383  LEU A N     1 
ATOM   3122  C  CA    . LEU A 1 383  ? 142.619 143.181 107.593 1.00 49.65  ? 383  LEU A CA    1 
ATOM   3123  C  C     . LEU A 1 383  ? 142.952 141.818 106.993 1.00 51.15  ? 383  LEU A C     1 
ATOM   3124  O  O     . LEU A 1 383  ? 143.779 141.066 107.512 1.00 54.09  ? 383  LEU A O     1 
ATOM   3125  C  CB    . LEU A 1 383  ? 143.361 144.269 106.820 1.00 47.89  ? 383  LEU A CB    1 
ATOM   3126  C  CG    . LEU A 1 383  ? 143.045 145.723 107.163 1.00 49.72  ? 383  LEU A CG    1 
ATOM   3127  C  CD1   . LEU A 1 383  ? 144.006 146.651 106.443 1.00 44.19  ? 383  LEU A CD1   1 
ATOM   3128  C  CD2   . LEU A 1 383  ? 141.607 146.045 106.791 1.00 49.03  ? 383  LEU A CD2   1 
ATOM   3129  N  N     . GLU A 1 384  ? 142.285 141.508 105.884 1.00 46.85  ? 384  GLU A N     1 
ATOM   3130  C  CA    . GLU A 1 384  ? 142.603 140.316 105.112 1.00 46.99  ? 384  GLU A CA    1 
ATOM   3131  C  C     . GLU A 1 384  ? 143.985 140.438 104.482 1.00 46.50  ? 384  GLU A C     1 
ATOM   3132  O  O     . GLU A 1 384  ? 144.369 141.501 103.988 1.00 48.75  ? 384  GLU A O     1 
ATOM   3133  C  CB    . GLU A 1 384  ? 141.551 140.098 104.025 1.00 50.21  ? 384  GLU A CB    1 
ATOM   3134  C  CG    . GLU A 1 384  ? 141.721 138.819 103.229 1.00 51.72  ? 384  GLU A CG    1 
ATOM   3135  C  CD    . GLU A 1 384  ? 141.429 137.578 104.045 1.00 60.80  ? 384  GLU A CD    1 
ATOM   3136  O  OE1   . GLU A 1 384  ? 140.754 137.694 105.089 1.00 65.29  ? 384  GLU A OE1   1 
ATOM   3137  O  OE2   . GLU A 1 384  ? 141.876 136.485 103.642 1.00 60.89  ? 384  GLU A OE2   1 
ATOM   3138  N  N     . TYR A 1 385  ? 144.734 139.340 104.500 1.00 42.62  ? 385  TYR A N     1 
ATOM   3139  C  CA    . TYR A 1 385  ? 146.092 139.288 103.971 1.00 38.72  ? 385  TYR A CA    1 
ATOM   3140  C  C     . TYR A 1 385  ? 146.125 138.348 102.774 1.00 41.51  ? 385  TYR A C     1 
ATOM   3141  O  O     . TYR A 1 385  ? 145.824 137.158 102.909 1.00 44.56  ? 385  TYR A O     1 
ATOM   3142  C  CB    . TYR A 1 385  ? 147.061 138.824 105.056 1.00 38.13  ? 385  TYR A CB    1 
ATOM   3143  C  CG    . TYR A 1 385  ? 148.520 139.102 104.783 1.00 35.35  ? 385  TYR A CG    1 
ATOM   3144  C  CD1   . TYR A 1 385  ? 149.297 138.195 104.080 1.00 35.98  ? 385  TYR A CD1   1 
ATOM   3145  C  CD2   . TYR A 1 385  ? 149.120 140.264 105.241 1.00 34.93  ? 385  TYR A CD2   1 
ATOM   3146  C  CE1   . TYR A 1 385  ? 150.629 138.439 103.841 1.00 36.58  ? 385  TYR A CE1   1 
ATOM   3147  C  CE2   . TYR A 1 385  ? 150.452 140.517 105.003 1.00 35.89  ? 385  TYR A CE2   1 
ATOM   3148  C  CZ    . TYR A 1 385  ? 151.201 139.601 104.303 1.00 39.26  ? 385  TYR A CZ    1 
ATOM   3149  O  OH    . TYR A 1 385  ? 152.531 139.848 104.062 1.00 44.67  ? 385  TYR A OH    1 
ATOM   3150  N  N     . ASN A 1 386  ? 146.492 138.879 101.609 1.00 39.27  ? 386  ASN A N     1 
ATOM   3151  C  CA    . ASN A 1 386  ? 146.551 138.072 100.392 1.00 38.11  ? 386  ASN A CA    1 
ATOM   3152  C  C     . ASN A 1 386  ? 147.521 138.745 99.430  1.00 42.58  ? 386  ASN A C     1 
ATOM   3153  O  O     . ASN A 1 386  ? 147.201 139.795 98.868  1.00 48.48  ? 386  ASN A O     1 
ATOM   3154  C  CB    . ASN A 1 386  ? 145.168 137.926 99.772  1.00 37.72  ? 386  ASN A CB    1 
ATOM   3155  C  CG    . ASN A 1 386  ? 145.109 136.834 98.728  1.00 45.25  ? 386  ASN A CG    1 
ATOM   3156  O  OD1   . ASN A 1 386  ? 146.133 136.275 98.339  1.00 48.67  ? 386  ASN A OD1   1 
ATOM   3157  N  ND2   . ASN A 1 386  ? 143.906 136.519 98.268  1.00 42.13  ? 386  ASN A ND2   1 
ATOM   3158  N  N     . LEU A 1 387  ? 148.696 138.140 99.242  1.00 41.37  ? 387  LEU A N     1 
ATOM   3159  C  CA    . LEU A 1 387  ? 149.725 138.743 98.405  1.00 42.99  ? 387  LEU A CA    1 
ATOM   3160  C  C     . LEU A 1 387  ? 149.360 138.764 96.927  1.00 47.57  ? 387  LEU A C     1 
ATOM   3161  O  O     . LEU A 1 387  ? 149.978 139.513 96.164  1.00 51.31  ? 387  LEU A O     1 
ATOM   3162  C  CB    . LEU A 1 387  ? 151.056 138.014 98.586  1.00 43.83  ? 387  LEU A CB    1 
ATOM   3163  C  CG    . LEU A 1 387  ? 151.716 138.071 99.964  1.00 45.26  ? 387  LEU A CG    1 
ATOM   3164  C  CD1   . LEU A 1 387  ? 152.950 137.193 99.988  1.00 41.19  ? 387  LEU A CD1   1 
ATOM   3165  C  CD2   . LEU A 1 387  ? 152.075 139.500 100.325 1.00 43.55  ? 387  LEU A CD2   1 
ATOM   3166  N  N     . THR A 1 388  ? 148.388 137.962 96.496  1.00 48.15  ? 388  THR A N     1 
ATOM   3167  C  CA    . THR A 1 388  ? 148.087 137.809 95.074  1.00 53.37  ? 388  THR A CA    1 
ATOM   3168  C  C     . THR A 1 388  ? 146.881 138.630 94.640  1.00 53.19  ? 388  THR A C     1 
ATOM   3169  O  O     . THR A 1 388  ? 146.144 138.220 93.740  1.00 54.45  ? 388  THR A O     1 
ATOM   3170  C  CB    . THR A 1 388  ? 147.871 136.339 94.737  1.00 51.77  ? 388  THR A CB    1 
ATOM   3171  O  OG1   . THR A 1 388  ? 146.589 135.921 95.220  1.00 50.65  ? 388  THR A OG1   1 
ATOM   3172  C  CG2   . THR A 1 388  ? 148.941 135.491 95.384  1.00 49.72  ? 388  THR A CG2   1 
ATOM   3173  N  N     . THR A 1 389  ? 146.649 139.793 95.247  1.00 51.69  ? 389  THR A N     1 
ATOM   3174  C  CA    . THR A 1 389  ? 145.530 140.646 94.858  1.00 55.20  ? 389  THR A CA    1 
ATOM   3175  C  C     . THR A 1 389  ? 145.943 141.674 93.811  1.00 58.51  ? 389  THR A C     1 
ATOM   3176  O  O     . THR A 1 389  ? 145.384 141.698 92.710  1.00 56.48  ? 389  THR A O     1 
ATOM   3177  C  CB    . THR A 1 389  ? 144.938 141.346 96.089  1.00 55.25  ? 389  THR A CB    1 
ATOM   3178  O  OG1   . THR A 1 389  ? 144.711 140.385 97.124  1.00 53.28  ? 389  THR A OG1   1 
ATOM   3179  C  CG2   . THR A 1 389  ? 143.618 142.009 95.738  1.00 57.71  ? 389  THR A CG2   1 
ATOM   3180  N  N     . THR A 1 390  ? 146.922 142.522 94.137  1.00 58.12  ? 390  THR A N     1 
ATOM   3181  C  CA    . THR A 1 390  ? 147.467 143.520 93.212  1.00 59.57  ? 390  THR A CA    1 
ATOM   3182  C  C     . THR A 1 390  ? 146.374 144.395 92.602  1.00 60.77  ? 390  THR A C     1 
ATOM   3183  O  O     . THR A 1 390  ? 146.496 144.850 91.464  1.00 59.95  ? 390  THR A O     1 
ATOM   3184  C  CB    . THR A 1 390  ? 148.300 142.870 92.101  1.00 59.99  ? 390  THR A CB    1 
ATOM   3185  O  OG1   . THR A 1 390  ? 147.430 142.374 91.076  1.00 58.00  ? 390  THR A OG1   1 
ATOM   3186  C  CG2   . THR A 1 390  ? 149.146 141.730 92.651  1.00 57.76  ? 390  THR A CG2   1 
ATOM   3187  N  N     . GLU A 1 391  ? 145.294 144.629 93.344  1.00 61.50  ? 391  GLU A N     1 
ATOM   3188  C  CA    . GLU A 1 391  ? 144.168 145.398 92.833  1.00 56.34  ? 391  GLU A CA    1 
ATOM   3189  C  C     . GLU A 1 391  ? 143.412 146.012 94.001  1.00 58.57  ? 391  GLU A C     1 
ATOM   3190  O  O     . GLU A 1 391  ? 143.063 145.306 94.951  1.00 59.50  ? 391  GLU A O     1 
ATOM   3191  C  CB    . GLU A 1 391  ? 143.233 144.512 92.006  1.00 55.43  ? 391  GLU A CB    1 
ATOM   3192  C  CG    . GLU A 1 391  ? 142.154 145.267 91.270  1.00 56.72  ? 391  GLU A CG    1 
ATOM   3193  C  CD    . GLU A 1 391  ? 142.584 145.663 89.879  1.00 67.51  ? 391  GLU A CD    1 
ATOM   3194  O  OE1   . GLU A 1 391  ? 143.694 145.265 89.471  1.00 67.57  ? 391  GLU A OE1   1 
ATOM   3195  O  OE2   . GLU A 1 391  ? 141.816 146.370 89.193  1.00 68.54  ? 391  GLU A OE2   1 
ATOM   3196  N  N     . VAL A 1 392  ? 143.167 147.317 93.931  1.00 52.05  ? 392  VAL A N     1 
ATOM   3197  C  CA    . VAL A 1 392  ? 142.438 148.044 94.964  1.00 49.11  ? 392  VAL A CA    1 
ATOM   3198  C  C     . VAL A 1 392  ? 141.081 148.418 94.385  1.00 50.60  ? 392  VAL A C     1 
ATOM   3199  O  O     . VAL A 1 392  ? 140.998 149.210 93.439  1.00 53.05  ? 392  VAL A O     1 
ATOM   3200  C  CB    . VAL A 1 392  ? 143.204 149.288 95.435  1.00 44.82  ? 392  VAL A CB    1 
ATOM   3201  C  CG1   . VAL A 1 392  ? 142.457 149.978 96.562  1.00 42.93  ? 392  VAL A CG1   1 
ATOM   3202  C  CG2   . VAL A 1 392  ? 144.610 148.914 95.864  1.00 45.86  ? 392  VAL A CG2   1 
ATOM   3203  N  N     . VAL A 1 393  ? 140.014 147.854 94.949  1.00 49.38  ? 393  VAL A N     1 
ATOM   3204  C  CA    . VAL A 1 393  ? 138.657 148.047 94.451  1.00 48.25  ? 393  VAL A CA    1 
ATOM   3205  C  C     . VAL A 1 393  ? 137.769 148.514 95.593  1.00 50.46  ? 393  VAL A C     1 
ATOM   3206  O  O     . VAL A 1 393  ? 137.821 147.958 96.695  1.00 52.91  ? 393  VAL A O     1 
ATOM   3207  C  CB    . VAL A 1 393  ? 138.080 146.761 93.830  1.00 50.32  ? 393  VAL A CB    1 
ATOM   3208  C  CG1   . VAL A 1 393  ? 136.844 147.082 93.015  1.00 51.30  ? 393  VAL A CG1   1 
ATOM   3209  C  CG2   . VAL A 1 393  ? 139.114 146.073 92.967  1.00 55.93  ? 393  VAL A CG2   1 
ATOM   3210  N  N     . MET A 1 394  ? 136.955 149.530 95.326  1.00 53.79  ? 394  MET A N     1 
ATOM   3211  C  CA    . MET A 1 394  ? 135.924 149.995 96.240  1.00 51.22  ? 394  MET A CA    1 
ATOM   3212  C  C     . MET A 1 394  ? 134.604 150.057 95.489  1.00 54.21  ? 394  MET A C     1 
ATOM   3213  O  O     . MET A 1 394  ? 134.566 150.479 94.330  1.00 55.29  ? 394  MET A O     1 
ATOM   3214  C  CB    . MET A 1 394  ? 136.274 151.367 96.819  1.00 47.32  ? 394  MET A CB    1 
ATOM   3215  C  CG    . MET A 1 394  ? 135.322 151.844 97.891  1.00 51.51  ? 394  MET A CG    1 
ATOM   3216  S  SD    . MET A 1 394  ? 135.869 153.355 98.706  1.00 66.33  ? 394  MET A SD    1 
ATOM   3217  C  CE    . MET A 1 394  ? 137.170 152.719 99.756  1.00 42.86  ? 394  MET A CE    1 
ATOM   3218  N  N     . GLU A 1 395  ? 133.525 149.627 96.140  1.00 52.29  ? 395  GLU A N     1 
ATOM   3219  C  CA    . GLU A 1 395  ? 132.218 149.608 95.490  1.00 54.18  ? 395  GLU A CA    1 
ATOM   3220  C  C     . GLU A 1 395  ? 131.121 149.880 96.508  1.00 56.40  ? 395  GLU A C     1 
ATOM   3221  O  O     . GLU A 1 395  ? 131.028 149.188 97.526  1.00 58.80  ? 395  GLU A O     1 
ATOM   3222  C  CB    . GLU A 1 395  ? 131.986 148.274 94.773  1.00 53.48  ? 395  GLU A CB    1 
ATOM   3223  C  CG    . GLU A 1 395  ? 132.009 147.049 95.669  1.00 58.31  ? 395  GLU A CG    1 
ATOM   3224  C  CD    . GLU A 1 395  ? 133.343 146.331 95.638  1.00 63.70  ? 395  GLU A CD    1 
ATOM   3225  O  OE1   . GLU A 1 395  ? 134.368 146.997 95.389  1.00 60.95  ? 395  GLU A OE1   1 
ATOM   3226  O  OE2   . GLU A 1 395  ? 133.369 145.104 95.871  1.00 67.44  ? 395  GLU A OE2   1 
ATOM   3227  N  N     . ASN A 1 396  ? 130.308 150.901 96.230  1.00 57.65  ? 396  ASN A N     1 
ATOM   3228  C  CA    . ASN A 1 396  ? 129.093 151.200 96.991  1.00 54.75  ? 396  ASN A CA    1 
ATOM   3229  C  C     . ASN A 1 396  ? 129.368 151.331 98.488  1.00 53.47  ? 396  ASN A C     1 
ATOM   3230  O  O     . ASN A 1 396  ? 128.585 150.877 99.325  1.00 57.88  ? 396  ASN A O     1 
ATOM   3231  C  CB    . ASN A 1 396  ? 128.012 150.146 96.732  1.00 60.32  ? 396  ASN A CB    1 
ATOM   3232  C  CG    . ASN A 1 396  ? 127.868 149.787 95.257  1.00 66.85  ? 396  ASN A CG    1 
ATOM   3233  O  OD1   . ASN A 1 396  ? 128.278 150.552 94.384  1.00 67.07  ? 396  ASN A OD1   1 
ATOM   3234  N  ND2   . ASN A 1 396  ? 127.341 148.600 94.975  1.00 68.55  ? 396  ASN A ND2   1 
ATOM   3235  N  N     . VAL A 1 397  ? 130.488 151.958 98.833  1.00 50.94  ? 397  VAL A N     1 
ATOM   3236  C  CA    . VAL A 1 397  ? 130.857 152.132 100.234 1.00 51.93  ? 397  VAL A CA    1 
ATOM   3237  C  C     . VAL A 1 397  ? 130.158 153.368 100.790 1.00 51.46  ? 397  VAL A C     1 
ATOM   3238  O  O     . VAL A 1 397  ? 130.311 154.474 100.261 1.00 52.88  ? 397  VAL A O     1 
ATOM   3239  C  CB    . VAL A 1 397  ? 132.379 152.232 100.403 1.00 47.42  ? 397  VAL A CB    1 
ATOM   3240  C  CG1   . VAL A 1 397  ? 132.728 152.954 101.694 1.00 46.14  ? 397  VAL A CG1   1 
ATOM   3241  C  CG2   . VAL A 1 397  ? 132.991 150.850 100.402 1.00 48.15  ? 397  VAL A CG2   1 
ATOM   3242  N  N     . THR A 1 398  ? 129.367 153.175 101.843 1.00 49.78  ? 398  THR A N     1 
ATOM   3243  C  CA    . THR A 1 398  ? 128.804 154.259 102.635 1.00 49.66  ? 398  THR A CA    1 
ATOM   3244  C  C     . THR A 1 398  ? 129.146 154.014 104.097 1.00 48.63  ? 398  THR A C     1 
ATOM   3245  O  O     . THR A 1 398  ? 129.090 152.877 104.573 1.00 49.67  ? 398  THR A O     1 
ATOM   3246  C  CB    . THR A 1 398  ? 127.283 154.371 102.469 1.00 51.13  ? 398  THR A CB    1 
ATOM   3247  O  OG1   . THR A 1 398  ? 126.633 153.795 103.607 1.00 52.61  ? 398  THR A OG1   1 
ATOM   3248  C  CG2   . THR A 1 398  ? 126.820 153.649 101.215 1.00 50.01  ? 398  THR A CG2   1 
ATOM   3249  N  N     . ALA A 1 399  ? 129.499 155.081 104.811 1.00 43.67  ? 399  ALA A N     1 
ATOM   3250  C  CA    . ALA A 1 399  ? 130.009 154.948 106.166 1.00 43.08  ? 399  ALA A CA    1 
ATOM   3251  C  C     . ALA A 1 399  ? 129.446 156.051 107.048 1.00 45.34  ? 399  ALA A C     1 
ATOM   3252  O  O     . ALA A 1 399  ? 128.990 157.090 106.568 1.00 48.86  ? 399  ALA A O     1 
ATOM   3253  C  CB    . ALA A 1 399  ? 131.541 154.983 106.193 1.00 46.35  ? 399  ALA A CB    1 
ATOM   3254  N  N     . PHE A 1 400  ? 129.475 155.799 108.356 1.00 46.78  ? 400  PHE A N     1 
ATOM   3255  C  CA    . PHE A 1 400  ? 129.051 156.753 109.369 1.00 44.34  ? 400  PHE A CA    1 
ATOM   3256  C  C     . PHE A 1 400  ? 130.105 156.830 110.461 1.00 44.62  ? 400  PHE A C     1 
ATOM   3257  O  O     . PHE A 1 400  ? 130.629 155.803 110.900 1.00 48.20  ? 400  PHE A O     1 
ATOM   3258  C  CB    . PHE A 1 400  ? 127.708 156.363 110.007 1.00 46.25  ? 400  PHE A CB    1 
ATOM   3259  C  CG    . PHE A 1 400  ? 126.543 156.391 109.060 1.00 50.93  ? 400  PHE A CG    1 
ATOM   3260  C  CD1   . PHE A 1 400  ? 126.239 155.287 108.283 1.00 53.06  ? 400  PHE A CD1   1 
ATOM   3261  C  CD2   . PHE A 1 400  ? 125.738 157.513 108.966 1.00 54.34  ? 400  PHE A CD2   1 
ATOM   3262  C  CE1   . PHE A 1 400  ? 125.165 155.307 107.418 1.00 55.09  ? 400  PHE A CE1   1 
ATOM   3263  C  CE2   . PHE A 1 400  ? 124.661 157.539 108.105 1.00 57.43  ? 400  PHE A CE2   1 
ATOM   3264  C  CZ    . PHE A 1 400  ? 124.374 156.436 107.330 1.00 58.18  ? 400  PHE A CZ    1 
ATOM   3265  N  N     . TRP A 1 401  ? 130.419 158.050 110.896 1.00 42.53  ? 401  TRP A N     1 
ATOM   3266  C  CA    . TRP A 1 401  ? 131.260 158.211 112.075 1.00 43.45  ? 401  TRP A CA    1 
ATOM   3267  C  C     . TRP A 1 401  ? 130.499 157.940 113.364 1.00 50.29  ? 401  TRP A C     1 
ATOM   3268  O  O     . TRP A 1 401  ? 131.123 157.628 114.383 1.00 53.97  ? 401  TRP A O     1 
ATOM   3269  C  CB    . TRP A 1 401  ? 131.869 159.612 112.112 1.00 40.16  ? 401  TRP A CB    1 
ATOM   3270  C  CG    . TRP A 1 401  ? 133.115 159.739 111.302 1.00 37.45  ? 401  TRP A CG    1 
ATOM   3271  C  CD1   . TRP A 1 401  ? 133.286 160.473 110.170 1.00 35.60  ? 401  TRP A CD1   1 
ATOM   3272  C  CD2   . TRP A 1 401  ? 134.376 159.126 111.579 1.00 37.02  ? 401  TRP A CD2   1 
ATOM   3273  N  NE1   . TRP A 1 401  ? 134.575 160.346 109.715 1.00 34.63  ? 401  TRP A NE1   1 
ATOM   3274  C  CE2   . TRP A 1 401  ? 135.264 159.524 110.565 1.00 34.53  ? 401  TRP A CE2   1 
ATOM   3275  C  CE3   . TRP A 1 401  ? 134.839 158.273 112.583 1.00 41.70  ? 401  TRP A CE3   1 
ATOM   3276  C  CZ2   . TRP A 1 401  ? 136.589 159.100 110.524 1.00 35.05  ? 401  TRP A CZ2   1 
ATOM   3277  C  CZ3   . TRP A 1 401  ? 136.153 157.852 112.542 1.00 41.64  ? 401  TRP A CZ3   1 
ATOM   3278  C  CH2   . TRP A 1 401  ? 137.013 158.266 111.520 1.00 38.43  ? 401  TRP A CH2   1 
ATOM   3279  N  N     . GLU A 1 402  ? 129.177 158.052 113.342 1.00 53.66  ? 402  GLU A N     1 
ATOM   3280  C  CA    . GLU A 1 402  ? 128.362 157.791 114.520 1.00 54.27  ? 402  GLU A CA    1 
ATOM   3281  C  C     . GLU A 1 402  ? 128.403 156.315 114.893 1.00 54.35  ? 402  GLU A C     1 
ATOM   3282  O  O     . GLU A 1 402  ? 127.368 155.702 115.149 1.00 56.10  ? 402  GLU A O     1 
ATOM   3283  C  CB    . GLU A 1 402  ? 126.918 158.234 114.278 1.00 51.55  ? 402  GLU A CB    1 
ATOM   3284  N  N     . GLY A 1 437  ? 121.691 160.329 111.057 1.00 76.52  ? 437  GLY A N     1 
ATOM   3285  C  CA    . GLY A 1 437  ? 122.608 161.394 110.693 1.00 83.98  ? 437  GLY A CA    1 
ATOM   3286  C  C     . GLY A 1 437  ? 123.074 161.322 109.253 1.00 80.15  ? 437  GLY A C     1 
ATOM   3287  O  O     . GLY A 1 437  ? 122.766 160.368 108.540 1.00 80.66  ? 437  GLY A O     1 
ATOM   3288  N  N     . THR A 1 438  ? 123.812 162.339 108.821 1.00 77.36  ? 438  THR A N     1 
ATOM   3289  C  CA    . THR A 1 438  ? 124.331 162.370 107.458 1.00 76.42  ? 438  THR A CA    1 
ATOM   3290  C  C     . THR A 1 438  ? 125.518 161.421 107.329 1.00 70.79  ? 438  THR A C     1 
ATOM   3291  O  O     . THR A 1 438  ? 126.395 161.416 108.198 1.00 72.52  ? 438  THR A O     1 
ATOM   3292  C  CB    . THR A 1 438  ? 124.754 163.783 107.070 1.00 78.29  ? 438  THR A CB    1 
ATOM   3293  O  OG1   . THR A 1 438  ? 125.930 164.149 107.802 1.00 76.10  ? 438  THR A OG1   1 
ATOM   3294  C  CG2   . THR A 1 438  ? 123.640 164.774 107.378 1.00 76.80  ? 438  THR A CG2   1 
ATOM   3295  N  N     . PRO A 1 439  ? 125.573 160.603 106.281 1.00 63.33  ? 439  PRO A N     1 
ATOM   3296  C  CA    . PRO A 1 439  ? 126.747 159.746 106.080 1.00 58.22  ? 439  PRO A CA    1 
ATOM   3297  C  C     . PRO A 1 439  ? 127.967 160.570 105.700 1.00 54.95  ? 439  PRO A C     1 
ATOM   3298  O  O     . PRO A 1 439  ? 127.882 161.502 104.898 1.00 58.82  ? 439  PRO A O     1 
ATOM   3299  C  CB    . PRO A 1 439  ? 126.325 158.817 104.934 1.00 54.60  ? 439  PRO A CB    1 
ATOM   3300  C  CG    . PRO A 1 439  ? 124.850 159.012 104.770 1.00 59.15  ? 439  PRO A CG    1 
ATOM   3301  C  CD    . PRO A 1 439  ? 124.558 160.397 105.240 1.00 61.78  ? 439  PRO A CD    1 
ATOM   3302  N  N     . VAL A 1 440  ? 129.112 160.219 106.287 1.00 46.65  ? 440  VAL A N     1 
ATOM   3303  C  CA    . VAL A 1 440  ? 130.353 160.878 105.894 1.00 45.41  ? 440  VAL A CA    1 
ATOM   3304  C  C     . VAL A 1 440  ? 130.755 160.458 104.486 1.00 47.15  ? 440  VAL A C     1 
ATOM   3305  O  O     . VAL A 1 440  ? 131.323 161.255 103.729 1.00 46.75  ? 440  VAL A O     1 
ATOM   3306  C  CB    . VAL A 1 440  ? 131.462 160.593 106.926 1.00 42.97  ? 440  VAL A CB    1 
ATOM   3307  C  CG1   . VAL A 1 440  ? 131.780 159.112 106.990 1.00 41.90  ? 440  VAL A CG1   1 
ATOM   3308  C  CG2   . VAL A 1 440  ? 132.707 161.401 106.606 1.00 39.23  ? 440  VAL A CG2   1 
ATOM   3309  N  N     . LEU A 1 441  ? 130.461 159.218 104.109 1.00 48.40  ? 441  LEU A N     1 
ATOM   3310  C  CA    . LEU A 1 441  ? 130.716 158.688 102.779 1.00 47.48  ? 441  LEU A CA    1 
ATOM   3311  C  C     . LEU A 1 441  ? 129.409 158.139 102.235 1.00 47.67  ? 441  LEU A C     1 
ATOM   3312  O  O     . LEU A 1 441  ? 128.628 157.542 102.979 1.00 52.35  ? 441  LEU A O     1 
ATOM   3313  C  CB    . LEU A 1 441  ? 131.775 157.582 102.811 1.00 48.06  ? 441  LEU A CB    1 
ATOM   3314  C  CG    . LEU A 1 441  ? 133.207 157.909 102.387 1.00 43.74  ? 441  LEU A CG    1 
ATOM   3315  C  CD1   . LEU A 1 441  ? 133.813 158.987 103.267 1.00 37.41  ? 441  LEU A CD1   1 
ATOM   3316  C  CD2   . LEU A 1 441  ? 134.050 156.645 102.427 1.00 41.83  ? 441  LEU A CD2   1 
ATOM   3317  N  N     . LYS A 1 442  ? 129.166 158.337 100.942 1.00 47.59  ? 442  LYS A N     1 
ATOM   3318  C  CA    . LYS A 1 442  ? 127.879 157.962 100.349 1.00 52.25  ? 442  LYS A CA    1 
ATOM   3319  C  C     . LYS A 1 442  ? 128.119 157.421 98.940  1.00 55.54  ? 442  LYS A C     1 
ATOM   3320  O  O     . LYS A 1 442  ? 128.211 158.186 97.978  1.00 57.72  ? 442  LYS A O     1 
ATOM   3321  C  CB    . LYS A 1 442  ? 126.928 159.151 100.347 1.00 52.78  ? 442  LYS A CB    1 
ATOM   3322  C  CG    . LYS A 1 442  ? 125.478 158.795 100.094 1.00 56.78  ? 442  LYS A CG    1 
ATOM   3323  C  CD    . LYS A 1 442  ? 124.616 160.042 100.003 1.00 58.92  ? 442  LYS A CD    1 
ATOM   3324  C  CE    . LYS A 1 442  ? 123.148 159.707 100.195 1.00 60.70  ? 442  LYS A CE    1 
ATOM   3325  N  NZ    . LYS A 1 442  ? 122.274 160.886 99.958  1.00 60.86  ? 442  LYS A NZ    1 
ATOM   3326  N  N     . ASP A 1 443  ? 128.216 156.093 98.835  1.00 52.37  ? 443  ASP A N     1 
ATOM   3327  C  CA    . ASP A 1 443  ? 128.301 155.373 97.563  1.00 52.77  ? 443  ASP A CA    1 
ATOM   3328  C  C     . ASP A 1 443  ? 129.524 155.837 96.761  1.00 54.09  ? 443  ASP A C     1 
ATOM   3329  O  O     . ASP A 1 443  ? 129.428 156.555 95.764  1.00 58.05  ? 443  ASP A O     1 
ATOM   3330  C  CB    . ASP A 1 443  ? 126.995 155.529 96.772  1.00 57.26  ? 443  ASP A CB    1 
ATOM   3331  C  CG    . ASP A 1 443  ? 126.961 154.694 95.496  1.00 64.83  ? 443  ASP A CG    1 
ATOM   3332  O  OD1   . ASP A 1 443  ? 125.965 153.962 95.317  1.00 66.58  ? 443  ASP A OD1   1 
ATOM   3333  O  OD2   . ASP A 1 443  ? 127.888 154.759 94.666  1.00 64.26  ? 443  ASP A OD2   1 
ATOM   3334  N  N     . ILE A 1 444  ? 130.690 155.452 97.271  1.00 54.27  ? 444  ILE A N     1 
ATOM   3335  C  CA    . ILE A 1 444  ? 131.971 155.745 96.636  1.00 52.06  ? 444  ILE A CA    1 
ATOM   3336  C  C     . ILE A 1 444  ? 132.427 154.517 95.859  1.00 53.61  ? 444  ILE A C     1 
ATOM   3337  O  O     . ILE A 1 444  ? 132.385 153.395 96.377  1.00 53.02  ? 444  ILE A O     1 
ATOM   3338  C  CB    . ILE A 1 444  ? 133.024 156.157 97.678  1.00 48.99  ? 444  ILE A CB    1 
ATOM   3339  C  CG1   . ILE A 1 444  ? 132.511 157.327 98.517  1.00 48.78  ? 444  ILE A CG1   1 
ATOM   3340  C  CG2   . ILE A 1 444  ? 134.329 156.522 97.000  1.00 52.84  ? 444  ILE A CG2   1 
ATOM   3341  C  CD1   . ILE A 1 444  ? 132.087 158.522 97.701  1.00 48.36  ? 444  ILE A CD1   1 
ATOM   3342  N  N     . ASN A 1 445  ? 132.855 154.725 94.613  1.00 56.61  ? 445  ASN A N     1 
ATOM   3343  C  CA    . ASN A 1 445  ? 133.364 153.657 93.763  1.00 53.58  ? 445  ASN A CA    1 
ATOM   3344  C  C     . ASN A 1 445  ? 134.656 154.098 93.093  1.00 52.62  ? 445  ASN A C     1 
ATOM   3345  O  O     . ASN A 1 445  ? 134.746 155.218 92.583  1.00 56.10  ? 445  ASN A O     1 
ATOM   3346  C  CB    . ASN A 1 445  ? 132.351 153.264 92.681  1.00 55.29  ? 445  ASN A CB    1 
ATOM   3347  C  CG    . ASN A 1 445  ? 130.982 152.965 93.242  1.00 59.18  ? 445  ASN A CG    1 
ATOM   3348  O  OD1   . ASN A 1 445  ? 130.697 151.843 93.656  1.00 59.69  ? 445  ASN A OD1   1 
ATOM   3349  N  ND2   . ASN A 1 445  ? 130.119 153.971 93.255  1.00 58.50  ? 445  ASN A ND2   1 
ATOM   3350  N  N     . PHE A 1 446  ? 135.653 153.215 93.093  1.00 51.89  ? 446  PHE A N     1 
ATOM   3351  C  CA    . PHE A 1 446  ? 136.860 153.429 92.303  1.00 51.52  ? 446  PHE A CA    1 
ATOM   3352  C  C     . PHE A 1 446  ? 137.587 152.102 92.138  1.00 52.00  ? 446  PHE A C     1 
ATOM   3353  O  O     . PHE A 1 446  ? 137.327 151.135 92.858  1.00 50.14  ? 446  PHE A O     1 
ATOM   3354  C  CB    . PHE A 1 446  ? 137.774 154.502 92.922  1.00 48.91  ? 446  PHE A CB    1 
ATOM   3355  C  CG    . PHE A 1 446  ? 138.479 154.074 94.183  1.00 47.89  ? 446  PHE A CG    1 
ATOM   3356  C  CD1   . PHE A 1 446  ? 139.649 153.333 94.130  1.00 46.87  ? 446  PHE A CD1   1 
ATOM   3357  C  CD2   . PHE A 1 446  ? 137.992 154.451 95.421  1.00 49.28  ? 446  PHE A CD2   1 
ATOM   3358  C  CE1   . PHE A 1 446  ? 140.296 152.951 95.284  1.00 45.25  ? 446  PHE A CE1   1 
ATOM   3359  C  CE2   . PHE A 1 446  ? 138.639 154.074 96.577  1.00 49.85  ? 446  PHE A CE2   1 
ATOM   3360  C  CZ    . PHE A 1 446  ? 139.793 153.324 96.508  1.00 45.99  ? 446  PHE A CZ    1 
ATOM   3361  N  N     . LYS A 1 447  ? 138.495 152.071 91.164  1.00 52.49  ? 447  LYS A N     1 
ATOM   3362  C  CA    . LYS A 1 447  ? 139.291 150.888 90.864  1.00 51.77  ? 447  LYS A CA    1 
ATOM   3363  C  C     . LYS A 1 447  ? 140.629 151.328 90.292  1.00 55.87  ? 447  LYS A C     1 
ATOM   3364  O  O     . LYS A 1 447  ? 140.663 152.059 89.298  1.00 61.59  ? 447  LYS A O     1 
ATOM   3365  C  CB    . LYS A 1 447  ? 138.569 149.977 89.869  1.00 51.77  ? 447  LYS A CB    1 
ATOM   3366  C  CG    . LYS A 1 447  ? 139.374 148.769 89.437  1.00 55.40  ? 447  LYS A CG    1 
ATOM   3367  C  CD    . LYS A 1 447  ? 138.489 147.547 89.279  1.00 60.47  ? 447  LYS A CD    1 
ATOM   3368  C  CE    . LYS A 1 447  ? 138.507 147.045 87.843  1.00 68.68  ? 447  LYS A CE    1 
ATOM   3369  N  NZ    . LYS A 1 447  ? 138.468 145.558 87.763  1.00 68.02  ? 447  LYS A NZ    1 
ATOM   3370  N  N     . ILE A 1 448  ? 141.721 150.884 90.909  1.00 54.16  ? 448  ILE A N     1 
ATOM   3371  C  CA    . ILE A 1 448  ? 143.069 151.223 90.464  1.00 54.18  ? 448  ILE A CA    1 
ATOM   3372  C  C     . ILE A 1 448  ? 143.913 149.957 90.466  1.00 57.59  ? 448  ILE A C     1 
ATOM   3373  O  O     . ILE A 1 448  ? 143.716 149.067 91.299  1.00 58.47  ? 448  ILE A O     1 
ATOM   3374  C  CB    . ILE A 1 448  ? 143.712 152.320 91.338  1.00 50.54  ? 448  ILE A CB    1 
ATOM   3375  C  CG1   . ILE A 1 448  ? 143.760 151.892 92.803  1.00 49.70  ? 448  ILE A CG1   1 
ATOM   3376  C  CG2   . ILE A 1 448  ? 142.965 153.632 91.190  1.00 46.48  ? 448  ILE A CG2   1 
ATOM   3377  C  CD1   . ILE A 1 448  ? 144.414 152.905 93.706  1.00 42.26  ? 448  ILE A CD1   1 
ATOM   3378  N  N     . GLU A 1 449  ? 144.848 149.873 89.525  1.00 60.76  ? 449  GLU A N     1 
ATOM   3379  C  CA    . GLU A 1 449  ? 145.638 148.673 89.312  1.00 60.99  ? 449  GLU A CA    1 
ATOM   3380  C  C     . GLU A 1 449  ? 147.056 148.851 89.851  1.00 57.53  ? 449  GLU A C     1 
ATOM   3381  O  O     . GLU A 1 449  ? 147.433 149.907 90.362  1.00 58.48  ? 449  GLU A O     1 
ATOM   3382  C  CB    . GLU A 1 449  ? 145.650 148.315 87.826  1.00 63.51  ? 449  GLU A CB    1 
ATOM   3383  C  CG    . GLU A 1 449  ? 144.264 148.254 87.213  1.00 68.84  ? 449  GLU A CG    1 
ATOM   3384  C  CD    . GLU A 1 449  ? 144.282 147.806 85.768  1.00 88.20  ? 449  GLU A CD    1 
ATOM   3385  O  OE1   . GLU A 1 449  ? 145.375 147.481 85.260  1.00 93.86  ? 449  GLU A OE1   1 
ATOM   3386  O  OE2   . GLU A 1 449  ? 143.202 147.780 85.141  1.00 94.31  ? 449  GLU A OE2   1 
ATOM   3387  N  N     . ARG A 1 450  ? 147.848 147.787 89.730  1.00 58.08  ? 450  ARG A N     1 
ATOM   3388  C  CA    . ARG A 1 450  ? 149.223 147.784 90.213  1.00 56.86  ? 450  ARG A CA    1 
ATOM   3389  C  C     . ARG A 1 450  ? 150.050 148.859 89.520  1.00 55.76  ? 450  ARG A C     1 
ATOM   3390  O  O     . ARG A 1 450  ? 150.152 148.881 88.291  1.00 55.87  ? 450  ARG A O     1 
ATOM   3391  C  CB    . ARG A 1 450  ? 149.841 146.405 89.984  1.00 55.68  ? 450  ARG A CB    1 
ATOM   3392  C  CG    . ARG A 1 450  ? 151.172 146.157 90.685  1.00 57.05  ? 450  ARG A CG    1 
ATOM   3393  C  CD    . ARG A 1 450  ? 151.171 146.580 92.141  1.00 65.31  ? 450  ARG A CD    1 
ATOM   3394  N  NE    . ARG A 1 450  ? 152.349 146.076 92.837  1.00 72.92  ? 450  ARG A NE    1 
ATOM   3395  C  CZ    . ARG A 1 450  ? 152.819 146.573 93.972  1.00 69.05  ? 450  ARG A CZ    1 
ATOM   3396  N  NH1   . ARG A 1 450  ? 152.239 147.600 94.570  1.00 62.98  ? 450  ARG A NH1   1 
ATOM   3397  N  NH2   . ARG A 1 450  ? 153.906 146.032 94.516  1.00 63.82  ? 450  ARG A NH2   1 
ATOM   3398  N  N     . GLY A 1 451  ? 150.642 149.748 90.317  1.00 54.19  ? 451  GLY A N     1 
ATOM   3399  C  CA    . GLY A 1 451  ? 151.558 150.748 89.816  1.00 52.97  ? 451  GLY A CA    1 
ATOM   3400  C  C     . GLY A 1 451  ? 150.946 152.073 89.423  1.00 53.35  ? 451  GLY A C     1 
ATOM   3401  O  O     . GLY A 1 451  ? 151.665 152.932 88.901  1.00 51.23  ? 451  GLY A O     1 
ATOM   3402  N  N     . GLN A 1 452  ? 149.652 152.270 89.645  1.00 53.61  ? 452  GLN A N     1 
ATOM   3403  C  CA    . GLN A 1 452  ? 148.981 153.491 89.230  1.00 50.47  ? 452  GLN A CA    1 
ATOM   3404  C  C     . GLN A 1 452  ? 148.881 154.490 90.379  1.00 50.84  ? 452  GLN A C     1 
ATOM   3405  O  O     . GLN A 1 452  ? 149.003 154.142 91.555  1.00 53.21  ? 452  GLN A O     1 
ATOM   3406  C  CB    . GLN A 1 452  ? 147.589 153.179 88.683  1.00 51.64  ? 452  GLN A CB    1 
ATOM   3407  C  CG    . GLN A 1 452  ? 147.611 152.491 87.333  1.00 53.63  ? 452  GLN A CG    1 
ATOM   3408  C  CD    . GLN A 1 452  ? 146.261 152.498 86.653  1.00 60.02  ? 452  GLN A CD    1 
ATOM   3409  O  OE1   . GLN A 1 452  ? 145.237 152.225 87.276  1.00 59.86  ? 452  GLN A OE1   1 
ATOM   3410  N  NE2   . GLN A 1 452  ? 146.252 152.813 85.364  1.00 64.06  ? 452  GLN A NE2   1 
ATOM   3411  N  N     . LEU A 1 453  ? 148.660 155.751 90.015  1.00 48.00  ? 453  LEU A N     1 
ATOM   3412  C  CA    . LEU A 1 453  ? 148.516 156.852 90.958  1.00 43.00  ? 453  LEU A CA    1 
ATOM   3413  C  C     . LEU A 1 453  ? 147.076 157.347 90.955  1.00 43.87  ? 453  LEU A C     1 
ATOM   3414  O  O     . LEU A 1 453  ? 146.498 157.575 89.888  1.00 47.23  ? 453  LEU A O     1 
ATOM   3415  C  CB    . LEU A 1 453  ? 149.467 157.997 90.601  1.00 42.69  ? 453  LEU A CB    1 
ATOM   3416  C  CG    . LEU A 1 453  ? 149.378 159.305 91.391  1.00 39.37  ? 453  LEU A CG    1 
ATOM   3417  C  CD1   . LEU A 1 453  ? 149.636 159.082 92.869  1.00 37.82  ? 453  LEU A CD1   1 
ATOM   3418  C  CD2   . LEU A 1 453  ? 150.344 160.331 90.830  1.00 41.10  ? 453  LEU A CD2   1 
ATOM   3419  N  N     . LEU A 1 454  ? 146.497 157.497 92.143  1.00 41.10  ? 454  LEU A N     1 
ATOM   3420  C  CA    . LEU A 1 454  ? 145.166 158.065 92.314  1.00 39.00  ? 454  LEU A CA    1 
ATOM   3421  C  C     . LEU A 1 454  ? 145.276 159.412 93.015  1.00 41.68  ? 454  LEU A C     1 
ATOM   3422  O  O     . LEU A 1 454  ? 145.958 159.527 94.038  1.00 41.08  ? 454  LEU A O     1 
ATOM   3423  C  CB    . LEU A 1 454  ? 144.265 157.130 93.121  1.00 43.72  ? 454  LEU A CB    1 
ATOM   3424  C  CG    . LEU A 1 454  ? 142.835 157.616 93.374  1.00 43.65  ? 454  LEU A CG    1 
ATOM   3425  C  CD1   . LEU A 1 454  ? 142.107 157.876 92.069  1.00 42.58  ? 454  LEU A CD1   1 
ATOM   3426  C  CD2   . LEU A 1 454  ? 142.064 156.637 94.235  1.00 41.85  ? 454  LEU A CD2   1 
ATOM   3427  N  N     . ALA A 1 455  ? 144.606 160.421 92.468  1.00 43.30  ? 455  ALA A N     1 
ATOM   3428  C  CA    . ALA A 1 455  ? 144.581 161.761 93.041  1.00 39.87  ? 455  ALA A CA    1 
ATOM   3429  C  C     . ALA A 1 455  ? 143.190 162.042 93.591  1.00 40.14  ? 455  ALA A C     1 
ATOM   3430  O  O     . ALA A 1 455  ? 142.211 162.045 92.838  1.00 41.62  ? 455  ALA A O     1 
ATOM   3431  C  CB    . ALA A 1 455  ? 144.974 162.809 92.002  1.00 34.35  ? 455  ALA A CB    1 
ATOM   3432  N  N     . VAL A 1 456  ? 143.106 162.282 94.895  1.00 38.21  ? 456  VAL A N     1 
ATOM   3433  C  CA    . VAL A 1 456  ? 141.850 162.589 95.568  1.00 38.63  ? 456  VAL A CA    1 
ATOM   3434  C  C     . VAL A 1 456  ? 141.830 164.078 95.882  1.00 39.42  ? 456  VAL A C     1 
ATOM   3435  O  O     . VAL A 1 456  ? 142.739 164.593 96.543  1.00 43.54  ? 456  VAL A O     1 
ATOM   3436  C  CB    . VAL A 1 456  ? 141.677 161.753 96.845  1.00 39.22  ? 456  VAL A CB    1 
ATOM   3437  C  CG1   . VAL A 1 456  ? 140.420 162.167 97.583  1.00 33.57  ? 456  VAL A CG1   1 
ATOM   3438  C  CG2   . VAL A 1 456  ? 141.633 160.275 96.510  1.00 36.98  ? 456  VAL A CG2   1 
ATOM   3439  N  N     . ALA A 1 457  ? 140.796 164.771 95.412  1.00 40.19  ? 457  ALA A N     1 
ATOM   3440  C  CA    . ALA A 1 457  ? 140.655 166.206 95.609  1.00 38.99  ? 457  ALA A CA    1 
ATOM   3441  C  C     . ALA A 1 457  ? 139.287 166.510 96.207  1.00 40.54  ? 457  ALA A C     1 
ATOM   3442  O  O     . ALA A 1 457  ? 138.407 165.650 96.276  1.00 41.61  ? 457  ALA A O     1 
ATOM   3443  C  CB    . ALA A 1 457  ? 140.848 166.970 94.294  1.00 35.87  ? 457  ALA A CB    1 
ATOM   3444  N  N     . GLY A 1 458  ? 139.119 167.746 96.642  1.00 37.97  ? 458  GLY A N     1 
ATOM   3445  C  CA    . GLY A 1 458  ? 137.867 168.188 97.225  1.00 38.59  ? 458  GLY A CA    1 
ATOM   3446  C  C     . GLY A 1 458  ? 138.089 169.325 98.199  1.00 42.71  ? 458  GLY A C     1 
ATOM   3447  O  O     . GLY A 1 458  ? 139.214 169.667 98.557  1.00 43.62  ? 458  GLY A O     1 
ATOM   3448  N  N     . SER A 1 459  ? 136.977 169.917 98.626  1.00 42.23  ? 459  SER A N     1 
ATOM   3449  C  CA    . SER A 1 459  ? 137.003 171.038 99.551  1.00 38.67  ? 459  SER A CA    1 
ATOM   3450  C  C     . SER A 1 459  ? 137.171 170.555 100.990 1.00 39.20  ? 459  SER A C     1 
ATOM   3451  O  O     . SER A 1 459  ? 137.227 169.356 101.274 1.00 40.57  ? 459  SER A O     1 
ATOM   3452  C  CB    . SER A 1 459  ? 135.730 171.870 99.419  1.00 38.27  ? 459  SER A CB    1 
ATOM   3453  O  OG    . SER A 1 459  ? 135.798 172.741 98.305  1.00 46.93  ? 459  SER A OG    1 
ATOM   3454  N  N     . THR A 1 460  ? 137.264 171.518 101.903 1.00 36.98  ? 460  THR A N     1 
ATOM   3455  C  CA    . THR A 1 460  ? 137.421 171.213 103.319 1.00 36.42  ? 460  THR A CA    1 
ATOM   3456  C  C     . THR A 1 460  ? 136.183 170.512 103.862 1.00 36.58  ? 460  THR A C     1 
ATOM   3457  O  O     . THR A 1 460  ? 135.054 170.965 103.651 1.00 37.65  ? 460  THR A O     1 
ATOM   3458  C  CB    . THR A 1 460  ? 137.686 172.496 104.105 1.00 38.12  ? 460  THR A CB    1 
ATOM   3459  O  OG1   . THR A 1 460  ? 138.928 173.067 103.680 1.00 43.40  ? 460  THR A OG1   1 
ATOM   3460  C  CG2   . THR A 1 460  ? 137.761 172.207 105.590 1.00 37.91  ? 460  THR A CG2   1 
ATOM   3461  N  N     . GLY A 1 461  ? 136.399 169.407 104.570 1.00 32.91  ? 461  GLY A N     1 
ATOM   3462  C  CA    . GLY A 1 461  ? 135.312 168.637 105.132 1.00 30.99  ? 461  GLY A CA    1 
ATOM   3463  C  C     . GLY A 1 461  ? 134.612 167.713 104.165 1.00 35.28  ? 461  GLY A C     1 
ATOM   3464  O  O     . GLY A 1 461  ? 133.564 167.161 104.513 1.00 38.65  ? 461  GLY A O     1 
ATOM   3465  N  N     . ALA A 1 462  ? 135.162 167.515 102.966 1.00 34.98  ? 462  ALA A N     1 
ATOM   3466  C  CA    . ALA A 1 462  ? 134.526 166.644 101.987 1.00 32.95  ? 462  ALA A CA    1 
ATOM   3467  C  C     . ALA A 1 462  ? 134.629 165.171 102.358 1.00 34.84  ? 462  ALA A C     1 
ATOM   3468  O  O     . ALA A 1 462  ? 133.795 164.378 101.913 1.00 44.12  ? 462  ALA A O     1 
ATOM   3469  C  CB    . ALA A 1 462  ? 135.135 166.875 100.606 1.00 36.03  ? 462  ALA A CB    1 
ATOM   3470  N  N     . GLY A 1 463  ? 135.622 164.788 103.155 1.00 30.95  ? 463  GLY A N     1 
ATOM   3471  C  CA    . GLY A 1 463  ? 135.780 163.403 103.554 1.00 30.69  ? 463  GLY A CA    1 
ATOM   3472  C  C     . GLY A 1 463  ? 136.987 162.726 102.942 1.00 31.30  ? 463  GLY A C     1 
ATOM   3473  O  O     . GLY A 1 463  ? 136.984 161.509 102.740 1.00 34.81  ? 463  GLY A O     1 
ATOM   3474  N  N     . LYS A 1 464  ? 138.025 163.506 102.631 1.00 31.80  ? 464  LYS A N     1 
ATOM   3475  C  CA    . LYS A 1 464  ? 139.234 162.938 102.043 1.00 27.63  ? 464  LYS A CA    1 
ATOM   3476  C  C     . LYS A 1 464  ? 139.998 162.077 103.043 1.00 29.49  ? 464  LYS A C     1 
ATOM   3477  O  O     . LYS A 1 464  ? 140.553 161.037 102.675 1.00 35.12  ? 464  LYS A O     1 
ATOM   3478  C  CB    . LYS A 1 464  ? 140.118 164.055 101.489 1.00 29.12  ? 464  LYS A CB    1 
ATOM   3479  C  CG    . LYS A 1 464  ? 139.436 164.881 100.408 1.00 30.01  ? 464  LYS A CG    1 
ATOM   3480  C  CD    . LYS A 1 464  ? 140.382 165.883 99.772  1.00 33.98  ? 464  LYS A CD    1 
ATOM   3481  C  CE    . LYS A 1 464  ? 140.995 166.805 100.802 1.00 34.87  ? 464  LYS A CE    1 
ATOM   3482  N  NZ    . LYS A 1 464  ? 139.963 167.643 101.463 1.00 35.63  ? 464  LYS A NZ    1 
ATOM   3483  N  N     . THR A 1 465  ? 140.051 162.497 104.308 1.00 29.68  ? 465  THR A N     1 
ATOM   3484  C  CA    . THR A 1 465  ? 140.726 161.697 105.326 1.00 26.18  ? 465  THR A CA    1 
ATOM   3485  C  C     . THR A 1 465  ? 139.904 160.468 105.698 1.00 28.74  ? 465  THR A C     1 
ATOM   3486  O  O     . THR A 1 465  ? 140.461 159.397 105.976 1.00 34.52  ? 465  THR A O     1 
ATOM   3487  C  CB    . THR A 1 465  ? 141.007 162.556 106.558 1.00 26.91  ? 465  THR A CB    1 
ATOM   3488  O  OG1   . THR A 1 465  ? 141.874 163.636 106.195 1.00 31.60  ? 465  THR A OG1   1 
ATOM   3489  C  CG2   . THR A 1 465  ? 141.677 161.741 107.639 1.00 27.11  ? 465  THR A CG2   1 
ATOM   3490  N  N     . SER A 1 466  ? 138.577 160.608 105.720 1.00 32.09  ? 466  SER A N     1 
ATOM   3491  C  CA    . SER A 1 466  ? 137.712 159.481 106.051 1.00 32.43  ? 466  SER A CA    1 
ATOM   3492  C  C     . SER A 1 466  ? 137.836 158.353 105.036 1.00 31.90  ? 466  SER A C     1 
ATOM   3493  O  O     . SER A 1 466  ? 137.682 157.182 105.393 1.00 32.23  ? 466  SER A O     1 
ATOM   3494  C  CB    . SER A 1 466  ? 136.263 159.950 106.149 1.00 31.37  ? 466  SER A CB    1 
ATOM   3495  O  OG    . SER A 1 466  ? 136.077 160.783 107.276 1.00 29.49  ? 466  SER A OG    1 
ATOM   3496  N  N     . LEU A 1 467  ? 138.109 158.679 103.773 1.00 29.39  ? 467  LEU A N     1 
ATOM   3497  C  CA    . LEU A 1 467  ? 138.291 157.638 102.767 1.00 31.08  ? 467  LEU A CA    1 
ATOM   3498  C  C     . LEU A 1 467  ? 139.518 156.785 103.073 1.00 34.35  ? 467  LEU A C     1 
ATOM   3499  O  O     . LEU A 1 467  ? 139.466 155.549 102.992 1.00 36.93  ? 467  LEU A O     1 
ATOM   3500  C  CB    . LEU A 1 467  ? 138.400 158.277 101.385 1.00 30.02  ? 467  LEU A CB    1 
ATOM   3501  C  CG    . LEU A 1 467  ? 138.337 157.362 100.166 1.00 35.00  ? 467  LEU A CG    1 
ATOM   3502  C  CD1   . LEU A 1 467  ? 136.986 156.685 100.101 1.00 37.51  ? 467  LEU A CD1   1 
ATOM   3503  C  CD2   . LEU A 1 467  ? 138.591 158.155 98.903  1.00 36.64  ? 467  LEU A CD2   1 
ATOM   3504  N  N     . LEU A 1 468  ? 140.627 157.425 103.448 1.00 33.43  ? 468  LEU A N     1 
ATOM   3505  C  CA    . LEU A 1 468  ? 141.815 156.673 103.828 1.00 32.46  ? 468  LEU A CA    1 
ATOM   3506  C  C     . LEU A 1 468  ? 141.596 155.910 105.124 1.00 34.22  ? 468  LEU A C     1 
ATOM   3507  O  O     . LEU A 1 468  ? 142.138 154.814 105.293 1.00 35.25  ? 468  LEU A O     1 
ATOM   3508  C  CB    . LEU A 1 468  ? 143.015 157.606 103.965 1.00 32.89  ? 468  LEU A CB    1 
ATOM   3509  C  CG    . LEU A 1 468  ? 143.400 158.413 102.728 1.00 31.05  ? 468  LEU A CG    1 
ATOM   3510  C  CD1   . LEU A 1 468  ? 144.583 159.314 103.039 1.00 30.51  ? 468  LEU A CD1   1 
ATOM   3511  C  CD2   . LEU A 1 468  ? 143.699 157.502 101.556 1.00 27.84  ? 468  LEU A CD2   1 
ATOM   3512  N  N     . MET A 1 469  ? 140.819 156.471 106.053 1.00 34.90  ? 469  MET A N     1 
ATOM   3513  C  CA    . MET A 1 469  ? 140.486 155.732 107.267 1.00 32.59  ? 469  MET A CA    1 
ATOM   3514  C  C     . MET A 1 469  ? 139.681 154.480 106.944 1.00 31.78  ? 469  MET A C     1 
ATOM   3515  O  O     . MET A 1 469  ? 139.867 153.435 107.576 1.00 35.13  ? 469  MET A O     1 
ATOM   3516  C  CB    . MET A 1 469  ? 139.718 156.625 108.240 1.00 33.19  ? 469  MET A CB    1 
ATOM   3517  C  CG    . MET A 1 469  ? 140.524 157.768 108.825 1.00 33.81  ? 469  MET A CG    1 
ATOM   3518  S  SD    . MET A 1 469  ? 141.941 157.215 109.790 1.00 60.96  ? 469  MET A SD    1 
ATOM   3519  C  CE    . MET A 1 469  ? 143.277 157.643 108.683 1.00 40.85  ? 469  MET A CE    1 
ATOM   3520  N  N     . VAL A 1 470  ? 138.770 154.573 105.974 1.00 34.13  ? 470  VAL A N     1 
ATOM   3521  C  CA    . VAL A 1 470  ? 138.007 153.402 105.550 1.00 34.07  ? 470  VAL A CA    1 
ATOM   3522  C  C     . VAL A 1 470  ? 138.926 152.365 104.921 1.00 33.23  ? 470  VAL A C     1 
ATOM   3523  O  O     . VAL A 1 470  ? 138.805 151.165 105.191 1.00 35.36  ? 470  VAL A O     1 
ATOM   3524  C  CB    . VAL A 1 470  ? 136.882 153.815 104.584 1.00 33.11  ? 470  VAL A CB    1 
ATOM   3525  C  CG1   . VAL A 1 470  ? 136.324 152.599 103.871 1.00 34.53  ? 470  VAL A CG1   1 
ATOM   3526  C  CG2   . VAL A 1 470  ? 135.784 154.531 105.334 1.00 36.44  ? 470  VAL A CG2   1 
ATOM   3527  N  N     . ILE A 1 471  ? 139.859 152.808 104.075 1.00 33.15  ? 471  ILE A N     1 
ATOM   3528  C  CA    . ILE A 1 471  ? 140.782 151.868 103.443 1.00 33.39  ? 471  ILE A CA    1 
ATOM   3529  C  C     . ILE A 1 471  ? 141.647 151.175 104.492 1.00 32.62  ? 471  ILE A C     1 
ATOM   3530  O  O     . ILE A 1 471  ? 141.866 149.960 104.432 1.00 34.70  ? 471  ILE A O     1 
ATOM   3531  C  CB    . ILE A 1 471  ? 141.638 152.587 102.384 1.00 32.42  ? 471  ILE A CB    1 
ATOM   3532  C  CG1   . ILE A 1 471  ? 140.763 153.070 101.228 1.00 34.26  ? 471  ILE A CG1   1 
ATOM   3533  C  CG2   . ILE A 1 471  ? 142.731 151.670 101.859 1.00 28.63  ? 471  ILE A CG2   1 
ATOM   3534  C  CD1   . ILE A 1 471  ? 141.431 154.100 100.351 1.00 35.74  ? 471  ILE A CD1   1 
ATOM   3535  N  N     . MET A 1 472  ? 142.137 151.929 105.479 1.00 35.96  ? 472  MET A N     1 
ATOM   3536  C  CA    . MET A 1 472  ? 142.990 151.367 106.522 1.00 33.44  ? 472  MET A CA    1 
ATOM   3537  C  C     . MET A 1 472  ? 142.250 150.404 107.438 1.00 35.74  ? 472  MET A C     1 
ATOM   3538  O  O     . MET A 1 472  ? 142.896 149.611 108.130 1.00 40.45  ? 472  MET A O     1 
ATOM   3539  C  CB    . MET A 1 472  ? 143.596 152.489 107.362 1.00 37.24  ? 472  MET A CB    1 
ATOM   3540  C  CG    . MET A 1 472  ? 144.681 153.283 106.669 1.00 37.37  ? 472  MET A CG    1 
ATOM   3541  S  SD    . MET A 1 472  ? 145.280 154.630 107.699 1.00 52.25  ? 472  MET A SD    1 
ATOM   3542  C  CE    . MET A 1 472  ? 145.272 153.846 109.304 1.00 41.82  ? 472  MET A CE    1 
ATOM   3543  N  N     . GLY A 1 473  ? 140.924 150.460 107.473 1.00 35.43  ? 473  GLY A N     1 
ATOM   3544  C  CA    . GLY A 1 473  ? 140.149 149.631 108.368 1.00 34.90  ? 473  GLY A CA    1 
ATOM   3545  C  C     . GLY A 1 473  ? 139.825 150.254 109.705 1.00 39.26  ? 473  GLY A C     1 
ATOM   3546  O  O     . GLY A 1 473  ? 139.279 149.566 110.573 1.00 41.93  ? 473  GLY A O     1 
ATOM   3547  N  N     . GLU A 1 474  ? 140.148 151.533 109.903 1.00 39.37  ? 474  GLU A N     1 
ATOM   3548  C  CA    . GLU A 1 474  ? 139.811 152.216 111.145 1.00 37.63  ? 474  GLU A CA    1 
ATOM   3549  C  C     . GLU A 1 474  ? 138.368 152.697 111.177 1.00 38.61  ? 474  GLU A C     1 
ATOM   3550  O  O     . GLU A 1 474  ? 137.870 153.045 112.251 1.00 42.13  ? 474  GLU A O     1 
ATOM   3551  C  CB    . GLU A 1 474  ? 140.751 153.404 111.364 1.00 34.84  ? 474  GLU A CB    1 
ATOM   3552  C  CG    . GLU A 1 474  ? 142.234 153.062 111.348 1.00 37.64  ? 474  GLU A CG    1 
ATOM   3553  C  CD    . GLU A 1 474  ? 142.657 152.127 112.468 1.00 43.39  ? 474  GLU A CD    1 
ATOM   3554  O  OE1   . GLU A 1 474  ? 141.879 151.933 113.423 1.00 46.78  ? 474  GLU A OE1   1 
ATOM   3555  O  OE2   . GLU A 1 474  ? 143.777 151.582 112.392 1.00 39.60  ? 474  GLU A OE2   1 
ATOM   3556  N  N     . LEU A 1 475  ? 137.693 152.734 110.031 1.00 36.78  ? 475  LEU A N     1 
ATOM   3557  C  CA    . LEU A 1 475  ? 136.300 153.164 109.936 1.00 39.84  ? 475  LEU A CA    1 
ATOM   3558  C  C     . LEU A 1 475  ? 135.541 152.087 109.170 1.00 44.87  ? 475  LEU A C     1 
ATOM   3559  O  O     . LEU A 1 475  ? 135.695 151.959 107.953 1.00 47.35  ? 475  LEU A O     1 
ATOM   3560  C  CB    . LEU A 1 475  ? 136.187 154.522 109.251 1.00 39.68  ? 475  LEU A CB    1 
ATOM   3561  C  CG    . LEU A 1 475  ? 134.785 155.088 109.013 1.00 37.55  ? 475  LEU A CG    1 
ATOM   3562  C  CD1   . LEU A 1 475  ? 134.026 155.215 110.314 1.00 44.52  ? 475  LEU A CD1   1 
ATOM   3563  C  CD2   . LEU A 1 475  ? 134.859 156.430 108.316 1.00 34.04  ? 475  LEU A CD2   1 
ATOM   3564  N  N     . GLU A 1 476  ? 134.739 151.312 109.881 1.00 47.54  ? 476  GLU A N     1 
ATOM   3565  C  CA    . GLU A 1 476  ? 134.018 150.205 109.265 1.00 49.63  ? 476  GLU A CA    1 
ATOM   3566  C  C     . GLU A 1 476  ? 132.863 150.714 108.415 1.00 51.32  ? 476  GLU A C     1 
ATOM   3567  O  O     . GLU A 1 476  ? 132.009 151.450 108.925 1.00 54.45  ? 476  GLU A O     1 
ATOM   3568  C  CB    . GLU A 1 476  ? 133.505 149.254 110.338 1.00 50.43  ? 476  GLU A CB    1 
ATOM   3569  C  CG    . GLU A 1 476  ? 134.489 149.004 111.464 1.00 54.07  ? 476  GLU A CG    1 
ATOM   3570  C  CD    . GLU A 1 476  ? 135.520 147.945 111.121 1.00 65.44  ? 476  GLU A CD    1 
ATOM   3571  O  OE1   . GLU A 1 476  ? 136.049 147.309 112.056 1.00 63.69  ? 476  GLU A OE1   1 
ATOM   3572  O  OE2   . GLU A 1 476  ? 135.802 147.740 109.922 1.00 64.84  ? 476  GLU A OE2   1 
ATOM   3573  N  N     . PRO A 1 477  ? 132.792 150.358 107.135 1.00 50.60  ? 477  PRO A N     1 
ATOM   3574  C  CA    . PRO A 1 477  ? 131.654 150.785 106.317 1.00 49.34  ? 477  PRO A CA    1 
ATOM   3575  C  C     . PRO A 1 477  ? 130.394 150.018 106.681 1.00 53.17  ? 477  PRO A C     1 
ATOM   3576  O  O     . PRO A 1 477  ? 130.428 148.812 106.932 1.00 57.16  ? 477  PRO A O     1 
ATOM   3577  C  CB    . PRO A 1 477  ? 132.111 150.469 104.890 1.00 49.33  ? 477  PRO A CB    1 
ATOM   3578  C  CG    . PRO A 1 477  ? 133.015 149.300 105.056 1.00 46.05  ? 477  PRO A CG    1 
ATOM   3579  C  CD    . PRO A 1 477  ? 133.727 149.511 106.374 1.00 50.51  ? 477  PRO A CD    1 
ATOM   3580  N  N     . SER A 1 478  ? 129.270 150.735 106.716 1.00 53.14  ? 478  SER A N     1 
ATOM   3581  C  CA    . SER A 1 478  ? 127.991 150.081 106.956 1.00 52.36  ? 478  SER A CA    1 
ATOM   3582  C  C     . SER A 1 478  ? 127.472 149.362 105.720 1.00 54.56  ? 478  SER A C     1 
ATOM   3583  O  O     . SER A 1 478  ? 126.563 148.534 105.836 1.00 56.39  ? 478  SER A O     1 
ATOM   3584  C  CB    . SER A 1 478  ? 126.958 151.099 107.439 1.00 50.00  ? 478  SER A CB    1 
ATOM   3585  O  OG    . SER A 1 478  ? 126.623 152.010 106.411 1.00 48.03  ? 478  SER A OG    1 
ATOM   3586  N  N     . GLU A 1 479  ? 128.025 149.656 104.546 1.00 56.48  ? 479  GLU A N     1 
ATOM   3587  C  CA    . GLU A 1 479  ? 127.568 149.048 103.306 1.00 57.35  ? 479  GLU A CA    1 
ATOM   3588  C  C     . GLU A 1 479  ? 128.681 149.152 102.275 1.00 55.22  ? 479  GLU A C     1 
ATOM   3589  O  O     . GLU A 1 479  ? 129.399 150.152 102.223 1.00 55.56  ? 479  GLU A O     1 
ATOM   3590  C  CB    . GLU A 1 479  ? 126.291 149.727 102.802 1.00 56.57  ? 479  GLU A CB    1 
ATOM   3591  C  CG    . GLU A 1 479  ? 125.904 149.384 101.380 1.00 62.79  ? 479  GLU A CG    1 
ATOM   3592  C  CD    . GLU A 1 479  ? 124.677 150.137 100.925 1.00 74.56  ? 479  GLU A CD    1 
ATOM   3593  O  OE1   . GLU A 1 479  ? 123.988 150.719 101.787 1.00 73.38  ? 479  GLU A OE1   1 
ATOM   3594  O  OE2   . GLU A 1 479  ? 124.405 150.153 99.706  1.00 79.88  ? 479  GLU A OE2   1 
ATOM   3595  N  N     . GLY A 1 480  ? 128.809 148.115 101.453 1.00 54.83  ? 480  GLY A N     1 
ATOM   3596  C  CA    . GLY A 1 480  ? 129.831 148.062 100.425 1.00 54.24  ? 480  GLY A CA    1 
ATOM   3597  C  C     . GLY A 1 480  ? 131.029 147.236 100.850 1.00 58.55  ? 480  GLY A C     1 
ATOM   3598  O  O     . GLY A 1 480  ? 131.092 146.675 101.948 1.00 61.15  ? 480  GLY A O     1 
ATOM   3599  N  N     . LYS A 1 481  ? 132.005 147.168 99.944  1.00 55.90  ? 481  LYS A N     1 
ATOM   3600  C  CA    . LYS A 1 481  ? 133.189 146.344 100.138 1.00 52.85  ? 481  LYS A CA    1 
ATOM   3601  C  C     . LYS A 1 481  ? 134.437 147.126 99.760  1.00 50.89  ? 481  LYS A C     1 
ATOM   3602  O  O     . LYS A 1 481  ? 134.394 148.037 98.931  1.00 56.33  ? 481  LYS A O     1 
ATOM   3603  C  CB    . LYS A 1 481  ? 133.123 145.056 99.306  1.00 59.94  ? 481  LYS A CB    1 
ATOM   3604  C  CG    . LYS A 1 481  ? 131.797 144.327 99.409  1.00 68.40  ? 481  LYS A CG    1 
ATOM   3605  C  CD    . LYS A 1 481  ? 131.817 142.993 98.690  1.00 76.34  ? 481  LYS A CD    1 
ATOM   3606  C  CE    . LYS A 1 481  ? 130.406 142.450 98.540  1.00 86.94  ? 481  LYS A CE    1 
ATOM   3607  N  NZ    . LYS A 1 481  ? 129.736 142.278 99.859  1.00 84.48  ? 481  LYS A NZ    1 
ATOM   3608  N  N     . ILE A 1 482  ? 135.551 146.759 100.388 1.00 47.92  ? 482  ILE A N     1 
ATOM   3609  C  CA    . ILE A 1 482  ? 136.870 147.294 100.067 1.00 48.35  ? 482  ILE A CA    1 
ATOM   3610  C  C     . ILE A 1 482  ? 137.846 146.124 100.031 1.00 49.49  ? 482  ILE A C     1 
ATOM   3611  O  O     . ILE A 1 482  ? 137.878 145.308 100.958 1.00 49.64  ? 482  ILE A O     1 
ATOM   3612  C  CB    . ILE A 1 482  ? 137.315 148.375 101.077 1.00 48.26  ? 482  ILE A CB    1 
ATOM   3613  C  CG1   . ILE A 1 482  ? 138.735 148.867 100.776 1.00 47.11  ? 482  ILE A CG1   1 
ATOM   3614  C  CG2   . ILE A 1 482  ? 137.187 147.883 102.510 1.00 46.35  ? 482  ILE A CG2   1 
ATOM   3615  C  CD1   . ILE A 1 482  ? 138.940 149.363 99.363  1.00 49.43  ? 482  ILE A CD1   1 
ATOM   3616  N  N     . LYS A 1 483  ? 138.619 146.020 98.951  1.00 49.87  ? 483  LYS A N     1 
ATOM   3617  C  CA    . LYS A 1 483  ? 139.464 144.858 98.707  1.00 49.17  ? 483  LYS A CA    1 
ATOM   3618  C  C     . LYS A 1 483  ? 140.863 145.292 98.295  1.00 49.01  ? 483  LYS A C     1 
ATOM   3619  O  O     . LYS A 1 483  ? 141.015 146.099 97.374  1.00 52.27  ? 483  LYS A O     1 
ATOM   3620  C  CB    . LYS A 1 483  ? 138.849 143.973 97.623  1.00 53.83  ? 483  LYS A CB    1 
ATOM   3621  C  CG    . LYS A 1 483  ? 139.731 142.836 97.161  1.00 62.55  ? 483  LYS A CG    1 
ATOM   3622  C  CD    . LYS A 1 483  ? 138.980 141.942 96.193  1.00 67.41  ? 483  LYS A CD    1 
ATOM   3623  C  CE    . LYS A 1 483  ? 138.549 142.729 94.972  1.00 71.14  ? 483  LYS A CE    1 
ATOM   3624  N  NZ    . LYS A 1 483  ? 137.839 141.884 93.975  1.00 65.40  ? 483  LYS A NZ    1 
ATOM   3625  N  N     . HIS A 1 484  ? 141.877 144.742 98.961  1.00 50.46  ? 484  HIS A N     1 
ATOM   3626  C  CA    . HIS A 1 484  ? 143.273 144.983 98.609  1.00 48.74  ? 484  HIS A CA    1 
ATOM   3627  C  C     . HIS A 1 484  ? 144.139 143.946 99.318  1.00 46.42  ? 484  HIS A C     1 
ATOM   3628  O  O     . HIS A 1 484  ? 143.644 143.099 100.065 1.00 46.38  ? 484  HIS A O     1 
ATOM   3629  C  CB    . HIS A 1 484  ? 143.699 146.416 98.943  1.00 44.67  ? 484  HIS A CB    1 
ATOM   3630  C  CG    . HIS A 1 484  ? 143.562 146.772 100.390 1.00 42.46  ? 484  HIS A CG    1 
ATOM   3631  N  ND1   . HIS A 1 484  ? 144.504 146.429 101.334 1.00 43.00  ? 484  HIS A ND1   1 
ATOM   3632  C  CD2   . HIS A 1 484  ? 142.590 147.439 101.054 1.00 40.17  ? 484  HIS A CD2   1 
ATOM   3633  C  CE1   . HIS A 1 484  ? 144.121 146.873 102.518 1.00 39.66  ? 484  HIS A CE1   1 
ATOM   3634  N  NE2   . HIS A 1 484  ? 142.961 147.487 102.376 1.00 35.72  ? 484  HIS A NE2   1 
ATOM   3635  N  N     . SER A 1 485  ? 145.451 144.019 99.068  1.00 46.98  ? 485  SER A N     1 
ATOM   3636  C  CA    . SER A 1 485  ? 146.368 142.984 99.542  1.00 44.20  ? 485  SER A CA    1 
ATOM   3637  C  C     . SER A 1 485  ? 146.474 142.948 101.060 1.00 41.08  ? 485  SER A C     1 
ATOM   3638  O  O     . SER A 1 485  ? 146.584 141.866 101.646 1.00 43.57  ? 485  SER A O     1 
ATOM   3639  C  CB    . SER A 1 485  ? 147.753 143.190 98.930  1.00 44.31  ? 485  SER A CB    1 
ATOM   3640  O  OG    . SER A 1 485  ? 147.760 142.827 97.563  1.00 50.23  ? 485  SER A OG    1 
ATOM   3641  N  N     . GLY A 1 486  ? 146.460 144.104 101.713 1.00 40.41  ? 486  GLY A N     1 
ATOM   3642  C  CA    . GLY A 1 486  ? 146.611 144.175 103.149 1.00 38.37  ? 486  GLY A CA    1 
ATOM   3643  C  C     . GLY A 1 486  ? 147.961 144.659 103.630 1.00 38.77  ? 486  GLY A C     1 
ATOM   3644  O  O     . GLY A 1 486  ? 148.164 144.757 104.845 1.00 39.20  ? 486  GLY A O     1 
ATOM   3645  N  N     . ARG A 1 487  ? 148.892 144.944 102.722 1.00 38.01  ? 487  ARG A N     1 
ATOM   3646  C  CA    . ARG A 1 487  ? 150.172 145.557 103.060 1.00 34.52  ? 487  ARG A CA    1 
ATOM   3647  C  C     . ARG A 1 487  ? 150.111 147.028 102.669 1.00 37.54  ? 487  ARG A C     1 
ATOM   3648  O  O     . ARG A 1 487  ? 150.124 147.359 101.480 1.00 44.98  ? 487  ARG A O     1 
ATOM   3649  C  CB    . ARG A 1 487  ? 151.322 144.849 102.348 1.00 38.60  ? 487  ARG A CB    1 
ATOM   3650  C  CG    . ARG A 1 487  ? 151.292 143.345 102.480 1.00 42.85  ? 487  ARG A CG    1 
ATOM   3651  C  CD    . ARG A 1 487  ? 152.684 142.754 102.422 1.00 43.55  ? 487  ARG A CD    1 
ATOM   3652  N  NE    . ARG A 1 487  ? 153.438 143.243 101.275 1.00 48.89  ? 487  ARG A NE    1 
ATOM   3653  C  CZ    . ARG A 1 487  ? 154.692 143.668 101.330 1.00 52.68  ? 487  ARG A CZ    1 
ATOM   3654  N  NH1   . ARG A 1 487  ? 155.366 143.685 102.468 1.00 51.19  ? 487  ARG A NH1   1 
ATOM   3655  N  NH2   . ARG A 1 487  ? 155.289 144.076 100.213 1.00 47.52  ? 487  ARG A NH2   1 
ATOM   3656  N  N     . ILE A 1 488  ? 150.053 147.909 103.665 1.00 32.12  ? 488  ILE A N     1 
ATOM   3657  C  CA    . ILE A 1 488  ? 149.880 149.336 103.433 1.00 33.85  ? 488  ILE A CA    1 
ATOM   3658  C  C     . ILE A 1 488  ? 150.948 150.115 104.185 1.00 37.06  ? 488  ILE A C     1 
ATOM   3659  O  O     . ILE A 1 488  ? 151.521 149.639 105.170 1.00 38.01  ? 488  ILE A O     1 
ATOM   3660  C  CB    . ILE A 1 488  ? 148.471 149.822 103.847 1.00 34.58  ? 488  ILE A CB    1 
ATOM   3661  C  CG1   . ILE A 1 488  ? 148.383 149.974 105.364 1.00 38.37  ? 488  ILE A CG1   1 
ATOM   3662  C  CG2   . ILE A 1 488  ? 147.396 148.881 103.341 1.00 35.44  ? 488  ILE A CG2   1 
ATOM   3663  C  CD1   . ILE A 1 488  ? 147.388 151.002 105.812 1.00 38.75  ? 488  ILE A CD1   1 
ATOM   3664  N  N     . SER A 1 489  ? 151.223 151.321 103.694 1.00 36.44  ? 489  SER A N     1 
ATOM   3665  C  CA    . SER A 1 489  ? 152.063 152.302 104.364 1.00 32.91  ? 489  SER A CA    1 
ATOM   3666  C  C     . SER A 1 489  ? 151.309 153.623 104.407 1.00 36.30  ? 489  SER A C     1 
ATOM   3667  O  O     . SER A 1 489  ? 150.654 154.001 103.432 1.00 37.60  ? 489  SER A O     1 
ATOM   3668  C  CB    . SER A 1 489  ? 153.402 152.474 103.647 1.00 32.10  ? 489  SER A CB    1 
ATOM   3669  O  OG    . SER A 1 489  ? 154.230 153.391 104.332 1.00 34.34  ? 489  SER A OG    1 
ATOM   3670  N  N     . PHE A 1 490  ? 151.402 154.325 105.533 1.00 35.20  ? 490  PHE A N     1 
ATOM   3671  C  CA    . PHE A 1 490  ? 150.525 155.453 105.809 1.00 33.19  ? 490  PHE A CA    1 
ATOM   3672  C  C     . PHE A 1 490  ? 151.326 156.678 106.227 1.00 36.37  ? 490  PHE A C     1 
ATOM   3673  O  O     . PHE A 1 490  ? 152.307 156.568 106.967 1.00 39.27  ? 490  PHE A O     1 
ATOM   3674  C  CB    . PHE A 1 490  ? 149.511 155.080 106.901 1.00 34.06  ? 490  PHE A CB    1 
ATOM   3675  C  CG    . PHE A 1 490  ? 148.636 156.214 107.333 1.00 33.87  ? 490  PHE A CG    1 
ATOM   3676  C  CD1   . PHE A 1 490  ? 147.875 156.906 106.410 1.00 34.09  ? 490  PHE A CD1   1 
ATOM   3677  C  CD2   . PHE A 1 490  ? 148.561 156.576 108.665 1.00 32.30  ? 490  PHE A CD2   1 
ATOM   3678  C  CE1   . PHE A 1 490  ? 147.067 157.948 106.805 1.00 34.87  ? 490  PHE A CE1   1 
ATOM   3679  C  CE2   . PHE A 1 490  ? 147.752 157.615 109.067 1.00 33.66  ? 490  PHE A CE2   1 
ATOM   3680  C  CZ    . PHE A 1 490  ? 147.004 158.302 108.136 1.00 35.79  ? 490  PHE A CZ    1 
ATOM   3681  N  N     . CYS A 1 491  ? 150.897 157.845 105.746 1.00 35.49  ? 491  CYS A N     1 
ATOM   3682  C  CA    . CYS A 1 491  ? 151.476 159.132 106.122 1.00 32.59  ? 491  CYS A CA    1 
ATOM   3683  C  C     . CYS A 1 491  ? 150.343 160.051 106.559 1.00 38.81  ? 491  CYS A C     1 
ATOM   3684  O  O     . CYS A 1 491  ? 149.539 160.487 105.730 1.00 39.30  ? 491  CYS A O     1 
ATOM   3685  C  CB    . CYS A 1 491  ? 152.261 159.746 104.964 1.00 31.87  ? 491  CYS A CB    1 
ATOM   3686  S  SG    . CYS A 1 491  ? 153.098 161.290 105.365 1.00 43.59  ? 491  CYS A SG    1 
ATOM   3687  N  N     . SER A 1 492  ? 150.281 160.344 107.854 1.00 40.40  ? 492  SER A N     1 
ATOM   3688  C  CA    . SER A 1 492  ? 149.164 161.087 108.417 1.00 35.59  ? 492  SER A CA    1 
ATOM   3689  C  C     . SER A 1 492  ? 149.291 162.583 108.149 1.00 35.07  ? 492  SER A C     1 
ATOM   3690  O  O     . SER A 1 492  ? 150.388 163.115 107.961 1.00 40.91  ? 492  SER A O     1 
ATOM   3691  C  CB    . SER A 1 492  ? 149.066 160.836 109.921 1.00 34.93  ? 492  SER A CB    1 
ATOM   3692  O  OG    . SER A 1 492  ? 147.926 161.469 110.472 1.00 42.39  ? 492  SER A OG    1 
ATOM   3693  N  N     . GLN A 1 493  ? 148.142 163.261 108.131 1.00 35.17  ? 493  GLN A N     1 
ATOM   3694  C  CA    . GLN A 1 493  ? 148.134 164.707 107.940 1.00 35.87  ? 493  GLN A CA    1 
ATOM   3695  C  C     . GLN A 1 493  ? 148.669 165.436 109.168 1.00 39.02  ? 493  GLN A C     1 
ATOM   3696  O  O     . GLN A 1 493  ? 149.172 166.559 109.051 1.00 40.07  ? 493  GLN A O     1 
ATOM   3697  C  CB    . GLN A 1 493  ? 146.721 165.174 107.585 1.00 31.41  ? 493  GLN A CB    1 
ATOM   3698  C  CG    . GLN A 1 493  ? 146.607 166.639 107.219 1.00 33.72  ? 493  GLN A CG    1 
ATOM   3699  C  CD    . GLN A 1 493  ? 145.233 167.002 106.702 1.00 33.45  ? 493  GLN A CD    1 
ATOM   3700  O  OE1   . GLN A 1 493  ? 144.250 166.323 106.987 1.00 36.86  ? 493  GLN A OE1   1 
ATOM   3701  N  NE2   . GLN A 1 493  ? 145.159 168.078 105.930 1.00 29.58  ? 493  GLN A NE2   1 
ATOM   3702  N  N     . PHE A 1 494  ? 148.568 164.823 110.345 1.00 36.99  ? 494  PHE A N     1 
ATOM   3703  C  CA    . PHE A 1 494  ? 149.227 165.309 111.550 1.00 36.18  ? 494  PHE A CA    1 
ATOM   3704  C  C     . PHE A 1 494  ? 150.469 164.458 111.787 1.00 41.83  ? 494  PHE A C     1 
ATOM   3705  O  O     . PHE A 1 494  ? 150.375 163.229 111.880 1.00 40.65  ? 494  PHE A O     1 
ATOM   3706  C  CB    . PHE A 1 494  ? 148.289 165.258 112.756 1.00 44.74  ? 494  PHE A CB    1 
ATOM   3707  C  CG    . PHE A 1 494  ? 148.876 165.854 114.008 1.00 53.97  ? 494  PHE A CG    1 
ATOM   3708  C  CD1   . PHE A 1 494  ? 149.701 165.107 114.834 1.00 54.07  ? 494  PHE A CD1   1 
ATOM   3709  C  CD2   . PHE A 1 494  ? 148.616 167.171 114.346 1.00 56.49  ? 494  PHE A CD2   1 
ATOM   3710  C  CE1   . PHE A 1 494  ? 150.246 165.660 115.976 1.00 52.25  ? 494  PHE A CE1   1 
ATOM   3711  C  CE2   . PHE A 1 494  ? 149.158 167.728 115.486 1.00 63.40  ? 494  PHE A CE2   1 
ATOM   3712  C  CZ    . PHE A 1 494  ? 149.974 166.971 116.302 1.00 59.86  ? 494  PHE A CZ    1 
ATOM   3713  N  N     . SER A 1 495  ? 151.624 165.110 111.878 1.00 42.75  ? 495  SER A N     1 
ATOM   3714  C  CA    . SER A 1 495  ? 152.900 164.405 111.933 1.00 38.68  ? 495  SER A CA    1 
ATOM   3715  C  C     . SER A 1 495  ? 153.163 163.860 113.332 1.00 40.43  ? 495  SER A C     1 
ATOM   3716  O  O     . SER A 1 495  ? 153.180 164.616 114.308 1.00 41.67  ? 495  SER A O     1 
ATOM   3717  C  CB    . SER A 1 495  ? 154.020 165.344 111.503 1.00 39.45  ? 495  SER A CB    1 
ATOM   3718  O  OG    . SER A 1 495  ? 153.903 165.657 110.128 1.00 43.93  ? 495  SER A OG    1 
ATOM   3719  N  N     . TRP A 1 496  ? 153.378 162.548 113.426 1.00 40.96  ? 496  TRP A N     1 
ATOM   3720  C  CA    . TRP A 1 496  ? 153.671 161.887 114.691 1.00 32.83  ? 496  TRP A CA    1 
ATOM   3721  C  C     . TRP A 1 496  ? 155.166 161.607 114.805 1.00 33.89  ? 496  TRP A C     1 
ATOM   3722  O  O     . TRP A 1 496  ? 155.763 161.009 113.904 1.00 34.63  ? 496  TRP A O     1 
ATOM   3723  C  CB    . TRP A 1 496  ? 152.874 160.588 114.809 1.00 25.62  ? 496  TRP A CB    1 
ATOM   3724  C  CG    . TRP A 1 496  ? 153.213 159.777 116.017 1.00 27.19  ? 496  TRP A CG    1 
ATOM   3725  C  CD1   . TRP A 1 496  ? 152.992 160.115 117.319 1.00 30.52  ? 496  TRP A CD1   1 
ATOM   3726  C  CD2   . TRP A 1 496  ? 153.824 158.486 116.037 1.00 27.54  ? 496  TRP A CD2   1 
ATOM   3727  N  NE1   . TRP A 1 496  ? 153.436 159.118 118.148 1.00 29.83  ? 496  TRP A NE1   1 
ATOM   3728  C  CE2   . TRP A 1 496  ? 153.952 158.106 117.384 1.00 30.05  ? 496  TRP A CE2   1 
ATOM   3729  C  CE3   . TRP A 1 496  ? 154.281 157.616 115.045 1.00 28.28  ? 496  TRP A CE3   1 
ATOM   3730  C  CZ2   . TRP A 1 496  ? 154.514 156.892 117.765 1.00 29.66  ? 496  TRP A CZ2   1 
ATOM   3731  C  CZ3   . TRP A 1 496  ? 154.838 156.415 115.424 1.00 29.72  ? 496  TRP A CZ3   1 
ATOM   3732  C  CH2   . TRP A 1 496  ? 154.949 156.062 116.771 1.00 29.51  ? 496  TRP A CH2   1 
ATOM   3733  N  N     . ILE A 1 497  ? 155.763 162.032 115.917 1.00 33.84  ? 497  ILE A N     1 
ATOM   3734  C  CA    . ILE A 1 497  ? 157.193 161.881 116.171 1.00 32.33  ? 497  ILE A CA    1 
ATOM   3735  C  C     . ILE A 1 497  ? 157.363 161.180 117.511 1.00 34.23  ? 497  ILE A C     1 
ATOM   3736  O  O     . ILE A 1 497  ? 156.840 161.649 118.528 1.00 41.71  ? 497  ILE A O     1 
ATOM   3737  C  CB    . ILE A 1 497  ? 157.924 163.235 116.179 1.00 33.95  ? 497  ILE A CB    1 
ATOM   3738  C  CG1   . ILE A 1 497  ? 157.769 163.954 114.838 1.00 30.02  ? 497  ILE A CG1   1 
ATOM   3739  C  CG2   . ILE A 1 497  ? 159.392 163.045 116.504 1.00 35.39  ? 497  ILE A CG2   1 
ATOM   3740  C  CD1   . ILE A 1 497  ? 158.494 163.292 113.698 1.00 26.92  ? 497  ILE A CD1   1 
ATOM   3741  N  N     . MET A 1 498  ? 158.082 160.064 117.514 1.00 33.95  ? 498  MET A N     1 
ATOM   3742  C  CA    . MET A 1 498  ? 158.346 159.316 118.733 1.00 37.43  ? 498  MET A CA    1 
ATOM   3743  C  C     . MET A 1 498  ? 159.720 159.662 119.296 1.00 42.56  ? 498  MET A C     1 
ATOM   3744  O  O     . MET A 1 498  ? 160.600 160.135 118.570 1.00 40.99  ? 498  MET A O     1 
ATOM   3745  C  CB    . MET A 1 498  ? 158.245 157.817 118.458 1.00 35.15  ? 498  MET A CB    1 
ATOM   3746  C  CG    . MET A 1 498  ? 158.797 157.380 117.119 1.00 37.58  ? 498  MET A CG    1 
ATOM   3747  S  SD    . MET A 1 498  ? 159.439 155.696 117.149 1.00 52.14  ? 498  MET A SD    1 
ATOM   3748  C  CE    . MET A 1 498  ? 161.146 155.986 117.598 1.00 46.95  ? 498  MET A CE    1 
ATOM   3749  N  N     . PRO A 1 499  ? 159.928 159.461 120.600 1.00 42.71  ? 499  PRO A N     1 
ATOM   3750  C  CA    . PRO A 1 499  ? 161.245 159.739 121.186 1.00 38.63  ? 499  PRO A CA    1 
ATOM   3751  C  C     . PRO A 1 499  ? 162.338 158.889 120.556 1.00 41.72  ? 499  PRO A C     1 
ATOM   3752  O  O     . PRO A 1 499  ? 162.143 157.711 120.253 1.00 44.53  ? 499  PRO A O     1 
ATOM   3753  C  CB    . PRO A 1 499  ? 161.051 159.400 122.669 1.00 36.78  ? 499  PRO A CB    1 
ATOM   3754  C  CG    . PRO A 1 499  ? 159.592 159.517 122.889 1.00 37.87  ? 499  PRO A CG    1 
ATOM   3755  C  CD    . PRO A 1 499  ? 158.966 159.028 121.625 1.00 39.45  ? 499  PRO A CD    1 
ATOM   3756  N  N     . GLY A 1 500  ? 163.502 159.500 120.378 1.00 42.04  ? 500  GLY A N     1 
ATOM   3757  C  CA    . GLY A 1 500  ? 164.625 158.888 119.705 1.00 40.46  ? 500  GLY A CA    1 
ATOM   3758  C  C     . GLY A 1 500  ? 165.217 159.817 118.671 1.00 43.44  ? 500  GLY A C     1 
ATOM   3759  O  O     . GLY A 1 500  ? 164.812 160.967 118.518 1.00 48.11  ? 500  GLY A O     1 
ATOM   3760  N  N     . THR A 1 501  ? 166.203 159.295 117.951 1.00 40.73  ? 501  THR A N     1 
ATOM   3761  C  CA    . THR A 1 501  ? 166.881 160.069 116.925 1.00 39.98  ? 501  THR A CA    1 
ATOM   3762  C  C     . THR A 1 501  ? 166.068 160.080 115.631 1.00 39.62  ? 501  THR A C     1 
ATOM   3763  O  O     . THR A 1 501  ? 165.052 159.396 115.496 1.00 42.32  ? 501  THR A O     1 
ATOM   3764  C  CB    . THR A 1 501  ? 168.282 159.510 116.679 1.00 46.24  ? 501  THR A CB    1 
ATOM   3765  O  OG1   . THR A 1 501  ? 168.189 158.296 115.925 1.00 45.50  ? 501  THR A OG1   1 
ATOM   3766  C  CG2   . THR A 1 501  ? 168.977 159.226 117.997 1.00 44.34  ? 501  THR A CG2   1 
ATOM   3767  N  N     . ILE A 1 502  ? 166.526 160.887 114.671 1.00 39.99  ? 502  ILE A N     1 
ATOM   3768  C  CA    . ILE A 1 502  ? 165.880 160.932 113.360 1.00 36.53  ? 502  ILE A CA    1 
ATOM   3769  C  C     . ILE A 1 502  ? 165.990 159.582 112.663 1.00 38.31  ? 502  ILE A C     1 
ATOM   3770  O  O     . ILE A 1 502  ? 165.027 159.098 112.051 1.00 39.67  ? 502  ILE A O     1 
ATOM   3771  C  CB    . ILE A 1 502  ? 166.487 162.059 112.504 1.00 39.93  ? 502  ILE A CB    1 
ATOM   3772  C  CG1   . ILE A 1 502  ? 166.221 163.424 113.142 1.00 37.25  ? 502  ILE A CG1   1 
ATOM   3773  C  CG2   . ILE A 1 502  ? 165.951 162.013 111.087 1.00 41.13  ? 502  ILE A CG2   1 
ATOM   3774  C  CD1   . ILE A 1 502  ? 166.936 164.558 112.456 1.00 37.80  ? 502  ILE A CD1   1 
ATOM   3775  N  N     . LYS A 1 503  ? 167.162 158.951 112.747 1.00 42.22  ? 503  LYS A N     1 
ATOM   3776  C  CA    . LYS A 1 503  ? 167.366 157.664 112.092 1.00 39.50  ? 503  LYS A CA    1 
ATOM   3777  C  C     . LYS A 1 503  ? 166.447 156.597 112.671 1.00 34.86  ? 503  LYS A C     1 
ATOM   3778  O  O     . LYS A 1 503  ? 165.910 155.769 111.931 1.00 33.83  ? 503  LYS A O     1 
ATOM   3779  C  CB    . LYS A 1 503  ? 168.829 157.246 112.216 1.00 38.45  ? 503  LYS A CB    1 
ATOM   3780  C  CG    . LYS A 1 503  ? 169.186 155.981 111.463 1.00 40.62  ? 503  LYS A CG    1 
ATOM   3781  C  CD    . LYS A 1 503  ? 170.674 155.716 111.548 1.00 41.09  ? 503  LYS A CD    1 
ATOM   3782  C  CE    . LYS A 1 503  ? 171.460 156.811 110.849 1.00 48.53  ? 503  LYS A CE    1 
ATOM   3783  N  NZ    . LYS A 1 503  ? 172.920 156.533 110.815 1.00 50.78  ? 503  LYS A NZ    1 
ATOM   3784  N  N     . GLU A 1 504  ? 166.259 156.597 113.992 1.00 36.41  ? 504  GLU A N     1 
ATOM   3785  C  CA    . GLU A 1 504  ? 165.336 155.653 114.611 1.00 35.60  ? 504  GLU A CA    1 
ATOM   3786  C  C     . GLU A 1 504  ? 163.893 155.939 114.223 1.00 35.76  ? 504  GLU A C     1 
ATOM   3787  O  O     . GLU A 1 504  ? 163.087 155.009 114.111 1.00 40.22  ? 504  GLU A O     1 
ATOM   3788  C  CB    . GLU A 1 504  ? 165.489 155.689 116.128 1.00 38.81  ? 504  GLU A CB    1 
ATOM   3789  C  CG    . GLU A 1 504  ? 166.903 155.429 116.602 1.00 45.30  ? 504  GLU A CG    1 
ATOM   3790  C  CD    . GLU A 1 504  ? 166.951 154.799 117.974 1.00 57.29  ? 504  GLU A CD    1 
ATOM   3791  O  OE1   . GLU A 1 504  ? 167.520 153.695 118.100 1.00 64.14  ? 504  GLU A OE1   1 
ATOM   3792  O  OE2   . GLU A 1 504  ? 166.421 155.408 118.927 1.00 53.43  ? 504  GLU A OE2   1 
ATOM   3793  N  N     . ASN A 1 505  ? 163.542 157.212 114.036 1.00 35.53  ? 505  ASN A N     1 
ATOM   3794  C  CA    . ASN A 1 505  ? 162.202 157.549 113.571 1.00 30.94  ? 505  ASN A CA    1 
ATOM   3795  C  C     . ASN A 1 505  ? 161.958 157.035 112.159 1.00 30.98  ? 505  ASN A C     1 
ATOM   3796  O  O     . ASN A 1 505  ? 160.870 156.535 111.857 1.00 31.43  ? 505  ASN A O     1 
ATOM   3797  C  CB    . ASN A 1 505  ? 161.987 159.060 113.634 1.00 28.62  ? 505  ASN A CB    1 
ATOM   3798  C  CG    . ASN A 1 505  ? 161.458 159.517 114.973 1.00 34.80  ? 505  ASN A CG    1 
ATOM   3799  O  OD1   . ASN A 1 505  ? 160.250 159.613 115.172 1.00 39.09  ? 505  ASN A OD1   1 
ATOM   3800  N  ND2   . ASN A 1 505  ? 162.360 159.807 115.898 1.00 36.43  ? 505  ASN A ND2   1 
ATOM   3801  N  N     . ILE A 1 506  ? 162.953 157.152 111.281 1.00 33.06  ? 506  ILE A N     1 
ATOM   3802  C  CA    . ILE A 1 506  ? 162.768 156.725 109.896 1.00 28.72  ? 506  ILE A CA    1 
ATOM   3803  C  C     . ILE A 1 506  ? 162.811 155.204 109.774 1.00 29.23  ? 506  ILE A C     1 
ATOM   3804  O  O     . ILE A 1 506  ? 161.965 154.603 109.102 1.00 30.84  ? 506  ILE A O     1 
ATOM   3805  C  CB    . ILE A 1 506  ? 163.815 157.402 108.996 1.00 29.31  ? 506  ILE A CB    1 
ATOM   3806  C  CG1   . ILE A 1 506  ? 163.550 158.904 108.921 1.00 29.68  ? 506  ILE A CG1   1 
ATOM   3807  C  CG2   . ILE A 1 506  ? 163.806 156.790 107.611 1.00 28.53  ? 506  ILE A CG2   1 
ATOM   3808  C  CD1   . ILE A 1 506  ? 164.684 159.689 108.328 1.00 35.12  ? 506  ILE A CD1   1 
ATOM   3809  N  N     . ILE A 1 507  ? 163.788 154.558 110.415 1.00 33.09  ? 507  ILE A N     1 
ATOM   3810  C  CA    . ILE A 1 507  ? 163.909 153.101 110.344 1.00 33.38  ? 507  ILE A CA    1 
ATOM   3811  C  C     . ILE A 1 507  ? 162.700 152.439 110.993 1.00 36.15  ? 507  ILE A C     1 
ATOM   3812  O  O     . ILE A 1 507  ? 162.101 151.513 110.434 1.00 40.70  ? 507  ILE A O     1 
ATOM   3813  C  CB    . ILE A 1 507  ? 165.229 152.640 110.990 1.00 34.20  ? 507  ILE A CB    1 
ATOM   3814  C  CG1   . ILE A 1 507  ? 166.367 152.614 109.966 1.00 36.98  ? 507  ILE A CG1   1 
ATOM   3815  C  CG2   . ILE A 1 507  ? 165.079 151.272 111.618 1.00 38.41  ? 507  ILE A CG2   1 
ATOM   3816  C  CD1   . ILE A 1 507  ? 166.584 153.899 109.223 1.00 36.04  ? 507  ILE A CD1   1 
ATOM   3817  N  N     . PHE A 1 508  ? 162.330 152.906 112.185 1.00 32.84  ? 508  PHE A N     1 
ATOM   3818  C  CA    . PHE A 1 508  ? 161.069 152.550 112.834 1.00 33.25  ? 508  PHE A CA    1 
ATOM   3819  C  C     . PHE A 1 508  ? 160.984 151.045 113.105 1.00 37.60  ? 508  PHE A C     1 
ATOM   3820  O  O     . PHE A 1 508  ? 159.994 150.382 112.794 1.00 38.60  ? 508  PHE A O     1 
ATOM   3821  C  CB    . PHE A 1 508  ? 159.886 153.051 111.998 1.00 34.12  ? 508  PHE A CB    1 
ATOM   3822  C  CG    . PHE A 1 508  ? 158.560 152.982 112.696 1.00 34.58  ? 508  PHE A CG    1 
ATOM   3823  C  CD1   . PHE A 1 508  ? 158.441 153.346 114.023 1.00 37.61  ? 508  PHE A CD1   1 
ATOM   3824  C  CD2   . PHE A 1 508  ? 157.419 152.617 112.004 1.00 31.94  ? 508  PHE A CD2   1 
ATOM   3825  C  CE1   . PHE A 1 508  ? 157.221 153.303 114.660 1.00 37.40  ? 508  PHE A CE1   1 
ATOM   3826  C  CE2   . PHE A 1 508  ? 156.194 152.578 112.634 1.00 32.01  ? 508  PHE A CE2   1 
ATOM   3827  C  CZ    . PHE A 1 508  ? 156.095 152.919 113.964 1.00 33.60  ? 508  PHE A CZ    1 
ATOM   3828  N  N     . GLY A 1 509  ? 162.050 150.508 113.695 1.00 43.88  ? 509  GLY A N     1 
ATOM   3829  C  CA    . GLY A 1 509  ? 162.010 149.178 114.272 1.00 41.21  ? 509  GLY A CA    1 
ATOM   3830  C  C     . GLY A 1 509  ? 162.352 148.007 113.377 1.00 42.13  ? 509  GLY A C     1 
ATOM   3831  O  O     . GLY A 1 509  ? 161.924 146.885 113.663 1.00 43.31  ? 509  GLY A O     1 
ATOM   3832  N  N     . VAL A 1 510  ? 163.110 148.220 112.302 1.00 44.98  ? 510  VAL A N     1 
ATOM   3833  C  CA    . VAL A 1 510  ? 163.549 147.141 111.427 1.00 48.41  ? 510  VAL A CA    1 
ATOM   3834  C  C     . VAL A 1 510  ? 165.044 147.284 111.155 1.00 54.81  ? 510  VAL A C     1 
ATOM   3835  O  O     . VAL A 1 510  ? 165.710 148.184 111.664 1.00 52.56  ? 510  VAL A O     1 
ATOM   3836  C  CB    . VAL A 1 510  ? 162.756 147.091 110.106 1.00 46.70  ? 510  VAL A CB    1 
ATOM   3837  C  CG1   . VAL A 1 510  ? 161.303 146.747 110.370 1.00 46.39  ? 510  VAL A CG1   1 
ATOM   3838  C  CG2   . VAL A 1 510  ? 162.875 148.408 109.372 1.00 46.74  ? 510  VAL A CG2   1 
ATOM   3839  N  N     . SER A 1 511  ? 165.565 146.365 110.342 1.00 58.86  ? 511  SER A N     1 
ATOM   3840  C  CA    . SER A 1 511  ? 166.990 146.330 110.036 1.00 57.55  ? 511  SER A CA    1 
ATOM   3841  C  C     . SER A 1 511  ? 167.411 147.542 109.213 1.00 55.28  ? 511  SER A C     1 
ATOM   3842  O  O     . SER A 1 511  ? 166.704 147.965 108.295 1.00 54.73  ? 511  SER A O     1 
ATOM   3843  C  CB    . SER A 1 511  ? 167.334 145.043 109.290 1.00 61.73  ? 511  SER A CB    1 
ATOM   3844  O  OG    . SER A 1 511  ? 167.329 143.931 110.167 1.00 65.62  ? 511  SER A OG    1 
ATOM   3845  N  N     . TYR A 1 512  ? 168.574 148.093 109.548 1.00 52.83  ? 512  TYR A N     1 
ATOM   3846  C  CA    . TYR A 1 512  ? 169.121 149.252 108.853 1.00 50.39  ? 512  TYR A CA    1 
ATOM   3847  C  C     . TYR A 1 512  ? 169.762 148.819 107.539 1.00 52.31  ? 512  TYR A C     1 
ATOM   3848  O  O     . TYR A 1 512  ? 170.689 148.003 107.533 1.00 55.97  ? 512  TYR A O     1 
ATOM   3849  C  CB    . TYR A 1 512  ? 170.141 149.954 109.746 1.00 48.34  ? 512  TYR A CB    1 
ATOM   3850  C  CG    . TYR A 1 512  ? 170.879 151.108 109.101 1.00 50.28  ? 512  TYR A CG    1 
ATOM   3851  C  CD1   . TYR A 1 512  ? 170.310 152.371 109.029 1.00 49.26  ? 512  TYR A CD1   1 
ATOM   3852  C  CD2   . TYR A 1 512  ? 172.152 150.935 108.581 1.00 48.09  ? 512  TYR A CD2   1 
ATOM   3853  C  CE1   . TYR A 1 512  ? 170.987 153.423 108.450 1.00 51.91  ? 512  TYR A CE1   1 
ATOM   3854  C  CE2   . TYR A 1 512  ? 172.834 151.983 107.999 1.00 47.35  ? 512  TYR A CE2   1 
ATOM   3855  C  CZ    . TYR A 1 512  ? 172.248 153.223 107.937 1.00 52.45  ? 512  TYR A CZ    1 
ATOM   3856  O  OH    . TYR A 1 512  ? 172.929 154.267 107.357 1.00 54.74  ? 512  TYR A OH    1 
ATOM   3857  N  N     . ASP A 1 513  ? 169.266 149.360 106.428 1.00 52.17  ? 513  ASP A N     1 
ATOM   3858  C  CA    . ASP A 1 513  ? 169.868 149.174 105.113 1.00 51.09  ? 513  ASP A CA    1 
ATOM   3859  C  C     . ASP A 1 513  ? 170.415 150.518 104.655 1.00 53.90  ? 513  ASP A C     1 
ATOM   3860  O  O     . ASP A 1 513  ? 169.667 151.497 104.566 1.00 56.78  ? 513  ASP A O     1 
ATOM   3861  C  CB    . ASP A 1 513  ? 168.852 148.628 104.111 1.00 55.18  ? 513  ASP A CB    1 
ATOM   3862  C  CG    . ASP A 1 513  ? 169.470 148.320 102.762 1.00 62.93  ? 513  ASP A CG    1 
ATOM   3863  O  OD1   . ASP A 1 513  ? 170.538 147.675 102.729 1.00 68.78  ? 513  ASP A OD1   1 
ATOM   3864  O  OD2   . ASP A 1 513  ? 168.884 148.716 101.734 1.00 63.31  ? 513  ASP A OD2   1 
ATOM   3865  N  N     . GLU A 1 514  ? 171.715 150.562 104.368 1.00 54.51  ? 514  GLU A N     1 
ATOM   3866  C  CA    . GLU A 1 514  ? 172.383 151.839 104.137 1.00 56.86  ? 514  GLU A CA    1 
ATOM   3867  C  C     . GLU A 1 514  ? 171.978 152.452 102.800 1.00 55.55  ? 514  GLU A C     1 
ATOM   3868  O  O     . GLU A 1 514  ? 171.721 153.658 102.714 1.00 59.90  ? 514  GLU A O     1 
ATOM   3869  C  CB    . GLU A 1 514  ? 173.898 151.645 104.218 1.00 61.60  ? 514  GLU A CB    1 
ATOM   3870  C  CG    . GLU A 1 514  ? 174.699 152.928 104.351 1.00 65.93  ? 514  GLU A CG    1 
ATOM   3871  C  CD    . GLU A 1 514  ? 175.138 153.485 103.018 1.00 71.32  ? 514  GLU A CD    1 
ATOM   3872  O  OE1   . GLU A 1 514  ? 174.977 152.785 101.997 1.00 70.02  ? 514  GLU A OE1   1 
ATOM   3873  O  OE2   . GLU A 1 514  ? 175.658 154.619 102.993 1.00 77.48  ? 514  GLU A OE2   1 
ATOM   3874  N  N     . TYR A 1 515  ? 171.923 151.639 101.743 1.00 51.72  ? 515  TYR A N     1 
ATOM   3875  C  CA    . TYR A 1 515  ? 171.627 152.163 100.411 1.00 53.07  ? 515  TYR A CA    1 
ATOM   3876  C  C     . TYR A 1 515  ? 170.235 152.785 100.350 1.00 54.58  ? 515  TYR A C     1 
ATOM   3877  O  O     . TYR A 1 515  ? 170.067 153.916 99.871  1.00 54.77  ? 515  TYR A O     1 
ATOM   3878  C  CB    . TYR A 1 515  ? 171.771 151.049 99.374  1.00 55.25  ? 515  TYR A CB    1 
ATOM   3879  C  CG    . TYR A 1 515  ? 171.326 151.434 97.981  1.00 57.66  ? 515  TYR A CG    1 
ATOM   3880  C  CD1   . TYR A 1 515  ? 171.961 152.451 97.285  1.00 61.11  ? 515  TYR A CD1   1 
ATOM   3881  C  CD2   . TYR A 1 515  ? 170.280 150.768 97.358  1.00 59.31  ? 515  TYR A CD2   1 
ATOM   3882  C  CE1   . TYR A 1 515  ? 171.558 152.804 96.013  1.00 62.62  ? 515  TYR A CE1   1 
ATOM   3883  C  CE2   . TYR A 1 515  ? 169.872 151.113 96.086  1.00 63.47  ? 515  TYR A CE2   1 
ATOM   3884  C  CZ    . TYR A 1 515  ? 170.513 152.131 95.419  1.00 66.07  ? 515  TYR A CZ    1 
ATOM   3885  O  OH    . TYR A 1 515  ? 170.108 152.476 94.151  1.00 67.97  ? 515  TYR A OH    1 
ATOM   3886  N  N     . ARG A 1 516  ? 169.220 152.059 100.829 1.00 52.22  ? 516  ARG A N     1 
ATOM   3887  C  CA    . ARG A 1 516  ? 167.866 152.600 100.794 1.00 49.30  ? 516  ARG A CA    1 
ATOM   3888  C  C     . ARG A 1 516  ? 167.739 153.816 101.699 1.00 49.26  ? 516  ARG A C     1 
ATOM   3889  O  O     . ARG A 1 516  ? 167.017 154.762 101.376 1.00 50.44  ? 516  ARG A O     1 
ATOM   3890  C  CB    . ARG A 1 516  ? 166.834 151.533 101.175 1.00 51.63  ? 516  ARG A CB    1 
ATOM   3891  C  CG    . ARG A 1 516  ? 165.406 152.060 101.035 1.00 53.60  ? 516  ARG A CG    1 
ATOM   3892  C  CD    . ARG A 1 516  ? 164.354 151.013 100.686 1.00 56.10  ? 516  ARG A CD    1 
ATOM   3893  N  NE    . ARG A 1 516  ? 163.827 150.283 101.831 1.00 56.92  ? 516  ARG A NE    1 
ATOM   3894  C  CZ    . ARG A 1 516  ? 163.997 148.986 102.038 1.00 64.56  ? 516  ARG A CZ    1 
ATOM   3895  N  NH1   . ARG A 1 516  ? 164.697 148.239 101.201 1.00 70.63  ? 516  ARG A NH1   1 
ATOM   3896  N  NH2   . ARG A 1 516  ? 163.429 148.420 103.097 1.00 60.11  ? 516  ARG A NH2   1 
ATOM   3897  N  N     . TYR A 1 517  ? 168.434 153.810 102.838 1.00 48.77  ? 517  TYR A N     1 
ATOM   3898  C  CA    . TYR A 1 517  ? 168.411 154.973 103.718 1.00 46.32  ? 517  TYR A CA    1 
ATOM   3899  C  C     . TYR A 1 517  ? 168.964 156.207 103.022 1.00 47.40  ? 517  TYR A C     1 
ATOM   3900  O  O     . TYR A 1 517  ? 168.355 157.282 103.073 1.00 46.61  ? 517  TYR A O     1 
ATOM   3901  C  CB    . TYR A 1 517  ? 169.204 154.686 104.990 1.00 44.78  ? 517  TYR A CB    1 
ATOM   3902  C  CG    . TYR A 1 517  ? 169.048 155.752 106.045 1.00 48.67  ? 517  TYR A CG    1 
ATOM   3903  C  CD1   . TYR A 1 517  ? 167.861 155.892 106.739 1.00 45.37  ? 517  TYR A CD1   1 
ATOM   3904  C  CD2   . TYR A 1 517  ? 170.091 156.611 106.352 1.00 51.29  ? 517  TYR A CD2   1 
ATOM   3905  C  CE1   . TYR A 1 517  ? 167.712 156.860 107.701 1.00 44.04  ? 517  TYR A CE1   1 
ATOM   3906  C  CE2   . TYR A 1 517  ? 169.950 157.582 107.316 1.00 49.68  ? 517  TYR A CE2   1 
ATOM   3907  C  CZ    . TYR A 1 517  ? 168.757 157.701 107.987 1.00 47.17  ? 517  TYR A CZ    1 
ATOM   3908  O  OH    . TYR A 1 517  ? 168.600 158.663 108.952 1.00 49.22  ? 517  TYR A OH    1 
ATOM   3909  N  N     . ARG A 1 518  ? 170.113 156.070 102.359 1.00 51.03  ? 518  ARG A N     1 
ATOM   3910  C  CA    . ARG A 1 518  ? 170.690 157.209 101.653 1.00 50.47  ? 518  ARG A CA    1 
ATOM   3911  C  C     . ARG A 1 518  ? 169.766 157.687 100.542 1.00 50.59  ? 518  ARG A C     1 
ATOM   3912  O  O     . ARG A 1 518  ? 169.546 158.893 100.387 1.00 51.23  ? 518  ARG A O     1 
ATOM   3913  C  CB    . ARG A 1 518  ? 172.059 156.845 101.075 1.00 51.22  ? 518  ARG A CB    1 
ATOM   3914  C  CG    . ARG A 1 518  ? 173.118 156.359 102.061 1.00 55.19  ? 518  ARG A CG    1 
ATOM   3915  C  CD    . ARG A 1 518  ? 172.935 156.874 103.480 1.00 61.59  ? 518  ARG A CD    1 
ATOM   3916  N  NE    . ARG A 1 518  ? 173.087 158.323 103.559 1.00 74.71  ? 518  ARG A NE    1 
ATOM   3917  C  CZ    . ARG A 1 518  ? 173.454 158.977 104.653 1.00 79.95  ? 518  ARG A CZ    1 
ATOM   3918  N  NH1   . ARG A 1 518  ? 173.716 158.342 105.784 1.00 77.94  ? 518  ARG A NH1   1 
ATOM   3919  N  NH2   . ARG A 1 518  ? 173.562 160.302 104.610 1.00 80.78  ? 518  ARG A NH2   1 
ATOM   3920  N  N     . SER A 1 519  ? 169.202 156.753 99.772  1.00 50.60  ? 519  SER A N     1 
ATOM   3921  C  CA    . SER A 1 519  ? 168.336 157.142 98.664  1.00 47.20  ? 519  SER A CA    1 
ATOM   3922  C  C     . SER A 1 519  ? 167.073 157.843 99.157  1.00 46.00  ? 519  SER A C     1 
ATOM   3923  O  O     . SER A 1 519  ? 166.646 158.845 98.573  1.00 46.00  ? 519  SER A O     1 
ATOM   3924  C  CB    . SER A 1 519  ? 167.979 155.917 97.826  1.00 48.08  ? 519  SER A CB    1 
ATOM   3925  O  OG    . SER A 1 519  ? 167.081 155.074 98.521  1.00 52.38  ? 519  SER A OG    1 
ATOM   3926  N  N     . VAL A 1 520  ? 166.471 157.344 100.239 1.00 46.85  ? 520  VAL A N     1 
ATOM   3927  C  CA    . VAL A 1 520  ? 165.241 157.941 100.750 1.00 43.84  ? 520  VAL A CA    1 
ATOM   3928  C  C     . VAL A 1 520  ? 165.522 159.307 101.360 1.00 41.03  ? 520  VAL A C     1 
ATOM   3929  O  O     . VAL A 1 520  ? 164.745 160.251 101.176 1.00 41.03  ? 520  VAL A O     1 
ATOM   3930  C  CB    . VAL A 1 520  ? 164.566 156.994 101.760 1.00 42.41  ? 520  VAL A CB    1 
ATOM   3931  C  CG1   . VAL A 1 520  ? 163.470 157.717 102.521 1.00 35.90  ? 520  VAL A CG1   1 
ATOM   3932  C  CG2   . VAL A 1 520  ? 164.004 155.778 101.049 1.00 37.27  ? 520  VAL A CG2   1 
ATOM   3933  N  N     . ILE A 1 521  ? 166.632 159.442 102.090 1.00 43.03  ? 521  ILE A N     1 
ATOM   3934  C  CA    . ILE A 1 521  ? 166.994 160.744 102.645 1.00 42.73  ? 521  ILE A CA    1 
ATOM   3935  C  C     . ILE A 1 521  ? 167.227 161.753 101.531 1.00 41.12  ? 521  ILE A C     1 
ATOM   3936  O  O     . ILE A 1 521  ? 166.771 162.899 101.606 1.00 43.39  ? 521  ILE A O     1 
ATOM   3937  C  CB    . ILE A 1 521  ? 168.226 160.612 103.559 1.00 44.02  ? 521  ILE A CB    1 
ATOM   3938  C  CG1   . ILE A 1 521  ? 167.839 159.960 104.884 1.00 42.91  ? 521  ILE A CG1   1 
ATOM   3939  C  CG2   . ILE A 1 521  ? 168.862 161.968 103.802 1.00 39.74  ? 521  ILE A CG2   1 
ATOM   3940  C  CD1   . ILE A 1 521  ? 166.968 160.827 105.744 1.00 41.25  ? 521  ILE A CD1   1 
ATOM   3941  N  N     . LYS A 1 522  ? 167.930 161.344 100.474 1.00 42.49  ? 522  LYS A N     1 
ATOM   3942  C  CA    . LYS A 1 522  ? 168.207 162.259 99.373  1.00 42.42  ? 522  LYS A CA    1 
ATOM   3943  C  C     . LYS A 1 522  ? 166.933 162.640 98.627  1.00 44.33  ? 522  LYS A C     1 
ATOM   3944  O  O     . LYS A 1 522  ? 166.781 163.789 98.197  1.00 44.26  ? 522  LYS A O     1 
ATOM   3945  C  CB    . LYS A 1 522  ? 169.221 161.627 98.423  1.00 46.82  ? 522  LYS A CB    1 
ATOM   3946  C  CG    . LYS A 1 522  ? 169.733 162.551 97.341  1.00 51.76  ? 522  LYS A CG    1 
ATOM   3947  C  CD    . LYS A 1 522  ? 170.838 161.883 96.544  1.00 57.19  ? 522  LYS A CD    1 
ATOM   3948  C  CE    . LYS A 1 522  ? 171.563 162.880 95.657  1.00 68.51  ? 522  LYS A CE    1 
ATOM   3949  N  NZ    . LYS A 1 522  ? 170.658 163.491 94.650  1.00 68.22  ? 522  LYS A NZ    1 
ATOM   3950  N  N     . ALA A 1 523  ? 166.012 161.689 98.452  1.00 48.19  ? 523  ALA A N     1 
ATOM   3951  C  CA    . ALA A 1 523  ? 164.797 161.968 97.692  1.00 43.38  ? 523  ALA A CA    1 
ATOM   3952  C  C     . ALA A 1 523  ? 163.854 162.906 98.435  1.00 42.97  ? 523  ALA A C     1 
ATOM   3953  O  O     . ALA A 1 523  ? 163.128 163.677 97.799  1.00 44.71  ? 523  ALA A O     1 
ATOM   3954  C  CB    . ALA A 1 523  ? 164.078 160.665 97.348  1.00 41.24  ? 523  ALA A CB    1 
ATOM   3955  N  N     . CYS A 1 524  ? 163.844 162.860 99.765  1.00 41.74  ? 524  CYS A N     1 
ATOM   3956  C  CA    . CYS A 1 524  ? 162.932 163.669 100.564 1.00 37.67  ? 524  CYS A CA    1 
ATOM   3957  C  C     . CYS A 1 524  ? 163.493 165.041 100.914 1.00 38.99  ? 524  CYS A C     1 
ATOM   3958  O  O     . CYS A 1 524  ? 162.892 165.743 101.733 1.00 43.48  ? 524  CYS A O     1 
ATOM   3959  C  CB    . CYS A 1 524  ? 162.551 162.927 101.848 1.00 37.36  ? 524  CYS A CB    1 
ATOM   3960  S  SG    . CYS A 1 524  ? 161.496 161.490 101.580 1.00 53.57  ? 524  CYS A SG    1 
ATOM   3961  N  N     . GLN A 1 525  ? 164.636 165.422 100.345 1.00 39.35  ? 525  GLN A N     1 
ATOM   3962  C  CA    . GLN A 1 525  ? 165.243 166.740 100.518 1.00 38.69  ? 525  GLN A CA    1 
ATOM   3963  C  C     . GLN A 1 525  ? 165.679 167.007 101.954 1.00 40.26  ? 525  GLN A C     1 
ATOM   3964  O  O     . GLN A 1 525  ? 165.840 168.167 102.345 1.00 44.10  ? 525  GLN A O     1 
ATOM   3965  C  CB    . GLN A 1 525  ? 164.303 167.857 100.046 1.00 38.53  ? 525  GLN A CB    1 
ATOM   3966  C  CG    . GLN A 1 525  ? 163.829 167.725 98.609  1.00 41.42  ? 525  GLN A CG    1 
ATOM   3967  C  CD    . GLN A 1 525  ? 164.962 167.722 97.607  1.00 48.46  ? 525  GLN A CD    1 
ATOM   3968  O  OE1   . GLN A 1 525  ? 165.888 168.527 97.696  1.00 51.72  ? 525  GLN A OE1   1 
ATOM   3969  N  NE2   . GLN A 1 525  ? 164.893 166.815 96.641  1.00 48.00  ? 525  GLN A NE2   1 
ATOM   3970  N  N     . LEU A 1 526  ? 165.869 165.961 102.756 1.00 37.32  ? 526  LEU A N     1 
ATOM   3971  C  CA    . LEU A 1 526  ? 166.303 166.117 104.138 1.00 40.95  ? 526  LEU A CA    1 
ATOM   3972  C  C     . LEU A 1 526  ? 167.809 166.278 104.281 1.00 44.51  ? 526  LEU A C     1 
ATOM   3973  O  O     . LEU A 1 526  ? 168.282 166.543 105.391 1.00 44.11  ? 526  LEU A O     1 
ATOM   3974  C  CB    . LEU A 1 526  ? 165.846 164.920 104.973 1.00 36.04  ? 526  LEU A CB    1 
ATOM   3975  C  CG    . LEU A 1 526  ? 164.381 164.869 105.393 1.00 31.21  ? 526  LEU A CG    1 
ATOM   3976  C  CD1   . LEU A 1 526  ? 164.076 163.532 106.028 1.00 31.63  ? 526  LEU A CD1   1 
ATOM   3977  C  CD2   . LEU A 1 526  ? 164.084 165.995 106.362 1.00 29.38  ? 526  LEU A CD2   1 
ATOM   3978  N  N     . GLU A 1 527  ? 168.570 166.121 103.198 1.00 49.89  ? 527  GLU A N     1 
ATOM   3979  C  CA    . GLU A 1 527  ? 170.024 166.096 103.310 1.00 52.26  ? 527  GLU A CA    1 
ATOM   3980  C  C     . GLU A 1 527  ? 170.591 167.453 103.713 1.00 51.88  ? 527  GLU A C     1 
ATOM   3981  O  O     . GLU A 1 527  ? 171.611 167.509 104.410 1.00 54.15  ? 527  GLU A O     1 
ATOM   3982  C  CB    . GLU A 1 527  ? 170.634 165.621 101.992 1.00 55.93  ? 527  GLU A CB    1 
ATOM   3983  C  CG    . GLU A 1 527  ? 172.145 165.491 102.005 1.00 65.14  ? 527  GLU A CG    1 
ATOM   3984  C  CD    . GLU A 1 527  ? 172.664 164.702 100.822 1.00 76.74  ? 527  GLU A CD    1 
ATOM   3985  O  OE1   . GLU A 1 527  ? 171.834 164.230 100.018 1.00 74.27  ? 527  GLU A OE1   1 
ATOM   3986  O  OE2   . GLU A 1 527  ? 173.899 164.556 100.694 1.00 79.99  ? 527  GLU A OE2   1 
ATOM   3987  N  N     . GLU A 1 528  ? 169.960 168.550 103.288 1.00 52.31  ? 528  GLU A N     1 
ATOM   3988  C  CA    . GLU A 1 528  ? 170.450 169.873 103.669 1.00 56.25  ? 528  GLU A CA    1 
ATOM   3989  C  C     . GLU A 1 528  ? 170.170 170.180 105.135 1.00 55.79  ? 528  GLU A C     1 
ATOM   3990  O  O     . GLU A 1 528  ? 171.036 170.711 105.838 1.00 55.63  ? 528  GLU A O     1 
ATOM   3991  C  CB    . GLU A 1 528  ? 169.831 170.948 102.776 1.00 56.39  ? 528  GLU A CB    1 
ATOM   3992  C  CG    . GLU A 1 528  ? 169.958 172.353 103.342 1.00 57.18  ? 528  GLU A CG    1 
ATOM   3993  C  CD    . GLU A 1 528  ? 170.294 173.383 102.285 1.00 69.57  ? 528  GLU A CD    1 
ATOM   3994  O  OE1   . GLU A 1 528  ? 171.392 173.293 101.698 1.00 77.15  ? 528  GLU A OE1   1 
ATOM   3995  O  OE2   . GLU A 1 528  ? 169.463 174.283 102.043 1.00 63.78  ? 528  GLU A OE2   1 
ATOM   3996  N  N     . ASP A 1 529  ? 168.968 169.854 105.615 1.00 51.30  ? 529  ASP A N     1 
ATOM   3997  C  CA    . ASP A 1 529  ? 168.599 170.202 106.984 1.00 47.91  ? 529  ASP A CA    1 
ATOM   3998  C  C     . ASP A 1 529  ? 169.411 169.411 108.000 1.00 49.77  ? 529  ASP A C     1 
ATOM   3999  O  O     . ASP A 1 529  ? 169.745 169.929 109.072 1.00 54.09  ? 529  ASP A O     1 
ATOM   4000  C  CB    . ASP A 1 529  ? 167.105 169.974 107.198 1.00 46.04  ? 529  ASP A CB    1 
ATOM   4001  C  CG    . ASP A 1 529  ? 166.255 170.745 106.215 1.00 49.81  ? 529  ASP A CG    1 
ATOM   4002  O  OD1   . ASP A 1 529  ? 166.244 170.378 105.023 1.00 54.34  ? 529  ASP A OD1   1 
ATOM   4003  O  OD2   . ASP A 1 529  ? 165.598 171.720 106.632 1.00 46.81  ? 529  ASP A OD2   1 
ATOM   4004  N  N     . ILE A 1 530  ? 169.729 168.155 107.688 1.00 48.61  ? 530  ILE A N     1 
ATOM   4005  C  CA    . ILE A 1 530  ? 170.526 167.344 108.600 1.00 52.06  ? 530  ILE A CA    1 
ATOM   4006  C  C     . ILE A 1 530  ? 171.931 167.915 108.737 1.00 55.15  ? 530  ILE A C     1 
ATOM   4007  O  O     . ILE A 1 530  ? 172.528 167.863 109.820 1.00 59.88  ? 530  ILE A O     1 
ATOM   4008  C  CB    . ILE A 1 530  ? 170.542 165.880 108.120 1.00 53.08  ? 530  ILE A CB    1 
ATOM   4009  C  CG1   . ILE A 1 530  ? 169.170 165.239 108.328 1.00 47.09  ? 530  ILE A CG1   1 
ATOM   4010  C  CG2   . ILE A 1 530  ? 171.605 165.079 108.842 1.00 55.08  ? 530  ILE A CG2   1 
ATOM   4011  C  CD1   . ILE A 1 530  ? 168.972 163.967 107.542 1.00 45.73  ? 530  ILE A CD1   1 
ATOM   4012  N  N     . SER A 1 531  ? 172.473 168.489 107.662 1.00 52.85  ? 531  SER A N     1 
ATOM   4013  C  CA    . SER A 1 531  ? 173.818 169.049 107.717 1.00 57.19  ? 531  SER A CA    1 
ATOM   4014  C  C     . SER A 1 531  ? 173.919 170.202 108.710 1.00 60.01  ? 531  SER A C     1 
ATOM   4015  O  O     . SER A 1 531  ? 174.989 170.422 109.288 1.00 63.13  ? 531  SER A O     1 
ATOM   4016  C  CB    . SER A 1 531  ? 174.245 169.516 106.327 1.00 54.53  ? 531  SER A CB    1 
ATOM   4017  O  OG    . SER A 1 531  ? 173.796 170.836 106.080 1.00 54.01  ? 531  SER A OG    1 
ATOM   4018  N  N     . LYS A 1 532  ? 172.829 170.943 108.926 1.00 58.09  ? 532  LYS A N     1 
ATOM   4019  C  CA    . LYS A 1 532  ? 172.867 172.061 109.866 1.00 55.96  ? 532  LYS A CA    1 
ATOM   4020  C  C     . LYS A 1 532  ? 173.057 171.598 111.304 1.00 56.99  ? 532  LYS A C     1 
ATOM   4021  O  O     . LYS A 1 532  ? 173.672 172.311 112.104 1.00 58.46  ? 532  LYS A O     1 
ATOM   4022  C  CB    . LYS A 1 532  ? 171.592 172.897 109.757 1.00 53.19  ? 532  LYS A CB    1 
ATOM   4023  C  CG    . LYS A 1 532  ? 171.711 174.110 108.854 1.00 52.08  ? 532  LYS A CG    1 
ATOM   4024  C  CD    . LYS A 1 532  ? 171.685 173.749 107.386 1.00 53.53  ? 532  LYS A CD    1 
ATOM   4025  C  CE    . LYS A 1 532  ? 171.743 175.007 106.542 1.00 54.94  ? 532  LYS A CE    1 
ATOM   4026  N  NZ    . LYS A 1 532  ? 171.664 174.726 105.088 1.00 58.63  ? 532  LYS A NZ    1 
ATOM   4027  N  N     . PHE A 1 533  ? 172.539 170.426 111.654 1.00 57.31  ? 533  PHE A N     1 
ATOM   4028  C  CA    . PHE A 1 533  ? 172.638 169.941 113.022 1.00 61.67  ? 533  PHE A CA    1 
ATOM   4029  C  C     . PHE A 1 533  ? 174.072 169.553 113.348 1.00 68.81  ? 533  PHE A C     1 
ATOM   4030  O  O     . PHE A 1 533  ? 174.763 168.930 112.538 1.00 67.58  ? 533  PHE A O     1 
ATOM   4031  C  CB    . PHE A 1 533  ? 171.711 168.747 113.235 1.00 61.91  ? 533  PHE A CB    1 
ATOM   4032  C  CG    . PHE A 1 533  ? 170.276 169.032 112.914 1.00 58.77  ? 533  PHE A CG    1 
ATOM   4033  C  CD1   . PHE A 1 533  ? 169.693 170.229 113.295 1.00 57.47  ? 533  PHE A CD1   1 
ATOM   4034  C  CD2   . PHE A 1 533  ? 169.508 168.107 112.232 1.00 57.04  ? 533  PHE A CD2   1 
ATOM   4035  C  CE1   . PHE A 1 533  ? 168.375 170.496 113.002 1.00 52.82  ? 533  PHE A CE1   1 
ATOM   4036  C  CE2   . PHE A 1 533  ? 168.186 168.368 111.936 1.00 54.92  ? 533  PHE A CE2   1 
ATOM   4037  C  CZ    . PHE A 1 533  ? 167.619 169.565 112.322 1.00 52.29  ? 533  PHE A CZ    1 
ATOM   4038  N  N     . ALA A 1 534  ? 174.517 169.931 114.547 1.00 74.05  ? 534  ALA A N     1 
ATOM   4039  C  CA    . ALA A 1 534  ? 175.884 169.628 114.959 1.00 78.68  ? 534  ALA A CA    1 
ATOM   4040  C  C     . ALA A 1 534  ? 176.100 168.126 115.092 1.00 76.52  ? 534  ALA A C     1 
ATOM   4041  O  O     . ALA A 1 534  ? 177.197 167.623 114.826 1.00 73.44  ? 534  ALA A O     1 
ATOM   4042  C  CB    . ALA A 1 534  ? 176.205 170.337 116.274 1.00 75.32  ? 534  ALA A CB    1 
ATOM   4043  N  N     . GLU A 1 535  ? 175.065 167.395 115.500 1.00 73.92  ? 535  GLU A N     1 
ATOM   4044  C  CA    . GLU A 1 535  ? 175.155 165.957 115.710 1.00 70.17  ? 535  GLU A CA    1 
ATOM   4045  C  C     . GLU A 1 535  ? 174.663 165.166 114.500 1.00 67.72  ? 535  GLU A C     1 
ATOM   4046  O  O     . GLU A 1 535  ? 174.525 163.942 114.581 1.00 66.15  ? 535  GLU A O     1 
ATOM   4047  C  CB    . GLU A 1 535  ? 174.379 165.572 116.972 1.00 68.94  ? 535  GLU A CB    1 
ATOM   4048  C  CG    . GLU A 1 535  ? 174.773 164.236 117.578 1.00 71.72  ? 535  GLU A CG    1 
ATOM   4049  C  CD    . GLU A 1 535  ? 174.516 164.176 119.069 1.00 78.22  ? 535  GLU A CD    1 
ATOM   4050  O  OE1   . GLU A 1 535  ? 173.350 164.348 119.482 1.00 76.92  ? 535  GLU A OE1   1 
ATOM   4051  O  OE2   . GLU A 1 535  ? 175.483 163.954 119.828 1.00 80.16  ? 535  GLU A OE2   1 
ATOM   4052  N  N     . LYS A 1 536  ? 174.406 165.845 113.382 1.00 68.08  ? 536  LYS A N     1 
ATOM   4053  C  CA    . LYS A 1 536  ? 174.052 165.231 112.097 1.00 63.82  ? 536  LYS A CA    1 
ATOM   4054  C  C     . LYS A 1 536  ? 172.768 164.425 112.260 1.00 63.21  ? 536  LYS A C     1 
ATOM   4055  O  O     . LYS A 1 536  ? 171.747 165.004 112.669 1.00 62.45  ? 536  LYS A O     1 
ATOM   4056  C  CB    . LYS A 1 536  ? 175.262 164.443 111.591 1.00 67.61  ? 536  LYS A CB    1 
ATOM   4057  C  CG    . LYS A 1 536  ? 176.517 165.270 111.401 1.00 69.96  ? 536  LYS A CG    1 
ATOM   4058  C  CD    . LYS A 1 536  ? 176.249 166.471 110.521 1.00 70.38  ? 536  LYS A CD    1 
ATOM   4059  C  CE    . LYS A 1 536  ? 177.539 167.169 110.143 1.00 75.18  ? 536  LYS A CE    1 
ATOM   4060  N  NZ    . LYS A 1 536  ? 177.283 168.497 109.525 1.00 74.17  ? 536  LYS A NZ    1 
ATOM   4061  N  N     . ASP A 1 537  ? 172.762 163.122 111.977 1.00 62.51  ? 537  ASP A N     1 
ATOM   4062  C  CA    . ASP A 1 537  ? 171.541 162.327 111.956 1.00 55.31  ? 537  ASP A CA    1 
ATOM   4063  C  C     . ASP A 1 537  ? 171.163 161.757 113.314 1.00 56.32  ? 537  ASP A C     1 
ATOM   4064  O  O     . ASP A 1 537  ? 170.063 161.214 113.452 1.00 53.17  ? 537  ASP A O     1 
ATOM   4065  C  CB    . ASP A 1 537  ? 171.685 161.180 110.955 1.00 53.90  ? 537  ASP A CB    1 
ATOM   4066  C  CG    . ASP A 1 537  ? 170.457 161.004 110.096 1.00 56.80  ? 537  ASP A CG    1 
ATOM   4067  O  OD1   . ASP A 1 537  ? 169.345 161.248 110.601 1.00 58.95  ? 537  ASP A OD1   1 
ATOM   4068  O  OD2   . ASP A 1 537  ? 170.603 160.621 108.917 1.00 60.37  ? 537  ASP A OD2   1 
ATOM   4069  N  N     . ASN A 1 538  ? 172.039 161.855 114.309 1.00 60.29  ? 538  ASN A N     1 
ATOM   4070  C  CA    . ASN A 1 538  ? 171.818 161.236 115.606 1.00 56.18  ? 538  ASN A CA    1 
ATOM   4071  C  C     . ASN A 1 538  ? 171.320 162.221 116.652 1.00 55.52  ? 538  ASN A C     1 
ATOM   4072  O  O     . ASN A 1 538  ? 171.400 161.929 117.848 1.00 54.78  ? 538  ASN A O     1 
ATOM   4073  C  CB    . ASN A 1 538  ? 173.101 160.563 116.091 1.00 60.16  ? 538  ASN A CB    1 
ATOM   4074  C  CG    . ASN A 1 538  ? 173.519 159.408 115.206 1.00 65.35  ? 538  ASN A CG    1 
ATOM   4075  O  OD1   . ASN A 1 538  ? 172.892 158.350 115.205 1.00 60.28  ? 538  ASN A OD1   1 
ATOM   4076  N  ND2   . ASN A 1 538  ? 174.582 159.610 114.440 1.00 64.87  ? 538  ASN A ND2   1 
ATOM   4077  N  N     . ILE A 1 539  ? 170.826 163.386 116.234 1.00 56.59  ? 539  ILE A N     1 
ATOM   4078  C  CA    . ILE A 1 539  ? 170.262 164.338 117.182 1.00 57.38  ? 539  ILE A CA    1 
ATOM   4079  C  C     . ILE A 1 539  ? 169.015 163.733 117.810 1.00 52.31  ? 539  ILE A C     1 
ATOM   4080  O  O     . ILE A 1 539  ? 168.137 163.209 117.114 1.00 49.65  ? 539  ILE A O     1 
ATOM   4081  C  CB    . ILE A 1 539  ? 169.978 165.680 116.497 1.00 57.61  ? 539  ILE A CB    1 
ATOM   4082  C  CG1   . ILE A 1 539  ? 169.525 166.720 117.521 1.00 57.27  ? 539  ILE A CG1   1 
ATOM   4083  C  CG2   . ILE A 1 539  ? 168.978 165.524 115.365 1.00 55.63  ? 539  ILE A CG2   1 
ATOM   4084  C  CD1   . ILE A 1 539  ? 169.497 168.128 116.982 1.00 58.73  ? 539  ILE A CD1   1 
ATOM   4085  N  N     . VAL A 1 540  ? 168.947 163.770 119.136 1.00 48.30  ? 540  VAL A N     1 
ATOM   4086  C  CA    . VAL A 1 540  ? 167.873 163.105 119.865 1.00 46.01  ? 540  VAL A CA    1 
ATOM   4087  C  C     . VAL A 1 540  ? 166.631 163.986 119.857 1.00 48.79  ? 540  VAL A C     1 
ATOM   4088  O  O     . VAL A 1 540  ? 166.685 165.162 120.236 1.00 52.28  ? 540  VAL A O     1 
ATOM   4089  C  CB    . VAL A 1 540  ? 168.313 162.777 121.299 1.00 42.95  ? 540  VAL A CB    1 
ATOM   4090  C  CG1   . VAL A 1 540  ? 167.178 162.121 122.060 1.00 44.98  ? 540  VAL A CG1   1 
ATOM   4091  C  CG2   . VAL A 1 540  ? 169.534 161.877 121.280 1.00 44.70  ? 540  VAL A CG2   1 
ATOM   4092  N  N     . LEU A 1 541  ? 165.510 163.419 119.424 1.00 46.98  ? 541  LEU A N     1 
ATOM   4093  C  CA    . LEU A 1 541  ? 164.237 164.120 119.383 1.00 42.60  ? 541  LEU A CA    1 
ATOM   4094  C  C     . LEU A 1 541  ? 163.380 163.720 120.575 1.00 44.94  ? 541  LEU A C     1 
ATOM   4095  O  O     . LEU A 1 541  ? 163.402 162.566 121.011 1.00 42.58  ? 541  LEU A O     1 
ATOM   4096  C  CB    . LEU A 1 541  ? 163.485 163.819 118.086 1.00 38.43  ? 541  LEU A CB    1 
ATOM   4097  C  CG    . LEU A 1 541  ? 164.233 164.067 116.779 1.00 38.85  ? 541  LEU A CG    1 
ATOM   4098  C  CD1   . LEU A 1 541  ? 163.417 163.570 115.601 1.00 36.73  ? 541  LEU A CD1   1 
ATOM   4099  C  CD2   . LEU A 1 541  ? 164.562 165.539 116.628 1.00 41.77  ? 541  LEU A CD2   1 
ATOM   4100  N  N     . GLY A 1 542  ? 162.631 164.683 121.103 1.00 48.80  ? 542  GLY A N     1 
ATOM   4101  C  CA    . GLY A 1 542  ? 161.701 164.417 122.177 1.00 41.92  ? 542  GLY A CA    1 
ATOM   4102  C  C     . GLY A 1 542  ? 160.358 163.938 121.668 1.00 45.28  ? 542  GLY A C     1 
ATOM   4103  O  O     . GLY A 1 542  ? 160.128 163.766 120.472 1.00 46.86  ? 542  GLY A O     1 
ATOM   4104  N  N     . GLU A 1 543  ? 159.449 163.717 122.613 1.00 48.56  ? 543  GLU A N     1 
ATOM   4105  C  CA    . GLU A 1 543  ? 158.095 163.298 122.273 1.00 48.09  ? 543  GLU A CA    1 
ATOM   4106  C  C     . GLU A 1 543  ? 157.360 164.452 121.602 1.00 50.24  ? 543  GLU A C     1 
ATOM   4107  O  O     . GLU A 1 543  ? 157.066 165.468 122.242 1.00 53.44  ? 543  GLU A O     1 
ATOM   4108  C  CB    . GLU A 1 543  ? 157.360 162.836 123.530 1.00 48.25  ? 543  GLU A CB    1 
ATOM   4109  C  CG    . GLU A 1 543  ? 156.256 161.812 123.300 1.00 48.80  ? 543  GLU A CG    1 
ATOM   4110  C  CD    . GLU A 1 543  ? 155.051 162.386 122.580 1.00 57.10  ? 543  GLU A CD    1 
ATOM   4111  O  OE1   . GLU A 1 543  ? 154.498 163.397 123.057 1.00 63.08  ? 543  GLU A OE1   1 
ATOM   4112  O  OE2   . GLU A 1 543  ? 154.656 161.825 121.536 1.00 52.60  ? 543  GLU A OE2   1 
ATOM   4113  N  N     . GLY A 1 544  ? 157.059 164.295 120.315 1.00 44.01  ? 544  GLY A N     1 
ATOM   4114  C  CA    . GLY A 1 544  ? 156.416 165.331 119.540 1.00 42.94  ? 544  GLY A CA    1 
ATOM   4115  C  C     . GLY A 1 544  ? 157.336 166.153 118.664 1.00 45.99  ? 544  GLY A C     1 
ATOM   4116  O  O     . GLY A 1 544  ? 156.845 166.857 117.773 1.00 45.15  ? 544  GLY A O     1 
ATOM   4117  N  N     . GLY A 1 545  ? 158.645 166.095 118.887 1.00 46.63  ? 545  GLY A N     1 
ATOM   4118  C  CA    . GLY A 1 545  ? 159.587 166.758 117.997 1.00 40.65  ? 545  GLY A CA    1 
ATOM   4119  C  C     . GLY A 1 545  ? 159.436 168.261 117.917 1.00 41.35  ? 545  GLY A C     1 
ATOM   4120  O  O     . GLY A 1 545  ? 159.511 168.829 116.821 1.00 41.75  ? 545  GLY A O     1 
ATOM   4121  N  N     . ILE A 1 546  ? 159.224 168.925 119.056 1.00 46.66  ? 546  ILE A N     1 
ATOM   4122  C  CA    . ILE A 1 546  ? 159.053 170.375 119.063 1.00 45.88  ? 546  ILE A CA    1 
ATOM   4123  C  C     . ILE A 1 546  ? 160.327 171.100 118.651 1.00 42.71  ? 546  ILE A C     1 
ATOM   4124  O  O     . ILE A 1 546  ? 160.277 172.280 118.289 1.00 40.53  ? 546  ILE A O     1 
ATOM   4125  C  CB    . ILE A 1 546  ? 158.568 170.862 120.446 1.00 48.06  ? 546  ILE A CB    1 
ATOM   4126  C  CG1   . ILE A 1 546  ? 159.690 170.783 121.486 1.00 49.77  ? 546  ILE A CG1   1 
ATOM   4127  C  CG2   . ILE A 1 546  ? 157.353 170.061 120.892 1.00 50.09  ? 546  ILE A CG2   1 
ATOM   4128  C  CD1   . ILE A 1 546  ? 159.794 169.448 122.197 1.00 52.02  ? 546  ILE A CD1   1 
ATOM   4129  N  N     . THR A 1 547  ? 161.475 170.421 118.704 1.00 42.50  ? 547  THR A N     1 
ATOM   4130  C  CA    . THR A 1 547  ? 162.730 171.010 118.251 1.00 38.79  ? 547  THR A CA    1 
ATOM   4131  C  C     . THR A 1 547  ? 162.720 171.298 116.755 1.00 40.72  ? 547  THR A C     1 
ATOM   4132  O  O     . THR A 1 547  ? 163.447 172.185 116.297 1.00 45.20  ? 547  THR A O     1 
ATOM   4133  C  CB    . THR A 1 547  ? 163.890 170.074 118.598 1.00 40.45  ? 547  THR A CB    1 
ATOM   4134  O  OG1   . THR A 1 547  ? 163.838 169.748 119.992 1.00 47.49  ? 547  THR A OG1   1 
ATOM   4135  C  CG2   . THR A 1 547  ? 165.229 170.724 118.297 1.00 40.14  ? 547  THR A CG2   1 
ATOM   4136  N  N     . LEU A 1 548  ? 161.903 170.587 115.991 1.00 39.96  ? 548  LEU A N     1 
ATOM   4137  C  CA    . LEU A 1 548  ? 161.871 170.708 114.545 1.00 34.75  ? 548  LEU A CA    1 
ATOM   4138  C  C     . LEU A 1 548  ? 160.840 171.744 114.104 1.00 36.64  ? 548  LEU A C     1 
ATOM   4139  O  O     . LEU A 1 548  ? 160.036 172.240 114.894 1.00 42.17  ? 548  LEU A O     1 
ATOM   4140  C  CB    . LEU A 1 548  ? 161.558 169.355 113.916 1.00 34.85  ? 548  LEU A CB    1 
ATOM   4141  C  CG    . LEU A 1 548  ? 162.471 168.206 114.332 1.00 35.62  ? 548  LEU A CG    1 
ATOM   4142  C  CD1   . LEU A 1 548  ? 161.928 166.900 113.802 1.00 28.88  ? 548  LEU A CD1   1 
ATOM   4143  C  CD2   . LEU A 1 548  ? 163.886 168.448 113.839 1.00 32.14  ? 548  LEU A CD2   1 
ATOM   4144  N  N     . SER A 1 549  ? 160.879 172.071 112.818 1.00 35.08  ? 549  SER A N     1 
ATOM   4145  C  CA    . SER A 1 549  ? 159.868 172.914 112.201 1.00 32.86  ? 549  SER A CA    1 
ATOM   4146  C  C     . SER A 1 549  ? 158.752 172.046 111.620 1.00 33.15  ? 549  SER A C     1 
ATOM   4147  O  O     . SER A 1 549  ? 158.821 170.817 111.624 1.00 35.33  ? 549  SER A O     1 
ATOM   4148  C  CB    . SER A 1 549  ? 160.501 173.802 111.131 1.00 29.28  ? 549  SER A CB    1 
ATOM   4149  O  OG    . SER A 1 549  ? 160.738 173.086 109.937 1.00 33.60  ? 549  SER A OG    1 
ATOM   4150  N  N     . GLY A 1 550  ? 157.698 172.704 111.130 1.00 30.52  ? 550  GLY A N     1 
ATOM   4151  C  CA    . GLY A 1 550  ? 156.552 171.963 110.624 1.00 30.19  ? 550  GLY A CA    1 
ATOM   4152  C  C     . GLY A 1 550  ? 156.870 171.144 109.388 1.00 31.96  ? 550  GLY A C     1 
ATOM   4153  O  O     . GLY A 1 550  ? 156.500 169.968 109.294 1.00 36.88  ? 550  GLY A O     1 
ATOM   4154  N  N     . GLY A 1 551  ? 157.584 171.742 108.433 1.00 31.75  ? 551  GLY A N     1 
ATOM   4155  C  CA    . GLY A 1 551  ? 157.957 171.008 107.240 1.00 27.85  ? 551  GLY A CA    1 
ATOM   4156  C  C     . GLY A 1 551  ? 159.018 169.962 107.470 1.00 29.24  ? 551  GLY A C     1 
ATOM   4157  O  O     . GLY A 1 551  ? 159.020 168.938 106.781 1.00 31.45  ? 551  GLY A O     1 
ATOM   4158  N  N     . GLN A 1 552  ? 159.898 170.174 108.450 1.00 28.73  ? 552  GLN A N     1 
ATOM   4159  C  CA    . GLN A 1 552  ? 160.865 169.142 108.804 1.00 26.16  ? 552  GLN A CA    1 
ATOM   4160  C  C     . GLN A 1 552  ? 160.171 167.913 109.374 1.00 27.43  ? 552  GLN A C     1 
ATOM   4161  O  O     . GLN A 1 552  ? 160.517 166.779 109.021 1.00 29.89  ? 552  GLN A O     1 
ATOM   4162  C  CB    . GLN A 1 552  ? 161.884 169.698 109.795 1.00 25.80  ? 552  GLN A CB    1 
ATOM   4163  C  CG    . GLN A 1 552  ? 162.948 170.560 109.150 1.00 30.26  ? 552  GLN A CG    1 
ATOM   4164  C  CD    . GLN A 1 552  ? 163.911 171.152 110.153 1.00 32.57  ? 552  GLN A CD    1 
ATOM   4165  O  OE1   . GLN A 1 552  ? 163.777 170.943 111.355 1.00 37.54  ? 552  GLN A OE1   1 
ATOM   4166  N  NE2   . GLN A 1 552  ? 164.879 171.916 109.663 1.00 30.33  ? 552  GLN A NE2   1 
ATOM   4167  N  N     . ARG A 1 553  ? 159.182 168.115 110.248 1.00 25.67  ? 553  ARG A N     1 
ATOM   4168  C  CA    . ARG A 1 553  ? 158.406 166.988 110.753 1.00 25.27  ? 553  ARG A CA    1 
ATOM   4169  C  C     . ARG A 1 553  ? 157.628 166.310 109.633 1.00 26.77  ? 553  ARG A C     1 
ATOM   4170  O  O     . ARG A 1 553  ? 157.548 165.075 109.585 1.00 29.01  ? 553  ARG A O     1 
ATOM   4171  C  CB    . ARG A 1 553  ? 157.458 167.443 111.862 1.00 26.93  ? 553  ARG A CB    1 
ATOM   4172  C  CG    . ARG A 1 553  ? 158.146 167.867 113.147 1.00 30.25  ? 553  ARG A CG    1 
ATOM   4173  C  CD    . ARG A 1 553  ? 157.144 168.101 114.271 1.00 30.10  ? 553  ARG A CD    1 
ATOM   4174  N  NE    . ARG A 1 553  ? 156.336 169.298 114.082 1.00 37.29  ? 553  ARG A NE    1 
ATOM   4175  C  CZ    . ARG A 1 553  ? 156.585 170.470 114.652 1.00 41.65  ? 553  ARG A CZ    1 
ATOM   4176  N  NH1   . ARG A 1 553  ? 157.616 170.640 115.462 1.00 39.63  ? 553  ARG A NH1   1 
ATOM   4177  N  NH2   . ARG A 1 553  ? 155.777 171.497 114.406 1.00 44.19  ? 553  ARG A NH2   1 
ATOM   4178  N  N     . ALA A 1 554  ? 157.055 167.099 108.719 1.00 24.44  ? 554  ALA A N     1 
ATOM   4179  C  CA    . ALA A 1 554  ? 156.312 166.512 107.607 1.00 24.37  ? 554  ALA A CA    1 
ATOM   4180  C  C     . ALA A 1 554  ? 157.211 165.648 106.731 1.00 28.48  ? 554  ALA A C     1 
ATOM   4181  O  O     . ALA A 1 554  ? 156.824 164.544 106.327 1.00 29.55  ? 554  ALA A O     1 
ATOM   4182  C  CB    . ALA A 1 554  ? 155.655 167.615 106.778 1.00 24.53  ? 554  ALA A CB    1 
ATOM   4183  N  N     . ARG A 1 555  ? 158.425 166.121 106.444 1.00 27.10  ? 555  ARG A N     1 
ATOM   4184  C  CA    . ARG A 1 555  ? 159.340 165.353 105.609 1.00 24.81  ? 555  ARG A CA    1 
ATOM   4185  C  C     . ARG A 1 555  ? 159.919 164.146 106.332 1.00 24.57  ? 555  ARG A C     1 
ATOM   4186  O  O     . ARG A 1 555  ? 160.174 163.124 105.693 1.00 30.37  ? 555  ARG A O     1 
ATOM   4187  C  CB    . ARG A 1 555  ? 160.459 166.250 105.083 1.00 25.52  ? 555  ARG A CB    1 
ATOM   4188  C  CG    . ARG A 1 555  ? 159.982 167.252 104.053 1.00 26.24  ? 555  ARG A CG    1 
ATOM   4189  C  CD    . ARG A 1 555  ? 161.086 168.179 103.592 1.00 27.08  ? 555  ARG A CD    1 
ATOM   4190  N  NE    . ARG A 1 555  ? 161.493 169.104 104.640 1.00 32.75  ? 555  ARG A NE    1 
ATOM   4191  C  CZ    . ARG A 1 555  ? 162.703 169.634 104.743 1.00 35.63  ? 555  ARG A CZ    1 
ATOM   4192  N  NH1   . ARG A 1 555  ? 163.663 169.335 103.886 1.00 39.54  ? 555  ARG A NH1   1 
ATOM   4193  N  NH2   . ARG A 1 555  ? 162.950 170.498 105.722 1.00 35.50  ? 555  ARG A NH2   1 
ATOM   4194  N  N     . ILE A 1 556  ? 160.111 164.216 107.650 1.00 21.87  ? 556  ILE A N     1 
ATOM   4195  C  CA    . ILE A 1 556  ? 160.542 163.022 108.371 1.00 20.95  ? 556  ILE A CA    1 
ATOM   4196  C  C     . ILE A 1 556  ? 159.441 161.967 108.368 1.00 24.68  ? 556  ILE A C     1 
ATOM   4197  O  O     . ILE A 1 556  ? 159.709 160.770 108.205 1.00 28.29  ? 556  ILE A O     1 
ATOM   4198  C  CB    . ILE A 1 556  ? 160.989 163.384 109.797 1.00 25.90  ? 556  ILE A CB    1 
ATOM   4199  C  CG1   . ILE A 1 556  ? 162.319 164.136 109.748 1.00 25.75  ? 556  ILE A CG1   1 
ATOM   4200  C  CG2   . ILE A 1 556  ? 161.112 162.138 110.656 1.00 27.13  ? 556  ILE A CG2   1 
ATOM   4201  C  CD1   . ILE A 1 556  ? 162.674 164.833 111.023 1.00 23.23  ? 556  ILE A CD1   1 
ATOM   4202  N  N     . SER A 1 557  ? 158.183 162.388 108.523 1.00 24.87  ? 557  SER A N     1 
ATOM   4203  C  CA    . SER A 1 557  ? 157.078 161.436 108.431 1.00 26.19  ? 557  SER A CA    1 
ATOM   4204  C  C     . SER A 1 557  ? 156.984 160.827 107.034 1.00 27.39  ? 557  SER A C     1 
ATOM   4205  O  O     . SER A 1 557  ? 156.752 159.619 106.888 1.00 29.66  ? 557  SER A O     1 
ATOM   4206  C  CB    . SER A 1 557  ? 155.769 162.125 108.811 1.00 30.48  ? 557  SER A CB    1 
ATOM   4207  O  OG    . SER A 1 557  ? 154.686 161.212 108.809 1.00 38.94  ? 557  SER A OG    1 
ATOM   4208  N  N     . LEU A 1 558  ? 157.180 161.642 105.995 1.00 25.62  ? 558  LEU A N     1 
ATOM   4209  C  CA    . LEU A 1 558  ? 157.179 161.115 104.633 1.00 23.62  ? 558  LEU A CA    1 
ATOM   4210  C  C     . LEU A 1 558  ? 158.325 160.135 104.408 1.00 26.84  ? 558  LEU A C     1 
ATOM   4211  O  O     . LEU A 1 558  ? 158.150 159.116 103.732 1.00 32.45  ? 558  LEU A O     1 
ATOM   4212  C  CB    . LEU A 1 558  ? 157.253 162.260 103.626 1.00 26.52  ? 558  LEU A CB    1 
ATOM   4213  C  CG    . LEU A 1 558  ? 157.142 161.858 102.155 1.00 26.41  ? 558  LEU A CG    1 
ATOM   4214  C  CD1   . LEU A 1 558  ? 155.805 161.210 101.869 1.00 24.79  ? 558  LEU A CD1   1 
ATOM   4215  C  CD2   . LEU A 1 558  ? 157.367 163.052 101.248 1.00 26.48  ? 558  LEU A CD2   1 
ATOM   4216  N  N     . ALA A 1 559  ? 159.508 160.430 104.949 1.00 26.13  ? 559  ALA A N     1 
ATOM   4217  C  CA    . ALA A 1 559  ? 160.631 159.508 104.820 1.00 27.68  ? 559  ALA A CA    1 
ATOM   4218  C  C     . ALA A 1 559  ? 160.349 158.191 105.531 1.00 27.16  ? 559  ALA A C     1 
ATOM   4219  O  O     . ALA A 1 559  ? 160.701 157.118 105.026 1.00 26.61  ? 559  ALA A O     1 
ATOM   4220  C  CB    . ALA A 1 559  ? 161.903 160.151 105.369 1.00 24.85  ? 559  ALA A CB    1 
ATOM   4221  N  N     . ARG A 1 560  ? 159.722 158.250 106.709 1.00 26.77  ? 560  ARG A N     1 
ATOM   4222  C  CA    . ARG A 1 560  ? 159.351 157.021 107.402 1.00 24.94  ? 560  ARG A CA    1 
ATOM   4223  C  C     . ARG A 1 560  ? 158.380 156.203 106.562 1.00 27.82  ? 560  ARG A C     1 
ATOM   4224  O  O     . ARG A 1 560  ? 158.496 154.976 106.474 1.00 28.88  ? 560  ARG A O     1 
ATOM   4225  C  CB    . ARG A 1 560  ? 158.744 157.331 108.773 1.00 22.96  ? 560  ARG A CB    1 
ATOM   4226  C  CG    . ARG A 1 560  ? 158.207 156.088 109.474 1.00 22.64  ? 560  ARG A CG    1 
ATOM   4227  C  CD    . ARG A 1 560  ? 157.662 156.345 110.871 1.00 25.45  ? 560  ARG A CD    1 
ATOM   4228  N  NE    . ARG A 1 560  ? 156.689 157.429 110.932 1.00 28.19  ? 560  ARG A NE    1 
ATOM   4229  C  CZ    . ARG A 1 560  ? 156.826 158.518 111.676 1.00 26.39  ? 560  ARG A CZ    1 
ATOM   4230  N  NH1   . ARG A 1 560  ? 157.887 158.704 112.441 1.00 25.97  ? 560  ARG A NH1   1 
ATOM   4231  N  NH2   . ARG A 1 560  ? 155.869 159.439 111.659 1.00 26.42  ? 560  ARG A NH2   1 
ATOM   4232  N  N     . ALA A 1 561  ? 157.405 156.871 105.941 1.00 29.02  ? 561  ALA A N     1 
ATOM   4233  C  CA    . ALA A 1 561  ? 156.458 156.160 105.087 1.00 27.26  ? 561  ALA A CA    1 
ATOM   4234  C  C     . ALA A 1 561  ? 157.150 155.520 103.888 1.00 31.31  ? 561  ALA A C     1 
ATOM   4235  O  O     . ALA A 1 561  ? 156.873 154.366 103.547 1.00 33.83  ? 561  ALA A O     1 
ATOM   4236  C  CB    . ALA A 1 561  ? 155.356 157.108 104.619 1.00 28.89  ? 561  ALA A CB    1 
ATOM   4237  N  N     . VAL A 1 562  ? 158.051 156.256 103.233 1.00 31.94  ? 562  VAL A N     1 
ATOM   4238  C  CA    . VAL A 1 562  ? 158.672 155.761 102.006 1.00 31.43  ? 562  VAL A CA    1 
ATOM   4239  C  C     . VAL A 1 562  ? 159.638 154.617 102.300 1.00 34.47  ? 562  VAL A C     1 
ATOM   4240  O  O     . VAL A 1 562  ? 159.739 153.659 101.525 1.00 38.77  ? 562  VAL A O     1 
ATOM   4241  C  CB    . VAL A 1 562  ? 159.368 156.913 101.260 1.00 33.66  ? 562  VAL A CB    1 
ATOM   4242  C  CG1   . VAL A 1 562  ? 160.171 156.380 100.094 1.00 35.35  ? 562  VAL A CG1   1 
ATOM   4243  C  CG2   . VAL A 1 562  ? 158.339 157.911 100.770 1.00 38.90  ? 562  VAL A CG2   1 
ATOM   4244  N  N     . TYR A 1 563  ? 160.365 154.697 103.417 1.00 35.22  ? 563  TYR A N     1 
ATOM   4245  C  CA    . TYR A 1 563  ? 161.356 153.673 103.737 1.00 34.56  ? 563  TYR A CA    1 
ATOM   4246  C  C     . TYR A 1 563  ? 160.723 152.295 103.888 1.00 37.70  ? 563  TYR A C     1 
ATOM   4247  O  O     . TYR A 1 563  ? 161.392 151.280 103.666 1.00 41.95  ? 563  TYR A O     1 
ATOM   4248  C  CB    . TYR A 1 563  ? 162.097 154.060 105.017 1.00 32.69  ? 563  TYR A CB    1 
ATOM   4249  C  CG    . TYR A 1 563  ? 163.241 153.147 105.399 1.00 37.12  ? 563  TYR A CG    1 
ATOM   4250  C  CD1   . TYR A 1 563  ? 164.502 153.318 104.851 1.00 40.16  ? 563  TYR A CD1   1 
ATOM   4251  C  CD2   . TYR A 1 563  ? 163.061 152.126 106.320 1.00 39.28  ? 563  TYR A CD2   1 
ATOM   4252  C  CE1   . TYR A 1 563  ? 165.548 152.494 105.203 1.00 41.78  ? 563  TYR A CE1   1 
ATOM   4253  C  CE2   . TYR A 1 563  ? 164.103 151.297 106.676 1.00 41.85  ? 563  TYR A CE2   1 
ATOM   4254  C  CZ    . TYR A 1 563  ? 165.344 151.486 106.114 1.00 41.99  ? 563  TYR A CZ    1 
ATOM   4255  O  OH    . TYR A 1 563  ? 166.388 150.665 106.465 1.00 41.14  ? 563  TYR A OH    1 
ATOM   4256  N  N     . LYS A 1 564  ? 159.448 152.234 104.263 1.00 37.29  ? 564  LYS A N     1 
ATOM   4257  C  CA    . LYS A 1 564  ? 158.782 150.963 104.509 1.00 35.17  ? 564  LYS A CA    1 
ATOM   4258  C  C     . LYS A 1 564  ? 158.324 150.332 103.200 1.00 37.89  ? 564  LYS A C     1 
ATOM   4259  O  O     . LYS A 1 564  ? 157.836 151.020 102.300 1.00 43.47  ? 564  LYS A O     1 
ATOM   4260  C  CB    . LYS A 1 564  ? 157.586 151.168 105.440 1.00 35.75  ? 564  LYS A CB    1 
ATOM   4261  C  CG    . LYS A 1 564  ? 157.070 149.898 106.094 1.00 38.94  ? 564  LYS A CG    1 
ATOM   4262  C  CD    . LYS A 1 564  ? 155.742 149.442 105.536 1.00 37.34  ? 564  LYS A CD    1 
ATOM   4263  C  CE    . LYS A 1 564  ? 155.348 148.110 106.143 1.00 37.42  ? 564  LYS A CE    1 
ATOM   4264  N  NZ    . LYS A 1 564  ? 154.017 147.647 105.682 1.00 35.87  ? 564  LYS A NZ    1 
ATOM   4265  N  N     . ASP A 1 565  ? 158.484 149.016 103.099 1.00 40.78  ? 565  ASP A N     1 
ATOM   4266  C  CA    . ASP A 1 565  ? 158.112 148.275 101.900 1.00 44.35  ? 565  ASP A CA    1 
ATOM   4267  C  C     . ASP A 1 565  ? 156.663 147.809 102.011 1.00 47.38  ? 565  ASP A C     1 
ATOM   4268  O  O     . ASP A 1 565  ? 156.319 147.042 102.916 1.00 48.75  ? 565  ASP A O     1 
ATOM   4269  C  CB    . ASP A 1 565  ? 159.045 147.084 101.696 1.00 45.77  ? 565  ASP A CB    1 
ATOM   4270  C  CG    . ASP A 1 565  ? 158.743 146.321 100.425 1.00 58.24  ? 565  ASP A CG    1 
ATOM   4271  O  OD1   . ASP A 1 565  ? 158.365 146.961 99.423  1.00 59.60  ? 565  ASP A OD1   1 
ATOM   4272  O  OD2   . ASP A 1 565  ? 158.875 145.079 100.429 1.00 62.87  ? 565  ASP A OD2   1 
