data_9IP3
# 
_entry.id   9IP3 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9IP3         pdb_00009ip3 10.2210/pdb9ip3/pdb 
WWPDB D_1300049252 ?            ?                   
EMDB  EMD-60756    ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-04-09 ? 
2 'Structure model' 1 1 2025-04-16 ? 
# 
_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' 
# 
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' 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.page_last'               
2 2 'Structure model' '_citation.pdbx_database_id_PubMed' 
3 2 'Structure model' '_citation.title'                   
4 2 '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                        9IP3 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-10 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB  .                                                                                                           9IP2      
unspecified            
EMDB 
;Cryo-EM structure of the RNA-dependent RNA polymerase complex in 
a compact conformation from Ebola virus
;
EMD-60756 'associated EM volume' 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              hengru@zju.edu.cn 
_pdbx_contact_author.name_first         Heng 
_pdbx_contact_author.name_last          Ru 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-7761-193X 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Li, G.'   1 ? 
'Du, T.'   2 ? 
'Wang, J.' 3 ? 
'Wu, S.'   4 ? 
'Ru, H.'   5 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Nat Commun' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2041-1723 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            16 
_citation.language                  ? 
_citation.page_first                3080 
_citation.page_last                 3080 
_citation.title                     
'Structural insights into the RNA-dependent RNA polymerase complexes from highly pathogenic Marburg and Ebola viruses.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41467-025-58308-1 
_citation.pdbx_database_id_PubMed   40164610 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Li, G.'    1 ? 
primary 'Du, T.'    2 ? 
primary 'Wang, J.'  3 ? 
primary 'Jie, K.'   4 ? 
primary 'Ren, Z.'   5 ? 
primary 'Zhang, X.' 6 ? 
primary 'Zhang, L.' 7 ? 
primary 'Wu, S.'    8 ? 
primary 'Ru, H.'    9 ? 
# 
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 'Maltose/maltodextrin-binding periplasmic protein,RNA-directed RNA polymerase L' 207335.219 1 
2.7.7.48,3.6.1.-,2.7.7.88,2.1.1.375 ? ? 
;Sequence reference for Ebola virus - Eckron (Zaire, 1976) (12900) is not available in UniProt at the time of biocuration. Current sequence reference is from UniProt ID Q05318.
;
2 polymer     man 'Maltose/maltodextrin-binding periplasmic protein,Polymerase cofactor VP35'      72190.336  4 ? ? ? 