ATOM   4273  N  N     . ALA A 1 566  ? 155.821 148.263 101.085 1.00 45.37  ? 566  ALA A N     1 
ATOM   4274  C  CA    . ALA A 1 566  ? 154.405 147.930 101.103 1.00 38.99  ? 566  ALA A CA    1 
ATOM   4275  C  C     . ALA A 1 566  ? 153.890 147.867 99.672  1.00 41.42  ? 566  ALA A C     1 
ATOM   4276  O  O     . ALA A 1 566  ? 154.608 148.171 98.718  1.00 45.29  ? 566  ALA A O     1 
ATOM   4277  C  CB    . ALA A 1 566  ? 153.605 148.943 101.925 1.00 34.86  ? 566  ALA A CB    1 
ATOM   4278  N  N     . ASP A 1 567  ? 152.631 147.450 99.533  1.00 39.25  ? 567  ASP A N     1 
ATOM   4279  C  CA    . ASP A 1 567  ? 151.978 147.389 98.231  1.00 41.09  ? 567  ASP A CA    1 
ATOM   4280  C  C     . ASP A 1 567  ? 151.120 148.608 97.931  1.00 43.38  ? 567  ASP A C     1 
ATOM   4281  O  O     . ASP A 1 567  ? 150.865 148.893 96.756  1.00 46.57  ? 567  ASP A O     1 
ATOM   4282  C  CB    . ASP A 1 567  ? 151.100 146.139 98.129  1.00 47.75  ? 567  ASP A CB    1 
ATOM   4283  C  CG    . ASP A 1 567  ? 151.896 144.857 98.208  1.00 57.78  ? 567  ASP A CG    1 
ATOM   4284  O  OD1   . ASP A 1 567  ? 153.126 144.905 98.003  1.00 58.83  ? 567  ASP A OD1   1 
ATOM   4285  O  OD2   . ASP A 1 567  ? 151.291 143.800 98.477  1.00 58.06  ? 567  ASP A OD2   1 
ATOM   4286  N  N     . LEU A 1 568  ? 150.661 149.322 98.955  1.00 42.14  ? 568  LEU A N     1 
ATOM   4287  C  CA    . LEU A 1 568  ? 149.795 150.480 98.783  1.00 36.40  ? 568  LEU A CA    1 
ATOM   4288  C  C     . LEU A 1 568  ? 150.274 151.587 99.704  1.00 33.88  ? 568  LEU A C     1 
ATOM   4289  O  O     . LEU A 1 568  ? 150.506 151.348 100.892 1.00 32.63  ? 568  LEU A O     1 
ATOM   4290  C  CB    . LEU A 1 568  ? 148.338 150.121 99.090  1.00 36.90  ? 568  LEU A CB    1 
ATOM   4291  C  CG    . LEU A 1 568  ? 147.276 151.220 99.060  1.00 38.08  ? 568  LEU A CG    1 
ATOM   4292  C  CD1   . LEU A 1 568  ? 147.171 151.844 97.681  1.00 40.00  ? 568  LEU A CD1   1 
ATOM   4293  C  CD2   . LEU A 1 568  ? 145.939 150.661 99.503  1.00 35.71  ? 568  LEU A CD2   1 
ATOM   4294  N  N     . TYR A 1 569  ? 150.418 152.791 99.160  1.00 36.38  ? 569  TYR A N     1 
ATOM   4295  C  CA    . TYR A 1 569  ? 150.914 153.944 99.902  1.00 33.87  ? 569  TYR A CA    1 
ATOM   4296  C  C     . TYR A 1 569  ? 149.811 154.989 99.999  1.00 34.80  ? 569  TYR A C     1 
ATOM   4297  O  O     . TYR A 1 569  ? 149.285 155.436 98.976  1.00 38.40  ? 569  TYR A O     1 
ATOM   4298  C  CB    . TYR A 1 569  ? 152.157 154.529 99.234  1.00 32.03  ? 569  TYR A CB    1 
ATOM   4299  C  CG    . TYR A 1 569  ? 153.369 153.628 99.317  1.00 38.16  ? 569  TYR A CG    1 
ATOM   4300  C  CD1   . TYR A 1 569  ? 153.539 152.572 98.431  1.00 38.16  ? 569  TYR A CD1   1 
ATOM   4301  C  CD2   . TYR A 1 569  ? 154.339 153.832 100.286 1.00 39.45  ? 569  TYR A CD2   1 
ATOM   4302  C  CE1   . TYR A 1 569  ? 154.641 151.748 98.508  1.00 39.60  ? 569  TYR A CE1   1 
ATOM   4303  C  CE2   . TYR A 1 569  ? 155.444 153.012 100.369 1.00 38.55  ? 569  TYR A CE2   1 
ATOM   4304  C  CZ    . TYR A 1 569  ? 155.590 151.974 99.479  1.00 43.34  ? 569  TYR A CZ    1 
ATOM   4305  O  OH    . TYR A 1 569  ? 156.692 151.159 99.563  1.00 48.33  ? 569  TYR A OH    1 
ATOM   4306  N  N     . LEU A 1 570  ? 149.466 155.373 101.225 1.00 31.43  ? 570  LEU A N     1 
ATOM   4307  C  CA    . LEU A 1 570  ? 148.396 156.328 101.496 1.00 29.83  ? 570  LEU A CA    1 
ATOM   4308  C  C     . LEU A 1 570  ? 149.031 157.619 102.000 1.00 31.09  ? 570  LEU A C     1 
ATOM   4309  O  O     . LEU A 1 570  ? 149.494 157.688 103.141 1.00 36.15  ? 570  LEU A O     1 
ATOM   4310  C  CB    . LEU A 1 570  ? 147.411 155.757 102.509 1.00 30.59  ? 570  LEU A CB    1 
ATOM   4311  C  CG    . LEU A 1 570  ? 146.712 154.464 102.090 1.00 27.10  ? 570  LEU A CG    1 
ATOM   4312  C  CD1   . LEU A 1 570  ? 145.814 153.973 103.204 1.00 28.07  ? 570  LEU A CD1   1 
ATOM   4313  C  CD2   . LEU A 1 570  ? 145.929 154.660 100.807 1.00 29.77  ? 570  LEU A CD2   1 
ATOM   4314  N  N     . LEU A 1 571  ? 149.049 158.640 101.151 1.00 28.71  ? 571  LEU A N     1 
ATOM   4315  C  CA    . LEU A 1 571  ? 149.725 159.903 101.434 1.00 32.07  ? 571  LEU A CA    1 
ATOM   4316  C  C     . LEU A 1 571  ? 148.665 160.978 101.656 1.00 35.55  ? 571  LEU A C     1 
ATOM   4317  O  O     . LEU A 1 571  ? 148.070 161.480 100.699 1.00 37.98  ? 571  LEU A O     1 
ATOM   4318  C  CB    . LEU A 1 571  ? 150.665 160.265 100.290 1.00 36.83  ? 571  LEU A CB    1 
ATOM   4319  C  CG    . LEU A 1 571  ? 151.688 159.197 99.890  1.00 31.16  ? 571  LEU A CG    1 
ATOM   4320  C  CD1   . LEU A 1 571  ? 152.531 159.671 98.726  1.00 30.16  ? 571  LEU A CD1   1 
ATOM   4321  C  CD2   . LEU A 1 571  ? 152.570 158.818 101.063 1.00 29.25  ? 571  LEU A CD2   1 
ATOM   4322  N  N     . ASP A 1 572  ? 148.432 161.334 102.919 1.00 35.76  ? 572  ASP A N     1 
ATOM   4323  C  CA    . ASP A 1 572  ? 147.381 162.285 103.286 1.00 38.70  ? 572  ASP A CA    1 
ATOM   4324  C  C     . ASP A 1 572  ? 147.966 163.690 103.353 1.00 42.26  ? 572  ASP A C     1 
ATOM   4325  O  O     . ASP A 1 572  ? 148.383 164.164 104.410 1.00 45.23  ? 572  ASP A O     1 
ATOM   4326  C  CB    . ASP A 1 572  ? 146.740 161.888 104.609 1.00 37.92  ? 572  ASP A CB    1 
ATOM   4327  C  CG    . ASP A 1 572  ? 145.443 162.632 104.878 1.00 39.80  ? 572  ASP A CG    1 
ATOM   4328  O  OD1   . ASP A 1 572  ? 144.906 163.261 103.943 1.00 40.19  ? 572  ASP A OD1   1 
ATOM   4329  O  OD2   . ASP A 1 572  ? 144.963 162.593 106.029 1.00 38.13  ? 572  ASP A OD2   1 
ATOM   4330  N  N     . SER A 1 573  ? 147.991 164.367 102.203 1.00 42.01  ? 573  SER A N     1 
ATOM   4331  C  CA    . SER A 1 573  ? 148.397 165.764 102.077 1.00 41.99  ? 573  SER A CA    1 
ATOM   4332  C  C     . SER A 1 573  ? 149.789 166.017 102.644 1.00 44.73  ? 573  SER A C     1 
ATOM   4333  O  O     . SER A 1 573  ? 149.929 166.766 103.619 1.00 46.48  ? 573  SER A O     1 
ATOM   4334  C  CB    . SER A 1 573  ? 147.385 166.673 102.774 1.00 41.92  ? 573  SER A CB    1 
ATOM   4335  O  OG    . SER A 1 573  ? 146.091 166.496 102.232 1.00 49.05  ? 573  SER A OG    1 
ATOM   4336  N  N     . PRO A 1 574  ? 150.839 165.419 102.074 1.00 45.91  ? 574  PRO A N     1 
ATOM   4337  C  CA    . PRO A 1 574  ? 152.184 165.639 102.623 1.00 42.68  ? 574  PRO A CA    1 
ATOM   4338  C  C     . PRO A 1 574  ? 152.750 167.019 102.333 1.00 42.21  ? 574  PRO A C     1 
ATOM   4339  O  O     . PRO A 1 574  ? 153.602 167.486 103.097 1.00 41.30  ? 574  PRO A O     1 
ATOM   4340  C  CB    . PRO A 1 574  ? 153.017 164.543 101.947 1.00 43.38  ? 574  PRO A CB    1 
ATOM   4341  C  CG    . PRO A 1 574  ? 152.330 164.324 100.652 1.00 43.56  ? 574  PRO A CG    1 
ATOM   4342  C  CD    . PRO A 1 574  ? 150.863 164.473 100.945 1.00 46.43  ? 574  PRO A CD    1 
ATOM   4343  N  N     . PHE A 1 575  ? 152.312 167.684 101.270 1.00 43.58  ? 575  PHE A N     1 
ATOM   4344  C  CA    . PHE A 1 575  ? 152.884 168.969 100.864 1.00 41.38  ? 575  PHE A CA    1 
ATOM   4345  C  C     . PHE A 1 575  ? 152.084 170.130 101.451 1.00 43.49  ? 575  PHE A C     1 
ATOM   4346  O  O     . PHE A 1 575  ? 151.565 170.986 100.738 1.00 45.01  ? 575  PHE A O     1 
ATOM   4347  C  CB    . PHE A 1 575  ? 152.943 169.063 99.343  1.00 44.18  ? 575  PHE A CB    1 
ATOM   4348  C  CG    . PHE A 1 575  ? 153.441 167.815 98.673  1.00 49.42  ? 575  PHE A CG    1 
ATOM   4349  C  CD1   . PHE A 1 575  ? 154.629 167.226 99.068  1.00 47.75  ? 575  PHE A CD1   1 
ATOM   4350  C  CD2   . PHE A 1 575  ? 152.725 167.239 97.641  1.00 46.73  ? 575  PHE A CD2   1 
ATOM   4351  C  CE1   . PHE A 1 575  ? 155.086 166.081 98.451  1.00 44.75  ? 575  PHE A CE1   1 
ATOM   4352  C  CE2   . PHE A 1 575  ? 153.179 166.095 97.021  1.00 48.43  ? 575  PHE A CE2   1 
ATOM   4353  C  CZ    . PHE A 1 575  ? 154.360 165.515 97.426  1.00 44.50  ? 575  PHE A CZ    1 
ATOM   4354  N  N     . GLY A 1 576  ? 151.995 170.159 102.777 1.00 44.15  ? 576  GLY A N     1 
ATOM   4355  C  CA    . GLY A 1 576  ? 151.206 171.174 103.444 1.00 36.95  ? 576  GLY A CA    1 
ATOM   4356  C  C     . GLY A 1 576  ? 152.021 172.328 103.988 1.00 39.69  ? 576  GLY A C     1 
ATOM   4357  O  O     . GLY A 1 576  ? 151.575 173.477 103.958 1.00 40.42  ? 576  GLY A O     1 
ATOM   4358  N  N     . TYR A 1 577  ? 153.224 172.037 104.485 1.00 38.49  ? 577  TYR A N     1 
ATOM   4359  C  CA    . TYR A 1 577  ? 154.094 173.048 105.073 1.00 35.01  ? 577  TYR A CA    1 
ATOM   4360  C  C     . TYR A 1 577  ? 155.366 173.249 104.260 1.00 37.80  ? 577  TYR A C     1 
ATOM   4361  O  O     . TYR A 1 577  ? 156.392 173.658 104.809 1.00 37.94  ? 577  TYR A O     1 
ATOM   4362  C  CB    . TYR A 1 577  ? 154.448 172.679 106.514 1.00 34.07  ? 577  TYR A CB    1 
ATOM   4363  C  CG    . TYR A 1 577  ? 153.259 172.582 107.442 1.00 40.45  ? 577  TYR A CG    1 
ATOM   4364  C  CD1   . TYR A 1 577  ? 152.504 173.701 107.752 1.00 41.25  ? 577  TYR A CD1   1 
ATOM   4365  C  CD2   . TYR A 1 577  ? 152.895 171.370 108.007 1.00 38.62  ? 577  TYR A CD2   1 
ATOM   4366  C  CE1   . TYR A 1 577  ? 151.421 173.616 108.599 1.00 39.88  ? 577  TYR A CE1   1 
ATOM   4367  C  CE2   . TYR A 1 577  ? 151.814 171.276 108.854 1.00 35.23  ? 577  TYR A CE2   1 
ATOM   4368  C  CZ    . TYR A 1 577  ? 151.081 172.402 109.147 1.00 38.43  ? 577  TYR A CZ    1 
ATOM   4369  O  OH    . TYR A 1 577  ? 150.000 172.315 109.992 1.00 46.43  ? 577  TYR A OH    1 
ATOM   4370  N  N     . LEU A 1 578  ? 155.321 172.968 102.962 1.00 39.81  ? 578  LEU A N     1 
ATOM   4371  C  CA    . LEU A 1 578  ? 156.489 173.034 102.100 1.00 36.69  ? 578  LEU A CA    1 
ATOM   4372  C  C     . LEU A 1 578  ? 156.340 174.173 101.103 1.00 40.43  ? 578  LEU A C     1 
ATOM   4373  O  O     . LEU A 1 578  ? 155.242 174.435 100.604 1.00 45.32  ? 578  LEU A O     1 
ATOM   4374  C  CB    . LEU A 1 578  ? 156.686 171.717 101.349 1.00 33.38  ? 578  LEU A CB    1 
ATOM   4375  C  CG    . LEU A 1 578  ? 156.871 170.464 102.203 1.00 32.68  ? 578  LEU A CG    1 
ATOM   4376  C  CD1   . LEU A 1 578  ? 157.057 169.257 101.313 1.00 37.09  ? 578  LEU A CD1   1 
ATOM   4377  C  CD2   . LEU A 1 578  ? 158.043 170.618 103.153 1.00 33.44  ? 578  LEU A CD2   1 
ATOM   4378  N  N     . ASP A 1 579  ? 157.449 174.849 100.824 1.00 39.94  ? 579  ASP A N     1 
ATOM   4379  C  CA    . ASP A 1 579  ? 157.481 175.854 99.776  1.00 39.51  ? 579  ASP A CA    1 
ATOM   4380  C  C     . ASP A 1 579  ? 157.342 175.192 98.408  1.00 41.53  ? 579  ASP A C     1 
ATOM   4381  O  O     . ASP A 1 579  ? 157.477 173.976 98.262  1.00 44.66  ? 579  ASP A O     1 
ATOM   4382  C  CB    . ASP A 1 579  ? 158.774 176.662 99.858  1.00 42.78  ? 579  ASP A CB    1 
ATOM   4383  C  CG    . ASP A 1 579  ? 160.005 175.784 99.902  1.00 45.87  ? 579  ASP A CG    1 
ATOM   4384  O  OD1   . ASP A 1 579  ? 160.238 175.139 100.944 1.00 42.04  ? 579  ASP A OD1   1 
ATOM   4385  O  OD2   . ASP A 1 579  ? 160.748 175.746 98.900  1.00 50.17  ? 579  ASP A OD2   1 
ATOM   4386  N  N     . VAL A 1 580  ? 157.043 176.012 97.398  1.00 43.04  ? 580  VAL A N     1 
ATOM   4387  C  CA    . VAL A 1 580  ? 156.739 175.477 96.073  1.00 47.62  ? 580  VAL A CA    1 
ATOM   4388  C  C     . VAL A 1 580  ? 157.924 174.721 95.485  1.00 51.36  ? 580  VAL A C     1 
ATOM   4389  O  O     . VAL A 1 580  ? 157.742 173.698 94.815  1.00 53.92  ? 580  VAL A O     1 
ATOM   4390  C  CB    . VAL A 1 580  ? 156.266 176.605 95.135  1.00 52.16  ? 580  VAL A CB    1 
ATOM   4391  C  CG1   . VAL A 1 580  ? 154.921 177.131 95.590  1.00 57.90  ? 580  VAL A CG1   1 
ATOM   4392  C  CG2   . VAL A 1 580  ? 157.283 177.726 95.092  1.00 54.73  ? 580  VAL A CG2   1 
ATOM   4393  N  N     . LEU A 1 581  ? 159.148 175.190 95.727  1.00 48.34  ? 581  LEU A N     1 
ATOM   4394  C  CA    . LEU A 1 581  ? 160.311 174.559 95.114  1.00 45.63  ? 581  LEU A CA    1 
ATOM   4395  C  C     . LEU A 1 581  ? 160.607 173.199 95.741  1.00 44.97  ? 581  LEU A C     1 
ATOM   4396  O  O     . LEU A 1 581  ? 160.848 172.218 95.029  1.00 48.68  ? 581  LEU A O     1 
ATOM   4397  C  CB    . LEU A 1 581  ? 161.519 175.487 95.225  1.00 51.41  ? 581  LEU A CB    1 
ATOM   4398  C  CG    . LEU A 1 581  ? 162.805 175.042 94.532  1.00 57.57  ? 581  LEU A CG    1 
ATOM   4399  C  CD1   . LEU A 1 581  ? 162.555 174.811 93.057  1.00 54.72  ? 581  LEU A CD1   1 
ATOM   4400  C  CD2   . LEU A 1 581  ? 163.891 176.082 94.734  1.00 59.15  ? 581  LEU A CD2   1 
ATOM   4401  N  N     . THR A 1 582  ? 160.587 173.123 97.075  1.00 40.71  ? 582  THR A N     1 
ATOM   4402  C  CA    . THR A 1 582  ? 160.778 171.843 97.750  1.00 40.91  ? 582  THR A CA    1 
ATOM   4403  C  C     . THR A 1 582  ? 159.647 170.878 97.425  1.00 41.99  ? 582  THR A C     1 
ATOM   4404  O  O     . THR A 1 582  ? 159.881 169.682 97.214  1.00 44.55  ? 582  THR A O     1 
ATOM   4405  C  CB    . THR A 1 582  ? 160.878 172.055 99.260  1.00 41.33  ? 582  THR A CB    1 
ATOM   4406  O  OG1   . THR A 1 582  ? 162.017 172.871 99.552  1.00 45.33  ? 582  THR A OG1   1 
ATOM   4407  C  CG2   . THR A 1 582  ? 161.028 170.730 99.977  1.00 38.73  ? 582  THR A CG2   1 
ATOM   4408  N  N     . GLU A 1 583  ? 158.415 171.383 97.382  1.00 42.70  ? 583  GLU A N     1 
ATOM   4409  C  CA    . GLU A 1 583  ? 157.275 170.561 96.993  1.00 40.35  ? 583  GLU A CA    1 
ATOM   4410  C  C     . GLU A 1 583  ? 157.472 169.976 95.603  1.00 42.65  ? 583  GLU A C     1 
ATOM   4411  O  O     . GLU A 1 583  ? 157.269 168.775 95.387  1.00 47.75  ? 583  GLU A O     1 
ATOM   4412  C  CB    . GLU A 1 583  ? 155.999 171.399 97.047  1.00 43.22  ? 583  GLU A CB    1 
ATOM   4413  C  CG    . GLU A 1 583  ? 154.793 170.744 96.412  1.00 47.85  ? 583  GLU A CG    1 
ATOM   4414  C  CD    . GLU A 1 583  ? 153.635 171.708 96.249  1.00 55.73  ? 583  GLU A CD    1 
ATOM   4415  O  OE1   . GLU A 1 583  ? 152.872 171.900 97.219  1.00 56.21  ? 583  GLU A OE1   1 
ATOM   4416  O  OE2   . GLU A 1 583  ? 153.492 172.283 95.150  1.00 58.27  ? 583  GLU A OE2   1 
ATOM   4417  N  N     . LYS A 1 584  ? 157.864 170.816 94.645  1.00 42.65  ? 584  LYS A N     1 
ATOM   4418  C  CA    . LYS A 1 584  ? 158.063 170.352 93.278  1.00 43.75  ? 584  LYS A CA    1 
ATOM   4419  C  C     . LYS A 1 584  ? 159.177 169.316 93.205  1.00 46.76  ? 584  LYS A C     1 
ATOM   4420  O  O     . LYS A 1 584  ? 159.041 168.290 92.529  1.00 47.07  ? 584  LYS A O     1 
ATOM   4421  C  CB    . LYS A 1 584  ? 158.368 171.541 92.368  1.00 41.00  ? 584  LYS A CB    1 
ATOM   4422  C  CG    . LYS A 1 584  ? 158.621 171.167 90.925  1.00 46.78  ? 584  LYS A CG    1 
ATOM   4423  C  CD    . LYS A 1 584  ? 158.893 172.396 90.081  1.00 53.88  ? 584  LYS A CD    1 
ATOM   4424  C  CE    . LYS A 1 584  ? 159.184 172.019 88.639  1.00 59.06  ? 584  LYS A CE    1 
ATOM   4425  N  NZ    . LYS A 1 584  ? 159.506 173.212 87.813  1.00 63.36  ? 584  LYS A NZ    1 
ATOM   4426  N  N     . GLU A 1 585  ? 160.292 169.570 93.893  1.00 45.67  ? 585  GLU A N     1 
ATOM   4427  C  CA    . GLU A 1 585  ? 161.407 168.627 93.872  1.00 42.95  ? 585  GLU A CA    1 
ATOM   4428  C  C     . GLU A 1 585  ? 161.000 167.275 94.448  1.00 44.94  ? 585  GLU A C     1 
ATOM   4429  O  O     . GLU A 1 585  ? 161.300 166.223 93.869  1.00 47.45  ? 585  GLU A O     1 
ATOM   4430  C  CB    . GLU A 1 585  ? 162.595 169.205 94.637  1.00 45.48  ? 585  GLU A CB    1 
ATOM   4431  C  CG    . GLU A 1 585  ? 163.330 170.305 93.901  1.00 49.68  ? 585  GLU A CG    1 
ATOM   4432  C  CD    . GLU A 1 585  ? 164.401 170.962 94.752  1.00 59.22  ? 585  GLU A CD    1 
ATOM   4433  O  OE1   . GLU A 1 585  ? 164.429 170.717 95.977  1.00 59.08  ? 585  GLU A OE1   1 
ATOM   4434  O  OE2   . GLU A 1 585  ? 165.221 171.721 94.194  1.00 58.46  ? 585  GLU A OE2   1 
ATOM   4435  N  N     . ILE A 1 586  ? 160.311 167.283 95.594  1.00 43.67  ? 586  ILE A N     1 
ATOM   4436  C  CA    . ILE A 1 586  ? 159.884 166.028 96.207  1.00 41.46  ? 586  ILE A CA    1 
ATOM   4437  C  C     . ILE A 1 586  ? 158.906 165.293 95.304  1.00 42.17  ? 586  ILE A C     1 
ATOM   4438  O  O     . ILE A 1 586  ? 159.008 164.076 95.122  1.00 47.29  ? 586  ILE A O     1 
ATOM   4439  C  CB    . ILE A 1 586  ? 159.283 166.279 97.602  1.00 38.08  ? 586  ILE A CB    1 
ATOM   4440  C  CG1   . ILE A 1 586  ? 160.348 166.804 98.560  1.00 37.60  ? 586  ILE A CG1   1 
ATOM   4441  C  CG2   . ILE A 1 586  ? 158.666 165.012 98.153  1.00 38.32  ? 586  ILE A CG2   1 
ATOM   4442  C  CD1   . ILE A 1 586  ? 159.789 167.283 99.870  1.00 35.72  ? 586  ILE A CD1   1 
ATOM   4443  N  N     . PHE A 1 587  ? 157.947 166.012 94.718  1.00 42.91  ? 587  PHE A N     1 
ATOM   4444  C  CA    . PHE A 1 587  ? 156.968 165.355 93.860  1.00 44.46  ? 587  PHE A CA    1 
ATOM   4445  C  C     . PHE A 1 587  ? 157.628 164.751 92.626  1.00 48.73  ? 587  PHE A C     1 
ATOM   4446  O  O     . PHE A 1 587  ? 157.257 163.654 92.191  1.00 51.22  ? 587  PHE A O     1 
ATOM   4447  C  CB    . PHE A 1 587  ? 155.875 166.343 93.458  1.00 45.40  ? 587  PHE A CB    1 
ATOM   4448  C  CG    . PHE A 1 587  ? 154.777 165.730 92.639  1.00 48.33  ? 587  PHE A CG    1 
ATOM   4449  C  CD1   . PHE A 1 587  ? 153.865 164.866 93.219  1.00 49.52  ? 587  PHE A CD1   1 
ATOM   4450  C  CD2   . PHE A 1 587  ? 154.654 166.018 91.293  1.00 46.95  ? 587  PHE A CD2   1 
ATOM   4451  C  CE1   . PHE A 1 587  ? 152.856 164.299 92.473  1.00 46.10  ? 587  PHE A CE1   1 
ATOM   4452  C  CE2   . PHE A 1 587  ? 153.644 165.454 90.541  1.00 45.93  ? 587  PHE A CE2   1 
ATOM   4453  C  CZ    . PHE A 1 587  ? 152.744 164.594 91.133  1.00 46.28  ? 587  PHE A CZ    1 
ATOM   4454  N  N     . GLU A 1 588  ? 158.609 165.448 92.049  1.00 50.18  ? 588  GLU A N     1 
ATOM   4455  C  CA    . GLU A 1 588  ? 159.231 164.981 90.817  1.00 50.75  ? 588  GLU A CA    1 
ATOM   4456  C  C     . GLU A 1 588  ? 160.283 163.904 91.036  1.00 51.88  ? 588  GLU A C     1 
ATOM   4457  O  O     . GLU A 1 588  ? 160.556 163.137 90.107  1.00 56.96  ? 588  GLU A O     1 
ATOM   4458  C  CB    . GLU A 1 588  ? 159.867 166.155 90.069  1.00 51.93  ? 588  GLU A CB    1 
ATOM   4459  C  CG    . GLU A 1 588  ? 158.871 167.185 89.573  1.00 57.01  ? 588  GLU A CG    1 
ATOM   4460  C  CD    . GLU A 1 588  ? 158.290 166.833 88.219  1.00 64.31  ? 588  GLU A CD    1 
ATOM   4461  O  OE1   . GLU A 1 588  ? 158.935 167.145 87.197  1.00 73.48  ? 588  GLU A OE1   1 
ATOM   4462  O  OE2   . GLU A 1 588  ? 157.189 166.245 88.177  1.00 64.43  ? 588  GLU A OE2   1 
ATOM   4463  N  N     . SER A 1 589  ? 160.876 163.813 92.228  1.00 52.60  ? 589  SER A N     1 
ATOM   4464  C  CA    . SER A 1 589  ? 161.964 162.867 92.442  1.00 51.99  ? 589  SER A CA    1 
ATOM   4465  C  C     . SER A 1 589  ? 161.688 161.797 93.487  1.00 49.39  ? 589  SER A C     1 
ATOM   4466  O  O     . SER A 1 589  ? 162.531 160.912 93.662  1.00 51.39  ? 589  SER A O     1 
ATOM   4467  C  CB    . SER A 1 589  ? 163.246 163.614 92.839  1.00 55.41  ? 589  SER A CB    1 
ATOM   4468  O  OG    . SER A 1 589  ? 163.213 163.985 94.205  1.00 55.65  ? 589  SER A OG    1 
ATOM   4469  N  N     . CYS A 1 590  ? 160.554 161.840 94.183  1.00 49.36  ? 590  CYS A N     1 
ATOM   4470  C  CA    . CYS A 1 590  ? 160.221 160.847 95.197  1.00 49.65  ? 590  CYS A CA    1 
ATOM   4471  C  C     . CYS A 1 590  ? 158.942 160.091 94.880  1.00 54.22  ? 590  CYS A C     1 
ATOM   4472  O  O     . CYS A 1 590  ? 158.911 158.861 94.991  1.00 54.94  ? 590  CYS A O     1 
ATOM   4473  C  CB    . CYS A 1 590  ? 160.099 161.521 96.572  1.00 50.02  ? 590  CYS A CB    1 
ATOM   4474  S  SG    . CYS A 1 590  ? 159.968 160.376 97.962  1.00 59.98  ? 590  CYS A SG    1 
ATOM   4475  N  N     . VAL A 1 591  ? 157.877 160.794 94.497  1.00 56.87  ? 591  VAL A N     1 
ATOM   4476  C  CA    . VAL A 1 591  ? 156.592 160.141 94.273  1.00 56.17  ? 591  VAL A CA    1 
ATOM   4477  C  C     . VAL A 1 591  ? 156.522 159.547 92.873  1.00 55.83  ? 591  VAL A C     1 
ATOM   4478  O  O     . VAL A 1 591  ? 156.110 158.397 92.691  1.00 59.22  ? 591  VAL A O     1 
ATOM   4479  C  CB    . VAL A 1 591  ? 155.439 161.131 94.528  1.00 55.10  ? 591  VAL A CB    1 
ATOM   4480  C  CG1   . VAL A 1 591  ? 154.102 160.490 94.200  1.00 47.82  ? 591  VAL A CG1   1 
ATOM   4481  C  CG2   . VAL A 1 591  ? 155.460 161.607 95.970  1.00 51.55  ? 591  VAL A CG2   1 
ATOM   4482  N  N     . CYS A 1 592  ? 156.920 160.316 91.861  1.00 55.33  ? 592  CYS A N     1 
ATOM   4483  C  CA    . CYS A 1 592  ? 156.786 159.874 90.480  1.00 54.16  ? 592  CYS A CA    1 
ATOM   4484  C  C     . CYS A 1 592  ? 157.993 159.104 89.964  1.00 53.52  ? 592  CYS A C     1 
ATOM   4485  O  O     . CYS A 1 592  ? 157.897 158.482 88.902  1.00 53.87  ? 592  CYS A O     1 
ATOM   4486  C  CB    . CYS A 1 592  ? 156.532 161.077 89.564  1.00 54.25  ? 592  CYS A CB    1 
ATOM   4487  S  SG    . CYS A 1 592  ? 154.960 161.918 89.845  1.00 63.30  ? 592  CYS A SG    1 
ATOM   4488  N  N     . LYS A 1 593  ? 159.118 159.122 90.679  1.00 55.02  ? 593  LYS A N     1 
ATOM   4489  C  CA    . LYS A 1 593  ? 160.330 158.482 90.179  1.00 54.47  ? 593  LYS A CA    1 
ATOM   4490  C  C     . LYS A 1 593  ? 160.791 157.335 91.069  1.00 51.11  ? 593  LYS A C     1 
ATOM   4491  O  O     . LYS A 1 593  ? 161.018 156.222 90.587  1.00 50.23  ? 593  LYS A O     1 
ATOM   4492  C  CB    . LYS A 1 593  ? 161.450 159.512 90.044  1.00 55.07  ? 593  LYS A CB    1 
ATOM   4493  C  CG    . LYS A 1 593  ? 162.711 158.974 89.400  1.00 54.65  ? 593  LYS A CG    1 
ATOM   4494  C  CD    . LYS A 1 593  ? 163.821 160.004 89.456  1.00 57.24  ? 593  LYS A CD    1 
ATOM   4495  C  CE    . LYS A 1 593  ? 163.486 161.215 88.606  1.00 62.27  ? 593  LYS A CE    1 
ATOM   4496  N  NZ    . LYS A 1 593  ? 164.496 162.296 88.761  1.00 60.02  ? 593  LYS A NZ    1 
ATOM   4497  N  N     . LEU A 1 594  ? 160.930 157.599 92.369  1.00 50.84  ? 594  LEU A N     1 
ATOM   4498  C  CA    . LEU A 1 594  ? 161.513 156.610 93.268  1.00 50.74  ? 594  LEU A CA    1 
ATOM   4499  C  C     . LEU A 1 594  ? 160.600 155.408 93.465  1.00 54.80  ? 594  LEU A C     1 
ATOM   4500  O  O     . LEU A 1 594  ? 161.087 154.284 93.629  1.00 57.94  ? 594  LEU A O     1 
ATOM   4501  C  CB    . LEU A 1 594  ? 161.837 157.255 94.615  1.00 50.13  ? 594  LEU A CB    1 
ATOM   4502  C  CG    . LEU A 1 594  ? 162.826 156.517 95.513  1.00 44.39  ? 594  LEU A CG    1 
ATOM   4503  C  CD1   . LEU A 1 594  ? 164.206 156.534 94.889  1.00 47.04  ? 594  LEU A CD1   1 
ATOM   4504  C  CD2   . LEU A 1 594  ? 162.855 157.136 96.899  1.00 42.12  ? 594  LEU A CD2   1 
ATOM   4505  N  N     . MET A 1 595  ? 159.288 155.617 93.452  1.00 55.14  ? 595  MET A N     1 
ATOM   4506  C  CA    . MET A 1 595  ? 158.310 154.554 93.665  1.00 56.12  ? 595  MET A CA    1 
ATOM   4507  C  C     . MET A 1 595  ? 157.240 154.590 92.577  1.00 55.00  ? 595  MET A C     1 
ATOM   4508  O  O     . MET A 1 595  ? 156.039 154.484 92.827  1.00 55.98  ? 595  MET A O     1 
ATOM   4509  C  CB    . MET A 1 595  ? 157.741 154.648 95.083  1.00 55.11  ? 595  MET A CB    1 
ATOM   4510  C  CG    . MET A 1 595  ? 156.811 155.817 95.375  1.00 56.12  ? 595  MET A CG    1 
ATOM   4511  S  SD    . MET A 1 595  ? 156.738 156.136 97.149  1.00 64.61  ? 595  MET A SD    1 
ATOM   4512  C  CE    . MET A 1 595  ? 155.416 157.336 97.240  1.00 53.74  ? 595  MET A CE    1 
ATOM   4513  N  N     . ALA A 1 596  ? 157.692 154.711 91.326  1.00 55.27  ? 596  ALA A N     1 
ATOM   4514  C  CA    . ALA A 1 596  ? 156.784 154.734 90.186  1.00 57.44  ? 596  ALA A CA    1 
ATOM   4515  C  C     . ALA A 1 596  ? 156.128 153.385 89.922  1.00 59.76  ? 596  ALA A C     1 
ATOM   4516  O  O     . ALA A 1 596  ? 155.109 153.335 89.226  1.00 58.60  ? 596  ALA A O     1 
ATOM   4517  C  CB    . ALA A 1 596  ? 157.528 155.199 88.935  1.00 53.27  ? 596  ALA A CB    1 
ATOM   4518  N  N     . ASN A 1 597  ? 156.686 152.294 90.443  1.00 60.48  ? 597  ASN A N     1 
ATOM   4519  C  CA    . ASN A 1 597  ? 156.125 150.964 90.250  1.00 61.29  ? 597  ASN A CA    1 
ATOM   4520  C  C     . ASN A 1 597  ? 155.180 150.549 91.368  1.00 62.01  ? 597  ASN A C     1 
ATOM   4521  O  O     . ASN A 1 597  ? 154.620 149.450 91.313  1.00 65.52  ? 597  ASN A O     1 
ATOM   4522  C  CB    . ASN A 1 597  ? 157.246 149.929 90.116  1.00 64.97  ? 597  ASN A CB    1 
ATOM   4523  C  CG    . ASN A 1 597  ? 158.144 150.192 88.926  1.00 74.31  ? 597  ASN A CG    1 
ATOM   4524  O  OD1   . ASN A 1 597  ? 159.367 150.244 89.054  1.00 81.17  ? 597  ASN A OD1   1 
ATOM   4525  N  ND2   . ASN A 1 597  ? 157.540 150.354 87.755  1.00 70.41  ? 597  ASN A ND2   1 
ATOM   4526  N  N     . LYS A 1 598  ? 154.992 151.393 92.375  1.00 56.54  ? 598  LYS A N     1 
ATOM   4527  C  CA    . LYS A 1 598  ? 154.118 151.089 93.495  1.00 55.85  ? 598  LYS A CA    1 
ATOM   4528  C  C     . LYS A 1 598  ? 152.745 151.714 93.279  1.00 53.63  ? 598  LYS A C     1 
ATOM   4529  O  O     . LYS A 1 598  ? 152.613 152.765 92.649  1.00 55.48  ? 598  LYS A O     1 
ATOM   4530  C  CB    . LYS A 1 598  ? 154.724 151.610 94.798  1.00 52.94  ? 598  LYS A CB    1 
ATOM   4531  C  CG    . LYS A 1 598  ? 156.050 150.972 95.175  1.00 54.56  ? 598  LYS A CG    1 
ATOM   4532  C  CD    . LYS A 1 598  ? 155.921 149.475 95.381  1.00 58.69  ? 598  LYS A CD    1 
ATOM   4533  C  CE    . LYS A 1 598  ? 157.142 148.921 96.093  1.00 56.16  ? 598  LYS A CE    1 
ATOM   4534  N  NZ    . LYS A 1 598  ? 156.996 147.480 96.423  1.00 54.39  ? 598  LYS A NZ    1 
ATOM   4535  N  N     . THR A 1 599  ? 151.718 151.047 93.797  1.00 51.41  ? 599  THR A N     1 
ATOM   4536  C  CA    . THR A 1 599  ? 150.385 151.632 93.839  1.00 48.90  ? 599  THR A CA    1 
ATOM   4537  C  C     . THR A 1 599  ? 150.307 152.631 94.983  1.00 47.33  ? 599  THR A C     1 
ATOM   4538  O  O     . THR A 1 599  ? 150.762 152.356 96.095  1.00 49.14  ? 599  THR A O     1 
ATOM   4539  C  CB    . THR A 1 599  ? 149.320 150.552 94.020  1.00 49.54  ? 599  THR A CB    1 
ATOM   4540  O  OG1   . THR A 1 599  ? 149.590 149.459 93.136  1.00 54.74  ? 599  THR A OG1   1 
ATOM   4541  C  CG2   . THR A 1 599  ? 147.942 151.109 93.717  1.00 46.04  ? 599  THR A CG2   1 
ATOM   4542  N  N     . ARG A 1 600  ? 149.728 153.795 94.709  1.00 43.46  ? 600  ARG A N     1 
ATOM   4543  C  CA    . ARG A 1 600  ? 149.723 154.861 95.696  1.00 43.62  ? 600  ARG A CA    1 
ATOM   4544  C  C     . ARG A 1 600  ? 148.569 155.819 95.442  1.00 41.61  ? 600  ARG A C     1 
ATOM   4545  O  O     . ARG A 1 600  ? 148.156 156.035 94.301  1.00 40.16  ? 600  ARG A O     1 
ATOM   4546  C  CB    . ARG A 1 600  ? 151.078 155.581 95.705  1.00 43.94  ? 600  ARG A CB    1 
ATOM   4547  C  CG    . ARG A 1 600  ? 151.414 156.298 94.421  1.00 44.02  ? 600  ARG A CG    1 
ATOM   4548  C  CD    . ARG A 1 600  ? 152.910 156.215 94.152  1.00 42.39  ? 600  ARG A CD    1 
ATOM   4549  N  NE    . ARG A 1 600  ? 153.288 156.892 92.918  1.00 48.82  ? 600  ARG A NE    1 
ATOM   4550  C  CZ    . ARG A 1 600  ? 153.154 156.367 91.708  1.00 45.36  ? 600  ARG A CZ    1 
ATOM   4551  N  NH1   . ARG A 1 600  ? 152.671 155.150 91.532  1.00 44.87  ? 600  ARG A NH1   1 
ATOM   4552  N  NH2   . ARG A 1 600  ? 153.517 157.081 90.648  1.00 44.97  ? 600  ARG A NH2   1 
ATOM   4553  N  N     . ILE A 1 601  ? 148.048 156.375 96.534  1.00 41.76  ? 601  ILE A N     1 
ATOM   4554  C  CA    . ILE A 1 601  ? 146.914 157.293 96.526  1.00 38.45  ? 601  ILE A CA    1 
ATOM   4555  C  C     . ILE A 1 601  ? 147.367 158.588 97.180  1.00 38.51  ? 601  ILE A C     1 
ATOM   4556  O  O     . ILE A 1 601  ? 147.824 158.581 98.329  1.00 36.49  ? 601  ILE A O     1 
ATOM   4557  C  CB    . ILE A 1 601  ? 145.701 156.706 97.266  1.00 38.41  ? 601  ILE A CB    1 
ATOM   4558  C  CG1   . ILE A 1 601  ? 145.319 155.348 96.678  1.00 36.38  ? 601  ILE A CG1   1 
ATOM   4559  C  CG2   . ILE A 1 601  ? 144.526 157.661 97.213  1.00 41.49  ? 601  ILE A CG2   1 
ATOM   4560  C  CD1   . ILE A 1 601  ? 144.174 154.682 97.393  1.00 34.89  ? 601  ILE A CD1   1 
ATOM   4561  N  N     . LEU A 1 602  ? 147.247 159.694 96.454  1.00 40.12  ? 602  LEU A N     1 
ATOM   4562  C  CA    . LEU A 1 602  ? 147.721 160.994 96.913  1.00 39.30  ? 602  LEU A CA    1 
ATOM   4563  C  C     . LEU A 1 602  ? 146.538 161.934 97.104  1.00 41.23  ? 602  LEU A C     1 
ATOM   4564  O  O     . LEU A 1 602  ? 145.756 162.147 96.173  1.00 43.93  ? 602  LEU A O     1 
ATOM   4565  C  CB    . LEU A 1 602  ? 148.716 161.584 95.916  1.00 36.33  ? 602  LEU A CB    1 
ATOM   4566  C  CG    . LEU A 1 602  ? 149.371 162.912 96.286  1.00 42.16  ? 602  LEU A CG    1 
ATOM   4567  C  CD1   . LEU A 1 602  ? 150.232 162.754 97.525  1.00 40.48  ? 602  LEU A CD1   1 
ATOM   4568  C  CD2   . LEU A 1 602  ? 150.183 163.444 95.125  1.00 43.78  ? 602  LEU A CD2   1 
ATOM   4569  N  N     . VAL A 1 603  ? 146.414 162.500 98.301  1.00 40.90  ? 603  VAL A N     1 
ATOM   4570  C  CA    . VAL A 1 603  ? 145.431 163.544 98.569  1.00 42.86  ? 603  VAL A CA    1 
ATOM   4571  C  C     . VAL A 1 603  ? 146.071 164.889 98.252  1.00 45.01  ? 603  VAL A C     1 
ATOM   4572  O  O     . VAL A 1 603  ? 147.068 165.272 98.872  1.00 47.27  ? 603  VAL A O     1 
ATOM   4573  C  CB    . VAL A 1 603  ? 144.940 163.493 100.023 1.00 39.86  ? 603  VAL A CB    1 
ATOM   4574  C  CG1   . VAL A 1 603  ? 143.952 164.610 100.283 1.00 39.81  ? 603  VAL A CG1   1 
ATOM   4575  C  CG2   . VAL A 1 603  ? 144.303 162.149 100.321 1.00 35.51  ? 603  VAL A CG2   1 
ATOM   4576  N  N     . THR A 1 604  ? 145.495 165.609 97.294  1.00 45.02  ? 604  THR A N     1 
ATOM   4577  C  CA    . THR A 1 604  ? 146.097 166.843 96.811  1.00 49.70  ? 604  THR A CA    1 
ATOM   4578  C  C     . THR A 1 604  ? 145.027 167.680 96.129  1.00 55.90  ? 604  THR A C     1 
ATOM   4579  O  O     . THR A 1 604  ? 143.978 167.172 95.728  1.00 59.45  ? 604  THR A O     1 
ATOM   4580  C  CB    . THR A 1 604  ? 147.248 166.565 95.840  1.00 52.50  ? 604  THR A CB    1 
ATOM   4581  O  OG1   . THR A 1 604  ? 147.874 167.799 95.474  1.00 60.90  ? 604  THR A OG1   1 
ATOM   4582  C  CG2   . THR A 1 604  ? 146.722 165.892 94.586  1.00 45.58  ? 604  THR A CG2   1 
ATOM   4583  N  N     . SER A 1 605  ? 145.308 168.977 96.009  1.00 57.89  ? 605  SER A N     1 
ATOM   4584  C  CA    . SER A 1 605  ? 144.420 169.903 95.323  1.00 60.33  ? 605  SER A CA    1 
ATOM   4585  C  C     . SER A 1 605  ? 145.057 170.575 94.115  1.00 62.08  ? 605  SER A C     1 
ATOM   4586  O  O     . SER A 1 605  ? 144.351 171.263 93.370  1.00 68.58  ? 605  SER A O     1 
ATOM   4587  C  CB    . SER A 1 605  ? 143.926 170.986 96.293  1.00 62.56  ? 605  SER A CB    1 
ATOM   4588  O  OG    . SER A 1 605  ? 144.970 171.885 96.627  1.00 62.61  ? 605  SER A OG    1 
ATOM   4589  N  N     . LYS A 1 606  ? 146.358 170.401 93.904  1.00 55.87  ? 606  LYS A N     1 
ATOM   4590  C  CA    . LYS A 1 606  ? 147.053 171.136 92.857  1.00 58.27  ? 606  LYS A CA    1 
ATOM   4591  C  C     . LYS A 1 606  ? 146.772 170.540 91.484  1.00 58.00  ? 606  LYS A C     1 
ATOM   4592  O  O     . LYS A 1 606  ? 146.732 169.320 91.314  1.00 60.16  ? 606  LYS A O     1 
ATOM   4593  C  CB    . LYS A 1 606  ? 148.555 171.147 93.128  1.00 60.07  ? 606  LYS A CB    1 
ATOM   4594  C  CG    . LYS A 1 606  ? 148.952 171.997 94.320  1.00 60.12  ? 606  LYS A CG    1 
ATOM   4595  C  CD    . LYS A 1 606  ? 150.419 172.367 94.273  1.00 59.96  ? 606  LYS A CD    1 
ATOM   4596  C  CE    . LYS A 1 606  ? 150.636 173.662 93.508  1.00 64.84  ? 606  LYS A CE    1 
ATOM   4597  N  NZ    . LYS A 1 606  ? 150.538 173.482 92.034  1.00 69.40  ? 606  LYS A NZ    1 
ATOM   4598  N  N     . MET A 1 607  ? 146.587 171.420 90.496  1.00 58.40  ? 607  MET A N     1 
ATOM   4599  C  CA    . MET A 1 607  ? 146.270 170.982 89.140  1.00 60.51  ? 607  MET A CA    1 
ATOM   4600  C  C     . MET A 1 607  ? 147.440 170.258 88.485  1.00 62.07  ? 607  MET A C     1 
ATOM   4601  O  O     . MET A 1 607  ? 147.236 169.290 87.738  1.00 64.99  ? 607  MET A O     1 
ATOM   4602  C  CB    . MET A 1 607  ? 145.862 172.190 88.298  1.00 65.49  ? 607  MET A CB    1 
ATOM   4603  C  CG    . MET A 1 607  ? 145.050 171.855 87.066  1.00 72.19  ? 607  MET A CG    1 
ATOM   4604  S  SD    . MET A 1 607  ? 143.417 171.222 87.492  1.00 91.92  ? 607  MET A SD    1 
ATOM   4605  C  CE    . MET A 1 607  ? 142.558 171.425 85.934  1.00 79.57  ? 607  MET A CE    1 
ATOM   4606  N  N     . GLU A 1 608  ? 148.667 170.707 88.755  1.00 62.12  ? 608  GLU A N     1 
ATOM   4607  C  CA    . GLU A 1 608  ? 149.842 170.058 88.185  1.00 63.31  ? 608  GLU A CA    1 
ATOM   4608  C  C     . GLU A 1 608  ? 149.953 168.618 88.661  1.00 58.86  ? 608  GLU A C     1 
ATOM   4609  O  O     . GLU A 1 608  ? 150.373 167.736 87.904  1.00 57.47  ? 608  GLU A O     1 
ATOM   4610  C  CB    . GLU A 1 608  ? 151.098 170.839 88.559  1.00 67.34  ? 608  GLU A CB    1 
ATOM   4611  C  CG    . GLU A 1 608  ? 151.322 172.080 87.727  1.00 75.46  ? 608  GLU A CG    1 
ATOM   4612  C  CD    . GLU A 1 608  ? 152.746 172.577 87.814  1.00 88.45  ? 608  GLU A CD    1 
ATOM   4613  O  OE1   . GLU A 1 608  ? 153.285 172.641 88.939  1.00 87.57  ? 608  GLU A OE1   1 
ATOM   4614  O  OE2   . GLU A 1 608  ? 153.326 172.903 86.758  1.00 91.91  ? 608  GLU A OE2   1 
ATOM   4615  N  N     . HIS A 1 609  ? 149.579 168.367 89.917  1.00 57.06  ? 609  HIS A N     1 
ATOM   4616  C  CA    . HIS A 1 609  ? 149.585 167.009 90.440  1.00 52.74  ? 609  HIS A CA    1 
ATOM   4617  C  C     . HIS A 1 609  ? 148.493 166.169 89.797  1.00 51.17  ? 609  HIS A C     1 
ATOM   4618  O  O     . HIS A 1 609  ? 148.670 164.961 89.607  1.00 55.23  ? 609  HIS A O     1 
ATOM   4619  C  CB    . HIS A 1 609  ? 149.403 167.038 91.956  1.00 49.95  ? 609  HIS A CB    1 
ATOM   4620  C  CG    . HIS A 1 609  ? 150.528 167.700 92.688  1.00 51.07  ? 609  HIS A CG    1 
ATOM   4621  N  ND1   . HIS A 1 609  ? 151.511 168.422 92.047  1.00 53.06  ? 609  HIS A ND1   1 
ATOM   4622  C  CD2   . HIS A 1 609  ? 150.824 167.753 94.007  1.00 51.67  ? 609  HIS A CD2   1 
ATOM   4623  C  CE1   . HIS A 1 609  ? 152.365 168.889 92.939  1.00 53.39  ? 609  HIS A CE1   1 
ATOM   4624  N  NE2   . HIS A 1 609  ? 151.971 168.497 94.136  1.00 53.59  ? 609  HIS A NE2   1 
ATOM   4625  N  N     . LEU A 1 610  ? 147.362 166.790 89.459  1.00 50.18  ? 610  LEU A N     1 
ATOM   4626  C  CA    . LEU A 1 610  ? 146.278 166.070 88.803  1.00 50.29  ? 610  LEU A CA    1 
ATOM   4627  C  C     . LEU A 1 610  ? 146.619 165.721 87.362  1.00 56.53  ? 610  LEU A C     1 
ATOM   4628  O  O     . LEU A 1 610  ? 146.084 164.748 86.823  1.00 60.04  ? 610  LEU A O     1 
ATOM   4629  C  CB    . LEU A 1 610  ? 144.993 166.894 88.851  1.00 54.36  ? 610  LEU A CB    1 
ATOM   4630  C  CG    . LEU A 1 610  ? 144.019 166.656 90.006  1.00 50.79  ? 610  LEU A CG    1 
ATOM   4631  C  CD1   . LEU A 1 610  ? 144.653 166.941 91.356  1.00 47.52  ? 610  LEU A CD1   1 
ATOM   4632  C  CD2   . LEU A 1 610  ? 142.773 167.499 89.809  1.00 48.54  ? 610  LEU A CD2   1 
ATOM   4633  N  N     . LYS A 1 611  ? 147.490 166.503 86.719  1.00 60.16  ? 611  LYS A N     1 
ATOM   4634  C  CA    . LYS A 1 611  ? 147.841 166.202 85.333  1.00 60.35  ? 611  LYS A CA    1 
ATOM   4635  C  C     . LYS A 1 611  ? 148.575 164.870 85.209  1.00 57.26  ? 611  LYS A C     1 
ATOM   4636  O  O     . LYS A 1 611  ? 148.372 164.136 84.236  1.00 60.86  ? 611  LYS A O     1 
ATOM   4637  C  CB    . LYS A 1 611  ? 148.674 167.330 84.729  1.00 62.93  ? 611  LYS A CB    1 
ATOM   4638  C  CG    . LYS A 1 611  ? 147.870 168.572 84.408  1.00 68.20  ? 611  LYS A CG    1 
ATOM   4639  C  CD    . LYS A 1 611  ? 148.764 169.748 84.061  1.00 75.17  ? 611  LYS A CD    1 
ATOM   4640  C  CE    . LYS A 1 611  ? 147.953 171.028 83.943  1.00 79.61  ? 611  LYS A CE    1 
ATOM   4641  N  NZ    . LYS A 1 611  ? 148.809 172.221 83.704  1.00 78.62  ? 611  LYS A NZ    1 
ATOM   4642  N  N     . LYS A 1 612  ? 149.431 164.539 86.172  1.00 55.63  ? 612  LYS A N     1 
ATOM   4643  C  CA    . LYS A 1 612  ? 150.228 163.320 86.100  1.00 55.69  ? 612  LYS A CA    1 
ATOM   4644  C  C     . LYS A 1 612  ? 149.551 162.114 86.740  1.00 56.81  ? 612  LYS A C     1 
ATOM   4645  O  O     . LYS A 1 612  ? 150.178 161.057 86.847  1.00 62.04  ? 612  LYS A O     1 
ATOM   4646  C  CB    . LYS A 1 612  ? 151.597 163.531 86.748  1.00 55.39  ? 612  LYS A CB    1 
ATOM   4647  C  CG    . LYS A 1 612  ? 152.679 163.957 85.779  1.00 61.39  ? 612  LYS A CG    1 
ATOM   4648  C  CD    . LYS A 1 612  ? 153.905 163.075 85.931  1.00 67.12  ? 612  LYS A CD    1 
ATOM   4649  C  CE    . LYS A 1 612  ? 153.824 161.885 84.987  1.00 68.58  ? 612  LYS A CE    1 
ATOM   4650  N  NZ    . LYS A 1 612  ? 154.967 160.944 85.139  1.00 62.12  ? 612  LYS A NZ    1 
ATOM   4651  N  N     . ALA A 1 613  ? 148.302 162.244 87.171  1.00 56.94  ? 613  ALA A N     1 
ATOM   4652  C  CA    . ALA A 1 613  ? 147.590 161.141 87.798  1.00 51.99  ? 613  ALA A CA    1 
ATOM   4653  C  C     . ALA A 1 613  ? 146.830 160.327 86.759  1.00 57.25  ? 613  ALA A C     1 
ATOM   4654  O  O     . ALA A 1 613  ? 146.256 160.879 85.816  1.00 55.92  ? 613  ALA A O     1 
ATOM   4655  C  CB    . ALA A 1 613  ? 146.626 161.661 88.863  1.00 46.88  ? 613  ALA A CB    1 
ATOM   4656  N  N     . ASP A 1 614  ? 146.846 159.003 86.931  1.00 55.06  ? 614  ASP A N     1 
ATOM   4657  C  CA    . ASP A 1 614  ? 146.087 158.128 86.042  1.00 54.24  ? 614  ASP A CA    1 
ATOM   4658  C  C     . ASP A 1 614  ? 144.585 158.290 86.247  1.00 56.86  ? 614  ASP A C     1 
ATOM   4659  O  O     . ASP A 1 614  ? 143.818 158.291 85.278  1.00 58.06  ? 614  ASP A O     1 
ATOM   4660  C  CB    . ASP A 1 614  ? 146.502 156.673 86.256  1.00 56.49  ? 614  ASP A CB    1 
ATOM   4661  C  CG    . ASP A 1 614  ? 147.976 156.444 85.999  1.00 65.51  ? 614  ASP A CG    1 
ATOM   4662  O  OD1   . ASP A 1 614  ? 148.789 156.685 86.916  1.00 61.43  ? 614  ASP A OD1   1 
ATOM   4663  O  OD2   . ASP A 1 614  ? 148.323 156.025 84.875  1.00 70.34  ? 614  ASP A OD2   1 
ATOM   4664  N  N     . LYS A 1 615  ? 144.147 158.421 87.496  1.00 54.71  ? 615  LYS A N     1 
ATOM   4665  C  CA    . LYS A 1 615  ? 142.739 158.552 87.831  1.00 51.24  ? 615  LYS A CA    1 
ATOM   4666  C  C     . LYS A 1 615  ? 142.557 159.710 88.799  1.00 50.41  ? 615  LYS A C     1 
ATOM   4667  O  O     . LYS A 1 615  ? 143.459 160.039 89.572  1.00 52.13  ? 615  LYS A O     1 
ATOM   4668  C  CB    . LYS A 1 615  ? 142.182 157.266 88.453  1.00 55.33  ? 615  LYS A CB    1 
ATOM   4669  C  CG    . LYS A 1 615  ? 141.926 156.142 87.465  1.00 56.18  ? 615  LYS A CG    1 
ATOM   4670  C  CD    . LYS A 1 615  ? 140.822 156.513 86.496  1.00 62.91  ? 615  LYS A CD    1 
ATOM   4671  C  CE    . LYS A 1 615  ? 140.432 155.337 85.623  1.00 64.42  ? 615  LYS A CE    1 
ATOM   4672  N  NZ    . LYS A 1 615  ? 139.357 155.706 84.664  1.00 69.43  ? 615  LYS A NZ    1 
ATOM   4673  N  N     . ILE A 1 616  ? 141.383 160.333 88.743  1.00 50.53  ? 616  ILE A N     1 
ATOM   4674  C  CA    . ILE A 1 616  ? 141.055 161.472 89.589  1.00 49.87  ? 616  ILE A CA    1 
ATOM   4675  C  C     . ILE A 1 616  ? 139.708 161.216 90.248  1.00 48.63  ? 616  ILE A C     1 
ATOM   4676  O  O     . ILE A 1 616  ? 138.745 160.840 89.572  1.00 50.55  ? 616  ILE A O     1 
ATOM   4677  C  CB    . ILE A 1 616  ? 141.028 162.785 88.785  1.00 48.61  ? 616  ILE A CB    1 
ATOM   4678  C  CG1   . ILE A 1 616  ? 142.430 163.133 88.289  1.00 47.67  ? 616  ILE A CG1   1 
ATOM   4679  C  CG2   . ILE A 1 616  ? 140.476 163.920 89.625  1.00 48.29  ? 616  ILE A CG2   1 
ATOM   4680  C  CD1   . ILE A 1 616  ? 142.451 164.246 87.278  1.00 54.05  ? 616  ILE A CD1   1 
ATOM   4681  N  N     . LEU A 1 617  ? 139.644 161.408 91.563  1.00 42.97  ? 617  LEU A N     1 
ATOM   4682  C  CA    . LEU A 1 617  ? 138.404 161.312 92.321  1.00 42.35  ? 617  LEU A CA    1 
ATOM   4683  C  C     . LEU A 1 617  ? 138.175 162.623 93.054  1.00 44.82  ? 617  LEU A C     1 
ATOM   4684  O  O     . LEU A 1 617  ? 139.031 163.061 93.828  1.00 46.32  ? 617  LEU A O     1 
ATOM   4685  C  CB    . LEU A 1 617  ? 138.449 160.155 93.320  1.00 42.39  ? 617  LEU A CB    1 
ATOM   4686  C  CG    . LEU A 1 617  ? 137.203 159.963 94.188  1.00 42.17  ? 617  LEU A CG    1 
ATOM   4687  C  CD1   . LEU A 1 617  ? 135.989 159.663 93.329  1.00 46.24  ? 617  LEU A CD1   1 
ATOM   4688  C  CD2   . LEU A 1 617  ? 137.417 158.868 95.214  1.00 41.01  ? 617  LEU A CD2   1 
ATOM   4689  N  N     . ILE A 1 618  ? 137.022 163.239 92.820  1.00 45.35  ? 618  ILE A N     1 
ATOM   4690  C  CA    . ILE A 1 618  ? 136.667 164.512 93.435  1.00 46.08  ? 618  ILE A CA    1 
ATOM   4691  C  C     . ILE A 1 618  ? 135.477 164.276 94.352  1.00 47.10  ? 618  ILE A C     1 
ATOM   4692  O  O     . ILE A 1 618  ? 134.437 163.767 93.915  1.00 49.54  ? 618  ILE A O     1 
ATOM   4693  C  CB    . ILE A 1 618  ? 136.351 165.584 92.382  1.00 46.85  ? 618  ILE A CB    1 
ATOM   4694  C  CG1   . ILE A 1 618  ? 137.521 165.746 91.412  1.00 42.39  ? 618  ILE A CG1   1 
ATOM   4695  C  CG2   . ILE A 1 618  ? 136.038 166.907 93.048  1.00 45.49  ? 618  ILE A CG2   1 
ATOM   4696  C  CD1   . ILE A 1 618  ? 137.252 166.727 90.300  1.00 41.22  ? 618  ILE A CD1   1 
ATOM   4697  N  N     . LEU A 1 619  ? 135.628 164.645 95.618  1.00 43.66  ? 619  LEU A N     1 
ATOM   4698  C  CA    . LEU A 1 619  ? 134.581 164.491 96.615  1.00 43.20  ? 619  LEU A CA    1 
ATOM   4699  C  C     . LEU A 1 619  ? 133.908 165.830 96.882  1.00 49.90  ? 619  LEU A C     1 
ATOM   4700  O  O     . LEU A 1 619  ? 134.532 166.889 96.789  1.00 51.24  ? 619  LEU A O     1 
ATOM   4701  C  CB    . LEU A 1 619  ? 135.151 163.930 97.917  1.00 39.59  ? 619  LEU A CB    1 
ATOM   4702  C  CG    . LEU A 1 619  ? 135.734 162.520 97.851  1.00 37.87  ? 619  LEU A CG    1 
ATOM   4703  C  CD1   . LEU A 1 619  ? 136.341 162.137 99.186  1.00 33.74  ? 619  LEU A CD1   1 
ATOM   4704  C  CD2   . LEU A 1 619  ? 134.674 161.519 97.432  1.00 43.09  ? 619  LEU A CD2   1 
ATOM   4705  N  N     . HIS A 1 620  ? 132.618 165.774 97.211  1.00 49.03  ? 620  HIS A N     1 
ATOM   4706  C  CA    . HIS A 1 620  ? 131.866 166.980 97.555  1.00 51.18  ? 620  HIS A CA    1 
ATOM   4707  C  C     . HIS A 1 620  ? 130.810 166.583 98.583  1.00 54.56  ? 620  HIS A C     1 
ATOM   4708  O  O     . HIS A 1 620  ? 129.782 166.004 98.223  1.00 57.14  ? 620  HIS A O     1 
ATOM   4709  C  CB    . HIS A 1 620  ? 131.237 167.612 96.322  1.00 53.96  ? 620  HIS A CB    1 
ATOM   4710  C  CG    . HIS A 1 620  ? 130.524 168.896 96.603  1.00 60.31  ? 620  HIS A CG    1 
ATOM   4711  N  ND1   . HIS A 1 620  ? 131.123 169.956 97.248  1.00 62.07  ? 620  HIS A ND1   1 
ATOM   4712  C  CD2   . HIS A 1 620  ? 129.256 169.288 96.333  1.00 60.64  ? 620  HIS A CD2   1 
ATOM   4713  C  CE1   . HIS A 1 620  ? 130.256 170.947 97.359  1.00 62.68  ? 620  HIS A CE1   1 
ATOM   4714  N  NE2   . HIS A 1 620  ? 129.116 170.567 96.813  1.00 65.12  ? 620  HIS A NE2   1 
ATOM   4715  N  N     . GLU A 1 621  ? 131.072 166.903 99.850  1.00 53.23  ? 621  GLU A N     1 
ATOM   4716  C  CA    . GLU A 1 621  ? 130.182 166.554 100.959 1.00 52.81  ? 621  GLU A CA    1 
ATOM   4717  C  C     . GLU A 1 621  ? 129.935 165.049 101.027 1.00 54.39  ? 621  GLU A C     1 
ATOM   4718  O  O     . GLU A 1 621  ? 128.820 164.594 101.287 1.00 56.44  ? 621  GLU A O     1 
ATOM   4719  C  CB    . GLU A 1 621  ? 128.861 167.319 100.874 1.00 59.81  ? 621  GLU A CB    1 
ATOM   4720  C  CG    . GLU A 1 621  ? 128.753 168.472 101.856 1.00 67.98  ? 621  GLU A CG    1 
ATOM   4721  C  CD    . GLU A 1 621  ? 128.037 169.671 101.273 1.00 71.42  ? 621  GLU A CD    1 
ATOM   4722  O  OE1   . GLU A 1 621  ? 128.335 170.805 101.701 1.00 71.64  ? 621  GLU A OE1   1 
ATOM   4723  O  OE2   . GLU A 1 621  ? 127.180 169.480 100.386 1.00 69.30  ? 621  GLU A OE2   1 
ATOM   4724  N  N     . GLY A 1 622  ? 130.986 164.266 100.793 1.00 53.80  ? 622  GLY A N     1 
ATOM   4725  C  CA    . GLY A 1 622  ? 130.893 162.825 100.888 1.00 50.83  ? 622  GLY A CA    1 
ATOM   4726  C  C     . GLY A 1 622  ? 130.310 162.129 99.682  1.00 51.95  ? 622  GLY A C     1 
ATOM   4727  O  O     . GLY A 1 622  ? 130.035 160.926 99.757  1.00 52.09  ? 622  GLY A O     1 
ATOM   4728  N  N     . SER A 1 623  ? 130.102 162.838 98.578  1.00 52.88  ? 623  SER A N     1 
ATOM   4729  C  CA    . SER A 1 623  ? 129.553 162.262 97.361  1.00 50.24  ? 623  SER A CA    1 
ATOM   4730  C  C     . SER A 1 623  ? 130.577 162.360 96.240  1.00 49.86  ? 623  SER A C     1 
ATOM   4731  O  O     . SER A 1 623  ? 131.367 163.307 96.192  1.00 53.62  ? 623  SER A O     1 
ATOM   4732  C  CB    . SER A 1 623  ? 128.258 162.967 96.953  1.00 53.16  ? 623  SER A CB    1 
ATOM   4733  O  OG    . SER A 1 623  ? 127.222 162.698 97.880  1.00 60.27  ? 623  SER A OG    1 
ATOM   4734  N  N     . SER A 1 624  ? 130.563 161.378 95.344  1.00 49.73  ? 624  SER A N     1 
ATOM   4735  C  CA    . SER A 1 624  ? 131.500 161.334 94.224  1.00 50.46  ? 624  SER A CA    1 
ATOM   4736  C  C     . SER A 1 624  ? 131.071 162.353 93.177  1.00 50.26  ? 624  SER A C     1 
ATOM   4737  O  O     . SER A 1 624  ? 130.198 162.085 92.350  1.00 48.55  ? 624  SER A O     1 
ATOM   4738  C  CB    . SER A 1 624  ? 131.560 159.930 93.635  1.00 51.00  ? 624  SER A CB    1 
ATOM   4739  O  OG    . SER A 1 624  ? 132.482 159.862 92.563  1.00 48.59  ? 624  SER A OG    1 
ATOM   4740  N  N     . TYR A 1 625  ? 131.682 163.539 93.216  1.00 51.56  ? 625  TYR A N     1 
ATOM   4741  C  CA    . TYR A 1 625  ? 131.350 164.574 92.243  1.00 51.79  ? 625  TYR A CA    1 
ATOM   4742  C  C     . TYR A 1 625  ? 131.891 164.230 90.859  1.00 53.46  ? 625  TYR A C     1 
ATOM   4743  O  O     . TYR A 1 625  ? 131.254 164.539 89.846  1.00 52.33  ? 625  TYR A O     1 
ATOM   4744  C  CB    . TYR A 1 625  ? 131.886 165.925 92.717  1.00 52.66  ? 625  TYR A CB    1 
ATOM   4745  C  CG    . TYR A 1 625  ? 131.777 167.037 91.699  1.00 55.56  ? 625  TYR A CG    1 
ATOM   4746  C  CD1   . TYR A 1 625  ? 130.540 167.499 91.279  1.00 57.95  ? 625  TYR A CD1   1 
ATOM   4747  C  CD2   . TYR A 1 625  ? 132.913 167.627 91.166  1.00 54.81  ? 625  TYR A CD2   1 
ATOM   4748  C  CE1   . TYR A 1 625  ? 130.436 168.516 90.353  1.00 62.02  ? 625  TYR A CE1   1 
ATOM   4749  C  CE2   . TYR A 1 625  ? 132.819 168.645 90.239  1.00 59.68  ? 625  TYR A CE2   1 
ATOM   4750  C  CZ    . TYR A 1 625  ? 131.579 169.085 89.837  1.00 67.95  ? 625  TYR A CZ    1 
ATOM   4751  O  OH    . TYR A 1 625  ? 131.482 170.099 88.914  1.00 72.42  ? 625  TYR A OH    1 
ATOM   4752  N  N     . PHE A 1 626  ? 133.063 163.603 90.793  1.00 50.46  ? 626  PHE A N     1 
ATOM   4753  C  CA    . PHE A 1 626  ? 133.656 163.224 89.518  1.00 49.69  ? 626  PHE A CA    1 
ATOM   4754  C  C     . PHE A 1 626  ? 134.596 162.047 89.725  1.00 53.56  ? 626  PHE A C     1 
ATOM   4755  O  O     . PHE A 1 626  ? 135.295 161.974 90.738  1.00 54.34  ? 626  PHE A O     1 
ATOM   4756  C  CB    . PHE A 1 626  ? 134.416 164.394 88.885  1.00 51.57  ? 626  PHE A CB    1 
ATOM   4757  C  CG    . PHE A 1 626  ? 135.167 164.028 87.636  1.00 52.05  ? 626  PHE A CG    1 
ATOM   4758  C  CD1   . PHE A 1 626  ? 134.515 163.931 86.422  1.00 52.25  ? 626  PHE A CD1   1 
ATOM   4759  C  CD2   . PHE A 1 626  ? 136.529 163.782 87.680  1.00 55.44  ? 626  PHE A CD2   1 
ATOM   4760  C  CE1   . PHE A 1 626  ? 135.206 163.594 85.276  1.00 55.72  ? 626  PHE A CE1   1 
ATOM   4761  C  CE2   . PHE A 1 626  ? 137.225 163.445 86.539  1.00 56.61  ? 626  PHE A CE2   1 
ATOM   4762  C  CZ    . PHE A 1 626  ? 136.563 163.351 85.336  1.00 58.59  ? 626  PHE A CZ    1 
ATOM   4763  N  N     . TYR A 1 627  ? 134.612 161.135 88.755  1.00 54.73  ? 627  TYR A N     1 
ATOM   4764  C  CA    . TYR A 1 627  ? 135.579 160.046 88.735  1.00 53.68  ? 627  TYR A CA    1 
ATOM   4765  C  C     . TYR A 1 627  ? 135.945 159.745 87.290  1.00 54.91  ? 627  TYR A C     1 
ATOM   4766  O  O     . TYR A 1 627  ? 135.060 159.478 86.472  1.00 54.61  ? 627  TYR A O     1 
ATOM   4767  C  CB    . TYR A 1 627  ? 135.025 158.788 89.408  1.00 54.80  ? 627  TYR A CB    1 
ATOM   4768  C  CG    . TYR A 1 627  ? 135.974 157.612 89.357  1.00 55.21  ? 627  TYR A CG    1 
ATOM   4769  C  CD1   . TYR A 1 627  ? 137.178 157.641 90.043  1.00 53.94  ? 627  TYR A CD1   1 
ATOM   4770  C  CD2   . TYR A 1 627  ? 135.677 156.488 88.602  1.00 52.26  ? 627  TYR A CD2   1 
ATOM   4771  C  CE1   . TYR A 1 627  ? 138.051 156.577 89.993  1.00 54.62  ? 627  TYR A CE1   1 
ATOM   4772  C  CE2   . TYR A 1 627  ? 136.545 155.420 88.546  1.00 54.70  ? 627  TYR A CE2   1 
ATOM   4773  C  CZ    . TYR A 1 627  ? 137.730 155.470 89.242  1.00 57.20  ? 627  TYR A CZ    1 
ATOM   4774  O  OH    . TYR A 1 627  ? 138.596 154.406 89.188  1.00 58.63  ? 627  TYR A OH    1 
ATOM   4775  N  N     . GLY A 1 628  ? 137.235 159.777 86.983  1.00 55.91  ? 628  GLY A N     1 
ATOM   4776  C  CA    . GLY A 1 628  ? 137.679 159.518 85.627  1.00 59.95  ? 628  GLY A CA    1 
ATOM   4777  C  C     . GLY A 1 628  ? 139.088 160.042 85.407  1.00 64.63  ? 628  GLY A C     1 
ATOM   4778  O  O     . GLY A 1 628  ? 139.826 160.295 86.355  1.00 62.18  ? 628  GLY A O     1 
ATOM   4779  N  N     . THR A 1 629  ? 139.433 160.186 84.131  1.00 68.45  ? 629  THR A N     1 
ATOM   4780  C  CA    . THR A 1 629  ? 140.752 160.624 83.699  1.00 69.32  ? 629  THR A CA    1 
ATOM   4781  C  C     . THR A 1 629  ? 140.770 162.144 83.530  1.00 72.50  ? 629  THR A C     1 
ATOM   4782  O  O     . THR A 1 629  ? 139.737 162.779 83.312  1.00 75.84  ? 629  THR A O     1 
ATOM   4783  C  CB    . THR A 1 629  ? 141.125 159.916 82.390  1.00 67.18  ? 629  THR A CB    1 
ATOM   4784  O  OG1   . THR A 1 629  ? 141.185 158.504 82.619  1.00 68.72  ? 629  THR A OG1   1 
ATOM   4785  C  CG2   . THR A 1 629  ? 142.478 160.365 81.857  1.00 67.33  ? 629  THR A CG2   1 
ATOM   4786  N  N     . PHE A 1 630  ? 141.967 162.727 83.649  1.00 71.65  ? 630  PHE A N     1 
ATOM   4787  C  CA    . PHE A 1 630  ? 142.116 164.169 83.478  1.00 73.56  ? 630  PHE A CA    1 
ATOM   4788  C  C     . PHE A 1 630  ? 141.694 164.629 82.089  1.00 75.81  ? 630  PHE A C     1 
ATOM   4789  O  O     . PHE A 1 630  ? 141.261 165.775 81.923  1.00 77.12  ? 630  PHE A O     1 
ATOM   4790  C  CB    . PHE A 1 630  ? 143.563 164.584 83.740  1.00 74.46  ? 630  PHE A CB    1 
ATOM   4791  C  CG    . PHE A 1 630  ? 143.772 166.070 83.762  1.00 73.76  ? 630  PHE A CG    1 
ATOM   4792  C  CD1   . PHE A 1 630  ? 143.176 166.854 84.733  1.00 71.42  ? 630  PHE A CD1   1 
ATOM   4793  C  CD2   . PHE A 1 630  ? 144.561 166.683 82.806  1.00 72.53  ? 630  PHE A CD2   1 
ATOM   4794  C  CE1   . PHE A 1 630  ? 143.368 168.219 84.754  1.00 73.06  ? 630  PHE A CE1   1 
ATOM   4795  C  CE2   . PHE A 1 630  ? 144.756 168.049 82.822  1.00 75.67  ? 630  PHE A CE2   1 
ATOM   4796  C  CZ    . PHE A 1 630  ? 144.158 168.818 83.799  1.00 76.06  ? 630  PHE A CZ    1 
ATOM   4797  N  N     . SER A 1 631  ? 141.824 163.766 81.080  1.00 76.28  ? 631  SER A N     1 
ATOM   4798  C  CA    . SER A 1 631  ? 141.441 164.155 79.727  1.00 80.37  ? 631  SER A CA    1 
ATOM   4799  C  C     . SER A 1 631  ? 139.951 164.454 79.642  1.00 81.96  ? 631  SER A C     1 
ATOM   4800  O  O     . SER A 1 631  ? 139.537 165.407 78.972  1.00 83.15  ? 631  SER A O     1 
ATOM   4801  C  CB    . SER A 1 631  ? 141.827 163.060 78.734  1.00 79.39  ? 631  SER A CB    1 
ATOM   4802  O  OG    . SER A 1 631  ? 143.231 163.022 78.546  1.00 83.56  ? 631  SER A OG    1 
ATOM   4803  N  N     . GLU A 1 632  ? 139.130 163.655 80.318  1.00 80.02  ? 632  GLU A N     1 
ATOM   4804  C  CA    . GLU A 1 632  ? 137.691 163.863 80.331  1.00 80.74  ? 632  GLU A CA    1 
ATOM   4805  C  C     . GLU A 1 632  ? 137.224 164.728 81.492  1.00 79.97  ? 632  GLU A C     1 
ATOM   4806  O  O     . GLU A 1 632  ? 136.023 164.997 81.598  1.00 81.69  ? 632  GLU A O     1 
ATOM   4807  C  CB    . GLU A 1 632  ? 136.970 162.513 80.356  1.00 81.83  ? 632  GLU A CB    1 
ATOM   4808  C  CG    . GLU A 1 632  ? 137.425 161.586 81.462  1.00 80.23  ? 632  GLU A CG    1 
ATOM   4809  C  CD    . GLU A 1 632  ? 136.918 160.174 81.274  1.00 82.65  ? 632  GLU A CD    1 
ATOM   4810  O  OE1   . GLU A 1 632  ? 137.405 159.493 80.348  1.00 83.03  ? 632  GLU A OE1   1 
ATOM   4811  O  OE2   . GLU A 1 632  ? 136.043 159.740 82.053  1.00 81.42  ? 632  GLU A OE2   1 
ATOM   4812  N  N     . LEU A 1 633  ? 138.134 165.161 82.367  1.00 78.38  ? 633  LEU A N     1 
ATOM   4813  C  CA    . LEU A 1 633  ? 137.775 166.167 83.362  1.00 76.14  ? 633  LEU A CA    1 
ATOM   4814  C  C     . LEU A 1 633  ? 137.542 167.523 82.711  1.00 77.84  ? 633  LEU A C     1 
ATOM   4815  O  O     . LEU A 1 633  ? 136.610 168.245 83.082  1.00 75.69  ? 633  LEU A O     1 
ATOM   4816  C  CB    . LEU A 1 633  ? 138.866 166.271 84.428  1.00 73.66  ? 633  LEU A CB    1 
ATOM   4817  C  CG    . LEU A 1 633  ? 138.675 167.348 85.500  1.00 68.92  ? 633  LEU A CG    1 
ATOM   4818  C  CD1   . LEU A 1 633  ? 137.331 167.208 86.195  1.00 65.43  ? 633  LEU A CD1   1 
ATOM   4819  C  CD2   . LEU A 1 633  ? 139.811 167.319 86.511  1.00 67.26  ? 633  LEU A CD2   1 
ATOM   4820  N  N     . GLN A 1 634  ? 138.373 167.883 81.737  1.00 83.80  ? 634  GLN A N     1 
ATOM   4821  C  CA    . GLN A 1 634  ? 138.301 169.185 81.090  1.00 89.44  ? 634  GLN A CA    1 
ATOM   4822  C  C     . GLN A 1 634  ? 137.244 169.254 79.992  1.00 88.41  ? 634  GLN A C     1 
ATOM   4823  O  O     . GLN A 1 634  ? 137.259 170.202 79.200  1.00 86.99  ? 634  GLN A O     1 
ATOM   4824  C  CB    . GLN A 1 634  ? 139.675 169.563 80.530  1.00 90.60  ? 634  GLN A CB    1 
ATOM   4825  C  CG    . GLN A 1 634  ? 140.218 168.612 79.485  1.00 92.89  ? 634  GLN A CG    1 
ATOM   4826  C  CD    . GLN A 1 634  ? 141.576 169.043 78.973  1.00 101.60 ? 634  GLN A CD    1 
ATOM   4827  O  OE1   . GLN A 1 634  ? 142.283 169.805 79.631  1.00 102.20 ? 634  GLN A OE1   1 
ATOM   4828  N  NE2   . GLN A 1 634  ? 141.950 168.556 77.796  1.00 104.93 ? 634  GLN A NE2   1 
ATOM   4829  N  N     . ASN A 1 635  ? 136.338 168.284 79.920  1.00 88.52  ? 635  ASN A N     1 
ATOM   4830  C  CA    . ASN A 1 635  ? 135.183 168.377 79.032  1.00 87.27  ? 635  ASN A CA    1 
ATOM   4831  C  C     . ASN A 1 635  ? 133.891 168.417 79.840  1.00 84.54  ? 635  ASN A C     1 
ATOM   4832  O  O     . ASN A 1 635  ? 133.022 167.560 79.682  1.00 82.03  ? 635  ASN A O     1 
ATOM   4833  C  CB    . ASN A 1 635  ? 135.145 167.208 78.043  1.00 88.36  ? 635  ASN A CB    1 
ATOM   4834  C  CG    . ASN A 1 635  ? 136.375 167.145 77.164  1.00 89.00  ? 635  ASN A CG    1 
ATOM   4835  O  OD1   . ASN A 1 635  ? 137.055 166.121 77.098  1.00 89.75  ? 635  ASN A OD1   1 
ATOM   4836  N  ND2   . ASN A 1 635  ? 136.667 168.242 76.477  1.00 85.21  ? 635  ASN A ND2   1 
ATOM   4837  N  N     . ASP A 1 806  ? 163.722 149.528 92.715  1.00 71.74  ? 806  ASP A N     1 
ATOM   4838  C  CA    . ASP A 1 806  ? 165.095 149.043 92.787  1.00 77.37  ? 806  ASP A CA    1 
ATOM   4839  C  C     . ASP A 1 806  ? 165.585 148.980 94.230  1.00 74.11  ? 806  ASP A C     1 
ATOM   4840  O  O     . ASP A 1 806  ? 166.322 148.069 94.606  1.00 71.15  ? 806  ASP A O     1 
ATOM   4841  C  CB    . ASP A 1 806  ? 166.018 149.936 91.960  1.00 79.20  ? 806  ASP A CB    1 
ATOM   4842  C  CG    . ASP A 1 806  ? 167.476 149.538 92.079  1.00 79.65  ? 806  ASP A CG    1 
ATOM   4843  O  OD1   . ASP A 1 806  ? 167.886 148.565 91.411  1.00 78.94  ? 806  ASP A OD1   1 
ATOM   4844  O  OD2   . ASP A 1 806  ? 168.211 150.197 92.843  1.00 74.67  ? 806  ASP A OD2   1 
ATOM   4845  N  N     . ILE A 1 807  ? 165.167 149.955 95.039  1.00 70.92  ? 807  ILE A N     1 
ATOM   4846  C  CA    . ILE A 1 807  ? 165.615 149.997 96.426  1.00 67.57  ? 807  ILE A CA    1 
ATOM   4847  C  C     . ILE A 1 807  ? 164.856 148.991 97.284  1.00 70.35  ? 807  ILE A C     1 
ATOM   4848  O  O     . ILE A 1 807  ? 165.366 148.539 98.316  1.00 68.79  ? 807  ILE A O     1 
ATOM   4849  C  CB    . ILE A 1 807  ? 165.495 151.428 96.982  1.00 61.82  ? 807  ILE A CB    1 
ATOM   4850  C  CG1   . ILE A 1 807  ? 164.030 151.831 97.139  1.00 62.73  ? 807  ILE A CG1   1 
ATOM   4851  C  CG2   . ILE A 1 807  ? 166.208 152.409 96.074  1.00 61.25  ? 807  ILE A CG2   1 
ATOM   4852  C  CD1   . ILE A 1 807  ? 163.840 153.185 97.785  1.00 55.37  ? 807  ILE A CD1   1 
ATOM   4853  N  N     . TYR A 1 808  ? 163.642 148.620 96.887  1.00 71.25  ? 808  TYR A N     1 
ATOM   4854  C  CA    . TYR A 1 808  ? 162.826 147.694 97.674  1.00 71.47  ? 808  TYR A CA    1 
ATOM   4855  C  C     . TYR A 1 808  ? 163.125 146.240 97.322  1.00 78.69  ? 808  TYR A C     1 
ATOM   4856  O  O     . TYR A 1 808  ? 162.229 145.462 96.998  1.00 77.21  ? 808  TYR A O     1 
ATOM   4857  C  CB    . TYR A 1 808  ? 161.347 148.001 97.473  1.00 67.30  ? 808  TYR A CB    1 
ATOM   4858  C  CG    . TYR A 1 808  ? 160.937 149.410 97.836  1.00 64.38  ? 808  TYR A CG    1 
ATOM   4859  C  CD1   . TYR A 1 808  ? 160.943 149.840 99.154  1.00 60.21  ? 808  TYR A CD1   1 
ATOM   4860  C  CD2   . TYR A 1 808  ? 160.533 150.306 96.857  1.00 61.63  ? 808  TYR A CD2   1 
ATOM   4861  C  CE1   . TYR A 1 808  ? 160.566 151.126 99.486  1.00 57.18  ? 808  TYR A CE1   1 
ATOM   4862  C  CE2   . TYR A 1 808  ? 160.153 151.592 97.181  1.00 59.23  ? 808  TYR A CE2   1 
ATOM   4863  C  CZ    . TYR A 1 808  ? 160.171 151.997 98.496  1.00 60.14  ? 808  TYR A CZ    1 
ATOM   4864  O  OH    . TYR A 1 808  ? 159.793 153.277 98.819  1.00 59.29  ? 808  TYR A OH    1 
ATOM   4865  N  N     . SER A 1 809  ? 164.399 145.859 97.388  1.00 83.68  ? 809  SER A N     1 
ATOM   4866  C  CA    . SER A 1 809  ? 164.805 144.499 97.054  1.00 86.17  ? 809  SER A CA    1 
ATOM   4867  C  C     . SER A 1 809  ? 164.841 143.591 98.278  1.00 91.08  ? 809  SER A C     1 
ATOM   4868  O  O     . SER A 1 809  ? 164.277 142.492 98.259  1.00 90.88  ? 809  SER A O     1 
ATOM   4869  C  CB    . SER A 1 809  ? 166.175 144.514 96.372  1.00 79.19  ? 809  SER A CB    1 
ATOM   4870  O  OG    . SER A 1 809  ? 166.527 143.222 95.910  1.00 85.61  ? 809  SER A OG    1 
ATOM   4871  N  N     . ARG A 1 810  ? 165.496 144.037 99.344  1.00 94.20  ? 810  ARG A N     1 
ATOM   4872  C  CA    . ARG A 1 810  ? 165.717 143.203 100.514 1.00 95.01  ? 810  ARG A CA    1 
ATOM   4873  C  C     . ARG A 1 810  ? 164.508 143.240 101.441 1.00 93.26  ? 810  ARG A C     1 
ATOM   4874  O  O     . ARG A 1 810  ? 163.786 144.238 101.517 1.00 92.37  ? 810  ARG A O     1 
ATOM   4875  C  CB    . ARG A 1 810  ? 166.965 143.673 101.259 1.00 90.17  ? 810  ARG A CB    1 
ATOM   4876  C  CG    . ARG A 1 810  ? 168.249 143.423 100.490 1.00 90.63  ? 810  ARG A CG    1 
ATOM   4877  C  CD    . ARG A 1 810  ? 169.380 144.315 100.979 1.00 87.87  ? 810  ARG A CD    1 
ATOM   4878  N  NE    . ARG A 1 810  ? 169.521 144.324 102.431 1.00 94.82  ? 810  ARG A NE    1 
ATOM   4879  C  CZ    . ARG A 1 810  ? 169.829 143.266 103.168 1.00 102.63 ? 810  ARG A CZ    1 
ATOM   4880  N  NH1   . ARG A 1 810  ? 170.077 142.087 102.620 1.00 104.43 ? 810  ARG A NH1   1 
ATOM   4881  N  NH2   . ARG A 1 810  ? 169.910 143.398 104.489 1.00 98.39  ? 810  ARG A NH2   1 
ATOM   4882  N  N     . ARG A 1 811  ? 164.280 142.129 102.140 1.00 90.79  ? 811  ARG A N     1 
ATOM   4883  C  CA    . ARG A 1 811  ? 163.200 142.031 103.120 1.00 93.92  ? 811  ARG A CA    1 
ATOM   4884  C  C     . ARG A 1 811  ? 163.805 142.301 104.493 1.00 88.80  ? 811  ARG A C     1 
ATOM   4885  O  O     . ARG A 1 811  ? 164.419 141.420 105.099 1.00 89.12  ? 811  ARG A O     1 
ATOM   4886  C  CB    . ARG A 1 811  ? 162.510 140.671 103.055 1.00 99.09  ? 811  ARG A CB    1 
ATOM   4887  C  CG    . ARG A 1 811  ? 161.880 140.378 101.699 1.00 100.27 ? 811  ARG A CG    1 
ATOM   4888  C  CD    . ARG A 1 811  ? 160.747 139.359 101.762 1.00 102.38 ? 811  ARG A CD    1 
ATOM   4889  N  NE    . ARG A 1 811  ? 161.198 137.997 102.013 1.00 111.02 ? 811  ARG A NE    1 
ATOM   4890  C  CZ    . ARG A 1 811  ? 161.000 137.346 103.151 1.00 114.40 ? 811  ARG A CZ    1 
ATOM   4891  N  NH1   . ARG A 1 811  ? 160.345 137.900 104.159 1.00 112.27 ? 811  ARG A NH1   1 
ATOM   4892  N  NH2   . ARG A 1 811  ? 161.459 136.104 103.277 1.00 114.18 ? 811  ARG A NH2   1 
ATOM   4893  N  N     . LEU A 1 812  ? 163.629 143.523 104.983 1.00 85.23  ? 812  LEU A N     1 
ATOM   4894  C  CA    . LEU A 1 812  ? 164.277 143.957 106.214 1.00 83.50  ? 812  LEU A CA    1 
ATOM   4895  C  C     . LEU A 1 812  ? 163.471 143.603 107.458 1.00 82.22  ? 812  LEU A C     1 
ATOM   4896  O  O     . LEU A 1 812  ? 163.999 143.609 108.570 1.00 80.14  ? 812  LEU A O     1 
ATOM   4897  C  CB    . LEU A 1 812  ? 164.528 145.464 106.174 1.00 73.87  ? 812  LEU A CB    1 
ATOM   4898  C  CG    . LEU A 1 812  ? 165.391 145.985 105.024 1.00 74.86  ? 812  LEU A CG    1 
ATOM   4899  C  CD1   . LEU A 1 812  ? 165.655 147.464 105.210 1.00 63.62  ? 812  LEU A CD1   1 
ATOM   4900  C  CD2   . LEU A 1 812  ? 166.699 145.216 104.927 1.00 77.86  ? 812  LEU A CD2   1 
HETATM 4901  N  N     . SEP A 1 813  ? 162.193 143.300 107.270 1.00 82.64  ? 813  SEP A N     1 
HETATM 4902  C  CA    . SEP A 1 813  ? 161.337 142.924 108.386 1.00 83.51  ? 813  SEP A CA    1 
HETATM 4903  C  CB    . SEP A 1 813  ? 159.864 143.051 108.006 1.00 77.84  ? 813  SEP A CB    1 
HETATM 4904  O  OG    . SEP A 1 813  ? 159.554 144.378 107.623 1.00 76.64  ? 813  SEP A OG    1 
HETATM 4905  C  C     . SEP A 1 813  ? 161.652 141.502 108.830 1.00 91.99  ? 813  SEP A C     1 
HETATM 4906  O  O     . SEP A 1 813  ? 161.531 141.170 110.010 1.00 89.97  ? 813  SEP A O     1 
HETATM 4907  P  P     . SEP A 1 813  ? 157.973 144.512 107.355 1.00 88.78  ? 813  SEP A P     1 
HETATM 4908  O  O1P   . SEP A 1 813  ? 157.563 146.067 107.335 1.00 67.96  ? 813  SEP A O1P   1 
HETATM 4909  O  O2P   . SEP A 1 813  ? 157.597 143.841 105.940 1.00 79.14  ? 813  SEP A O2P   1 
HETATM 4910  O  O3P   . SEP A 1 813  ? 157.170 143.765 108.532 1.00 80.48  ? 813  SEP A O3P   1 
ATOM   4911  N  N     . GLN A 1 814  ? 162.050 140.673 107.868 1.00 97.00  ? 814  GLN A N     1 
ATOM   4912  C  CA    . GLN A 1 814  ? 162.458 139.293 108.121 1.00 97.62  ? 814  GLN A CA    1 
ATOM   4913  C  C     . GLN A 1 814  ? 161.396 138.518 108.894 1.00 98.79  ? 814  GLN A C     1 
ATOM   4914  O  O     . GLN A 1 814  ? 160.209 138.589 108.576 1.00 98.73  ? 814  GLN A O     1 
ATOM   4915  C  CB    . GLN A 1 814  ? 163.789 139.266 108.876 1.00 93.96  ? 814  GLN A CB    1 
ATOM   4916  C  CG    . GLN A 1 814  ? 164.930 139.928 108.126 1.00 90.89  ? 814  GLN A CG    1 
ATOM   4917  C  CD    . GLN A 1 814  ? 166.152 140.144 108.993 1.00 97.05  ? 814  GLN A CD    1 
ATOM   4918  O  OE1   . GLN A 1 814  ? 166.278 139.555 110.066 1.00 101.10 ? 814  GLN A OE1   1 
ATOM   4919  N  NE2   . GLN A 1 814  ? 167.061 140.996 108.532 1.00 92.53  ? 814  GLN A NE2   1 
ATOM   4920  N  N     . ILE A 1 820  ? 163.740 143.103 120.560 1.00 71.05  ? 820  ILE A N     1 
ATOM   4921  C  CA    . ILE A 1 820  ? 165.001 143.799 120.759 1.00 72.37  ? 820  ILE A CA    1 
ATOM   4922  C  C     . ILE A 1 820  ? 165.799 143.001 121.780 1.00 76.39  ? 820  ILE A C     1 
ATOM   4923  O  O     . ILE A 1 820  ? 166.349 141.949 121.459 1.00 81.29  ? 820  ILE A O     1 
ATOM   4924  C  CB    . ILE A 1 820  ? 164.775 145.245 121.214 1.00 68.90  ? 820  ILE A CB    1 
ATOM   4925  C  CG1   . ILE A 1 820  ? 163.763 145.932 120.303 1.00 56.92  ? 820  ILE A CG1   1 
ATOM   4926  C  CG2   . ILE A 1 820  ? 166.072 146.034 121.152 1.00 66.76  ? 820  ILE A CG2   1 
ATOM   4927  C  CD1   . ILE A 1 820  ? 163.188 147.188 120.893 1.00 51.00  ? 820  ILE A CD1   1 
ATOM   4928  N  N     . SER A 1 821  ? 165.868 143.502 123.014 1.00 72.09  ? 821  SER A N     1 
ATOM   4929  C  CA    . SER A 1 821  ? 166.451 142.732 124.108 1.00 69.86  ? 821  SER A CA    1 
ATOM   4930  C  C     . SER A 1 821  ? 165.594 142.686 125.365 1.00 68.41  ? 821  SER A C     1 
ATOM   4931  O  O     . SER A 1 821  ? 165.730 141.728 126.132 1.00 73.97  ? 821  SER A O     1 
ATOM   4932  C  CB    . SER A 1 821  ? 167.834 143.286 124.475 1.00 71.42  ? 821  SER A CB    1 
ATOM   4933  O  OG    . SER A 1 821  ? 168.437 142.508 125.493 1.00 70.48  ? 821  SER A OG    1 
ATOM   4934  N  N     . GLU A 1 822  ? 164.755 143.691 125.624 1.00 63.38  ? 822  GLU A N     1 
ATOM   4935  C  CA    . GLU A 1 822  ? 163.776 143.695 126.709 1.00 56.39  ? 822  GLU A CA    1 
ATOM   4936  C  C     . GLU A 1 822  ? 164.438 143.834 128.078 1.00 56.03  ? 822  GLU A C     1 
ATOM   4937  O  O     . GLU A 1 822  ? 163.757 144.095 129.074 1.00 52.91  ? 822  GLU A O     1 
ATOM   4938  C  CB    . GLU A 1 822  ? 162.914 142.425 126.636 1.00 52.59  ? 822  GLU A CB    1 
ATOM   4939  C  CG    . GLU A 1 822  ? 161.773 142.326 127.629 1.00 50.85  ? 822  GLU A CG    1 
ATOM   4940  C  CD    . GLU A 1 822  ? 162.169 141.567 128.884 1.00 61.60  ? 822  GLU A CD    1 
ATOM   4941  O  OE1   . GLU A 1 822  ? 163.285 141.007 128.910 1.00 65.02  ? 822  GLU A OE1   1 
ATOM   4942  O  OE2   . GLU A 1 822  ? 161.370 141.527 129.842 1.00 53.38  ? 822  GLU A OE2   1 
ATOM   4943  N  N     . GLU A 1 823  ? 165.761 143.725 128.140 1.00 61.82  ? 823  GLU A N     1 
ATOM   4944  C  CA    . GLU A 1 823  ? 166.465 143.965 129.388 1.00 63.38  ? 823  GLU A CA    1 
ATOM   4945  C  C     . GLU A 1 823  ? 167.164 145.317 129.352 1.00 67.20  ? 823  GLU A C     1 
ATOM   4946  O  O     . GLU A 1 823  ? 167.503 145.846 128.293 1.00 71.26  ? 823  GLU A O     1 
ATOM   4947  C  CB    . GLU A 1 823  ? 167.473 142.854 129.686 1.00 66.96  ? 823  GLU A CB    1 
ATOM   4948  C  CG    . GLU A 1 823  ? 168.570 142.681 128.664 1.00 73.02  ? 823  GLU A CG    1 
ATOM   4949  C  CD    . GLU A 1 823  ? 169.699 141.812 129.184 1.00 80.81  ? 823  GLU A CD    1 
ATOM   4950  O  OE1   . GLU A 1 823  ? 170.634 142.362 129.804 1.00 78.11  ? 823  GLU A OE1   1 
ATOM   4951  O  OE2   . GLU A 1 823  ? 169.647 140.580 128.987 1.00 85.03  ? 823  GLU A OE2   1 
ATOM   4952  N  N     . ILE A 1 824  ? 167.385 145.867 130.532 1.00 68.93  ? 824  ILE A N     1 
ATOM   4953  C  CA    . ILE A 1 824  ? 167.939 147.206 130.678 1.00 72.80  ? 824  ILE A CA    1 
ATOM   4954  C  C     . ILE A 1 824  ? 169.452 147.117 130.816 1.00 74.77  ? 824  ILE A C     1 
ATOM   4955  O  O     . ILE A 1 824  ? 169.984 146.234 131.498 1.00 73.08  ? 824  ILE A O     1 
ATOM   4956  C  CB    . ILE A 1 824  ? 167.301 147.935 131.879 1.00 67.40  ? 824  ILE A CB    1 
ATOM   4957  C  CG1   . ILE A 1 824  ? 167.660 147.258 133.207 1.00 57.88  ? 824  ILE A CG1   1 
ATOM   4958  C  CG2   . ILE A 1 824  ? 165.793 148.004 131.712 1.00 57.21  ? 824  ILE A CG2   1 
ATOM   4959  C  CD1   . ILE A 1 824  ? 166.699 146.174 133.650 1.00 50.40  ? 824  ILE A CD1   1 
ATOM   4960  N  N     . ASN A 1 825  ? 170.149 148.020 130.141 1.00 79.98  ? 825  ASN A N     1 
ATOM   4961  C  CA    . ASN A 1 825  ? 171.593 148.162 130.246 1.00 81.70  ? 825  ASN A CA    1 
ATOM   4962  C  C     . ASN A 1 825  ? 171.929 149.520 130.851 1.00 84.41  ? 825  ASN A C     1 
ATOM   4963  O  O     . ASN A 1 825  ? 171.050 150.262 131.299 1.00 86.61  ? 825  ASN A O     1 
ATOM   4964  C  CB    . ASN A 1 825  ? 172.260 147.969 128.880 1.00 86.05  ? 825  ASN A CB    1 
ATOM   4965  C  CG    . ASN A 1 825  ? 171.388 148.433 127.731 1.00 85.26  ? 825  ASN A CG    1 
ATOM   4966  O  OD1   . ASN A 1 825  ? 171.142 149.626 127.561 1.00 84.59  ? 825  ASN A OD1   1 
ATOM   4967  N  ND2   . ASN A 1 825  ? 170.917 147.484 126.930 1.00 81.48  ? 825  ASN A ND2   1 
ATOM   4968  N  N     . GLU A 1 826  ? 173.226 149.837 130.871 1.00 86.57  ? 826  GLU A N     1 
ATOM   4969  C  CA    . GLU A 1 826  ? 173.678 151.079 131.490 1.00 87.13  ? 826  GLU A CA    1 
ATOM   4970  C  C     . GLU A 1 826  ? 173.063 152.304 130.826 1.00 87.74  ? 826  GLU A C     1 
ATOM   4971  O  O     . GLU A 1 826  ? 172.803 153.308 131.500 1.00 82.74  ? 826  GLU A O     1 
ATOM   4972  C  CB    . GLU A 1 826  ? 175.205 151.164 131.442 1.00 86.03  ? 826  GLU A CB    1 
ATOM   4973  C  CG    . GLU A 1 826  ? 175.783 151.244 130.036 1.00 89.53  ? 826  GLU A CG    1 
ATOM   4974  C  CD    . GLU A 1 826  ? 177.279 151.471 130.030 1.00 91.18  ? 826  GLU A CD    1 
ATOM   4975  O  OE1   . GLU A 1 826  ? 177.940 151.113 131.026 1.00 91.26  ? 826  GLU A OE1   1 
ATOM   4976  O  OE2   . GLU A 1 826  ? 177.793 152.015 129.030 1.00 91.77  ? 826  GLU A OE2   1 
ATOM   4977  N  N     . GLU A 1 827  ? 172.819 152.246 129.514 1.00 89.73  ? 827  GLU A N     1 
ATOM   4978  C  CA    . GLU A 1 827  ? 172.301 153.412 128.805 1.00 88.81  ? 827  GLU A CA    1 
ATOM   4979  C  C     . GLU A 1 827  ? 170.904 153.780 129.283 1.00 84.84  ? 827  GLU A C     1 
ATOM   4980  O  O     . GLU A 1 827  ? 170.585 154.965 129.436 1.00 84.20  ? 827  GLU A O     1 
ATOM   4981  C  CB    . GLU A 1 827  ? 172.303 153.158 127.298 1.00 94.00  ? 827  GLU A CB    1 
ATOM   4982  C  CG    . GLU A 1 827  ? 173.672 152.845 126.722 1.00 93.91  ? 827  GLU A CG    1 
ATOM   4983  C  CD    . GLU A 1 827  ? 173.644 151.676 125.761 1.00 95.34  ? 827  GLU A CD    1 
ATOM   4984  O  OE1   . GLU A 1 827  ? 172.929 151.762 124.740 1.00 90.48  ? 827  GLU A OE1   1 
ATOM   4985  O  OE2   . GLU A 1 827  ? 174.335 150.670 126.025 1.00 93.21  ? 827  GLU A OE2   1 
ATOM   4986  N  N     . ASP A 1 828  ? 170.053 152.779 129.519 1.00 84.39  ? 828  ASP A N     1 
ATOM   4987  C  CA    . ASP A 1 828  ? 168.692 153.053 129.966 1.00 86.19  ? 828  ASP A CA    1 
ATOM   4988  C  C     . ASP A 1 828  ? 168.662 153.609 131.384 1.00 85.79  ? 828  ASP A C     1 
ATOM   4989  O  O     . ASP A 1 828  ? 167.830 154.468 131.695 1.00 80.36  ? 828  ASP A O     1 
ATOM   4990  C  CB    . ASP A 1 828  ? 167.850 151.781 129.880 1.00 84.55  ? 828  ASP A CB    1 
ATOM   4991  C  CG    . ASP A 1 828  ? 167.957 151.102 128.531 1.00 84.04  ? 828  ASP A CG    1 
ATOM   4992  O  OD1   . ASP A 1 828  ? 167.884 151.805 127.502 1.00 84.54  ? 828  ASP A OD1   1 
ATOM   4993  O  OD2   . ASP A 1 828  ? 168.111 149.864 128.499 1.00 79.66  ? 828  ASP A OD2   1 
ATOM   4994  N  N     . LEU A 1 829  ? 169.559 153.136 132.250 1.00 85.85  ? 829  LEU A N     1 
ATOM   4995  C  CA    . LEU A 1 829  ? 169.580 153.557 133.645 1.00 81.12  ? 829  LEU A CA    1 
ATOM   4996  C  C     . LEU A 1 829  ? 170.111 154.970 133.831 1.00 79.43  ? 829  LEU A C     1 
ATOM   4997  O  O     . LEU A 1 829  ? 169.817 155.596 134.854 1.00 77.12  ? 829  LEU A O     1 
ATOM   4998  C  CB    . LEU A 1 829  ? 170.427 152.585 134.468 1.00 77.59  ? 829  LEU A CB    1 
ATOM   4999  C  CG    . LEU A 1 829  ? 170.333 152.657 135.993 1.00 73.81  ? 829  LEU A CG    1 
ATOM   5000  C  CD1   . LEU A 1 829  ? 168.932 152.323 136.477 1.00 68.10  ? 829  LEU A CD1   1 
ATOM   5001  C  CD2   . LEU A 1 829  ? 171.363 151.739 136.629 1.00 70.56  ? 829  LEU A CD2   1 
ATOM   5002  N  N     . LYS A 1 830  ? 170.880 155.480 132.866 1.00 83.81  ? 830  LYS A N     1 
ATOM   5003  C  CA    . LYS A 1 830  ? 171.505 156.792 133.007 1.00 85.98  ? 830  LYS A CA    1 
ATOM   5004  C  C     . LYS A 1 830  ? 170.481 157.893 133.246 1.00 86.49  ? 830  LYS A C     1 
ATOM   5005  O  O     . LYS A 1 830  ? 170.777 158.877 133.933 1.00 84.23  ? 830  LYS A O     1 
ATOM   5006  C  CB    . LYS A 1 830  ? 172.331 157.103 131.759 1.00 86.97  ? 830  LYS A CB    1 
ATOM   5007  C  CG    . LYS A 1 830  ? 173.129 158.389 131.831 1.00 86.17  ? 830  LYS A CG    1 
ATOM   5008  C  CD    . LYS A 1 830  ? 173.935 158.596 130.564 1.00 90.24  ? 830  LYS A CD    1 
ATOM   5009  C  CE    . LYS A 1 830  ? 174.844 157.408 130.307 1.00 88.07  ? 830  LYS A CE    1 
ATOM   5010  N  NZ    . LYS A 1 830  ? 175.779 157.176 131.441 1.00 84.96  ? 830  LYS A NZ    1 
ATOM   5011  N  N     . GLU A 1 831  ? 169.276 157.746 132.695 1.00 88.81  ? 831  GLU A N     1 
ATOM   5012  C  CA    . GLU A 1 831  ? 168.282 158.811 132.779 1.00 87.11  ? 831  GLU A CA    1 
ATOM   5013  C  C     . GLU A 1 831  ? 167.755 158.997 134.197 1.00 83.98  ? 831  GLU A C     1 
ATOM   5014  O  O     . GLU A 1 831  ? 167.396 160.117 134.577 1.00 78.95  ? 831  GLU A O     1 
ATOM   5015  C  CB    . GLU A 1 831  ? 167.135 158.518 131.812 1.00 84.90  ? 831  GLU A CB    1 
ATOM   5016  C  CG    . GLU A 1 831  ? 167.508 157.599 130.643 1.00 90.25  ? 831  GLU A CG    1 
ATOM   5017  C  CD    . GLU A 1 831  ? 168.367 158.272 129.577 1.00 94.22  ? 831  GLU A CD    1 
ATOM   5018  O  OE1   . GLU A 1 831  ? 169.301 159.025 129.925 1.00 88.45  ? 831  GLU A OE1   1 
ATOM   5019  O  OE2   . GLU A 1 831  ? 168.106 158.043 128.378 1.00 94.15  ? 831  GLU A OE2   1 
ATOM   5020  N  N     . CYS A 1 832  ? 167.702 157.925 134.993 1.00 85.37  ? 832  CYS A N     1 
ATOM   5021  C  CA    . CYS A 1 832  ? 167.148 158.031 136.340 1.00 77.94  ? 832  CYS A CA    1 
ATOM   5022  C  C     . CYS A 1 832  ? 168.030 158.870 137.253 1.00 73.86  ? 832  CYS A C     1 
ATOM   5023  O  O     . CYS A 1 832  ? 167.520 159.537 138.159 1.00 72.52  ? 832  CYS A O     1 
ATOM   5024  C  CB    . CYS A 1 832  ? 166.939 156.641 136.943 1.00 71.22  ? 832  CYS A CB    1 
ATOM   5025  S  SG    . CYS A 1 832  ? 165.601 155.684 136.195 1.00 82.57  ? 832  CYS A SG    1 
ATOM   5026  N  N     . PHE A 1 833  ? 169.340 158.847 137.043 1.00 75.90  ? 833  PHE A N     1 
ATOM   5027  C  CA    . PHE A 1 833  ? 170.249 159.628 137.871 1.00 77.06  ? 833  PHE A CA    1 
ATOM   5028  C  C     . PHE A 1 833  ? 170.262 161.090 137.441 1.00 77.55  ? 833  PHE A C     1 
ATOM   5029  O  O     . PHE A 1 833  ? 170.583 161.976 138.233 1.00 77.79  ? 833  PHE A O     1 
ATOM   5030  C  CB    . PHE A 1 833  ? 171.662 159.047 137.813 1.00 73.78  ? 833  PHE A CB    1 
ATOM   5031  C  CG    . PHE A 1 833  ? 171.810 157.742 138.536 1.00 69.64  ? 833  PHE A CG    1 
ATOM   5032  C  CD1   . PHE A 1 833  ? 171.516 156.547 137.902 1.00 71.64  ? 833  PHE A CD1   1 
ATOM   5033  C  CD2   . PHE A 1 833  ? 172.247 157.708 139.848 1.00 63.20  ? 833  PHE A CD2   1 
ATOM   5034  C  CE1   . PHE A 1 833  ? 171.652 155.344 138.565 1.00 66.91  ? 833  PHE A CE1   1 
ATOM   5035  C  CE2   . PHE A 1 833  ? 172.386 156.512 140.514 1.00 62.32  ? 833  PHE A CE2   1 
ATOM   5036  C  CZ    . PHE A 1 833  ? 172.090 155.327 139.873 1.00 65.89  ? 833  PHE A CZ    1 
ATOM   5037  N  N     . TRP A 1 846  ? 165.060 168.361 157.220 1.00 58.57  ? 846  TRP A N     1 
ATOM   5038  C  CA    . TRP A 1 846  ? 166.245 169.046 156.719 1.00 71.51  ? 846  TRP A CA    1 
ATOM   5039  C  C     . TRP A 1 846  ? 165.821 170.191 155.803 1.00 73.89  ? 846  TRP A C     1 
ATOM   5040  O  O     . TRP A 1 846  ? 165.955 170.103 154.586 1.00 78.37  ? 846  TRP A O     1 
ATOM   5041  C  CB    . TRP A 1 846  ? 167.163 168.061 155.983 1.00 74.67  ? 846  TRP A CB    1 
ATOM   5042  C  CG    . TRP A 1 846  ? 168.432 168.667 155.447 1.00 82.59  ? 846  TRP A CG    1 
ATOM   5043  C  CD1   . TRP A 1 846  ? 169.557 168.967 156.161 1.00 82.85  ? 846  TRP A CD1   1 
ATOM   5044  C  CD2   . TRP A 1 846  ? 168.723 169.001 154.086 1.00 80.39  ? 846  TRP A CD2   1 
ATOM   5045  N  NE1   . TRP A 1 846  ? 170.518 169.491 155.334 1.00 85.65  ? 846  TRP A NE1   1 
ATOM   5046  C  CE2   . TRP A 1 846  ? 170.031 169.520 154.054 1.00 86.23  ? 846  TRP A CE2   1 
ATOM   5047  C  CE3   . TRP A 1 846  ? 168.002 168.921 152.892 1.00 76.54  ? 846  TRP A CE3   1 
ATOM   5048  C  CZ2   . TRP A 1 846  ? 170.632 169.957 152.878 1.00 88.63  ? 846  TRP A CZ2   1 
ATOM   5049  C  CZ3   . TRP A 1 846  ? 168.597 169.359 151.728 1.00 86.55  ? 846  TRP A CZ3   1 
ATOM   5050  C  CH2   . TRP A 1 846  ? 169.899 169.869 151.728 1.00 88.75  ? 846  TRP A CH2   1 
ATOM   5051  N  N     . ASN A 1 847  ? 165.261 171.246 156.398 1.00 62.75  ? 847  ASN A N     1 
ATOM   5052  C  CA    . ASN A 1 847  ? 164.790 172.418 155.663 1.00 59.57  ? 847  ASN A CA    1 
ATOM   5053  C  C     . ASN A 1 847  ? 163.664 172.060 154.701 1.00 53.25  ? 847  ASN A C     1 
ATOM   5054  O  O     . ASN A 1 847  ? 163.204 172.910 153.933 1.00 55.00  ? 847  ASN A O     1 
ATOM   5055  C  CB    . ASN A 1 847  ? 165.939 173.092 154.912 1.00 63.97  ? 847  ASN A CB    1 
ATOM   5056  C  CG    . ASN A 1 847  ? 167.019 173.597 155.842 1.00 72.32  ? 847  ASN A CG    1 
ATOM   5057  O  OD1   . ASN A 1 847  ? 166.884 174.659 156.447 1.00 76.90  ? 847  ASN A OD1   1 
ATOM   5058  N  ND2   . ASN A 1 847  ? 168.098 172.834 155.966 1.00 71.40  ? 847  ASN A ND2   1 
ATOM   5059  N  N     . THR A 1 848  ? 163.223 170.805 154.729 1.00 49.90  ? 848  THR A N     1 
ATOM   5060  C  CA    . THR A 1 848  ? 162.017 170.366 154.040 1.00 48.39  ? 848  THR A CA    1 
ATOM   5061  C  C     . THR A 1 848  ? 160.845 170.214 154.995 1.00 49.28  ? 848  THR A C     1 
ATOM   5062  O  O     . THR A 1 848  ? 159.714 170.553 154.641 1.00 48.13  ? 848  THR A O     1 
ATOM   5063  C  CB    . THR A 1 848  ? 162.266 169.038 153.315 1.00 49.25  ? 848  THR A CB    1 
ATOM   5064  O  OG1   . THR A 1 848  ? 163.381 169.177 152.428 1.00 48.30  ? 848  THR A OG1   1 
ATOM   5065  C  CG2   . THR A 1 848  ? 161.047 168.623 152.508 1.00 44.06  ? 848  THR A CG2   1 
ATOM   5066  N  N     . TYR A 1 849  ? 161.099 169.708 156.203 1.00 49.27  ? 849  TYR A N     1 
ATOM   5067  C  CA    . TYR A 1 849  ? 160.087 169.730 157.251 1.00 43.24  ? 849  TYR A CA    1 
ATOM   5068  C  C     . TYR A 1 849  ? 159.773 171.162 157.661 1.00 43.11  ? 849  TYR A C     1 
ATOM   5069  O  O     . TYR A 1 849  ? 158.605 171.543 157.796 1.00 44.20  ? 849  TYR A O     1 
ATOM   5070  C  CB    . TYR A 1 849  ? 160.571 168.926 158.457 1.00 42.57  ? 849  TYR A CB    1 
ATOM   5071  C  CG    . TYR A 1 849  ? 160.629 167.434 158.232 1.00 45.24  ? 849  TYR A CG    1 
ATOM   5072  C  CD1   . TYR A 1 849  ? 161.729 166.851 157.624 1.00 47.36  ? 849  TYR A CD1   1 
ATOM   5073  C  CD2   . TYR A 1 849  ? 159.596 166.607 158.643 1.00 47.16  ? 849  TYR A CD2   1 
ATOM   5074  C  CE1   . TYR A 1 849  ? 161.794 165.490 157.418 1.00 47.72  ? 849  TYR A CE1   1 
ATOM   5075  C  CE2   . TYR A 1 849  ? 159.653 165.241 158.442 1.00 47.13  ? 849  TYR A CE2   1 
ATOM   5076  C  CZ    . TYR A 1 849  ? 160.755 164.689 157.829 1.00 47.80  ? 849  TYR A CZ    1 
ATOM   5077  O  OH    . TYR A 1 849  ? 160.817 163.332 157.626 1.00 47.17  ? 849  TYR A OH    1 
ATOM   5078  N  N     . LEU A 1 850  ? 160.815 171.971 157.856 1.00 44.97  ? 850  LEU A N     1 
ATOM   5079  C  CA    . LEU A 1 850  ? 160.632 173.340 158.321 1.00 46.43  ? 850  LEU A CA    1 
ATOM   5080  C  C     . LEU A 1 850  ? 159.895 174.185 157.292 1.00 44.20  ? 850  LEU A C     1 
ATOM   5081  O  O     . LEU A 1 850  ? 159.041 175.004 157.647 1.00 44.66  ? 850  LEU A O     1 
ATOM   5082  C  CB    . LEU A 1 850  ? 161.991 173.957 158.644 1.00 47.98  ? 850  LEU A CB    1 
ATOM   5083  C  CG    . LEU A 1 850  ? 162.001 175.153 159.591 1.00 50.69  ? 850  LEU A CG    1 
ATOM   5084  C  CD1   . LEU A 1 850  ? 161.669 174.697 160.998 1.00 46.79  ? 850  LEU A CD1   1 
ATOM   5085  C  CD2   . LEU A 1 850  ? 163.351 175.847 159.552 1.00 51.94  ? 850  LEU A CD2   1 
ATOM   5086  N  N     . ARG A 1 851  ? 160.226 174.014 156.012 1.00 43.22  ? 851  ARG A N     1 
ATOM   5087  C  CA    . ARG A 1 851  ? 159.553 174.774 154.965 1.00 41.58  ? 851  ARG A CA    1 
ATOM   5088  C  C     . ARG A 1 851  ? 158.118 174.297 154.775 1.00 42.21  ? 851  ARG A C     1 
ATOM   5089  O  O     . ARG A 1 851  ? 157.222 175.102 154.500 1.00 41.35  ? 851  ARG A O     1 
ATOM   5090  C  CB    . ARG A 1 851  ? 160.347 174.667 153.666 1.00 38.27  ? 851  ARG A CB    1 
ATOM   5091  C  CG    . ARG A 1 851  ? 159.880 175.583 152.561 1.00 39.65  ? 851  ARG A CG    1 
ATOM   5092  C  CD    . ARG A 1 851  ? 160.785 175.446 151.352 1.00 42.99  ? 851  ARG A CD    1 
ATOM   5093  N  NE    . ARG A 1 851  ? 160.314 176.223 150.212 1.00 46.03  ? 851  ARG A NE    1 
ATOM   5094  C  CZ    . ARG A 1 851  ? 160.881 176.207 149.014 1.00 45.31  ? 851  ARG A CZ    1 
ATOM   5095  N  NH1   . ARG A 1 851  ? 161.955 175.476 148.768 1.00 42.01  ? 851  ARG A NH1   1 
ATOM   5096  N  NH2   . ARG A 1 851  ? 160.358 176.943 148.039 1.00 45.03  ? 851  ARG A NH2   1 
ATOM   5097  N  N     . TYR A 1 852  ? 157.886 172.991 154.916 1.00 42.33  ? 852  TYR A N     1 
ATOM   5098  C  CA    . TYR A 1 852  ? 156.536 172.448 154.799 1.00 39.25  ? 852  TYR A CA    1 
ATOM   5099  C  C     . TYR A 1 852  ? 155.640 172.946 155.926 1.00 43.58  ? 852  TYR A C     1 
ATOM   5100  O  O     . TYR A 1 852  ? 154.458 173.236 155.708 1.00 43.24  ? 852  TYR A O     1 
ATOM   5101  C  CB    . TYR A 1 852  ? 156.600 170.921 154.790 1.00 36.80  ? 852  TYR A CB    1 
ATOM   5102  C  CG    . TYR A 1 852  ? 155.268 170.215 154.706 1.00 33.46  ? 852  TYR A CG    1 
ATOM   5103  C  CD1   . TYR A 1 852  ? 154.608 170.083 153.494 1.00 32.04  ? 852  TYR A CD1   1 
ATOM   5104  C  CD2   . TYR A 1 852  ? 154.687 169.652 155.830 1.00 35.51  ? 852  TYR A CD2   1 
ATOM   5105  C  CE1   . TYR A 1 852  ? 153.397 169.429 153.410 1.00 32.04  ? 852  TYR A CE1   1 
ATOM   5106  C  CE2   . TYR A 1 852  ? 153.476 168.996 155.754 1.00 37.32  ? 852  TYR A CE2   1 
ATOM   5107  C  CZ    . TYR A 1 852  ? 152.836 168.888 154.542 1.00 37.15  ? 852  TYR A CZ    1 
ATOM   5108  O  OH    . TYR A 1 852  ? 151.631 168.234 154.464 1.00 33.35  ? 852  TYR A OH    1 
ATOM   5109  N  N     . ILE A 1 853  ? 156.180 173.037 157.143 1.00 45.52  ? 853  ILE A N     1 
ATOM   5110  C  CA    . ILE A 1 853  ? 155.370 173.452 158.285 1.00 42.87  ? 853  ILE A CA    1 
ATOM   5111  C  C     . ILE A 1 853  ? 154.970 174.919 158.168 1.00 45.87  ? 853  ILE A C     1 
ATOM   5112  O  O     . ILE A 1 853  ? 153.810 175.278 158.403 1.00 50.06  ? 853  ILE A O     1 
ATOM   5113  C  CB    . ILE A 1 853  ? 156.117 173.165 159.600 1.00 42.63  ? 853  ILE A CB    1 
ATOM   5114  C  CG1   . ILE A 1 853  ? 156.151 171.661 159.872 1.00 44.67  ? 853  ILE A CG1   1 
ATOM   5115  C  CG2   . ILE A 1 853  ? 155.470 173.892 160.763 1.00 43.63  ? 853  ILE A CG2   1 
ATOM   5116  C  CD1   . ILE A 1 853  ? 157.191 171.253 160.888 1.00 45.87  ? 853  ILE A CD1   1 
ATOM   5117  N  N     . THR A 1 854  ? 155.906 175.788 157.792 1.00 45.58  ? 854  THR A N     1 
ATOM   5118  C  CA    . THR A 1 854  ? 155.666 177.226 157.791 1.00 47.31  ? 854  THR A CA    1 
ATOM   5119  C  C     . THR A 1 854  ? 154.956 177.718 156.534 1.00 48.47  ? 854  THR A C     1 
ATOM   5120  O  O     . THR A 1 854  ? 154.907 178.929 156.303 1.00 50.23  ? 854  THR A O     1 
ATOM   5121  C  CB    . THR A 1 854  ? 156.984 177.984 157.971 1.00 50.31  ? 854  THR A CB    1 
ATOM   5122  O  OG1   . THR A 1 854  ? 157.839 177.742 156.850 1.00 50.83  ? 854  THR A OG1   1 
ATOM   5123  C  CG2   . THR A 1 854  ? 157.681 177.535 159.241 1.00 43.92  ? 854  THR A CG2   1 
ATOM   5124  N  N     . VAL A 1 855  ? 154.415 176.812 155.715 1.00 49.85  ? 855  VAL A N     1 
ATOM   5125  C  CA    . VAL A 1 855  ? 153.580 177.231 154.592 1.00 46.28  ? 855  VAL A CA    1 
ATOM   5126  C  C     . VAL A 1 855  ? 152.323 177.929 155.098 1.00 48.87  ? 855  VAL A C     1 
ATOM   5127  O  O     . VAL A 1 855  ? 151.900 178.955 154.553 1.00 52.01  ? 855  VAL A O     1 
ATOM   5128  C  CB    . VAL A 1 855  ? 153.236 176.024 153.696 1.00 46.42  ? 855  VAL A CB    1 
ATOM   5129  C  CG1   . VAL A 1 855  ? 152.137 176.380 152.713 1.00 42.06  ? 855  VAL A CG1   1 
ATOM   5130  C  CG2   . VAL A 1 855  ? 154.462 175.549 152.946 1.00 43.20  ? 855  VAL A CG2   1 
ATOM   5131  N  N     . HIS A 1 856  ? 151.717 177.392 156.155 1.00 48.33  ? 856  HIS A N     1 
ATOM   5132  C  CA    . HIS A 1 856  ? 150.416 177.840 156.632 1.00 45.88  ? 856  HIS A CA    1 
ATOM   5133  C  C     . HIS A 1 856  ? 150.505 178.083 158.132 1.00 50.54  ? 856  HIS A C     1 
ATOM   5134  O  O     . HIS A 1 856  ? 150.986 177.221 158.871 1.00 55.23  ? 856  HIS A O     1 
ATOM   5135  C  CB    . HIS A 1 856  ? 149.344 176.791 156.308 1.00 45.97  ? 856  HIS A CB    1 
ATOM   5136  C  CG    . HIS A 1 856  ? 147.942 177.309 156.351 1.00 44.37  ? 856  HIS A CG    1 
ATOM   5137  N  ND1   . HIS A 1 856  ? 147.630 178.634 156.137 1.00 47.51  ? 856  HIS A ND1   1 
ATOM   5138  C  CD2   . HIS A 1 856  ? 146.764 176.673 156.550 1.00 42.16  ? 856  HIS A CD2   1 
ATOM   5139  C  CE1   . HIS A 1 856  ? 146.321 178.793 156.219 1.00 45.68  ? 856  HIS A CE1   1 
ATOM   5140  N  NE2   . HIS A 1 856  ? 145.773 177.619 156.470 1.00 48.53  ? 856  HIS A NE2   1 
ATOM   5141  N  N     . LYS A 1 857  ? 150.042 179.255 158.577 1.00 49.60  ? 857  LYS A N     1 
ATOM   5142  C  CA    . LYS A 1 857  ? 150.197 179.639 159.979 1.00 53.30  ? 857  LYS A CA    1 
ATOM   5143  C  C     . LYS A 1 857  ? 149.233 178.876 160.883 1.00 52.41  ? 857  LYS A C     1 
ATOM   5144  O  O     . LYS A 1 857  ? 149.529 178.642 162.068 1.00 56.43  ? 857  LYS A O     1 
ATOM   5145  C  CB    . LYS A 1 857  ? 149.980 181.145 160.116 1.00 55.17  ? 857  LYS A CB    1 
ATOM   5146  C  CG    . LYS A 1 857  ? 150.726 181.797 161.264 1.00 67.15  ? 857  LYS A CG    1 
ATOM   5147  C  CD    . LYS A 1 857  ? 152.215 181.897 160.966 1.00 75.52  ? 857  LYS A CD    1 
ATOM   5148  C  CE    . LYS A 1 857  ? 152.953 182.637 162.070 1.00 75.98  ? 857  LYS A CE    1 
ATOM   5149  N  NZ    . LYS A 1 857  ? 152.644 184.092 162.050 1.00 71.47  ? 857  LYS A NZ    1 
ATOM   5150  N  N     . SER A 1 858  ? 148.082 178.478 160.338 1.00 46.94  ? 858  SER A N     1 
ATOM   5151  C  CA    . SER A 1 858  ? 147.102 177.738 161.121 1.00 48.56  ? 858  SER A CA    1 
ATOM   5152  C  C     . SER A 1 858  ? 147.662 176.408 161.606 1.00 50.67  ? 858  SER A C     1 
ATOM   5153  O  O     . SER A 1 858  ? 147.278 175.929 162.678 1.00 54.38  ? 858  SER A O     1 
ATOM   5154  C  CB    . SER A 1 858  ? 145.837 177.519 160.295 1.00 45.97  ? 858  SER A CB    1 
ATOM   5155  O  OG    . SER A 1 858  ? 144.845 176.862 161.060 1.00 57.41  ? 858  SER A OG    1 
ATOM   5156  N  N     . LEU A 1 859  ? 148.579 175.808 160.847 1.00 46.58  ? 859  LEU A N     1 
ATOM   5157  C  CA    . LEU A 1 859  ? 149.225 174.581 161.300 1.00 45.51  ? 859  LEU A CA    1 
ATOM   5158  C  C     . LEU A 1 859  ? 150.055 174.828 162.555 1.00 50.06  ? 859  LEU A C     1 
ATOM   5159  O  O     . LEU A 1 859  ? 150.034 174.020 163.492 1.00 50.43  ? 859  LEU A O     1 
ATOM   5160  C  CB    . LEU A 1 859  ? 150.094 174.010 160.182 1.00 44.21  ? 859  LEU A CB    1 
ATOM   5161  C  CG    . LEU A 1 859  ? 150.727 172.644 160.441 1.00 45.74  ? 859  LEU A CG    1 
ATOM   5162  C  CD1   . LEU A 1 859  ? 149.656 171.610 160.722 1.00 46.63  ? 859  LEU A CD1   1 
ATOM   5163  C  CD2   . LEU A 1 859  ? 151.593 172.215 159.274 1.00 46.74  ? 859  LEU A CD2   1 
ATOM   5164  N  N     . ILE A 1 860  ? 150.784 175.945 162.592 1.00 51.16  ? 860  ILE A N     1 
ATOM   5165  C  CA    . ILE A 1 860  ? 151.558 176.295 163.779 1.00 50.30  ? 860  ILE A CA    1 
ATOM   5166  C  C     . ILE A 1 860  ? 150.637 176.505 164.970 1.00 49.63  ? 860  ILE A C     1 
ATOM   5167  O  O     . ILE A 1 860  ? 150.915 176.034 166.083 1.00 53.43  ? 860  ILE A O     1 
ATOM   5168  C  CB    . ILE A 1 860  ? 152.416 177.544 163.507 1.00 50.98  ? 860  ILE A CB    1 
ATOM   5169  C  CG1   . ILE A 1 860  ? 153.377 177.290 162.347 1.00 50.91  ? 860  ILE A CG1   1 
ATOM   5170  C  CG2   . ILE A 1 860  ? 153.176 177.948 164.754 1.00 52.52  ? 860  ILE A CG2   1 
ATOM   5171  C  CD1   . ILE A 1 860  ? 154.067 178.533 161.855 1.00 49.96  ? 860  ILE A CD1   1 
ATOM   5172  N  N     . PHE A 1 861  ? 149.520 177.209 164.759 1.00 48.93  ? 861  PHE A N     1 
ATOM   5173  C  CA    . PHE A 1 861  ? 148.592 177.431 165.867 1.00 48.19  ? 861  PHE A CA    1 
ATOM   5174  C  C     . PHE A 1 861  ? 148.011 176.118 166.381 1.00 45.24  ? 861  PHE A C     1 
ATOM   5175  O  O     . PHE A 1 861  ? 147.903 175.911 167.598 1.00 46.86  ? 861  PHE A O     1 
ATOM   5176  C  CB    . PHE A 1 861  ? 147.477 178.388 165.445 1.00 47.68  ? 861  PHE A CB    1 
ATOM   5177  C  CG    . PHE A 1 861  ? 147.969 179.725 164.975 1.00 53.49  ? 861  PHE A CG    1 
ATOM   5178  C  CD1   . PHE A 1 861  ? 149.097 180.300 165.537 1.00 56.96  ? 861  PHE A CD1   1 
ATOM   5179  C  CD2   . PHE A 1 861  ? 147.292 180.418 163.986 1.00 53.72  ? 861  PHE A CD2   1 
ATOM   5180  C  CE1   . PHE A 1 861  ? 149.551 181.535 165.112 1.00 62.93  ? 861  PHE A CE1   1 
ATOM   5181  C  CE2   . PHE A 1 861  ? 147.739 181.655 163.556 1.00 57.28  ? 861  PHE A CE2   1 
ATOM   5182  C  CZ    . PHE A 1 861  ? 148.869 182.215 164.121 1.00 63.97  ? 861  PHE A CZ    1 
ATOM   5183  N  N     . VAL A 1 862  ? 147.650 175.211 165.472 1.00 44.21  ? 862  VAL A N     1 
ATOM   5184  C  CA    . VAL A 1 862  ? 147.076 173.933 165.879 1.00 44.49  ? 862  VAL A CA    1 
ATOM   5185  C  C     . VAL A 1 862  ? 148.099 173.101 166.644 1.00 46.08  ? 862  VAL A C     1 
ATOM   5186  O  O     . VAL A 1 862  ? 147.767 172.441 167.638 1.00 50.13  ? 862  VAL A O     1 
ATOM   5187  C  CB    . VAL A 1 862  ? 146.532 173.186 164.650 1.00 38.51  ? 862  VAL A CB    1 
ATOM   5188  C  CG1   . VAL A 1 862  ? 146.244 171.739 164.987 1.00 40.16  ? 862  VAL A CG1   1 
ATOM   5189  C  CG2   . VAL A 1 862  ? 145.280 173.871 164.142 1.00 38.13  ? 862  VAL A CG2   1 
ATOM   5190  N  N     . LEU A 1 863  ? 149.358 173.118 166.201 1.00 42.26  ? 863  LEU A N     1 
ATOM   5191  C  CA    . LEU A 1 863  ? 150.388 172.365 166.909 1.00 41.37  ? 863  LEU A CA    1 
ATOM   5192  C  C     . LEU A 1 863  ? 150.628 172.928 168.305 1.00 44.34  ? 863  LEU A C     1 
ATOM   5193  O  O     . LEU A 1 863  ? 150.829 172.167 169.261 1.00 46.04  ? 863  LEU A O     1 
ATOM   5194  C  CB    . LEU A 1 863  ? 151.683 172.353 166.100 1.00 46.40  ? 863  LEU A CB    1 
ATOM   5195  C  CG    . LEU A 1 863  ? 151.673 171.460 164.858 1.00 42.41  ? 863  LEU A CG    1 
ATOM   5196  C  CD1   . LEU A 1 863  ? 152.962 171.616 164.065 1.00 38.44  ? 863  LEU A CD1   1 
ATOM   5197  C  CD2   . LEU A 1 863  ? 151.443 170.009 165.233 1.00 39.07  ? 863  LEU A CD2   1 
ATOM   5198  N  N     . ILE A 1 864  ? 150.602 174.255 168.449 1.00 44.58  ? 864  ILE A N     1 
ATOM   5199  C  CA    . ILE A 1 864  ? 150.761 174.850 169.775 1.00 43.73  ? 864  ILE A CA    1 
ATOM   5200  C  C     . ILE A 1 864  ? 149.597 174.459 170.682 1.00 43.93  ? 864  ILE A C     1 
ATOM   5201  O  O     . ILE A 1 864  ? 149.786 174.155 171.869 1.00 45.63  ? 864  ILE A O     1 
ATOM   5202  C  CB    . ILE A 1 864  ? 150.907 176.377 169.657 1.00 40.02  ? 864  ILE A CB    1 
ATOM   5203  C  CG1   . ILE A 1 864  ? 152.260 176.734 169.044 1.00 41.72  ? 864  ILE A CG1   1 
ATOM   5204  C  CG2   . ILE A 1 864  ? 150.763 177.035 171.015 1.00 38.64  ? 864  ILE A CG2   1 
ATOM   5205  C  CD1   . ILE A 1 864  ? 152.328 178.141 168.503 1.00 44.65  ? 864  ILE A CD1   1 
ATOM   5206  N  N     . TRP A 1 865  ? 148.378 174.464 170.139 1.00 41.07  ? 865  TRP A N     1 
ATOM   5207  C  CA    . TRP A 1 865  ? 147.207 174.022 170.895 1.00 41.02  ? 865  TRP A CA    1 
ATOM   5208  C  C     . TRP A 1 865  ? 147.368 172.583 171.382 1.00 43.56  ? 865  TRP A C     1 
ATOM   5209  O  O     . TRP A 1 865  ? 147.127 172.277 172.564 1.00 45.54  ? 865  TRP A O     1 
ATOM   5210  C  CB    . TRP A 1 865  ? 145.975 174.183 170.003 1.00 41.73  ? 865  TRP A CB    1 
ATOM   5211  C  CG    . TRP A 1 865  ? 144.714 173.521 170.446 1.00 47.34  ? 865  TRP A CG    1 
ATOM   5212  C  CD1   . TRP A 1 865  ? 144.205 172.344 169.981 1.00 45.43  ? 865  TRP A CD1   1 
ATOM   5213  C  CD2   . TRP A 1 865  ? 143.772 174.016 171.400 1.00 49.53  ? 865  TRP A CD2   1 
ATOM   5214  N  NE1   . TRP A 1 865  ? 143.015 172.064 170.603 1.00 47.15  ? 865  TRP A NE1   1 
ATOM   5215  C  CE2   . TRP A 1 865  ? 142.726 173.079 171.476 1.00 47.76  ? 865  TRP A CE2   1 
ATOM   5216  C  CE3   . TRP A 1 865  ? 143.716 175.155 172.203 1.00 48.25  ? 865  TRP A CE3   1 
ATOM   5217  C  CZ2   . TRP A 1 865  ? 141.642 173.242 172.327 1.00 46.48  ? 865  TRP A CZ2   1 
ATOM   5218  C  CZ3   . TRP A 1 865  ? 142.639 175.317 173.045 1.00 48.41  ? 865  TRP A CZ3   1 
ATOM   5219  C  CH2   . TRP A 1 865  ? 141.617 174.366 173.101 1.00 48.53  ? 865  TRP A CH2   1 
ATOM   5220  N  N     . CYS A 1 866  ? 147.812 171.695 170.490 1.00 43.92  ? 866  CYS A N     1 
ATOM   5221  C  CA    . CYS A 1 866  ? 148.005 170.298 170.862 1.00 43.43  ? 866  CYS A CA    1 
ATOM   5222  C  C     . CYS A 1 866  ? 149.061 170.160 171.950 1.00 42.24  ? 866  CYS A C     1 
ATOM   5223  O  O     . CYS A 1 866  ? 148.891 169.384 172.900 1.00 41.97  ? 866  CYS A O     1 
ATOM   5224  C  CB    . CYS A 1 866  ? 148.399 169.482 169.632 1.00 40.72  ? 866  CYS A CB    1 
ATOM   5225  S  SG    . CYS A 1 866  ? 147.099 169.314 168.392 1.00 54.46  ? 866  CYS A SG    1 
ATOM   5226  N  N     . LEU A 1 867  ? 150.157 170.911 171.833 1.00 43.05  ? 867  LEU A N     1 
ATOM   5227  C  CA    . LEU A 1 867  ? 151.217 170.835 172.833 1.00 43.22  ? 867  LEU A CA    1 
ATOM   5228  C  C     . LEU A 1 867  ? 150.729 171.301 174.201 1.00 44.93  ? 867  LEU A C     1 
ATOM   5229  O  O     . LEU A 1 867  ? 151.062 170.691 175.227 1.00 46.94  ? 867  LEU A O     1 
ATOM   5230  C  CB    . LEU A 1 867  ? 152.415 171.664 172.377 1.00 41.86  ? 867  LEU A CB    1 
ATOM   5231  C  CG    . LEU A 1 867  ? 153.625 171.690 173.307 1.00 43.98  ? 867  LEU A CG    1 
ATOM   5232  C  CD1   . LEU A 1 867  ? 154.128 170.282 173.550 1.00 46.46  ? 867  LEU A CD1   1 
ATOM   5233  C  CD2   . LEU A 1 867  ? 154.722 172.561 172.719 1.00 46.55  ? 867  LEU A CD2   1 
ATOM   5234  N  N     . VAL A 1 868  ? 149.948 172.384 174.239 1.00 43.25  ? 868  VAL A N     1 
ATOM   5235  C  CA    . VAL A 1 868  ? 149.454 172.892 175.517 1.00 41.30  ? 868  VAL A CA    1 
ATOM   5236  C  C     . VAL A 1 868  ? 148.541 171.871 176.184 1.00 42.83  ? 868  VAL A C     1 
ATOM   5237  O  O     . VAL A 1 868  ? 148.638 171.622 177.397 1.00 46.37  ? 868  VAL A O     1 
ATOM   5238  C  CB    . VAL A 1 868  ? 148.743 174.242 175.315 1.00 41.37  ? 868  VAL A CB    1 
ATOM   5239  C  CG1   . VAL A 1 868  ? 147.883 174.576 176.523 1.00 41.95  ? 868  VAL A CG1   1 
ATOM   5240  C  CG2   . VAL A 1 868  ? 149.762 175.333 175.067 1.00 37.31  ? 868  VAL A CG2   1 
ATOM   5241  N  N     . ILE A 1 869  ? 147.641 171.259 175.408 1.00 42.22  ? 869  ILE A N     1 
ATOM   5242  C  CA    . ILE A 1 869  ? 146.763 170.251 176.000 1.00 41.53  ? 869  ILE A CA    1 
ATOM   5243  C  C     . ILE A 1 869  ? 147.567 169.050 176.487 1.00 47.56  ? 869  ILE A C     1 
ATOM   5244  O  O     . ILE A 1 869  ? 147.270 168.472 177.541 1.00 50.44  ? 869  ILE A O     1 
ATOM   5245  C  CB    . ILE A 1 869  ? 145.665 169.834 175.010 1.00 40.88  ? 869  ILE A CB    1 
ATOM   5246  C  CG1   . ILE A 1 869  ? 144.695 170.985 174.790 1.00 43.88  ? 869  ILE A CG1   1 
ATOM   5247  C  CG2   . ILE A 1 869  ? 144.912 168.624 175.522 1.00 42.07  ? 869  ILE A CG2   1 
ATOM   5248  C  CD1   . ILE A 1 869  ? 143.867 170.805 173.574 1.00 45.23  ? 869  ILE A CD1   1 
ATOM   5249  N  N     . PHE A 1 870  ? 148.599 168.656 175.735 1.00 46.80  ? 870  PHE A N     1 
ATOM   5250  C  CA    . PHE A 1 870  ? 149.442 167.546 176.168 1.00 44.85  ? 870  PHE A CA    1 
ATOM   5251  C  C     . PHE A 1 870  ? 150.118 167.847 177.500 1.00 44.51  ? 870  PHE A C     1 
ATOM   5252  O  O     . PHE A 1 870  ? 150.166 166.987 178.390 1.00 46.74  ? 870  PHE A O     1 
ATOM   5253  C  CB    . PHE A 1 870  ? 150.488 167.241 175.099 1.00 42.19  ? 870  PHE A CB    1 
ATOM   5254  C  CG    . PHE A 1 870  ? 151.556 166.287 175.548 1.00 40.85  ? 870  PHE A CG    1 
ATOM   5255  C  CD1   . PHE A 1 870  ? 151.272 164.946 175.733 1.00 39.34  ? 870  PHE A CD1   1 
ATOM   5256  C  CD2   . PHE A 1 870  ? 152.845 166.732 175.781 1.00 41.77  ? 870  PHE A CD2   1 
ATOM   5257  C  CE1   . PHE A 1 870  ? 152.249 164.072 176.144 1.00 36.47  ? 870  PHE A CE1   1 
ATOM   5258  C  CE2   . PHE A 1 870  ? 153.829 165.858 176.193 1.00 36.86  ? 870  PHE A CE2   1 
ATOM   5259  C  CZ    . PHE A 1 870  ? 153.530 164.527 176.373 1.00 35.24  ? 870  PHE A CZ    1 
ATOM   5260  N  N     . LEU A 1 871  ? 150.648 169.061 177.655 1.00 45.38  ? 871  LEU A N     1 
ATOM   5261  C  CA    . LEU A 1 871  ? 151.306 169.417 178.910 1.00 45.55  ? 871  LEU A CA    1 
ATOM   5262  C  C     . LEU A 1 871  ? 150.318 169.428 180.070 1.00 46.22  ? 871  LEU A C     1 
ATOM   5263  O  O     . LEU A 1 871  ? 150.645 168.979 181.178 1.00 48.19  ? 871  LEU A O     1 
ATOM   5264  C  CB    . LEU A 1 871  ? 151.997 170.773 178.781 1.00 41.09  ? 871  LEU A CB    1 
ATOM   5265  C  CG    . LEU A 1 871  ? 153.238 170.809 177.891 1.00 45.07  ? 871  LEU A CG    1 
ATOM   5266  C  CD1   . LEU A 1 871  ? 153.702 172.238 177.680 1.00 44.62  ? 871  LEU A CD1   1 
ATOM   5267  C  CD2   . LEU A 1 871  ? 154.344 169.964 178.495 1.00 40.92  ? 871  LEU A CD2   1 
ATOM   5268  N  N     . ALA A 1 872  ? 149.102 169.929 179.834 1.00 45.52  ? 872  ALA A N     1 
ATOM   5269  C  CA    . ALA A 1 872  ? 148.097 169.919 180.895 1.00 46.40  ? 872  ALA A CA    1 
ATOM   5270  C  C     . ALA A 1 872  ? 147.748 168.495 181.315 1.00 46.89  ? 872  ALA A C     1 
ATOM   5271  O  O     . ALA A 1 872  ? 147.629 168.204 182.514 1.00 45.98  ? 872  ALA A O     1 
ATOM   5272  C  CB    . ALA A 1 872  ? 146.844 170.666 180.443 1.00 46.59  ? 872  ALA A CB    1 
ATOM   5273  N  N     . GLU A 1 873  ? 147.589 167.593 180.343 1.00 46.94  ? 873  GLU A N     1 
ATOM   5274  C  CA    . GLU A 1 873  ? 147.293 166.201 180.670 1.00 45.52  ? 873  GLU A CA    1 
ATOM   5275  C  C     . GLU A 1 873  ? 148.430 165.559 181.452 1.00 46.35  ? 873  GLU A C     1 
ATOM   5276  O  O     . GLU A 1 873  ? 148.189 164.805 182.404 1.00 48.36  ? 873  GLU A O     1 
ATOM   5277  C  CB    . GLU A 1 873  ? 147.018 165.404 179.397 1.00 47.20  ? 873  GLU A CB    1 
ATOM   5278  C  CG    . GLU A 1 873  ? 145.679 165.681 178.758 1.00 51.99  ? 873  GLU A CG    1 
ATOM   5279  C  CD    . GLU A 1 873  ? 145.506 164.933 177.456 1.00 58.26  ? 873  GLU A CD    1 
ATOM   5280  O  OE1   . GLU A 1 873  ? 146.509 164.397 176.941 1.00 56.34  ? 873  GLU A OE1   1 
ATOM   5281  O  OE2   . GLU A 1 873  ? 144.367 164.875 176.949 1.00 63.63  ? 873  GLU A OE2   1 
ATOM   5282  N  N     . VAL A 1 874  ? 149.675 165.832 181.057 1.00 45.61  ? 874  VAL A N     1 
ATOM   5283  C  CA    . VAL A 1 874  ? 150.815 165.260 181.768 1.00 44.45  ? 874  VAL A CA    1 
ATOM   5284  C  C     . VAL A 1 874  ? 150.837 165.738 183.214 1.00 46.22  ? 874  VAL A C     1 
ATOM   5285  O  O     . VAL A 1 874  ? 151.054 164.946 184.141 1.00 48.26  ? 874  VAL A O     1 
ATOM   5286  C  CB    . VAL A 1 874  ? 152.126 165.598 181.036 1.00 45.12  ? 874  VAL A CB    1 
ATOM   5287  C  CG1   . VAL A 1 874  ? 153.308 165.450 181.971 1.00 46.89  ? 874  VAL A CG1   1 
ATOM   5288  C  CG2   . VAL A 1 874  ? 152.297 164.701 179.825 1.00 41.56  ? 874  VAL A CG2   1 
ATOM   5289  N  N     . ALA A 1 875  ? 150.602 167.035 183.431 1.00 47.59  ? 875  ALA A N     1 
ATOM   5290  C  CA    . ALA A 1 875  ? 150.593 167.558 184.795 1.00 46.48  ? 875  ALA A CA    1 
ATOM   5291  C  C     . ALA A 1 875  ? 149.482 166.927 185.627 1.00 47.51  ? 875  ALA A C     1 
ATOM   5292  O  O     . ALA A 1 875  ? 149.698 166.557 186.790 1.00 49.59  ? 875  ALA A O     1 
ATOM   5293  C  CB    . ALA A 1 875  ? 150.450 169.079 184.778 1.00 42.15  ? 875  ALA A CB    1 
ATOM   5294  N  N     . ALA A 1 876  ? 148.285 166.791 185.050 1.00 46.06  ? 876  ALA A N     1 
ATOM   5295  C  CA    . ALA A 1 876  ? 147.177 166.201 185.795 1.00 43.45  ? 876  ALA A CA    1 
ATOM   5296  C  C     . ALA A 1 876  ? 147.475 164.755 186.170 1.00 48.58  ? 876  ALA A C     1 
ATOM   5297  O  O     . ALA A 1 876  ? 147.239 164.331 187.311 1.00 52.69  ? 876  ALA A O     1 
ATOM   5298  C  CB    . ALA A 1 876  ? 145.886 166.288 184.982 1.00 40.89  ? 876  ALA A CB    1 
ATOM   5299  N  N     . SER A 1 877  ? 148.000 163.979 185.219 1.00 50.53  ? 877  SER A N     1 
ATOM   5300  C  CA    . SER A 1 877  ? 148.300 162.580 185.498 1.00 49.70  ? 877  SER A CA    1 
ATOM   5301  C  C     . SER A 1 877  ? 149.392 162.453 186.551 1.00 49.43  ? 877  SER A C     1 
ATOM   5302  O  O     . SER A 1 877  ? 149.324 161.576 187.419 1.00 49.45  ? 877  SER A O     1 
ATOM   5303  C  CB    . SER A 1 877  ? 148.708 161.860 184.215 1.00 46.93  ? 877  SER A CB    1 
ATOM   5304  O  OG    . SER A 1 877  ? 150.019 162.223 183.828 1.00 51.23  ? 877  SER A OG    1 
ATOM   5305  N  N     . LEU A 1 878  ? 150.402 163.326 186.498 1.00 49.20  ? 878  LEU A N     1 
ATOM   5306  C  CA    . LEU A 1 878  ? 151.464 163.275 187.497 1.00 49.70  ? 878  LEU A CA    1 
ATOM   5307  C  C     . LEU A 1 878  ? 150.921 163.596 188.885 1.00 51.57  ? 878  LEU A C     1 
ATOM   5308  O  O     . LEU A 1 878  ? 151.282 162.935 189.864 1.00 57.12  ? 878  LEU A O     1 
ATOM   5309  C  CB    . LEU A 1 878  ? 152.592 164.233 187.099 1.00 48.67  ? 878  LEU A CB    1 
ATOM   5310  C  CG    . LEU A 1 878  ? 154.012 164.157 187.678 1.00 48.44  ? 878  LEU A CG    1 
ATOM   5311  C  CD1   . LEU A 1 878  ? 154.845 165.273 187.075 1.00 53.65  ? 878  LEU A CD1   1 
ATOM   5312  C  CD2   . LEU A 1 878  ? 154.078 164.229 189.191 1.00 50.87  ? 878  LEU A CD2   1 
ATOM   5313  N  N     . VAL A 1 879  ? 150.048 164.601 188.991 1.00 51.37  ? 879  VAL A N     1 
ATOM   5314  C  CA    . VAL A 1 879  ? 149.472 164.936 190.292 1.00 51.68  ? 879  VAL A CA    1 
ATOM   5315  C  C     . VAL A 1 879  ? 148.654 163.770 190.835 1.00 53.37  ? 879  VAL A C     1 
ATOM   5316  O  O     . VAL A 1 879  ? 148.771 163.402 192.014 1.00 58.01  ? 879  VAL A O     1 
ATOM   5317  C  CB    . VAL A 1 879  ? 148.630 166.221 190.191 1.00 53.09  ? 879  VAL A CB    1 
ATOM   5318  C  CG1   . VAL A 1 879  ? 147.525 166.217 191.233 1.00 49.48  ? 879  VAL A CG1   1 
ATOM   5319  C  CG2   . VAL A 1 879  ? 149.515 167.440 190.359 1.00 52.28  ? 879  VAL A CG2   1 
ATOM   5320  N  N     . VAL A 1 880  ? 147.822 163.161 189.985 1.00 55.53  ? 880  VAL A N     1 
ATOM   5321  C  CA    . VAL A 1 880  ? 146.980 162.062 190.449 1.00 55.28  ? 880  VAL A CA    1 
ATOM   5322  C  C     . VAL A 1 880  ? 147.833 160.875 190.879 1.00 55.51  ? 880  VAL A C     1 
ATOM   5323  O  O     . VAL A 1 880  ? 147.555 160.229 191.897 1.00 56.20  ? 880  VAL A O     1 
ATOM   5324  C  CB    . VAL A 1 880  ? 145.963 161.663 189.366 1.00 55.27  ? 880  VAL A CB    1 
ATOM   5325  C  CG1   . VAL A 1 880  ? 145.317 160.330 189.713 1.00 50.87  ? 880  VAL A CG1   1 
ATOM   5326  C  CG2   . VAL A 1 880  ? 144.907 162.742 189.211 1.00 52.46  ? 880  VAL A CG2   1 
ATOM   5327  N  N     . LEU A 1 881  ? 148.884 160.566 190.117 1.00 58.69  ? 881  LEU A N     1 
ATOM   5328  C  CA    . LEU A 1 881  ? 149.747 159.444 190.471 1.00 57.14  ? 881  LEU A CA    1 
ATOM   5329  C  C     . LEU A 1 881  ? 150.521 159.719 191.754 1.00 59.78  ? 881  LEU A C     1 
ATOM   5330  O  O     . LEU A 1 881  ? 150.743 158.805 192.556 1.00 64.97  ? 881  LEU A O     1 
ATOM   5331  C  CB    . LEU A 1 881  ? 150.704 159.139 189.319 1.00 55.06  ? 881  LEU A CB    1 
ATOM   5332  C  CG    . LEU A 1 881  ? 151.244 157.715 189.222 1.00 52.95  ? 881  LEU A CG    1 
ATOM   5333  C  CD1   . LEU A 1 881  ? 150.170 156.785 188.699 1.00 51.88  ? 881  LEU A CD1   1 
ATOM   5334  C  CD2   . LEU A 1 881  ? 152.469 157.674 188.325 1.00 55.50  ? 881  LEU A CD2   1 
ATOM   5335  N  N     . TRP A 1 882  ? 150.952 160.966 191.963 1.00 61.35  ? 882  TRP A N     1 
ATOM   5336  C  CA    . TRP A 1 882  ? 151.621 161.313 193.211 1.00 66.53  ? 882  TRP A CA    1 
ATOM   5337  C  C     . TRP A 1 882  ? 150.677 161.222 194.399 1.00 69.73  ? 882  TRP A C     1 
ATOM   5338  O  O     . TRP A 1 882  ? 151.116 160.928 195.517 1.00 72.53  ? 882  TRP A O     1 
ATOM   5339  C  CB    . TRP A 1 882  ? 152.209 162.720 193.131 1.00 67.77  ? 882  TRP A CB    1 
ATOM   5340  C  CG    . TRP A 1 882  ? 152.789 163.184 194.431 1.00 76.86  ? 882  TRP A CG    1 
ATOM   5341  C  CD1   . TRP A 1 882  ? 154.061 162.984 194.879 1.00 79.14  ? 882  TRP A CD1   1 
ATOM   5342  C  CD2   . TRP A 1 882  ? 152.111 163.912 195.462 1.00 80.46  ? 882  TRP A CD2   1 
ATOM   5343  N  NE1   . TRP A 1 882  ? 154.220 163.553 196.119 1.00 83.44  ? 882  TRP A NE1   1 
ATOM   5344  C  CE2   . TRP A 1 882  ? 153.036 164.126 196.499 1.00 85.16  ? 882  TRP A CE2   1 
ATOM   5345  C  CE3   . TRP A 1 882  ? 150.811 164.405 195.606 1.00 78.40  ? 882  TRP A CE3   1 
ATOM   5346  C  CZ2   . TRP A 1 882  ? 152.705 164.813 197.665 1.00 85.29  ? 882  TRP A CZ2   1 
ATOM   5347  C  CZ3   . TRP A 1 882  ? 150.484 165.086 196.765 1.00 81.91  ? 882  TRP A CZ3   1 
ATOM   5348  C  CH2   . TRP A 1 882  ? 151.427 165.284 197.778 1.00 86.02  ? 882  TRP A CH2   1 
ATOM   5349  N  N     . LEU A 1 883  ? 149.385 161.493 194.187 1.00 68.05  ? 883  LEU A N     1 
ATOM   5350  C  CA    . LEU A 1 883  ? 148.436 161.440 195.296 1.00 65.83  ? 883  LEU A CA    1 
ATOM   5351  C  C     . LEU A 1 883  ? 148.395 160.062 195.944 1.00 65.08  ? 883  LEU A C     1 
ATOM   5352  O  O     . LEU A 1 883  ? 148.139 159.952 197.147 1.00 66.96  ? 883  LEU A O     1 
ATOM   5353  C  CB    . LEU A 1 883  ? 147.041 161.840 194.818 1.00 67.81  ? 883  LEU A CB    1 
ATOM   5354  C  CG    . LEU A 1 883  ? 146.215 162.650 195.819 1.00 73.11  ? 883  LEU A CG    1 
ATOM   5355  C  CD1   . LEU A 1 883  ? 146.857 164.000 196.061 1.00 75.03  ? 883  LEU A CD1   1 
ATOM   5356  C  CD2   . LEU A 1 883  ? 144.785 162.821 195.334 1.00 70.38  ? 883  LEU A CD2   1 
ATOM   5357  N  N     . LEU A 1 884  ? 148.646 159.009 195.174 1.00 67.56  ? 884  LEU A N     1 
ATOM   5358  C  CA    . LEU A 1 884  ? 148.665 157.653 195.713 1.00 69.16  ? 884  LEU A CA    1 
ATOM   5359  C  C     . LEU A 1 884  ? 150.003 157.355 196.382 1.00 75.29  ? 884  LEU A C     1 
ATOM   5360  O  O     . LEU A 1 884  ? 150.051 156.940 197.540 1.00 76.65  ? 884  LEU A O     1 
ATOM   5361  C  CB    . LEU A 1 884  ? 148.392 156.619 194.614 1.00 67.08  ? 884  LEU A CB    1 
ATOM   5362  C  CG    . LEU A 1 884  ? 146.975 156.350 194.088 1.00 70.00  ? 884  LEU A CG    1 
ATOM   5363  C  CD1   . LEU A 1 884  ? 146.105 157.598 194.021 1.00 64.42  ? 884  LEU A CD1   1 
ATOM   5364  C  CD2   . LEU A 1 884  ? 147.044 155.678 192.724 1.00 62.85  ? 884  LEU A CD2   1 
ATOM   5365  N  N     . TYR A 1 903  ? 138.622 147.883 200.992 1.00 81.68  ? 903  TYR A N     1 
ATOM   5366  C  CA    . TYR A 1 903  ? 138.236 148.382 199.679 1.00 79.93  ? 903  TYR A CA    1 
ATOM   5367  C  C     . TYR A 1 903  ? 138.065 147.238 198.688 1.00 76.02  ? 903  TYR A C     1 
ATOM   5368  O  O     . TYR A 1 903  ? 138.404 146.092 198.982 1.00 73.40  ? 903  TYR A O     1 
ATOM   5369  C  CB    . TYR A 1 903  ? 139.273 149.379 199.158 1.00 75.02  ? 903  TYR A CB    1 
ATOM   5370  N  N     . ALA A 1 904  ? 137.529 147.561 197.509 1.00 72.02  ? 904  ALA A N     1 
ATOM   5371  C  CA    . ALA A 1 904  ? 137.331 146.566 196.465 1.00 66.31  ? 904  ALA A CA    1 
ATOM   5372  C  C     . ALA A 1 904  ? 138.631 146.147 195.792 1.00 63.32  ? 904  ALA A C     1 
ATOM   5373  O  O     . ALA A 1 904  ? 138.632 145.154 195.058 1.00 63.92  ? 904  ALA A O     1 
ATOM   5374  C  CB    . ALA A 1 904  ? 136.356 147.096 195.413 1.00 65.43  ? 904  ALA A CB    1 
ATOM   5375  N  N     . VAL A 1 905  ? 139.725 146.866 196.022 1.00 60.25  ? 905  VAL A N     1 
ATOM   5376  C  CA    . VAL A 1 905  ? 141.021 146.558 195.431 1.00 56.22  ? 905  VAL A CA    1 
ATOM   5377  C  C     . VAL A 1 905  ? 142.001 146.294 196.563 1.00 58.86  ? 905  VAL A C     1 
ATOM   5378  O  O     . VAL A 1 905  ? 142.072 147.071 197.522 1.00 62.81  ? 905  VAL A O     1 
ATOM   5379  C  CB    . VAL A 1 905  ? 141.521 147.700 194.528 1.00 55.57  ? 905  VAL A CB    1 
ATOM   5380  C  CG1   . VAL A 1 905  ? 142.881 147.361 193.952 1.00 56.74  ? 905  VAL A CG1   1 
ATOM   5381  C  CG2   . VAL A 1 905  ? 140.523 147.979 193.419 1.00 58.79  ? 905  VAL A CG2   1 
ATOM   5382  N  N     . ILE A 1 906  ? 142.750 145.201 196.454 1.00 56.03  ? 906  ILE A N     1 
ATOM   5383  C  CA    . ILE A 1 906  ? 143.661 144.760 197.503 1.00 55.98  ? 906  ILE A CA    1 
ATOM   5384  C  C     . ILE A 1 906  ? 145.079 145.149 197.110 1.00 59.86  ? 906  ILE A C     1 
ATOM   5385  O  O     . ILE A 1 906  ? 145.568 144.756 196.044 1.00 61.62  ? 906  ILE A O     1 
ATOM   5386  C  CB    . ILE A 1 906  ? 143.547 143.247 197.738 1.00 51.84  ? 906  ILE A CB    1 
ATOM   5387  C  CG1   . ILE A 1 906  ? 142.125 142.893 198.166 1.00 54.03  ? 906  ILE A CG1   1 
ATOM   5388  C  CG2   . ILE A 1 906  ? 144.543 142.796 198.787 1.00 47.18  ? 906  ILE A CG2   1 
ATOM   5389  C  CD1   . ILE A 1 906  ? 141.745 141.466 197.878 1.00 56.60  ? 906  ILE A CD1   1 
ATOM   5390  N  N     . ILE A 1 907  ? 145.741 145.916 197.972 1.00 59.68  ? 907  ILE A N     1 
ATOM   5391  C  CA    . ILE A 1 907  ? 147.095 146.403 197.730 1.00 57.41  ? 907  ILE A CA    1 
ATOM   5392  C  C     . ILE A 1 907  ? 147.887 146.297 199.026 1.00 60.51  ? 907  ILE A C     1 
ATOM   5393  O  O     . ILE A 1 907  ? 147.399 146.689 200.090 1.00 62.83  ? 907  ILE A O     1 
ATOM   5394  C  CB    . ILE A 1 907  ? 147.088 147.853 197.205 1.00 57.43  ? 907  ILE A CB    1 
ATOM   5395  C  CG1   . ILE A 1 907  ? 148.506 148.421 197.161 1.00 58.25  ? 907  ILE A CG1   1 
ATOM   5396  C  CG2   . ILE A 1 907  ? 146.171 148.728 198.040 1.00 59.72  ? 907  ILE A CG2   1 
ATOM   5397  C  CD1   . ILE A 1 907  ? 148.606 149.746 196.446 1.00 58.72  ? 907  ILE A CD1   1 
ATOM   5398  N  N     . THR A 1 908  ? 149.099 145.755 198.942 1.00 61.56  ? 908  THR A N     1 
ATOM   5399  C  CA    . THR A 1 908  ? 149.990 145.633 200.088 1.00 62.51  ? 908  THR A CA    1 
ATOM   5400  C  C     . THR A 1 908  ? 151.274 146.413 199.832 1.00 61.46  ? 908  THR A C     1 
ATOM   5401  O  O     . THR A 1 908  ? 151.544 146.862 198.717 1.00 64.57  ? 908  THR A O     1 
ATOM   5402  C  CB    . THR A 1 908  ? 150.311 144.164 200.395 1.00 65.18  ? 908  THR A CB    1 
ATOM   5403  O  OG1   . THR A 1 908  ? 151.077 144.085 201.603 1.00 70.68  ? 908  THR A OG1   1 
ATOM   5404  C  CG2   . THR A 1 908  ? 151.108 143.547 199.266 1.00 61.26  ? 908  THR A CG2   1 
ATOM   5405  N  N     . SER A 1 909  ? 152.068 146.576 200.894 1.00 61.77  ? 909  SER A N     1 
ATOM   5406  C  CA    . SER A 1 909  ? 153.284 147.380 200.799 1.00 61.83  ? 909  SER A CA    1 
ATOM   5407  C  C     . SER A 1 909  ? 154.303 146.769 199.847 1.00 62.72  ? 909  SER A C     1 
ATOM   5408  O  O     . SER A 1 909  ? 155.039 147.502 199.177 1.00 59.33  ? 909  SER A O     1 
ATOM   5409  C  CB    . SER A 1 909  ? 153.905 147.561 202.183 1.00 62.64  ? 909  SER A CB    1 
ATOM   5410  O  OG    . SER A 1 909  ? 154.357 146.324 202.701 1.00 63.03  ? 909  SER A OG    1 
ATOM   5411  N  N     . THR A 1 910  ? 154.370 145.441 199.773 1.00 64.20  ? 910  THR A N     1 
ATOM   5412  C  CA    . THR A 1 910  ? 155.346 144.768 198.926 1.00 63.29  ? 910  THR A CA    1 
ATOM   5413  C  C     . THR A 1 910  ? 154.865 144.571 197.494 1.00 60.26  ? 910  THR A C     1 
ATOM   5414  O  O     . THR A 1 910  ? 155.644 144.099 196.659 1.00 59.07  ? 910  THR A O     1 
ATOM   5415  C  CB    . THR A 1 910  ? 155.720 143.405 199.519 1.00 61.41  ? 910  THR A CB    1 
ATOM   5416  O  OG1   . THR A 1 910  ? 154.601 142.517 199.420 1.00 65.35  ? 910  THR A OG1   1 
ATOM   5417  C  CG2   . THR A 1 910  ? 156.112 143.548 200.979 1.00 57.65  ? 910  THR A CG2   1 
ATOM   5418  N  N     . SER A 1 911  ? 153.612 144.912 197.189 1.00 54.63  ? 911  SER A N     1 
ATOM   5419  C  CA    . SER A 1 911  ? 153.078 144.793 195.837 1.00 48.58  ? 911  SER A CA    1 
ATOM   5420  C  C     . SER A 1 911  ? 152.592 146.122 195.278 1.00 46.15  ? 911  SER A C     1 
ATOM   5421  O  O     . SER A 1 911  ? 151.848 146.131 194.292 1.00 45.93  ? 911  SER A O     1 
ATOM   5422  C  CB    . SER A 1 911  ? 151.934 143.777 195.795 1.00 51.97  ? 911  SER A CB    1 
ATOM   5423  O  OG    . SER A 1 911  ? 150.696 144.398 196.081 1.00 52.33  ? 911  SER A OG    1 
ATOM   5424  N  N     . SER A 1 912  ? 152.986 147.244 195.881 1.00 46.98  ? 912  SER A N     1 
ATOM   5425  C  CA    . SER A 1 912  ? 152.533 148.553 195.427 1.00 44.06  ? 912  SER A CA    1 
ATOM   5426  C  C     . SER A 1 912  ? 153.236 149.021 194.160 1.00 40.52  ? 912  SER A C     1 
ATOM   5427  O  O     . SER A 1 912  ? 152.863 150.067 193.620 1.00 40.97  ? 912  SER A O     1 
ATOM   5428  C  CB    . SER A 1 912  ? 152.734 149.584 196.535 1.00 44.69  ? 912  SER A CB    1 
ATOM   5429  O  OG    . SER A 1 912  ? 154.103 149.921 196.663 1.00 49.70  ? 912  SER A OG    1 
ATOM   5430  N  N     . TYR A 1 913  ? 154.243 148.287 193.682 1.00 38.43  ? 913  TYR A N     1 
ATOM   5431  C  CA    . TYR A 1 913  ? 154.957 148.679 192.473 1.00 34.28  ? 913  TYR A CA    1 
ATOM   5432  C  C     . TYR A 1 913  ? 154.129 148.492 191.207 1.00 35.08  ? 913  TYR A C     1 
ATOM   5433  O  O     . TYR A 1 913  ? 154.528 148.982 190.147 1.00 38.80  ? 913  TYR A O     1 
ATOM   5434  C  CB    . TYR A 1 913  ? 156.278 147.909 192.380 1.00 34.76  ? 913  TYR A CB    1 
ATOM   5435  C  CG    . TYR A 1 913  ? 156.146 146.420 192.128 1.00 36.14  ? 913  TYR A CG    1 
ATOM   5436  C  CD1   . TYR A 1 913  ? 156.076 145.910 190.839 1.00 34.09  ? 913  TYR A CD1   1 
ATOM   5437  C  CD2   . TYR A 1 913  ? 156.108 145.524 193.184 1.00 38.49  ? 913  TYR A CD2   1 
ATOM   5438  C  CE1   . TYR A 1 913  ? 155.963 144.555 190.615 1.00 32.52  ? 913  TYR A CE1   1 
ATOM   5439  C  CE2   . TYR A 1 913  ? 155.994 144.170 192.967 1.00 36.62  ? 913  TYR A CE2   1 
ATOM   5440  C  CZ    . TYR A 1 913  ? 155.923 143.691 191.683 1.00 33.28  ? 913  TYR A CZ    1 
ATOM   5441  O  OH    . TYR A 1 913  ? 155.810 142.341 191.464 1.00 36.44  ? 913  TYR A OH    1 
ATOM   5442  N  N     . TYR A 1 914  ? 152.996 147.791 191.289 1.00 33.12  ? 914  TYR A N     1 
ATOM   5443  C  CA    . TYR A 1 914  ? 152.139 147.601 190.122 1.00 32.73  ? 914  TYR A CA    1 
ATOM   5444  C  C     . TYR A 1 914  ? 151.475 148.887 189.648 1.00 35.70  ? 914  TYR A C     1 
ATOM   5445  O  O     . TYR A 1 914  ? 150.925 148.910 188.540 1.00 37.87  ? 914  TYR A O     1 
ATOM   5446  C  CB    . TYR A 1 914  ? 151.069 146.559 190.424 1.00 30.03  ? 914  TYR A CB    1 
ATOM   5447  C  CG    . TYR A 1 914  ? 151.541 145.133 190.320 1.00 30.85  ? 914  TYR A CG    1 
ATOM   5448  C  CD1   . TYR A 1 914  ? 151.922 144.601 189.099 1.00 35.34  ? 914  TYR A CD1   1 
ATOM   5449  C  CD2   . TYR A 1 914  ? 151.599 144.318 191.436 1.00 32.69  ? 914  TYR A CD2   1 
ATOM   5450  C  CE1   . TYR A 1 914  ? 152.345 143.295 188.991 1.00 35.08  ? 914  TYR A CE1   1 
ATOM   5451  C  CE2   . TYR A 1 914  ? 152.026 143.012 191.337 1.00 33.92  ? 914  TYR A CE2   1 
ATOM   5452  C  CZ    . TYR A 1 914  ? 152.397 142.506 190.113 1.00 35.39  ? 914  TYR A CZ    1 
ATOM   5453  O  OH    . TYR A 1 914  ? 152.821 141.206 190.008 1.00 42.42  ? 914  TYR A OH    1 
ATOM   5454  N  N     . VAL A 1 915  ? 151.490 149.945 190.459 1.00 33.25  ? 915  VAL A N     1 
ATOM   5455  C  CA    . VAL A 1 915  ? 150.839 151.189 190.060 1.00 33.90  ? 915  VAL A CA    1 
ATOM   5456  C  C     . VAL A 1 915  ? 151.478 151.744 188.794 1.00 37.94  ? 915  VAL A C     1 
ATOM   5457  O  O     . VAL A 1 915  ? 150.783 152.161 187.859 1.00 39.36  ? 915  VAL A O     1 
ATOM   5458  C  CB    . VAL A 1 915  ? 150.888 152.209 191.212 1.00 35.28  ? 915  VAL A CB    1 
ATOM   5459  C  CG1   . VAL A 1 915  ? 150.502 153.589 190.715 1.00 34.18  ? 915  VAL A CG1   1 
ATOM   5460  C  CG2   . VAL A 1 915  ? 149.980 151.772 192.345 1.00 35.21  ? 915  VAL A CG2   1 
ATOM   5461  N  N     . PHE A 1 916  ? 152.811 151.743 188.734 1.00 36.62  ? 916  PHE A N     1 
ATOM   5462  C  CA    . PHE A 1 916  ? 153.498 152.291 187.570 1.00 37.47  ? 916  PHE A CA    1 
ATOM   5463  C  C     . PHE A 1 916  ? 153.299 151.408 186.347 1.00 38.62  ? 916  PHE A C     1 
ATOM   5464  O  O     . PHE A 1 916  ? 153.175 151.911 185.225 1.00 41.83  ? 916  PHE A O     1 
ATOM   5465  C  CB    . PHE A 1 916  ? 154.983 152.466 187.875 1.00 43.70  ? 916  PHE A CB    1 
ATOM   5466  C  CG    . PHE A 1 916  ? 155.254 153.400 189.013 1.00 50.35  ? 916  PHE A CG    1 
ATOM   5467  C  CD1   . PHE A 1 916  ? 155.185 154.770 188.837 1.00 54.52  ? 916  PHE A CD1   1 
ATOM   5468  C  CD2   . PHE A 1 916  ? 155.570 152.905 190.264 1.00 51.05  ? 916  PHE A CD2   1 
ATOM   5469  C  CE1   . PHE A 1 916  ? 155.429 155.630 189.888 1.00 56.07  ? 916  PHE A CE1   1 
ATOM   5470  C  CE2   . PHE A 1 916  ? 155.816 153.757 191.317 1.00 58.80  ? 916  PHE A CE2   1 
ATOM   5471  C  CZ    . PHE A 1 916  ? 155.746 155.122 191.129 1.00 60.61  ? 916  PHE A CZ    1 
ATOM   5472  N  N     . TYR A 1 917  ? 153.258 150.090 186.545 1.00 36.29  ? 917  TYR A N     1 
ATOM   5473  C  CA    . TYR A 1 917  ? 153.010 149.176 185.436 1.00 32.23  ? 917  TYR A CA    1 
ATOM   5474  C  C     . TYR A 1 917  ? 151.627 149.408 184.841 1.00 33.00  ? 917  TYR A C     1 
ATOM   5475  O  O     . TYR A 1 917  ? 151.466 149.466 183.616 1.00 35.92  ? 917  TYR A O     1 
ATOM   5476  C  CB    . TYR A 1 917  ? 153.158 147.733 185.914 1.00 32.42  ? 917  TYR A CB    1 
ATOM   5477  C  CG    . TYR A 1 917  ? 154.592 147.269 186.004 1.00 34.24  ? 917  TYR A CG    1 
ATOM   5478  C  CD1   . TYR A 1 917  ? 155.396 147.663 187.060 1.00 36.06  ? 917  TYR A CD1   1 
ATOM   5479  C  CD2   . TYR A 1 917  ? 155.141 146.440 185.039 1.00 34.85  ? 917  TYR A CD2   1 
ATOM   5480  C  CE1   . TYR A 1 917  ? 156.703 147.249 187.153 1.00 35.88  ? 917  TYR A CE1   1 
ATOM   5481  C  CE2   . TYR A 1 917  ? 156.452 146.019 185.125 1.00 35.86  ? 917  TYR A CE2   1 
ATOM   5482  C  CZ    . TYR A 1 917  ? 157.228 146.428 186.186 1.00 38.40  ? 917  TYR A CZ    1 
ATOM   5483  O  OH    . TYR A 1 917  ? 158.534 146.017 186.287 1.00 39.62  ? 917  TYR A OH    1 
ATOM   5484  N  N     . ILE A 1 918  ? 150.618 149.573 185.697 1.00 36.19  ? 918  ILE A N     1 
ATOM   5485  C  CA    . ILE A 1 918  ? 149.266 149.831 185.212 1.00 37.06  ? 918  ILE A CA    1 
ATOM   5486  C  C     . ILE A 1 918  ? 149.185 151.195 184.533 1.00 37.41  ? 918  ILE A C     1 
ATOM   5487  O  O     . ILE A 1 918  ? 148.514 151.351 183.503 1.00 40.45  ? 918  ILE A O     1 
ATOM   5488  C  CB    . ILE A 1 918  ? 148.257 149.701 186.368 1.00 32.51  ? 918  ILE A CB    1 
ATOM   5489  C  CG1   . ILE A 1 918  ? 148.149 148.241 186.806 1.00 33.24  ? 918  ILE A CG1   1 
ATOM   5490  C  CG2   . ILE A 1 918  ? 146.898 150.223 185.955 1.00 29.75  ? 918  ILE A CG2   1 
ATOM   5491  C  CD1   . ILE A 1 918  ? 147.511 148.056 188.157 1.00 32.59  ? 918  ILE A CD1   1 
ATOM   5492  N  N     . TYR A 1 919  ? 149.857 152.204 185.094 1.00 35.07  ? 919  TYR A N     1 
ATOM   5493  C  CA    . TYR A 1 919  ? 149.862 153.521 184.464 1.00 37.21  ? 919  TYR A CA    1 
ATOM   5494  C  C     . TYR A 1 919  ? 150.468 153.464 183.069 1.00 39.37  ? 919  TYR A C     1 
ATOM   5495  O  O     . TYR A 1 919  ? 149.941 154.063 182.127 1.00 41.86  ? 919  TYR A O     1 
ATOM   5496  C  CB    . TYR A 1 919  ? 150.622 154.529 185.322 1.00 41.77  ? 919  TYR A CB    1 
ATOM   5497  C  CG    . TYR A 1 919  ? 150.753 155.863 184.633 1.00 46.47  ? 919  TYR A CG    1 
ATOM   5498  C  CD1   . TYR A 1 919  ? 149.661 156.706 184.505 1.00 48.88  ? 919  TYR A CD1   1 
ATOM   5499  C  CD2   . TYR A 1 919  ? 151.955 156.258 184.070 1.00 47.44  ? 919  TYR A CD2   1 
ATOM   5500  C  CE1   . TYR A 1 919  ? 149.771 157.916 183.860 1.00 50.65  ? 919  TYR A CE1   1 
ATOM   5501  C  CE2   . TYR A 1 919  ? 152.072 157.463 183.419 1.00 49.32  ? 919  TYR A CE2   1 
ATOM   5502  C  CZ    . TYR A 1 919  ? 150.978 158.291 183.318 1.00 51.58  ? 919  TYR A CZ    1 
ATOM   5503  O  OH    . TYR A 1 919  ? 151.090 159.499 182.674 1.00 54.76  ? 919  TYR A OH    1 
ATOM   5504  N  N     . VAL A 1 920  ? 151.600 152.773 182.922 1.00 40.37  ? 920  VAL A N     1 
ATOM   5505  C  CA    . VAL A 1 920  ? 152.210 152.645 181.603 1.00 37.11  ? 920  VAL A CA    1 
ATOM   5506  C  C     . VAL A 1 920  ? 151.301 151.857 180.670 1.00 38.35  ? 920  VAL A C     1 
ATOM   5507  O  O     . VAL A 1 920  ? 151.213 152.159 179.474 1.00 41.34  ? 920  VAL A O     1 
ATOM   5508  C  CB    . VAL A 1 920  ? 153.607 152.006 181.726 1.00 38.36  ? 920  VAL A CB    1 
ATOM   5509  C  CG1   . VAL A 1 920  ? 154.095 151.503 180.380 1.00 38.80  ? 920  VAL A CG1   1 
ATOM   5510  C  CG2   . VAL A 1 920  ? 154.592 153.006 182.304 1.00 35.50  ? 920  VAL A CG2   1 
ATOM   5511  N  N     . GLY A 1 921  ? 150.587 150.861 181.198 1.00 35.74  ? 921  GLY A N     1 
ATOM   5512  C  CA    . GLY A 1 921  ? 149.678 150.094 180.365 1.00 33.95  ? 921  GLY A CA    1 
ATOM   5513  C  C     . GLY A 1 921  ? 148.491 150.889 179.860 1.00 38.15  ? 921  GLY A C     1 
ATOM   5514  O  O     . GLY A 1 921  ? 147.988 150.625 178.765 1.00 42.30  ? 921  GLY A O     1 
ATOM   5515  N  N     . VAL A 1 922  ? 148.020 151.862 180.640 1.00 40.97  ? 922  VAL A N     1 
ATOM   5516  C  CA    . VAL A 1 922  ? 146.833 152.634 180.272 1.00 40.93  ? 922  VAL A CA    1 
ATOM   5517  C  C     . VAL A 1 922  ? 147.162 154.042 179.802 1.00 42.36  ? 922  VAL A C     1 
ATOM   5518  O  O     . VAL A 1 922  ? 146.237 154.827 179.555 1.00 45.02  ? 922  VAL A O     1 
ATOM   5519  C  CB    . VAL A 1 922  ? 145.810 152.691 181.423 1.00 38.14  ? 922  VAL A CB    1 
ATOM   5520  C  CG1   . VAL A 1 922  ? 145.395 151.289 181.848 1.00 37.52  ? 922  VAL A CG1   1 
ATOM   5521  C  CG2   . VAL A 1 922  ? 146.363 153.484 182.598 1.00 37.45  ? 922  VAL A CG2   1 
ATOM   5522  N  N     . ALA A 1 923  ? 148.443 154.397 179.685 1.00 43.29  ? 923  ALA A N     1 
ATOM   5523  C  CA    . ALA A 1 923  ? 148.804 155.738 179.234 1.00 41.97  ? 923  ALA A CA    1 
ATOM   5524  C  C     . ALA A 1 923  ? 148.378 156.025 177.800 1.00 44.26  ? 923  ALA A C     1 
ATOM   5525  O  O     . ALA A 1 923  ? 148.211 157.196 177.443 1.00 46.44  ? 923  ALA A O     1 
ATOM   5526  C  CB    . ALA A 1 923  ? 150.310 155.951 179.368 1.00 41.31  ? 923  ALA A CB    1 
ATOM   5527  N  N     . ASP A 1 924  ? 148.205 154.999 176.965 1.00 44.85  ? 924  ASP A N     1 
ATOM   5528  C  CA    . ASP A 1 924  ? 147.838 155.248 175.576 1.00 45.98  ? 924  ASP A CA    1 
ATOM   5529  C  C     . ASP A 1 924  ? 146.446 155.856 175.441 1.00 46.58  ? 924  ASP A C     1 
ATOM   5530  O  O     . ASP A 1 924  ? 146.113 156.378 174.373 1.00 45.92  ? 924  ASP A O     1 
ATOM   5531  C  CB    . ASP A 1 924  ? 147.943 153.955 174.761 1.00 45.39  ? 924  ASP A CB    1 
ATOM   5532  C  CG    . ASP A 1 924  ? 146.678 153.123 174.807 1.00 49.41  ? 924  ASP A CG    1 
ATOM   5533  O  OD1   . ASP A 1 924  ? 146.256 152.628 173.741 1.00 48.14  ? 924  ASP A OD1   1 
ATOM   5534  O  OD2   . ASP A 1 924  ? 146.113 152.944 175.907 1.00 49.63  ? 924  ASP A OD2   1 
ATOM   5535  N  N     . THR A 1 925  ? 145.631 155.801 176.493 1.00 46.70  ? 925  THR A N     1 
ATOM   5536  C  CA    . THR A 1 925  ? 144.321 156.439 176.508 1.00 44.34  ? 925  THR A CA    1 
ATOM   5537  C  C     . THR A 1 925  ? 144.334 157.807 177.170 1.00 45.05  ? 925  THR A C     1 
ATOM   5538  O  O     . THR A 1 925  ? 143.638 158.714 176.706 1.00 47.04  ? 925  THR A O     1 
ATOM   5539  C  CB    . THR A 1 925  ? 143.304 155.548 177.230 1.00 44.59  ? 925  THR A CB    1 
ATOM   5540  O  OG1   . THR A 1 925  ? 143.289 154.251 176.624 1.00 49.41  ? 925  THR A OG1   1 
ATOM   5541  C  CG2   . THR A 1 925  ? 141.914 156.147 177.151 1.00 41.74  ? 925  THR A CG2   1 
ATOM   5542  N  N     . LEU A 1 926  ? 145.122 157.980 178.232 1.00 44.05  ? 926  LEU A N     1 
ATOM   5543  C  CA    . LEU A 1 926  ? 145.191 159.263 178.919 1.00 44.62  ? 926  LEU A CA    1 
ATOM   5544  C  C     . LEU A 1 926  ? 145.875 160.331 178.079 1.00 47.15  ? 926  LEU A C     1 
ATOM   5545  O  O     . LEU A 1 926  ? 145.767 161.518 178.401 1.00 47.05  ? 926  LEU A O     1 
ATOM   5546  C  CB    . LEU A 1 926  ? 145.925 159.102 180.250 1.00 43.23  ? 926  LEU A CB    1 
ATOM   5547  C  CG    . LEU A 1 926  ? 145.289 158.140 181.254 1.00 43.30  ? 926  LEU A CG    1 
ATOM   5548  C  CD1   . LEU A 1 926  ? 146.212 157.916 182.435 1.00 42.37  ? 926  LEU A CD1   1 
ATOM   5549  C  CD2   . LEU A 1 926  ? 143.940 158.661 181.719 1.00 43.28  ? 926  LEU A CD2   1 
ATOM   5550  N  N     . LEU A 1 927  ? 146.582 159.938 177.021 1.00 44.63  ? 927  LEU A N     1 
ATOM   5551  C  CA    . LEU A 1 927  ? 147.318 160.871 176.179 1.00 42.66  ? 927  LEU A CA    1 
ATOM   5552  C  C     . LEU A 1 927  ? 146.799 160.900 174.747 1.00 45.97  ? 927  LEU A C     1 
ATOM   5553  O  O     . LEU A 1 927  ? 147.427 161.524 173.885 1.00 48.56  ? 927  LEU A O     1 
ATOM   5554  C  CB    . LEU A 1 927  ? 148.809 160.525 176.196 1.00 40.49  ? 927  LEU A CB    1 
ATOM   5555  C  CG    . LEU A 1 927  ? 149.480 160.594 177.570 1.00 44.26  ? 927  LEU A CG    1 
ATOM   5556  C  CD1   . LEU A 1 927  ? 150.869 159.985 177.534 1.00 40.40  ? 927  LEU A CD1   1 
ATOM   5557  C  CD2   . LEU A 1 927  ? 149.535 162.027 178.070 1.00 46.49  ? 927  LEU A CD2   1 
ATOM   5558  N  N     . ALA A 1 928  ? 145.675 160.244 174.472 1.00 46.31  ? 928  ALA A N     1 
ATOM   5559  C  CA    . ALA A 1 928  ? 145.119 160.211 173.125 1.00 44.76  ? 928  ALA A CA    1 
ATOM   5560  C  C     . ALA A 1 928  ? 144.541 161.569 172.743 1.00 48.31  ? 928  ALA A C     1 
ATOM   5561  O  O     . ALA A 1 928  ? 143.938 162.255 173.573 1.00 45.93  ? 928  ALA A O     1 
ATOM   5562  C  CB    . ALA A 1 928  ? 144.044 159.132 173.025 1.00 41.46  ? 928  ALA A CB    1 
ATOM   5563  N  N     . MET A 1 929  ? 144.731 161.957 171.483 1.00 47.85  ? 929  MET A N     1 
ATOM   5564  C  CA    . MET A 1 929  ? 144.249 163.241 170.981 1.00 44.37  ? 929  MET A CA    1 
ATOM   5565  C  C     . MET A 1 929  ? 142.790 163.110 170.553 1.00 46.39  ? 929  MET A C     1 
ATOM   5566  O  O     . MET A 1 929  ? 142.469 162.343 169.640 1.00 47.29  ? 929  MET A O     1 
ATOM   5567  C  CB    . MET A 1 929  ? 145.126 163.724 169.828 1.00 43.61  ? 929  MET A CB    1 
ATOM   5568  C  CG    . MET A 1 929  ? 146.498 164.209 170.275 1.00 46.46  ? 929  MET A CG    1 
ATOM   5569  S  SD    . MET A 1 929  ? 147.526 164.906 168.969 1.00 49.49  ? 929  MET A SD    1 
ATOM   5570  C  CE    . MET A 1 929  ? 147.233 163.753 167.639 1.00 45.08  ? 929  MET A CE    1 
ATOM   5571  N  N     . GLY A 1 930  ? 141.907 163.849 171.218 1.00 46.01  ? 930  GLY A N     1 
ATOM   5572  C  CA    . GLY A 1 930  ? 140.497 163.841 170.891 1.00 41.22  ? 930  GLY A CA    1 
ATOM   5573  C  C     . GLY A 1 930  ? 140.185 164.654 169.647 1.00 44.49  ? 930  GLY A C     1 
ATOM   5574  O  O     . GLY A 1 930  ? 141.055 165.230 168.994 1.00 46.04  ? 930  GLY A O     1 
ATOM   5575  N  N     . PHE A 1 931  ? 138.892 164.691 169.310 1.00 45.21  ? 931  PHE A N     1 
ATOM   5576  C  CA    . PHE A 1 931  ? 138.466 165.364 168.086 1.00 45.64  ? 931  PHE A CA    1 
ATOM   5577  C  C     . PHE A 1 931  ? 138.613 166.880 168.165 1.00 47.15  ? 931  PHE A C     1 
ATOM   5578  O  O     . PHE A 1 931  ? 138.507 167.553 167.135 1.00 49.17  ? 931  PHE A O     1 
ATOM   5579  C  CB    . PHE A 1 931  ? 137.025 164.978 167.734 1.00 46.90  ? 931  PHE A CB    1 
ATOM   5580  C  CG    . PHE A 1 931  ? 136.025 165.302 168.803 1.00 49.23  ? 931  PHE A CG    1 
ATOM   5581  C  CD1   . PHE A 1 931  ? 135.393 166.533 168.833 1.00 50.64  ? 931  PHE A CD1   1 
ATOM   5582  C  CD2   . PHE A 1 931  ? 135.702 164.366 169.767 1.00 52.63  ? 931  PHE A CD2   1 
ATOM   5583  C  CE1   . PHE A 1 931  ? 134.471 166.831 169.815 1.00 54.95  ? 931  PHE A CE1   1 
ATOM   5584  C  CE2   . PHE A 1 931  ? 134.779 164.654 170.752 1.00 57.47  ? 931  PHE A CE2   1 
ATOM   5585  C  CZ    . PHE A 1 931  ? 134.162 165.890 170.776 1.00 58.92  ? 931  PHE A CZ    1 
ATOM   5586  N  N     . PHE A 1 932  ? 138.842 167.438 169.354 1.00 47.96  ? 932  PHE A N     1 
ATOM   5587  C  CA    . PHE A 1 932  ? 139.228 168.841 169.433 1.00 47.57  ? 932  PHE A CA    1 
ATOM   5588  C  C     . PHE A 1 932  ? 140.670 169.069 169.007 1.00 46.78  ? 932  PHE A C     1 
ATOM   5589  O  O     . PHE A 1 932  ? 141.060 170.221 168.788 1.00 48.17  ? 932  PHE A O     1 
ATOM   5590  C  CB    . PHE A 1 932  ? 139.022 169.381 170.849 1.00 51.28  ? 932  PHE A CB    1 
ATOM   5591  C  CG    . PHE A 1 932  ? 137.583 169.471 171.265 1.00 60.07  ? 932  PHE A CG    1 
ATOM   5592  C  CD1   . PHE A 1 932  ? 137.148 168.875 172.436 1.00 60.96  ? 932  PHE A CD1   1 
ATOM   5593  C  CD2   . PHE A 1 932  ? 136.666 170.156 170.488 1.00 61.91  ? 932  PHE A CD2   1 
ATOM   5594  C  CE1   . PHE A 1 932  ? 135.827 168.959 172.824 1.00 62.27  ? 932  PHE A CE1   1 
ATOM   5595  C  CE2   . PHE A 1 932  ? 135.343 170.243 170.869 1.00 65.15  ? 932  PHE A CE2   1 
ATOM   5596  C  CZ    . PHE A 1 932  ? 134.922 169.644 172.040 1.00 64.52  ? 932  PHE A CZ    1 
ATOM   5597  N  N     . ARG A 1 933  ? 141.465 168.011 168.893 1.00 47.09  ? 933  ARG A N     1 
ATOM   5598  C  CA    . ARG A 1 933  ? 142.846 168.103 168.446 1.00 45.09  ? 933  ARG A CA    1 
ATOM   5599  C  C     . ARG A 1 933  ? 143.120 167.361 167.148 1.00 44.20  ? 933  ARG A C     1 
ATOM   5600  O  O     . ARG A 1 933  ? 144.002 167.775 166.395 1.00 47.11  ? 933  ARG A O     1 
ATOM   5601  C  CB    . ARG A 1 933  ? 143.796 167.569 169.530 1.00 40.78  ? 933  ARG A CB    1 
ATOM   5602  C  CG    . ARG A 1 933  ? 143.919 168.465 170.745 1.00 39.86  ? 933  ARG A CG    1 
ATOM   5603  C  CD    . ARG A 1 933  ? 145.109 168.067 171.595 1.00 43.46  ? 933  ARG A CD    1 
ATOM   5604  N  NE    . ARG A 1 933  ? 144.862 166.824 172.315 1.00 46.81  ? 933  ARG A NE    1 
ATOM   5605  C  CZ    . ARG A 1 933  ? 145.783 166.164 173.002 1.00 48.03  ? 933  ARG A CZ    1 
ATOM   5606  N  NH1   . ARG A 1 933  ? 147.030 166.594 173.075 1.00 46.20  ? 933  ARG A NH1   1 
ATOM   5607  N  NH2   . ARG A 1 933  ? 145.444 165.041 173.629 1.00 45.96  ? 933  ARG A NH2   1 
ATOM   5608  N  N     . GLY A 1 934  ? 142.397 166.280 166.870 1.00 41.27  ? 934  GLY A N     1 
ATOM   5609  C  CA    . GLY A 1 934  ? 142.658 165.464 165.701 1.00 40.06  ? 934  GLY A CA    1 
ATOM   5610  C  C     . GLY A 1 934  ? 142.143 166.012 164.386 1.00 42.19  ? 934  GLY A C     1 
ATOM   5611  O  O     . GLY A 1 934  ? 142.780 165.820 163.347 1.00 46.73  ? 934  GLY A O     1 
ATOM   5612  N  N     . LEU A 1 935  ? 140.995 166.688 164.409 1.00 40.01  ? 935  LEU A N     1 
ATOM   5613  C  CA    . LEU A 1 935  ? 140.338 167.147 163.187 1.00 39.55  ? 935  LEU A CA    1 
ATOM   5614  C  C     . LEU A 1 935  ? 140.969 168.415 162.604 1.00 39.37  ? 935  LEU A C     1 
ATOM   5615  O  O     . LEU A 1 935  ? 141.215 168.469 161.387 1.00 42.13  ? 935  LEU A O     1 
ATOM   5616  C  CB    . LEU A 1 935  ? 138.843 167.363 163.450 1.00 40.26  ? 935  LEU A CB    1 
ATOM   5617  C  CG    . LEU A 1 935  ? 137.970 166.114 163.599 1.00 39.50  ? 935  LEU A CG    1 
ATOM   5618  C  CD1   . LEU A 1 935  ? 136.582 166.493 164.081 1.00 35.64  ? 935  LEU A CD1   1 
ATOM   5619  C  CD2   . LEU A 1 935  ? 137.880 165.346 162.294 1.00 34.40  ? 935  LEU A CD2   1 
ATOM   5620  N  N     . PRO A 1 936  ? 141.239 169.457 163.407 1.00 40.46  ? 936  PRO A N     1 
ATOM   5621  C  CA    . PRO A 1 936  ? 141.905 170.640 162.838 1.00 40.69  ? 936  PRO A CA    1 
ATOM   5622  C  C     . PRO A 1 936  ? 143.261 170.333 162.232 1.00 40.38  ? 936  PRO A C     1 
ATOM   5623  O  O     . PRO A 1 936  ? 143.644 170.961 161.236 1.00 44.51  ? 936  PRO A O     1 
ATOM   5624  C  CB    . PRO A 1 936  ? 142.025 171.590 164.039 1.00 38.76  ? 936  PRO A CB    1 
ATOM   5625  C  CG    . PRO A 1 936  ? 140.960 171.160 164.966 1.00 35.82  ? 936  PRO A CG    1 
ATOM   5626  C  CD    . PRO A 1 936  ? 140.911 169.676 164.828 1.00 40.14  ? 936  PRO A CD    1 
ATOM   5627  N  N     . LEU A 1 937  ? 143.993 169.373 162.798 1.00 35.72  ? 937  LEU A N     1 
ATOM   5628  C  CA    . LEU A 1 937  ? 145.303 169.023 162.262 1.00 36.78  ? 937  LEU A CA    1 
ATOM   5629  C  C     . LEU A 1 937  ? 145.190 168.519 160.827 1.00 36.60  ? 937  LEU A C     1 
ATOM   5630  O  O     . LEU A 1 937  ? 145.899 168.992 159.930 1.00 41.01  ? 937  LEU A O     1 
ATOM   5631  C  CB    . LEU A 1 937  ? 145.960 167.976 163.160 1.00 36.62  ? 937  LEU A CB    1 
ATOM   5632  C  CG    . LEU A 1 937  ? 147.368 167.515 162.789 1.00 38.93  ? 937  LEU A CG    1 
ATOM   5633  C  CD1   . LEU A 1 937  ? 148.318 168.695 162.767 1.00 40.11  ? 937  LEU A CD1   1 
ATOM   5634  C  CD2   . LEU A 1 937  ? 147.856 166.448 163.750 1.00 33.65  ? 937  LEU A CD2   1 
ATOM   5635  N  N     . VAL A 1 938  ? 144.278 167.576 160.588 1.00 33.01  ? 938  VAL A N     1 
ATOM   5636  C  CA    . VAL A 1 938  ? 144.103 167.020 159.250 1.00 35.57  ? 938  VAL A CA    1 
ATOM   5637  C  C     . VAL A 1 938  ? 143.553 168.077 158.298 1.00 37.49  ? 938  VAL A C     1 
ATOM   5638  O  O     . VAL A 1 938  ? 143.946 168.144 157.123 1.00 40.88  ? 938  VAL A O     1 
ATOM   5639  C  CB    . VAL A 1 938  ? 143.193 165.781 159.310 1.00 37.66  ? 938  VAL A CB    1 
ATOM   5640  C  CG1   . VAL A 1 938  ? 142.902 165.275 157.920 1.00 40.22  ? 938  VAL A CG1   1 
ATOM   5641  C  CG2   . VAL A 1 938  ? 143.826 164.689 160.154 1.00 32.98  ? 938  VAL A CG2   1 
ATOM   5642  N  N     . HIS A 1 939  ? 142.634 168.915 158.786 1.00 35.49  ? 939  HIS A N     1 
ATOM   5643  C  CA    . HIS A 1 939  ? 142.078 169.980 157.957 1.00 32.19  ? 939  HIS A CA    1 
ATOM   5644  C  C     . HIS A 1 939  ? 143.182 170.904 157.444 1.00 35.01  ? 939  HIS A C     1 
ATOM   5645  O  O     . HIS A 1 939  ? 143.284 171.180 156.236 1.00 38.87  ? 939  HIS A O     1 
ATOM   5646  C  CB    . HIS A 1 939  ? 141.039 170.751 158.778 1.00 32.41  ? 939  HIS A CB    1 
ATOM   5647  C  CG    . HIS A 1 939  ? 140.373 171.873 158.043 1.00 37.36  ? 939  HIS A CG    1 
ATOM   5648  N  ND1   . HIS A 1 939  ? 139.193 171.711 157.351 1.00 36.49  ? 939  HIS A ND1   1 
ATOM   5649  C  CD2   . HIS A 1 939  ? 140.709 173.177 157.910 1.00 38.23  ? 939  HIS A CD2   1 
ATOM   5650  C  CE1   . HIS A 1 939  ? 138.836 172.865 156.818 1.00 34.63  ? 939  HIS A CE1   1 
ATOM   5651  N  NE2   . HIS A 1 939  ? 139.741 173.771 157.140 1.00 36.41  ? 939  HIS A NE2   1 
ATOM   5652  N  N     . THR A 1 940  ? 144.053 171.355 158.349 1.00 32.52  ? 940  THR A N     1 
ATOM   5653  C  CA    . THR A 1 940  ? 145.139 172.244 157.956 1.00 33.49  ? 940  THR A CA    1 
ATOM   5654  C  C     . THR A 1 940  ? 146.160 171.536 157.072 1.00 35.27  ? 940  THR A C     1 
ATOM   5655  O  O     . THR A 1 940  ? 146.730 172.156 156.162 1.00 39.95  ? 940  THR A O     1 
ATOM   5656  C  CB    . THR A 1 940  ? 145.810 172.814 159.201 1.00 38.35  ? 940  THR A CB    1 
ATOM   5657  O  OG1   . THR A 1 940  ? 144.820 173.032 160.211 1.00 34.95  ? 940  THR A OG1   1 
ATOM   5658  C  CG2   . THR A 1 940  ? 146.481 174.128 158.881 1.00 45.02  ? 940  THR A CG2   1 
ATOM   5659  N  N     . LEU A 1 941  ? 146.403 170.246 157.316 1.00 32.20  ? 941  LEU A N     1 
ATOM   5660  C  CA    . LEU A 1 941  ? 147.343 169.513 156.477 1.00 29.55  ? 941  LEU A CA    1 
ATOM   5661  C  C     . LEU A 1 941  ? 146.832 169.377 155.048 1.00 32.78  ? 941  LEU A C     1 
ATOM   5662  O  O     . LEU A 1 941  ? 147.630 169.333 154.107 1.00 34.32  ? 941  LEU A O     1 
ATOM   5663  C  CB    . LEU A 1 941  ? 147.627 168.139 157.084 1.00 28.67  ? 941  LEU A CB    1 
ATOM   5664  C  CG    . LEU A 1 941  ? 148.598 168.142 158.268 1.00 31.17  ? 941  LEU A CG    1 
ATOM   5665  C  CD1   . LEU A 1 941  ? 148.584 166.810 158.994 1.00 29.98  ? 941  LEU A CD1   1 
ATOM   5666  C  CD2   . LEU A 1 941  ? 150.000 168.496 157.827 1.00 36.21  ? 941  LEU A CD2   1 
ATOM   5667  N  N     . ILE A 1 942  ? 145.514 169.292 154.863 1.00 31.47  ? 942  ILE A N     1 
ATOM   5668  C  CA    . ILE A 1 942  ? 144.976 169.296 153.502 1.00 30.13  ? 942  ILE A CA    1 
ATOM   5669  C  C     . ILE A 1 942  ? 145.075 170.687 152.873 1.00 30.95  ? 942  ILE A C     1 
ATOM   5670  O  O     . ILE A 1 942  ? 145.385 170.821 151.672 1.00 34.46  ? 942  ILE A O     1 
ATOM   5671  C  CB    . ILE A 1 942  ? 143.527 168.781 153.506 1.00 31.49  ? 942  ILE A CB    1 
ATOM   5672  C  CG1   . ILE A 1 942  ? 143.490 167.301 153.877 1.00 28.62  ? 942  ILE A CG1   1 
ATOM   5673  C  CG2   . ILE A 1 942  ? 142.872 168.995 152.157 1.00 33.42  ? 942  ILE A CG2   1 
ATOM   5674  C  CD1   . ILE A 1 942  ? 142.138 166.832 154.313 1.00 33.27  ? 942  ILE A CD1   1 
ATOM   5675  N  N     . THR A 1 943  ? 144.837 171.738 153.663 1.00 29.84  ? 943  THR A N     1 
ATOM   5676  C  CA    . THR A 1 943  ? 144.960 173.090 153.121 1.00 29.20  ? 943  THR A CA    1 
ATOM   5677  C  C     . THR A 1 943  ? 146.378 173.370 152.632 1.00 30.75  ? 943  THR A C     1 
ATOM   5678  O  O     . THR A 1 943  ? 146.568 174.066 151.620 1.00 37.00  ? 943  THR A O     1 
ATOM   5679  C  CB    . THR A 1 943  ? 144.550 174.113 154.178 1.00 30.91  ? 943  THR A CB    1 
ATOM   5680  O  OG1   . THR A 1 943  ? 143.244 173.789 154.665 1.00 35.12  ? 943  THR A OG1   1 
ATOM   5681  C  CG2   . THR A 1 943  ? 144.520 175.507 153.590 1.00 30.81  ? 943  THR A CG2   1 
ATOM   5682  N  N     . VAL A 1 944  ? 147.376 172.818 153.323 1.00 31.01  ? 944  VAL A N     1 
ATOM   5683  C  CA    . VAL A 1 944  ? 148.766 173.011 152.913 1.00 30.01  ? 944  VAL A CA    1 
ATOM   5684  C  C     . VAL A 1 944  ? 148.993 172.455 151.509 1.00 32.74  ? 944  VAL A C     1 
ATOM   5685  O  O     . VAL A 1 944  ? 149.626 173.098 150.660 1.00 36.06  ? 944  VAL A O     1 
ATOM   5686  C  CB    . VAL A 1 944  ? 149.717 172.365 153.935 1.00 29.73  ? 944  VAL A CB    1 
ATOM   5687  C  CG1   . VAL A 1 944  ? 151.117 172.260 153.366 1.00 29.66  ? 944  VAL A CG1   1 
ATOM   5688  C  CG2   . VAL A 1 944  ? 149.718 173.158 155.227 1.00 35.58  ? 944  VAL A CG2   1 
ATOM   5689  N  N     . SER A 1 945  ? 148.480 171.251 151.244 1.00 32.35  ? 945  SER A N     1 
ATOM   5690  C  CA    . SER A 1 945  ? 148.656 170.648 149.928 1.00 31.09  ? 945  SER A CA    1 
ATOM   5691  C  C     . SER A 1 945  ? 147.911 171.422 148.852 1.00 31.99  ? 945  SER A C     1 
ATOM   5692  O  O     . SER A 1 945  ? 148.392 171.522 147.715 1.00 36.29  ? 945  SER A O     1 
ATOM   5693  C  CB    . SER A 1 945  ? 148.189 169.194 149.941 1.00 35.30  ? 945  SER A CB    1 
ATOM   5694  O  OG    . SER A 1 945  ? 146.791 169.111 150.140 1.00 36.83  ? 945  SER A OG    1 
ATOM   5695  N  N     . LYS A 1 946  ? 146.744 171.980 149.183 1.00 30.98  ? 946  LYS A N     1 
ATOM   5696  C  CA    . LYS A 1 946  ? 146.054 172.831 148.212 1.00 31.36  ? 946  LYS A CA    1 
ATOM   5697  C  C     . LYS A 1 946  ? 146.921 174.021 147.813 1.00 30.88  ? 946  LYS A C     1 
ATOM   5698  O  O     . LYS A 1 946  ? 147.091 174.319 146.618 1.00 32.49  ? 946  LYS A O     1 
ATOM   5699  C  CB    . LYS A 1 946  ? 144.726 173.315 148.786 1.00 32.42  ? 946  LYS A CB    1 
ATOM   5700  C  CG    . LYS A 1 946  ? 143.894 174.109 147.804 1.00 38.46  ? 946  LYS A CG    1 
ATOM   5701  C  CD    . LYS A 1 946  ? 142.819 174.901 148.517 1.00 38.70  ? 946  LYS A CD    1 
ATOM   5702  C  CE    . LYS A 1 946  ? 143.416 176.065 149.277 1.00 36.30  ? 946  LYS A CE    1 
ATOM   5703  N  NZ    . LYS A 1 946  ? 142.358 176.921 149.874 1.00 40.23  ? 946  LYS A NZ    1 
ATOM   5704  N  N     . ILE A 1 947  ? 147.497 174.698 148.808 1.00 30.25  ? 947  ILE A N     1 
ATOM   5705  C  CA    . ILE A 1 947  ? 148.344 175.854 148.523 1.00 30.06  ? 947  ILE A CA    1 
ATOM   5706  C  C     . ILE A 1 947  ? 149.542 175.445 147.673 1.00 30.31  ? 947  ILE A C     1 
ATOM   5707  O  O     . ILE A 1 947  ? 149.917 176.143 146.718 1.00 32.21  ? 947  ILE A O     1 
ATOM   5708  C  CB    . ILE A 1 947  ? 148.784 176.530 149.833 1.00 31.14  ? 947  ILE A CB    1 
ATOM   5709  C  CG1   . ILE A 1 947  ? 147.585 177.170 150.532 1.00 33.24  ? 947  ILE A CG1   1 
ATOM   5710  C  CG2   . ILE A 1 947  ? 149.855 177.568 149.566 1.00 31.44  ? 947  ILE A CG2   1 
ATOM   5711  C  CD1   . ILE A 1 947  ? 147.822 177.467 151.993 1.00 33.99  ? 947  ILE A CD1   1 
ATOM   5712  N  N     . LEU A 1 948  ? 150.162 174.307 148.004 1.00 29.59  ? 948  LEU A N     1 
ATOM   5713  C  CA    . LEU A 1 948  ? 151.349 173.876 147.269 1.00 27.24  ? 948  LEU A CA    1 
ATOM   5714  C  C     . LEU A 1 948  ? 151.026 173.533 145.820 1.00 27.25  ? 948  LEU A C     1 
ATOM   5715  O  O     . LEU A 1 948  ? 151.809 173.852 144.920 1.00 27.20  ? 948  LEU A O     1 
ATOM   5716  C  CB    . LEU A 1 948  ? 152.010 172.689 147.965 1.00 29.72  ? 948  LEU A CB    1 
ATOM   5717  C  CG    . LEU A 1 948  ? 152.740 172.999 149.271 1.00 32.43  ? 948  LEU A CG    1 
ATOM   5718  C  CD1   . LEU A 1 948  ? 153.248 171.721 149.907 1.00 29.90  ? 948  LEU A CD1   1 
ATOM   5719  C  CD2   . LEU A 1 948  ? 153.881 173.967 149.033 1.00 34.78  ? 948  LEU A CD2   1 
ATOM   5720  N  N     . HIS A 1 949  ? 149.888 172.879 145.568 1.00 29.36  ? 949  HIS A N     1 
ATOM   5721  C  CA    . HIS A 1 949  ? 149.505 172.598 144.185 1.00 29.40  ? 949  HIS A CA    1 
ATOM   5722  C  C     . HIS A 1 949  ? 149.285 173.883 143.398 1.00 30.36  ? 949  HIS A C     1 
ATOM   5723  O  O     . HIS A 1 949  ? 149.706 173.993 142.235 1.00 31.78  ? 949  HIS A O     1 
ATOM   5724  C  CB    . HIS A 1 949  ? 148.249 171.731 144.142 1.00 28.47  ? 949  HIS A CB    1 
ATOM   5725  C  CG    . HIS A 1 949  ? 147.726 171.497 142.757 1.00 35.05  ? 949  HIS A CG    1 
ATOM   5726  N  ND1   . HIS A 1 949  ? 146.945 172.417 142.093 1.00 34.37  ? 949  HIS A ND1   1 
ATOM   5727  C  CD2   . HIS A 1 949  ? 147.873 170.451 141.911 1.00 37.15  ? 949  HIS A CD2   1 
ATOM   5728  C  CE1   . HIS A 1 949  ? 146.632 171.946 140.899 1.00 32.94  ? 949  HIS A CE1   1 
ATOM   5729  N  NE2   . HIS A 1 949  ? 147.183 170.754 140.764 1.00 35.16  ? 949  HIS A NE2   1 
ATOM   5730  N  N     . HIS A 1 950  ? 148.618 174.866 144.010 1.00 31.41  ? 950  HIS A N     1 
ATOM   5731  C  CA    . HIS A 1 950  ? 148.410 176.132 143.314 1.00 27.84  ? 950  HIS A CA    1 
ATOM   5732  C  C     . HIS A 1 950  ? 149.741 176.792 142.960 1.00 28.22  ? 950  HIS A C     1 
ATOM   5733  O  O     . HIS A 1 950  ? 149.945 177.231 141.817 1.00 30.87  ? 950  HIS A O     1 
ATOM   5734  C  CB    . HIS A 1 950  ? 147.554 177.058 144.175 1.00 31.94  ? 950  HIS A CB    1 
ATOM   5735  C  CG    . HIS A 1 950  ? 147.220 178.360 143.520 1.00 41.27  ? 950  HIS A CG    1 
ATOM   5736  N  ND1   . HIS A 1 950  ? 148.019 179.476 143.635 1.00 39.89  ? 950  HIS A ND1   1 
ATOM   5737  C  CD2   . HIS A 1 950  ? 146.169 178.728 142.750 1.00 41.42  ? 950  HIS A CD2   1 
ATOM   5738  C  CE1   . HIS A 1 950  ? 147.478 180.474 142.961 1.00 38.07  ? 950  HIS A CE1   1 
ATOM   5739  N  NE2   . HIS A 1 950  ? 146.354 180.047 142.415 1.00 43.06  ? 950  HIS A NE2   1 
ATOM   5740  N  N     . LYS A 1 951  ? 150.673 176.838 143.919 1.00 27.28  ? 951  LYS A N     1 
ATOM   5741  C  CA    . LYS A 1 951  ? 151.980 177.437 143.655 1.00 28.79  ? 951  LYS A CA    1 
ATOM   5742  C  C     . LYS A 1 951  ? 152.734 176.678 142.573 1.00 28.77  ? 951  LYS A C     1 
ATOM   5743  O  O     . LYS A 1 951  ? 153.416 177.284 141.742 1.00 27.99  ? 951  LYS A O     1 
ATOM   5744  C  CB    . LYS A 1 951  ? 152.819 177.482 144.931 1.00 32.56  ? 951  LYS A CB    1 
ATOM   5745  C  CG    . LYS A 1 951  ? 152.436 178.558 145.917 1.00 31.52  ? 951  LYS A CG    1 
ATOM   5746  C  CD    . LYS A 1 951  ? 153.338 178.500 147.134 1.00 32.02  ? 951  LYS A CD    1 
ATOM   5747  C  CE    . LYS A 1 951  ? 152.971 179.569 148.139 1.00 39.10  ? 951  LYS A CE    1 
ATOM   5748  N  NZ    . LYS A 1 951  ? 153.299 180.924 147.635 1.00 42.57  ? 951  LYS A NZ    1 
ATOM   5749  N  N     . MET A 1 952  ? 152.648 175.348 142.587 1.00 31.02  ? 952  MET A N     1 
ATOM   5750  C  CA    . MET A 1 952  ? 153.364 174.537 141.608 1.00 27.64  ? 952  MET A CA    1 
ATOM   5751  C  C     . MET A 1 952  ? 152.863 174.810 140.195 1.00 31.32  ? 952  MET A C     1 
ATOM   5752  O  O     . MET A 1 952  ? 153.661 174.989 139.264 1.00 33.26  ? 952  MET A O     1 
ATOM   5753  C  CB    . MET A 1 952  ? 153.209 173.062 141.974 1.00 28.44  ? 952  MET A CB    1 
ATOM   5754  C  CG    . MET A 1 952  ? 154.100 172.099 141.230 1.00 35.71  ? 952  MET A CG    1 
ATOM   5755  S  SD    . MET A 1 952  ? 153.357 170.459 141.221 1.00 44.40  ? 952  MET A SD    1 
ATOM   5756  C  CE    . MET A 1 952  ? 154.688 169.486 140.542 1.00 32.92  ? 952  MET A CE    1 
ATOM   5757  N  N     . LEU A 1 953  ? 151.540 174.859 140.017 1.00 32.97  ? 953  LEU A N     1 
ATOM   5758  C  CA    . LEU A 1 953  ? 150.992 175.166 138.699 1.00 29.64  ? 953  LEU A CA    1 
ATOM   5759  C  C     . LEU A 1 953  ? 151.397 176.564 138.243 1.00 29.56  ? 953  LEU A C     1 
ATOM   5760  O  O     . LEU A 1 953  ? 151.800 176.760 137.086 1.00 28.24  ? 953  LEU A O     1 
ATOM   5761  C  CB    . LEU A 1 953  ? 149.471 175.029 138.722 1.00 34.10  ? 953  LEU A CB    1 
ATOM   5762  C  CG    . LEU A 1 953  ? 148.737 175.229 137.395 1.00 36.36  ? 953  LEU A CG    1 
ATOM   5763  C  CD1   . LEU A 1 953  ? 149.073 174.114 136.422 1.00 35.85  ? 953  LEU A CD1   1 
ATOM   5764  C  CD2   . LEU A 1 953  ? 147.243 175.319 137.616 1.00 38.05  ? 953  LEU A CD2   1 
ATOM   5765  N  N     . HIS A 1 954  ? 151.315 177.546 139.147 1.00 32.41  ? 954  HIS A N     1 
ATOM   5766  C  CA    . HIS A 1 954  ? 151.698 178.909 138.791 1.00 33.93  ? 954  HIS A CA    1 
ATOM   5767  C  C     . HIS A 1 954  ? 153.163 178.986 138.378 1.00 33.12  ? 954  HIS A C     1 
ATOM   5768  O  O     . HIS A 1 954  ? 153.509 179.659 137.401 1.00 31.84  ? 954  HIS A O     1 
ATOM   5769  C  CB    . HIS A 1 954  ? 151.427 179.854 139.960 1.00 37.18  ? 954  HIS A CB    1 
ATOM   5770  C  CG    . HIS A 1 954  ? 151.706 181.289 139.648 1.00 42.61  ? 954  HIS A CG    1 
ATOM   5771  N  ND1   . HIS A 1 954  ? 150.972 182.009 138.733 1.00 45.33  ? 954  HIS A ND1   1 
ATOM   5772  C  CD2   . HIS A 1 954  ? 152.657 182.132 140.114 1.00 43.86  ? 954  HIS A CD2   1 
ATOM   5773  C  CE1   . HIS A 1 954  ? 151.449 183.239 138.660 1.00 49.83  ? 954  HIS A CE1   1 
ATOM   5774  N  NE2   . HIS A 1 954  ? 152.473 183.339 139.487 1.00 52.43  ? 954  HIS A NE2   1 
ATOM   5775  N  N     . SER A 1 955  ? 154.041 178.310 139.119 1.00 35.82  ? 955  SER A N     1 
ATOM   5776  C  CA    . SER A 1 955  ? 155.462 178.324 138.790 1.00 32.93  ? 955  SER A CA    1 
ATOM   5777  C  C     . SER A 1 955  ? 155.730 177.656 137.449 1.00 34.66  ? 955  SER A C     1 
ATOM   5778  O  O     . SER A 1 955  ? 156.577 178.122 136.679 1.00 34.84  ? 955  SER A O     1 
ATOM   5779  C  CB    . SER A 1 955  ? 156.264 177.640 139.897 1.00 29.41  ? 955  SER A CB    1 
ATOM   5780  O  OG    . SER A 1 955  ? 157.652 177.697 139.630 1.00 39.35  ? 955  SER A OG    1 
ATOM   5781  N  N     . VAL A 1 956  ? 155.031 176.559 137.154 1.00 35.15  ? 956  VAL A N     1 
ATOM   5782  C  CA    . VAL A 1 956  ? 155.257 175.871 135.886 1.00 29.59  ? 956  VAL A CA    1 
ATOM   5783  C  C     . VAL A 1 956  ? 154.845 176.748 134.711 1.00 28.79  ? 956  VAL A C     1 
ATOM   5784  O  O     . VAL A 1 956  ? 155.570 176.853 133.715 1.00 32.59  ? 956  VAL A O     1 
ATOM   5785  C  CB    . VAL A 1 956  ? 154.522 174.520 135.868 1.00 32.56  ? 956  VAL A CB    1 
ATOM   5786  C  CG1   . VAL A 1 956  ? 154.392 174.013 134.448 1.00 29.68  ? 956  VAL A CG1   1 
ATOM   5787  C  CG2   . VAL A 1 956  ? 155.269 173.516 136.719 1.00 33.48  ? 956  VAL A CG2   1 
ATOM   5788  N  N     . LEU A 1 957  ? 153.681 177.399 134.803 1.00 33.14  ? 957  LEU A N     1 
ATOM   5789  C  CA    . LEU A 1 957  ? 153.217 178.184 133.660 1.00 29.64  ? 957  LEU A CA    1 
ATOM   5790  C  C     . LEU A 1 957  ? 154.073 179.415 133.382 1.00 32.55  ? 957  LEU A C     1 
ATOM   5791  O  O     . LEU A 1 957  ? 153.985 179.970 132.283 1.00 36.95  ? 957  LEU A O     1 
ATOM   5792  C  CB    . LEU A 1 957  ? 151.764 178.615 133.846 1.00 32.53  ? 957  LEU A CB    1 
ATOM   5793  C  CG    . LEU A 1 957  ? 150.705 177.521 133.729 1.00 32.14  ? 957  LEU A CG    1 
ATOM   5794  C  CD1   . LEU A 1 957  ? 149.350 178.064 134.111 1.00 36.25  ? 957  LEU A CD1   1 
ATOM   5795  C  CD2   . LEU A 1 957  ? 150.674 176.952 132.325 1.00 30.88  ? 957  LEU A CD2   1 
ATOM   5796  N  N     . GLN A 1 958  ? 154.882 179.867 134.341 1.00 36.19  ? 958  GLN A N     1 
ATOM   5797  C  CA    . GLN A 1 958  ? 155.660 181.090 134.185 1.00 35.65  ? 958  GLN A CA    1 
ATOM   5798  C  C     . GLN A 1 958  ? 157.105 180.852 133.766 1.00 34.10  ? 958  GLN A C     1 
ATOM   5799  O  O     . GLN A 1 958  ? 157.847 181.823 133.592 1.00 36.96  ? 958  GLN A O     1 
ATOM   5800  C  CB    . GLN A 1 958  ? 155.648 181.893 135.491 1.00 38.86  ? 958  GLN A CB    1 
ATOM   5801  C  CG    . GLN A 1 958  ? 154.305 182.509 135.834 1.00 44.94  ? 958  GLN A CG    1 
ATOM   5802  C  CD    . GLN A 1 958  ? 154.110 183.870 135.207 1.00 52.19  ? 958  GLN A CD    1 
ATOM   5803  O  OE1   . GLN A 1 958  ? 154.888 184.792 135.446 1.00 59.72  ? 958  GLN A OE1   1 
ATOM   5804  N  NE2   . GLN A 1 958  ? 153.063 184.008 134.403 1.00 51.29  ? 958  GLN A NE2   1 
ATOM   5805  N  N     . ALA A 1 959  ? 157.521 179.600 133.608 1.00 34.82  ? 959  ALA A N     1 
ATOM   5806  C  CA    . ALA A 1 959  ? 158.916 179.292 133.330 1.00 37.65  ? 959  ALA A CA    1 
ATOM   5807  C  C     . ALA A 1 959  ? 159.293 179.671 131.897 1.00 45.36  ? 959  ALA A C     1 
ATOM   5808  O  O     . ALA A 1 959  ? 158.435 179.716 131.011 1.00 46.90  ? 959  ALA A O     1 
ATOM   5809  C  CB    . ALA A 1 959  ? 159.183 177.808 133.561 1.00 35.60  ? 959  ALA A CB    1 
ATOM   5810  N  N     . PRO A 1 960  ? 160.572 179.955 131.646 1.00 43.80  ? 960  PRO A N     1 
ATOM   5811  C  CA    . PRO A 1 960  ? 161.013 180.209 130.271 1.00 41.58  ? 960  PRO A CA    1 
ATOM   5812  C  C     . PRO A 1 960  ? 160.964 178.954 129.414 1.00 40.47  ? 960  PRO A C     1 
ATOM   5813  O  O     . PRO A 1 960  ? 161.008 177.827 129.912 1.00 39.63  ? 960  PRO A O     1 
ATOM   5814  C  CB    . PRO A 1 960  ? 162.451 180.708 130.447 1.00 40.62  ? 960  PRO A CB    1 
ATOM   5815  C  CG    . PRO A 1 960  ? 162.907 180.071 131.696 1.00 43.81  ? 960  PRO A CG    1 
ATOM   5816  C  CD    . PRO A 1 960  ? 161.696 180.026 132.595 1.00 45.57  ? 960  PRO A CD    1 
ATOM   5817  N  N     . MET A 1 961  ? 160.855 179.170 128.102 1.00 42.60  ? 961  MET A N     1 
ATOM   5818  C  CA    . MET A 1 961  ? 160.736 178.056 127.165 1.00 43.53  ? 961  MET A CA    1 
ATOM   5819  C  C     . MET A 1 961  ? 161.969 177.162 127.165 1.00 45.28  ? 961  MET A C     1 
ATOM   5820  O  O     . MET A 1 961  ? 161.860 175.964 126.884 1.00 46.25  ? 961  MET A O     1 
ATOM   5821  C  CB    . MET A 1 961  ? 160.465 178.586 125.754 1.00 39.88  ? 961  MET A CB    1 
ATOM   5822  C  CG    . MET A 1 961  ? 159.143 179.330 125.585 1.00 37.69  ? 961  MET A CG    1 
ATOM   5823  S  SD    . MET A 1 961  ? 157.590 178.401 125.678 1.00 48.33  ? 961  MET A SD    1 
ATOM   5824  C  CE    . MET A 1 961  ? 158.106 176.690 125.584 1.00 41.31  ? 961  MET A CE    1 
ATOM   5825  N  N     . SER A 1 962  ? 163.147 177.718 127.452 1.00 44.05  ? 962  SER A N     1 
ATOM   5826  C  CA    . SER A 1 962  ? 164.357 176.903 127.468 1.00 44.36  ? 962  SER A CA    1 
ATOM   5827  C  C     . SER A 1 962  ? 164.275 175.825 128.541 1.00 46.93  ? 962  SER A C     1 
ATOM   5828  O  O     . SER A 1 962  ? 164.718 174.690 128.332 1.00 50.35  ? 962  SER A O     1 
ATOM   5829  C  CB    . SER A 1 962  ? 165.582 177.787 127.684 1.00 41.04  ? 962  SER A CB    1 
ATOM   5830  O  OG    . SER A 1 962  ? 165.589 178.332 128.990 1.00 46.79  ? 962  SER A OG    1 
ATOM   5831  N  N     . THR A 1 963  ? 163.711 176.166 129.700 1.00 44.52  ? 963  THR A N     1 
ATOM   5832  C  CA    . THR A 1 963  ? 163.524 175.184 130.762 1.00 41.96  ? 963  THR A CA    1 
ATOM   5833  C  C     . THR A 1 963  ? 162.450 174.168 130.396 1.00 43.32  ? 963  THR A C     1 
ATOM   5834  O  O     . THR A 1 963  ? 162.606 172.969 130.654 1.00 43.38  ? 963  THR A O     1 
ATOM   5835  C  CB    . THR A 1 963  ? 163.164 175.898 132.064 1.00 43.39  ? 963  THR A CB    1 
ATOM   5836  O  OG1   . THR A 1 963  ? 164.272 176.698 132.495 1.00 46.76  ? 963  THR A OG1   1 
ATOM   5837  C  CG2   . THR A 1 963  ? 162.813 174.900 133.147 1.00 43.91  ? 963  THR A CG2   1 
ATOM   5838  N  N     . LEU A 1 964  ? 161.356 174.628 129.786 1.00 46.07  ? 964  LEU A N     1 
ATOM   5839  C  CA    . LEU A 1 964  ? 160.214 173.754 129.544 1.00 42.89  ? 964  LEU A CA    1 
ATOM   5840  C  C     . LEU A 1 964  ? 160.494 172.720 128.463 1.00 47.84  ? 964  LEU A C     1 
ATOM   5841  O  O     . LEU A 1 964  ? 159.922 171.626 128.500 1.00 50.94  ? 964  LEU A O     1 
ATOM   5842  C  CB    . LEU A 1 964  ? 158.987 174.585 129.174 1.00 40.96  ? 964  LEU A CB    1 
ATOM   5843  C  CG    . LEU A 1 964  ? 158.449 175.495 130.279 1.00 43.75  ? 964  LEU A CG    1 
ATOM   5844  C  CD1   . LEU A 1 964  ? 157.467 176.504 129.717 1.00 41.63  ? 964  LEU A CD1   1 
ATOM   5845  C  CD2   . LEU A 1 964  ? 157.801 174.671 131.378 1.00 39.30  ? 964  LEU A CD2   1 
ATOM   5846  N  N     . ASN A 1 965  ? 161.355 173.039 127.494 1.00 47.26  ? 965  ASN A N     1 
ATOM   5847  C  CA    . ASN A 1 965  ? 161.619 172.098 126.409 1.00 48.08  ? 965  ASN A CA    1 
ATOM   5848  C  C     . ASN A 1 965  ? 162.319 170.840 126.904 1.00 50.94  ? 965  ASN A C     1 
ATOM   5849  O  O     . ASN A 1 965  ? 162.146 169.767 126.315 1.00 54.35  ? 965  ASN A O     1 
ATOM   5850  C  CB    . ASN A 1 965  ? 162.449 172.768 125.316 1.00 49.05  ? 965  ASN A CB    1 
ATOM   5851  C  CG    . ASN A 1 965  ? 161.650 173.765 124.504 1.00 54.01  ? 965  ASN A CG    1 
ATOM   5852  O  OD1   . ASN A 1 965  ? 160.425 173.679 124.422 1.00 54.46  ? 965  ASN A OD1   1 
ATOM   5853  N  ND2   . ASN A 1 965  ? 162.341 174.720 123.894 1.00 54.72  ? 965  ASN A ND2   1 
ATOM   5854  N  N     . THR A 1 966  ? 163.108 170.944 127.973 1.00 46.94  ? 966  THR A N     1 
ATOM   5855  C  CA    . THR A 1 966  ? 163.824 169.785 128.492 1.00 49.05  ? 966  THR A CA    1 
ATOM   5856  C  C     . THR A 1 966  ? 162.934 168.839 129.289 1.00 50.56  ? 966  THR A C     1 
ATOM   5857  O  O     . THR A 1 966  ? 163.295 167.670 129.458 1.00 51.64  ? 966  THR A O     1 
ATOM   5858  C  CB    . THR A 1 966  ? 164.998 170.241 129.358 1.00 49.52  ? 966  THR A CB    1 
ATOM   5859  O  OG1   . THR A 1 966  ? 164.507 170.757 130.601 1.00 50.60  ? 966  THR A OG1   1 
ATOM   5860  C  CG2   . THR A 1 966  ? 165.794 171.313 128.641 1.00 47.42  ? 966  THR A CG2   1 
ATOM   5861  N  N     . LEU A 1 967  ? 161.796 169.311 129.787 1.00 49.46  ? 967  LEU A N     1 
ATOM   5862  C  CA    . LEU A 1 967  ? 160.890 168.452 130.534 1.00 46.32  ? 967  LEU A CA    1 
ATOM   5863  C  C     . LEU A 1 967  ? 160.184 167.473 129.604 1.00 49.57  ? 967  LEU A C     1 
ATOM   5864  O  O     . LEU A 1 967  ? 159.960 167.751 128.423 1.00 51.42  ? 967  LEU A O     1 
ATOM   5865  C  CB    . LEU A 1 967  ? 159.857 169.288 131.286 1.00 46.63  ? 967  LEU A CB    1 
ATOM   5866  C  CG    . LEU A 1 967  ? 160.391 170.288 132.311 1.00 48.54  ? 967  LEU A CG    1 
ATOM   5867  C  CD1   . LEU A 1 967  ? 159.252 171.107 132.882 1.00 45.65  ? 967  LEU A CD1   1 
ATOM   5868  C  CD2   . LEU A 1 967  ? 161.152 169.578 133.415 1.00 47.15  ? 967  LEU A CD2   1 
ATOM   5869  N  N     . LYS A 1 968  ? 159.831 166.316 130.150 1.00 49.25  ? 968  LYS A N     1 
ATOM   5870  C  CA    . LYS A 1 968  ? 159.138 165.276 129.407 1.00 47.83  ? 968  LYS A CA    1 
ATOM   5871  C  C     . LYS A 1 968  ? 157.704 165.148 129.903 1.00 45.80  ? 968  LYS A C     1 
ATOM   5872  O  O     . LYS A 1 968  ? 157.396 165.473 131.052 1.00 45.91  ? 968  LYS A O     1 
ATOM   5873  C  CB    . LYS A 1 968  ? 159.867 163.937 129.535 1.00 46.19  ? 968  LYS A CB    1 
ATOM   5874  C  CG    . LYS A 1 968  ? 161.231 163.937 128.874 1.00 49.08  ? 968  LYS A CG    1 
ATOM   5875  C  CD    . LYS A 1 968  ? 161.979 162.643 129.118 1.00 53.59  ? 968  LYS A CD    1 
ATOM   5876  C  CE    . LYS A 1 968  ? 163.335 162.677 128.441 1.00 50.16  ? 968  LYS A CE    1 
ATOM   5877  N  NZ    . LYS A 1 968  ? 164.204 163.728 129.033 1.00 44.23  ? 968  LYS A NZ    1 
ATOM   5878  N  N     . ALA A 1 969  ? 156.827 164.679 129.013 1.00 41.60  ? 969  ALA A N     1 
ATOM   5879  C  CA    . ALA A 1 969  ? 155.409 164.574 129.344 1.00 41.13  ? 969  ALA A CA    1 
ATOM   5880  C  C     . ALA A 1 969  ? 155.177 163.609 130.498 1.00 40.20  ? 969  ALA A C     1 
ATOM   5881  O  O     . ALA A 1 969  ? 154.367 163.881 131.396 1.00 39.68  ? 969  ALA A O     1 
ATOM   5882  C  CB    . ALA A 1 969  ? 154.618 164.135 128.113 1.00 38.32  ? 969  ALA A CB    1 
ATOM   5883  N  N     . GLY A 1 970  ? 155.883 162.477 130.496 1.00 39.17  ? 970  GLY A N     1 
ATOM   5884  C  CA    . GLY A 1 970  ? 155.692 161.498 131.547 1.00 37.97  ? 970  GLY A CA    1 
ATOM   5885  C  C     . GLY A 1 970  ? 156.124 161.986 132.908 1.00 37.84  ? 970  GLY A C     1 
ATOM   5886  O  O     . GLY A 1 970  ? 155.486 161.659 133.910 1.00 40.07  ? 970  GLY A O     1 
ATOM   5887  N  N     . GLY A 1 971  ? 157.172 162.801 132.968 1.00 37.51  ? 971  GLY A N     1 
ATOM   5888  C  CA    . GLY A 1 971  ? 157.608 163.361 134.230 1.00 38.61  ? 971  GLY A CA    1 
ATOM   5889  C  C     . GLY A 1 971  ? 156.623 164.361 134.796 1.00 41.57  ? 971  GLY A C     1 
ATOM   5890  O  O     . GLY A 1 971  ? 156.364 164.376 136.004 1.00 42.11  ? 971  GLY A O     1 
ATOM   5891  N  N     . ILE A 1 972  ? 156.055 165.198 133.926 1.00 39.90  ? 972  ILE A N     1 
ATOM   5892  C  CA    . ILE A 1 972  ? 155.045 166.155 134.367 1.00 36.85  ? 972  ILE A CA    1 
ATOM   5893  C  C     . ILE A 1 972  ? 153.800 165.430 134.856 1.00 34.38  ? 972  ILE A C     1 
ATOM   5894  O  O     . ILE A 1 972  ? 153.231 165.782 135.897 1.00 36.24  ? 972  ILE A O     1 
ATOM   5895  C  CB    . ILE A 1 972  ? 154.718 167.150 133.239 1.00 40.15  ? 972  ILE A CB    1 
ATOM   5896  C  CG1   . ILE A 1 972  ? 155.864 168.142 133.053 1.00 39.25  ? 972  ILE A CG1   1 
ATOM   5897  C  CG2   . ILE A 1 972  ? 153.413 167.873 133.519 1.00 39.74  ? 972  ILE A CG2   1 
ATOM   5898  C  CD1   . ILE A 1 972  ? 155.903 168.767 131.687 1.00 42.42  ? 972  ILE A CD1   1 
ATOM   5899  N  N     . LEU A 1 973  ? 153.356 164.408 134.120 1.00 34.69  ? 973  LEU A N     1 
ATOM   5900  C  CA    . LEU A 1 973  ? 152.219 163.619 134.583 1.00 32.91  ? 973  LEU A CA    1 
ATOM   5901  C  C     . LEU A 1 973  ? 152.525 162.944 135.913 1.00 32.90  ? 973  LEU A C     1 
ATOM   5902  O  O     . LEU A 1 973  ? 151.678 162.919 136.812 1.00 34.29  ? 973  LEU A O     1 
ATOM   5903  C  CB    . LEU A 1 973  ? 151.830 162.580 133.533 1.00 34.00  ? 973  LEU A CB    1 
ATOM   5904  C  CG    . LEU A 1 973  ? 150.807 163.017 132.486 1.00 37.39  ? 973  LEU A CG    1 
ATOM   5905  C  CD1   . LEU A 1 973  ? 150.827 162.059 131.313 1.00 39.45  ? 973  LEU A CD1   1 
ATOM   5906  C  CD2   . LEU A 1 973  ? 149.413 163.104 133.088 1.00 32.88  ? 973  LEU A CD2   1 
ATOM   5907  N  N     . ASN A 1 974  ? 153.737 162.406 136.063 1.00 36.37  ? 974  ASN A N     1 
ATOM   5908  C  CA    . ASN A 1 974  ? 154.126 161.760 137.311 1.00 34.15  ? 974  ASN A CA    1 
ATOM   5909  C  C     . ASN A 1 974  ? 154.053 162.735 138.479 1.00 33.62  ? 974  ASN A C     1 
ATOM   5910  O  O     . ASN A 1 974  ? 153.454 162.436 139.517 1.00 34.11  ? 974  ASN A O     1 
ATOM   5911  C  CB    . ASN A 1 974  ? 155.539 161.189 137.166 1.00 33.83  ? 974  ASN A CB    1 
ATOM   5912  C  CG    . ASN A 1 974  ? 155.958 160.344 138.348 1.00 37.08  ? 974  ASN A CG    1 
ATOM   5913  O  OD1   . ASN A 1 974  ? 155.122 159.809 139.072 1.00 40.26  ? 974  ASN A OD1   1 
ATOM   5914  N  ND2   . ASN A 1 974  ? 157.263 160.212 138.546 1.00 36.66  ? 974  ASN A ND2   1 
ATOM   5915  N  N     . ARG A 1 975  ? 154.621 163.928 138.310 1.00 36.90  ? 975  ARG A N     1 
ATOM   5916  C  CA    . ARG A 1 975  ? 154.698 164.861 139.427 1.00 36.45  ? 975  ARG A CA    1 
ATOM   5917  C  C     . ARG A 1 975  ? 153.361 165.529 139.726 1.00 35.41  ? 975  ARG A C     1 
ATOM   5918  O  O     . ARG A 1 975  ? 153.107 165.891 140.878 1.00 36.46  ? 975  ARG A O     1 
ATOM   5919  C  CB    . ARG A 1 975  ? 155.788 165.899 139.163 1.00 35.97  ? 975  ARG A CB    1 
ATOM   5920  C  CG    . ARG A 1 975  ? 156.466 166.386 140.428 1.00 39.04  ? 975  ARG A CG    1 
ATOM   5921  C  CD    . ARG A 1 975  ? 157.685 167.233 140.132 1.00 38.11  ? 975  ARG A CD    1 
ATOM   5922  N  NE    . ARG A 1 975  ? 158.783 166.407 139.648 1.00 36.72  ? 975  ARG A NE    1 
ATOM   5923  C  CZ    . ARG A 1 975  ? 160.065 166.657 139.871 1.00 38.83  ? 975  ARG A CZ    1 
ATOM   5924  N  NH1   . ARG A 1 975  ? 160.452 167.713 140.566 1.00 39.51  ? 975  ARG A NH1   1 
ATOM   5925  N  NH2   . ARG A 1 975  ? 160.982 165.824 139.390 1.00 41.11  ? 975  ARG A NH2   1 
ATOM   5926  N  N     . PHE A 1 976  ? 152.494 165.701 138.728 1.00 35.15  ? 976  PHE A N     1 
ATOM   5927  C  CA    . PHE A 1 976  ? 151.169 166.247 139.005 1.00 32.91  ? 976  PHE A CA    1 
ATOM   5928  C  C     . PHE A 1 976  ? 150.154 165.193 139.427 1.00 34.07  ? 976  PHE A C     1 
ATOM   5929  O  O     . PHE A 1 976  ? 149.084 165.559 139.919 1.00 39.27  ? 976  PHE A O     1 
ATOM   5930  C  CB    . PHE A 1 976  ? 150.640 167.012 137.789 1.00 31.83  ? 976  PHE A CB    1 
ATOM   5931  C  CG    . PHE A 1 976  ? 151.082 168.447 137.738 1.00 32.24  ? 976  PHE A CG    1 
ATOM   5932  C  CD1   . PHE A 1 976  ? 150.458 169.402 138.520 1.00 32.78  ? 976  PHE A CD1   1 
ATOM   5933  C  CD2   . PHE A 1 976  ? 152.125 168.840 136.921 1.00 32.98  ? 976  PHE A CD2   1 
ATOM   5934  C  CE1   . PHE A 1 976  ? 150.858 170.718 138.483 1.00 33.31  ? 976  PHE A CE1   1 
ATOM   5935  C  CE2   . PHE A 1 976  ? 152.532 170.157 136.880 1.00 35.19  ? 976  PHE A CE2   1 
ATOM   5936  C  CZ    . PHE A 1 976  ? 151.898 171.097 137.662 1.00 33.95  ? 976  PHE A CZ    1 
ATOM   5937  N  N     . SER A 1 977  ? 150.440 163.905 139.245 1.00 36.81  ? 977  SER A N     1 
ATOM   5938  C  CA    . SER A 1 977  ? 149.500 162.890 139.703 1.00 36.02  ? 977  SER A CA    1 
ATOM   5939  C  C     . SER A 1 977  ? 149.928 162.234 141.010 1.00 39.08  ? 977  SER A C     1 
ATOM   5940  O  O     . SER A 1 977  ? 149.221 162.332 142.019 1.00 40.66  ? 977  SER A O     1 
ATOM   5941  C  CB    . SER A 1 977  ? 149.316 161.823 138.624 1.00 33.69  ? 977  SER A CB    1 
ATOM   5942  O  OG    . SER A 1 977  ? 148.355 160.864 139.020 1.00 40.67  ? 977  SER A OG    1 
ATOM   5943  N  N     . LYS A 1 978  ? 151.099 161.594 141.017 1.00 35.69  ? 978  LYS A N     1 
ATOM   5944  C  CA    . LYS A 1 978  ? 151.461 160.741 142.144 1.00 31.78  ? 978  LYS A CA    1 
ATOM   5945  C  C     . LYS A 1 978  ? 151.788 161.564 143.381 1.00 38.35  ? 978  LYS A C     1 
ATOM   5946  O  O     . LYS A 1 978  ? 151.317 161.260 144.484 1.00 45.33  ? 978  LYS A O     1 
ATOM   5947  C  CB    . LYS A 1 978  ? 152.642 159.848 141.764 1.00 33.98  ? 978  LYS A CB    1 
ATOM   5948  C  CG    . LYS A 1 978  ? 152.931 158.752 142.766 1.00 41.89  ? 978  LYS A CG    1 
ATOM   5949  C  CD    . LYS A 1 978  ? 151.798 157.751 142.810 1.00 41.65  ? 978  LYS A CD    1 
ATOM   5950  C  CE    . LYS A 1 978  ? 152.127 156.574 143.707 1.00 43.92  ? 978  LYS A CE    1 
ATOM   5951  N  NZ    . LYS A 1 978  ? 150.993 155.617 143.789 1.00 45.68  ? 978  LYS A NZ    1 
ATOM   5952  N  N     . ASP A 1 979  ? 152.591 162.617 143.217 1.00 34.08  ? 979  ASP A N     1 
ATOM   5953  C  CA    . ASP A 1 979  ? 152.977 163.433 144.362 1.00 31.27  ? 979  ASP A CA    1 
ATOM   5954  C  C     . ASP A 1 979  ? 151.780 164.172 144.941 1.00 35.54  ? 979  ASP A C     1 
ATOM   5955  O  O     . ASP A 1 979  ? 151.647 164.287 146.164 1.00 41.59  ? 979  ASP A O     1 
ATOM   5956  C  CB    . ASP A 1 979  ? 154.078 164.412 143.958 1.00 35.58  ? 979  ASP A CB    1 
ATOM   5957  C  CG    . ASP A 1 979  ? 155.303 163.712 143.412 1.00 43.98  ? 979  ASP A CG    1 
ATOM   5958  O  OD1   . ASP A 1 979  ? 155.334 162.465 143.449 1.00 45.16  ? 979  ASP A OD1   1 
ATOM   5959  O  OD2   . ASP A 1 979  ? 156.236 164.402 142.953 1.00 41.36  ? 979  ASP A OD2   1 
ATOM   5960  N  N     . ILE A 1 980  ? 150.892 164.668 144.080 1.00 34.43  ? 980  ILE A N     1 
ATOM   5961  C  CA    . ILE A 1 980  ? 149.700 165.355 144.562 1.00 32.63  ? 980  ILE A CA    1 
ATOM   5962  C  C     . ILE A 1 980  ? 148.783 164.387 145.301 1.00 36.29  ? 980  ILE A C     1 
ATOM   5963  O  O     . ILE A 1 980  ? 148.247 164.713 146.368 1.00 40.45  ? 980  ILE A O     1 
ATOM   5964  C  CB    . ILE A 1 980  ? 148.984 166.055 143.394 1.00 35.97  ? 980  ILE A CB    1 
ATOM   5965  C  CG1   . ILE A 1 980  ? 149.922 167.065 142.731 1.00 39.49  ? 980  ILE A CG1   1 
ATOM   5966  C  CG2   . ILE A 1 980  ? 147.731 166.751 143.879 1.00 35.62  ? 980  ILE A CG2   1 
ATOM   5967  C  CD1   . ILE A 1 980  ? 150.437 168.130 143.666 1.00 36.65  ? 980  ILE A CD1   1 
ATOM   5968  N  N     . ALA A 1 981  ? 148.599 163.177 144.764 1.00 35.28  ? 981  ALA A N     1 
ATOM   5969  C  CA    . ALA A 1 981  ? 147.771 162.195 145.457 1.00 38.84  ? 981  ALA A CA    1 
ATOM   5970  C  C     . ALA A 1 981  ? 148.367 161.825 146.808 1.00 40.51  ? 981  ALA A C     1 
ATOM   5971  O  O     . ALA A 1 981  ? 147.636 161.654 147.792 1.00 45.20  ? 981  ALA A O     1 
ATOM   5972  C  CB    . ALA A 1 981  ? 147.594 160.948 144.592 1.00 38.36  ? 981  ALA A CB    1 
ATOM   5973  N  N     . ILE A 1 982  ? 149.693 161.692 146.875 1.00 35.93  ? 982  ILE A N     1 
ATOM   5974  C  CA    . ILE A 1 982  ? 150.342 161.371 148.141 1.00 37.17  ? 982  ILE A CA    1 
ATOM   5975  C  C     . ILE A 1 982  ? 150.147 162.498 149.146 1.00 35.62  ? 982  ILE A C     1 
ATOM   5976  O  O     . ILE A 1 982  ? 149.830 162.257 150.316 1.00 37.37  ? 982  ILE A O     1 
ATOM   5977  C  CB    . ILE A 1 982  ? 151.833 161.061 147.916 1.00 36.51  ? 982  ILE A CB    1 
ATOM   5978  C  CG1   . ILE A 1 982  ? 151.999 159.678 147.284 1.00 37.38  ? 982  ILE A CG1   1 
ATOM   5979  C  CG2   . ILE A 1 982  ? 152.600 161.144 149.222 1.00 35.81  ? 982  ILE A CG2   1 
ATOM   5980  C  CD1   . ILE A 1 982  ? 153.337 159.464 146.621 1.00 33.35  ? 982  ILE A CD1   1 
ATOM   5981  N  N     . LEU A 1 983  ? 150.325 163.746 148.709 1.00 35.06  ? 983  LEU A N     1 
ATOM   5982  C  CA    . LEU A 1 983  ? 150.158 164.873 149.619 1.00 34.90  ? 983  LEU A CA    1 
ATOM   5983  C  C     . LEU A 1 983  ? 148.715 165.025 150.078 1.00 40.47  ? 983  LEU A C     1 
ATOM   5984  O  O     . LEU A 1 983  ? 148.467 165.566 151.161 1.00 40.23  ? 983  LEU A O     1 
ATOM   5985  C  CB    . LEU A 1 983  ? 150.637 166.166 148.961 1.00 31.77  ? 983  LEU A CB    1 
ATOM   5986  C  CG    . LEU A 1 983  ? 152.063 166.611 149.283 1.00 33.30  ? 983  LEU A CG    1 
ATOM   5987  C  CD1   . LEU A 1 983  ? 153.076 165.600 148.778 1.00 34.59  ? 983  LEU A CD1   1 
ATOM   5988  C  CD2   . LEU A 1 983  ? 152.339 167.990 148.710 1.00 29.96  ? 983  LEU A CD2   1 
ATOM   5989  N  N     . ASP A 1 984  ? 147.754 164.574 149.273 1.00 42.25  ? 984  ASP A N     1 
ATOM   5990  C  CA    . ASP A 1 984  ? 146.355 164.719 149.657 1.00 42.03  ? 984  ASP A CA    1 
ATOM   5991  C  C     . ASP A 1 984  ? 145.842 163.581 150.533 1.00 42.85  ? 984  ASP A C     1 
ATOM   5992  O  O     . ASP A 1 984  ? 145.049 163.825 151.448 1.00 43.35  ? 984  ASP A O     1 
ATOM   5993  C  CB    . ASP A 1 984  ? 145.476 164.845 148.412 1.00 45.29  ? 984  ASP A CB    1 
ATOM   5994  C  CG    . ASP A 1 984  ? 145.731 166.125 147.654 1.00 45.28  ? 984  ASP A CG    1 
ATOM   5995  O  OD1   . ASP A 1 984  ? 145.995 167.154 148.310 1.00 42.08  ? 984  ASP A OD1   1 
ATOM   5996  O  OD2   . ASP A 1 984  ? 145.658 166.108 146.409 1.00 44.74  ? 984  ASP A OD2   1 
ATOM   5997  N  N     . ASP A 1 985  ? 146.255 162.338 150.278 1.00 41.35  ? 985  ASP A N     1 
ATOM   5998  C  CA    . ASP A 1 985  ? 145.691 161.194 150.992 1.00 44.46  ? 985  ASP A CA    1 
ATOM   5999  C  C     . ASP A 1 985  ? 146.583 160.671 152.115 1.00 43.05  ? 985  ASP A C     1 
ATOM   6000  O  O     . ASP A 1 985  ? 146.148 160.586 153.266 1.00 42.17  ? 985  ASP A O     1 
ATOM   6001  C  CB    . ASP A 1 985  ? 145.386 160.065 150.003 1.00 50.50  ? 985  ASP A CB    1 
ATOM   6002  C  CG    . ASP A 1 985  ? 144.208 160.380 149.116 1.00 61.49  ? 985  ASP A CG    1 
ATOM   6003  O  OD1   . ASP A 1 985  ? 143.681 161.507 149.217 1.00 58.49  ? 985  ASP A OD1   1 
ATOM   6004  O  OD2   . ASP A 1 985  ? 143.802 159.501 148.328 1.00 68.84  ? 985  ASP A OD2   1 
ATOM   6005  N  N     . LEU A 1 986  ? 147.826 160.309 151.797 1.00 36.85  ? 986  LEU A N     1 
ATOM   6006  C  CA    . LEU A 1 986  ? 148.622 159.506 152.721 1.00 34.16  ? 986  LEU A CA    1 
ATOM   6007  C  C     . LEU A 1 986  ? 149.241 160.352 153.828 1.00 34.41  ? 986  LEU A C     1 
ATOM   6008  O  O     . LEU A 1 986  ? 149.178 159.988 155.006 1.00 37.25  ? 986  LEU A O     1 
ATOM   6009  C  CB    . LEU A 1 986  ? 149.701 158.750 151.950 1.00 36.51  ? 986  LEU A CB    1 
ATOM   6010  C  CG    . LEU A 1 986  ? 149.212 157.537 151.157 1.00 37.66  ? 986  LEU A CG    1 
ATOM   6011  C  CD1   . LEU A 1 986  ? 149.259 157.810 149.664 1.00 41.56  ? 986  LEU A CD1   1 
ATOM   6012  C  CD2   . LEU A 1 986  ? 150.029 156.308 151.505 1.00 42.65  ? 986  LEU A CD2   1 
ATOM   6013  N  N     . LEU A 1 987  ? 149.859 161.472 153.468 1.00 29.82  ? 987  LEU A N     1 
ATOM   6014  C  CA    . LEU A 1 987  ? 150.643 162.228 154.441 1.00 30.34  ? 987  LEU A CA    1 
ATOM   6015  C  C     . LEU A 1 987  ? 149.843 162.737 155.640 1.00 32.80  ? 987  LEU A C     1 
ATOM   6016  O  O     . LEU A 1 987  ? 150.333 162.590 156.776 1.00 36.60  ? 987  LEU A O     1 
ATOM   6017  C  CB    . LEU A 1 987  ? 151.346 163.386 153.719 1.00 31.63  ? 987  LEU A CB    1 
ATOM   6018  C  CG    . LEU A 1 987  ? 152.513 164.101 154.401 1.00 33.31  ? 987  LEU A CG    1 
ATOM   6019  C  CD1   . LEU A 1 987  ? 153.646 163.142 154.721 1.00 31.91  ? 987  LEU A CD1   1 
ATOM   6020  C  CD2   . LEU A 1 987  ? 153.008 165.232 153.521 1.00 31.49  ? 987  LEU A CD2   1 
ATOM   6021  N  N     . PRO A 1 988  ? 148.655 163.343 155.483 1.00 33.83  ? 988  PRO A N     1 
ATOM   6022  C  CA    . PRO A 1 988  ? 147.962 163.885 156.666 1.00 32.68  ? 988  PRO A CA    1 
ATOM   6023  C  C     . PRO A 1 988  ? 147.623 162.845 157.720 1.00 32.54  ? 988  PRO A C     1 
ATOM   6024  O  O     . PRO A 1 988  ? 147.696 163.145 158.917 1.00 35.44  ? 988  PRO A O     1 
ATOM   6025  C  CB    . PRO A 1 988  ? 146.699 164.523 156.067 1.00 33.91  ? 988  PRO A CB    1 
ATOM   6026  C  CG    . PRO A 1 988  ? 147.049 164.801 154.657 1.00 31.49  ? 988  PRO A CG    1 
ATOM   6027  C  CD    . PRO A 1 988  ? 147.922 163.663 154.247 1.00 36.03  ? 988  PRO A CD    1 
ATOM   6028  N  N     . LEU A 1 989  ? 147.245 161.632 157.316 1.00 32.24  ? 989  LEU A N     1 
ATOM   6029  C  CA    . LEU A 1 989  ? 146.887 160.608 158.289 1.00 32.04  ? 989  LEU A CA    1 
ATOM   6030  C  C     . LEU A 1 989  ? 148.093 159.850 158.825 1.00 31.48  ? 989  LEU A C     1 
ATOM   6031  O  O     . LEU A 1 989  ? 147.979 159.200 159.866 1.00 36.31  ? 989  LEU A O     1 
ATOM   6032  C  CB    . LEU A 1 989  ? 145.883 159.623 157.684 1.00 35.43  ? 989  LEU A CB    1 
ATOM   6033  C  CG    . LEU A 1 989  ? 144.389 159.913 157.885 1.00 39.51  ? 989  LEU A CG    1 
ATOM   6034  C  CD1   . LEU A 1 989  ? 144.010 159.833 159.357 1.00 31.80  ? 989  LEU A CD1   1 
ATOM   6035  C  CD2   . LEU A 1 989  ? 143.983 161.257 157.302 1.00 38.32  ? 989  LEU A CD2   1 
ATOM   6036  N  N     . THR A 1 990  ? 149.236 159.908 158.141 1.00 31.82  ? 990  THR A N     1 
ATOM   6037  C  CA    . THR A 1 990  ? 150.453 159.289 158.658 1.00 30.41  ? 990  THR A CA    1 
ATOM   6038  C  C     . THR A 1 990  ? 151.137 160.184 159.685 1.00 32.53  ? 990  THR A C     1 
ATOM   6039  O  O     . THR A 1 990  ? 151.642 159.699 160.712 1.00 36.44  ? 990  THR A O     1 
ATOM   6040  C  CB    . THR A 1 990  ? 151.405 158.975 157.503 1.00 29.77  ? 990  THR A CB    1 
ATOM   6041  O  OG1   . THR A 1 990  ? 150.776 158.061 156.597 1.00 31.23  ? 990  THR A OG1   1 
ATOM   6042  C  CG2   . THR A 1 990  ? 152.688 158.361 158.018 1.00 31.41  ? 990  THR A CG2   1 
ATOM   6043  N  N     . ILE A 1 991  ? 151.142 161.494 159.427 1.00 28.74  ? 991  ILE A N     1 
ATOM   6044  C  CA    . ILE A 1 991  ? 151.709 162.438 160.384 1.00 28.43  ? 991  ILE A CA    1 
ATOM   6045  C  C     . ILE A 1 991  ? 150.952 162.370 161.704 1.00 32.46  ? 991  ILE A C     1 
ATOM   6046  O  O     . ILE A 1 991  ? 151.543 162.480 162.787 1.00 35.88  ? 991  ILE A O     1 
ATOM   6047  C  CB    . ILE A 1 991  ? 151.706 163.858 159.789 1.00 31.76  ? 991  ILE A CB    1 
ATOM   6048  C  CG1   . ILE A 1 991  ? 152.844 164.012 158.778 1.00 32.14  ? 991  ILE A CG1   1 
ATOM   6049  C  CG2   . ILE A 1 991  ? 151.814 164.909 160.872 1.00 32.77  ? 991  ILE A CG2   1 
ATOM   6050  C  CD1   . ILE A 1 991  ? 152.760 165.266 157.953 1.00 31.33  ? 991  ILE A CD1   1 
ATOM   6051  N  N     . PHE A 1 992  ? 149.634 162.174 161.633 1.00 32.09  ? 992  PHE A N     1 
ATOM   6052  C  CA    . PHE A 1 992  ? 148.812 162.070 162.834 1.00 33.87  ? 992  PHE A CA    1 
ATOM   6053  C  C     . PHE A 1 992  ? 149.265 160.918 163.725 1.00 35.83  ? 992  PHE A C     1 
ATOM   6054  O  O     . PHE A 1 992  ? 149.476 161.096 164.932 1.00 40.42  ? 992  PHE A O     1 
ATOM   6055  C  CB    . PHE A 1 992  ? 147.347 161.904 162.428 1.00 35.55  ? 992  PHE A CB    1 
ATOM   6056  C  CG    . PHE A 1 992  ? 146.452 161.458 163.543 1.00 42.25  ? 992  PHE A CG    1 
ATOM   6057  C  CD1   . PHE A 1 992  ? 146.027 162.352 164.509 1.00 42.04  ? 992  PHE A CD1   1 
ATOM   6058  C  CD2   . PHE A 1 992  ? 146.028 160.141 163.622 1.00 42.50  ? 992  PHE A CD2   1 
ATOM   6059  C  CE1   . PHE A 1 992  ? 145.202 161.941 165.535 1.00 43.61  ? 992  PHE A CE1   1 
ATOM   6060  C  CE2   . PHE A 1 992  ? 145.205 159.724 164.647 1.00 43.89  ? 992  PHE A CE2   1 
ATOM   6061  C  CZ    . PHE A 1 992  ? 144.791 160.626 165.606 1.00 41.98  ? 992  PHE A CZ    1 
ATOM   6062  N  N     . ASP A 1 993  ? 149.425 159.725 163.145 1.00 33.83  ? 993  ASP A N     1 
ATOM   6063  C  CA    . ASP A 1 993  ? 149.863 158.572 163.925 1.00 34.86  ? 993  ASP A CA    1 
ATOM   6064  C  C     . ASP A 1 993  ? 151.266 158.771 164.479 1.00 33.36  ? 993  ASP A C     1 
ATOM   6065  O  O     . ASP A 1 993  ? 151.545 158.394 165.626 1.00 37.73  ? 993  ASP A O     1 
ATOM   6066  C  CB    . ASP A 1 993  ? 149.803 157.304 163.078 1.00 36.52  ? 993  ASP A CB    1 
ATOM   6067  C  CG    . ASP A 1 993  ? 148.391 156.922 162.704 1.00 46.64  ? 993  ASP A CG    1 
ATOM   6068  O  OD1   . ASP A 1 993  ? 147.994 155.775 162.990 1.00 49.37  ? 993  ASP A OD1   1 
ATOM   6069  O  OD2   . ASP A 1 993  ? 147.675 157.770 162.137 1.00 44.55  ? 993  ASP A OD2   1 
ATOM   6070  N  N     . PHE A 1 994  ? 152.166 159.357 163.684 1.00 29.64  ? 994  PHE A N     1 
ATOM   6071  C  CA    . PHE A 1 994  ? 153.520 159.575 164.184 1.00 28.51  ? 994  PHE A CA    1 
ATOM   6072  C  C     . PHE A 1 994  ? 153.513 160.497 165.399 1.00 29.78  ? 994  PHE A C     1 
ATOM   6073  O  O     . PHE A 1 994  ? 154.164 160.211 166.416 1.00 29.66  ? 994  PHE A O     1 
ATOM   6074  C  CB    . PHE A 1 994  ? 154.399 160.145 163.072 1.00 32.19  ? 994  PHE A CB    1 
ATOM   6075  C  CG    . PHE A 1 994  ? 155.781 160.511 163.520 1.00 33.50  ? 994  PHE A CG    1 
ATOM   6076  C  CD1   . PHE A 1 994  ? 156.605 159.562 164.097 1.00 30.24  ? 994  PHE A CD1   1 
ATOM   6077  C  CD2   . PHE A 1 994  ? 156.261 161.797 163.358 1.00 31.01  ? 994  PHE A CD2   1 
ATOM   6078  C  CE1   . PHE A 1 994  ? 157.874 159.889 164.509 1.00 27.11  ? 994  PHE A CE1   1 
ATOM   6079  C  CE2   . PHE A 1 994  ? 157.534 162.129 163.767 1.00 30.55  ? 994  PHE A CE2   1 
ATOM   6080  C  CZ    . PHE A 1 994  ? 158.341 161.173 164.342 1.00 27.62  ? 994  PHE A CZ    1 
ATOM   6081  N  N     . ILE A 1 995  ? 152.750 161.591 165.325 1.00 31.84  ? 995  ILE A N     1 
ATOM   6082  C  CA    . ILE A 1 995  ? 152.675 162.535 166.438 1.00 32.23  ? 995  ILE A CA    1 
ATOM   6083  C  C     . ILE A 1 995  ? 152.039 161.883 167.661 1.00 35.51  ? 995  ILE A C     1 
ATOM   6084  O  O     . ILE A 1 995  ? 152.482 162.096 168.798 1.00 36.90  ? 995  ILE A O     1 
ATOM   6085  C  CB    . ILE A 1 995  ? 151.914 163.802 166.008 1.00 32.12  ? 995  ILE A CB    1 
ATOM   6086  C  CG1   . ILE A 1 995  ? 152.767 164.639 165.055 1.00 35.17  ? 995  ILE A CG1   1 
ATOM   6087  C  CG2   . ILE A 1 995  ? 151.492 164.618 167.218 1.00 33.92  ? 995  ILE A CG2   1 
ATOM   6088  C  CD1   . ILE A 1 995  ? 152.003 165.745 164.384 1.00 34.95  ? 995  ILE A CD1   1 
ATOM   6089  N  N     . GLN A 1 996  ? 150.987 161.088 167.452 1.00 34.51  ? 996  GLN A N     1 
ATOM   6090  C  CA    . GLN A 1 996  ? 150.333 160.417 168.571 1.00 33.19  ? 996  GLN A CA    1 
ATOM   6091  C  C     . GLN A 1 996  ? 151.301 159.491 169.300 1.00 34.43  ? 996  GLN A C     1 
ATOM   6092  O  O     . GLN A 1 996  ? 151.376 159.496 170.538 1.00 37.47  ? 996  GLN A O     1 
ATOM   6093  C  CB    . GLN A 1 996  ? 149.116 159.642 168.067 1.00 32.88  ? 996  GLN A CB    1 
ATOM   6094  C  CG    . GLN A 1 996  ? 148.351 158.901 169.146 1.00 38.03  ? 996  GLN A CG    1 
ATOM   6095  C  CD    . GLN A 1 996  ? 147.709 159.830 170.148 1.00 45.28  ? 996  GLN A CD    1 
ATOM   6096  O  OE1   . GLN A 1 996  ? 146.585 160.285 169.952 1.00 46.89  ? 996  GLN A OE1   1 
ATOM   6097  N  NE2   . GLN A 1 996  ? 148.418 160.116 171.232 1.00 43.77  ? 996  GLN A NE2   1 
ATOM   6098  N  N     . LEU A 1 997  ? 152.059 158.692 168.544 1.00 32.04  ? 997  LEU A N     1 
ATOM   6099  C  CA    . LEU A 1 997  ? 153.011 157.775 169.163 1.00 30.53  ? 997  LEU A CA    1 
ATOM   6100  C  C     . LEU A 1 997  ? 154.102 158.532 169.912 1.00 32.37  ? 997  LEU A C     1 
ATOM   6101  O  O     . LEU A 1 997  ? 154.489 158.142 171.025 1.00 33.63  ? 997  LEU A O     1 
ATOM   6102  C  CB    . LEU A 1 997  ? 153.618 156.859 168.105 1.00 29.51  ? 997  LEU A CB    1 
ATOM   6103  C  CG    . LEU A 1 997  ? 152.688 155.762 167.588 1.00 25.86  ? 997  LEU A CG    1 
ATOM   6104  C  CD1   . LEU A 1 997  ? 153.273 155.098 166.361 1.00 26.04  ? 997  LEU A CD1   1 
ATOM   6105  C  CD2   . LEU A 1 997  ? 152.419 154.743 168.675 1.00 29.92  ? 997  LEU A CD2   1 
ATOM   6106  N  N     . LEU A 1 998  ? 154.603 159.626 169.325 1.00 32.72  ? 998  LEU A N     1 
ATOM   6107  C  CA    . LEU A 1 998  ? 155.613 160.426 170.013 1.00 32.10  ? 998  LEU A CA    1 
ATOM   6108  C  C     . LEU A 1 998  ? 155.085 160.962 171.334 1.00 34.11  ? 998  LEU A C     1 
ATOM   6109  O  O     . LEU A 1 998  ? 155.778 160.914 172.359 1.00 35.85  ? 998  LEU A O     1 
ATOM   6110  C  CB    . LEU A 1 998  ? 156.076 161.589 169.137 1.00 29.26  ? 998  LEU A CB    1 
ATOM   6111  C  CG    . LEU A 1 998  ? 157.220 161.371 168.155 1.00 34.26  ? 998  LEU A CG    1 
ATOM   6112  C  CD1   . LEU A 1 998  ? 157.400 162.632 167.332 1.00 31.65  ? 998  LEU A CD1   1 
ATOM   6113  C  CD2   . LEU A 1 998  ? 158.499 161.007 168.887 1.00 30.31  ? 998  LEU A CD2   1 
ATOM   6114  N  N     . LEU A 1 999  ? 153.861 161.500 171.325 1.00 33.99  ? 999  LEU A N     1 
ATOM   6115  C  CA    . LEU A 1 999  ? 153.301 162.068 172.546 1.00 31.96  ? 999  LEU A CA    1 
ATOM   6116  C  C     . LEU A 1 999  ? 153.122 161.002 173.616 1.00 33.21  ? 999  LEU A C     1 
ATOM   6117  O  O     . LEU A 1 999  ? 153.425 161.240 174.790 1.00 32.84  ? 999  LEU A O     1 
ATOM   6118  C  CB    . LEU A 1 999  ? 151.971 162.762 172.257 1.00 35.10  ? 999  LEU A CB    1 
ATOM   6119  C  CG    . LEU A 1 999  ? 152.037 164.064 171.462 1.00 35.90  ? 999  LEU A CG    1 
ATOM   6120  C  CD1   . LEU A 1 999  ? 150.640 164.578 171.175 1.00 35.38  ? 999  LEU A CD1   1 
ATOM   6121  C  CD2   . LEU A 1 999  ? 152.859 165.106 172.194 1.00 35.23  ? 999  LEU A CD2   1 
ATOM   6122  N  N     . ILE A 1 1000 ? 152.646 159.816 173.229 1.00 34.55  ? 1000 ILE A N     1 
ATOM   6123  C  CA    . ILE A 1 1000 ? 152.466 158.742 174.205 1.00 35.44  ? 1000 ILE A CA    1 
ATOM   6124  C  C     . ILE A 1 1000 ? 153.799 158.376 174.847 1.00 35.20  ? 1000 ILE A C     1 
ATOM   6125  O  O     . ILE A 1 1000 ? 153.915 158.290 176.079 1.00 37.10  ? 1000 ILE A O     1 
ATOM   6126  C  CB    . ILE A 1 1000 ? 151.806 157.516 173.549 1.00 34.76  ? 1000 ILE A CB    1 
ATOM   6127  C  CG1   . ILE A 1 1000 ? 150.338 157.799 173.226 1.00 38.49  ? 1000 ILE A CG1   1 
ATOM   6128  C  CG2   . ILE A 1 1000 ? 151.930 156.303 174.446 1.00 32.14  ? 1000 ILE A CG2   1 
ATOM   6129  C  CD1   . ILE A 1 1000 ? 149.727 156.813 172.252 1.00 39.75  ? 1000 ILE A CD1   1 
ATOM   6130  N  N     . VAL A 1 1001 ? 154.831 158.180 174.022 1.00 36.04  ? 1001 VAL A N     1 
ATOM   6131  C  CA    . VAL A 1 1001 ? 156.125 157.756 174.551 1.00 35.11  ? 1001 VAL A CA    1 
ATOM   6132  C  C     . VAL A 1 1001 ? 156.705 158.823 175.474 1.00 34.45  ? 1001 VAL A C     1 
ATOM   6133  O  O     . VAL A 1 1001 ? 157.156 158.525 176.590 1.00 36.35  ? 1001 VAL A O     1 
ATOM   6134  C  CB    . VAL A 1 1001 ? 157.089 157.420 173.399 1.00 34.20  ? 1001 VAL A CB    1 
ATOM   6135  C  CG1   . VAL A 1 1001 ? 158.502 157.235 173.919 1.00 33.61  ? 1001 VAL A CG1   1 
ATOM   6136  C  CG2   . VAL A 1 1001 ? 156.624 156.179 172.678 1.00 34.19  ? 1001 VAL A CG2   1 
ATOM   6137  N  N     . ILE A 1 1002 ? 156.689 160.084 175.031 1.00 32.11  ? 1002 ILE A N     1 
ATOM   6138  C  CA    . ILE A 1 1002 ? 157.286 161.158 175.819 1.00 32.57  ? 1002 ILE A CA    1 
ATOM   6139  C  C     . ILE A 1 1002 ? 156.541 161.346 177.133 1.00 35.33  ? 1002 ILE A C     1 
ATOM   6140  O  O     . ILE A 1 1002 ? 157.158 161.524 178.191 1.00 37.97  ? 1002 ILE A O     1 
ATOM   6141  C  CB    . ILE A 1 1002 ? 157.336 162.461 175.003 1.00 34.04  ? 1002 ILE A CB    1 
ATOM   6142  C  CG1   . ILE A 1 1002 ? 158.361 162.340 173.876 1.00 35.32  ? 1002 ILE A CG1   1 
ATOM   6143  C  CG2   . ILE A 1 1002 ? 157.669 163.640 175.898 1.00 31.05  ? 1002 ILE A CG2   1 
ATOM   6144  C  CD1   . ILE A 1 1002 ? 158.252 163.425 172.837 1.00 33.80  ? 1002 ILE A CD1   1 
ATOM   6145  N  N     . GLY A 1 1003 ? 155.207 161.302 177.098 1.00 34.00  ? 1003 GLY A N     1 
ATOM   6146  C  CA    . GLY A 1 1003 ? 154.452 161.481 178.326 1.00 32.44  ? 1003 GLY A CA    1 
ATOM   6147  C  C     . GLY A 1 1003 ? 154.695 160.369 179.325 1.00 38.38  ? 1003 GLY A C     1 
ATOM   6148  O  O     . GLY A 1 1003 ? 154.893 160.629 180.516 1.00 39.86  ? 1003 GLY A O     1 
ATOM   6149  N  N     . ALA A 1 1004 ? 154.711 159.117 178.857 1.00 40.76  ? 1004 ALA A N     1 
ATOM   6150  C  CA    . ALA A 1 1004 ? 154.973 158.007 179.767 1.00 38.26  ? 1004 ALA A CA    1 
ATOM   6151  C  C     . ALA A 1 1004 ? 156.354 158.132 180.394 1.00 38.66  ? 1004 ALA A C     1 
ATOM   6152  O  O     . ALA A 1 1004 ? 156.513 157.984 181.614 1.00 39.69  ? 1004 ALA A O     1 
ATOM   6153  C  CB    . ALA A 1 1004 ? 154.834 156.677 179.028 1.00 39.31  ? 1004 ALA A CB    1 
ATOM   6154  N  N     . ILE A 1 1005 ? 157.366 158.437 179.575 1.00 41.91  ? 1005 ILE A N     1 
ATOM   6155  C  CA    . ILE A 1 1005 ? 158.728 158.541 180.093 1.00 40.68  ? 1005 ILE A CA    1 
ATOM   6156  C  C     . ILE A 1 1005 ? 158.827 159.660 181.120 1.00 42.93  ? 1005 ILE A C     1 
ATOM   6157  O  O     . ILE A 1 1005 ? 159.389 159.476 182.204 1.00 47.60  ? 1005 ILE A O     1 
ATOM   6158  C  CB    . ILE A 1 1005 ? 159.732 158.741 178.945 1.00 41.45  ? 1005 ILE A CB    1 
ATOM   6159  C  CG1   . ILE A 1 1005 ? 159.799 157.484 178.075 1.00 41.42  ? 1005 ILE A CG1   1 
ATOM   6160  C  CG2   . ILE A 1 1005 ? 161.101 159.090 179.503 1.00 41.92  ? 1005 ILE A CG2   1 
ATOM   6161  C  CD1   . ILE A 1 1005 ? 161.120 157.288 177.370 1.00 41.44  ? 1005 ILE A CD1   1 
ATOM   6162  N  N     . ALA A 1 1006 ? 158.281 160.837 180.799 1.00 40.90  ? 1006 ALA A N     1 
ATOM   6163  C  CA    . ALA A 1 1006 ? 158.377 161.970 181.716 1.00 40.28  ? 1006 ALA A CA    1 
ATOM   6164  C  C     . ALA A 1 1006 ? 157.675 161.675 183.035 1.00 44.49  ? 1006 ALA A C     1 
ATOM   6165  O  O     . ALA A 1 1006 ? 158.242 161.889 184.116 1.00 46.54  ? 1006 ALA A O     1 
ATOM   6166  C  CB    . ALA A 1 1006 ? 157.796 163.225 181.066 1.00 40.19  ? 1006 ALA A CB    1 
ATOM   6167  N  N     . VAL A 1 1007 ? 156.441 161.168 182.967 1.00 44.55  ? 1007 VAL A N     1 
ATOM   6168  C  CA    . VAL A 1 1007 ? 155.676 160.943 184.189 1.00 47.31  ? 1007 VAL A CA    1 
ATOM   6169  C  C     . VAL A 1 1007 ? 156.359 159.903 185.065 1.00 50.19  ? 1007 VAL A C     1 
ATOM   6170  O  O     . VAL A 1 1007 ? 156.472 160.082 186.284 1.00 51.32  ? 1007 VAL A O     1 
ATOM   6171  C  CB    . VAL A 1 1007 ? 154.229 160.537 183.857 1.00 47.47  ? 1007 VAL A CB    1 
ATOM   6172  C  CG1   . VAL A 1 1007 ? 153.521 160.062 185.115 1.00 45.60  ? 1007 VAL A CG1   1 
ATOM   6173  C  CG2   . VAL A 1 1007 ? 153.477 161.700 183.230 1.00 46.07  ? 1007 VAL A CG2   1 
ATOM   6174  N  N     . VAL A 1 1008 ? 156.839 158.807 184.469 1.00 52.82  ? 1008 VAL A N     1 
ATOM   6175  C  CA    . VAL A 1 1008 ? 157.471 157.768 185.275 1.00 51.04  ? 1008 VAL A CA    1 
ATOM   6176  C  C     . VAL A 1 1008 ? 158.800 158.256 185.841 1.00 51.63  ? 1008 VAL A C     1 
ATOM   6177  O  O     . VAL A 1 1008 ? 159.114 158.015 187.012 1.00 55.65  ? 1008 VAL A O     1 
ATOM   6178  C  CB    . VAL A 1 1008 ? 157.637 156.477 184.454 1.00 51.27  ? 1008 VAL A CB    1 
ATOM   6179  C  CG1   . VAL A 1 1008 ? 158.579 155.521 185.153 1.00 51.28  ? 1008 VAL A CG1   1 
ATOM   6180  C  CG2   . VAL A 1 1008 ? 156.288 155.817 184.247 1.00 49.80  ? 1008 VAL A CG2   1 
ATOM   6181  N  N     . ALA A 1 1009 ? 159.593 158.967 185.035 1.00 51.01  ? 1009 ALA A N     1 
ATOM   6182  C  CA    . ALA A 1 1009 ? 160.921 159.375 185.476 1.00 51.12  ? 1009 ALA A CA    1 
ATOM   6183  C  C     . ALA A 1 1009 ? 160.868 160.472 186.529 1.00 52.41  ? 1009 ALA A C     1 
ATOM   6184  O  O     . ALA A 1 1009 ? 161.815 160.612 187.311 1.00 53.61  ? 1009 ALA A O     1 
ATOM   6185  C  CB    . ALA A 1 1009 ? 161.754 159.836 184.283 1.00 50.36  ? 1009 ALA A CB    1 
ATOM   6186  N  N     . VAL A 1 1010 ? 159.797 161.270 186.565 1.00 53.01  ? 1010 VAL A N     1 
ATOM   6187  C  CA    . VAL A 1 1010 ? 159.709 162.292 187.605 1.00 55.11  ? 1010 VAL A CA    1 
ATOM   6188  C  C     . VAL A 1 1010 ? 159.656 161.646 188.985 1.00 55.53  ? 1010 VAL A C     1 
ATOM   6189  O  O     . VAL A 1 1010 ? 160.364 162.062 189.909 1.00 55.29  ? 1010 VAL A O     1 
ATOM   6190  C  CB    . VAL A 1 1010 ? 158.499 163.212 187.363 1.00 55.87  ? 1010 VAL A CB    1 
ATOM   6191  C  CG1   . VAL A 1 1010 ? 157.989 163.776 188.679 1.00 53.88  ? 1010 VAL A CG1   1 
ATOM   6192  C  CG2   . VAL A 1 1010 ? 158.874 164.343 186.422 1.00 55.76  ? 1010 VAL A CG2   1 
ATOM   6193  N  N     . LEU A 1 1011 ? 158.837 160.608 189.142 1.00 56.19  ? 1011 LEU A N     1 
ATOM   6194  C  CA    . LEU A 1 1011 ? 158.675 159.932 190.421 1.00 54.59  ? 1011 LEU A CA    1 
ATOM   6195  C  C     . LEU A 1 1011 ? 159.725 158.857 190.675 1.00 56.67  ? 1011 LEU A C     1 
ATOM   6196  O  O     . LEU A 1 1011 ? 159.852 158.400 191.814 1.00 58.50  ? 1011 LEU A O     1 
ATOM   6197  C  CB    . LEU A 1 1011 ? 157.277 159.314 190.509 1.00 59.18  ? 1011 LEU A CB    1 
ATOM   6198  C  CG    . LEU A 1 1011 ? 156.121 160.314 190.481 1.00 59.63  ? 1011 LEU A CG    1 
ATOM   6199  C  CD1   . LEU A 1 1011 ? 154.793 159.591 190.392 1.00 55.61  ? 1011 LEU A CD1   1 
ATOM   6200  C  CD2   . LEU A 1 1011 ? 156.159 161.210 191.707 1.00 58.28  ? 1011 LEU A CD2   1 
ATOM   6201  N  N     . GLN A 1 1012 ? 160.470 158.443 189.653 1.00 59.65  ? 1012 GLN A N     1 
ATOM   6202  C  CA    . GLN A 1 1012 ? 161.564 157.492 189.818 1.00 59.67  ? 1012 GLN A CA    1 
ATOM   6203  C  C     . GLN A 1 1012 ? 162.596 157.722 188.720 1.00 57.19  ? 1012 GLN A C     1 
ATOM   6204  O  O     . GLN A 1 1012 ? 162.413 157.262 187.587 1.00 57.16  ? 1012 GLN A O     1 
ATOM   6205  C  CB    . GLN A 1 1012 ? 161.051 156.051 189.795 1.00 59.11  ? 1012 GLN A CB    1 
ATOM   6206  C  CG    . GLN A 1 1012 ? 162.131 154.954 189.760 1.00 62.70  ? 1012 GLN A CG    1 
ATOM   6207  C  CD    . GLN A 1 1012 ? 163.060 154.927 190.974 1.00 65.40  ? 1012 GLN A CD    1 
ATOM   6208  O  OE1   . GLN A 1 1012 ? 163.424 155.958 191.536 1.00 68.94  ? 1012 GLN A OE1   1 
ATOM   6209  N  NE2   . GLN A 1 1012 ? 163.449 153.725 191.378 1.00 65.59  ? 1012 GLN A NE2   1 
ATOM   6210  N  N     . PRO A 1 1013 ? 163.688 158.434 189.016 1.00 56.37  ? 1013 PRO A N     1 
ATOM   6211  C  CA    . PRO A 1 1013 ? 164.613 158.850 187.951 1.00 57.66  ? 1013 PRO A CA    1 
ATOM   6212  C  C     . PRO A 1 1013 ? 165.467 157.732 187.372 1.00 56.51  ? 1013 PRO A C     1 
ATOM   6213  O  O     . PRO A 1 1013 ? 166.160 157.976 186.377 1.00 57.09  ? 1013 PRO A O     1 
ATOM   6214  C  CB    . PRO A 1 1013 ? 165.483 159.904 188.644 1.00 55.81  ? 1013 PRO A CB    1 
ATOM   6215  C  CG    . PRO A 1 1013 ? 165.485 159.484 190.069 1.00 57.95  ? 1013 PRO A CG    1 
ATOM   6216  C  CD    . PRO A 1 1013 ? 164.101 158.949 190.331 1.00 55.61  ? 1013 PRO A CD    1 
ATOM   6217  N  N     . TYR A 1 1014 ? 165.454 156.528 187.943 1.00 55.81  ? 1014 TYR A N     1 
ATOM   6218  C  CA    . TYR A 1 1014 ? 166.285 155.454 187.412 1.00 55.21  ? 1014 TYR A CA    1 
ATOM   6219  C  C     . TYR A 1 1014 ? 165.724 154.823 186.145 1.00 55.45  ? 1014 TYR A C     1 
ATOM   6220  O  O     . TYR A 1 1014 ? 166.442 154.070 185.479 1.00 57.29  ? 1014 TYR A O     1 
ATOM   6221  C  CB    . TYR A 1 1014 ? 166.503 154.371 188.468 1.00 55.76  ? 1014 TYR A CB    1 
ATOM   6222  C  CG    . TYR A 1 1014 ? 167.632 154.677 189.423 1.00 62.25  ? 1014 TYR A CG    1 
ATOM   6223  C  CD1   . TYR A 1 1014 ? 168.914 154.914 188.951 1.00 65.73  ? 1014 TYR A CD1   1 
ATOM   6224  C  CD2   . TYR A 1 1014 ? 167.422 154.716 190.793 1.00 64.94  ? 1014 TYR A CD2   1 
ATOM   6225  C  CE1   . TYR A 1 1014 ? 169.954 155.189 189.812 1.00 71.27  ? 1014 TYR A CE1   1 
ATOM   6226  C  CE2   . TYR A 1 1014 ? 168.459 154.990 191.664 1.00 70.06  ? 1014 TYR A CE2   1 
ATOM   6227  C  CZ    . TYR A 1 1014 ? 169.723 155.225 191.167 1.00 76.54  ? 1014 TYR A CZ    1 
ATOM   6228  O  OH    . TYR A 1 1014 ? 170.761 155.499 192.028 1.00 83.16  ? 1014 TYR A OH    1 
ATOM   6229  N  N     . ILE A 1 1015 ? 164.467 155.095 185.799 1.00 55.94  ? 1015 ILE A N     1 
ATOM   6230  C  CA    . ILE A 1 1015 ? 163.914 154.544 184.566 1.00 53.21  ? 1015 ILE A CA    1 
ATOM   6231  C  C     . ILE A 1 1015 ? 164.549 155.208 183.350 1.00 53.43  ? 1015 ILE A C     1 
ATOM   6232  O  O     . ILE A 1 1015 ? 164.888 154.541 182.365 1.00 53.68  ? 1015 ILE A O     1 
ATOM   6233  C  CB    . ILE A 1 1015 ? 162.382 154.692 184.563 1.00 51.44  ? 1015 ILE A CB    1 
ATOM   6234  C  CG1   . ILE A 1 1015 ? 161.788 154.045 185.813 1.00 47.94  ? 1015 ILE A CG1   1 
ATOM   6235  C  CG2   . ILE A 1 1015 ? 161.790 154.078 183.307 1.00 47.33  ? 1015 ILE A CG2   1 
ATOM   6236  C  CD1   . ILE A 1 1015 ? 161.653 152.551 185.718 1.00 44.77  ? 1015 ILE A CD1   1 
ATOM   6237  N  N     . PHE A 1 1016 ? 164.731 156.528 183.406 1.00 50.87  ? 1016 PHE A N     1 
ATOM   6238  C  CA    . PHE A 1 1016 ? 165.304 157.256 182.278 1.00 53.75  ? 1016 PHE A CA    1 
ATOM   6239  C  C     . PHE A 1 1016 ? 166.734 156.804 181.999 1.00 55.36  ? 1016 PHE A C     1 
ATOM   6240  O  O     . PHE A 1 1016 ? 167.136 156.652 180.835 1.00 54.36  ? 1016 PHE A O     1 
ATOM   6241  C  CB    . PHE A 1 1016 ? 165.242 158.756 182.569 1.00 53.66  ? 1016 PHE A CB    1 
ATOM   6242  C  CG    . PHE A 1 1016 ? 165.807 159.618 181.482 1.00 58.34  ? 1016 PHE A CG    1 
ATOM   6243  C  CD1   . PHE A 1 1016 ? 165.160 159.733 180.265 1.00 59.10  ? 1016 PHE A CD1   1 
ATOM   6244  C  CD2   . PHE A 1 1016 ? 166.974 160.329 181.686 1.00 58.02  ? 1016 PHE A CD2   1 
ATOM   6245  C  CE1   . PHE A 1 1016 ? 165.675 160.533 179.268 1.00 59.78  ? 1016 PHE A CE1   1 
ATOM   6246  C  CE2   . PHE A 1 1016 ? 167.494 161.130 180.692 1.00 59.02  ? 1016 PHE A CE2   1 
ATOM   6247  C  CZ    . PHE A 1 1016 ? 166.844 161.232 179.482 1.00 58.06  ? 1016 PHE A CZ    1 
ATOM   6248  N  N     . VAL A 1 1017 ? 167.513 156.581 183.058 1.00 53.61  ? 1017 VAL A N     1 
ATOM   6249  C  CA    . VAL A 1 1017 ? 168.880 156.096 182.901 1.00 52.49  ? 1017 VAL A CA    1 
ATOM   6250  C  C     . VAL A 1 1017 ? 168.883 154.740 182.213 1.00 52.72  ? 1017 VAL A C     1 
ATOM   6251  O  O     . VAL A 1 1017 ? 169.753 154.446 181.384 1.00 53.10  ? 1017 VAL A O     1 
ATOM   6252  C  CB    . VAL A 1 1017 ? 169.581 156.040 184.271 1.00 54.29  ? 1017 VAL A CB    1 
ATOM   6253  C  CG1   . VAL A 1 1017 ? 170.959 155.425 184.142 1.00 55.93  ? 1017 VAL A CG1   1 
ATOM   6254  C  CG2   . VAL A 1 1017 ? 169.672 157.432 184.871 1.00 53.90  ? 1017 VAL A CG2   1 
ATOM   6255  N  N     . ALA A 1 1018 ? 167.907 153.894 182.540 1.00 52.63  ? 1018 ALA A N     1 
ATOM   6256  C  CA    . ALA A 1 1018 ? 167.813 152.589 181.900 1.00 47.39  ? 1018 ALA A CA    1 
ATOM   6257  C  C     . ALA A 1 1018 ? 167.409 152.705 180.437 1.00 49.39  ? 1018 ALA A C     1 
ATOM   6258  O  O     . ALA A 1 1018 ? 167.885 151.927 179.603 1.00 52.27  ? 1018 ALA A O     1 
ATOM   6259  C  CB    . ALA A 1 1018 ? 166.820 151.708 182.654 1.00 45.46  ? 1018 ALA A CB    1 
ATOM   6260  N  N     . THR A 1 1019 ? 166.542 153.663 180.104 1.00 49.95  ? 1019 THR A N     1 
ATOM   6261  C  CA    . THR A 1 1019 ? 166.054 153.786 178.734 1.00 46.93  ? 1019 THR A CA    1 
ATOM   6262  C  C     . THR A 1 1019 ? 167.035 154.481 177.797 1.00 47.56  ? 1019 THR A C     1 
ATOM   6263  O  O     . THR A 1 1019 ? 166.913 154.322 176.578 1.00 46.96  ? 1019 THR A O     1 
ATOM   6264  C  CB    . THR A 1 1019 ? 164.722 154.542 178.701 1.00 46.88  ? 1019 THR A CB    1 
ATOM   6265  O  OG1   . THR A 1 1019 ? 164.912 155.873 179.192 1.00 52.50  ? 1019 THR A OG1   1 
ATOM   6266  C  CG2   . THR A 1 1019 ? 163.677 153.837 179.536 1.00 43.39  ? 1019 THR A CG2   1 
ATOM   6267  N  N     . VAL A 1 1020 ? 167.986 155.253 178.330 1.00 48.26  ? 1020 VAL A N     1 
ATOM   6268  C  CA    . VAL A 1 1020 ? 168.881 156.038 177.467 1.00 46.35  ? 1020 VAL A CA    1 
ATOM   6269  C  C     . VAL A 1 1020 ? 169.611 155.197 176.415 1.00 45.00  ? 1020 VAL A C     1 
ATOM   6270  O  O     . VAL A 1 1020 ? 169.559 155.557 175.227 1.00 45.95  ? 1020 VAL A O     1 
ATOM   6271  C  CB    . VAL A 1 1020 ? 169.842 156.873 178.329 1.00 46.26  ? 1020 VAL A CB    1 
ATOM   6272  C  CG1   . VAL A 1 1020 ? 171.111 157.197 177.565 1.00 47.05  ? 1020 VAL A CG1   1 
ATOM   6273  C  CG2   . VAL A 1 1020 ? 169.162 158.151 178.785 1.00 47.80  ? 1020 VAL A CG2   1 
ATOM   6274  N  N     . PRO A 1 1021 ? 170.296 154.096 176.758 1.00 44.10  ? 1021 PRO A N     1 
ATOM   6275  C  CA    . PRO A 1 1021 ? 171.096 153.393 175.735 1.00 42.24  ? 1021 PRO A CA    1 
ATOM   6276  C  C     . PRO A 1 1021 ? 170.281 152.818 174.586 1.00 40.79  ? 1021 PRO A C     1 
ATOM   6277  O  O     . PRO A 1 1021 ? 170.765 152.808 173.447 1.00 40.79  ? 1021 PRO A O     1 
ATOM   6278  C  CB    . PRO A 1 1021 ? 171.799 152.286 176.536 1.00 40.64  ? 1021 PRO A CB    1 
ATOM   6279  C  CG    . PRO A 1 1021 ? 170.957 152.090 177.729 1.00 43.11  ? 1021 PRO A CG    1 
ATOM   6280  C  CD    . PRO A 1 1021 ? 170.445 153.454 178.075 1.00 41.98  ? 1021 PRO A CD    1 
ATOM   6281  N  N     . VAL A 1 1022 ? 169.057 152.353 174.840 1.00 40.07  ? 1022 VAL A N     1 
ATOM   6282  C  CA    . VAL A 1 1022 ? 168.246 151.791 173.763 1.00 39.22  ? 1022 VAL A CA    1 
ATOM   6283  C  C     . VAL A 1 1022 ? 167.800 152.890 172.807 1.00 40.05  ? 1022 VAL A C     1 
ATOM   6284  O  O     . VAL A 1 1022 ? 167.755 152.694 171.584 1.00 41.45  ? 1022 VAL A O     1 
ATOM   6285  C  CB    . VAL A 1 1022 ? 167.048 151.027 174.350 1.00 38.03  ? 1022 VAL A CB    1 
ATOM   6286  C  CG1   . VAL A 1 1022 ? 166.279 150.330 173.248 1.00 38.85  ? 1022 VAL A CG1   1 
ATOM   6287  C  CG2   . VAL A 1 1022 ? 167.521 150.035 175.391 1.00 42.62  ? 1022 VAL A CG2   1 
ATOM   6288  N  N     . ILE A 1 1023 ? 167.465 154.061 173.353 1.00 37.65  ? 1023 ILE A N     1 
ATOM   6289  C  CA    . ILE A 1 1023 ? 167.143 155.219 172.525 1.00 36.41  ? 1023 ILE A CA    1 
ATOM   6290  C  C     . ILE A 1 1023 ? 168.331 155.574 171.644 1.00 37.38  ? 1023 ILE A C     1 
ATOM   6291  O  O     . ILE A 1 1023 ? 168.184 155.839 170.442 1.00 39.96  ? 1023 ILE A O     1 
ATOM   6292  C  CB    . ILE A 1 1023 ? 166.729 156.407 173.413 1.00 37.50  ? 1023 ILE A CB    1 
ATOM   6293  C  CG1   . ILE A 1 1023 ? 165.399 156.126 174.108 1.00 42.38  ? 1023 ILE A CG1   1 
ATOM   6294  C  CG2   . ILE A 1 1023 ? 166.648 157.691 172.604 1.00 37.59  ? 1023 ILE A CG2   1 
ATOM   6295  C  CD1   . ILE A 1 1023 ? 165.164 156.978 175.333 1.00 41.88  ? 1023 ILE A CD1   1 
ATOM   6296  N  N     . VAL A 1 1024 ? 169.529 155.582 172.233 1.00 35.76  ? 1024 VAL A N     1 
ATOM   6297  C  CA    . VAL A 1 1024 ? 170.727 155.911 171.465 1.00 34.80  ? 1024 VAL A CA    1 
ATOM   6298  C  C     . VAL A 1 1024 ? 170.934 154.910 170.333 1.00 36.77  ? 1024 VAL A C     1 
ATOM   6299  O  O     . VAL A 1 1024 ? 171.245 155.292 169.198 1.00 38.29  ? 1024 VAL A O     1 
ATOM   6300  C  CB    . VAL A 1 1024 ? 171.952 155.982 172.394 1.00 35.18  ? 1024 VAL A CB    1 
ATOM   6301  C  CG1   . VAL A 1 1024 ? 173.235 155.980 171.586 1.00 35.44  ? 1024 VAL A CG1   1 
ATOM   6302  C  CG2   . VAL A 1 1024 ? 171.874 157.218 173.266 1.00 34.70  ? 1024 VAL A CG2   1 
ATOM   6303  N  N     . ALA A 1 1025 ? 170.771 153.617 170.625 1.00 35.52  ? 1025 ALA A N     1 
ATOM   6304  C  CA    . ALA A 1 1025 ? 170.961 152.595 169.599 1.00 30.58  ? 1025 ALA A CA    1 
ATOM   6305  C  C     . ALA A 1 1025 ? 169.972 152.762 168.451 1.00 34.57  ? 1025 ALA A C     1 
ATOM   6306  O  O     . ALA A 1 1025 ? 170.356 152.693 167.273 1.00 36.44  ? 1025 ALA A O     1 
ATOM   6307  C  CB    . ALA A 1 1025 ? 170.835 151.204 170.214 1.00 28.14  ? 1025 ALA A CB    1 
ATOM   6308  N  N     . PHE A 1 1026 ? 168.693 152.989 168.770 1.00 35.10  ? 1026 PHE A N     1 
ATOM   6309  C  CA    . PHE A 1 1026 ? 167.708 153.188 167.708 1.00 35.09  ? 1026 PHE A CA    1 
ATOM   6310  C  C     . PHE A 1 1026 ? 168.034 154.416 166.868 1.00 34.96  ? 1026 PHE A C     1 
ATOM   6311  O  O     . PHE A 1 1026 ? 167.936 154.373 165.634 1.00 34.59  ? 1026 PHE A O     1 
ATOM   6312  C  CB    . PHE A 1 1026 ? 166.294 153.304 168.281 1.00 34.68  ? 1026 PHE A CB    1 
ATOM   6313  C  CG    . PHE A 1 1026 ? 165.752 152.028 168.861 1.00 35.86  ? 1026 PHE A CG    1 
ATOM   6314  C  CD1   . PHE A 1 1026 ? 166.250 150.800 168.468 1.00 36.55  ? 1026 PHE A CD1   1 
ATOM   6315  C  CD2   . PHE A 1 1026 ? 164.704 152.061 169.765 1.00 34.11  ? 1026 PHE A CD2   1 
ATOM   6316  C  CE1   . PHE A 1 1026 ? 165.735 149.630 168.989 1.00 37.29  ? 1026 PHE A CE1   1 
ATOM   6317  C  CE2   . PHE A 1 1026 ? 164.184 150.894 170.288 1.00 35.79  ? 1026 PHE A CE2   1 
ATOM   6318  C  CZ    . PHE A 1 1026 ? 164.698 149.678 169.899 1.00 36.55  ? 1026 PHE A CZ    1 
ATOM   6319  N  N     . ILE A 1 1027 ? 168.429 155.518 167.512 1.00 37.18  ? 1027 ILE A N     1 
ATOM   6320  C  CA    . ILE A 1 1027 ? 168.714 156.737 166.761 1.00 35.15  ? 1027 ILE A CA    1 
ATOM   6321  C  C     . ILE A 1 1027 ? 169.909 156.530 165.839 1.00 35.07  ? 1027 ILE A C     1 
ATOM   6322  O  O     . ILE A 1 1027 ? 169.894 156.954 164.674 1.00 34.21  ? 1027 ILE A O     1 
ATOM   6323  C  CB    . ILE A 1 1027 ? 168.926 157.917 167.726 1.00 37.64  ? 1027 ILE A CB    1 
ATOM   6324  C  CG1   . ILE A 1 1027 ? 167.590 158.590 168.043 1.00 35.61  ? 1027 ILE A CG1   1 
ATOM   6325  C  CG2   . ILE A 1 1027 ? 169.898 158.927 167.146 1.00 36.71  ? 1027 ILE A CG2   1 
ATOM   6326  C  CD1   . ILE A 1 1027 ? 167.606 159.407 169.314 1.00 33.38  ? 1027 ILE A CD1   1 
ATOM   6327  N  N     . MET A 1 1028 ? 170.953 155.859 166.333 1.00 35.16  ? 1028 MET A N     1 
ATOM   6328  C  CA    . MET A 1 1028 ? 172.128 155.607 165.505 1.00 34.82  ? 1028 MET A CA    1 
ATOM   6329  C  C     . MET A 1 1028 ? 171.790 154.733 164.304 1.00 34.54  ? 1028 MET A C     1 
ATOM   6330  O  O     . MET A 1 1028 ? 172.208 155.030 163.175 1.00 38.57  ? 1028 MET A O     1 
ATOM   6331  C  CB    . MET A 1 1028 ? 173.226 154.957 166.343 1.00 35.30  ? 1028 MET A CB    1 
ATOM   6332  C  CG    . MET A 1 1028 ? 173.803 155.855 167.415 1.00 35.63  ? 1028 MET A CG    1 
ATOM   6333  S  SD    . MET A 1 1028 ? 174.903 157.117 166.756 1.00 73.98  ? 1028 MET A SD    1 
ATOM   6334  C  CE    . MET A 1 1028 ? 176.484 156.496 167.324 1.00 57.41  ? 1028 MET A CE    1 
ATOM   6335  N  N     . LEU A 1 1029 ? 171.023 153.661 164.517 1.00 30.97  ? 1029 LEU A N     1 
ATOM   6336  C  CA    . LEU A 1 1029 ? 170.677 152.796 163.393 1.00 29.00  ? 1029 LEU A CA    1 
ATOM   6337  C  C     . LEU A 1 1029 ? 169.821 153.533 162.369 1.00 29.09  ? 1029 LEU A C     1 
ATOM   6338  O  O     . LEU A 1 1029 ? 170.017 153.374 161.157 1.00 32.37  ? 1029 LEU A O     1 
ATOM   6339  C  CB    . LEU A 1 1029 ? 169.963 151.542 163.892 1.00 27.94  ? 1029 LEU A CB    1 
ATOM   6340  C  CG    . LEU A 1 1029 ? 169.755 150.467 162.829 1.00 24.40  ? 1029 LEU A CG    1 
ATOM   6341  C  CD1   . LEU A 1 1029 ? 171.091 149.994 162.314 1.00 25.25  ? 1029 LEU A CD1   1 
ATOM   6342  C  CD2   . LEU A 1 1029 ? 168.968 149.302 163.385 1.00 28.27  ? 1029 LEU A CD2   1 
ATOM   6343  N  N     . ARG A 1 1030 ? 168.873 154.350 162.834 1.00 30.51  ? 1030 ARG A N     1 
ATOM   6344  C  CA    . ARG A 1 1030 ? 168.031 155.114 161.919 1.00 30.46  ? 1030 ARG A CA    1 
ATOM   6345  C  C     . ARG A 1 1030 ? 168.860 156.084 161.085 1.00 32.52  ? 1030 ARG A C     1 
ATOM   6346  O  O     . ARG A 1 1030 ? 168.649 156.225 159.870 1.00 33.47  ? 1030 ARG A O     1 
ATOM   6347  C  CB    . ARG A 1 1030 ? 166.966 155.863 162.718 1.00 29.92  ? 1030 ARG A CB    1 
ATOM   6348  C  CG    . ARG A 1 1030 ? 165.977 156.637 161.888 1.00 33.97  ? 1030 ARG A CG    1 
ATOM   6349  C  CD    . ARG A 1 1030 ? 165.081 157.475 162.772 1.00 33.42  ? 1030 ARG A CD    1 
ATOM   6350  N  NE    . ARG A 1 1030 ? 164.225 158.354 161.986 1.00 39.01  ? 1030 ARG A NE    1 
ATOM   6351  C  CZ    . ARG A 1 1030 ? 164.600 159.533 161.511 1.00 37.82  ? 1030 ARG A CZ    1 
ATOM   6352  N  NH1   . ARG A 1 1030 ? 165.816 160.007 161.725 1.00 35.97  ? 1030 ARG A NH1   1 
ATOM   6353  N  NH2   . ARG A 1 1030 ? 163.737 160.250 160.800 1.00 37.50  ? 1030 ARG A NH2   1 
ATOM   6354  N  N     . ALA A 1 1031 ? 169.803 156.778 161.731 1.00 33.10  ? 1031 ALA A N     1 
ATOM   6355  C  CA    . ALA A 1 1031 ? 170.660 157.712 161.012 1.00 29.70  ? 1031 ALA A CA    1 
ATOM   6356  C  C     . ALA A 1 1031 ? 171.498 156.993 159.968 1.00 31.76  ? 1031 ALA A C     1 
ATOM   6357  O  O     . ALA A 1 1031 ? 171.698 157.504 158.860 1.00 33.19  ? 1031 ALA A O     1 
ATOM   6358  C  CB    . ALA A 1 1031 ? 171.557 158.465 161.993 1.00 33.16  ? 1031 ALA A CB    1 
ATOM   6359  N  N     . TYR A 1 1032 ? 172.003 155.804 160.304 1.00 34.04  ? 1032 TYR A N     1 
ATOM   6360  C  CA    . TYR A 1 1032 ? 172.770 155.031 159.333 1.00 31.06  ? 1032 TYR A CA    1 
ATOM   6361  C  C     . TYR A 1 1032 ? 171.905 154.627 158.142 1.00 31.32  ? 1032 TYR A C     1 
ATOM   6362  O  O     . TYR A 1 1032 ? 172.342 154.703 156.989 1.00 35.03  ? 1032 TYR A O     1 
ATOM   6363  C  CB    . TYR A 1 1032 ? 173.376 153.802 160.013 1.00 32.79  ? 1032 TYR A CB    1 
ATOM   6364  C  CG    . TYR A 1 1032 ? 174.192 152.913 159.103 1.00 34.86  ? 1032 TYR A CG    1 
ATOM   6365  C  CD1   . TYR A 1 1032 ? 175.521 153.200 158.837 1.00 37.63  ? 1032 TYR A CD1   1 
ATOM   6366  C  CD2   . TYR A 1 1032 ? 173.640 151.777 158.530 1.00 32.77  ? 1032 TYR A CD2   1 
ATOM   6367  C  CE1   . TYR A 1 1032 ? 176.270 152.392 158.016 1.00 38.49  ? 1032 TYR A CE1   1 
ATOM   6368  C  CE2   . TYR A 1 1032 ? 174.384 150.963 157.707 1.00 34.17  ? 1032 TYR A CE2   1 
ATOM   6369  C  CZ    . TYR A 1 1032 ? 175.698 151.277 157.453 1.00 37.90  ? 1032 TYR A CZ    1 
ATOM   6370  O  OH    . TYR A 1 1032 ? 176.448 150.468 156.638 1.00 44.79  ? 1032 TYR A OH    1 
ATOM   6371  N  N     . PHE A 1 1033 ? 170.669 154.198 158.403 1.00 27.74  ? 1033 PHE A N     1 
ATOM   6372  C  CA    . PHE A 1 1033 ? 169.822 153.655 157.341 1.00 26.16  ? 1033 PHE A CA    1 
ATOM   6373  C  C     . PHE A 1 1033 ? 169.336 154.734 156.373 1.00 31.39  ? 1033 PHE A C     1 
ATOM   6374  O  O     . PHE A 1 1033 ? 169.282 154.507 155.153 1.00 35.89  ? 1033 PHE A O     1 
ATOM   6375  C  CB    . PHE A 1 1033 ? 168.638 152.924 157.963 1.00 28.64  ? 1033 PHE A CB    1 
ATOM   6376  C  CG    . PHE A 1 1033 ? 167.621 152.445 156.970 1.00 31.21  ? 1033 PHE A CG    1 
ATOM   6377  C  CD1   . PHE A 1 1033 ? 167.945 151.481 156.035 1.00 29.28  ? 1033 PHE A CD1   1 
ATOM   6378  C  CD2   . PHE A 1 1033 ? 166.333 152.947 156.985 1.00 27.82  ? 1033 PHE A CD2   1 
ATOM   6379  C  CE1   . PHE A 1 1033 ? 167.008 151.034 155.134 1.00 26.31  ? 1033 PHE A CE1   1 
ATOM   6380  C  CE2   . PHE A 1 1033 ? 165.395 152.503 156.087 1.00 24.06  ? 1033 PHE A CE2   1 
ATOM   6381  C  CZ    . PHE A 1 1033 ? 165.731 151.546 155.161 1.00 24.22  ? 1033 PHE A CZ    1 
ATOM   6382  N  N     . LEU A 1 1034 ? 168.954 155.904 156.895 1.00 33.66  ? 1034 LEU A N     1 
ATOM   6383  C  CA    . LEU A 1 1034 ? 168.304 156.895 156.039 1.00 31.54  ? 1034 LEU A CA    1 
ATOM   6384  C  C     . LEU A 1 1034 ? 169.213 157.383 154.917 1.00 36.91  ? 1034 LEU A C     1 
ATOM   6385  O  O     . LEU A 1 1034 ? 168.719 157.752 153.844 1.00 41.25  ? 1034 LEU A O     1 
ATOM   6386  C  CB    . LEU A 1 1034 ? 167.816 158.077 156.872 1.00 30.95  ? 1034 LEU A CB    1 
ATOM   6387  C  CG    . LEU A 1 1034 ? 166.542 157.838 157.676 1.00 36.47  ? 1034 LEU A CG    1 
ATOM   6388  C  CD1   . LEU A 1 1034 ? 166.182 159.080 158.464 1.00 40.22  ? 1034 LEU A CD1   1 
ATOM   6389  C  CD2   . LEU A 1 1034 ? 165.409 157.434 156.757 1.00 36.18  ? 1034 LEU A CD2   1 
ATOM   6390  N  N     . GLN A 1 1035 ? 170.534 157.360 155.132 1.00 39.53  ? 1035 GLN A N     1 
ATOM   6391  C  CA    . GLN A 1 1035 ? 171.477 157.849 154.126 1.00 38.43  ? 1035 GLN A CA    1 
ATOM   6392  C  C     . GLN A 1 1035 ? 171.275 157.161 152.784 1.00 37.06  ? 1035 GLN A C     1 
ATOM   6393  O  O     . GLN A 1 1035 ? 171.279 157.815 151.735 1.00 39.35  ? 1035 GLN A O     1 
ATOM   6394  C  CB    . GLN A 1 1035 ? 172.913 157.642 154.609 1.00 41.53  ? 1035 GLN A CB    1 
ATOM   6395  C  CG    . GLN A 1 1035 ? 173.345 158.543 155.744 1.00 42.20  ? 1035 GLN A CG    1 
ATOM   6396  C  CD    . GLN A 1 1035 ? 173.527 159.979 155.307 1.00 52.47  ? 1035 GLN A CD    1 
ATOM   6397  O  OE1   . GLN A 1 1035 ? 173.613 160.271 154.115 1.00 53.42  ? 1035 GLN A OE1   1 
ATOM   6398  N  NE2   . GLN A 1 1035 ? 173.595 160.886 156.271 1.00 59.50  ? 1035 GLN A NE2   1 
ATOM   6399  N  N     . THR A 1 1036 ? 171.102 155.843 152.795 1.00 35.78  ? 1036 THR A N     1 
ATOM   6400  C  CA    . THR A 1 1036 ? 170.870 155.092 151.570 1.00 34.41  ? 1036 THR A CA    1 
ATOM   6401  C  C     . THR A 1 1036 ? 169.391 154.981 151.232 1.00 35.65  ? 1036 THR A C     1 
ATOM   6402  O  O     . THR A 1 1036 ? 169.034 154.926 150.044 1.00 40.15  ? 1036 THR A O     1 
ATOM   6403  C  CB    . THR A 1 1036 ? 171.480 153.692 151.694 1.00 35.49  ? 1036 THR A CB    1 
ATOM   6404  O  OG1   . THR A 1 1036 ? 172.845 153.804 152.109 1.00 44.07  ? 1036 THR A OG1   1 
ATOM   6405  C  CG2   . THR A 1 1036 ? 171.436 152.961 150.366 1.00 33.68  ? 1036 THR A CG2   1 
ATOM   6406  N  N     . SER A 1 1037 ? 168.521 154.957 152.248 1.00 32.72  ? 1037 SER A N     1 
ATOM   6407  C  CA    . SER A 1 1037 ? 167.093 154.846 151.976 1.00 30.38  ? 1037 SER A CA    1 
ATOM   6408  C  C     . SER A 1 1037 ? 166.590 156.026 151.151 1.00 36.23  ? 1037 SER A C     1 
ATOM   6409  O  O     . SER A 1 1037 ? 165.799 155.845 150.217 1.00 38.59  ? 1037 SER A O     1 
ATOM   6410  C  CB    . SER A 1 1037 ? 166.317 154.737 153.287 1.00 35.62  ? 1037 SER A CB    1 
ATOM   6411  O  OG    . SER A 1 1037 ? 164.941 154.511 153.047 1.00 40.99  ? 1037 SER A OG    1 
ATOM   6412  N  N     . GLN A 1 1038 ? 167.038 157.242 151.476 1.00 36.62  ? 1038 GLN A N     1 
ATOM   6413  C  CA    . GLN A 1 1038 ? 166.556 158.420 150.759 1.00 35.16  ? 1038 GLN A CA    1 
ATOM   6414  C  C     . GLN A 1 1038 ? 166.990 158.402 149.298 1.00 37.20  ? 1038 GLN A C     1 
ATOM   6415  O  O     . GLN A 1 1038 ? 166.206 158.743 148.402 1.00 42.25  ? 1038 GLN A O     1 
ATOM   6416  C  CB    . GLN A 1 1038 ? 167.048 159.687 151.452 1.00 36.89  ? 1038 GLN A CB    1 
ATOM   6417  C  CG    . GLN A 1 1038 ? 166.353 159.959 152.773 1.00 41.77  ? 1038 GLN A CG    1 
ATOM   6418  C  CD    . GLN A 1 1038 ? 166.938 161.139 153.516 1.00 45.52  ? 1038 GLN A CD    1 
ATOM   6419  O  OE1   . GLN A 1 1038 ? 167.984 161.667 153.143 1.00 50.46  ? 1038 GLN A OE1   1 
ATOM   6420  N  NE2   . GLN A 1 1038 ? 166.262 161.562 154.576 1.00 43.12  ? 1038 GLN A NE2   1 
ATOM   6421  N  N     . GLN A 1 1039 ? 168.234 157.995 149.037 1.00 35.72  ? 1039 GLN A N     1 
ATOM   6422  C  CA    . GLN A 1 1039 ? 168.721 157.919 147.665 1.00 35.13  ? 1039 GLN A CA    1 
ATOM   6423  C  C     . GLN A 1 1039 ? 167.953 156.877 146.862 1.00 32.68  ? 1039 GLN A C     1 
ATOM   6424  O  O     . GLN A 1 1039 ? 167.559 157.131 145.714 1.00 33.40  ? 1039 GLN A O     1 
ATOM   6425  C  CB    . GLN A 1 1039 ? 170.214 157.602 147.664 1.00 37.01  ? 1039 GLN A CB    1 
ATOM   6426  C  CG    . GLN A 1 1039 ? 171.075 158.695 148.259 1.00 40.97  ? 1039 GLN A CG    1 
ATOM   6427  C  CD    . GLN A 1 1039 ? 172.550 158.462 148.026 1.00 43.76  ? 1039 GLN A CD    1 
ATOM   6428  O  OE1   . GLN A 1 1039 ? 173.043 158.624 146.914 1.00 52.33  ? 1039 GLN A OE1   1 
ATOM   6429  N  NE2   . GLN A 1 1039 ? 173.266 158.089 149.077 1.00 38.92  ? 1039 GLN A NE2   1 
ATOM   6430  N  N     . LEU A 1 1040 ? 167.722 155.700 147.450 1.00 33.31  ? 1040 LEU A N     1 
ATOM   6431  C  CA    . LEU A 1 1040 ? 166.968 154.671 146.740 1.00 31.70  ? 1040 LEU A CA    1 
ATOM   6432  C  C     . LEU A 1 1040 ? 165.534 155.116 146.478 1.00 34.64  ? 1040 LEU A C     1 
ATOM   6433  O  O     . LEU A 1 1040 ? 164.970 154.819 145.417 1.00 35.82  ? 1040 LEU A O     1 
ATOM   6434  C  CB    . LEU A 1 1040 ? 166.993 153.363 147.525 1.00 31.95  ? 1040 LEU A CB    1 
ATOM   6435  C  CG    . LEU A 1 1040 ? 168.299 152.576 147.449 1.00 28.10  ? 1040 LEU A CG    1 
ATOM   6436  C  CD1   . LEU A 1 1040 ? 168.237 151.357 148.341 1.00 28.68  ? 1040 LEU A CD1   1 
ATOM   6437  C  CD2   . LEU A 1 1040 ? 168.588 152.173 146.019 1.00 28.65  ? 1040 LEU A CD2   1 
ATOM   6438  N  N     . LYS A 1 1041 ? 164.930 155.835 147.428 1.00 38.81  ? 1041 LYS A N     1 
ATOM   6439  C  CA    . LYS A 1 1041 ? 163.573 156.332 147.228 1.00 36.30  ? 1041 LYS A CA    1 
ATOM   6440  C  C     . LYS A 1 1041 ? 163.519 157.361 146.109 1.00 36.54  ? 1041 LYS A C     1 
ATOM   6441  O  O     . LYS A 1 1041 ? 162.580 157.363 145.304 1.00 39.62  ? 1041 LYS A O     1 
ATOM   6442  C  CB    . LYS A 1 1041 ? 163.037 156.934 148.525 1.00 31.99  ? 1041 LYS A CB    1 
ATOM   6443  C  CG    . LYS A 1 1041 ? 161.562 157.266 148.473 1.00 34.64  ? 1041 LYS A CG    1 
ATOM   6444  C  CD    . LYS A 1 1041 ? 160.744 156.006 148.285 1.00 33.52  ? 1041 LYS A CD    1 
ATOM   6445  C  CE    . LYS A 1 1041 ? 159.273 156.307 148.118 1.00 32.26  ? 1041 LYS A CE    1 
ATOM   6446  N  NZ    . LYS A 1 1041 ? 158.501 155.058 147.905 1.00 34.77  ? 1041 LYS A NZ    1 
ATOM   6447  N  N     . GLN A 1 1042 ? 164.518 158.240 146.039 1.00 36.12  ? 1042 GLN A N     1 
ATOM   6448  C  CA    . GLN A 1 1042 ? 164.562 159.212 144.953 1.00 37.98  ? 1042 GLN A CA    1 
ATOM   6449  C  C     . GLN A 1 1042 ? 164.704 158.522 143.601 1.00 39.74  ? 1042 GLN A C     1 
ATOM   6450  O  O     . GLN A 1 1042 ? 164.027 158.891 142.631 1.00 39.51  ? 1042 GLN A O     1 
ATOM   6451  C  CB    . GLN A 1 1042 ? 165.711 160.187 145.187 1.00 38.84  ? 1042 GLN A CB    1 
ATOM   6452  C  CG    . GLN A 1 1042 ? 165.817 161.289 144.164 1.00 43.95  ? 1042 GLN A CG    1 
ATOM   6453  C  CD    . GLN A 1 1042 ? 166.856 162.319 144.545 1.00 55.47  ? 1042 GLN A CD    1 
ATOM   6454  O  OE1   . GLN A 1 1042 ? 167.646 162.110 145.466 1.00 53.30  ? 1042 GLN A OE1   1 
ATOM   6455  N  NE2   . GLN A 1 1042 ? 166.860 163.444 143.838 1.00 57.56  ? 1042 GLN A NE2   1 
ATOM   6456  N  N     . LEU A 1 1043 ? 165.562 157.501 143.526 1.00 42.85  ? 1043 LEU A N     1 
ATOM   6457  C  CA    . LEU A 1 1043 ? 165.715 156.761 142.277 1.00 38.88  ? 1043 LEU A CA    1 
ATOM   6458  C  C     . LEU A 1 1043 ? 164.415 156.080 141.872 1.00 37.67  ? 1043 LEU A C     1 
ATOM   6459  O  O     . LEU A 1 1043 ? 164.038 156.105 140.695 1.00 39.38  ? 1043 LEU A O     1 
ATOM   6460  C  CB    . LEU A 1 1043 ? 166.827 155.722 142.405 1.00 35.44  ? 1043 LEU A CB    1 
ATOM   6461  C  CG    . LEU A 1 1043 ? 168.273 156.202 142.346 1.00 39.01  ? 1043 LEU A CG    1 
ATOM   6462  C  CD1   . LEU A 1 1043 ? 169.214 155.062 142.692 1.00 42.84  ? 1043 LEU A CD1   1 
ATOM   6463  C  CD2   . LEU A 1 1043 ? 168.585 156.763 140.976 1.00 46.22  ? 1043 LEU A CD2   1 
ATOM   6464  N  N     . GLU A 1 1044 ? 163.722 155.459 142.828 1.00 38.51  ? 1044 GLU A N     1 
ATOM   6465  C  CA    . GLU A 1 1044 ? 162.469 154.781 142.506 1.00 38.72  ? 1044 GLU A CA    1 
ATOM   6466  C  C     . GLU A 1 1044 ? 161.406 155.775 142.056 1.00 40.64  ? 1044 GLU A C     1 
ATOM   6467  O  O     . GLU A 1 1044 ? 160.626 155.485 141.142 1.00 40.39  ? 1044 GLU A O     1 
ATOM   6468  C  CB    . GLU A 1 1044 ? 161.983 153.975 143.711 1.00 40.22  ? 1044 GLU A CB    1 
ATOM   6469  C  CG    . GLU A 1 1044 ? 160.664 153.245 143.497 1.00 43.46  ? 1044 GLU A CG    1 
ATOM   6470  C  CD    . GLU A 1 1044 ? 159.456 154.046 143.946 1.00 46.55  ? 1044 GLU A CD    1 
ATOM   6471  O  OE1   . GLU A 1 1044 ? 159.615 154.941 144.800 1.00 47.37  ? 1044 GLU A OE1   1 
ATOM   6472  O  OE2   . GLU A 1 1044 ? 158.344 153.778 143.446 1.00 44.61  ? 1044 GLU A OE2   1 
ATOM   6473  N  N     . SER A 1 1045 ? 161.351 156.949 142.693 1.00 37.95  ? 1045 SER A N     1 
ATOM   6474  C  CA    . SER A 1 1045 ? 160.390 157.966 142.280 1.00 35.97  ? 1045 SER A CA    1 
ATOM   6475  C  C     . SER A 1 1045 ? 160.677 158.458 140.869 1.00 39.16  ? 1045 SER A C     1 
ATOM   6476  O  O     . SER A 1 1045 ? 159.749 158.696 140.088 1.00 36.72  ? 1045 SER A O     1 
ATOM   6477  C  CB    . SER A 1 1045 ? 160.401 159.131 143.265 1.00 39.66  ? 1045 SER A CB    1 
ATOM   6478  O  OG    . SER A 1 1045 ? 159.789 158.765 144.487 1.00 40.22  ? 1045 SER A OG    1 
ATOM   6479  N  N     . GLU A 1 1046 ? 161.954 158.614 140.520 1.00 44.59  ? 1046 GLU A N     1 
ATOM   6480  C  CA    . GLU A 1 1046 ? 162.281 159.072 139.175 1.00 41.41  ? 1046 GLU A CA    1 
ATOM   6481  C  C     . GLU A 1 1046 ? 162.041 157.995 138.122 1.00 41.57  ? 1046 GLU A C     1 
ATOM   6482  O  O     . GLU A 1 1046 ? 161.891 158.315 136.939 1.00 43.67  ? 1046 GLU A O     1 
ATOM   6483  C  CB    . GLU A 1 1046 ? 163.731 159.551 139.119 1.00 45.96  ? 1046 GLU A CB    1 
ATOM   6484  C  CG    . GLU A 1 1046 ? 164.063 160.343 137.870 1.00 53.61  ? 1046 GLU A CG    1 
ATOM   6485  C  CD    . GLU A 1 1046 ? 163.251 161.618 137.753 1.00 59.37  ? 1046 GLU A CD    1 
ATOM   6486  O  OE1   . GLU A 1 1046 ? 163.077 162.312 138.777 1.00 57.24  ? 1046 GLU A OE1   1 
ATOM   6487  O  OE2   . GLU A 1 1046 ? 162.773 161.917 136.639 1.00 59.19  ? 1046 GLU A OE2   1 
ATOM   6488  N  N     . GLY A 1 1047 ? 161.987 156.726 138.524 1.00 42.50  ? 1047 GLY A N     1 
ATOM   6489  C  CA    . GLY A 1 1047 ? 161.841 155.640 137.571 1.00 35.06  ? 1047 GLY A CA    1 
ATOM   6490  C  C     . GLY A 1 1047 ? 160.442 155.452 137.020 1.00 33.31  ? 1047 GLY A C     1 
ATOM   6491  O  O     . GLY A 1 1047 ? 160.261 154.623 136.123 1.00 31.84  ? 1047 GLY A O     1 
ATOM   6492  N  N     . ARG A 1 1048 ? 159.454 156.188 137.532 1.00 36.20  ? 1048 ARG A N     1 
ATOM   6493  C  CA    . ARG A 1 1048 ? 158.081 156.037 137.064 1.00 33.62  ? 1048 ARG A CA    1 
ATOM   6494  C  C     . ARG A 1 1048 ? 157.799 156.806 135.779 1.00 37.07  ? 1048 ARG A C     1 
ATOM   6495  O  O     . ARG A 1 1048 ? 156.803 156.518 135.109 1.00 39.29  ? 1048 ARG A O     1 
ATOM   6496  C  CB    . ARG A 1 1048 ? 157.100 156.493 138.146 1.00 34.70  ? 1048 ARG A CB    1 
ATOM   6497  C  CG    . ARG A 1 1048 ? 157.288 155.826 139.498 1.00 37.50  ? 1048 ARG A CG    1 
ATOM   6498  C  CD    . ARG A 1 1048 ? 156.139 156.164 140.435 1.00 34.41  ? 1048 ARG A CD    1 
ATOM   6499  N  NE    . ARG A 1 1048 ? 156.136 157.559 140.854 1.00 37.59  ? 1048 ARG A NE    1 
ATOM   6500  C  CZ    . ARG A 1 1048 ? 156.360 157.972 142.093 1.00 40.18  ? 1048 ARG A CZ    1 
ATOM   6501  N  NH1   . ARG A 1 1048 ? 156.600 157.118 143.073 1.00 43.65  ? 1048 ARG A NH1   1 
ATOM   6502  N  NH2   . ARG A 1 1048 ? 156.336 159.275 142.357 1.00 32.99  ? 1048 ARG A NH2   1 
ATOM   6503  N  N     . SER A 1 1049 ? 158.644 157.776 135.430 1.00 36.45  ? 1049 SER A N     1 
ATOM   6504  C  CA    . SER A 1 1049 ? 158.378 158.625 134.270 1.00 36.36  ? 1049 SER A CA    1 
ATOM   6505  C  C     . SER A 1 1049 ? 158.365 157.895 132.929 1.00 35.58  ? 1049 SER A C     1 
ATOM   6506  O  O     . SER A 1 1049 ? 157.445 158.156 132.131 1.00 36.73  ? 1049 SER A O     1 
ATOM   6507  C  CB    . SER A 1 1049 ? 159.399 159.768 134.238 1.00 39.51  ? 1049 SER A CB    1 
ATOM   6508  O  OG    . SER A 1 1049 ? 159.267 160.598 135.375 1.00 47.80  ? 1049 SER A OG    1 
ATOM   6509  N  N     . PRO A 1 1050 ? 159.326 157.017 132.600 1.00 34.79  ? 1050 PRO A N     1 
ATOM   6510  C  CA    . PRO A 1 1050 ? 159.328 156.421 131.254 1.00 35.17  ? 1050 PRO A CA    1 
ATOM   6511  C  C     . PRO A 1 1050 ? 158.085 155.614 130.939 1.00 34.79  ? 1050 PRO A C     1 
ATOM   6512  O  O     . PRO A 1 1050 ? 157.687 155.551 129.771 1.00 36.65  ? 1050 PRO A O     1 
ATOM   6513  C  CB    . PRO A 1 1050 ? 160.588 155.542 131.262 1.00 29.90  ? 1050 PRO A CB    1 
ATOM   6514  C  CG    . PRO A 1 1050 ? 161.441 156.128 132.320 1.00 28.35  ? 1050 PRO A CG    1 
ATOM   6515  C  CD    . PRO A 1 1050 ? 160.476 156.533 133.379 1.00 34.40  ? 1050 PRO A CD    1 
ATOM   6516  N  N     . ILE A 1 1051 ? 157.445 155.017 131.945 1.00 31.02  ? 1051 ILE A N     1 
ATOM   6517  C  CA    . ILE A 1 1051 ? 156.219 154.260 131.704 1.00 30.00  ? 1051 ILE A CA    1 
ATOM   6518  C  C     . ILE A 1 1051 ? 155.125 155.181 131.177 1.00 32.55  ? 1051 ILE A C     1 
ATOM   6519  O  O     . ILE A 1 1051 ? 154.465 154.884 130.172 1.00 36.69  ? 1051 ILE A O     1 
ATOM   6520  C  CB    . ILE A 1 1051 ? 155.783 153.540 132.992 1.00 30.22  ? 1051 ILE A CB    1 
ATOM   6521  C  CG1   . ILE A 1 1051 ? 156.837 152.511 133.403 1.00 32.36  ? 1051 ILE A CG1   1 
ATOM   6522  C  CG2   . ILE A 1 1051 ? 154.437 152.871 132.801 1.00 31.15  ? 1051 ILE A CG2   1 
ATOM   6523  C  CD1   . ILE A 1 1051 ? 156.673 151.994 134.810 1.00 28.08  ? 1051 ILE A CD1   1 
ATOM   6524  N  N     . PHE A 1 1052 ? 154.943 156.333 131.827 1.00 30.66  ? 1052 PHE A N     1 
ATOM   6525  C  CA    . PHE A 1 1052 ? 153.925 157.275 131.383 1.00 29.78  ? 1052 PHE A CA    1 
ATOM   6526  C  C     . PHE A 1 1052 ? 154.298 157.918 130.057 1.00 30.50  ? 1052 PHE A C     1 
ATOM   6527  O  O     . PHE A 1 1052 ? 153.418 158.173 129.225 1.00 31.73  ? 1052 PHE A O     1 
ATOM   6528  C  CB    . PHE A 1 1052 ? 153.696 158.349 132.446 1.00 32.92  ? 1052 PHE A CB    1 
ATOM   6529  C  CG    . PHE A 1 1052 ? 153.228 157.810 133.766 1.00 35.12  ? 1052 PHE A CG    1 
ATOM   6530  C  CD1   . PHE A 1 1052 ? 152.333 156.756 133.821 1.00 37.37  ? 1052 PHE A CD1   1 
ATOM   6531  C  CD2   . PHE A 1 1052 ? 153.667 158.370 134.952 1.00 36.76  ? 1052 PHE A CD2   1 
ATOM   6532  C  CE1   . PHE A 1 1052 ? 151.896 156.261 135.033 1.00 37.58  ? 1052 PHE A CE1   1 
ATOM   6533  C  CE2   . PHE A 1 1052 ? 153.231 157.880 136.167 1.00 39.26  ? 1052 PHE A CE2   1 
ATOM   6534  C  CZ    . PHE A 1 1052 ? 152.346 156.825 136.206 1.00 38.62  ? 1052 PHE A CZ    1 
ATOM   6535  N  N     . THR A 1 1053 ? 155.589 158.180 129.835 1.00 30.04  ? 1053 THR A N     1 
ATOM   6536  C  CA    . THR A 1 1053 ? 156.005 158.725 128.547 1.00 30.98  ? 1053 THR A CA    1 
ATOM   6537  C  C     . THR A 1 1053 ? 155.674 157.762 127.414 1.00 29.03  ? 1053 THR A C     1 
ATOM   6538  O  O     . THR A 1 1053 ? 155.141 158.173 126.373 1.00 30.64  ? 1053 THR A O     1 
ATOM   6539  C  CB    . THR A 1 1053 ? 157.501 159.036 128.556 1.00 33.13  ? 1053 THR A CB    1 
ATOM   6540  O  OG1   . THR A 1 1053 ? 157.800 159.947 129.619 1.00 37.75  ? 1053 THR A OG1   1 
ATOM   6541  C  CG2   . THR A 1 1053 ? 157.915 159.660 127.239 1.00 32.49  ? 1053 THR A CG2   1 
ATOM   6542  N  N     . HIS A 1 1054 ? 155.965 156.472 127.608 1.00 28.72  ? 1054 HIS A N     1 
ATOM   6543  C  CA    . HIS A 1 1054 ? 155.638 155.484 126.590 1.00 27.68  ? 1054 HIS A CA    1 
ATOM   6544  C  C     . HIS A 1 1054 ? 154.136 155.369 126.392 1.00 28.53  ? 1054 HIS A C     1 
ATOM   6545  O  O     . HIS A 1 1054 ? 153.669 155.237 125.260 1.00 31.24  ? 1054 HIS A O     1 
ATOM   6546  C  CB    . HIS A 1 1054 ? 156.233 154.123 126.946 1.00 26.64  ? 1054 HIS A CB    1 
ATOM   6547  C  CG    . HIS A 1 1054 ? 156.271 153.169 125.793 1.00 29.53  ? 1054 HIS A CG    1 
ATOM   6548  N  ND1   . HIS A 1 1054 ? 157.218 153.245 124.795 1.00 29.38  ? 1054 HIS A ND1   1 
ATOM   6549  C  CD2   . HIS A 1 1054 ? 155.471 152.125 125.472 1.00 29.18  ? 1054 HIS A CD2   1 
ATOM   6550  C  CE1   . HIS A 1 1054 ? 157.000 152.287 123.912 1.00 31.94  ? 1054 HIS A CE1   1 
ATOM   6551  N  NE2   . HIS A 1 1054 ? 155.947 151.592 124.300 1.00 30.16  ? 1054 HIS A NE2   1 
ATOM   6552  N  N     . LEU A 1 1055 ? 153.362 155.416 127.476 1.00 28.04  ? 1055 LEU A N     1 
ATOM   6553  C  CA    . LEU A 1 1055 ? 151.913 155.309 127.336 1.00 26.35  ? 1055 LEU A CA    1 
ATOM   6554  C  C     . LEU A 1 1055 ? 151.345 156.477 126.532 1.00 29.64  ? 1055 LEU A C     1 
ATOM   6555  O  O     . LEU A 1 1055 ? 150.502 156.284 125.644 1.00 31.78  ? 1055 LEU A O     1 
ATOM   6556  C  CB    . LEU A 1 1055 ? 151.273 155.238 128.720 1.00 29.17  ? 1055 LEU A CB    1 
ATOM   6557  C  CG    . LEU A 1 1055 ? 149.840 154.727 128.832 1.00 37.56  ? 1055 LEU A CG    1 
ATOM   6558  C  CD1   . LEU A 1 1055 ? 149.783 153.266 128.435 1.00 34.46  ? 1055 LEU A CD1   1 
ATOM   6559  C  CD2   . LEU A 1 1055 ? 149.324 154.920 130.244 1.00 38.57  ? 1055 LEU A CD2   1 
ATOM   6560  N  N     . VAL A 1 1056 ? 151.820 157.693 126.811 1.00 29.41  ? 1056 VAL A N     1 
ATOM   6561  C  CA    . VAL A 1 1056 ? 151.346 158.868 126.086 1.00 29.09  ? 1056 VAL A CA    1 
ATOM   6562  C  C     . VAL A 1 1056 ? 151.711 158.771 124.608 1.00 30.59  ? 1056 VAL A C     1 
ATOM   6563  O  O     . VAL A 1 1056 ? 150.860 158.951 123.724 1.00 32.18  ? 1056 VAL A O     1 
ATOM   6564  C  CB    . VAL A 1 1056 ? 151.917 160.148 126.721 1.00 28.74  ? 1056 VAL A CB    1 
ATOM   6565  C  CG1   . VAL A 1 1056 ? 151.782 161.319 125.768 1.00 32.82  ? 1056 VAL A CG1   1 
ATOM   6566  C  CG2   . VAL A 1 1056 ? 151.226 160.440 128.040 1.00 30.94  ? 1056 VAL A CG2   1 
ATOM   6567  N  N     . THR A 1 1057 ? 152.980 158.472 124.315 1.00 32.08  ? 1057 THR A N     1 
ATOM   6568  C  CA    . THR A 1 1057 ? 153.394 158.421 122.917 1.00 29.71  ? 1057 THR A CA    1 
ATOM   6569  C  C     . THR A 1 1057 ? 152.755 157.250 122.179 1.00 30.83  ? 1057 THR A C     1 
ATOM   6570  O  O     . THR A 1 1057 ? 152.603 157.306 120.955 1.00 33.42  ? 1057 THR A O     1 
ATOM   6571  C  CB    . THR A 1 1057 ? 154.921 158.365 122.817 1.00 27.88  ? 1057 THR A CB    1 
ATOM   6572  O  OG1   . THR A 1 1057 ? 155.323 158.641 121.470 1.00 34.30  ? 1057 THR A OG1   1 
ATOM   6573  C  CG2   . THR A 1 1057 ? 155.451 157.012 123.228 1.00 26.67  ? 1057 THR A CG2   1 
ATOM   6574  N  N     . SER A 1 1058 ? 152.368 156.192 122.897 1.00 31.38  ? 1058 SER A N     1 
ATOM   6575  C  CA    . SER A 1 1058 ? 151.667 155.082 122.264 1.00 30.20  ? 1058 SER A CA    1 