;Sequence reference for Ebola virus - Eckron (Zaire, 1976) (12900) is not available in UniProt at the time of biocuration. Current sequence reference is from UniProt ID Q05127.
;
3 non-polymer syn 'ZINC ION'                                                                       65.409     1 ? ? ? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 'MMBP,Maltodextrin-binding protein,Maltose-binding protein,MBP,Protein L,Large structural protein,Replicase,Transcriptase' 
2 'MMBP,Maltodextrin-binding protein,Maltose-binding protein,MBP,Ebola VP35,eVP35'                                           
# 
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 no 
;MGSGWSHPQFEKGGGSGGGSGGSAWSHPQFEKGSASHHHHHHGTKTEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVT
VEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLI
YNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDIKDVGVDNAGAKAGLTFLV
DLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKVNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELA
KEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQT
VDEALKDAQTGTDYDIPTTLEVLFQGPGSMATQHTQYPDARLSSPIVLDQCDLVTRACGLYSSYSLNPQLRNCKLPKHIY
RLKYDVTVTKFLSDVPVATLPIDFIVPVLLKALSGNGFCPVEPRCQQFLDEIIKYTMQDALFLKYYLKNVGAQEDCVDEH
FQEKILSSIQGNEFLHQMFFWYDLAILTRRGRLNRGNSRSTWFVHDDLIDILGYGDYVFWKIPISMLPLNTQGIPHAAMD
WYQASVFKEAVQGHTHIVSVSTADVLIMCKDLITCRFNTTLISKIAEIEDPVCSDYPNFKIVSMLYQSGDYLLSILGSDG
YKIIKFLEPLCLAKIQLCSKYTERKGRFLTQMHLAVNHTLEEITEMRALKPSQAQKIREFHRTLIRLEMTPQQLCELFSI
QKHWGHPVLHSETAIQKVKKHATVLKALRPIVIFETYCVFKYSIAKHYFDSQGSWYSVTSDRNLTPGLNSYIKRNQFPPL
PMIKELLWEFYHLDHPPLFSTKIISDLSIFIKDRATAVERTCWDAVFEPNVLGYNPPHKFSTKRVPEQFLEQENFSIENV
LSYAQKLEYLLPQYRNFSFSLKEKELNVGRTFGKLPYPTRNVQTLCEALLADGLAKAFPSNMMVVTEREQKESLLHQASW
HHTSDDFGEHATVRGSSFVTDLEKYNLAFRYEFTAPFIEYCNRCYGVKNVFNWMHYTIPQCYMHVSDYYNPPHNLTLENR
DNPPEGPSSYRGHMGGIEGLQQKLWTSISCAQISLVEIKTGFKLRSAVMGDNQCITVLSVFPLETDADEQEQSAEDNAAR
VAASLAKVTSACGIFLKPDETFVHSGFIYFGKKQYLNGVQLPQSLKTATRMAPLSDAIFDDLQGTLASIGTAFERSISET
RHIFPCRITAAFHTFFSVRILQYHHLGFNKGFDLGQLTLGKPLDFGTISLALAVPQVLGGLSFLNPEKCFYRNLGDPVTS
GLFQLKTYLRMIEMDDLFLPLIAKNPGNCTAIDFVLNPSGLNVPGSQDLTSFLRQIVRRTITLSAKNKLINTLFHASADF
EDEMVCKWLLSSTPVMSRFAADIFSRTPSGKRLQILGYLEGTRTLLASKIINNNTETPVLDRLRKITLQRWSLWFSYLDH
CDNILAEALTQITCTVDLAQILREYSWAHILEGRPLIGATLPCMIEQFKVFWLKPYEQCPQCSNAKQPGGKPFVSVAVKK
HIVSAWPNASRISWTIGDGIPYIGSRTEDKIGQPAIKPKCPSAALREAIELASRLTWVTQGSSNSDLLIKPFLEARVNLS
VQEILQMTPSHYSGNIVHRYNDQYSPHSFMANRMSNSATRLIVSTNTLGEFSGGGQSARDSNIIFQNVINYAVALFDIKF
RNTEATDIQYNRAHLHLTKCCTREVPAQYLTYTSTLDLDLTRYRENELIYDSNPLKGGLNCNISFDNPFSRDYKDDDDK
;
;MGSGWSHPQFEKGGGSGGGSGGSAWSHPQFEKGSASHHHHHHGTKTEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVT
VEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLI
YNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDIKDVGVDNAGAKAGLTFLV
DLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKVNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELA
KEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQT
VDEALKDAQTGTDYDIPTTLEVLFQGPGSMATQHTQYPDARLSSPIVLDQCDLVTRACGLYSSYSLNPQLRNCKLPKHIY
RLKYDVTVTKFLSDVPVATLPIDFIVPVLLKALSGNGFCPVEPRCQQFLDEIIKYTMQDALFLKYYLKNVGAQEDCVDEH
FQEKILSSIQGNEFLHQMFFWYDLAILTRRGRLNRGNSRSTWFVHDDLIDILGYGDYVFWKIPISMLPLNTQGIPHAAMD
WYQASVFKEAVQGHTHIVSVSTADVLIMCKDLITCRFNTTLISKIAEIEDPVCSDYPNFKIVSMLYQSGDYLLSILGSDG
YKIIKFLEPLCLAKIQLCSKYTERKGRFLTQMHLAVNHTLEEITEMRALKPSQAQKIREFHRTLIRLEMTPQQLCELFSI
QKHWGHPVLHSETAIQKVKKHATVLKALRPIVIFETYCVFKYSIAKHYFDSQGSWYSVTSDRNLTPGLNSYIKRNQFPPL
PMIKELLWEFYHLDHPPLFSTKIISDLSIFIKDRATAVERTCWDAVFEPNVLGYNPPHKFSTKRVPEQFLEQENFSIENV
LSYAQKLEYLLPQYRNFSFSLKEKELNVGRTFGKLPYPTRNVQTLCEALLADGLAKAFPSNMMVVTEREQKESLLHQASW
HHTSDDFGEHATVRGSSFVTDLEKYNLAFRYEFTAPFIEYCNRCYGVKNVFNWMHYTIPQCYMHVSDYYNPPHNLTLENR
DNPPEGPSSYRGHMGGIEGLQQKLWTSISCAQISLVEIKTGFKLRSAVMGDNQCITVLSVFPLETDADEQEQSAEDNAAR
VAASLAKVTSACGIFLKPDETFVHSGFIYFGKKQYLNGVQLPQSLKTATRMAPLSDAIFDDLQGTLASIGTAFERSISET
RHIFPCRITAAFHTFFSVRILQYHHLGFNKGFDLGQLTLGKPLDFGTISLALAVPQVLGGLSFLNPEKCFYRNLGDPVTS
GLFQLKTYLRMIEMDDLFLPLIAKNPGNCTAIDFVLNPSGLNVPGSQDLTSFLRQIVRRTITLSAKNKLINTLFHASADF
EDEMVCKWLLSSTPVMSRFAADIFSRTPSGKRLQILGYLEGTRTLLASKIINNNTETPVLDRLRKITLQRWSLWFSYLDH
CDNILAEALTQITCTVDLAQILREYSWAHILEGRPLIGATLPCMIEQFKVFWLKPYEQCPQCSNAKQPGGKPFVSVAVKK
HIVSAWPNASRISWTIGDGIPYIGSRTEDKIGQPAIKPKCPSAALREAIELASRLTWVTQGSSNSDLLIKPFLEARVNLS
VQEILQMTPSHYSGNIVHRYNDQYSPHSFMANRMSNSATRLIVSTNTLGEFSGGGQSARDSNIIFQNVINYAVALFDIKF
RNTEATDIQYNRAHLHLTKCCTREVPAQYLTYTSTLDLDLTRYRENELIYDSNPLKGGLNCNISFDNPFSRDYKDDDDK
;
A       ? 
2 'polypeptide(L)' no no 
;MGSSHHHHHHGTKTEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFG
GYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALM
FNLQEPYFTWPLIAADGGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTING
PWAWSNIDTSKVNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYE
EELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQTGTDYDIPTTENLYFQGGSNHSF
EEVVQTLASLATVVQQQTIASESLEQRITSLENGLKPVYDMAKTISSLNRVCAEMVAKYDLLVMTTGRATATAAATEAYW
AEHGQPPPGPSLYEESAIRGKIESRDETVPQSVREAFNNLNSTTSLTEENFGKPDISAKDLRNIMYDHLPGFGTAFHQLV
QVICKLGKDSNSLDIIHAEFQASLAEGDSPQCALIQITKRVPIFQDAAPPVIHIRSRGDIPRACQKSLRPVPPSPKIDRG
WVCVFQLQDGKTLGLKI
;
;MGSSHHHHHHGTKTEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFG
GYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALM
FNLQEPYFTWPLIAADGGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTING
PWAWSNIDTSKVNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYE
EELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQTGTDYDIPTTENLYFQGGSNHSF
EEVVQTLASLATVVQQQTIASESLEQRITSLENGLKPVYDMAKTISSLNRVCAEMVAKYDLLVMTTGRATATAAATEAYW
AEHGQPPPGPSLYEESAIRGKIESRDETVPQSVREAFNNLNSTTSLTEENFGKPDISAKDLRNIMYDHLPGFGTAFHQLV
QVICKLGKDSNSLDIIHAEFQASLAEGDSPQCALIQITKRVPIFQDAAPPVIHIRSRGDIPRACQKSLRPVPPSPKIDRG
WVCVFQLQDGKTLGLKI
;
B,C,D,E ? 