ATOM   6576  C  C     . SER A 1 1058 ? 150.238 155.460 121.914 1.00 30.31  ? 1058 SER A C     1 
ATOM   6577  O  O     . SER A 1 1058 ? 149.736 155.081 120.851 1.00 31.10  ? 1058 SER A O     1 
ATOM   6578  C  CB    . SER A 1 1058 ? 151.683 153.859 123.178 1.00 29.94  ? 1058 SER A CB    1 
ATOM   6579  O  OG    . SER A 1 1058 ? 152.983 153.311 123.259 1.00 32.25  ? 1058 SER A OG    1 
ATOM   6580  N  N     . LEU A 1 1059 ? 149.556 156.187 122.802 1.00 31.39  ? 1059 LEU A N     1 
ATOM   6581  C  CA    . LEU A 1 1059 ? 148.195 156.605 122.482 1.00 30.66  ? 1059 LEU A CA    1 
ATOM   6582  C  C     . LEU A 1 1059 ? 148.172 157.625 121.353 1.00 32.83  ? 1059 LEU A C     1 
ATOM   6583  O  O     . LEU A 1 1059 ? 147.239 157.634 120.542 1.00 32.61  ? 1059 LEU A O     1 
ATOM   6584  C  CB    . LEU A 1 1059 ? 147.489 157.160 123.716 1.00 31.01  ? 1059 LEU A CB    1 
ATOM   6585  C  CG    . LEU A 1 1059 ? 146.933 156.095 124.655 1.00 37.25  ? 1059 LEU A CG    1 
ATOM   6586  C  CD1   . LEU A 1 1059 ? 146.382 156.724 125.918 1.00 40.71  ? 1059 LEU A CD1   1 
ATOM   6587  C  CD2   . LEU A 1 1059 ? 145.863 155.292 123.937 1.00 36.61  ? 1059 LEU A CD2   1 
ATOM   6588  N  N     . LYS A 1 1060 ? 149.181 158.496 121.281 1.00 36.04  ? 1060 LYS A N     1 
ATOM   6589  C  CA    . LYS A 1 1060 ? 149.161 159.516 120.235 1.00 32.61  ? 1060 LYS A CA    1 
ATOM   6590  C  C     . LYS A 1 1060 ? 149.310 158.927 118.835 1.00 34.29  ? 1060 LYS A C     1 
ATOM   6591  O  O     . LYS A 1 1060 ? 148.785 159.496 117.873 1.00 36.34  ? 1060 LYS A O     1 
ATOM   6592  C  CB    . LYS A 1 1060 ? 150.245 160.561 120.487 1.00 33.52  ? 1060 LYS A CB    1 
ATOM   6593  C  CG    . LYS A 1 1060 ? 149.880 161.555 121.563 1.00 41.08  ? 1060 LYS A CG    1 
ATOM   6594  C  CD    . LYS A 1 1060 ? 150.938 162.623 121.726 1.00 45.56  ? 1060 LYS A CD    1 
ATOM   6595  C  CE    . LYS A 1 1060 ? 150.549 163.592 122.827 1.00 55.53  ? 1060 LYS A CE    1 
ATOM   6596  N  NZ    . LYS A 1 1060 ? 149.322 164.356 122.468 1.00 54.56  ? 1060 LYS A NZ    1 
ATOM   6597  N  N     . GLY A 1 1061 ? 150.007 157.804 118.690 1.00 33.10  ? 1061 GLY A N     1 
ATOM   6598  C  CA    . GLY A 1 1061 ? 150.303 157.283 117.368 1.00 29.47  ? 1061 GLY A CA    1 
ATOM   6599  C  C     . GLY A 1 1061 ? 149.748 155.908 117.059 1.00 30.48  ? 1061 GLY A C     1 
ATOM   6600  O  O     . GLY A 1 1061 ? 150.375 155.138 116.330 1.00 31.30  ? 1061 GLY A O     1 
ATOM   6601  N  N     . LEU A 1 1062 ? 148.577 155.584 117.611 1.00 30.38  ? 1062 LEU A N     1 
ATOM   6602  C  CA    . LEU A 1 1062 ? 148.058 154.221 117.525 1.00 28.92  ? 1062 LEU A CA    1 
ATOM   6603  C  C     . LEU A 1 1062 ? 147.745 153.809 116.089 1.00 32.96  ? 1062 LEU A C     1 
ATOM   6604  O  O     . LEU A 1 1062 ? 148.027 152.671 115.689 1.00 33.99  ? 1062 LEU A O     1 
ATOM   6605  C  CB    . LEU A 1 1062 ? 146.817 154.086 118.405 1.00 28.82  ? 1062 LEU A CB    1 
ATOM   6606  C  CG    . LEU A 1 1062 ? 146.226 152.685 118.528 1.00 31.95  ? 1062 LEU A CG    1 
ATOM   6607  C  CD1   . LEU A 1 1062 ? 147.306 151.679 118.869 1.00 30.69  ? 1062 LEU A CD1   1 
ATOM   6608  C  CD2   . LEU A 1 1062 ? 145.157 152.676 119.590 1.00 33.82  ? 1062 LEU A CD2   1 
ATOM   6609  N  N     . TRP A 1 1063 ? 147.149 154.707 115.299 1.00 33.51  ? 1063 TRP A N     1 
ATOM   6610  C  CA    . TRP A 1 1063 ? 146.808 154.346 113.927 1.00 31.87  ? 1063 TRP A CA    1 
ATOM   6611  C  C     . TRP A 1 1063 ? 148.046 154.092 113.081 1.00 32.87  ? 1063 TRP A C     1 
ATOM   6612  O  O     . TRP A 1 1063 ? 148.039 153.189 112.239 1.00 36.40  ? 1063 TRP A O     1 
ATOM   6613  C  CB    . TRP A 1 1063 ? 145.937 155.420 113.278 1.00 32.25  ? 1063 TRP A CB    1 
ATOM   6614  C  CG    . TRP A 1 1063 ? 144.591 155.582 113.910 1.00 38.18  ? 1063 TRP A CG    1 
ATOM   6615  C  CD1   . TRP A 1 1063 ? 143.920 154.659 114.656 1.00 37.51  ? 1063 TRP A CD1   1 
ATOM   6616  C  CD2   . TRP A 1 1063 ? 143.723 156.714 113.799 1.00 42.82  ? 1063 TRP A CD2   1 
ATOM   6617  N  NE1   . TRP A 1 1063 ? 142.702 155.160 115.046 1.00 37.06  ? 1063 TRP A NE1   1 
ATOM   6618  C  CE2   . TRP A 1 1063 ? 142.556 156.419 114.528 1.00 40.20  ? 1063 TRP A CE2   1 
ATOM   6619  C  CE3   . TRP A 1 1063 ? 143.826 157.956 113.166 1.00 42.07  ? 1063 TRP A CE3   1 
ATOM   6620  C  CZ2   . TRP A 1 1063 ? 141.500 157.318 114.639 1.00 41.41  ? 1063 TRP A CZ2   1 
ATOM   6621  C  CZ3   . TRP A 1 1063 ? 142.778 158.846 113.278 1.00 39.45  ? 1063 TRP A CZ3   1 
ATOM   6622  C  CH2   . TRP A 1 1063 ? 141.631 158.523 114.008 1.00 40.65  ? 1063 TRP A CH2   1 
ATOM   6623  N  N     . THR A 1 1064 ? 149.117 154.855 113.294 1.00 31.68  ? 1064 THR A N     1 
ATOM   6624  C  CA    . THR A 1 1064 ? 150.361 154.588 112.582 1.00 31.09  ? 1064 THR A CA    1 
ATOM   6625  C  C     . THR A 1 1064 ? 150.935 153.234 112.976 1.00 31.56  ? 1064 THR A C     1 
ATOM   6626  O  O     . THR A 1 1064 ? 151.418 152.481 112.120 1.00 34.80  ? 1064 THR A O     1 
ATOM   6627  C  CB    . THR A 1 1064 ? 151.369 155.702 112.858 1.00 31.65  ? 1064 THR A CB    1 
ATOM   6628  O  OG1   . THR A 1 1064 ? 150.786 156.969 112.528 1.00 33.07  ? 1064 THR A OG1   1 
ATOM   6629  C  CG2   . THR A 1 1064 ? 152.619 155.505 112.032 1.00 26.78  ? 1064 THR A CG2   1 
ATOM   6630  N  N     . LEU A 1 1065 ? 150.871 152.902 114.268 1.00 32.00  ? 1065 LEU A N     1 
ATOM   6631  C  CA    . LEU A 1 1065 ? 151.379 151.619 114.741 1.00 29.96  ? 1065 LEU A CA    1 
ATOM   6632  C  C     . LEU A 1 1065 ? 150.611 150.458 114.131 1.00 31.72  ? 1065 LEU A C     1 
ATOM   6633  O  O     . LEU A 1 1065 ? 151.210 149.461 113.716 1.00 32.93  ? 1065 LEU A O     1 
ATOM   6634  C  CB    . LEU A 1 1065 ? 151.304 151.554 116.264 1.00 30.15  ? 1065 LEU A CB    1 
ATOM   6635  C  CG    . LEU A 1 1065 ? 152.421 152.247 117.032 1.00 30.46  ? 1065 LEU A CG    1 
ATOM   6636  C  CD1   . LEU A 1 1065 ? 152.034 152.413 118.488 1.00 32.57  ? 1065 LEU A CD1   1 
ATOM   6637  C  CD2   . LEU A 1 1065 ? 153.691 151.445 116.895 1.00 34.35  ? 1065 LEU A CD2   1 
ATOM   6638  N  N     . ARG A 1 1066 ? 149.283 150.562 114.068 1.00 31.63  ? 1066 ARG A N     1 
ATOM   6639  C  CA    . ARG A 1 1066 ? 148.509 149.474 113.483 1.00 30.12  ? 1066 ARG A CA    1 
ATOM   6640  C  C     . ARG A 1 1066 ? 148.625 149.433 111.965 1.00 35.15  ? 1066 ARG A C     1 
ATOM   6641  O  O     . ARG A 1 1066 ? 148.508 148.354 111.373 1.00 42.16  ? 1066 ARG A O     1 
ATOM   6642  C  CB    . ARG A 1 1066 ? 147.043 149.570 113.900 1.00 28.37  ? 1066 ARG A CB    1 
ATOM   6643  C  CG    . ARG A 1 1066 ? 146.821 149.305 115.371 1.00 33.91  ? 1066 ARG A CG    1 
ATOM   6644  C  CD    . ARG A 1 1066 ? 145.464 148.671 115.624 1.00 35.54  ? 1066 ARG A CD    1 
ATOM   6645  N  NE    . ARG A 1 1066 ? 144.365 149.621 115.503 1.00 37.82  ? 1066 ARG A NE    1 
ATOM   6646  C  CZ    . ARG A 1 1066 ? 143.660 150.082 116.526 1.00 36.97  ? 1066 ARG A CZ    1 
ATOM   6647  N  NH1   . ARG A 1 1066 ? 143.914 149.704 117.766 1.00 34.49  ? 1066 ARG A NH1   1 
ATOM   6648  N  NH2   . ARG A 1 1066 ? 142.673 150.942 116.298 1.00 40.70  ? 1066 ARG A NH2   1 
ATOM   6649  N  N     . ALA A 1 1067 ? 148.847 150.579 111.316 1.00 34.54  ? 1067 ALA A N     1 
ATOM   6650  C  CA    . ALA A 1 1067 ? 149.049 150.581 109.872 1.00 30.53  ? 1067 ALA A CA    1 
ATOM   6651  C  C     . ALA A 1 1067 ? 150.365 149.915 109.494 1.00 34.27  ? 1067 ALA A C     1 
ATOM   6652  O  O     . ALA A 1 1067 ? 150.403 149.084 108.581 1.00 35.77  ? 1067 ALA A O     1 
ATOM   6653  C  CB    . ALA A 1 1067 ? 148.999 152.010 109.337 1.00 32.82  ? 1067 ALA A CB    1 
ATOM   6654  N  N     . PHE A 1 1068 ? 151.456 150.261 110.182 1.00 35.89  ? 1068 PHE A N     1 
ATOM   6655  C  CA    . PHE A 1 1068 ? 152.744 149.662 109.844 1.00 31.99  ? 1068 PHE A CA    1 
ATOM   6656  C  C     . PHE A 1 1068 ? 152.865 148.238 110.374 1.00 37.27  ? 1068 PHE A C     1 
ATOM   6657  O  O     . PHE A 1 1068 ? 153.422 147.369 109.696 1.00 44.85  ? 1068 PHE A O     1 
ATOM   6658  C  CB    . PHE A 1 1068 ? 153.891 150.518 110.379 1.00 30.47  ? 1068 PHE A CB    1 
ATOM   6659  C  CG    . PHE A 1 1068 ? 154.150 151.765 109.583 1.00 32.43  ? 1068 PHE A CG    1 
ATOM   6660  C  CD1   . PHE A 1 1068 ? 153.212 152.779 109.522 1.00 33.96  ? 1068 PHE A CD1   1 
ATOM   6661  C  CD2   . PHE A 1 1068 ? 155.339 151.922 108.895 1.00 33.40  ? 1068 PHE A CD2   1 
ATOM   6662  C  CE1   . PHE A 1 1068 ? 153.455 153.923 108.794 1.00 32.94  ? 1068 PHE A CE1   1 
ATOM   6663  C  CE2   . PHE A 1 1068 ? 155.585 153.064 108.164 1.00 29.15  ? 1068 PHE A CE2   1 
ATOM   6664  C  CZ    . PHE A 1 1068 ? 154.643 154.065 108.114 1.00 28.68  ? 1068 PHE A CZ    1 
ATOM   6665  N  N     . GLY A 1 1069 ? 152.351 147.976 111.571 1.00 38.17  ? 1069 GLY A N     1 
ATOM   6666  C  CA    . GLY A 1 1069 ? 152.486 146.665 112.169 1.00 33.44  ? 1069 GLY A CA    1 
ATOM   6667  C  C     . GLY A 1 1069 ? 153.621 146.526 113.155 1.00 35.04  ? 1069 GLY A C     1 
ATOM   6668  O  O     . GLY A 1 1069 ? 154.224 145.450 113.239 1.00 37.21  ? 1069 GLY A O     1 
ATOM   6669  N  N     . ARG A 1 1070 ? 153.934 147.579 113.908 1.00 33.98  ? 1070 ARG A N     1 
ATOM   6670  C  CA    . ARG A 1 1070 ? 155.046 147.599 114.860 1.00 32.88  ? 1070 ARG A CA    1 
ATOM   6671  C  C     . ARG A 1 1070 ? 154.605 147.400 116.304 1.00 34.41  ? 1070 ARG A C     1 
ATOM   6672  O  O     . ARG A 1 1070 ? 155.195 147.990 117.211 1.00 37.08  ? 1070 ARG A O     1 
ATOM   6673  C  CB    . ARG A 1 1070 ? 155.817 148.906 114.719 1.00 33.32  ? 1070 ARG A CB    1 
ATOM   6674  C  CG    . ARG A 1 1070 ? 156.383 149.191 113.344 1.00 35.69  ? 1070 ARG A CG    1 
ATOM   6675  C  CD    . ARG A 1 1070 ? 157.414 148.152 112.940 1.00 36.66  ? 1070 ARG A CD    1 
ATOM   6676  N  NE    . ARG A 1 1070 ? 157.963 148.420 111.618 1.00 40.79  ? 1070 ARG A NE    1 
ATOM   6677  C  CZ    . ARG A 1 1070 ? 157.670 147.731 110.526 1.00 46.33  ? 1070 ARG A CZ    1 
ATOM   6678  N  NH1   . ARG A 1 1070 ? 156.848 146.697 110.562 1.00 46.34  ? 1070 ARG A NH1   1 
ATOM   6679  N  NH2   . ARG A 1 1070 ? 158.224 148.082 109.370 1.00 48.75  ? 1070 ARG A NH2   1 
ATOM   6680  N  N     . GLN A 1 1071 ? 153.571 146.594 116.558 1.00 33.03  ? 1071 GLN A N     1 
ATOM   6681  C  CA    . GLN A 1 1071 ? 153.149 146.365 117.940 1.00 28.82  ? 1071 GLN A CA    1 
ATOM   6682  C  C     . GLN A 1 1071 ? 154.217 145.678 118.788 1.00 32.21  ? 1071 GLN A C     1 
ATOM   6683  O  O     . GLN A 1 1071 ? 154.449 146.126 119.927 1.00 36.27  ? 1071 GLN A O     1 
ATOM   6684  C  CB    . GLN A 1 1071 ? 151.832 145.585 117.956 1.00 28.20  ? 1071 GLN A CB    1 
ATOM   6685  C  CG    . GLN A 1 1071 ? 150.658 146.324 117.345 1.00 27.26  ? 1071 GLN A CG    1 
ATOM   6686  C  CD    . GLN A 1 1071 ? 150.383 145.900 115.923 1.00 33.32  ? 1071 GLN A CD    1 
ATOM   6687  O  OE1   . GLN A 1 1071 ? 151.291 145.508 115.197 1.00 35.28  ? 1071 GLN A OE1   1 
ATOM   6688  N  NE2   . GLN A 1 1071 ? 149.121 145.962 115.520 1.00 29.55  ? 1071 GLN A NE2   1 
ATOM   6689  N  N     . PRO A 1 1072 ? 154.878 144.602 118.337 1.00 32.46  ? 1072 PRO A N     1 
ATOM   6690  C  CA    . PRO A 1 1072 ? 155.869 143.946 119.208 1.00 36.20  ? 1072 PRO A CA    1 
ATOM   6691  C  C     . PRO A 1 1072 ? 157.022 144.846 119.615 1.00 33.55  ? 1072 PRO A C     1 
ATOM   6692  O  O     . PRO A 1 1072 ? 157.544 144.709 120.729 1.00 38.17  ? 1072 PRO A O     1 
ATOM   6693  C  CB    . PRO A 1 1072 ? 156.351 142.763 118.356 1.00 39.39  ? 1072 PRO A CB    1 
ATOM   6694  C  CG    . PRO A 1 1072 ? 155.255 142.521 117.395 1.00 31.97  ? 1072 PRO A CG    1 
ATOM   6695  C  CD    . PRO A 1 1072 ? 154.734 143.874 117.065 1.00 30.41  ? 1072 PRO A CD    1 
ATOM   6696  N  N     . TYR A 1 1073 ? 157.427 145.770 118.744 1.00 28.28  ? 1073 TYR A N     1 
ATOM   6697  C  CA    . TYR A 1 1073 ? 158.493 146.711 119.068 1.00 29.28  ? 1073 TYR A CA    1 
ATOM   6698  C  C     . TYR A 1 1073 ? 158.122 147.559 120.283 1.00 32.99  ? 1073 TYR A C     1 
ATOM   6699  O  O     . TYR A 1 1073 ? 158.898 147.683 121.245 1.00 35.58  ? 1073 TYR A O     1 
ATOM   6700  C  CB    . TYR A 1 1073 ? 158.757 147.576 117.831 1.00 28.01  ? 1073 TYR A CB    1 
ATOM   6701  C  CG    . TYR A 1 1073 ? 159.845 148.615 117.939 1.00 32.08  ? 1073 TYR A CG    1 
ATOM   6702  C  CD1   . TYR A 1 1073 ? 161.160 148.255 118.177 1.00 33.30  ? 1073 TYR A CD1   1 
ATOM   6703  C  CD2   . TYR A 1 1073 ? 159.556 149.958 117.761 1.00 34.51  ? 1073 TYR A CD2   1 
ATOM   6704  C  CE1   . TYR A 1 1073 ? 162.153 149.209 118.259 1.00 38.11  ? 1073 TYR A CE1   1 
ATOM   6705  C  CE2   . TYR A 1 1073 ? 160.540 150.915 117.845 1.00 37.17  ? 1073 TYR A CE2   1 
ATOM   6706  C  CZ    . TYR A 1 1073 ? 161.837 150.537 118.095 1.00 41.04  ? 1073 TYR A CZ    1 
ATOM   6707  O  OH    . TYR A 1 1073 ? 162.822 151.492 118.175 1.00 42.47  ? 1073 TYR A OH    1 
ATOM   6708  N  N     . PHE A 1 1074 ? 156.909 148.110 120.277 1.00 28.20  ? 1074 PHE A N     1 
ATOM   6709  C  CA    . PHE A 1 1074 ? 156.471 148.944 121.387 1.00 28.29  ? 1074 PHE A CA    1 
ATOM   6710  C  C     . PHE A 1 1074 ? 156.203 148.122 122.640 1.00 31.19  ? 1074 PHE A C     1 
ATOM   6711  O  O     . PHE A 1 1074 ? 156.428 148.607 123.758 1.00 35.36  ? 1074 PHE A O     1 
ATOM   6712  C  CB    . PHE A 1 1074 ? 155.240 149.743 120.971 1.00 29.16  ? 1074 PHE A CB    1 
ATOM   6713  C  CG    . PHE A 1 1074 ? 155.570 151.070 120.363 1.00 33.17  ? 1074 PHE A CG    1 
ATOM   6714  C  CD1   . PHE A 1 1074 ? 156.317 151.140 119.203 1.00 32.35  ? 1074 PHE A CD1   1 
ATOM   6715  C  CD2   . PHE A 1 1074 ? 155.146 152.246 120.952 1.00 34.57  ? 1074 PHE A CD2   1 
ATOM   6716  C  CE1   . PHE A 1 1074 ? 156.634 152.353 118.641 1.00 35.07  ? 1074 PHE A CE1   1 
ATOM   6717  C  CE2   . PHE A 1 1074 ? 155.459 153.466 120.392 1.00 34.61  ? 1074 PHE A CE2   1 
ATOM   6718  C  CZ    . PHE A 1 1074 ? 156.205 153.518 119.234 1.00 37.11  ? 1074 PHE A CZ    1 
ATOM   6719  N  N     . GLU A 1 1075 ? 155.751 146.876 122.484 1.00 30.29  ? 1075 GLU A N     1 
ATOM   6720  C  CA    . GLU A 1 1075 ? 155.606 146.010 123.650 1.00 28.71  ? 1075 GLU A CA    1 
ATOM   6721  C  C     . GLU A 1 1075 ? 156.955 145.743 124.310 1.00 28.43  ? 1075 GLU A C     1 
ATOM   6722  O  O     . GLU A 1 1075 ? 157.065 145.755 125.544 1.00 31.08  ? 1075 GLU A O     1 
ATOM   6723  C  CB    . GLU A 1 1075 ? 154.929 144.704 123.244 1.00 31.23  ? 1075 GLU A CB    1 
ATOM   6724  C  CG    . GLU A 1 1075 ? 153.466 144.871 122.892 1.00 35.22  ? 1075 GLU A CG    1 
ATOM   6725  C  CD    . GLU A 1 1075 ? 152.866 143.633 122.260 1.00 48.05  ? 1075 GLU A CD    1 
ATOM   6726  O  OE1   . GLU A 1 1075 ? 153.574 142.611 122.156 1.00 55.05  ? 1075 GLU A OE1   1 
ATOM   6727  O  OE2   . GLU A 1 1075 ? 151.684 143.684 121.862 1.00 49.53  ? 1075 GLU A OE2   1 
ATOM   6728  N  N     . THR A 1 1076 ? 157.995 145.521 123.506 1.00 27.03  ? 1076 THR A N     1 
ATOM   6729  C  CA    . THR A 1 1076 ? 159.330 145.318 124.059 1.00 27.00  ? 1076 THR A CA    1 
ATOM   6730  C  C     . THR A 1 1076 ? 159.826 146.566 124.778 1.00 31.03  ? 1076 THR A C     1 
ATOM   6731  O  O     . THR A 1 1076 ? 160.443 146.474 125.850 1.00 38.97  ? 1076 THR A O     1 
ATOM   6732  C  CB    . THR A 1 1076 ? 160.301 144.924 122.949 1.00 30.04  ? 1076 THR A CB    1 
ATOM   6733  O  OG1   . THR A 1 1076 ? 159.821 143.746 122.292 1.00 32.05  ? 1076 THR A OG1   1 
ATOM   6734  C  CG2   . THR A 1 1076 ? 161.669 144.646 123.519 1.00 41.55  ? 1076 THR A CG2   1 
ATOM   6735  N  N     . LEU A 1 1077 ? 159.561 147.745 124.208 1.00 29.27  ? 1077 LEU A N     1 
ATOM   6736  C  CA    . LEU A 1 1077 ? 159.976 148.982 124.869 1.00 27.17  ? 1077 LEU A CA    1 
ATOM   6737  C  C     . LEU A 1 1077 ? 159.264 149.165 126.210 1.00 28.98  ? 1077 LEU A C     1 
ATOM   6738  O  O     . LEU A 1 1077 ? 159.877 149.598 127.200 1.00 32.71  ? 1077 LEU A O     1 
ATOM   6739  C  CB    . LEU A 1 1077 ? 159.719 150.174 123.951 1.00 30.25  ? 1077 LEU A CB    1 
ATOM   6740  C  CG    . LEU A 1 1077 ? 160.611 150.293 122.714 1.00 32.54  ? 1077 LEU A CG    1 
ATOM   6741  C  CD1   . LEU A 1 1077 ? 160.031 151.286 121.724 1.00 30.61  ? 1077 LEU A CD1   1 
ATOM   6742  C  CD2   . LEU A 1 1077 ? 162.020 150.684 123.103 1.00 32.75  ? 1077 LEU A CD2   1 
ATOM   6743  N  N     . PHE A 1 1078 ? 157.974 148.822 126.268 1.00 27.12  ? 1078 PHE A N     1 
ATOM   6744  C  CA    . PHE A 1 1078 ? 157.240 148.929 127.527 1.00 25.76  ? 1078 PHE A CA    1 
ATOM   6745  C  C     . PHE A 1 1078 ? 157.771 147.946 128.566 1.00 28.41  ? 1078 PHE A C     1 
ATOM   6746  O  O     . PHE A 1 1078 ? 157.858 148.276 129.758 1.00 32.94  ? 1078 PHE A O     1 
ATOM   6747  C  CB    . PHE A 1 1078 ? 155.749 148.709 127.280 1.00 25.97  ? 1078 PHE A CB    1 
ATOM   6748  C  CG    . PHE A 1 1078 ? 154.885 149.005 128.472 1.00 28.03  ? 1078 PHE A CG    1 
ATOM   6749  C  CD1   . PHE A 1 1078 ? 154.652 150.312 128.861 1.00 28.11  ? 1078 PHE A CD1   1 
ATOM   6750  C  CD2   . PHE A 1 1078 ? 154.285 147.984 129.186 1.00 28.21  ? 1078 PHE A CD2   1 
ATOM   6751  C  CE1   . PHE A 1 1078 ? 153.859 150.594 129.946 1.00 28.49  ? 1078 PHE A CE1   1 
ATOM   6752  C  CE2   . PHE A 1 1078 ? 153.486 148.263 130.275 1.00 29.93  ? 1078 PHE A CE2   1 
ATOM   6753  C  CZ    . PHE A 1 1078 ? 153.273 149.571 130.654 1.00 26.90  ? 1078 PHE A CZ    1 
ATOM   6754  N  N     . HIS A 1 1079 ? 158.131 146.734 128.136 1.00 26.93  ? 1079 HIS A N     1 
ATOM   6755  C  CA    . HIS A 1 1079 ? 158.743 145.785 129.063 1.00 24.91  ? 1079 HIS A CA    1 
ATOM   6756  C  C     . HIS A 1 1079 ? 160.062 146.315 129.609 1.00 28.32  ? 1079 HIS A C     1 
ATOM   6757  O  O     . HIS A 1 1079 ? 160.367 146.140 130.797 1.00 35.25  ? 1079 HIS A O     1 
ATOM   6758  C  CB    . HIS A 1 1079 ? 158.948 144.434 128.382 1.00 28.15  ? 1079 HIS A CB    1 
ATOM   6759  C  CG    . HIS A 1 1079 ? 157.686 143.654 128.201 1.00 32.38  ? 1079 HIS A CG    1 
ATOM   6760  N  ND1   . HIS A 1 1079 ? 156.445 144.165 128.509 1.00 30.78  ? 1079 HIS A ND1   1 
ATOM   6761  C  CD2   . HIS A 1 1079 ? 157.473 142.397 127.746 1.00 33.80  ? 1079 HIS A CD2   1 
ATOM   6762  C  CE1   . HIS A 1 1079 ? 155.522 143.257 128.252 1.00 31.24  ? 1079 HIS A CE1   1 
ATOM   6763  N  NE2   . HIS A 1 1079 ? 156.119 142.175 127.787 1.00 31.56  ? 1079 HIS A NE2   1 
ATOM   6764  N  N     . LYS A 1 1080 ? 160.855 146.969 128.758 1.00 28.51  ? 1080 LYS A N     1 
ATOM   6765  C  CA    . LYS A 1 1080 ? 162.095 147.573 129.239 1.00 30.10  ? 1080 LYS A CA    1 
ATOM   6766  C  C     . LYS A 1 1080 ? 161.823 148.627 130.305 1.00 31.95  ? 1080 LYS A C     1 
ATOM   6767  O  O     . LYS A 1 1080 ? 162.522 148.685 131.325 1.00 36.70  ? 1080 LYS A O     1 
ATOM   6768  C  CB    . LYS A 1 1080 ? 162.876 148.184 128.078 1.00 34.70  ? 1080 LYS A CB    1 
ATOM   6769  C  CG    . LYS A 1 1080 ? 164.039 147.335 127.619 1.00 51.18  ? 1080 LYS A CG    1 
ATOM   6770  C  CD    . LYS A 1 1080 ? 165.076 148.167 126.890 1.00 55.54  ? 1080 LYS A CD    1 
ATOM   6771  C  CE    . LYS A 1 1080 ? 164.545 148.696 125.577 1.00 55.12  ? 1080 LYS A CE    1 
ATOM   6772  N  NZ    . LYS A 1 1080 ? 164.382 147.605 124.580 1.00 52.89  ? 1080 LYS A NZ    1 
ATOM   6773  N  N     . ALA A 1 1081 ? 160.808 149.469 130.091 1.00 31.44  ? 1081 ALA A N     1 
ATOM   6774  C  CA    . ALA A 1 1081 ? 160.478 150.476 131.099 1.00 28.00  ? 1081 ALA A CA    1 
ATOM   6775  C  C     . ALA A 1 1081 ? 160.042 149.844 132.422 1.00 31.70  ? 1081 ALA A C     1 
ATOM   6776  O  O     . ALA A 1 1081 ? 160.458 150.299 133.505 1.00 34.60  ? 1081 ALA A O     1 
ATOM   6777  C  CB    . ALA A 1 1081 ? 159.386 151.406 130.574 1.00 25.32  ? 1081 ALA A CB    1 
ATOM   6778  N  N     . LEU A 1 1082 ? 159.228 148.784 132.357 1.00 27.77  ? 1082 LEU A N     1 
ATOM   6779  C  CA    . LEU A 1 1082 ? 158.792 148.116 133.582 1.00 25.16  ? 1082 LEU A CA    1 
ATOM   6780  C  C     . LEU A 1 1082 ? 159.975 147.527 134.339 1.00 26.76  ? 1082 LEU A C     1 
ATOM   6781  O  O     . LEU A 1 1082 ? 160.050 147.633 135.572 1.00 28.88  ? 1082 LEU A O     1 
ATOM   6782  C  CB    . LEU A 1 1082 ? 157.774 147.021 133.263 1.00 26.27  ? 1082 LEU A CB    1 
ATOM   6783  C  CG    . LEU A 1 1082 ? 156.379 147.416 132.780 1.00 26.76  ? 1082 LEU A CG    1 
ATOM   6784  C  CD1   . LEU A 1 1082 ? 155.621 146.185 132.322 1.00 24.85  ? 1082 LEU A CD1   1 
ATOM   6785  C  CD2   . LEU A 1 1082 ? 155.615 148.132 133.873 1.00 27.66  ? 1082 LEU A CD2   1 
ATOM   6786  N  N     . ASN A 1 1083 ? 160.911 146.904 133.617 1.00 27.94  ? 1083 ASN A N     1 
ATOM   6787  C  CA    . ASN A 1 1083 ? 162.096 146.355 134.268 1.00 28.52  ? 1083 ASN A CA    1 
ATOM   6788  C  C     . ASN A 1 1083 ? 162.939 147.451 134.906 1.00 28.45  ? 1083 ASN A C     1 
ATOM   6789  O  O     . ASN A 1 1083 ? 163.500 147.255 135.996 1.00 28.98  ? 1083 ASN A O     1 
ATOM   6790  C  CB    . ASN A 1 1083 ? 162.927 145.564 133.261 1.00 29.12  ? 1083 ASN A CB    1 
ATOM   6791  C  CG    . ASN A 1 1083 ? 162.226 144.313 132.780 1.00 30.54  ? 1083 ASN A CG    1 
ATOM   6792  O  OD1   . ASN A 1 1083 ? 161.259 143.858 133.385 1.00 35.39  ? 1083 ASN A OD1   1 
ATOM   6793  N  ND2   . ASN A 1 1083 ? 162.717 143.744 131.690 1.00 31.62  ? 1083 ASN A ND2   1 
ATOM   6794  N  N     . LEU A 1 1084 ? 163.029 148.608 134.247 1.00 32.03  ? 1084 LEU A N     1 
ATOM   6795  C  CA    . LEU A 1 1084 ? 163.744 149.740 134.825 1.00 33.49  ? 1084 LEU A CA    1 
ATOM   6796  C  C     . LEU A 1 1084 ? 163.156 150.132 136.175 1.00 35.85  ? 1084 LEU A C     1 
ATOM   6797  O  O     . LEU A 1 1084 ? 163.892 150.372 137.138 1.00 39.04  ? 1084 LEU A O     1 
ATOM   6798  C  CB    . LEU A 1 1084 ? 163.712 150.928 133.865 1.00 35.78  ? 1084 LEU A CB    1 
ATOM   6799  C  CG    . LEU A 1 1084 ? 164.395 152.203 134.368 1.00 44.35  ? 1084 LEU A CG    1 
ATOM   6800  C  CD1   . LEU A 1 1084 ? 165.893 152.004 134.476 1.00 54.23  ? 1084 LEU A CD1   1 
ATOM   6801  C  CD2   . LEU A 1 1084 ? 164.071 153.388 133.474 1.00 43.44  ? 1084 LEU A CD2   1 
ATOM   6802  N  N     . HIS A 1 1085 ? 161.827 150.219 136.263 1.00 32.49  ? 1085 HIS A N     1 
ATOM   6803  C  CA    . HIS A 1 1085 ? 161.221 150.568 137.553 1.00 25.36  ? 1085 HIS A CA    1 
ATOM   6804  C  C     . HIS A 1 1085 ? 161.466 149.483 138.606 1.00 30.19  ? 1085 HIS A C     1 
ATOM   6805  O  O     . HIS A 1 1085 ? 161.797 149.784 139.770 1.00 34.94  ? 1085 HIS A O     1 
ATOM   6806  C  CB    . HIS A 1 1085 ? 159.725 150.823 137.377 1.00 26.83  ? 1085 HIS A CB    1 
ATOM   6807  C  CG    . HIS A 1 1085 ? 159.006 151.120 138.657 1.00 30.87  ? 1085 HIS A CG    1 
ATOM   6808  N  ND1   . HIS A 1 1085 ? 158.204 150.195 139.291 1.00 33.95  ? 1085 HIS A ND1   1 
ATOM   6809  C  CD2   . HIS A 1 1085 ? 158.967 152.238 139.420 1.00 32.12  ? 1085 HIS A CD2   1 
ATOM   6810  C  CE1   . HIS A 1 1085 ? 157.704 150.731 140.390 1.00 33.29  ? 1085 HIS A CE1   1 
ATOM   6811  N  NE2   . HIS A 1 1085 ? 158.151 151.969 140.491 1.00 33.58  ? 1085 HIS A NE2   1 
ATOM   6812  N  N     . THR A 1 1086 ? 161.317 148.214 138.212 1.00 31.14  ? 1086 THR A N     1 
ATOM   6813  C  CA    . THR A 1 1086 ? 161.461 147.114 139.163 1.00 27.95  ? 1086 THR A CA    1 
ATOM   6814  C  C     . THR A 1 1086 ? 162.857 147.065 139.771 1.00 29.79  ? 1086 THR A C     1 
ATOM   6815  O  O     . THR A 1 1086 ? 163.006 146.740 140.960 1.00 32.99  ? 1086 THR A O     1 
ATOM   6816  C  CB    . THR A 1 1086 ? 161.135 145.791 138.475 1.00 27.71  ? 1086 THR A CB    1 
ATOM   6817  O  OG1   . THR A 1 1086 ? 159.795 145.837 137.976 1.00 30.85  ? 1086 THR A OG1   1 
ATOM   6818  C  CG2   . THR A 1 1086 ? 161.268 144.631 139.437 1.00 28.84  ? 1086 THR A CG2   1 
ATOM   6819  N  N     . ALA A 1 1087 ? 163.883 147.401 138.982 1.00 29.54  ? 1087 ALA A N     1 
ATOM   6820  C  CA    . ALA A 1 1087 ? 165.256 147.327 139.476 1.00 31.37  ? 1087 ALA A CA    1 
ATOM   6821  C  C     . ALA A 1 1087 ? 165.454 148.169 140.732 1.00 33.40  ? 1087 ALA A C     1 
ATOM   6822  O  O     . ALA A 1 1087 ? 166.179 147.766 141.648 1.00 36.44  ? 1087 ALA A O     1 
ATOM   6823  C  CB    . ALA A 1 1087 ? 166.228 147.766 138.382 1.00 32.79  ? 1087 ALA A CB    1 
ATOM   6824  N  N     . ASN A 1 1088 ? 164.824 149.341 140.794 1.00 34.32  ? 1088 ASN A N     1 
ATOM   6825  C  CA    . ASN A 1 1088 ? 164.961 150.203 141.964 1.00 31.59  ? 1088 ASN A CA    1 
ATOM   6826  C  C     . ASN A 1 1088 ? 163.995 149.806 143.073 1.00 33.03  ? 1088 ASN A C     1 
ATOM   6827  O  O     . ASN A 1 1088 ? 164.359 149.821 144.263 1.00 33.23  ? 1088 ASN A O     1 
ATOM   6828  C  CB    . ASN A 1 1088 ? 164.725 151.657 141.561 1.00 34.63  ? 1088 ASN A CB    1 
ATOM   6829  C  CG    . ASN A 1 1088 ? 165.728 152.149 140.545 1.00 38.17  ? 1088 ASN A CG    1 
ATOM   6830  O  OD1   . ASN A 1 1088 ? 166.928 151.920 140.677 1.00 39.90  ? 1088 ASN A OD1   1 
ATOM   6831  N  ND2   . ASN A 1 1088 ? 165.238 152.815 139.509 1.00 41.21  ? 1088 ASN A ND2   1 
ATOM   6832  N  N     . TRP A 1 1089 ? 162.760 149.450 142.702 1.00 30.54  ? 1089 TRP A N     1 
ATOM   6833  C  CA    . TRP A 1 1089 ? 161.755 149.171 143.722 1.00 30.57  ? 1089 TRP A CA    1 
ATOM   6834  C  C     . TRP A 1 1089 ? 162.147 147.960 144.568 1.00 31.52  ? 1089 TRP A C     1 
ATOM   6835  O  O     . TRP A 1 1089 ? 161.951 147.956 145.796 1.00 32.58  ? 1089 TRP A O     1 
ATOM   6836  C  CB    . TRP A 1 1089 ? 160.395 148.977 143.050 1.00 29.76  ? 1089 TRP A CB    1 
ATOM   6837  C  CG    . TRP A 1 1089 ? 159.257 148.665 143.969 1.00 31.78  ? 1089 TRP A CG    1 
ATOM   6838  C  CD1   . TRP A 1 1089 ? 158.436 147.581 143.911 1.00 33.83  ? 1089 TRP A CD1   1 
ATOM   6839  C  CD2   . TRP A 1 1089 ? 158.801 149.455 145.071 1.00 35.54  ? 1089 TRP A CD2   1 
ATOM   6840  N  NE1   . TRP A 1 1089 ? 157.502 147.641 144.912 1.00 40.58  ? 1089 TRP A NE1   1 
ATOM   6841  C  CE2   . TRP A 1 1089 ? 157.705 148.783 145.639 1.00 35.52  ? 1089 TRP A CE2   1 
ATOM   6842  C  CE3   . TRP A 1 1089 ? 159.217 150.662 145.637 1.00 37.94  ? 1089 TRP A CE3   1 
ATOM   6843  C  CZ2   . TRP A 1 1089 ? 157.019 149.275 146.740 1.00 32.23  ? 1089 TRP A CZ2   1 
ATOM   6844  C  CZ3   . TRP A 1 1089 ? 158.535 151.148 146.729 1.00 37.44  ? 1089 TRP A CZ3   1 
ATOM   6845  C  CH2   . TRP A 1 1089 ? 157.449 150.456 147.269 1.00 33.44  ? 1089 TRP A CH2   1 
ATOM   6846  N  N     . PHE A 1 1090 ? 162.729 146.937 143.936 1.00 28.87  ? 1090 PHE A N     1 
ATOM   6847  C  CA    . PHE A 1 1090 ? 163.095 145.728 144.669 1.00 26.74  ? 1090 PHE A CA    1 
ATOM   6848  C  C     . PHE A 1 1090 ? 164.168 146.009 145.717 1.00 30.97  ? 1090 PHE A C     1 
ATOM   6849  O  O     . PHE A 1 1090 ? 164.072 145.536 146.859 1.00 32.87  ? 1090 PHE A O     1 
ATOM   6850  C  CB    . PHE A 1 1090 ? 163.567 144.658 143.687 1.00 29.97  ? 1090 PHE A CB    1 
ATOM   6851  C  CG    . PHE A 1 1090 ? 163.868 143.336 144.324 1.00 37.38  ? 1090 PHE A CG    1 
ATOM   6852  C  CD1   . PHE A 1 1090 ? 162.843 142.498 144.726 1.00 38.28  ? 1090 PHE A CD1   1 
ATOM   6853  C  CD2   . PHE A 1 1090 ? 165.176 142.926 144.515 1.00 40.28  ? 1090 PHE A CD2   1 
ATOM   6854  C  CE1   . PHE A 1 1090 ? 163.115 141.280 145.308 1.00 39.50  ? 1090 PHE A CE1   1 
ATOM   6855  C  CE2   . PHE A 1 1090 ? 165.455 141.708 145.099 1.00 41.24  ? 1090 PHE A CE2   1 
ATOM   6856  C  CZ    . PHE A 1 1090 ? 164.423 140.884 145.496 1.00 40.74  ? 1090 PHE A CZ    1 
ATOM   6857  N  N     . LEU A 1 1091 ? 165.191 146.785 145.350 1.00 31.63  ? 1091 LEU A N     1 
ATOM   6858  C  CA    . LEU A 1 1091 ? 166.246 147.128 146.297 1.00 30.08  ? 1091 LEU A CA    1 
ATOM   6859  C  C     . LEU A 1 1091 ? 165.707 147.968 147.446 1.00 28.82  ? 1091 LEU A C     1 
ATOM   6860  O  O     . LEU A 1 1091 ? 166.115 147.782 148.603 1.00 31.25  ? 1091 LEU A O     1 
ATOM   6861  C  CB    . LEU A 1 1091 ? 167.375 147.871 145.586 1.00 30.61  ? 1091 LEU A CB    1 
ATOM   6862  C  CG    . LEU A 1 1091 ? 168.374 147.034 144.792 1.00 35.91  ? 1091 LEU A CG    1 
ATOM   6863  C  CD1   . LEU A 1 1091 ? 169.290 147.943 143.990 1.00 39.22  ? 1091 LEU A CD1   1 
ATOM   6864  C  CD2   . LEU A 1 1091 ? 169.171 146.132 145.718 1.00 31.12  ? 1091 LEU A CD2   1 
ATOM   6865  N  N     . TYR A 1 1092 ? 164.794 148.898 147.149 1.00 26.31  ? 1092 TYR A N     1 
ATOM   6866  C  CA    . TYR A 1 1092 ? 164.200 149.689 148.223 1.00 27.03  ? 1092 TYR A CA    1 
ATOM   6867  C  C     . TYR A 1 1092 ? 163.506 148.791 149.244 1.00 28.83  ? 1092 TYR A C     1 
ATOM   6868  O  O     . TYR A 1 1092 ? 163.727 148.917 150.460 1.00 29.45  ? 1092 TYR A O     1 
ATOM   6869  C  CB    . TYR A 1 1092 ? 163.216 150.709 147.652 1.00 28.45  ? 1092 TYR A CB    1 
ATOM   6870  C  CG    . TYR A 1 1092 ? 162.565 151.562 148.715 1.00 31.57  ? 1092 TYR A CG    1 
ATOM   6871  C  CD1   . TYR A 1 1092 ? 163.231 152.646 149.262 1.00 31.23  ? 1092 TYR A CD1   1 
ATOM   6872  C  CD2   . TYR A 1 1092 ? 161.292 151.272 149.181 1.00 31.49  ? 1092 TYR A CD2   1 
ATOM   6873  C  CE1   . TYR A 1 1092 ? 162.647 153.419 150.238 1.00 30.87  ? 1092 TYR A CE1   1 
ATOM   6874  C  CE2   . TYR A 1 1092 ? 160.701 152.039 150.157 1.00 29.73  ? 1092 TYR A CE2   1 
ATOM   6875  C  CZ    . TYR A 1 1092 ? 161.381 153.110 150.682 1.00 31.82  ? 1092 TYR A CZ    1 
ATOM   6876  O  OH    . TYR A 1 1092 ? 160.789 153.880 151.655 1.00 35.22  ? 1092 TYR A OH    1 
ATOM   6877  N  N     . LEU A 1 1093 ? 162.675 147.860 148.763 1.00 26.49  ? 1093 LEU A N     1 
ATOM   6878  C  CA    . LEU A 1 1093 ? 161.958 146.983 149.688 1.00 28.02  ? 1093 LEU A CA    1 
ATOM   6879  C  C     . LEU A 1 1093 ? 162.916 146.106 150.488 1.00 29.27  ? 1093 LEU A C     1 
ATOM   6880  O  O     . LEU A 1 1093 ? 162.711 145.889 151.692 1.00 29.48  ? 1093 LEU A O     1 
ATOM   6881  C  CB    . LEU A 1 1093 ? 160.948 146.116 148.938 1.00 32.24  ? 1093 LEU A CB    1 
ATOM   6882  C  CG    . LEU A 1 1093 ? 159.694 146.792 148.384 1.00 32.39  ? 1093 LEU A CG    1 
ATOM   6883  C  CD1   . LEU A 1 1093 ? 158.914 145.834 147.502 1.00 31.13  ? 1093 LEU A CD1   1 
ATOM   6884  C  CD2   . LEU A 1 1093 ? 158.828 147.297 149.518 1.00 28.09  ? 1093 LEU A CD2   1 
ATOM   6885  N  N     . SER A 1 1094 ? 163.968 145.597 149.840 1.00 28.41  ? 1094 SER A N     1 
ATOM   6886  C  CA    . SER A 1 1094 ? 164.904 144.719 150.538 1.00 26.50  ? 1094 SER A CA    1 
ATOM   6887  C  C     . SER A 1 1094 ? 165.625 145.452 151.663 1.00 25.38  ? 1094 SER A C     1 
ATOM   6888  O  O     . SER A 1 1094 ? 165.756 144.923 152.778 1.00 28.42  ? 1094 SER A O     1 
ATOM   6889  C  CB    . SER A 1 1094 ? 165.910 144.139 149.547 1.00 30.28  ? 1094 SER A CB    1 
ATOM   6890  O  OG    . SER A 1 1094 ? 165.281 143.237 148.659 1.00 32.14  ? 1094 SER A OG    1 
ATOM   6891  N  N     . THR A 1 1095 ? 166.086 146.679 151.403 1.00 22.58  ? 1095 THR A N     1 
ATOM   6892  C  CA    . THR A 1 1095 ? 166.766 147.418 152.463 1.00 24.29  ? 1095 THR A CA    1 
ATOM   6893  C  C     . THR A 1 1095 ? 165.812 147.796 153.594 1.00 24.98  ? 1095 THR A C     1 
ATOM   6894  O  O     . THR A 1 1095 ? 166.214 147.798 154.768 1.00 24.84  ? 1095 THR A O     1 
ATOM   6895  C  CB    . THR A 1 1095 ? 167.444 148.664 151.897 1.00 28.19  ? 1095 THR A CB    1 
ATOM   6896  O  OG1   . THR A 1 1095 ? 166.461 149.524 151.310 1.00 30.50  ? 1095 THR A OG1   1 
ATOM   6897  C  CG2   . THR A 1 1095 ? 168.478 148.280 150.854 1.00 24.61  ? 1095 THR A CG2   1 
ATOM   6898  N  N     . LEU A 1 1096 ? 164.550 148.102 153.274 1.00 25.37  ? 1096 LEU A N     1 
ATOM   6899  C  CA    . LEU A 1 1096 ? 163.590 148.390 154.338 1.00 23.22  ? 1096 LEU A CA    1 
ATOM   6900  C  C     . LEU A 1 1096 ? 163.385 147.177 155.244 1.00 23.16  ? 1096 LEU A C     1 
ATOM   6901  O  O     . LEU A 1 1096 ? 163.351 147.306 156.479 1.00 25.11  ? 1096 LEU A O     1 
ATOM   6902  C  CB    . LEU A 1 1096 ? 162.266 148.851 153.730 1.00 24.13  ? 1096 LEU A CB    1 
ATOM   6903  C  CG    . LEU A 1 1096 ? 161.156 149.253 154.701 1.00 25.38  ? 1096 LEU A CG    1 
ATOM   6904  C  CD1   . LEU A 1 1096 ? 161.609 150.397 155.579 1.00 25.03  ? 1096 LEU A CD1   1 
ATOM   6905  C  CD2   . LEU A 1 1096 ? 159.901 149.633 153.947 1.00 22.90  ? 1096 LEU A CD2   1 
ATOM   6906  N  N     . ARG A 1 1097 ? 163.253 145.988 154.648 1.00 24.68  ? 1097 ARG A N     1 
ATOM   6907  C  CA    . ARG A 1 1097 ? 163.113 144.771 155.448 1.00 24.02  ? 1097 ARG A CA    1 
ATOM   6908  C  C     . ARG A 1 1097 ? 164.336 144.540 156.328 1.00 25.34  ? 1097 ARG A C     1 
ATOM   6909  O  O     . ARG A 1 1097 ? 164.207 144.154 157.502 1.00 26.02  ? 1097 ARG A O     1 
ATOM   6910  C  CB    . ARG A 1 1097 ? 162.875 143.571 154.534 1.00 23.00  ? 1097 ARG A CB    1 
ATOM   6911  C  CG    . ARG A 1 1097 ? 162.492 142.287 155.251 1.00 25.34  ? 1097 ARG A CG    1 
ATOM   6912  C  CD    . ARG A 1 1097 ? 161.361 142.474 156.244 1.00 28.43  ? 1097 ARG A CD    1 
ATOM   6913  N  NE    . ARG A 1 1097 ? 160.214 143.159 155.666 1.00 33.50  ? 1097 ARG A NE    1 
ATOM   6914  C  CZ    . ARG A 1 1097 ? 159.369 143.912 156.357 1.00 33.16  ? 1097 ARG A CZ    1 
ATOM   6915  N  NH1   . ARG A 1 1097 ? 159.494 144.070 157.663 1.00 32.85  ? 1097 ARG A NH1   1 
ATOM   6916  N  NH2   . ARG A 1 1097 ? 158.374 144.519 155.721 1.00 32.93  ? 1097 ARG A NH2   1 
ATOM   6917  N  N     . TRP A 1 1098 ? 165.530 144.768 155.776 1.00 26.43  ? 1098 TRP A N     1 
ATOM   6918  C  CA    . TRP A 1 1098 ? 166.755 144.622 156.558 1.00 22.11  ? 1098 TRP A CA    1 
ATOM   6919  C  C     . TRP A 1 1098 ? 166.724 145.518 157.792 1.00 22.26  ? 1098 TRP A C     1 
ATOM   6920  O  O     . TRP A 1 1098 ? 167.021 145.075 158.911 1.00 26.50  ? 1098 TRP A O     1 
ATOM   6921  C  CB    . TRP A 1 1098 ? 167.963 144.967 155.687 1.00 24.83  ? 1098 TRP A CB    1 
ATOM   6922  C  CG    . TRP A 1 1098 ? 169.275 144.952 156.408 1.00 25.81  ? 1098 TRP A CG    1 
ATOM   6923  C  CD1   . TRP A 1 1098 ? 170.097 143.883 156.577 1.00 26.01  ? 1098 TRP A CD1   1 
ATOM   6924  C  CD2   . TRP A 1 1098 ? 169.895 146.045 157.094 1.00 27.28  ? 1098 TRP A CD2   1 
ATOM   6925  N  NE1   . TRP A 1 1098 ? 171.205 144.246 157.297 1.00 27.15  ? 1098 TRP A NE1   1 
ATOM   6926  C  CE2   . TRP A 1 1098 ? 171.100 145.568 157.632 1.00 24.95  ? 1098 TRP A CE2   1 
ATOM   6927  C  CE3   . TRP A 1 1098 ? 169.550 147.383 157.298 1.00 25.96  ? 1098 TRP A CE3   1 
ATOM   6928  C  CZ2   . TRP A 1 1098 ? 171.963 146.376 158.361 1.00 23.90  ? 1098 TRP A CZ2   1 
ATOM   6929  C  CZ3   . TRP A 1 1098 ? 170.406 148.183 158.023 1.00 25.97  ? 1098 TRP A CZ3   1 
ATOM   6930  C  CH2   . TRP A 1 1098 ? 171.598 147.678 158.545 1.00 26.85  ? 1098 TRP A CH2   1 
ATOM   6931  N  N     . PHE A 1 1099 ? 166.364 146.791 157.599 1.00 23.15  ? 1099 PHE A N     1 
ATOM   6932  C  CA    . PHE A 1 1099 ? 166.332 147.734 158.718 1.00 23.65  ? 1099 PHE A CA    1 
ATOM   6933  C  C     . PHE A 1 1099 ? 165.347 147.294 159.793 1.00 24.65  ? 1099 PHE A C     1 
ATOM   6934  O  O     . PHE A 1 1099 ? 165.659 147.326 160.992 1.00 28.36  ? 1099 PHE A O     1 
ATOM   6935  C  CB    . PHE A 1 1099 ? 165.979 149.133 158.214 1.00 25.42  ? 1099 PHE A CB    1 
ATOM   6936  C  CG    . PHE A 1 1099 ? 165.732 150.130 159.311 1.00 23.77  ? 1099 PHE A CG    1 
ATOM   6937  C  CD1   . PHE A 1 1099 ? 166.787 150.715 159.988 1.00 24.05  ? 1099 PHE A CD1   1 
ATOM   6938  C  CD2   . PHE A 1 1099 ? 164.441 150.490 159.657 1.00 23.55  ? 1099 PHE A CD2   1 
ATOM   6939  C  CE1   . PHE A 1 1099 ? 166.561 151.632 160.991 1.00 23.97  ? 1099 PHE A CE1   1 
ATOM   6940  C  CE2   . PHE A 1 1099 ? 164.209 151.404 160.663 1.00 24.16  ? 1099 PHE A CE2   1 
ATOM   6941  C  CZ    . PHE A 1 1099 ? 165.272 151.978 161.329 1.00 24.81  ? 1099 PHE A CZ    1 
ATOM   6942  N  N     . GLN A 1 1100 ? 164.143 146.891 159.380 1.00 25.36  ? 1100 GLN A N     1 
ATOM   6943  C  CA    . GLN A 1 1100 ? 163.131 146.497 160.357 1.00 23.80  ? 1100 GLN A CA    1 
ATOM   6944  C  C     . GLN A 1 1100 ? 163.597 145.298 161.177 1.00 26.67  ? 1100 GLN A C     1 
ATOM   6945  O  O     . GLN A 1 1100 ? 163.438 145.265 162.411 1.00 27.95  ? 1100 GLN A O     1 
ATOM   6946  C  CB    . GLN A 1 1100 ? 161.823 146.180 159.639 1.00 24.56  ? 1100 GLN A CB    1 
ATOM   6947  C  CG    . GLN A 1 1100 ? 161.246 147.358 158.875 1.00 27.28  ? 1100 GLN A CG    1 
ATOM   6948  C  CD    . GLN A 1 1100 ? 159.773 147.562 159.128 1.00 33.39  ? 1100 GLN A CD    1 
ATOM   6949  O  OE1   . GLN A 1 1100 ? 159.058 146.623 159.469 1.00 37.87  ? 1100 GLN A OE1   1 
ATOM   6950  N  NE2   . GLN A 1 1100 ? 159.304 148.789 158.944 1.00 30.51  ? 1100 GLN A NE2   1 
ATOM   6951  N  N     . MET A 1 1101 ? 164.200 144.312 160.508 1.00 27.74  ? 1101 MET A N     1 
ATOM   6952  C  CA    . MET A 1 1101 ? 164.658 143.123 161.215 1.00 26.42  ? 1101 MET A CA    1 
ATOM   6953  C  C     . MET A 1 1101 ? 165.776 143.464 162.194 1.00 27.78  ? 1101 MET A C     1 
ATOM   6954  O  O     . MET A 1 1101 ? 165.819 142.923 163.306 1.00 30.29  ? 1101 MET A O     1 
ATOM   6955  C  CB    . MET A 1 1101 ? 165.105 142.064 160.207 1.00 26.23  ? 1101 MET A CB    1 
ATOM   6956  C  CG    . MET A 1 1101 ? 164.906 140.637 160.676 1.00 31.13  ? 1101 MET A CG    1 
ATOM   6957  S  SD    . MET A 1 1101 ? 165.675 139.423 159.592 1.00 49.06  ? 1101 MET A SD    1 
ATOM   6958  C  CE    . MET A 1 1101 ? 165.599 137.959 160.618 1.00 34.32  ? 1101 MET A CE    1 
ATOM   6959  N  N     . ARG A 1 1102 ? 166.677 144.375 161.811 1.00 27.64  ? 1102 ARG A N     1 
ATOM   6960  C  CA    . ARG A 1 1102 ? 167.745 144.764 162.731 1.00 28.63  ? 1102 ARG A CA    1 
ATOM   6961  C  C     . ARG A 1 1102 ? 167.201 145.485 163.960 1.00 28.10  ? 1102 ARG A C     1 
ATOM   6962  O  O     . ARG A 1 1102 ? 167.694 145.277 165.078 1.00 28.82  ? 1102 ARG A O     1 
ATOM   6963  C  CB    . ARG A 1 1102 ? 168.780 145.631 162.015 1.00 25.54  ? 1102 ARG A CB    1 
ATOM   6964  C  CG    . ARG A 1 1102 ? 169.598 144.895 160.973 1.00 24.66  ? 1102 ARG A CG    1 
ATOM   6965  C  CD    . ARG A 1 1102 ? 170.374 143.756 161.616 1.00 28.94  ? 1102 ARG A CD    1 
ATOM   6966  N  NE    . ARG A 1 1102 ? 171.047 142.901 160.645 1.00 31.11  ? 1102 ARG A NE    1 
ATOM   6967  C  CZ    . ARG A 1 1102 ? 170.440 142.017 159.865 1.00 28.11  ? 1102 ARG A CZ    1 
ATOM   6968  N  NH1   . ARG A 1 1102 ? 169.129 141.850 159.898 1.00 26.92  ? 1102 ARG A NH1   1 
ATOM   6969  N  NH2   . ARG A 1 1102 ? 171.168 141.282 159.029 1.00 24.16  ? 1102 ARG A NH2   1 
ATOM   6970  N  N     . ILE A 1 1103 ? 166.192 146.341 163.778 1.00 29.06  ? 1103 ILE A N     1 
ATOM   6971  C  CA    . ILE A 1 1103 ? 165.588 147.023 164.924 1.00 29.22  ? 1103 ILE A CA    1 
ATOM   6972  C  C     . ILE A 1 1103 ? 164.988 146.009 165.895 1.00 28.89  ? 1103 ILE A C     1 
ATOM   6973  O  O     . ILE A 1 1103 ? 165.204 146.080 167.121 1.00 27.05  ? 1103 ILE A O     1 
ATOM   6974  C  CB    . ILE A 1 1103 ? 164.533 148.037 164.444 1.00 24.23  ? 1103 ILE A CB    1 
ATOM   6975  C  CG1   . ILE A 1 1103 ? 165.194 149.257 163.807 1.00 26.18  ? 1103 ILE A CG1   1 
ATOM   6976  C  CG2   . ILE A 1 1103 ? 163.654 148.476 165.592 1.00 23.90  ? 1103 ILE A CG2   1 
ATOM   6977  C  CD1   . ILE A 1 1103 ? 165.803 150.204 164.809 1.00 29.02  ? 1103 ILE A CD1   1 
ATOM   6978  N  N     . GLU A 1 1104 ? 164.249 145.031 165.363 1.00 30.27  ? 1104 GLU A N     1 
ATOM   6979  C  CA    . GLU A 1 1104 ? 163.643 144.043 166.250 1.00 29.99  ? 1104 GLU A CA    1 
ATOM   6980  C  C     . GLU A 1 1104 ? 164.706 143.201 166.952 1.00 33.07  ? 1104 GLU A C     1 
ATOM   6981  O  O     . GLU A 1 1104 ? 164.550 142.846 168.127 1.00 36.84  ? 1104 GLU A O     1 
ATOM   6982  C  CB    . GLU A 1 1104 ? 162.670 143.155 165.476 1.00 29.77  ? 1104 GLU A CB    1 
ATOM   6983  C  CG    . GLU A 1 1104 ? 161.957 142.147 166.355 1.00 38.12  ? 1104 GLU A CG    1 
ATOM   6984  C  CD    . GLU A 1 1104 ? 160.719 141.562 165.705 1.00 49.06  ? 1104 GLU A CD    1 
ATOM   6985  O  OE1   . GLU A 1 1104 ? 160.324 142.047 164.625 1.00 46.90  ? 1104 GLU A OE1   1 
ATOM   6986  O  OE2   . GLU A 1 1104 ? 160.136 140.620 166.282 1.00 54.31  ? 1104 GLU A OE2   1 
ATOM   6987  N  N     . MET A 1 1105 ? 165.800 142.885 166.255 1.00 32.19  ? 1105 MET A N     1 
ATOM   6988  C  CA    . MET A 1 1105 ? 166.868 142.100 166.869 1.00 29.67  ? 1105 MET A CA    1 
ATOM   6989  C  C     . MET A 1 1105 ? 167.545 142.859 168.007 1.00 29.20  ? 1105 MET A C     1 
ATOM   6990  O  O     . MET A 1 1105 ? 167.885 142.266 169.041 1.00 34.10  ? 1105 MET A O     1 
ATOM   6991  C  CB    . MET A 1 1105 ? 167.887 141.695 165.809 1.00 29.63  ? 1105 MET A CB    1 
ATOM   6992  C  CG    . MET A 1 1105 ? 167.668 140.301 165.257 1.00 32.96  ? 1105 MET A CG    1 
ATOM   6993  S  SD    . MET A 1 1105 ? 168.303 140.119 163.583 1.00 50.12  ? 1105 MET A SD    1 
ATOM   6994  C  CE    . MET A 1 1105 ? 170.059 140.047 163.903 1.00 37.31  ? 1105 MET A CE    1 
ATOM   6995  N  N     . ILE A 1 1106 ? 167.753 144.167 167.835 1.00 30.04  ? 1106 ILE A N     1 
ATOM   6996  C  CA    . ILE A 1 1106 ? 168.324 144.973 168.915 1.00 30.91  ? 1106 ILE A CA    1 
ATOM   6997  C  C     . ILE A 1 1106 ? 167.416 144.937 170.136 1.00 34.72  ? 1106 ILE A C     1 
ATOM   6998  O  O     . ILE A 1 1106 ? 167.874 144.736 171.276 1.00 33.87  ? 1106 ILE A O     1 
ATOM   6999  C  CB    . ILE A 1 1106 ? 168.551 146.421 168.446 1.00 28.57  ? 1106 ILE A CB    1 
ATOM   7000  C  CG1   . ILE A 1 1106 ? 169.710 146.504 167.458 1.00 29.50  ? 1106 ILE A CG1   1 
ATOM   7001  C  CG2   . ILE A 1 1106 ? 168.812 147.328 169.631 1.00 27.77  ? 1106 ILE A CG2   1 
ATOM   7002  C  CD1   . ILE A 1 1106 ? 169.763 147.817 166.723 1.00 26.88  ? 1106 ILE A CD1   1 
ATOM   7003  N  N     . PHE A 1 1107 ? 166.112 145.122 169.912 1.00 34.64  ? 1107 PHE A N     1 
ATOM   7004  C  CA    . PHE A 1 1107 ? 165.161 145.074 171.019 1.00 31.93  ? 1107 PHE A CA    1 
ATOM   7005  C  C     . PHE A 1 1107 ? 165.229 143.734 171.744 1.00 32.17  ? 1107 PHE A C     1 
ATOM   7006  O  O     . PHE A 1 1107 ? 165.273 143.680 172.981 1.00 32.99  ? 1107 PHE A O     1 
ATOM   7007  C  CB    . PHE A 1 1107 ? 163.753 145.337 170.491 1.00 33.56  ? 1107 PHE A CB    1 
ATOM   7008  C  CG    . PHE A 1 1107 ? 162.685 145.258 171.538 1.00 37.17  ? 1107 PHE A CG    1 
ATOM   7009  C  CD1   . PHE A 1 1107 ? 162.513 146.285 172.448 1.00 41.16  ? 1107 PHE A CD1   1 
ATOM   7010  C  CD2   . PHE A 1 1107 ? 161.845 144.162 171.606 1.00 39.00  ? 1107 PHE A CD2   1 
ATOM   7011  C  CE1   . PHE A 1 1107 ? 161.531 146.218 173.408 1.00 39.01  ? 1107 PHE A CE1   1 
ATOM   7012  C  CE2   . PHE A 1 1107 ? 160.861 144.089 172.565 1.00 40.48  ? 1107 PHE A CE2   1 
ATOM   7013  C  CZ    . PHE A 1 1107 ? 160.703 145.120 173.466 1.00 40.12  ? 1107 PHE A CZ    1 
ATOM   7014  N  N     . VAL A 1 1108 ? 165.260 142.642 170.979 1.00 36.49  ? 1108 VAL A N     1 
ATOM   7015  C  CA    . VAL A 1 1108 ? 165.262 141.304 171.565 1.00 33.22  ? 1108 VAL A CA    1 
ATOM   7016  C  C     . VAL A 1 1108 ? 166.513 141.078 172.407 1.00 35.06  ? 1108 VAL A C     1 
ATOM   7017  O  O     . VAL A 1 1108 ? 166.448 140.495 173.498 1.00 37.88  ? 1108 VAL A O     1 
ATOM   7018  C  CB    . VAL A 1 1108 ? 165.123 140.245 170.456 1.00 33.54  ? 1108 VAL A CB    1 
ATOM   7019  C  CG1   . VAL A 1 1108 ? 165.546 138.878 170.958 1.00 38.88  ? 1108 VAL A CG1   1 
ATOM   7020  C  CG2   . VAL A 1 1108 ? 163.695 140.211 169.935 1.00 38.07  ? 1108 VAL A CG2   1 
ATOM   7021  N  N     . ILE A 1 1109 ? 167.674 141.521 171.916 1.00 35.03  ? 1109 ILE A N     1 
ATOM   7022  C  CA    . ILE A 1 1109 ? 168.900 141.272 172.670 1.00 34.70  ? 1109 ILE A CA    1 
ATOM   7023  C  C     . ILE A 1 1109 ? 168.920 142.079 173.970 1.00 37.46  ? 1109 ILE A C     1 
ATOM   7024  O  O     . ILE A 1 1109 ? 169.319 141.557 175.030 1.00 38.64  ? 1109 ILE A O     1 
ATOM   7025  C  CB    . ILE A 1 1109 ? 170.136 141.541 171.784 1.00 35.45  ? 1109 ILE A CB    1 
ATOM   7026  C  CG1   . ILE A 1 1109 ? 171.260 140.564 172.124 1.00 39.16  ? 1109 ILE A CG1   1 
ATOM   7027  C  CG2   . ILE A 1 1109 ? 170.634 142.980 171.894 1.00 37.77  ? 1109 ILE A CG2   1 
ATOM   7028  C  CD1   . ILE A 1 1109 ? 172.224 140.346 170.987 1.00 43.61  ? 1109 ILE A CD1   1 
ATOM   7029  N  N     . PHE A 1 1110 ? 168.448 143.332 173.936 1.00 36.93  ? 1110 PHE A N     1 
ATOM   7030  C  CA    . PHE A 1 1110 ? 168.381 144.100 175.177 1.00 34.48  ? 1110 PHE A CA    1 
ATOM   7031  C  C     . PHE A 1 1110 ? 167.432 143.443 176.170 1.00 39.36  ? 1110 PHE A C     1 
ATOM   7032  O  O     . PHE A 1 1110 ? 167.724 143.376 177.374 1.00 38.74  ? 1110 PHE A O     1 
ATOM   7033  C  CB    . PHE A 1 1110 ? 167.944 145.539 174.897 1.00 36.99  ? 1110 PHE A CB    1 
ATOM   7034  C  CG    . PHE A 1 1110 ? 169.084 146.496 174.691 1.00 41.55  ? 1110 PHE A CG    1 
ATOM   7035  C  CD1   . PHE A 1 1110 ? 169.966 146.775 175.721 1.00 38.82  ? 1110 PHE A CD1   1 
ATOM   7036  C  CD2   . PHE A 1 1110 ? 169.264 147.129 173.473 1.00 40.89  ? 1110 PHE A CD2   1 
ATOM   7037  C  CE1   . PHE A 1 1110 ? 171.009 147.656 175.537 1.00 36.88  ? 1110 PHE A CE1   1 
ATOM   7038  C  CE2   . PHE A 1 1110 ? 170.306 148.012 173.282 1.00 37.88  ? 1110 PHE A CE2   1 
ATOM   7039  C  CZ    . PHE A 1 1110 ? 171.180 148.276 174.316 1.00 36.72  ? 1110 PHE A CZ    1 
ATOM   7040  N  N     . PHE A 1 1111 ? 166.293 142.945 175.678 1.00 42.08  ? 1111 PHE A N     1 
ATOM   7041  C  CA    . PHE A 1 1111 ? 165.324 142.309 176.561 1.00 36.71  ? 1111 PHE A CA    1 
ATOM   7042  C  C     . PHE A 1 1111 ? 165.895 141.048 177.199 1.00 39.93  ? 1111 PHE A C     1 
ATOM   7043  O  O     . PHE A 1 1111 ? 165.682 140.805 178.390 1.00 45.27  ? 1111 PHE A O     1 
ATOM   7044  C  CB    . PHE A 1 1111 ? 164.043 141.992 175.793 1.00 38.31  ? 1111 PHE A CB    1 
ATOM   7045  C  CG    . PHE A 1 1111 ? 162.791 142.214 176.592 1.00 47.32  ? 1111 PHE A CG    1 
ATOM   7046  C  CD1   . PHE A 1 1111 ? 162.615 141.599 177.820 1.00 48.19  ? 1111 PHE A CD1   1 
ATOM   7047  C  CD2   . PHE A 1 1111 ? 161.794 143.047 176.116 1.00 46.38  ? 1111 PHE A CD2   1 
ATOM   7048  C  CE1   . PHE A 1 1111 ? 161.468 141.808 178.556 1.00 43.11  ? 1111 PHE A CE1   1 
ATOM   7049  C  CE2   . PHE A 1 1111 ? 160.645 143.259 176.846 1.00 43.64  ? 1111 PHE A CE2   1 
ATOM   7050  C  CZ    . PHE A 1 1111 ? 160.482 142.640 178.069 1.00 45.41  ? 1111 PHE A CZ    1 
ATOM   7051  N  N     . ILE A 1 1112 ? 166.619 140.233 176.427 1.00 41.07  ? 1112 ILE A N     1 
ATOM   7052  C  CA    . ILE A 1 1112 ? 167.226 139.024 176.987 1.00 41.80  ? 1112 ILE A CA    1 
ATOM   7053  C  C     . ILE A 1 1112 ? 168.207 139.383 178.097 1.00 39.22  ? 1112 ILE A C     1 
ATOM   7054  O  O     . ILE A 1 1112 ? 168.196 138.784 179.187 1.00 40.35  ? 1112 ILE A O     1 
ATOM   7055  C  CB    . ILE A 1 1112 ? 167.909 138.196 175.882 1.00 43.52  ? 1112 ILE A CB    1 
ATOM   7056  C  CG1   . ILE A 1 1112 ? 166.868 137.565 174.956 1.00 46.73  ? 1112 ILE A CG1   1 
ATOM   7057  C  CG2   . ILE A 1 1112 ? 168.805 137.132 176.485 1.00 39.14  ? 1112 ILE A CG2   1 
ATOM   7058  C  CD1   . ILE A 1 1112 ? 167.451 136.983 173.686 1.00 43.62  ? 1112 ILE A CD1   1 
ATOM   7059  N  N     . ALA A 1 1113 ? 169.074 140.368 177.837 1.00 39.19  ? 1113 ALA A N     1 
ATOM   7060  C  CA    . ALA A 1 1113 ? 170.066 140.744 178.842 1.00 40.31  ? 1113 ALA A CA    1 
ATOM   7061  C  C     . ALA A 1 1113 ? 169.398 141.218 180.128 1.00 42.78  ? 1113 ALA A C     1 
ATOM   7062  O  O     . ALA A 1 1113 ? 169.749 140.768 181.230 1.00 41.41  ? 1113 ALA A O     1 
ATOM   7063  C  CB    . ALA A 1 1113 ? 170.994 141.824 178.287 1.00 38.20  ? 1113 ALA A CB    1 
ATOM   7064  N  N     . VAL A 1 1114 ? 168.412 142.113 180.008 1.00 46.65  ? 1114 VAL A N     1 
ATOM   7065  C  CA    . VAL A 1 1114 ? 167.790 142.648 181.217 1.00 46.14  ? 1114 VAL A CA    1 
ATOM   7066  C  C     . VAL A 1 1114 ? 166.967 141.580 181.927 1.00 43.10  ? 1114 VAL A C     1 
ATOM   7067  O  O     . VAL A 1 1114 ? 166.885 141.578 183.160 1.00 44.42  ? 1114 VAL A O     1 
ATOM   7068  C  CB    . VAL A 1 1114 ? 166.945 143.899 180.907 1.00 45.69  ? 1114 VAL A CB    1 
ATOM   7069  C  CG1   . VAL A 1 1114 ? 167.811 144.987 180.290 1.00 43.43  ? 1114 VAL A CG1   1 
ATOM   7070  C  CG2   . VAL A 1 1114 ? 165.774 143.553 180.006 1.00 44.99  ? 1114 VAL A CG2   1 
ATOM   7071  N  N     . THR A 1 1115 ? 166.362 140.649 181.183 1.00 43.98  ? 1115 THR A N     1 
ATOM   7072  C  CA    . THR A 1 1115 ? 165.589 139.582 181.812 1.00 45.07  ? 1115 THR A CA    1 
ATOM   7073  C  C     . THR A 1 1115 ? 166.479 138.703 182.678 1.00 46.01  ? 1115 THR A C     1 
ATOM   7074  O  O     . THR A 1 1115 ? 166.154 138.417 183.839 1.00 48.92  ? 1115 THR A O     1 
ATOM   7075  C  CB    . THR A 1 1115 ? 164.884 138.741 180.745 1.00 42.73  ? 1115 THR A CB    1 
ATOM   7076  O  OG1   . THR A 1 1115 ? 163.812 139.493 180.164 1.00 47.55  ? 1115 THR A OG1   1 
ATOM   7077  C  CG2   . THR A 1 1115 ? 164.335 137.454 181.344 1.00 38.27  ? 1115 THR A CG2   1 
ATOM   7078  N  N     . PHE A 1 1116 ? 167.616 138.265 182.131 1.00 45.91  ? 1116 PHE A N     1 
ATOM   7079  C  CA    . PHE A 1 1116 ? 168.503 137.421 182.930 1.00 44.70  ? 1116 PHE A CA    1 
ATOM   7080  C  C     . PHE A 1 1116 ? 169.096 138.186 184.108 1.00 45.37  ? 1116 PHE A C     1 
ATOM   7081  O  O     . PHE A 1 1116 ? 169.223 137.630 185.207 1.00 46.75  ? 1116 PHE A O     1 
ATOM   7082  C  CB    . PHE A 1 1116 ? 169.595 136.807 182.059 1.00 49.40  ? 1116 PHE A CB    1 
ATOM   7083  C  CG    . PHE A 1 1116 ? 169.230 135.460 181.503 1.00 58.25  ? 1116 PHE A CG    1 
ATOM   7084  C  CD1   . PHE A 1 1116 ? 168.834 134.438 182.351 1.00 60.54  ? 1116 PHE A CD1   1 
ATOM   7085  C  CD2   . PHE A 1 1116 ? 169.272 135.215 180.142 1.00 59.33  ? 1116 PHE A CD2   1 
ATOM   7086  C  CE1   . PHE A 1 1116 ? 168.494 133.195 181.854 1.00 63.91  ? 1116 PHE A CE1   1 
ATOM   7087  C  CE2   . PHE A 1 1116 ? 168.933 133.974 179.639 1.00 60.26  ? 1116 PHE A CE2   1 
ATOM   7088  C  CZ    . PHE A 1 1116 ? 168.544 132.964 180.495 1.00 63.85  ? 1116 PHE A CZ    1 
ATOM   7089  N  N     . ILE A 1 1117 ? 169.451 139.461 183.913 1.00 46.22  ? 1117 ILE A N     1 
ATOM   7090  C  CA    . ILE A 1 1117 ? 169.970 140.252 185.029 1.00 45.31  ? 1117 ILE A CA    1 
ATOM   7091  C  C     . ILE A 1 1117 ? 168.928 140.350 186.138 1.00 48.94  ? 1117 ILE A C     1 
ATOM   7092  O  O     . ILE A 1 1117 ? 169.242 140.202 187.326 1.00 51.75  ? 1117 ILE A O     1 
ATOM   7093  C  CB    . ILE A 1 1117 ? 170.412 141.645 184.548 1.00 47.49  ? 1117 ILE A CB    1 
ATOM   7094  C  CG1   . ILE A 1 1117 ? 171.683 141.552 183.708 1.00 49.40  ? 1117 ILE A CG1   1 
ATOM   7095  C  CG2   . ILE A 1 1117 ? 170.647 142.567 185.729 1.00 46.98  ? 1117 ILE A CG2   1 
ATOM   7096  C  CD1   . ILE A 1 1117 ? 171.955 142.793 182.884 1.00 45.64  ? 1117 ILE A CD1   1 
ATOM   7097  N  N     . SER A 1 1118 ? 167.670 140.597 185.763 1.00 49.48  ? 1118 SER A N     1 
ATOM   7098  C  CA    . SER A 1 1118 ? 166.598 140.715 186.746 1.00 44.09  ? 1118 SER A CA    1 
ATOM   7099  C  C     . SER A 1 1118 ? 166.398 139.413 187.509 1.00 46.06  ? 1118 SER A C     1 
ATOM   7100  O  O     . SER A 1 1118 ? 166.243 139.417 188.734 1.00 49.42  ? 1118 SER A O     1 
ATOM   7101  C  CB    . SER A 1 1118 ? 165.303 141.133 186.053 1.00 42.72  ? 1118 SER A CB    1 
ATOM   7102  O  OG    . SER A 1 1118 ? 165.434 142.420 185.482 1.00 48.83  ? 1118 SER A OG    1 
ATOM   7103  N  N     . ILE A 1 1119 ? 166.393 138.283 186.799 1.00 48.32  ? 1119 ILE A N     1 
ATOM   7104  C  CA    . ILE A 1 1119 ? 166.142 137.013 187.476 1.00 49.62  ? 1119 ILE A CA    1 
ATOM   7105  C  C     . ILE A 1 1119 ? 167.294 136.659 188.409 1.00 52.43  ? 1119 ILE A C     1 
ATOM   7106  O  O     . ILE A 1 1119 ? 167.078 136.153 189.516 1.00 55.42  ? 1119 ILE A O     1 
ATOM   7107  C  CB    . ILE A 1 1119 ? 165.869 135.893 186.457 1.00 50.35  ? 1119 ILE A CB    1 
ATOM   7108  C  CG1   . ILE A 1 1119 ? 164.523 136.115 185.770 1.00 46.42  ? 1119 ILE A CG1   1 
ATOM   7109  C  CG2   . ILE A 1 1119 ? 165.883 134.535 187.130 1.00 51.36  ? 1119 ILE A CG2   1 
ATOM   7110  C  CD1   . ILE A 1 1119 ? 164.380 135.372 184.471 1.00 49.61  ? 1119 ILE A CD1   1 
ATOM   7111  N  N     . LEU A 1 1120 ? 168.532 136.928 187.994 1.00 52.63  ? 1120 LEU A N     1 
ATOM   7112  C  CA    . LEU A 1 1120 ? 169.661 136.551 188.838 1.00 53.24  ? 1120 LEU A CA    1 
ATOM   7113  C  C     . LEU A 1 1120 ? 169.853 137.492 190.019 1.00 58.37  ? 1120 LEU A C     1 
ATOM   7114  O  O     . LEU A 1 1120 ? 170.296 137.051 191.085 1.00 62.04  ? 1120 LEU A O     1 
ATOM   7115  C  CB    . LEU A 1 1120 ? 170.945 136.489 188.010 1.00 53.19  ? 1120 LEU A CB    1 
ATOM   7116  C  CG    . LEU A 1 1120 ? 171.424 135.103 187.578 1.00 54.12  ? 1120 LEU A CG    1 
ATOM   7117  C  CD1   . LEU A 1 1120 ? 170.270 134.241 187.089 1.00 54.51  ? 1120 LEU A CD1   1 
ATOM   7118  C  CD2   . LEU A 1 1120 ? 172.489 135.231 186.506 1.00 49.33  ? 1120 LEU A CD2   1 
ATOM   7119  N  N     . THR A 1 1121 ? 169.528 138.777 189.860 1.00 59.80  ? 1121 THR A N     1 
ATOM   7120  C  CA    . THR A 1 1121 ? 169.843 139.753 190.899 1.00 59.64  ? 1121 THR A CA    1 
ATOM   7121  C  C     . THR A 1 1121 ? 168.982 139.572 192.145 1.00 62.67  ? 1121 THR A C     1 
ATOM   7122  O  O     . THR A 1 1121 ? 169.470 139.775 193.263 1.00 67.54  ? 1121 THR A O     1 
ATOM   7123  C  CB    . THR A 1 1121 ? 169.682 141.171 190.345 1.00 58.12  ? 1121 THR A CB    1 
ATOM   7124  O  OG1   . THR A 1 1121 ? 170.613 141.373 189.275 1.00 58.21  ? 1121 THR A OG1   1 
ATOM   7125  C  CG2   . THR A 1 1121 ? 169.945 142.206 191.420 1.00 56.48  ? 1121 THR A CG2   1 
ATOM   7126  N  N     . THR A 1 1122 ? 167.720 139.180 191.984 1.00 61.87  ? 1122 THR A N     1 
ATOM   7127  C  CA    . THR A 1 1122 ? 166.809 139.112 193.121 1.00 63.52  ? 1122 THR A CA    1 
ATOM   7128  C  C     . THR A 1 1122 ? 167.274 138.061 194.123 1.00 69.67  ? 1122 THR A C     1 
ATOM   7129  O  O     . THR A 1 1122 ? 167.716 136.972 193.745 1.00 73.50  ? 1122 THR A O     1 
ATOM   7130  C  CB    . THR A 1 1122 ? 165.381 138.820 192.654 1.00 64.47  ? 1122 THR A CB    1 
ATOM   7131  O  OG1   . THR A 1 1122 ? 164.486 138.875 193.772 1.00 68.12  ? 1122 THR A OG1   1 
ATOM   7132  C  CG2   . THR A 1 1122 ? 165.280 137.457 191.991 1.00 61.23  ? 1122 THR A CG2   1 
ATOM   7133  N  N     . GLY A 1 1123 ? 167.208 138.409 195.405 1.00 72.84  ? 1123 GLY A N     1 
ATOM   7134  C  CA    . GLY A 1 1123 ? 167.669 137.529 196.461 1.00 77.03  ? 1123 GLY A CA    1 
ATOM   7135  C  C     . GLY A 1 1123 ? 166.557 137.009 197.346 1.00 79.31  ? 1123 GLY A C     1 
ATOM   7136  O  O     . GLY A 1 1123 ? 165.584 136.428 196.856 1.00 77.54  ? 1123 GLY A O     1 
ATOM   7137  N  N     . GLU A 1 1124 ? 166.695 137.207 198.655 1.00 82.02  ? 1124 GLU A N     1 
ATOM   7138  C  CA    . GLU A 1 1124 ? 165.703 136.768 199.627 1.00 85.24  ? 1124 GLU A CA    1 
ATOM   7139  C  C     . GLU A 1 1124 ? 164.630 137.814 199.897 1.00 79.75  ? 1124 GLU A C     1 
ATOM   7140  O  O     . GLU A 1 1124 ? 163.730 137.562 200.704 1.00 76.83  ? 1124 GLU A O     1 
ATOM   7141  C  CB    . GLU A 1 1124 ? 166.385 136.390 200.945 1.00 90.86  ? 1124 GLU A CB    1 
ATOM   7142  C  CG    . GLU A 1 1124 ? 167.512 135.381 200.801 1.00 96.78  ? 1124 GLU A CG    1 
ATOM   7143  C  CD    . GLU A 1 1124 ? 168.880 136.032 200.878 1.00 96.72  ? 1124 GLU A CD    1 
ATOM   7144  O  OE1   . GLU A 1 1124 ? 168.968 137.257 200.651 1.00 92.78  ? 1124 GLU A OE1   1 
ATOM   7145  O  OE2   . GLU A 1 1124 ? 169.864 135.320 201.168 1.00 95.85  ? 1124 GLU A OE2   1 
ATOM   7146  N  N     . GLY A 1 1125 ? 164.709 138.980 199.263 1.00 77.11  ? 1125 GLY A N     1 
ATOM   7147  C  CA    . GLY A 1 1125 ? 163.736 140.027 199.499 1.00 75.31  ? 1125 GLY A CA    1 
ATOM   7148  C  C     . GLY A 1 1125 ? 163.191 140.642 198.228 1.00 69.74  ? 1125 GLY A C     1 
ATOM   7149  O  O     . GLY A 1 1125 ? 163.121 139.978 197.189 1.00 69.50  ? 1125 GLY A O     1 
ATOM   7150  N  N     . GLU A 1 1126 ? 162.778 141.905 198.308 1.00 64.03  ? 1126 GLU A N     1 
ATOM   7151  C  CA    . GLU A 1 1126 ? 162.321 142.634 197.133 1.00 62.66  ? 1126 GLU A CA    1 
ATOM   7152  C  C     . GLU A 1 1126 ? 163.425 142.723 196.088 1.00 59.93  ? 1126 GLU A C     1 
ATOM   7153  O  O     . GLU A 1 1126 ? 164.564 143.077 196.400 1.00 63.51  ? 1126 GLU A O     1 
ATOM   7154  C  CB    . GLU A 1 1126 ? 161.870 144.039 197.535 1.00 65.37  ? 1126 GLU A CB    1 
ATOM   7155  C  CG    . GLU A 1 1126 ? 160.396 144.164 197.867 1.00 70.67  ? 1126 GLU A CG    1 
ATOM   7156  C  CD    . GLU A 1 1126 ? 159.557 144.541 196.660 1.00 72.08  ? 1126 GLU A CD    1 
ATOM   7157  O  OE1   . GLU A 1 1126 ? 159.064 145.687 196.615 1.00 71.26  ? 1126 GLU A OE1   1 
ATOM   7158  O  OE2   . GLU A 1 1126 ? 159.393 143.694 195.758 1.00 67.51  ? 1126 GLU A OE2   1 
ATOM   7159  N  N     . GLY A 1 1127 ? 163.082 142.395 194.845 1.00 53.46  ? 1127 GLY A N     1 
ATOM   7160  C  CA    . GLY A 1 1127 ? 163.993 142.607 193.738 1.00 51.06  ? 1127 GLY A CA    1 
ATOM   7161  C  C     . GLY A 1 1127 ? 163.735 143.938 193.067 1.00 47.33  ? 1127 GLY A C     1 
ATOM   7162  O  O     . GLY A 1 1127 ? 162.828 144.052 192.240 1.00 49.53  ? 1127 GLY A O     1 
ATOM   7163  N  N     . ARG A 1 1128 ? 164.531 144.953 193.409 1.00 48.46  ? 1128 ARG A N     1 
ATOM   7164  C  CA    . ARG A 1 1128 ? 164.250 146.315 192.966 1.00 48.10  ? 1128 ARG A CA    1 
ATOM   7165  C  C     . ARG A 1 1128 ? 164.820 146.625 191.586 1.00 48.22  ? 1128 ARG A C     1 
ATOM   7166  O  O     . ARG A 1 1128 ? 164.327 147.536 190.912 1.00 48.80  ? 1128 ARG A O     1 
ATOM   7167  C  CB    . ARG A 1 1128 ? 164.773 147.314 193.997 1.00 51.20  ? 1128 ARG A CB    1 
ATOM   7168  C  CG    . ARG A 1 1128 ? 164.082 147.199 195.344 1.00 54.87  ? 1128 ARG A CG    1 
ATOM   7169  C  CD    . ARG A 1 1128 ? 164.597 148.228 196.334 1.00 63.55  ? 1128 ARG A CD    1 
ATOM   7170  N  NE    . ARG A 1 1128 ? 164.011 148.049 197.657 1.00 76.66  ? 1128 ARG A NE    1 
ATOM   7171  C  CZ    . ARG A 1 1128 ? 164.413 147.149 198.544 1.00 77.10  ? 1128 ARG A CZ    1 
ATOM   7172  N  NH1   . ARG A 1 1128 ? 165.433 146.342 198.298 1.00 69.72  ? 1128 ARG A NH1   1 
ATOM   7173  N  NH2   . ARG A 1 1128 ? 163.775 147.055 199.707 1.00 67.28  ? 1128 ARG A NH2   1 
ATOM   7174  N  N     . VAL A 1 1129 ? 165.859 145.908 191.157 1.00 45.97  ? 1129 VAL A N     1 
ATOM   7175  C  CA    . VAL A 1 1129 ? 166.452 146.165 189.847 1.00 42.46  ? 1129 VAL A CA    1 
ATOM   7176  C  C     . VAL A 1 1129 ? 165.510 145.723 188.730 1.00 44.94  ? 1129 VAL A C     1 
ATOM   7177  O  O     . VAL A 1 1129 ? 165.348 146.421 187.713 1.00 50.15  ? 1129 VAL A O     1 
ATOM   7178  C  CB    . VAL A 1 1129 ? 167.819 145.466 189.749 1.00 44.86  ? 1129 VAL A CB    1 
ATOM   7179  C  CG1   . VAL A 1 1129 ? 168.358 145.533 188.333 1.00 45.27  ? 1129 VAL A CG1   1 
ATOM   7180  C  CG2   . VAL A 1 1129 ? 168.796 146.079 190.734 1.00 46.56  ? 1129 VAL A CG2   1 
ATOM   7181  N  N     . GLY A 1 1130 ? 164.874 144.562 188.902 1.00 39.78  ? 1130 GLY A N     1 
ATOM   7182  C  CA    . GLY A 1 1130 ? 164.040 144.015 187.849 1.00 38.36  ? 1130 GLY A CA    1 
ATOM   7183  C  C     . GLY A 1 1130 ? 162.827 144.863 187.545 1.00 41.79  ? 1130 GLY A C     1 
ATOM   7184  O  O     . GLY A 1 1130 ? 162.397 144.938 186.391 1.00 47.22  ? 1130 GLY A O     1 
ATOM   7185  N  N     . ILE A 1 1131 ? 162.279 145.533 188.557 1.00 38.71  ? 1131 ILE A N     1 
ATOM   7186  C  CA    . ILE A 1 1131 ? 161.127 146.400 188.338 1.00 41.99  ? 1131 ILE A CA    1 
ATOM   7187  C  C     . ILE A 1 1131 ? 161.481 147.516 187.366 1.00 42.17  ? 1131 ILE A C     1 
ATOM   7188  O  O     . ILE A 1 1131 ? 160.790 147.735 186.358 1.00 42.59  ? 1131 ILE A O     1 
ATOM   7189  C  CB    . ILE A 1 1131 ? 160.639 146.960 189.684 1.00 42.37  ? 1131 ILE A CB    1 
ATOM   7190  C  CG1   . ILE A 1 1131 ? 160.725 145.885 190.768 1.00 39.20  ? 1131 ILE A CG1   1 
ATOM   7191  C  CG2   . ILE A 1 1131 ? 159.230 147.497 189.559 1.00 44.27  ? 1131 ILE A CG2   1 
ATOM   7192  C  CD1   . ILE A 1 1131 ? 160.045 146.263 192.059 1.00 37.68  ? 1131 ILE A CD1   1 
ATOM   7193  N  N     . ILE A 1 1132 ? 162.593 148.202 187.630 1.00 39.63  ? 1132 ILE A N     1 
ATOM   7194  C  CA    . ILE A 1 1132 ? 163.022 149.305 186.783 1.00 37.56  ? 1132 ILE A CA    1 
ATOM   7195  C  C     . ILE A 1 1132 ? 163.320 148.804 185.379 1.00 39.81  ? 1132 ILE A C     1 
ATOM   7196  O  O     . ILE A 1 1132 ? 162.882 149.396 184.381 1.00 42.09  ? 1132 ILE A O     1 
ATOM   7197  C  CB    . ILE A 1 1132 ? 164.251 149.993 187.404 1.00 41.02  ? 1132 ILE A CB    1 
ATOM   7198  C  CG1   . ILE A 1 1132 ? 163.841 150.852 188.599 1.00 45.23  ? 1132 ILE A CG1   1 
ATOM   7199  C  CG2   . ILE A 1 1132 ? 164.983 150.824 186.365 1.00 48.48  ? 1132 ILE A CG2   1 
ATOM   7200  C  CD1   . ILE A 1 1132 ? 164.762 150.706 189.789 1.00 46.65  ? 1132 ILE A CD1   1 
ATOM   7201  N  N     . LEU A 1 1133 ? 164.053 147.691 185.280 1.00 40.53  ? 1133 LEU A N     1 
ATOM   7202  C  CA    . LEU A 1 1133 ? 164.480 147.214 183.969 1.00 37.71  ? 1133 LEU A CA    1 
ATOM   7203  C  C     . LEU A 1 1133 ? 163.284 146.794 183.118 1.00 36.69  ? 1133 LEU A C     1 
ATOM   7204  O  O     . LEU A 1 1133 ? 163.193 147.143 181.930 1.00 40.69  ? 1133 LEU A O     1 
ATOM   7205  C  CB    . LEU A 1 1133 ? 165.471 146.065 184.140 1.00 39.85  ? 1133 LEU A CB    1 
ATOM   7206  C  CG    . LEU A 1 1133 ? 166.833 146.516 184.682 1.00 39.07  ? 1133 LEU A CG    1 
ATOM   7207  C  CD1   . LEU A 1 1133 ? 167.794 145.344 184.800 1.00 40.17  ? 1133 LEU A CD1   1 
ATOM   7208  C  CD2   . LEU A 1 1133 ? 167.432 147.643 183.856 1.00 40.99  ? 1133 LEU A CD2   1 
ATOM   7209  N  N     . THR A 1 1134 ? 162.334 146.073 183.720 1.00 32.98  ? 1134 THR A N     1 
ATOM   7210  C  CA    . THR A 1 1134 ? 161.179 145.605 182.966 1.00 34.66  ? 1134 THR A CA    1 
ATOM   7211  C  C     . THR A 1 1134 ? 160.257 146.752 182.572 1.00 33.15  ? 1134 THR A C     1 
ATOM   7212  O  O     . THR A 1 1134 ? 159.686 146.732 181.475 1.00 33.17  ? 1134 THR A O     1 
ATOM   7213  C  CB    . THR A 1 1134 ? 160.420 144.555 183.775 1.00 37.80  ? 1134 THR A CB    1 
ATOM   7214  O  OG1   . THR A 1 1134 ? 161.330 143.535 184.196 1.00 36.14  ? 1134 THR A OG1   1 
ATOM   7215  C  CG2   . THR A 1 1134 ? 159.351 143.913 182.923 1.00 38.88  ? 1134 THR A CG2   1 
ATOM   7216  N  N     . LEU A 1 1135 ? 160.113 147.771 183.426 1.00 34.31  ? 1135 LEU A N     1 
ATOM   7217  C  CA    . LEU A 1 1135 ? 159.288 148.914 183.042 1.00 33.20  ? 1135 LEU A CA    1 
ATOM   7218  C  C     . LEU A 1 1135 ? 159.926 149.689 181.889 1.00 35.02  ? 1135 LEU A C     1 
ATOM   7219  O  O     . LEU A 1 1135 ? 159.231 150.132 180.956 1.00 37.96  ? 1135 LEU A O     1 
ATOM   7220  C  CB    . LEU A 1 1135 ? 159.065 149.809 184.260 1.00 31.61  ? 1135 LEU A CB    1 
ATOM   7221  C  CG    . LEU A 1 1135 ? 158.029 150.926 184.173 1.00 36.57  ? 1135 LEU A CG    1 
ATOM   7222  C  CD1   . LEU A 1 1135 ? 156.670 150.347 183.849 1.00 37.72  ? 1135 LEU A CD1   1 
ATOM   7223  C  CD2   . LEU A 1 1135 ? 157.974 151.689 185.483 1.00 36.41  ? 1135 LEU A CD2   1 
ATOM   7224  N  N     . ALA A 1 1136 ? 161.254 149.832 181.917 1.00 34.04  ? 1136 ALA A N     1 
ATOM   7225  C  CA    . ALA A 1 1136 ? 161.948 150.493 180.819 1.00 31.74  ? 1136 ALA A CA    1 
ATOM   7226  C  C     . ALA A 1 1136 ? 161.732 149.745 179.509 1.00 34.19  ? 1136 ALA A C     1 
ATOM   7227  O  O     . ALA A 1 1136 ? 161.487 150.356 178.459 1.00 37.46  ? 1136 ALA A O     1 
ATOM   7228  C  CB    . ALA A 1 1136 ? 163.437 150.606 181.138 1.00 33.87  ? 1136 ALA A CB    1 
ATOM   7229  N  N     . MET A 1 1137 ? 161.820 148.414 179.549 1.00 34.57  ? 1137 MET A N     1 
ATOM   7230  C  CA    . MET A 1 1137 ? 161.575 147.649 178.329 1.00 36.07  ? 1137 MET A CA    1 
ATOM   7231  C  C     . MET A 1 1137 ? 160.130 147.780 177.856 1.00 35.79  ? 1137 MET A C     1 
ATOM   7232  O  O     . MET A 1 1137 ? 159.873 147.831 176.642 1.00 38.24  ? 1137 MET A O     1 
ATOM   7233  C  CB    . MET A 1 1137 ? 161.946 146.184 178.541 1.00 37.23  ? 1137 MET A CB    1 
ATOM   7234  C  CG    . MET A 1 1137 ? 163.388 145.984 178.962 1.00 40.69  ? 1137 MET A CG    1 
ATOM   7235  S  SD    . MET A 1 1137 ? 164.579 146.767 177.853 1.00 56.76  ? 1137 MET A SD    1 
ATOM   7236  C  CE    . MET A 1 1137 ? 164.114 146.074 176.270 1.00 38.33  ? 1137 MET A CE    1 
ATOM   7237  N  N     . ASN A 1 1138 ? 159.178 147.847 178.790 1.00 33.64  ? 1138 ASN A N     1 
ATOM   7238  C  CA    . ASN A 1 1138 ? 157.788 148.046 178.392 1.00 35.70  ? 1138 ASN A CA    1 
ATOM   7239  C  C     . ASN A 1 1138 ? 157.584 149.379 177.683 1.00 36.80  ? 1138 ASN A C     1 
ATOM   7240  O  O     . ASN A 1 1138 ? 156.708 149.485 176.819 1.00 37.65  ? 1138 ASN A O     1 
ATOM   7241  C  CB    . ASN A 1 1138 ? 156.866 147.942 179.606 1.00 37.12  ? 1138 ASN A CB    1 
ATOM   7242  C  CG    . ASN A 1 1138 ? 156.646 146.512 180.047 1.00 41.61  ? 1138 ASN A CG    1 
ATOM   7243  O  OD1   . ASN A 1 1138 ? 156.518 145.609 179.222 1.00 37.92  ? 1138 ASN A OD1   1 
ATOM   7244  N  ND2   . ASN A 1 1138 ? 156.587 146.299 181.353 1.00 44.03  ? 1138 ASN A ND2   1 
ATOM   7245  N  N     . ILE A 1 1139 ? 158.366 150.403 178.029 1.00 34.99  ? 1139 ILE A N     1 
ATOM   7246  C  CA    . ILE A 1 1139 ? 158.271 151.662 177.280 1.00 34.71  ? 1139 ILE A CA    1 
ATOM   7247  C  C     . ILE A 1 1139 ? 158.969 151.556 175.917 1.00 37.90  ? 1139 ILE A C     1 
ATOM   7248  O  O     . ILE A 1 1139 ? 158.487 152.086 174.897 1.00 39.67  ? 1139 ILE A O     1 
ATOM   7249  C  CB    . ILE A 1 1139 ? 158.834 152.820 178.120 1.00 31.39  ? 1139 ILE A CB    1 
ATOM   7250  C  CG1   . ILE A 1 1139 ? 158.037 152.971 179.413 1.00 34.57  ? 1139 ILE A CG1   1 
ATOM   7251  C  CG2   . ILE A 1 1139 ? 158.789 154.111 177.333 1.00 32.70  ? 1139 ILE A CG2   1 
ATOM   7252  C  CD1   . ILE A 1 1139 ? 158.708 153.847 180.441 1.00 35.89  ? 1139 ILE A CD1   1 
ATOM   7253  N  N     . MET A 1 1140 ? 160.118 150.879 175.872 1.00 35.87  ? 1140 MET A N     1 
ATOM   7254  C  CA    . MET A 1 1140 ? 160.823 150.727 174.604 1.00 33.96  ? 1140 MET A CA    1 
ATOM   7255  C  C     . MET A 1 1140 ? 159.997 149.961 173.579 1.00 35.74  ? 1140 MET A C     1 
ATOM   7256  O  O     . MET A 1 1140 ? 160.189 150.149 172.366 1.00 40.92  ? 1140 MET A O     1 
ATOM   7257  C  CB    . MET A 1 1140 ? 162.164 150.030 174.831 1.00 35.75  ? 1140 MET A CB    1 
ATOM   7258  C  CG    . MET A 1 1140 ? 163.214 150.812 175.638 1.00 36.16  ? 1140 MET A CG    1 
ATOM   7259  S  SD    . MET A 1 1140 ? 163.589 152.512 175.137 1.00 56.99  ? 1140 MET A SD    1 
ATOM   7260  C  CE    . MET A 1 1140 ? 162.311 153.475 175.942 1.00 44.69  ? 1140 MET A CE    1 
ATOM   7261  N  N     . SER A 1 1141 ? 159.068 149.122 174.043 1.00 36.06  ? 1141 SER A N     1 
ATOM   7262  C  CA    . SER A 1 1141 ? 158.188 148.414 173.118 1.00 37.75  ? 1141 SER A CA    1 
ATOM   7263  C  C     . SER A 1 1141 ? 157.401 149.381 172.238 1.00 39.19  ? 1141 SER A C     1 
ATOM   7264  O  O     . SER A 1 1141 ? 157.244 149.147 171.035 1.00 42.94  ? 1141 SER A O     1 
ATOM   7265  C  CB    . SER A 1 1141 ? 157.233 147.507 173.890 1.00 38.29  ? 1141 SER A CB    1 
ATOM   7266  O  OG    . SER A 1 1141 ? 156.381 146.810 173.000 1.00 43.39  ? 1141 SER A OG    1 
ATOM   7267  N  N     . THR A 1 1142 ? 156.885 150.466 172.822 1.00 38.88  ? 1142 THR A N     1 
ATOM   7268  C  CA    . THR A 1 1142 ? 156.187 151.488 172.044 1.00 39.40  ? 1142 THR A CA    1 
ATOM   7269  C  C     . THR A 1 1142 ? 157.155 152.384 171.278 1.00 38.56  ? 1142 THR A C     1 
ATOM   7270  O  O     . THR A 1 1142 ? 156.821 152.871 170.182 1.00 36.83  ? 1142 THR A O     1 
ATOM   7271  C  CB    . THR A 1 1142 ? 155.310 152.337 172.968 1.00 36.71  ? 1142 THR A CB    1 
ATOM   7272  O  OG1   . THR A 1 1142 ? 154.521 151.477 173.797 1.00 39.93  ? 1142 THR A OG1   1 
ATOM   7273  C  CG2   . THR A 1 1142 ? 154.382 153.241 172.165 1.00 32.33  ? 1142 THR A CG2   1 
ATOM   7274  N  N     . LEU A 1 1143 ? 158.346 152.618 171.838 1.00 34.39  ? 1143 LEU A N     1 
ATOM   7275  C  CA    . LEU A 1 1143 ? 159.332 153.426 171.120 1.00 31.47  ? 1143 LEU A CA    1 
ATOM   7276  C  C     . LEU A 1 1143 ? 159.681 152.810 169.765 1.00 35.84  ? 1143 LEU A C     1 
ATOM   7277  O  O     . LEU A 1 1143 ? 159.914 153.530 168.783 1.00 37.14  ? 1143 LEU A O     1 
ATOM   7278  C  CB    . LEU A 1 1143 ? 160.590 153.603 171.967 1.00 33.44  ? 1143 LEU A CB    1 
ATOM   7279  C  CG    . LEU A 1 1143 ? 161.678 154.449 171.302 1.00 38.70  ? 1143 LEU A CG    1 
ATOM   7280  C  CD1   . LEU A 1 1143 ? 161.190 155.866 171.058 1.00 38.04  ? 1143 LEU A CD1   1 
ATOM   7281  C  CD2   . LEU A 1 1143 ? 162.945 154.457 172.124 1.00 37.31  ? 1143 LEU A CD2   1 
ATOM   7282  N  N     . GLN A 1 1144 ? 159.719 151.477 169.694 1.00 35.91  ? 1144 GLN A N     1 
ATOM   7283  C  CA    . GLN A 1 1144 ? 160.015 150.802 168.427 1.00 32.34  ? 1144 GLN A CA    1 
ATOM   7284  C  C     . GLN A 1 1144 ? 158.996 151.150 167.337 1.00 34.80  ? 1144 GLN A C     1 
ATOM   7285  O  O     . GLN A 1 1144 ? 159.365 151.473 166.193 1.00 37.15  ? 1144 GLN A O     1 
ATOM   7286  C  CB    . GLN A 1 1144 ? 160.053 149.293 168.663 1.00 30.51  ? 1144 GLN A CB    1 
ATOM   7287  C  CG    . GLN A 1 1144 ? 160.130 148.448 167.413 1.00 36.63  ? 1144 GLN A CG    1 
ATOM   7288  C  CD    . GLN A 1 1144 ? 160.288 146.973 167.726 1.00 36.20  ? 1144 GLN A CD    1 
ATOM   7289  O  OE1   . GLN A 1 1144 ? 160.290 146.571 168.889 1.00 38.10  ? 1144 GLN A OE1   1 
ATOM   7290  N  NE2   . GLN A 1 1144 ? 160.409 146.157 166.688 1.00 32.12  ? 1144 GLN A NE2   1 
ATOM   7291  N  N     . TRP A 1 1145 ? 157.707 151.099 167.677 1.00 33.54  ? 1145 TRP A N     1 
ATOM   7292  C  CA    . TRP A 1 1145 ? 156.657 151.441 166.724 1.00 33.23  ? 1145 TRP A CA    1 
ATOM   7293  C  C     . TRP A 1 1145 ? 156.725 152.909 166.331 1.00 31.87  ? 1145 TRP A C     1 
ATOM   7294  O  O     . TRP A 1 1145 ? 156.489 153.254 165.162 1.00 32.90  ? 1145 TRP A O     1 
ATOM   7295  C  CB    . TRP A 1 1145 ? 155.302 151.077 167.331 1.00 33.80  ? 1145 TRP A CB    1 
ATOM   7296  C  CG    . TRP A 1 1145 ? 154.116 151.203 166.432 1.00 32.07  ? 1145 TRP A CG    1 
ATOM   7297  C  CD1   . TRP A 1 1145 ? 154.114 151.261 165.072 1.00 32.29  ? 1145 TRP A CD1   1 
ATOM   7298  C  CD2   . TRP A 1 1145 ? 152.745 151.203 166.837 1.00 35.43  ? 1145 TRP A CD2   1 
ATOM   7299  N  NE1   . TRP A 1 1145 ? 152.822 151.343 164.607 1.00 36.29  ? 1145 TRP A NE1   1 
ATOM   7300  C  CE2   . TRP A 1 1145 ? 151.964 151.303 165.673 1.00 33.85  ? 1145 TRP A CE2   1 
ATOM   7301  C  CE3   . TRP A 1 1145 ? 152.102 151.143 168.076 1.00 35.55  ? 1145 TRP A CE3   1 
ATOM   7302  C  CZ2   . TRP A 1 1145 ? 150.571 151.346 165.710 1.00 31.87  ? 1145 TRP A CZ2   1 
ATOM   7303  C  CZ3   . TRP A 1 1145 ? 150.723 151.186 168.112 1.00 34.15  ? 1145 TRP A CZ3   1 
ATOM   7304  C  CH2   . TRP A 1 1145 ? 149.973 151.287 166.938 1.00 32.85  ? 1145 TRP A CH2   1 
ATOM   7305  N  N     . ALA A 1 1146 ? 157.078 153.782 167.278 1.00 30.31  ? 1146 ALA A N     1 
ATOM   7306  C  CA    . ALA A 1 1146 ? 157.280 155.185 166.923 1.00 28.26  ? 1146 ALA A CA    1 
ATOM   7307  C  C     . ALA A 1 1146 ? 158.395 155.342 165.892 1.00 30.92  ? 1146 ALA A C     1 
ATOM   7308  O  O     . ALA A 1 1146 ? 158.284 156.152 164.962 1.00 34.67  ? 1146 ALA A O     1 
ATOM   7309  C  CB    . ALA A 1 1146 ? 157.582 156.008 168.174 1.00 28.29  ? 1146 ALA A CB    1 
ATOM   7310  N  N     . VAL A 1 1147 ? 159.475 154.569 166.034 1.00 32.90  ? 1147 VAL A N     1 
ATOM   7311  C  CA    . VAL A 1 1147 ? 160.588 154.670 165.086 1.00 32.35  ? 1147 VAL A CA    1 
ATOM   7312  C  C     . VAL A 1 1147 ? 160.161 154.210 163.693 1.00 28.52  ? 1147 VAL A C     1 
ATOM   7313  O  O     . VAL A 1 1147 ? 160.523 154.826 162.677 1.00 29.02  ? 1147 VAL A O     1 
ATOM   7314  C  CB    . VAL A 1 1147 ? 161.803 153.874 165.596 1.00 30.30  ? 1147 VAL A CB    1 
ATOM   7315  C  CG1   . VAL A 1 1147 ? 162.803 153.656 164.478 1.00 27.32  ? 1147 VAL A CG1   1 
ATOM   7316  C  CG2   . VAL A 1 1147 ? 162.459 154.603 166.753 1.00 28.97  ? 1147 VAL A CG2   1 
ATOM   7317  N  N     . ASN A 1 1148 ? 159.391 153.123 163.617 1.00 27.63  ? 1148 ASN A N     1 
ATOM   7318  C  CA    . ASN A 1 1148 ? 158.913 152.685 162.303 1.00 28.33  ? 1148 ASN A CA    1 
ATOM   7319  C  C     . ASN A 1 1148 ? 158.007 153.734 161.659 1.00 32.38  ? 1148 ASN A C     1 
ATOM   7320  O  O     . ASN A 1 1148 ? 158.091 153.985 160.444 1.00 34.55  ? 1148 ASN A O     1 
ATOM   7321  C  CB    . ASN A 1 1148 ? 158.196 151.342 162.417 1.00 28.98  ? 1148 ASN A CB    1 
ATOM   7322  C  CG    . ASN A 1 1148 ? 159.148 150.195 162.692 1.00 33.06  ? 1148 ASN A CG    1 
ATOM   7323  O  OD1   . ASN A 1 1148 ? 160.297 150.207 162.253 1.00 30.81  ? 1148 ASN A OD1   1 
ATOM   7324  N  ND2   . ASN A 1 1148 ? 158.675 149.198 163.424 1.00 34.17  ? 1148 ASN A ND2   1 
ATOM   7325  N  N     . SER A 1 1149 ? 157.150 154.377 162.458 1.00 32.40  ? 1149 SER A N     1 
ATOM   7326  C  CA    . SER A 1 1149 ? 156.330 155.456 161.913 1.00 29.24  ? 1149 SER A CA    1 
ATOM   7327  C  C     . SER A 1 1149 ? 157.185 156.612 161.405 1.00 30.30  ? 1149 SER A C     1 
ATOM   7328  O  O     . SER A 1 1149 ? 156.853 157.229 160.383 1.00 33.96  ? 1149 SER A O     1 
ATOM   7329  C  CB    . SER A 1 1149 ? 155.345 155.952 162.967 1.00 30.03  ? 1149 SER A CB    1 
ATOM   7330  O  OG    . SER A 1 1149 ? 154.241 155.076 163.070 1.00 37.39  ? 1149 SER A OG    1 
ATOM   7331  N  N     . SER A 1 1150 ? 158.281 156.919 162.102 1.00 30.67  ? 1150 SER A N     1 
ATOM   7332  C  CA    . SER A 1 1150 ? 159.175 157.974 161.632 1.00 28.78  ? 1150 SER A CA    1 
ATOM   7333  C  C     . SER A 1 1150 ? 159.778 157.618 160.281 1.00 28.51  ? 1150 SER A C     1 
ATOM   7334  O  O     . SER A 1 1150 ? 159.902 158.478 159.398 1.00 31.25  ? 1150 SER A O     1 
ATOM   7335  C  CB    . SER A 1 1150 ? 160.285 158.219 162.650 1.00 30.39  ? 1150 SER A CB    1 
ATOM   7336  O  OG    . SER A 1 1150 ? 161.371 157.336 162.433 1.00 31.75  ? 1150 SER A OG    1 
ATOM   7337  N  N     . ILE A 1 1151 ? 160.150 156.350 160.100 1.00 31.20  ? 1151 ILE A N     1 
ATOM   7338  C  CA    . ILE A 1 1151 ? 160.712 155.938 158.815 1.00 32.27  ? 1151 ILE A CA    1 
ATOM   7339  C  C     . ILE A 1 1151 ? 159.681 156.103 157.703 1.00 33.02  ? 1151 ILE A C     1 
ATOM   7340  O  O     . ILE A 1 1151 ? 160.000 156.573 156.603 1.00 32.17  ? 1151 ILE A O     1 
ATOM   7341  C  CB    . ILE A 1 1151 ? 161.241 154.494 158.893 1.00 28.36  ? 1151 ILE A CB    1 
ATOM   7342  C  CG1   . ILE A 1 1151 ? 162.479 154.436 159.787 1.00 29.41  ? 1151 ILE A CG1   1 
ATOM   7343  C  CG2   . ILE A 1 1151 ? 161.560 153.963 157.509 1.00 23.58  ? 1151 ILE A CG2   1 
ATOM   7344  C  CD1   . ILE A 1 1151 ? 163.663 155.177 159.224 1.00 29.85  ? 1151 ILE A CD1   1 
ATOM   7345  N  N     . ASP A 1 1152 ? 158.425 155.745 157.978 1.00 33.81  ? 1152 ASP A N     1 
ATOM   7346  C  CA    . ASP A 1 1152 ? 157.385 155.905 156.961 1.00 30.56  ? 1152 ASP A CA    1 
ATOM   7347  C  C     . ASP A 1 1152 ? 157.160 157.376 156.603 1.00 32.44  ? 1152 ASP A C     1 
ATOM   7348  O  O     . ASP A 1 1152 ? 157.000 157.721 155.422 1.00 34.69  ? 1152 ASP A O     1 
ATOM   7349  C  CB    . ASP A 1 1152 ? 156.090 155.254 157.439 1.00 32.36  ? 1152 ASP A CB    1 
ATOM   7350  C  CG    . ASP A 1 1152 ? 154.945 155.462 156.478 1.00 43.07  ? 1152 ASP A CG    1 
ATOM   7351  O  OD1   . ASP A 1 1152 ? 155.183 155.474 155.252 1.00 47.47  ? 1152 ASP A OD1   1 
ATOM   7352  O  OD2   . ASP A 1 1152 ? 153.798 155.594 156.951 1.00 49.37  ? 1152 ASP A OD2   1 
ATOM   7353  N  N     . VAL A 1 1153 ? 157.139 158.258 157.605 1.00 33.35  ? 1153 VAL A N     1 
ATOM   7354  C  CA    . VAL A 1 1153 ? 156.951 159.683 157.328 1.00 31.80  ? 1153 VAL A CA    1 
ATOM   7355  C  C     . VAL A 1 1153 ? 158.094 160.215 156.467 1.00 34.53  ? 1153 VAL A C     1 
ATOM   7356  O  O     . VAL A 1 1153 ? 157.879 160.969 155.504 1.00 35.00  ? 1153 VAL A O     1 
ATOM   7357  C  CB    . VAL A 1 1153 ? 156.818 160.474 158.642 1.00 30.23  ? 1153 VAL A CB    1 
ATOM   7358  C  CG1   . VAL A 1 1153 ? 156.961 161.960 158.383 1.00 30.09  ? 1153 VAL A CG1   1 
ATOM   7359  C  CG2   . VAL A 1 1153 ? 155.493 160.182 159.304 1.00 29.64  ? 1153 VAL A CG2   1 
ATOM   7360  N  N     . ASP A 1 1154 ? 159.330 159.837 156.810 1.00 37.84  ? 1154 ASP A N     1 
ATOM   7361  C  CA    . ASP A 1 1154 ? 160.477 160.280 156.022 1.00 35.29  ? 1154 ASP A CA    1 
ATOM   7362  C  C     . ASP A 1 1154 ? 160.396 159.763 154.594 1.00 35.75  ? 1154 ASP A C     1 
ATOM   7363  O  O     . ASP A 1 1154 ? 160.806 160.453 153.653 1.00 36.71  ? 1154 ASP A O     1 
ATOM   7364  C  CB    . ASP A 1 1154 ? 161.782 159.834 156.674 1.00 36.37  ? 1154 ASP A CB    1 
ATOM   7365  C  CG    . ASP A 1 1154 ? 162.989 160.517 156.070 1.00 47.83  ? 1154 ASP A CG    1 
ATOM   7366  O  OD1   . ASP A 1 1154 ? 163.245 161.688 156.413 1.00 54.22  ? 1154 ASP A OD1   1 
ATOM   7367  O  OD2   . ASP A 1 1154 ? 163.676 159.887 155.241 1.00 50.79  ? 1154 ASP A OD2   1 
ATOM   7368  N  N     . SER A 1 1155 ? 159.879 158.548 154.412 1.00 36.00  ? 1155 SER A N     1 
ATOM   7369  C  CA    . SER A 1 1155 ? 159.671 158.037 153.062 1.00 31.91  ? 1155 SER A CA    1 
ATOM   7370  C  C     . SER A 1 1155 ? 158.683 158.902 152.292 1.00 33.87  ? 1155 SER A C     1 
ATOM   7371  O  O     . SER A 1 1155 ? 158.886 159.186 151.107 1.00 33.74  ? 1155 SER A O     1 
ATOM   7372  C  CB    . SER A 1 1155 ? 159.182 156.592 153.111 1.00 33.57  ? 1155 SER A CB    1 
ATOM   7373  O  OG    . SER A 1 1155 ? 158.901 156.116 151.808 1.00 35.92  ? 1155 SER A OG    1 
ATOM   7374  N  N     . LEU A 1 1156 ? 157.601 159.328 152.950 1.00 37.73  ? 1156 LEU A N     1 
ATOM   7375  C  CA    . LEU A 1 1156 ? 156.586 160.112 152.245 1.00 33.63  ? 1156 LEU A CA    1 
ATOM   7376  C  C     . LEU A 1 1156 ? 157.050 161.532 151.930 1.00 31.42  ? 1156 LEU A C     1 
ATOM   7377  O  O     . LEU A 1 1156 ? 156.525 162.155 151.001 1.00 31.55  ? 1156 LEU A O     1 
ATOM   7378  C  CB    . LEU A 1 1156 ? 155.287 160.159 153.045 1.00 33.40  ? 1156 LEU A CB    1 
ATOM   7379  C  CG    . LEU A 1 1156 ? 154.445 158.888 153.093 1.00 37.61  ? 1156 LEU A CG    1 
ATOM   7380  C  CD1   . LEU A 1 1156 ? 153.252 159.098 153.999 1.00 36.12  ? 1156 LEU A CD1   1 
ATOM   7381  C  CD2   . LEU A 1 1156 ? 153.993 158.511 151.696 1.00 35.38  ? 1156 LEU A CD2   1 
ATOM   7382  N  N     . MET A 1 1157 ? 158.002 162.073 152.693 1.00 31.30  ? 1157 MET A N     1 
ATOM   7383  C  CA    . MET A 1 1157 ? 158.383 163.474 152.488 1.00 32.53  ? 1157 MET A CA    1 
ATOM   7384  C  C     . MET A 1 1157 ? 159.173 163.727 151.198 1.00 35.15  ? 1157 MET A C     1 
ATOM   7385  O  O     . MET A 1 1157 ? 159.395 164.895 150.838 1.00 38.61  ? 1157 MET A O     1 
ATOM   7386  C  CB    . MET A 1 1157 ? 159.176 163.970 153.695 1.00 35.50  ? 1157 MET A CB    1 
ATOM   7387  C  CG    . MET A 1 1157 ? 158.321 164.176 154.938 1.00 39.70  ? 1157 MET A CG    1 
ATOM   7388  S  SD    . MET A 1 1157 ? 157.066 165.461 154.765 1.00 44.02  ? 1157 MET A SD    1 
ATOM   7389  C  CE    . MET A 1 1157 ? 158.088 166.919 154.624 1.00 36.18  ? 1157 MET A CE    1 
ATOM   7390  N  N     . ARG A 1 1158 ? 159.590 162.677 150.485 1.00 33.91  ? 1158 ARG A N     1 
ATOM   7391  C  CA    . ARG A 1 1158 ? 160.287 162.871 149.215 1.00 33.54  ? 1158 ARG A CA    1 
ATOM   7392  C  C     . ARG A 1 1158 ? 159.405 163.559 148.178 1.00 33.48  ? 1158 ARG A C     1 
ATOM   7393  O  O     . ARG A 1 1158 ? 159.903 164.345 147.363 1.00 36.72  ? 1158 ARG A O     1 
ATOM   7394  C  CB    . ARG A 1 1158 ? 160.772 161.530 148.668 1.00 36.30  ? 1158 ARG A CB    1 
ATOM   7395  C  CG    . ARG A 1 1158 ? 161.794 160.767 149.509 1.00 41.65  ? 1158 ARG A CG    1 
ATOM   7396  C  CD    . ARG A 1 1158 ? 162.975 161.608 149.997 1.00 47.15  ? 1158 ARG A CD    1 
ATOM   7397  N  NE    . ARG A 1 1158 ? 162.743 162.250 151.285 1.00 53.61  ? 1158 ARG A NE    1 
ATOM   7398  C  CZ    . ARG A 1 1158 ? 163.284 163.403 151.654 1.00 53.59  ? 1158 ARG A CZ    1 
ATOM   7399  N  NH1   . ARG A 1 1158 ? 164.109 164.064 150.858 1.00 49.29  ? 1158 ARG A NH1   1 
ATOM   7400  N  NH2   . ARG A 1 1158 ? 163.000 163.898 152.854 1.00 48.65  ? 1158 ARG A NH2   1 
ATOM   7401  N  N     . SER A 1 1159 ? 158.102 163.270 148.183 1.00 32.05  ? 1159 SER A N     1 
ATOM   7402  C  CA    . SER A 1 1159 ? 157.190 163.921 147.248 1.00 29.16  ? 1159 SER A CA    1 
ATOM   7403  C  C     . SER A 1 1159 ? 157.085 165.415 147.522 1.00 30.27  ? 1159 SER A C     1 
ATOM   7404  O  O     . SER A 1 1159 ? 157.015 166.221 146.587 1.00 34.43  ? 1159 SER A O     1 
ATOM   7405  C  CB    . SER A 1 1159 ? 155.815 163.263 147.322 1.00 32.22  ? 1159 SER A CB    1 
ATOM   7406  O  OG    . SER A 1 1159 ? 155.812 162.028 146.633 1.00 32.66  ? 1159 SER A OG    1 
ATOM   7407  N  N     . VAL A 1 1160 ? 157.069 165.803 148.798 1.00 33.12  ? 1160 VAL A N     1 
ATOM   7408  C  CA    . VAL A 1 1160 ? 157.083 167.218 149.147 1.00 30.26  ? 1160 VAL A CA    1 
ATOM   7409  C  C     . VAL A 1 1160 ? 158.372 167.863 148.660 1.00 33.61  ? 1160 VAL A C     1 
ATOM   7410  O  O     . VAL A 1 1160 ? 158.370 168.995 148.154 1.00 34.04  ? 1160 VAL A O     1 
ATOM   7411  C  CB    . VAL A 1 1160 ? 156.902 167.393 150.666 1.00 28.78  ? 1160 VAL A CB    1 
ATOM   7412  C  CG1   . VAL A 1 1160 ? 157.058 168.853 151.060 1.00 30.56  ? 1160 VAL A CG1   1 
ATOM   7413  C  CG2   . VAL A 1 1160 ? 155.556 166.849 151.108 1.00 28.75  ? 1160 VAL A CG2   1 
ATOM   7414  N  N     . SER A 1 1161 ? 159.492 167.152 148.802 1.00 33.83  ? 1161 SER A N     1 
ATOM   7415  C  CA    . SER A 1 1161 ? 160.758 167.685 148.307 1.00 32.33  ? 1161 SER A CA    1 
ATOM   7416  C  C     . SER A 1 1161 ? 160.712 167.911 146.798 1.00 33.53  ? 1161 SER A C     1 
ATOM   7417  O  O     . SER A 1 1161 ? 161.174 168.945 146.301 1.00 36.02  ? 1161 SER A O     1 
ATOM   7418  C  CB    . SER A 1 1161 ? 161.905 166.745 148.672 1.00 35.05  ? 1161 SER A CB    1 
ATOM   7419  O  OG    . SER A 1 1161 ? 163.149 167.284 148.266 1.00 37.01  ? 1161 SER A OG    1 
ATOM   7420  N  N     . ARG A 1 1162 ? 160.143 166.960 146.055 1.00 33.32  ? 1162 ARG A N     1 
ATOM   7421  C  CA    . ARG A 1 1162 ? 160.073 167.099 144.601 1.00 30.99  ? 1162 ARG A CA    1 
ATOM   7422  C  C     . ARG A 1 1162 ? 159.136 168.232 144.193 1.00 33.85  ? 1162 ARG A C     1 
ATOM   7423  O  O     . ARG A 1 1162 ? 159.417 168.970 143.238 1.00 35.94  ? 1162 ARG A O     1 
ATOM   7424  C  CB    . ARG A 1 1162 ? 159.645 165.775 143.969 1.00 32.20  ? 1162 ARG A CB    1 
ATOM   7425  C  CG    . ARG A 1 1162 ? 160.638 164.658 144.232 1.00 34.08  ? 1162 ARG A CG    1 
ATOM   7426  C  CD    . ARG A 1 1162 ? 160.176 163.302 143.726 1.00 35.25  ? 1162 ARG A CD    1 
ATOM   7427  N  NE    . ARG A 1 1162 ? 160.487 163.096 142.317 1.00 39.51  ? 1162 ARG A NE    1 
ATOM   7428  C  CZ    . ARG A 1 1162 ? 159.582 162.918 141.366 1.00 45.37  ? 1162 ARG A CZ    1 
ATOM   7429  N  NH1   . ARG A 1 1162 ? 158.288 162.894 141.638 1.00 43.62  ? 1162 ARG A NH1   1 
ATOM   7430  N  NH2   . ARG A 1 1162 ? 159.986 162.753 140.111 1.00 46.88  ? 1162 ARG A NH2   1 
ATOM   7431  N  N     . VAL A 1 1163 ? 158.027 168.402 144.915 1.00 36.23  ? 1163 VAL A N     1 
ATOM   7432  C  CA    . VAL A 1 1163 ? 157.110 169.496 144.609 1.00 34.71  ? 1163 VAL A CA    1 
ATOM   7433  C  C     . VAL A 1 1163 ? 157.786 170.843 144.844 1.00 34.28  ? 1163 VAL A C     1 
ATOM   7434  O  O     . VAL A 1 1163 ? 157.689 171.754 144.011 1.00 36.74  ? 1163 VAL A O     1 
ATOM   7435  C  CB    . VAL A 1 1163 ? 155.816 169.353 145.430 1.00 32.41  ? 1163 VAL A CB    1 
ATOM   7436  C  CG1   . VAL A 1 1163 ? 155.046 170.659 145.437 1.00 31.18  ? 1163 VAL A CG1   1 
ATOM   7437  C  CG2   . VAL A 1 1163 ? 154.957 168.227 144.875 1.00 30.40  ? 1163 VAL A CG2   1 
ATOM   7438  N  N     . PHE A 1 1164 ? 158.489 170.992 145.972 1.00 34.94  ? 1164 PHE A N     1 
ATOM   7439  C  CA    . PHE A 1 1164 ? 159.222 172.234 146.211 1.00 34.49  ? 1164 PHE A CA    1 
ATOM   7440  C  C     . PHE A 1 1164 ? 160.303 172.458 145.165 1.00 37.12  ? 1164 PHE A C     1 
ATOM   7441  O  O     . PHE A 1 1164 ? 160.566 173.601 144.779 1.00 40.84  ? 1164 PHE A O     1 
ATOM   7442  C  CB    . PHE A 1 1164 ? 159.842 172.239 147.608 1.00 36.99  ? 1164 PHE A CB    1 
ATOM   7443  C  CG    . PHE A 1 1164 ? 158.909 172.698 148.688 1.00 38.89  ? 1164 PHE A CG    1 
ATOM   7444  C  CD1   . PHE A 1 1164 ? 158.209 173.884 148.555 1.00 38.58  ? 1164 PHE A CD1   1 
ATOM   7445  C  CD2   . PHE A 1 1164 ? 158.749 171.958 149.845 1.00 36.02  ? 1164 PHE A CD2   1 
ATOM   7446  C  CE1   . PHE A 1 1164 ? 157.359 174.317 149.549 1.00 32.68  ? 1164 PHE A CE1   1 
ATOM   7447  C  CE2   . PHE A 1 1164 ? 157.899 172.385 150.842 1.00 36.21  ? 1164 PHE A CE2   1 
ATOM   7448  C  CZ    . PHE A 1 1164 ? 157.203 173.565 150.694 1.00 37.93  ? 1164 PHE A CZ    1 
ATOM   7449  N  N     . LYS A 1 1165 ? 160.942 171.384 144.699 1.00 38.69  ? 1165 LYS A N     1 
ATOM   7450  C  CA    . LYS A 1 1165 ? 161.928 171.512 143.634 1.00 37.86  ? 1165 LYS A CA    1 
ATOM   7451  C  C     . LYS A 1 1165 ? 161.296 172.027 142.348 1.00 37.11  ? 1165 LYS A C     1 
ATOM   7452  O  O     . LYS A 1 1165 ? 161.922 172.800 141.616 1.00 36.21  ? 1165 LYS A O     1 
ATOM   7453  C  CB    . LYS A 1 1165 ? 162.602 170.162 143.404 1.00 38.97  ? 1165 LYS A CB    1 
ATOM   7454  C  CG    . LYS A 1 1165 ? 163.811 170.189 142.503 1.00 45.07  ? 1165 LYS A CG    1 
ATOM   7455  C  CD    . LYS A 1 1165 ? 164.342 168.782 142.321 1.00 51.56  ? 1165 LYS A CD    1 
ATOM   7456  C  CE    . LYS A 1 1165 ? 164.785 168.201 143.658 1.00 51.82  ? 1165 LYS A CE    1 
ATOM   7457  N  NZ    . LYS A 1 1165 ? 164.266 166.821 143.867 1.00 46.60  ? 1165 LYS A NZ    1 
ATOM   7458  N  N     . PHE A 1 1166 ? 160.063 171.612 142.062 1.00 40.20  ? 1166 PHE A N     1 
ATOM   7459  C  CA    . PHE A 1 1166 ? 159.363 172.124 140.888 1.00 38.89  ? 1166 PHE A CA    1 
ATOM   7460  C  C     . PHE A 1 1166 ? 158.900 173.564 141.073 1.00 37.21  ? 1166 PHE A C     1 
ATOM   7461  O  O     . PHE A 1 1166 ? 158.768 174.298 140.089 1.00 37.03  ? 1166 PHE A O     1 
ATOM   7462  C  CB    . PHE A 1 1166 ? 158.167 171.233 140.556 1.00 38.16  ? 1166 PHE A CB    1 
ATOM   7463  C  CG    . PHE A 1 1166 ? 158.159 170.733 139.143 1.00 41.30  ? 1166 PHE A CG    1 
ATOM   7464  C  CD1   . PHE A 1 1166 ? 159.266 170.091 138.619 1.00 42.09  ? 1166 PHE A CD1   1 
ATOM   7465  C  CD2   . PHE A 1 1166 ? 157.045 170.895 138.342 1.00 42.15  ? 1166 PHE A CD2   1 
ATOM   7466  C  CE1   . PHE A 1 1166 ? 159.265 169.625 137.326 1.00 39.50  ? 1166 PHE A CE1   1 
ATOM   7467  C  CE2   . PHE A 1 1166 ? 157.038 170.430 137.045 1.00 43.72  ? 1166 PHE A CE2   1 
ATOM   7468  C  CZ    . PHE A 1 1166 ? 158.150 169.794 136.537 1.00 42.63  ? 1166 PHE A CZ    1 
ATOM   7469  N  N     . ILE A 1 1167 ? 158.637 173.982 142.313 1.00 38.12  ? 1167 ILE A N     1 
ATOM   7470  C  CA    . ILE A 1 1167 ? 158.189 175.353 142.547 1.00 35.25  ? 1167 ILE A CA    1 
ATOM   7471  C  C     . ILE A 1 1167 ? 159.314 176.357 142.305 1.00 39.21  ? 1167 ILE A C     1 
ATOM   7472  O  O     . ILE A 1 1167 ? 159.061 177.489 141.877 1.00 43.83  ? 1167 ILE A O     1 
ATOM   7473  C  CB    . ILE A 1 1167 ? 157.604 175.479 143.968 1.00 38.06  ? 1167 ILE A CB    1 
ATOM   7474  C  CG1   . ILE A 1 1167 ? 156.271 174.739 144.058 1.00 33.86  ? 1167 ILE A CG1   1 
ATOM   7475  C  CG2   . ILE A 1 1167 ? 157.413 176.931 144.363 1.00 33.24  ? 1167 ILE A CG2   1 
ATOM   7476  C  CD1   . ILE A 1 1167 ? 155.815 174.480 145.468 1.00 33.36  ? 1167 ILE A CD1   1 
ATOM   7477  N  N     . ASP A 1 1168 ? 160.566 175.965 142.542 1.00 42.69  ? 1168 ASP A N     1 
ATOM   7478  C  CA    . ASP A 1 1168 ? 161.704 176.875 142.477 1.00 43.82  ? 1168 ASP A CA    1 
ATOM   7479  C  C     . ASP A 1 1168 ? 162.212 177.111 141.056 1.00 47.01  ? 1168 ASP A C     1 
ATOM   7480  O  O     . ASP A 1 1168 ? 163.373 177.500 140.882 1.00 45.08  ? 1168 ASP A O     1 
ATOM   7481  C  CB    . ASP A 1 1168 ? 162.847 176.354 143.349 1.00 43.52  ? 1168 ASP A CB    1 
ATOM   7482  C  CG    . ASP A 1 1168 ? 162.449 176.193 144.800 1.00 49.69  ? 1168 ASP A CG    1 
ATOM   7483  O  OD1   . ASP A 1 1168 ? 161.476 176.845 145.229 1.00 45.29  ? 1168 ASP A OD1   1 
ATOM   7484  O  OD2   . ASP A 1 1168 ? 163.113 175.415 145.513 1.00 54.70  ? 1168 ASP A OD2   1 
ATOM   7485  N  N     . MET A 1 1169 ? 161.385 176.880 140.046 1.00 48.21  ? 1169 MET A N     1 
ATOM   7486  C  CA    . MET A 1 1169 ? 161.806 177.123 138.675 1.00 46.96  ? 1169 MET A CA    1 
ATOM   7487  C  C     . MET A 1 1169 ? 162.004 178.621 138.444 1.00 53.46  ? 1169 MET A C     1 
ATOM   7488  O  O     . MET A 1 1169 ? 161.279 179.439 139.022 1.00 55.80  ? 1169 MET A O     1 
ATOM   7489  C  CB    . MET A 1 1169 ? 160.771 176.572 137.694 1.00 46.24  ? 1169 MET A CB    1 
ATOM   7490  C  CG    . MET A 1 1169 ? 161.044 175.157 137.236 1.00 46.01  ? 1169 MET A CG    1 
ATOM   7491  S  SD    . MET A 1 1169 ? 159.590 174.399 136.493 1.00 55.87  ? 1169 MET A SD    1 
ATOM   7492  C  CE    . MET A 1 1169 ? 160.288 172.873 135.877 1.00 46.24  ? 1169 MET A CE    1 
ATOM   7493  N  N     . PRO A 1 1170 ? 162.973 179.014 137.619 1.00 54.08  ? 1170 PRO A N     1 
ATOM   7494  C  CA    . PRO A 1 1170 ? 163.183 180.441 137.353 1.00 56.38  ? 1170 PRO A CA    1 
ATOM   7495  C  C     . PRO A 1 1170 ? 162.039 181.054 136.559 1.00 57.12  ? 1170 PRO A C     1 
ATOM   7496  O  O     . PRO A 1 1170 ? 161.323 180.372 135.823 1.00 53.11  ? 1170 PRO A O     1 
ATOM   7497  C  CB    . PRO A 1 1170 ? 164.490 180.460 136.555 1.00 52.02  ? 1170 PRO A CB    1 
ATOM   7498  C  CG    . PRO A 1 1170 ? 164.507 179.145 135.862 1.00 49.97  ? 1170 PRO A CG    1 
ATOM   7499  C  CD    . PRO A 1 1170 ? 163.893 178.171 136.838 1.00 51.65  ? 1170 PRO A CD    1 
ATOM   7500  N  N     . THR A 1 1171 ? 161.869 182.363 136.732 1.00 58.57  ? 1171 THR A N     1 
ATOM   7501  C  CA    . THR A 1 1171 ? 160.815 183.115 136.064 1.00 55.19  ? 1171 THR A CA    1 
ATOM   7502  C  C     . THR A 1 1171 ? 161.307 183.637 134.720 1.00 57.88  ? 1171 THR A C     1 
ATOM   7503  O  O     . THR A 1 1171 ? 162.470 184.027 134.579 1.00 62.59  ? 1171 THR A O     1 
ATOM   7504  C  CB    . THR A 1 1171 ? 160.354 184.278 136.945 1.00 57.43  ? 1171 THR A CB    1 
ATOM   7505  O  OG1   . THR A 1 1171 ? 159.973 183.779 138.231 1.00 63.61  ? 1171 THR A OG1   1 
ATOM   7506  C  CG2   . THR A 1 1171 ? 159.166 184.991 136.327 1.00 55.66  ? 1171 THR A CG2   1 
ATOM   7507  N  N     . GLU A 1 1172 ? 160.411 183.641 133.730 1.00 54.09  ? 1172 GLU A N     1 
ATOM   7508  C  CA    . GLU A 1 1172 ? 160.783 184.082 132.389 1.00 54.63  ? 1172 GLU A CA    1 
ATOM   7509  C  C     . GLU A 1 1172 ? 161.144 185.562 132.350 1.00 63.00  ? 1172 GLU A C     1 
ATOM   7510  O  O     . GLU A 1 1172 ? 162.051 185.955 131.609 1.00 59.06  ? 1172 GLU A O     1 
ATOM   7511  C  CB    . GLU A 1 1172 ? 159.645 183.788 131.412 1.00 51.71  ? 1172 GLU A CB    1 
ATOM   7512  C  CG    . GLU A 1 1172 ? 160.000 184.002 129.952 1.00 51.62  ? 1172 GLU A CG    1 
ATOM   7513  C  CD    . GLU A 1 1172 ? 158.882 183.590 129.014 1.00 54.59  ? 1172 GLU A CD    1 
ATOM   7514  O  OE1   . GLU A 1 1172 ? 157.706 183.867 129.328 1.00 53.51  ? 1172 GLU A OE1   1 
ATOM   7515  O  OE2   . GLU A 1 1172 ? 159.181 182.989 127.961 1.00 51.46  ? 1172 GLU A OE2   1 
ATOM   7516  N  N     . GLY A 1 1173 ? 160.456 186.391 133.127 1.00 66.74  ? 1173 GLY A N     1 
ATOM   7517  C  CA    . GLY A 1 1173 ? 160.704 187.822 133.117 1.00 62.43  ? 1173 GLY A CA    1 
ATOM   7518  C  C     . GLY A 1 1173 ? 161.950 188.236 133.875 1.00 66.15  ? 1173 GLY A C     1 
ATOM   7519  O  O     . GLY A 1 1173 ? 162.360 189.396 133.832 1.00 66.17  ? 1173 GLY A O     1 
ATOM   7520  N  N     . ILE A 1 1203 ? 146.071 205.665 124.110 1.00 75.99  ? 1203 ILE A N     1 
ATOM   7521  C  CA    . ILE A 1 1203 ? 146.433 204.299 123.755 1.00 79.54  ? 1203 ILE A CA    1 
ATOM   7522  C  C     . ILE A 1 1203 ? 147.824 204.257 123.132 1.00 76.54  ? 1203 ILE A C     1 
ATOM   7523  O  O     . ILE A 1 1203 ? 148.167 205.083 122.287 1.00 77.25  ? 1203 ILE A O     1 
ATOM   7524  C  CB    . ILE A 1 1203 ? 145.386 203.674 122.812 1.00 77.35  ? 1203 ILE A CB    1 
ATOM   7525  C  CG1   . ILE A 1 1203 ? 145.189 204.548 121.572 1.00 77.87  ? 1203 ILE A CG1   1 
ATOM   7526  C  CG2   . ILE A 1 1203 ? 144.066 203.464 123.540 1.00 72.05  ? 1203 ILE A CG2   1 
ATOM   7527  C  CD1   . ILE A 1 1203 ? 144.305 203.929 120.517 1.00 78.63  ? 1203 ILE A CD1   1 
ATOM   7528  N  N     . TRP A 1 1204 ? 148.633 203.298 123.575 1.00 71.34  ? 1204 TRP A N     1 
ATOM   7529  C  CA    . TRP A 1 1204 ? 149.986 203.131 123.063 1.00 65.72  ? 1204 TRP A CA    1 
ATOM   7530  C  C     . TRP A 1 1204 ? 149.990 202.590 121.632 1.00 72.89  ? 1204 TRP A C     1 
ATOM   7531  O  O     . TRP A 1 1204 ? 150.534 203.256 120.740 1.00 73.51  ? 1204 TRP A O     1 
ATOM   7532  C  CB    . TRP A 1 1204 ? 150.804 202.247 124.009 1.00 55.36  ? 1204 TRP A CB    1 
ATOM   7533  C  CG    . TRP A 1 1204 ? 151.994 201.604 123.381 1.00 53.97  ? 1204 TRP A CG    1 
ATOM   7534  C  CD1   . TRP A 1 1204 ? 152.937 202.200 122.596 1.00 51.95  ? 1204 TRP A CD1   1 
ATOM   7535  C  CD2   . TRP A 1 1204 ? 152.382 200.235 123.505 1.00 53.06  ? 1204 TRP A CD2   1 
ATOM   7536  N  NE1   . TRP A 1 1204 ? 153.879 201.279 122.212 1.00 53.09  ? 1204 TRP A NE1   1 
ATOM   7537  C  CE2   . TRP A 1 1204 ? 153.562 200.066 122.761 1.00 51.65  ? 1204 TRP A CE2   1 
ATOM   7538  C  CE3   . TRP A 1 1204 ? 151.841 199.132 124.171 1.00 48.40  ? 1204 TRP A CE3   1 
ATOM   7539  C  CZ2   . TRP A 1 1204 ? 154.212 198.841 122.664 1.00 47.19  ? 1204 TRP A CZ2   1 
ATOM   7540  C  CZ3   . TRP A 1 1204 ? 152.486 197.919 124.073 1.00 47.07  ? 1204 TRP A CZ3   1 
ATOM   7541  C  CH2   . TRP A 1 1204 ? 153.657 197.781 123.324 1.00 48.52  ? 1204 TRP A CH2   1 
ATOM   7542  N  N     . PRO A 1 1205 ? 149.412 201.400 121.345 1.00 74.68  ? 1205 PRO A N     1 
ATOM   7543  C  CA    . PRO A 1 1205 ? 149.477 200.899 119.965 1.00 69.37  ? 1205 PRO A CA    1 
ATOM   7544  C  C     . PRO A 1 1205 ? 148.496 201.624 119.057 1.00 71.14  ? 1205 PRO A C     1 
ATOM   7545  O  O     . PRO A 1 1205 ? 147.400 201.122 118.791 1.00 75.56  ? 1205 PRO A O     1 
ATOM   7546  C  CB    . PRO A 1 1205 ? 149.121 199.416 120.113 1.00 64.33  ? 1205 PRO A CB    1 
ATOM   7547  C  CG    . PRO A 1 1205 ? 148.212 199.384 121.278 1.00 64.92  ? 1205 PRO A CG    1 
ATOM   7548  C  CD    . PRO A 1 1205 ? 148.701 200.449 122.223 1.00 66.59  ? 1205 PRO A CD    1 
ATOM   7549  N  N     . SER A 1 1206 ? 148.876 202.802 118.569 1.00 69.26  ? 1206 SER A N     1 
ATOM   7550  C  CA    . SER A 1 1206 ? 147.981 203.636 117.779 1.00 76.29  ? 1206 SER A CA    1 
ATOM   7551  C  C     . SER A 1 1206 ? 148.171 203.453 116.281 1.00 78.43  ? 1206 SER A C     1 
ATOM   7552  O  O     . SER A 1 1206 ? 147.192 203.266 115.554 1.00 75.39  ? 1206 SER A O     1 
ATOM   7553  C  CB    . SER A 1 1206 ? 148.172 205.114 118.146 1.00 76.36  ? 1206 SER A CB    1 
ATOM   7554  O  OG    . SER A 1 1206 ? 149.466 205.566 117.789 1.00 73.66  ? 1206 SER A OG    1 
ATOM   7555  N  N     . GLY A 1 1207 ? 149.409 203.502 115.797 1.00 77.60  ? 1207 GLY A N     1 
ATOM   7556  C  CA    . GLY A 1 1207 ? 149.669 203.337 114.381 1.00 71.78  ? 1207 GLY A CA    1 
ATOM   7557  C  C     . GLY A 1 1207 ? 150.089 201.934 113.996 1.00 70.05  ? 1207 GLY A C     1 
ATOM   7558  O  O     . GLY A 1 1207 ? 149.581 201.369 113.023 1.00 71.54  ? 1207 GLY A O     1 
ATOM   7559  N  N     . GLY A 1 1208 ? 151.009 201.356 114.762 1.00 68.03  ? 1208 GLY A N     1 
ATOM   7560  C  CA    . GLY A 1 1208 ? 151.606 200.086 114.408 1.00 59.24  ? 1208 GLY A CA    1 
ATOM   7561  C  C     . GLY A 1 1208 ? 152.943 200.187 113.713 1.00 60.93  ? 1208 GLY A C     1 
ATOM   7562  O  O     . GLY A 1 1208 ? 153.341 199.240 113.028 1.00 66.58  ? 1208 GLY A O     1 
ATOM   7563  N  N     . GLN A 1 1209 ? 153.642 201.309 113.857 1.00 58.95  ? 1209 GLN A N     1 
ATOM   7564  C  CA    . GLN A 1 1209 ? 154.971 201.460 113.281 1.00 58.12  ? 1209 GLN A CA    1 
ATOM   7565  C  C     . GLN A 1 1209 ? 155.987 200.659 114.088 1.00 56.09  ? 1209 GLN A C     1 
ATOM   7566  O  O     . GLN A 1 1209 ? 156.086 200.815 115.308 1.00 59.37  ? 1209 GLN A O     1 
ATOM   7567  C  CB    . GLN A 1 1209 ? 155.348 202.941 113.244 1.00 58.10  ? 1209 GLN A CB    1 
ATOM   7568  C  CG    . GLN A 1 1209 ? 156.575 203.288 112.416 1.00 60.27  ? 1209 GLN A CG    1 
ATOM   7569  C  CD    . GLN A 1 1209 ? 157.876 203.007 113.138 1.00 57.70  ? 1209 GLN A CD    1 
ATOM   7570  O  OE1   . GLN A 1 1209 ? 157.951 203.104 114.363 1.00 56.63  ? 1209 GLN A OE1   1 
ATOM   7571  N  NE2   . GLN A 1 1209 ? 158.910 202.663 112.383 1.00 55.53  ? 1209 GLN A NE2   1 
ATOM   7572  N  N     . MET A 1 1210 ? 156.745 199.803 113.405 1.00 53.38  ? 1210 MET A N     1 
ATOM   7573  C  CA    . MET A 1 1210 ? 157.732 198.936 114.035 1.00 51.86  ? 1210 MET A CA    1 
ATOM   7574  C  C     . MET A 1 1210 ? 159.128 199.257 113.519 1.00 52.96  ? 1210 MET A C     1 
ATOM   7575  O  O     . MET A 1 1210 ? 159.308 199.566 112.338 1.00 58.22  ? 1210 MET A O     1 
ATOM   7576  C  CB    . MET A 1 1210 ? 157.422 197.461 113.771 1.00 52.91  ? 1210 MET A CB    1 
ATOM   7577  C  CG    . MET A 1 1210 ? 156.125 196.971 114.379 1.00 57.77  ? 1210 MET A CG    1 
ATOM   7578  S  SD    . MET A 1 1210 ? 155.786 195.262 113.923 1.00 89.81  ? 1210 MET A SD    1 
ATOM   7579  C  CE    . MET A 1 1210 ? 157.127 194.419 114.758 1.00 54.76  ? 1210 MET A CE    1 
ATOM   7580  N  N     . THR A 1 1211 ? 160.116 199.179 114.409 1.00 50.31  ? 1211 THR A N     1 
ATOM   7581  C  CA    . THR A 1 1211 ? 161.516 199.373 114.053 1.00 51.71  ? 1211 THR A CA    1 
ATOM   7582  C  C     . THR A 1 1211 ? 162.360 198.321 114.756 1.00 50.15  ? 1211 THR A C     1 
ATOM   7583  O  O     . THR A 1 1211 ? 162.244 198.140 115.971 1.00 51.39  ? 1211 THR A O     1 
ATOM   7584  C  CB    . THR A 1 1211 ? 162.001 200.776 114.432 1.00 50.10  ? 1211 THR A CB    1 
ATOM   7585  O  OG1   . THR A 1 1211 ? 161.183 201.758 113.788 1.00 51.80  ? 1211 THR A OG1   1 
ATOM   7586  C  CG2   . THR A 1 1211 ? 163.440 200.975 114.000 1.00 48.26  ? 1211 THR A CG2   1 
ATOM   7587  N  N     . VAL A 1 1212 ? 163.208 197.634 113.993 1.00 47.89  ? 1212 VAL A N     1 
ATOM   7588  C  CA    . VAL A 1 1212 ? 164.084 196.590 114.510 1.00 48.17  ? 1212 VAL A CA    1 
ATOM   7589  C  C     . VAL A 1 1212 ? 165.521 196.956 114.170 1.00 53.90  ? 1212 VAL A C     1 
ATOM   7590  O  O     . VAL A 1 1212 ? 165.797 197.464 113.078 1.00 57.84  ? 1212 VAL A O     1 
ATOM   7591  C  CB    . VAL A 1 1212 ? 163.717 195.206 113.936 1.00 46.58  ? 1212 VAL A CB    1 
ATOM   7592  C  CG1   . VAL A 1 1212 ? 164.638 194.132 114.486 1.00 45.83  ? 1212 VAL A CG1   1 
ATOM   7593  C  CG2   . VAL A 1 1212 ? 162.268 194.876 114.242 1.00 47.20  ? 1212 VAL A CG2   1 
ATOM   7594  N  N     . LYS A 1 1213 ? 166.434 196.711 115.108 1.00 52.57  ? 1213 LYS A N     1 
ATOM   7595  C  CA    . LYS A 1 1213 ? 167.831 197.085 114.916 1.00 56.98  ? 1213 LYS A CA    1 
ATOM   7596  C  C     . LYS A 1 1213 ? 168.735 196.056 115.576 1.00 60.10  ? 1213 LYS A C     1 
ATOM   7597  O  O     . LYS A 1 1213 ? 168.682 195.880 116.796 1.00 61.76  ? 1213 LYS A O     1 
ATOM   7598  C  CB    . LYS A 1 1213 ? 168.094 198.477 115.488 1.00 56.69  ? 1213 LYS A CB    1 
ATOM   7599  C  CG    . LYS A 1 1213 ? 169.492 198.999 115.247 1.00 63.99  ? 1213 LYS A CG    1 
ATOM   7600  C  CD    . LYS A 1 1213 ? 169.655 200.387 115.834 1.00 68.62  ? 1213 LYS A CD    1 
ATOM   7601  C  CE    . LYS A 1 1213 ? 171.021 200.960 115.512 1.00 73.18  ? 1213 LYS A CE    1 
ATOM   7602  N  NZ    . LYS A 1 1213 ? 171.158 201.256 114.060 1.00 72.37  ? 1213 LYS A NZ    1 
ATOM   7603  N  N     . ASP A 1 1214 ? 169.569 195.396 114.769 1.00 60.54  ? 1214 ASP A N     1 
ATOM   7604  C  CA    . ASP A 1 1214 ? 170.589 194.464 115.252 1.00 62.01  ? 1214 ASP A CA    1 
ATOM   7605  C  C     . ASP A 1 1214 ? 169.984 193.366 116.125 1.00 61.97  ? 1214 ASP A C     1 
ATOM   7606  O  O     . ASP A 1 1214 ? 170.410 193.125 117.257 1.00 60.89  ? 1214 ASP A O     1 
ATOM   7607  C  CB    . ASP A 1 1214 ? 171.696 195.210 115.997 1.00 63.35  ? 1214 ASP A CB    1 
ATOM   7608  C  CG    . ASP A 1 1214 ? 172.369 196.261 115.138 1.00 69.03  ? 1214 ASP A CG    1 
ATOM   7609  O  OD1   . ASP A 1 1214 ? 172.582 196.002 113.935 1.00 73.03  ? 1214 ASP A OD1   1 
ATOM   7610  O  OD2   . ASP A 1 1214 ? 172.690 197.345 115.666 1.00 72.25  ? 1214 ASP A OD2   1 
ATOM   7611  N  N     . LEU A 1 1215 ? 168.975 192.692 115.583 1.00 60.84  ? 1215 LEU A N     1 
ATOM   7612  C  CA    . LEU A 1 1215 ? 168.286 191.636 116.310 1.00 56.26  ? 1215 LEU A CA    1 
ATOM   7613  C  C     . LEU A 1 1215 ? 169.004 190.304 116.121 1.00 55.81  ? 1215 LEU A C     1 
ATOM   7614  O  O     . LEU A 1 1215 ? 169.310 189.911 114.993 1.00 61.59  ? 1215 LEU A O     1 
ATOM   7615  C  CB    . LEU A 1 1215 ? 166.840 191.525 115.832 1.00 56.62  ? 1215 LEU A CB    1 
ATOM   7616  C  CG    . LEU A 1 1215 ? 165.900 190.653 116.663 1.00 54.97  ? 1215 LEU A CG    1 
ATOM   7617  C  CD1   . LEU A 1 1215 ? 165.586 191.345 117.971 1.00 51.29  ? 1215 LEU A CD1   1 
ATOM   7618  C  CD2   . LEU A 1 1215 ? 164.629 190.349 115.896 1.00 53.80  ? 1215 LEU A CD2   1 
ATOM   7619  N  N     . THR A 1 1216 ? 169.276 189.615 117.226 1.00 55.43  ? 1216 THR A N     1 
ATOM   7620  C  CA    . THR A 1 1216 ? 169.888 188.292 117.205 1.00 57.91  ? 1216 THR A CA    1 
ATOM   7621  C  C     . THR A 1 1216 ? 169.013 187.330 117.995 1.00 54.80  ? 1216 THR A C     1 
ATOM   7622  O  O     . THR A 1 1216 ? 168.555 187.664 119.092 1.00 57.36  ? 1216 THR A O     1 
ATOM   7623  C  CB    . THR A 1 1216 ? 171.301 188.327 117.792 1.00 62.43  ? 1216 THR A CB    1 
ATOM   7624  O  OG1   . THR A 1 1216 ? 172.105 189.253 117.053 1.00 63.85  ? 1216 THR A OG1   1 
ATOM   7625  C  CG2   . THR A 1 1216 ? 171.942 186.953 117.724 1.00 61.47  ? 1216 THR A CG2   1 
ATOM   7626  N  N     . ALA A 1 1217 ? 168.785 186.141 117.443 1.00 50.35  ? 1217 ALA A N     1 
ATOM   7627  C  CA    . ALA A 1 1217 ? 167.911 185.151 118.054 1.00 54.16  ? 1217 ALA A CA    1 
ATOM   7628  C  C     . ALA A 1 1217 ? 168.626 183.813 118.160 1.00 55.86  ? 1217 ALA A C     1 
ATOM   7629  O  O     . ALA A 1 1217 ? 169.374 183.426 117.259 1.00 60.25  ? 1217 ALA A O     1 
ATOM   7630  C  CB    . ALA A 1 1217 ? 166.616 184.984 117.252 1.00 55.70  ? 1217 ALA A CB    1 
ATOM   7631  N  N     . LYS A 1 1218 ? 168.388 183.110 119.265 1.00 50.07  ? 1218 LYS A N     1 
ATOM   7632  C  CA    . LYS A 1 1218 ? 168.985 181.802 119.495 1.00 49.43  ? 1218 LYS A CA    1 
ATOM   7633  C  C     . LYS A 1 1218 ? 168.180 181.080 120.566 1.00 51.74  ? 1218 LYS A C     1 
ATOM   7634  O  O     . LYS A 1 1218 ? 167.663 181.711 121.489 1.00 55.20  ? 1218 LYS A O     1 
ATOM   7635  C  CB    . LYS A 1 1218 ? 170.456 181.934 119.902 1.00 57.82  ? 1218 LYS A CB    1 
ATOM   7636  C  CG    . LYS A 1 1218 ? 170.682 182.711 121.180 1.00 59.30  ? 1218 LYS A CG    1 
ATOM   7637  C  CD    . LYS A 1 1218 ? 172.075 183.303 121.211 1.00 61.38  ? 1218 LYS A CD    1 
ATOM   7638  C  CE    . LYS A 1 1218 ? 173.124 182.229 121.040 1.00 69.84  ? 1218 LYS A CE    1 
ATOM   7639  N  NZ    . LYS A 1 1218 ? 174.496 182.803 121.030 1.00 76.03  ? 1218 LYS A NZ    1 
ATOM   7640  N  N     . TYR A 1 1219 ? 168.069 179.759 120.427 1.00 53.30  ? 1219 TYR A N     1 
ATOM   7641  C  CA    . TYR A 1 1219 ? 167.202 178.990 121.314 1.00 53.34  ? 1219 TYR A CA    1 
ATOM   7642  C  C     . TYR A 1 1219 ? 167.888 178.596 122.616 1.00 58.64  ? 1219 TYR A C     1 
ATOM   7643  O  O     . TYR A 1 1219 ? 167.206 178.356 123.618 1.00 57.30  ? 1219 TYR A O     1 
ATOM   7644  C  CB    . TYR A 1 1219 ? 166.687 177.747 120.589 1.00 41.83  ? 1219 TYR A CB    1 
ATOM   7645  C  CG    . TYR A 1 1219 ? 165.645 178.066 119.546 1.00 37.34  ? 1219 TYR A CG    1 
ATOM   7646  C  CD1   . TYR A 1 1219 ? 164.303 178.146 119.882 1.00 37.40  ? 1219 TYR A CD1   1 
ATOM   7647  C  CD2   . TYR A 1 1219 ? 166.006 178.317 118.234 1.00 38.56  ? 1219 TYR A CD2   1 
ATOM   7648  C  CE1   . TYR A 1 1219 ? 163.349 178.448 118.937 1.00 39.05  ? 1219 TYR A CE1   1 
ATOM   7649  C  CE2   . TYR A 1 1219 ? 165.059 178.621 117.282 1.00 37.81  ? 1219 TYR A CE2   1 
ATOM   7650  C  CZ    . TYR A 1 1219 ? 163.732 178.686 117.639 1.00 37.80  ? 1219 TYR A CZ    1 
ATOM   7651  O  OH    . TYR A 1 1219 ? 162.785 178.986 116.691 1.00 39.38  ? 1219 TYR A OH    1 
ATOM   7652  N  N     . THR A 1 1220 ? 169.213 178.516 122.629 1.00 63.01  ? 1220 THR A N     1 
ATOM   7653  C  CA    . THR A 1 1220 ? 169.958 178.128 123.816 1.00 66.68  ? 1220 THR A CA    1 
ATOM   7654  C  C     . THR A 1 1220 ? 170.962 179.216 124.164 1.00 71.86  ? 1220 THR A C     1 
ATOM   7655  O  O     . THR A 1 1220 ? 171.692 179.699 123.294 1.00 74.02  ? 1220 THR A O     1 
ATOM   7656  C  CB    . THR A 1 1220 ? 170.677 176.789 123.600 1.00 73.36  ? 1220 THR A CB    1 
ATOM   7657  O  OG1   . THR A 1 1220 ? 169.756 175.712 123.810 1.00 70.51  ? 1220 THR A OG1   1 
ATOM   7658  C  CG2   . THR A 1 1220 ? 171.848 176.634 124.554 1.00 75.77  ? 1220 THR A CG2   1 
ATOM   7659  N  N     . GLU A 1 1221 ? 170.999 179.595 125.441 1.00 78.55  ? 1221 GLU A N     1 
ATOM   7660  C  CA    . GLU A 1 1221 ? 171.934 180.611 125.912 1.00 82.54  ? 1221 GLU A CA    1 
ATOM   7661  C  C     . GLU A 1 1221 ? 173.356 180.088 125.756 1.00 82.50  ? 1221 GLU A C     1 
ATOM   7662  O  O     . GLU A 1 1221 ? 173.806 179.241 126.534 1.00 80.55  ? 1221 GLU A O     1 
ATOM   7663  C  CB    . GLU A 1 1221 ? 171.637 180.971 127.364 1.00 81.74  ? 1221 GLU A CB    1 
ATOM   7664  C  CG    . GLU A 1 1221 ? 172.632 181.942 127.981 1.00 89.93  ? 1221 GLU A CG    1 
ATOM   7665  C  CD    . GLU A 1 1221 ? 172.287 183.393 127.701 1.00 93.34  ? 1221 GLU A CD    1 
ATOM   7666  O  OE1   . GLU A 1 1221 ? 171.364 183.921 128.353 1.00 95.24  ? 1221 GLU A OE1   1 
ATOM   7667  O  OE2   . GLU A 1 1221 ? 172.935 184.001 126.823 1.00 89.82  ? 1221 GLU A OE2   1 
ATOM   7668  N  N     . GLY A 1 1222 ? 174.067 180.600 124.756 1.00 82.05  ? 1222 GLY A N     1 
ATOM   7669  C  CA    . GLY A 1 1222 ? 175.375 180.085 124.418 1.00 82.82  ? 1222 GLY A CA    1 
ATOM   7670  C  C     . GLY A 1 1222 ? 175.386 179.056 123.312 1.00 83.95  ? 1222 GLY A C     1 
ATOM   7671  O  O     . GLY A 1 1222 ? 176.313 178.241 123.248 1.00 87.57  ? 1222 GLY A O     1 
ATOM   7672  N  N     . GLY A 1 1223 ? 174.376 179.057 122.440 1.00 78.42  ? 1223 GLY A N     1 
ATOM   7673  C  CA    . GLY A 1 1223 ? 174.298 178.137 121.337 1.00 77.02  ? 1223 GLY A CA    1 
ATOM   7674  C  C     . GLY A 1 1223 ? 174.494 178.809 119.994 1.00 78.98  ? 1223 GLY A C     1 
ATOM   7675  O  O     . GLY A 1 1223 ? 175.025 179.923 119.889 1.00 79.35  ? 1223 GLY A O     1 
ATOM   7676  N  N     . ASN A 1 1224 ? 174.068 178.111 118.944 1.00 77.53  ? 1224 ASN A N     1 
ATOM   7677  C  CA    . ASN A 1 1224 ? 174.122 178.662 117.598 1.00 76.37  ? 1224 ASN A CA    1 
ATOM   7678  C  C     . ASN A 1 1224 ? 173.031 179.707 117.401 1.00 74.47  ? 1224 ASN A C     1 
ATOM   7679  O  O     . ASN A 1 1224 ? 171.930 179.590 117.947 1.00 75.72  ? 1224 ASN A O     1 
ATOM   7680  C  CB    . ASN A 1 1224 ? 173.968 177.549 116.564 1.00 76.69  ? 1224 ASN A CB    1 
ATOM   7681  C  CG    . ASN A 1 1224 ? 174.330 177.999 115.165 1.00 83.04  ? 1224 ASN A CG    1 
ATOM   7682  O  OD1   . ASN A 1 1224 ? 175.152 178.897 114.983 1.00 84.70  ? 1224 ASN A OD1   1 
ATOM   7683  N  ND2   . ASN A 1 1224 ? 173.707 177.386 114.167 1.00 81.17  ? 1224 ASN A ND2   1 
ATOM   7684  N  N     . ALA A 1 1225 ? 173.340 180.734 116.615 1.00 66.52  ? 1225 ALA A N     1 
ATOM   7685  C  CA    . ALA A 1 1225 ? 172.393 181.801 116.325 1.00 65.97  ? 1225 ALA A CA    1 
ATOM   7686  C  C     . ALA A 1 1225 ? 171.660 181.510 115.022 1.00 66.71  ? 1225 ALA A C     1 
ATOM   7687  O  O     . ALA A 1 1225 ? 172.290 181.237 113.996 1.00 69.60  ? 1225 ALA A O     1 
ATOM   7688  C  CB    . ALA A 1 1225 ? 173.107 183.149 116.238 1.00 65.53  ? 1225 ALA A CB    1 
ATOM   7689  N  N     . ILE A 1 1226 ? 170.332 181.573 115.066 1.00 63.04  ? 1226 ILE A N     1 
ATOM   7690  C  CA    . ILE A 1 1226 ? 169.529 181.323 113.875 1.00 59.38  ? 1226 ILE A CA    1 
ATOM   7691  C  C     . ILE A 1 1226 ? 169.379 182.582 113.024 1.00 63.33  ? 1226 ILE A C     1 
ATOM   7692  O  O     . ILE A 1 1226 ? 169.316 182.493 111.795 1.00 66.11  ? 1226 ILE A O     1 
ATOM   7693  C  CB    . ILE A 1 1226 ? 168.156 180.757 114.272 1.00 53.59  ? 1226 ILE A CB    1 
ATOM   7694  C  CG1   . ILE A 1 1226 ? 168.318 179.501 115.128 1.00 49.14  ? 1226 ILE A CG1   1 
ATOM   7695  C  CG2   . ILE A 1 1226 ? 167.332 180.429 113.042 1.00 53.68  ? 1226 ILE A CG2   1 
ATOM   7696  C  CD1   . ILE A 1 1226 ? 169.105 178.408 114.456 1.00 47.63  ? 1226 ILE A CD1   1 
ATOM   7697  N  N     . LEU A 1 1227 ? 169.325 183.754 113.651 1.00 63.32  ? 1227 LEU A N     1 
ATOM   7698  C  CA    . LEU A 1 1227 ? 169.259 185.028 112.953 1.00 60.69  ? 1227 LEU A CA    1 
ATOM   7699  C  C     . LEU A 1 1227 ? 170.301 185.961 113.547 1.00 63.89  ? 1227 LEU A C     1 
ATOM   7700  O  O     . LEU A 1 1227 ? 170.493 185.988 114.766 1.00 68.55  ? 1227 LEU A O     1 
ATOM   7701  C  CB    . LEU A 1 1227 ? 167.866 185.654 113.058 1.00 59.68  ? 1227 LEU A CB    1 
ATOM   7702  C  CG    . LEU A 1 1227 ? 166.721 184.926 112.350 1.00 56.32  ? 1227 LEU A CG    1 
ATOM   7703  C  CD1   . LEU A 1 1227 ? 165.399 185.582 112.692 1.00 45.63  ? 1227 LEU A CD1   1 
ATOM   7704  C  CD2   . LEU A 1 1227 ? 166.930 184.902 110.845 1.00 54.15  ? 1227 LEU A CD2   1 
ATOM   7705  N  N     . GLU A 1 1228 ? 170.973 186.725 112.688 1.00 63.42  ? 1228 GLU A N     1 
ATOM   7706  C  CA    . GLU A 1 1228 ? 172.115 187.530 113.108 1.00 65.03  ? 1228 GLU A CA    1 
ATOM   7707  C  C     . GLU A 1 1228 ? 172.021 188.918 112.493 1.00 64.57  ? 1228 GLU A C     1 
ATOM   7708  O  O     . GLU A 1 1228 ? 172.010 189.054 111.267 1.00 69.35  ? 1228 GLU A O     1 
ATOM   7709  C  CB    . GLU A 1 1228 ? 173.427 186.853 112.702 1.00 71.10  ? 1228 GLU A CB    1 
ATOM   7710  C  CG    . GLU A 1 1228 ? 173.616 185.470 113.304 1.00 76.83  ? 1228 GLU A CG    1 
ATOM   7711  C  CD    . GLU A 1 1228 ? 174.788 184.723 112.704 1.00 87.83  ? 1228 GLU A CD    1 
ATOM   7712  O  OE1   . GLU A 1 1228 ? 175.554 185.335 111.933 1.00 89.13  ? 1228 GLU A OE1   1 
ATOM   7713  O  OE2   . GLU A 1 1228 ? 174.937 183.519 113.000 1.00 88.37  ? 1228 GLU A OE2   1 
ATOM   7714  N  N     . ASN A 1 1229 ? 171.966 189.941 113.350 1.00 61.89  ? 1229 ASN A N     1 
ATOM   7715  C  CA    . ASN A 1 1229 ? 172.024 191.346 112.936 1.00 62.80  ? 1229 ASN A CA    1 
ATOM   7716  C  C     . ASN A 1 1229 ? 170.914 191.695 111.944 1.00 63.02  ? 1229 ASN A C     1 
ATOM   7717  O  O     . ASN A 1 1229 ? 171.163 192.182 110.840 1.00 67.58  ? 1229 ASN A O     1 
ATOM   7718  C  CB    . ASN A 1 1229 ? 173.401 191.687 112.364 1.00 66.73  ? 1229 ASN A CB    1 
ATOM   7719  C  CG    . ASN A 1 1229 ? 174.464 191.801 113.439 1.00 70.44  ? 1229 ASN A CG    1 
ATOM   7720  O  OD1   . ASN A 1 1229 ? 174.959 192.891 113.725 1.00 68.51  ? 1229 ASN A OD1   1 
ATOM   7721  N  ND2   . ASN A 1 1229 ? 174.815 190.674 114.047 1.00 69.24  ? 1229 ASN A ND2   1 
ATOM   7722  N  N     . ILE A 1 1230 ? 169.675 191.442 112.354 1.00 60.75  ? 1230 ILE A N     1 
ATOM   7723  C  CA    . ILE A 1 1230 ? 168.506 191.768 111.543 1.00 58.16  ? 1230 ILE A CA    1 
ATOM   7724  C  C     . ILE A 1 1230 ? 168.102 193.211 111.816 1.00 56.51  ? 1230 ILE A C     1 
ATOM   7725  O  O     . ILE A 1 1230 ? 168.054 193.646 112.972 1.00 60.00  ? 1230 ILE A O     1 
ATOM   7726  C  CB    . ILE A 1 1230 ? 167.350 190.796 111.837 1.00 55.29  ? 1230 ILE A CB    1 