# 
_pdbx_entity_nonpoly.entity_id   3 
_pdbx_entity_nonpoly.name        'ZINC ION' 
_pdbx_entity_nonpoly.comp_id     ZN 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1    MET n 
1 2    GLY n 
1 3    SER n 
1 4    GLY n 
1 5    TRP n 
1 6    SER n 
1 7    HIS n 
1 8    PRO n 
1 9    GLN n 
1 10   PHE n 
1 11   GLU n 
1 12   LYS n 
1 13   GLY n 
1 14   GLY n 
1 15   GLY n 
1 16   SER n 
1 17   GLY n 
1 18   GLY n 
1 19   GLY n 
1 20   SER n 
1 21   GLY n 
1 22   GLY n 
1 23   SER n 
1 24   ALA n 
1 25   TRP n 
1 26   SER n 
1 27   HIS n 
1 28   PRO n 
1 29   GLN n 
1 30   PHE n 
1 31   GLU n 
1 32   LYS n 
1 33   GLY n 
1 34   SER n 
1 35   ALA n 
1 36   SER n 
1 37   HIS n 
1 38   HIS n 
1 39   HIS n 
1 40   HIS n 
1 41   HIS n 
1 42   HIS n 
1 43   GLY n 
1 44   THR n 
1 45   LYS n 
1 46   THR n 
1 47   GLU n 
1 48   GLU n 
1 49   GLY n 
1 50   LYS n 
1 51   LEU n 
1 52   VAL n 
1 53   ILE n 
1 54   TRP n 
1 55   ILE n 
1 56   ASN n 
1 57   GLY n 
1 58   ASP n 
1 59   LYS n 
1 60   GLY n 
1 61   TYR n 
1 62   ASN n 
1 63   GLY n 
1 64   LEU n 
1 65   ALA n 
1 66   GLU n 
1 67   VAL n 
1 68   GLY n 
1 69   LYS n 
1 70   LYS n 
1 71   PHE n 
1 72   GLU n 
1 73   LYS n 
1 74   ASP n 
1 75   THR n 
1 76   GLY n 
1 77   ILE n 
1 78   LYS n 
1 79   VAL n 
1 80   THR n 
1 81   VAL n 
1 82   GLU n 
1 83   HIS n 
1 84   PRO n 
1 85   ASP n 
1 86   LYS n 
1 87   LEU n 
1 88   GLU n 
1 89   GLU n 
1 90   LYS n 
1 91   PHE n 
1 92   PRO n 
1 93   GLN n 
1 94   VAL n 
1 95   ALA n 
1 96   ALA n 
1 97   THR n 
1 98   GLY n 
1 99   ASP n 
1 100  GLY n 
1 101  PRO n 
1 102  ASP n 
1 103  ILE n 
1 104  ILE n 
1 105  PHE n 
1 106  TRP n 
1 107  ALA n 
1 108  HIS n 
1 109  ASP n 
1 110  ARG n 
1 111  PHE n 
1 112  GLY n 
1 113  GLY n 
1 114  TYR n 
1 115  ALA n 
1 116  GLN n 
1 117  SER n 
1 118  GLY n 
1 119  LEU n 
1 120  LEU n 
1 121  ALA n 
1 122  GLU n 
1 123  ILE n 
1 124  THR n 
1 125  PRO n 
1 126  ASP n 
1 127  LYS n 
1 128  ALA n 
1 129  PHE n 
1 130  GLN n 
1 131  ASP n 
1 132  LYS n 
1 133  LEU n 
1 134  TYR n 
1 135  PRO n 
1 136  PHE n 
1 137  THR n 
1 138  TRP n 
1 139  ASP n 
1 140  ALA n 
1 141  VAL n 
1 142  ARG n 
1 143  TYR n 
1 144  ASN n 
1 145  GLY n 
1 146  LYS n 
1 147  LEU n 
1 148  ILE n 
1 149  ALA n 
1 150  TYR n 
1 151  PRO n 
1 152  ILE n 
1 153  ALA n 
1 154  VAL n 
1 155  GLU n 
1 156  ALA n 
1 157  LEU n 
1 158  SER n 
1 159  LEU n 
1 160  ILE n 
1 161  TYR n 
1 162  ASN n 
1 163  LYS n 
1 164  ASP n 
1 165  LEU n 
1 166  LEU n 
1 167  PRO n 
1 168  ASN n 
1 169  PRO n 
1 170  PRO n 
1 171  LYS n 
1 172  THR n 
1 173  TRP n 
1 174  GLU n 
1 175  GLU n 
1 176  ILE n 
1 177  PRO n 
1 178  ALA n 
1 179  LEU n 
1 180  ASP n 
1 181  LYS n 