ATOM   7727  C  CG1   . ILE A 1 1230 ? 167.452 189.532 110.976 1.00 57.01  ? 1230 ILE A CG1   1 
ATOM   7728  C  CG2   . ILE A 1 1230 ? 166.006 191.461 111.610 1.00 52.74  ? 1230 ILE A CG2   1 
ATOM   7729  C  CD1   . ILE A 1 1230 ? 168.720 188.736 111.150 1.00 59.52  ? 1230 ILE A CD1   1 
ATOM   7730  N  N     . SER A 1 1231 ? 167.830 193.968 110.752 1.00 55.03  ? 1231 SER A N     1 
ATOM   7731  C  CA    . SER A 1 1231 ? 167.404 195.354 110.900 1.00 55.34  ? 1231 SER A CA    1 
ATOM   7732  C  C     . SER A 1 1231 ? 166.479 195.740 109.756 1.00 55.41  ? 1231 SER A C     1 
ATOM   7733  O  O     . SER A 1 1231 ? 166.832 195.561 108.588 1.00 57.51  ? 1231 SER A O     1 
ATOM   7734  C  CB    . SER A 1 1231 ? 168.610 196.295 110.938 1.00 55.71  ? 1231 SER A CB    1 
ATOM   7735  O  OG    . SER A 1 1231 ? 168.191 197.640 111.080 1.00 59.76  ? 1231 SER A OG    1 
ATOM   7736  N  N     . PHE A 1 1232 ? 165.307 196.276 110.097 1.00 52.61  ? 1232 PHE A N     1 
ATOM   7737  C  CA    . PHE A 1 1232 ? 164.343 196.739 109.106 1.00 52.42  ? 1232 PHE A CA    1 
ATOM   7738  C  C     . PHE A 1 1232 ? 163.300 197.605 109.803 1.00 53.66  ? 1232 PHE A C     1 
ATOM   7739  O  O     . PHE A 1 1232 ? 163.253 197.686 111.032 1.00 52.66  ? 1232 PHE A O     1 
ATOM   7740  C  CB    . PHE A 1 1232 ? 163.696 195.564 108.358 1.00 51.42  ? 1232 PHE A CB    1 
ATOM   7741  C  CG    . PHE A 1 1232 ? 162.960 194.595 109.245 1.00 46.37  ? 1232 PHE A CG    1 
ATOM   7742  C  CD1   . PHE A 1 1232 ? 161.682 194.877 109.698 1.00 49.11  ? 1232 PHE A CD1   1 
ATOM   7743  C  CD2   . PHE A 1 1232 ? 163.545 193.399 109.618 1.00 44.90  ? 1232 PHE A CD2   1 
ATOM   7744  C  CE1   . PHE A 1 1232 ? 161.007 193.990 110.508 1.00 50.26  ? 1232 PHE A CE1   1 
ATOM   7745  C  CE2   . PHE A 1 1232 ? 162.872 192.508 110.427 1.00 46.59  ? 1232 PHE A CE2   1 
ATOM   7746  C  CZ    . PHE A 1 1232 ? 161.603 192.804 110.872 1.00 49.22  ? 1232 PHE A CZ    1 
ATOM   7747  N  N     . SER A 1 1233 ? 162.467 198.261 108.996 1.00 53.18  ? 1233 SER A N     1 
ATOM   7748  C  CA    . SER A 1 1233 ? 161.417 199.139 109.491 1.00 51.87  ? 1233 SER A CA    1 
ATOM   7749  C  C     . SER A 1 1233 ? 160.114 198.859 108.758 1.00 56.90  ? 1233 SER A C     1 
ATOM   7750  O  O     . SER A 1 1233 ? 160.115 198.431 107.601 1.00 62.17  ? 1233 SER A O     1 
ATOM   7751  C  CB    . SER A 1 1233 ? 161.795 200.613 109.326 1.00 51.97  ? 1233 SER A CB    1 
ATOM   7752  O  OG    . SER A 1 1233 ? 160.803 201.455 109.883 1.00 57.74  ? 1233 SER A OG    1 
ATOM   7753  N  N     . ILE A 1 1234 ? 158.998 199.105 109.443 1.00 57.39  ? 1234 ILE A N     1 
ATOM   7754  C  CA    . ILE A 1 1234 ? 157.663 198.871 108.901 1.00 59.12  ? 1234 ILE A CA    1 
ATOM   7755  C  C     . ILE A 1 1234 ? 156.822 200.124 109.106 1.00 60.93  ? 1234 ILE A C     1 
ATOM   7756  O  O     . ILE A 1 1234 ? 156.753 200.655 110.220 1.00 61.11  ? 1234 ILE A O     1 
ATOM   7757  C  CB    . ILE A 1 1234 ? 156.989 197.653 109.560 1.00 59.95  ? 1234 ILE A CB    1 
ATOM   7758  C  CG1   . ILE A 1 1234 ? 157.684 196.362 109.131 1.00 60.82  ? 1234 ILE A CG1   1 
ATOM   7759  C  CG2   . ILE A 1 1234 ? 155.517 197.600 109.212 1.00 54.69  ? 1234 ILE A CG2   1 
ATOM   7760  C  CD1   . ILE A 1 1234 ? 157.267 195.150 109.929 1.00 58.06  ? 1234 ILE A CD1   1 
ATOM   7761  N  N     . SER A 1 1235 ? 156.187 200.594 108.035 1.00 64.67  ? 1235 SER A N     1 
ATOM   7762  C  CA    . SER A 1 1235 ? 155.295 201.738 108.130 1.00 69.20  ? 1235 SER A CA    1 
ATOM   7763  C  C     . SER A 1 1235 ? 153.968 201.323 108.767 1.00 69.06  ? 1235 SER A C     1 
ATOM   7764  O  O     . SER A 1 1235 ? 153.568 200.160 108.681 1.00 71.87  ? 1235 SER A O     1 
ATOM   7765  C  CB    . SER A 1 1235 ? 155.048 202.332 106.746 1.00 71.34  ? 1235 SER A CB    1 
ATOM   7766  O  OG    . SER A 1 1235 ? 154.240 201.473 105.962 1.00 74.65  ? 1235 SER A OG    1 
ATOM   7767  N  N     . PRO A 1 1236 ? 153.268 202.254 109.416 1.00 68.27  ? 1236 PRO A N     1 
ATOM   7768  C  CA    . PRO A 1 1236 ? 151.997 201.902 110.061 1.00 68.81  ? 1236 PRO A CA    1 
ATOM   7769  C  C     . PRO A 1 1236 ? 150.930 201.520 109.045 1.00 69.78  ? 1236 PRO A C     1 
ATOM   7770  O  O     . PRO A 1 1236 ? 150.732 202.204 108.039 1.00 72.38  ? 1236 PRO A O     1 
ATOM   7771  C  CB    . PRO A 1 1236 ? 151.622 203.180 110.821 1.00 71.19  ? 1236 PRO A CB    1 
ATOM   7772  C  CG    . PRO A 1 1236 ? 152.280 204.267 110.062 1.00 72.47  ? 1236 PRO A CG    1 
ATOM   7773  C  CD    . PRO A 1 1236 ? 153.574 203.687 109.558 1.00 69.60  ? 1236 PRO A CD    1 
ATOM   7774  N  N     . GLY A 1 1237 ? 150.235 200.418 109.323 1.00 67.39  ? 1237 GLY A N     1 
ATOM   7775  C  CA    . GLY A 1 1237 ? 149.146 199.964 108.478 1.00 65.92  ? 1237 GLY A CA    1 
ATOM   7776  C  C     . GLY A 1 1237 ? 149.584 199.405 107.141 1.00 69.16  ? 1237 GLY A C     1 
ATOM   7777  O  O     . GLY A 1 1237 ? 149.055 199.793 106.096 1.00 71.02  ? 1237 GLY A O     1 
ATOM   7778  N  N     . GLN A 1 1238 ? 150.551 198.493 107.159 1.00 67.10  ? 1238 GLN A N     1 
ATOM   7779  C  CA    . GLN A 1 1238 ? 151.108 197.923 105.943 1.00 66.90  ? 1238 GLN A CA    1 
ATOM   7780  C  C     . GLN A 1 1238 ? 151.120 196.404 106.038 1.00 62.58  ? 1238 GLN A C     1 
ATOM   7781  O  O     . GLN A 1 1238 ? 151.428 195.845 107.093 1.00 62.01  ? 1238 GLN A O     1 
ATOM   7782  C  CB    . GLN A 1 1238 ? 152.527 198.451 105.702 1.00 66.32  ? 1238 GLN A CB    1 
ATOM   7783  C  CG    . GLN A 1 1238 ? 153.223 197.875 104.489 1.00 68.59  ? 1238 GLN A CG    1 
ATOM   7784  C  CD    . GLN A 1 1238 ? 154.209 198.848 103.881 1.00 74.21  ? 1238 GLN A CD    1 
ATOM   7785  O  OE1   . GLN A 1 1238 ? 155.411 198.590 103.842 1.00 73.50  ? 1238 GLN A OE1   1 
ATOM   7786  N  NE2   . GLN A 1 1238 ? 153.703 199.978 103.404 1.00 75.12  ? 1238 GLN A NE2   1 
ATOM   7787  N  N     . ARG A 1 1239 ? 150.772 195.741 104.936 1.00 60.43  ? 1239 ARG A N     1 
ATOM   7788  C  CA    . ARG A 1 1239 ? 150.879 194.288 104.852 1.00 56.51  ? 1239 ARG A CA    1 
ATOM   7789  C  C     . ARG A 1 1239 ? 152.277 193.911 104.378 1.00 57.30  ? 1239 ARG A C     1 
ATOM   7790  O  O     . ARG A 1 1239 ? 152.743 194.404 103.346 1.00 62.97  ? 1239 ARG A O     1 
ATOM   7791  C  CB    . ARG A 1 1239 ? 149.819 193.717 103.915 1.00 59.50  ? 1239 ARG A CB    1 
ATOM   7792  C  CG    . ARG A 1 1239 ? 148.426 193.680 104.509 1.00 62.84  ? 1239 ARG A CG    1 
ATOM   7793  C  CD    . ARG A 1 1239 ? 147.354 193.746 103.436 1.00 67.35  ? 1239 ARG A CD    1 
ATOM   7794  N  NE    . ARG A 1 1239 ? 146.025 193.915 104.012 1.00 72.31  ? 1239 ARG A NE    1 
ATOM   7795  C  CZ    . ARG A 1 1239 ? 145.593 195.027 104.592 1.00 76.92  ? 1239 ARG A CZ    1 
ATOM   7796  N  NH1   . ARG A 1 1239 ? 146.351 196.109 104.665 1.00 74.81  ? 1239 ARG A NH1   1 
ATOM   7797  N  NH2   . ARG A 1 1239 ? 144.369 195.055 105.110 1.00 69.79  ? 1239 ARG A NH2   1 
ATOM   7798  N  N     . VAL A 1 1240 ? 152.944 193.040 105.131 1.00 49.74  ? 1240 VAL A N     1 
ATOM   7799  C  CA    . VAL A 1 1240 ? 154.318 192.639 104.859 1.00 49.30  ? 1240 VAL A CA    1 
ATOM   7800  C  C     . VAL A 1 1240 ? 154.352 191.128 104.675 1.00 49.49  ? 1240 VAL A C     1 
ATOM   7801  O  O     . VAL A 1 1240 ? 153.816 190.386 105.505 1.00 49.30  ? 1240 VAL A O     1 
ATOM   7802  C  CB    . VAL A 1 1240 ? 155.267 193.077 105.988 1.00 50.21  ? 1240 VAL A CB    1 
ATOM   7803  C  CG1   . VAL A 1 1240 ? 156.695 192.684 105.665 1.00 54.17  ? 1240 VAL A CG1   1 
ATOM   7804  C  CG2   . VAL A 1 1240 ? 155.163 194.571 106.216 1.00 56.30  ? 1240 VAL A CG2   1 
ATOM   7805  N  N     . GLY A 1 1241 ? 154.968 190.678 103.583 1.00 49.32  ? 1241 GLY A N     1 
ATOM   7806  C  CA    . GLY A 1 1241 ? 155.085 189.259 103.305 1.00 47.54  ? 1241 GLY A CA    1 
ATOM   7807  C  C     . GLY A 1 1241 ? 156.424 188.705 103.747 1.00 47.44  ? 1241 GLY A C     1 
ATOM   7808  O  O     . GLY A 1 1241 ? 157.475 189.265 103.427 1.00 50.99  ? 1241 GLY A O     1 
ATOM   7809  N  N     . LEU A 1 1242 ? 156.380 187.603 104.488 1.00 46.47  ? 1242 LEU A N     1 
ATOM   7810  C  CA    . LEU A 1 1242 ? 157.570 186.923 104.988 1.00 45.15  ? 1242 LEU A CA    1 
ATOM   7811  C  C     . LEU A 1 1242 ? 157.628 185.539 104.354 1.00 44.75  ? 1242 LEU A C     1 
ATOM   7812  O  O     . LEU A 1 1242 ? 156.787 184.684 104.647 1.00 44.64  ? 1242 LEU A O     1 
ATOM   7813  C  CB    . LEU A 1 1242 ? 157.537 186.836 106.513 1.00 43.77  ? 1242 LEU A CB    1 
ATOM   7814  C  CG    . LEU A 1 1242 ? 158.646 186.066 107.232 1.00 43.17  ? 1242 LEU A CG    1 
ATOM   7815  C  CD1   . LEU A 1 1242 ? 160.011 186.651 106.920 1.00 41.95  ? 1242 LEU A CD1   1 
ATOM   7816  C  CD2   . LEU A 1 1242 ? 158.393 186.054 108.727 1.00 37.80  ? 1242 LEU A CD2   1 
ATOM   7817  N  N     . LEU A 1 1243 ? 158.618 185.316 103.494 1.00 46.10  ? 1243 LEU A N     1 
ATOM   7818  C  CA    . LEU A 1 1243 ? 158.719 184.081 102.730 1.00 46.51  ? 1243 LEU A CA    1 
ATOM   7819  C  C     . LEU A 1 1243 ? 160.143 183.543 102.786 1.00 42.75  ? 1243 LEU A C     1 
ATOM   7820  O  O     . LEU A 1 1243 ? 161.093 184.261 103.102 1.00 46.77  ? 1243 LEU A O     1 
ATOM   7821  C  CB    . LEU A 1 1243 ? 158.279 184.289 101.274 1.00 44.84  ? 1243 LEU A CB    1 
ATOM   7822  C  CG    . LEU A 1 1243 ? 159.078 185.253 100.396 1.00 46.16  ? 1243 LEU A CG    1 
ATOM   7823  C  CD1   . LEU A 1 1243 ? 158.967 184.838 98.945  1.00 52.92  ? 1243 LEU A CD1   1 
ATOM   7824  C  CD2   . LEU A 1 1243 ? 158.584 186.674 100.567 1.00 49.92  ? 1243 LEU A CD2   1 
ATOM   7825  N  N     . GLY A 1 1244 ? 160.279 182.265 102.471 1.00 42.42  ? 1244 GLY A N     1 
ATOM   7826  C  CA    . GLY A 1 1244 ? 161.568 181.604 102.519 1.00 40.45  ? 1244 GLY A CA    1 
ATOM   7827  C  C     . GLY A 1 1244 ? 161.409 180.103 102.511 1.00 42.39  ? 1244 GLY A C     1 
ATOM   7828  O  O     . GLY A 1 1244 ? 160.302 179.566 102.532 1.00 49.04  ? 1244 GLY A O     1 
ATOM   7829  N  N     . ARG A 1 1245 ? 162.552 179.424 102.476 1.00 38.15  ? 1245 ARG A N     1 
ATOM   7830  C  CA    . ARG A 1 1245 ? 162.564 177.971 102.420 1.00 37.70  ? 1245 ARG A CA    1 
ATOM   7831  C  C     . ARG A 1 1245 ? 162.120 177.371 103.753 1.00 38.85  ? 1245 ARG A C     1 
ATOM   7832  O  O     . ARG A 1 1245 ? 162.126 178.028 104.796 1.00 40.36  ? 1245 ARG A O     1 
ATOM   7833  C  CB    . ARG A 1 1245 ? 163.959 177.457 102.062 1.00 39.96  ? 1245 ARG A CB    1 
ATOM   7834  C  CG    . ARG A 1 1245 ? 163.983 176.013 101.589 1.00 44.46  ? 1245 ARG A CG    1 
ATOM   7835  C  CD    . ARG A 1 1245 ? 165.388 175.525 101.310 1.00 46.94  ? 1245 ARG A CD    1 
ATOM   7836  N  NE    . ARG A 1 1245 ? 165.403 174.106 100.978 1.00 46.27  ? 1245 ARG A NE    1 
ATOM   7837  C  CZ    . ARG A 1 1245 ? 165.407 173.126 101.871 1.00 43.63  ? 1245 ARG A CZ    1 
ATOM   7838  N  NH1   . ARG A 1 1245 ? 165.393 173.374 103.169 1.00 39.86  ? 1245 ARG A NH1   1 
ATOM   7839  N  NH2   . ARG A 1 1245 ? 165.422 171.866 101.450 1.00 41.38  ? 1245 ARG A NH2   1 
ATOM   7840  N  N     . THR A 1 1246 ? 161.721 176.102 103.701 1.00 38.93  ? 1246 THR A N     1 
ATOM   7841  C  CA    . THR A 1 1246 ? 161.409 175.353 104.910 1.00 36.97  ? 1246 THR A CA    1 
ATOM   7842  C  C     . THR A 1 1246 ? 162.631 175.268 105.815 1.00 34.34  ? 1246 THR A C     1 
ATOM   7843  O  O     . THR A 1 1246 ? 163.731 174.940 105.364 1.00 37.94  ? 1246 THR A O     1 
ATOM   7844  C  CB    . THR A 1 1246 ? 160.929 173.947 104.545 1.00 36.10  ? 1246 THR A CB    1 
ATOM   7845  O  OG1   . THR A 1 1246 ? 159.808 174.035 103.659 1.00 36.04  ? 1246 THR A OG1   1 
ATOM   7846  C  CG2   . THR A 1 1246 ? 160.523 173.180 105.783 1.00 36.72  ? 1246 THR A CG2   1 
ATOM   7847  N  N     . GLY A 1 1247 ? 162.435 175.563 107.096 1.00 32.08  ? 1247 GLY A N     1 
ATOM   7848  C  CA    . GLY A 1 1247 ? 163.519 175.511 108.054 1.00 28.89  ? 1247 GLY A CA    1 
ATOM   7849  C  C     . GLY A 1 1247 ? 164.465 176.685 108.012 1.00 32.74  ? 1247 GLY A C     1 
ATOM   7850  O  O     . GLY A 1 1247 ? 165.515 176.640 108.655 1.00 34.82  ? 1247 GLY A O     1 
ATOM   7851  N  N     . SER A 1 1248 ? 164.125 177.743 107.276 1.00 34.22  ? 1248 SER A N     1 
ATOM   7852  C  CA    . SER A 1 1248 ? 165.009 178.898 107.175 1.00 32.27  ? 1248 SER A CA    1 
ATOM   7853  C  C     . SER A 1 1248 ? 164.959 179.785 108.414 1.00 34.11  ? 1248 SER A C     1 
ATOM   7854  O  O     . SER A 1 1248 ? 165.968 180.409 108.758 1.00 39.44  ? 1248 SER A O     1 
ATOM   7855  C  CB    . SER A 1 1248 ? 164.666 179.710 105.926 1.00 35.24  ? 1248 SER A CB    1 
ATOM   7856  O  OG    . SER A 1 1248 ? 163.443 180.403 106.083 1.00 43.56  ? 1248 SER A OG    1 
ATOM   7857  N  N     . GLY A 1 1249 ? 163.819 179.858 109.098 1.00 32.19  ? 1249 GLY A N     1 
ATOM   7858  C  CA    . GLY A 1 1249 ? 163.729 180.670 110.296 1.00 30.50  ? 1249 GLY A CA    1 
ATOM   7859  C  C     . GLY A 1 1249 ? 162.617 181.700 110.301 1.00 31.72  ? 1249 GLY A C     1 
ATOM   7860  O  O     . GLY A 1 1249 ? 162.736 182.737 110.957 1.00 31.93  ? 1249 GLY A O     1 
ATOM   7861  N  N     . LYS A 1 1250 ? 161.537 181.435 109.561 1.00 34.83  ? 1250 LYS A N     1 
ATOM   7862  C  CA    . LYS A 1 1250 ? 160.397 182.348 109.549 1.00 30.99  ? 1250 LYS A CA    1 
ATOM   7863  C  C     . LYS A 1 1250 ? 159.666 182.358 110.887 1.00 30.52  ? 1250 LYS A C     1 
ATOM   7864  O  O     . LYS A 1 1250 ? 159.220 183.413 111.348 1.00 34.15  ? 1250 LYS A O     1 
ATOM   7865  C  CB    . LYS A 1 1250 ? 159.443 181.975 108.418 1.00 30.65  ? 1250 LYS A CB    1 
ATOM   7866  C  CG    . LYS A 1 1250 ? 160.075 182.037 107.046 1.00 32.46  ? 1250 LYS A CG    1 
ATOM   7867  C  CD    . LYS A 1 1250 ? 159.053 181.771 105.961 1.00 38.15  ? 1250 LYS A CD    1 
ATOM   7868  C  CE    . LYS A 1 1250 ? 158.391 180.424 106.156 1.00 34.89  ? 1250 LYS A CE    1 
ATOM   7869  N  NZ    . LYS A 1 1250 ? 159.369 179.311 106.058 1.00 35.56  ? 1250 LYS A NZ    1 
ATOM   7870  N  N     . SER A 1 1251 ? 159.508 181.191 111.513 1.00 30.13  ? 1251 SER A N     1 
ATOM   7871  C  CA    . SER A 1 1251 ? 158.842 181.136 112.810 1.00 26.41  ? 1251 SER A CA    1 
ATOM   7872  C  C     . SER A 1 1251 ? 159.720 181.702 113.917 1.00 28.94  ? 1251 SER A C     1 
ATOM   7873  O  O     . SER A 1 1251 ? 159.203 182.213 114.917 1.00 33.77  ? 1251 SER A O     1 
ATOM   7874  C  CB    . SER A 1 1251 ? 158.447 179.699 113.139 1.00 27.75  ? 1251 SER A CB    1 
ATOM   7875  O  OG    . SER A 1 1251 ? 157.249 179.339 112.479 1.00 32.74  ? 1251 SER A OG    1 
ATOM   7876  N  N     . THR A 1 1252 ? 161.042 181.616 113.758 1.00 32.10  ? 1252 THR A N     1 
ATOM   7877  C  CA    . THR A 1 1252 ? 161.957 182.148 114.763 1.00 31.77  ? 1252 THR A CA    1 
ATOM   7878  C  C     . THR A 1 1252 ? 161.829 183.661 114.884 1.00 32.51  ? 1252 THR A C     1 
ATOM   7879  O  O     . THR A 1 1252 ? 161.884 184.204 115.990 1.00 34.83  ? 1252 THR A O     1 
ATOM   7880  C  CB    . THR A 1 1252 ? 163.391 181.751 114.421 1.00 32.44  ? 1252 THR A CB    1 
ATOM   7881  O  OG1   . THR A 1 1252 ? 163.501 180.324 114.429 1.00 34.91  ? 1252 THR A OG1   1 
ATOM   7882  C  CG2   . THR A 1 1252 ? 164.362 182.321 115.433 1.00 35.83  ? 1252 THR A CG2   1 
ATOM   7883  N  N     . LEU A 1 1253 ? 161.647 184.360 113.762 1.00 32.71  ? 1253 LEU A N     1 
ATOM   7884  C  CA    . LEU A 1 1253 ? 161.473 185.809 113.809 1.00 30.68  ? 1253 LEU A CA    1 
ATOM   7885  C  C     . LEU A 1 1253 ? 160.191 186.192 114.544 1.00 35.34  ? 1253 LEU A C     1 
ATOM   7886  O  O     . LEU A 1 1253 ? 160.189 187.117 115.370 1.00 38.41  ? 1253 LEU A O     1 
ATOM   7887  C  CB    . LEU A 1 1253 ? 161.472 186.371 112.389 1.00 30.30  ? 1253 LEU A CB    1 
ATOM   7888  C  CG    . LEU A 1 1253 ? 161.414 187.885 112.190 1.00 36.18  ? 1253 LEU A CG    1 
ATOM   7889  C  CD1   . LEU A 1 1253 ? 162.620 188.560 112.815 1.00 38.96  ? 1253 LEU A CD1   1 
ATOM   7890  C  CD2   . LEU A 1 1253 ? 161.322 188.222 110.714 1.00 38.86  ? 1253 LEU A CD2   1 
ATOM   7891  N  N     . LEU A 1 1254 ? 159.094 185.483 114.266 1.00 34.32  ? 1254 LEU A N     1 
ATOM   7892  C  CA    . LEU A 1 1254 ? 157.833 185.772 114.939 1.00 31.02  ? 1254 LEU A CA    1 
ATOM   7893  C  C     . LEU A 1 1254 ? 157.903 185.450 116.423 1.00 32.97  ? 1254 LEU A C     1 
ATOM   7894  O  O     . LEU A 1 1254 ? 157.299 186.156 117.236 1.00 34.91  ? 1254 LEU A O     1 
ATOM   7895  C  CB    . LEU A 1 1254 ? 156.693 184.996 114.283 1.00 30.10  ? 1254 LEU A CB    1 
ATOM   7896  C  CG    . LEU A 1 1254 ? 156.370 185.368 112.837 1.00 34.40  ? 1254 LEU A CG    1 
ATOM   7897  C  CD1   . LEU A 1 1254 ? 155.350 184.409 112.255 1.00 34.54  ? 1254 LEU A CD1   1 
ATOM   7898  C  CD2   . LEU A 1 1254 ? 155.882 186.802 112.744 1.00 35.59  ? 1254 LEU A CD2   1 
ATOM   7899  N  N     . SER A 1 1255 ? 158.624 184.391 116.798 1.00 33.90  ? 1255 SER A N     1 
ATOM   7900  C  CA    . SER A 1 1255 ? 158.851 184.130 118.215 1.00 32.58  ? 1255 SER A CA    1 
ATOM   7901  C  C     . SER A 1 1255 ? 159.755 185.187 118.837 1.00 33.73  ? 1255 SER A C     1 
ATOM   7902  O  O     . SER A 1 1255 ? 159.647 185.465 120.034 1.00 35.64  ? 1255 SER A O     1 
ATOM   7903  C  CB    . SER A 1 1255 ? 159.449 182.737 118.409 1.00 33.63  ? 1255 SER A CB    1 
ATOM   7904  O  OG    . SER A 1 1255 ? 158.464 181.736 118.232 1.00 39.19  ? 1255 SER A OG    1 
ATOM   7905  N  N     . ALA A 1 1256 ? 160.658 185.773 118.047 1.00 34.65  ? 1256 ALA A N     1 
ATOM   7906  C  CA    . ALA A 1 1256 ? 161.529 186.826 118.556 1.00 33.86  ? 1256 ALA A CA    1 
ATOM   7907  C  C     . ALA A 1 1256 ? 160.769 188.122 118.798 1.00 36.80  ? 1256 ALA A C     1 
ATOM   7908  O  O     . ALA A 1 1256 ? 161.146 188.900 119.681 1.00 39.65  ? 1256 ALA A O     1 
ATOM   7909  C  CB    . ALA A 1 1256 ? 162.688 187.067 117.590 1.00 33.82  ? 1256 ALA A CB    1 
ATOM   7910  N  N     . PHE A 1 1257 ? 159.712 188.382 118.025 1.00 36.39  ? 1257 PHE A N     1 
ATOM   7911  C  CA    . PHE A 1 1257 ? 158.888 189.557 118.301 1.00 34.57  ? 1257 PHE A CA    1 
ATOM   7912  C  C     . PHE A 1 1257 ? 158.240 189.467 119.678 1.00 37.54  ? 1257 PHE A C     1 
ATOM   7913  O  O     . PHE A 1 1257 ? 158.120 190.474 120.383 1.00 43.80  ? 1257 PHE A O     1 
ATOM   7914  C  CB    . PHE A 1 1257 ? 157.816 189.731 117.227 1.00 34.80  ? 1257 PHE A CB    1 
ATOM   7915  C  CG    . PHE A 1 1257 ? 158.346 190.203 115.911 1.00 42.62  ? 1257 PHE A CG    1 
ATOM   7916  C  CD1   . PHE A 1 1257 ? 159.304 191.197 115.854 1.00 47.94  ? 1257 PHE A CD1   1 
ATOM   7917  C  CD2   . PHE A 1 1257 ? 157.872 189.668 114.729 1.00 45.31  ? 1257 PHE A CD2   1 
ATOM   7918  C  CE1   . PHE A 1 1257 ? 159.792 191.636 114.643 1.00 49.27  ? 1257 PHE A CE1   1 
ATOM   7919  C  CE2   . PHE A 1 1257 ? 158.351 190.105 113.513 1.00 44.84  ? 1257 PHE A CE2   1 
ATOM   7920  C  CZ    . PHE A 1 1257 ? 159.313 191.091 113.469 1.00 47.99  ? 1257 PHE A CZ    1 
ATOM   7921  N  N     . LEU A 1 1258 ? 157.816 188.271 120.075 1.00 35.61  ? 1258 LEU A N     1 
ATOM   7922  C  CA    . LEU A 1 1258 ? 157.156 188.059 121.355 1.00 32.77  ? 1258 LEU A CA    1 
ATOM   7923  C  C     . LEU A 1 1258 ? 158.122 187.759 122.493 1.00 36.22  ? 1258 LEU A C     1 
ATOM   7924  O  O     . LEU A 1 1258 ? 157.676 187.606 123.633 1.00 39.11  ? 1258 LEU A O     1 
ATOM   7925  C  CB    . LEU A 1 1258 ? 156.144 186.918 121.235 1.00 34.58  ? 1258 LEU A CB    1 
ATOM   7926  C  CG    . LEU A 1 1258 ? 154.955 187.174 120.311 1.00 38.24  ? 1258 LEU A CG    1 
ATOM   7927  C  CD1   . LEU A 1 1258 ? 154.122 185.918 120.147 1.00 32.41  ? 1258 LEU A CD1   1 
ATOM   7928  C  CD2   . LEU A 1 1258 ? 154.110 188.301 120.870 1.00 37.35  ? 1258 LEU A CD2   1 
ATOM   7929  N  N     . ARG A 1 1259 ? 159.423 187.674 122.211 1.00 37.98  ? 1259 ARG A N     1 
ATOM   7930  C  CA    . ARG A 1 1259 ? 160.444 187.344 123.209 1.00 38.57  ? 1259 ARG A CA    1 
ATOM   7931  C  C     . ARG A 1 1259 ? 160.184 185.981 123.843 1.00 39.67  ? 1259 ARG A C     1 
ATOM   7932  O  O     . ARG A 1 1259 ? 160.258 185.817 125.061 1.00 41.98  ? 1259 ARG A O     1 
ATOM   7933  C  CB    . ARG A 1 1259 ? 160.561 188.422 124.287 1.00 36.01  ? 1259 ARG A CB    1 
ATOM   7934  C  CG    . ARG A 1 1259 ? 160.582 189.828 123.754 1.00 42.70  ? 1259 ARG A CG    1 
ATOM   7935  C  CD    . ARG A 1 1259 ? 160.996 190.811 124.826 1.00 43.84  ? 1259 ARG A CD    1 
ATOM   7936  N  NE    . ARG A 1 1259 ? 162.431 190.732 125.066 1.00 49.43  ? 1259 ARG A NE    1 
ATOM   7937  C  CZ    . ARG A 1 1259 ? 163.129 191.630 125.745 1.00 50.27  ? 1259 ARG A CZ    1 
ATOM   7938  N  NH1   . ARG A 1 1259 ? 162.554 192.699 126.269 1.00 53.10  ? 1259 ARG A NH1   1 
ATOM   7939  N  NH2   . ARG A 1 1259 ? 164.438 191.456 125.894 1.00 50.03  ? 1259 ARG A NH2   1 
ATOM   7940  N  N     . LEU A 1 1260 ? 159.874 184.995 123.008 1.00 34.81  ? 1260 LEU A N     1 
ATOM   7941  C  CA    . LEU A 1 1260 ? 159.731 183.623 123.467 1.00 34.57  ? 1260 LEU A CA    1 
ATOM   7942  C  C     . LEU A 1 1260 ? 161.050 182.865 123.466 1.00 41.68  ? 1260 LEU A C     1 
ATOM   7943  O  O     . LEU A 1 1260 ? 161.056 181.666 123.763 1.00 48.45  ? 1260 LEU A O     1 
ATOM   7944  C  CB    . LEU A 1 1260 ? 158.707 182.885 122.606 1.00 35.37  ? 1260 LEU A CB    1 
ATOM   7945  C  CG    . LEU A 1 1260 ? 157.248 183.291 122.804 1.00 35.18  ? 1260 LEU A CG    1 
ATOM   7946  C  CD1   . LEU A 1 1260 ? 156.394 182.761 121.673 1.00 37.79  ? 1260 LEU A CD1   1 
ATOM   7947  C  CD2   . LEU A 1 1260 ? 156.735 182.785 124.138 1.00 34.21  ? 1260 LEU A CD2   1 
ATOM   7948  N  N     . LEU A 1 1261 ? 162.157 183.524 123.136 1.00 41.90  ? 1261 LEU A N     1 
ATOM   7949  C  CA    . LEU A 1 1261 ? 163.466 182.889 123.140 1.00 44.12  ? 1261 LEU A CA    1 
ATOM   7950  C  C     . LEU A 1 1261 ? 164.516 183.915 123.539 1.00 47.76  ? 1261 LEU A C     1 
ATOM   7951  O  O     . LEU A 1 1261 ? 164.222 185.099 123.722 1.00 47.62  ? 1261 LEU A O     1 
ATOM   7952  C  CB    . LEU A 1 1261 ? 163.776 182.245 121.780 1.00 40.16  ? 1261 LEU A CB    1 
ATOM   7953  C  CG    . LEU A 1 1261 ? 163.579 182.998 120.458 1.00 40.39  ? 1261 LEU A CG    1 
ATOM   7954  C  CD1   . LEU A 1 1261 ? 164.526 184.171 120.281 1.00 45.01  ? 1261 LEU A CD1   1 
ATOM   7955  C  CD2   . LEU A 1 1261 ? 163.707 182.037 119.289 1.00 37.80  ? 1261 LEU A CD2   1 
ATOM   7956  N  N     . ASN A 1 1262 ? 165.752 183.442 123.684 1.00 50.96  ? 1262 ASN A N     1 
ATOM   7957  C  CA    . ASN A 1 1262 ? 166.867 184.308 124.057 1.00 50.27  ? 1262 ASN A CA    1 
ATOM   7958  C  C     . ASN A 1 1262 ? 167.145 185.283 122.923 1.00 48.85  ? 1262 ASN A C     1 
ATOM   7959  O  O     . ASN A 1 1262 ? 167.600 184.884 121.847 1.00 49.72  ? 1262 ASN A O     1 
ATOM   7960  C  CB    . ASN A 1 1262 ? 168.102 183.471 124.376 1.00 53.13  ? 1262 ASN A CB    1 
ATOM   7961  C  CG    . ASN A 1 1262 ? 167.862 182.487 125.499 1.00 58.11  ? 1262 ASN A CG    1 
ATOM   7962  O  OD1   . ASN A 1 1262 ? 167.442 182.864 126.593 1.00 58.03  ? 1262 ASN A OD1   1 
ATOM   7963  N  ND2   . ASN A 1 1262 ? 168.125 181.215 125.234 1.00 60.88  ? 1262 ASN A ND2   1 
ATOM   7964  N  N     . THR A 1 1263 ? 166.883 186.563 123.164 1.00 51.91  ? 1263 THR A N     1 
ATOM   7965  C  CA    . THR A 1 1263 ? 166.937 187.586 122.133 1.00 51.29  ? 1263 THR A CA    1 
ATOM   7966  C  C     . THR A 1 1263 ? 167.866 188.705 122.574 1.00 51.70  ? 1263 THR A C     1 
ATOM   7967  O  O     . THR A 1 1263 ? 167.935 189.032 123.762 1.00 53.89  ? 1263 THR A O     1 
ATOM   7968  C  CB    . THR A 1 1263 ? 165.539 188.158 121.847 1.00 54.09  ? 1263 THR A CB    1 
ATOM   7969  O  OG1   . THR A 1 1263 ? 164.592 187.090 121.733 1.00 51.40  ? 1263 THR A OG1   1 
ATOM   7970  C  CG2   . THR A 1 1263 ? 165.539 188.946 120.560 1.00 54.94  ? 1263 THR A CG2   1 
ATOM   7971  N  N     . GLU A 1 1264 ? 168.581 189.287 121.614 1.00 56.19  ? 1264 GLU A N     1 
ATOM   7972  C  CA    . GLU A 1 1264 ? 169.411 190.453 121.867 1.00 61.82  ? 1264 GLU A CA    1 
ATOM   7973  C  C     . GLU A 1 1264 ? 169.175 191.474 120.763 1.00 61.11  ? 1264 GLU A C     1 
ATOM   7974  O  O     . GLU A 1 1264 ? 169.083 191.123 119.585 1.00 62.29  ? 1264 GLU A O     1 
ATOM   7975  C  CB    . GLU A 1 1264 ? 170.895 190.080 121.944 1.00 64.81  ? 1264 GLU A CB    1 
ATOM   7976  C  CG    . GLU A 1 1264 ? 171.689 190.909 122.936 1.00 73.60  ? 1264 GLU A CG    1 
ATOM   7977  C  CD    . GLU A 1 1264 ? 173.101 190.398 123.120 1.00 91.25  ? 1264 GLU A CD    1 
ATOM   7978  O  OE1   . GLU A 1 1264 ? 173.955 191.171 123.604 1.00 96.83  ? 1264 GLU A OE1   1 
ATOM   7979  O  OE2   . GLU A 1 1264 ? 173.355 189.224 122.782 1.00 89.49  ? 1264 GLU A OE2   1 
ATOM   7980  N  N     . GLY A 1 1265 ? 169.096 192.744 121.152 1.00 56.95  ? 1265 GLY A N     1 
ATOM   7981  C  CA    . GLY A 1 1265 ? 168.773 193.797 120.208 1.00 54.25  ? 1265 GLY A CA    1 
ATOM   7982  C  C     . GLY A 1 1265 ? 167.693 194.739 120.699 1.00 56.30  ? 1265 GLY A C     1 
ATOM   7983  O  O     . GLY A 1 1265 ? 167.437 194.817 121.903 1.00 61.93  ? 1265 GLY A O     1 
ATOM   7984  N  N     . GLU A 1 1266 ? 167.052 195.461 119.780 1.00 52.78  ? 1266 GLU A N     1 
ATOM   7985  C  CA    . GLU A 1 1266 ? 166.099 196.504 120.142 1.00 53.66  ? 1266 GLU A CA    1 
ATOM   7986  C  C     . GLU A 1 1266 ? 164.918 196.488 119.184 1.00 51.58  ? 1266 GLU A C     1 
ATOM   7987  O  O     . GLU A 1 1266 ? 165.109 196.445 117.966 1.00 54.64  ? 1266 GLU A O     1 
ATOM   7988  C  CB    . GLU A 1 1266 ? 166.772 197.881 120.117 1.00 55.26  ? 1266 GLU A CB    1 
ATOM   7989  C  CG    . GLU A 1 1266 ? 165.971 198.982 120.781 1.00 55.77  ? 1266 GLU A CG    1 
ATOM   7990  C  CD    . GLU A 1 1266 ? 165.770 198.731 122.261 1.00 62.35  ? 1266 GLU A CD    1 
ATOM   7991  O  OE1   . GLU A 1 1266 ? 166.654 198.107 122.884 1.00 63.10  ? 1266 GLU A OE1   1 
ATOM   7992  O  OE2   . GLU A 1 1266 ? 164.732 199.161 122.805 1.00 59.28  ? 1266 GLU A OE2   1 
ATOM   7993  N  N     . ILE A 1 1267 ? 163.704 196.526 119.733 1.00 47.77  ? 1267 ILE A N     1 
ATOM   7994  C  CA    . ILE A 1 1267 ? 162.475 196.632 118.953 1.00 46.40  ? 1267 ILE A CA    1 
ATOM   7995  C  C     . ILE A 1 1267 ? 161.593 197.701 119.583 1.00 47.93  ? 1267 ILE A C     1 
ATOM   7996  O  O     . ILE A 1 1267 ? 161.371 197.689 120.799 1.00 48.60  ? 1267 ILE A O     1 
ATOM   7997  C  CB    . ILE A 1 1267 ? 161.718 195.292 118.868 1.00 44.40  ? 1267 ILE A CB    1 
ATOM   7998  C  CG1   . ILE A 1 1267 ? 162.629 194.189 118.336 1.00 45.38  ? 1267 ILE A CG1   1 
ATOM   7999  C  CG2   . ILE A 1 1267 ? 160.497 195.427 117.977 1.00 39.41  ? 1267 ILE A CG2   1 
ATOM   8000  C  CD1   . ILE A 1 1267 ? 161.944 192.857 118.190 1.00 45.65  ? 1267 ILE A CD1   1 
ATOM   8001  N  N     . GLN A 1 1268 ? 161.095 198.621 118.761 1.00 49.71  ? 1268 GLN A N     1 
ATOM   8002  C  CA    . GLN A 1 1268 ? 160.255 199.724 119.208 1.00 48.69  ? 1268 GLN A CA    1 
ATOM   8003  C  C     . GLN A 1 1268 ? 158.942 199.713 118.439 1.00 49.33  ? 1268 GLN A C     1 
ATOM   8004  O  O     . GLN A 1 1268 ? 158.936 199.500 117.223 1.00 55.76  ? 1268 GLN A O     1 
ATOM   8005  C  CB    . GLN A 1 1268 ? 160.965 201.061 119.006 1.00 47.17  ? 1268 GLN A CB    1 
ATOM   8006  C  CG    . GLN A 1 1268 ? 162.198 201.235 119.863 1.00 53.50  ? 1268 GLN A CG    1 
ATOM   8007  C  CD    . GLN A 1 1268 ? 162.946 202.508 119.543 1.00 57.16  ? 1268 GLN A CD    1 
ATOM   8008  O  OE1   . GLN A 1 1268 ? 162.496 203.319 118.735 1.00 54.56  ? 1268 GLN A OE1   1 
ATOM   8009  N  NE2   . GLN A 1 1268 ? 164.097 202.693 120.178 1.00 53.84  ? 1268 GLN A NE2   1 
ATOM   8010  N  N     . ILE A 1 1269 ? 157.836 199.939 119.142 1.00 45.99  ? 1269 ILE A N     1 
ATOM   8011  C  CA    . ILE A 1 1269 ? 156.527 200.107 118.521 1.00 48.97  ? 1269 ILE A CA    1 
ATOM   8012  C  C     . ILE A 1 1269 ? 156.011 201.488 118.896 1.00 52.90  ? 1269 ILE A C     1 
ATOM   8013  O  O     . ILE A 1 1269 ? 155.740 201.755 120.073 1.00 55.33  ? 1269 ILE A O     1 
ATOM   8014  C  CB    . ILE A 1 1269 ? 155.534 199.017 118.954 1.00 48.36  ? 1269 ILE A CB    1 
ATOM   8015  C  CG1   . ILE A 1 1269 ? 155.941 197.659 118.386 1.00 47.26  ? 1269 ILE A CG1   1 
ATOM   8016  C  CG2   . ILE A 1 1269 ? 154.131 199.365 118.500 1.00 45.19  ? 1269 ILE A CG2   1 
ATOM   8017  C  CD1   . ILE A 1 1269 ? 155.317 196.494 119.111 1.00 43.38  ? 1269 ILE A CD1   1 
ATOM   8018  N  N     . ASP A 1 1270 ? 155.869 202.357 117.895 1.00 53.82  ? 1270 ASP A N     1 
ATOM   8019  C  CA    . ASP A 1 1270 ? 155.429 203.739 118.095 1.00 55.58  ? 1270 ASP A CA    1 
ATOM   8020  C  C     . ASP A 1 1270 ? 156.319 204.471 119.097 1.00 55.42  ? 1270 ASP A C     1 
ATOM   8021  O  O     . ASP A 1 1270 ? 155.850 205.263 119.915 1.00 57.77  ? 1270 ASP A O     1 
ATOM   8022  C  CB    . ASP A 1 1270 ? 153.964 203.794 118.528 1.00 56.86  ? 1270 ASP A CB    1 
ATOM   8023  C  CG    . ASP A 1 1270 ? 153.033 203.198 117.498 1.00 63.91  ? 1270 ASP A CG    1 
ATOM   8024  O  OD1   . ASP A 1 1270 ? 153.291 203.377 116.291 1.00 65.40  ? 1270 ASP A OD1   1 
ATOM   8025  O  OD2   . ASP A 1 1270 ? 152.039 202.556 117.895 1.00 69.02  ? 1270 ASP A OD2   1 
ATOM   8026  N  N     . GLY A 1 1271 ? 157.623 204.204 119.028 1.00 53.84  ? 1271 GLY A N     1 
ATOM   8027  C  CA    . GLY A 1 1271 ? 158.593 204.887 119.855 1.00 51.74  ? 1271 GLY A CA    1 
ATOM   8028  C  C     . GLY A 1 1271 ? 158.808 204.312 121.237 1.00 54.08  ? 1271 GLY A C     1 
ATOM   8029  O  O     . GLY A 1 1271 ? 159.685 204.801 121.959 1.00 55.19  ? 1271 GLY A O     1 
ATOM   8030  N  N     . VAL A 1 1272 ? 158.052 203.295 121.635 1.00 53.67  ? 1272 VAL A N     1 
ATOM   8031  C  CA    . VAL A 1 1272 ? 158.157 202.726 122.973 1.00 50.02  ? 1272 VAL A CA    1 
ATOM   8032  C  C     . VAL A 1 1272 ? 159.054 201.496 122.922 1.00 50.80  ? 1272 VAL A C     1 
ATOM   8033  O  O     . VAL A 1 1272 ? 158.719 200.499 122.275 1.00 52.93  ? 1272 VAL A O     1 
ATOM   8034  C  CB    . VAL A 1 1272 ? 156.773 202.374 123.534 1.00 47.06  ? 1272 VAL A CB    1 
ATOM   8035  C  CG1   . VAL A 1 1272 ? 156.914 201.620 124.839 1.00 43.93  ? 1272 VAL A CG1   1 
ATOM   8036  C  CG2   . VAL A 1 1272 ? 155.952 203.632 123.732 1.00 48.18  ? 1272 VAL A CG2   1 
ATOM   8037  N  N     . SER A 1 1273 ? 160.189 201.563 123.615 1.00 49.54  ? 1273 SER A N     1 
ATOM   8038  C  CA    . SER A 1 1273 ? 161.118 200.442 123.653 1.00 50.32  ? 1273 SER A CA    1 
ATOM   8039  C  C     . SER A 1 1273 ? 160.521 199.264 124.417 1.00 50.66  ? 1273 SER A C     1 
ATOM   8040  O  O     . SER A 1 1273 ? 159.702 199.431 125.324 1.00 53.47  ? 1273 SER A O     1 
ATOM   8041  C  CB    . SER A 1 1273 ? 162.438 200.863 124.294 1.00 50.06  ? 1273 SER A CB    1 
ATOM   8042  O  OG    . SER A 1 1273 ? 163.261 199.734 124.526 1.00 51.66  ? 1273 SER A OG    1 
ATOM   8043  N  N     . TRP A 1 1274 ? 160.933 198.056 124.029 1.00 47.50  ? 1274 TRP A N     1 
ATOM   8044  C  CA    . TRP A 1 1274 ? 160.450 196.845 124.683 1.00 48.24  ? 1274 TRP A CA    1 
ATOM   8045  C  C     . TRP A 1 1274 ? 161.138 196.568 126.015 1.00 52.45  ? 1274 TRP A C     1 
ATOM   8046  O  O     . TRP A 1 1274 ? 160.716 195.651 126.727 1.00 51.76  ? 1274 TRP A O     1 
ATOM   8047  C  CB    . TRP A 1 1274 ? 160.589 195.649 123.736 1.00 48.29  ? 1274 TRP A CB    1 
ATOM   8048  C  CG    . TRP A 1 1274 ? 161.987 195.225 123.413 1.00 48.59  ? 1274 TRP A CG    1 
ATOM   8049  C  CD1   . TRP A 1 1274 ? 163.138 195.907 123.673 1.00 52.55  ? 1274 TRP A CD1   1 
ATOM   8050  C  CD2   . TRP A 1 1274 ? 162.375 194.033 122.724 1.00 48.48  ? 1274 TRP A CD2   1 
ATOM   8051  N  NE1   . TRP A 1 1274 ? 164.220 195.203 123.206 1.00 53.78  ? 1274 TRP A NE1   1 
ATOM   8052  C  CE2   . TRP A 1 1274 ? 163.777 194.050 122.618 1.00 51.66  ? 1274 TRP A CE2   1 
ATOM   8053  C  CE3   . TRP A 1 1274 ? 161.672 192.950 122.191 1.00 43.89  ? 1274 TRP A CE3   1 
ATOM   8054  C  CZ2   . TRP A 1 1274 ? 164.490 193.026 122.005 1.00 50.11  ? 1274 TRP A CZ2   1 
ATOM   8055  C  CZ3   . TRP A 1 1274 ? 162.380 191.935 121.584 1.00 43.15  ? 1274 TRP A CZ3   1 
ATOM   8056  C  CH2   . TRP A 1 1274 ? 163.774 191.979 121.495 1.00 47.71  ? 1274 TRP A CH2   1 
ATOM   8057  N  N     . ASP A 1 1275 ? 162.184 197.316 126.361 1.00 55.63  ? 1275 ASP A N     1 
ATOM   8058  C  CA    . ASP A 1 1275 ? 162.764 197.253 127.696 1.00 56.25  ? 1275 ASP A CA    1 
ATOM   8059  C  C     . ASP A 1 1275 ? 162.088 198.200 128.677 1.00 57.07  ? 1275 ASP A C     1 
ATOM   8060  O  O     . ASP A 1 1275 ? 162.382 198.141 129.876 1.00 57.25  ? 1275 ASP A O     1 
ATOM   8061  C  CB    . ASP A 1 1275 ? 164.262 197.565 127.647 1.00 54.95  ? 1275 ASP A CB    1 
ATOM   8062  C  CG    . ASP A 1 1275 ? 165.077 196.407 127.121 1.00 62.82  ? 1275 ASP A CG    1 
ATOM   8063  O  OD1   . ASP A 1 1275 ? 164.869 195.271 127.596 1.00 65.41  ? 1275 ASP A OD1   1 
ATOM   8064  O  OD2   . ASP A 1 1275 ? 165.926 196.630 126.233 1.00 63.49  ? 1275 ASP A OD2   1 
ATOM   8065  N  N     . SER A 1 1276 ? 161.194 199.065 128.200 1.00 57.21  ? 1276 SER A N     1 
ATOM   8066  C  CA    . SER A 1 1276 ? 160.521 200.018 129.075 1.00 55.44  ? 1276 SER A CA    1 
ATOM   8067  C  C     . SER A 1 1276 ? 159.363 199.366 129.824 1.00 59.42  ? 1276 SER A C     1 
ATOM   8068  O  O     . SER A 1 1276 ? 159.311 199.397 131.058 1.00 64.28  ? 1276 SER A O     1 
ATOM   8069  C  CB    . SER A 1 1276 ? 160.030 201.216 128.260 1.00 51.74  ? 1276 SER A CB    1 
ATOM   8070  O  OG    . SER A 1 1276 ? 159.403 202.175 129.091 1.00 54.84  ? 1276 SER A OG    1 
ATOM   8071  N  N     . ILE A 1 1277 ? 158.425 198.779 129.094 1.00 56.75  ? 1277 ILE A N     1 
ATOM   8072  C  CA    . ILE A 1 1277 ? 157.235 198.198 129.696 1.00 55.80  ? 1277 ILE A CA    1 
ATOM   8073  C  C     . ILE A 1 1277 ? 157.490 196.736 130.037 1.00 55.43  ? 1277 ILE A C     1 
ATOM   8074  O  O     . ILE A 1 1277 ? 158.459 196.122 129.587 1.00 56.66  ? 1277 ILE A O     1 
ATOM   8075  C  CB    . ILE A 1 1277 ? 156.010 198.346 128.774 1.00 57.35  ? 1277 ILE A CB    1 
ATOM   8076  C  CG1   . ILE A 1 1277 ? 156.233 197.581 127.472 1.00 54.40  ? 1277 ILE A CG1   1 
ATOM   8077  C  CG2   . ILE A 1 1277 ? 155.726 199.811 128.494 1.00 56.13  ? 1277 ILE A CG2   1 
ATOM   8078  C  CD1   . ILE A 1 1277 ? 155.043 197.595 126.561 1.00 52.41  ? 1277 ILE A CD1   1 
ATOM   8079  N  N     . THR A 1 1278 ? 156.603 196.173 130.854 1.00 55.47  ? 1278 THR A N     1 
ATOM   8080  C  CA    . THR A 1 1278 ? 156.710 194.778 131.248 1.00 53.63  ? 1278 THR A CA    1 
ATOM   8081  C  C     . THR A 1 1278 ? 156.349 193.852 130.089 1.00 53.52  ? 1278 THR A C     1 
ATOM   8082  O  O     . THR A 1 1278 ? 155.750 194.259 129.091 1.00 54.49  ? 1278 THR A O     1 
ATOM   8083  C  CB    . THR A 1 1278 ? 155.805 194.482 132.442 1.00 54.58  ? 1278 THR A CB    1 
ATOM   8084  O  OG1   . THR A 1 1278 ? 154.455 194.332 131.992 1.00 55.30  ? 1278 THR A OG1   1 
ATOM   8085  C  CG2   . THR A 1 1278 ? 155.874 195.611 133.448 1.00 57.34  ? 1278 THR A CG2   1 
ATOM   8086  N  N     . LEU A 1 1279 ? 156.729 192.582 130.242 1.00 50.62  ? 1279 LEU A N     1 
ATOM   8087  C  CA    . LEU A 1 1279 ? 156.511 191.596 129.190 1.00 49.28  ? 1279 LEU A CA    1 
ATOM   8088  C  C     . LEU A 1 1279 ? 155.029 191.342 128.942 1.00 53.52  ? 1279 LEU A C     1 
ATOM   8089  O  O     . LEU A 1 1279 ? 154.616 191.155 127.790 1.00 54.27  ? 1279 LEU A O     1 
ATOM   8090  C  CB    . LEU A 1 1279 ? 157.224 190.296 129.558 1.00 44.40  ? 1279 LEU A CB    1 
ATOM   8091  C  CG    . LEU A 1 1279 ? 157.258 189.159 128.543 1.00 43.91  ? 1279 LEU A CG    1 
ATOM   8092  C  CD1   . LEU A 1 1279 ? 157.861 189.630 127.234 1.00 43.63  ? 1279 LEU A CD1   1 
ATOM   8093  C  CD2   . LEU A 1 1279 ? 158.051 188.000 129.113 1.00 46.56  ? 1279 LEU A CD2   1 
ATOM   8094  N  N     . GLN A 1 1280 ? 154.215 191.331 130.000 1.00 53.12  ? 1280 GLN A N     1 
ATOM   8095  C  CA    . GLN A 1 1280 ? 152.783 191.107 129.831 1.00 51.60  ? 1280 GLN A CA    1 
ATOM   8096  C  C     . GLN A 1 1280 ? 152.144 192.234 129.031 1.00 52.37  ? 1280 GLN A C     1 
ATOM   8097  O  O     . GLN A 1 1280 ? 151.285 191.988 128.178 1.00 52.39  ? 1280 GLN A O     1 
ATOM   8098  C  CB    . GLN A 1 1280 ? 152.111 190.963 131.197 1.00 60.00  ? 1280 GLN A CB    1 
ATOM   8099  C  CG    . GLN A 1 1280 ? 150.627 191.296 131.215 1.00 66.99  ? 1280 GLN A CG    1 
ATOM   8100  C  CD    . GLN A 1 1280 ? 149.762 190.156 130.717 1.00 74.61  ? 1280 GLN A CD    1 
ATOM   8101  O  OE1   . GLN A 1 1280 ? 150.114 188.985 130.859 1.00 76.31  ? 1280 GLN A OE1   1 
ATOM   8102  N  NE2   . GLN A 1 1280 ? 148.622 190.494 130.129 1.00 68.32  ? 1280 GLN A NE2   1 
ATOM   8103  N  N     . GLN A 1 1281 ? 152.551 193.476 129.294 1.00 52.68  ? 1281 GLN A N     1 
ATOM   8104  C  CA    . GLN A 1 1281 ? 152.062 194.598 128.503 1.00 50.72  ? 1281 GLN A CA    1 
ATOM   8105  C  C     . GLN A 1 1281 ? 152.507 194.484 127.050 1.00 52.95  ? 1281 GLN A C     1 
ATOM   8106  O  O     . GLN A 1 1281 ? 151.731 194.770 126.132 1.00 53.86  ? 1281 GLN A O     1 
ATOM   8107  C  CB    . GLN A 1 1281 ? 152.552 195.911 129.108 1.00 51.79  ? 1281 GLN A CB    1 
ATOM   8108  C  CG    . GLN A 1 1281 ? 151.931 196.241 130.448 1.00 56.18  ? 1281 GLN A CG    1 
ATOM   8109  C  CD    . GLN A 1 1281 ? 152.527 197.483 131.074 1.00 61.79  ? 1281 GLN A CD    1 
ATOM   8110  O  OE1   . GLN A 1 1281 ? 153.679 197.483 131.510 1.00 64.42  ? 1281 GLN A OE1   1 
ATOM   8111  N  NE2   . GLN A 1 1281 ? 151.747 198.555 131.116 1.00 62.31  ? 1281 GLN A NE2   1 
ATOM   8112  N  N     . TRP A 1 1282 ? 153.760 194.083 126.826 1.00 52.67  ? 1282 TRP A N     1 
ATOM   8113  C  CA    . TRP A 1 1282 ? 154.283 193.975 125.467 1.00 43.63  ? 1282 TRP A CA    1 
ATOM   8114  C  C     . TRP A 1 1282 ? 153.527 192.929 124.659 1.00 43.62  ? 1282 TRP A C     1 
ATOM   8115  O  O     . TRP A 1 1282 ? 153.154 193.171 123.506 1.00 47.33  ? 1282 TRP A O     1 
ATOM   8116  C  CB    . TRP A 1 1282 ? 155.778 193.658 125.512 1.00 39.51  ? 1282 TRP A CB    1 
ATOM   8117  C  CG    . TRP A 1 1282 ? 156.431 193.561 124.170 1.00 40.63  ? 1282 TRP A CG    1 
ATOM   8118  C  CD1   . TRP A 1 1282 ? 156.680 192.422 123.461 1.00 42.16  ? 1282 TRP A CD1   1 
ATOM   8119  C  CD2   . TRP A 1 1282 ? 156.905 194.643 123.366 1.00 40.73  ? 1282 TRP A CD2   1 
ATOM   8120  N  NE1   . TRP A 1 1282 ? 157.289 192.727 122.272 1.00 39.28  ? 1282 TRP A NE1   1 
ATOM   8121  C  CE2   . TRP A 1 1282 ? 157.435 194.086 122.188 1.00 39.58  ? 1282 TRP A CE2   1 
ATOM   8122  C  CE3   . TRP A 1 1282 ? 156.933 196.028 123.528 1.00 44.10  ? 1282 TRP A CE3   1 
ATOM   8123  C  CZ2   . TRP A 1 1282 ? 157.987 194.864 121.181 1.00 39.10  ? 1282 TRP A CZ2   1 
ATOM   8124  C  CZ3   . TRP A 1 1282 ? 157.480 196.798 122.528 1.00 43.95  ? 1282 TRP A CZ3   1 
ATOM   8125  C  CH2   . TRP A 1 1282 ? 158.001 196.216 121.370 1.00 42.99  ? 1282 TRP A CH2   1 
ATOM   8126  N  N     . ARG A 1 1283 ? 153.283 191.758 125.248 1.00 42.38  ? 1283 ARG A N     1 
ATOM   8127  C  CA    . ARG A 1 1283 ? 152.626 190.699 124.489 1.00 39.78  ? 1283 ARG A CA    1 
ATOM   8128  C  C     . ARG A 1 1283 ? 151.163 191.016 124.215 1.00 43.34  ? 1283 ARG A C     1 
ATOM   8129  O  O     . ARG A 1 1283 ? 150.591 190.501 123.249 1.00 42.81  ? 1283 ARG A O     1 
ATOM   8130  C  CB    . ARG A 1 1283 ? 152.755 189.364 125.217 1.00 39.82  ? 1283 ARG A CB    1 
ATOM   8131  C  CG    . ARG A 1 1283 ? 154.161 188.816 125.205 1.00 36.76  ? 1283 ARG A CG    1 
ATOM   8132  C  CD    . ARG A 1 1283 ? 154.240 187.466 125.864 1.00 30.10  ? 1283 ARG A CD    1 
ATOM   8133  N  NE    . ARG A 1 1283 ? 155.613 186.982 125.900 1.00 32.84  ? 1283 ARG A NE    1 
ATOM   8134  C  CZ    . ARG A 1 1283 ? 156.038 185.996 126.677 1.00 37.47  ? 1283 ARG A CZ    1 
ATOM   8135  N  NH1   . ARG A 1 1283 ? 155.217 185.356 127.491 1.00 40.18  ? 1283 ARG A NH1   1 
ATOM   8136  N  NH2   . ARG A 1 1283 ? 157.318 185.644 126.633 1.00 37.73  ? 1283 ARG A NH2   1 
ATOM   8137  N  N     . LYS A 1 1284 ? 150.540 191.851 125.045 1.00 46.14  ? 1284 LYS A N     1 
ATOM   8138  C  CA    . LYS A 1 1284 ? 149.134 192.184 124.855 1.00 47.22  ? 1284 LYS A CA    1 
ATOM   8139  C  C     . LYS A 1 1284 ? 148.889 193.048 123.626 1.00 47.36  ? 1284 LYS A C     1 
ATOM   8140  O  O     . LYS A 1 1284 ? 147.729 193.237 123.248 1.00 51.56  ? 1284 LYS A O     1 
ATOM   8141  C  CB    . LYS A 1 1284 ? 148.588 192.891 126.094 1.00 50.80  ? 1284 LYS A CB    1 
ATOM   8142  C  CG    . LYS A 1 1284 ? 147.947 191.956 127.102 1.00 56.67  ? 1284 LYS A CG    1 
ATOM   8143  C  CD    . LYS A 1 1284 ? 146.820 191.169 126.465 1.00 59.00  ? 1284 LYS A CD    1 
ATOM   8144  C  CE    . LYS A 1 1284 ? 145.499 191.910 126.568 1.00 60.99  ? 1284 LYS A CE    1 
ATOM   8145  N  NZ    . LYS A 1 1284 ? 144.566 191.542 125.466 1.00 62.11  ? 1284 LYS A NZ    1 
ATOM   8146  N  N     . ALA A 1 1285 ? 149.939 193.582 123.005 1.00 45.59  ? 1285 ALA A N     1 
ATOM   8147  C  CA    . ALA A 1 1285 ? 149.791 194.424 121.826 1.00 46.68  ? 1285 ALA A CA    1 
ATOM   8148  C  C     . ALA A 1 1285 ? 149.680 193.634 120.528 1.00 41.18  ? 1285 ALA A C     1 
ATOM   8149  O  O     . ALA A 1 1285 ? 149.419 194.235 119.482 1.00 42.91  ? 1285 ALA A O     1 
ATOM   8150  C  CB    . ALA A 1 1285 ? 150.969 195.396 121.729 1.00 45.54  ? 1285 ALA A CB    1 
ATOM   8151  N  N     . PHE A 1 1286 ? 149.868 192.318 120.565 1.00 37.03  ? 1286 PHE A N     1 
ATOM   8152  C  CA    . PHE A 1 1286 ? 149.925 191.493 119.366 1.00 38.48  ? 1286 PHE A CA    1 
ATOM   8153  C  C     . PHE A 1 1286 ? 148.738 190.543 119.301 1.00 44.08  ? 1286 PHE A C     1 
ATOM   8154  O  O     . PHE A 1 1286 ? 148.278 190.036 120.328 1.00 49.98  ? 1286 PHE A O     1 
ATOM   8155  C  CB    . PHE A 1 1286 ? 151.217 190.674 119.324 1.00 37.72  ? 1286 PHE A CB    1 
ATOM   8156  C  CG    . PHE A 1 1286 ? 152.457 191.495 119.131 1.00 38.29  ? 1286 PHE A CG    1 
ATOM   8157  C  CD1   . PHE A 1 1286 ? 152.802 191.966 117.880 1.00 39.55  ? 1286 PHE A CD1   1 
ATOM   8158  C  CD2   . PHE A 1 1286 ? 153.287 191.778 120.199 1.00 35.64  ? 1286 PHE A CD2   1 
ATOM   8159  C  CE1   . PHE A 1 1286 ? 153.944 192.714 117.701 1.00 38.74  ? 1286 PHE A CE1   1 
ATOM   8160  C  CE2   . PHE A 1 1286 ? 154.428 192.525 120.027 1.00 34.30  ? 1286 PHE A CE2   1 
ATOM   8161  C  CZ    . PHE A 1 1286 ? 154.759 192.992 118.776 1.00 37.42  ? 1286 PHE A CZ    1 
ATOM   8162  N  N     . GLY A 1 1287 ? 148.245 190.312 118.090 1.00 41.90  ? 1287 GLY A N     1 
ATOM   8163  C  CA    . GLY A 1 1287 ? 147.329 189.215 117.802 1.00 38.16  ? 1287 GLY A CA    1 
ATOM   8164  C  C     . GLY A 1 1287 ? 148.049 188.194 116.939 1.00 39.06  ? 1287 GLY A C     1 
ATOM   8165  O  O     . GLY A 1 1287 ? 148.744 188.560 115.989 1.00 41.30  ? 1287 GLY A O     1 
ATOM   8166  N  N     . VAL A 1 1288 ? 147.883 186.914 117.269 1.00 37.46  ? 1288 VAL A N     1 
ATOM   8167  C  CA    . VAL A 1 1288 ? 148.713 185.867 116.689 1.00 34.74  ? 1288 VAL A CA    1 
ATOM   8168  C  C     . VAL A 1 1288 ? 147.850 184.737 116.146 1.00 35.49  ? 1288 VAL A C     1 
ATOM   8169  O  O     . VAL A 1 1288 ? 146.741 184.485 116.626 1.00 38.01  ? 1288 VAL A O     1 
ATOM   8170  C  CB    . VAL A 1 1288 ? 149.728 185.310 117.714 1.00 31.99  ? 1288 VAL A CB    1 
ATOM   8171  C  CG1   . VAL A 1 1288 ? 150.681 186.396 118.166 1.00 34.73  ? 1288 VAL A CG1   1 
ATOM   8172  C  CG2   . VAL A 1 1288 ? 149.008 184.699 118.900 1.00 33.14  ? 1288 VAL A CG2   1 
ATOM   8173  N  N     . ILE A 1 1289 ? 148.369 184.068 115.125 1.00 38.02  ? 1289 ILE A N     1 
ATOM   8174  C  CA    . ILE A 1 1289 ? 147.863 182.784 114.660 1.00 36.05  ? 1289 ILE A CA    1 
ATOM   8175  C  C     . ILE A 1 1289 ? 149.025 181.799 114.653 1.00 37.82  ? 1289 ILE A C     1 
ATOM   8176  O  O     . ILE A 1 1289 ? 149.843 181.795 113.733 1.00 41.07  ? 1289 ILE A O     1 
ATOM   8177  C  CB    . ILE A 1 1289 ? 147.217 182.894 113.266 1.00 37.44  ? 1289 ILE A CB    1 
ATOM   8178  C  CG1   . ILE A 1 1289 ? 145.941 183.732 113.325 1.00 38.40  ? 1289 ILE A CG1   1 
ATOM   8179  C  CG2   . ILE A 1 1289 ? 146.889 181.518 112.717 1.00 37.13  ? 1289 ILE A CG2   1 
ATOM   8180  C  CD1   . ILE A 1 1289 ? 145.287 183.940 111.982 1.00 31.54  ? 1289 ILE A CD1   1 
ATOM   8181  N  N     . PRO A 1 1290 ? 149.153 180.968 115.686 1.00 35.71  ? 1290 PRO A N     1 
ATOM   8182  C  CA    . PRO A 1 1290 ? 150.261 180.008 115.727 1.00 37.34  ? 1290 PRO A CA    1 
ATOM   8183  C  C     . PRO A 1 1290 ? 150.137 178.958 114.633 1.00 38.15  ? 1290 PRO A C     1 
ATOM   8184  O  O     . PRO A 1 1290 ? 149.041 178.634 114.171 1.00 40.33  ? 1290 PRO A O     1 
ATOM   8185  C  CB    . PRO A 1 1290 ? 150.135 179.380 117.121 1.00 37.93  ? 1290 PRO A CB    1 
ATOM   8186  C  CG    . PRO A 1 1290 ? 149.317 180.348 117.905 1.00 33.96  ? 1290 PRO A CG    1 
ATOM   8187  C  CD    . PRO A 1 1290 ? 148.353 180.921 116.916 1.00 34.48  ? 1290 PRO A CD    1 
ATOM   8188  N  N     . GLN A 1 1291 ? 151.288 178.431 114.212 1.00 38.12  ? 1291 GLN A N     1 
ATOM   8189  C  CA    . GLN A 1 1291 ? 151.291 177.392 113.188 1.00 45.26  ? 1291 GLN A CA    1 
ATOM   8190  C  C     . GLN A 1 1291 ? 150.687 176.090 113.700 1.00 46.11  ? 1291 GLN A C     1 
ATOM   8191  O  O     . GLN A 1 1291 ? 150.113 175.327 112.916 1.00 46.54  ? 1291 GLN A O     1 
ATOM   8192  C  CB    . GLN A 1 1291 ? 152.714 177.158 112.680 1.00 39.84  ? 1291 GLN A CB    1 
ATOM   8193  C  CG    . GLN A 1 1291 ? 152.783 176.534 111.298 1.00 32.73  ? 1291 GLN A CG    1 
ATOM   8194  C  CD    . GLN A 1 1291 ? 154.187 176.136 110.910 1.00 38.98  ? 1291 GLN A CD    1 
ATOM   8195  O  OE1   . GLN A 1 1291 ? 155.135 176.349 111.662 1.00 45.24  ? 1291 GLN A OE1   1 
ATOM   8196  N  NE2   . GLN A 1 1291 ? 154.330 175.554 109.730 1.00 41.52  ? 1291 GLN A NE2   1 
ATOM   8197  N  N     . LYS A 1 1292 ? 150.809 175.814 114.996 1.00 43.61  ? 1292 LYS A N     1 
ATOM   8198  C  CA    . LYS A 1 1292 ? 150.227 174.626 115.610 1.00 45.41  ? 1292 LYS A CA    1 
ATOM   8199  C  C     . LYS A 1 1292 ? 148.994 175.034 116.408 1.00 44.64  ? 1292 LYS A C     1 
ATOM   8200  O  O     . LYS A 1 1292 ? 149.080 175.886 117.297 1.00 44.91  ? 1292 LYS A O     1 
ATOM   8201  C  CB    . LYS A 1 1292 ? 151.246 173.923 116.505 1.00 46.67  ? 1292 LYS A CB    1 
ATOM   8202  C  CG    . LYS A 1 1292 ? 150.735 172.645 117.141 1.00 49.75  ? 1292 LYS A CG    1 
ATOM   8203  C  CD    . LYS A 1 1292 ? 151.708 172.128 118.185 1.00 52.99  ? 1292 LYS A CD    1 
ATOM   8204  C  CE    . LYS A 1 1292 ? 151.148 170.920 118.913 1.00 52.12  ? 1292 LYS A CE    1 
ATOM   8205  N  NZ    . LYS A 1 1292 ? 151.947 170.591 120.125 1.00 45.05  ? 1292 LYS A NZ    1 
ATOM   8206  N  N     . VAL A 1 1293 ? 147.856 174.424 116.090 1.00 43.41  ? 1293 VAL A N     1 
ATOM   8207  C  CA    . VAL A 1 1293 ? 146.569 174.833 116.647 1.00 40.75  ? 1293 VAL A CA    1 
ATOM   8208  C  C     . VAL A 1 1293 ? 146.355 174.159 117.996 1.00 46.03  ? 1293 VAL A C     1 
ATOM   8209  O  O     . VAL A 1 1293 ? 146.516 172.941 118.129 1.00 47.07  ? 1293 VAL A O     1 
ATOM   8210  C  CB    . VAL A 1 1293 ? 145.433 174.498 115.669 1.00 38.08  ? 1293 VAL A CB    1 
ATOM   8211  C  CG1   . VAL A 1 1293 ? 144.090 174.886 116.254 1.00 39.31  ? 1293 VAL A CG1   1 
ATOM   8212  C  CG2   . VAL A 1 1293 ? 145.664 175.194 114.340 1.00 38.63  ? 1293 VAL A CG2   1 
ATOM   8213  N  N     . PHE A 1 1294 ? 145.995 174.954 119.004 1.00 38.81  ? 1294 PHE A N     1 
ATOM   8214  C  CA    . PHE A 1 1294 ? 145.740 174.460 120.352 1.00 32.78  ? 1294 PHE A CA    1 
ATOM   8215  C  C     . PHE A 1 1294 ? 144.238 174.440 120.612 1.00 35.86  ? 1294 PHE A C     1 
ATOM   8216  O  O     . PHE A 1 1294 ? 143.583 175.487 120.575 1.00 37.80  ? 1294 PHE A O     1 
ATOM   8217  C  CB    . PHE A 1 1294 ? 146.456 175.329 121.386 1.00 32.41  ? 1294 PHE A CB    1 
ATOM   8218  C  CG    . PHE A 1 1294 ? 146.031 175.072 122.807 1.00 34.08  ? 1294 PHE A CG    1 
ATOM   8219  C  CD1   . PHE A 1 1294 ? 145.954 173.782 123.303 1.00 34.80  ? 1294 PHE A CD1   1 
ATOM   8220  C  CD2   . PHE A 1 1294 ? 145.740 176.124 123.655 1.00 29.88  ? 1294 PHE A CD2   1 
ATOM   8221  C  CE1   . PHE A 1 1294 ? 145.573 173.548 124.608 1.00 31.47  ? 1294 PHE A CE1   1 
ATOM   8222  C  CE2   . PHE A 1 1294 ? 145.360 175.894 124.960 1.00 30.14  ? 1294 PHE A CE2   1 
ATOM   8223  C  CZ    . PHE A 1 1294 ? 145.277 174.604 125.436 1.00 27.84  ? 1294 PHE A CZ    1 
ATOM   8224  N  N     . ILE A 1 1295 ? 143.699 173.252 120.873 1.00 36.15  ? 1295 ILE A N     1 
ATOM   8225  C  CA    . ILE A 1 1295 ? 142.301 173.071 121.246 1.00 35.39  ? 1295 ILE A CA    1 
ATOM   8226  C  C     . ILE A 1 1295 ? 142.248 172.203 122.494 1.00 42.52  ? 1295 ILE A C     1 
ATOM   8227  O  O     . ILE A 1 1295 ? 142.851 171.125 122.530 1.00 49.76  ? 1295 ILE A O     1 
ATOM   8228  C  CB    . ILE A 1 1295 ? 141.482 172.439 120.104 1.00 36.37  ? 1295 ILE A CB    1 
ATOM   8229  C  CG1   . ILE A 1 1295 ? 141.282 173.449 118.976 1.00 38.43  ? 1295 ILE A CG1   1 
ATOM   8230  C  CG2   . ILE A 1 1295 ? 140.144 171.933 120.609 1.00 38.78  ? 1295 ILE A CG2   1 
ATOM   8231  C  CD1   . ILE A 1 1295 ? 140.769 172.841 117.707 1.00 39.62  ? 1295 ILE A CD1   1 
ATOM   8232  N  N     . PHE A 1 1296 ? 141.534 172.670 123.512 1.00 41.42  ? 1296 PHE A N     1 
ATOM   8233  C  CA    . PHE A 1 1296 ? 141.409 171.965 124.779 1.00 42.86  ? 1296 PHE A CA    1 
ATOM   8234  C  C     . PHE A 1 1296 ? 139.982 171.470 124.979 1.00 46.98  ? 1296 PHE A C     1 
ATOM   8235  O  O     . PHE A 1 1296 ? 139.057 171.841 124.253 1.00 45.24  ? 1296 PHE A O     1 
ATOM   8236  C  CB    . PHE A 1 1296 ? 141.851 172.862 125.944 1.00 39.04  ? 1296 PHE A CB    1 
ATOM   8237  C  CG    . PHE A 1 1296 ? 141.018 174.101 126.117 1.00 38.63  ? 1296 PHE A CG    1 
ATOM   8238  C  CD1   . PHE A 1 1296 ? 141.319 175.253 125.412 1.00 37.96  ? 1296 PHE A CD1   1 
ATOM   8239  C  CD2   . PHE A 1 1296 ? 139.947 174.121 126.992 1.00 39.10  ? 1296 PHE A CD2   1 
ATOM   8240  C  CE1   . PHE A 1 1296 ? 140.565 176.396 125.571 1.00 39.27  ? 1296 PHE A CE1   1 
ATOM   8241  C  CE2   . PHE A 1 1296 ? 139.187 175.262 127.151 1.00 40.16  ? 1296 PHE A CE2   1 
ATOM   8242  C  CZ    . PHE A 1 1296 ? 139.498 176.399 126.441 1.00 38.96  ? 1296 PHE A CZ    1 
ATOM   8243  N  N     . SER A 1 1297 ? 139.815 170.608 125.980 1.00 51.89  ? 1297 SER A N     1 
ATOM   8244  C  CA    . SER A 1 1297 ? 138.511 170.022 126.267 1.00 49.79  ? 1297 SER A CA    1 
ATOM   8245  C  C     . SER A 1 1297 ? 137.564 171.092 126.792 1.00 47.84  ? 1297 SER A C     1 
ATOM   8246  O  O     . SER A 1 1297 ? 137.851 171.751 127.796 1.00 53.27  ? 1297 SER A O     1 
ATOM   8247  C  CB    . SER A 1 1297 ? 138.647 168.887 127.277 1.00 50.15  ? 1297 SER A CB    1 
ATOM   8248  O  OG    . SER A 1 1297 ? 139.223 167.739 126.684 1.00 55.41  ? 1297 SER A OG    1 
ATOM   8249  N  N     . GLY A 1 1298 ? 136.439 171.257 126.119 1.00 43.07  ? 1298 GLY A N     1 
ATOM   8250  C  CA    . GLY A 1 1298 ? 135.465 172.250 126.513 1.00 40.59  ? 1298 GLY A CA    1 
ATOM   8251  C  C     . GLY A 1 1298 ? 134.531 172.552 125.364 1.00 43.15  ? 1298 GLY A C     1 
ATOM   8252  O  O     . GLY A 1 1298 ? 134.683 172.046 124.254 1.00 46.49  ? 1298 GLY A O     1 
ATOM   8253  N  N     . THR A 1 1299 ? 133.550 173.393 125.662 1.00 41.89  ? 1299 THR A N     1 
ATOM   8254  C  CA    . THR A 1 1299 ? 132.577 173.785 124.660 1.00 40.95  ? 1299 THR A CA    1 
ATOM   8255  C  C     . THR A 1 1299 ? 133.223 174.686 123.610 1.00 41.82  ? 1299 THR A C     1 
ATOM   8256  O  O     . THR A 1 1299 ? 134.339 175.183 123.779 1.00 44.53  ? 1299 THR A O     1 
ATOM   8257  C  CB    . THR A 1 1299 ? 131.391 174.491 125.316 1.00 42.32  ? 1299 THR A CB    1 
ATOM   8258  O  OG1   . THR A 1 1299 ? 131.779 175.809 125.715 1.00 42.47  ? 1299 THR A OG1   1 
ATOM   8259  C  CG2   . THR A 1 1299 ? 130.932 173.723 126.538 1.00 41.13  ? 1299 THR A CG2   1 
ATOM   8260  N  N     . PHE A 1 1300 ? 132.506 174.875 122.499 1.00 41.82  ? 1300 PHE A N     1 
ATOM   8261  C  CA    . PHE A 1 1300 ? 132.958 175.802 121.467 1.00 40.57  ? 1300 PHE A CA    1 
ATOM   8262  C  C     . PHE A 1 1300 ? 133.159 177.200 122.040 1.00 44.71  ? 1300 PHE A C     1 
ATOM   8263  O  O     . PHE A 1 1300 ? 134.172 177.859 121.777 1.00 49.10  ? 1300 PHE A O     1 
ATOM   8264  C  CB    . PHE A 1 1300 ? 131.946 175.847 120.320 1.00 42.03  ? 1300 PHE A CB    1 
ATOM   8265  C  CG    . PHE A 1 1300 ? 132.148 174.789 119.274 1.00 46.85  ? 1300 PHE A CG    1 
ATOM   8266  C  CD1   . PHE A 1 1300 ? 133.133 174.928 118.312 1.00 49.06  ? 1300 PHE A CD1   1 
ATOM   8267  C  CD2   . PHE A 1 1300 ? 131.328 173.675 119.228 1.00 46.47  ? 1300 PHE A CD2   1 
ATOM   8268  C  CE1   . PHE A 1 1300 ? 133.314 173.964 117.340 1.00 46.04  ? 1300 PHE A CE1   1 
ATOM   8269  C  CE2   . PHE A 1 1300 ? 131.500 172.709 118.257 1.00 48.25  ? 1300 PHE A CE2   1 
ATOM   8270  C  CZ    . PHE A 1 1300 ? 132.494 172.852 117.312 1.00 50.38  ? 1300 PHE A CZ    1 
ATOM   8271  N  N     . ARG A 1 1301 ? 132.190 177.665 122.830 1.00 41.94  ? 1301 ARG A N     1 
ATOM   8272  C  CA    . ARG A 1 1301 ? 132.250 179.013 123.384 1.00 39.42  ? 1301 ARG A CA    1 
ATOM   8273  C  C     . ARG A 1 1301 ? 133.450 179.181 124.307 1.00 40.61  ? 1301 ARG A C     1 
ATOM   8274  O  O     . ARG A 1 1301 ? 134.097 180.234 124.309 1.00 44.54  ? 1301 ARG A O     1 
ATOM   8275  C  CB    . ARG A 1 1301 ? 130.952 179.323 124.125 1.00 44.19  ? 1301 ARG A CB    1 
ATOM   8276  C  CG    . ARG A 1 1301 ? 130.921 180.671 124.816 1.00 48.25  ? 1301 ARG A CG    1 
ATOM   8277  C  CD    . ARG A 1 1301 ? 129.506 181.066 125.205 1.00 53.27  ? 1301 ARG A CD    1 
ATOM   8278  N  NE    . ARG A 1 1301 ? 128.871 180.052 126.036 1.00 54.33  ? 1301 ARG A NE    1 
ATOM   8279  C  CZ    . ARG A 1 1301 ? 127.943 179.209 125.606 1.00 56.46  ? 1301 ARG A CZ    1 
ATOM   8280  N  NH1   . ARG A 1 1301 ? 127.481 179.264 124.370 1.00 55.15  ? 1301 ARG A NH1   1 
ATOM   8281  N  NH2   . ARG A 1 1301 ? 127.464 178.291 126.440 1.00 59.93  ? 1301 ARG A NH2   1 
ATOM   8282  N  N     . LYS A 1 1302 ? 133.755 178.161 125.110 1.00 38.27  ? 1302 LYS A N     1 
ATOM   8283  C  CA    . LYS A 1 1302 ? 134.905 178.251 126.004 1.00 39.09  ? 1302 LYS A CA    1 
ATOM   8284  C  C     . LYS A 1 1302 ? 136.212 178.281 125.224 1.00 42.22  ? 1302 LYS A C     1 
ATOM   8285  O  O     . LYS A 1 1302 ? 137.150 178.990 125.603 1.00 43.05  ? 1302 LYS A O     1 
ATOM   8286  C  CB    . LYS A 1 1302 ? 134.898 177.089 126.994 1.00 41.44  ? 1302 LYS A CB    1 
ATOM   8287  C  CG    . LYS A 1 1302 ? 135.873 177.270 128.138 1.00 44.38  ? 1302 LYS A CG    1 
ATOM   8288  C  CD    . LYS A 1 1302 ? 135.512 178.494 128.951 1.00 46.71  ? 1302 LYS A CD    1 
ATOM   8289  C  CE    . LYS A 1 1302 ? 136.468 178.697 130.107 1.00 45.51  ? 1302 LYS A CE    1 
ATOM   8290  N  NZ    . LYS A 1 1302 ? 136.260 177.690 131.180 1.00 49.52  ? 1302 LYS A NZ    1 
ATOM   8291  N  N     . ASN A 1 1303 ? 136.297 177.511 124.138 1.00 42.68  ? 1303 ASN A N     1 
ATOM   8292  C  CA    . ASN A 1 1303 ? 137.492 177.545 123.303 1.00 38.42  ? 1303 ASN A CA    1 
ATOM   8293  C  C     . ASN A 1 1303 ? 137.654 178.887 122.607 1.00 39.16  ? 1303 ASN A C     1 
ATOM   8294  O  O     . ASN A 1 1303 ? 138.784 179.335 122.385 1.00 41.34  ? 1303 ASN A O     1 
ATOM   8295  C  CB    . ASN A 1 1303 ? 137.449 176.421 122.267 1.00 38.64  ? 1303 ASN A CB    1 
ATOM   8296  C  CG    . ASN A 1 1303 ? 138.029 175.121 122.788 1.00 38.48  ? 1303 ASN A CG    1 
ATOM   8297  O  OD1   . ASN A 1 1303 ? 139.239 174.912 122.753 1.00 40.75  ? 1303 ASN A OD1   1 
ATOM   8298  N  ND2   . ASN A 1 1303 ? 137.167 174.239 123.271 1.00 37.69  ? 1303 ASN A ND2   1 
ATOM   8299  N  N     . LEU A 1 1304 ? 136.547 179.540 122.251 1.00 41.46  ? 1304 LEU A N     1 
ATOM   8300  C  CA    . LEU A 1 1304 ? 136.646 180.805 121.534 1.00 39.43  ? 1304 LEU A CA    1 
ATOM   8301  C  C     . LEU A 1 1304 ? 137.063 181.961 122.438 1.00 42.27  ? 1304 LEU A C     1 
ATOM   8302  O  O     . LEU A 1 1304 ? 137.774 182.864 121.984 1.00 39.88  ? 1304 LEU A O     1 
ATOM   8303  C  CB    . LEU A 1 1304 ? 135.321 181.117 120.841 1.00 42.42  ? 1304 LEU A CB    1 
ATOM   8304  C  CG    . LEU A 1 1304 ? 135.065 180.248 119.609 1.00 48.80  ? 1304 LEU A CG    1 
ATOM   8305  C  CD1   . LEU A 1 1304 ? 133.614 180.324 119.183 1.00 47.91  ? 1304 LEU A CD1   1 
ATOM   8306  C  CD2   . LEU A 1 1304 ? 135.988 180.640 118.466 1.00 46.78  ? 1304 LEU A CD2   1 
ATOM   8307  N  N     . ASP A 1 1305 ? 136.652 181.959 123.705 1.00 45.13  ? 1305 ASP A N     1 
ATOM   8308  C  CA    . ASP A 1 1305 ? 137.056 183.008 124.643 1.00 45.43  ? 1305 ASP A CA    1 
ATOM   8309  C  C     . ASP A 1 1305 ? 137.030 182.456 126.058 1.00 45.76  ? 1305 ASP A C     1 
ATOM   8310  O  O     . ASP A 1 1305 ? 135.987 182.451 126.725 1.00 46.70  ? 1305 ASP A O     1 
ATOM   8311  C  CB    . ASP A 1 1305 ? 136.174 184.249 124.529 1.00 47.07  ? 1305 ASP A CB    1 
ATOM   8312  C  CG    . ASP A 1 1305 ? 134.703 183.925 124.560 1.00 52.79  ? 1305 ASP A CG    1 
ATOM   8313  O  OD1   . ASP A 1 1305 ? 134.288 182.994 123.840 1.00 54.35  ? 1305 ASP A OD1   1 
ATOM   8314  O  OD2   . ASP A 1 1305 ? 133.967 184.597 125.313 1.00 55.98  ? 1305 ASP A OD2   1 
ATOM   8315  N  N     . PRO A 1 1306 ? 138.171 181.977 126.554 1.00 43.47  ? 1306 PRO A N     1 
ATOM   8316  C  CA    . PRO A 1 1306 ? 138.209 181.436 127.921 1.00 45.27  ? 1306 PRO A CA    1 
ATOM   8317  C  C     . PRO A 1 1306 ? 137.901 182.460 129.002 1.00 48.86  ? 1306 PRO A C     1 
ATOM   8318  O  O     . PRO A 1 1306 ? 137.524 182.065 130.111 1.00 50.68  ? 1306 PRO A O     1 
ATOM   8319  C  CB    . PRO A 1 1306 ? 139.645 180.908 128.046 1.00 41.10  ? 1306 PRO A CB    1 
ATOM   8320  C  CG    . PRO A 1 1306 ? 140.087 180.682 126.642 1.00 36.01  ? 1306 PRO A CG    1 
ATOM   8321  C  CD    . PRO A 1 1306 ? 139.448 181.782 125.854 1.00 36.57  ? 1306 PRO A CD    1 
ATOM   8322  N  N     . TYR A 1 1307 ? 138.051 183.754 128.726 1.00 48.41  ? 1307 TYR A N     1 
ATOM   8323  C  CA    . TYR A 1 1307 ? 137.821 184.778 129.735 1.00 47.62  ? 1307 TYR A CA    1 
ATOM   8324  C  C     . TYR A 1 1307 ? 136.360 185.183 129.861 1.00 53.54  ? 1307 TYR A C     1 
ATOM   8325  O  O     . TYR A 1 1307 ? 136.021 185.914 130.797 1.00 56.32  ? 1307 TYR A O     1 
ATOM   8326  C  CB    . TYR A 1 1307 ? 138.666 186.022 129.439 1.00 49.34  ? 1307 TYR A CB    1 
ATOM   8327  C  CG    . TYR A 1 1307 ? 140.130 185.854 129.776 1.00 49.60  ? 1307 TYR A CG    1 
ATOM   8328  C  CD1   . TYR A 1 1307 ? 140.589 186.040 131.070 1.00 46.53  ? 1307 TYR A CD1   1 
ATOM   8329  C  CD2   . TYR A 1 1307 ? 141.051 185.509 128.799 1.00 49.85  ? 1307 TYR A CD2   1 
ATOM   8330  C  CE1   . TYR A 1 1307 ? 141.922 185.883 131.383 1.00 44.63  ? 1307 TYR A CE1   1 
ATOM   8331  C  CE2   . TYR A 1 1307 ? 142.384 185.352 129.103 1.00 48.49  ? 1307 TYR A CE2   1 
ATOM   8332  C  CZ    . TYR A 1 1307 ? 142.815 185.540 130.396 1.00 47.93  ? 1307 TYR A CZ    1 
ATOM   8333  O  OH    . TYR A 1 1307 ? 144.146 185.387 130.703 1.00 47.55  ? 1307 TYR A OH    1 
ATOM   8334  N  N     . GLU A 1 1308 ? 135.496 184.739 128.947 1.00 56.06  ? 1308 GLU A N     1 
ATOM   8335  C  CA    . GLU A 1 1308 ? 134.060 185.006 129.009 1.00 54.32  ? 1308 GLU A CA    1 
ATOM   8336  C  C     . GLU A 1 1308 ? 133.778 186.510 128.990 1.00 56.43  ? 1308 GLU A C     1 
ATOM   8337  O  O     . GLU A 1 1308 ? 133.176 187.077 129.902 1.00 56.46  ? 1308 GLU A O     1 
ATOM   8338  C  CB    . GLU A 1 1308 ? 133.437 184.326 130.232 1.00 48.11  ? 1308 GLU A CB    1 
ATOM   8339  C  CG    . GLU A 1 1308 ? 133.586 182.815 130.206 1.00 53.69  ? 1308 GLU A CG    1 
ATOM   8340  C  CD    . GLU A 1 1308 ? 133.628 182.203 131.588 1.00 60.66  ? 1308 GLU A CD    1 
ATOM   8341  O  OE1   . GLU A 1 1308 ? 133.569 182.961 132.577 1.00 58.49  ? 1308 GLU A OE1   1 
ATOM   8342  O  OE2   . GLU A 1 1308 ? 133.720 180.961 131.684 1.00 58.43  ? 1308 GLU A OE2   1 
ATOM   8343  N  N     . GLN A 1 1309 ? 134.241 187.149 127.918 1.00 56.51  ? 1309 GLN A N     1 
ATOM   8344  C  CA    . GLN A 1 1309 ? 134.094 188.584 127.714 1.00 54.04  ? 1309 GLN A CA    1 
ATOM   8345  C  C     . GLN A 1 1309 ? 132.945 188.944 126.782 1.00 57.26  ? 1309 GLN A C     1 
ATOM   8346  O  O     . GLN A 1 1309 ? 132.227 189.914 127.041 1.00 64.42  ? 1309 GLN A O     1 
ATOM   8347  C  CB    . GLN A 1 1309 ? 135.391 189.164 127.147 1.00 56.08  ? 1309 GLN A CB    1 
ATOM   8348  C  CG    . GLN A 1 1309 ? 136.563 189.128 128.101 1.00 57.07  ? 1309 GLN A CG    1 
ATOM   8349  C  CD    . GLN A 1 1309 ? 137.766 189.868 127.560 1.00 57.09  ? 1309 GLN A CD    1 
ATOM   8350  O  OE1   . GLN A 1 1309 ? 138.037 189.847 126.360 1.00 53.18  ? 1309 GLN A OE1   1 
ATOM   8351  N  NE2   . GLN A 1 1309 ? 138.496 190.532 128.447 1.00 62.19  ? 1309 GLN A NE2   1 
ATOM   8352  N  N     . TRP A 1 1310 ? 132.763 188.194 125.700 1.00 56.94  ? 1310 TRP A N     1 
ATOM   8353  C  CA    . TRP A 1 1310 ? 131.839 188.551 124.633 1.00 60.43  ? 1310 TRP A CA    1 
ATOM   8354  C  C     . TRP A 1 1310 ? 130.587 187.685 124.675 1.00 63.26  ? 1310 TRP A C     1 
ATOM   8355  O  O     . TRP A 1 1310 ? 130.648 186.499 125.012 1.00 65.87  ? 1310 TRP A O     1 
ATOM   8356  C  CB    . TRP A 1 1310 ? 132.526 188.418 123.273 1.00 61.72  ? 1310 TRP A CB    1 
ATOM   8357  C  CG    . TRP A 1 1310 ? 133.799 189.187 123.198 1.00 59.24  ? 1310 TRP A CG    1 
ATOM   8358  C  CD1   . TRP A 1 1310 ? 133.940 190.538 123.288 1.00 59.97  ? 1310 TRP A CD1   1 
ATOM   8359  C  CD2   . TRP A 1 1310 ? 135.118 188.652 123.067 1.00 55.56  ? 1310 TRP A CD2   1 
ATOM   8360  N  NE1   . TRP A 1 1310 ? 135.265 190.881 123.194 1.00 59.82  ? 1310 TRP A NE1   1 
ATOM   8361  C  CE2   . TRP A 1 1310 ? 136.009 189.740 123.061 1.00 58.33  ? 1310 TRP A CE2   1 
ATOM   8362  C  CE3   . TRP A 1 1310 ? 135.632 187.359 122.943 1.00 52.68  ? 1310 TRP A CE3   1 
ATOM   8363  C  CZ2   . TRP A 1 1310 ? 137.386 189.576 122.939 1.00 57.00  ? 1310 TRP A CZ2   1 
ATOM   8364  C  CZ3   . TRP A 1 1310 ? 137.000 187.198 122.820 1.00 51.84  ? 1310 TRP A CZ3   1 
ATOM   8365  C  CH2   . TRP A 1 1310 ? 137.860 188.299 122.821 1.00 55.22  ? 1310 TRP A CH2   1 
ATOM   8366  N  N     . SER A 1 1311 ? 129.452 188.292 124.338 1.00 63.78  ? 1311 SER A N     1 
ATOM   8367  C  CA    . SER A 1 1311 ? 128.173 187.599 124.334 1.00 66.59  ? 1311 SER A CA    1 
ATOM   8368  C  C     . SER A 1 1311 ? 128.007 186.771 123.059 1.00 69.46  ? 1311 SER A C     1 
ATOM   8369  O  O     . SER A 1 1311 ? 128.794 186.862 122.113 1.00 71.81  ? 1311 SER A O     1 
ATOM   8370  C  CB    . SER A 1 1311 ? 127.027 188.597 124.471 1.00 69.00  ? 1311 SER A CB    1 
ATOM   8371  O  OG    . SER A 1 1311 ? 126.757 189.230 123.234 1.00 72.23  ? 1311 SER A OG    1 
ATOM   8372  N  N     . ASP A 1 1312 ? 126.957 185.946 123.051 1.00 65.31  ? 1312 ASP A N     1 
ATOM   8373  C  CA    . ASP A 1 1312 ? 126.725 185.035 121.935 1.00 64.44  ? 1312 ASP A CA    1 
ATOM   8374  C  C     . ASP A 1 1312 ? 126.416 185.771 120.638 1.00 67.59  ? 1312 ASP A C     1 
ATOM   8375  O  O     . ASP A 1 1312 ? 126.619 185.217 119.555 1.00 70.16  ? 1312 ASP A O     1 
ATOM   8376  C  CB    . ASP A 1 1312 ? 125.598 184.064 122.280 1.00 68.23  ? 1312 ASP A CB    1 
ATOM   8377  C  CG    . ASP A 1 1312 ? 125.971 183.124 123.403 1.00 72.61  ? 1312 ASP A CG    1 
ATOM   8378  O  OD1   . ASP A 1 1312 ? 126.858 183.488 124.202 1.00 71.95  ? 1312 ASP A OD1   1 
ATOM   8379  O  OD2   . ASP A 1 1312 ? 125.383 182.027 123.487 1.00 70.13  ? 1312 ASP A OD2   1 
ATOM   8380  N  N     . GLN A 1 1313 ? 125.910 187.004 120.717 1.00 67.43  ? 1313 GLN A N     1 
ATOM   8381  C  CA    . GLN A 1 1313 ? 125.690 187.780 119.500 1.00 67.58  ? 1313 GLN A CA    1 
ATOM   8382  C  C     . GLN A 1 1313 ? 127.005 188.021 118.767 1.00 66.12  ? 1313 GLN A C     1 
ATOM   8383  O  O     . GLN A 1 1313 ? 127.115 187.778 117.558 1.00 69.29  ? 1313 GLN A O     1 
ATOM   8384  C  CB    . GLN A 1 1313 ? 125.013 189.110 119.833 1.00 71.12  ? 1313 GLN A CB    1 
ATOM   8385  C  CG    . GLN A 1 1313 ? 123.495 189.059 119.906 1.00 78.47  ? 1313 GLN A CG    1 
ATOM   8386  C  CD    . GLN A 1 1313 ? 122.992 188.156 121.013 1.00 84.49  ? 1313 GLN A CD    1 
ATOM   8387  O  OE1   . GLN A 1 1313 ? 122.142 187.295 120.790 1.00 89.59  ? 1313 GLN A OE1   1 
ATOM   8388  N  NE2   . GLN A 1 1313 ? 123.519 188.347 122.216 1.00 77.70  ? 1313 GLN A NE2   1 
ATOM   8389  N  N     . GLU A 1 1314 ? 128.024 188.480 119.495 1.00 62.48  ? 1314 GLU A N     1 
ATOM   8390  C  CA    . GLU A 1 1314 ? 129.321 188.757 118.887 1.00 63.91  ? 1314 GLU A CA    1 
ATOM   8391  C  C     . GLU A 1 1314 ? 129.987 187.479 118.390 1.00 61.68  ? 1314 GLU A C     1 
ATOM   8392  O  O     . GLU A 1 1314 ? 130.576 187.459 117.301 1.00 58.56  ? 1314 GLU A O     1 
ATOM   8393  C  CB    . GLU A 1 1314 ? 130.212 189.474 119.898 1.00 64.35  ? 1314 GLU A CB    1 
ATOM   8394  C  CG    . GLU A 1 1314 ? 129.691 190.842 120.291 1.00 70.07  ? 1314 GLU A CG    1 
ATOM   8395  C  CD    . GLU A 1 1314 ? 130.130 191.262 121.682 1.00 74.72  ? 1314 GLU A CD    1 
ATOM   8396  O  OE1   . GLU A 1 1314 ? 129.477 190.844 122.661 1.00 69.05  ? 1314 GLU A OE1   1 
ATOM   8397  O  OE2   . GLU A 1 1314 ? 131.123 192.009 121.798 1.00 76.53  ? 1314 GLU A OE2   1 
ATOM   8398  N  N     . ILE A 1 1315 ? 129.900 186.403 119.173 1.00 58.64  ? 1315 ILE A N     1 
ATOM   8399  C  CA    . ILE A 1 1315 ? 130.505 185.141 118.766 1.00 56.39  ? 1315 ILE A CA    1 
ATOM   8400  C  C     . ILE A 1 1315 ? 129.837 184.607 117.506 1.00 56.27  ? 1315 ILE A C     1 
ATOM   8401  O  O     . ILE A 1 1315 ? 130.514 184.141 116.584 1.00 59.60  ? 1315 ILE A O     1 
ATOM   8402  C  CB    . ILE A 1 1315 ? 130.451 184.123 119.919 1.00 53.59  ? 1315 ILE A CB    1 
ATOM   8403  C  CG1   . ILE A 1 1315 ? 131.295 184.610 121.096 1.00 50.65  ? 1315 ILE A CG1   1 
ATOM   8404  C  CG2   . ILE A 1 1315 ? 130.929 182.766 119.455 1.00 54.76  ? 1315 ILE A CG2   1 
ATOM   8405  C  CD1   . ILE A 1 1315 ? 131.056 183.842 122.367 1.00 53.34  ? 1315 ILE A CD1   1 
ATOM   8406  N  N     . TRP A 1 1316 ? 128.505 184.666 117.441 1.00 56.19  ? 1316 TRP A N     1 
ATOM   8407  C  CA    . TRP A 1 1316 ? 127.807 184.225 116.238 1.00 58.32  ? 1316 TRP A CA    1 
ATOM   8408  C  C     . TRP A 1 1316 ? 128.150 185.099 115.039 1.00 59.16  ? 1316 TRP A C     1 
ATOM   8409  O  O     . TRP A 1 1316 ? 128.299 184.595 113.922 1.00 58.33  ? 1316 TRP A O     1 
ATOM   8410  C  CB    . TRP A 1 1316 ? 126.299 184.198 116.474 1.00 60.47  ? 1316 TRP A CB    1 
ATOM   8411  C  CG    . TRP A 1 1316 ? 125.816 182.938 117.118 1.00 64.82  ? 1316 TRP A CG    1 
ATOM   8412  C  CD1   . TRP A 1 1316 ? 125.155 182.822 118.302 1.00 66.59  ? 1316 TRP A CD1   1 
ATOM   8413  C  CD2   . TRP A 1 1316 ? 125.936 181.610 116.594 1.00 67.55  ? 1316 TRP A CD2   1 
ATOM   8414  N  NE1   . TRP A 1 1316 ? 124.868 181.503 118.557 1.00 65.18  ? 1316 TRP A NE1   1 
ATOM   8415  C  CE2   . TRP A 1 1316 ? 125.336 180.740 117.521 1.00 66.71  ? 1316 TRP A CE2   1 
ATOM   8416  C  CE3   . TRP A 1 1316 ? 126.499 181.073 115.432 1.00 63.46  ? 1316 TRP A CE3   1 
ATOM   8417  C  CZ2   . TRP A 1 1316 ? 125.281 179.364 117.324 1.00 66.94  ? 1316 TRP A CZ2   1 
ATOM   8418  C  CZ3   . TRP A 1 1316 ? 126.444 179.708 115.239 1.00 62.44  ? 1316 TRP A CZ3   1 
ATOM   8419  C  CH2   . TRP A 1 1316 ? 125.840 178.869 116.179 1.00 67.36  ? 1316 TRP A CH2   1 
ATOM   8420  N  N     . LYS A 1 1317 ? 128.290 186.410 115.245 1.00 60.30  ? 1317 LYS A N     1 
ATOM   8421  C  CA    . LYS A 1 1317 ? 128.653 187.284 114.133 1.00 61.79  ? 1317 LYS A CA    1 
ATOM   8422  C  C     . LYS A 1 1317 ? 130.032 186.928 113.586 1.00 59.96  ? 1317 LYS A C     1 
ATOM   8423  O  O     . LYS A 1 1317 ? 130.231 186.835 112.366 1.00 60.89  ? 1317 LYS A O     1 
ATOM   8424  C  CB    . LYS A 1 1317 ? 128.607 188.743 114.584 1.00 61.38  ? 1317 LYS A CB    1 
ATOM   8425  C  CG    . LYS A 1 1317 ? 128.939 189.727 113.487 1.00 67.78  ? 1317 LYS A CG    1 
ATOM   8426  C  CD    . LYS A 1 1317 ? 129.104 191.132 114.031 1.00 76.62  ? 1317 LYS A CD    1 
ATOM   8427  C  CE    . LYS A 1 1317 ? 130.197 191.868 113.286 1.00 78.24  ? 1317 LYS A CE    1 
ATOM   8428  N  NZ    . LYS A 1 1317 ? 129.869 191.982 111.837 1.00 75.84  ? 1317 LYS A NZ    1 
ATOM   8429  N  N     . VAL A 1 1318 ? 130.998 186.707 114.481 1.00 58.22  ? 1318 VAL A N     1 
ATOM   8430  C  CA    . VAL A 1 1318 ? 132.348 186.367 114.040 1.00 55.83  ? 1318 VAL A CA    1 
ATOM   8431  C  C     . VAL A 1 1318 ? 132.367 184.997 113.372 1.00 53.63  ? 1318 VAL A C     1 
ATOM   8432  O  O     . VAL A 1 1318 ? 133.045 184.796 112.358 1.00 56.96  ? 1318 VAL A O     1 
ATOM   8433  C  CB    . VAL A 1 1318 ? 133.331 186.439 115.221 1.00 54.63  ? 1318 VAL A CB    1 
ATOM   8434  C  CG1   . VAL A 1 1318 ? 134.670 185.856 114.825 1.00 48.25  ? 1318 VAL A CG1   1 
ATOM   8435  C  CG2   . VAL A 1 1318 ? 133.497 187.877 115.678 1.00 51.36  ? 1318 VAL A CG2   1 
ATOM   8436  N  N     . ALA A 1 1319 ? 131.625 184.034 113.923 1.00 53.71  ? 1319 ALA A N     1 
ATOM   8437  C  CA    . ALA A 1 1319 ? 131.555 182.713 113.308 1.00 54.60  ? 1319 ALA A CA    1 
ATOM   8438  C  C     . ALA A 1 1319 ? 130.906 182.769 111.934 1.00 57.35  ? 1319 ALA A C     1 
ATOM   8439  O  O     . ALA A 1 1319 ? 131.275 181.999 111.042 1.00 59.21  ? 1319 ALA A O     1 
ATOM   8440  C  CB    . ALA A 1 1319 ? 130.791 181.750 114.214 1.00 52.92  ? 1319 ALA A CB    1 
ATOM   8441  N  N     . ASP A 1 1320 ? 129.934 183.662 111.747 1.00 60.97  ? 1320 ASP A N     1 
ATOM   8442  C  CA    . ASP A 1 1320 ? 129.329 183.832 110.433 1.00 62.63  ? 1320 ASP A CA    1 
ATOM   8443  C  C     . ASP A 1 1320 ? 130.319 184.439 109.449 1.00 62.71  ? 1320 ASP A C     1 
ATOM   8444  O  O     . ASP A 1 1320 ? 130.391 184.011 108.291 1.00 59.45  ? 1320 ASP A O     1 
ATOM   8445  C  CB    . ASP A 1 1320 ? 128.077 184.702 110.543 1.00 65.57  ? 1320 ASP A CB    1 
ATOM   8446  C  CG    . ASP A 1 1320 ? 127.007 184.309 109.552 1.00 71.02  ? 1320 ASP A CG    1 
ATOM   8447  O  OD1   . ASP A 1 1320 ? 127.363 183.841 108.451 1.00 73.97  ? 1320 ASP A OD1   1 
ATOM   8448  O  OD2   . ASP A 1 1320 ? 125.812 184.467 109.873 1.00 70.68  ? 1320 ASP A OD2   1 
ATOM   8449  N  N     . GLU A 1 1321 ? 131.088 185.437 109.889 1.00 64.76  ? 1321 GLU A N     1 
ATOM   8450  C  CA    . GLU A 1 1321 ? 132.096 186.022 109.008 1.00 60.33  ? 1321 GLU A CA    1 
ATOM   8451  C  C     . GLU A 1 1321 ? 133.156 184.999 108.614 1.00 57.90  ? 1321 GLU A C     1 
ATOM   8452  O  O     . GLU A 1 1321 ? 133.555 184.926 107.446 1.00 58.40  ? 1321 GLU A O     1 
ATOM   8453  C  CB    . GLU A 1 1321 ? 132.749 187.232 109.673 1.00 57.96  ? 1321 GLU A CB    1 
ATOM   8454  C  CG    . GLU A 1 1321 ? 131.992 188.527 109.469 1.00 67.58  ? 1321 GLU A CG    1 
ATOM   8455  C  CD    . GLU A 1 1321 ? 132.758 189.730 109.978 1.00 81.42  ? 1321 GLU A CD    1 
ATOM   8456  O  OE1   . GLU A 1 1321 ? 133.718 189.542 110.754 1.00 74.95  ? 1321 GLU A OE1   1 
ATOM   8457  O  OE2   . GLU A 1 1321 ? 132.400 190.866 109.602 1.00 88.83  ? 1321 GLU A OE2   1 
ATOM   8458  N  N     . VAL A 1 1322 ? 133.623 184.195 109.572 1.00 58.79  ? 1322 VAL A N     1 
ATOM   8459  C  CA    . VAL A 1 1322 ? 134.689 183.232 109.298 1.00 55.51  ? 1322 VAL A CA    1 
ATOM   8460  C  C     . VAL A 1 1322 ? 134.180 181.997 108.569 1.00 56.09  ? 1322 VAL A C     1 
ATOM   8461  O  O     . VAL A 1 1322 ? 134.967 181.300 107.917 1.00 56.28  ? 1322 VAL A O     1 
ATOM   8462  C  CB    . VAL A 1 1322 ? 135.382 182.879 110.630 1.00 50.09  ? 1322 VAL A CB    1 
ATOM   8463  C  CG1   . VAL A 1 1322 ? 136.369 181.743 110.465 1.00 45.41  ? 1322 VAL A CG1   1 
ATOM   8464  C  CG2   . VAL A 1 1322 ? 136.084 184.102 111.192 1.00 48.69  ? 1322 VAL A CG2   1 
ATOM   8465  N  N     . GLY A 1 1323 ? 132.879 181.739 108.606 1.00 58.67  ? 1323 GLY A N     1 
ATOM   8466  C  CA    . GLY A 1 1323 ? 132.334 180.572 107.940 1.00 58.31  ? 1323 GLY A CA    1 
ATOM   8467  C  C     . GLY A 1 1323 ? 132.275 179.331 108.799 1.00 59.26  ? 1323 GLY A C     1 
ATOM   8468  O  O     . GLY A 1 1323 ? 132.475 178.221 108.294 1.00 62.02  ? 1323 GLY A O     1 
ATOM   8469  N  N     . LEU A 1 1324 ? 132.004 179.487 110.094 1.00 58.22  ? 1324 LEU A N     1 
ATOM   8470  C  CA    . LEU A 1 1324 ? 131.900 178.366 111.016 1.00 54.78  ? 1324 LEU A CA    1 
ATOM   8471  C  C     . LEU A 1 1324 ? 130.469 178.038 111.416 1.00 58.40  ? 1324 LEU A C     1 
ATOM   8472  O  O     . LEU A 1 1324 ? 130.261 177.065 112.147 1.00 64.14  ? 1324 LEU A O     1 
ATOM   8473  C  CB    . LEU A 1 1324 ? 132.719 178.644 112.280 1.00 51.32  ? 1324 LEU A CB    1 
ATOM   8474  C  CG    . LEU A 1 1324 ? 134.226 178.429 112.181 1.00 50.33  ? 1324 LEU A CG    1 
ATOM   8475  C  CD1   . LEU A 1 1324 ? 134.914 179.010 113.399 1.00 42.65  ? 1324 LEU A CD1   1 
ATOM   8476  C  CD2   . LEU A 1 1324 ? 134.533 176.950 112.036 1.00 47.33  ? 1324 LEU A CD2   1 
ATOM   8477  N  N     . ARG A 1 1325 ? 129.485 178.825 110.974 1.00 58.84  ? 1325 ARG A N     1 
ATOM   8478  C  CA    . ARG A 1 1325 ? 128.103 178.585 111.379 1.00 63.72  ? 1325 ARG A CA    1 
ATOM   8479  C  C     . ARG A 1 1325 ? 127.628 177.204 110.945 1.00 62.56  ? 1325 ARG A C     1 
ATOM   8480  O  O     . ARG A 1 1325 ? 126.994 176.480 111.720 1.00 63.56  ? 1325 ARG A O     1 
ATOM   8481  C  CB    . ARG A 1 1325 ? 127.189 179.668 110.810 1.00 62.61  ? 1325 ARG A CB    1 
ATOM   8482  C  CG    . ARG A 1 1325 ? 125.718 179.423 111.102 1.00 64.60  ? 1325 ARG A CG    1 
ATOM   8483  C  CD    . ARG A 1 1325 ? 124.845 180.552 110.600 1.00 68.83  ? 1325 ARG A CD    1 
ATOM   8484  N  NE    . ARG A 1 1325 ? 125.012 181.763 111.392 1.00 74.42  ? 1325 ARG A NE    1 
ATOM   8485  C  CZ    . ARG A 1 1325 ? 124.459 181.963 112.580 1.00 72.42  ? 1325 ARG A CZ    1 
ATOM   8486  N  NH1   . ARG A 1 1325 ? 123.695 181.046 113.152 1.00 70.32  ? 1325 ARG A NH1   1 
ATOM   8487  N  NH2   . ARG A 1 1325 ? 124.674 183.114 113.210 1.00 66.92  ? 1325 ARG A NH2   1 
ATOM   8488  N  N     . SER A 1 1326 ? 127.921 176.823 109.701 1.00 60.31  ? 1326 SER A N     1 
ATOM   8489  C  CA    . SER A 1 1326 ? 127.494 175.517 109.210 1.00 61.16  ? 1326 SER A CA    1 
ATOM   8490  C  C     . SER A 1 1326 ? 128.163 174.389 109.986 1.00 61.89  ? 1326 SER A C     1 
ATOM   8491  O  O     . SER A 1 1326 ? 127.552 173.340 110.222 1.00 61.21  ? 1326 SER A O     1 
ATOM   8492  C  CB    . SER A 1 1326 ? 127.792 175.396 107.717 1.00 64.31  ? 1326 SER A CB    1 
ATOM   8493  O  OG    . SER A 1 1326 ? 126.912 176.202 106.953 1.00 70.35  ? 1326 SER A OG    1 
ATOM   8494  N  N     . VAL A 1 1327 ? 129.420 174.583 110.385 1.00 61.26  ? 1327 VAL A N     1 
ATOM   8495  C  CA    . VAL A 1 1327 ? 130.144 173.544 111.110 1.00 57.96  ? 1327 VAL A CA    1 
ATOM   8496  C  C     . VAL A 1 1327 ? 129.593 173.387 112.521 1.00 59.84  ? 1327 VAL A C     1 
ATOM   8497  O  O     . VAL A 1 1327 ? 129.428 172.267 113.017 1.00 62.38  ? 1327 VAL A O     1 
ATOM   8498  C  CB    . VAL A 1 1327 ? 131.649 173.862 111.121 1.00 54.66  ? 1327 VAL A CB    1 
ATOM   8499  C  CG1   . VAL A 1 1327 ? 132.420 172.766 111.833 1.00 51.23  ? 1327 VAL A CG1   1 
ATOM   8500  C  CG2   . VAL A 1 1327 ? 132.154 174.053 109.704 1.00 53.37  ? 1327 VAL A CG2   1 
ATOM   8501  N  N     . ILE A 1 1328 ? 129.302 174.504 113.191 1.00 58.74  ? 1328 ILE A N     1 
ATOM   8502  C  CA    . ILE A 1 1328 ? 128.839 174.445 114.574 1.00 58.54  ? 1328 ILE A CA    1 
ATOM   8503  C  C     . ILE A 1 1328 ? 127.439 173.850 114.649 1.00 60.57  ? 1328 ILE A C     1 
ATOM   8504  O  O     . ILE A 1 1328 ? 127.142 173.036 115.531 1.00 63.89  ? 1328 ILE A O     1 
ATOM   8505  C  CB    . ILE A 1 1328 ? 128.900 175.844 115.211 1.00 60.52  ? 1328 ILE A CB    1 
ATOM   8506  C  CG1   . ILE A 1 1328 ? 130.354 176.298 115.340 1.00 57.95  ? 1328 ILE A CG1   1 
ATOM   8507  C  CG2   . ILE A 1 1328 ? 128.229 175.845 116.572 1.00 58.30  ? 1328 ILE A CG2   1 
ATOM   8508  C  CD1   . ILE A 1 1328 ? 130.511 177.767 115.618 1.00 55.92  ? 1328 ILE A CD1   1 
ATOM   8509  N  N     . GLU A 1 1329 ? 126.563 174.228 113.717 1.00 60.38  ? 1329 GLU A N     1 
ATOM   8510  C  CA    . GLU A 1 1329 ? 125.200 173.711 113.696 1.00 61.70  ? 1329 GLU A CA    1 
ATOM   8511  C  C     . GLU A 1 1329 ? 125.134 172.232 113.341 1.00 60.14  ? 1329 GLU A C     1 
ATOM   8512  O  O     . GLU A 1 1329 ? 124.067 171.626 113.476 1.00 60.09  ? 1329 GLU A O     1 
ATOM   8513  C  CB    . GLU A 1 1329 ? 124.357 174.522 112.712 1.00 66.24  ? 1329 GLU A CB    1 
ATOM   8514  C  CG    . GLU A 1 1329 ? 124.056 175.935 113.184 1.00 70.18  ? 1329 GLU A CG    1 
ATOM   8515  C  CD    . GLU A 1 1329 ? 123.176 176.698 112.217 1.00 77.59  ? 1329 GLU A CD    1 
ATOM   8516  O  OE1   . GLU A 1 1329 ? 122.692 176.084 111.244 1.00 82.59  ? 1329 GLU A OE1   1 
ATOM   8517  O  OE2   . GLU A 1 1329 ? 122.976 177.913 112.423 1.00 77.43  ? 1329 GLU A OE2   1 
ATOM   8518  N  N     . GLN A 1 1330 ? 126.241 171.647 112.880 1.00 61.37  ? 1330 GLN A N     1 
ATOM   8519  C  CA    . GLN A 1 1330 ? 126.273 170.222 112.568 1.00 60.00  ? 1330 GLN A CA    1 
ATOM   8520  C  C     . GLN A 1 1330 ? 126.073 169.361 113.809 1.00 60.44  ? 1330 GLN A C     1 
ATOM   8521  O  O     . GLN A 1 1330 ? 125.562 168.240 113.710 1.00 59.36  ? 1330 GLN A O     1 
ATOM   8522  C  CB    . GLN A 1 1330 ? 127.603 169.884 111.892 1.00 60.71  ? 1330 GLN A CB    1 
ATOM   8523  C  CG    . GLN A 1 1330 ? 127.756 168.451 111.423 1.00 62.73  ? 1330 GLN A CG    1 
ATOM   8524  C  CD    . GLN A 1 1330 ? 129.133 168.181 110.852 1.00 61.93  ? 1330 GLN A CD    1 
ATOM   8525  O  OE1   . GLN A 1 1330 ? 129.850 169.105 110.468 1.00 60.34  ? 1330 GLN A OE1   1 
ATOM   8526  N  NE2   . GLN A 1 1330 ? 129.518 166.912 110.808 1.00 55.55  ? 1330 GLN A NE2   1 
ATOM   8527  N  N     . PHE A 1 1331 ? 126.470 169.861 114.981 1.00 61.77  ? 1331 PHE A N     1 
ATOM   8528  C  CA    . PHE A 1 1331 ? 126.544 169.133 116.238 1.00 58.66  ? 1331 PHE A CA    1 
ATOM   8529  C  C     . PHE A 1 1331 ? 125.321 169.404 117.113 1.00 61.19  ? 1331 PHE A C     1 
ATOM   8530  O  O     . PHE A 1 1331 ? 124.677 170.449 116.984 1.00 61.40  ? 1331 PHE A O     1 
ATOM   8531  C  CB    . PHE A 1 1331 ? 127.818 169.516 116.983 1.00 56.50  ? 1331 PHE A CB    1 
ATOM   8532  C  CG    . PHE A 1 1331 ? 129.066 169.211 116.214 1.00 55.19  ? 1331 PHE A CG    1 
ATOM   8533  C  CD1   . PHE A 1 1331 ? 129.455 167.900 116.003 1.00 54.62  ? 1331 PHE A CD1   1 
ATOM   8534  C  CD2   . PHE A 1 1331 ? 129.835 170.228 115.680 1.00 55.41  ? 1331 PHE A CD2   1 
ATOM   8535  C  CE1   . PHE A 1 1331 ? 130.592 167.608 115.287 1.00 56.87  ? 1331 PHE A CE1   1 
ATOM   8536  C  CE2   . PHE A 1 1331 ? 130.977 169.941 114.962 1.00 56.86  ? 1331 PHE A CE2   1 
ATOM   8537  C  CZ    . PHE A 1 1331 ? 131.354 168.628 114.766 1.00 56.25  ? 1331 PHE A CZ    1 
ATOM   8538  N  N     . PRO A 1 1332 ? 124.985 168.457 118.001 1.00 62.72  ? 1332 PRO A N     1 
ATOM   8539  C  CA    . PRO A 1 1332 ? 123.757 168.602 118.807 1.00 66.61  ? 1332 PRO A CA    1 
ATOM   8540  C  C     . PRO A 1 1332 ? 123.659 169.898 119.595 1.00 70.66  ? 1332 PRO A C     1 
ATOM   8541  O  O     . PRO A 1 1332 ? 122.689 170.650 119.428 1.00 72.34  ? 1332 PRO A O     1 
ATOM   8542  C  CB    . PRO A 1 1332 ? 123.817 167.378 119.732 1.00 62.46  ? 1332 PRO A CB    1 
ATOM   8543  C  CG    . PRO A 1 1332 ? 124.598 166.378 118.972 1.00 59.16  ? 1332 PRO A CG    1 
ATOM   8544  C  CD    . PRO A 1 1332 ? 125.637 167.158 118.228 1.00 58.89  ? 1332 PRO A CD    1 
ATOM   8545  N  N     . GLY A 1 1333 ? 124.628 170.179 120.459 1.00 66.17  ? 1333 GLY A N     1 
ATOM   8546  C  CA    . GLY A 1 1333 ? 124.612 171.416 121.212 1.00 59.41  ? 1333 GLY A CA    1 
ATOM   8547  C  C     . GLY A 1 1333 ? 125.267 172.553 120.457 1.00 62.17  ? 1333 GLY A C     1 
ATOM   8548  O  O     . GLY A 1 1333 ? 126.494 172.610 120.343 1.00 62.46  ? 1333 GLY A O     1 
ATOM   8549  N  N     . LYS A 1 1334 ? 124.457 173.466 119.932 1.00 61.89  ? 1334 LYS A N     1 
ATOM   8550  C  CA    . LYS A 1 1334 ? 124.975 174.584 119.153 1.00 64.96  ? 1334 LYS A CA    1 
ATOM   8551  C  C     . LYS A 1 1334 ? 125.719 175.538 120.078 1.00 64.95  ? 1334 LYS A C     1 
ATOM   8552  O  O     . LYS A 1 1334 ? 125.101 176.216 120.907 1.00 69.16  ? 1334 LYS A O     1 
ATOM   8553  C  CB    . LYS A 1 1334 ? 123.830 175.286 118.432 1.00 66.86  ? 1334 LYS A CB    1 
ATOM   8554  C  CG    . LYS A 1 1334 ? 123.187 174.436 117.353 1.00 69.52  ? 1334 LYS A CG    1 
ATOM   8555  C  CD    . LYS A 1 1334 ? 121.984 175.128 116.744 1.00 75.46  ? 1334 LYS A CD    1 
ATOM   8556  C  CE    . LYS A 1 1334 ? 120.902 175.349 117.786 1.00 78.17  ? 1334 LYS A CE    1 
ATOM   8557  N  NZ    . LYS A 1 1334 ? 120.450 174.061 118.382 1.00 73.79  ? 1334 LYS A NZ    1 
ATOM   8558  N  N     . LEU A 1 1335 ? 127.049 175.563 119.950 1.00 59.20  ? 1335 LEU A N     1 
ATOM   8559  C  CA    . LEU A 1 1335 ? 127.958 176.383 120.749 1.00 54.94  ? 1335 LEU A CA    1 
ATOM   8560  C  C     . LEU A 1 1335 ? 128.105 175.833 122.163 1.00 51.55  ? 1335 LEU A C     1 
ATOM   8561  O  O     . LEU A 1 1335 ? 128.892 176.356 122.957 1.00 47.36  ? 1335 LEU A O     1 
ATOM   8562  C  CB    . LEU A 1 1335 ? 127.501 177.844 120.783 1.00 54.91  ? 1335 LEU A CB    1 
ATOM   8563  C  CG    . LEU A 1 1335 ? 128.597 178.901 120.688 1.00 52.20  ? 1335 LEU A CG    1 
ATOM   8564  C  CD1   . LEU A 1 1335 ? 129.241 178.863 119.315 1.00 51.42  ? 1335 LEU A CD1   1 
ATOM   8565  C  CD2   . LEU A 1 1335 ? 128.030 180.281 120.974 1.00 56.85  ? 1335 LEU A CD2   1 
ATOM   8566  N  N     . ASP A 1 1336 ? 127.360 174.778 122.486 1.00 55.76  ? 1336 ASP A N     1 
ATOM   8567  C  CA    . ASP A 1 1336 ? 127.477 174.089 123.764 1.00 54.18  ? 1336 ASP A CA    1 
ATOM   8568  C  C     . ASP A 1 1336 ? 128.053 172.686 123.630 1.00 50.30  ? 1336 ASP A C     1 
ATOM   8569  O  O     . ASP A 1 1336 ? 128.100 171.953 124.622 1.00 44.20  ? 1336 ASP A O     1 
ATOM   8570  C  CB    . ASP A 1 1336 ? 126.113 174.019 124.459 1.00 57.91  ? 1336 ASP A CB    1 
ATOM   8571  C  CG    . ASP A 1 1336 ? 125.843 175.226 125.334 1.00 66.17  ? 1336 ASP A CG    1 
ATOM   8572  O  OD1   . ASP A 1 1336 ? 126.450 175.326 126.422 1.00 67.78  ? 1336 ASP A OD1   1 
ATOM   8573  O  OD2   . ASP A 1 1336 ? 125.019 176.076 124.937 1.00 64.43  ? 1336 ASP A OD2   1 
ATOM   8574  N  N     . PHE A 1 1337 ? 128.472 172.290 122.432 1.00 49.28  ? 1337 PHE A N     1 
ATOM   8575  C  CA    . PHE A 1 1337 ? 129.006 170.953 122.213 1.00 47.62  ? 1337 PHE A CA    1 
ATOM   8576  C  C     . PHE A 1 1337 ? 130.415 170.862 122.790 1.00 47.38  ? 1337 PHE A C     1 
ATOM   8577  O  O     . PHE A 1 1337 ? 131.265 171.709 122.501 1.00 49.10  ? 1337 PHE A O     1 
ATOM   8578  C  CB    . PHE A 1 1337 ? 129.005 170.634 120.721 1.00 49.42  ? 1337 PHE A CB    1 
ATOM   8579  C  CG    . PHE A 1 1337 ? 129.510 169.263 120.388 1.00 49.56  ? 1337 PHE A CG    1 
ATOM   8580  C  CD1   . PHE A 1 1337 ? 128.669 168.169 120.474 1.00 51.18  ? 1337 PHE A CD1   1 
ATOM   8581  C  CD2   . PHE A 1 1337 ? 130.816 169.068 119.980 1.00 47.90  ? 1337 PHE A CD2   1 
ATOM   8582  C  CE1   . PHE A 1 1337 ? 129.120 166.909 120.166 1.00 50.72  ? 1337 PHE A CE1   1 
ATOM   8583  C  CE2   . PHE A 1 1337 ? 131.274 167.809 119.673 1.00 47.97  ? 1337 PHE A CE2   1 
ATOM   8584  C  CZ    . PHE A 1 1337 ? 130.425 166.728 119.764 1.00 50.23  ? 1337 PHE A CZ    1 
ATOM   8585  N  N     . VAL A 1 1338 ? 130.659 169.847 123.614 1.00 43.01  ? 1338 VAL A N     1 
ATOM   8586  C  CA    . VAL A 1 1338 ? 131.955 169.671 124.263 1.00 43.40  ? 1338 VAL A CA    1 
ATOM   8587  C  C     . VAL A 1 1338 ? 132.924 168.994 123.300 1.00 49.52  ? 1338 VAL A C     1 
ATOM   8588  O  O     . VAL A 1 1338 ? 132.661 167.891 122.810 1.00 51.78  ? 1338 VAL A O     1 
ATOM   8589  C  CB    . VAL A 1 1338 ? 131.814 168.865 125.560 1.00 41.34  ? 1338 VAL A CB    1 
ATOM   8590  C  CG1   . VAL A 1 1338 ? 133.179 168.592 126.166 1.00 44.55  ? 1338 VAL A CG1   1 
ATOM   8591  C  CG2   . VAL A 1 1338 ? 130.932 169.608 126.541 1.00 42.06  ? 1338 VAL A CG2   1 
ATOM   8592  N  N     . LEU A 1 1339 ? 134.050 169.654 123.030 1.00 47.02  ? 1339 LEU A N     1 
ATOM   8593  C  CA    . LEU A 1 1339 ? 135.086 169.094 122.172 1.00 44.89  ? 1339 LEU A CA    1 
ATOM   8594  C  C     . LEU A 1 1339 ? 136.056 168.250 122.990 1.00 49.33  ? 1339 LEU A C     1 
ATOM   8595  O  O     . LEU A 1 1339 ? 136.566 168.702 124.019 1.00 53.99  ? 1339 LEU A O     1 
ATOM   8596  C  CB    . LEU A 1 1339 ? 135.839 170.213 121.453 1.00 42.25  ? 1339 LEU A CB    1 
ATOM   8597  C  CG    . LEU A 1 1339 ? 135.022 171.039 120.462 1.00 39.69  ? 1339 LEU A CG    1 
ATOM   8598  C  CD1   . LEU A 1 1339 ? 135.775 172.288 120.056 1.00 37.46  ? 1339 LEU A CD1   1 
ATOM   8599  C  CD2   . LEU A 1 1339 ? 134.671 170.205 119.247 1.00 41.57  ? 1339 LEU A CD2   1 
ATOM   8600  N  N     . VAL A 1 1340 ? 136.320 167.027 122.527 1.00 50.49  ? 1340 VAL A N     1 
ATOM   8601  C  CA    . VAL A 1 1340 ? 137.198 166.099 123.225 1.00 53.52  ? 1340 VAL A CA    1 
ATOM   8602  C  C     . VAL A 1 1340 ? 138.299 165.644 122.277 1.00 59.51  ? 1340 VAL A C     1 
ATOM   8603  O  O     . VAL A 1 1340 ? 138.158 165.693 121.053 1.00 61.69  ? 1340 VAL A O     1 
ATOM   8604  C  CB    . VAL A 1 1340 ? 136.435 164.876 123.782 1.00 52.20  ? 1340 VAL A CB    1 
ATOM   8605  C  CG1   . VAL A 1 1340 ? 135.371 165.313 124.774 1.00 50.02  ? 1340 VAL A CG1   1 
ATOM   8606  C  CG2   . VAL A 1 1340 ? 135.825 164.072 122.654 1.00 58.19  ? 1340 VAL A CG2   1 
ATOM   8607  N  N     . ASP A 1 1341 ? 139.405 165.184 122.869 1.00 61.17  ? 1341 ASP A N     1 
ATOM   8608  C  CA    . ASP A 1 1341 ? 140.584 164.721 122.130 1.00 60.12  ? 1341 ASP A CA    1 
ATOM   8609  C  C     . ASP A 1 1341 ? 141.136 165.803 121.205 1.00 60.01  ? 1341 ASP A C     1 
ATOM   8610  O  O     . ASP A 1 1341 ? 141.534 165.532 120.071 1.00 59.76  ? 1341 ASP A O     1 
ATOM   8611  C  CB    . ASP A 1 1341 ? 140.283 163.444 121.341 1.00 61.35  ? 1341 ASP A CB    1 
ATOM   8612  C  CG    . ASP A 1 1341 ? 140.117 162.235 122.233 1.00 74.63  ? 1341 ASP A CG    1 
ATOM   8613  O  OD1   . ASP A 1 1341 ? 140.911 162.085 123.185 1.00 80.78  ? 1341 ASP A OD1   1 
ATOM   8614  O  OD2   . ASP A 1 1341 ? 139.199 161.427 121.977 1.00 78.39  ? 1341 ASP A OD2   1 
ATOM   8615  N  N     . GLY A 1 1342 ? 141.173 167.038 121.695 1.00 52.75  ? 1342 GLY A N     1 
ATOM   8616  C  CA    . GLY A 1 1342 ? 141.702 168.126 120.898 1.00 52.48  ? 1342 GLY A CA    1 
ATOM   8617  C  C     . GLY A 1 1342 ? 140.900 168.439 119.657 1.00 52.61  ? 1342 GLY A C     1 
ATOM   8618  O  O     . GLY A 1 1342 ? 141.482 168.782 118.625 1.00 54.88  ? 1342 GLY A O     1 
ATOM   8619  N  N     . GLY A 1 1343 ? 139.577 168.325 119.724 1.00 52.26  ? 1343 GLY A N     1 
ATOM   8620  C  CA    . GLY A 1 1343 ? 138.738 168.591 118.573 1.00 43.94  ? 1343 GLY A CA    1 
ATOM   8621  C  C     . GLY A 1 1343 ? 138.847 167.532 117.498 1.00 43.33  ? 1343 GLY A C     1 
ATOM   8622  O  O     . GLY A 1 1343 ? 138.976 167.848 116.313 1.00 40.57  ? 1343 GLY A O     1 
ATOM   8623  N  N     . CYS A 1 1344 ? 138.805 166.262 117.906 1.00 48.46  ? 1344 CYS A N     1 
ATOM   8624  C  CA    . CYS A 1 1344 ? 138.915 165.163 116.954 1.00 47.13  ? 1344 CYS A CA    1 
ATOM   8625  C  C     . CYS A 1 1344 ? 137.760 165.130 115.962 1.00 43.18  ? 1344 CYS A C     1 
ATOM   8626  O  O     . CYS A 1 1344 ? 137.904 164.547 114.884 1.00 44.16  ? 1344 CYS A O     1 
ATOM   8627  C  CB    . CYS A 1 1344 ? 138.998 163.831 117.701 1.00 51.29  ? 1344 CYS A CB    1 
ATOM   8628  S  SG    . CYS A 1 1344 ? 137.453 163.307 118.481 1.00 71.43  ? 1344 CYS A SG    1 
ATOM   8629  N  N     . VAL A 1 1345 ? 136.617 165.732 116.303 1.00 42.81  ? 1345 VAL A N     1 
ATOM   8630  C  CA    . VAL A 1 1345 ? 135.472 165.754 115.394 1.00 39.59  ? 1345 VAL A CA    1 
ATOM   8631  C  C     . VAL A 1 1345 ? 135.617 166.777 114.281 1.00 41.01  ? 1345 VAL A C     1 
ATOM   8632  O  O     . VAL A 1 1345 ? 134.797 166.790 113.356 1.00 40.99  ? 1345 VAL A O     1 
ATOM   8633  C  CB    . VAL A 1 1345 ? 134.159 166.032 116.150 1.00 38.90  ? 1345 VAL A CB    1 
ATOM   8634  C  CG1   . VAL A 1 1345 ? 133.903 164.950 117.189 1.00 41.08  ? 1345 VAL A CG1   1 
ATOM   8635  C  CG2   . VAL A 1 1345 ? 134.190 167.410 116.793 1.00 38.18  ? 1345 VAL A CG2   1 
ATOM   8636  N  N     . LEU A 1 1346 ? 136.625 167.639 114.345 1.00 40.59  ? 1346 LEU A N     1 
ATOM   8637  C  CA    . LEU A 1 1346 ? 136.816 168.680 113.348 1.00 36.29  ? 1346 LEU A CA    1 
ATOM   8638  C  C     . LEU A 1 1346 ? 137.795 168.240 112.268 1.00 36.92  ? 1346 LEU A C     1 
ATOM   8639  O  O     . LEU A 1 1346 ? 138.634 167.361 112.478 1.00 40.14  ? 1346 LEU A O     1 
ATOM   8640  C  CB    . LEU A 1 1346 ? 137.316 169.966 114.005 1.00 34.35  ? 1346 LEU A CB    1 
ATOM   8641  C  CG    . LEU A 1 1346 ? 136.344 170.679 114.943 1.00 32.86  ? 1346 LEU A CG    1 
ATOM   8642  C  CD1   . LEU A 1 1346 ? 137.037 171.822 115.656 1.00 32.07  ? 1346 LEU A CD1   1 
ATOM   8643  C  CD2   . LEU A 1 1346 ? 135.140 171.181 114.174 1.00 36.08  ? 1346 LEU A CD2   1 
ATOM   8644  N  N     . SER A 1 1347 ? 137.668 168.856 111.097 1.00 36.90  ? 1347 SER A N     1 
ATOM   8645  C  CA    . SER A 1 1347 ? 138.639 168.676 110.034 1.00 34.27  ? 1347 SER A CA    1 
ATOM   8646  C  C     . SER A 1 1347 ? 139.888 169.510 110.315 1.00 37.58  ? 1347 SER A C     1 
ATOM   8647  O  O     . SER A 1 1347 ? 139.955 170.281 111.274 1.00 40.46  ? 1347 SER A O     1 
ATOM   8648  C  CB    . SER A 1 1347 ? 138.038 169.066 108.687 1.00 30.27  ? 1347 SER A CB    1 
ATOM   8649  O  OG    . SER A 1 1347 ? 136.902 168.279 108.399 1.00 35.36  ? 1347 SER A OG    1 
ATOM   8650  N  N     . HIS A 1 1348 ? 140.895 169.337 109.460 1.00 35.28  ? 1348 HIS A N     1 
ATOM   8651  C  CA    . HIS A 1 1348 ? 142.119 170.117 109.599 1.00 34.11  ? 1348 HIS A CA    1 
ATOM   8652  C  C     . HIS A 1 1348 ? 141.877 171.596 109.316 1.00 36.61  ? 1348 HIS A C     1 
ATOM   8653  O  O     . HIS A 1 1348 ? 142.462 172.460 109.978 1.00 40.64  ? 1348 HIS A O     1 
ATOM   8654  C  CB    . HIS A 1 1348 ? 143.200 169.554 108.680 1.00 37.05  ? 1348 HIS A CB    1 
ATOM   8655  C  CG    . HIS A 1 1348 ? 144.592 169.930 109.080 1.00 40.72  ? 1348 HIS A CG    1 
ATOM   8656  N  ND1   . HIS A 1 1348 ? 145.384 169.117 109.862 1.00 40.02  ? 1348 HIS A ND1   1 
ATOM   8657  C  CD2   . HIS A 1 1348 ? 145.338 171.023 108.795 1.00 40.93  ? 1348 HIS A CD2   1 
ATOM   8658  C  CE1   . HIS A 1 1348 ? 146.555 169.699 110.049 1.00 42.55  ? 1348 HIS A CE1   1 
ATOM   8659  N  NE2   . HIS A 1 1348 ? 146.553 170.856 109.411 1.00 41.91  ? 1348 HIS A NE2   1 
ATOM   8660  N  N     . GLY A 1 1349 ? 141.031 171.911 108.330 1.00 32.99  ? 1349 GLY A N     1 
ATOM   8661  C  CA    . GLY A 1 1349 ? 140.742 173.298 108.005 1.00 28.99  ? 1349 GLY A CA    1 
ATOM   8662  C  C     . GLY A 1 1349 ? 139.798 173.992 108.963 1.00 34.99  ? 1349 GLY A C     1 
ATOM   8663  O  O     . GLY A 1 1349 ? 139.857 175.220 109.103 1.00 37.04  ? 1349 GLY A O     1 
ATOM   8664  N  N     . HIS A 1 1350 ? 138.934 173.234 109.637 1.00 36.16  ? 1350 HIS A N     1 
ATOM   8665  C  CA    . HIS A 1 1350 ? 138.063 173.841 110.633 1.00 32.07  ? 1350 HIS A CA    1 
ATOM   8666  C  C     . HIS A 1 1350 ? 138.862 174.375 111.811 1.00 34.47  ? 1350 HIS A C     1 
ATOM   8667  O  O     . HIS A 1 1350 ? 138.475 175.378 112.417 1.00 38.43  ? 1350 HIS A O     1 
ATOM   8668  C  CB    . HIS A 1 1350 ? 137.018 172.831 111.096 1.00 30.89  ? 1350 HIS A CB    1 
ATOM   8669  C  CG    . HIS A 1 1350 ? 136.090 172.392 110.009 1.00 37.46  ? 1350 HIS A CG    1 
ATOM   8670  N  ND1   . HIS A 1 1350 ? 135.432 171.181 110.033 1.00 39.40  ? 1350 HIS A ND1   1 
ATOM   8671  C  CD2   . HIS A 1 1350 ? 135.717 173.001 108.859 1.00 36.71  ? 1350 HIS A CD2   1 
ATOM   8672  C  CE1   . HIS A 1 1350 ? 134.690 171.066 108.946 1.00 37.51  ? 1350 HIS A CE1   1 
ATOM   8673  N  NE2   . HIS A 1 1350 ? 134.845 172.156 108.217 1.00 33.99  ? 1350 HIS A NE2   1 
ATOM   8674  N  N     . LYS A 1 1351 ? 139.994 173.746 112.126 1.00 33.81  ? 1351 LYS A N     1 
ATOM   8675  C  CA    . LYS A 1 1351 ? 140.867 174.269 113.170 1.00 34.96  ? 1351 LYS A CA    1 
ATOM   8676  C  C     . LYS A 1 1351 ? 141.549 175.562 112.733 1.00 32.96  ? 1351 LYS A C     1 
ATOM   8677  O  O     . LYS A 1 1351 ? 141.728 176.480 113.546 1.00 36.39  ? 1351 LYS A O     1 
ATOM   8678  C  CB    . LYS A 1 1351 ? 141.900 173.211 113.538 1.00 37.89  ? 1351 LYS A CB    1 
ATOM   8679  C  CG    . LYS A 1 1351 ? 141.300 171.960 114.153 1.00 34.03  ? 1351 LYS A CG    1 
ATOM   8680  C  CD    . LYS A 1 1351 ? 142.386 171.042 114.674 1.00 38.68  ? 1351 LYS A CD    1 
ATOM   8681  C  CE    . LYS A 1 1351 ? 141.815 169.727 115.158 1.00 37.71  ? 1351 LYS A CE    1 
ATOM   8682  N  NZ    . LYS A 1 1351 ? 141.385 168.881 114.017 1.00 38.99  ? 1351 LYS A NZ    1 
ATOM   8683  N  N     . GLN A 1 1352 ? 141.916 175.661 111.454 1.00 28.28  ? 1352 GLN A N     1 
ATOM   8684  C  CA    . GLN A 1 1352 ? 142.434 176.918 110.927 1.00 32.61  ? 1352 GLN A CA    1 
ATOM   8685  C  C     . GLN A 1 1352 ? 141.388 178.018 111.035 1.00 36.75  ? 1352 GLN A C     1 
ATOM   8686  O  O     . GLN A 1 1352 ? 141.706 179.159 111.390 1.00 40.53  ? 1352 GLN A O     1 
ATOM   8687  C  CB    . GLN A 1 1352 ? 142.858 176.739 109.468 1.00 38.33  ? 1352 GLN A CB    1 
ATOM   8688  C  CG    . GLN A 1 1352 ? 143.917 175.672 109.207 1.00 38.54  ? 1352 GLN A CG    1 
ATOM   8689  C  CD    . GLN A 1 1352 ? 145.203 175.904 109.968 1.00 45.59  ? 1352 GLN A CD    1 
ATOM   8690  O  OE1   . GLN A 1 1352 ? 145.756 174.986 110.571 1.00 45.84  ? 1352 GLN A OE1   1 
ATOM   8691  N  NE2   . GLN A 1 1352 ? 145.699 177.132 109.927 1.00 45.68  ? 1352 GLN A NE2   1 
ATOM   8692  N  N     . LEU A 1 1353 ? 140.131 177.684 110.743 1.00 36.10  ? 1353 LEU A N     1 
ATOM   8693  C  CA    . LEU A 1 1353 ? 139.060 178.669 110.864 1.00 32.64  ? 1353 LEU A CA    1 
ATOM   8694  C  C     . LEU A 1 1353 ? 138.815 179.051 112.321 1.00 32.03  ? 1353 LEU A C     1 
ATOM   8695  O  O     . LEU A 1 1353 ? 138.471 180.200 112.616 1.00 35.39  ? 1353 LEU A O     1 
ATOM   8696  C  CB    . LEU A 1 1353 ? 137.783 178.135 110.221 1.00 36.46  ? 1353 LEU A CB    1 
ATOM   8697  C  CG    . LEU A 1 1353 ? 137.867 177.945 108.705 1.00 38.45  ? 1353 LEU A CG    1 
ATOM   8698  C  CD1   . LEU A 1 1353 ? 136.668 177.163 108.181 1.00 36.35  ? 1353 LEU A CD1   1 
ATOM   8699  C  CD2   . LEU A 1 1353 ? 138.005 179.280 107.996 1.00 39.12  ? 1353 LEU A CD2   1 
ATOM   8700  N  N     . MET A 1 1354 ? 138.975 178.102 113.245 1.00 31.26  ? 1354 MET A N     1 
ATOM   8701  C  CA    . MET A 1 1354 ? 138.867 178.422 114.667 1.00 31.03  ? 1354 MET A CA    1 
ATOM   8702  C  C     . MET A 1 1354 ? 139.945 179.410 115.091 1.00 31.84  ? 1354 MET A C     1 
ATOM   8703  O  O     . MET A 1 1354 ? 139.672 180.367 115.828 1.00 35.45  ? 1354 MET A O     1 
ATOM   8704  C  CB    . MET A 1 1354 ? 138.959 177.144 115.501 1.00 35.71  ? 1354 MET A CB    1 
ATOM   8705  C  CG    . MET A 1 1354 ? 137.758 176.218 115.381 1.00 39.73  ? 1354 MET A CG    1 
ATOM   8706  S  SD    . MET A 1 1354 ? 136.502 176.500 116.640 1.00 64.11  ? 1354 MET A SD    1 
ATOM   8707  C  CE    . MET A 1 1354 ? 137.503 176.536 118.123 1.00 45.67  ? 1354 MET A CE    1 
ATOM   8708  N  N     . CYS A 1 1355 ? 141.179 179.195 114.632 1.00 31.65  ? 1355 CYS A N     1 
ATOM   8709  C  CA    . CYS A 1 1355 ? 142.244 180.147 114.934 1.00 30.86  ? 1355 CYS A CA    1 
ATOM   8710  C  C     . CYS A 1 1355 ? 141.975 181.510 114.311 1.00 32.05  ? 1355 CYS A C     1 
ATOM   8711  O  O     . CYS A 1 1355 ? 142.253 182.544 114.932 1.00 33.52  ? 1355 CYS A O     1 
ATOM   8712  C  CB    . CYS A 1 1355 ? 143.591 179.609 114.457 1.00 34.62  ? 1355 CYS A CB    1 
ATOM   8713  S  SG    . CYS A 1 1355 ? 144.318 178.372 115.538 1.00 54.40  ? 1355 CYS A SG    1 
ATOM   8714  N  N     . LEU A 1 1356 ? 141.430 181.534 113.095 1.00 33.64  ? 1356 LEU A N     1 
ATOM   8715  C  CA    . LEU A 1 1356 ? 141.078 182.807 112.474 1.00 31.61  ? 1356 LEU A CA    1 
ATOM   8716  C  C     . LEU A 1 1356 ? 140.004 183.533 113.275 1.00 31.99  ? 1356 LEU A C     1 
ATOM   8717  O  O     . LEU A 1 1356 ? 140.072 184.755 113.448 1.00 36.67  ? 1356 LEU A O     1 
ATOM   8718  C  CB    . LEU A 1 1356 ? 140.615 182.574 111.038 1.00 36.30  ? 1356 LEU A CB    1 
ATOM   8719  C  CG    . LEU A 1 1356 ? 140.381 183.820 110.183 1.00 42.05  ? 1356 LEU A CG    1 
ATOM   8720  C  CD1   . LEU A 1 1356 ? 141.679 184.576 109.967 1.00 39.18  ? 1356 LEU A CD1   1 
ATOM   8721  C  CD2   . LEU A 1 1356 ? 139.746 183.455 108.855 1.00 41.58  ? 1356 LEU A CD2   1 
ATOM   8722  N  N     . ALA A 1 1357 ? 139.004 182.799 113.768 1.00 33.25  ? 1357 ALA A N     1 
ATOM   8723  C  CA    . ALA A 1 1357 ? 137.964 183.410 114.589 1.00 32.29  ? 1357 ALA A CA    1 
ATOM   8724  C  C     . ALA A 1 1357 ? 138.542 183.974 115.879 1.00 33.72  ? 1357 ALA A C     1 
ATOM   8725  O  O     . ALA A 1 1357 ? 138.168 185.073 116.306 1.00 36.76  ? 1357 ALA A O     1 
ATOM   8726  C  CB    . ALA A 1 1357 ? 136.867 182.392 114.893 1.00 31.82  ? 1357 ALA A CB    1 
ATOM   8727  N  N     . ARG A 1 1358 ? 139.465 183.242 116.509 1.00 35.18  ? 1358 ARG A N     1 
ATOM   8728  C  CA    . ARG A 1 1358 ? 140.113 183.770 117.708 1.00 32.06  ? 1358 ARG A CA    1 
ATOM   8729  C  C     . ARG A 1 1358 ? 140.866 185.057 117.403 1.00 32.01  ? 1358 ARG A C     1 
ATOM   8730  O  O     . ARG A 1 1358 ? 140.798 186.019 118.174 1.00 33.50  ? 1358 ARG A O     1 
ATOM   8731  C  CB    . ARG A 1 1358 ? 141.072 182.745 118.309 1.00 27.43  ? 1358 ARG A CB    1 
ATOM   8732  C  CG    . ARG A 1 1358 ? 140.432 181.531 118.935 1.00 26.65  ? 1358 ARG A CG    1 
ATOM   8733  C  CD    . ARG A 1 1358 ? 141.518 180.560 119.352 1.00 25.04  ? 1358 ARG A CD    1 
ATOM   8734  N  NE    . ARG A 1 1358 ? 140.991 179.300 119.854 1.00 28.21  ? 1358 ARG A NE    1 
ATOM   8735  C  CZ    . ARG A 1 1358 ? 141.730 178.223 120.080 1.00 32.41  ? 1358 ARG A CZ    1 
ATOM   8736  N  NH1   . ARG A 1 1358 ? 143.031 178.218 119.847 1.00 32.12  ? 1358 ARG A NH1   1 
ATOM   8737  N  NH2   . ARG A 1 1358 ? 141.148 177.124 120.546 1.00 34.56  ? 1358 ARG A NH2   1 
ATOM   8738  N  N     . SER A 1 1359 ? 141.592 185.093 116.285 1.00 34.26  ? 1359 SER A N     1 
ATOM   8739  C  CA    . SER A 1 1359 ? 142.343 186.298 115.945 1.00 36.56  ? 1359 SER A CA    1 
ATOM   8740  C  C     . SER A 1 1359 ? 141.420 187.468 115.626 1.00 40.58  ? 1359 SER A C     1 
ATOM   8741  O  O     . SER A 1 1359 ? 141.750 188.618 115.933 1.00 41.63  ? 1359 SER A O     1 
ATOM   8742  C  CB    . SER A 1 1359 ? 143.277 186.027 114.767 1.00 39.21  ? 1359 SER A CB    1 
ATOM   8743  O  OG    . SER A 1 1359 ? 142.574 186.089 113.539 1.00 39.69  ? 1359 SER A OG    1 
ATOM   8744  N  N     . VAL A 1 1360 ? 140.268 187.200 115.011 1.00 41.20  ? 1360 VAL A N     1 
ATOM   8745  C  CA    . VAL A 1 1360 ? 139.328 188.272 114.695 1.00 41.79  ? 1360 VAL A CA    1 
ATOM   8746  C  C     . VAL A 1 1360 ? 138.683 188.820 115.962 1.00 42.07  ? 1360 VAL A C     1 
ATOM   8747  O  O     . VAL A 1 1360 ? 138.467 190.031 116.087 1.00 42.75  ? 1360 VAL A O     1 
ATOM   8748  C  CB    . VAL A 1 1360 ? 138.271 187.772 113.693 1.00 40.01  ? 1360 VAL A CB    1 
ATOM   8749  C  CG1   . VAL A 1 1360 ? 137.107 188.741 113.620 1.00 41.81  ? 1360 VAL A CG1   1 
ATOM   8750  C  CG2   . VAL A 1 1360 ? 138.889 187.594 112.323 1.00 36.83  ? 1360 VAL A CG2   1 
ATOM   8751  N  N     . LEU A 1 1361 ? 138.377 187.946 116.924 1.00 42.94  ? 1361 LEU A N     1 
ATOM   8752  C  CA    . LEU A 1 1361 ? 137.660 188.380 118.119 1.00 41.92  ? 1361 LEU A CA    1 
ATOM   8753  C  C     . LEU A 1 1361 ? 138.459 189.406 118.916 1.00 45.71  ? 1361 LEU A C     1 
ATOM   8754  O  O     . LEU A 1 1361 ? 137.886 190.351 119.470 1.00 53.43  ? 1361 LEU A O     1 
ATOM   8755  C  CB    . LEU A 1 1361 ? 137.313 187.175 118.990 1.00 42.78  ? 1361 LEU A CB    1 
ATOM   8756  C  CG    . LEU A 1 1361 ? 135.931 186.566 118.745 1.00 42.91  ? 1361 LEU A CG    1 
ATOM   8757  C  CD1   . LEU A 1 1361 ? 135.807 185.220 119.438 1.00 43.25  ? 1361 LEU A CD1   1 
ATOM   8758  C  CD2   . LEU A 1 1361 ? 134.834 187.512 119.198 1.00 46.40  ? 1361 LEU A CD2   1 
ATOM   8759  N  N     . SER A 1 1362 ? 139.776 189.238 118.995 1.00 47.76  ? 1362 SER A N     1 
ATOM   8760  C  CA    . SER A 1 1362 ? 140.633 190.155 119.742 1.00 53.25  ? 1362 SER A CA    1 
ATOM   8761  C  C     . SER A 1 1362 ? 141.111 191.263 118.809 1.00 55.61  ? 1362 SER A C     1 
ATOM   8762  O  O     . SER A 1 1362 ? 141.882 191.010 117.877 1.00 55.79  ? 1362 SER A O     1 
ATOM   8763  C  CB    . SER A 1 1362 ? 141.818 189.415 120.352 1.00 49.77  ? 1362 SER A CB    1 
ATOM   8764  O  OG    . SER A 1 1362 ? 142.979 189.598 119.561 1.00 50.64  ? 1362 SER A OG    1 
ATOM   8765  N  N     . LYS A 1 1363 ? 140.667 192.490 119.066 1.00 54.53  ? 1363 LYS A N     1 
ATOM   8766  C  CA    . LYS A 1 1363 ? 141.010 193.636 118.226 1.00 57.98  ? 1363 LYS A CA    1 
ATOM   8767  C  C     . LYS A 1 1363 ? 142.426 194.082 118.567 1.00 64.00  ? 1363 LYS A C     1 
ATOM   8768  O  O     . LYS A 1 1363 ? 142.671 194.654 119.632 1.00 67.08  ? 1363 LYS A O     1 
ATOM   8769  C  CB    . LYS A 1 1363 ? 140.015 194.773 118.430 1.00 64.35  ? 1363 LYS A CB    1 
ATOM   8770  C  CG    . LYS A 1 1363 ? 138.553 194.381 118.272 1.00 63.06  ? 1363 LYS A CG    1 
ATOM   8771  C  CD    . LYS A 1 1363 ? 137.931 194.039 119.618 1.00 64.20  ? 1363 LYS A CD    1 
ATOM   8772  C  CE    . LYS A 1 1363 ? 136.432 193.816 119.508 1.00 68.57  ? 1363 LYS A CE    1 
ATOM   8773  N  NZ    . LYS A 1 1363 ? 136.105 192.557 118.785 1.00 68.23  ? 1363 LYS A NZ    1 
ATOM   8774  N  N     . ALA A 1 1364 ? 143.364 193.825 117.658 1.00 61.16  ? 1364 ALA A N     1 
ATOM   8775  C  CA    . ALA A 1 1364 ? 144.762 194.185 117.842 1.00 55.17  ? 1364 ALA A CA    1 
ATOM   8776  C  C     . ALA A 1 1364 ? 145.233 195.016 116.658 1.00 60.19  ? 1364 ALA A C     1 
ATOM   8777  O  O     . ALA A 1 1364 ? 144.675 194.934 115.561 1.00 61.92  ? 1364 ALA A O     1 
ATOM   8778  C  CB    . ALA A 1 1364 ? 145.647 192.947 117.995 1.00 50.06  ? 1364 ALA A CB    1 
ATOM   8779  N  N     . LYS A 1 1365 ? 146.261 195.832 116.892 1.00 58.24  ? 1365 LYS A N     1 
ATOM   8780  C  CA    . LYS A 1 1365 ? 146.776 196.712 115.852 1.00 55.28  ? 1365 LYS A CA    1 
ATOM   8781  C  C     . LYS A 1 1365 ? 147.961 196.129 115.097 1.00 51.22  ? 1365 LYS A C     1 
ATOM   8782  O  O     . LYS A 1 1365 ? 148.291 196.626 114.015 1.00 53.38  ? 1365 LYS A O     1 
ATOM   8783  C  CB    . LYS A 1 1365 ? 147.169 198.063 116.451 1.00 56.47  ? 1365 LYS A CB    1 
ATOM   8784  C  CG    . LYS A 1 1365 ? 146.001 198.795 117.082 1.00 65.84  ? 1365 LYS A CG    1 
ATOM   8785  C  CD    . LYS A 1 1365 ? 145.008 199.234 116.023 1.00 66.58  ? 1365 LYS A CD    1 
ATOM   8786  C  CE    . LYS A 1 1365 ? 145.529 200.410 115.225 1.00 70.47  ? 1365 LYS A CE    1 
ATOM   8787  N  NZ    . LYS A 1 1365 ? 144.539 200.861 114.214 1.00 71.61  ? 1365 LYS A NZ    1 
ATOM   8788  N  N     . ILE A 1 1366 ? 148.610 195.101 115.635 1.00 48.02  ? 1366 ILE A N     1 
ATOM   8789  C  CA    . ILE A 1 1366 ? 149.683 194.393 114.950 1.00 46.98  ? 1366 ILE A CA    1 
ATOM   8790  C  C     . ILE A 1 1366 ? 149.347 192.910 114.967 1.00 44.17  ? 1366 ILE A C     1 
ATOM   8791  O  O     . ILE A 1 1366 ? 149.018 192.357 116.021 1.00 45.78  ? 1366 ILE A O     1 
ATOM   8792  C  CB    . ILE A 1 1366 ? 151.055 194.652 115.601 1.00 43.92  ? 1366 ILE A CB    1 
ATOM   8793  C  CG1   . ILE A 1 1366 ? 151.328 196.154 115.679 1.00 44.97  ? 1366 ILE A CG1   1 
ATOM   8794  C  CG2   . ILE A 1 1366 ? 152.152 193.959 114.817 1.00 45.33  ? 1366 ILE A CG2   1 
ATOM   8795  C  CD1   . ILE A 1 1366 ? 152.574 196.505 116.441 1.00 44.22  ? 1366 ILE A CD1   1 
ATOM   8796  N  N     . LEU A 1 1367 ? 149.422 192.270 113.803 1.00 39.71  ? 1367 LEU A N     1 
ATOM   8797  C  CA    . LEU A 1 1367 ? 148.988 190.889 113.637 1.00 37.87  ? 1367 LEU A CA    1 
ATOM   8798  C  C     . LEU A 1 1367 ? 150.149 190.050 113.126 1.00 37.36  ? 1367 LEU A C     1 
ATOM   8799  O  O     . LEU A 1 1367 ? 150.748 190.377 112.097 1.00 42.78  ? 1367 LEU A O     1 
ATOM   8800  C  CB    . LEU A 1 1367 ? 147.802 190.811 112.677 1.00 36.86  ? 1367 LEU A CB    1 
ATOM   8801  C  CG    . LEU A 1 1367 ? 146.474 191.272 113.275 1.00 38.22  ? 1367 LEU A CG    1 
ATOM   8802  C  CD1   . LEU A 1 1367 ? 145.532 191.689 112.176 1.00 42.27  ? 1367 LEU A CD1   1 
ATOM   8803  C  CD2   . LEU A 1 1367 ? 145.851 190.178 114.121 1.00 36.46  ? 1367 LEU A CD2   1 
ATOM   8804  N  N     . LEU A 1 1368 ? 150.459 188.972 113.840 1.00 35.92  ? 1368 LEU A N     1 
ATOM   8805  C  CA    . LEU A 1 1368 ? 151.520 188.040 113.467 1.00 37.37  ? 1368 LEU A CA    1 
ATOM   8806  C  C     . LEU A 1 1368 ? 150.854 186.750 112.998 1.00 39.93  ? 1368 LEU A C     1 
ATOM   8807  O  O     . LEU A 1 1368 ? 150.474 185.899 113.803 1.00 41.80  ? 1368 LEU A O     1 
ATOM   8808  C  CB    . LEU A 1 1368 ? 152.471 187.786 114.629 1.00 32.76  ? 1368 LEU A CB    1 
ATOM   8809  C  CG    . LEU A 1 1368 ? 153.177 188.996 115.239 1.00 33.15  ? 1368 LEU A CG    1 
ATOM   8810  C  CD1   . LEU A 1 1368 ? 154.082 188.547 116.366 1.00 29.29  ? 1368 LEU A CD1   1 
ATOM   8811  C  CD2   . LEU A 1 1368 ? 153.963 189.754 114.187 1.00 36.99  ? 1368 LEU A CD2   1 
ATOM   8812  N  N     . LEU A 1 1369 ? 150.719 186.611 111.684 1.00 39.10  ? 1369 LEU A N     1 
ATOM   8813  C  CA    . LEU A 1 1369 ? 150.039 185.479 111.068 1.00 37.75  ? 1369 LEU A CA    1 
ATOM   8814  C  C     . LEU A 1 1369 ? 151.080 184.488 110.564 1.00 41.58  ? 1369 LEU A C     1 
ATOM   8815  O  O     . LEU A 1 1369 ? 151.935 184.845 109.748 1.00 45.89  ? 1369 LEU A O     1 
ATOM   8816  C  CB    . LEU A 1 1369 ? 149.140 185.957 109.929 1.00 39.80  ? 1369 LEU A CB    1 
ATOM   8817  C  CG    . LEU A 1 1369 ? 147.671 186.261 110.244 1.00 40.53  ? 1369 LEU A CG    1 
ATOM   8818  C  CD1   . LEU A 1 1369 ? 147.525 187.155 111.458 1.00 35.92  ? 1369 LEU A CD1   1 
ATOM   8819  C  CD2   . LEU A 1 1369 ? 147.012 186.908 109.043 1.00 41.82  ? 1369 LEU A CD2   1 
ATOM   8820  N  N     . ASP A 1 1370 ? 151.007 183.249 111.045 1.00 42.04  ? 1370 ASP A N     1 
ATOM   8821  C  CA    . ASP A 1 1370 ? 151.981 182.206 110.726 1.00 41.92  ? 1370 ASP A CA    1 
ATOM   8822  C  C     . ASP A 1 1370 ? 151.292 181.152 109.861 1.00 42.30  ? 1370 ASP A C     1 
ATOM   8823  O  O     . ASP A 1 1370 ? 150.784 180.150 110.364 1.00 43.43  ? 1370 ASP A O     1 
ATOM   8824  C  CB    . ASP A 1 1370 ? 152.557 181.594 112.001 1.00 45.65  ? 1370 ASP A CB    1 
ATOM   8825  C  CG    . ASP A 1 1370 ? 153.827 180.803 111.751 1.00 48.32  ? 1370 ASP A CG    1 
ATOM   8826  O  OD1   . ASP A 1 1370 ? 154.210 180.642 110.575 1.00 52.77  ? 1370 ASP A OD1   1 
ATOM   8827  O  OD2   . ASP A 1 1370 ? 154.443 180.341 112.734 1.00 43.59  ? 1370 ASP A OD2   1 
ATOM   8828  N  N     . GLN A 1 1371 ? 151.296 181.387 108.547 1.00 45.94  ? 1371 GLN A N     1 
ATOM   8829  C  CA    . GLN A 1 1371 ? 150.697 180.521 107.535 1.00 47.36  ? 1371 GLN A CA    1 
ATOM   8830  C  C     . GLN A 1 1371 ? 149.248 180.220 107.895 1.00 47.16  ? 1371 GLN A C     1 
ATOM   8831  O  O     . GLN A 1 1371 ? 148.923 179.088 108.273 1.00 45.79  ? 1371 GLN A O     1 
ATOM   8832  C  CB    . GLN A 1 1371 ? 151.511 179.236 107.375 1.00 42.67  ? 1371 GLN A CB    1 
ATOM   8833  C  CG    . GLN A 1 1371 ? 151.166 178.437 106.133 1.00 49.06  ? 1371 GLN A CG    1 
ATOM   8834  C  CD    . GLN A 1 1371 ? 152.094 177.264 105.918 1.00 50.22  ? 1371 GLN A CD    1 
ATOM   8835  O  OE1   . GLN A 1 1371 ? 153.031 177.049 106.685 1.00 49.73  ? 1371 GLN A OE1   1 
ATOM   8836  N  NE2   . GLN A 1 1371 ? 151.846 176.501 104.861 1.00 44.62  ? 1371 GLN A NE2   1 
ATOM   8837  N  N     . PRO A 1 1372 ? 148.357 181.213 107.809 1.00 45.77  ? 1372 PRO A N     1 
ATOM   8838  C  CA    . PRO A 1 1372 ? 146.966 180.989 108.230 1.00 44.76  ? 1372 PRO A CA    1 
ATOM   8839  C  C     . PRO A 1 1372 ? 146.256 179.905 107.444 1.00 47.41  ? 1372 PRO A C     1 
ATOM   8840  O  O     . PRO A 1 1372 ? 145.382 179.228 107.997 1.00 49.77  ? 1372 PRO A O     1 
ATOM   8841  C  CB    . PRO A 1 1372 ? 146.312 182.361 108.009 1.00 42.33  ? 1372 PRO A CB    1 
ATOM   8842  C  CG    . PRO A 1 1372 ? 147.441 183.326 108.025 1.00 40.47  ? 1372 PRO A CG    1 
ATOM   8843  C  CD    . PRO A 1 1372 ? 148.569 182.599 107.369 1.00 44.91  ? 1372 PRO A CD    1 
ATOM   8844  N  N     . SER A 1 1373 ? 146.601 179.711 106.178 1.00 43.11  ? 1373 SER A N     1 
ATOM   8845  C  CA    . SER A 1 1373 ? 145.922 178.750 105.315 1.00 45.46  ? 1373 SER A CA    1 
ATOM   8846  C  C     . SER A 1 1373 ? 146.938 177.715 104.843 1.00 47.47  ? 1373 SER A C     1 
ATOM   8847  O  O     . SER A 1 1373 ? 147.495 177.823 103.749 1.00 52.65  ? 1373 SER A O     1 
ATOM   8848  C  CB    . SER A 1 1373 ? 145.268 179.470 104.143 1.00 47.74  ? 1373 SER A CB    1 
ATOM   8849  O  OG    . SER A 1 1373 ? 146.243 179.919 103.219 1.00 48.47  ? 1373 SER A OG    1 
ATOM   8850  N  N     . ALA A 1 1374 ? 147.163 176.699 105.675 1.00 44.62  ? 1374 ALA A N     1 
ATOM   8851  C  CA    . ALA A 1 1374 ? 148.145 175.671 105.350 1.00 45.83  ? 1374 ALA A CA    1 
ATOM   8852  C  C     . ALA A 1 1374 ? 147.600 174.679 104.332 1.00 49.17  ? 1374 ALA A C     1 
ATOM   8853  O  O     . ALA A 1 1374 ? 148.121 174.559 103.217 1.00 52.25  ? 1374 ALA A O     1 
ATOM   8854  C  CB    . ALA A 1 1374 ? 148.586 174.951 106.623 1.00 42.03  ? 1374 ALA A CB    1 
ATOM   8855  N  N     . HIS A 1 1375 ? 146.547 173.956 104.702 1.00 45.98  ? 1375 HIS A N     1 
ATOM   8856  C  CA    . HIS A 1 1375 ? 146.056 172.830 103.921 1.00 46.94  ? 1375 HIS A CA    1 
ATOM   8857  C  C     . HIS A 1 1375 ? 144.790 173.160 103.141 1.00 50.53  ? 1375 HIS A C     1 
ATOM   8858  O  O     . HIS A 1 1375 ? 144.175 172.256 102.567 1.00 51.48  ? 1375 HIS A O     1 
ATOM   8859  C  CB    . HIS A 1 1375 ? 145.797 171.635 104.839 1.00 45.62  ? 1375 HIS A CB    1 
ATOM   8860  C  CG    . HIS A 1 1375 ? 147.039 170.902 105.243 1.00 45.31  ? 1375 HIS A CG    1 
ATOM   8861  N  ND1   . HIS A 1 1375 ? 147.524 169.821 104.541 1.00 45.09  ? 1375 HIS A ND1   1 
ATOM   8862  C  CD2   . HIS A 1 1375 ? 147.902 171.104 106.266 1.00 43.28  ? 1375 HIS A CD2   1 
ATOM   8863  C  CE1   . HIS A 1 1375 ? 148.627 169.382 105.119 1.00 43.69  ? 1375 HIS A CE1   1 
ATOM   8864  N  NE2   . HIS A 1 1375 ? 148.880 170.144 106.167 1.00 41.92  ? 1375 HIS A NE2   1 
ATOM   8865  N  N     . LEU A 1 1376 ? 144.382 174.424 103.117 1.00 49.22  ? 1376 LEU A N     1 
ATOM   8866  C  CA    . LEU A 1 1376 ? 143.094 174.792 102.550 1.00 44.62  ? 1376 LEU A CA    1 
ATOM   8867  C  C     . LEU A 1 1376 ? 143.112 174.740 101.027 1.00 48.54  ? 1376 LEU A C     1 
ATOM   8868  O  O     . LEU A 1 1376 ? 144.143 174.951 100.384 1.00 54.98  ? 1376 LEU A O     1 
ATOM   8869  C  CB    . LEU A 1 1376 ? 142.692 176.188 103.015 1.00 41.62  ? 1376 LEU A CB    1 
ATOM   8870  C  CG    . LEU A 1 1376 ? 142.623 176.378 104.528 1.00 40.09  ? 1376 LEU A CG    1 
ATOM   8871  C  CD1   . LEU A 1 1376 ? 142.122 177.762 104.867 1.00 41.59  ? 1376 LEU A CD1   1 
ATOM   8872  C  CD2   . LEU A 1 1376 ? 141.737 175.320 105.151 1.00 41.75  ? 1376 LEU A CD2   1 
ATOM   8873  N  N     . ASP A 1 1377 ? 141.947 174.445 100.456 1.00 47.64  ? 1377 ASP A N     1 
ATOM   8874  C  CA    . ASP A 1 1377 ? 141.743 174.512 99.021  1.00 47.01  ? 1377 ASP A CA    1 
ATOM   8875  C  C     . ASP A 1 1377 ? 141.620 175.968 98.572  1.00 49.61  ? 1377 ASP A C     1 
ATOM   8876  O  O     . ASP A 1 1377 ? 141.400 176.860 99.393  1.00 51.54  ? 1377 ASP A O     1 
ATOM   8877  C  CB    . ASP A 1 1377 ? 140.491 173.726 98.640  1.00 49.14  ? 1377 ASP A CB    1 
ATOM   8878  C  CG    . ASP A 1 1377 ? 139.306 174.062 99.518  1.00 50.76  ? 1377 ASP A CG    1 
ATOM   8879  O  OD1   . ASP A 1 1377 ? 139.343 173.730 100.721 1.00 50.64  ? 1377 ASP A OD1   1 
ATOM   8880  O  OD2   . ASP A 1 1377 ? 138.334 174.656 99.008  1.00 50.27  ? 1377 ASP A OD2   1 
ATOM   8881  N  N     . PRO A 1 1378 ? 141.780 176.238 97.271  1.00 52.91  ? 1378 PRO A N     1 
ATOM   8882  C  CA    . PRO A 1 1378 ? 141.683 177.632 96.800  1.00 53.51  ? 1378 PRO A CA    1 
ATOM   8883  C  C     . PRO A 1 1378 ? 140.350 178.302 97.091  1.00 52.73  ? 1378 PRO A C     1 
ATOM   8884  O  O     . PRO A 1 1378 ? 140.316 179.526 97.265  1.00 53.58  ? 1378 PRO A O     1 
ATOM   8885  C  CB    . PRO A 1 1378 ? 141.930 177.507 95.289  1.00 52.48  ? 1378 PRO A CB    1 
ATOM   8886  C  CG    . PRO A 1 1378 ? 142.717 176.260 95.144  1.00 54.50  ? 1378 PRO A CG    1 
ATOM   8887  C  CD    . PRO A 1 1378 ? 142.167 175.328 96.180  1.00 53.91  ? 1378 PRO A CD    1 
ATOM   8888  N  N     . VAL A 1 1379 ? 139.250 177.550 97.142  1.00 53.14  ? 1379 VAL A N     1 
ATOM   8889  C  CA    . VAL A 1 1379 ? 137.951 178.168 97.395  1.00 54.15  ? 1379 VAL A CA    1 
ATOM   8890  C  C     . VAL A 1 1379 ? 137.868 178.676 98.830  1.00 52.07  ? 1379 VAL A C     1 
ATOM   8891  O  O     . VAL A 1 1379 ? 137.376 179.782 99.085  1.00 53.45  ? 1379 VAL A O     1 
ATOM   8892  C  CB    . VAL A 1 1379 ? 136.816 177.178 97.073  1.00 55.61  ? 1379 VAL A CB    1 
ATOM   8893  C  CG1   . VAL A 1 1379 ? 135.469 177.785 97.420  1.00 52.08  ? 1379 VAL A CG1   1 
ATOM   8894  C  CG2   . VAL A 1 1379 ? 136.856 176.790 95.604  1.00 52.89  ? 1379 VAL A CG2   1 
ATOM   8895  N  N     . THR A 1 1380 ? 138.353 177.884 99.788  1.00 49.15  ? 1380 THR A N     1 
ATOM   8896  C  CA    . THR A 1 1380 ? 138.306 178.279 101.191 1.00 47.22  ? 1380 THR A CA    1 
ATOM   8897  C  C     . THR A 1 1380 ? 139.282 179.410 101.504 1.00 49.83  ? 1380 THR A C     1 
ATOM   8898  O  O     . THR A 1 1380 ? 139.052 180.169 102.450 1.00 52.77  ? 1380 THR A O     1 
ATOM   8899  C  CB    . THR A 1 1380 ? 138.588 177.060 102.075 1.00 47.22  ? 1380 THR A CB    1 
ATOM   8900  O  OG1   . THR A 1 1380 ? 137.617 176.043 101.804 1.00 47.35  ? 1380 THR A OG1   1 
ATOM   8901  C  CG2   . THR A 1 1380 ? 138.508 177.419 103.546 1.00 45.13  ? 1380 THR A CG2   1 
ATOM   8902  N  N     . TYR A 1 1381 ? 140.350 179.553 100.716 1.00 47.29  ? 1381 TYR A N     1 
ATOM   8903  C  CA    . TYR A 1 1381 ? 141.297 180.645 100.920 1.00 48.63  ? 1381 TYR A CA    1 
ATOM   8904  C  C     . TYR A 1 1381 ? 140.644 182.011 100.726 1.00 53.97  ? 1381 TYR A C     1 
ATOM   8905  O  O     . TYR A 1 1381 ? 141.119 183.016 101.278 1.00 56.33  ? 1381 TYR A O     1 
ATOM   8906  C  CB    . TYR A 1 1381 ? 142.483 180.474 99.973  1.00 52.11  ? 1381 TYR A CB    1 
ATOM   8907  C  CG    . TYR A 1 1381 ? 143.310 181.722 99.790  1.00 55.02  ? 1381 TYR A CG    1 
ATOM   8908  C  CD1   . TYR A 1 1381 ? 144.145 182.177 100.795 1.00 52.93  ? 1381 TYR A CD1   1 
ATOM   8909  C  CD2   . TYR A 1 1381 ? 143.258 182.439 98.605  1.00 58.57  ? 1381 TYR A CD2   1 
ATOM   8910  C  CE1   . TYR A 1 1381 ? 144.897 183.315 100.631 1.00 56.12  ? 1381 TYR A CE1   1 
ATOM   8911  C  CE2   . TYR A 1 1381 ? 144.009 183.578 98.431  1.00 62.75  ? 1381 TYR A CE2   1 
ATOM   8912  C  CZ    . TYR A 1 1381 ? 144.827 184.012 99.447  1.00 63.47  ? 1381 TYR A CZ    1 
ATOM   8913  O  OH    . TYR A 1 1381 ? 145.580 185.149 99.279  1.00 65.40  ? 1381 TYR A OH    1 
ATOM   8914  N  N     . GLN A 1 1382 ? 139.558 182.071 99.951  1.00 53.23  ? 1382 GLN A N     1 
ATOM   8915  C  CA    . GLN A 1 1382 ? 138.869 183.338 99.746  1.00 52.96  ? 1382 GLN A CA    1 
ATOM   8916  C  C     . GLN A 1 1382 ? 138.333 183.901 101.053 1.00 51.53  ? 1382 GLN A C     1 
ATOM   8917  O  O     . GLN A 1 1382 ? 138.223 185.122 101.202 1.00 52.32  ? 1382 GLN A O     1 
ATOM   8918  C  CB    . GLN A 1 1382 ? 137.733 183.163 98.739  1.00 53.69  ? 1382 GLN A CB    1 
ATOM   8919  C  CG    . GLN A 1 1382 ? 138.182 182.647 97.386  1.00 58.25  ? 1382 GLN A CG    1 
ATOM   8920  C  CD    . GLN A 1 1382 ? 139.279 183.492 96.779  1.00 61.35  ? 1382 GLN A CD    1 
ATOM   8921  O  OE1   . GLN A 1 1382 ? 139.213 184.720 96.794  1.00 61.05  ? 1382 GLN A OE1   1 
ATOM   8922  N  NE2   . GLN A 1 1382 ? 140.306 182.838 96.252  1.00 65.08  ? 1382 GLN A NE2   1 
ATOM   8923  N  N     . ILE A 1 1383 ? 138.018 183.035 102.016 1.00 49.05  ? 1383 ILE A N     1 
ATOM   8924  C  CA    . ILE A 1 1383 ? 137.572 183.506 103.323 1.00 51.08  ? 1383 ILE A CA    1 
ATOM   8925  C  C     . ILE A 1 1383 ? 138.685 184.281 104.017 1.00 49.81  ? 1383 ILE A C     1 
ATOM   8926  O  O     . ILE A 1 1383 ? 138.460 185.365 104.566 1.00 53.63  ? 1383 ILE A O     1 
ATOM   8927  C  CB    . ILE A 1 1383 ? 137.089 182.322 104.179 1.00 51.49  ? 1383 ILE A CB    1 
ATOM   8928  C  CG1   . ILE A 1 1383 ? 135.947 181.588 103.473 1.00 52.40  ? 1383 ILE A CG1   1 
ATOM   8929  C  CG2   . ILE A 1 1383 ? 136.659 182.801 105.550 1.00 51.77  ? 1383 ILE A CG2   1 
ATOM   8930  C  CD1   . ILE A 1 1383 ? 135.612 180.255 104.091 1.00 49.99  ? 1383 ILE A CD1   1 
ATOM   8931  N  N     . ILE A 1 1384 ? 139.906 183.740 103.991 1.00 47.46  ? 1384 ILE A N     1 
ATOM   8932  C  CA    . ILE A 1 1384 ? 141.042 184.423 104.603 1.00 44.03  ? 1384 ILE A CA    1 
ATOM   8933  C  C     . ILE A 1 1384 ? 141.329 185.730 103.881 1.00 47.05  ? 1384 ILE A C     1 
ATOM   8934  O  O     . ILE A 1 1384 ? 141.601 186.757 104.512 1.00 49.56  ? 1384 ILE A O     1 
ATOM   8935  C  CB    . ILE A 1 1384 ? 142.283 183.508 104.627 1.00 46.61  ? 1384 ILE A CB    1 
ATOM   8936  C  CG1   . ILE A 1 1384 ? 142.111 182.361 105.628 1.00 48.34  ? 1384 ILE A CG1   1 
ATOM   8937  C  CG2   . ILE A 1 1384 ? 143.532 184.307 104.963 1.00 47.73  ? 1384 ILE A CG2   1 
ATOM   8938  C  CD1   . ILE A 1 1384 ? 141.248 181.218 105.151 1.00 47.01  ? 1384 ILE A CD1   1 
ATOM   8939  N  N     . ARG A 1 1385 ? 141.277 185.713 102.548 1.00 50.86  ? 1385 ARG A N     1 
ATOM   8940  C  CA    . ARG A 1 1385 ? 141.535 186.934 101.788 1.00 50.99  ? 1385 ARG A CA    1 
ATOM   8941  C  C     . ARG A 1 1385 ? 140.513 188.021 102.113 1.00 55.04  ? 1385 ARG A C     1 
ATOM   8942  O  O     . ARG A 1 1385 ? 140.873 189.188 102.327 1.00 58.83  ? 1385 ARG A O     1 
ATOM   8943  C  CB    . ARG A 1 1385 ? 141.537 186.611 100.296 1.00 53.81  ? 1385 ARG A CB    1 
ATOM   8944  C  CG    . ARG A 1 1385 ? 141.836 187.775 99.381  1.00 59.20  ? 1385 ARG A CG    1 
ATOM   8945  C  CD    . ARG A 1 1385 ? 141.876 187.283 97.947  1.00 67.38  ? 1385 ARG A CD    1 
ATOM   8946  N  NE    . ARG A 1 1385 ? 142.002 188.358 96.973  1.00 78.99  ? 1385 ARG A NE    1 
ATOM   8947  C  CZ    . ARG A 1 1385 ? 141.191 188.527 95.938  1.00 81.95  ? 1385 ARG A CZ    1 
ATOM   8948  N  NH1   . ARG A 1 1385 ? 140.181 187.702 95.710  1.00 81.97  ? 1385 ARG A NH1   1 
ATOM   8949  N  NH2   . ARG A 1 1385 ? 141.401 189.544 95.108  1.00 80.87  ? 1385 ARG A NH2   1 
ATOM   8950  N  N     . ARG A 1 1386 ? 139.234 187.651 102.166 1.00 54.37  ? 1386 ARG A N     1 
ATOM   8951  C  CA    . ARG A 1 1386 ? 138.187 188.612 102.490 1.00 53.29  ? 1386 ARG A CA    1 
ATOM   8952  C  C     . ARG A 1 1386 ? 138.328 189.135 103.913 1.00 53.49  ? 1386 ARG A C     1 
ATOM   8953  O  O     . ARG A 1 1386 ? 138.159 190.334 104.156 1.00 57.29  ? 1386 ARG A O     1 
ATOM   8954  C  CB    . ARG A 1 1386 ? 136.823 187.962 102.268 1.00 56.26  ? 1386 ARG A CB    1 
ATOM   8955  C  CG    . ARG A 1 1386 ? 135.647 188.715 102.838 1.00 61.17  ? 1386 ARG A CG    1 
ATOM   8956  C  CD    . ARG A 1 1386 ? 134.355 188.245 102.184 1.00 63.94  ? 1386 ARG A CD    1 
ATOM   8957  N  NE    . ARG A 1 1386 ? 134.228 186.791 102.173 1.00 69.31  ? 1386 ARG A NE    1 
ATOM   8958  C  CZ    . ARG A 1 1386 ? 134.030 186.038 103.246 1.00 68.23  ? 1386 ARG A CZ    1 
ATOM   8959  N  NH1   . ARG A 1 1386 ? 133.905 186.569 104.451 1.00 61.53  ? 1386 ARG A NH1   1 
ATOM   8960  N  NH2   . ARG A 1 1386 ? 133.950 184.719 103.106 1.00 64.17  ? 1386 ARG A NH2   1 
ATOM   8961  N  N     . THR A 1 1387 ? 138.647 188.257 104.868 1.00 52.86  ? 1387 THR A N     1 
ATOM   8962  C  CA    . THR A 1 1387 ? 138.846 188.708 106.241 1.00 52.66  ? 1387 THR A CA    1 
ATOM   8963  C  C     . THR A 1 1387 ? 140.026 189.664 106.339 1.00 49.72  ? 1387 THR A C     1 
ATOM   8964  O  O     . THR A 1 1387 ? 139.975 190.653 107.080 1.00 49.37  ? 1387 THR A O     1 
ATOM   8965  C  CB    . THR A 1 1387 ? 139.050 187.510 107.166 1.00 53.06  ? 1387 THR A CB    1 
ATOM   8966  O  OG1   . THR A 1 1387 ? 137.887 186.674 107.133 1.00 56.74  ? 1387 THR A OG1   1 
ATOM   8967  C  CG2   . THR A 1 1387 ? 139.291 187.972 108.587 1.00 47.31  ? 1387 THR A CG2   1 
ATOM   8968  N  N     . LEU A 1 1388 ? 141.098 189.389 105.596 1.00 53.97  ? 1388 LEU A N     1 
ATOM   8969  C  CA    . LEU A 1 1388 ? 142.253 190.280 105.597 1.00 55.47  ? 1388 LEU A CA    1 
ATOM   8970  C  C     . LEU A 1 1388 ? 141.891 191.648 105.038 1.00 55.65  ? 1388 LEU A C     1 
ATOM   8971  O  O     . LEU A 1 1388 ? 142.302 192.678 105.582 1.00 59.23  ? 1388 LEU A O     1 
ATOM   8972  C  CB    . LEU A 1 1388 ? 143.394 189.658 104.794 1.00 57.04  ? 1388 LEU A CB    1 
ATOM   8973  C  CG    . LEU A 1 1388 ? 144.801 190.095 105.197 1.00 59.58  ? 1388 LEU A CG    1 
ATOM   8974  C  CD1   . LEU A 1 1388 ? 145.171 189.506 106.546 1.00 55.70  ? 1388 LEU A CD1   1 
ATOM   8975  C  CD2   . LEU A 1 1388 ? 145.817 189.698 104.137 1.00 62.64  ? 1388 LEU A CD2   1 
ATOM   8976  N  N     . LYS A 1 1389 ? 141.133 191.679 103.940 1.00 58.09  ? 1389 LYS A N     1 
ATOM   8977  C  CA    . LYS A 1 1389 ? 140.742 192.962 103.360 1.00 61.37  ? 1389 LYS A CA    1 
ATOM   8978  C  C     . LYS A 1 1389 ? 139.827 193.749 104.295 1.00 61.83  ? 1389 LYS A C     1 
ATOM   8979  O  O     . LYS A 1 1389 ? 140.029 194.949 104.513 1.00 63.18  ? 1389 LYS A O     1 
ATOM   8980  C  CB    . LYS A 1 1389 ? 140.063 192.752 102.007 1.00 64.13  ? 1389 LYS A CB    1 
ATOM   8981  C  CG    . LYS A 1 1389 ? 141.024 192.619 100.839 1.00 70.34  ? 1389 LYS A CG    1 
ATOM   8982  C  CD    . LYS A 1 1389 ? 140.386 193.143 99.557  1.00 81.11  ? 1389 LYS A CD    1 
ATOM   8983  C  CE    . LYS A 1 1389 ? 141.313 192.999 98.360  1.00 90.77  ? 1389 LYS A CE    1 
ATOM   8984  N  NZ    . LYS A 1 1389 ? 141.452 191.583 97.931  1.00 86.03  ? 1389 LYS A NZ    1 
ATOM   8985  N  N     . GLN A 1 1390 ? 138.815 193.092 104.860 1.00 62.47  ? 1390 GLN A N     1 
ATOM   8986  C  CA    . GLN A 1 1390 ? 137.760 193.808 105.576 1.00 61.14  ? 1390 GLN A CA    1 
ATOM   8987  C  C     . GLN A 1 1390 ? 138.063 193.995 107.062 1.00 58.15  ? 1390 GLN A C     1 
ATOM   8988  O  O     . GLN A 1 1390 ? 138.109 195.127 107.552 1.00 55.69  ? 1390 GLN A O     1 
ATOM   8989  C  CB    . GLN A 1 1390 ? 136.427 193.078 105.388 1.00 63.74  ? 1390 GLN A CB    1 
ATOM   8990  C  CG    . GLN A 1 1390 ? 136.170 192.653 103.951 1.00 65.20  ? 1390 GLN A CG    1 
ATOM   8991  C  CD    . GLN A 1 1390 ? 134.733 192.259 103.696 1.00 68.39  ? 1390 GLN A CD    1 
ATOM   8992  O  OE1   . GLN A 1 1390 ? 133.951 192.083 104.630 1.00 65.05  ? 1390 GLN A OE1   1 
ATOM   8993  N  NE2   . GLN A 1 1390 ? 134.378 192.109 102.425 1.00 68.37  ? 1390 GLN A NE2   1 
ATOM   8994  N  N     . ALA A 1 1391 ? 138.272 192.895 107.789 1.00 58.91  ? 1391 ALA A N     1 
ATOM   8995  C  CA    . ALA A 1 1391 ? 138.358 192.968 109.246 1.00 53.90  ? 1391 ALA A CA    1 
ATOM   8996  C  C     . ALA A 1 1391 ? 139.615 193.688 109.722 1.00 56.01  ? 1391 ALA A C     1 
ATOM   8997  O  O     . ALA A 1 1391 ? 139.600 194.309 110.791 1.00 57.53  ? 1391 ALA A O     1 
ATOM   8998  C  CB    . ALA A 1 1391 ? 138.294 191.566 109.849 1.00 47.78  ? 1391 ALA A CB    1 
ATOM   8999  N  N     . PHE A 1 1392 ? 140.704 193.625 108.958 1.00 52.08  ? 1392 PHE A N     1 
ATOM   9000  C  CA    . PHE A 1 1392 ? 141.983 194.154 109.416 1.00 51.00  ? 1392 PHE A CA    1 
ATOM   9001  C  C     . PHE A 1 1392 ? 142.442 195.336 108.570 1.00 61.86  ? 1392 PHE A C     1 
ATOM   9002  O  O     . PHE A 1 1392 ? 143.608 195.394 108.167 1.00 66.58  ? 1392 PHE A O     1 
ATOM   9003  C  CB    . PHE A 1 1392 ? 143.056 193.065 109.396 1.00 48.86  ? 1392 PHE A CB    1 
ATOM   9004  C  CG    . PHE A 1 1392 ? 142.701 191.843 110.188 1.00 49.64  ? 1392 PHE A CG    1 
ATOM   9005  C  CD1   . PHE A 1 1392 ? 142.069 191.951 111.413 1.00 48.30  ? 1392 PHE A CD1   1 
ATOM   9006  C  CD2   . PHE A 1 1392 ? 143.016 190.583 109.711 1.00 48.74  ? 1392 PHE A CD2   1 
ATOM   9007  C  CE1   . PHE A 1 1392 ? 141.749 190.826 112.142 1.00 45.15  ? 1392 PHE A CE1   1 
ATOM   9008  C  CE2   . PHE A 1 1392 ? 142.699 189.455 110.435 1.00 38.94  ? 1392 PHE A CE2   1 
ATOM   9009  C  CZ    . PHE A 1 1392 ? 142.064 189.577 111.653 1.00 41.48  ? 1392 PHE A CZ    1 
ATOM   9010  N  N     . ALA A 1 1393 ? 141.537 196.271 108.281 1.00 63.36  ? 1393 ALA A N     1 
ATOM   9011  C  CA    . ALA A 1 1393 ? 141.841 197.378 107.382 1.00 64.84  ? 1393 ALA A CA    1 
ATOM   9012  C  C     . ALA A 1 1393 ? 143.005 198.228 107.879 1.00 71.26  ? 1393 ALA A C     1 
ATOM   9013  O  O     . ALA A 1 1393 ? 144.050 198.294 107.224 1.00 76.09  ? 1393 ALA A O     1 
ATOM   9014  C  CB    . ALA A 1 1393 ? 140.605 198.257 107.187 1.00 64.78  ? 1393 ALA A CB    1 
ATOM   9015  N  N     . ASP A 1 1394 ? 142.840 198.884 109.021 1.00 71.53  ? 1394 ASP A N     1 
ATOM   9016  C  CA    . ASP A 1 1394 ? 143.887 199.746 109.578 1.00 71.94  ? 1394 ASP A CA    1 
ATOM   9017  C  C     . ASP A 1 1394 ? 144.744 199.002 110.595 1.00 68.56  ? 1394 ASP A C     1 
ATOM   9018  O  O     . ASP A 1 1394 ? 144.863 199.407 111.750 1.00 70.55  ? 1394 ASP A O     1 
ATOM   9019  C  CB    . ASP A 1 1394 ? 143.263 200.992 110.195 1.00 77.08  ? 1394 ASP A CB    1 
ATOM   9020  C  CG    . ASP A 1 1394 ? 142.470 201.805 109.189 1.00 79.78  ? 1394 ASP A CG    1 
ATOM   9021  O  OD1   . ASP A 1 1394 ? 142.880 201.860 108.010 1.00 82.24  ? 1394 ASP A OD1   1 
ATOM   9022  O  OD2   . ASP A 1 1394 ? 141.438 202.390 109.577 1.00 79.23  ? 1394 ASP A OD2   1 
ATOM   9023  N  N     . CYS A 1 1395 ? 145.358 197.901 110.173 1.00 63.89  ? 1395 CYS A N     1 
ATOM   9024  C  CA    . CYS A 1 1395 ? 146.221 197.105 111.033 1.00 61.51  ? 1395 CYS A CA    1 
ATOM   9025  C  C     . CYS A 1 1395 ? 147.495 196.748 110.284 1.00 62.57  ? 1395 CYS A C     1 
ATOM   9026  O  O     . CYS A 1 1395 ? 147.472 196.548 109.067 1.00 65.73  ? 1395 CYS A O     1 
ATOM   9027  C  CB    . CYS A 1 1395 ? 145.517 195.827 111.500 1.00 59.07  ? 1395 CYS A CB    1 
ATOM   9028  S  SG    . CYS A 1 1395 ? 144.097 196.109 112.577 1.00 72.64  ? 1395 CYS A SG    1 
ATOM   9029  N  N     . THR A 1 1396 ? 148.605 196.677 111.015 1.00 56.79  ? 1396 THR A N     1 
ATOM   9030  C  CA    . THR A 1 1396 ? 149.864 196.199 110.453 1.00 54.18  ? 1396 THR A CA    1 
ATOM   9031  C  C     . THR A 1 1396 ? 149.864 194.676 110.498 1.00 53.58  ? 1396 THR A C     1 
ATOM   9032  O  O     . THR A 1 1396 ? 149.875 194.081 111.580 1.00 53.91  ? 1396 THR A O     1 
ATOM   9033  C  CB    . THR A 1 1396 ? 151.054 196.769 111.217 1.00 54.11  ? 1396 THR A CB    1 
ATOM   9034  O  OG1   . THR A 1 1396 ? 151.103 198.189 111.039 1.00 57.96  ? 1396 THR A OG1   1 
ATOM   9035  C  CG2   . THR A 1 1396 ? 152.345 196.162 110.708 1.00 54.70  ? 1396 THR A CG2   1 
ATOM   9036  N  N     . VAL A 1 1397 ? 149.843 194.043 109.328 1.00 49.00  ? 1397 VAL A N     1 
ATOM   9037  C  CA    . VAL A 1 1397 ? 149.774 192.593 109.205 1.00 43.55  ? 1397 VAL A CA    1 
ATOM   9038  C  C     . VAL A 1 1397 ? 151.098 192.087 108.652 1.00 41.84  ? 1397 VAL A C     1 
ATOM   9039  O  O     . VAL A 1 1397 ? 151.552 192.546 107.598 1.00 49.03  ? 1397 VAL A O     1 
ATOM   9040  C  CB    . VAL A 1 1397 ? 148.606 192.163 108.302 1.00 45.24  ? 1397 VAL A CB    1 
ATOM   9041  C  CG1   . VAL A 1 1397 ? 148.616 190.659 108.101 1.00 47.36  ? 1397 VAL A CG1   1 
ATOM   9042  C  CG2   . VAL A 1 1397 ? 147.285 192.619 108.891 1.00 44.51  ? 1397 VAL A CG2   1 
ATOM   9043  N  N     . ILE A 1 1398 ? 151.715 191.148 109.361 1.00 40.94  ? 1398 ILE A N     1 
ATOM   9044  C  CA    . ILE A 1 1398 ? 152.923 190.471 108.906 1.00 44.90  ? 1398 ILE A CA    1 
ATOM   9045  C  C     . ILE A 1 1398 ? 152.511 189.052 108.537 1.00 44.87  ? 1398 ILE A C     1 
ATOM   9046  O  O     . ILE A 1 1398 ? 152.319 188.201 109.411 1.00 43.17  ? 1398 ILE A O     1 
ATOM   9047  C  CB    . ILE A 1 1398 ? 154.029 190.486 109.965 1.00 43.48  ? 1398 ILE A CB    1 
ATOM   9048  C  CG1   . ILE A 1 1398 ? 154.424 191.926 110.286 1.00 48.15  ? 1398 ILE A CG1   1 
ATOM   9049  C  CG2   . ILE A 1 1398 ? 155.240 189.709 109.481 1.00 40.73  ? 1398 ILE A CG2   1 
ATOM   9050  C  CD1   . ILE A 1 1398 ? 155.424 192.047 111.400 1.00 54.47  ? 1398 ILE A CD1   1 
ATOM   9051  N  N     . LEU A 1 1399 ? 152.362 188.797 107.241 1.00 46.83  ? 1399 LEU A N     1 
ATOM   9052  C  CA    . LEU A 1 1399 ? 151.778 187.557 106.736 1.00 44.48  ? 1399 LEU A CA    1 
ATOM   9053  C  C     . LEU A 1 1399 ? 152.892 186.618 106.290 1.00 44.17  ? 1399 LEU A C     1 
ATOM   9054  O  O     . LEU A 1 1399 ? 153.449 186.768 105.200 1.00 46.50  ? 1399 LEU A O     1 
ATOM   9055  C  CB    . LEU A 1 1399 ? 150.811 187.856 105.596 1.00 48.75  ? 1399 LEU A CB    1 
ATOM   9056  C  CG    . LEU A 1 1399 ? 150.108 186.677 104.928 1.00 54.95  ? 1399 LEU A CG    1 
ATOM   9057  C  CD1   . LEU A 1 1399 ? 149.272 185.916 105.937 1.00 49.37  ? 1399 LEU A CD1   1 
ATOM   9058  C  CD2   . LEU A 1 1399 ? 149.249 187.175 103.783 1.00 56.45  ? 1399 LEU A CD2   1 
ATOM   9059  N  N     . CYS A 1 1400 ? 153.216 185.646 107.137 1.00 43.51  ? 1400 CYS A N     1 
ATOM   9060  C  CA    . CYS A 1 1400 ? 154.137 184.577 106.775 1.00 44.82  ? 1400 CYS A CA    1 
ATOM   9061  C  C     . CYS A 1 1400 ? 153.349 183.447 106.129 1.00 52.02  ? 1400 CYS A C     1 
ATOM   9062  O  O     . CYS A 1 1400 ? 152.475 182.858 106.770 1.00 53.06  ? 1400 CYS A O     1 
ATOM   9063  C  CB    . CYS A 1 1400 ? 154.880 184.077 108.011 1.00 42.60  ? 1400 CYS A CB    1 
ATOM   9064  S  SG    . CYS A 1 1400 ? 155.802 182.550 107.775 1.00 55.94  ? 1400 CYS A SG    1 
ATOM   9065  N  N     . GLU A 1 1401 ? 153.645 183.141 104.868 1.00 53.36  ? 1401 GLU A N     1 
ATOM   9066  C  CA    . GLU A 1 1401 ? 152.882 182.120 104.166 1.00 52.06  ? 1401 GLU A CA    1 
ATOM   9067  C  C     . GLU A 1 1401 ? 153.672 181.608 102.971 1.00 52.71  ? 1401 GLU A C     1 
ATOM   9068  O  O     . GLU A 1 1401 ? 154.448 182.346 102.359 1.00 50.81  ? 1401 GLU A O     1 
ATOM   9069  C  CB    . GLU A 1 1401 ? 151.518 182.658 103.718 1.00 52.83  ? 1401 GLU A CB    1 
ATOM   9070  C  CG    . GLU A 1 1401 ? 150.598 181.608 103.126 1.00 54.06  ? 1401 GLU A CG    1 
ATOM   9071  C  CD    . GLU A 1 1401 ? 149.156 181.805 103.524 1.00 57.20  ? 1401 GLU A CD    1 
ATOM   9072  O  OE1   . GLU A 1 1401 ? 148.610 182.895 103.257 1.00 62.84  ? 1401 GLU A OE1   1 
ATOM   9073  O  OE2   . GLU A 1 1401 ? 148.565 180.865 104.092 1.00 54.41  ? 1401 GLU A OE2   1 
ATOM   9074  N  N     . HIS A 1 1402 ? 153.469 180.327 102.659 1.00 52.41  ? 1402 HIS A N     1 
ATOM   9075  C  CA    . HIS A 1 1402 ? 154.059 179.685 101.493 1.00 49.25  ? 1402 HIS A CA    1 
ATOM   9076  C  C     . HIS A 1 1402 ? 153.213 179.818 100.235 1.00 51.76  ? 1402 HIS A C     1 
ATOM   9077  O  O     . HIS A 1 1402 ? 153.707 179.521 99.143  1.00 54.12  ? 1402 HIS A O     1 
ATOM   9078  C  CB    . HIS A 1 1402 ? 154.302 178.200 101.776 1.00 44.79  ? 1402 HIS A CB    1 
ATOM   9079  C  CG    . HIS A 1 1402 ? 155.527 177.935 102.590 1.00 47.28  ? 1402 HIS A CG    1 
ATOM   9080  N  ND1   . HIS A 1 1402 ? 155.568 176.988 103.590 1.00 42.30  ? 1402 HIS A ND1   1 
ATOM   9081  C  CD2   . HIS A 1 1402 ? 156.763 178.486 102.545 1.00 47.60  ? 1402 HIS A CD2   1 
ATOM   9082  C  CE1   . HIS A 1 1402 ? 156.773 176.973 104.129 1.00 38.95  ? 1402 HIS A CE1   1 
ATOM   9083  N  NE2   . HIS A 1 1402 ? 157.518 177.871 103.512 1.00 42.82  ? 1402 HIS A NE2   1 
ATOM   9084  N  N     . ARG A 1 1403 ? 151.960 180.250 100.356 1.00 53.28  ? 1403 ARG A N     1 
ATOM   9085  C  CA    . ARG A 1 1403 ? 151.083 180.349 99.196  1.00 53.97  ? 1403 ARG A CA    1 
ATOM   9086  C  C     . ARG A 1 1403 ? 151.483 181.545 98.344  1.00 57.71  ? 1403 ARG A C     1 
ATOM   9087  O  O     . ARG A 1 1403 ? 151.594 182.668 98.846  1.00 61.82  ? 1403 ARG A O     1 
ATOM   9088  C  CB    . ARG A 1 1403 ? 149.628 180.465 99.639  1.00 53.59  ? 1403 ARG A CB    1 
ATOM   9089  C  CG    . ARG A 1 1403 ? 148.628 180.209 98.530  1.00 54.00  ? 1403 ARG A CG    1 
ATOM   9090  C  CD    . ARG A 1 1403 ? 147.208 180.382 99.025  1.00 54.18  ? 1403 ARG A CD    1 
ATOM   9091  N  NE    . ARG A 1 1403 ? 146.845 179.374 100.013 1.00 55.91  ? 1403 ARG A NE    1 
ATOM   9092  C  CZ    . ARG A 1 1403 ? 146.190 178.254 99.740  1.00 49.69  ? 1403 ARG A CZ    1 
ATOM   9093  N  NH1   . ARG A 1 1403 ? 145.809 177.958 98.510  1.00 45.91  ? 1403 ARG A NH1   1 
ATOM   9094  N  NH2   . ARG A 1 1403 ? 145.908 177.410 100.728 1.00 46.30  ? 1403 ARG A NH2   1 
ATOM   9095  N  N     . ILE A 1 1404 ? 151.707 181.300 97.053  1.00 58.42  ? 1404 ILE A N     1 
ATOM   9096  C  CA    . ILE A 1 1404 ? 152.152 182.364 96.161  1.00 62.96  ? 1404 ILE A CA    1 
ATOM   9097  C  C     . ILE A 1 1404 ? 151.043 183.380 95.925  1.00 66.39  ? 1404 ILE A C     1 
ATOM   9098  O  O     . ILE A 1 1404 ? 151.307 184.583 95.820  1.00 66.66  ? 1404 ILE A O     1 
ATOM   9099  C  CB    . ILE A 1 1404 ? 152.666 181.759 94.843  1.00 66.65  ? 1404 ILE A CB    1 
ATOM   9100  C  CG1   . ILE A 1 1404 ? 153.897 180.892 95.106  1.00 63.75  ? 1404 ILE A CG1   1 
ATOM   9101  C  CG2   . ILE A 1 1404 ? 152.999 182.846 93.849  1.00 67.61  ? 1404 ILE A CG2   1 
ATOM   9102  C  CD1   . ILE A 1 1404 ? 155.065 181.658 95.683  1.00 60.14  ? 1404 ILE A CD1   1 
ATOM   9103  N  N     . GLU A 1 1405 ? 149.791 182.924 95.845  1.00 69.11  ? 1405 GLU A N     1 
ATOM   9104  C  CA    . GLU A 1 1405 ? 148.681 183.840 95.602  1.00 70.62  ? 1405 GLU A CA    1 
ATOM   9105  C  C     . GLU A 1 1405 ? 148.532 184.857 96.728  1.00 69.68  ? 1405 GLU A C     1 
ATOM   9106  O  O     . GLU A 1 1405 ? 148.067 185.978 96.495  1.00 70.89  ? 1405 GLU A O     1 
ATOM   9107  C  CB    . GLU A 1 1405 ? 147.386 183.047 95.415  1.00 71.78  ? 1405 GLU A CB    1 
ATOM   9108  C  CG    . GLU A 1 1405 ? 146.167 183.894 95.102  1.00 82.35  ? 1405 GLU A CG    1 
ATOM   9109  C  CD    . GLU A 1 1405 ? 144.908 183.068 94.923  1.00 88.61  ? 1405 GLU A CD    1 
ATOM   9110  O  OE1   . GLU A 1 1405 ? 144.985 181.827 95.036  1.00 87.86  ? 1405 GLU A OE1   1 
ATOM   9111  O  OE2   . GLU A 1 1405 ? 143.840 183.661 94.667  1.00 90.21  ? 1405 GLU A OE2   1 
ATOM   9112  N  N     . ALA A 1 1406 ? 148.931 184.492 97.949  1.00 67.61  ? 1406 ALA A N     1 
ATOM   9113  C  CA    . ALA A 1 1406 ? 148.805 185.398 99.084  1.00 64.94  ? 1406 ALA A CA    1 
ATOM   9114  C  C     . ALA A 1 1406 ? 149.746 186.593 98.992  1.00 66.41  ? 1406 ALA A C     1 
ATOM   9115  O  O     . ALA A 1 1406 ? 149.523 187.593 99.681  1.00 69.21  ? 1406 ALA A O     1 
ATOM   9116  C  CB    . ALA A 1 1406 ? 149.054 184.642 100.389 1.00 59.35  ? 1406 ALA A CB    1 
ATOM   9117  N  N     . MET A 1 1407 ? 150.784 186.518 98.162  1.00 65.84  ? 1407 MET A N     1 
ATOM   9118  C  CA    . MET A 1 1407 ? 151.721 187.624 98.020  1.00 64.80  ? 1407 MET A CA    1 
ATOM   9119  C  C     . MET A 1 1407 ? 151.170 188.776 97.194  1.00 68.68  ? 1407 MET A C     1 
ATOM   9120  O  O     . MET A 1 1407 ? 151.786 189.847 97.170  1.00 70.22  ? 1407 MET A O     1 
ATOM   9121  C  CB    . MET A 1 1407 ? 153.028 187.129 97.395  1.00 65.86  ? 1407 MET A CB    1 
ATOM   9122  C  CG    . MET A 1 1407 ? 153.887 186.298 98.333  1.00 71.77  ? 1407 MET A CG    1 
ATOM   9123  S  SD    . MET A 1 1407 ? 154.011 187.031 99.978  1.00 84.13  ? 1407 MET A SD    1 
ATOM   9124  C  CE    . MET A 1 1407 ? 153.226 185.780 100.989 1.00 66.15  ? 1407 MET A CE    1 
ATOM   9125  N  N     . LEU A 1 1408 ? 150.037 188.588 96.516  1.00 73.34  ? 1408 LEU A N     1 
ATOM   9126  C  CA    . LEU A 1 1408 ? 149.458 189.676 95.736  1.00 72.94  ? 1408 LEU A CA    1 
ATOM   9127  C  C     . LEU A 1 1408 ? 149.025 190.830 96.629  1.00 71.27  ? 1408 LEU A C     1 
ATOM   9128  O  O     . LEU A 1 1408 ? 149.226 191.999 96.282  1.00 72.51  ? 1408 LEU A O     1 
ATOM   9129  C  CB    . LEU A 1 1408 ? 148.275 189.162 94.920  1.00 76.83  ? 1408 LEU A CB    1 
ATOM   9130  C  CG    . LEU A 1 1408 ? 148.621 188.358 93.668  1.00 80.38  ? 1408 LEU A CG    1 
ATOM   9131  C  CD1   . LEU A 1 1408 ? 147.372 187.703 93.101  1.00 82.70  ? 1408 LEU A CD1   1 
ATOM   9132  C  CD2   . LEU A 1 1408 ? 149.296 189.235 92.626  1.00 81.11  ? 1408 LEU A CD2   1 
ATOM   9133  N  N     . GLU A 1 1409 ? 148.427 190.525 97.776  1.00 70.10  ? 1409 GLU A N     1 
ATOM   9134  C  CA    . GLU A 1 1409 ? 147.963 191.554 98.706  1.00 71.29  ? 1409 GLU A CA    1 
ATOM   9135  C  C     . GLU A 1 1409 ? 149.027 191.910 99.742  1.00 71.31  ? 1409 GLU A C     1 
ATOM   9136  O  O     . GLU A 1 1409 ? 148.782 191.940 100.947 1.00 73.11  ? 1409 GLU A O     1 
ATOM   9137  C  CB    . GLU A 1 1409 ? 146.672 191.095 99.371  1.00 73.06  ? 1409 GLU A CB    1 
ATOM   9138  C  CG    . GLU A 1 1409 ? 146.802 189.816 100.179 1.00 72.26  ? 1409 GLU A CG    1 
ATOM   9139  C  CD    . GLU A 1 1409 ? 146.054 188.664 99.552  1.00 77.65  ? 1409 GLU A CD    1 
ATOM   9140  O  OE1   . GLU A 1 1409 ? 145.690 188.775 98.363  1.00 77.80  ? 1409 GLU A OE1   1 
ATOM   9141  O  OE2   . GLU A 1 1409 ? 145.835 187.647 100.243 1.00 76.82  ? 1409 GLU A OE2   1 
ATOM   9142  N  N     . CYS A 1 1410 ? 150.228 192.218 99.264  1.00 69.53  ? 1410 CYS A N     1 
ATOM   9143  C  CA    . CYS A 1 1410 ? 151.329 192.633 100.117 1.00 64.62  ? 1410 CYS A CA    1 
ATOM   9144  C  C     . CYS A 1 1410 ? 152.015 193.838 99.494  1.00 64.63  ? 1410 CYS A C     1 
ATOM   9145  O  O     . CYS A 1 1410 ? 152.017 194.009 98.273  1.00 68.35  ? 1410 CYS A O     1 
ATOM   9146  C  CB    . CYS A 1 1410 ? 152.344 191.503 100.329 1.00 61.43  ? 1410 CYS A CB    1 
ATOM   9147  S  SG    . CYS A 1 1410 ? 151.791 190.176 101.423 1.00 62.14  ? 1410 CYS A SG    1 
ATOM   9148  N  N     . GLN A 1 1411 ? 152.599 194.675 100.350 1.00 63.94  ? 1411 GLN A N     1 
ATOM   9149  C  CA    . GLN A 1 1411 ? 153.269 195.886 99.903  1.00 66.08  ? 1411 GLN A CA    1 
ATOM   9150  C  C     . GLN A 1 1411 ? 154.768 195.879 100.157 1.00 63.71  ? 1411 GLN A C     1 
ATOM   9151  O  O     . GLN A 1 1411 ? 155.490 196.639 99.506  1.00 62.27  ? 1411 GLN A O     1 
ATOM   9152  C  CB    . GLN A 1 1411 ? 152.650 197.112 100.588 1.00 69.70  ? 1411 GLN A CB    1 
ATOM   9153  C  CG    . GLN A 1 1411 ? 151.261 197.450 100.077 1.00 70.53  ? 1411 GLN A CG    1 
ATOM   9154  C  CD    . GLN A 1 1411 ? 150.350 197.959 101.173 1.00 78.48  ? 1411 GLN A CD    1 
ATOM   9155  O  OE1   . GLN A 1 1411 ? 149.211 197.512 101.308 1.00 77.27  ? 1411 GLN A OE1   1 
ATOM   9156  N  NE2   . GLN A 1 1411 ? 150.847 198.901 101.962 1.00 79.10  ? 1411 GLN A NE2   1 
ATOM   9157  N  N     . GLN A 1 1412 ? 155.245 195.050 101.081 1.00 61.55  ? 1412 GLN A N     1 
ATOM   9158  C  CA    . GLN A 1 1412 ? 156.662 194.913 101.374 1.00 58.70  ? 1412 GLN A CA    1 
ATOM   9159  C  C     . GLN A 1 1412 ? 156.957 193.438 101.598 1.00 56.68  ? 1412 GLN A C     1 
ATOM   9160  O  O     . GLN A 1 1412 ? 156.093 192.684 102.050 1.00 57.19  ? 1412 GLN A O     1 
ATOM   9161  C  CB    . GLN A 1 1412 ? 157.054 195.746 102.603 1.00 64.59  ? 1412 GLN A CB    1 
ATOM   9162  C  CG    . GLN A 1 1412 ? 158.527 195.718 102.967 1.00 65.29  ? 1412 GLN A CG    1 
ATOM   9163  C  CD    . GLN A 1 1412 ? 158.801 196.410 104.286 1.00 73.80  ? 1412 GLN A CD    1 
ATOM   9164  O  OE1   . GLN A 1 1412 ? 159.705 196.028 105.028 1.00 74.18  ? 1412 GLN A OE1   1 
ATOM   9165  N  NE2   . GLN A 1 1412 ? 158.014 197.436 104.588 1.00 75.52  ? 1412 GLN A NE2   1 
ATOM   9166  N  N     . PHE A 1 1413 ? 158.181 193.028 101.275 1.00 56.31  ? 1413 PHE A N     1 
ATOM   9167  C  CA    . PHE A 1 1413 ? 158.567 191.627 101.344 1.00 54.46  ? 1413 PHE A CA    1 
ATOM   9168  C  C     . PHE A 1 1413 ? 159.871 191.470 102.107 1.00 54.28  ? 1413 PHE A C     1 
ATOM   9169  O  O     . PHE A 1 1413 ? 160.781 192.294 101.981 1.00 60.36  ? 1413 PHE A O     1 
ATOM   9170  C  CB    . PHE A 1 1413 ? 158.703 191.026 99.941  1.00 53.57  ? 1413 PHE A CB    1 
ATOM   9171  C  CG    . PHE A 1 1413 ? 157.431 191.056 99.149  1.00 56.04  ? 1413 PHE A CG    1 
ATOM   9172  C  CD1   . PHE A 1 1413 ? 156.446 190.111 99.365  1.00 54.21  ? 1413 PHE A CD1   1 
ATOM   9173  C  CD2   . PHE A 1 1413 ? 157.207 192.046 98.212  1.00 60.94  ? 1413 PHE A CD2   1 
ATOM   9174  C  CE1   . PHE A 1 1413 ? 155.272 190.140 98.646  1.00 56.87  ? 1413 PHE A CE1   1 
ATOM   9175  C  CE2   . PHE A 1 1413 ? 156.034 192.082 97.493  1.00 61.42  ? 1413 PHE A CE2   1 
ATOM   9176  C  CZ    . PHE A 1 1413 ? 155.065 191.128 97.710  1.00 59.32  ? 1413 PHE A CZ    1 
ATOM   9177  N  N     . LEU A 1 1414 ? 159.951 190.404 102.900 1.00 51.39  ? 1414 LEU A N     1 
ATOM   9178  C  CA    . LEU A 1 1414 ? 161.153 190.042 103.637 1.00 52.68  ? 1414 LEU A CA    1 
ATOM   9179  C  C     . LEU A 1 1414 ? 161.499 188.599 103.307 1.00 53.24  ? 1414 LEU A C     1 
ATOM   9180  O  O     . LEU A 1 1414 ? 160.642 187.717 103.410 1.00 51.76  ? 1414 LEU A O     1 
ATOM   9181  C  CB    . LEU A 1 1414 ? 160.949 190.207 105.145 1.00 51.44  ? 1414 LEU A CB    1 
ATOM   9182  C  CG    . LEU A 1 1414 ? 160.774 191.625 105.690 1.00 56.05  ? 1414 LEU A CG    1 
ATOM   9183  C  CD1   . LEU A 1 1414 ? 160.467 191.579 107.177 1.00 51.80  ? 1414 LEU A CD1   1 
ATOM   9184  C  CD2   . LEU A 1 1414 ? 161.994 192.487 105.413 1.00 55.18  ? 1414 LEU A CD2   1 
ATOM   9185  N  N     . VAL A 1 1415 ? 162.746 188.358 102.911 1.00 52.90  ? 1415 VAL A N     1 
ATOM   9186  C  CA    . VAL A 1 1415 ? 163.204 187.034 102.507 1.00 54.05  ? 1415 VAL A CA    1 
ATOM   9187  C  C     . VAL A 1 1415 ? 164.319 186.609 103.450 1.00 54.26  ? 1415 VAL A C     1 
ATOM   9188  O  O     . VAL A 1 1415 ? 165.295 187.347 103.637 1.00 57.31  ? 1415 VAL A O     1 
ATOM   9189  C  CB    . VAL A 1 1415 ? 163.689 187.012 101.049 1.00 56.15  ? 1415 VAL A CB    1 
ATOM   9190  C  CG1   . VAL A 1 1415 ? 164.192 185.629 100.680 1.00 56.33  ? 1415 VAL A CG1   1 
ATOM   9191  C  CG2   . VAL A 1 1415 ? 162.576 187.435 100.119 1.00 54.16  ? 1415 VAL A CG2   1 
ATOM   9192  N  N     . ILE A 1 1416 ? 164.174 185.429 104.044 1.00 52.19  ? 1416 ILE A N     1 
ATOM   9193  C  CA    . ILE A 1 1416 ? 165.172 184.873 104.949 1.00 54.07  ? 1416 ILE A CA    1 
ATOM   9194  C  C     . ILE A 1 1416 ? 166.019 183.877 104.169 1.00 61.17  ? 1416 ILE A C     1 
ATOM   9195  O  O     . ILE A 1 1416 ? 165.516 182.857 103.688 1.00 62.47  ? 1416 ILE A O     1 
ATOM   9196  C  CB    . ILE A 1 1416 ? 164.526 184.210 106.172 1.00 48.62  ? 1416 ILE A CB    1 
ATOM   9197  C  CG1   . ILE A 1 1416 ? 163.785 185.247 107.014 1.00 47.23  ? 1416 ILE A CG1   1 
ATOM   9198  C  CG2   . ILE A 1 1416 ? 165.574 183.497 107.008 1.00 48.59  ? 1416 ILE A CG2   1 
ATOM   9199  C  CD1   . ILE A 1 1416 ? 162.972 184.645 108.126 1.00 41.21  ? 1416 ILE A CD1   1 
ATOM   9200  N  N     . GLU A 1 1417 ? 167.309 184.178 104.042 1.00 64.86  ? 1417 GLU A N     1 
ATOM   9201  C  CA    . GLU A 1 1417 ? 168.285 183.260 103.475 1.00 66.78  ? 1417 GLU A CA    1 
ATOM   9202  C  C     . GLU A 1 1417 ? 169.616 183.507 104.163 1.00 71.64  ? 1417 GLU A C     1 
ATOM   9203  O  O     . GLU A 1 1417 ? 169.882 184.616 104.632 1.00 71.35  ? 1417 GLU A O     1 
ATOM   9204  C  CB    . GLU A 1 1417 ? 168.422 183.427 101.956 1.00 66.05  ? 1417 GLU A CB    1 
ATOM   9205  C  CG    . GLU A 1 1417 ? 167.457 182.572 101.150 1.00 72.09  ? 1417 GLU A CG    1 
ATOM   9206  C  CD    . GLU A 1 1417 ? 167.218 183.112 99.756  1.00 77.42  ? 1417 GLU A CD    1 
ATOM   9207  O  OE1   . GLU A 1 1417 ? 166.553 182.422 98.954  1.00 75.93  ? 1417 GLU A OE1   1 
ATOM   9208  O  OE2   . GLU A 1 1417 ? 167.689 184.231 99.464  1.00 77.93  ? 1417 GLU A OE2   1 
ATOM   9209  N  N     . GLU A 1 1418 ? 170.427 182.449 104.258 1.00 72.35  ? 1418 GLU A N     1 
ATOM   9210  C  CA    . GLU A 1 1418 ? 171.787 182.501 104.812 1.00 70.78  ? 1418 GLU A CA    1 
ATOM   9211  C  C     . GLU A 1 1418 ? 171.827 183.164 106.191 1.00 72.67  ? 1418 GLU A C     1 
ATOM   9212  O  O     . GLU A 1 1418 ? 172.812 183.812 106.555 1.00 72.95  ? 1418 GLU A O     1 
ATOM   9213  C  CB    . GLU A 1 1418 ? 172.773 183.175 103.840 1.00 74.50  ? 1418 GLU A CB    1 
ATOM   9214  C  CG    . GLU A 1 1418 ? 172.668 184.693 103.692 1.00 78.13  ? 1418 GLU A CG    1 
ATOM   9215  C  CD    . GLU A 1 1418 ? 173.191 185.200 102.366 1.00 79.26  ? 1418 GLU A CD    1 
ATOM   9216  O  OE1   . GLU A 1 1418 ? 174.391 185.006 102.083 1.00 81.04  ? 1418 GLU A OE1   1 
ATOM   9217  O  OE2   . GLU A 1 1418 ? 172.394 185.788 101.605 1.00 80.56  ? 1418 GLU A OE2   1 
ATOM   9218  N  N     . ASN A 1 1419 ? 170.754 182.985 106.968 1.00 72.06  ? 1419 ASN A N     1 
ATOM   9219  C  CA    . ASN A 1 1419 ? 170.651 183.471 108.349 1.00 69.65  ? 1419 ASN A CA    1 
ATOM   9220  C  C     . ASN A 1 1419 ? 170.598 184.998 108.424 1.00 69.38  ? 1419 ASN A C     1 
ATOM   9221  O  O     . ASN A 1 1419 ? 171.092 185.598 109.378 1.00 70.15  ? 1419 ASN A O     1 
ATOM   9222  C  CB    . ASN A 1 1419 ? 171.790 182.933 109.220 1.00 66.56  ? 1419 ASN A CB    1 
ATOM   9223  C  CG    . ASN A 1 1419 ? 171.453 181.609 109.867 1.00 70.44  ? 1419 ASN A CG    1 
ATOM   9224  O  OD1   . ASN A 1 1419 ? 170.685 180.818 109.323 1.00 70.50  ? 1419 ASN A OD1   1 
ATOM   9225  N  ND2   . ASN A 1 1419 ? 172.025 181.361 111.039 1.00 73.60  ? 1419 ASN A ND2   1 
ATOM   9226  N  N     . LYS A 1 1420 ? 169.981 185.631 107.429 1.00 64.01  ? 1420 LYS A N     1 
ATOM   9227  C  CA    . LYS A 1 1420 ? 169.734 187.064 107.501 1.00 66.05  ? 1420 LYS A CA    1 
ATOM   9228  C  C     . LYS A 1 1420 ? 168.607 187.432 106.550 1.00 64.59  ? 1420 LYS A C     1 
ATOM   9229  O  O     . LYS A 1 1420 ? 168.297 186.692 105.614 1.00 64.10  ? 1420 LYS A O     1 
ATOM   9230  C  CB    . LYS A 1 1420 ? 170.990 187.882 107.191 1.00 67.58  ? 1420 LYS A CB    1 
ATOM   9231  C  CG    . LYS A 1 1420 ? 171.733 187.459 105.949 1.00 70.98  ? 1420 LYS A CG    1 
ATOM   9232  C  CD    . LYS A 1 1420 ? 173.048 188.205 105.855 1.00 75.36  ? 1420 LYS A CD    1 
ATOM   9233  C  CE    . LYS A 1 1420 ? 173.836 188.062 107.146 1.00 77.48  ? 1420 LYS A CE    1 
ATOM   9234  N  NZ    . LYS A 1 1420 ? 174.011 186.635 107.530 1.00 76.74  ? 1420 LYS A NZ    1 
ATOM   9235  N  N     . VAL A 1 1421 ? 167.999 188.586 106.809 1.00 62.58  ? 1421 VAL A N     1 
ATOM   9236  C  CA    . VAL A 1 1421 ? 166.779 189.017 106.137 1.00 58.73  ? 1421 VAL A CA    1 
ATOM   9237  C  C     . VAL A 1 1421 ? 167.125 190.039 105.063 1.00 60.92  ? 1421 VAL A C     1 
ATOM   9238  O  O     . VAL A 1 1421 ? 167.816 191.028 105.335 1.00 63.79  ? 1421 VAL A O     1 
ATOM   9239  C  CB    . VAL A 1 1421 ? 165.776 189.600 107.147 1.00 56.22  ? 1421 VAL A CB    1 
ATOM   9240  C  CG1   . VAL A 1 1421 ? 164.603 190.225 106.427 1.00 58.10  ? 1421 VAL A CG1   1 
ATOM   9241  C  CG2   . VAL A 1 1421 ? 165.300 188.520 108.104 1.00 53.03  ? 1421 VAL A CG2   1 
ATOM   9242  N  N     . ARG A 1 1422 ? 166.641 189.804 103.845 1.00 59.49  ? 1422 ARG A N     1 
ATOM   9243  C  CA    . ARG A 1 1422 ? 166.772 190.747 102.743 1.00 61.90  ? 1422 ARG A CA    1 
ATOM   9244  C  C     . ARG A 1 1422 ? 165.412 191.349 102.418 1.00 60.62  ? 1422 ARG A C     1 
ATOM   9245  O  O     . ARG A 1 1422 ? 164.400 190.641 102.390 1.00 61.15  ? 1422 ARG A O     1 
ATOM   9246  C  CB    . ARG A 1 1422 ? 167.356 190.071 101.503 1.00 69.66  ? 1422 ARG A CB    1 
ATOM   9247  C  CG    . ARG A 1 1422 ? 168.591 189.233 101.779 1.00 71.43  ? 1422 ARG A CG    1 
ATOM   9248  C  CD    . ARG A 1 1422 ? 169.853 189.960 101.347 1.00 79.62  ? 1422 ARG A CD    1 
ATOM   9249  N  NE    . ARG A 1 1422 ? 169.588 190.934 100.294 1.00 85.04  ? 1422 ARG A NE    1 
ATOM   9250  C  CZ    . ARG A 1 1422 ? 169.805 190.724 99.003  1.00 86.43  ? 1422 ARG A CZ    1 
ATOM   9251  N  NH1   . ARG A 1 1422 ? 170.291 189.576 98.561  1.00 82.80  ? 1422 ARG A NH1   1 
ATOM   9252  N  NH2   . ARG A 1 1422 ? 169.526 191.692 98.134  1.00 82.22  ? 1422 ARG A NH2   1 
ATOM   9253  N  N     . GLN A 1 1423 ? 165.393 192.654 102.168 1.00 62.42  ? 1423 GLN A N     1 
ATOM   9254  C  CA    . GLN A 1 1423 ? 164.157 193.415 102.035 1.00 62.00  ? 1423 GLN A CA    1 
ATOM   9255  C  C     . GLN A 1 1423 ? 163.928 193.808 100.581 1.00 65.27  ? 1423 GLN A C     1 
ATOM   9256  O  O     . GLN A 1 1423 ? 164.839 194.317 99.918  1.00 65.27  ? 1423 GLN A O     1 
ATOM   9257  C  CB    . GLN A 1 1423 ? 164.210 194.658 102.923 1.00 63.45  ? 1423 GLN A CB    1 
ATOM   9258  C  CG    . GLN A 1 1423 ? 162.951 195.501 102.936 1.00 65.59  ? 1423 GLN A CG    1 
ATOM   9259  C  CD    . GLN A 1 1423 ? 163.005 196.589 103.992 1.00 71.64  ? 1423 GLN A CD    1 
ATOM   9260  O  OE1   . GLN A 1 1423 ? 163.960 196.671 104.765 1.00 70.12  ? 1423 GLN A OE1   1 
ATOM   9261  N  NE2   . GLN A 1 1423 ? 161.977 197.427 104.033 1.00 68.94  ? 1423 GLN A NE2   1 
ATOM   9262  N  N     . TYR A 1 1424 ? 162.709 193.581 100.094 1.00 63.99  ? 1424 TYR A N     1 
ATOM   9263  C  CA    . TYR A 1 1424 ? 162.328 193.896 98.725  1.00 62.67  ? 1424 TYR A CA    1 
ATOM   9264  C  C     . TYR A 1 1424 ? 161.014 194.661 98.726  1.00 67.00  ? 1424 TYR A C     1 
ATOM   9265  O  O     . TYR A 1 1424 ? 160.210 194.543 99.653  1.00 73.53  ? 1424 TYR A O     1 
ATOM   9266  C  CB    . TYR A 1 1424 ? 162.174 192.637 97.866  1.00 65.17  ? 1424 TYR A CB    1 
ATOM   9267  C  CG    . TYR A 1 1424 ? 163.458 191.878 97.645  1.00 70.00  ? 1424 TYR A CG    1 
ATOM   9268  C  CD1   . TYR A 1 1424 ? 164.282 192.171 96.569  1.00 73.64  ? 1424 TYR A CD1   1 
ATOM   9269  C  CD2   . TYR A 1 1424 ? 163.839 190.858 98.502  1.00 70.18  ? 1424 TYR A CD2   1 
ATOM   9270  C  CE1   . TYR A 1 1424 ? 165.455 191.476 96.361  1.00 75.03  ? 1424 TYR A CE1   1 
ATOM   9271  C  CE2   . TYR A 1 1424 ? 165.009 190.158 98.303  1.00 70.66  ? 1424 TYR A CE2   1 
ATOM   9272  C  CZ    . TYR A 1 1424 ? 165.812 190.471 97.231  1.00 76.71  ? 1424 TYR A CZ    1 
ATOM   9273  O  OH    . TYR A 1 1424 ? 166.980 189.774 97.027  1.00 81.74  ? 1424 TYR A OH    1 
ATOM   9274  N  N     . ASP A 1 1425 ? 160.804 195.455 97.678  1.00 67.69  ? 1425 ASP A N     1 
ATOM   9275  C  CA    . ASP A 1 1425 ? 159.581 196.242 97.560  1.00 70.52  ? 1425 ASP A CA    1 
ATOM   9276  C  C     . ASP A 1 1425 ? 158.493 195.505 96.781  1.00 73.29  ? 1425 ASP A C     1 
ATOM   9277  O  O     . ASP A 1 1425 ? 157.402 195.264 97.306  1.00 72.40  ? 1425 ASP A O     1 
ATOM   9278  C  CB    . ASP A 1 1425 ? 159.892 197.592 96.909  1.00 72.54  ? 1425 ASP A CB    1 
ATOM   9279  C  CG    . ASP A 1 1425 ? 160.265 198.650 97.925  1.00 81.56  ? 1425 ASP A CG    1 
ATOM   9280  O  OD1   . ASP A 1 1425 ? 161.473 198.923 98.085  1.00 85.13  ? 1425 ASP A OD1   1 
ATOM   9281  O  OD2   . ASP A 1 1425 ? 159.351 199.205 98.569  1.00 81.15  ? 1425 ASP A OD2   1 
ATOM   9282  N  N     . SER A 1 1426 ? 158.777 195.139 95.534  1.00 76.34  ? 1426 SER A N     1 
ATOM   9283  C  CA    . SER A 1 1426 ? 157.795 194.521 94.655  1.00 78.08  ? 1426 SER A CA    1 
ATOM   9284  C  C     . SER A 1 1426 ? 158.087 193.035 94.484  1.00 76.09  ? 1426 SER A C     1 
ATOM   9285  O  O     . SER A 1 1426 ? 159.228 192.587 94.627  1.00 74.95  ? 1426 SER A O     1 
ATOM   9286  C  CB    . SER A 1 1426 ? 157.774 195.206 93.285  1.00 77.52  ? 1426 SER A CB    1 
ATOM   9287  O  OG    . SER A 1 1426 ? 158.918 194.863 92.525  1.00 76.83  ? 1426 SER A OG    1 
ATOM   9288  N  N     . ILE A 1 1427 ? 157.033 192.272 94.185  1.00 73.72  ? 1427 ILE A N     1 
ATOM   9289  C  CA    . ILE A 1 1427 ? 157.182 190.830 94.019  1.00 73.61  ? 1427 ILE A CA    1 
ATOM   9290  C  C     . ILE A 1 1427 ? 157.891 190.498 92.710  1.00 78.17  ? 1427 ILE A C     1 
ATOM   9291  O  O     . ILE A 1 1427 ? 158.624 189.505 92.631  1.00 78.32  ? 1427 ILE A O     1 
ATOM   9292  C  CB    . ILE A 1 1427 ? 155.809 190.133 94.131  1.00 71.89  ? 1427 ILE A CB    1 
ATOM   9293  C  CG1   . ILE A 1 1427 ? 155.980 188.620 94.264  1.00 67.42  ? 1427 ILE A CG1   1 
ATOM   9294  C  CG2   . ILE A 1 1427 ? 154.918 190.470 92.951  1.00 74.17  ? 1427 ILE A CG2   1 
ATOM   9295  C  CD1   . ILE A 1 1427 ? 156.866 188.210 95.407  1.00 66.63  ? 1427 ILE A CD1   1 
ATOM   9296  N  N     . GLN A 1 1428 ? 157.697 191.311 91.667  1.00 81.08  ? 1428 GLN A N     1 
ATOM   9297  C  CA    . GLN A 1 1428 ? 158.375 191.060 90.398  1.00 83.04  ? 1428 GLN A CA    1 
ATOM   9298  C  C     . GLN A 1 1428 ? 159.880 191.243 90.539  1.00 82.23  ? 1428 GLN A C     1 
ATOM   9299  O  O     . GLN A 1 1428 ? 160.666 190.433 90.034  1.00 83.22  ? 1428 GLN A O     1 
ATOM   9300  C  CB    . GLN A 1 1428 ? 157.822 191.979 89.310  1.00 83.10  ? 1428 GLN A CB    1 
ATOM   9301  C  CG    . GLN A 1 1428 ? 156.482 191.539 88.749  1.00 85.28  ? 1428 GLN A CG    1 
ATOM   9302  C  CD    . GLN A 1 1428 ? 155.313 192.070 89.553  1.00 86.81  ? 1428 GLN A CD    1 
ATOM   9303  O  OE1   . GLN A 1 1428 ? 155.486 192.586 90.656  1.00 84.55  ? 1428 GLN A OE1   1 
ATOM   9304  N  NE2   . GLN A 1 1428 ? 154.111 191.941 89.004  1.00 90.66  ? 1428 GLN A NE2   1 
ATOM   9305  N  N     . LYS A 1 1429 ? 160.298 192.313 91.219  1.00 80.38  ? 1429 LYS A N     1 
ATOM   9306  C  CA    . LYS A 1 1429 ? 161.715 192.516 91.502  1.00 81.63  ? 1429 LYS A CA    1 
ATOM   9307  C  C     . LYS A 1 1429 ? 162.287 191.351 92.300  1.00 82.59  ? 1429 LYS A C     1 
ATOM   9308  O  O     . LYS A 1 1429 ? 163.406 190.897 92.037  1.00 84.29  ? 1429 LYS A O     1 
ATOM   9309  C  CB    . LYS A 1 1429 ? 161.902 193.833 92.257  1.00 80.58  ? 1429 LYS A CB    1 
ATOM   9310  C  CG    . LYS A 1 1429 ? 163.283 194.070 92.850  1.00 80.78  ? 1429 LYS A CG    1 
ATOM   9311  C  CD    . LYS A 1 1429 ? 164.392 193.955 91.822  1.00 85.63  ? 1429 LYS A CD    1 
ATOM   9312  C  CE    . LYS A 1 1429 ? 165.720 194.389 92.421  1.00 81.68  ? 1429 LYS A CE    1 
ATOM   9313  N  NZ    . LYS A 1 1429 ? 166.822 194.356 91.425  1.00 77.40  ? 1429 LYS A NZ    1 
ATOM   9314  N  N     . LEU A 1 1430 ? 161.533 190.859 93.284  1.00 79.25  ? 1430 LEU A N     1 
ATOM   9315  C  CA    . LEU A 1 1430 ? 161.993 189.733 94.090  1.00 77.09  ? 1430 LEU A CA    1 
ATOM   9316  C  C     . LEU A 1 1430 ? 162.175 188.482 93.238  1.00 80.27  ? 1430 LEU A C     1 
ATOM   9317  O  O     . LEU A 1 1430 ? 163.179 187.772 93.364  1.00 79.73  ? 1430 LEU A O     1 
ATOM   9318  C  CB    . LEU A 1 1430 ? 160.999 189.482 95.227  1.00 73.89  ? 1430 LEU A CB    1 
ATOM   9319  C  CG    . LEU A 1 1430 ? 161.213 188.378 96.265  1.00 69.14  ? 1430 LEU A CG    1 
ATOM   9320  C  CD1   . LEU A 1 1430 ? 160.488 188.765 97.535  1.00 64.39  ? 1430 LEU A CD1   1 
ATOM   9321  C  CD2   . LEU A 1 1430 ? 160.701 187.038 95.776  1.00 70.72  ? 1430 LEU A CD2   1 
ATOM   9322  N  N     . LEU A 1 1431 ? 161.209 188.197 92.362  1.00 80.88  ? 1431 LEU A N     1 
ATOM   9323  C  CA    . LEU A 1 1431 ? 161.221 186.934 91.632  1.00 79.69  ? 1431 LEU A CA    1 
ATOM   9324  C  C     . LEU A 1 1431 ? 162.277 186.911 90.535  1.00 82.20  ? 1431 LEU A C     1 
ATOM   9325  O  O     . LEU A 1 1431 ? 162.847 185.851 90.253  1.00 83.27  ? 1431 LEU A O     1 
ATOM   9326  C  CB    . LEU A 1 1431 ? 159.839 186.662 91.038  1.00 79.09  ? 1431 LEU A CB    1 
ATOM   9327  C  CG    . LEU A 1 1431 ? 158.751 186.206 92.010  1.00 76.48  ? 1431 LEU A CG    1 
ATOM   9328  C  CD1   . LEU A 1 1431 ? 157.392 186.228 91.330  1.00 76.50  ? 1431 LEU A CD1   1 
ATOM   9329  C  CD2   . LEU A 1 1431 ? 159.065 184.820 92.551  1.00 74.07  ? 1431 LEU A CD2   1 
ATOM   9330  N  N     . ASN A 1 1432 ? 162.554 188.057 89.910  1.00 83.14  ? 1432 ASN A N     1 
ATOM   9331  C  CA    . ASN A 1 1432 ? 163.459 188.083 88.766  1.00 85.33  ? 1432 ASN A CA    1 
ATOM   9332  C  C     . ASN A 1 1432 ? 164.893 187.725 89.134  1.00 85.96  ? 1432 ASN A C     1 
ATOM   9333  O  O     . ASN A 1 1432 ? 165.669 187.358 88.247  1.00 87.33  ? 1432 ASN A O     1 
ATOM   9334  C  CB    . ASN A 1 1432 ? 163.430 189.457 88.098  1.00 86.57  ? 1432 ASN A CB    1 
ATOM   9335  C  CG    . ASN A 1 1432 ? 162.142 189.711 87.344  1.00 89.76  ? 1432 ASN A CG    1 
ATOM   9336  O  OD1   . ASN A 1 1432 ? 161.383 188.785 87.061  1.00 87.65  ? 1432 ASN A OD1   1 
ATOM   9337  N  ND2   . ASN A 1 1432 ? 161.891 190.971 87.009  1.00 86.58  ? 1432 ASN A ND2   1 
ATOM   9338  N  N     . GLU A 1 1433 ? 165.268 187.828 90.409  1.00 87.03  ? 1433 GLU A N     1 
ATOM   9339  C  CA    . GLU A 1 1433 ? 166.637 187.511 90.799  1.00 88.84  ? 1433 GLU A CA    1 
ATOM   9340  C  C     . GLU A 1 1433 ? 166.837 186.012 90.997  1.00 88.37  ? 1433 GLU A C     1 
ATOM   9341  O  O     . GLU A 1 1433 ? 167.776 185.427 90.447  1.00 87.14  ? 1433 GLU A O     1 
ATOM   9342  C  CB    . GLU A 1 1433 ? 167.011 188.279 92.067  1.00 87.77  ? 1433 GLU A CB    1 
ATOM   9343  C  CG    . GLU A 1 1433 ? 166.989 189.786 91.897  1.00 90.14  ? 1433 GLU A CG    1 
ATOM   9344  C  CD    . GLU A 1 1433 ? 167.497 190.511 93.122  1.00 94.68  ? 1433 GLU A CD    1 
ATOM   9345  O  OE1   . GLU A 1 1433 ? 167.950 189.832 94.066  1.00 93.76  ? 1433 GLU A OE1   1 
ATOM   9346  O  OE2   . GLU A 1 1433 ? 167.449 191.758 93.140  1.00 95.25  ? 1433 GLU A OE2   1 
ATOM   9347  N  N     . ARG A 1 1434 ? 165.965 185.373 91.778  1.00 86.13  ? 1434 ARG A N     1 
ATOM   9348  C  CA    . ARG A 1 1434 ? 166.070 183.939 92.053  1.00 83.48  ? 1434 ARG A CA    1 
ATOM   9349  C  C     . ARG A 1 1434 ? 165.263 183.180 91.003  1.00 85.94  ? 1434 ARG A C     1 
ATOM   9350  O  O     . ARG A 1 1434 ? 164.075 182.893 91.159  1.00 84.34  ? 1434 ARG A O     1 
ATOM   9351  C  CB    . ARG A 1 1434 ? 165.616 183.631 93.474  1.00 80.10  ? 1434 ARG A CB    1 
ATOM   9352  C  CG    . ARG A 1 1434 ? 164.404 184.421 93.930  1.00 82.18  ? 1434 ARG A CG    1 
ATOM   9353  C  CD    . ARG A 1 1434 ? 164.146 184.206 95.413  1.00 80.78  ? 1434 ARG A CD    1 
ATOM   9354  N  NE    . ARG A 1 1434 ? 165.227 184.732 96.238  1.00 77.41  ? 1434 ARG A NE    1 
ATOM   9355  C  CZ    . ARG A 1 1434 ? 165.491 186.021 96.409  1.00 75.25  ? 1434 ARG A CZ    1 
ATOM   9356  N  NH1   . ARG A 1 1434 ? 164.765 186.960 95.827  1.00 78.52  ? 1434 ARG A NH1   1 
ATOM   9357  N  NH2   . ARG A 1 1434 ? 166.511 186.377 97.185  1.00 70.84  ? 1434 ARG A NH2   1 
ATOM   9358  N  N     . SER A 1 1435 ? 165.942 182.862 89.896  1.00 88.14  ? 1435 SER A N     1 
ATOM   9359  C  CA    . SER A 1 1435 ? 165.277 182.238 88.755  1.00 84.95  ? 1435 SER A CA    1 
ATOM   9360  C  C     . SER A 1 1435 ? 164.718 180.863 89.105  1.00 82.48  ? 1435 SER A C     1 
ATOM   9361  O  O     . SER A 1 1435 ? 163.594 180.528 88.718  1.00 84.21  ? 1435 SER A O     1 
ATOM   9362  C  CB    . SER A 1 1435 ? 166.251 182.124 87.585  1.00 84.69  ? 1435 SER A CB    1 
ATOM   9363  O  OG    . SER A 1 1435 ? 167.260 181.167 87.859  1.00 87.10  ? 1435 SER A OG    1 
ATOM   9364  N  N     . LEU A 1 1436 ? 165.492 180.049 89.827  1.00 79.77  ? 1436 LEU A N     1 
ATOM   9365  C  CA    . LEU A 1 1436 ? 165.078 178.672 90.086  1.00 79.14  ? 1436 LEU A CA    1 
ATOM   9366  C  C     . LEU A 1 1436 ? 163.785 178.624 90.891  1.00 78.09  ? 1436 LEU A C     1 
ATOM   9367  O  O     . LEU A 1 1436 ? 162.944 177.744 90.680  1.00 77.16  ? 1436 LEU A O     1 
ATOM   9368  C  CB    . LEU A 1 1436 ? 166.192 177.921 90.812  1.00 78.20  ? 1436 LEU A CB    1 
ATOM   9369  C  CG    . LEU A 1 1436 ? 166.037 176.403 90.916  1.00 77.20  ? 1436 LEU A CG    1 
ATOM   9370  C  CD1   . LEU A 1 1436 ? 166.008 175.773 89.535  1.00 74.68  ? 1436 LEU A CD1   1 
ATOM   9371  C  CD2   . LEU A 1 1436 ? 167.149 175.806 91.761  1.00 73.45  ? 1436 LEU A CD2   1 
ATOM   9372  N  N     . PHE A 1 1437 ? 163.617 179.559 91.827  1.00 78.63  ? 1437 PHE A N     1 
ATOM   9373  C  CA    . PHE A 1 1437 ? 162.365 179.655 92.568  1.00 74.61  ? 1437 PHE A CA    1 
ATOM   9374  C  C     . PHE A 1 1437 ? 161.233 180.137 91.671  1.00 74.93  ? 1437 PHE A C     1 
ATOM   9375  O  O     . PHE A 1 1437 ? 160.076 179.743 91.852  1.00 72.84  ? 1437 PHE A O     1 
ATOM   9376  C  CB    . PHE A 1 1437 ? 162.547 180.588 93.764  1.00 74.51  ? 1437 PHE A CB    1 
ATOM   9377  C  CG    . PHE A 1 1437 ? 161.321 180.737 94.616  1.00 79.66  ? 1437 PHE A CG    1 
ATOM   9378  C  CD1   . PHE A 1 1437 ? 160.910 179.710 95.447  1.00 76.08  ? 1437 PHE A CD1   1 
ATOM   9379  C  CD2   . PHE A 1 1437 ? 160.591 181.914 94.605  1.00 79.42  ? 1437 PHE A CD2   1 
ATOM   9380  C  CE1   . PHE A 1 1437 ? 159.790 179.848 96.239  1.00 69.12  ? 1437 PHE A CE1   1 
ATOM   9381  C  CE2   . PHE A 1 1437 ? 159.469 182.057 95.396  1.00 72.82  ? 1437 PHE A CE2   1 
ATOM   9382  C  CZ    . PHE A 1 1437 ? 159.068 181.022 96.213  1.00 70.03  ? 1437 PHE A CZ    1 
ATOM   9383  N  N     . ARG A 1 1438 ? 161.548 180.998 90.700  1.00 77.13  ? 1438 ARG A N     1 
ATOM   9384  C  CA    . ARG A 1 1438 ? 160.525 181.520 89.801  1.00 77.22  ? 1438 ARG A CA    1 
ATOM   9385  C  C     . ARG A 1 1438 ? 160.056 180.472 88.798  1.00 78.54  ? 1438 ARG A C     1 
ATOM   9386  O  O     . ARG A 1 1438 ? 158.910 180.525 88.341  1.00 81.23  ? 1438 ARG A O     1 
ATOM   9387  C  CB    . ARG A 1 1438 ? 161.049 182.763 89.084  1.00 80.34  ? 1438 ARG A CB    1 
ATOM   9388  C  CG    . ARG A 1 1438 ? 160.023 183.477 88.228  1.00 82.96  ? 1438 ARG A CG    1 
ATOM   9389  C  CD    . ARG A 1 1438 ? 160.697 184.350 87.184  1.00 83.74  ? 1438 ARG A CD    1 
ATOM   9390  N  NE    . ARG A 1 1438 ? 162.081 183.955 86.952  1.00 88.45  ? 1438 ARG A NE    1 
ATOM   9391  C  CZ    . ARG A 1 1438 ? 162.954 184.663 86.250  1.00 91.89  ? 1438 ARG A CZ    1 
ATOM   9392  N  NH1   . ARG A 1 1438 ? 162.623 185.818 85.697  1.00 91.93  ? 1438 ARG A NH1   1 
ATOM   9393  N  NH2   . ARG A 1 1438 ? 164.192 184.201 86.101  1.00 90.45  ? 1438 ARG A NH2   1 
ATOM   9394  N  N     . GLN A 1 1439 ? 160.921 179.522 88.436  1.00 79.26  ? 1439 GLN A N     1 
ATOM   9395  C  CA    . GLN A 1 1439 ? 160.511 178.445 87.541  1.00 78.32  ? 1439 GLN A CA    1 
ATOM   9396  C  C     . GLN A 1 1439 ? 159.491 177.509 88.174  1.00 78.15  ? 1439 GLN A C     1 
ATOM   9397  O  O     . GLN A 1 1439 ? 158.765 176.823 87.447  1.00 75.50  ? 1439 GLN A O     1 
ATOM   9398  C  CB    . GLN A 1 1439 ? 161.732 177.641 87.087  1.00 80.17  ? 1439 GLN A CB    1 
ATOM   9399  C  CG    . GLN A 1 1439 ? 162.750 178.425 86.268  1.00 85.40  ? 1439 GLN A CG    1 
ATOM   9400  C  CD    . GLN A 1 1439 ? 162.147 179.110 85.049  1.00 90.79  ? 1439 GLN A CD    1 
ATOM   9401  O  OE1   . GLN A 1 1439 ? 161.177 178.624 84.470  1.00 89.92  ? 1439 GLN A OE1   1 
ATOM   9402  N  NE2   . GLN A 1 1439 ? 162.692 180.266 84.684  1.00 89.76  ? 1439 GLN A NE2   1 
ATOM   9403  N  N     . ALA A 1 1440 ? 159.417 177.463 89.503  1.00 78.10  ? 1440 ALA A N     1 
ATOM   9404  C  CA    . ALA A 1 1440 ? 158.494 176.565 90.183  1.00 74.11  ? 1440 ALA A CA    1 
ATOM   9405  C  C     . ALA A 1 1440 ? 157.082 177.124 90.295  1.00 75.77  ? 1440 ALA A C     1 
ATOM   9406  O  O     . ALA A 1 1440 ? 156.192 176.413 90.770  1.00 74.67  ? 1440 ALA A O     1 
ATOM   9407  C  CB    . ALA A 1 1440 ? 159.024 176.230 91.578  1.00 62.86  ? 1440 ALA A CB    1 
ATOM   9408  N  N     . ILE A 1 1441 ? 156.854 178.368 89.875  1.00 77.20  ? 1441 ILE A N     1 
ATOM   9409  C  CA    . ILE A 1 1441 ? 155.538 178.981 90.008  1.00 78.62  ? 1441 ILE A CA    1 
ATOM   9410  C  C     . ILE A 1 1441 ? 154.580 178.365 88.997  1.00 86.16  ? 1441 ILE A C     1 
ATOM   9411  O  O     . ILE A 1 1441 ? 154.890 178.264 87.803  1.00 86.86  ? 1441 ILE A O     1 
ATOM   9412  C  CB    . ILE A 1 1441 ? 155.633 180.503 89.827  1.00 78.35  ? 1441 ILE A CB    1 
ATOM   9413  C  CG1   . ILE A 1 1441 ? 156.693 181.087 90.760  1.00 78.46  ? 1441 ILE A CG1   1 
ATOM   9414  C  CG2   . ILE A 1 1441 ? 154.290 181.151 90.093  1.00 79.96  ? 1441 ILE A CG2   1 
ATOM   9415  C  CD1   . ILE A 1 1441 ? 156.347 180.979 92.223  1.00 78.19  ? 1441 ILE A CD1   1 
ATOM   9416  N  N     . SER A 1 1442 ? 153.408 177.952 89.475  1.00 89.25  ? 1442 SER A N     1 
ATOM   9417  C  CA    . SER A 1 1442 ? 152.406 177.348 88.610  1.00 90.82  ? 1442 SER A CA    1 
ATOM   9418  C  C     . SER A 1 1442 ? 151.926 178.359 87.568  1.00 95.35  ? 1442 SER A C     1 
ATOM   9419  O  O     . SER A 1 1442 ? 151.951 179.569 87.810  1.00 96.17  ? 1442 SER A O     1 
ATOM   9420  C  CB    . SER A 1 1442 ? 151.223 176.849 89.435  1.00 89.00  ? 1442 SER A CB    1 
ATOM   9421  O  OG    . SER A 1 1442 ? 150.355 177.915 89.778  1.00 90.86  ? 1442 SER A OG    1 
ATOM   9422  N  N     . PRO A 1 1443 ? 151.499 177.891 86.391  1.00 96.38  ? 1443 PRO A N     1 
ATOM   9423  C  CA    . PRO A 1 1443 ? 151.023 178.830 85.362  1.00 96.33  ? 1443 PRO A CA    1 
ATOM   9424  C  C     . PRO A 1 1443 ? 149.820 179.649 85.790  1.00 95.65  ? 1443 PRO A C     1 
ATOM   9425  O  O     . PRO A 1 1443 ? 149.675 180.795 85.345  1.00 98.61  ? 1443 PRO A O     1 
ATOM   9426  C  CB    . PRO A 1 1443 ? 150.685 177.911 84.180  1.00 97.68  ? 1443 PRO A CB    1 
ATOM   9427  C  CG    . PRO A 1 1443 ? 150.418 176.584 84.800  1.00 97.41  ? 1443 PRO A CG    1 
ATOM   9428  C  CD    . PRO A 1 1443 ? 151.366 176.490 85.958  1.00 92.52  ? 1443 PRO A CD    1 
ATOM   9429  N  N     . SER A 1 1444 ? 148.946 179.098 86.635  1.00 94.21  ? 1444 SER A N     1 
ATOM   9430  C  CA    . SER A 1 1444 ? 147.777 179.851 87.075  1.00 98.27  ? 1444 SER A CA    1 
ATOM   9431  C  C     . SER A 1 1444 ? 148.170 181.063 87.909  1.00 99.80  ? 1444 SER A C     1 
ATOM   9432  O  O     . SER A 1 1444 ? 147.510 182.105 87.833  1.00 99.00  ? 1444 SER A O     1 
ATOM   9433  C  CB    . SER A 1 1444 ? 146.834 178.947 87.866  1.00 98.85  ? 1444 SER A CB    1 
ATOM   9434  O  OG    . SER A 1 1444 ? 145.645 179.637 88.207  1.00 104.63 ? 1444 SER A OG    1 
ATOM   9435  N  N     . ASP A 1 1445 ? 149.224 180.945 88.717  1.00 96.61  ? 1445 ASP A N     1 
ATOM   9436  C  CA    . ASP A 1 1445 ? 149.740 182.088 89.459  1.00 91.71  ? 1445 ASP A CA    1 
ATOM   9437  C  C     . ASP A 1 1445 ? 150.697 182.934 88.637  1.00 89.90  ? 1445 ASP A C     1 
ATOM   9438  O  O     . ASP A 1 1445 ? 150.892 184.114 88.949  1.00 90.91  ? 1445 ASP A O     1 
ATOM   9439  C  CB    . ASP A 1 1445 ? 150.446 181.623 90.734  1.00 91.63  ? 1445 ASP A CB    1 
ATOM   9440  C  CG    . ASP A 1 1445 ? 149.481 181.081 91.766  1.00 93.53  ? 1445 ASP A CG    1 
ATOM   9441  O  OD1   . ASP A 1 1445 ? 148.289 181.446 91.712  1.00 95.41  ? 1445 ASP A OD1   1 
ATOM   9442  O  OD2   . ASP A 1 1445 ? 149.915 180.297 92.636  1.00 90.52  ? 1445 ASP A OD2   1 
ATOM   9443  N  N     . ARG A 1 1446 ? 151.309 182.355 87.603  1.00 92.48  ? 1446 ARG A N     1 
ATOM   9444  C  CA    . ARG A 1 1446 ? 152.255 183.111 86.791  1.00 94.77  ? 1446 ARG A CA    1 
ATOM   9445  C  C     . ARG A 1 1446 ? 151.552 184.210 86.005  1.00 96.42  ? 1446 ARG A C     1 
ATOM   9446  O  O     . ARG A 1 1446 ? 152.091 185.311 85.852  1.00 96.90  ? 1446 ARG A O     1 
ATOM   9447  C  CB    . ARG A 1 1446 ? 153.011 182.169 85.856  1.00 94.90  ? 1446 ARG A CB    1 
ATOM   9448  C  CG    . ARG A 1 1446 ? 154.225 182.798 85.203  1.00 99.84  ? 1446 ARG A CG    1 
ATOM   9449  C  CD    . ARG A 1 1446 ? 154.749 181.936 84.057  1.00 102.15 ? 1446 ARG A CD    1 
ATOM   9450  N  NE    . ARG A 1 1446 ? 156.186 182.066 83.816  1.00 103.26 ? 1446 ARG A NE    1 
ATOM   9451  C  CZ    . ARG A 1 1446 ? 157.144 181.958 84.731  1.00 99.44  ? 1446 ARG A CZ    1 
ATOM   9452  N  NH1   . ARG A 1 1446 ? 156.880 181.619 85.983  1.00 92.53  ? 1446 ARG A NH1   1 
ATOM   9453  N  NH2   . ARG A 1 1446 ? 158.407 182.170 84.373  1.00 91.25  ? 1446 ARG A NH2   1 
ATOM   9454  N  N     . VAL A 1 1447 ? 150.350 183.928 85.496  1.00 96.23  ? 1447 VAL A N     1 
ATOM   9455  C  CA    . VAL A 1 1447 ? 149.587 184.955 84.796  1.00 96.78  ? 1447 VAL A CA    1 
ATOM   9456  C  C     . VAL A 1 1447 ? 149.116 186.037 85.762  1.00 96.60  ? 1447 VAL A C     1 
ATOM   9457  O  O     . VAL A 1 1447 ? 148.984 187.205 85.379  1.00 95.81  ? 1447 VAL A O     1 
ATOM   9458  C  CB    . VAL A 1 1447 ? 148.409 184.325 84.029  1.00 95.48  ? 1447 VAL A CB    1 
ATOM   9459  C  CG1   . VAL A 1 1447 ? 148.923 183.452 82.893  1.00 94.41  ? 1447 VAL A CG1   1 
ATOM   9460  C  CG2   . VAL A 1 1447 ? 147.531 183.517 84.967  1.00 91.80  ? 1447 VAL A CG2   1 
ATOM   9461  N  N     . LYS A 1 1448 ? 148.855 185.677 87.021  1.00 96.09  ? 1448 LYS A N     1 
ATOM   9462  C  CA    . LYS A 1 1448 ? 148.439 186.672 88.006  1.00 95.57  ? 1448 LYS A CA    1 
ATOM   9463  C  C     . LYS A 1 1448 ? 149.597 187.584 88.391  1.00 93.28  ? 1448 LYS A C     1 
ATOM   9464  O  O     . LYS A 1 1448 ? 149.440 188.808 88.463  1.00 92.12  ? 1448 LYS A O     1 
ATOM   9465  C  CB    . LYS A 1 1448 ? 147.868 185.981 89.244  1.00 93.51  ? 1448 LYS A CB    1 
ATOM   9466  C  CG    . LYS A 1 1448 ? 146.392 185.652 89.146  1.00 95.06  ? 1448 LYS A CG    1 
ATOM   9467  C  CD    . LYS A 1 1448 ? 145.859 185.101 90.457  1.00 92.23  ? 1448 LYS A CD    1 
ATOM   9468  C  CE    . LYS A 1 1448 ? 144.346 185.225 90.533  1.00 92.81  ? 1448 LYS A CE    1 
ATOM   9469  N  NZ    . LYS A 1 1448 ? 143.805 184.656 91.797  1.00 95.03  ? 1448 LYS A NZ    1 
ATOM   9470  N  N     . LEU A 1 1449 ? 150.770 187.004 88.650  1.00 93.84  ? 1449 LEU A N     1 
ATOM   9471  C  CA    . LEU A 1 1449 ? 151.909 187.804 89.083  1.00 92.79  ? 1449 LEU A CA    1 
ATOM   9472  C  C     . LEU A 1 1449 ? 152.493 188.647 87.959  1.00 94.55  ? 1449 LEU A C     1 
ATOM   9473  O  O     . LEU A 1 1449 ? 153.128 189.669 88.236  1.00 95.35  ? 1449 LEU A O     1 
ATOM   9474  C  CB    . LEU A 1 1449 ? 153.000 186.904 89.661  1.00 90.29  ? 1449 LEU A CB    1 
ATOM   9475  C  CG    . LEU A 1 1449 ? 152.674 186.174 90.961  1.00 86.47  ? 1449 LEU A CG    1 
ATOM   9476  C  CD1   . LEU A 1 1449 ? 153.784 185.195 91.285  1.00 83.59  ? 1449 LEU A CD1   1 
ATOM   9477  C  CD2   . LEU A 1 1449 ? 152.466 187.158 92.100  1.00 83.01  ? 1449 LEU A CD2   1 
ATOM   9478  N  N     . PHE A 1 1450 ? 152.295 188.248 86.705  1.00 97.59  ? 1450 PHE A N     1 
ATOM   9479  C  CA    . PHE A 1 1450 ? 152.819 188.968 85.545  1.00 99.37  ? 1450 PHE A CA    1 
ATOM   9480  C  C     . PHE A 1 1450 ? 151.677 189.231 84.574  1.00 103.22 ? 1450 PHE A C     1 
ATOM   9481  O  O     . PHE A 1 1450 ? 151.570 188.581 83.527  1.00 102.17 ? 1450 PHE A O     1 
ATOM   9482  C  CB    . PHE A 1 1450 ? 153.941 188.183 84.863  1.00 97.10  ? 1450 PHE A CB    1 
ATOM   9483  C  CG    . PHE A 1 1450 ? 155.131 187.927 85.743  1.00 99.29  ? 1450 PHE A CG    1 
ATOM   9484  C  CD1   . PHE A 1 1450 ? 156.024 188.943 86.036  1.00 95.69  ? 1450 PHE A CD1   1 
ATOM   9485  C  CD2   . PHE A 1 1450 ? 155.365 186.664 86.261  1.00 100.93 ? 1450 PHE A CD2   1 
ATOM   9486  C  CE1   . PHE A 1 1450 ? 157.124 188.706 86.841  1.00 93.94  ? 1450 PHE A CE1   1 
ATOM   9487  C  CE2   . PHE A 1 1450 ? 156.463 186.422 87.067  1.00 98.64  ? 1450 PHE A CE2   1 
ATOM   9488  C  CZ    . PHE A 1 1450 ? 157.343 187.444 87.358  1.00 94.23  ? 1450 PHE A CZ    1 
ATOM   9489  N  N     . PRO A 1 1451 ? 150.797 190.190 84.893  1.00 105.34 ? 1451 PRO A N     1 
ATOM   9490  C  CA    . PRO A 1 1451 ? 149.643 190.490 84.043  1.00 105.68 ? 1451 PRO A CA    1 
ATOM   9491  C  C     . PRO A 1 1451 ? 150.031 191.211 82.755  1.00 102.83 ? 1451 PRO A C     1 
ATOM   9492  O  O     . PRO A 1 1451 ? 149.513 190.864 81.694  1.00 97.23  ? 1451 PRO A O     1 
ATOM   9493  C  CB    . PRO A 1 1451 ? 148.786 191.389 84.934  1.00 104.27 ? 1451 PRO A CB    1 
ATOM   9494  C  CG    . PRO A 1 1451 ? 149.778 192.095 85.785  1.00 100.40 ? 1451 PRO A CG    1 
ATOM   9495  C  CD    . PRO A 1 1451 ? 150.859 191.084 86.063  1.00 101.25 ? 1451 PRO A CD    1 
ATOM   9496  N  N     . GLN B 2 13   ? 129.019 109.546 118.394 1.00 115.67 ? 13   GLN G N     1 
ATOM   9497  C  CA    . GLN B 2 13   ? 129.053 108.625 119.520 1.00 118.55 ? 13   GLN G CA    1 
ATOM   9498  C  C     . GLN B 2 13   ? 129.186 107.204 119.010 1.00 119.36 ? 13   GLN G C     1 
ATOM   9499  O  O     . GLN B 2 13   ? 130.242 106.825 118.496 1.00 118.02 ? 13   GLN G O     1 
ATOM   9500  C  CB    . GLN B 2 13   ? 127.792 108.766 120.366 1.00 119.66 ? 13   GLN G CB    1 
ATOM   9501  N  N     . GLU B 2 14   ? 128.081 106.456 119.043 1.00 119.17 ? 14   GLU G N     1 
ATOM   9502  C  CA    . GLU B 2 14   ? 128.057 105.052 118.608 1.00 118.28 ? 14   GLU G CA    1 
ATOM   9503  C  C     . GLU B 2 14   ? 128.454 104.913 117.150 1.00 115.41 ? 14   GLU G C     1 
ATOM   9504  O  O     . GLU B 2 14   ? 129.223 104.023 116.793 1.00 113.27 ? 14   GLU G O     1 
ATOM   9505  C  CB    . GLU B 2 14   ? 126.679 104.423 118.825 1.00 117.27 ? 14   GLU G CB    1 
ATOM   9506  N  N     . SER B 2 15   ? 128.006 105.848 116.321 1.00 112.06 ? 15   SER G N     1 
ATOM   9507  C  CA    . SER B 2 15   ? 128.351 105.842 114.920 1.00 111.14 ? 15   SER G CA    1 
ATOM   9508  C  C     . SER B 2 15   ? 129.877 105.915 114.784 1.00 109.47 ? 15   SER G C     1 
ATOM   9509  O  O     . SER B 2 15   ? 130.433 105.243 113.933 1.00 108.16 ? 15   SER G O     1 
ATOM   9510  C  CB    . SER B 2 15   ? 127.700 107.044 114.236 1.00 110.42 ? 15   SER G CB    1 
ATOM   9511  O  OG    . SER B 2 15   ? 128.038 107.124 112.866 1.00 106.29 ? 15   SER G OG    1 
ATOM   9512  N  N     . VAL B 2 16   ? 130.569 106.755 115.548 1.00 108.49 ? 16   VAL G N     1 
ATOM   9513  C  CA    . VAL B 2 16   ? 132.018 106.711 115.465 1.00 107.43 ? 16   VAL G CA    1 
ATOM   9514  C  C     . VAL B 2 16   ? 132.580 105.422 116.071 1.00 104.72 ? 16   VAL G C     1 
ATOM   9515  O  O     . VAL B 2 16   ? 133.504 104.839 115.529 1.00 103.95 ? 16   VAL G O     1 
ATOM   9516  C  CB    . VAL B 2 16   ? 132.741 107.999 115.946 1.00 104.58 ? 16   VAL G CB    1 
ATOM   9517  C  CG1   . VAL B 2 16   ? 133.570 107.770 117.198 1.00 99.72  ? 16   VAL G CG1   1 
ATOM   9518  C  CG2   . VAL B 2 16   ? 133.647 108.508 114.843 1.00 96.98  ? 16   VAL G CG2   1 
ATOM   9519  N  N     . LYS B 2 17   ? 132.001 104.938 117.163 1.00 104.15 ? 17   LYS G N     1 
ATOM   9520  C  CA    . LYS B 2 17   ? 132.598 103.775 117.813 1.00 106.23 ? 17   LYS G CA    1 
ATOM   9521  C  C     . LYS B 2 17   ? 132.367 102.461 117.114 1.00 105.62 ? 17   LYS G C     1 
ATOM   9522  O  O     . LYS B 2 17   ? 133.219 101.590 117.160 1.00 104.36 ? 17   LYS G O     1 
ATOM   9523  C  CB    . LYS B 2 17   ? 132.223 103.695 119.292 1.00 108.40 ? 17   LYS G CB    1 
ATOM   9524  C  CG    . LYS B 2 17   ? 133.425 103.800 120.219 1.00 107.12 ? 17   LYS G CG    1 
ATOM   9525  C  CD    . LYS B 2 17   ? 133.147 104.719 121.395 1.00 107.79 ? 17   LYS G CD    1 
ATOM   9526  C  CE    . LYS B 2 17   ? 132.381 103.993 122.486 1.00 108.62 ? 17   LYS G CE    1 
ATOM   9527  N  NZ    . LYS B 2 17   ? 131.871 104.904 123.547 1.00 107.39 ? 17   LYS G NZ    1 
ATOM   9528  N  N     . GLU B 2 18   ? 131.202 102.309 116.502 1.00 105.15 ? 18   GLU G N     1 
ATOM   9529  C  CA    . GLU B 2 18   ? 130.892 101.107 115.764 1.00 104.27 ? 18   GLU G CA    1 
ATOM   9530  C  C     . GLU B 2 18   ? 131.662 101.064 114.481 1.00 103.64 ? 18   GLU G C     1 
ATOM   9531  O  O     . GLU B 2 18   ? 132.141 100.014 114.070 1.00 103.86 ? 18   GLU G O     1 
ATOM   9532  C  CB    . GLU B 2 18   ? 129.399 101.009 115.459 1.00 109.36 ? 18   GLU G CB    1 
ATOM   9533  C  CG    . GLU B 2 18   ? 128.964 99.677  114.846 1.00 113.96 ? 18   GLU G CG    1 
ATOM   9534  C  CD    . GLU B 2 18   ? 127.724 99.093  115.512 1.00 121.47 ? 18   GLU G CD    1 
ATOM   9535  O  OE1   . GLU B 2 18   ? 126.643 99.707  115.423 1.00 119.68 ? 18   GLU G OE1   1 
ATOM   9536  O  OE2   . GLU B 2 18   ? 127.829 98.018  116.132 1.00 122.79 ? 18   GLU G OE2   1 
ATOM   9537  N  N     . PHE B 2 19   ? 131.770 102.216 113.839 1.00 102.61 ? 19   PHE G N     1 
ATOM   9538  C  CA    . PHE B 2 19   ? 132.431 102.301 112.543 1.00 100.21 ? 19   PHE G CA    1 
ATOM   9539  C  C     . PHE B 2 19   ? 133.936 102.116 112.588 1.00 97.29  ? 19   PHE G C     1 
ATOM   9540  O  O     . PHE B 2 19   ? 134.502 101.544 111.670 1.00 96.85  ? 19   PHE G O     1 
ATOM   9541  C  CB    . PHE B 2 19   ? 132.001 103.566 111.792 1.00 97.87  ? 19   PHE G CB    1 
ATOM   9542  C  CG    . PHE B 2 19   ? 133.092 104.227 111.028 1.00 94.56  ? 19   PHE G CG    1 
ATOM   9543  C  CD1   . PHE B 2 19   ? 133.208 104.035 109.675 1.00 93.54  ? 19   PHE G CD1   1 
ATOM   9544  C  CD2   . PHE B 2 19   ? 133.975 105.068 111.658 1.00 91.23  ? 19   PHE G CD2   1 
ATOM   9545  C  CE1   . PHE B 2 19   ? 134.204 104.651 108.962 1.00 90.11  ? 19   PHE G CE1   1 
ATOM   9546  C  CE2   . PHE B 2 19   ? 134.979 105.690 110.955 1.00 88.52  ? 19   PHE G CE2   1 
ATOM   9547  C  CZ    . PHE B 2 19   ? 135.093 105.480 109.603 1.00 87.20  ? 19   PHE G CZ    1 
ATOM   9548  N  N     . LEU B 2 20   ? 134.591 102.571 113.645 1.00 94.64  ? 20   LEU G N     1 
ATOM   9549  C  CA    . LEU B 2 20   ? 136.025 102.364 113.732 1.00 91.34  ? 20   LEU G CA    1 
ATOM   9550  C  C     . LEU B 2 20   ? 136.355 100.877 113.708 1.00 92.19  ? 20   LEU G C     1 
ATOM   9551  O  O     . LEU B 2 20   ? 137.119 100.445 112.872 1.00 94.07  ? 20   LEU G O     1 
ATOM   9552  C  CB    . LEU B 2 20   ? 136.594 103.002 114.994 1.00 87.63  ? 20   LEU G CB    1 
ATOM   9553  C  CG    . LEU B 2 20   ? 136.991 104.474 114.902 1.00 84.34  ? 20   LEU G CG    1 
ATOM   9554  C  CD1   . LEU B 2 20   ? 137.205 105.053 116.280 1.00 76.94  ? 20   LEU G CD1   1 
ATOM   9555  C  CD2   . LEU B 2 20   ? 138.230 104.667 114.057 1.00 78.02  ? 20   LEU G CD2   1 
ATOM   9556  N  N     . ALA B 2 21   ? 135.728 100.110 114.593 1.00 94.79  ? 21   ALA G N     1 
ATOM   9557  C  CA    . ALA B 2 21   ? 135.932 98.674  114.751 1.00 93.71  ? 21   ALA G CA    1 
ATOM   9558  C  C     . ALA B 2 21   ? 135.882 97.962  113.406 1.00 91.83  ? 21   ALA G C     1 
ATOM   9559  O  O     . ALA B 2 21   ? 136.689 97.061  113.139 1.00 89.72  ? 21   ALA G O     1 
ATOM   9560  C  CB    . ALA B 2 21   ? 134.893 98.095  115.709 1.00 91.20  ? 21   ALA G CB    1 
ATOM   9561  N  N     . LYS B 2 22   ? 134.951 98.365  112.540 1.00 91.75  ? 22   LYS G N     1 
ATOM   9562  C  CA    . LYS B 2 22   ? 134.884 97.785  111.204 1.00 93.61  ? 22   LYS G CA    1 
ATOM   9563  C  C     . LYS B 2 22   ? 136.124 98.140  110.393 1.00 91.92  ? 22   LYS G C     1 
ATOM   9564  O  O     . LYS B 2 22   ? 136.636 97.308  109.636 1.00 91.93  ? 22   LYS G O     1 
ATOM   9565  C  CB    . LYS B 2 22   ? 133.614 98.255  110.494 1.00 95.19  ? 22   LYS G CB    1 
ATOM   9566  C  CG    . LYS B 2 22   ? 133.126 97.325  109.394 1.00 93.13  ? 22   LYS G CG    1 
ATOM   9567  C  CD    . LYS B 2 22   ? 131.891 97.876  108.685 1.00 96.83  ? 22   LYS G CD    1 
ATOM   9568  C  CE    . LYS B 2 22   ? 131.085 98.816  109.574 1.00 99.43  ? 22   LYS G CE    1 
ATOM   9569  N  NZ    . LYS B 2 22   ? 130.268 98.078  110.577 1.00 94.91  ? 22   LYS G NZ    1 
ATOM   9570  N  N     . ALA B 2 23   ? 136.629 99.367  110.548 1.00 90.93  ? 23   ALA G N     1 
ATOM   9571  C  CA    . ALA B 2 23   ? 137.855 99.749  109.855 1.00 89.07  ? 23   ALA G CA    1 
ATOM   9572  C  C     . ALA B 2 23   ? 139.039 98.911  110.324 1.00 87.09  ? 23   ALA G C     1 
ATOM   9573  O  O     . ALA B 2 23   ? 139.863 98.487  109.511 1.00 86.40  ? 23   ALA G O     1 
ATOM   9574  C  CB    . ALA B 2 23   ? 138.134 101.237 110.061 1.00 83.56  ? 23   ALA G CB    1 
ATOM   9575  N  N     . LYS B 2 24   ? 139.137 98.670  111.631 1.00 87.58  ? 24   LYS G N     1 
ATOM   9576  C  CA    . LYS B 2 24   ? 140.179 97.805  112.182 1.00 83.73  ? 24   LYS G CA    1 
ATOM   9577  C  C     . LYS B 2 24   ? 140.086 96.395  111.604 1.00 86.02  ? 24   LYS G C     1 
ATOM   9578  O  O     . LYS B 2 24   ? 141.090 95.807  111.165 1.00 89.59  ? 24   LYS G O     1 
ATOM   9579  C  CB    . LYS B 2 24   ? 140.032 97.781  113.706 1.00 83.83  ? 24   LYS G CB    1 
ATOM   9580  C  CG    . LYS B 2 24   ? 140.678 96.618  114.428 1.00 82.27  ? 24   LYS G CG    1 
ATOM   9581  C  CD    . LYS B 2 24   ? 142.182 96.661  114.341 1.00 82.34  ? 24   LYS G CD    1 
ATOM   9582  C  CE    . LYS B 2 24   ? 142.771 97.703  115.271 1.00 76.11  ? 24   LYS G CE    1 
ATOM   9583  N  NZ    . LYS B 2 24   ? 144.255 97.605  115.308 1.00 68.84  ? 24   LYS G NZ    1 
ATOM   9584  N  N     . GLU B 2 25   ? 138.870 95.844  111.595 1.00 88.89  ? 25   GLU G N     1 
ATOM   9585  C  CA    . GLU B 2 25   ? 138.650 94.490  111.103 1.00 91.79  ? 25   GLU G CA    1 
ATOM   9586  C  C     . GLU B 2 25   ? 139.009 94.377  109.627 1.00 92.79  ? 25   GLU G C     1 
ATOM   9587  O  O     . GLU B 2 25   ? 139.585 93.373  109.194 1.00 93.56  ? 25   GLU G O     1 
ATOM   9588  C  CB    . GLU B 2 25   ? 137.192 94.099  111.346 1.00 96.35  ? 25   GLU G CB    1 
ATOM   9589  C  CG    . GLU B 2 25   ? 136.824 92.669  111.012 1.00 100.65 ? 25   GLU G CG    1 
ATOM   9590  C  CD    . GLU B 2 25   ? 135.429 92.319  111.503 1.00 109.00 ? 25   GLU G CD    1 
ATOM   9591  O  OE1   . GLU B 2 25   ? 134.591 93.239  111.617 1.00 108.28 ? 25   GLU G OE1   1 
ATOM   9592  O  OE2   . GLU B 2 25   ? 135.174 91.131  111.792 1.00 110.71 ? 25   GLU G OE2   1 
ATOM   9593  N  N     . ASP B 2 26   ? 138.669 95.399  108.839 1.00 91.65  ? 26   ASP G N     1 
ATOM   9594  C  CA    . ASP B 2 26   ? 139.012 95.396  107.422 1.00 89.94  ? 26   ASP G CA    1 
ATOM   9595  C  C     . ASP B 2 26   ? 140.515 95.576  107.224 1.00 88.00  ? 26   ASP G C     1 
ATOM   9596  O  O     . ASP B 2 26   ? 141.109 94.954  106.337 1.00 89.84  ? 26   ASP G O     1 
ATOM   9597  C  CB    . ASP B 2 26   ? 138.224 96.497  106.708 1.00 90.38  ? 26   ASP G CB    1 
ATOM   9598  C  CG    . ASP B 2 26   ? 138.379 96.462  105.195 1.00 93.39  ? 26   ASP G CG    1 
ATOM   9599  O  OD1   . ASP B 2 26   ? 137.711 97.274  104.523 1.00 95.95  ? 26   ASP G OD1   1 
ATOM   9600  O  OD2   . ASP B 2 26   ? 139.132 95.617  104.669 1.00 94.22  ? 26   ASP G OD2   1 
ATOM   9601  N  N     . PHE B 2 27   ? 141.149 96.411  108.052 1.00 85.28  ? 27   PHE G N     1 
ATOM   9602  C  CA    . PHE B 2 27   ? 142.575 96.686  107.900 1.00 83.73  ? 27   PHE G CA    1 
ATOM   9603  C  C     . PHE B 2 27   ? 143.411 95.433  108.102 1.00 87.67  ? 27   PHE G C     1 
ATOM   9604  O  O     . PHE B 2 27   ? 144.339 95.166  107.328 1.00 87.55  ? 27   PHE G O     1 
ATOM   9605  C  CB    . PHE B 2 27   ? 143.012 97.776  108.877 1.00 80.05  ? 27   PHE G CB    1 
ATOM   9606  C  CG    . PHE B 2 27   ? 144.503 97.933  108.972 1.00 76.57  ? 27   PHE G CG    1 
ATOM   9607  C  CD1   . PHE B 2 27   ? 145.209 98.586  107.981 1.00 80.34  ? 27   PHE G CD1   1 
ATOM   9608  C  CD2   . PHE B 2 27   ? 145.198 97.416  110.052 1.00 75.04  ? 27   PHE G CD2   1 
ATOM   9609  C  CE1   . PHE B 2 27   ? 146.580 98.726  108.065 1.00 79.64  ? 27   PHE G CE1   1 
ATOM   9610  C  CE2   . PHE B 2 27   ? 146.568 97.552  110.140 1.00 76.92  ? 27   PHE G CE2   1 
ATOM   9611  C  CZ    . PHE B 2 27   ? 147.260 98.208  109.145 1.00 75.77  ? 27   PHE G CZ    1 
ATOM   9612  N  N     . LEU B 2 28   ? 143.113 94.658  109.150 1.00 89.63  ? 28   LEU G N     1 
ATOM   9613  C  CA    . LEU B 2 28   ? 143.886 93.431  109.363 1.00 88.30  ? 28   LEU G CA    1 
ATOM   9614  C  C     . LEU B 2 28   ? 143.749 92.458  108.199 1.00 92.40  ? 28   LEU G C     1 
ATOM   9615  O  O     . LEU B 2 28   ? 144.704 91.737  107.878 1.00 97.88  ? 28   LEU G O     1 
ATOM   9616  C  CB    . LEU B 2 28   ? 143.496 92.741  110.673 1.00 85.39  ? 28   LEU G CB    1 
ATOM   9617  C  CG    . LEU B 2 28   ? 143.944 93.295  112.032 1.00 87.89  ? 28   LEU G CG    1 
ATOM   9618  C  CD1   . LEU B 2 28   ? 143.918 94.800  112.107 1.00 84.02  ? 28   LEU G CD1   1 
ATOM   9619  C  CD2   . LEU B 2 28   ? 143.088 92.695  113.141 1.00 88.78  ? 28   LEU G CD2   1 
ATOM   9620  N  N     . LYS B 2 29   ? 142.588 92.437  107.542 1.00 92.79  ? 29   LYS G N     1 
ATOM   9621  C  CA    . LYS B 2 29   ? 142.386 91.523  106.424 1.00 95.41  ? 29   LYS G CA    1 
ATOM   9622  C  C     . LYS B 2 29   ? 143.403 91.778  105.318 1.00 97.75  ? 29   LYS G C     1 
ATOM   9623  O  O     . LYS B 2 29   ? 144.126 90.869  104.898 1.00 98.61  ? 29   LYS G O     1 
ATOM   9624  C  CB    . LYS B 2 29   ? 140.961 91.661  105.891 1.00 95.98  ? 29   LYS G CB    1 
ATOM   9625  C  CG    . LYS B 2 29   ? 140.207 90.351  105.794 1.00 97.72  ? 29   LYS G CG    1 
ATOM   9626  C  CD    . LYS B 2 29   ? 138.789 90.576  105.304 1.00 101.01 ? 29   LYS G CD    1 
ATOM   9627  C  CE    . LYS B 2 29   ? 138.010 89.276  105.255 1.00 106.35 ? 29   LYS G CE    1 
ATOM   9628  N  NZ    . LYS B 2 29   ? 136.652 89.474  104.685 1.00 107.66 ? 29   LYS G NZ    1 
ATOM   9629  N  N     . LYS B 2 30   ? 143.495 93.025  104.852 1.00 96.05  ? 30   LYS G N     1 
ATOM   9630  C  CA    . LYS B 2 30   ? 144.456 93.340  103.803 1.00 95.18  ? 30   LYS G CA    1 
ATOM   9631  C  C     . LYS B 2 30   ? 145.883 93.379  104.324 1.00 94.24  ? 30   LYS G C     1 
ATOM   9632  O  O     . LYS B 2 30   ? 146.821 93.256  103.529 1.00 92.57  ? 30   LYS G O     1 
ATOM   9633  C  CB    . LYS B 2 30   ? 144.099 94.666  103.136 1.00 89.57  ? 30   LYS G CB    1 
ATOM   9634  C  CG    . LYS B 2 30   ? 142.781 94.630  102.382 1.00 88.58  ? 30   LYS G CG    1 
ATOM   9635  C  CD    . LYS B 2 30   ? 142.619 95.847  101.488 1.00 87.58  ? 30   LYS G CD    1 
ATOM   9636  C  CE    . LYS B 2 30   ? 141.320 96.580  101.774 1.00 86.37  ? 30   LYS G CE    1 
ATOM   9637  N  NZ    . LYS B 2 30   ? 141.357 97.283  103.084 1.00 84.78  ? 30   LYS G NZ    1 
ATOM   9638  N  N     . TRP B 2 31   ? 146.073 93.546  105.634 1.00 95.58  ? 31   TRP G N     1 
ATOM   9639  C  CA    . TRP B 2 31   ? 147.412 93.419  106.194 1.00 96.68  ? 31   TRP G CA    1 
ATOM   9640  C  C     . TRP B 2 31   ? 147.924 91.992  106.068 1.00 100.63 ? 31   TRP G C     1 
ATOM   9641  O  O     . TRP B 2 31   ? 149.119 91.774  105.837 1.00 99.79  ? 31   TRP G O     1 
ATOM   9642  C  CB    . TRP B 2 31   ? 147.419 93.864  107.655 1.00 92.00  ? 31   TRP G CB    1 
ATOM   9643  C  CG    . TRP B 2 31   ? 148.779 93.838  108.275 1.00 94.66  ? 31   TRP G CG    1 
ATOM   9644  C  CD1   . TRP B 2 31   ? 149.335 92.813  108.983 1.00 97.14  ? 31   TRP G CD1   1 
ATOM   9645  C  CD2   . TRP B 2 31   ? 149.758 94.879  108.242 1.00 94.64  ? 31   TRP G CD2   1 
ATOM   9646  N  NE1   . TRP B 2 31   ? 150.600 93.153  109.394 1.00 98.45  ? 31   TRP G NE1   1 
ATOM   9647  C  CE2   . TRP B 2 31   ? 150.883 94.417  108.951 1.00 99.51  ? 31   TRP G CE2   1 
ATOM   9648  C  CE3   . TRP B 2 31   ? 149.793 96.158  107.682 1.00 89.07  ? 31   TRP G CE3   1 
ATOM   9649  C  CZ2   . TRP B 2 31   ? 152.029 95.188  109.115 1.00 96.06  ? 31   TRP G CZ2   1 
ATOM   9650  C  CZ3   . TRP B 2 31   ? 150.931 96.921  107.845 1.00 89.96  ? 31   TRP G CZ3   1 
ATOM   9651  C  CH2   . TRP B 2 31   ? 152.033 96.435  108.556 1.00 92.91  ? 31   TRP G CH2   1 
ATOM   9652  N  N     . GLU B 2 32   ? 147.039 91.006  106.222 1.00 103.27 ? 32   GLU G N     1 
ATOM   9653  C  CA    . GLU B 2 32   ? 147.481 89.617  106.156 1.00 104.97 ? 32   GLU G CA    1 
ATOM   9654  C  C     . GLU B 2 32   ? 147.654 89.138  104.716 1.00 105.68 ? 32   GLU G C     1 
ATOM   9655  O  O     . GLU B 2 32   ? 148.755 88.751  104.311 1.00 100.86 ? 32   GLU G O     1 
ATOM   9656  C  CB    . GLU B 2 32   ? 146.506 88.718  106.920 1.00 101.80 ? 32   GLU G CB    1 
ATOM   9657  C  CG    . GLU B 2 32   ? 146.467 89.014  108.407 1.00 103.20 ? 32   GLU G CG    1 
ATOM   9658  C  CD    . GLU B 2 32   ? 147.709 88.522  109.126 1.00 106.96 ? 32   GLU G CD    1 
ATOM   9659  O  OE1   . GLU B 2 32   ? 148.455 87.708  108.543 1.00 107.72 ? 32   GLU G OE1   1 
ATOM   9660  O  OE2   . GLU B 2 32   ? 147.945 88.958  110.271 1.00 106.37 ? 32   GLU G OE2   1 
ATOM   9661  N  N     . ASN B 2 33   ? 146.582 89.152  103.926 1.00 107.74 ? 33   ASN G N     1 
ATOM   9662  C  CA    . ASN B 2 33   ? 146.689 88.643  102.563 1.00 110.24 ? 33   ASN G CA    1 
ATOM   9663  C  C     . ASN B 2 33   ? 146.836 89.777  101.550 1.00 110.47 ? 33   ASN G C     1 
ATOM   9664  O  O     . ASN B 2 33   ? 145.842 90.359  101.102 1.00 109.57 ? 33   ASN G O     1 
ATOM   9665  C  CB    . ASN B 2 33   ? 145.493 87.741  102.235 1.00 107.95 ? 33   ASN G CB    1 
ATOM   9666  C  CG    . ASN B 2 33   ? 144.162 88.464  102.311 1.00 107.89 ? 33   ASN G CG    1 
ATOM   9667  O  OD1   . ASN B 2 33   ? 143.615 88.666  103.394 1.00 102.90 ? 33   ASN G OD1   1 
ATOM   9668  N  ND2   . ASN B 2 33   ? 143.636 88.861  101.160 1.00 113.55 ? 33   ASN G ND2   1 
ATOM   9669  N  N     . PRO B 2 34   ? 148.064 90.119  101.174 1.00 109.81 ? 34   PRO G N     1 
ATOM   9670  C  CA    . PRO B 2 34   ? 148.283 91.186  100.195 1.00 109.76 ? 34   PRO G CA    1 
ATOM   9671  C  C     . PRO B 2 34   ? 148.528 90.635  98.793  1.00 113.49 ? 34   PRO G C     1 
ATOM   9672  O  O     . PRO B 2 34   ? 148.548 89.425  98.560  1.00 113.82 ? 34   PRO G O     1 
ATOM   9673  C  CB    . PRO B 2 34   ? 149.534 91.893  100.733 1.00 104.37 ? 34   PRO G CB    1 
ATOM   9674  N  N     . ALA B 2 35   ? 148.712 91.562  97.855  1.00 115.13 ? 35   ALA G N     1 
ATOM   9675  C  CA    . ALA B 2 35   ? 149.042 91.237  96.476  1.00 117.20 ? 35   ALA G CA    1 
ATOM   9676  C  C     . ALA B 2 35   ? 150.269 92.030  96.051  1.00 119.54 ? 35   ALA G C     1 
ATOM   9677  O  O     . ALA B 2 35   ? 150.487 93.157  96.505  1.00 119.09 ? 35   ALA G O     1 
ATOM   9678  C  CB    . ALA B 2 35   ? 147.872 91.531  95.526  1.00 115.09 ? 35   ALA G CB    1 
ATOM   9679  N  N     . GLN B 2 36   ? 151.071 91.432  95.174  1.00 121.12 ? 36   GLN G N     1 
ATOM   9680  C  CA    . GLN B 2 36   ? 152.320 92.038  94.736  1.00 122.96 ? 36   GLN G CA    1 
ATOM   9681  C  C     . GLN B 2 36   ? 152.516 91.790  93.248  1.00 123.47 ? 36   GLN G C     1 
ATOM   9682  O  O     . GLN B 2 36   ? 151.811 90.985  92.633  1.00 121.27 ? 36   GLN G O     1 
ATOM   9683  C  CB    . GLN B 2 36   ? 153.520 91.495  95.524  1.00 118.07 ? 36   GLN G CB    1 
ATOM   9684  N  N     . ASN B 2 37   ? 153.491 92.504  92.678  1.00 124.81 ? 37   ASN G N     1 
ATOM   9685  C  CA    . ASN B 2 37   ? 153.846 92.380  91.262  1.00 125.10 ? 37   ASN G CA    1 
ATOM   9686  C  C     . ASN B 2 37   ? 152.647 92.661  90.361  1.00 121.59 ? 37   ASN G C     1 
ATOM   9687  O  O     . ASN B 2 37   ? 152.390 91.940  89.396  1.00 118.37 ? 37   ASN G O     1 
ATOM   9688  C  CB    . ASN B 2 37   ? 154.442 91.003  90.959  1.00 123.37 ? 37   ASN G CB    1 
ATOM   9689  N  N     . THR B 2 38   ? 151.906 93.724  90.680  1.00 119.79 ? 38   THR G N     1 
ATOM   9690  C  CA    . THR B 2 38   ? 150.688 94.021  89.935  1.00 122.32 ? 38   THR G CA    1 
ATOM   9691  C  C     . THR B 2 38   ? 150.980 94.442  88.500  1.00 125.92 ? 38   THR G C     1 
ATOM   9692  O  O     . THR B 2 38   ? 150.222 94.088  87.590  1.00 124.97 ? 38   THR G O     1 
ATOM   9693  C  CB    . THR B 2 38   ? 149.884 95.110  90.647  1.00 113.96 ? 38   THR G CB    1 
ATOM   9694  N  N     . ALA B 2 39   ? 152.064 95.181  88.269  1.00 125.71 ? 39   ALA G N     1 
ATOM   9695  C  CA    . ALA B 2 39   ? 152.322 95.684  86.927  1.00 122.88 ? 39   ALA G CA    1 
ATOM   9696  C  C     . ALA B 2 39   ? 153.804 95.974  86.751  1.00 120.30 ? 39   ALA G C     1 
ATOM   9697  O  O     . ALA B 2 39   ? 154.522 96.241  87.718  1.00 116.12 ? 39   ALA G O     1 
ATOM   9698  C  CB    . ALA B 2 39   ? 151.499 96.944  86.637  1.00 119.21 ? 39   ALA G CB    1 
ATOM   9699  N  N     . HIS B 2 40   ? 154.244 95.921  85.496  1.00 122.00 ? 40   HIS G N     1 
ATOM   9700  C  CA    . HIS B 2 40   ? 155.596 96.269  85.092  1.00 122.55 ? 40   HIS G CA    1 
ATOM   9701  C  C     . HIS B 2 40   ? 155.530 97.374  84.047  1.00 122.04 ? 40   HIS G C     1 
ATOM   9702  O  O     . HIS B 2 40   ? 154.478 97.635  83.456  1.00 121.37 ? 40   HIS G O     1 
ATOM   9703  C  CB    . HIS B 2 40   ? 156.346 95.052  84.531  1.00 120.39 ? 40   HIS G CB    1 
ATOM   9704  N  N     . LEU B 2 41   ? 156.668 98.026  83.817  1.00 121.25 ? 41   LEU G N     1 
ATOM   9705  C  CA    . LEU B 2 41   ? 156.672 99.193  82.945  1.00 122.68 ? 41   LEU G CA    1 
ATOM   9706  C  C     . LEU B 2 41   ? 156.578 98.794  81.479  1.00 124.78 ? 41   LEU G C     1 
ATOM   9707  O  O     . LEU B 2 41   ? 157.593 98.721  80.779  1.00 121.68 ? 41   LEU G O     1 
ATOM   9708  C  CB    . LEU B 2 41   ? 157.931 100.030 83.183  1.00 117.39 ? 41   LEU G CB    1 
ATOM   9709  N  N     . ASP B 2 42   ? 155.360 98.527  81.011  1.00 126.93 ? 42   ASP G N     1 
ATOM   9710  C  CA    . ASP B 2 42   ? 155.089 98.377  79.588  1.00 125.80 ? 42   ASP G CA    1 
ATOM   9711  C  C     . ASP B 2 42   ? 153.910 99.261  79.203  1.00 127.75 ? 42   ASP G C     1 
ATOM   9712  O  O     . ASP B 2 42   ? 153.876 99.830  78.107  1.00 127.35 ? 42   ASP G O     1 
ATOM   9713  C  CB    . ASP B 2 42   ? 154.812 96.915  79.236  1.00 123.61 ? 42   ASP G CB    1 
ATOM   9714  N  N     . GLN B 2 43   ? 152.937 99.375  80.109  1.00 126.68 ? 43   GLN G N     1 
ATOM   9715  C  CA    . GLN B 2 43   ? 151.744 100.182 79.891  1.00 126.26 ? 43   GLN G CA    1 
ATOM   9716  C  C     . GLN B 2 43   ? 151.906 101.626 80.348  1.00 127.05 ? 43   GLN G C     1 
ATOM   9717  O  O     . GLN B 2 43   ? 150.960 102.410 80.212  1.00 124.74 ? 43   GLN G O     1 
ATOM   9718  C  CB    . GLN B 2 43   ? 150.549 99.546  80.603  1.00 124.57 ? 43   GLN G CB    1 
ATOM   9719  N  N     . PHE B 2 44   ? 153.062 101.989 80.895  1.00 127.36 ? 44   PHE G N     1 
ATOM   9720  C  CA    . PHE B 2 44   ? 153.290 103.322 81.438  1.00 120.74 ? 44   PHE G CA    1 
ATOM   9721  C  C     . PHE B 2 44   ? 153.978 104.217 80.414  1.00 118.78 ? 44   PHE G C     1 
ATOM   9722  O  O     . PHE B 2 44   ? 154.953 103.807 79.777  1.00 117.04 ? 44   PHE G O     1 
ATOM   9723  C  CB    . PHE B 2 44   ? 154.137 103.238 82.708  1.00 114.12 ? 44   PHE G CB    1 
ATOM   9724  N  N     . GLU B 2 45   ? 153.465 105.436 80.256  1.00 117.23 ? 45   GLU G N     1 
ATOM   9725  C  CA    . GLU B 2 45   ? 154.159 106.471 79.509  1.00 114.05 ? 45   GLU G CA    1 
ATOM   9726  C  C     . GLU B 2 45   ? 155.010 107.319 80.453  1.00 111.71 ? 45   GLU G C     1 
ATOM   9727  O  O     . GLU B 2 45   ? 155.033 107.115 81.668  1.00 113.14 ? 45   GLU G O     1 
ATOM   9728  C  CB    . GLU B 2 45   ? 153.174 107.347 78.738  1.00 112.32 ? 45   GLU G CB    1 
ATOM   9729  C  CG    . GLU B 2 45   ? 152.535 106.678 77.539  1.00 114.62 ? 45   GLU G CG    1 
ATOM   9730  C  CD    . GLU B 2 45   ? 151.984 107.687 76.552  1.00 115.80 ? 45   GLU G CD    1 
ATOM   9731  O  OE1   . GLU B 2 45   ? 152.035 108.898 76.853  1.00 113.01 ? 45   GLU G OE1   1 
ATOM   9732  O  OE2   . GLU B 2 45   ? 151.507 107.276 75.474  1.00 117.98 ? 45   GLU G OE2   1 
ATOM   9733  N  N     . ARG B 2 46   ? 155.728 108.287 79.881  1.00 109.63 ? 46   ARG G N     1 
ATOM   9734  C  CA    . ARG B 2 46   ? 156.633 109.168 80.628  1.00 108.79 ? 46   ARG G CA    1 
ATOM   9735  C  C     . ARG B 2 46   ? 156.425 110.592 80.115  1.00 105.36 ? 46   ARG G C     1 
ATOM   9736  O  O     . ARG B 2 46   ? 157.034 111.001 79.124  1.00 102.90 ? 46   ARG G O     1 
ATOM   9737  C  CB    . ARG B 2 46   ? 158.079 108.714 80.483  1.00 112.09 ? 46   ARG G CB    1 
ATOM   9738  C  CG    . ARG B 2 46   ? 158.295 107.258 80.859  1.00 115.67 ? 46   ARG G CG    1 
ATOM   9739  C  CD    . ARG B 2 46   ? 159.589 106.704 80.301  1.00 119.41 ? 46   ARG G CD    1 
ATOM   9740  N  NE    . ARG B 2 46   ? 159.534 105.252 80.197  1.00 122.57 ? 46   ARG G NE    1 
ATOM   9741  C  CZ    . ARG B 2 46   ? 158.831 104.592 79.286  1.00 123.83 ? 46   ARG G CZ    1 
ATOM   9742  N  NH1   . ARG B 2 46   ? 158.121 105.226 78.367  1.00 122.92 ? 46   ARG G NH1   1 
ATOM   9743  N  NH2   . ARG B 2 46   ? 158.841 103.262 79.297  1.00 123.96 ? 46   ARG G NH2   1 
ATOM   9744  N  N     . ILE B 2 47   ? 155.562 111.343 80.798  1.00 104.52 ? 47   ILE G N     1 
ATOM   9745  C  CA    . ILE B 2 47   ? 155.167 112.665 80.328  1.00 103.04 ? 47   ILE G CA    1 
ATOM   9746  C  C     . ILE B 2 47   ? 155.958 113.765 81.024  1.00 99.31  ? 47   ILE G C     1 
ATOM   9747  O  O     . ILE B 2 47   ? 156.727 114.492 80.386  1.00 95.96  ? 47   ILE G O     1 
ATOM   9748  C  CB    . ILE B 2 47   ? 153.657 112.885 80.526  1.00 97.22  ? 47   ILE G CB    1 
ATOM   9749  C  CG1   . ILE B 2 47   ? 152.859 111.885 79.691  1.00 95.43  ? 47   ILE G CG1   1 
ATOM   9750  C  CG2   . ILE B 2 47   ? 153.275 114.309 80.167  1.00 94.83  ? 47   ILE G CG2   1 
ATOM   9751  C  CD1   . ILE B 2 47   ? 151.406 111.816 80.070  1.00 95.18  ? 47   ILE G CD1   1 
ATOM   9752  N  N     . LYS B 2 48   ? 155.779 113.890 82.332  1.00 97.39  ? 48   LYS G N     1 
ATOM   9753  C  CA    . LYS B 2 48   ? 156.262 115.030 83.099  1.00 96.86  ? 48   LYS G CA    1 
ATOM   9754  C  C     . LYS B 2 48   ? 157.135 114.549 84.253  1.00 94.99  ? 48   LYS G C     1 
ATOM   9755  O  O     . LYS B 2 48   ? 157.407 113.358 84.404  1.00 98.67  ? 48   LYS G O     1 
ATOM   9756  C  CB    . LYS B 2 48   ? 155.084 115.859 83.622  1.00 98.87  ? 48   LYS G CB    1 
ATOM   9757  C  CG    . LYS B 2 48   ? 154.763 117.105 82.812  1.00 98.61  ? 48   LYS G CG    1 
ATOM   9758  C  CD    . LYS B 2 48   ? 155.999 117.948 82.552  1.00 100.12 ? 48   LYS G CD    1 
ATOM   9759  C  CE    . LYS B 2 48   ? 156.479 118.628 83.827  1.00 101.84 ? 48   LYS G CE    1 
ATOM   9760  N  NZ    . LYS B 2 48   ? 155.420 119.474 84.443  1.00 99.88  ? 48   LYS G NZ    1 
ATOM   9761  N  N     . THR B 2 49   ? 157.546 115.488 85.084  1.00 93.41  ? 49   THR G N     1 
ATOM   9762  C  CA    . THR B 2 49   ? 158.303 115.175 86.277  1.00 94.76  ? 49   THR G CA    1 
ATOM   9763  C  C     . THR B 2 49   ? 157.734 116.070 87.360  1.00 93.97  ? 49   THR G C     1 
ATOM   9764  O  O     . THR B 2 49   ? 158.166 117.197 87.515  1.00 99.08  ? 49   THR G O     1 
ATOM   9765  C  CB    . THR B 2 49   ? 159.807 115.425 86.112  1.00 96.17  ? 49   THR G CB    1 
ATOM   9766  O  OG1   . THR B 2 49   ? 160.428 114.248 85.600  1.00 95.25  ? 49   THR G OG1   1 
ATOM   9767  C  CG2   . THR B 2 49   ? 160.449 115.764 87.449  1.00 96.23  ? 49   THR G CG2   1 
ATOM   9768  N  N     . LEU B 2 50   ? 156.728 115.572 88.070  1.00 88.76  ? 50   LEU G N     1 
ATOM   9769  C  CA    . LEU B 2 50   ? 156.068 116.311 89.144  1.00 86.54  ? 50   LEU G CA    1 
ATOM   9770  C  C     . LEU B 2 50   ? 156.893 116.706 90.359  1.00 89.52  ? 50   LEU G C     1 
ATOM   9771  O  O     . LEU B 2 50   ? 156.834 117.838 90.795  1.00 90.12  ? 50   LEU G O     1 
ATOM   9772  C  CB    . LEU B 2 50   ? 154.848 115.541 89.629  1.00 85.94  ? 50   LEU G CB    1 
ATOM   9773  C  CG    . LEU B 2 50   ? 153.650 115.524 88.697  1.00 81.95  ? 50   LEU G CG    1 
ATOM   9774  C  CD1   . LEU B 2 50   ? 154.125 115.849 87.300  1.00 86.73  ? 50   LEU G CD1   1 
ATOM   9775  C  CD2   . LEU B 2 50   ? 152.956 114.175 88.725  1.00 77.67  ? 50   LEU G CD2   1 
ATOM   9776  N  N     . GLY B 2 51   ? 157.638 115.774 90.930  1.00 90.88  ? 51   GLY G N     1 
ATOM   9777  C  CA    . GLY B 2 51   ? 158.414 116.084 92.114  1.00 91.47  ? 51   GLY G CA    1 
ATOM   9778  C  C     . GLY B 2 51   ? 159.824 115.546 92.175  1.00 94.36  ? 51   GLY G C     1 
ATOM   9779  O  O     . GLY B 2 51   ? 160.350 114.999 91.213  1.00 93.36  ? 51   GLY G O     1 
ATOM   9780  N  N     . THR B 2 52   ? 160.442 115.697 93.333  1.00 100.19 ? 52   THR G N     1 
ATOM   9781  C  CA    . THR B 2 52   ? 161.812 115.261 93.515  1.00 99.50  ? 52   THR G CA    1 
ATOM   9782  C  C     . THR B 2 52   ? 161.986 114.379 94.758  1.00 100.77 ? 52   THR G C     1 
ATOM   9783  O  O     . THR B 2 52   ? 161.771 113.182 94.689  1.00 98.21  ? 52   THR G O     1 
ATOM   9784  C  CB    . THR B 2 52   ? 162.746 116.483 93.531  1.00 30.00  ? 52   THR G CB    1 
ATOM   9785  O  OG1   . THR B 2 52   ? 163.930 116.199 94.278  1.00 30.00  ? 52   THR G OG1   1 
ATOM   9786  C  CG2   . THR B 2 52   ? 162.032 117.672 94.137  1.00 30.00  ? 52   THR G CG2   1 
ATOM   9787  N  N     . GLY B 2 53   ? 162.363 114.963 95.890  1.00 102.46 ? 53   GLY G N     1 
ATOM   9788  C  CA    . GLY B 2 53   ? 162.549 114.197 97.105  1.00 100.51 ? 53   GLY G CA    1 
ATOM   9789  C  C     . GLY B 2 53   ? 163.992 113.799 97.361  1.00 105.06 ? 53   GLY G C     1 
ATOM   9790  O  O     . GLY B 2 53   ? 164.795 113.680 96.447  1.00 105.80 ? 53   GLY G O     1 
ATOM   9791  N  N     . SER B 2 54   ? 164.318 113.550 98.622  1.00 105.12 ? 54   SER G N     1 
ATOM   9792  C  CA    . SER B 2 54   ? 165.675 113.171 99.000  1.00 107.02 ? 54   SER G CA    1 
ATOM   9793  C  C     . SER B 2 54   ? 166.015 111.707 98.716  1.00 109.28 ? 54   SER G C     1 
ATOM   9794  O  O     . SER B 2 54   ? 167.174 111.310 98.815  1.00 108.87 ? 54   SER G O     1 
ATOM   9795  C  CB    . SER B 2 54   ? 165.918 113.491 100.473 1.00 30.00  ? 54   SER G CB    1 
ATOM   9796  O  OG    . SER B 2 54   ? 164.863 113.010 101.273 1.00 30.00  ? 54   SER G OG    1 
ATOM   9797  N  N     . PHE B 2 55   ? 165.011 110.901 98.384  1.00 108.61 ? 55   PHE G N     1 
ATOM   9798  C  CA    . PHE B 2 55   ? 165.242 109.496 98.088  1.00 107.96 ? 55   PHE G CA    1 
ATOM   9799  C  C     . PHE B 2 55   ? 164.749 109.087 96.697  1.00 106.92 ? 55   PHE G C     1 
ATOM   9800  O  O     . PHE B 2 55   ? 165.477 108.464 95.931  1.00 105.54 ? 55   PHE G O     1 
ATOM   9801  C  CB    . PHE B 2 55   ? 164.612 108.614 99.169  1.00 30.00  ? 55   PHE G CB    1 
ATOM   9802  C  CG    . PHE B 2 55   ? 164.858 109.103 100.564 1.00 30.00  ? 55   PHE G CG    1 
ATOM   9803  C  CD1   . PHE B 2 55   ? 166.098 108.970 101.147 1.00 30.00  ? 55   PHE G CD1   1 
ATOM   9804  C  CD2   . PHE B 2 55   ? 163.852 109.703 101.283 1.00 30.00  ? 55   PHE G CD2   1 
ATOM   9805  C  CE1   . PHE B 2 55   ? 166.327 109.424 102.426 1.00 30.00  ? 55   PHE G CE1   1 
ATOM   9806  C  CE2   . PHE B 2 55   ? 164.072 110.167 102.559 1.00 30.00  ? 55   PHE G CE2   1 
ATOM   9807  C  CZ    . PHE B 2 55   ? 165.314 110.028 103.131 1.00 30.00  ? 55   PHE G CZ    1 
ATOM   9808  N  N     . GLY B 2 56   ? 163.526 109.488 96.389  1.00 104.05 ? 56   GLY G N     1 
ATOM   9809  C  CA    . GLY B 2 56   ? 162.919 109.135 95.131  1.00 103.61 ? 56   GLY G CA    1 
ATOM   9810  C  C     . GLY B 2 56   ? 162.879 110.158 94.018  1.00 104.00 ? 56   GLY G C     1 
ATOM   9811  O  O     . GLY B 2 56   ? 163.749 111.023 93.909  1.00 102.66 ? 56   GLY G O     1 
ATOM   9812  N  N     . ARG B 2 57   ? 161.860 110.007 93.175  1.00 102.74 ? 57   ARG G N     1 
ATOM   9813  C  CA    . ARG B 2 57   ? 161.593 110.868 92.037  1.00 100.85 ? 57   ARG G CA    1 
ATOM   9814  C  C     . ARG B 2 57   ? 160.200 110.489 91.572  1.00 99.91  ? 57   ARG G C     1 
ATOM   9815  O  O     . ARG B 2 57   ? 159.949 109.322 91.329  1.00 101.05 ? 57   ARG G O     1 
ATOM   9816  C  CB    . ARG B 2 57   ? 162.612 110.618 90.930  1.00 98.13  ? 57   ARG G CB    1 
ATOM   9817  C  CG    . ARG B 2 57   ? 162.077 110.858 89.532  1.00 100.53 ? 57   ARG G CG    1 
ATOM   9818  C  CD    . ARG B 2 57   ? 162.154 112.325 89.160  1.00 100.57 ? 57   ARG G CD    1 
ATOM   9819  N  NE    . ARG B 2 57   ? 162.723 112.507 87.832  1.00 104.07 ? 57   ARG G NE    1 
ATOM   9820  C  CZ    . ARG B 2 57   ? 163.952 112.954 87.597  1.00 104.02 ? 57   ARG G CZ    1 
ATOM   9821  N  NH1   . ARG B 2 57   ? 164.377 113.076 86.351  1.00 100.55 ? 57   ARG G NH1   1 
ATOM   9822  N  NH2   . ARG B 2 57   ? 164.758 113.280 88.600  1.00 101.22 ? 57   ARG G NH2   1 
ATOM   9823  N  N     . VAL B 2 58   ? 159.299 111.462 91.459  1.00 95.99  ? 58   VAL G N     1 
ATOM   9824  C  CA    . VAL B 2 58   ? 157.916 111.214 91.048  1.00 91.77  ? 58   VAL G CA    1 
ATOM   9825  C  C     . VAL B 2 58   ? 157.574 111.819 89.703  1.00 92.42  ? 58   VAL G C     1 
ATOM   9826  O  O     . VAL B 2 58   ? 157.651 113.021 89.539  1.00 93.84  ? 58   VAL G O     1 
ATOM   9827  C  CB    . VAL B 2 58   ? 156.948 111.831 92.052  1.00 87.13  ? 58   VAL G CB    1 
ATOM   9828  C  CG1   . VAL B 2 58   ? 155.519 111.459 91.706  1.00 81.80  ? 58   VAL G CG1   1 
ATOM   9829  C  CG2   . VAL B 2 58   ? 157.313 111.410 93.463  1.00 87.31  ? 58   VAL G CG2   1 
ATOM   9830  N  N     . MET B 2 59   ? 157.142 110.993 88.760  1.00 90.87  ? 59   MET G N     1 
ATOM   9831  C  CA    . MET B 2 59   ? 156.834 111.470 87.419  1.00 91.13  ? 59   MET G CA    1 
ATOM   9832  C  C     . MET B 2 59   ? 155.442 111.093 86.909  1.00 90.69  ? 59   MET G C     1 
ATOM   9833  O  O     . MET B 2 59   ? 154.963 110.018 87.183  1.00 90.90  ? 59   MET G O     1 
ATOM   9834  C  CB    . MET B 2 59   ? 157.900 110.946 86.465  1.00 93.27  ? 59   MET G CB    1 
ATOM   9835  C  CG    . MET B 2 59   ? 157.996 109.437 86.387  1.00 95.68  ? 59   MET G CG    1 
ATOM   9836  S  SD    . MET B 2 59   ? 157.045 108.768 85.010  1.00 108.06 ? 59   MET G SD    1 
ATOM   9837  C  CE    . MET B 2 59   ? 158.331 108.218 83.890  1.00 99.31  ? 59   MET G CE    1 
ATOM   9838  N  N     . LEU B 2 60   ? 154.802 111.974 86.147  1.00 90.58  ? 60   LEU G N     1 
ATOM   9839  C  CA    . LEU B 2 60   ? 153.464 111.696 85.635  1.00 90.28  ? 60   LEU G CA    1 
ATOM   9840  C  C     . LEU B 2 60   ? 153.470 110.540 84.641  1.00 93.33  ? 60   LEU G C     1 
ATOM   9841  O  O     . LEU B 2 60   ? 154.400 110.390 83.844  1.00 97.91  ? 60   LEU G O     1 
ATOM   9842  C  CB    . LEU B 2 60   ? 152.889 112.949 84.972  1.00 90.71  ? 60   LEU G CB    1 
ATOM   9843  C  CG    . LEU B 2 60   ? 151.445 112.903 84.469  1.00 91.83  ? 60   LEU G CG    1 
ATOM   9844  C  CD1   . LEU B 2 60   ? 150.482 112.684 85.618  1.00 88.82  ? 60   LEU G CD1   1 
ATOM   9845  C  CD2   . LEU B 2 60   ? 151.098 114.176 83.720  1.00 91.99  ? 60   LEU G CD2   1 
ATOM   9846  N  N     . VAL B 2 61   ? 152.417 109.721 84.694  1.00 91.58  ? 61   VAL G N     1 
ATOM   9847  C  CA    . VAL B 2 61   ? 152.268 108.540 83.854  1.00 94.33  ? 61   VAL G CA    1 
ATOM   9848  C  C     . VAL B 2 61   ? 150.819 108.452 83.383  1.00 100.58 ? 61   VAL G C     1 
ATOM   9849  O  O     . VAL B 2 61   ? 149.902 108.963 84.027  1.00 102.00 ? 61   VAL G O     1 
ATOM   9850  C  CB    . VAL B 2 61   ? 152.684 107.257 84.618  1.00 95.10  ? 61   VAL G CB    1 
ATOM   9851  C  CG1   . VAL B 2 61   ? 152.298 105.996 83.877  1.00 103.01 ? 61   VAL G CG1   1 
ATOM   9852  C  CG2   . VAL B 2 61   ? 154.170 107.256 84.874  1.00 94.69  ? 61   VAL G CG2   1 
ATOM   9853  N  N     . LYS B 2 62   ? 150.619 107.804 82.234  1.00 105.37 ? 62   LYS G N     1 
ATOM   9854  C  CA    . LYS B 2 62   ? 149.292 107.387 81.804  1.00 108.82 ? 62   LYS G CA    1 
ATOM   9855  C  C     . LYS B 2 62   ? 149.324 105.924 81.384  1.00 113.04 ? 62   LYS G C     1 
ATOM   9856  O  O     . LYS B 2 62   ? 150.342 105.415 80.908  1.00 112.82 ? 62   LYS G O     1 
ATOM   9857  C  CB    . LYS B 2 62   ? 148.749 108.237 80.642  1.00 109.95 ? 62   LYS G CB    1 
ATOM   9858  C  CG    . LYS B 2 62   ? 149.175 107.764 79.259  1.00 112.66 ? 62   LYS G CG    1 
ATOM   9859  C  CD    . LYS B 2 62   ? 148.508 108.585 78.164  1.00 112.45 ? 62   LYS G CD    1 
ATOM   9860  C  CE    . LYS B 2 62   ? 148.999 110.019 78.161  1.00 108.96 ? 62   LYS G CE    1 
ATOM   9861  N  NZ    . LYS B 2 62   ? 148.517 110.770 76.969  1.00 100.31 ? 62   LYS G NZ    1 
ATOM   9862  N  N     . HIS B 2 63   ? 148.196 105.249 81.592  1.00 118.27 ? 63   HIS G N     1 
ATOM   9863  C  CA    . HIS B 2 63   ? 147.991 103.898 81.088  1.00 124.96 ? 63   HIS G CA    1 
ATOM   9864  C  C     . HIS B 2 63   ? 147.352 103.985 79.708  1.00 125.43 ? 63   HIS G C     1 
ATOM   9865  O  O     . HIS B 2 63   ? 146.230 104.486 79.576  1.00 123.40 ? 63   HIS G O     1 
ATOM   9866  C  CB    . HIS B 2 63   ? 147.091 103.113 82.040  1.00 124.44 ? 63   HIS G CB    1 
ATOM   9867  C  CG    . HIS B 2 63   ? 147.706 101.853 82.564  1.00 126.17 ? 63   HIS G CG    1 
ATOM   9868  N  ND1   . HIS B 2 63   ? 148.936 101.827 83.186  1.00 124.03 ? 63   HIS G ND1   1 
ATOM   9869  C  CD2   . HIS B 2 63   ? 147.252 100.577 82.575  1.00 128.13 ? 63   HIS G CD2   1 
ATOM   9870  C  CE1   . HIS B 2 63   ? 149.217 100.588 83.549  1.00 123.65 ? 63   HIS G CE1   1 
ATOM   9871  N  NE2   . HIS B 2 63   ? 148.212 99.810  83.189  1.00 128.31 ? 63   HIS G NE2   1 
ATOM   9872  N  N     . MET B 2 64   ? 148.046 103.500 78.676  1.00 128.02 ? 64   MET G N     1 
ATOM   9873  C  CA    . MET B 2 64   ? 147.468 103.597 77.340  1.00 129.37 ? 64   MET G CA    1 
ATOM   9874  C  C     . MET B 2 64   ? 146.328 102.613 77.122  1.00 131.79 ? 64   MET G C     1 
ATOM   9875  O  O     . MET B 2 64   ? 145.504 102.838 76.231  1.00 131.22 ? 64   MET G O     1 
ATOM   9876  C  CB    . MET B 2 64   ? 148.527 103.396 76.251  1.00 127.97 ? 64   MET G CB    1 
ATOM   9877  C  CG    . MET B 2 64   ? 149.629 104.445 76.239  1.00 127.79 ? 64   MET G CG    1 
ATOM   9878  S  SD    . MET B 2 64   ? 151.251 103.751 75.862  1.00 137.42 ? 64   MET G SD    1 
ATOM   9879  C  CE    . MET B 2 64   ? 151.377 102.461 77.088  1.00 126.48 ? 64   MET G CE    1 
ATOM   9880  N  N     . GLU B 2 65   ? 146.256 101.538 77.907  1.00 130.85 ? 65   GLU G N     1 
ATOM   9881  C  CA    . GLU B 2 65   ? 145.158 100.590 77.765  1.00 129.78 ? 65   GLU G CA    1 
ATOM   9882  C  C     . GLU B 2 65   ? 143.877 101.060 78.443  1.00 128.31 ? 65   GLU G C     1 
ATOM   9883  O  O     . GLU B 2 65   ? 142.818 100.474 78.197  1.00 127.40 ? 65   GLU G O     1 
ATOM   9884  C  CB    . GLU B 2 65   ? 145.560 99.219  78.316  1.00 132.55 ? 65   GLU G CB    1 
ATOM   9885  C  CG    . GLU B 2 65   ? 145.564 99.117  79.831  1.00 138.34 ? 65   GLU G CG    1 
ATOM   9886  C  CD    . GLU B 2 65   ? 146.011 97.751  80.316  1.00 141.65 ? 65   GLU G CD    1 
ATOM   9887  O  OE1   . GLU B 2 65   ? 146.639 97.017  79.525  1.00 142.80 ? 65   GLU G OE1   1 
ATOM   9888  O  OE2   . GLU B 2 65   ? 145.727 97.410  81.485  1.00 139.22 ? 65   GLU G OE2   1 
ATOM   9889  N  N     . THR B 2 66   ? 143.944 102.085 79.288  1.00 126.61 ? 66   THR G N     1 
ATOM   9890  C  CA    . THR B 2 66   ? 142.761 102.683 79.900  1.00 125.12 ? 66   THR G CA    1 
ATOM   9891  C  C     . THR B 2 66   ? 142.622 104.168 79.612  1.00 124.16 ? 66   THR G C     1 
ATOM   9892  O  O     . THR B 2 66   ? 141.504 104.648 79.411  1.00 121.73 ? 66   THR G O     1 
ATOM   9893  C  CB    . THR B 2 66   ? 142.769 102.471 81.424  1.00 124.36 ? 66   THR G CB    1 
ATOM   9894  O  OG1   . THR B 2 66   ? 143.687 103.385 82.035  1.00 121.19 ? 66   THR G OG1   1 
ATOM   9895  C  CG2   . THR B 2 66   ? 143.164 101.046 81.773  1.00 125.59 ? 66   THR G CG2   1 
ATOM   9896  N  N     . GLY B 2 67   ? 143.727 104.914 79.589  1.00 123.93 ? 67   GLY G N     1 
ATOM   9897  C  CA    . GLY B 2 67   ? 143.710 106.339 79.351  1.00 122.68 ? 67   GLY G CA    1 
ATOM   9898  C  C     . GLY B 2 67   ? 143.844 107.189 80.598  1.00 123.68 ? 67   GLY G C     1 
ATOM   9899  O  O     . GLY B 2 67   ? 144.107 108.392 80.485  1.00 122.57 ? 67   GLY G O     1 
ATOM   9900  N  N     . ASN B 2 68   ? 143.671 106.597 81.777  1.00 121.86 ? 68   ASN G N     1 
ATOM   9901  C  CA    . ASN B 2 68   ? 143.736 107.350 83.022  1.00 117.03 ? 68   ASN G CA    1 
ATOM   9902  C  C     . ASN B 2 68   ? 145.174 107.735 83.350  1.00 113.74 ? 68   ASN G C     1 
ATOM   9903  O  O     . ASN B 2 68   ? 146.098 106.935 83.176  1.00 112.66 ? 68   ASN G O     1 
ATOM   9904  C  CB    . ASN B 2 68   ? 143.133 106.529 84.161  1.00 114.01 ? 68   ASN G CB    1 
ATOM   9905  C  CG    . ASN B 2 68   ? 141.679 106.178 83.919  1.00 117.38 ? 68   ASN G CG    1 
ATOM   9906  O  OD1   . ASN B 2 68   ? 140.997 106.822 83.122  1.00 117.54 ? 68   ASN G OD1   1 
ATOM   9907  N  ND2   . ASN B 2 68   ? 141.196 105.148 84.604  1.00 115.92 ? 68   ASN G ND2   1 
ATOM   9908  N  N     . HIS B 2 69   ? 145.360 108.966 83.819  1.00 110.45 ? 69   HIS G N     1 
ATOM   9909  C  CA    . HIS B 2 69   ? 146.676 109.435 84.231  1.00 108.79 ? 69   HIS G CA    1 
ATOM   9910  C  C     . HIS B 2 69   ? 146.949 109.066 85.684  1.00 104.28 ? 69   HIS G C     1 
ATOM   9911  O  O     . HIS B 2 69   ? 146.048 109.092 86.526  1.00 102.16 ? 69   HIS G O     1 
ATOM   9912  C  CB    . HIS B 2 69   ? 146.790 110.948 84.048  1.00 110.32 ? 69   HIS G CB    1 
ATOM   9913  C  CG    . HIS B 2 69   ? 146.900 111.378 82.618  1.00 113.92 ? 69   HIS G CG    1 
ATOM   9914  N  ND1   . HIS B 2 69   ? 145.828 111.363 81.752  1.00 116.29 ? 69   HIS G ND1   1 
ATOM   9915  C  CD2   . HIS B 2 69   ? 147.957 111.826 81.901  1.00 110.27 ? 69   HIS G CD2   1 
ATOM   9916  C  CE1   . HIS B 2 69   ? 146.218 111.787 80.564  1.00 115.85 ? 69   HIS G CE1   1 
ATOM   9917  N  NE2   . HIS B 2 69   ? 147.506 112.074 80.627  1.00 112.48 ? 69   HIS G NE2   1 
ATOM   9918  N  N     . TYR B 2 70   ? 148.202 108.718 85.972  1.00 98.24  ? 70   TYR G N     1 
ATOM   9919  C  CA    . TYR B 2 70   ? 148.617 108.329 87.312  1.00 90.36  ? 70   TYR G CA    1 
ATOM   9920  C  C     . TYR B 2 70   ? 149.986 108.922 87.614  1.00 87.56  ? 70   TYR G C     1 
ATOM   9921  O  O     . TYR B 2 70   ? 150.715 109.348 86.716  1.00 91.88  ? 70   TYR G O     1 
ATOM   9922  C  CB    . TYR B 2 70   ? 148.676 106.805 87.472  1.00 88.98  ? 70   TYR G CB    1 
ATOM   9923  C  CG    . TYR B 2 70   ? 147.348 106.099 87.333  1.00 94.81  ? 70   TYR G CG    1 
ATOM   9924  C  CD1   . TYR B 2 70   ? 146.272 106.435 88.138  1.00 95.36  ? 70   TYR G CD1   1 
ATOM   9925  C  CD2   . TYR B 2 70   ? 147.177 105.087 86.400  1.00 101.12 ? 70   TYR G CD2   1 
ATOM   9926  C  CE1   . TYR B 2 70   ? 145.060 105.788 88.015  1.00 98.16  ? 70   TYR G CE1   1 
ATOM   9927  C  CE2   . TYR B 2 70   ? 145.970 104.435 86.270  1.00 106.14 ? 70   TYR G CE2   1 
ATOM   9928  C  CZ    . TYR B 2 70   ? 144.914 104.789 87.079  1.00 104.70 ? 70   TYR G CZ    1 
ATOM   9929  O  OH    . TYR B 2 70   ? 143.709 104.140 86.951  1.00 105.53 ? 70   TYR G OH    1 
ATOM   9930  N  N     . ALA B 2 71   ? 150.322 108.954 88.898  1.00 83.35  ? 71   ALA G N     1 
ATOM   9931  C  CA    . ALA B 2 71   ? 151.663 109.299 89.339  1.00 83.36  ? 71   ALA G CA    1 
ATOM   9932  C  C     . ALA B 2 71   ? 152.479 108.032 89.580  1.00 86.45  ? 71   ALA G C     1 
ATOM   9933  O  O     . ALA B 2 71   ? 151.936 106.946 89.788  1.00 90.33  ? 71   ALA G O     1 
ATOM   9934  C  CB    . ALA B 2 71   ? 151.614 110.145 90.610  1.00 75.92  ? 71   ALA G CB    1 
ATOM   9935  N  N     . MET B 2 72   ? 153.797 108.124 89.523  1.00 87.60  ? 72   MET G N     1 
ATOM   9936  C  CA    . MET B 2 72   ? 154.627 106.957 89.764  1.00 88.47  ? 72   MET G CA    1 
ATOM   9937  C  C     . MET B 2 72   ? 155.843 107.404 90.505  1.00 92.47  ? 72   MET G C     1 
ATOM   9938  O  O     . MET B 2 72   ? 156.520 108.303 90.067  1.00 93.99  ? 72   MET G O     1 
ATOM   9939  C  CB    . MET B 2 72   ? 155.079 106.322 88.471  1.00 90.58  ? 72   MET G CB    1 
ATOM   9940  C  CG    . MET B 2 72   ? 156.459 105.702 88.583  1.00 94.38  ? 72   MET G CG    1 
ATOM   9941  S  SD    . MET B 2 72   ? 156.851 104.605 87.210  1.00 98.97  ? 72   MET G SD    1 
ATOM   9942  C  CE    . MET B 2 72   ? 155.255 104.483 86.426  1.00 100.35 ? 72   MET G CE    1 
ATOM   9943  N  N     . LYS B 2 73   ? 156.123 106.774 91.632  1.00 94.40  ? 73   LYS G N     1 
ATOM   9944  C  CA    . LYS B 2 73   ? 157.267 107.143 92.438  1.00 95.95  ? 73   LYS G CA    1 
ATOM   9945  C  C     . LYS B 2 73   ? 158.382 106.146 92.205  1.00 102.34 ? 73   LYS G C     1 
ATOM   9946  O  O     . LYS B 2 73   ? 158.175 104.956 92.364  1.00 104.87 ? 73   LYS G O     1 
ATOM   9947  C  CB    . LYS B 2 73   ? 156.863 107.158 93.899  1.00 95.42  ? 73   LYS G CB    1 
ATOM   9948  C  CG    . LYS B 2 73   ? 158.024 107.115 94.860  1.00 97.93  ? 73   LYS G CG    1 
ATOM   9949  C  CD    . LYS B 2 73   ? 157.843 108.135 95.959  1.00 95.58  ? 73   LYS G CD    1 
ATOM   9950  C  CE    . LYS B 2 73   ? 158.676 107.779 97.168  1.00 95.04  ? 73   LYS G CE    1 
ATOM   9951  N  NZ    . LYS B 2 73   ? 157.926 108.030 98.426  1.00 90.37  ? 73   LYS G NZ    1 
ATOM   9952  N  N     . ILE B 2 74   ? 159.561 106.627 91.817  1.00 103.75 ? 74   ILE G N     1 
ATOM   9953  C  CA    . ILE B 2 74   ? 160.700 105.750 91.549  1.00 106.47 ? 74   ILE G CA    1 
ATOM   9954  C  C     . ILE B 2 74   ? 161.774 105.857 92.617  1.00 107.84 ? 74   ILE G C     1 
ATOM   9955  O  O     . ILE B 2 74   ? 162.268 106.934 92.891  1.00 106.66 ? 74   ILE G O     1 
ATOM   9956  C  CB    . ILE B 2 74   ? 161.372 106.080 90.209  1.00 105.64 ? 74   ILE G CB    1 
ATOM   9957  C  CG1   . ILE B 2 74   ? 160.395 105.916 89.055  1.00 103.39 ? 74   ILE G CG1   1 
ATOM   9958  C  CG2   . ILE B 2 74   ? 162.591 105.204 90.007  1.00 106.07 ? 74   ILE G CG2   1 
ATOM   9959  C  CD1   . ILE B 2 74   ? 160.172 107.197 88.291  1.00 100.96 ? 74   ILE G CD1   1 
ATOM   9960  N  N     . LEU B 2 75   ? 162.145 104.720 93.187  1.00 113.41 ? 75   LEU G N     1 
ATOM   9961  C  CA    . LEU B 2 75   ? 163.150 104.614 94.237  1.00 114.78 ? 75   LEU G CA    1 
ATOM   9962  C  C     . LEU B 2 75   ? 164.332 103.797 93.735  1.00 119.25 ? 75   LEU G C     1 
ATOM   9963  O  O     . LEU B 2 75   ? 164.157 102.843 92.971  1.00 117.75 ? 75   LEU G O     1 
ATOM   9964  C  CB    . LEU B 2 75   ? 162.577 103.968 95.507  1.00 112.64 ? 75   LEU G CB    1 
ATOM   9965  C  CG    . LEU B 2 75   ? 161.263 104.513 96.074  1.00 105.98 ? 75   LEU G CG    1 
ATOM   9966  C  CD1   . LEU B 2 75   ? 160.063 103.792 95.476  1.00 104.79 ? 75   LEU G CD1   1 
ATOM   9967  C  CD2   . LEU B 2 75   ? 161.256 104.404 97.588  1.00 98.57  ? 75   LEU G CD2   1 
ATOM   9968  N  N     . ASP B 2 76   ? 165.535 104.173 94.168  1.00 122.05 ? 76   ASP G N     1 
ATOM   9969  C  CA    . ASP B 2 76   ? 166.762 103.501 93.751  1.00 123.59 ? 76   ASP G CA    1 
ATOM   9970  C  C     . ASP B 2 76   ? 167.137 102.424 94.764  1.00 124.74 ? 76   ASP G C     1 
ATOM   9971  O  O     . ASP B 2 76   ? 167.292 102.713 95.954  1.00 123.57 ? 76   ASP G O     1 
ATOM   9972  C  CB    . ASP B 2 76   ? 167.903 104.506 93.600  1.00 120.79 ? 76   ASP G CB    1 
ATOM   9973  N  N     . LYS B 2 77   ? 167.297 101.187 94.285  1.00 123.08 ? 77   LYS G N     1 
ATOM   9974  C  CA    . LYS B 2 77   ? 167.654 100.076 95.164  1.00 121.63 ? 77   LYS G CA    1 
ATOM   9975  C  C     . LYS B 2 77   ? 168.999 100.322 95.841  1.00 122.52 ? 77   LYS G C     1 
ATOM   9976  O  O     . LYS B 2 77   ? 169.127 100.215 97.069  1.00 121.05 ? 77   LYS G O     1 
ATOM   9977  C  CB    . LYS B 2 77   ? 167.704 98.784  94.350  1.00 120.25 ? 77   LYS G CB    1 
ATOM   9978  C  CG    . LYS B 2 77   ? 166.356 98.268  93.887  1.00 119.24 ? 77   LYS G CG    1 
ATOM   9979  C  CD    . LYS B 2 77   ? 166.469 96.834  93.406  1.00 122.24 ? 77   LYS G CD    1 
ATOM   9980  C  CE    . LYS B 2 77   ? 165.214 96.388  92.682  1.00 122.17 ? 77   LYS G CE    1 
ATOM   9981  N  NZ    . LYS B 2 77   ? 165.303 94.964  92.261  1.00 120.96 ? 77   LYS G NZ    1 
ATOM   9982  N  N     . GLN B 2 78   ? 170.014 100.665 95.044  1.00 122.40 ? 78   GLN G N     1 
ATOM   9983  C  CA    . GLN B 2 78   ? 171.361 100.851 95.572  1.00 122.29 ? 78   GLN G CA    1 
ATOM   9984  C  C     . GLN B 2 78   ? 171.416 102.010 96.556  1.00 123.20 ? 78   GLN G C     1 
ATOM   9985  O  O     . GLN B 2 78   ? 172.092 101.926 97.586  1.00 122.20 ? 78   GLN G O     1 
ATOM   9986  C  CB    . GLN B 2 78   ? 172.342 101.073 94.421  1.00 119.53 ? 78   GLN G CB    1 
ATOM   9987  C  CG    . GLN B 2 78   ? 173.789 101.239 94.852  1.00 119.91 ? 78   GLN G CG    1 
ATOM   9988  C  CD    . GLN B 2 78   ? 174.169 102.694 95.058  1.00 120.43 ? 78   GLN G CD    1 
ATOM   9989  O  OE1   . GLN B 2 78   ? 174.379 103.138 96.187  1.00 120.72 ? 78   GLN G OE1   1 
ATOM   9990  N  NE2   . GLN B 2 78   ? 174.266 103.443 93.964  1.00 116.31 ? 78   GLN G NE2   1 
ATOM   9991  N  N     . LYS B 2 79   ? 170.691 103.072 96.247  1.00 122.02 ? 79   LYS G N     1 
ATOM   9992  C  CA    . LYS B 2 79   ? 170.655 104.228 97.118  1.00 120.26 ? 79   LYS G CA    1 
ATOM   9993  C  C     . LYS B 2 79   ? 169.968 103.836 98.413  1.00 120.87 ? 79   LYS G C     1 
ATOM   9994  O  O     . LYS B 2 79   ? 170.429 104.183 99.494  1.00 118.56 ? 79   LYS G O     1 
ATOM   9995  C  CB    . LYS B 2 79   ? 169.908 105.371 96.442  1.00 117.39 ? 79   LYS G CB    1 
ATOM   9996  C  CG    . LYS B 2 79   ? 170.485 106.744 96.717  1.00 115.27 ? 79   LYS G CG    1 
ATOM   9997  C  CD    . LYS B 2 79   ? 169.388 107.796 96.794  1.00 115.15 ? 79   LYS G CD    1 
ATOM   9998  C  CE    . LYS B 2 79   ? 169.643 108.772 97.932  1.00 114.13 ? 79   LYS G CE    1 
ATOM   9999  N  NZ    . LYS B 2 79   ? 168.425 109.515 98.344  1.00 109.27 ? 79   LYS G NZ    1 
ATOM   10000 N  N     . VAL B 2 80   ? 168.871 103.091 98.296  1.00 122.56 ? 80   VAL G N     1 
ATOM   10001 C  CA    . VAL B 2 80   ? 168.121 102.648 99.469  1.00 121.06 ? 80   VAL G CA    1 
ATOM   10002 C  C     . VAL B 2 80   ? 169.026 101.866 100.413 1.00 121.12 ? 80   VAL G C     1 
ATOM   10003 O  O     . VAL B 2 80   ? 169.058 102.120 101.624 1.00 117.42 ? 80   VAL G O     1 
ATOM   10004 C  CB    . VAL B 2 80   ? 166.895 101.816 99.048  1.00 118.16 ? 80   VAL G CB    1 
ATOM   10005 C  CG1   . VAL B 2 80   ? 166.468 100.898 100.176 1.00 117.18 ? 80   VAL G CG1   1 
ATOM   10006 C  CG2   . VAL B 2 80   ? 165.741 102.728 98.666  1.00 114.70 ? 80   VAL G CG2   1 
ATOM   10007 N  N     . VAL B 2 81   ? 169.790 100.912 99.873  1.00 122.88 ? 81   VAL G N     1 
ATOM   10008 C  CA    . VAL B 2 81   ? 170.689 100.149 100.736 1.00 122.51 ? 81   VAL G CA    1 
ATOM   10009 C  C     . VAL B 2 81   ? 171.869 100.996 101.198 1.00 121.36 ? 81   VAL G C     1 
ATOM   10010 O  O     . VAL B 2 81   ? 172.472 100.701 102.235 1.00 120.76 ? 81   VAL G O     1 
ATOM   10011 C  CB    . VAL B 2 81   ? 171.178 98.859  100.044 1.00 121.63 ? 81   VAL G CB    1 
ATOM   10012 C  CG1   . VAL B 2 81   ? 170.033 98.166  99.325  1.00 120.65 ? 81   VAL G CG1   1 
ATOM   10013 C  CG2   . VAL B 2 81   ? 172.325 99.149  99.087  1.00 119.33 ? 81   VAL G CG2   1 
ATOM   10014 N  N     . LYS B 2 82   ? 172.211 102.050 100.455 1.00 121.02 ? 82   LYS G N     1 
ATOM   10015 C  CA    . LYS B 2 82   ? 173.314 102.921 100.839 1.00 120.32 ? 82   LYS G CA    1 
ATOM   10016 C  C     . LYS B 2 82   ? 172.926 103.856 101.977 1.00 119.60 ? 82   LYS G C     1 
ATOM   10017 O  O     . LYS B 2 82   ? 173.743 104.133 102.862 1.00 118.90 ? 82   LYS G O     1 
ATOM   10018 C  CB    . LYS B 2 82   ? 173.785 103.724 99.627  1.00 120.82 ? 82   LYS G CB    1 
ATOM   10019 C  CG    . LYS B 2 82   ? 174.944 104.655 99.910  1.00 120.84 ? 82   LYS G CG    1 
ATOM   10020 C  CD    . LYS B 2 82   ? 175.392 105.357 98.643  1.00 120.67 ? 82   LYS G CD    1 
ATOM   10021 C  CE    . LYS B 2 82   ? 176.570 106.272 98.914  1.00 119.63 ? 82   LYS G CE    1 
ATOM   10022 N  NZ    . LYS B 2 82   ? 176.199 107.391 99.820  1.00 114.49 ? 82   LYS G NZ    1 
ATOM   10023 N  N     . LEU B 2 83   ? 171.677 104.288 101.960 1.00 120.41 ? 83   LEU G N     1 
ATOM   10024 C  CA    . LEU B 2 83   ? 171.170 105.204 102.960 1.00 120.79 ? 83   LEU G CA    1 
ATOM   10025 C  C     . LEU B 2 83   ? 170.884 104.565 104.300 1.00 119.97 ? 83   LEU G C     1 
ATOM   10026 O  O     . LEU B 2 83   ? 170.394 105.263 105.193 1.00 116.60 ? 83   LEU G O     1 
ATOM   10027 C  CB    . LEU B 2 83   ? 169.899 105.872 102.452 1.00 119.89 ? 83   LEU G CB    1 
ATOM   10028 C  CG    . LEU B 2 83   ? 170.119 106.833 101.294 1.00 117.37 ? 83   LEU G CG    1 
ATOM   10029 C  CD1   . LEU B 2 83   ? 168.828 107.554 100.998 1.00 116.20 ? 83   LEU G CD1   1 