1 182  GLU n 
1 183  LEU n 
1 184  LYS n 
1 185  ALA n 
1 186  LYS n 
1 187  GLY n 
1 188  LYS n 
1 189  SER n 
1 190  ALA n 
1 191  LEU n 
1 192  MET n 
1 193  PHE n 
1 194  ASN n 
1 195  LEU n 
1 196  GLN n 
1 197  GLU n 
1 198  PRO n 
1 199  TYR n 
1 200  PHE n 
1 201  THR n 
1 202  TRP n 
1 203  PRO n 
1 204  LEU n 
1 205  ILE n 
1 206  ALA n 
1 207  ALA n 
1 208  ASP n 
1 209  GLY n 
1 210  GLY n 
1 211  TYR n 
1 212  ALA n 
1 213  PHE n 
1 214  LYS n 
1 215  TYR n 
1 216  GLU n 
1 217  ASN n 
1 218  GLY n 
1 219  LYS n 
1 220  TYR n 
1 221  ASP n 
1 222  ILE n 
1 223  LYS n 
1 224  ASP n 
1 225  VAL n 
1 226  GLY n 
1 227  VAL n 
1 228  ASP n 
1 229  ASN n 
1 230  ALA n 
1 231  GLY n 
1 232  ALA n 
1 233  LYS n 
1 234  ALA n 
1 235  GLY n 
1 236  LEU n 
1 237  THR n 
1 238  PHE n 
1 239  LEU n 
1 240  VAL n 
1 241  ASP n 
1 242  LEU n 
1 243  ILE n 
1 244  LYS n 
1 245  ASN n 
1 246  LYS n 
1 247  HIS n 
1 248  MET n 
1 249  ASN n 
1 250  ALA n 
1 251  ASP n 
1 252  THR n 
1 253  ASP n 
1 254  TYR n 
1 255  SER n 
1 256  ILE n 
1 257  ALA n 
1 258  GLU n 
1 259  ALA n 
1 260  ALA n 
1 261  PHE n 
1 262  ASN n 
1 263  LYS n 
1 264  GLY n 
1 265  GLU n 
1 266  THR n 
1 267  ALA n 
1 268  MET n 
1 269  THR n 
1 270  ILE n 
1 271  ASN n 
1 272  GLY n 
1 273  PRO n 
1 274  TRP n 
1 275  ALA n 
1 276  TRP n 
1 277  SER n 
1 278  ASN n 
1 279  ILE n 
1 280  ASP n 
1 281  THR n 
1 282  SER n 
1 283  LYS n 
1 284  VAL n 
1 285  ASN n 
1 286  TYR n 
1 287  GLY n 
1 288  VAL n 
1 289  THR n 
1 290  VAL n 
1 291  LEU n 
1 292  PRO n 
1 293  THR n 
1 294  PHE n 
1 295  LYS n 
1 296  GLY n 
1 297  GLN n 
1 298  PRO n 
1 299  SER n 
1 300  LYS n 
1 301  PRO n 
1 302  PHE n 
1 303  VAL n 
1 304  GLY n 
1 305  VAL n 
1 306  LEU n 
1 307  SER n 
1 308  ALA n 
1 309  GLY n 
1 310  ILE n 
1 311  ASN n 
1 312  ALA n 
1 313  ALA n 
1 314  SER n 
1 315  PRO n 
1 316  ASN n 
1 317  LYS n 
1 318  GLU n 
1 319  LEU n 
1 320  ALA n 
1 321  LYS n 
1 322  GLU n 
1 323  PHE n 
1 324  LEU n 
1 325  GLU n 
1 326  ASN n 
1 327  TYR n 
1 328  LEU n 
1 329  LEU n 
1 330  THR n 
1 331  ASP n 
1 332  GLU n 
1 333  GLY n 
1 334  LEU n 
1 335  GLU n 
1 336  ALA n 
1 337  VAL n 
1 338  ASN n 
1 339  LYS n 
1 340  ASP n 
1 341  LYS n 
1 342  PRO n 
1 343  LEU n 
1 344  GLY n 
1 345  ALA n 
1 346  VAL n 
1 347  ALA n 
1 348  LEU n 
1 349  LYS n 
1 350  SER n 
1 351  TYR n 
1 352  GLU n 
1 353  GLU n 
1 354  GLU n 
1 355  LEU n 
1 356  ALA n 
1 357  LYS n 
1 358  ASP n 
1 359  PRO n 
1 360  ARG n 
1 361  ILE n 
1 362  ALA n 
1 363  ALA n 
1 364  THR n 
1 365  MET n 
1 366  GLU n 
1 367  ASN n 
1 368  ALA n 
1 369  GLN n 
1 370  LYS n 
1 371  GLY n 
1 372  GLU n 
1 373  ILE n 
1 374  MET n 
1 375  PRO n 
1 376  ASN n 
1 377  ILE n 
1 378  PRO n 
1 379  GLN n 
1 380  MET n 
1 381  SER n 
1 382  ALA n 
1 383  PHE n 
1 384  TRP n 
1 385  TYR n 
1 386  ALA n 
1 387  VAL n 
1 388  ARG n 
1 389  THR n 
1 390  ALA n 
1 391  VAL n 
1 392  ILE n 
1 393  ASN n 
1 394  ALA n 
1 395  ALA n 
1 396  SER n 
1 397  GLY n 
1 398  ARG n 
1 399  GLN n 
1 400  THR n 
1 401  VAL n 
1 402  ASP n 
1 403  GLU n 
1 404  ALA n 
1 405  LEU n 
1 406  LYS n 
1 407  ASP n 
1 408  ALA n 
1 409  GLN n 
1 410  THR n 
1 411  GLY n 
1 412  THR n 
1 413  ASP n 
1 414  TYR n 
1 415  ASP n 
1 416  ILE n 
1 417  PRO n 
1 418  THR n 
1 419  THR n 
1 420  LEU n 
1 421  GLU n 
1 422  VAL n 
1 423  LEU n 
1 424  PHE n 
1 425  GLN n 
1 426  GLY n 
1 427  PRO n 
1 428  GLY n 
1 429  SER n 
1 430  MET n 
1 431  ALA n 
1 432  THR n 
1 433  GLN n 
1 434  HIS n 
1 435  THR n 
1 436  GLN n 
1 437  TYR n 
1 438  PRO n 
1 439  ASP n 
1 440  ALA n 
1 441  ARG n 
1 442  LEU n 
1 443  SER n 
1 444  SER n 
1 445  PRO n 
1 446  ILE n 
1 447  VAL n 
1 448  LEU n 
1 449  ASP n 
1 450  GLN n 
1 451  CYS n 
1 452  ASP n 
1 453  LEU n 
1 454  VAL n 
1 455  THR n 
1 456  ARG n 
1 457  ALA n 
1 458  CYS n 
1 459  GLY n 
1 460  LEU n 
1 461  TYR n 
1 462  SER n 
1 463  SER n 
1 464  TYR n 
1 465  SER n 
1 466  LEU n 
1 467  ASN n 
1 468  PRO n 
1 469  GLN n 
1 470  LEU n 
1 471  ARG n 
1 472  ASN n 
1 473  CYS n 
1 474  LYS n 
1 475  LEU n 
1 476  PRO n 
1 477  LYS n 
1 478  HIS n 
1 479  ILE n 
1 480  TYR n 
1 481  ARG n 
1 482  LEU n 
1 483  LYS n 
1 484  TYR n 
1 485  ASP n 
1 486  VAL n 
1 487  THR n 
1 488  VAL n 
1 489  THR n 
1 490  LYS n 
1 491  PHE n 
1 492  LEU n 
1 493  SER n 
1 494  ASP n 
1 495  VAL n 
1 496  PRO n 
1 497  VAL n 
1 498  ALA n 
1 499  THR n 
1 500  LEU n 
1 501  PRO n 
1 502  ILE n 
1 503  ASP n 
1 504  PHE n 
1 505  ILE n 
1 506  VAL n 
1 507  PRO n 
1 508  VAL n 
1 509  LEU n 
1 510  LEU n 
1 511  LYS n 
1 512  ALA n 
1 513  LEU n 
1 514  SER n 
1 515  GLY n 
1 516  ASN n 
1 517  GLY n 
1 518  PHE n 
1 519  CYS n 
1 520  PRO n 
1 521  VAL n 
1 522  GLU n 
1 523  PRO n 
1 524  ARG n 
1 525  CYS n 
1 526  GLN n 
1 527  GLN n 
1 528  PHE n 
1 529  LEU n 
1 530  ASP n 
1 531  GLU n 
1 532  ILE n 
1 533  ILE n 
1 534  LYS n 
1 535  TYR n 
1 536  THR n 
1 537  MET n 
1 538  GLN n 
1 539  ASP n 
1 540  ALA n 
1 541  LEU n 
1 542  PHE n 
1 543  LEU n 
1 544  LYS n 
1 545  TYR n 
1 546  TYR n 
1 547  LEU n 
1 548  LYS n 
1 549  ASN n 
1 550  VAL n 
1 551  GLY n 
1 552  ALA n 
1 553  GLN n 
1 554  GLU n 
1 555  ASP n 
1 556  CYS n 
1 557  VAL n 
1 558  ASP n 
1 559  GLU n 
1 560  HIS n 
1 561  PHE n 
1 562  GLN n 
1 563  GLU n 
1 564  LYS n 
1 565  ILE n 
1 566  LEU n 