ATOM   10030 C  CD2   . LEU B 2 83   ? 171.243 107.811 101.591 1.00 112.92 ? 83   LEU G CD2   1 
ATOM   10031 N  N     . LYS B 2 84   ? 171.121 103.247 104.410 1.00 121.21 ? 84   LYS G N     1 
ATOM   10032 C  CA    . LYS B 2 84   ? 170.919 102.481 105.640 1.00 121.70 ? 84   LYS G CA    1 
ATOM   10033 C  C     . LYS B 2 84   ? 169.475 102.590 106.133 1.00 122.15 ? 84   LYS G C     1 
ATOM   10034 O  O     . LYS B 2 84   ? 169.217 102.627 107.336 1.00 119.85 ? 84   LYS G O     1 
ATOM   10035 C  CB    . LYS B 2 84   ? 171.903 102.909 106.734 1.00 119.02 ? 84   LYS G CB    1 
ATOM   10036 C  CG    . LYS B 2 84   ? 172.909 101.843 107.136 1.00 119.62 ? 84   LYS G CG    1 
ATOM   10037 C  CD    . LYS B 2 84   ? 172.223 100.703 107.864 1.00 122.81 ? 84   LYS G CD    1 
ATOM   10038 C  CE    . LYS B 2 84   ? 173.103 100.154 108.973 1.00 119.31 ? 84   LYS G CE    1 
ATOM   10039 N  NZ    . LYS B 2 84   ? 172.414 99.086  109.746 1.00 112.53 ? 84   LYS G NZ    1 
ATOM   10040 N  N     . GLN B 2 85   ? 168.537 102.530 105.194 1.00 120.38 ? 85   GLN G N     1 
ATOM   10041 C  CA    . GLN B 2 85   ? 167.121 102.545 105.500 1.00 115.69 ? 85   GLN G CA    1 
ATOM   10042 C  C     . GLN B 2 85   ? 166.423 101.648 104.494 1.00 114.31 ? 85   GLN G C     1 
ATOM   10043 O  O     . GLN B 2 85   ? 165.991 102.077 103.435 1.00 114.00 ? 85   GLN G O     1 
ATOM   10044 C  CB    . GLN B 2 85   ? 166.554 103.957 105.556 1.00 111.35 ? 85   GLN G CB    1 
ATOM   10045 C  CG    . GLN B 2 85   ? 166.281 104.633 104.240 1.00 117.04 ? 85   GLN G CG    1 
ATOM   10046 C  CD    . GLN B 2 85   ? 165.889 106.068 104.457 1.00 120.02 ? 85   GLN G CD    1 
ATOM   10047 O  OE1   . GLN B 2 85   ? 166.067 106.599 105.549 1.00 117.57 ? 85   GLN G OE1   1 
ATOM   10048 N  NE2   . GLN B 2 85   ? 165.353 106.705 103.428 1.00 118.23 ? 85   GLN G NE2   1 
ATOM   10049 N  N     . ILE B 2 86   ? 166.345 100.373 104.843 1.00 110.41 ? 86   ILE G N     1 
ATOM   10050 C  CA    . ILE B 2 86   ? 165.740 99.373  103.970 1.00 109.20 ? 86   ILE G CA    1 
ATOM   10051 C  C     . ILE B 2 86   ? 164.359 98.966  104.470 1.00 104.37 ? 86   ILE G C     1 
ATOM   10052 O  O     . ILE B 2 86   ? 163.457 98.694  103.674 1.00 101.88 ? 86   ILE G O     1 
ATOM   10053 C  CB    . ILE B 2 86   ? 166.677 98.153  103.833 1.00 110.32 ? 86   ILE G CB    1 
ATOM   10054 C  CG1   . ILE B 2 86   ? 168.054 98.575  103.308 1.00 110.59 ? 86   ILE G CG1   1 
ATOM   10055 C  CG2   . ILE B 2 86   ? 166.078 97.118  102.900 1.00 109.92 ? 86   ILE G CG2   1 
ATOM   10056 C  CD1   . ILE B 2 86   ? 169.076 98.890  104.386 1.00 113.16 ? 86   ILE G CD1   1 
ATOM   10057 N  N     . GLU B 2 87   ? 164.173 98.917  105.790 1.00 101.95 ? 87   GLU G N     1 
ATOM   10058 C  CA    . GLU B 2 87   ? 162.887 98.507  106.343 1.00 99.33  ? 87   GLU G CA    1 
ATOM   10059 C  C     . GLU B 2 87   ? 161.820 99.569  106.108 1.00 96.52  ? 87   GLU G C     1 
ATOM   10060 O  O     . GLU B 2 87   ? 160.638 99.245  105.948 1.00 94.80  ? 87   GLU G O     1 
ATOM   10061 C  CB    . GLU B 2 87   ? 163.044 98.204  107.833 1.00 100.63 ? 87   GLU G CB    1 
ATOM   10062 C  CG    . GLU B 2 87   ? 161.807 97.646  108.514 1.00 107.84 ? 87   GLU G CG    1 
ATOM   10063 C  CD    . GLU B 2 87   ? 162.064 97.284  109.967 1.00 112.87 ? 87   GLU G CD    1 
ATOM   10064 O  OE1   . GLU B 2 87   ? 162.094 98.197  110.818 1.00 111.00 ? 87   GLU G OE1   1 
ATOM   10065 O  OE2   . GLU B 2 87   ? 162.244 96.082  110.257 1.00 115.03 ? 87   GLU G OE2   1 
ATOM   10066 N  N     . HIS B 2 88   ? 162.220 100.843 106.088 1.00 94.56  ? 88   HIS G N     1 
ATOM   10067 C  CA    . HIS B 2 88   ? 161.256 101.926 105.921 1.00 87.42  ? 88   HIS G CA    1 
ATOM   10068 C  C     . HIS B 2 88   ? 160.543 101.845 104.577 1.00 90.15  ? 88   HIS G C     1 
ATOM   10069 O  O     . HIS B 2 88   ? 159.320 102.011 104.505 1.00 92.01  ? 88   HIS G O     1 
ATOM   10070 C  CB    . HIS B 2 88   ? 161.957 103.275 106.069 1.00 82.98  ? 88   HIS G CB    1 
ATOM   10071 C  CG    . HIS B 2 88   ? 162.072 103.739 107.485 1.00 84.19  ? 88   HIS G CG    1 
ATOM   10072 N  ND1   . HIS B 2 88   ? 161.455 103.089 108.532 1.00 83.66  ? 88   HIS G ND1   1 
ATOM   10073 C  CD2   . HIS B 2 88   ? 162.735 104.787 108.031 1.00 86.36  ? 88   HIS G CD2   1 
ATOM   10074 C  CE1   . HIS B 2 88   ? 161.731 103.717 109.660 1.00 83.18  ? 88   HIS G CE1   1 
ATOM   10075 N  NE2   . HIS B 2 88   ? 162.505 104.751 109.384 1.00 84.97  ? 88   HIS G NE2   1 
ATOM   10076 N  N     . THR B 2 89   ? 161.283 101.576 103.501 1.00 91.03  ? 89   THR G N     1 
ATOM   10077 C  CA    . THR B 2 89   ? 160.667 101.581 102.180 1.00 89.54  ? 89   THR G CA    1 
ATOM   10078 C  C     . THR B 2 89   ? 159.779 100.366 101.954 1.00 91.18  ? 89   THR G C     1 
ATOM   10079 O  O     . THR B 2 89   ? 158.830 100.438 101.166 1.00 89.81  ? 89   THR G O     1 
ATOM   10080 C  CB    . THR B 2 89   ? 161.735 101.658 101.089 1.00 91.63  ? 89   THR G CB    1 
ATOM   10081 O  OG1   . THR B 2 89   ? 161.105 101.607 99.805  1.00 94.14  ? 89   THR G OG1   1 
ATOM   10082 C  CG2   . THR B 2 89   ? 162.709 100.507 101.212 1.00 93.63  ? 89   THR G CG2   1 
ATOM   10083 N  N     . LEU B 2 90   ? 160.069 99.247  102.619 1.00 92.54  ? 90   LEU G N     1 
ATOM   10084 C  CA    . LEU B 2 90   ? 159.174 98.097  102.550 1.00 89.84  ? 90   LEU G CA    1 
ATOM   10085 C  C     . LEU B 2 90   ? 157.938 98.302  103.416 1.00 87.63  ? 90   LEU G C     1 
ATOM   10086 O  O     . LEU B 2 90   ? 156.836 97.888  103.039 1.00 87.45  ? 90   LEU G O     1 
ATOM   10087 C  CB    . LEU B 2 90   ? 159.914 96.828  102.965 1.00 92.87  ? 90   LEU G CB    1 
ATOM   10088 C  CG    . LEU B 2 90   ? 160.862 96.237  101.923 1.00 104.44 ? 90   LEU G CG    1 
ATOM   10089 C  CD1   . LEU B 2 90   ? 161.997 95.504  102.609 1.00 105.55 ? 90   LEU G CD1   1 
ATOM   10090 C  CD2   . LEU B 2 90   ? 160.108 95.305  100.989 1.00 105.93 ? 90   LEU G CD2   1 
ATOM   10091 N  N     . ASN B 2 91   ? 158.101 98.937  104.580 1.00 88.51  ? 91   ASN G N     1 
ATOM   10092 C  CA    . ASN B 2 91   ? 156.953 99.214  105.435 1.00 84.21  ? 91   ASN G CA    1 
ATOM   10093 C  C     . ASN B 2 91   ? 156.020 100.237 104.800 1.00 81.95  ? 91   ASN G C     1 
ATOM   10094 O  O     . ASN B 2 91   ? 154.804 100.172 105.004 1.00 82.14  ? 91   ASN G O     1 
ATOM   10095 C  CB    . ASN B 2 91   ? 157.425 99.692  106.807 1.00 82.06  ? 91   ASN G CB    1 
ATOM   10096 C  CG    . ASN B 2 91   ? 156.608 99.106  107.938 1.00 82.90  ? 91   ASN G CG    1 
ATOM   10097 O  OD1   . ASN B 2 91   ? 156.142 97.970  107.858 1.00 83.90  ? 91   ASN G OD1   1 
ATOM   10098 N  ND2   . ASN B 2 91   ? 156.443 99.873  109.008 1.00 78.07  ? 91   ASN G ND2   1 
ATOM   10099 N  N     . GLU B 2 92   ? 156.567 101.177 104.029 1.00 81.54  ? 92   GLU G N     1 
ATOM   10100 C  CA    . GLU B 2 92   ? 155.732 102.085 103.247 1.00 78.29  ? 92   GLU G CA    1 
ATOM   10101 C  C     . GLU B 2 92   ? 154.819 101.312 102.304 1.00 79.47  ? 92   GLU G C     1 
ATOM   10102 O  O     . GLU B 2 92   ? 153.603 101.532 102.268 1.00 82.24  ? 92   GLU G O     1 
ATOM   10103 C  CB    . GLU B 2 92   ? 156.617 103.052 102.461 1.00 74.82  ? 92   GLU G CB    1 
ATOM   10104 C  CG    . GLU B 2 92   ? 155.860 103.942 101.493 1.00 75.24  ? 92   GLU G CG    1 
ATOM   10105 C  CD    . GLU B 2 92   ? 156.779 104.863 100.712 1.00 79.13  ? 92   GLU G CD    1 
ATOM   10106 O  OE1   . GLU B 2 92   ? 158.000 104.603 100.688 1.00 82.25  ? 92   GLU G OE1   1 
ATOM   10107 O  OE2   . GLU B 2 92   ? 156.284 105.848 100.126 1.00 79.08  ? 92   GLU G OE2   1 
ATOM   10108 N  N     . LYS B 2 93   ? 155.403 100.408 101.516 1.00 81.84  ? 93   LYS G N     1 
ATOM   10109 C  CA    . LYS B 2 93   ? 154.624 99.583  100.600 1.00 85.11  ? 93   LYS G CA    1 
ATOM   10110 C  C     . LYS B 2 93   ? 153.594 98.753  101.355 1.00 84.17  ? 93   LYS G C     1 
ATOM   10111 O  O     . LYS B 2 93   ? 152.451 98.602  100.910 1.00 84.68  ? 93   LYS G O     1 
ATOM   10112 C  CB    . LYS B 2 93   ? 155.569 98.691  99.791  1.00 90.32  ? 93   LYS G CB    1 
ATOM   10113 C  CG    . LYS B 2 93   ? 154.968 97.408  99.232  1.00 90.73  ? 93   LYS G CG    1 
ATOM   10114 C  CD    . LYS B 2 93   ? 153.875 97.675  98.213  1.00 91.91  ? 93   LYS G CD    1 
ATOM   10115 C  CE    . LYS B 2 93   ? 153.487 96.393  97.496  1.00 98.13  ? 93   LYS G CE    1 
ATOM   10116 N  NZ    . LYS B 2 93   ? 153.033 95.339  98.443  1.00 102.49 ? 93   LYS G NZ    1 
ATOM   10117 N  N     . ARG B 2 94   ? 153.990 98.193  102.499 1.00 83.64  ? 94   ARG G N     1 
ATOM   10118 C  CA    . ARG B 2 94   ? 153.077 97.346  103.260 1.00 82.97  ? 94   ARG G CA    1 
ATOM   10119 C  C     . ARG B 2 94   ? 151.886 98.137  103.790 1.00 80.03  ? 94   ARG G C     1 
ATOM   10120 O  O     . ARG B 2 94   ? 150.748 97.657  103.752 1.00 85.19  ? 94   ARG G O     1 
ATOM   10121 C  CB    . ARG B 2 94   ? 153.819 96.669  104.409 1.00 87.78  ? 94   ARG G CB    1 
ATOM   10122 C  CG    . ARG B 2 94   ? 154.755 95.556  103.974 1.00 89.78  ? 94   ARG G CG    1 
ATOM   10123 C  CD    . ARG B 2 94   ? 153.999 94.414  103.308 1.00 90.15  ? 94   ARG G CD    1 
ATOM   10124 N  NE    . ARG B 2 94   ? 152.858 93.945  104.086 1.00 97.50  ? 94   ARG G NE    1 
ATOM   10125 C  CZ    . ARG B 2 94   ? 152.917 93.442  105.313 1.00 96.53  ? 94   ARG G CZ    1 
ATOM   10126 N  NH1   . ARG B 2 94   ? 154.067 93.296  105.952 1.00 96.21  ? 94   ARG G NH1   1 
ATOM   10127 N  NH2   . ARG B 2 94   ? 151.790 93.072  105.915 1.00 95.71  ? 94   ARG G NH2   1 
ATOM   10128 N  N     . ILE B 2 95   ? 152.126 99.349  104.288 1.00 77.37  ? 95   ILE G N     1 
ATOM   10129 C  CA    . ILE B 2 95   ? 151.051 100.130 104.893 1.00 75.82  ? 95   ILE G CA    1 
ATOM   10130 C  C     . ILE B 2 95   ? 150.148 100.746 103.831 1.00 76.80  ? 95   ILE G C     1 
ATOM   10131 O  O     . ILE B 2 95   ? 148.920 100.727 103.965 1.00 75.66  ? 95   ILE G O     1 
ATOM   10132 C  CB    . ILE B 2 95   ? 151.637 101.202 105.828 1.00 72.82  ? 95   ILE G CB    1 
ATOM   10133 C  CG1   . ILE B 2 95   ? 152.261 100.550 107.063 1.00 72.01  ? 95   ILE G CG1   1 
ATOM   10134 C  CG2   . ILE B 2 95   ? 150.573 102.204 106.228 1.00 65.84  ? 95   ILE G CG2   1 
ATOM   10135 C  CD1   . ILE B 2 95   ? 153.176 101.465 107.836 1.00 66.93  ? 95   ILE G CD1   1 
ATOM   10136 N  N     . LEU B 2 96   ? 150.731 101.292 102.760 1.00 77.40  ? 96   LEU G N     1 
ATOM   10137 C  CA    . LEU B 2 96   ? 149.935 102.046 101.793 1.00 76.30  ? 96   LEU G CA    1 
ATOM   10138 C  C     . LEU B 2 96   ? 148.852 101.197 101.145 1.00 77.42  ? 96   LEU G C     1 
ATOM   10139 O  O     . LEU B 2 96   ? 147.787 101.717 100.795 1.00 75.31  ? 96   LEU G O     1 
ATOM   10140 C  CB    . LEU B 2 96   ? 150.836 102.637 100.712 1.00 80.42  ? 96   LEU G CB    1 
ATOM   10141 C  CG    . LEU B 2 96   ? 150.525 104.081 100.325 1.00 82.45  ? 96   LEU G CG    1 
ATOM   10142 C  CD1   . LEU B 2 96   ? 150.784 105.000 101.491 1.00 72.74  ? 96   LEU G CD1   1 
ATOM   10143 C  CD2   . LEU B 2 96   ? 151.345 104.496 99.121  1.00 83.59  ? 96   LEU G CD2   1 
ATOM   10144 N  N     . GLN B 2 97   ? 149.100 99.903  100.973 1.00 79.24  ? 97   GLN G N     1 
ATOM   10145 C  CA    . GLN B 2 97   ? 148.125 99.039  100.324 1.00 82.17  ? 97   GLN G CA    1 
ATOM   10146 C  C     . GLN B 2 97   ? 147.055 98.529  101.281 1.00 82.67  ? 97   GLN G C     1 
ATOM   10147 O  O     . GLN B 2 97   ? 146.091 97.901  100.831 1.00 85.40  ? 97   GLN G O     1 
ATOM   10148 C  CB    . GLN B 2 97   ? 148.842 97.869  99.648  1.00 83.16  ? 97   GLN G CB    1 
ATOM   10149 C  CG    . GLN B 2 97   ? 149.561 96.930  100.602 1.00 83.63  ? 97   GLN G CG    1 
ATOM   10150 C  CD    . GLN B 2 97   ? 148.678 95.803  101.089 1.00 89.77  ? 97   GLN G CD    1 
ATOM   10151 O  OE1   . GLN B 2 97   ? 147.930 95.209  100.313 1.00 96.79  ? 97   GLN G OE1   1 
ATOM   10152 N  NE2   . GLN B 2 97   ? 148.762 95.499  102.379 1.00 89.68  ? 97   GLN G NE2   1 
ATOM   10153 N  N     . ALA B 2 98   ? 147.201 98.776  102.582 1.00 81.17  ? 98   ALA G N     1 
ATOM   10154 C  CA    . ALA B 2 98   ? 146.247 98.300  103.576 1.00 79.27  ? 98   ALA G CA    1 
ATOM   10155 C  C     . ALA B 2 98   ? 145.288 99.378  104.066 1.00 74.83  ? 98   ALA G C     1 
ATOM   10156 O  O     . ALA B 2 98   ? 144.122 99.080  104.334 1.00 75.70  ? 98   ALA G O     1 
ATOM   10157 C  CB    . ALA B 2 98   ? 146.990 97.699  104.772 1.00 78.16  ? 98   ALA G CB    1 
ATOM   10158 N  N     . VAL B 2 99   ? 145.747 100.625 104.194 1.00 70.39  ? 99   VAL G N     1 
ATOM   10159 C  CA    . VAL B 2 99   ? 144.905 101.678 104.749 1.00 65.32  ? 99   VAL G CA    1 
ATOM   10160 C  C     . VAL B 2 99   ? 143.827 102.074 103.746 1.00 65.93  ? 99   VAL G C     1 
ATOM   10161 O  O     . VAL B 2 99   ? 143.942 101.829 102.538 1.00 71.68  ? 99   VAL G O     1 
ATOM   10162 C  CB    . VAL B 2 99   ? 145.752 102.894 105.162 1.00 63.12  ? 99   VAL G CB    1 
ATOM   10163 C  CG1   . VAL B 2 99   ? 146.699 102.523 106.289 1.00 62.08  ? 99   VAL G CG1   1 
ATOM   10164 C  CG2   . VAL B 2 99   ? 146.519 103.435 103.971 1.00 67.63  ? 99   VAL G CG2   1 
ATOM   10165 N  N     . ASN B 2 100  ? 142.758 102.686 104.255 1.00 60.21  ? 100  ASN G N     1 
ATOM   10166 C  CA    . ASN B 2 100  ? 141.629 103.095 103.421 1.00 57.19  ? 100  ASN G CA    1 
ATOM   10167 C  C     . ASN B 2 100  ? 140.930 104.263 104.104 1.00 55.09  ? 100  ASN G C     1 
ATOM   10168 O  O     . ASN B 2 100  ? 140.235 104.066 105.104 1.00 51.65  ? 100  ASN G O     1 
ATOM   10169 C  CB    . ASN B 2 100  ? 140.667 101.932 103.201 1.00 57.71  ? 100  ASN G CB    1 
ATOM   10170 C  CG    . ASN B 2 100  ? 139.598 102.244 102.175 1.00 62.19  ? 100  ASN G CG    1 
ATOM   10171 O  OD1   . ASN B 2 100  ? 139.839 102.176 100.971 1.00 64.86  ? 100  ASN G OD1   1 
ATOM   10172 N  ND2   . ASN B 2 100  ? 138.407 102.589 102.648 1.00 60.62  ? 100  ASN G ND2   1 
ATOM   10173 N  N     . PHE B 2 101  ? 141.105 105.468 103.566 1.00 55.15  ? 101  PHE G N     1 
ATOM   10174 C  CA    . PHE B 2 101  ? 140.505 106.663 104.146 1.00 49.82  ? 101  PHE G CA    1 
ATOM   10175 C  C     . PHE B 2 101  ? 140.377 107.714 103.055 1.00 52.23  ? 101  PHE G C     1 
ATOM   10176 O  O     . PHE B 2 101  ? 141.232 107.780 102.165 1.00 56.73  ? 101  PHE G O     1 
ATOM   10177 C  CB    . PHE B 2 101  ? 141.350 107.193 105.314 1.00 47.63  ? 101  PHE G CB    1 
ATOM   10178 C  CG    . PHE B 2 101  ? 140.573 108.009 106.304 1.00 47.41  ? 101  PHE G CG    1 
ATOM   10179 C  CD1   . PHE B 2 101  ? 139.565 107.430 107.054 1.00 45.79  ? 101  PHE G CD1   1 
ATOM   10180 C  CD2   . PHE B 2 101  ? 140.852 109.350 106.492 1.00 44.67  ? 101  PHE G CD2   1 
ATOM   10181 C  CE1   . PHE B 2 101  ? 138.847 108.173 107.961 1.00 45.45  ? 101  PHE G CE1   1 
ATOM   10182 C  CE2   . PHE B 2 101  ? 140.137 110.098 107.401 1.00 43.62  ? 101  PHE G CE2   1 
ATOM   10183 C  CZ    . PHE B 2 101  ? 139.133 109.509 108.136 1.00 44.91  ? 101  PHE G CZ    1 
ATOM   10184 N  N     . PRO B 2 102  ? 139.327 108.542 103.088 1.00 51.43  ? 102  PRO G N     1 
ATOM   10185 C  CA    . PRO B 2 102  ? 139.118 109.515 102.004 1.00 50.08  ? 102  PRO G CA    1 
ATOM   10186 C  C     . PRO B 2 102  ? 140.139 110.641 101.958 1.00 50.69  ? 102  PRO G C     1 
ATOM   10187 O  O     . PRO B 2 102  ? 140.128 111.410 100.989 1.00 52.82  ? 102  PRO G O     1 
ATOM   10188 C  CB    . PRO B 2 102  ? 137.712 110.058 102.290 1.00 51.05  ? 102  PRO G CB    1 
ATOM   10189 C  CG    . PRO B 2 102  ? 137.542 109.880 103.752 1.00 49.63  ? 102  PRO G CG    1 
ATOM   10190 C  CD    . PRO B 2 102  ? 138.226 108.579 104.063 1.00 53.46  ? 102  PRO G CD    1 
ATOM   10191 N  N     . PHE B 2 103  ? 141.010 110.774 102.959 1.00 48.20  ? 103  PHE G N     1 
ATOM   10192 C  CA    . PHE B 2 103  ? 142.032 111.813 102.969 1.00 45.98  ? 103  PHE G CA    1 
ATOM   10193 C  C     . PHE B 2 103  ? 143.439 111.246 102.827 1.00 43.48  ? 103  PHE G C     1 
ATOM   10194 O  O     . PHE B 2 103  ? 144.413 111.926 103.160 1.00 43.77  ? 103  PHE G O     1 
ATOM   10195 C  CB    . PHE B 2 103  ? 141.924 112.660 104.238 1.00 43.95  ? 103  PHE G CB    1 
ATOM   10196 C  CG    . PHE B 2 103  ? 140.575 113.295 104.436 1.00 43.73  ? 103  PHE G CG    1 
ATOM   10197 C  CD1   . PHE B 2 103  ? 139.888 113.837 103.366 1.00 47.12  ? 103  PHE G CD1   1 
ATOM   10198 C  CD2   . PHE B 2 103  ? 139.997 113.352 105.691 1.00 41.80  ? 103  PHE G CD2   1 
ATOM   10199 C  CE1   . PHE B 2 103  ? 138.652 114.422 103.545 1.00 50.09  ? 103  PHE G CE1   1 
ATOM   10200 C  CE2   . PHE B 2 103  ? 138.760 113.934 105.875 1.00 40.18  ? 103  PHE G CE2   1 
ATOM   10201 C  CZ    . PHE B 2 103  ? 138.087 114.469 104.801 1.00 42.85  ? 103  PHE G CZ    1 
ATOM   10202 N  N     . LEU B 2 104  ? 143.565 110.012 102.347 1.00 46.16  ? 104  LEU G N     1 
ATOM   10203 C  CA    . LEU B 2 104  ? 144.854 109.372 102.128 1.00 49.36  ? 104  LEU G CA    1 
ATOM   10204 C  C     . LEU B 2 104  ? 144.997 108.993 100.662 1.00 57.71  ? 104  LEU G C     1 
ATOM   10205 O  O     . LEU B 2 104  ? 144.032 108.555 100.028 1.00 64.64  ? 104  LEU G O     1 
ATOM   10206 C  CB    . LEU B 2 104  ? 145.015 108.126 103.004 1.00 50.13  ? 104  LEU G CB    1 
ATOM   10207 C  CG    . LEU B 2 104  ? 145.011 108.345 104.516 1.00 45.52  ? 104  LEU G CG    1 
ATOM   10208 C  CD1   . LEU B 2 104  ? 145.110 107.021 105.248 1.00 41.66  ? 104  LEU G CD1   1 
ATOM   10209 C  CD2   . LEU B 2 104  ? 146.141 109.268 104.918 1.00 44.80  ? 104  LEU G CD2   1 
ATOM   10210 N  N     . VAL B 2 105  ? 146.204 109.168 100.127 1.00 56.56  ? 105  VAL G N     1 
ATOM   10211 C  CA    . VAL B 2 105  ? 146.470 108.841 98.730  1.00 62.86  ? 105  VAL G CA    1 
ATOM   10212 C  C     . VAL B 2 105  ? 146.452 107.327 98.561  1.00 65.88  ? 105  VAL G C     1 
ATOM   10213 O  O     . VAL B 2 105  ? 147.172 106.600 99.254  1.00 66.11  ? 105  VAL G O     1 
ATOM   10214 C  CB    . VAL B 2 105  ? 147.808 109.438 98.276  1.00 61.59  ? 105  VAL G CB    1 
ATOM   10215 C  CG1   . VAL B 2 105  ? 148.229 108.837 96.952  1.00 64.94  ? 105  VAL G CG1   1 
ATOM   10216 C  CG2   . VAL B 2 105  ? 147.702 110.946 98.164  1.00 59.36  ? 105  VAL G CG2   1 
ATOM   10217 N  N     . LYS B 2 106  ? 145.624 106.846 97.637  1.00 67.17  ? 106  LYS G N     1 
ATOM   10218 C  CA    . LYS B 2 106  ? 145.449 105.419 97.418  1.00 74.64  ? 106  LYS G CA    1 
ATOM   10219 C  C     . LYS B 2 106  ? 146.523 104.860 96.487  1.00 76.88  ? 106  LYS G C     1 
ATOM   10220 O  O     . LYS B 2 106  ? 147.248 105.594 95.811  1.00 77.88  ? 106  LYS G O     1 
ATOM   10221 C  CB    . LYS B 2 106  ? 144.060 105.137 96.849  1.00 77.56  ? 106  LYS G CB    1 
ATOM   10222 C  CG    . LYS B 2 106  ? 143.540 106.232 95.945  1.00 79.10  ? 106  LYS G CG    1 
ATOM   10223 C  CD    . LYS B 2 106  ? 142.137 105.923 95.461  1.00 84.16  ? 106  LYS G CD    1 
ATOM   10224 C  CE    . LYS B 2 106  ? 141.121 106.847 96.111  1.00 87.84  ? 106  LYS G CE    1 
ATOM   10225 N  NZ    . LYS B 2 106  ? 140.035 107.234 95.168  1.00 89.00  ? 106  LYS G NZ    1 
ATOM   10226 N  N     . LEU B 2 107  ? 146.620 103.532 96.470  1.00 79.56  ? 107  LEU G N     1 
ATOM   10227 C  CA    . LEU B 2 107  ? 147.604 102.810 95.676  1.00 84.02  ? 107  LEU G CA    1 
ATOM   10228 C  C     . LEU B 2 107  ? 146.906 101.891 94.683  1.00 86.95  ? 107  LEU G C     1 
ATOM   10229 O  O     . LEU B 2 107  ? 145.921 101.229 95.023  1.00 87.26  ? 107  LEU G O     1 
ATOM   10230 C  CB    . LEU B 2 107  ? 148.534 101.993 96.571  1.00 83.31  ? 107  LEU G CB    1 
ATOM   10231 C  CG    . LEU B 2 107  ? 149.763 101.414 95.875  1.00 86.89  ? 107  LEU G CG    1 
ATOM   10232 C  CD1   . LEU B 2 107  ? 150.900 102.403 95.933  1.00 86.97  ? 107  LEU G CD1   1 
ATOM   10233 C  CD2   . LEU B 2 107  ? 150.166 100.091 96.502  1.00 87.76  ? 107  LEU G CD2   1 
ATOM   10234 N  N     . GLU B 2 108  ? 147.416 101.858 93.451  1.00 88.34  ? 108  GLU G N     1 
ATOM   10235 C  CA    . GLU B 2 108  ? 146.847 101.036 92.390  1.00 90.71  ? 108  GLU G CA    1 
ATOM   10236 C  C     . GLU B 2 108  ? 147.723 99.842  92.031  1.00 92.59  ? 108  GLU G C     1 
ATOM   10237 O  O     . GLU B 2 108  ? 147.256 98.701  92.074  1.00 93.39  ? 108  GLU G O     1 
ATOM   10238 C  CB    . GLU B 2 108  ? 146.583 101.895 91.146  1.00 94.81  ? 108  GLU G CB    1 
ATOM   10239 C  CG    . GLU B 2 108  ? 145.120 102.257 90.922  1.00 95.79  ? 108  GLU G CG    1 
ATOM   10240 C  CD    . GLU B 2 108  ? 144.558 103.204 91.969  1.00 92.75  ? 108  GLU G CD    1 
ATOM   10241 O  OE1   . GLU B 2 108  ? 143.355 103.525 91.882  1.00 90.92  ? 108  GLU G OE1   1 
ATOM   10242 O  OE2   . GLU B 2 108  ? 145.310 103.649 92.861  1.00 90.59  ? 108  GLU G OE2   1 
ATOM   10243 N  N     . PHE B 2 109  ? 148.986 100.068 91.675  1.00 95.46  ? 109  PHE G N     1 
ATOM   10244 C  CA    . PHE B 2 109  ? 149.860 98.998  91.217  1.00 102.21 ? 109  PHE G CA    1 
ATOM   10245 C  C     . PHE B 2 109  ? 151.226 99.113  91.880  1.00 102.72 ? 109  PHE G C     1 
ATOM   10246 O  O     . PHE B 2 109  ? 151.594 100.158 92.421  1.00 100.88 ? 109  PHE G O     1 
ATOM   10247 C  CB    . PHE B 2 109  ? 150.029 99.010  89.690  1.00 104.59 ? 109  PHE G CB    1 
ATOM   10248 C  CG    . PHE B 2 109  ? 148.758 99.284  88.940  1.00 102.88 ? 109  PHE G CG    1 
ATOM   10249 C  CD1   . PHE B 2 109  ? 147.836 98.277  88.718  1.00 103.59 ? 109  PHE G CD1   1 
ATOM   10250 C  CD2   . PHE B 2 109  ? 148.494 100.549 88.446  1.00 101.62 ? 109  PHE G CD2   1 
ATOM   10251 C  CE1   . PHE B 2 109  ? 146.668 98.530  88.023  1.00 100.35 ? 109  PHE G CE1   1 
ATOM   10252 C  CE2   . PHE B 2 109  ? 147.331 100.809 87.751  1.00 103.70 ? 109  PHE G CE2   1 
ATOM   10253 C  CZ    . PHE B 2 109  ? 146.416 99.799  87.538  1.00 103.67 ? 109  PHE G CZ    1 
ATOM   10254 N  N     . SER B 2 110  ? 151.973 98.011  91.835  1.00 108.53 ? 110  SER G N     1 
ATOM   10255 C  CA    . SER B 2 110  ? 153.326 97.948  92.372  1.00 111.43 ? 110  SER G CA    1 
ATOM   10256 C  C     . SER B 2 110  ? 154.229 97.252  91.364  1.00 114.89 ? 110  SER G C     1 
ATOM   10257 O  O     . SER B 2 110  ? 153.804 96.310  90.690  1.00 115.49 ? 110  SER G O     1 
ATOM   10258 C  CB    . SER B 2 110  ? 153.359 97.211  93.714  1.00 110.44 ? 110  SER G CB    1 
ATOM   10259 O  OG    . SER B 2 110  ? 152.939 98.058  94.768  1.00 104.30 ? 110  SER G OG    1 
ATOM   10260 N  N     . PHE B 2 111  ? 155.471 97.719  91.265  1.00 115.60 ? 111  PHE G N     1 
ATOM   10261 C  CA    . PHE B 2 111  ? 156.415 97.257  90.257  1.00 117.42 ? 111  PHE G CA    1 
ATOM   10262 C  C     . PHE B 2 111  ? 157.562 96.475  90.884  1.00 122.56 ? 111  PHE G C     1 
ATOM   10263 O  O     . PHE B 2 111  ? 157.830 96.568  92.084  1.00 123.44 ? 111  PHE G O     1 
ATOM   10264 C  CB    . PHE B 2 111  ? 156.995 98.428  89.451  1.00 116.57 ? 111  PHE G CB    1 
ATOM   10265 C  CG    . PHE B 2 111  ? 156.037 99.036  88.461  1.00 116.38 ? 111  PHE G CG    1 
ATOM   10266 C  CD1   . PHE B 2 111  ? 154.707 99.243  88.780  1.00 118.16 ? 111  PHE G CD1   1 
ATOM   10267 C  CD2   . PHE B 2 111  ? 156.481 99.400  87.202  1.00 115.16 ? 111  PHE G CD2   1 
ATOM   10268 C  CE1   . PHE B 2 111  ? 153.839 99.797  87.864  1.00 118.27 ? 111  PHE G CE1   1 
ATOM   10269 C  CE2   . PHE B 2 111  ? 155.618 99.958  86.284  1.00 116.00 ? 111  PHE G CE2   1 
ATOM   10270 C  CZ    . PHE B 2 111  ? 154.294 100.156 86.615  1.00 118.15 ? 111  PHE G CZ    1 
ATOM   10271 N  N     . LYS B 2 112  ? 158.238 95.689  90.038  1.00 125.20 ? 112  LYS G N     1 
ATOM   10272 C  CA    . LYS B 2 112  ? 159.424 94.940  90.459  1.00 126.63 ? 112  LYS G CA    1 
ATOM   10273 C  C     . LYS B 2 112  ? 160.265 94.626  89.221  1.00 127.65 ? 112  LYS G C     1 
ATOM   10274 O  O     . LYS B 2 112  ? 159.941 93.700  88.473  1.00 125.95 ? 112  LYS G O     1 
ATOM   10275 C  CB    . LYS B 2 112  ? 159.038 93.672  91.200  1.00 126.63 ? 112  LYS G CB    1 
ATOM   10276 C  CG    . LYS B 2 112  ? 160.231 92.892  91.732  1.00 129.49 ? 112  LYS G CG    1 
ATOM   10277 C  CD    . LYS B 2 112  ? 160.843 93.553  92.955  1.00 128.04 ? 112  LYS G CD    1 
ATOM   10278 C  CE    . LYS B 2 112  ? 162.331 93.247  93.044  1.00 127.66 ? 112  LYS G CE    1 
ATOM   10279 N  NZ    . LYS B 2 112  ? 162.950 93.789  94.283  1.00 124.79 ? 112  LYS G NZ    1 
ATOM   10280 N  N     . ASP B 2 113  ? 161.332 95.392  89.020  1.00 128.55 ? 113  ASP G N     1 
ATOM   10281 C  CA    . ASP B 2 113  ? 162.310 95.099  87.981  1.00 126.99 ? 113  ASP G CA    1 
ATOM   10282 C  C     . ASP B 2 113  ? 163.694 94.929  88.615  1.00 126.91 ? 113  ASP G C     1 
ATOM   10283 O  O     . ASP B 2 113  ? 163.850 94.947  89.839  1.00 126.18 ? 113  ASP G O     1 
ATOM   10284 C  CB    . ASP B 2 113  ? 162.294 96.179  86.895  1.00 123.40 ? 113  ASP G CB    1 
ATOM   10285 C  CG    . ASP B 2 113  ? 162.998 97.454  87.316  1.00 125.32 ? 113  ASP G CG    1 
ATOM   10286 O  OD1   . ASP B 2 113  ? 163.066 97.734  88.528  1.00 127.03 ? 113  ASP G OD1   1 
ATOM   10287 O  OD2   . ASP B 2 113  ? 163.491 98.178  86.428  1.00 123.41 ? 113  ASP G OD2   1 
ATOM   10288 N  N     . ASN B 2 114  ? 164.705 94.769  87.763  1.00 125.68 ? 114  ASN G N     1 
ATOM   10289 C  CA    . ASN B 2 114  ? 166.065 94.502  88.210  1.00 126.40 ? 114  ASN G CA    1 
ATOM   10290 C  C     . ASN B 2 114  ? 166.826 95.752  88.634  1.00 125.35 ? 114  ASN G C     1 
ATOM   10291 O  O     . ASN B 2 114  ? 167.877 95.628  89.271  1.00 125.72 ? 114  ASN G O     1 
ATOM   10292 C  CB    . ASN B 2 114  ? 166.855 93.794  87.103  1.00 124.40 ? 114  ASN G CB    1 
ATOM   10293 C  CG    . ASN B 2 114  ? 167.762 92.704  87.639  1.00 121.15 ? 114  ASN G CG    1 
ATOM   10294 O  OD1   . ASN B 2 114  ? 168.121 92.700  88.817  1.00 121.13 ? 114  ASN G OD1   1 
ATOM   10295 N  ND2   . ASN B 2 114  ? 168.147 91.777  86.770  1.00 114.22 ? 114  ASN G ND2   1 
ATOM   10296 N  N     . SER B 2 115  ? 166.335 96.944  88.304  1.00 124.83 ? 115  SER G N     1 
ATOM   10297 C  CA    . SER B 2 115  ? 167.064 98.178  88.572  1.00 124.13 ? 115  SER G CA    1 
ATOM   10298 C  C     . SER B 2 115  ? 166.453 99.011  89.688  1.00 123.18 ? 115  SER G C     1 
ATOM   10299 O  O     . SER B 2 115  ? 167.159 99.402  90.623  1.00 119.98 ? 115  SER G O     1 
ATOM   10300 C  CB    . SER B 2 115  ? 167.159 99.018  87.291  1.00 121.63 ? 115  SER G CB    1 
ATOM   10301 O  OG    . SER B 2 115  ? 167.960 100.167 87.497  1.00 120.20 ? 115  SER G OG    1 
ATOM   10302 N  N     . ASN B 2 116  ? 165.151 99.290  89.626  1.00 122.47 ? 116  ASN G N     1 
ATOM   10303 C  CA    . ASN B 2 116  ? 164.538 100.210 90.575  1.00 121.08 ? 116  ASN G CA    1 
ATOM   10304 C  C     . ASN B 2 116  ? 163.277 99.636  91.208  1.00 120.58 ? 116  ASN G C     1 
ATOM   10305 O  O     . ASN B 2 116  ? 162.970 98.451  91.050  1.00 121.02 ? 116  ASN G O     1 
ATOM   10306 C  CB    . ASN B 2 116  ? 164.209 101.537 89.888  1.00 119.90 ? 116  ASN G CB    1 
ATOM   10307 C  CG    . ASN B 2 116  ? 165.443 102.261 89.396  1.00 119.05 ? 116  ASN G CG    1 
ATOM   10308 O  OD1   . ASN B 2 116  ? 165.866 102.089 88.253  1.00 116.60 ? 116  ASN G OD1   1 
ATOM   10309 N  ND2   . ASN B 2 116  ? 166.029 103.081 90.258  1.00 118.30 ? 116  ASN G ND2   1 
ATOM   10310 N  N     . LEU B 2 117  ? 162.558 100.470 91.955  1.00 117.68 ? 117  LEU G N     1 
ATOM   10311 C  CA    . LEU B 2 117  ? 161.254 100.122 92.497  1.00 117.38 ? 117  LEU G CA    1 
ATOM   10312 C  C     . LEU B 2 117  ? 160.276 101.234 92.154  1.00 117.94 ? 117  LEU G C     1 
ATOM   10313 O  O     . LEU B 2 117  ? 160.601 102.418 92.291  1.00 116.80 ? 117  LEU G O     1 
ATOM   10314 C  CB    . LEU B 2 117  ? 161.312 99.919  94.013  1.00 115.29 ? 117  LEU G CB    1 
ATOM   10315 C  CG    . LEU B 2 117  ? 162.026 98.658  94.498  1.00 118.85 ? 117  LEU G CG    1 
ATOM   10316 C  CD1   . LEU B 2 117  ? 162.236 98.715  95.999  1.00 116.68 ? 117  LEU G CD1   1 
ATOM   10317 C  CD2   . LEU B 2 117  ? 161.243 97.416  94.109  1.00 121.43 ? 117  LEU G CD2   1 
ATOM   10318 N  N     . TYR B 2 118  ? 159.081 100.855 91.711  1.00 116.00 ? 118  TYR G N     1 
ATOM   10319 C  CA    . TYR B 2 118  ? 158.074 101.822 91.306  1.00 111.09 ? 118  TYR G CA    1 
ATOM   10320 C  C     . TYR B 2 118  ? 156.731 101.490 91.937  1.00 109.30 ? 118  TYR G C     1 
ATOM   10321 O  O     . TYR B 2 118  ? 156.406 100.325 92.182  1.00 110.70 ? 118  TYR G O     1 
ATOM   10322 C  CB    . TYR B 2 118  ? 157.917 101.893 89.778  1.00 111.17 ? 118  TYR G CB    1 
ATOM   10323 C  CG    . TYR B 2 118  ? 159.192 101.686 88.988  1.00 114.02 ? 118  TYR G CG    1 
ATOM   10324 C  CD1   . TYR B 2 118  ? 159.653 100.413 88.686  1.00 115.63 ? 118  TYR G CD1   1 
ATOM   10325 C  CD2   . TYR B 2 118  ? 159.928 102.771 88.538  1.00 113.33 ? 118  TYR G CD2   1 
ATOM   10326 C  CE1   . TYR B 2 118  ? 160.813 100.227 87.960  1.00 116.63 ? 118  TYR G CE1   1 
ATOM   10327 C  CE2   . TYR B 2 118  ? 161.089 102.596 87.814  1.00 116.72 ? 118  TYR G CE2   1 
ATOM   10328 C  CZ    . TYR B 2 118  ? 161.528 101.322 87.527  1.00 117.92 ? 118  TYR G CZ    1 
ATOM   10329 O  OH    . TYR B 2 118  ? 162.684 101.140 86.806  1.00 114.46 ? 118  TYR G OH    1 
ATOM   10330 N  N     . MET B 2 119  ? 155.956 102.541 92.196  1.00 106.38 ? 119  MET G N     1 
ATOM   10331 C  CA    . MET B 2 119  ? 154.609 102.451 92.738  1.00 99.78  ? 119  MET G CA    1 
ATOM   10332 C  C     . MET B 2 119  ? 153.705 103.370 91.930  1.00 94.57  ? 119  MET G C     1 
ATOM   10333 O  O     . MET B 2 119  ? 154.164 104.355 91.349  1.00 96.20  ? 119  MET G O     1 
ATOM   10334 C  CB    . MET B 2 119  ? 154.577 102.845 94.223  1.00 98.71  ? 119  MET G CB    1 
ATOM   10335 C  CG    . MET B 2 119  ? 155.770 102.334 95.021  1.00 102.09 ? 119  MET G CG    1 
ATOM   10336 S  SD    . MET B 2 119  ? 155.453 102.078 96.775  1.00 109.12 ? 119  MET G SD    1 
ATOM   10337 C  CE    . MET B 2 119  ? 154.149 103.267 97.061  1.00 97.33  ? 119  MET G CE    1 
ATOM   10338 N  N     . VAL B 2 120  ? 152.416 103.046 91.891  1.00 92.96  ? 120  VAL G N     1 
ATOM   10339 C  CA    . VAL B 2 120  ? 151.446 103.793 91.096  1.00 91.75  ? 120  VAL G CA    1 
ATOM   10340 C  C     . VAL B 2 120  ? 150.382 104.343 92.035  1.00 90.08  ? 120  VAL G C     1 
ATOM   10341 O  O     . VAL B 2 120  ? 149.613 103.578 92.631  1.00 92.55  ? 120  VAL G O     1 
ATOM   10342 C  CB    . VAL B 2 120  ? 150.816 102.931 89.995  1.00 94.63  ? 120  VAL G CB    1 
ATOM   10343 C  CG1   . VAL B 2 120  ? 149.836 103.755 89.180  1.00 93.87  ? 120  VAL G CG1   1 
ATOM   10344 C  CG2   . VAL B 2 120  ? 151.892 102.355 89.102  1.00 96.10  ? 120  VAL G CG2   1 
ATOM   10345 N  N     . MET B 2 121  ? 150.331 105.664 92.158  1.00 85.87  ? 121  MET G N     1 
ATOM   10346 C  CA    . MET B 2 121  ? 149.353 106.353 92.985  1.00 80.82  ? 121  MET G CA    1 
ATOM   10347 C  C     . MET B 2 121  ? 148.263 106.964 92.110  1.00 79.98  ? 121  MET G C     1 
ATOM   10348 O  O     . MET B 2 121  ? 148.305 106.895 90.880  1.00 87.57  ? 121  MET G O     1 
ATOM   10349 C  CB    . MET B 2 121  ? 150.035 107.441 93.818  1.00 76.74  ? 121  MET G CB    1 
ATOM   10350 C  CG    . MET B 2 121  ? 151.356 107.015 94.432  1.00 80.42  ? 121  MET G CG    1 
ATOM   10351 S  SD    . MET B 2 121  ? 151.902 108.133 95.733  1.00 83.14  ? 121  MET G SD    1 
ATOM   10352 C  CE    . MET B 2 121  ? 152.652 106.982 96.878  1.00 77.02  ? 121  MET G CE    1 
ATOM   10353 N  N     . GLU B 2 122  ? 147.266 107.553 92.762  1.00 73.85  ? 122  GLU G N     1 
ATOM   10354 C  CA    . GLU B 2 122  ? 146.320 108.390 92.041  1.00 73.06  ? 122  GLU G CA    1 
ATOM   10355 C  C     . GLU B 2 122  ? 146.906 109.783 91.839  1.00 75.23  ? 122  GLU G C     1 
ATOM   10356 O  O     . GLU B 2 122  ? 147.731 110.255 92.624  1.00 77.32  ? 122  GLU G O     1 
ATOM   10357 C  CB    . GLU B 2 122  ? 144.989 108.487 92.784  1.00 72.83  ? 122  GLU G CB    1 
ATOM   10358 C  CG    . GLU B 2 122  ? 145.018 109.364 94.021  1.00 78.89  ? 122  GLU G CG    1 
ATOM   10359 C  CD    . GLU B 2 122  ? 143.639 109.575 94.609  1.00 87.33  ? 122  GLU G CD    1 
ATOM   10360 O  OE1   . GLU B 2 122  ? 142.647 109.233 93.930  1.00 89.73  ? 122  GLU G OE1   1 
ATOM   10361 O  OE2   . GLU B 2 122  ? 143.545 110.082 95.746  1.00 83.74  ? 122  GLU G OE2   1 
ATOM   10362 N  N     . TYR B 2 123  ? 146.478 110.441 90.767  1.00 74.76  ? 123  TYR G N     1 
ATOM   10363 C  CA    . TYR B 2 123  ? 146.990 111.766 90.446  1.00 72.07  ? 123  TYR G CA    1 
ATOM   10364 C  C     . TYR B 2 123  ? 146.202 112.827 91.205  1.00 71.59  ? 123  TYR G C     1 
ATOM   10365 O  O     . TYR B 2 123  ? 144.969 112.851 91.154  1.00 72.78  ? 123  TYR G O     1 
ATOM   10366 C  CB    . TYR B 2 123  ? 146.908 112.016 88.941  1.00 76.14  ? 123  TYR G CB    1 
ATOM   10367 C  CG    . TYR B 2 123  ? 147.447 113.359 88.510  1.00 73.62  ? 123  TYR G CG    1 
ATOM   10368 C  CD1   . TYR B 2 123  ? 148.714 113.771 88.892  1.00 74.09  ? 123  TYR G CD1   1 
ATOM   10369 C  CD2   . TYR B 2 123  ? 146.693 114.212 87.719  1.00 74.22  ? 123  TYR G CD2   1 
ATOM   10370 C  CE1   . TYR B 2 123  ? 149.215 114.994 88.500  1.00 74.67  ? 123  TYR G CE1   1 
ATOM   10371 C  CE2   . TYR B 2 123  ? 147.187 115.438 87.323  1.00 73.96  ? 123  TYR G CE2   1 
ATOM   10372 C  CZ    . TYR B 2 123  ? 148.448 115.824 87.718  1.00 76.50  ? 123  TYR G CZ    1 
ATOM   10373 O  OH    . TYR B 2 123  ? 148.947 117.044 87.329  1.00 80.97  ? 123  TYR G OH    1 
ATOM   10374 N  N     . VAL B 2 124  ? 146.914 113.696 91.915  1.00 70.10  ? 124  VAL G N     1 
ATOM   10375 C  CA    . VAL B 2 124  ? 146.288 114.786 92.661  1.00 68.16  ? 124  VAL G CA    1 
ATOM   10376 C  C     . VAL B 2 124  ? 146.703 116.095 92.000  1.00 68.11  ? 124  VAL G C     1 
ATOM   10377 O  O     . VAL B 2 124  ? 147.825 116.574 92.221  1.00 68.58  ? 124  VAL G O     1 
ATOM   10378 C  CB    . VAL B 2 124  ? 146.679 114.746 94.146  1.00 61.55  ? 124  VAL G CB    1 
ATOM   10379 C  CG1   . VAL B 2 124  ? 145.997 115.863 94.903  1.00 56.37  ? 124  VAL G CG1   1 
ATOM   10380 C  CG2   . VAL B 2 124  ? 146.322 113.402 94.749  1.00 61.69  ? 124  VAL G CG2   1 
ATOM   10381 N  N     . PRO B 2 125  ? 145.833 116.713 91.195  1.00 67.61  ? 125  PRO G N     1 
ATOM   10382 C  CA    . PRO B 2 125  ? 146.280 117.786 90.296  1.00 68.85  ? 125  PRO G CA    1 
ATOM   10383 C  C     . PRO B 2 125  ? 146.499 119.143 90.949  1.00 67.95  ? 125  PRO G C     1 
ATOM   10384 O  O     . PRO B 2 125  ? 147.121 120.008 90.319  1.00 71.59  ? 125  PRO G O     1 
ATOM   10385 C  CB    . PRO B 2 125  ? 145.143 117.859 89.269  1.00 71.13  ? 125  PRO G CB    1 
ATOM   10386 C  CG    . PRO B 2 125  ? 143.939 117.460 90.053  1.00 68.94  ? 125  PRO G CG    1 
ATOM   10387 C  CD    . PRO B 2 125  ? 144.417 116.372 90.983  1.00 64.84  ? 125  PRO G CD    1 
ATOM   10388 N  N     . GLY B 2 126  ? 146.026 119.368 92.169  1.00 62.24  ? 126  GLY G N     1 
ATOM   10389 C  CA    . GLY B 2 126  ? 146.072 120.709 92.716  1.00 60.89  ? 126  GLY G CA    1 
ATOM   10390 C  C     . GLY B 2 126  ? 147.399 121.174 93.269  1.00 61.55  ? 126  GLY G C     1 
ATOM   10391 O  O     . GLY B 2 126  ? 147.519 122.341 93.650  1.00 61.25  ? 126  GLY G O     1 
ATOM   10392 N  N     . GLY B 2 127  ? 148.404 120.308 93.332  1.00 60.62  ? 127  GLY G N     1 
ATOM   10393 C  CA    . GLY B 2 127  ? 149.705 120.709 93.823  1.00 57.64  ? 127  GLY G CA    1 
ATOM   10394 C  C     . GLY B 2 127  ? 149.783 120.746 95.337  1.00 54.50  ? 127  GLY G C     1 
ATOM   10395 O  O     . GLY B 2 127  ? 148.830 120.458 96.060  1.00 56.76  ? 127  GLY G O     1 
ATOM   10396 N  N     . GLU B 2 128  ? 150.964 121.120 95.819  1.00 56.51  ? 128  GLU G N     1 
ATOM   10397 C  CA    . GLU B 2 128  ? 151.249 121.097 97.246  1.00 53.48  ? 128  GLU G CA    1 
ATOM   10398 C  C     . GLU B 2 128  ? 150.545 122.231 97.981  1.00 51.67  ? 128  GLU G C     1 
ATOM   10399 O  O     . GLU B 2 128  ? 150.180 123.254 97.396  1.00 52.33  ? 128  GLU G O     1 
ATOM   10400 C  CB    . GLU B 2 128  ? 152.752 121.199 97.488  1.00 53.70  ? 128  GLU G CB    1 
ATOM   10401 C  CG    . GLU B 2 128  ? 153.575 120.113 96.839  1.00 57.87  ? 128  GLU G CG    1 
ATOM   10402 C  CD    . GLU B 2 128  ? 155.057 120.366 96.994  1.00 68.16  ? 128  GLU G CD    1 
ATOM   10403 O  OE1   . GLU B 2 128  ? 155.416 121.373 97.639  1.00 67.35  ? 128  GLU G OE1   1 
ATOM   10404 O  OE2   . GLU B 2 128  ? 155.862 119.567 96.473  1.00 71.66  ? 128  GLU G OE2   1 
ATOM   10405 N  N     . MET B 2 129  ? 150.348 122.026 99.284  1.00 50.56  ? 129  MET G N     1 
ATOM   10406 C  CA    . MET B 2 129  ? 149.912 123.105 100.164 1.00 50.22  ? 129  MET G CA    1 
ATOM   10407 C  C     . MET B 2 129  ? 151.031 124.115 100.396 1.00 49.40  ? 129  MET G C     1 
ATOM   10408 O  O     . MET B 2 129  ? 150.766 125.297 100.642 1.00 52.87  ? 129  MET G O     1 
ATOM   10409 C  CB    . MET B 2 129  ? 149.423 122.523 101.489 1.00 49.31  ? 129  MET G CB    1 
ATOM   10410 C  CG    . MET B 2 129  ? 148.576 123.458 102.325 1.00 49.55  ? 129  MET G CG    1 
ATOM   10411 S  SD    . MET B 2 129  ? 148.704 123.069 104.079 1.00 56.01  ? 129  MET G SD    1 
ATOM   10412 C  CE    . MET B 2 129  ? 149.766 124.394 104.641 1.00 48.54  ? 129  MET G CE    1 
ATOM   10413 N  N     . PHE B 2 130  ? 152.283 123.657 100.351 1.00 48.89  ? 130  PHE G N     1 
ATOM   10414 C  CA    . PHE B 2 130  ? 153.432 124.531 100.574 1.00 52.35  ? 130  PHE G CA    1 
ATOM   10415 C  C     . PHE B 2 130  ? 153.477 125.679 99.572  1.00 56.07  ? 130  PHE G C     1 
ATOM   10416 O  O     . PHE B 2 130  ? 153.688 126.842 99.943  1.00 54.98  ? 130  PHE G O     1 
ATOM   10417 C  CB    . PHE B 2 130  ? 154.717 123.706 100.494 1.00 57.12  ? 130  PHE G CB    1 
ATOM   10418 C  CG    . PHE B 2 130  ? 155.971 124.529 100.488 1.00 64.64  ? 130  PHE G CG    1 
ATOM   10419 C  CD1   . PHE B 2 130  ? 156.442 125.103 101.653 1.00 65.17  ? 130  PHE G CD1   1 
ATOM   10420 C  CD2   . PHE B 2 130  ? 156.691 124.709 99.318  1.00 64.75  ? 130  PHE G CD2   1 
ATOM   10421 C  CE1   . PHE B 2 130  ? 157.599 125.854 101.653 1.00 67.76  ? 130  PHE G CE1   1 
ATOM   10422 C  CE2   . PHE B 2 130  ? 157.852 125.461 99.311  1.00 65.24  ? 130  PHE G CE2   1 
ATOM   10423 C  CZ    . PHE B 2 130  ? 158.306 126.034 100.481 1.00 67.29  ? 130  PHE G CZ    1 
ATOM   10424 N  N     . SER B 2 131  ? 153.303 125.362 98.287  1.00 57.07  ? 131  SER G N     1 
ATOM   10425 C  CA    . SER B 2 131  ? 153.396 126.386 97.257  1.00 53.12  ? 131  SER G CA    1 
ATOM   10426 C  C     . SER B 2 131  ? 152.312 127.438 97.417  1.00 53.63  ? 131  SER G C     1 
ATOM   10427 O  O     . SER B 2 131  ? 152.591 128.635 97.300  1.00 55.82  ? 131  SER G O     1 
ATOM   10428 C  CB    . SER B 2 131  ? 153.311 125.740 95.875  1.00 54.37  ? 131  SER G CB    1 
ATOM   10429 O  OG    . SER B 2 131  ? 154.534 125.111 95.540  1.00 65.60  ? 131  SER G OG    1 
ATOM   10430 N  N     . HIS B 2 132  ? 151.090 127.021 97.740  1.00 53.27  ? 132  HIS G N     1 
ATOM   10431 C  CA    . HIS B 2 132  ? 150.011 127.980 97.927  1.00 47.81  ? 132  HIS G CA    1 
ATOM   10432 C  C     . HIS B 2 132  ? 150.194 128.792 99.200  1.00 45.03  ? 132  HIS G C     1 
ATOM   10433 O  O     . HIS B 2 132  ? 149.855 129.978 99.225  1.00 49.26  ? 132  HIS G O     1 
ATOM   10434 C  CB    . HIS B 2 132  ? 148.669 127.251 97.950  1.00 49.04  ? 132  HIS G CB    1 
ATOM   10435 C  CG    . HIS B 2 132  ? 148.346 126.555 96.666  1.00 61.15  ? 132  HIS G CG    1 
ATOM   10436 N  ND1   . HIS B 2 132  ? 148.756 125.268 96.397  1.00 59.44  ? 132  HIS G ND1   1 
ATOM   10437 C  CD2   . HIS B 2 132  ? 147.676 126.975 95.568  1.00 66.56  ? 132  HIS G CD2   1 
ATOM   10438 C  CE1   . HIS B 2 132  ? 148.337 124.919 95.193  1.00 58.93  ? 132  HIS G CE1   1 
ATOM   10439 N  NE2   . HIS B 2 132  ? 147.679 125.937 94.669  1.00 63.46  ? 132  HIS G NE2   1 
ATOM   10440 N  N     . LEU B 2 133  ? 150.729 128.181 100.258 1.00 43.08  ? 133  LEU G N     1 
ATOM   10441 C  CA    . LEU B 2 133  ? 150.994 128.929 101.480 1.00 40.84  ? 133  LEU G CA    1 
ATOM   10442 C  C     . LEU B 2 133  ? 152.046 130.005 101.250 1.00 46.30  ? 133  LEU G C     1 
ATOM   10443 O  O     . LEU B 2 133  ? 151.906 131.132 101.740 1.00 46.11  ? 133  LEU G O     1 
ATOM   10444 C  CB    . LEU B 2 133  ? 151.433 127.981 102.595 1.00 44.32  ? 133  LEU G CB    1 
ATOM   10445 C  CG    . LEU B 2 133  ? 151.760 128.620 103.947 1.00 38.93  ? 133  LEU G CG    1 
ATOM   10446 C  CD1   . LEU B 2 133  ? 150.600 129.455 104.445 1.00 35.13  ? 133  LEU G CD1   1 
ATOM   10447 C  CD2   . LEU B 2 133  ? 152.129 127.564 104.969 1.00 36.61  ? 133  LEU G CD2   1 
ATOM   10448 N  N     . ARG B 2 134  ? 153.108 129.678 100.511 1.00 50.54  ? 134  ARG G N     1 
ATOM   10449 C  CA    . ARG B 2 134  ? 154.122 130.686 100.218 1.00 49.03  ? 134  ARG G CA    1 
ATOM   10450 C  C     . ARG B 2 134  ? 153.622 131.716 99.214  1.00 48.56  ? 134  ARG G C     1 
ATOM   10451 O  O     . ARG B 2 134  ? 154.082 132.862 99.226  1.00 49.63  ? 134  ARG G O     1 
ATOM   10452 C  CB    . ARG B 2 134  ? 155.404 130.025 99.710  1.00 51.52  ? 134  ARG G CB    1 
ATOM   10453 C  CG    . ARG B 2 134  ? 156.064 129.096 100.714 1.00 59.30  ? 134  ARG G CG    1 
ATOM   10454 C  CD    . ARG B 2 134  ? 155.981 129.673 102.123 1.00 61.03  ? 134  ARG G CD    1 
ATOM   10455 N  NE    . ARG B 2 134  ? 156.038 128.643 103.152 1.00 66.54  ? 134  ARG G NE    1 
ATOM   10456 C  CZ    . ARG B 2 134  ? 156.840 128.680 104.207 1.00 70.04  ? 134  ARG G CZ    1 
ATOM   10457 N  NH1   . ARG B 2 134  ? 157.667 129.693 104.411 1.00 74.89  ? 134  ARG G NH1   1 
ATOM   10458 N  NH2   . ARG B 2 134  ? 156.804 127.682 105.085 1.00 59.59  ? 134  ARG G NH2   1 
ATOM   10459 N  N     . ARG B 2 135  ? 152.683 131.331 98.350  1.00 49.52  ? 135  ARG G N     1 
ATOM   10460 C  CA    . ARG B 2 135  ? 152.153 132.257 97.357  1.00 46.56  ? 135  ARG G CA    1 
ATOM   10461 C  C     . ARG B 2 135  ? 151.218 133.278 97.997  1.00 46.66  ? 135  ARG G C     1 
ATOM   10462 O  O     . ARG B 2 135  ? 151.261 134.467 97.667  1.00 50.24  ? 135  ARG G O     1 
ATOM   10463 C  CB    . ARG B 2 135  ? 151.435 131.462 96.268  1.00 50.58  ? 135  ARG G CB    1 
ATOM   10464 C  CG    . ARG B 2 135  ? 150.304 132.177 95.575  1.00 54.71  ? 135  ARG G CG    1 
ATOM   10465 C  CD    . ARG B 2 135  ? 149.744 131.287 94.484  1.00 58.30  ? 135  ARG G CD    1 
ATOM   10466 N  NE    . ARG B 2 135  ? 150.790 130.480 93.868  1.00 64.91  ? 135  ARG G NE    1 
ATOM   10467 C  CZ    . ARG B 2 135  ? 150.593 129.281 93.337  1.00 68.22  ? 135  ARG G CZ    1 
ATOM   10468 N  NH1   . ARG B 2 135  ? 149.396 128.720 93.326  1.00 66.78  ? 135  ARG G NH1   1 
ATOM   10469 N  NH2   . ARG B 2 135  ? 151.626 128.624 92.818  1.00 64.91  ? 135  ARG G NH2   1 
ATOM   10470 N  N     . ILE B 2 136  ? 150.363 132.828 98.917  1.00 43.35  ? 136  ILE G N     1 
ATOM   10471 C  CA    . ILE B 2 136  ? 149.384 133.716 99.535  1.00 40.39  ? 136  ILE G CA    1 
ATOM   10472 C  C     . ILE B 2 136  ? 149.976 134.435 100.748 1.00 42.31  ? 136  ILE G C     1 
ATOM   10473 O  O     . ILE B 2 136  ? 149.510 135.516 101.124 1.00 43.74  ? 136  ILE G O     1 
ATOM   10474 C  CB    . ILE B 2 136  ? 148.123 132.910 99.895  1.00 43.45  ? 136  ILE G CB    1 
ATOM   10475 C  CG1   . ILE B 2 136  ? 147.433 132.418 98.624  1.00 46.98  ? 136  ILE G CG1   1 
ATOM   10476 C  CG2   . ILE B 2 136  ? 147.140 133.735 100.699 1.00 39.03  ? 136  ILE G CG2   1 
ATOM   10477 C  CD1   . ILE B 2 136  ? 146.319 131.431 98.880  1.00 48.51  ? 136  ILE G CD1   1 
ATOM   10478 N  N     . GLY B 2 137  ? 151.034 133.889 101.341 1.00 42.53  ? 137  GLY G N     1 
ATOM   10479 C  CA    . GLY B 2 137  ? 151.614 134.453 102.545 1.00 41.31  ? 137  GLY G CA    1 
ATOM   10480 C  C     . GLY B 2 137  ? 151.134 133.825 103.838 1.00 39.84  ? 137  GLY G C     1 
ATOM   10481 O  O     . GLY B 2 137  ? 151.956 133.365 104.635 1.00 41.59  ? 137  GLY G O     1 
ATOM   10482 N  N     . ARG B 2 138  ? 149.822 133.797 104.068 1.00 34.08  ? 138  ARG G N     1 
ATOM   10483 C  CA    . ARG B 2 138  ? 149.279 133.136 105.247 1.00 31.42  ? 138  ARG G CA    1 
ATOM   10484 C  C     . ARG B 2 138  ? 147.782 132.938 105.068 1.00 36.23  ? 138  ARG G C     1 
ATOM   10485 O  O     . ARG B 2 138  ? 147.121 133.708 104.368 1.00 44.45  ? 138  ARG G O     1 
ATOM   10486 C  CB    . ARG B 2 138  ? 149.571 133.930 106.525 1.00 28.64  ? 138  ARG G CB    1 
ATOM   10487 C  CG    . ARG B 2 138  ? 148.792 135.216 106.673 1.00 30.90  ? 138  ARG G CG    1 
ATOM   10488 C  CD    . ARG B 2 138  ? 149.403 136.083 107.758 1.00 32.27  ? 138  ARG G CD    1 
ATOM   10489 N  NE    . ARG B 2 138  ? 148.579 137.244 108.069 1.00 30.38  ? 138  ARG G NE    1 
ATOM   10490 C  CZ    . ARG B 2 138  ? 149.054 138.397 108.516 1.00 31.93  ? 138  ARG G CZ    1 
ATOM   10491 N  NH1   . ARG B 2 138  ? 150.349 138.582 108.708 1.00 28.73  ? 138  ARG G NH1   1 
ATOM   10492 N  NH2   . ARG B 2 138  ? 148.210 139.390 108.776 1.00 32.92  ? 138  ARG G NH2   1 
ATOM   10493 N  N     . PHE B 2 139  ? 147.262 131.890 105.701 1.00 33.57  ? 139  PHE G N     1 
ATOM   10494 C  CA    . PHE B 2 139  ? 145.841 131.578 105.655 1.00 34.12  ? 139  PHE G CA    1 
ATOM   10495 C  C     . PHE B 2 139  ? 145.100 132.237 106.810 1.00 37.22  ? 139  PHE G C     1 
ATOM   10496 O  O     . PHE B 2 139  ? 145.647 132.429 107.898 1.00 39.38  ? 139  PHE G O     1 
ATOM   10497 C  CB    . PHE B 2 139  ? 145.604 130.069 105.709 1.00 33.13  ? 139  PHE G CB    1 
ATOM   10498 C  CG    . PHE B 2 139  ? 146.272 129.305 104.610 1.00 35.88  ? 139  PHE G CG    1 
ATOM   10499 C  CD1   . PHE B 2 139  ? 146.361 129.834 103.338 1.00 36.36  ? 139  PHE G CD1   1 
ATOM   10500 C  CD2   . PHE B 2 139  ? 146.795 128.048 104.845 1.00 35.30  ? 139  PHE G CD2   1 
ATOM   10501 C  CE1   . PHE B 2 139  ? 146.969 129.129 102.322 1.00 38.64  ? 139  PHE G CE1   1 
ATOM   10502 C  CE2   . PHE B 2 139  ? 147.405 127.338 103.834 1.00 35.72  ? 139  PHE G CE2   1 
ATOM   10503 C  CZ    . PHE B 2 139  ? 147.492 127.879 102.571 1.00 38.13  ? 139  PHE G CZ    1 
ATOM   10504 N  N     . SER B 2 140  ? 143.844 132.591 106.558 1.00 36.36  ? 140  SER G N     1 
ATOM   10505 C  CA    . SER B 2 140  ? 142.968 133.048 107.624 1.00 37.70  ? 140  SER G CA    1 
ATOM   10506 C  C     . SER B 2 140  ? 142.542 131.871 108.497 1.00 37.39  ? 140  SER G C     1 
ATOM   10507 O  O     . SER B 2 140  ? 142.649 130.704 108.111 1.00 41.14  ? 140  SER G O     1 
ATOM   10508 C  CB    . SER B 2 140  ? 141.745 133.759 107.048 1.00 40.22  ? 140  SER G CB    1 
ATOM   10509 O  OG    . SER B 2 140  ? 140.915 132.854 106.345 1.00 39.62  ? 140  SER G OG    1 
ATOM   10510 N  N     . GLU B 2 141  ? 142.063 132.192 109.698 1.00 33.04  ? 141  GLU G N     1 
ATOM   10511 C  CA    . GLU B 2 141  ? 141.722 131.143 110.654 1.00 31.73  ? 141  GLU G CA    1 
ATOM   10512 C  C     . GLU B 2 141  ? 140.632 130.188 110.178 1.00 34.26  ? 141  GLU G C     1 
ATOM   10513 O  O     . GLU B 2 141  ? 140.769 128.981 110.436 1.00 36.29  ? 141  GLU G O     1 
ATOM   10514 C  CB    . GLU B 2 141  ? 141.359 131.767 112.006 1.00 28.74  ? 141  GLU G CB    1 
ATOM   10515 C  CG    . GLU B 2 141  ? 142.504 132.542 112.626 1.00 31.18  ? 141  GLU G CG    1 
ATOM   10516 C  CD    . GLU B 2 141  ? 142.240 132.921 114.066 1.00 37.69  ? 141  GLU G CD    1 
ATOM   10517 O  OE1   . GLU B 2 141  ? 141.264 132.404 114.646 1.00 42.92  ? 141  GLU G OE1   1 
ATOM   10518 O  OE2   . GLU B 2 141  ? 143.011 133.730 114.621 1.00 32.08  ? 141  GLU G OE2   1 
ATOM   10519 N  N     . PRO B 2 142  ? 139.540 130.620 109.534 1.00 34.17  ? 142  PRO G N     1 
ATOM   10520 C  CA    . PRO B 2 142  ? 138.615 129.620 108.970 1.00 35.23  ? 142  PRO G CA    1 
ATOM   10521 C  C     . PRO B 2 142  ? 139.262 128.739 107.914 1.00 35.09  ? 142  PRO G C     1 
ATOM   10522 O  O     . PRO B 2 142  ? 139.016 127.523 107.871 1.00 39.59  ? 142  PRO G O     1 
ATOM   10523 C  CB    . PRO B 2 142  ? 137.484 130.481 108.389 1.00 35.10  ? 142  PRO G CB    1 
ATOM   10524 C  CG    . PRO B 2 142  ? 137.575 131.769 109.122 1.00 32.15  ? 142  PRO G CG    1 
ATOM   10525 C  CD    . PRO B 2 142  ? 139.033 131.987 109.336 1.00 34.47  ? 142  PRO G CD    1 
ATOM   10526 N  N     . HIS B 2 143  ? 140.125 129.324 107.082 1.00 32.92  ? 143  HIS G N     1 
ATOM   10527 C  CA    . HIS B 2 143  ? 140.819 128.560 106.051 1.00 33.69  ? 143  HIS G CA    1 
ATOM   10528 C  C     . HIS B 2 143  ? 141.753 127.525 106.666 1.00 32.81  ? 143  HIS G C     1 
ATOM   10529 O  O     . HIS B 2 143  ? 141.817 126.384 106.199 1.00 35.52  ? 143  HIS G O     1 
ATOM   10530 C  CB    . HIS B 2 143  ? 141.586 129.522 105.144 1.00 36.36  ? 143  HIS G CB    1 
ATOM   10531 C  CG    . HIS B 2 143  ? 142.039 128.919 103.851 1.00 39.77  ? 143  HIS G CG    1 
ATOM   10532 N  ND1   . HIS B 2 143  ? 142.615 129.668 102.848 1.00 39.26  ? 143  HIS G ND1   1 
ATOM   10533 C  CD2   . HIS B 2 143  ? 142.013 127.643 103.401 1.00 40.11  ? 143  HIS G CD2   1 
ATOM   10534 C  CE1   . HIS B 2 143  ? 142.919 128.880 101.833 1.00 41.44  ? 143  HIS G CE1   1 
ATOM   10535 N  NE2   . HIS B 2 143  ? 142.563 127.646 102.142 1.00 41.66  ? 143  HIS G NE2   1 
ATOM   10536 N  N     . ALA B 2 144  ? 142.482 127.905 107.716 1.00 28.65  ? 144  ALA G N     1 
ATOM   10537 C  CA    . ALA B 2 144  ? 143.359 126.959 108.397 1.00 27.22  ? 144  ALA G CA    1 
ATOM   10538 C  C     . ALA B 2 144  ? 142.562 125.892 109.139 1.00 30.59  ? 144  ALA G C     1 
ATOM   10539 O  O     . ALA B 2 144  ? 142.961 124.721 109.174 1.00 36.35  ? 144  ALA G O     1 
ATOM   10540 C  CB    . ALA B 2 144  ? 144.280 127.706 109.357 1.00 25.72  ? 144  ALA G CB    1 
ATOM   10541 N  N     . ARG B 2 145  ? 141.437 126.283 109.742 1.00 28.62  ? 145  ARG G N     1 
ATOM   10542 C  CA    . ARG B 2 145  ? 140.612 125.346 110.496 1.00 24.51  ? 145  ARG G CA    1 
ATOM   10543 C  C     . ARG B 2 145  ? 140.015 124.282 109.586 1.00 27.00  ? 145  ARG G C     1 
ATOM   10544 O  O     . ARG B 2 145  ? 139.866 123.120 109.990 1.00 31.83  ? 145  ARG G O     1 
ATOM   10545 C  CB    . ARG B 2 145  ? 139.514 126.114 111.231 1.00 23.19  ? 145  ARG G CB    1 
ATOM   10546 C  CG    . ARG B 2 145  ? 138.702 125.287 112.195 1.00 28.79  ? 145  ARG G CG    1 
ATOM   10547 C  CD    . ARG B 2 145  ? 137.508 126.064 112.706 1.00 30.01  ? 145  ARG G CD    1 
ATOM   10548 N  NE    . ARG B 2 145  ? 137.897 127.358 113.252 1.00 31.10  ? 145  ARG G NE    1 
ATOM   10549 C  CZ    . ARG B 2 145  ? 137.375 128.516 112.874 1.00 35.07  ? 145  ARG G CZ    1 
ATOM   10550 N  NH1   . ARG B 2 145  ? 136.422 128.578 111.961 1.00 39.10  ? 145  ARG G NH1   1 
ATOM   10551 N  NH2   . ARG B 2 145  ? 137.818 129.640 113.430 1.00 28.87  ? 145  ARG G NH2   1 
ATOM   10552 N  N     . PHE B 2 146  ? 139.688 124.658 108.348 1.00 27.70  ? 146  PHE G N     1 
ATOM   10553 C  CA    . PHE B 2 146  ? 139.142 123.693 107.399 1.00 27.18  ? 146  PHE G CA    1 
ATOM   10554 C  C     . PHE B 2 146  ? 140.104 122.531 107.167 1.00 31.10  ? 146  PHE G C     1 
ATOM   10555 O  O     . PHE B 2 146  ? 139.682 121.372 107.101 1.00 34.14  ? 146  PHE G O     1 
ATOM   10556 C  CB    . PHE B 2 146  ? 138.810 124.404 106.086 1.00 31.54  ? 146  PHE G CB    1 
ATOM   10557 C  CG    . PHE B 2 146  ? 138.303 123.492 105.008 1.00 36.24  ? 146  PHE G CG    1 
ATOM   10558 C  CD1   . PHE B 2 146  ? 137.019 122.982 105.065 1.00 37.93  ? 146  PHE G CD1   1 
ATOM   10559 C  CD2   . PHE B 2 146  ? 139.099 123.168 103.926 1.00 35.33  ? 146  PHE G CD2   1 
ATOM   10560 C  CE1   . PHE B 2 146  ? 136.546 122.150 104.077 1.00 41.07  ? 146  PHE G CE1   1 
ATOM   10561 C  CE2   . PHE B 2 146  ? 138.631 122.337 102.932 1.00 40.08  ? 146  PHE G CE2   1 
ATOM   10562 C  CZ    . PHE B 2 146  ? 137.351 121.828 103.008 1.00 43.64  ? 146  PHE G CZ    1 
ATOM   10563 N  N     . TYR B 2 147  ? 141.402 122.820 107.042 1.00 28.77  ? 147  TYR G N     1 
ATOM   10564 C  CA    . TYR B 2 147  ? 142.400 121.770 106.853 1.00 27.05  ? 147  TYR G CA    1 
ATOM   10565 C  C     . TYR B 2 147  ? 142.728 121.050 108.156 1.00 28.90  ? 147  TYR G C     1 
ATOM   10566 O  O     . TYR B 2 147  ? 142.980 119.835 108.157 1.00 30.49  ? 147  TYR G O     1 
ATOM   10567 C  CB    . TYR B 2 147  ? 143.671 122.364 106.252 1.00 27.80  ? 147  TYR G CB    1 
ATOM   10568 C  CG    . TYR B 2 147  ? 143.479 123.036 104.913 1.00 33.84  ? 147  TYR G CG    1 
ATOM   10569 C  CD1   . TYR B 2 147  ? 142.643 122.492 103.951 1.00 36.80  ? 147  TYR G CD1   1 
ATOM   10570 C  CD2   . TYR B 2 147  ? 144.126 124.226 104.619 1.00 33.07  ? 147  TYR G CD2   1 
ATOM   10571 C  CE1   . TYR B 2 147  ? 142.470 123.107 102.727 1.00 36.30  ? 147  TYR G CE1   1 
ATOM   10572 C  CE2   . TYR B 2 147  ? 143.956 124.847 103.402 1.00 32.19  ? 147  TYR G CE2   1 
ATOM   10573 C  CZ    . TYR B 2 147  ? 143.127 124.284 102.460 1.00 35.33  ? 147  TYR G CZ    1 
ATOM   10574 O  OH    . TYR B 2 147  ? 142.951 124.899 101.245 1.00 36.52  ? 147  TYR G OH    1 
ATOM   10575 N  N     . ALA B 2 148  ? 142.758 121.790 109.268 1.00 29.58  ? 148  ALA G N     1 
ATOM   10576 C  CA    . ALA B 2 148  ? 143.086 121.179 110.550 1.00 23.01  ? 148  ALA G CA    1 
ATOM   10577 C  C     . ALA B 2 148  ? 142.057 120.128 110.937 1.00 26.33  ? 148  ALA G C     1 
ATOM   10578 O  O     . ALA B 2 148  ? 142.404 119.108 111.540 1.00 32.02  ? 148  ALA G O     1 
ATOM   10579 C  CB    . ALA B 2 148  ? 143.201 122.250 111.631 1.00 19.89  ? 148  ALA G CB    1 
ATOM   10580 N  N     . ALA B 2 149  ? 140.784 120.355 110.599 1.00 23.52  ? 149  ALA G N     1 
ATOM   10581 C  CA    . ALA B 2 149  ? 139.763 119.349 110.882 1.00 23.48  ? 149  ALA G CA    1 
ATOM   10582 C  C     . ALA B 2 149  ? 140.050 118.046 110.144 1.00 29.09  ? 149  ALA G C     1 
ATOM   10583 O  O     . ALA B 2 149  ? 139.926 116.952 110.714 1.00 32.28  ? 149  ALA G O     1 
ATOM   10584 C  CB    . ALA B 2 149  ? 138.385 119.885 110.504 1.00 27.08  ? 149  ALA G CB    1 
ATOM   10585 N  N     . GLN B 2 150  ? 140.447 118.145 108.876 1.00 30.32  ? 150  GLN G N     1 
ATOM   10586 C  CA    . GLN B 2 150  ? 140.771 116.957 108.097 1.00 30.33  ? 150  GLN G CA    1 
ATOM   10587 C  C     . GLN B 2 150  ? 141.977 116.234 108.676 1.00 30.43  ? 150  GLN G C     1 
ATOM   10588 O  O     . GLN B 2 150  ? 141.997 114.999 108.742 1.00 33.05  ? 150  GLN G O     1 
ATOM   10589 C  CB    . GLN B 2 150  ? 141.035 117.350 106.648 1.00 32.40  ? 150  GLN G CB    1 
ATOM   10590 C  CG    . GLN B 2 150  ? 139.843 117.963 105.954 1.00 35.26  ? 150  GLN G CG    1 
ATOM   10591 C  CD    . GLN B 2 150  ? 140.189 118.477 104.583 1.00 40.83  ? 150  GLN G CD    1 
ATOM   10592 O  OE1   . GLN B 2 150  ? 140.695 117.738 103.744 1.00 47.64  ? 150  GLN G OE1   1 
ATOM   10593 N  NE2   . GLN B 2 150  ? 139.925 119.753 104.345 1.00 39.22  ? 150  GLN G NE2   1 
ATOM   10594 N  N     . ILE B 2 151  ? 142.990 116.987 109.104 1.00 29.85  ? 151  ILE G N     1 
ATOM   10595 C  CA    . ILE B 2 151  ? 144.171 116.349 109.678 1.00 30.20  ? 151  ILE G CA    1 
ATOM   10596 C  C     . ILE B 2 151  ? 143.822 115.663 110.995 1.00 29.64  ? 151  ILE G C     1 
ATOM   10597 O  O     . ILE B 2 151  ? 144.339 114.582 111.306 1.00 30.22  ? 151  ILE G O     1 
ATOM   10598 C  CB    . ILE B 2 151  ? 145.309 117.370 109.850 1.00 29.61  ? 151  ILE G CB    1 
ATOM   10599 C  CG1   . ILE B 2 151  ? 145.678 117.982 108.502 1.00 27.17  ? 151  ILE G CG1   1 
ATOM   10600 C  CG2   . ILE B 2 151  ? 146.529 116.698 110.432 1.00 30.94  ? 151  ILE G CG2   1 
ATOM   10601 C  CD1   . ILE B 2 151  ? 146.225 116.981 107.525 1.00 25.34  ? 151  ILE G CD1   1 
ATOM   10602 N  N     . VAL B 2 152  ? 142.930 116.269 111.780 1.00 27.02  ? 152  VAL G N     1 
ATOM   10603 C  CA    . VAL B 2 152  ? 142.500 115.661 113.036 1.00 26.43  ? 152  VAL G CA    1 
ATOM   10604 C  C     . VAL B 2 152  ? 141.777 114.347 112.773 1.00 29.48  ? 152  VAL G C     1 
ATOM   10605 O  O     . VAL B 2 152  ? 142.035 113.335 113.439 1.00 36.74  ? 152  VAL G O     1 
ATOM   10606 C  CB    . VAL B 2 152  ? 141.621 116.647 113.826 1.00 25.96  ? 152  VAL G CB    1 
ATOM   10607 C  CG1   . VAL B 2 152  ? 140.804 115.915 114.874 1.00 28.38  ? 152  VAL G CG1   1 
ATOM   10608 C  CG2   . VAL B 2 152  ? 142.478 117.715 114.471 1.00 22.24  ? 152  VAL G CG2   1 
ATOM   10609 N  N     . LEU B 2 153  ? 140.872 114.335 111.793 1.00 28.79  ? 153  LEU G N     1 
ATOM   10610 C  CA    . LEU B 2 153  ? 140.174 113.094 111.463 1.00 32.09  ? 153  LEU G CA    1 
ATOM   10611 C  C     . LEU B 2 153  ? 141.143 112.027 110.968 1.00 33.76  ? 153  LEU G C     1 
ATOM   10612 O  O     . LEU B 2 153  ? 141.011 110.846 111.318 1.00 34.59  ? 153  LEU G O     1 
ATOM   10613 C  CB    . LEU B 2 153  ? 139.090 113.350 110.418 1.00 35.52  ? 153  LEU G CB    1 
ATOM   10614 C  CG    . LEU B 2 153  ? 137.847 114.116 110.870 1.00 37.61  ? 153  LEU G CG    1 
ATOM   10615 C  CD1   . LEU B 2 153  ? 137.003 114.515 109.674 1.00 42.39  ? 153  LEU G CD1   1 
ATOM   10616 C  CD2   . LEU B 2 153  ? 137.033 113.286 111.848 1.00 33.89  ? 153  LEU G CD2   1 
ATOM   10617 N  N     . THR B 2 154  ? 142.127 112.422 110.155 1.00 35.35  ? 154  THR G N     1 
ATOM   10618 C  CA    . THR B 2 154  ? 143.089 111.452 109.642 1.00 34.53  ? 154  THR G CA    1 
ATOM   10619 C  C     . THR B 2 154  ? 143.933 110.851 110.762 1.00 34.21  ? 154  THR G C     1 
ATOM   10620 O  O     . THR B 2 154  ? 144.170 109.638 110.779 1.00 35.51  ? 154  THR G O     1 
ATOM   10621 C  CB    . THR B 2 154  ? 143.980 112.103 108.586 1.00 32.48  ? 154  THR G CB    1 
ATOM   10622 O  OG1   . THR B 2 154  ? 143.168 112.576 107.507 1.00 37.32  ? 154  THR G OG1   1 
ATOM   10623 C  CG2   . THR B 2 154  ? 144.981 111.106 108.049 1.00 29.14  ? 154  THR G CG2   1 
ATOM   10624 N  N     . PHE B 2 155  ? 144.398 111.677 111.704 1.00 33.17  ? 155  PHE G N     1 
ATOM   10625 C  CA    . PHE B 2 155  ? 145.163 111.126 112.819 1.00 33.55  ? 155  PHE G CA    1 
ATOM   10626 C  C     . PHE B 2 155  ? 144.305 110.253 113.721 1.00 36.13  ? 155  PHE G C     1 
ATOM   10627 O  O     . PHE B 2 155  ? 144.799 109.251 114.248 1.00 42.49  ? 155  PHE G O     1 
ATOM   10628 C  CB    . PHE B 2 155  ? 145.834 112.229 113.642 1.00 33.64  ? 155  PHE G CB    1 
ATOM   10629 C  CG    . PHE B 2 155  ? 147.039 112.836 112.985 1.00 33.75  ? 155  PHE G CG    1 
ATOM   10630 C  CD1   . PHE B 2 155  ? 147.805 112.099 112.100 1.00 33.32  ? 155  PHE G CD1   1 
ATOM   10631 C  CD2   . PHE B 2 155  ? 147.434 114.127 113.289 1.00 32.10  ? 155  PHE G CD2   1 
ATOM   10632 C  CE1   . PHE B 2 155  ? 148.917 112.648 111.503 1.00 34.17  ? 155  PHE G CE1   1 
ATOM   10633 C  CE2   . PHE B 2 155  ? 148.549 114.681 112.698 1.00 31.38  ? 155  PHE G CE2   1 
ATOM   10634 C  CZ    . PHE B 2 155  ? 149.292 113.941 111.804 1.00 35.13  ? 155  PHE G CZ    1 
ATOM   10635 N  N     . GLU B 2 156  ? 143.029 110.598 113.909 1.00 36.75  ? 156  GLU G N     1 
ATOM   10636 C  CA    . GLU B 2 156  ? 142.151 109.722 114.679 1.00 36.70  ? 156  GLU G CA    1 
ATOM   10637 C  C     . GLU B 2 156  ? 142.006 108.365 114.002 1.00 39.31  ? 156  GLU G C     1 
ATOM   10638 O  O     . GLU B 2 156  ? 142.012 107.324 114.667 1.00 40.88  ? 156  GLU G O     1 
ATOM   10639 C  CB    . GLU B 2 156  ? 140.782 110.367 114.875 1.00 38.20  ? 156  GLU G CB    1 
ATOM   10640 C  CG    . GLU B 2 156  ? 139.812 109.463 115.610 1.00 45.68  ? 156  GLU G CG    1 
ATOM   10641 C  CD    . GLU B 2 156  ? 138.441 110.070 115.764 1.00 57.71  ? 156  GLU G CD    1 
ATOM   10642 O  OE1   . GLU B 2 156  ? 138.162 111.086 115.096 1.00 59.26  ? 156  GLU G OE1   1 
ATOM   10643 O  OE2   . GLU B 2 156  ? 137.642 109.531 116.558 1.00 61.28  ? 156  GLU G OE2   1 
ATOM   10644 N  N     . TYR B 2 157  ? 141.859 108.358 112.676 1.00 40.93  ? 157  TYR G N     1 
ATOM   10645 C  CA    . TYR B 2 157  ? 141.785 107.089 111.956 1.00 39.47  ? 157  TYR G CA    1 
ATOM   10646 C  C     . TYR B 2 157  ? 143.072 106.288 112.110 1.00 45.31  ? 157  TYR G C     1 
ATOM   10647 O  O     . TYR B 2 157  ? 143.039 105.085 112.391 1.00 46.94  ? 157  TYR G O     1 
ATOM   10648 C  CB    . TYR B 2 157  ? 141.493 107.331 110.477 1.00 38.26  ? 157  TYR G CB    1 
ATOM   10649 C  CG    . TYR B 2 157  ? 141.616 106.085 109.631 1.00 42.65  ? 157  TYR G CG    1 
ATOM   10650 C  CD1   . TYR B 2 157  ? 140.586 105.162 109.574 1.00 47.18  ? 157  TYR G CD1   1 
ATOM   10651 C  CD2   . TYR B 2 157  ? 142.763 105.830 108.892 1.00 44.92  ? 157  TYR G CD2   1 
ATOM   10652 C  CE1   . TYR B 2 157  ? 140.692 104.025 108.807 1.00 48.59  ? 157  TYR G CE1   1 
ATOM   10653 C  CE2   . TYR B 2 157  ? 142.876 104.693 108.124 1.00 47.25  ? 157  TYR G CE2   1 
ATOM   10654 C  CZ    . TYR B 2 157  ? 141.839 103.794 108.086 1.00 48.50  ? 157  TYR G CZ    1 
ATOM   10655 O  OH    . TYR B 2 157  ? 141.950 102.661 107.317 1.00 51.67  ? 157  TYR G OH    1 
ATOM   10656 N  N     . LEU B 2 158  ? 144.222 106.938 111.911 1.00 46.36  ? 158  LEU G N     1 
ATOM   10657 C  CA    . LEU B 2 158  ? 145.489 106.209 111.908 1.00 42.67  ? 158  LEU G CA    1 
ATOM   10658 C  C     . LEU B 2 158  ? 145.828 105.661 113.288 1.00 44.86  ? 158  LEU G C     1 
ATOM   10659 O  O     . LEU B 2 158  ? 146.264 104.512 113.410 1.00 50.75  ? 158  LEU G O     1 
ATOM   10660 C  CB    . LEU B 2 158  ? 146.618 107.102 111.395 1.00 39.14  ? 158  LEU G CB    1 
ATOM   10661 C  CG    . LEU B 2 158  ? 146.605 107.428 109.902 1.00 37.14  ? 158  LEU G CG    1 
ATOM   10662 C  CD1   . LEU B 2 158  ? 147.692 108.430 109.567 1.00 35.83  ? 158  LEU G CD1   1 
ATOM   10663 C  CD2   . LEU B 2 158  ? 146.773 106.165 109.080 1.00 35.46  ? 158  LEU G CD2   1 
ATOM   10664 N  N     . HIS B 2 159  ? 145.638 106.460 114.339 1.00 44.24  ? 159  HIS G N     1 
ATOM   10665 C  CA    . HIS B 2 159  ? 145.972 105.995 115.679 1.00 44.12  ? 159  HIS G CA    1 
ATOM   10666 C  C     . HIS B 2 159  ? 145.052 104.882 116.154 1.00 49.14  ? 159  HIS G C     1 
ATOM   10667 O  O     . HIS B 2 159  ? 145.411 104.154 117.084 1.00 52.43  ? 159  HIS G O     1 
ATOM   10668 C  CB    . HIS B 2 159  ? 145.939 107.161 116.663 1.00 40.80  ? 159  HIS G CB    1 
ATOM   10669 C  CG    . HIS B 2 159  ? 147.023 108.168 116.441 1.00 40.82  ? 159  HIS G CG    1 
ATOM   10670 N  ND1   . HIS B 2 159  ? 147.284 109.186 117.330 1.00 44.66  ? 159  HIS G ND1   1 
ATOM   10671 C  CD2   . HIS B 2 159  ? 147.928 108.298 115.443 1.00 39.25  ? 159  HIS G CD2   1 
ATOM   10672 C  CE1   . HIS B 2 159  ? 148.294 109.910 116.882 1.00 42.29  ? 159  HIS G CE1   1 
ATOM   10673 N  NE2   . HIS B 2 159  ? 148.704 109.391 115.739 1.00 38.76  ? 159  HIS G NE2   1 
ATOM   10674 N  N     . SER B 2 160  ? 143.875 104.735 115.544 1.00 49.28  ? 160  SER G N     1 
ATOM   10675 C  CA    . SER B 2 160  ? 143.002 103.618 115.885 1.00 53.38  ? 160  SER G CA    1 
ATOM   10676 C  C     . SER B 2 160  ? 143.623 102.282 115.501 1.00 55.57  ? 160  SER G C     1 
ATOM   10677 O  O     . SER B 2 160  ? 143.272 101.246 116.075 1.00 56.76  ? 160  SER G O     1 
ATOM   10678 C  CB    . SER B 2 160  ? 141.647 103.789 115.202 1.00 51.75  ? 160  SER G CB    1 
ATOM   10679 O  OG    . SER B 2 160  ? 140.804 102.686 115.469 1.00 58.86  ? 160  SER G OG    1 
ATOM   10680 N  N     . LEU B 2 161  ? 144.535 102.283 114.530 1.00 55.10  ? 161  LEU G N     1 
ATOM   10681 C  CA    . LEU B 2 161  ? 145.191 101.076 114.048 1.00 54.57  ? 161  LEU G CA    1 
ATOM   10682 C  C     . LEU B 2 161  ? 146.597 100.907 114.609 1.00 57.38  ? 161  LEU G C     1 
ATOM   10683 O  O     . LEU B 2 161  ? 147.330 100.027 114.149 1.00 60.14  ? 161  LEU G O     1 
ATOM   10684 C  CB    . LEU B 2 161  ? 145.249 101.083 112.520 1.00 56.10  ? 161  LEU G CB    1 
ATOM   10685 C  CG    . LEU B 2 161  ? 143.960 101.382 111.761 1.00 56.40  ? 161  LEU G CG    1 
ATOM   10686 C  CD1   . LEU B 2 161  ? 144.229 101.419 110.275 1.00 56.26  ? 161  LEU G CD1   1 
ATOM   10687 C  CD2   . LEU B 2 161  ? 142.917 100.338 112.080 1.00 65.96  ? 161  LEU G CD2   1 
ATOM   10688 N  N     . ASP B 2 162  ? 146.988 101.736 115.579 1.00 58.08  ? 162  ASP G N     1 
ATOM   10689 C  CA    . ASP B 2 162  ? 148.330 101.705 116.163 1.00 61.58  ? 162  ASP G CA    1 
ATOM   10690 C  C     . ASP B 2 162  ? 149.400 102.023 115.121 1.00 61.46  ? 162  ASP G C     1 
ATOM   10691 O  O     . ASP B 2 162  ? 150.455 101.388 115.074 1.00 66.17  ? 162  ASP G O     1 
ATOM   10692 C  CB    . ASP B 2 162  ? 148.614 100.362 116.843 1.00 67.98  ? 162  ASP G CB    1 
ATOM   10693 C  CG    . ASP B 2 162  ? 147.503 99.936  117.778 1.00 71.80  ? 162  ASP G CG    1 
ATOM   10694 O  OD1   . ASP B 2 162  ? 147.720 99.966  119.006 1.00 71.99  ? 162  ASP G OD1   1 
ATOM   10695 O  OD2   . ASP B 2 162  ? 146.414 99.572  117.290 1.00 72.94  ? 162  ASP G OD2   1 
ATOM   10696 N  N     . LEU B 2 163  ? 149.126 103.012 114.277 1.00 55.19  ? 163  LEU G N     1 
ATOM   10697 C  CA    . LEU B 2 163  ? 150.051 103.458 113.242 1.00 49.74  ? 163  LEU G CA    1 
ATOM   10698 C  C     . LEU B 2 163  ? 150.491 104.885 113.540 1.00 49.91  ? 163  LEU G C     1 
ATOM   10699 O  O     . LEU B 2 163  ? 149.649 105.768 113.732 1.00 53.57  ? 163  LEU G O     1 
ATOM   10700 C  CB    . LEU B 2 163  ? 149.405 103.379 111.860 1.00 47.34  ? 163  LEU G CB    1 
ATOM   10701 C  CG    . LEU B 2 163  ? 149.288 101.993 111.230 1.00 54.10  ? 163  LEU G CG    1 
ATOM   10702 C  CD1   . LEU B 2 163  ? 148.245 101.998 110.132 1.00 52.54  ? 163  LEU G CD1   1 
ATOM   10703 C  CD2   . LEU B 2 163  ? 150.630 101.561 110.678 1.00 58.82  ? 163  LEU G CD2   1 
ATOM   10704 N  N     . ILE B 2 164  ? 151.796 105.103 113.590 1.00 50.57  ? 164  ILE G N     1 
ATOM   10705 C  CA    . ILE B 2 164  ? 152.356 106.447 113.666 1.00 50.38  ? 164  ILE G CA    1 
ATOM   10706 C  C     . ILE B 2 164  ? 152.670 106.914 112.254 1.00 52.71  ? 164  ILE G C     1 
ATOM   10707 O  O     . ILE B 2 164  ? 153.123 106.129 111.414 1.00 56.95  ? 164  ILE G O     1 
ATOM   10708 C  CB    . ILE B 2 164  ? 153.612 106.480 114.556 1.00 47.05  ? 164  ILE G CB    1 
ATOM   10709 C  CG1   . ILE B 2 164  ? 153.375 105.708 115.850 1.00 56.15  ? 164  ILE G CG1   1 
ATOM   10710 C  CG2   . ILE B 2 164  ? 153.997 107.909 114.886 1.00 48.00  ? 164  ILE G CG2   1 
ATOM   10711 C  CD1   . ILE B 2 164  ? 154.583 105.683 116.756 1.00 61.96  ? 164  ILE G CD1   1 
ATOM   10712 N  N     . TYR B 2 165  ? 152.425 108.194 111.984 1.00 47.86  ? 165  TYR G N     1 
ATOM   10713 C  CA    . TYR B 2 165  ? 152.707 108.753 110.669 1.00 44.87  ? 165  TYR G CA    1 
ATOM   10714 C  C     . TYR B 2 165  ? 154.107 109.356 110.617 1.00 46.80  ? 165  TYR G C     1 
ATOM   10715 O  O     . TYR B 2 165  ? 154.895 109.027 109.727 1.00 52.66  ? 165  TYR G O     1 
ATOM   10716 C  CB    . TYR B 2 165  ? 151.641 109.790 110.310 1.00 47.20  ? 165  TYR G CB    1 
ATOM   10717 C  CG    . TYR B 2 165  ? 151.853 110.481 108.987 1.00 45.89  ? 165  TYR G CG    1 
ATOM   10718 C  CD1   . TYR B 2 165  ? 152.001 109.751 107.819 1.00 47.72  ? 165  TYR G CD1   1 
ATOM   10719 C  CD2   . TYR B 2 165  ? 151.863 111.860 108.902 1.00 43.91  ? 165  TYR G CD2   1 
ATOM   10720 C  CE1   . TYR B 2 165  ? 152.184 110.378 106.608 1.00 49.62  ? 165  TYR G CE1   1 
ATOM   10721 C  CE2   . TYR B 2 165  ? 152.033 112.491 107.697 1.00 44.79  ? 165  TYR G CE2   1 
ATOM   10722 C  CZ    . TYR B 2 165  ? 152.200 111.748 106.552 1.00 49.30  ? 165  TYR G CZ    1 
ATOM   10723 O  OH    . TYR B 2 165  ? 152.376 112.378 105.344 1.00 49.48  ? 165  TYR G OH    1 
ATOM   10724 N  N     . ARG B 2 166  ? 154.416 110.251 111.554 1.00 45.87  ? 166  ARG G N     1 
ATOM   10725 C  CA    . ARG B 2 166  ? 155.778 110.650 111.895 1.00 48.02  ? 166  ARG G CA    1 
ATOM   10726 C  C     . ARG B 2 166  ? 156.478 111.440 110.792 1.00 49.02  ? 166  ARG G C     1 
ATOM   10727 O  O     . ARG B 2 166  ? 157.700 111.602 110.828 1.00 54.26  ? 166  ARG G O     1 
ATOM   10728 C  CB    . ARG B 2 166  ? 156.614 109.425 112.285 1.00 50.38  ? 166  ARG G CB    1 
ATOM   10729 C  CG    . ARG B 2 166  ? 157.754 109.710 113.241 1.00 53.15  ? 166  ARG G CG    1 
ATOM   10730 C  CD    . ARG B 2 166  ? 158.282 108.428 113.853 1.00 54.92  ? 166  ARG G CD    1 
ATOM   10731 N  NE    . ARG B 2 166  ? 158.659 107.458 112.832 1.00 59.40  ? 166  ARG G NE    1 
ATOM   10732 C  CZ    . ARG B 2 166  ? 159.161 106.259 113.088 1.00 63.26  ? 166  ARG G CZ    1 
ATOM   10733 N  NH1   . ARG B 2 166  ? 159.383 105.853 114.327 1.00 68.50  ? 166  ARG G NH1   1 
ATOM   10734 N  NH2   . ARG B 2 166  ? 159.452 105.448 112.076 1.00 62.82  ? 166  ARG G NH2   1 
ATOM   10735 N  N     . ASP B 2 167  ? 155.745 111.931 109.797 1.00 48.51  ? 167  ASP G N     1 
ATOM   10736 C  CA    . ASP B 2 167  ? 156.302 112.937 108.902 1.00 48.06  ? 167  ASP G CA    1 
ATOM   10737 C  C     . ASP B 2 167  ? 155.214 113.877 108.408 1.00 46.54  ? 167  ASP G C     1 
ATOM   10738 O  O     . ASP B 2 167  ? 154.654 113.667 107.330 1.00 50.62  ? 167  ASP G O     1 
ATOM   10739 C  CB    . ASP B 2 167  ? 156.995 112.270 107.715 1.00 54.90  ? 167  ASP G CB    1 
ATOM   10740 C  CG    . ASP B 2 167  ? 157.927 113.212 106.979 1.00 66.69  ? 167  ASP G CG    1 
ATOM   10741 O  OD1   . ASP B 2 167  ? 158.394 114.193 107.594 1.00 68.31  ? 167  ASP G OD1   1 
ATOM   10742 O  OD2   . ASP B 2 167  ? 158.187 112.974 105.781 1.00 68.95  ? 167  ASP G OD2   1 
ATOM   10743 N  N     . LEU B 2 168  ? 154.955 114.949 109.148 1.00 44.15  ? 168  LEU G N     1 
ATOM   10744 C  CA    . LEU B 2 168  ? 153.901 115.894 108.810 1.00 43.12  ? 168  LEU G CA    1 
ATOM   10745 C  C     . LEU B 2 168  ? 154.525 117.238 108.462 1.00 43.21  ? 168  LEU G C     1 
ATOM   10746 O  O     . LEU B 2 168  ? 155.197 117.850 109.298 1.00 45.04  ? 168  LEU G O     1 
ATOM   10747 C  CB    . LEU B 2 168  ? 152.911 116.042 109.964 1.00 42.99  ? 168  LEU G CB    1 
ATOM   10748 C  CG    . LEU B 2 168  ? 151.727 116.978 109.715 1.00 38.13  ? 168  LEU G CG    1 
ATOM   10749 C  CD1   . LEU B 2 168  ? 150.858 116.442 108.592 1.00 37.70  ? 168  LEU G CD1   1 
ATOM   10750 C  CD2   . LEU B 2 168  ? 150.914 117.165 110.977 1.00 32.99  ? 168  LEU G CD2   1 
ATOM   10751 N  N     . LYS B 2 169  ? 154.291 117.699 107.236 1.00 40.29  ? 169  LYS G N     1 
ATOM   10752 C  CA    . LYS B 2 169  ? 154.841 118.961 106.765 1.00 40.62  ? 169  LYS G CA    1 
ATOM   10753 C  C     . LYS B 2 169  ? 154.079 119.379 105.519 1.00 44.70  ? 169  LYS G C     1 
ATOM   10754 O  O     . LYS B 2 169  ? 153.505 118.523 104.838 1.00 44.90  ? 169  LYS G O     1 
ATOM   10755 C  CB    . LYS B 2 169  ? 156.346 118.832 106.487 1.00 45.90  ? 169  LYS G CB    1 
ATOM   10756 C  CG    . LYS B 2 169  ? 156.709 117.799 105.446 1.00 50.42  ? 169  LYS G CG    1 
ATOM   10757 C  CD    . LYS B 2 169  ? 158.211 117.621 105.368 1.00 49.91  ? 169  LYS G CD    1 
ATOM   10758 C  CE    . LYS B 2 169  ? 158.592 116.696 104.235 1.00 53.85  ? 169  LYS G CE    1 
ATOM   10759 N  NZ    . LYS B 2 169  ? 160.064 116.559 104.113 1.00 62.42  ? 169  LYS G NZ    1 
ATOM   10760 N  N     . PRO B 2 170  ? 154.032 120.679 105.209 1.00 46.96  ? 170  PRO G N     1 
ATOM   10761 C  CA    . PRO B 2 170  ? 153.196 121.142 104.089 1.00 45.75  ? 170  PRO G CA    1 
ATOM   10762 C  C     . PRO B 2 170  ? 153.528 120.511 102.750 1.00 47.20  ? 170  PRO G C     1 
ATOM   10763 O  O     . PRO B 2 170  ? 152.641 120.406 101.894 1.00 53.59  ? 170  PRO G O     1 
ATOM   10764 C  CB    . PRO B 2 170  ? 153.453 122.655 104.074 1.00 45.39  ? 170  PRO G CB    1 
ATOM   10765 C  CG    . PRO B 2 170  ? 153.772 122.984 105.479 1.00 40.45  ? 170  PRO G CG    1 
ATOM   10766 C  CD    . PRO B 2 170  ? 154.560 121.807 105.992 1.00 44.00  ? 170  PRO G CD    1 
ATOM   10767 N  N     . GLU B 2 171  ? 154.774 120.088 102.531 1.00 44.35  ? 171  GLU G N     1 
ATOM   10768 C  CA    . GLU B 2 171  ? 155.131 119.485 101.253 1.00 48.15  ? 171  GLU G CA    1 
ATOM   10769 C  C     . GLU B 2 171  ? 154.509 118.107 101.064 1.00 51.62  ? 171  GLU G C     1 
ATOM   10770 O  O     . GLU B 2 171  ? 154.450 117.619 99.931  1.00 55.89  ? 171  GLU G O     1 
ATOM   10771 C  CB    . GLU B 2 171  ? 156.651 119.400 101.112 1.00 49.70  ? 171  GLU G CB    1 
ATOM   10772 C  CG    . GLU B 2 171  ? 157.370 120.731 101.279 1.00 56.48  ? 171  GLU G CG    1 
ATOM   10773 C  CD    . GLU B 2 171  ? 157.695 121.056 102.723 1.00 60.76  ? 171  GLU G CD    1 
ATOM   10774 O  OE1   . GLU B 2 171  ? 157.617 120.145 103.567 1.00 59.94  ? 171  GLU G OE1   1 
ATOM   10775 O  OE2   . GLU B 2 171  ? 158.024 122.225 103.016 1.00 60.30  ? 171  GLU G OE2   1 
ATOM   10776 N  N     . ASN B 2 172  ? 154.050 117.470 102.136 1.00 49.42  ? 172  ASN G N     1 
ATOM   10777 C  CA    . ASN B 2 172  ? 153.401 116.169 102.052 1.00 48.07  ? 172  ASN G CA    1 
ATOM   10778 C  C     . ASN B 2 172  ? 151.890 116.263 101.899 1.00 47.24  ? 172  ASN G C     1 
ATOM   10779 O  O     . ASN B 2 172  ? 151.232 115.228 101.759 1.00 46.63  ? 172  ASN G O     1 
ATOM   10780 C  CB    . ASN B 2 172  ? 153.738 115.332 103.289 1.00 47.91  ? 172  ASN G CB    1 
ATOM   10781 C  CG    . ASN B 2 172  ? 155.189 114.907 103.329 1.00 53.75  ? 172  ASN G CG    1 
ATOM   10782 O  OD1   . ASN B 2 172  ? 155.892 114.967 102.323 1.00 60.80  ? 172  ASN G OD1   1 
ATOM   10783 N  ND2   . ASN B 2 172  ? 155.646 114.477 104.495 1.00 52.14  ? 172  ASN G ND2   1 
ATOM   10784 N  N     . LEU B 2 173  ? 151.326 117.467 101.920 1.00 48.76  ? 173  LEU G N     1 
ATOM   10785 C  CA    . LEU B 2 173  ? 149.885 117.669 101.844 1.00 43.35  ? 173  LEU G CA    1 
ATOM   10786 C  C     . LEU B 2 173  ? 149.524 118.208 100.466 1.00 45.85  ? 173  LEU G C     1 
ATOM   10787 O  O     . LEU B 2 173  ? 150.021 119.262 100.058 1.00 51.00  ? 173  LEU G O     1 
ATOM   10788 C  CB    . LEU B 2 173  ? 149.421 118.629 102.938 1.00 38.55  ? 173  LEU G CB    1 
ATOM   10789 C  CG    . LEU B 2 173  ? 149.765 118.216 104.368 1.00 36.30  ? 173  LEU G CG    1 
ATOM   10790 C  CD1   . LEU B 2 173  ? 149.282 119.259 105.349 1.00 37.36  ? 173  LEU G CD1   1 
ATOM   10791 C  CD2   . LEU B 2 173  ? 149.158 116.865 104.688 1.00 35.25  ? 173  LEU G CD2   1 
ATOM   10792 N  N     . LEU B 2 174  ? 148.657 117.492 99.760  1.00 41.95  ? 174  LEU G N     1 
ATOM   10793 C  CA    . LEU B 2 174  ? 148.249 117.847 98.412  1.00 43.97  ? 174  LEU G CA    1 
ATOM   10794 C  C     . LEU B 2 174  ? 146.788 118.278 98.398  1.00 47.04  ? 174  LEU G C     1 
ATOM   10795 O  O     . LEU B 2 174  ? 146.001 117.893 99.266  1.00 52.61  ? 174  LEU G O     1 
ATOM   10796 C  CB    . LEU B 2 174  ? 148.455 116.669 97.459  1.00 47.46  ? 174  LEU G CB    1 
ATOM   10797 C  CG    . LEU B 2 174  ? 149.886 116.145 97.353  1.00 45.35  ? 174  LEU G CG    1 
ATOM   10798 C  CD1   . LEU B 2 174  ? 149.943 114.921 96.464  1.00 50.34  ? 174  LEU G CD1   1 
ATOM   10799 C  CD2   . LEU B 2 174  ? 150.810 117.225 96.829  1.00 51.04  ? 174  LEU G CD2   1 
ATOM   10800 N  N     . ILE B 2 175  ? 146.435 119.090 97.405  1.00 45.04  ? 175  ILE G N     1 
ATOM   10801 C  CA    . ILE B 2 175  ? 145.077 119.592 97.218  1.00 46.03  ? 175  ILE G CA    1 
ATOM   10802 C  C     . ILE B 2 175  ? 144.478 118.908 96.000  1.00 51.88  ? 175  ILE G C     1 
ATOM   10803 O  O     . ILE B 2 175  ? 145.099 118.883 94.934  1.00 60.01  ? 175  ILE G O     1 
ATOM   10804 C  CB    . ILE B 2 175  ? 145.061 121.119 97.037  1.00 45.47  ? 175  ILE G CB    1 
ATOM   10805 C  CG1   . ILE B 2 175  ? 145.922 121.799 98.099  1.00 46.05  ? 175  ILE G CG1   1 
ATOM   10806 C  CG2   . ILE B 2 175  ? 143.641 121.643 97.076  1.00 51.68  ? 175  ILE G CG2   1 
ATOM   10807 C  CD1   . ILE B 2 175  ? 145.426 121.589 99.496  1.00 44.71  ? 175  ILE G CD1   1 
ATOM   10808 N  N     . ASP B 2 176  ? 143.280 118.352 96.152  1.00 48.14  ? 176  ASP G N     1 
ATOM   10809 C  CA    . ASP B 2 176  ? 142.607 117.727 95.025  1.00 53.88  ? 176  ASP G CA    1 
ATOM   10810 C  C     . ASP B 2 176  ? 141.675 118.720 94.327  1.00 63.24  ? 176  ASP G C     1 
ATOM   10811 O  O     . ASP B 2 176  ? 141.662 119.918 94.618  1.00 64.69  ? 176  ASP G O     1 
ATOM   10812 C  CB    . ASP B 2 176  ? 141.881 116.457 95.473  1.00 53.00  ? 176  ASP G CB    1 
ATOM   10813 C  CG    . ASP B 2 176  ? 140.769 116.721 96.476  1.00 59.73  ? 176  ASP G CG    1 
ATOM   10814 O  OD1   . ASP B 2 176  ? 140.205 117.833 96.509  1.00 60.56  ? 176  ASP G OD1   1 
ATOM   10815 O  OD2   . ASP B 2 176  ? 140.453 115.790 97.245  1.00 62.24  ? 176  ASP G OD2   1 
ATOM   10816 N  N     . GLN B 2 177  ? 140.887 118.206 93.378  1.00 68.48  ? 177  GLN G N     1 
ATOM   10817 C  CA    . GLN B 2 177  ? 140.026 119.060 92.564  1.00 68.23  ? 177  GLN G CA    1 
ATOM   10818 C  C     . GLN B 2 177  ? 138.975 119.774 93.406  1.00 68.18  ? 177  GLN G C     1 
ATOM   10819 O  O     . GLN B 2 177  ? 138.676 120.950 93.170  1.00 71.02  ? 177  GLN G O     1 
ATOM   10820 C  CB    . GLN B 2 177  ? 139.359 118.231 91.468  1.00 74.46  ? 177  GLN G CB    1 
ATOM   10821 C  CG    . GLN B 2 177  ? 140.157 118.160 90.183  1.00 83.63  ? 177  GLN G CG    1 
ATOM   10822 C  CD    . GLN B 2 177  ? 139.590 117.161 89.199  1.00 92.82  ? 177  GLN G CD    1 
ATOM   10823 O  OE1   . GLN B 2 177  ? 139.859 115.963 89.290  1.00 96.71  ? 177  GLN G OE1   1 
ATOM   10824 N  NE2   . GLN B 2 177  ? 138.801 117.648 88.247  1.00 91.89  ? 177  GLN G NE2   1 
ATOM   10825 N  N     . GLN B 2 178  ? 138.394 119.082 94.385  1.00 64.82  ? 178  GLN G N     1 
ATOM   10826 C  CA    . GLN B 2 178  ? 137.355 119.682 95.213  1.00 64.33  ? 178  GLN G CA    1 
ATOM   10827 C  C     . GLN B 2 178  ? 137.908 120.625 96.272  1.00 63.27  ? 178  GLN G C     1 
ATOM   10828 O  O     . GLN B 2 178  ? 137.126 121.344 96.902  1.00 61.35  ? 178  GLN G O     1 
ATOM   10829 C  CB    . GLN B 2 178  ? 136.517 118.596 95.892  1.00 62.63  ? 178  GLN G CB    1 
ATOM   10830 C  CG    . GLN B 2 178  ? 135.453 117.968 95.009  1.00 66.77  ? 178  GLN G CG    1 
ATOM   10831 C  CD    . GLN B 2 178  ? 136.034 117.249 93.809  1.00 76.10  ? 178  GLN G CD    1 
ATOM   10832 O  OE1   . GLN B 2 178  ? 135.791 117.630 92.665  1.00 77.31  ? 178  GLN G OE1   1 
ATOM   10833 N  NE2   . GLN B 2 178  ? 136.811 116.202 94.065  1.00 72.43  ? 178  GLN G NE2   1 
ATOM   10834 N  N     . GLY B 2 179  ? 139.220 120.646 96.481  1.00 61.89  ? 179  GLY G N     1 
ATOM   10835 C  CA    . GLY B 2 179  ? 139.826 121.487 97.489  1.00 55.98  ? 179  GLY G CA    1 
ATOM   10836 C  C     . GLY B 2 179  ? 140.164 120.804 98.795  1.00 54.97  ? 179  GLY G C     1 
ATOM   10837 O  O     . GLY B 2 179  ? 140.552 121.491 99.746  1.00 54.29  ? 179  GLY G O     1 
ATOM   10838 N  N     . TYR B 2 180  ? 140.028 119.485 98.875  1.00 54.10  ? 180  TYR G N     1 
ATOM   10839 C  CA    . TYR B 2 180  ? 140.312 118.744 100.092 1.00 48.53  ? 180  TYR G CA    1 
ATOM   10840 C  C     . TYR B 2 180  ? 141.752 118.237 100.103 1.00 48.66  ? 180  TYR G C     1 
ATOM   10841 O  O     . TYR B 2 180  ? 142.425 118.172 99.072  1.00 49.04  ? 180  TYR G O     1 
ATOM   10842 C  CB    . TYR B 2 180  ? 139.335 117.577 100.247 1.00 50.16  ? 180  TYR G CB    1 
ATOM   10843 C  CG    . TYR B 2 180  ? 137.985 117.994 100.787 1.00 50.69  ? 180  TYR G CG    1 
ATOM   10844 C  CD1   . TYR B 2 180  ? 137.051 118.613 99.972  1.00 55.42  ? 180  TYR G CD1   1 
ATOM   10845 C  CD2   . TYR B 2 180  ? 137.655 117.783 102.117 1.00 48.53  ? 180  TYR G CD2   1 
ATOM   10846 C  CE1   . TYR B 2 180  ? 135.821 119.002 100.462 1.00 55.30  ? 180  TYR G CE1   1 
ATOM   10847 C  CE2   . TYR B 2 180  ? 136.427 118.169 102.616 1.00 51.95  ? 180  TYR G CE2   1 
ATOM   10848 C  CZ    . TYR B 2 180  ? 135.514 118.779 101.784 1.00 55.11  ? 180  TYR G CZ    1 
ATOM   10849 O  OH    . TYR B 2 180  ? 134.290 119.164 102.277 1.00 55.10  ? 180  TYR G OH    1 
ATOM   10850 N  N     . ILE B 2 181  ? 142.216 117.875 101.296 1.00 49.31  ? 181  ILE G N     1 
ATOM   10851 C  CA    . ILE B 2 181  ? 143.594 117.447 101.514 1.00 43.14  ? 181  ILE G CA    1 
ATOM   10852 C  C     . ILE B 2 181  ? 143.745 115.976 101.150 1.00 46.76  ? 181  ILE G C     1 
ATOM   10853 O  O     . ILE B 2 181  ? 142.842 115.166 101.385 1.00 52.28  ? 181  ILE G O     1 
ATOM   10854 C  CB    . ILE B 2 181  ? 144.002 117.701 102.976 1.00 39.88  ? 181  ILE G CB    1 
ATOM   10855 C  CG1   . ILE B 2 181  ? 143.925 119.190 103.306 1.00 41.71  ? 181  ILE G CG1   1 
ATOM   10856 C  CG2   . ILE B 2 181  ? 145.402 117.191 103.248 1.00 41.21  ? 181  ILE G CG2   1 
ATOM   10857 C  CD1   . ILE B 2 181  ? 145.034 120.007 102.695 1.00 38.20  ? 181  ILE G CD1   1 
ATOM   10858 N  N     . GLN B 2 182  ? 144.887 115.631 100.555 1.00 44.25  ? 182  GLN G N     1 
ATOM   10859 C  CA    . GLN B 2 182  ? 145.294 114.248 100.334 1.00 42.41  ? 182  GLN G CA    1 
ATOM   10860 C  C     . GLN B 2 182  ? 146.683 114.064 100.932 1.00 46.63  ? 182  GLN G C     1 
ATOM   10861 O  O     . GLN B 2 182  ? 147.606 114.811 100.595 1.00 53.60  ? 182  GLN G O     1 
ATOM   10862 C  CB    . GLN B 2 182  ? 145.300 113.903 98.845  1.00 48.46  ? 182  GLN G CB    1 
ATOM   10863 C  CG    . GLN B 2 182  ? 143.931 113.920 98.186  1.00 52.22  ? 182  GLN G CG    1 
ATOM   10864 C  CD    . GLN B 2 182  ? 142.964 112.931 98.801  1.00 54.16  ? 182  GLN G CD    1 
ATOM   10865 O  OE1   . GLN B 2 182  ? 143.296 111.765 99.000  1.00 58.32  ? 182  GLN G OE1   1 
ATOM   10866 N  NE2   . GLN B 2 182  ? 141.755 113.392 99.099  1.00 52.51  ? 182  GLN G NE2   1 
ATOM   10867 N  N     . VAL B 2 183  ? 146.829 113.081 101.816 1.00 46.67  ? 183  VAL G N     1 
ATOM   10868 C  CA    . VAL B 2 183  ? 148.073 112.862 102.549 1.00 44.79  ? 183  VAL G CA    1 
ATOM   10869 C  C     . VAL B 2 183  ? 148.875 111.759 101.871 1.00 52.61  ? 183  VAL G C     1 
ATOM   10870 O  O     . VAL B 2 183  ? 148.334 110.696 101.544 1.00 59.04  ? 183  VAL G O     1 
ATOM   10871 C  CB    . VAL B 2 183  ? 147.788 112.513 104.019 1.00 40.48  ? 183  VAL G CB    1 
ATOM   10872 C  CG1   . VAL B 2 183  ? 149.074 112.183 104.745 1.00 42.06  ? 183  VAL G CG1   1 
ATOM   10873 C  CG2   . VAL B 2 183  ? 147.074 113.661 104.705 1.00 38.50  ? 183  VAL G CG2   1 
ATOM   10874 N  N     . THR B 2 184  ? 150.167 112.008 101.659 1.00 52.48  ? 184  THR G N     1 
ATOM   10875 C  CA    . THR B 2 184  ? 151.054 111.084 100.963 1.00 53.70  ? 184  THR G CA    1 
ATOM   10876 C  C     . THR B 2 184  ? 152.364 110.935 101.735 1.00 59.56  ? 184  THR G C     1 
ATOM   10877 O  O     . THR B 2 184  ? 152.497 111.390 102.874 1.00 59.49  ? 184  THR G O     1 
ATOM   10878 C  CB    . THR B 2 184  ? 151.316 111.555 99.528  1.00 55.78  ? 184  THR G CB    1 
ATOM   10879 O  OG1   . THR B 2 184  ? 152.048 110.549 98.818  1.00 64.87  ? 184  THR G OG1   1 
ATOM   10880 C  CG2   . THR B 2 184  ? 152.097 112.863 99.519  1.00 51.63  ? 184  THR G CG2   1 
ATOM   10881 N  N     . ASP B 2 185  ? 153.336 110.279 101.091 1.00 62.12  ? 185  ASP G N     1 
ATOM   10882 C  CA    . ASP B 2 185  ? 154.689 110.105 101.614 1.00 60.15  ? 185  ASP G CA    1 
ATOM   10883 C  C     . ASP B 2 185  ? 154.702 109.368 102.949 1.00 65.22  ? 185  ASP G C     1 
ATOM   10884 O  O     . ASP B 2 185  ? 155.096 109.933 103.975 1.00 67.61  ? 185  ASP G O     1 
ATOM   10885 C  CB    . ASP B 2 185  ? 155.385 111.460 101.754 1.00 62.20  ? 185  ASP G CB    1 
ATOM   10886 C  CG    . ASP B 2 185  ? 156.879 111.330 101.985 1.00 69.03  ? 185  ASP G CG    1 
ATOM   10887 O  OD1   . ASP B 2 185  ? 157.379 110.189 102.045 1.00 69.49  ? 185  ASP G OD1   1 
ATOM   10888 O  OD2   . ASP B 2 185  ? 157.554 112.374 102.105 1.00 71.69  ? 185  ASP G OD2   1 
ATOM   10889 N  N     . PHE B 2 186  ? 154.273 108.108 102.943 1.00 64.45  ? 186  PHE G N     1 
ATOM   10890 C  CA    . PHE B 2 186  ? 154.279 107.258 104.125 1.00 62.97  ? 186  PHE G CA    1 
ATOM   10891 C  C     . PHE B 2 186  ? 155.629 106.589 104.364 1.00 65.87  ? 186  PHE G C     1 
ATOM   10892 O  O     . PHE B 2 186  ? 155.669 105.446 104.833 1.00 66.93  ? 186  PHE G O     1 
ATOM   10893 C  CB    . PHE B 2 186  ? 153.182 106.201 104.015 1.00 57.90  ? 186  PHE G CB    1 
ATOM   10894 C  CG    . PHE B 2 186  ? 151.838 106.679 104.473 1.00 63.56  ? 186  PHE G CG    1 
ATOM   10895 C  CD1   . PHE B 2 186  ? 151.101 107.559 103.702 1.00 62.28  ? 186  PHE G CD1   1 
ATOM   10896 C  CD2   . PHE B 2 186  ? 151.311 106.246 105.674 1.00 64.48  ? 186  PHE G CD2   1 
ATOM   10897 C  CE1   . PHE B 2 186  ? 149.867 107.996 104.122 1.00 57.04  ? 186  PHE G CE1   1 
ATOM   10898 C  CE2   . PHE B 2 186  ? 150.078 106.680 106.099 1.00 56.83  ? 186  PHE G CE2   1 
ATOM   10899 C  CZ    . PHE B 2 186  ? 149.354 107.556 105.323 1.00 56.11  ? 186  PHE G CZ    1 
ATOM   10900 N  N     . GLY B 2 187  ? 156.730 107.266 104.034 1.00 66.01  ? 187  GLY G N     1 
ATOM   10901 C  CA    . GLY B 2 187  ? 158.048 106.669 104.141 1.00 64.01  ? 187  GLY G CA    1 
ATOM   10902 C  C     . GLY B 2 187  ? 158.497 106.360 105.555 1.00 66.30  ? 187  GLY G C     1 
ATOM   10903 O  O     . GLY B 2 187  ? 159.344 105.481 105.744 1.00 75.37  ? 187  GLY G O     1 
ATOM   10904 N  N     . PHE B 2 188  ? 157.957 107.056 106.555 1.00 61.95  ? 188  PHE G N     1 
ATOM   10905 C  CA    . PHE B 2 188  ? 158.369 106.850 107.940 1.00 59.98  ? 188  PHE G CA    1 
ATOM   10906 C  C     . PHE B 2 188  ? 157.267 106.257 108.807 1.00 55.97  ? 188  PHE G C     1 
ATOM   10907 O  O     . PHE B 2 188  ? 157.435 106.174 110.029 1.00 59.70  ? 188  PHE G O     1 
ATOM   10908 C  CB    . PHE B 2 188  ? 158.862 108.163 108.557 1.00 58.43  ? 188  PHE G CB    1 
ATOM   10909 C  CG    . PHE B 2 188  ? 160.097 108.712 107.907 1.00 68.51  ? 188  PHE G CG    1 
ATOM   10910 C  CD1   . PHE B 2 188  ? 161.058 107.863 107.389 1.00 73.73  ? 188  PHE G CD1   1 
ATOM   10911 C  CD2   . PHE B 2 188  ? 160.307 110.078 107.833 1.00 70.57  ? 188  PHE G CD2   1 
ATOM   10912 C  CE1   . PHE B 2 188  ? 162.199 108.365 106.795 1.00 75.34  ? 188  PHE G CE1   1 
ATOM   10913 C  CE2   . PHE B 2 188  ? 161.445 110.586 107.242 1.00 71.36  ? 188  PHE G CE2   1 
ATOM   10914 C  CZ    . PHE B 2 188  ? 162.392 109.729 106.722 1.00 73.58  ? 188  PHE G CZ    1 
ATOM   10915 N  N     . ALA B 2 189  ? 156.152 105.841 108.217 1.00 54.11  ? 189  ALA G N     1 
ATOM   10916 C  CA    . ALA B 2 189  ? 155.074 105.245 108.991 1.00 52.42  ? 189  ALA G CA    1 
ATOM   10917 C  C     . ALA B 2 189  ? 155.498 103.887 109.534 1.00 60.63  ? 189  ALA G C     1 
ATOM   10918 O  O     . ALA B 2 189  ? 156.182 103.115 108.858 1.00 64.62  ? 189  ALA G O     1 
ATOM   10919 C  CB    . ALA B 2 189  ? 153.820 105.099 108.133 1.00 53.12  ? 189  ALA G CB    1 
ATOM   10920 N  N     . LYS B 2 190  ? 155.093 103.599 110.770 1.00 60.64  ? 190  LYS G N     1 
ATOM   10921 C  CA    . LYS B 2 190  ? 155.439 102.337 111.406 1.00 60.73  ? 190  LYS G CA    1 
ATOM   10922 C  C     . LYS B 2 190  ? 154.298 101.888 112.305 1.00 62.75  ? 190  LYS G C     1 
ATOM   10923 O  O     . LYS B 2 190  ? 153.617 102.712 112.917 1.00 62.13  ? 190  LYS G O     1 
ATOM   10924 C  CB    . LYS B 2 190  ? 156.735 102.456 112.217 1.00 63.46  ? 190  LYS G CB    1 
ATOM   10925 C  CG    . LYS B 2 190  ? 157.223 101.137 112.785 1.00 67.45  ? 190  LYS G CG    1 
ATOM   10926 C  CD    . LYS B 2 190  ? 158.383 101.331 113.738 1.00 72.95  ? 190  LYS G CD    1 
ATOM   10927 C  CE    . LYS B 2 190  ? 158.711 100.036 114.461 1.00 72.70  ? 190  LYS G CE    1 
ATOM   10928 N  NZ    . LYS B 2 190  ? 159.670 100.253 115.577 1.00 77.21  ? 190  LYS G NZ    1 
ATOM   10929 N  N     . ARG B 2 191  ? 154.098 100.571 112.372 1.00 64.42  ? 191  ARG G N     1 
ATOM   10930 C  CA    . ARG B 2 191  ? 153.080 99.958  113.226 1.00 65.75  ? 191  ARG G CA    1 
ATOM   10931 C  C     . ARG B 2 191  ? 153.665 99.764  114.622 1.00 68.05  ? 191  ARG G C     1 
ATOM   10932 O  O     . ARG B 2 191  ? 154.216 98.717  114.968 1.00 66.42  ? 191  ARG G O     1 
ATOM   10933 C  CB    . ARG B 2 191  ? 152.607 98.643  112.623 1.00 68.59  ? 191  ARG G CB    1 
ATOM   10934 C  CG    . ARG B 2 191  ? 151.456 97.978  113.349 1.00 72.49  ? 191  ARG G CG    1 
ATOM   10935 C  CD    . ARG B 2 191  ? 150.871 96.863  112.498 1.00 79.70  ? 191  ARG G CD    1 
ATOM   10936 N  NE    . ARG B 2 191  ? 149.977 95.986  113.244 1.00 81.19  ? 191  ARG G NE    1 
ATOM   10937 C  CZ    . ARG B 2 191  ? 148.779 96.332  113.692 1.00 79.35  ? 191  ARG G CZ    1 
ATOM   10938 N  NH1   . ARG B 2 191  ? 148.289 97.545  113.495 1.00 77.01  ? 191  ARG G NH1   1 
ATOM   10939 N  NH2   . ARG B 2 191  ? 148.053 95.438  114.356 1.00 79.37  ? 191  ARG G NH2   1 
ATOM   10940 N  N     . VAL B 2 192  ? 153.535 100.804 115.440 1.00 69.23  ? 192  VAL G N     1 
ATOM   10941 C  CA    . VAL B 2 192  ? 154.055 100.818 116.802 1.00 65.50  ? 192  VAL G CA    1 
ATOM   10942 C  C     . VAL B 2 192  ? 152.895 100.658 117.770 1.00 70.03  ? 192  VAL G C     1 
ATOM   10943 O  O     . VAL B 2 192  ? 151.912 101.406 117.702 1.00 71.54  ? 192  VAL G O     1 
ATOM   10944 C  CB    . VAL B 2 192  ? 154.830 102.112 117.101 1.00 63.77  ? 192  VAL G CB    1 
ATOM   10945 C  CG1   . VAL B 2 192  ? 155.150 102.202 118.579 1.00 66.32  ? 192  VAL G CG1   1 
ATOM   10946 C  CG2   . VAL B 2 192  ? 156.105 102.172 116.291 1.00 66.31  ? 192  VAL G CG2   1 
ATOM   10947 N  N     . LYS B 2 193  ? 153.015 99.688  118.674 1.00 73.17  ? 193  LYS G N     1 
ATOM   10948 C  CA    . LYS B 2 193  ? 152.095 99.510  119.797 1.00 77.30  ? 193  LYS G CA    1 
ATOM   10949 C  C     . LYS B 2 193  ? 153.002 99.428  121.023 1.00 78.74  ? 193  LYS G C     1 
ATOM   10950 O  O     . LYS B 2 193  ? 153.432 98.349  121.436 1.00 85.94  ? 193  LYS G O     1 
ATOM   10951 C  CB    . LYS B 2 193  ? 151.219 98.266  119.610 1.00 78.83  ? 193  LYS G CB    1 
ATOM   10952 C  CG    . LYS B 2 193  ? 150.534 97.746  120.866 1.00 80.39  ? 193  LYS G CG    1 
ATOM   10953 C  CD    . LYS B 2 193  ? 150.062 96.293  120.717 1.00 85.38  ? 193  LYS G CD    1 
ATOM   10954 C  CE    . LYS B 2 193  ? 149.570 95.931  119.310 1.00 86.26  ? 193  LYS G CE    1 
ATOM   10955 N  NZ    . LYS B 2 193  ? 148.619 96.912  118.705 1.00 81.27  ? 193  LYS G NZ    1 
ATOM   10956 N  N     . GLY B 2 194  ? 153.321 100.589 121.587 1.00 72.37  ? 194  GLY G N     1 
ATOM   10957 C  CA    . GLY B 2 194  ? 154.347 100.651 122.606 1.00 73.25  ? 194  GLY G CA    1 
ATOM   10958 C  C     . GLY B 2 194  ? 155.272 101.838 122.438 1.00 72.25  ? 194  GLY G C     1 
ATOM   10959 O  O     . GLY B 2 194  ? 154.824 102.987 122.426 1.00 76.65  ? 194  GLY G O     1 
ATOM   10960 N  N     . ARG B 2 195  ? 156.570 101.569 122.310 1.00 67.59  ? 195  ARG G N     1 
ATOM   10961 C  CA    . ARG B 2 195  ? 157.590 102.602 122.230 1.00 65.89  ? 195  ARG G CA    1 
ATOM   10962 C  C     . ARG B 2 195  ? 158.475 102.366 121.012 1.00 66.25  ? 195  ARG G C     1 
ATOM   10963 O  O     . ARG B 2 195  ? 158.500 101.275 120.438 1.00 65.79  ? 195  ARG G O     1 
ATOM   10964 C  CB    . ARG B 2 195  ? 158.450 102.628 123.497 1.00 67.09  ? 195  ARG G CB    1 
ATOM   10965 C  CG    . ARG B 2 195  ? 158.947 104.000 123.888 1.00 70.43  ? 195  ARG G CG    1 
ATOM   10966 C  CD    . ARG B 2 195  ? 157.860 104.785 124.593 1.00 74.85  ? 195  ARG G CD    1 
ATOM   10967 N  NE    . ARG B 2 195  ? 157.576 104.235 125.912 1.00 84.53  ? 195  ARG G NE    1 
ATOM   10968 C  CZ    . ARG B 2 195  ? 158.319 104.450 126.989 1.00 85.97  ? 195  ARG G CZ    1 
ATOM   10969 N  NH1   . ARG B 2 195  ? 159.399 105.213 126.942 1.00 78.33  ? 195  ARG G NH1   1 
ATOM   10970 N  NH2   . ARG B 2 195  ? 157.971 103.885 128.141 1.00 86.34  ? 195  ARG G NH2   1 
ATOM   10971 N  N     . THR B 2 196  ? 159.201 103.413 120.619 1.00 64.58  ? 196  THR G N     1 
ATOM   10972 C  CA    . THR B 2 196  ? 160.182 103.321 119.546 1.00 67.15  ? 196  THR G CA    1 
ATOM   10973 C  C     . THR B 2 196  ? 161.275 104.353 119.788 1.00 67.00  ? 196  THR G C     1 
ATOM   10974 O  O     . THR B 2 196  ? 161.066 105.342 120.495 1.00 66.86  ? 196  THR G O     1 
ATOM   10975 C  CB    . THR B 2 196  ? 159.545 103.526 118.167 1.00 68.12  ? 196  THR G CB    1 
ATOM   10976 O  OG1   . THR B 2 196  ? 160.544 103.378 117.151 1.00 69.26  ? 196  THR G OG1   1 
ATOM   10977 C  CG2   . THR B 2 196  ? 158.924 104.905 118.064 1.00 66.95  ? 196  THR G CG2   1 
ATOM   10978 N  N     . TRP B 2 197  ? 162.444 104.111 119.201 1.00 67.95  ? 197  TRP G N     1 
ATOM   10979 C  CA    . TRP B 2 197  ? 163.622 104.934 119.479 1.00 71.61  ? 197  TRP G CA    1 
ATOM   10980 C  C     . TRP B 2 197  ? 164.297 105.514 118.237 1.00 71.76  ? 197  TRP G C     1 
ATOM   10981 O  O     . TRP B 2 197  ? 165.377 106.088 118.335 1.00 70.88  ? 197  TRP G O     1 
ATOM   10982 C  CB    . TRP B 2 197  ? 164.654 104.121 120.265 1.00 69.17  ? 197  TRP G CB    1 
ATOM   10983 C  CG    . TRP B 2 197  ? 164.245 103.847 121.669 1.00 69.03  ? 197  TRP G CG    1 
ATOM   10984 C  CD1   . TRP B 2 197  ? 164.555 104.585 122.772 1.00 70.68  ? 197  TRP G CD1   1 
ATOM   10985 C  CD2   . TRP B 2 197  ? 163.444 102.757 122.126 1.00 67.90  ? 197  TRP G CD2   1 
ATOM   10986 N  NE1   . TRP B 2 197  ? 163.995 104.019 123.891 1.00 70.23  ? 197  TRP G NE1   1 
ATOM   10987 C  CE2   . TRP B 2 197  ? 163.307 102.896 123.519 1.00 69.00  ? 197  TRP G CE2   1 
ATOM   10988 C  CE3   . TRP B 2 197  ? 162.828 101.675 121.493 1.00 66.98  ? 197  TRP G CE3   1 
ATOM   10989 C  CZ2   . TRP B 2 197  ? 162.580 101.994 124.290 1.00 66.78  ? 197  TRP G CZ2   1 
ATOM   10990 C  CZ3   . TRP B 2 197  ? 162.106 100.781 122.258 1.00 67.59  ? 197  TRP G CZ3   1 
ATOM   10991 C  CH2   . TRP B 2 197  ? 161.988 100.946 123.641 1.00 65.80  ? 197  TRP G CH2   1 
HETATM 10992 N  N     . TPO B 2 198  ? 163.669 105.370 117.076 1.00 68.86  ? 198  TPO G N     1 
HETATM 10993 C  CA    . TPO B 2 198  ? 164.280 105.839 115.838 1.00 67.06  ? 198  TPO G CA    1 
HETATM 10994 C  CB    . TPO B 2 198  ? 163.685 105.130 114.613 1.00 72.43  ? 198  TPO G CB    1 
HETATM 10995 C  CG2   . TPO B 2 198  ? 164.550 105.359 113.379 1.00 73.73  ? 198  TPO G CG2   1 
HETATM 10996 O  OG1   . TPO B 2 198  ? 163.591 103.757 114.889 1.00 77.19  ? 198  TPO G OG1   1 
HETATM 10997 P  P     . TPO B 2 198  ? 162.361 102.845 114.120 1.00 85.56  ? 198  TPO G P     1 
HETATM 10998 O  O1P   . TPO B 2 198  ? 161.173 103.776 114.326 1.00 75.17  ? 198  TPO G O1P   1 
HETATM 10999 O  O2P   . TPO B 2 198  ? 162.824 102.692 112.673 1.00 84.78  ? 198  TPO G O2P   1 
HETATM 11000 O  O3P   . TPO B 2 198  ? 162.287 101.526 114.886 1.00 81.05  ? 198  TPO G O3P   1 
HETATM 11001 C  C     . TPO B 2 198  ? 164.116 107.342 115.666 1.00 70.40  ? 198  TPO G C     1 
HETATM 11002 O  O     . TPO B 2 198  ? 163.038 107.887 115.889 1.00 72.05  ? 198  TPO G O     1 
ATOM   11003 N  N     . LEU B 2 199  ? 165.195 108.007 115.265 1.00 71.43  ? 199  LEU G N     1 
ATOM   11004 C  CA    . LEU B 2 199  ? 165.163 109.440 115.007 1.00 74.73  ? 199  LEU G CA    1 
ATOM   11005 C  C     . LEU B 2 199  ? 165.052 109.696 113.509 1.00 77.90  ? 199  LEU G C     1 
ATOM   11006 O  O     . LEU B 2 199  ? 165.989 109.436 112.755 1.00 80.94  ? 199  LEU G O     1 
ATOM   11007 C  CB    . LEU B 2 199  ? 166.411 110.118 115.579 1.00 73.45  ? 199  LEU G CB    1 
ATOM   11008 C  CG    . LEU B 2 199  ? 166.451 111.644 115.718 1.00 76.31  ? 199  LEU G CG    1 
ATOM   11009 C  CD1   . LEU B 2 199  ? 167.497 112.032 116.746 1.00 72.60  ? 199  LEU G CD1   1 
ATOM   11010 C  CD2   . LEU B 2 199  ? 166.748 112.337 114.398 1.00 71.05  ? 199  LEU G CD2   1 
ATOM   11011 N  N     . CYS B 2 200  ? 163.901 110.212 113.085 1.00 74.58  ? 200  CYS G N     1 
ATOM   11012 C  CA    . CYS B 2 200  ? 163.671 110.510 111.680 1.00 72.57  ? 200  CYS G CA    1 
ATOM   11013 C  C     . CYS B 2 200  ? 162.637 111.619 111.574 1.00 73.01  ? 200  CYS G C     1 
ATOM   11014 O  O     . CYS B 2 200  ? 161.778 111.771 112.446 1.00 72.18  ? 200  CYS G O     1 
ATOM   11015 C  CB    . CYS B 2 200  ? 163.205 109.269 110.912 1.00 73.57  ? 200  CYS G CB    1 
ATOM   11016 S  SG    . CYS B 2 200  ? 161.561 108.683 111.366 1.00 75.01  ? 200  CYS G SG    1 
ATOM   11017 N  N     . GLY B 2 201  ? 162.731 112.387 110.498 1.00 71.89  ? 201  GLY G N     1 
ATOM   11018 C  CA    . GLY B 2 201  ? 161.820 113.480 110.226 1.00 70.15  ? 201  GLY G CA    1 
ATOM   11019 C  C     . GLY B 2 201  ? 162.558 114.778 109.972 1.00 68.54  ? 201  GLY G C     1 
ATOM   11020 O  O     . GLY B 2 201  ? 163.789 114.830 109.907 1.00 70.23  ? 201  GLY G O     1 
ATOM   11021 N  N     . THR B 2 202  ? 161.775 115.848 109.826 1.00 67.85  ? 202  THR G N     1 
ATOM   11022 C  CA    . THR B 2 202  ? 162.246 117.196 109.528 1.00 62.82  ? 202  THR G CA    1 
ATOM   11023 C  C     . THR B 2 202  ? 162.453 117.961 110.826 1.00 58.96  ? 202  THR G C     1 
ATOM   11024 O  O     . THR B 2 202  ? 161.560 117.955 111.682 1.00 59.06  ? 202  THR G O     1 
ATOM   11025 C  CB    . THR B 2 202  ? 161.239 117.918 108.638 1.00 63.57  ? 202  THR G CB    1 
ATOM   11026 O  OG1   . THR B 2 202  ? 161.095 117.196 107.409 1.00 63.02  ? 202  THR G OG1   1 
ATOM   11027 C  CG2   . THR B 2 202  ? 161.693 119.327 108.320 1.00 61.28  ? 202  THR G CG2   1 
ATOM   11028 N  N     . PRO B 2 203  ? 163.605 118.612 111.015 1.00 56.02  ? 203  PRO G N     1 
ATOM   11029 C  CA    . PRO B 2 203  ? 163.941 119.140 112.350 1.00 58.70  ? 203  PRO G CA    1 
ATOM   11030 C  C     . PRO B 2 203  ? 162.938 120.127 112.931 1.00 59.71  ? 203  PRO G C     1 
ATOM   11031 O  O     . PRO B 2 203  ? 162.754 120.136 114.154 1.00 60.68  ? 203  PRO G O     1 
ATOM   11032 C  CB    . PRO B 2 203  ? 165.312 119.798 112.129 1.00 59.53  ? 203  PRO G CB    1 
ATOM   11033 C  CG    . PRO B 2 203  ? 165.396 120.033 110.655 1.00 59.00  ? 203  PRO G CG    1 
ATOM   11034 C  CD    . PRO B 2 203  ? 164.675 118.874 110.043 1.00 57.22  ? 203  PRO G CD    1 
ATOM   11035 N  N     . GLU B 2 204  ? 162.291 120.965 112.118 1.00 55.69  ? 204  GLU G N     1 
ATOM   11036 C  CA    . GLU B 2 204  ? 161.350 121.928 112.685 1.00 48.70  ? 204  GLU G CA    1 
ATOM   11037 C  C     . GLU B 2 204  ? 160.110 121.248 113.252 1.00 49.09  ? 204  GLU G C     1 
ATOM   11038 O  O     . GLU B 2 204  ? 159.440 121.812 114.123 1.00 48.38  ? 204  GLU G O     1 
ATOM   11039 C  CB    . GLU B 2 204  ? 160.941 122.970 111.643 1.00 44.62  ? 204  GLU G CB    1 
ATOM   11040 C  CG    . GLU B 2 204  ? 162.087 123.792 111.087 1.00 51.88  ? 204  GLU G CG    1 
ATOM   11041 C  CD    . GLU B 2 204  ? 162.754 123.143 109.896 1.00 63.89  ? 204  GLU G CD    1 
ATOM   11042 O  OE1   . GLU B 2 204  ? 162.084 122.361 109.192 1.00 64.78  ? 204  GLU G OE1   1 
ATOM   11043 O  OE2   . GLU B 2 204  ? 163.952 123.409 109.666 1.00 66.86  ? 204  GLU G OE2   1 
ATOM   11044 N  N     . TYR B 2 205  ? 159.793 120.044 112.781 1.00 49.38  ? 205  TYR G N     1 
ATOM   11045 C  CA    . TYR B 2 205  ? 158.576 119.341 113.164 1.00 47.54  ? 205  TYR G CA    1 
ATOM   11046 C  C     . TYR B 2 205  ? 158.825 118.202 114.143 1.00 51.67  ? 205  TYR G C     1 
ATOM   11047 O  O     . TYR B 2 205  ? 157.948 117.353 114.324 1.00 51.44  ? 205  TYR G O     1 
ATOM   11048 C  CB    . TYR B 2 205  ? 157.865 118.824 111.914 1.00 43.64  ? 205  TYR G CB    1 
ATOM   11049 C  CG    . TYR B 2 205  ? 157.250 119.929 111.090 1.00 43.34  ? 205  TYR G CG    1 
ATOM   11050 C  CD1   . TYR B 2 205  ? 158.004 120.639 110.169 1.00 41.35  ? 205  TYR G CD1   1 
ATOM   11051 C  CD2   . TYR B 2 205  ? 155.908 120.254 111.229 1.00 38.60  ? 205  TYR G CD2   1 
ATOM   11052 C  CE1   . TYR B 2 205  ? 157.445 121.651 109.421 1.00 39.01  ? 205  TYR G CE1   1 
ATOM   11053 C  CE2   . TYR B 2 205  ? 155.339 121.258 110.479 1.00 37.22  ? 205  TYR G CE2   1 
ATOM   11054 C  CZ    . TYR B 2 205  ? 156.112 121.956 109.579 1.00 42.96  ? 205  TYR G CZ    1 
ATOM   11055 O  OH    . TYR B 2 205  ? 155.545 122.961 108.832 1.00 46.23  ? 205  TYR G OH    1 
ATOM   11056 N  N     . LEU B 2 206  ? 159.994 118.158 114.773 1.00 52.21  ? 206  LEU G N     1 
ATOM   11057 C  CA    . LEU B 2 206  ? 160.329 117.088 115.700 1.00 49.32  ? 206  LEU G CA    1 
ATOM   11058 C  C     . LEU B 2 206  ? 159.956 117.456 117.131 1.00 48.37  ? 206  LEU G C     1 
ATOM   11059 O  O     . LEU B 2 206  ? 160.137 118.598 117.561 1.00 48.00  ? 206  LEU G O     1 
ATOM   11060 C  CB    . LEU B 2 206  ? 161.818 116.763 115.617 1.00 47.09  ? 206  LEU G CB    1 
ATOM   11061 C  CG    . LEU B 2 206  ? 162.309 116.124 114.323 1.00 54.40  ? 206  LEU G CG    1 
ATOM   11062 C  CD1   . LEU B 2 206  ? 163.815 115.964 114.362 1.00 56.83  ? 206  LEU G CD1   1 
ATOM   11063 C  CD2   . LEU B 2 206  ? 161.630 114.785 114.111 1.00 57.85  ? 206  LEU G CD2   1 
ATOM   11064 N  N     . ALA B 2 207  ? 159.443 116.470 117.864 1.00 46.97  ? 207  ALA G N     1 
ATOM   11065 C  CA    . ALA B 2 207  ? 159.034 116.642 119.248 1.00 39.59  ? 207  ALA G CA    1 
ATOM   11066 C  C     . ALA B 2 207  ? 160.244 116.673 120.177 1.00 45.94  ? 207  ALA G C     1 
ATOM   11067 O  O     . ALA B 2 207  ? 161.318 116.178 119.828 1.00 52.82  ? 207  ALA G O     1 
ATOM   11068 C  CB    . ALA B 2 207  ? 158.091 115.514 119.652 1.00 37.49  ? 207  ALA G CB    1 
ATOM   11069 N  N     . PRO B 2 208  ? 160.102 117.274 121.365 1.00 43.98  ? 208  PRO G N     1 
ATOM   11070 C  CA    . PRO B 2 208  ? 161.238 117.319 122.305 1.00 47.03  ? 208  PRO G CA    1 
ATOM   11071 C  C     . PRO B 2 208  ? 161.785 115.958 122.707 1.00 49.41  ? 208  PRO G C     1 
ATOM   11072 O  O     . PRO B 2 208  ? 163.006 115.804 122.823 1.00 53.89  ? 208  PRO G O     1 
ATOM   11073 C  CB    . PRO B 2 208  ? 160.656 118.068 123.512 1.00 41.87  ? 208  PRO G CB    1 
ATOM   11074 C  CG    . PRO B 2 208  ? 159.558 118.883 122.946 1.00 43.01  ? 208  PRO G CG    1 
ATOM   11075 C  CD    . PRO B 2 208  ? 158.950 118.034 121.875 1.00 42.31  ? 208  PRO G CD    1 
ATOM   11076 N  N     . GLU B 2 209  ? 160.923 114.964 122.929 1.00 48.68  ? 209  GLU G N     1 
ATOM   11077 C  CA    . GLU B 2 209  ? 161.418 113.657 123.348 1.00 50.07  ? 209  GLU G CA    1 
ATOM   11078 C  C     . GLU B 2 209  ? 162.166 112.946 122.228 1.00 52.89  ? 209  GLU G C     1 
ATOM   11079 O  O     . GLU B 2 209  ? 162.978 112.056 122.499 1.00 61.25  ? 209  GLU G O     1 
ATOM   11080 C  CB    . GLU B 2 209  ? 160.274 112.787 123.869 1.00 51.99  ? 209  GLU G CB    1 
ATOM   11081 C  CG    . GLU B 2 209  ? 159.177 112.492 122.870 1.00 52.91  ? 209  GLU G CG    1 
ATOM   11082 C  CD    . GLU B 2 209  ? 158.065 113.512 122.917 1.00 54.40  ? 209  GLU G CD    1 
ATOM   11083 O  OE1   . GLU B 2 209  ? 158.235 114.544 123.598 1.00 55.21  ? 209  GLU G OE1   1 
ATOM   11084 O  OE2   . GLU B 2 209  ? 157.017 113.279 122.281 1.00 53.23  ? 209  GLU G OE2   1 
ATOM   11085 N  N     . ILE B 2 210  ? 161.905 113.309 120.971 1.00 49.72  ? 210  ILE G N     1 
ATOM   11086 C  CA    . ILE B 2 210  ? 162.688 112.755 119.871 1.00 55.41  ? 210  ILE G CA    1 
ATOM   11087 C  C     . ILE B 2 210  ? 164.106 113.315 119.890 1.00 61.39  ? 210  ILE G C     1 
ATOM   11088 O  O     . ILE B 2 210  ? 165.078 112.588 119.654 1.00 63.37  ? 210  ILE G O     1 
ATOM   11089 C  CB    . ILE B 2 210  ? 161.990 113.018 118.525 1.00 52.72  ? 210  ILE G CB    1 
ATOM   11090 C  CG1   . ILE B 2 210  ? 160.591 112.408 118.518 1.00 52.39  ? 210  ILE G CG1   1 
ATOM   11091 C  CG2   . ILE B 2 210  ? 162.802 112.449 117.382 1.00 55.97  ? 210  ILE G CG2   1 
ATOM   11092 C  CD1   . ILE B 2 210  ? 159.749 112.841 117.344 1.00 49.53  ? 210  ILE G CD1   1 
ATOM   11093 N  N     . ILE B 2 211  ? 164.249 114.613 120.166 1.00 59.50  ? 211  ILE G N     1 
ATOM   11094 C  CA    . ILE B 2 211  ? 165.576 115.218 120.246 1.00 59.12  ? 211  ILE G CA    1 
ATOM   11095 C  C     . ILE B 2 211  ? 166.350 114.663 121.433 1.00 62.38  ? 211  ILE G C     1 
ATOM   11096 O  O     . ILE B 2 211  ? 167.542 114.349 121.324 1.00 65.18  ? 211  ILE G O     1 
ATOM   11097 C  CB    . ILE B 2 211  ? 165.468 116.754 120.311 1.00 61.73  ? 211  ILE G CB    1 
ATOM   11098 C  CG1   . ILE B 2 211  ? 165.381 117.358 118.910 1.00 64.19  ? 211  ILE G CG1   1 
ATOM   11099 C  CG2   . ILE B 2 211  ? 166.650 117.349 121.058 1.00 65.29  ? 211  ILE G CG2   1 
ATOM   11100 C  CD1   . ILE B 2 211  ? 164.204 116.911 118.104 1.00 61.81  ? 211  ILE G CD1   1 
ATOM   11101 N  N     . LEU B 2 212  ? 165.686 114.512 122.578 1.00 61.22  ? 212  LEU G N     1 
ATOM   11102 C  CA    . LEU B 2 212  ? 166.338 114.059 123.800 1.00 63.00  ? 212  LEU G CA    1 
ATOM   11103 C  C     . LEU B 2 212  ? 166.844 112.627 123.712 1.00 70.30  ? 212  LEU G C     1 
ATOM   11104 O  O     . LEU B 2 212  ? 167.427 112.143 124.688 1.00 75.99  ? 212  LEU G O     1 
ATOM   11105 C  CB    . LEU B 2 212  ? 165.378 114.194 124.982 1.00 62.24  ? 212  LEU G CB    1 
ATOM   11106 C  CG    . LEU B 2 212  ? 165.492 115.452 125.845 1.00 62.50  ? 212  LEU G CG    1 
ATOM   11107 C  CD1   . LEU B 2 212  ? 165.531 116.715 124.994 1.00 60.90  ? 212  LEU G CD1   1 
ATOM   11108 C  CD2   . LEU B 2 212  ? 164.337 115.502 126.829 1.00 63.83  ? 212  LEU G CD2   1 
ATOM   11109 N  N     . SER B 2 213  ? 166.626 111.944 122.586 1.00 70.81  ? 213  SER G N     1 
ATOM   11110 C  CA    . SER B 2 213  ? 167.141 110.596 122.350 1.00 73.66  ? 213  SER G CA    1 
ATOM   11111 C  C     . SER B 2 213  ? 166.614 109.618 123.399 1.00 76.16  ? 213  SER G C     1 
ATOM   11112 O  O     . SER B 2 213  ? 167.369 108.963 124.121 1.00 76.98  ? 213  SER G O     1 
ATOM   11113 C  CB    . SER B 2 213  ? 168.673 110.592 122.303 1.00 74.21  ? 213  SER G CB    1 
ATOM   11114 O  OG    . SER B 2 213  ? 169.148 111.272 121.155 1.00 74.16  ? 213  SER G OG    1 
ATOM   11115 N  N     . LYS B 2 214  ? 165.290 109.534 123.475 1.00 77.23  ? 214  LYS G N     1 
ATOM   11116 C  CA    . LYS B 2 214  ? 164.626 108.616 124.385 1.00 78.36  ? 214  LYS G CA    1 
ATOM   11117 C  C     . LYS B 2 214  ? 163.346 108.115 123.735 1.00 75.78  ? 214  LYS G C     1 
ATOM   11118 O  O     . LYS B 2 214  ? 162.875 108.660 122.733 1.00 73.88  ? 214  LYS G O     1 
ATOM   11119 C  CB    . LYS B 2 214  ? 164.333 109.274 125.734 1.00 77.96  ? 214  LYS G CB    1 
ATOM   11120 C  CG    . LYS B 2 214  ? 164.390 108.309 126.900 1.00 81.48  ? 214  LYS G CG    1 
ATOM   11121 C  CD    . LYS B 2 214  ? 165.824 107.886 127.177 1.00 82.81  ? 214  LYS G CD    1 
ATOM   11122 C  CE    . LYS B 2 214  ? 166.637 109.029 127.758 1.00 81.64  ? 214  LYS G CE    1 
ATOM   11123 N  NZ    . LYS B 2 214  ? 166.201 109.372 129.136 1.00 87.30  ? 214  LYS G NZ    1 
ATOM   11124 N  N     . GLY B 2 215  ? 162.789 107.058 124.319 1.00 73.37  ? 215  GLY G N     1 
ATOM   11125 C  CA    . GLY B 2 215  ? 161.624 106.427 123.725 1.00 70.92  ? 215  GLY G CA    1 
ATOM   11126 C  C     . GLY B 2 215  ? 160.450 107.385 123.639 1.00 71.36  ? 215  GLY G C     1 
ATOM   11127 O  O     . GLY B 2 215  ? 160.239 108.227 124.515 1.00 71.31  ? 215  GLY G O     1 
ATOM   11128 N  N     . TYR B 2 216  ? 159.685 107.257 122.559 1.00 66.71  ? 216  TYR G N     1 
ATOM   11129 C  CA    . TYR B 2 216  ? 158.530 108.103 122.316 1.00 60.81  ? 216  TYR G CA    1 
ATOM   11130 C  C     . TYR B 2 216  ? 157.404 107.266 121.728 1.00 61.25  ? 216  TYR G C     1 
ATOM   11131 O  O     . TYR B 2 216  ? 157.613 106.153 121.240 1.00 64.12  ? 216  TYR G O     1 
ATOM   11132 C  CB    . TYR B 2 216  ? 158.886 109.284 121.403 1.00 59.85  ? 216  TYR G CB    1 
ATOM   11133 C  CG    . TYR B 2 216  ? 159.310 108.898 120.004 1.00 59.97  ? 216  TYR G CG    1 
ATOM   11134 C  CD1   . TYR B 2 216  ? 158.378 108.720 118.995 1.00 62.13  ? 216  TYR G CD1   1 
ATOM   11135 C  CD2   . TYR B 2 216  ? 160.650 108.733 119.693 1.00 60.50  ? 216  TYR G CD2   1 
ATOM   11136 C  CE1   . TYR B 2 216  ? 158.769 108.376 117.720 1.00 63.89  ? 216  TYR G CE1   1 
ATOM   11137 C  CE2   . TYR B 2 216  ? 161.049 108.391 118.423 1.00 59.77  ? 216  TYR G CE2   1 
ATOM   11138 C  CZ    . TYR B 2 216  ? 160.107 108.212 117.440 1.00 61.34  ? 216  TYR G CZ    1 
ATOM   11139 O  OH    . TYR B 2 216  ? 160.508 107.870 116.171 1.00 64.30  ? 216  TYR G OH    1 
ATOM   11140 N  N     . ASN B 2 217  ? 156.200 107.818 121.785 1.00 59.12  ? 217  ASN G N     1 
ATOM   11141 C  CA    . ASN B 2 217  ? 154.989 107.150 121.333 1.00 55.71  ? 217  ASN G CA    1 
ATOM   11142 C  C     . ASN B 2 217  ? 154.239 108.053 120.353 1.00 56.17  ? 217  ASN G C     1 
ATOM   11143 O  O     . ASN B 2 217  ? 154.759 109.066 119.879 1.00 57.17  ? 217  ASN G O     1 
ATOM   11144 C  CB    . ASN B 2 217  ? 154.118 106.756 122.527 1.00 56.89  ? 217  ASN G CB    1 
ATOM   11145 C  CG    . ASN B 2 217  ? 153.610 107.956 123.294 1.00 59.91  ? 217  ASN G CG    1 
ATOM   11146 O  OD1   . ASN B 2 217  ? 154.288 108.978 123.386 1.00 56.66  ? 217  ASN G OD1   1 
ATOM   11147 N  ND2   . ASN B 2 217  ? 152.412 107.837 123.854 1.00 58.02  ? 217  ASN G ND2   1 
ATOM   11148 N  N     . LYS B 2 218  ? 152.999 107.666 120.050 1.00 54.82  ? 218  LYS G N     1 
ATOM   11149 C  CA    . LYS B 2 218  ? 152.177 108.345 119.055 1.00 49.22  ? 218  LYS G CA    1 
ATOM   11150 C  C     . LYS B 2 218  ? 151.845 109.790 119.415 1.00 45.84  ? 218  LYS G C     1 
ATOM   11151 O  O     . LYS B 2 218  ? 151.179 110.464 118.623 1.00 43.18  ? 218  LYS G O     1 
ATOM   11152 C  CB    . LYS B 2 218  ? 150.889 107.551 118.845 1.00 47.02  ? 218  LYS G CB    1 
ATOM   11153 C  CG    . LYS B 2 218  ? 149.946 107.593 120.030 1.00 47.94  ? 218  LYS G CG    1 
ATOM   11154 C  CD    . LYS B 2 218  ? 148.734 106.705 119.809 1.00 51.70  ? 218  LYS G CD    1 
ATOM   11155 C  CE    . LYS B 2 218  ? 147.756 106.820 120.966 1.00 50.79  ? 218  LYS G CE    1 
ATOM   11156 N  NZ    . LYS B 2 218  ? 146.556 105.963 120.772 1.00 54.26  ? 218  LYS G NZ    1 
ATOM   11157 N  N     . ALA B 2 219  ? 152.275 110.281 120.579 1.00 47.96  ? 219  ALA G N     1 
ATOM   11158 C  CA    . ALA B 2 219  ? 151.986 111.660 120.962 1.00 43.25  ? 219  ALA G CA    1 
ATOM   11159 C  C     . ALA B 2 219  ? 152.719 112.684 120.103 1.00 40.90  ? 219  ALA G C     1 
ATOM   11160 O  O     . ALA B 2 219  ? 152.391 113.872 120.170 1.00 43.36  ? 219  ALA G O     1 
ATOM   11161 C  CB    . ALA B 2 219  ? 152.334 111.880 122.434 1.00 44.91  ? 219  ALA G CB    1 
ATOM   11162 N  N     . VAL B 2 220  ? 153.715 112.265 119.320 1.00 39.52  ? 220  VAL G N     1 
ATOM   11163 C  CA    . VAL B 2 220  ? 154.494 113.219 118.532 1.00 37.83  ? 220  VAL G CA    1 
ATOM   11164 C  C     . VAL B 2 220  ? 153.656 113.848 117.421 1.00 36.59  ? 220  VAL G C     1 
ATOM   11165 O  O     . VAL B 2 220  ? 153.920 114.986 116.999 1.00 39.99  ? 220  VAL G O     1 
ATOM   11166 C  CB    . VAL B 2 220  ? 155.757 112.534 117.976 1.00 40.22  ? 220  VAL G CB    1 
ATOM   11167 C  CG1   . VAL B 2 220  ? 156.641 112.063 119.112 1.00 44.35  ? 220  VAL G CG1   1 
ATOM   11168 C  CG2   . VAL B 2 220  ? 155.382 111.365 117.086 1.00 41.24  ? 220  VAL G CG2   1 
ATOM   11169 N  N     . ASP B 2 221  ? 152.640 113.134 116.929 1.00 33.85  ? 221  ASP G N     1 
ATOM   11170 C  CA    . ASP B 2 221  ? 151.840 113.653 115.826 1.00 30.61  ? 221  ASP G CA    1 
ATOM   11171 C  C     . ASP B 2 221  ? 151.017 114.860 116.244 1.00 30.39  ? 221  ASP G C     1 
ATOM   11172 O  O     . ASP B 2 221  ? 150.739 115.732 115.417 1.00 34.30  ? 221  ASP G O     1 
ATOM   11173 C  CB    . ASP B 2 221  ? 150.936 112.558 115.269 1.00 34.12  ? 221  ASP G CB    1 
ATOM   11174 C  CG    . ASP B 2 221  ? 151.719 111.417 114.663 1.00 42.32  ? 221  ASP G CG    1 
ATOM   11175 O  OD1   . ASP B 2 221  ? 152.840 111.666 114.182 1.00 42.78  ? 221  ASP G OD1   1 
ATOM   11176 O  OD2   . ASP B 2 221  ? 151.217 110.276 114.661 1.00 43.33  ? 221  ASP G OD2   1 
ATOM   11177 N  N     . TRP B 2 222  ? 150.647 114.953 117.518 1.00 27.72  ? 222  TRP G N     1 
ATOM   11178 C  CA    . TRP B 2 222  ? 149.924 116.132 117.977 1.00 25.08  ? 222  TRP G CA    1 
ATOM   11179 C  C     . TRP B 2 222  ? 150.835 117.348 118.086 1.00 26.92  ? 222  TRP G C     1 
ATOM   11180 O  O     . TRP B 2 222  ? 150.397 118.470 117.808 1.00 31.74  ? 222  TRP G O     1 
ATOM   11181 C  CB    . TRP B 2 222  ? 149.243 115.829 119.308 1.00 28.56  ? 222  TRP G CB    1 