1 567  SER n 
1 568  SER n 
1 569  ILE n 
1 570  GLN n 
1 571  GLY n 
1 572  ASN n 
1 573  GLU n 
1 574  PHE n 
1 575  LEU n 
1 576  HIS n 
1 577  GLN n 
1 578  MET n 
1 579  PHE n 
1 580  PHE n 
1 581  TRP n 
1 582  TYR n 
1 583  ASP n 
1 584  LEU n 
1 585  ALA n 
1 586  ILE n 
1 587  LEU n 
1 588  THR n 
1 589  ARG n 
1 590  ARG n 
1 591  GLY n 
1 592  ARG n 
1 593  LEU n 
1 594  ASN n 
1 595  ARG n 
1 596  GLY n 
1 597  ASN n 
1 598  SER n 
1 599  ARG n 
1 600  SER n 
1 601  THR n 
1 602  TRP n 
1 603  PHE n 
1 604  VAL n 
1 605  HIS n 
1 606  ASP n 
1 607  ASP n 
1 608  LEU n 
1 609  ILE n 
1 610  ASP n 
1 611  ILE n 
1 612  LEU n 
1 613  GLY n 
1 614  TYR n 
1 615  GLY n 
1 616  ASP n 
1 617  TYR n 
1 618  VAL n 
1 619  PHE n 
1 620  TRP n 
1 621  LYS n 
1 622  ILE n 
1 623  PRO n 
1 624  ILE n 
1 625  SER n 
1 626  MET n 
1 627  LEU n 
1 628  PRO n 
1 629  LEU n 
1 630  ASN n 
1 631  THR n 
1 632  GLN n 
1 633  GLY n 
1 634  ILE n 
1 635  PRO n 
1 636  HIS n 
1 637  ALA n 
1 638  ALA n 
1 639  MET n 
1 640  ASP n 
1 641  TRP n 
1 642  TYR n 
1 643  GLN n 
1 644  ALA n 
1 645  SER n 
1 646  VAL n 
1 647  PHE n 
1 648  LYS n 
1 649  GLU n 
1 650  ALA n 
1 651  VAL n 
1 652  GLN n 
1 653  GLY n 
1 654  HIS n 
1 655  THR n 
1 656  HIS n 
1 657  ILE n 
1 658  VAL n 
1 659  SER n 
1 660  VAL n 
1 661  SER n 
1 662  THR n 
1 663  ALA n 
1 664  ASP n 
1 665  VAL n 
1 666  LEU n 
1 667  ILE n 
1 668  MET n 
1 669  CYS n 
1 670  LYS n 
1 671  ASP n 
1 672  LEU n 
1 673  ILE n 
1 674  THR n 
1 675  CYS n 
1 676  ARG n 
1 677  PHE n 
1 678  ASN n 
1 679  THR n 
1 680  THR n 
1 681  LEU n 
1 682  ILE n 
1 683  SER n 
1 684  LYS n 
1 685  ILE n 
1 686  ALA n 
1 687  GLU n 
1 688  ILE n 
1 689  GLU n 
1 690  ASP n 
1 691  PRO n 
1 692  VAL n 
1 693  CYS n 
1 694  SER n 
1 695  ASP n 
1 696  TYR n 
1 697  PRO n 
1 698  ASN n 
1 699  PHE n 
1 700  LYS n 
1 701  ILE n 
1 702  VAL n 
1 703  SER n 
1 704  MET n 
1 705  LEU n 
1 706  TYR n 
1 707  GLN n 
1 708  SER n 
1 709  GLY n 
1 710  ASP n 
1 711  TYR n 
1 712  LEU n 
1 713  LEU n 
1 714  SER n 
1 715  ILE n 
1 716  LEU n 
1 717  GLY n 
1 718  SER n 
1 719  ASP n 
1 720  GLY n 
1 721  TYR n 
1 722  LYS n 
1 723  ILE n 
1 724  ILE n 
1 725  LYS n 
1 726  PHE n 
1 727  LEU n 
1 728  GLU n 
1 729  PRO n 
1 730  LEU n 
1 731  CYS n 
1 732  LEU n 
1 733  ALA n 
1 734  LYS n 
1 735  ILE n 
1 736  GLN n 
1 737  LEU n 
1 738  CYS n 
1 739  SER n 
1 740  LYS n 
1 741  TYR n 
1 742  THR n 
1 743  GLU n 
1 744  ARG n 
1 745  LYS n 
1 746  GLY n 
1 747  ARG n 
1 748  PHE n 
1 749  LEU n 
1 750  THR n 
1 751  GLN n 
1 752  MET n 
1 753  HIS n 
1 754  LEU n 
1 755  ALA n 
1 756  VAL n 
1 757  ASN n 
1 758  HIS n 
1 759  THR n 