ATOM   11182 C  CG    . TRP B 2 222  ? 148.334 114.638 119.219 1.00 34.21  ? 222  TRP G CG    1 
ATOM   11183 C  CD1   . TRP B 2 222  ? 148.438 113.473 119.918 1.00 37.08  ? 222  TRP G CD1   1 
ATOM   11184 C  CD2   . TRP B 2 222  ? 147.181 114.498 118.378 1.00 34.70  ? 222  TRP G CD2   1 
ATOM   11185 N  NE1   . TRP B 2 222  ? 147.426 112.615 119.562 1.00 34.04  ? 222  TRP G NE1   1 
ATOM   11186 C  CE2   . TRP B 2 222  ? 146.640 113.223 118.620 1.00 33.24  ? 222  TRP G CE2   1 
ATOM   11187 C  CE3   . TRP B 2 222  ? 146.555 115.330 117.445 1.00 29.87  ? 222  TRP G CE3   1 
ATOM   11188 C  CZ2   . TRP B 2 222  ? 145.503 112.758 117.964 1.00 36.25  ? 222  TRP G CZ2   1 
ATOM   11189 C  CZ3   . TRP B 2 222  ? 145.429 114.867 116.794 1.00 27.68  ? 222  TRP G CZ3   1 
ATOM   11190 C  CH2   . TRP B 2 222  ? 144.914 113.594 117.056 1.00 35.36  ? 222  TRP G CH2   1 
ATOM   11191 N  N     . TRP B 2 223  ? 152.101 117.145 118.454 1.00 25.43  ? 223  TRP G N     1 
ATOM   11192 C  CA    . TRP B 2 223  ? 153.079 118.227 118.389 1.00 25.00  ? 223  TRP G CA    1 
ATOM   11193 C  C     . TRP B 2 223  ? 153.257 118.702 116.952 1.00 25.58  ? 223  TRP G C     1 
ATOM   11194 O  O     . TRP B 2 223  ? 153.309 119.911 116.676 1.00 27.64  ? 223  TRP G O     1 
ATOM   11195 C  CB    . TRP B 2 223  ? 154.409 117.752 118.973 1.00 27.26  ? 223  TRP G CB    1 
ATOM   11196 C  CG    . TRP B 2 223  ? 155.488 118.782 118.959 1.00 28.92  ? 223  TRP G CG    1 
ATOM   11197 C  CD1   . TRP B 2 223  ? 156.296 119.110 117.912 1.00 32.37  ? 223  TRP G CD1   1 
ATOM   11198 C  CD2   . TRP B 2 223  ? 155.890 119.609 120.051 1.00 28.74  ? 223  TRP G CD2   1 
ATOM   11199 N  NE1   . TRP B 2 223  ? 157.168 120.101 118.283 1.00 33.39  ? 223  TRP G NE1   1 
ATOM   11200 C  CE2   . TRP B 2 223  ? 156.938 120.424 119.593 1.00 30.77  ? 223  TRP G CE2   1 
ATOM   11201 C  CE3   . TRP B 2 223  ? 155.460 119.744 121.372 1.00 30.60  ? 223  TRP G CE3   1 
ATOM   11202 C  CZ2   . TRP B 2 223  ? 157.564 121.359 120.408 1.00 32.09  ? 223  TRP G CZ2   1 
ATOM   11203 C  CZ3   . TRP B 2 223  ? 156.083 120.670 122.179 1.00 31.73  ? 223  TRP G CZ3   1 
ATOM   11204 C  CH2   . TRP B 2 223  ? 157.122 121.466 121.696 1.00 32.76  ? 223  TRP G CH2   1 
ATOM   11205 N  N     . ALA B 2 224  ? 153.344 117.752 116.017 1.00 24.47  ? 224  ALA G N     1 
ATOM   11206 C  CA    . ALA B 2 224  ? 153.434 118.113 114.607 1.00 26.14  ? 224  ALA G CA    1 
ATOM   11207 C  C     . ALA B 2 224  ? 152.196 118.867 114.135 1.00 27.33  ? 224  ALA G C     1 
ATOM   11208 O  O     . ALA B 2 224  ? 152.311 119.806 113.341 1.00 30.37  ? 224  ALA G O     1 
ATOM   11209 C  CB    . ALA B 2 224  ? 153.646 116.860 113.760 1.00 28.00  ? 224  ALA G CB    1 
ATOM   11210 N  N     . LEU B 2 225  ? 151.011 118.480 114.609 1.00 24.40  ? 225  LEU G N     1 
ATOM   11211 C  CA    . LEU B 2 225  ? 149.796 119.208 114.254 1.00 23.94  ? 225  LEU G CA    1 
ATOM   11212 C  C     . LEU B 2 225  ? 149.813 120.629 114.804 1.00 21.95  ? 225  LEU G C     1 
ATOM   11213 O  O     . LEU B 2 225  ? 149.381 121.567 114.124 1.00 26.06  ? 225  LEU G O     1 
ATOM   11214 C  CB    . LEU B 2 225  ? 148.563 118.463 114.757 1.00 24.92  ? 225  LEU G CB    1 
ATOM   11215 C  CG    . LEU B 2 225  ? 147.241 119.138 114.383 1.00 23.05  ? 225  LEU G CG    1 
ATOM   11216 C  CD1   . LEU B 2 225  ? 147.105 119.263 112.883 1.00 22.06  ? 225  LEU G CD1   1 
ATOM   11217 C  CD2   . LEU B 2 225  ? 146.060 118.393 114.960 1.00 25.24  ? 225  LEU G CD2   1 
ATOM   11218 N  N     . GLY B 2 226  ? 150.289 120.809 116.035 1.00 19.25  ? 226  GLY G N     1 
ATOM   11219 C  CA    . GLY B 2 226  ? 150.392 122.155 116.573 1.00 18.37  ? 226  GLY G CA    1 
ATOM   11220 C  C     . GLY B 2 226  ? 151.326 123.025 115.756 1.00 21.41  ? 226  GLY G C     1 
ATOM   11221 O  O     . GLY B 2 226  ? 151.016 124.186 115.462 1.00 24.35  ? 226  GLY G O     1 
ATOM   11222 N  N     . VAL B 2 227  ? 152.465 122.466 115.344 1.00 22.40  ? 227  VAL G N     1 
ATOM   11223 C  CA    . VAL B 2 227  ? 153.395 123.224 114.512 1.00 22.08  ? 227  VAL G CA    1 
ATOM   11224 C  C     . VAL B 2 227  ? 152.771 123.542 113.156 1.00 22.69  ? 227  VAL G C     1 
ATOM   11225 O  O     . VAL B 2 227  ? 152.946 124.644 112.620 1.00 26.28  ? 227  VAL G O     1 
ATOM   11226 C  CB    . VAL B 2 227  ? 154.725 122.464 114.365 1.00 22.37  ? 227  VAL G CB    1 
ATOM   11227 C  CG1   . VAL B 2 227  ? 155.639 123.188 113.402 1.00 25.14  ? 227  VAL G CG1   1 
ATOM   11228 C  CG2   . VAL B 2 227  ? 155.399 122.315 115.710 1.00 24.95  ? 227  VAL G CG2   1 
ATOM   11229 N  N     . LEU B 2 228  ? 152.039 122.588 112.576 1.00 22.15  ? 228  LEU G N     1 
ATOM   11230 C  CA    . LEU B 2 228  ? 151.393 122.823 111.287 1.00 20.23  ? 228  LEU G CA    1 
ATOM   11231 C  C     . LEU B 2 228  ? 150.370 123.947 111.376 1.00 21.63  ? 228  LEU G C     1 
ATOM   11232 O  O     . LEU B 2 228  ? 150.301 124.810 110.494 1.00 23.38  ? 228  LEU G O     1 
ATOM   11233 C  CB    . LEU B 2 228  ? 150.726 121.543 110.789 1.00 22.70  ? 228  LEU G CB    1 
ATOM   11234 C  CG    . LEU B 2 228  ? 150.196 121.577 109.354 1.00 25.15  ? 228  LEU G CG    1 
ATOM   11235 C  CD1   . LEU B 2 228  ? 151.330 121.672 108.363 1.00 29.85  ? 228  LEU G CD1   1 
ATOM   11236 C  CD2   . LEU B 2 228  ? 149.337 120.367 109.060 1.00 29.51  ? 228  LEU G CD2   1 
ATOM   11237 N  N     . ILE B 2 229  ? 149.550 123.943 112.428 1.00 21.16  ? 229  ILE G N     1 
ATOM   11238 C  CA    . ILE B 2 229  ? 148.549 124.993 112.590 1.00 18.32  ? 229  ILE G CA    1 
ATOM   11239 C  C     . ILE B 2 229  ? 149.218 126.346 112.785 1.00 21.44  ? 229  ILE G C     1 
ATOM   11240 O  O     . ILE B 2 229  ? 148.790 127.356 112.208 1.00 22.61  ? 229  ILE G O     1 
ATOM   11241 C  CB    . ILE B 2 229  ? 147.599 124.661 113.754 1.00 19.46  ? 229  ILE G CB    1 
ATOM   11242 C  CG1   . ILE B 2 229  ? 146.684 123.494 113.388 1.00 20.17  ? 229  ILE G CG1   1 
ATOM   11243 C  CG2   . ILE B 2 229  ? 146.775 125.871 114.127 1.00 21.12  ? 229  ILE G CG2   1 
ATOM   11244 C  CD1   . ILE B 2 229  ? 145.949 122.914 114.570 1.00 17.74  ? 229  ILE G CD1   1 
ATOM   11245 N  N     . TYR B 2 230  ? 150.278 126.392 113.597 1.00 22.85  ? 230  TYR G N     1 
ATOM   11246 C  CA    . TYR B 2 230  ? 150.988 127.651 113.798 1.00 20.85  ? 230  TYR G CA    1 
ATOM   11247 C  C     . TYR B 2 230  ? 151.533 128.178 112.478 1.00 24.71  ? 230  TYR G C     1 
ATOM   11248 O  O     . TYR B 2 230  ? 151.419 129.371 112.178 1.00 28.83  ? 230  TYR G O     1 
ATOM   11249 C  CB    . TYR B 2 230  ? 152.117 127.465 114.812 1.00 19.80  ? 230  TYR G CB    1 
ATOM   11250 C  CG    . TYR B 2 230  ? 152.857 128.738 115.177 1.00 22.89  ? 230  TYR G CG    1 
ATOM   11251 C  CD1   . TYR B 2 230  ? 153.777 129.308 114.310 1.00 25.29  ? 230  TYR G CD1   1 
ATOM   11252 C  CD2   . TYR B 2 230  ? 152.652 129.352 116.400 1.00 25.36  ? 230  TYR G CD2   1 
ATOM   11253 C  CE1   . TYR B 2 230  ? 154.450 130.459 114.639 1.00 25.99  ? 230  TYR G CE1   1 
ATOM   11254 C  CE2   . TYR B 2 230  ? 153.327 130.502 116.739 1.00 25.75  ? 230  TYR G CE2   1 
ATOM   11255 C  CZ    . TYR B 2 230  ? 154.225 131.050 115.854 1.00 27.24  ? 230  TYR G CZ    1 
ATOM   11256 O  OH    . TYR B 2 230  ? 154.900 132.198 116.186 1.00 32.16  ? 230  TYR G OH    1 
ATOM   11257 N  N     . GLU B 2 231  ? 152.135 127.300 111.672 1.00 26.11  ? 231  GLU G N     1 
ATOM   11258 C  CA    . GLU B 2 231  ? 152.718 127.755 110.415 1.00 25.77  ? 231  GLU G CA    1 
ATOM   11259 C  C     . GLU B 2 231  ? 151.652 128.178 109.412 1.00 25.52  ? 231  GLU G C     1 
ATOM   11260 O  O     . GLU B 2 231  ? 151.857 129.141 108.668 1.00 29.25  ? 231  GLU G O     1 
ATOM   11261 C  CB    . GLU B 2 231  ? 153.606 126.668 109.819 1.00 29.21  ? 231  GLU G CB    1 
ATOM   11262 C  CG    . GLU B 2 231  ? 154.190 127.029 108.472 1.00 31.72  ? 231  GLU G CG    1 
ATOM   11263 C  CD    . GLU B 2 231  ? 155.375 126.167 108.109 1.00 41.73  ? 231  GLU G CD    1 
ATOM   11264 O  OE1   . GLU B 2 231  ? 156.008 125.613 109.031 1.00 47.32  ? 231  GLU G OE1   1 
ATOM   11265 O  OE2   . GLU B 2 231  ? 155.678 126.048 106.905 1.00 47.53  ? 231  GLU G OE2   1 
ATOM   11266 N  N     . MET B 2 232  ? 150.512 127.482 109.371 1.00 26.56  ? 232  MET G N     1 
ATOM   11267 C  CA    . MET B 2 232  ? 149.431 127.916 108.492 1.00 25.44  ? 232  MET G CA    1 
ATOM   11268 C  C     . MET B 2 232  ? 148.920 129.293 108.888 1.00 26.24  ? 232  MET G C     1 
ATOM   11269 O  O     . MET B 2 232  ? 148.709 130.155 108.029 1.00 28.41  ? 232  MET G O     1 
ATOM   11270 C  CB    . MET B 2 232  ? 148.280 126.912 108.515 1.00 23.86  ? 232  MET G CB    1 
ATOM   11271 C  CG    . MET B 2 232  ? 148.542 125.611 107.799 1.00 27.03  ? 232  MET G CG    1 
ATOM   11272 S  SD    . MET B 2 232  ? 146.998 124.761 107.432 1.00 40.65  ? 232  MET G SD    1 
ATOM   11273 C  CE    . MET B 2 232  ? 146.656 123.979 109.003 1.00 25.92  ? 232  MET G CE    1 
ATOM   11274 N  N     . ALA B 2 233  ? 148.724 129.523 110.188 1.00 24.13  ? 233  ALA G N     1 
ATOM   11275 C  CA    . ALA B 2 233  ? 148.129 130.779 110.625 1.00 22.76  ? 233  ALA G CA    1 
ATOM   11276 C  C     . ALA B 2 233  ? 149.102 131.949 110.547 1.00 26.33  ? 233  ALA G C     1 
ATOM   11277 O  O     . ALA B 2 233  ? 148.681 133.073 110.256 1.00 29.59  ? 233  ALA G O     1 
ATOM   11278 C  CB    . ALA B 2 233  ? 147.591 130.637 112.048 1.00 25.66  ? 233  ALA G CB    1 
ATOM   11279 N  N     . ALA B 2 234  ? 150.391 131.719 110.795 1.00 26.65  ? 234  ALA G N     1 
ATOM   11280 C  CA    . ALA B 2 234  ? 151.376 132.795 110.805 1.00 26.23  ? 234  ALA G CA    1 
ATOM   11281 C  C     . ALA B 2 234  ? 152.188 132.897 109.522 1.00 30.25  ? 234  ALA G C     1 
ATOM   11282 O  O     . ALA B 2 234  ? 152.616 133.997 109.164 1.00 34.39  ? 234  ALA G O     1 
ATOM   11283 C  CB    . ALA B 2 234  ? 152.335 132.630 111.987 1.00 28.20  ? 234  ALA G CB    1 
ATOM   11284 N  N     . GLY B 2 235  ? 152.416 131.787 108.825 1.00 32.30  ? 235  GLY G N     1 
ATOM   11285 C  CA    . GLY B 2 235  ? 153.204 131.787 107.611 1.00 28.39  ? 235  GLY G CA    1 
ATOM   11286 C  C     . GLY B 2 235  ? 154.659 131.417 107.785 1.00 33.47  ? 235  GLY G C     1 
ATOM   11287 O  O     . GLY B 2 235  ? 155.376 131.319 106.783 1.00 39.27  ? 235  GLY G O     1 
ATOM   11288 N  N     . TYR B 2 236  ? 155.119 131.218 109.017 1.00 36.20  ? 236  TYR G N     1 
ATOM   11289 C  CA    . TYR B 2 236  ? 156.487 130.809 109.301 1.00 34.44  ? 236  TYR G CA    1 
ATOM   11290 C  C     . TYR B 2 236  ? 156.489 129.924 110.537 1.00 34.74  ? 236  TYR G C     1 
ATOM   11291 O  O     . TYR B 2 236  ? 155.644 130.102 111.423 1.00 36.01  ? 236  TYR G O     1 
ATOM   11292 C  CB    . TYR B 2 236  ? 157.406 132.027 109.488 1.00 31.72  ? 236  TYR G CB    1 
ATOM   11293 C  CG    . TYR B 2 236  ? 156.957 132.997 110.555 1.00 34.27  ? 236  TYR G CG    1 
ATOM   11294 C  CD1   . TYR B 2 236  ? 157.338 132.836 111.878 1.00 37.27  ? 236  TYR G CD1   1 
ATOM   11295 C  CD2   . TYR B 2 236  ? 156.161 134.085 110.233 1.00 33.43  ? 236  TYR G CD2   1 
ATOM   11296 C  CE1   . TYR B 2 236  ? 156.929 133.723 112.849 1.00 33.82  ? 236  TYR G CE1   1 
ATOM   11297 C  CE2   . TYR B 2 236  ? 155.750 134.977 111.198 1.00 35.98  ? 236  TYR G CE2   1 
ATOM   11298 C  CZ    . TYR B 2 236  ? 156.136 134.791 112.504 1.00 35.71  ? 236  TYR G CZ    1 
ATOM   11299 O  OH    . TYR B 2 236  ? 155.729 135.678 113.470 1.00 40.38  ? 236  TYR G OH    1 
ATOM   11300 N  N     . PRO B 2 237  ? 157.413 128.963 110.628 1.00 36.25  ? 237  PRO G N     1 
ATOM   11301 C  CA    . PRO B 2 237  ? 157.342 127.977 111.707 1.00 34.90  ? 237  PRO G CA    1 
ATOM   11302 C  C     . PRO B 2 237  ? 157.625 128.611 113.055 1.00 34.83  ? 237  PRO G C     1 
ATOM   11303 O  O     . PRO B 2 237  ? 158.292 129.658 113.140 1.00 38.52  ? 237  PRO G O     1 
ATOM   11304 C  CB    . PRO B 2 237  ? 158.428 126.954 111.328 1.00 35.97  ? 237  PRO G CB    1 
ATOM   11305 C  CG    . PRO B 2 237  ? 159.348 127.685 110.426 1.00 37.51  ? 237  PRO G CG    1 
ATOM   11306 C  CD    . PRO B 2 237  ? 158.510 128.680 109.687 1.00 38.83  ? 237  PRO G CD    1 
ATOM   11307 N  N     . PRO B 2 238  ? 157.126 128.021 114.148 1.00 31.87  ? 238  PRO G N     1 
ATOM   11308 C  CA    . PRO B 2 238  ? 157.388 128.600 115.474 1.00 30.44  ? 238  PRO G CA    1 
ATOM   11309 C  C     . PRO B 2 238  ? 158.843 128.532 115.905 1.00 38.35  ? 238  PRO G C     1 
ATOM   11310 O  O     . PRO B 2 238  ? 159.293 129.415 116.643 1.00 39.04  ? 238  PRO G O     1 
ATOM   11311 C  CB    . PRO B 2 238  ? 156.484 127.776 116.399 1.00 29.40  ? 238  PRO G CB    1 
ATOM   11312 C  CG    . PRO B 2 238  ? 156.328 126.477 115.711 1.00 27.44  ? 238  PRO G CG    1 
ATOM   11313 C  CD    . PRO B 2 238  ? 156.338 126.780 114.235 1.00 31.10  ? 238  PRO G CD    1 
ATOM   11314 N  N     . PHE B 2 239  ? 159.592 127.518 115.478 1.00 43.24  ? 239  PHE G N     1 
ATOM   11315 C  CA    . PHE B 2 239  ? 161.000 127.358 115.841 1.00 41.37  ? 239  PHE G CA    1 
ATOM   11316 C  C     . PHE B 2 239  ? 161.827 127.520 114.571 1.00 51.03  ? 239  PHE G C     1 
ATOM   11317 O  O     . PHE B 2 239  ? 161.888 126.608 113.742 1.00 50.79  ? 239  PHE G O     1 
ATOM   11318 C  CB    . PHE B 2 239  ? 161.254 126.004 116.498 1.00 39.76  ? 239  PHE G CB    1 
ATOM   11319 C  CG    . PHE B 2 239  ? 160.341 125.708 117.648 1.00 38.96  ? 239  PHE G CG    1 
ATOM   11320 C  CD1   . PHE B 2 239  ? 160.438 126.425 118.824 1.00 37.46  ? 239  PHE G CD1   1 
ATOM   11321 C  CD2   . PHE B 2 239  ? 159.385 124.713 117.553 1.00 38.56  ? 239  PHE G CD2   1 
ATOM   11322 C  CE1   . PHE B 2 239  ? 159.605 126.158 119.882 1.00 38.98  ? 239  PHE G CE1   1 
ATOM   11323 C  CE2   . PHE B 2 239  ? 158.547 124.442 118.610 1.00 36.46  ? 239  PHE G CE2   1 
ATOM   11324 C  CZ    . PHE B 2 239  ? 158.658 125.166 119.777 1.00 36.25  ? 239  PHE G CZ    1 
ATOM   11325 N  N     . PHE B 2 240  ? 162.469 128.676 114.420 1.00 61.79  ? 240  PHE G N     1 
ATOM   11326 C  CA    . PHE B 2 240  ? 163.171 129.027 113.190 1.00 67.11  ? 240  PHE G CA    1 
ATOM   11327 C  C     . PHE B 2 240  ? 164.570 129.497 113.565 1.00 73.51  ? 240  PHE G C     1 
ATOM   11328 O  O     . PHE B 2 240  ? 164.734 130.594 114.108 1.00 75.60  ? 240  PHE G O     1 
ATOM   11329 C  CB    . PHE B 2 240  ? 162.409 130.113 112.423 1.00 63.76  ? 240  PHE G CB    1 
ATOM   11330 C  CG    . PHE B 2 240  ? 163.010 130.471 111.084 1.00 69.66  ? 240  PHE G CG    1 
ATOM   11331 C  CD1   . PHE B 2 240  ? 162.458 131.492 110.327 1.00 71.58  ? 240  PHE G CD1   1 
ATOM   11332 C  CD2   . PHE B 2 240  ? 164.074 129.759 110.554 1.00 70.25  ? 240  PHE G CD2   1 
ATOM   11333 C  CE1   . PHE B 2 240  ? 162.984 131.822 109.094 1.00 75.50  ? 240  PHE G CE1   1 
ATOM   11334 C  CE2   . PHE B 2 240  ? 164.604 130.085 109.324 1.00 71.14  ? 240  PHE G CE2   1 
ATOM   11335 C  CZ    . PHE B 2 240  ? 164.058 131.115 108.591 1.00 73.69  ? 240  PHE G CZ    1 
ATOM   11336 N  N     . ALA B 2 241  ? 165.570 128.669 113.280 1.00 74.57  ? 241  ALA G N     1 
ATOM   11337 C  CA    . ALA B 2 241  ? 166.967 129.053 113.400 1.00 78.62  ? 241  ALA G CA    1 
ATOM   11338 C  C     . ALA B 2 241  ? 167.704 128.630 112.139 1.00 82.82  ? 241  ALA G C     1 
ATOM   11339 O  O     . ALA B 2 241  ? 167.303 127.683 111.458 1.00 82.41  ? 241  ALA G O     1 
ATOM   11340 C  CB    . ALA B 2 241  ? 167.629 128.434 114.636 1.00 80.74  ? 241  ALA G CB    1 
ATOM   11341 N  N     . ASP B 2 242  ? 168.788 129.345 111.830 1.00 86.82  ? 242  ASP G N     1 
ATOM   11342 C  CA    . ASP B 2 242  ? 169.498 129.102 110.580 1.00 90.88  ? 242  ASP G CA    1 
ATOM   11343 C  C     . ASP B 2 242  ? 170.304 127.811 110.596 1.00 86.61  ? 242  ASP G C     1 
ATOM   11344 O  O     . ASP B 2 242  ? 170.665 127.310 109.526 1.00 84.42  ? 242  ASP G O     1 
ATOM   11345 C  CB    . ASP B 2 242  ? 170.421 130.277 110.258 1.00 96.11  ? 242  ASP G CB    1 
ATOM   11346 C  CG    . ASP B 2 242  ? 170.769 130.349 108.788 1.00 99.55  ? 242  ASP G CG    1 
ATOM   11347 O  OD1   . ASP B 2 242  ? 169.852 130.203 107.953 1.00 102.84 ? 242  ASP G OD1   1 
ATOM   11348 O  OD2   . ASP B 2 242  ? 171.960 130.541 108.466 1.00 94.95  ? 242  ASP G OD2   1 
ATOM   11349 N  N     . GLN B 2 243  ? 170.597 127.262 111.771 1.00 85.29  ? 243  GLN G N     1 
ATOM   11350 C  CA    . GLN B 2 243  ? 171.376 126.044 111.870 1.00 89.24  ? 243  GLN G CA    1 
ATOM   11351 C  C     . GLN B 2 243  ? 170.561 124.957 112.555 1.00 86.49  ? 243  GLN G C     1 
ATOM   11352 O  O     . GLN B 2 243  ? 169.885 125.234 113.556 1.00 85.04  ? 243  GLN G O     1 
ATOM   11353 C  CB    . GLN B 2 243  ? 172.682 126.282 112.645 1.00 93.09  ? 243  GLN G CB    1 
ATOM   11354 C  CG    . GLN B 2 243  ? 173.691 127.147 111.908 1.00 95.17  ? 243  GLN G CG    1 
ATOM   11355 C  CD    . GLN B 2 243  ? 174.146 126.529 110.598 1.00 96.66  ? 243  GLN G CD    1 
ATOM   11356 O  OE1   . GLN B 2 243  ? 174.172 125.308 110.450 1.00 95.37  ? 243  GLN G OE1   1 
ATOM   11357 N  NE2   . GLN B 2 243  ? 174.510 127.374 109.641 1.00 93.39  ? 243  GLN G NE2   1 
ATOM   11358 N  N     . PRO B 2 244  ? 170.585 123.722 112.045 1.00 86.05  ? 244  PRO G N     1 
ATOM   11359 C  CA    . PRO B 2 244  ? 169.832 122.638 112.697 1.00 83.25  ? 244  PRO G CA    1 
ATOM   11360 C  C     . PRO B 2 244  ? 170.184 122.441 114.162 1.00 83.36  ? 244  PRO G C     1 
ATOM   11361 O  O     . PRO B 2 244  ? 169.300 122.111 114.963 1.00 81.56  ? 244  PRO G O     1 
ATOM   11362 C  CB    . PRO B 2 244  ? 170.208 121.410 111.858 1.00 83.97  ? 244  PRO G CB    1 
ATOM   11363 C  CG    . PRO B 2 244  ? 170.519 121.965 110.516 1.00 84.67  ? 244  PRO G CG    1 
ATOM   11364 C  CD    . PRO B 2 244  ? 171.191 123.286 110.778 1.00 85.75  ? 244  PRO G CD    1 
ATOM   11365 N  N     . ILE B 2 245  ? 171.451 122.626 114.538 1.00 85.49  ? 245  ILE G N     1 
ATOM   11366 C  CA    . ILE B 2 245  ? 171.831 122.448 115.936 1.00 86.98  ? 245  ILE G CA    1 
ATOM   11367 C  C     . ILE B 2 245  ? 171.224 123.543 116.804 1.00 84.44  ? 245  ILE G C     1 
ATOM   11368 O  O     . ILE B 2 245  ? 170.916 123.311 117.980 1.00 81.73  ? 245  ILE G O     1 
ATOM   11369 C  CB    . ILE B 2 245  ? 173.366 122.385 116.077 1.00 92.73  ? 245  ILE G CB    1 
ATOM   11370 C  CG1   . ILE B 2 245  ? 173.759 121.868 117.464 1.00 92.73  ? 245  ILE G CG1   1 
ATOM   11371 C  CG2   . ILE B 2 245  ? 174.005 123.736 115.797 1.00 86.76  ? 245  ILE G CG2   1 
ATOM   11372 C  CD1   . ILE B 2 245  ? 175.095 121.156 117.499 1.00 84.94  ? 245  ILE G CD1   1 
ATOM   11373 N  N     . GLN B 2 246  ? 171.035 124.743 116.252 1.00 81.81  ? 246  GLN G N     1 
ATOM   11374 C  CA    . GLN B 2 246  ? 170.408 125.820 117.009 1.00 81.92  ? 246  GLN G CA    1 
ATOM   11375 C  C     . GLN B 2 246  ? 168.897 125.643 117.108 1.00 78.81  ? 246  GLN G C     1 
ATOM   11376 O  O     . GLN B 2 246  ? 168.283 126.124 118.066 1.00 75.01  ? 246  GLN G O     1 
ATOM   11377 C  CB    . GLN B 2 246  ? 170.745 127.169 116.374 1.00 85.76  ? 246  GLN G CB    1 
ATOM   11378 C  CG    . GLN B 2 246  ? 172.133 127.684 116.728 1.00 93.00  ? 246  GLN G CG    1 
ATOM   11379 C  CD    . GLN B 2 246  ? 172.390 129.088 116.216 1.00 102.15 ? 246  GLN G CD    1 
ATOM   11380 O  OE1   . GLN B 2 246  ? 172.494 129.312 115.009 1.00 100.31 ? 246  GLN G OE1   1 
ATOM   11381 N  NE2   . GLN B 2 246  ? 172.496 130.043 117.134 1.00 100.45 ? 246  GLN G NE2   1 
ATOM   11382 N  N     . ILE B 2 247  ? 168.288 124.970 116.129 1.00 77.12  ? 247  ILE G N     1 
ATOM   11383 C  CA    . ILE B 2 247  ? 166.850 124.716 116.169 1.00 70.06  ? 247  ILE G CA    1 
ATOM   11384 C  C     . ILE B 2 247  ? 166.502 123.806 117.341 1.00 68.94  ? 247  ILE G C     1 
ATOM   11385 O  O     . ILE B 2 247  ? 165.455 123.964 117.985 1.00 71.05  ? 247  ILE G O     1 
ATOM   11386 C  CB    . ILE B 2 247  ? 166.382 124.124 114.826 1.00 69.58  ? 247  ILE G CB    1 
ATOM   11387 C  CG1   . ILE B 2 247  ? 166.507 125.164 113.715 1.00 72.18  ? 247  ILE G CG1   1 
ATOM   11388 C  CG2   . ILE B 2 247  ? 164.955 123.630 114.914 1.00 61.09  ? 247  ILE G CG2   1 
ATOM   11389 C  CD1   . ILE B 2 247  ? 166.299 124.603 112.331 1.00 74.35  ? 247  ILE G CD1   1 
ATOM   11390 N  N     . TYR B 2 248  ? 167.373 122.837 117.634 1.00 65.79  ? 248  TYR G N     1 
ATOM   11391 C  CA    . TYR B 2 248  ? 167.107 121.903 118.722 1.00 63.51  ? 248  TYR G CA    1 
ATOM   11392 C  C     . TYR B 2 248  ? 167.063 122.603 120.071 1.00 63.89  ? 248  TYR G C     1 
ATOM   11393 O  O     . TYR B 2 248  ? 166.255 122.234 120.927 1.00 66.00  ? 248  TYR G O     1 
ATOM   11394 C  CB    . TYR B 2 248  ? 168.152 120.788 118.739 1.00 67.59  ? 248  TYR G CB    1 
ATOM   11395 C  CG    . TYR B 2 248  ? 168.048 119.809 117.587 1.00 73.00  ? 248  TYR G CG    1 
ATOM   11396 C  CD1   . TYR B 2 248  ? 167.112 119.987 116.577 1.00 71.37  ? 248  TYR G CD1   1 
ATOM   11397 C  CD2   . TYR B 2 248  ? 168.879 118.701 117.518 1.00 70.43  ? 248  TYR G CD2   1 
ATOM   11398 C  CE1   . TYR B 2 248  ? 167.014 119.095 115.529 1.00 72.39  ? 248  TYR G CE1   1 
ATOM   11399 C  CE2   . TYR B 2 248  ? 168.788 117.804 116.475 1.00 67.72  ? 248  TYR G CE2   1 
ATOM   11400 C  CZ    . TYR B 2 248  ? 167.854 118.005 115.483 1.00 72.54  ? 248  TYR G CZ    1 
ATOM   11401 O  OH    . TYR B 2 248  ? 167.759 117.113 114.440 1.00 72.47  ? 248  TYR G OH    1 
ATOM   11402 N  N     . GLU B 2 249  ? 167.915 123.605 120.286 1.00 63.92  ? 249  GLU G N     1 
ATOM   11403 C  CA    . GLU B 2 249  ? 167.876 124.321 121.556 1.00 67.00  ? 249  GLU G CA    1 
ATOM   11404 C  C     . GLU B 2 249  ? 166.575 125.091 121.725 1.00 64.83  ? 249  GLU G C     1 
ATOM   11405 O  O     . GLU B 2 249  ? 166.021 125.136 122.830 1.00 64.94  ? 249  GLU G O     1 
ATOM   11406 C  CB    . GLU B 2 249  ? 169.076 125.259 121.670 1.00 69.59  ? 249  GLU G CB    1 
ATOM   11407 C  CG    . GLU B 2 249  ? 170.362 124.561 122.079 1.00 70.18  ? 249  GLU G CG    1 
ATOM   11408 C  CD    . GLU B 2 249  ? 170.116 123.214 122.738 1.00 75.03  ? 249  GLU G CD    1 
ATOM   11409 O  OE1   . GLU B 2 249  ? 169.613 123.188 123.882 1.00 72.21  ? 249  GLU G OE1   1 
ATOM   11410 O  OE2   . GLU B 2 249  ? 170.412 122.179 122.104 1.00 78.15  ? 249  GLU G OE2   1 
ATOM   11411 N  N     . LYS B 2 250  ? 166.061 125.679 120.645 1.00 62.61  ? 250  LYS G N     1 
ATOM   11412 C  CA    . LYS B 2 250  ? 164.776 126.363 120.721 1.00 58.84  ? 250  LYS G CA    1 
ATOM   11413 C  C     . LYS B 2 250  ? 163.643 125.376 120.962 1.00 57.36  ? 250  LYS G C     1 
ATOM   11414 O  O     . LYS B 2 250  ? 162.688 125.686 121.682 1.00 60.44  ? 250  LYS G O     1 
ATOM   11415 C  CB    . LYS B 2 250  ? 164.527 127.165 119.445 1.00 57.63  ? 250  LYS G CB    1 
ATOM   11416 C  CG    . LYS B 2 250  ? 165.514 128.293 119.226 1.00 59.85  ? 250  LYS G CG    1 
ATOM   11417 C  CD    . LYS B 2 250  ? 165.089 129.191 118.080 1.00 63.93  ? 250  LYS G CD    1 
ATOM   11418 C  CE    . LYS B 2 250  ? 166.062 130.343 117.898 1.00 73.14  ? 250  LYS G CE    1 
ATOM   11419 N  NZ    . LYS B 2 250  ? 165.591 131.318 116.878 1.00 79.80  ? 250  LYS G NZ    1 
ATOM   11420 N  N     . ILE B 2 251  ? 163.721 124.188 120.359 1.00 53.46  ? 251  ILE G N     1 
ATOM   11421 C  CA    . ILE B 2 251  ? 162.662 123.203 120.562 1.00 49.42  ? 251  ILE G CA    1 
ATOM   11422 C  C     . ILE B 2 251  ? 162.664 122.699 121.999 1.00 55.58  ? 251  ILE G C     1 
ATOM   11423 O  O     . ILE B 2 251  ? 161.611 122.625 122.644 1.00 56.24  ? 251  ILE G O     1 
ATOM   11424 C  CB    . ILE B 2 251  ? 162.793 122.046 119.557 1.00 46.32  ? 251  ILE G CB    1 
ATOM   11425 C  CG1   . ILE B 2 251  ? 162.428 122.514 118.150 1.00 47.79  ? 251  ILE G CG1   1 
ATOM   11426 C  CG2   . ILE B 2 251  ? 161.901 120.896 119.960 1.00 44.52  ? 251  ILE G CG2   1 
ATOM   11427 C  CD1   . ILE B 2 251  ? 162.810 121.538 117.076 1.00 48.80  ? 251  ILE G CD1   1 
ATOM   11428 N  N     . VAL B 2 252  ? 163.841 122.358 122.533 1.00 59.01  ? 252  VAL G N     1 
ATOM   11429 C  CA    . VAL B 2 252  ? 163.909 121.855 123.904 1.00 55.76  ? 252  VAL G CA    1 
ATOM   11430 C  C     . VAL B 2 252  ? 163.549 122.945 124.904 1.00 57.76  ? 252  VAL G C     1 
ATOM   11431 O  O     . VAL B 2 252  ? 162.942 122.663 125.945 1.00 56.97  ? 252  VAL G O     1 
ATOM   11432 C  CB    . VAL B 2 252  ? 165.293 121.250 124.197 1.00 56.68  ? 252  VAL G CB    1 
ATOM   11433 C  CG1   . VAL B 2 252  ? 165.296 120.588 125.561 1.00 60.03  ? 252  VAL G CG1   1 
ATOM   11434 C  CG2   . VAL B 2 252  ? 165.650 120.223 123.143 1.00 55.00  ? 252  VAL G CG2   1 
ATOM   11435 N  N     . SER B 2 253  ? 163.905 124.200 124.619 1.00 58.27  ? 253  SER G N     1 
ATOM   11436 C  CA    . SER B 2 253  ? 163.438 125.296 125.461 1.00 60.92  ? 253  SER G CA    1 
ATOM   11437 C  C     . SER B 2 253  ? 161.917 125.378 125.457 1.00 65.89  ? 253  SER G C     1 
ATOM   11438 O  O     . SER B 2 253  ? 161.298 125.641 126.495 1.00 64.53  ? 253  SER G O     1 
ATOM   11439 C  CB    . SER B 2 253  ? 164.047 126.617 124.996 1.00 62.00  ? 253  SER G CB    1 
ATOM   11440 O  OG    . SER B 2 253  ? 163.575 127.693 125.786 1.00 66.38  ? 253  SER G OG    1 
ATOM   11441 N  N     . GLY B 2 254  ? 161.298 125.149 124.301 1.00 61.87  ? 254  GLY G N     1 
ATOM   11442 C  CA    . GLY B 2 254  ? 159.850 125.135 124.208 1.00 61.52  ? 254  GLY G CA    1 
ATOM   11443 C  C     . GLY B 2 254  ? 159.184 126.471 124.441 1.00 58.20  ? 254  GLY G C     1 
ATOM   11444 O  O     . GLY B 2 254  ? 158.037 126.513 124.894 1.00 57.52  ? 254  GLY G O     1 
ATOM   11445 N  N     . LYS B 2 255  ? 159.871 127.568 124.142 1.00 58.49  ? 255  LYS G N     1 
ATOM   11446 C  CA    . LYS B 2 255  ? 159.347 128.913 124.351 1.00 58.59  ? 255  LYS G CA    1 
ATOM   11447 C  C     . LYS B 2 255  ? 158.929 129.488 123.002 1.00 57.18  ? 255  LYS G C     1 
ATOM   11448 O  O     . LYS B 2 255  ? 159.762 129.651 122.105 1.00 58.70  ? 255  LYS G O     1 
ATOM   11449 C  CB    . LYS B 2 255  ? 160.394 129.793 125.028 1.00 58.47  ? 255  LYS G CB    1 
ATOM   11450 C  CG    . LYS B 2 255  ? 159.840 131.054 125.648 1.00 61.56  ? 255  LYS G CG    1 
ATOM   11451 C  CD    . LYS B 2 255  ? 160.949 131.859 126.296 1.00 67.23  ? 255  LYS G CD    1 
ATOM   11452 C  CE    . LYS B 2 255  ? 161.742 132.626 125.252 1.00 72.90  ? 255  LYS G CE    1 
ATOM   11453 N  NZ    . LYS B 2 255  ? 162.818 133.459 125.857 1.00 69.71  ? 255  LYS G NZ    1 
ATOM   11454 N  N     . VAL B 2 256  ? 157.641 129.793 122.860 1.00 52.94  ? 256  VAL G N     1 
ATOM   11455 C  CA    . VAL B 2 256  ? 157.095 130.343 121.626 1.00 48.52  ? 256  VAL G CA    1 
ATOM   11456 C  C     . VAL B 2 256  ? 156.424 131.674 121.928 1.00 41.20  ? 256  VAL G C     1 
ATOM   11457 O  O     . VAL B 2 256  ? 155.966 131.923 123.048 1.00 44.11  ? 256  VAL G O     1 
ATOM   11458 C  CB    . VAL B 2 256  ? 156.096 129.377 120.954 1.00 44.55  ? 256  VAL G CB    1 
ATOM   11459 C  CG1   . VAL B 2 256  ? 156.794 128.111 120.519 1.00 43.41  ? 256  VAL G CG1   1 
ATOM   11460 C  CG2   . VAL B 2 256  ? 154.961 129.054 121.904 1.00 41.20  ? 256  VAL G CG2   1 
ATOM   11461 N  N     . ARG B 2 257  ? 156.376 132.536 120.918 1.00 37.39  ? 257  ARG G N     1 
ATOM   11462 C  CA    . ARG B 2 257  ? 155.618 133.774 120.978 1.00 38.46  ? 257  ARG G CA    1 
ATOM   11463 C  C     . ARG B 2 257  ? 154.679 133.852 119.784 1.00 38.53  ? 257  ARG G C     1 
ATOM   11464 O  O     . ARG B 2 257  ? 155.009 133.405 118.682 1.00 43.38  ? 257  ARG G O     1 
ATOM   11465 C  CB    . ARG B 2 257  ? 156.529 135.004 121.011 1.00 40.39  ? 257  ARG G CB    1 
ATOM   11466 C  CG    . ARG B 2 257  ? 157.493 135.126 119.855 1.00 45.11  ? 257  ARG G CG    1 
ATOM   11467 C  CD    . ARG B 2 257  ? 157.832 136.586 119.615 1.00 54.15  ? 257  ARG G CD    1 
ATOM   11468 N  NE    . ARG B 2 257  ? 156.640 137.422 119.686 1.00 61.38  ? 257  ARG G NE    1 
ATOM   11469 C  CZ    . ARG B 2 257  ? 156.594 138.624 120.244 1.00 63.25  ? 257  ARG G CZ    1 
ATOM   11470 N  NH1   . ARG B 2 257  ? 157.665 139.170 120.796 1.00 61.88  ? 257  ARG G NH1   1 
ATOM   11471 N  NH2   . ARG B 2 257  ? 155.445 139.292 120.250 1.00 55.48  ? 257  ARG G NH2   1 
ATOM   11472 N  N     . PHE B 2 258  ? 153.503 134.421 120.015 1.00 35.26  ? 258  PHE G N     1 
ATOM   11473 C  CA    . PHE B 2 258  ? 152.464 134.391 119.000 1.00 32.57  ? 258  PHE G CA    1 
ATOM   11474 C  C     . PHE B 2 258  ? 152.329 135.741 118.309 1.00 38.25  ? 258  PHE G C     1 
ATOM   11475 O  O     . PHE B 2 258  ? 152.540 136.785 118.935 1.00 42.87  ? 258  PHE G O     1 
ATOM   11476 C  CB    . PHE B 2 258  ? 151.124 134.003 119.623 1.00 31.16  ? 258  PHE G CB    1 
ATOM   11477 C  CG    . PHE B 2 258  ? 151.152 132.688 120.344 1.00 30.15  ? 258  PHE G CG    1 
ATOM   11478 C  CD1   . PHE B 2 258  ? 151.189 131.500 119.640 1.00 31.03  ? 258  PHE G CD1   1 
ATOM   11479 C  CD2   . PHE B 2 258  ? 151.145 132.639 121.726 1.00 28.51  ? 258  PHE G CD2   1 
ATOM   11480 C  CE1   . PHE B 2 258  ? 151.217 130.293 120.300 1.00 30.28  ? 258  PHE G CE1   1 
ATOM   11481 C  CE2   . PHE B 2 258  ? 151.171 131.433 122.387 1.00 25.29  ? 258  PHE G CE2   1 
ATOM   11482 C  CZ    . PHE B 2 258  ? 151.207 130.260 121.674 1.00 24.62  ? 258  PHE G CZ    1 
ATOM   11483 N  N     . PRO B 2 259  ? 152.001 135.736 117.019 1.00 36.11  ? 259  PRO G N     1 
ATOM   11484 C  CA    . PRO B 2 259  ? 151.723 136.993 116.319 1.00 33.20  ? 259  PRO G CA    1 
ATOM   11485 C  C     . PRO B 2 259  ? 150.534 137.725 116.927 1.00 37.98  ? 259  PRO G C     1 
ATOM   11486 O  O     . PRO B 2 259  ? 149.632 137.118 117.506 1.00 36.66  ? 259  PRO G O     1 
ATOM   11487 C  CB    . PRO B 2 259  ? 151.433 136.542 114.885 1.00 33.24  ? 259  PRO G CB    1 
ATOM   11488 C  CG    . PRO B 2 259  ? 152.141 135.241 114.760 1.00 32.80  ? 259  PRO G CG    1 
ATOM   11489 C  CD    . PRO B 2 259  ? 152.018 134.590 116.099 1.00 32.46  ? 259  PRO G CD    1 
ATOM   11490 N  N     . SER B 2 260  ? 150.548 139.053 116.788 1.00 41.96  ? 260  SER G N     1 
ATOM   11491 C  CA    . SER B 2 260  ? 149.522 139.894 117.394 1.00 41.34  ? 260  SER G CA    1 
ATOM   11492 C  C     . SER B 2 260  ? 148.127 139.627 116.843 1.00 40.91  ? 260  SER G C     1 
ATOM   11493 O  O     . SER B 2 260  ? 147.140 139.952 117.510 1.00 47.72  ? 260  SER G O     1 
ATOM   11494 C  CB    . SER B 2 260  ? 149.882 141.367 117.197 1.00 37.40  ? 260  SER G CB    1 
ATOM   11495 O  OG    . SER B 2 260  ? 150.900 141.765 118.097 1.00 41.33  ? 260  SER G OG    1 
ATOM   11496 N  N     . HIS B 2 261  ? 148.014 139.055 115.648 1.00 35.00  ? 261  HIS G N     1 
ATOM   11497 C  CA    . HIS B 2 261  ? 146.713 138.795 115.047 1.00 33.51  ? 261  HIS G CA    1 
ATOM   11498 C  C     . HIS B 2 261  ? 146.116 137.452 115.454 1.00 37.56  ? 261  HIS G C     1 
ATOM   11499 O  O     . HIS B 2 261  ? 145.017 137.120 114.999 1.00 39.92  ? 261  HIS G O     1 
ATOM   11500 C  CB    . HIS B 2 261  ? 146.808 138.894 113.521 1.00 34.94  ? 261  HIS G CB    1 
ATOM   11501 C  CG    . HIS B 2 261  ? 147.639 137.820 112.892 1.00 37.46  ? 261  HIS G CG    1 
ATOM   11502 N  ND1   . HIS B 2 261  ? 148.993 137.959 112.675 1.00 37.47  ? 261  HIS G ND1   1 
ATOM   11503 C  CD2   . HIS B 2 261  ? 147.307 136.595 112.419 1.00 35.33  ? 261  HIS G CD2   1 
ATOM   11504 C  CE1   . HIS B 2 261  ? 149.460 136.863 112.104 1.00 34.81  ? 261  HIS G CE1   1 
ATOM   11505 N  NE2   . HIS B 2 261  ? 148.457 136.020 111.938 1.00 32.92  ? 261  HIS G NE2   1 
ATOM   11506 N  N     . PHE B 2 262  ? 146.809 136.673 116.282 1.00 35.37  ? 262  PHE G N     1 
ATOM   11507 C  CA    . PHE B 2 262  ? 146.251 135.427 116.794 1.00 33.44  ? 262  PHE G CA    1 
ATOM   11508 C  C     . PHE B 2 262  ? 145.147 135.698 117.810 1.00 35.46  ? 262  PHE G C     1 
ATOM   11509 O  O     . PHE B 2 262  ? 145.250 136.609 118.636 1.00 38.32  ? 262  PHE G O     1 
ATOM   11510 C  CB    . PHE B 2 262  ? 147.348 134.577 117.438 1.00 33.19  ? 262  PHE G CB    1 
ATOM   11511 C  CG    . PHE B 2 262  ? 148.128 133.740 116.465 1.00 31.65  ? 262  PHE G CG    1 
ATOM   11512 C  CD1   . PHE B 2 262  ? 148.366 134.181 115.178 1.00 32.70  ? 262  PHE G CD1   1 
ATOM   11513 C  CD2   . PHE B 2 262  ? 148.630 132.508 116.846 1.00 29.18  ? 262  PHE G CD2   1 
ATOM   11514 C  CE1   . PHE B 2 262  ? 149.080 133.410 114.287 1.00 30.62  ? 262  PHE G CE1   1 
ATOM   11515 C  CE2   . PHE B 2 262  ? 149.347 131.733 115.957 1.00 26.23  ? 262  PHE G CE2   1 
ATOM   11516 C  CZ    . PHE B 2 262  ? 149.572 132.185 114.677 1.00 25.83  ? 262  PHE G CZ    1 
ATOM   11517 N  N     . SER B 2 263  ? 144.084 134.902 117.742 1.00 32.28  ? 263  SER G N     1 
ATOM   11518 C  CA    . SER B 2 263  ? 142.992 134.986 118.701 1.00 27.53  ? 263  SER G CA    1 
ATOM   11519 C  C     . SER B 2 263  ? 143.322 134.201 119.970 1.00 31.59  ? 263  SER G C     1 
ATOM   11520 O  O     . SER B 2 263  ? 144.260 133.403 120.011 1.00 37.04  ? 263  SER G O     1 
ATOM   11521 C  CB    . SER B 2 263  ? 141.694 134.470 118.083 1.00 29.53  ? 263  SER G CB    1 
ATOM   11522 O  OG    . SER B 2 263  ? 141.718 133.063 117.942 1.00 31.42  ? 263  SER G OG    1 
ATOM   11523 N  N     . SER B 2 264  ? 142.537 134.454 121.023 1.00 31.78  ? 264  SER G N     1 
ATOM   11524 C  CA    . SER B 2 264  ? 142.766 133.786 122.302 1.00 31.68  ? 264  SER G CA    1 
ATOM   11525 C  C     . SER B 2 264  ? 142.531 132.282 122.221 1.00 35.51  ? 264  SER G C     1 
ATOM   11526 O  O     . SER B 2 264  ? 143.282 131.506 122.825 1.00 38.98  ? 264  SER G O     1 
ATOM   11527 C  CB    . SER B 2 264  ? 141.874 134.397 123.383 1.00 39.27  ? 264  SER G CB    1 
ATOM   11528 O  OG    . SER B 2 264  ? 142.439 135.590 123.896 1.00 50.24  ? 264  SER G OG    1 
ATOM   11529 N  N     . ASP B 2 265  ? 141.499 131.851 121.491 1.00 35.92  ? 265  ASP G N     1 
ATOM   11530 C  CA    . ASP B 2 265  ? 141.224 130.421 121.375 1.00 32.54  ? 265  ASP G CA    1 
ATOM   11531 C  C     . ASP B 2 265  ? 142.347 129.703 120.642 1.00 30.35  ? 265  ASP G C     1 
ATOM   11532 O  O     . ASP B 2 265  ? 142.755 128.604 121.038 1.00 32.70  ? 265  ASP G O     1 
ATOM   11533 C  CB    . ASP B 2 265  ? 139.895 130.199 120.658 1.00 36.60  ? 265  ASP G CB    1 
ATOM   11534 C  CG    . ASP B 2 265  ? 138.773 131.011 121.254 1.00 46.49  ? 265  ASP G CG    1 
ATOM   11535 O  OD1   . ASP B 2 265  ? 138.882 131.387 122.438 1.00 49.35  ? 265  ASP G OD1   1 
ATOM   11536 O  OD2   . ASP B 2 265  ? 137.787 131.280 120.539 1.00 50.42  ? 265  ASP G OD2   1 
ATOM   11537 N  N     . LEU B 2 266  ? 142.861 130.313 119.576 1.00 25.48  ? 266  LEU G N     1 
ATOM   11538 C  CA    . LEU B 2 266  ? 143.974 129.717 118.852 1.00 24.30  ? 266  LEU G CA    1 
ATOM   11539 C  C     . LEU B 2 266  ? 145.216 129.635 119.727 1.00 27.83  ? 266  LEU G C     1 
ATOM   11540 O  O     . LEU B 2 266  ? 145.927 128.625 119.709 1.00 31.70  ? 266  LEU G O     1 
ATOM   11541 C  CB    . LEU B 2 266  ? 144.253 130.517 117.582 1.00 23.49  ? 266  LEU G CB    1 
ATOM   11542 C  CG    . LEU B 2 266  ? 145.333 129.988 116.644 1.00 23.60  ? 266  LEU G CG    1 
ATOM   11543 C  CD1   . LEU B 2 266  ? 144.993 128.587 116.183 1.00 22.80  ? 266  LEU G CD1   1 
ATOM   11544 C  CD2   . LEU B 2 266  ? 145.496 130.914 115.457 1.00 24.94  ? 266  LEU G CD2   1 
ATOM   11545 N  N     . LYS B 2 267  ? 145.491 130.686 120.503 1.00 27.39  ? 267  LYS G N     1 
ATOM   11546 C  CA    . LYS B 2 267  ? 146.642 130.657 121.398 1.00 26.87  ? 267  LYS G CA    1 
ATOM   11547 C  C     . LYS B 2 267  ? 146.506 129.560 122.443 1.00 29.09  ? 267  LYS G C     1 
ATOM   11548 O  O     . LYS B 2 267  ? 147.476 128.855 122.739 1.00 30.78  ? 267  LYS G O     1 
ATOM   11549 C  CB    . LYS B 2 267  ? 146.826 132.013 122.074 1.00 28.35  ? 267  LYS G CB    1 
ATOM   11550 C  CG    . LYS B 2 267  ? 147.314 133.105 121.156 1.00 31.07  ? 267  LYS G CG    1 
ATOM   11551 C  CD    . LYS B 2 267  ? 147.870 134.262 121.954 1.00 33.18  ? 267  LYS G CD    1 
ATOM   11552 C  CE    . LYS B 2 267  ? 147.511 135.590 121.329 1.00 38.02  ? 267  LYS G CE    1 
ATOM   11553 N  NZ    . LYS B 2 267  ? 146.100 135.955 121.613 1.00 40.56  ? 267  LYS G NZ    1 
ATOM   11554 N  N     . ASP B 2 268  ? 145.314 129.406 123.023 1.00 28.74  ? 268  ASP G N     1 
ATOM   11555 C  CA    . ASP B 2 268  ? 145.103 128.360 124.021 1.00 29.30  ? 268  ASP G CA    1 
ATOM   11556 C  C     . ASP B 2 268  ? 145.278 126.971 123.413 1.00 30.19  ? 268  ASP G C     1 
ATOM   11557 O  O     . ASP B 2 268  ? 145.934 126.098 123.999 1.00 32.45  ? 268  ASP G O     1 
ATOM   11558 C  CB    . ASP B 2 268  ? 143.717 128.515 124.645 1.00 31.13  ? 268  ASP G CB    1 
ATOM   11559 C  CG    . ASP B 2 268  ? 143.489 127.562 125.795 1.00 40.34  ? 268  ASP G CG    1 
ATOM   11560 O  OD1   . ASP B 2 268  ? 144.236 127.646 126.791 1.00 44.04  ? 268  ASP G OD1   1 
ATOM   11561 O  OD2   . ASP B 2 268  ? 142.561 126.733 125.708 1.00 40.81  ? 268  ASP G OD2   1 
ATOM   11562 N  N     . LEU B 2 269  ? 144.706 126.753 122.227 1.00 27.09  ? 269  LEU G N     1 
ATOM   11563 C  CA    . LEU B 2 269  ? 144.868 125.468 121.555 1.00 24.98  ? 269  LEU G CA    1 
ATOM   11564 C  C     . LEU B 2 269  ? 146.332 125.174 121.266 1.00 26.81  ? 269  LEU G C     1 
ATOM   11565 O  O     . LEU B 2 269  ? 146.801 124.051 121.483 1.00 29.03  ? 269  LEU G O     1 
ATOM   11566 C  CB    . LEU B 2 269  ? 144.060 125.447 120.259 1.00 26.44  ? 269  LEU G CB    1 
ATOM   11567 C  CG    . LEU B 2 269  ? 144.080 124.137 119.473 1.00 22.31  ? 269  LEU G CG    1 
ATOM   11568 C  CD1   . LEU B 2 269  ? 143.555 122.989 120.311 1.00 23.13  ? 269  LEU G CD1   1 
ATOM   11569 C  CD2   . LEU B 2 269  ? 143.286 124.279 118.191 1.00 20.67  ? 269  LEU G CD2   1 
ATOM   11570 N  N     . LEU B 2 270  ? 147.071 126.170 120.773 1.00 27.23  ? 270  LEU G N     1 
ATOM   11571 C  CA    . LEU B 2 270  ? 148.471 125.950 120.437 1.00 23.03  ? 270  LEU G CA    1 
ATOM   11572 C  C     . LEU B 2 270  ? 149.322 125.734 121.679 1.00 25.53  ? 270  LEU G C     1 
ATOM   11573 O  O     . LEU B 2 270  ? 150.286 124.965 121.635 1.00 29.39  ? 270  LEU G O     1 
ATOM   11574 C  CB    . LEU B 2 270  ? 149.007 127.122 119.618 1.00 21.76  ? 270  LEU G CB    1 
ATOM   11575 C  CG    . LEU B 2 270  ? 148.485 127.169 118.181 1.00 22.24  ? 270  LEU G CG    1 
ATOM   11576 C  CD1   . LEU B 2 270  ? 148.912 128.451 117.488 1.00 22.85  ? 270  LEU G CD1   1 
ATOM   11577 C  CD2   . LEU B 2 270  ? 148.935 125.948 117.403 1.00 21.45  ? 270  LEU G CD2   1 
ATOM   11578 N  N     . ARG B 2 271  ? 148.993 126.399 122.788 1.00 24.36  ? 271  ARG G N     1 
ATOM   11579 C  CA    . ARG B 2 271  ? 149.706 126.130 124.031 1.00 26.60  ? 271  ARG G CA    1 
ATOM   11580 C  C     . ARG B 2 271  ? 149.462 124.707 124.507 1.00 29.96  ? 271  ARG G C     1 
ATOM   11581 O  O     . ARG B 2 271  ? 150.383 124.046 124.999 1.00 34.92  ? 271  ARG G O     1 
ATOM   11582 C  CB    . ARG B 2 271  ? 149.304 127.124 125.120 1.00 27.16  ? 271  ARG G CB    1 
ATOM   11583 C  CG    . ARG B 2 271  ? 149.831 128.525 124.927 1.00 28.55  ? 271  ARG G CG    1 
ATOM   11584 C  CD    . ARG B 2 271  ? 149.628 129.347 126.184 1.00 27.17  ? 271  ARG G CD    1 
ATOM   11585 N  NE    . ARG B 2 271  ? 149.847 130.770 125.960 1.00 29.82  ? 271  ARG G NE    1 
ATOM   11586 C  CZ    . ARG B 2 271  ? 148.892 131.634 125.654 1.00 29.85  ? 271  ARG G CZ    1 
ATOM   11587 N  NH1   . ARG B 2 271  ? 147.630 131.257 125.550 1.00 32.19  ? 271  ARG G NH1   1 
ATOM   11588 N  NH2   . ARG B 2 271  ? 149.210 132.908 125.450 1.00 30.40  ? 271  ARG G NH2   1 
ATOM   11589 N  N     . ASN B 2 272  ? 148.230 124.217 124.375 1.00 29.28  ? 272  ASN G N     1 
ATOM   11590 C  CA    . ASN B 2 272  ? 147.949 122.856 124.818 1.00 27.15  ? 272  ASN G CA    1 
ATOM   11591 C  C     . ASN B 2 272  ? 148.509 121.805 123.867 1.00 26.47  ? 272  ASN G C     1 
ATOM   11592 O  O     . ASN B 2 272  ? 148.761 120.672 124.290 1.00 31.39  ? 272  ASN G O     1 
ATOM   11593 C  CB    . ASN B 2 272  ? 146.447 122.663 124.997 1.00 29.70  ? 272  ASN G CB    1 
ATOM   11594 C  CG    . ASN B 2 272  ? 145.939 123.274 126.280 1.00 31.71  ? 272  ASN G CG    1 
ATOM   11595 O  OD1   . ASN B 2 272  ? 146.142 122.729 127.362 1.00 34.03  ? 272  ASN G OD1   1 
ATOM   11596 N  ND2   . ASN B 2 272  ? 145.279 124.417 126.168 1.00 32.34  ? 272  ASN G ND2   1 
ATOM   11597 N  N     . LEU B 2 273  ? 148.701 122.146 122.592 1.00 25.81  ? 273  LEU G N     1 
ATOM   11598 C  CA    . LEU B 2 273  ? 149.284 121.190 121.654 1.00 23.88  ? 273  LEU G CA    1 
ATOM   11599 C  C     . LEU B 2 273  ? 150.806 121.193 121.717 1.00 26.85  ? 273  LEU G C     1 
ATOM   11600 O  O     . LEU B 2 273  ? 151.432 120.129 121.679 1.00 30.50  ? 273  LEU G O     1 
ATOM   11601 C  CB    . LEU B 2 273  ? 148.813 121.487 120.232 1.00 20.39  ? 273  LEU G CB    1 
ATOM   11602 C  CG    . LEU B 2 273  ? 147.397 121.044 119.869 1.00 20.11  ? 273  LEU G CG    1 
ATOM   11603 C  CD1   . LEU B 2 273  ? 147.014 121.590 118.513 1.00 19.39  ? 273  LEU G CD1   1 
ATOM   11604 C  CD2   . LEU B 2 273  ? 147.290 119.535 119.881 1.00 20.58  ? 273  LEU G CD2   1 
ATOM   11605 N  N     . LEU B 2 274  ? 151.417 122.368 121.813 1.00 26.67  ? 274  LEU G N     1 
ATOM   11606 C  CA    . LEU B 2 274  ? 152.871 122.475 121.927 1.00 25.13  ? 274  LEU G CA    1 
ATOM   11607 C  C     . LEU B 2 274  ? 153.314 122.421 123.384 1.00 32.68  ? 274  LEU G C     1 
ATOM   11608 O  O     . LEU B 2 274  ? 153.990 123.314 123.889 1.00 37.33  ? 274  LEU G O     1 
ATOM   11609 C  CB    . LEU B 2 274  ? 153.359 123.750 121.252 1.00 23.85  ? 274  LEU G CB    1 
ATOM   11610 C  CG    . LEU B 2 274  ? 153.077 123.882 119.757 1.00 20.47  ? 274  LEU G CG    1 
ATOM   11611 C  CD1   . LEU B 2 274  ? 153.435 125.270 119.264 1.00 20.20  ? 274  LEU G CD1   1 
ATOM   11612 C  CD2   . LEU B 2 274  ? 153.846 122.829 118.993 1.00 24.34  ? 274  LEU G CD2   1 
ATOM   11613 N  N     . GLN B 2 275  ? 152.923 121.350 124.067 1.00 36.94  ? 275  GLN G N     1 
ATOM   11614 C  CA    . GLN B 2 275  ? 153.236 121.145 125.473 1.00 38.53  ? 275  GLN G CA    1 
ATOM   11615 C  C     . GLN B 2 275  ? 154.465 120.251 125.583 1.00 44.92  ? 275  GLN G C     1 
ATOM   11616 O  O     . GLN B 2 275  ? 154.460 119.120 125.085 1.00 43.15  ? 275  GLN G O     1 
ATOM   11617 C  CB    . GLN B 2 275  ? 152.049 120.519 126.202 1.00 38.95  ? 275  GLN G CB    1 
ATOM   11618 C  CG    . GLN B 2 275  ? 152.232 120.403 127.696 1.00 48.14  ? 275  GLN G CG    1 
ATOM   11619 C  CD    . GLN B 2 275  ? 152.139 121.740 128.390 1.00 54.21  ? 275  GLN G CD    1 
ATOM   11620 O  OE1   . GLN B 2 275  ? 151.105 122.405 128.342 1.00 51.74  ? 275  GLN G OE1   1 
ATOM   11621 N  NE2   . GLN B 2 275  ? 153.223 122.148 129.037 1.00 55.68  ? 275  GLN G NE2   1 
ATOM   11622 N  N     . VAL B 2 276  ? 155.515 120.764 126.229 1.00 49.26  ? 276  VAL G N     1 
ATOM   11623 C  CA    . VAL B 2 276  ? 156.747 119.994 126.386 1.00 48.41  ? 276  VAL G CA    1 
ATOM   11624 C  C     . VAL B 2 276  ? 156.498 118.753 127.232 1.00 51.75  ? 276  VAL G C     1 
ATOM   11625 O  O     . VAL B 2 276  ? 156.959 117.654 126.900 1.00 52.97  ? 276  VAL G O     1 
ATOM   11626 C  CB    . VAL B 2 276  ? 157.856 120.878 126.985 1.00 46.96  ? 276  VAL G CB    1 
ATOM   11627 C  CG1   . VAL B 2 276  ? 159.033 120.027 127.432 1.00 51.76  ? 276  VAL G CG1   1 
ATOM   11628 C  CG2   . VAL B 2 276  ? 158.305 121.924 125.979 1.00 44.11  ? 276  VAL G CG2   1 
ATOM   11629 N  N     . ASP B 2 277  ? 155.762 118.903 128.329 1.00 52.04  ? 277  ASP G N     1 
ATOM   11630 C  CA    . ASP B 2 277  ? 155.451 117.780 129.209 1.00 53.07  ? 277  ASP G CA    1 
ATOM   11631 C  C     . ASP B 2 277  ? 154.436 116.874 128.522 1.00 53.82  ? 277  ASP G C     1 
ATOM   11632 O  O     . ASP B 2 277  ? 153.254 117.216 128.427 1.00 54.51  ? 277  ASP G O     1 
ATOM   11633 C  CB    . ASP B 2 277  ? 154.916 118.298 130.541 1.00 58.67  ? 277  ASP G CB    1 
ATOM   11634 C  CG    . ASP B 2 277  ? 154.831 117.218 131.599 1.00 63.28  ? 277  ASP G CG    1 
ATOM   11635 O  OD1   . ASP B 2 277  ? 155.261 116.077 131.328 1.00 64.16  ? 277  ASP G OD1   1 
ATOM   11636 O  OD2   . ASP B 2 277  ? 154.334 117.511 132.705 1.00 60.03  ? 277  ASP G OD2   1 
ATOM   11637 N  N     . LEU B 2 278  ? 154.892 115.715 128.041 1.00 52.61  ? 278  LEU G N     1 
ATOM   11638 C  CA    . LEU B 2 278  ? 154.032 114.857 127.233 1.00 53.15  ? 278  LEU G CA    1 
ATOM   11639 C  C     . LEU B 2 278  ? 152.897 114.239 128.038 1.00 53.25  ? 278  LEU G C     1 
ATOM   11640 O  O     . LEU B 2 278  ? 151.947 113.721 127.442 1.00 59.67  ? 278  LEU G O     1 
ATOM   11641 C  CB    . LEU B 2 278  ? 154.866 113.770 126.545 1.00 51.37  ? 278  LEU G CB    1 
ATOM   11642 C  CG    . LEU B 2 278  ? 155.239 112.459 127.241 1.00 58.03  ? 278  LEU G CG    1 
ATOM   11643 C  CD1   . LEU B 2 278  ? 154.190 111.376 127.026 1.00 57.53  ? 278  LEU G CD1   1 
ATOM   11644 C  CD2   . LEU B 2 278  ? 156.598 111.987 126.754 1.00 53.62  ? 278  LEU G CD2   1 
ATOM   11645 N  N     . THR B 2 279  ? 152.969 114.272 129.368 1.00 52.00  ? 279  THR G N     1 
ATOM   11646 C  CA    . THR B 2 279  ? 151.840 113.831 130.179 1.00 56.25  ? 279  THR G CA    1 
ATOM   11647 C  C     . THR B 2 279  ? 150.714 114.854 130.214 1.00 58.12  ? 279  THR G C     1 
ATOM   11648 O  O     . THR B 2 279  ? 149.625 114.534 130.702 1.00 62.94  ? 279  THR G O     1 
ATOM   11649 C  CB    . THR B 2 279  ? 152.292 113.525 131.608 1.00 60.53  ? 279  THR G CB    1 
ATOM   11650 O  OG1   . THR B 2 279  ? 152.367 114.742 132.358 1.00 59.13  ? 279  THR G OG1   1 
ATOM   11651 C  CG2   . THR B 2 279  ? 153.655 112.853 131.607 1.00 58.47  ? 279  THR G CG2   1 
ATOM   11652 N  N     . LYS B 2 280  ? 150.949 116.065 129.715 1.00 55.62  ? 280  LYS G N     1 
ATOM   11653 C  CA    . LYS B 2 280  ? 149.971 117.143 129.742 1.00 55.52  ? 280  LYS G CA    1 
ATOM   11654 C  C     . LYS B 2 280  ? 149.508 117.558 128.353 1.00 54.96  ? 280  LYS G C     1 
ATOM   11655 O  O     . LYS B 2 280  ? 148.700 118.485 128.236 1.00 56.28  ? 280  LYS G O     1 
ATOM   11656 C  CB    . LYS B 2 280  ? 150.558 118.354 130.471 1.00 57.81  ? 280  LYS G CB    1 
ATOM   11657 C  CG    . LYS B 2 280  ? 150.857 118.102 131.938 1.00 62.96  ? 280  LYS G CG    1 
ATOM   11658 C  CD    . LYS B 2 280  ? 151.301 119.371 132.641 1.00 63.43  ? 280  LYS G CD    1 
ATOM   11659 C  CE    . LYS B 2 280  ? 150.152 120.347 132.791 1.00 67.15  ? 280  LYS G CE    1 
ATOM   11660 N  NZ    . LYS B 2 280  ? 150.560 121.547 133.565 1.00 68.34  ? 280  LYS G NZ    1 
ATOM   11661 N  N     . ARG B 2 281  ? 150.003 116.910 127.304 1.00 51.62  ? 281  ARG G N     1 
ATOM   11662 C  CA    . ARG B 2 281  ? 149.693 117.301 125.937 1.00 42.98  ? 281  ARG G CA    1 
ATOM   11663 C  C     . ARG B 2 281  ? 148.339 116.755 125.502 1.00 44.17  ? 281  ARG G C     1 
ATOM   11664 O  O     . ARG B 2 281  ? 147.971 115.628 125.841 1.00 48.93  ? 281  ARG G O     1 
ATOM   11665 C  CB    . ARG B 2 281  ? 150.794 116.810 124.996 1.00 40.45  ? 281  ARG G CB    1 
ATOM   11666 C  CG    . ARG B 2 281  ? 150.714 117.349 123.585 1.00 35.65  ? 281  ARG G CG    1 
ATOM   11667 C  CD    . ARG B 2 281  ? 151.803 116.752 122.718 1.00 33.62  ? 281  ARG G CD    1 
ATOM   11668 N  NE    . ARG B 2 281  ? 153.127 116.980 123.282 1.00 38.92  ? 281  ARG G NE    1 
ATOM   11669 C  CZ    . ARG B 2 281  ? 154.171 116.188 123.089 1.00 43.85  ? 281  ARG G CZ    1 
ATOM   11670 N  NH1   . ARG B 2 281  ? 154.082 115.095 122.351 1.00 44.12  ? 281  ARG G NH1   1 
ATOM   11671 N  NH2   . ARG B 2 281  ? 155.335 116.500 123.650 1.00 40.67  ? 281  ARG G NH2   1 
ATOM   11672 N  N     . PHE B 2 282  ? 147.597 117.571 124.754 1.00 43.17  ? 282  PHE G N     1 
ATOM   11673 C  CA    . PHE B 2 282  ? 146.293 117.164 124.241 1.00 40.29  ? 282  PHE G CA    1 
ATOM   11674 C  C     . PHE B 2 282  ? 146.419 115.966 123.311 1.00 42.54  ? 282  PHE G C     1 
ATOM   11675 O  O     . PHE B 2 282  ? 147.406 115.819 122.587 1.00 44.79  ? 282  PHE G O     1 
ATOM   11676 C  CB    . PHE B 2 282  ? 145.631 118.326 123.503 1.00 34.54  ? 282  PHE G CB    1 
ATOM   11677 C  CG    . PHE B 2 282  ? 144.812 119.216 124.386 1.00 35.40  ? 282  PHE G CG    1 
ATOM   11678 C  CD1   . PHE B 2 282  ? 145.084 119.310 125.736 1.00 37.34  ? 282  PHE G CD1   1 
ATOM   11679 C  CD2   . PHE B 2 282  ? 143.782 119.974 123.861 1.00 34.81  ? 282  PHE G CD2   1 
ATOM   11680 C  CE1   . PHE B 2 282  ? 144.338 120.132 126.550 1.00 35.53  ? 282  PHE G CE1   1 
ATOM   11681 C  CE2   . PHE B 2 282  ? 143.032 120.798 124.669 1.00 35.96  ? 282  PHE G CE2   1 
ATOM   11682 C  CZ    . PHE B 2 282  ? 143.310 120.877 126.017 1.00 34.87  ? 282  PHE G CZ    1 
ATOM   11683 N  N     . GLY B 2 283  ? 145.406 115.102 123.338 1.00 42.80  ? 283  GLY G N     1 
ATOM   11684 C  CA    . GLY B 2 283  ? 145.406 113.884 122.566 1.00 46.60  ? 283  GLY G CA    1 
ATOM   11685 C  C     . GLY B 2 283  ? 146.036 112.701 123.264 1.00 54.77  ? 283  GLY G C     1 
ATOM   11686 O  O     . GLY B 2 283  ? 145.683 111.557 122.959 1.00 59.99  ? 283  GLY G O     1 
ATOM   11687 N  N     . ASN B 2 284  ? 146.957 112.947 124.192 1.00 55.24  ? 284  ASN G N     1 
ATOM   11688 C  CA    . ASN B 2 284  ? 147.558 111.913 125.021 1.00 56.54  ? 284  ASN G CA    1 
ATOM   11689 C  C     . ASN B 2 284  ? 146.873 111.781 126.372 1.00 59.46  ? 284  ASN G C     1 
ATOM   11690 O  O     . ASN B 2 284  ? 147.232 110.896 127.152 1.00 60.03  ? 284  ASN G O     1 
ATOM   11691 C  CB    . ASN B 2 284  ? 149.047 112.208 125.223 1.00 52.99  ? 284  ASN G CB    1 
ATOM   11692 C  CG    . ASN B 2 284  ? 149.853 110.964 125.536 1.00 63.51  ? 284  ASN G CG    1 
ATOM   11693 O  OD1   . ASN B 2 284  ? 149.599 109.890 124.993 1.00 68.59  ? 284  ASN G OD1   1 
ATOM   11694 N  ND2   . ASN B 2 284  ? 150.835 111.105 126.417 1.00 61.17  ? 284  ASN G ND2   1 
ATOM   11695 N  N     . LEU B 2 285  ? 145.900 112.639 126.663 1.00 63.02  ? 285  LEU G N     1 
ATOM   11696 C  CA    . LEU B 2 285  ? 145.236 112.648 127.954 1.00 63.08  ? 285  LEU G CA    1 
ATOM   11697 C  C     . LEU B 2 285  ? 144.161 111.567 128.019 1.00 66.87  ? 285  LEU G C     1 
ATOM   11698 O  O     . LEU B 2 285  ? 143.998 110.745 127.114 1.00 65.70  ? 285  LEU G O     1 
ATOM   11699 C  CB    . LEU B 2 285  ? 144.645 114.024 128.240 1.00 60.82  ? 285  LEU G CB    1 
ATOM   11700 C  CG    . LEU B 2 285  ? 145.652 115.165 128.366 1.00 55.56  ? 285  LEU G CG    1 
ATOM   11701 C  CD1   . LEU B 2 285  ? 144.943 116.474 128.655 1.00 52.20  ? 285  LEU G CD1   1 
ATOM   11702 C  CD2   . LEU B 2 285  ? 146.662 114.850 129.448 1.00 56.41  ? 285  LEU G CD2   1 
ATOM   11703 N  N     . LYS B 2 286  ? 143.423 111.574 129.131 1.00 72.34  ? 286  LYS G N     1 
ATOM   11704 C  CA    . LYS B 2 286  ? 142.433 110.537 129.400 1.00 75.91  ? 286  LYS G CA    1 
ATOM   11705 C  C     . LYS B 2 286  ? 141.276 110.576 128.406 1.00 73.19  ? 286  LYS G C     1 
ATOM   11706 O  O     . LYS B 2 286  ? 140.684 109.533 128.107 1.00 69.53  ? 286  LYS G O     1 
ATOM   11707 C  CB    . LYS B 2 286  ? 141.906 110.655 130.838 1.00 76.75  ? 286  LYS G CB    1 
ATOM   11708 C  CG    . LYS B 2 286  ? 142.626 111.647 131.783 1.00 78.57  ? 286  LYS G CG    1 
ATOM   11709 C  CD    . LYS B 2 286  ? 144.127 111.368 131.966 1.00 78.39  ? 286  LYS G CD    1 
ATOM   11710 C  CE    . LYS B 2 286  ? 144.815 112.482 132.742 1.00 73.37  ? 286  LYS G CE    1 
ATOM   11711 N  NZ    . LYS B 2 286  ? 146.284 112.259 132.866 1.00 71.76  ? 286  LYS G NZ    1 
ATOM   11712 N  N     . ASN B 2 287  ? 140.934 111.758 127.891 1.00 71.32  ? 287  ASN G N     1 
ATOM   11713 C  CA    . ASN B 2 287  ? 139.840 111.890 126.936 1.00 70.18  ? 287  ASN G CA    1 
ATOM   11714 C  C     . ASN B 2 287  ? 140.218 111.474 125.520 1.00 66.16  ? 287  ASN G C     1 
ATOM   11715 O  O     . ASN B 2 287  ? 139.341 111.448 124.650 1.00 61.60  ? 287  ASN G O     1 
ATOM   11716 C  CB    . ASN B 2 287  ? 139.317 113.330 126.912 1.00 67.69  ? 287  ASN G CB    1 
ATOM   11717 C  CG    . ASN B 2 287  ? 138.587 113.710 128.183 1.00 74.08  ? 287  ASN G CG    1 
ATOM   11718 O  OD1   . ASN B 2 287  ? 137.463 113.268 128.422 1.00 76.98  ? 287  ASN G OD1   1 
ATOM   11719 N  ND2   . ASN B 2 287  ? 139.222 114.534 129.007 1.00 73.08  ? 287  ASN G ND2   1 
ATOM   11720 N  N     . GLY B 2 288  ? 141.486 111.163 125.261 1.00 66.30  ? 288  GLY G N     1 
ATOM   11721 C  CA    . GLY B 2 288  ? 141.881 110.809 123.907 1.00 63.81  ? 288  GLY G CA    1 
ATOM   11722 C  C     . GLY B 2 288  ? 141.742 112.001 122.982 1.00 57.67  ? 288  GLY G C     1 
ATOM   11723 O  O     . GLY B 2 288  ? 142.023 113.143 123.361 1.00 60.24  ? 288  GLY G O     1 
ATOM   11724 N  N     . VAL B 2 289  ? 141.303 111.746 121.751 1.00 52.86  ? 289  VAL G N     1 
ATOM   11725 C  CA    . VAL B 2 289  ? 141.045 112.856 120.843 1.00 49.79  ? 289  VAL G CA    1 
ATOM   11726 C  C     . VAL B 2 289  ? 139.597 113.300 121.020 1.00 51.52  ? 289  VAL G C     1 
ATOM   11727 O  O     . VAL B 2 289  ? 138.716 112.997 120.208 1.00 58.89  ? 289  VAL G O     1 
ATOM   11728 C  CB    . VAL B 2 289  ? 141.387 112.474 119.387 1.00 51.97  ? 289  VAL G CB    1 
ATOM   11729 C  CG1   . VAL B 2 289  ? 140.620 111.230 118.929 1.00 46.33  ? 289  VAL G CG1   1 
ATOM   11730 C  CG2   . VAL B 2 289  ? 141.154 113.653 118.444 1.00 46.95  ? 289  VAL G CG2   1 
ATOM   11731 N  N     . ASN B 2 290  ? 139.349 114.026 122.104 1.00 51.04  ? 290  ASN G N     1 
ATOM   11732 C  CA    . ASN B 2 290  ? 138.115 114.778 122.294 1.00 47.21  ? 290  ASN G CA    1 
ATOM   11733 C  C     . ASN B 2 290  ? 138.344 116.140 122.918 1.00 48.40  ? 290  ASN G C     1 
ATOM   11734 O  O     . ASN B 2 290  ? 137.464 117.000 122.816 1.00 47.85  ? 290  ASN G O     1 
ATOM   11735 C  CB    . ASN B 2 290  ? 137.120 113.988 123.147 1.00 49.42  ? 290  ASN G CB    1 
ATOM   11736 C  CG    . ASN B 2 290  ? 136.366 112.952 122.340 1.00 53.37  ? 290  ASN G CG    1 
ATOM   11737 O  OD1   . ASN B 2 290  ? 135.535 113.289 121.497 1.00 47.84  ? 290  ASN G OD1   1 
ATOM   11738 N  ND2   . ASN B 2 290  ? 136.658 111.681 122.589 1.00 56.89  ? 290  ASN G ND2   1 
ATOM   11739 N  N     . ASP B 2 291  ? 139.478 116.358 123.586 1.00 47.18  ? 291  ASP G N     1 
ATOM   11740 C  CA    . ASP B 2 291  ? 139.865 117.704 123.986 1.00 44.92  ? 291  ASP G CA    1 
ATOM   11741 C  C     . ASP B 2 291  ? 140.033 118.598 122.768 1.00 44.35  ? 291  ASP G C     1 
ATOM   11742 O  O     . ASP B 2 291  ? 139.704 119.789 122.809 1.00 45.84  ? 291  ASP G O     1 
ATOM   11743 C  CB    . ASP B 2 291  ? 141.163 117.651 124.790 1.00 47.89  ? 291  ASP G CB    1 
ATOM   11744 C  CG    . ASP B 2 291  ? 141.092 116.681 125.949 1.00 55.78  ? 291  ASP G CG    1 
ATOM   11745 O  OD1   . ASP B 2 291  ? 140.051 116.645 126.635 1.00 57.67  ? 291  ASP G OD1   1 
ATOM   11746 O  OD2   . ASP B 2 291  ? 142.079 115.951 126.171 1.00 59.18  ? 291  ASP G OD2   1 
ATOM   11747 N  N     . ILE B 2 292  ? 140.567 118.043 121.678 1.00 41.11  ? 292  ILE G N     1 
ATOM   11748 C  CA    . ILE B 2 292  ? 140.725 118.805 120.445 1.00 39.66  ? 292  ILE G CA    1 
ATOM   11749 C  C     . ILE B 2 292  ? 139.373 119.063 119.792 1.00 37.48  ? 292  ILE G C     1 
ATOM   11750 O  O     . ILE B 2 292  ? 139.074 120.189 119.381 1.00 41.19  ? 292  ILE G O     1 
ATOM   11751 C  CB    . ILE B 2 292  ? 141.682 118.068 119.492 1.00 34.93  ? 292  ILE G CB    1 
ATOM   11752 C  CG1   . ILE B 2 292  ? 143.045 117.874 120.154 1.00 33.23  ? 292  ILE G CG1   1 
ATOM   11753 C  CG2   . ILE B 2 292  ? 141.823 118.830 118.194 1.00 32.08  ? 292  ILE G CG2   1 
ATOM   11754 C  CD1   . ILE B 2 292  ? 143.938 116.907 119.428 1.00 30.97  ? 292  ILE G CD1   1 
ATOM   11755 N  N     . LYS B 2 293  ? 138.534 118.029 119.691 1.00 33.41  ? 293  LYS G N     1 
ATOM   11756 C  CA    . LYS B 2 293  ? 137.257 118.179 118.999 1.00 35.13  ? 293  LYS G CA    1 
ATOM   11757 C  C     . LYS B 2 293  ? 136.336 119.149 119.725 1.00 39.08  ? 293  LYS G C     1 
ATOM   11758 O  O     . LYS B 2 293  ? 135.634 119.942 119.088 1.00 41.83  ? 293  LYS G O     1 
ATOM   11759 C  CB    . LYS B 2 293  ? 136.581 116.821 118.840 1.00 33.40  ? 293  LYS G CB    1 
ATOM   11760 C  CG    . LYS B 2 293  ? 137.201 115.936 117.781 1.00 35.61  ? 293  LYS G CG    1 
ATOM   11761 C  CD    . LYS B 2 293  ? 136.299 114.759 117.474 1.00 38.91  ? 293  LYS G CD    1 
ATOM   11762 C  CE    . LYS B 2 293  ? 136.765 113.994 116.253 1.00 41.58  ? 293  LYS G CE    1 
ATOM   11763 N  NZ    . LYS B 2 293  ? 135.809 112.909 115.904 1.00 41.88  ? 293  LYS G NZ    1 
ATOM   11764 N  N     . ASN B 2 294  ? 136.319 119.101 121.053 1.00 38.58  ? 294  ASN G N     1 
ATOM   11765 C  CA    . ASN B 2 294  ? 135.432 119.936 121.848 1.00 40.49  ? 294  ASN G CA    1 
ATOM   11766 C  C     . ASN B 2 294  ? 136.030 121.294 122.182 1.00 39.36  ? 294  ASN G C     1 
ATOM   11767 O  O     . ASN B 2 294  ? 135.409 122.060 122.923 1.00 42.63  ? 294  ASN G O     1 
ATOM   11768 C  CB    . ASN B 2 294  ? 135.050 119.211 123.140 1.00 41.32  ? 294  ASN G CB    1 
ATOM   11769 C  CG    . ASN B 2 294  ? 134.382 117.878 122.882 1.00 47.05  ? 294  ASN G CG    1 
ATOM   11770 O  OD1   . ASN B 2 294  ? 134.656 116.893 123.562 1.00 46.43  ? 294  ASN G OD1   1 
ATOM   11771 N  ND2   . ASN B 2 294  ? 133.498 117.842 121.894 1.00 47.25  ? 294  ASN G ND2   1 
ATOM   11772 N  N     . HIS B 2 295  ? 137.215 121.606 121.666 1.00 35.18  ? 295  HIS G N     1 
ATOM   11773 C  CA    . HIS B 2 295  ? 137.818 122.901 121.935 1.00 29.31  ? 295  HIS G CA    1 
ATOM   11774 C  C     . HIS B 2 295  ? 136.984 124.017 121.317 1.00 32.85  ? 295  HIS G C     1 
ATOM   11775 O  O     . HIS B 2 295  ? 136.295 123.827 120.312 1.00 35.99  ? 295  HIS G O     1 
ATOM   11776 C  CB    . HIS B 2 295  ? 139.247 122.957 121.402 1.00 29.46  ? 295  HIS G CB    1 
ATOM   11777 C  CG    . HIS B 2 295  ? 140.089 124.002 122.064 1.00 27.26  ? 295  HIS G CG    1 
ATOM   11778 N  ND1   . HIS B 2 295  ? 140.164 125.297 121.604 1.00 27.77  ? 295  HIS G ND1   1 
ATOM   11779 C  CD2   . HIS B 2 295  ? 140.886 123.944 123.156 1.00 25.26  ? 295  HIS G CD2   1 
ATOM   11780 C  CE1   . HIS B 2 295  ? 140.970 125.994 122.383 1.00 25.42  ? 295  HIS G CE1   1 
ATOM   11781 N  NE2   . HIS B 2 295  ? 141.422 125.196 123.331 1.00 24.50  ? 295  HIS G NE2   1 
ATOM   11782 N  N     . LYS B 2 296  ? 137.042 125.192 121.947 1.00 32.92  ? 296  LYS G N     1 
ATOM   11783 C  CA    . LYS B 2 296  ? 136.233 126.322 121.504 1.00 32.42  ? 296  LYS G CA    1 
ATOM   11784 C  C     . LYS B 2 296  ? 136.616 126.784 120.103 1.00 33.89  ? 296  LYS G C     1 
ATOM   11785 O  O     . LYS B 2 296  ? 135.789 127.373 119.399 1.00 39.69  ? 296  LYS G O     1 
ATOM   11786 C  CB    . LYS B 2 296  ? 136.366 127.469 122.503 1.00 36.35  ? 296  LYS G CB    1 
ATOM   11787 C  CG    . LYS B 2 296  ? 135.444 128.643 122.251 1.00 42.13  ? 296  LYS G CG    1 
ATOM   11788 C  CD    . LYS B 2 296  ? 135.689 129.734 123.272 1.00 41.97  ? 296  LYS G CD    1 
ATOM   11789 C  CE    . LYS B 2 296  ? 134.960 131.008 122.907 1.00 45.00  ? 296  LYS G CE    1 
ATOM   11790 N  NZ    . LYS B 2 296  ? 135.472 132.166 123.689 1.00 45.63  ? 296  LYS G NZ    1 
ATOM   11791 N  N     . TRP B 2 297  ? 137.857 126.532 119.681 1.00 31.71  ? 297  TRP G N     1 
ATOM   11792 C  CA    . TRP B 2 297  ? 138.282 126.936 118.345 1.00 29.73  ? 297  TRP G CA    1 
ATOM   11793 C  C     . TRP B 2 297  ? 137.543 126.159 117.262 1.00 32.28  ? 297  TRP G C     1 
ATOM   11794 O  O     . TRP B 2 297  ? 137.277 126.703 116.185 1.00 33.87  ? 297  TRP G O     1 
ATOM   11795 C  CB    . TRP B 2 297  ? 139.795 126.762 118.207 1.00 26.49  ? 297  TRP G CB    1 
ATOM   11796 C  CG    . TRP B 2 297  ? 140.410 127.508 117.054 1.00 26.84  ? 297  TRP G CG    1 
ATOM   11797 C  CD1   . TRP B 2 297  ? 140.504 128.859 116.913 1.00 25.83  ? 297  TRP G CD1   1 
ATOM   11798 C  CD2   . TRP B 2 297  ? 141.061 126.940 115.911 1.00 25.89  ? 297  TRP G CD2   1 
ATOM   11799 N  NE1   . TRP B 2 297  ? 141.145 129.169 115.740 1.00 26.16  ? 297  TRP G NE1   1 
ATOM   11800 C  CE2   . TRP B 2 297  ? 141.500 128.007 115.109 1.00 24.72  ? 297  TRP G CE2   1 
ATOM   11801 C  CE3   . TRP B 2 297  ? 141.303 125.634 115.483 1.00 25.70  ? 297  TRP G CE3   1 
ATOM   11802 C  CZ2   . TRP B 2 297  ? 142.170 127.809 113.906 1.00 23.63  ? 297  TRP G CZ2   1 
ATOM   11803 C  CZ3   . TRP B 2 297  ? 141.967 125.440 114.290 1.00 23.22  ? 297  TRP G CZ3   1 
ATOM   11804 C  CH2   . TRP B 2 297  ? 142.393 126.519 113.517 1.00 23.06  ? 297  TRP G CH2   1 
ATOM   11805 N  N     . PHE B 2 298  ? 137.193 124.901 117.529 1.00 33.06  ? 298  PHE G N     1 
ATOM   11806 C  CA    . PHE B 2 298  ? 136.434 124.074 116.601 1.00 35.47  ? 298  PHE G CA    1 
ATOM   11807 C  C     . PHE B 2 298  ? 134.932 124.120 116.862 1.00 40.96  ? 298  PHE G C     1 
ATOM   11808 O  O     . PHE B 2 298  ? 134.228 123.156 116.540 1.00 43.99  ? 298  PHE G O     1 
ATOM   11809 C  CB    . PHE B 2 298  ? 136.920 122.624 116.660 1.00 35.15  ? 298  PHE G CB    1 
ATOM   11810 C  CG    . PHE B 2 298  ? 138.268 122.406 116.039 1.00 33.79  ? 298  PHE G CG    1 
ATOM   11811 C  CD1   . PHE B 2 298  ? 138.420 122.404 114.663 1.00 35.39  ? 298  PHE G CD1   1 
ATOM   11812 C  CD2   . PHE B 2 298  ? 139.381 122.183 116.828 1.00 31.17  ? 298  PHE G CD2   1 
ATOM   11813 C  CE1   . PHE B 2 298  ? 139.655 122.200 114.090 1.00 31.21  ? 298  PHE G CE1   1 
ATOM   11814 C  CE2   . PHE B 2 298  ? 140.619 121.974 116.258 1.00 31.67  ? 298  PHE G CE2   1 
ATOM   11815 C  CZ    . PHE B 2 298  ? 140.755 121.982 114.888 1.00 31.57  ? 298  PHE G CZ    1 
ATOM   11816 N  N     . ALA B 2 299  ? 134.430 125.208 117.448 1.00 43.02  ? 299  ALA G N     1 
ATOM   11817 C  CA    . ALA B 2 299  ? 133.017 125.279 117.809 1.00 43.46  ? 299  ALA G CA    1 
ATOM   11818 C  C     . ALA B 2 299  ? 132.109 125.251 116.588 1.00 51.81  ? 299  ALA G C     1 
ATOM   11819 O  O     . ALA B 2 299  ? 131.009 124.692 116.649 1.00 56.74  ? 299  ALA G O     1 
ATOM   11820 C  CB    . ALA B 2 299  ? 132.747 126.537 118.631 1.00 43.46  ? 299  ALA G CB    1 
ATOM   11821 N  N     . THR B 2 300  ? 132.537 125.846 115.477 1.00 50.71  ? 300  THR G N     1 
ATOM   11822 C  CA    . THR B 2 300  ? 131.704 125.965 114.289 1.00 56.31  ? 300  THR G CA    1 
ATOM   11823 C  C     . THR B 2 300  ? 132.016 124.900 113.243 1.00 57.01  ? 300  THR G C     1 
ATOM   11824 O  O     . THR B 2 300  ? 131.733 125.104 112.057 1.00 60.03  ? 300  THR G O     1 
ATOM   11825 C  CB    . THR B 2 300  ? 131.851 127.356 113.677 1.00 58.39  ? 300  THR G CB    1 
ATOM   11826 O  OG1   . THR B 2 300  ? 133.076 127.426 112.936 1.00 56.98  ? 300  THR G OG1   1 
ATOM   11827 C  CG2   . THR B 2 300  ? 131.864 128.414 114.766 1.00 54.88  ? 300  THR G CG2   1 
ATOM   11828 N  N     . THR B 2 301  ? 132.594 123.775 113.653 1.00 49.84  ? 301  THR G N     1 
ATOM   11829 C  CA    . THR B 2 301  ? 132.973 122.706 112.740 1.00 48.06  ? 301  THR G CA    1 
ATOM   11830 C  C     . THR B 2 301  ? 131.973 121.563 112.838 1.00 51.48  ? 301  THR G C     1 
ATOM   11831 O  O     . THR B 2 301  ? 131.628 121.125 113.940 1.00 52.91  ? 301  THR G O     1 
ATOM   11832 C  CB    . THR B 2 301  ? 134.382 122.202 113.048 1.00 44.68  ? 301  THR G CB    1 
ATOM   11833 O  OG1   . THR B 2 301  ? 135.319 123.273 112.891 1.00 45.59  ? 301  THR G OG1   1 
ATOM   11834 C  CG2   . THR B 2 301  ? 134.764 121.070 112.111 1.00 43.16  ? 301  THR G CG2   1 
ATOM   11835 N  N     . ASP B 2 302  ? 131.513 121.087 111.684 1.00 52.54  ? 302  ASP G N     1 
ATOM   11836 C  CA    . ASP B 2 302  ? 130.593 119.955 111.596 1.00 58.11  ? 302  ASP G CA    1 
ATOM   11837 C  C     . ASP B 2 302  ? 131.415 118.731 111.205 1.00 56.97  ? 302  ASP G C     1 
ATOM   11838 O  O     . ASP B 2 302  ? 131.748 118.543 110.033 1.00 61.15  ? 302  ASP G O     1 
ATOM   11839 C  CB    . ASP B 2 302  ? 129.487 120.246 110.587 1.00 63.26  ? 302  ASP G CB    1 
ATOM   11840 C  CG    . ASP B 2 302  ? 128.397 119.188 110.580 1.00 70.79  ? 302  ASP G CG    1 
ATOM   11841 O  OD1   . ASP B 2 302  ? 128.614 118.077 111.104 1.00 71.86  ? 302  ASP G OD1   1 
ATOM   11842 O  OD2   . ASP B 2 302  ? 127.310 119.471 110.037 1.00 71.25  ? 302  ASP G OD2   1 
ATOM   11843 N  N     . TRP B 2 303  ? 131.733 117.890 112.191 1.00 50.30  ? 303  TRP G N     1 
ATOM   11844 C  CA    . TRP B 2 303  ? 132.647 116.778 111.965 1.00 49.78  ? 303  TRP G CA    1 
ATOM   11845 C  C     . TRP B 2 303  ? 132.063 115.695 111.067 1.00 56.20  ? 303  TRP G C     1 
ATOM   11846 O  O     . TRP B 2 303  ? 132.823 114.884 110.528 1.00 58.67  ? 303  TRP G O     1 
ATOM   11847 C  CB    . TRP B 2 303  ? 133.084 116.180 113.303 1.00 47.04  ? 303  TRP G CB    1 
ATOM   11848 C  CG    . TRP B 2 303  ? 133.825 117.163 114.159 1.00 49.19  ? 303  TRP G CG    1 
ATOM   11849 C  CD1   . TRP B 2 303  ? 133.314 117.917 115.171 1.00 46.03  ? 303  TRP G CD1   1 
ATOM   11850 C  CD2   . TRP B 2 303  ? 135.210 117.511 114.059 1.00 45.61  ? 303  TRP G CD2   1 
ATOM   11851 N  NE1   . TRP B 2 303  ? 134.296 118.707 115.714 1.00 42.34  ? 303  TRP G NE1   1 
ATOM   11852 C  CE2   . TRP B 2 303  ? 135.469 118.476 115.047 1.00 41.10  ? 303  TRP G CE2   1 
ATOM   11853 C  CE3   . TRP B 2 303  ? 136.256 117.096 113.233 1.00 41.92  ? 303  TRP G CE3   1 
ATOM   11854 C  CZ2   . TRP B 2 303  ? 136.729 119.034 115.232 1.00 37.63  ? 303  TRP G CZ2   1 
ATOM   11855 C  CZ3   . TRP B 2 303  ? 137.505 117.649 113.418 1.00 37.13  ? 303  TRP G CZ3   1 
ATOM   11856 C  CH2   . TRP B 2 303  ? 137.732 118.607 114.408 1.00 35.44  ? 303  TRP G CH2   1 
ATOM   11857 N  N     . ILE B 2 304  ? 130.743 115.653 110.890 1.00 60.42  ? 304  ILE G N     1 
ATOM   11858 C  CA    . ILE B 2 304  ? 130.158 114.685 109.966 1.00 62.70  ? 304  ILE G CA    1 
ATOM   11859 C  C     . ILE B 2 304  ? 130.217 115.204 108.535 1.00 63.87  ? 304  ILE G C     1 
ATOM   11860 O  O     . ILE B 2 304  ? 130.560 114.464 107.604 1.00 65.42  ? 304  ILE G O     1 
ATOM   11861 C  CB    . ILE B 2 304  ? 128.716 114.333 110.381 1.00 65.26  ? 304  ILE G CB    1 
ATOM   11862 C  CG1   . ILE B 2 304  ? 128.679 113.626 111.742 1.00 64.51  ? 304  ILE G CG1   1 
ATOM   11863 C  CG2   . ILE B 2 304  ? 128.054 113.470 109.323 1.00 65.32  ? 304  ILE G CG2   1 
ATOM   11864 C  CD1   . ILE B 2 304  ? 128.667 114.555 112.947 1.00 64.34  ? 304  ILE G CD1   1 
ATOM   11865 N  N     . ALA B 2 305  ? 129.890 116.483 108.337 1.00 58.64  ? 305  ALA G N     1 
ATOM   11866 C  CA    . ALA B 2 305  ? 129.923 117.058 106.998 1.00 58.85  ? 305  ALA G CA    1 
ATOM   11867 C  C     . ALA B 2 305  ? 131.333 117.081 106.426 1.00 59.47  ? 305  ALA G C     1 
ATOM   11868 O  O     . ALA B 2 305  ? 131.515 116.843 105.228 1.00 60.81  ? 305  ALA G O     1 
ATOM   11869 C  CB    . ALA B 2 305  ? 129.335 118.467 107.021 1.00 59.38  ? 305  ALA G CB    1 
ATOM   11870 N  N     . ILE B 2 306  ? 132.338 117.362 107.257 1.00 56.26  ? 306  ILE G N     1 
ATOM   11871 C  CA    . ILE B 2 306  ? 133.718 117.369 106.781 1.00 55.19  ? 306  ILE G CA    1 
ATOM   11872 C  C     . ILE B 2 306  ? 134.126 115.977 106.315 1.00 54.96  ? 306  ILE G C     1 
ATOM   11873 O  O     . ILE B 2 306  ? 134.741 115.814 105.254 1.00 55.51  ? 306  ILE G O     1 
ATOM   11874 C  CB    . ILE B 2 306  ? 134.662 117.895 107.877 1.00 48.93  ? 306  ILE G CB    1 
ATOM   11875 C  CG1   . ILE B 2 306  ? 134.423 119.384 108.125 1.00 46.30  ? 306  ILE G CG1   1 
ATOM   11876 C  CG2   . ILE B 2 306  ? 136.108 117.651 107.495 1.00 43.90  ? 306  ILE G CG2   1 
ATOM   11877 C  CD1   . ILE B 2 306  ? 135.027 120.275 107.072 1.00 50.16  ? 306  ILE G CD1   1 
ATOM   11878 N  N     . TYR B 2 307  ? 133.788 114.951 107.099 1.00 54.23  ? 307  TYR G N     1 
ATOM   11879 C  CA    . TYR B 2 307  ? 134.104 113.581 106.711 1.00 55.59  ? 307  TYR G CA    1 
ATOM   11880 C  C     . TYR B 2 307  ? 133.398 113.196 105.418 1.00 56.30  ? 307  TYR G C     1 
ATOM   11881 O  O     . TYR B 2 307  ? 133.992 112.572 104.533 1.00 57.17  ? 307  TYR G O     1 
ATOM   11882 C  CB    . TYR B 2 307  ? 133.722 112.613 107.828 1.00 56.25  ? 307  TYR G CB    1 
ATOM   11883 C  CG    . TYR B 2 307  ? 133.841 111.164 107.422 1.00 59.58  ? 307  TYR G CG    1 
ATOM   11884 C  CD1   . TYR B 2 307  ? 135.080 110.576 107.237 1.00 56.82  ? 307  TYR G CD1   1 
ATOM   11885 C  CD2   . TYR B 2 307  ? 132.711 110.394 107.201 1.00 60.80  ? 307  TYR G CD2   1 
ATOM   11886 C  CE1   . TYR B 2 307  ? 135.190 109.258 106.860 1.00 59.55  ? 307  TYR G CE1   1 
ATOM   11887 C  CE2   . TYR B 2 307  ? 132.813 109.077 106.822 1.00 57.49  ? 307  TYR G CE2   1 
ATOM   11888 C  CZ    . TYR B 2 307  ? 134.054 108.514 106.653 1.00 61.87  ? 307  TYR G CZ    1 
ATOM   11889 O  OH    . TYR B 2 307  ? 134.162 107.198 106.276 1.00 69.59  ? 307  TYR G OH    1 
ATOM   11890 N  N     . GLN B 2 308  ? 132.120 113.550 105.296 1.00 58.23  ? 308  GLN G N     1 
ATOM   11891 C  CA    . GLN B 2 308  ? 131.367 113.184 104.105 1.00 62.39  ? 308  GLN G CA    1 
ATOM   11892 C  C     . GLN B 2 308  ? 131.614 114.121 102.932 1.00 62.83  ? 308  GLN G C     1 
ATOM   11893 O  O     . GLN B 2 308  ? 131.048 113.896 101.857 1.00 61.26  ? 308  GLN G O     1 
ATOM   11894 C  CB    . GLN B 2 308  ? 129.872 113.128 104.423 1.00 64.74  ? 308  GLN G CB    1 
ATOM   11895 C  CG    . GLN B 2 308  ? 129.479 111.935 105.276 1.00 63.03  ? 308  GLN G CG    1 
ATOM   11896 C  CD    . GLN B 2 308  ? 128.029 111.975 105.703 1.00 70.72  ? 308  GLN G CD    1 
ATOM   11897 O  OE1   . GLN B 2 308  ? 127.197 112.610 105.056 1.00 72.08  ? 308  GLN G OE1   1 
ATOM   11898 N  NE2   . GLN B 2 308  ? 127.716 111.293 106.797 1.00 72.71  ? 308  GLN G NE2   1 
ATOM   11899 N  N     . ARG B 2 309  ? 132.431 115.160 103.117 1.00 62.94  ? 309  ARG G N     1 
ATOM   11900 C  CA    . ARG B 2 309  ? 132.816 116.079 102.044 1.00 59.94  ? 309  ARG G CA    1 
ATOM   11901 C  C     . ARG B 2 309  ? 131.602 116.794 101.455 1.00 63.55  ? 309  ARG G C     1 
ATOM   11902 O  O     . ARG B 2 309  ? 131.320 116.717 100.259 1.00 65.19  ? 309  ARG G O     1 
ATOM   11903 C  CB    . ARG B 2 309  ? 133.616 115.357 100.958 1.00 54.64  ? 309  ARG G CB    1 
ATOM   11904 C  CG    . ARG B 2 309  ? 134.871 114.682 101.475 1.00 57.12  ? 309  ARG G CG    1 
ATOM   11905 C  CD    . ARG B 2 309  ? 135.352 113.610 100.520 1.00 58.78  ? 309  ARG G CD    1 
ATOM   11906 N  NE    . ARG B 2 309  ? 135.732 114.176 99.232  1.00 59.59  ? 309  ARG G NE    1 
ATOM   11907 C  CZ    . ARG B 2 309  ? 136.978 114.441 98.867  1.00 60.15  ? 309  ARG G CZ    1 
ATOM   11908 N  NH1   . ARG B 2 309  ? 137.998 114.208 99.675  1.00 58.89  ? 309  ARG G NH1   1 
ATOM   11909 N  NH2   . ARG B 2 309  ? 137.205 114.956 97.663  1.00 63.95  ? 309  ARG G NH2   1 
ATOM   11910 N  N     . LYS B 2 310  ? 130.876 117.498 102.322 1.00 61.94  ? 310  LYS G N     1 
ATOM   11911 C  CA    . LYS B 2 310  ? 129.748 118.318 101.914 1.00 62.13  ? 310  LYS G CA    1 
ATOM   11912 C  C     . LYS B 2 310  ? 129.932 119.789 102.251 1.00 61.82  ? 310  LYS G C     1 
ATOM   11913 O  O     . LYS B 2 310  ? 129.010 120.580 102.026 1.00 63.49  ? 310  LYS G O     1 
ATOM   11914 C  CB    . LYS B 2 310  ? 128.457 117.793 102.552 1.00 63.77  ? 310  LYS G CB    1 
ATOM   11915 C  CG    . LYS B 2 310  ? 127.813 116.666 101.766 1.00 67.85  ? 310  LYS G CG    1 
ATOM   11916 C  CD    . LYS B 2 310  ? 126.426 116.341 102.283 1.00 71.68  ? 310  LYS G CD    1 
ATOM   11917 C  CE    . LYS B 2 310  ? 126.493 115.352 103.432 1.00 69.29  ? 310  LYS G CE    1 
ATOM   11918 N  NZ    . LYS B 2 310  ? 126.725 113.963 102.947 1.00 66.73  ? 310  LYS G NZ    1 
ATOM   11919 N  N     . VAL B 2 311  ? 131.080 120.174 102.798 1.00 60.14  ? 311  VAL G N     1 
ATOM   11920 C  CA    . VAL B 2 311  ? 131.385 121.571 103.087 1.00 57.04  ? 311  VAL G CA    1 
ATOM   11921 C  C     . VAL B 2 311  ? 132.173 122.149 101.920 1.00 57.48  ? 311  VAL G C     1 
ATOM   11922 O  O     . VAL B 2 311  ? 133.144 121.543 101.454 1.00 62.63  ? 311  VAL G O     1 
ATOM   11923 C  CB    . VAL B 2 311  ? 132.170 121.703 104.401 1.00 52.66  ? 311  VAL G CB    1 
ATOM   11924 C  CG1   . VAL B 2 311  ? 132.563 123.148 104.637 1.00 48.21  ? 311  VAL G CG1   1 
ATOM   11925 C  CG2   . VAL B 2 311  ? 131.349 121.177 105.559 1.00 55.81  ? 311  VAL G CG2   1 
ATOM   11926 N  N     . GLU B 2 312  ? 131.754 123.317 101.442 1.00 54.28  ? 312  GLU G N     1 
ATOM   11927 C  CA    . GLU B 2 312  ? 132.420 123.937 100.306 1.00 60.02  ? 312  GLU G CA    1 
ATOM   11928 C  C     . GLU B 2 312  ? 133.798 124.449 100.710 1.00 58.60  ? 312  GLU G C     1 
ATOM   11929 O  O     . GLU B 2 312  ? 133.940 125.173 101.700 1.00 58.14  ? 312  GLU G O     1 
ATOM   11930 C  CB    . GLU B 2 312  ? 131.567 125.076 99.752  1.00 64.58  ? 312  GLU G CB    1 
ATOM   11931 C  CG    . GLU B 2 312  ? 130.162 124.648 99.374  1.00 70.62  ? 312  GLU G CG    1 
ATOM   11932 C  CD    . GLU B 2 312  ? 130.152 123.490 98.397  1.00 72.79  ? 312  GLU G CD    1 
ATOM   11933 O  OE1   . GLU B 2 312  ? 130.581 123.679 97.239  1.00 75.04  ? 312  GLU G OE1   1 
ATOM   11934 O  OE2   . GLU B 2 312  ? 129.722 122.386 98.791  1.00 67.41  ? 312  GLU G OE2   1 
ATOM   11935 N  N     . ALA B 2 313  ? 134.809 124.070 99.937  1.00 55.99  ? 313  ALA G N     1 
ATOM   11936 C  CA    . ALA B 2 313  ? 136.179 124.436 100.259 1.00 54.37  ? 313  ALA G CA    1 
ATOM   11937 C  C     . ALA B 2 313  ? 136.387 125.939 100.087 1.00 58.24  ? 313  ALA G C     1 
ATOM   11938 O  O     . ALA B 2 313  ? 135.779 126.555 99.207  1.00 59.76  ? 313  ALA G O     1 
ATOM   11939 C  CB    . ALA B 2 313  ? 137.157 123.667 99.375  1.00 56.54  ? 313  ALA G CB    1 
ATOM   11940 N  N     . PRO B 2 314  ? 137.222 126.561 100.924 1.00 56.94  ? 314  PRO G N     1 
ATOM   11941 C  CA    . PRO B 2 314  ? 137.563 127.973 100.714 1.00 60.13  ? 314  PRO G CA    1 
ATOM   11942 C  C     . PRO B 2 314  ? 138.529 128.204 99.563  1.00 59.69  ? 314  PRO G C     1 
ATOM   11943 O  O     . PRO B 2 314  ? 138.785 129.366 99.223  1.00 60.48  ? 314  PRO G O     1 
ATOM   11944 C  CB    . PRO B 2 314  ? 138.185 128.378 102.054 1.00 54.97  ? 314  PRO G CB    1 
ATOM   11945 C  CG    . PRO B 2 314  ? 138.818 127.125 102.534 1.00 49.99  ? 314  PRO G CG    1 
ATOM   11946 C  CD    . PRO B 2 314  ? 137.883 126.015 102.121 1.00 52.97  ? 314  PRO G CD    1 
ATOM   11947 N  N     . PHE B 2 315  ? 139.072 127.149 98.959  1.00 59.49  ? 315  PHE G N     1 
ATOM   11948 C  CA    . PHE B 2 315  ? 140.010 127.297 97.856  1.00 63.35  ? 315  PHE G CA    1 
ATOM   11949 C  C     . PHE B 2 315  ? 139.803 126.118 96.918  1.00 67.07  ? 315  PHE G C     1 
ATOM   11950 O  O     . PHE B 2 315  ? 139.836 124.964 97.355  1.00 67.88  ? 315  PHE G O     1 
ATOM   11951 C  CB    . PHE B 2 315  ? 141.455 127.371 98.387  1.00 63.68  ? 315  PHE G CB    1 
ATOM   11952 C  CG    . PHE B 2 315  ? 142.531 127.432 97.318  1.00 65.57  ? 315  PHE G CG    1 
ATOM   11953 C  CD1   . PHE B 2 315  ? 142.687 126.436 96.364  1.00 69.07  ? 315  PHE G CD1   1 
ATOM   11954 C  CD2   . PHE B 2 315  ? 143.391 128.515 97.279  1.00 69.23  ? 315  PHE G CD2   1 
ATOM   11955 C  CE1   . PHE B 2 315  ? 143.667 126.521 95.404  1.00 72.26  ? 315  PHE G CE1   1 
ATOM   11956 C  CE2   . PHE B 2 315  ? 144.376 128.604 96.321  1.00 73.47  ? 315  PHE G CE2   1 
ATOM   11957 C  CZ    . PHE B 2 315  ? 144.512 127.606 95.381  1.00 74.96  ? 315  PHE G CZ    1 
ATOM   11958 N  N     . ILE B 2 316  ? 139.590 126.411 95.640  1.00 67.34  ? 316  ILE G N     1 
ATOM   11959 C  CA    . ILE B 2 316  ? 139.432 125.402 94.603  1.00 71.98  ? 316  ILE G CA    1 
ATOM   11960 C  C     . ILE B 2 316  ? 140.528 125.620 93.565  1.00 75.54  ? 316  ILE G C     1 
ATOM   11961 O  O     . ILE B 2 316  ? 140.548 126.659 92.900  1.00 72.01  ? 316  ILE G O     1 
ATOM   11962 C  CB    . ILE B 2 316  ? 138.045 125.456 93.940  1.00 67.31  ? 316  ILE G CB    1 
ATOM   11963 C  CG1   . ILE B 2 316  ? 136.954 125.037 94.928  1.00 64.20  ? 316  ILE G CG1   1 
ATOM   11964 C  CG2   . ILE B 2 316  ? 138.008 124.572 92.703  1.00 65.51  ? 316  ILE G CG2   1 
ATOM   11965 C  CD1   . ILE B 2 316  ? 136.341 126.187 95.691  1.00 63.48  ? 316  ILE G CD1   1 
ATOM   11966 N  N     . PRO B 2 317  ? 141.459 124.683 93.389  1.00 76.55  ? 317  PRO G N     1 
ATOM   11967 C  CA    . PRO B 2 317  ? 142.503 124.871 92.376  1.00 78.62  ? 317  PRO G CA    1 
ATOM   11968 C  C     . PRO B 2 317  ? 141.930 124.796 90.968  1.00 87.03  ? 317  PRO G C     1 
ATOM   11969 O  O     . PRO B 2 317  ? 141.031 124.001 90.684  1.00 88.71  ? 317  PRO G O     1 
ATOM   11970 C  CB    . PRO B 2 317  ? 143.475 123.719 92.650  1.00 75.44  ? 317  PRO G CB    1 
ATOM   11971 C  CG    . PRO B 2 317  ? 142.623 122.661 93.244  1.00 71.61  ? 317  PRO G CG    1 
ATOM   11972 C  CD    . PRO B 2 317  ? 141.564 123.371 94.049  1.00 71.98  ? 317  PRO G CD    1 
ATOM   11973 N  N     . LYS B 2 318  ? 142.464 125.637 90.083  1.00 89.26  ? 318  LYS G N     1 
ATOM   11974 C  CA    . LYS B 2 318  ? 141.977 125.735 88.708  1.00 93.18  ? 318  LYS G CA    1 
ATOM   11975 C  C     . LYS B 2 318  ? 142.675 124.722 87.795  1.00 96.01  ? 318  LYS G C     1 
ATOM   11976 O  O     . LYS B 2 318  ? 143.423 125.063 86.878  1.00 96.90  ? 318  LYS G O     1 
ATOM   11977 C  CB    . LYS B 2 318  ? 142.148 127.160 88.200  1.00 97.32  ? 318  LYS G CB    1 
ATOM   11978 C  CG    . LYS B 2 318  ? 143.513 127.763 88.475  1.00 95.57  ? 318  LYS G CG    1 
ATOM   11979 C  CD    . LYS B 2 318  ? 143.382 129.129 89.127  1.00 93.77  ? 318  LYS G CD    1 
ATOM   11980 C  CE    . LYS B 2 318  ? 142.474 130.038 88.317  1.00 93.29  ? 318  LYS G CE    1 
ATOM   11981 N  NZ    . LYS B 2 318  ? 142.572 131.458 88.756  1.00 96.18  ? 318  LYS G NZ    1 
ATOM   11982 N  N     . PHE B 2 319  ? 142.410 123.446 88.063  1.00 96.74  ? 319  PHE G N     1 
ATOM   11983 C  CA    . PHE B 2 319  ? 142.893 122.385 87.189  1.00 100.86 ? 319  PHE G CA    1 
ATOM   11984 C  C     . PHE B 2 319  ? 142.185 122.461 85.843  1.00 106.13 ? 319  PHE G C     1 
ATOM   11985 O  O     . PHE B 2 319  ? 140.982 122.733 85.776  1.00 102.46 ? 319  PHE G O     1 
ATOM   11986 C  CB    . PHE B 2 319  ? 142.670 121.018 87.835  1.00 95.02  ? 319  PHE G CB    1 
ATOM   11987 N  N     . LYS B 2 320  ? 142.930 122.226 84.766  1.00 109.81 ? 320  LYS G N     1 
ATOM   11988 C  CA    . LYS B 2 320  ? 142.412 122.363 83.408  1.00 110.66 ? 320  LYS G CA    1 
ATOM   11989 C  C     . LYS B 2 320  ? 142.682 121.104 82.594  1.00 112.69 ? 320  LYS G C     1 
ATOM   11990 O  O     . LYS B 2 320  ? 143.146 121.159 81.454  1.00 111.67 ? 320  LYS G O     1 
ATOM   11991 C  CB    . LYS B 2 320  ? 143.010 123.587 82.723  1.00 108.10 ? 320  LYS G CB    1 
ATOM   11992 N  N     . GLY B 2 321  ? 142.393 119.942 83.173  1.00 113.25 ? 321  GLY G N     1 
ATOM   11993 C  CA    . GLY B 2 321  ? 142.471 118.700 82.440  1.00 114.81 ? 321  GLY G CA    1 
ATOM   11994 C  C     . GLY B 2 321  ? 143.293 117.624 83.120  1.00 114.62 ? 321  GLY G C     1 
ATOM   11995 O  O     . GLY B 2 321  ? 144.110 117.893 84.006  1.00 115.13 ? 321  GLY G O     1 
ATOM   11996 N  N     . PRO B 2 322  ? 143.081 116.370 82.710  1.00 112.12 ? 322  PRO G N     1 
ATOM   11997 C  CA    . PRO B 2 322  ? 143.836 115.267 83.325  1.00 114.31 ? 322  PRO G CA    1 
ATOM   11998 C  C     . PRO B 2 322  ? 145.327 115.330 83.055  1.00 112.62 ? 322  PRO G C     1 
ATOM   11999 O  O     . PRO B 2 322  ? 146.116 114.924 83.916  1.00 109.72 ? 322  PRO G O     1 
ATOM   12000 C  CB    . PRO B 2 322  ? 143.204 114.018 82.697  1.00 110.86 ? 322  PRO G CB    1 
ATOM   12001 N  N     . GLY B 2 323  ? 145.739 115.823 81.889  1.00 113.08 ? 323  GLY G N     1 
ATOM   12002 C  CA    . GLY B 2 323  ? 147.149 115.939 81.580  1.00 109.95 ? 323  GLY G CA    1 
ATOM   12003 C  C     . GLY B 2 323  ? 147.790 117.242 81.985  1.00 109.90 ? 323  GLY G C     1 
ATOM   12004 O  O     . GLY B 2 323  ? 149.011 117.384 81.874  1.00 109.44 ? 323  GLY G O     1 
ATOM   12005 N  N     . ASP B 2 324  ? 146.997 118.199 82.458  1.00 108.67 ? 324  ASP G N     1 
ATOM   12006 C  CA    . ASP B 2 324  ? 147.522 119.491 82.871  1.00 104.17 ? 324  ASP G CA    1 
ATOM   12007 C  C     . ASP B 2 324  ? 148.266 119.356 84.193  1.00 100.60 ? 324  ASP G C     1 
ATOM   12008 O  O     . ASP B 2 324  ? 147.779 118.712 85.127  1.00 99.91  ? 324  ASP G O     1 
ATOM   12009 C  CB    . ASP B 2 324  ? 146.391 120.509 83.001  1.00 102.54 ? 324  ASP G CB    1 
ATOM   12010 N  N     . THR B 2 325  ? 149.450 119.962 84.265  1.00 97.18  ? 325  THR G N     1 
ATOM   12011 C  CA    . THR B 2 325  ? 150.269 119.954 85.471  1.00 93.96  ? 325  THR G CA    1 
ATOM   12012 C  C     . THR B 2 325  ? 150.830 121.344 85.740  1.00 94.46  ? 325  THR G C     1 
ATOM   12013 O  O     . THR B 2 325  ? 151.999 121.501 86.107  1.00 93.62  ? 325  THR G O     1 
ATOM   12014 C  CB    . THR B 2 325  ? 151.400 118.932 85.364  1.00 90.12  ? 325  THR G CB    1 
ATOM   12015 N  N     . SER B 2 326  ? 150.000 122.375 85.560  1.00 95.63  ? 326  SER G N     1 
ATOM   12016 C  CA    . SER B 2 326  ? 150.472 123.744 85.749  1.00 92.74  ? 326  SER G CA    1 
ATOM   12017 C  C     . SER B 2 326  ? 150.673 124.079 87.221  1.00 90.60  ? 326  SER G C     1 
ATOM   12018 O  O     . SER B 2 326  ? 151.517 124.919 87.553  1.00 90.65  ? 326  SER G O     1 
ATOM   12019 C  CB    . SER B 2 326  ? 149.492 124.731 85.114  1.00 91.84  ? 326  SER G CB    1 
ATOM   12020 N  N     . ASN B 2 327  ? 149.916 123.438 88.114  1.00 88.63  ? 327  ASN G N     1 
ATOM   12021 C  CA    . ASN B 2 327  ? 150.051 123.712 89.540  1.00 86.08  ? 327  ASN G CA    1 
ATOM   12022 C  C     . ASN B 2 327  ? 151.382 123.230 90.097  1.00 86.71  ? 327  ASN G C     1 
ATOM   12023 O  O     . ASN B 2 327  ? 151.771 123.650 91.192  1.00 82.19  ? 327  ASN G O     1 
ATOM   12024 C  CB    . ASN B 2 327  ? 148.900 123.063 90.309  1.00 77.93  ? 327  ASN G CB    1 
ATOM   12025 C  CG    . ASN B 2 327  ? 147.551 123.627 89.923  1.00 75.15  ? 327  ASN G CG    1 
ATOM   12026 O  OD1   . ASN B 2 327  ? 147.361 124.841 89.888  1.00 77.80  ? 327  ASN G OD1   1 
ATOM   12027 N  ND2   . ASN B 2 327  ? 146.608 122.746 89.616  1.00 74.63  ? 327  ASN G ND2   1 
ATOM   12028 N  N     . PHE B 2 328  ? 152.079 122.358 89.378  1.00 90.67  ? 328  PHE G N     1 
ATOM   12029 C  CA    . PHE B 2 328  ? 153.368 121.844 89.808  1.00 91.52  ? 328  PHE G CA    1 
ATOM   12030 C  C     . PHE B 2 328  ? 154.503 122.641 89.174  1.00 96.38  ? 328  PHE G C     1 
ATOM   12031 O  O     . PHE B 2 328  ? 154.324 123.340 88.174  1.00 97.38  ? 328  PHE G O     1 
ATOM   12032 C  CB    . PHE B 2 328  ? 153.504 120.366 89.445  1.00 89.86  ? 328  PHE G CB    1 
ATOM   12033 C  CG    . PHE B 2 328  ? 152.568 119.472 90.199  1.00 81.65  ? 328  PHE G CG    1 
ATOM   12034 C  CD1   . PHE B 2 328  ? 151.295 119.221 89.721  1.00 78.94  ? 328  PHE G CD1   1 
ATOM   12035 C  CD2   . PHE B 2 328  ? 152.959 118.891 91.391  1.00 78.72  ? 328  PHE G CD2   1 
ATOM   12036 C  CE1   . PHE B 2 328  ? 150.431 118.401 90.413  1.00 76.29  ? 328  PHE G CE1   1 
ATOM   12037 C  CE2   . PHE B 2 328  ? 152.102 118.071 92.088  1.00 74.36  ? 328  PHE G CE2   1 
ATOM   12038 C  CZ    . PHE B 2 328  ? 150.836 117.824 91.600  1.00 75.28  ? 328  PHE G CZ    1 
ATOM   12039 N  N     . ASP B 2 329  ? 155.682 122.531 89.776  1.00 99.29  ? 329  ASP G N     1 
ATOM   12040 C  CA    . ASP B 2 329  ? 156.866 123.185 89.241  1.00 105.65 ? 329  ASP G CA    1 
ATOM   12041 C  C     . ASP B 2 329  ? 157.527 122.318 88.176  1.00 107.31 ? 329  ASP G C     1 
ATOM   12042 O  O     . ASP B 2 329  ? 157.401 121.090 88.174  1.00 104.75 ? 329  ASP G O     1 
ATOM   12043 C  CB    . ASP B 2 329  ? 157.865 123.489 90.356  1.00 107.42 ? 329  ASP G CB    1 
ATOM   12044 C  CG    . ASP B 2 329  ? 157.231 124.211 91.525  1.00 110.02 ? 329  ASP G CG    1 
ATOM   12045 O  OD1   . ASP B 2 329  ? 156.214 124.905 91.316  1.00 106.17 ? 329  ASP G OD1   1 
ATOM   12046 O  OD2   . ASP B 2 329  ? 157.748 124.085 92.654  1.00 113.89 ? 329  ASP G OD2   1 
ATOM   12047 N  N     . ASP B 2 330  ? 158.254 122.992 87.291  1.00 110.31 ? 330  ASP G N     1 
ATOM   12048 C  CA    . ASP B 2 330  ? 158.972 122.358 86.203  1.00 111.96 ? 330  ASP G CA    1 
ATOM   12049 C  C     . ASP B 2 330  ? 160.249 121.680 86.686  1.00 109.66 ? 330  ASP G C     1 
ATOM   12050 O  O     . ASP B 2 330  ? 161.087 122.288 87.347  1.00 107.92 ? 330  ASP G O     1 
ATOM   12051 C  CB    . ASP B 2 330  ? 159.316 123.392 85.134  1.00 110.41 ? 330  ASP G CB    1 
ATOM   12052 C  CG    . ASP B 2 330  ? 158.111 123.810 84.315  1.00 115.05 ? 330  ASP G CG    1 
ATOM   12053 O  OD1   . ASP B 2 330  ? 157.111 123.067 84.295  1.00 115.32 ? 330  ASP G OD1   1 
ATOM   12054 O  OD2   . ASP B 2 330  ? 158.159 124.885 83.687  1.00 117.27 ? 330  ASP G OD2   1 
ATOM   12055 N  N     . TYR B 2 331  ? 160.370 120.402 86.356  1.00 106.80 ? 331  TYR G N     1 
ATOM   12056 C  CA    . TYR B 2 331  ? 161.531 119.600 86.697  1.00 105.60 ? 331  TYR G CA    1 
ATOM   12057 C  C     . TYR B 2 331  ? 161.979 118.887 85.430  1.00 104.79 ? 331  TYR G C     1 
ATOM   12058 O  O     . TYR B 2 331  ? 161.238 118.819 84.443  1.00 101.31 ? 331  TYR G O     1 
ATOM   12059 C  CB    . TYR B 2 331  ? 161.196 118.564 87.773  1.00 104.27 ? 331  TYR G CB    1 
ATOM   12060 C  CG    . TYR B 2 331  ? 160.926 119.145 89.139  1.00 105.32 ? 331  TYR G CG    1 
ATOM   12061 C  CD1   . TYR B 2 331  ? 161.959 119.560 89.959  1.00 105.69 ? 331  TYR G CD1   1 
ATOM   12062 C  CD2   . TYR B 2 331  ? 159.638 119.277 89.606  1.00 103.66 ? 331  TYR G CD2   1 
ATOM   12063 C  CE1   . TYR B 2 331  ? 161.711 120.097 91.202  1.00 108.10 ? 331  TYR G CE1   1 
ATOM   12064 C  CE2   . TYR B 2 331  ? 159.380 119.805 90.846  1.00 104.10 ? 331  TYR G CE2   1 
ATOM   12065 C  CZ    . TYR B 2 331  ? 160.418 120.215 91.638  1.00 106.65 ? 331  TYR G CZ    1 
ATOM   12066 O  OH    . TYR B 2 331  ? 160.143 120.747 92.870  1.00 105.01 ? 331  TYR G OH    1 
ATOM   12067 N  N     . LYS B 2 343  ? 170.169 93.565  91.382  1.00 122.38 ? 343  LYS G N     1 
ATOM   12068 C  CA    . LYS B 2 343  ? 170.674 94.532  92.348  1.00 123.73 ? 343  LYS G CA    1 
ATOM   12069 C  C     . LYS B 2 343  ? 169.998 94.367  93.703  1.00 126.08 ? 343  LYS G C     1 
ATOM   12070 O  O     . LYS B 2 343  ? 168.887 94.856  93.909  1.00 126.31 ? 343  LYS G O     1 
ATOM   12071 C  CB    . LYS B 2 343  ? 170.469 95.960  91.836  1.00 122.18 ? 343  LYS G CB    1 
ATOM   12072 C  CG    . LYS B 2 343  ? 171.314 96.352  90.625  1.00 120.34 ? 343  LYS G CG    1 
ATOM   12073 C  CD    . LYS B 2 343  ? 172.811 96.353  90.922  1.00 122.89 ? 343  LYS G CD    1 
ATOM   12074 C  CE    . LYS B 2 343  ? 173.496 95.090  90.421  1.00 120.49 ? 343  LYS G CE    1 
ATOM   12075 N  NZ    . LYS B 2 343  ? 174.948 95.080  90.746  1.00 119.22 ? 343  LYS G NZ    1 
ATOM   12076 N  N     . CYS B 2 344  ? 170.677 93.674  94.620  1.00 127.13 ? 344  CYS G N     1 
ATOM   12077 C  CA    . CYS B 2 344  ? 170.195 93.486  95.990  1.00 129.39 ? 344  CYS G CA    1 
ATOM   12078 C  C     . CYS B 2 344  ? 168.784 92.898  96.004  1.00 131.02 ? 344  CYS G C     1 
ATOM   12079 O  O     . CYS B 2 344  ? 167.856 93.457  96.593  1.00 129.89 ? 344  CYS G O     1 
ATOM   12080 C  CB    . CYS B 2 344  ? 170.253 94.798  96.778  1.00 126.99 ? 344  CYS G CB    1 
ATOM   12081 N  N     . GLY B 2 345  ? 168.623 91.763  95.326  1.00 129.24 ? 345  GLY G N     1 
ATOM   12082 C  CA    . GLY B 2 345  ? 167.337 91.090  95.292  1.00 129.11 ? 345  GLY G CA    1 
ATOM   12083 C  C     . GLY B 2 345  ? 166.989 90.332  96.556  1.00 132.60 ? 345  GLY G C     1 
ATOM   12084 O  O     . GLY B 2 345  ? 165.823 89.962  96.730  1.00 132.75 ? 345  GLY G O     1 
ATOM   12085 N  N     . LYS B 2 346  ? 167.962 90.096  97.437  1.00 131.31 ? 346  LYS G N     1 
ATOM   12086 C  CA    . LYS B 2 346  ? 167.687 89.363  98.668  1.00 129.67 ? 346  LYS G CA    1 
ATOM   12087 C  C     . LYS B 2 346  ? 166.931 90.220  99.677  1.00 129.73 ? 346  LYS G C     1 
ATOM   12088 O  O     . LYS B 2 346  ? 166.011 89.732  100.342 1.00 128.72 ? 346  LYS G O     1 
ATOM   12089 C  CB    . LYS B 2 346  ? 168.992 88.849  99.278  1.00 125.46 ? 346  LYS G CB    1 
ATOM   12090 N  N     . GLU B 2 347  ? 167.304 91.495  99.806  1.00 129.08 ? 347  GLU G N     1 
ATOM   12091 C  CA    . GLU B 2 347  ? 166.654 92.359  100.787 1.00 127.06 ? 347  GLU G CA    1 
ATOM   12092 C  C     . GLU B 2 347  ? 165.228 92.701  100.373 1.00 126.09 ? 347  GLU G C     1 
ATOM   12093 O  O     . GLU B 2 347  ? 164.350 92.866  101.228 1.00 124.61 ? 347  GLU G O     1 
ATOM   12094 C  CB    . GLU B 2 347  ? 167.475 93.632  100.991 1.00 124.40 ? 347  GLU G CB    1 
ATOM   12095 N  N     . PHE B 2 348  ? 164.975 92.810  99.070  1.00 126.78 ? 348  PHE G N     1 
ATOM   12096 C  CA    . PHE B 2 348  ? 163.662 93.192  98.554  1.00 127.38 ? 348  PHE G CA    1 
ATOM   12097 C  C     . PHE B 2 348  ? 162.953 91.932  98.067  1.00 125.08 ? 348  PHE G C     1 
ATOM   12098 O  O     . PHE B 2 348  ? 163.102 91.512  96.920  1.00 121.25 ? 348  PHE G O     1 
ATOM   12099 C  CB    . PHE B 2 348  ? 163.798 94.232  97.449  1.00 127.25 ? 348  PHE G CB    1 
ATOM   12100 C  CG    . PHE B 2 348  ? 164.589 95.442  97.853  1.00 125.76 ? 348  PHE G CG    1 
ATOM   12101 C  CD1   . PHE B 2 348  ? 164.240 96.168  98.980  1.00 122.35 ? 348  PHE G CD1   1 
ATOM   12102 C  CD2   . PHE B 2 348  ? 165.684 95.849  97.111  1.00 125.56 ? 348  PHE G CD2   1 
ATOM   12103 C  CE1   . PHE B 2 348  ? 164.965 97.281  99.356  1.00 121.69 ? 348  PHE G CE1   1 
ATOM   12104 C  CE2   . PHE B 2 348  ? 166.416 96.960  97.482  1.00 127.07 ? 348  PHE G CE2   1 
ATOM   12105 C  CZ    . PHE B 2 348  ? 166.056 97.678  98.607  1.00 126.73 ? 348  PHE G CZ    1 
ATOM   12106 N  N     . SER B 2 349  ? 162.170 91.327  98.960  1.00 125.97 ? 349  SER G N     1 
ATOM   12107 C  CA    . SER B 2 349  ? 161.412 90.121  98.648  1.00 124.26 ? 349  SER G CA    1 
ATOM   12108 C  C     . SER B 2 349  ? 159.932 90.302  98.967  1.00 124.35 ? 349  SER G C     1 
ATOM   12109 O  O     . SER B 2 349  ? 159.222 89.327  99.225  1.00 121.78 ? 349  SER G O     1 
ATOM   12110 C  CB    . SER B 2 349  ? 161.977 88.915  99.398  1.00 122.18 ? 349  SER G CB    1 
ATOM   12111 N  N     . GLU B 2 350  ? 159.451 91.547  98.955  1.00 125.65 ? 350  GLU G N     1 
ATOM   12112 C  CA    . GLU B 2 350  ? 158.046 91.825  99.227  1.00 119.72 ? 350  GLU G CA    1 
ATOM   12113 C  C     . GLU B 2 350  ? 157.489 92.872  98.269  1.00 120.97 ? 350  GLU G C     1 
ATOM   12114 O  O     . GLU B 2 350  ? 156.574 93.623  98.626  1.00 116.61 ? 350  GLU G O     1 
ATOM   12115 C  CB    . GLU B 2 350  ? 157.848 92.280  100.675 1.00 114.28 ? 350  GLU G CB    1 
ATOM   12116 N  N     . PHE B 2 351  ? 158.022 92.934  97.055  1.00 124.37 ? 351  PHE G N     1 
ATOM   12117 C  CA    . PHE B 2 351  ? 157.540 93.876  96.053  1.00 124.78 ? 351  PHE G CA    1 
ATOM   12118 C  C     . PHE B 2 351  ? 157.051 93.130  94.815  1.00 127.64 ? 351  PHE G C     1 
ATOM   12119 O  O     . PHE B 2 351  ? 157.484 92.009  94.547  1.00 127.06 ? 351  PHE G O     1 
ATOM   12120 C  CB    . PHE B 2 351  ? 158.640 94.870  95.673  1.00 119.28 ? 351  PHE G CB    1 
ATOM   12121 C  CG    . PHE B 2 351  ? 158.579 96.167  96.429  1.00 117.77 ? 351  PHE G CG    1 
ATOM   12122 C  CD1   . PHE B 2 351  ? 157.606 97.108  96.139  1.00 115.64 ? 351  PHE G CD1   1 
ATOM   12123 C  CD2   . PHE B 2 351  ? 159.499 96.448  97.425  1.00 115.92 ? 351  PHE G CD2   1 
ATOM   12124 C  CE1   . PHE B 2 351  ? 157.550 98.301  96.829  1.00 113.18 ? 351  PHE G CE1   1 
ATOM   12125 C  CE2   . PHE B 2 351  ? 159.448 97.640  98.119  1.00 108.93 ? 351  PHE G CE2   1 
ATOM   12126 C  CZ    . PHE B 2 351  ? 158.474 98.568  97.820  1.00 108.26 ? 351  PHE G CZ    1 
ATOM   12127 O  OXT   . PHE B 2 351  ? 156.217 93.626  94.057  1.00 127.27 ? 351  PHE G OXT   1 
HETATM 12128 C  C1    . CLR C 3 .    ? 140.923 125.221 179.956 1.00 44.81  ? 1501 CLR A C1    1 
HETATM 12129 C  C2    . CLR C 3 .    ? 140.811 125.185 181.480 1.00 41.63  ? 1501 CLR A C2    1 
HETATM 12130 C  C3    . CLR C 3 .    ? 141.966 125.926 182.113 1.00 43.72  ? 1501 CLR A C3    1 
HETATM 12131 C  C4    . CLR C 3 .    ? 141.988 127.364 181.634 1.00 48.36  ? 1501 CLR A C4    1 
HETATM 12132 C  C5    . CLR C 3 .    ? 141.983 127.469 180.126 1.00 45.36  ? 1501 CLR A C5    1 
HETATM 12133 C  C6    . CLR C 3 .    ? 142.846 128.255 179.503 1.00 45.35  ? 1501 CLR A C6    1 
HETATM 12134 C  C7    . CLR C 3 .    ? 142.932 128.434 178.020 1.00 43.31  ? 1501 CLR A C7    1 
HETATM 12135 C  C8    . CLR C 3 .    ? 141.681 127.945 177.300 1.00 44.30  ? 1501 CLR A C8    1 
HETATM 12136 C  C9    . CLR C 3 .    ? 141.243 126.590 177.872 1.00 46.02  ? 1501 CLR A C9    1 
HETATM 12137 C  C10   . CLR C 3 .    ? 140.922 126.652 179.394 1.00 44.66  ? 1501 CLR A C10   1 
HETATM 12138 C  C11   . CLR C 3 .    ? 140.112 125.954 177.051 1.00 43.30  ? 1501 CLR A C11   1 
HETATM 12139 C  C12   . CLR C 3 .    ? 140.393 125.914 175.548 1.00 40.90  ? 1501 CLR A C12   1 
HETATM 12140 C  C13   . CLR C 3 .    ? 140.728 127.305 174.992 1.00 47.42  ? 1501 CLR A C13   1 
HETATM 12141 C  C14   . CLR C 3 .    ? 141.943 127.805 175.800 1.00 43.29  ? 1501 CLR A C14   1 
HETATM 12142 C  C15   . CLR C 3 .    ? 142.436 129.022 175.006 1.00 47.75  ? 1501 CLR A C15   1 
HETATM 12143 C  C16   . CLR C 3 .    ? 142.117 128.684 173.541 1.00 48.89  ? 1501 CLR A C16   1 
HETATM 12144 C  C17   . CLR C 3 .    ? 141.308 127.372 173.559 1.00 41.44  ? 1501 CLR A C17   1 
HETATM 12145 C  C18   . CLR C 3 .    ? 139.521 128.246 175.145 1.00 49.82  ? 1501 CLR A C18   1 
HETATM 12146 C  C19   . CLR C 3 .    ? 139.549 127.299 179.658 1.00 45.24  ? 1501 CLR A C19   1 
HETATM 12147 C  C20   . CLR C 3 .    ? 140.355 127.275 172.352 1.00 45.11  ? 1501 CLR A C20   1 
HETATM 12148 C  C21   . CLR C 3 .    ? 139.715 125.900 172.183 1.00 45.95  ? 1501 CLR A C21   1 
HETATM 12149 C  C22   . CLR C 3 .    ? 141.081 127.698 171.064 1.00 38.91  ? 1501 CLR A C22   1 
HETATM 12150 C  C23   . CLR C 3 .    ? 142.076 126.689 170.514 1.00 42.95  ? 1501 CLR A C23   1 
HETATM 12151 C  C24   . CLR C 3 .    ? 143.057 127.311 169.530 1.00 45.30  ? 1501 CLR A C24   1 
HETATM 12152 C  C25   . CLR C 3 .    ? 142.454 128.166 168.428 1.00 42.59  ? 1501 CLR A C25   1 
HETATM 12153 C  C26   . CLR C 3 .    ? 143.536 128.840 167.604 1.00 45.45  ? 1501 CLR A C26   1 
HETATM 12154 C  C27   . CLR C 3 .    ? 141.526 127.368 167.532 1.00 49.79  ? 1501 CLR A C27   1 
HETATM 12155 O  O1    . CLR C 3 .    ? 141.857 125.892 183.537 1.00 45.61  ? 1501 CLR A O1    1 
HETATM 12156 C  C1    . D10 D 4 .    ? 159.226 127.746 174.691 1.00 56.35  ? 1502 D10 A C1    1 
HETATM 12157 C  C2    . D10 D 4 .    ? 158.464 127.688 176.008 1.00 60.07  ? 1502 D10 A C2    1 
HETATM 12158 C  C3    . D10 D 4 .    ? 159.240 127.025 177.139 1.00 65.99  ? 1502 D10 A C3    1 
HETATM 12159 C  C4    . D10 D 4 .    ? 158.439 126.934 178.432 1.00 73.75  ? 1502 D10 A C4    1 
HETATM 12160 C  C5    . D10 D 4 .    ? 159.199 126.286 179.583 1.00 70.68  ? 1502 D10 A C5    1 
HETATM 12161 C  C6    . D10 D 4 .    ? 158.354 126.143 180.842 1.00 70.91  ? 1502 D10 A C6    1 
HETATM 12162 C  C7    . D10 D 4 .    ? 159.094 125.496 182.007 1.00 71.41  ? 1502 D10 A C7    1 
HETATM 12163 C  C8    . D10 D 4 .    ? 158.223 125.354 183.247 1.00 68.48  ? 1502 D10 A C8    1 
HETATM 12164 C  C9    . D10 D 4 .    ? 158.940 124.732 184.437 1.00 65.05  ? 1502 D10 A C9    1 
HETATM 12165 C  C10   . D10 D 4 .    ? 157.964 124.418 185.557 1.00 61.16  ? 1502 D10 A C10   1 
HETATM 12166 MG MG    . MG  E 5 .    ? 141.986 165.642 106.374 1.00 33.18  ? 1503 MG  A MG    1 
HETATM 12167 MG MG    . MG  F 5 .    ? 156.949 178.166 110.651 1.00 35.03  ? 1504 MG  A MG    1 
HETATM 12168 P  PG    . ATP G 6 .    ? 140.523 168.706 105.208 1.00 35.26  ? 1505 ATP A PG    1 
HETATM 12169 O  O1G   . ATP G 6 .    ? 140.578 169.254 103.829 1.00 34.89  ? 1505 ATP A O1G   1 
HETATM 12170 O  O2G   . ATP G 6 .    ? 140.323 169.766 106.271 1.00 34.95  ? 1505 ATP A O2G   1 
HETATM 12171 O  O3G   . ATP G 6 .    ? 141.727 167.854 105.581 1.00 32.52  ? 1505 ATP A O3G   1 
HETATM 12172 P  PB    . ATP G 6 .    ? 138.801 166.287 104.915 1.00 28.39  ? 1505 ATP A PB    1 
HETATM 12173 O  O1B   . ATP G 6 .    ? 138.251 166.294 103.553 1.00 30.62  ? 1505 ATP A O1B   1 
HETATM 12174 O  O2B   . ATP G 6 .    ? 139.966 165.340 105.159 1.00 30.15  ? 1505 ATP A O2B   1 
HETATM 12175 O  O3B   . ATP G 6 .    ? 139.279 167.726 105.374 1.00 38.16  ? 1505 ATP A O3B   1 
HETATM 12176 P  PA    . ATP G 6 .    ? 137.440 164.857 107.116 1.00 33.13  ? 1505 ATP A PA    1 
HETATM 12177 O  O1A   . ATP G 6 .    ? 137.398 163.484 106.576 1.00 30.79  ? 1505 ATP A O1A   1 
HETATM 12178 O  O2A   . ATP G 6 .    ? 138.459 165.098 108.226 1.00 30.46  ? 1505 ATP A O2A   1 
HETATM 12179 O  O3A   . ATP G 6 .    ? 137.682 165.953 105.995 1.00 29.43  ? 1505 ATP A O3A   1 
HETATM 12180 O  "O5'" . ATP G 6 .    ? 136.018 165.258 107.667 1.00 38.52  ? 1505 ATP A "O5'" 1 
HETATM 12181 C  "C5'" . ATP G 6 .    ? 134.821 165.039 106.892 1.00 34.01  ? 1505 ATP A "C5'" 1 
HETATM 12182 C  "C4'" . ATP G 6 .    ? 133.677 165.180 107.858 1.00 33.52  ? 1505 ATP A "C4'" 1 
HETATM 12183 O  "O4'" . ATP G 6 .    ? 133.808 164.170 108.879 1.00 35.41  ? 1505 ATP A "O4'" 1 
HETATM 12184 C  "C3'" . ATP G 6 .    ? 133.616 166.532 108.573 1.00 34.45  ? 1505 ATP A "C3'" 1 
HETATM 12185 O  "O3'" . ATP G 6 .    ? 132.322 167.117 108.475 1.00 41.64  ? 1505 ATP A "O3'" 1 
HETATM 12186 C  "C2'" . ATP G 6 .    ? 134.003 166.206 110.020 1.00 32.83  ? 1505 ATP A "C2'" 1 
HETATM 12187 O  "O2'" . ATP G 6 .    ? 133.277 167.014 110.938 1.00 36.54  ? 1505 ATP A "O2'" 1 
HETATM 12188 C  "C1'" . ATP G 6 .    ? 133.584 164.744 110.143 1.00 32.51  ? 1505 ATP A "C1'" 1 
HETATM 12189 N  N9    . ATP G 6 .    ? 134.359 163.991 111.120 1.00 32.26  ? 1505 ATP A N9    1 
HETATM 12190 C  C8    . ATP G 6 .    ? 135.699 163.711 111.075 1.00 33.31  ? 1505 ATP A C8    1 
HETATM 12191 N  N7    . ATP G 6 .    ? 136.134 163.011 112.093 1.00 34.94  ? 1505 ATP A N7    1 
HETATM 12192 C  C5    . ATP G 6 .    ? 134.998 162.812 112.863 1.00 37.70  ? 1505 ATP A C5    1 
HETATM 12193 C  C6    . ATP G 6 .    ? 134.780 162.140 114.080 1.00 38.22  ? 1505 ATP A C6    1 
HETATM 12194 N  N6    . ATP G 6 .    ? 135.740 161.515 114.767 1.00 39.97  ? 1505 ATP A N6    1 
HETATM 12195 N  N1    . ATP G 6 .    ? 133.525 162.131 114.577 1.00 32.70  ? 1505 ATP A N1    1 
HETATM 12196 C  C2    . ATP G 6 .    ? 132.560 162.753 113.897 1.00 31.77  ? 1505 ATP A C2    1 
HETATM 12197 N  N3    . ATP G 6 .    ? 132.645 163.417 112.743 1.00 35.58  ? 1505 ATP A N3    1 
HETATM 12198 C  C4    . ATP G 6 .    ? 133.896 163.411 112.275 1.00 36.57  ? 1505 ATP A C4    1 
HETATM 12199 P  PG    . ATP H 6 .    ? 158.721 175.881 108.288 1.00 32.12  ? 1506 ATP A PG    1 
HETATM 12200 O  O1G   . ATP H 6 .    ? 158.537 176.403 106.912 1.00 30.76  ? 1506 ATP A O1G   1 
HETATM 12201 O  O2G   . ATP H 6 .    ? 159.017 174.398 108.337 1.00 32.82  ? 1506 ATP A O2G   1 
HETATM 12202 O  O3G   . ATP H 6 .    ? 157.555 176.179 109.218 1.00 38.42  ? 1506 ATP A O3G   1 
HETATM 12203 P  PB    . ATP H 6 .    ? 160.485 178.011 109.423 1.00 29.20  ? 1506 ATP A PB    1 
HETATM 12204 O  O1B   . ATP H 6 .    ? 160.984 178.782 108.273 1.00 31.59  ? 1506 ATP A O1B   1 
HETATM 12205 O  O2B   . ATP H 6 .    ? 159.356 178.648 110.222 1.00 35.97  ? 1506 ATP A O2B   1 
HETATM 12206 O  O3B   . ATP H 6 .    ? 159.980 176.571 108.990 1.00 35.65  ? 1506 ATP A O3B   1 
HETATM 12207 P  PA    . ATP H 6 .    ? 161.832 177.558 112.016 1.00 27.54  ? 1506 ATP A PA    1 
HETATM 12208 O  O1A   . ATP H 6 .    ? 162.023 178.872 112.661 1.00 33.48  ? 1506 ATP A O1A   1 
HETATM 12209 O  O2A   . ATP H 6 .    ? 160.663 176.742 112.551 1.00 31.28  ? 1506 ATP A O2A   1 
HETATM 12210 O  O3A   . ATP H 6 .    ? 161.657 177.674 110.445 1.00 26.52  ? 1506 ATP A O3A   1 
HETATM 12211 O  "O5'" . ATP H 6 .    ? 163.155 176.708 112.154 1.00 35.22  ? 1506 ATP A "O5'" 1 
HETATM 12212 C  "C5'" . ATP H 6 .    ? 164.451 177.288 111.893 1.00 32.55  ? 1506 ATP A "C5'" 1 
HETATM 12213 C  "C4'" . ATP H 6 .    ? 165.481 176.450 112.605 1.00 32.48  ? 1506 ATP A "C4'" 1 
HETATM 12214 O  "O4'" . ATP H 6 .    ? 165.252 176.531 114.026 1.00 38.92  ? 1506 ATP A "O4'" 1 
HETATM 12215 C  "C3'" . ATP H 6 .    ? 165.469 174.964 112.235 1.00 32.01  ? 1506 ATP A "C3'" 1 
HETATM 12216 O  "O3'" . ATP H 6 .    ? 166.758 174.520 111.830 1.00 37.61  ? 1506 ATP A "O3'" 1 
HETATM 12217 C  "C2'" . ATP H 6 .    ? 164.998 174.264 113.516 1.00 33.32  ? 1506 ATP A "C2'" 1 
HETATM 12218 O  "O2'" . ATP H 6 .    ? 165.661 173.019 113.691 1.00 34.81  ? 1506 ATP A "O2'" 1 
HETATM 12219 C  "C1'" . ATP H 6 .    ? 165.419 175.256 114.596 1.00 33.99  ? 1506 ATP A "C1'" 1 
HETATM 12220 N  N9    . ATP H 6 .    ? 164.604 175.192 115.802 1.00 33.12  ? 1506 ATP A N9    1 
HETATM 12221 C  C8    . ATP H 6 .    ? 163.264 175.460 115.908 1.00 32.47  ? 1506 ATP A C8    1 
HETATM 12222 N  N7    . ATP H 6 .    ? 162.785 175.320 117.119 1.00 32.79  ? 1506 ATP A N7    1 
HETATM 12223 C  C5    . ATP H 6 .    ? 163.888 174.936 117.865 1.00 34.87  ? 1506 ATP A C5    1 
HETATM 12224 C  C6    . ATP H 6 .    ? 164.052 174.629 119.229 1.00 35.35  ? 1506 ATP A C6    1 
HETATM 12225 N  N6    . ATP H 6 .    ? 163.060 174.662 120.124 1.00 36.99  ? 1506 ATP A N6    1 
HETATM 12226 N  N1    . ATP H 6 .    ? 165.286 174.281 119.651 1.00 36.47  ? 1506 ATP A N1    1 
HETATM 12227 C  C2    . ATP H 6 .    ? 166.282 174.245 118.763 1.00 36.50  ? 1506 ATP A C2    1 
HETATM 12228 N  N3    . ATP H 6 .    ? 166.248 174.513 117.457 1.00 36.08  ? 1506 ATP A N3    1 
HETATM 12229 C  C4    . ATP H 6 .    ? 165.016 174.853 117.066 1.00 35.59  ? 1506 ATP A C4    1 
HETATM 12230 CL CL    . CL  I 7 .    ? 151.999 140.014 186.665 1.00 53.57  ? 1507 CL  A CL    1 
HETATM 12231 CL CL    . CL  J 7 .    ? 150.349 135.371 184.811 1.00 72.26  ? 1508 CL  A CL    1 
HETATM 12232 CL CL    . CL  K 7 .    ? 146.512 133.675 183.023 1.00 64.54  ? 1509 CL  A CL    1 
HETATM 12233 CL CL    . CL  L 7 .    ? 144.285 132.801 187.462 1.00 75.95  ? 1510 CL  A CL    1 
HETATM 12234 C  C1    . UND M 8 .    ? 134.634 133.144 170.515 1.00 47.93  ? 1511 UND A C1    1 
HETATM 12235 C  C2    . UND M 8 .    ? 134.880 131.766 171.116 1.00 59.77  ? 1511 UND A C2    1 
HETATM 12236 C  C3    . UND M 8 .    ? 135.210 131.807 172.602 1.00 59.89  ? 1511 UND A C3    1 
HETATM 12237 C  C4    . UND M 8 .    ? 135.316 130.425 173.232 1.00 56.58  ? 1511 UND A C4    1 
HETATM 12238 C  C5    . UND M 8 .    ? 135.230 130.450 174.753 1.00 57.48  ? 1511 UND A C5    1 
HETATM 12239 C  C6    . UND M 8 .    ? 135.189 129.059 175.368 1.00 56.26  ? 1511 UND A C6    1 
HETATM 12240 C  C7    . UND M 8 .    ? 135.048 129.066 176.885 1.00 52.73  ? 1511 UND A C7    1 
HETATM 12241 C  C8    . UND M 8 .    ? 135.205 127.677 177.491 1.00 58.76  ? 1511 UND A C8    1 
HETATM 12242 C  C9    . UND M 8 .    ? 134.966 127.629 178.994 1.00 64.27  ? 1511 UND A C9    1 
HETATM 12243 C  C10   . UND M 8 .    ? 135.013 126.211 179.544 1.00 63.98  ? 1511 UND A C10   1 
HETATM 12244 C  C11   . UND M 8 .    ? 134.643 126.104 181.018 1.00 58.12  ? 1511 UND A C11   1 
HETATM 12245 C  C1    . UND N 8 .    ? 148.001 127.276 168.433 1.00 47.93  ? 1512 UND A C1    1 
HETATM 12246 C  C2    . UND N 8 .    ? 147.843 126.419 169.683 1.00 59.77  ? 1512 UND A C2    1 
HETATM 12247 C  C3    . UND N 8 .    ? 148.296 127.122 170.956 1.00 59.89  ? 1512 UND A C3    1 
HETATM 12248 C  C4    . UND N 8 .    ? 148.008 126.322 172.219 1.00 56.58  ? 1512 UND A C4    1 
HETATM 12249 C  C5    . UND N 8 .    ? 148.066 127.163 173.489 1.00 57.48  ? 1512 UND A C5    1 
HETATM 12250 C  C6    . UND N 8 .    ? 147.635 126.394 174.729 1.00 56.26  ? 1512 UND A C6    1 
HETATM 12251 C  C7    . UND N 8 .    ? 147.635 127.236 175.999 1.00 52.73  ? 1512 UND A C7    1 
HETATM 12252 C  C8    . UND N 8 .    ? 147.390 126.401 177.251 1.00 58.76  ? 1512 UND A C8    1 
HETATM 12253 C  C9    . UND N 8 .    ? 147.279 127.223 178.528 1.00 64.27  ? 1512 UND A C9    1 
HETATM 12254 C  C10   . UND N 8 .    ? 146.917 126.372 179.736 1.00 63.98  ? 1512 UND A C10   1 
HETATM 12255 C  C11   . UND N 8 .    ? 146.661 127.173 181.006 1.00 58.12  ? 1512 UND A C11   1 
HETATM 12256 C  C1    . UND O 8 .    ? 153.093 128.575 174.944 1.00 47.93  ? 1513 UND A C1    1 
HETATM 12257 C  C2    . UND O 8 .    ? 153.474 127.703 176.133 1.00 59.77  ? 1513 UND A C2    1 
HETATM 12258 C  C3    . UND O 8 .    ? 153.564 128.475 177.443 1.00 59.89  ? 1513 UND A C3    1 
HETATM 12259 C  C4    . UND O 8 .    ? 153.805 127.581 178.651 1.00 56.58  ? 1513 UND A C4    1 
HETATM 12260 C  C5    . UND O 8 .    ? 153.488 128.263 179.976 1.00 57.48  ? 1513 UND A C5    1 
HETATM 12261 C  C6    . UND O 8 .    ? 153.589 127.322 181.168 1.00 56.26  ? 1513 UND A C6    1 
HETATM 12262 C  C7    . UND O 8 .    ? 153.222 127.975 182.494 1.00 52.73  ? 1513 UND A C7    1 
HETATM 12263 C  C8    . UND O 8 .    ? 153.517 127.076 183.688 1.00 58.76  ? 1513 UND A C8    1 
HETATM 12264 C  C9    . UND O 8 .    ? 153.066 127.653 185.022 1.00 64.27  ? 1513 UND A C9    1 
HETATM 12265 C  C10   . UND O 8 .    ? 153.267 126.680 186.174 1.00 63.98  ? 1513 UND A C10   1 
HETATM 12266 C  C11   . UND O 8 .    ? 152.702 127.164 187.503 1.00 58.12  ? 1513 UND A C11   1 
HETATM 12267 C  C1    . D10 P 4 .    ? 169.036 148.595 179.811 1.00 61.45  ? 1514 D10 A C1    1 
HETATM 12268 C  C2    . D10 P 4 .    ? 170.153 148.963 180.779 1.00 64.67  ? 1514 D10 A C2    1 
HETATM 12269 C  C3    . D10 P 4 .    ? 170.914 147.763 181.327 1.00 67.88  ? 1514 D10 A C3    1 
HETATM 12270 C  C4    . D10 P 4 .    ? 171.768 148.117 182.538 1.00 75.21  ? 1514 D10 A C4    1 
HETATM 12271 C  C5    . D10 P 4 .    ? 172.500 146.931 183.155 1.00 72.92  ? 1514 D10 A C5    1 
HETATM 12272 C  C6    . D10 P 4 .    ? 173.109 147.264 184.511 1.00 71.44  ? 1514 D10 A C6    1 
HETATM 12273 C  C7    . D10 P 4 .    ? 173.708 146.063 185.232 1.00 71.12  ? 1514 D10 A C7    1 
HETATM 12274 C  C8    . D10 P 4 .    ? 174.059 146.377 186.679 1.00 77.51  ? 1514 D10 A C8    1 
HETATM 12275 C  C9    . D10 P 4 .    ? 174.526 145.171 187.483 1.00 78.41  ? 1514 D10 A C9    1 
HETATM 12276 C  C10   . D10 P 4 .    ? 174.726 145.541 188.942 1.00 71.46  ? 1514 D10 A C10   1 
HETATM 12277 C  C1    . D10 Q 4 .    ? 171.989 151.584 183.750 1.00 64.90  ? 1515 D10 A C1    1 
HETATM 12278 C  C2    . D10 Q 4 .    ? 170.889 151.737 184.792 1.00 75.13  ? 1515 D10 A C2    1 
HETATM 12279 C  C3    . D10 Q 4 .    ? 171.067 150.852 186.020 1.00 77.56  ? 1515 D10 A C3    1 
HETATM 12280 C  C4    . D10 Q 4 .    ? 170.190 151.296 187.183 1.00 69.31  ? 1515 D10 A C4    1 
HETATM 12281 C  C5    . D10 Q 4 .    ? 170.205 150.356 188.382 1.00 66.38  ? 1515 D10 A C5    1 
HETATM 12282 C  C6    . D10 Q 4 .    ? 169.477 150.957 189.577 1.00 72.24  ? 1515 D10 A C6    1 
HETATM 12283 C  C7    . D10 Q 4 .    ? 169.245 149.994 190.734 1.00 70.52  ? 1515 D10 A C7    1 
HETATM 12284 C  C8    . D10 Q 4 .    ? 168.504 150.667 191.881 1.00 76.41  ? 1515 D10 A C8    1 
HETATM 12285 C  C9    . D10 Q 4 .    ? 167.988 149.712 192.948 1.00 75.52  ? 1515 D10 A C9    1 
HETATM 12286 C  C10   . D10 Q 4 .    ? 167.066 150.432 193.915 1.00 68.78  ? 1515 D10 A C10   1 
HETATM 12287 C  C1    . D10 R 4 .    ? 142.387 150.703 184.456 1.00 62.43  ? 1516 D10 A C1    1 
HETATM 12288 C  C2    . D10 R 4 .    ? 141.443 149.888 185.328 1.00 68.25  ? 1516 D10 A C2    1 
HETATM 12289 C  C3    . D10 R 4 .    ? 141.058 150.572 186.634 1.00 74.78  ? 1516 D10 A C3    1 
HETATM 12290 C  C4    . D10 R 4 .    ? 140.075 149.747 187.457 1.00 77.14  ? 1516 D10 A C4    1 
HETATM 12291 C  C5    . D10 R 4 .    ? 139.469 150.498 188.636 1.00 76.24  ? 1516 D10 A C5    1 
HETATM 12292 C  C6    . D10 R 4 .    ? 138.388 149.697 189.350 1.00 79.95  ? 1516 D10 A C6    1 
HETATM 12293 C  C7    . D10 R 4 .    ? 137.834 150.384 190.592 1.00 83.88  ? 1516 D10 A C7    1 
HETATM 12294 C  C8    . D10 R 4 .    ? 136.762 149.560 191.288 1.00 78.35  ? 1516 D10 A C8    1 
HETATM 12295 C  C9    . D10 R 4 .    ? 136.265 150.170 192.592 1.00 78.76  ? 1516 D10 A C9    1 
HETATM 12296 C  C10   . D10 R 4 .    ? 135.139 149.344 193.185 1.00 74.25  ? 1516 D10 A C10   1 
HETATM 12297 P  PG    . ATP S 6 .    ? 160.589 113.266 101.221 1.00 92.88  ? 401  ATP G PG    1 
HETATM 12298 O  O1G   . ATP S 6 .    ? 161.854 114.008 100.912 1.00 88.64  ? 401  ATP G O1G   1 
HETATM 12299 O  O2G   . ATP S 6 .    ? 159.506 114.125 101.829 1.00 79.72  ? 401  ATP G O2G   1 
HETATM 12300 O  O3G   . ATP S 6 .    ? 160.783 111.936 101.892 1.00 85.25  ? 401  ATP G O3G   1 
HETATM 12301 P  PB    . ATP S 6 .    ? 159.989 111.398 99.241  1.00 82.87  ? 401  ATP G PB    1 
HETATM 12302 O  O1B   . ATP S 6 .    ? 161.373 111.144 98.764  1.00 92.97  ? 401  ATP G O1B   1 
HETATM 12303 O  O2B   . ATP S 6 .    ? 159.419 110.498 100.285 1.00 79.20  ? 401  ATP G O2B   1 
HETATM 12304 O  O3B   . ATP S 6 .    ? 159.991 112.893 99.775  1.00 87.20  ? 401  ATP G O3B   1 
HETATM 12305 P  PA    . ATP S 6 .    ? 157.584 112.069 97.993  1.00 80.11  ? 401  ATP G PA    1 
HETATM 12306 O  O1A   . ATP S 6 .    ? 156.546 110.995 97.964  1.00 79.47  ? 401  ATP G O1A   1 
HETATM 12307 O  O2A   . ATP S 6 .    ? 157.566 113.124 99.014  1.00 71.02  ? 401  ATP G O2A   1 
HETATM 12308 O  O3A   . ATP S 6 .    ? 159.028 111.409 97.973  1.00 79.48  ? 401  ATP G O3A   1 
HETATM 12309 O  "O5'" . ATP S 6 .    ? 157.457 112.850 96.606  1.00 83.71  ? 401  ATP G "O5'" 1 
HETATM 12310 C  "C5'" . ATP S 6 .    ? 157.740 114.240 96.564  1.00 80.35  ? 401  ATP G "C5'" 1 
HETATM 12311 C  "C4'" . ATP S 6 .    ? 156.749 114.996 95.696  1.00 75.41  ? 401  ATP G "C4'" 1 
HETATM 12312 O  "O4'" . ATP S 6 .    ? 156.150 114.171 94.714  1.00 75.46  ? 401  ATP G "O4'" 1 
HETATM 12313 C  "C3'" . ATP S 6 .    ? 155.577 115.498 96.480  1.00 72.92  ? 401  ATP G "C3'" 1 
HETATM 12314 O  "O3'" . ATP S 6 .    ? 155.932 116.685 97.163  1.00 73.58  ? 401  ATP G "O3'" 1 
HETATM 12315 C  "C2'" . ATP S 6 .    ? 154.599 115.761 95.382  1.00 70.15  ? 401  ATP G "C2'" 1 
HETATM 12316 O  "O2'" . ATP S 6 .    ? 155.001 116.922 94.708  1.00 71.81  ? 401  ATP G "O2'" 1 
HETATM 12317 C  "C1'" . ATP S 6 .    ? 154.867 114.684 94.382  1.00 71.35  ? 401  ATP G "C1'" 1 
HETATM 12318 N  N9    . ATP S 6 .    ? 153.806 113.657 94.481  1.00 72.14  ? 401  ATP G N9    1 
HETATM 12319 C  C8    . ATP S 6 .    ? 153.829 112.549 95.218  1.00 71.13  ? 401  ATP G C8    1 
HETATM 12320 N  N7    . ATP S 6 .    ? 152.692 111.855 95.055  1.00 69.10  ? 401  ATP G N7    1 
HETATM 12321 C  C5    . ATP S 6 .    ? 151.921 112.521 94.206  1.00 66.55  ? 401  ATP G C5    1 
HETATM 12322 C  C6    . ATP S 6 .    ? 150.607 112.349 93.609  1.00 63.75  ? 401  ATP G C6    1 
HETATM 12323 N  N6    . ATP S 6 .    ? 149.835 111.295 93.884  1.00 64.08  ? 401  ATP G N6    1 
HETATM 12324 N  N1    . ATP S 6 .    ? 150.190 113.280 92.768  1.00 65.31  ? 401  ATP G N1    1 
HETATM 12325 C  C2    . ATP S 6 .    ? 150.904 114.347 92.467  1.00 64.48  ? 401  ATP G C2    1 
HETATM 12326 N  N3    . ATP S 6 .    ? 152.100 114.554 92.974  1.00 65.82  ? 401  ATP G N3    1 
HETATM 12327 C  C4    . ATP S 6 .    ? 152.656 113.699 93.830  1.00 67.64  ? 401  ATP G C4    1 
HETATM 12328 MG MG    . MG  T 5 .    ? 159.574 110.239 102.682 1.00 77.96  ? 402  MG  G MG    1 
HETATM 12329 MG MG    . MG  U 5 .    ? 157.441 114.196 100.934 1.00 69.10  ? 403  MG  G MG    1 
HETATM 12330 O  O     . HOH V 9 .    ? 142.754 165.536 104.606 1.00 32.67  ? 1601 HOH A O     1 
HETATM 12331 O  O     . HOH V 9 .    ? 141.295 165.958 108.247 1.00 29.75  ? 1602 HOH A O     1 
HETATM 12332 O  O     . HOH V 9 .    ? 144.361 129.826 189.693 1.00 48.53  ? 1603 HOH A O     1 
# 