1 760  LEU n 
1 761  GLU n 
1 762  GLU n 
1 763  ILE n 
1 764  THR n 
1 765  GLU n 
1 766  MET n 
1 767  ARG n 
1 768  ALA n 
1 769  LEU n 
1 770  LYS n 
1 771  PRO n 
1 772  SER n 
1 773  GLN n 
1 774  ALA n 
1 775  GLN n 
1 776  LYS n 
1 777  ILE n 
1 778  ARG n 
1 779  GLU n 
1 780  PHE n 
1 781  HIS n 
1 782  ARG n 
1 783  THR n 
1 784  LEU n 
1 785  ILE n 
1 786  ARG n 
1 787  LEU n 
1 788  GLU n 
1 789  MET n 
1 790  THR n 
1 791  PRO n 
1 792  GLN n 
1 793  GLN n 
1 794  LEU n 
1 795  CYS n 
1 796  GLU n 
1 797  LEU n 
1 798  PHE n 
1 799  SER n 
1 800  ILE n 
1 801  GLN n 
1 802  LYS n 
1 803  HIS n 
1 804  TRP n 
1 805  GLY n 
1 806  HIS n 
1 807  PRO n 
1 808  VAL n 
1 809  LEU n 
1 810  HIS n 
1 811  SER n 
1 812  GLU n 
1 813  THR n 
1 814  ALA n 
1 815  ILE n 
1 816  GLN n 
1 817  LYS n 
1 818  VAL n 
1 819  LYS n 
1 820  LYS n 
1 821  HIS n 
1 822  ALA n 
1 823  THR n 
1 824  VAL n 
1 825  LEU n 
1 826  LYS n 
1 827  ALA n 
1 828  LEU n 
1 829  ARG n 
1 830  PRO n 
1 831  ILE n 
1 832  VAL n 
1 833  ILE n 
1 834  PHE n 
1 835  GLU n 
1 836  THR n 
1 837  TYR n 
1 838  CYS n 
1 839  VAL n 
1 840  PHE n 
1 841  LYS n 
1 842  TYR n 
1 843  SER n 
1 844  ILE n 
1 845  ALA n 
1 846  LYS n 
1 847  HIS n 
1 848  TYR n 
1 849  PHE n 
1 850  ASP n 
1 851  SER n 
1 852  GLN n 
1 853  GLY n 
1 854  SER n 
1 855  TRP n 
1 856  TYR n 
1 857  SER n 
1 858  VAL n 
1 859  THR n 
1 860  SER n 
1 861  ASP n 
1 862  ARG n 
1 863  ASN n 
1 864  LEU n 
1 865  THR n 
1 866  PRO n 
1 867  GLY n 
1 868  LEU n 
1 869  ASN n 
1 870  SER n 
1 871  TYR n 
1 872  ILE n 
1 873  LYS n 
1 874  ARG n 
1 875  ASN n 
1 876  GLN n 
1 877  PHE n 
1 878  PRO n 
1 879  PRO n 
1 880  LEU n 
1 881  PRO n 
1 882  MET n 
1 883  ILE n 
1 884  LYS n 
1 885  GLU n 
1 886  LEU n 
1 887  LEU n 
1 888  TRP n 
1 889  GLU n 
1 890  PHE n 
1 891  TYR n 
1 892  HIS n 
1 893  LEU n 
1 894  ASP n 
1 895  HIS n 
1 896  PRO n 
1 897  PRO n 
1 898  LEU n 
1 899  PHE n 
1 900  SER n 
1 901  THR n 
1 902  LYS n 
1 903  ILE n 
1 904  ILE n 
1 905  SER n 
1 906  ASP n 
1 907  LEU n 
1 908  SER n 
1 909  ILE n 
1 910  PHE n 
1 911  ILE n 
1 912  LYS n 
1 913  ASP n 
1 914  ARG n 
1 915  ALA n 
1 916  THR n 
1 917  ALA n 
1 918  VAL n 
1 919  GLU n 
1 920  ARG n 
1 921  THR n 
1 922  CYS n 
1 923  TRP n 
1 924  ASP n 
1 925  ALA n 
1 926  VAL n 
1 927  PHE n 
1 928  GLU n 
1 929  PRO n 
1 930  ASN n 
1 931  VAL n 
1 932  LEU n 
1 933  GLY n 
1 934  TYR n 
1 935  ASN n 
1 936  PRO n 
1 937  PRO n 
1 938  HIS n 
1 939  LYS n 
1 940  PHE n 
1 941  SER n 
1 942  THR n 
1 943  LYS n 
1 944  ARG n 
1 945  VAL n 
1 946  PRO n 
1 947  GLU n 
1 948  GLN n 
1 949  PHE n 
1 950  LEU n 
1 951  GLU n 
1 952  GLN n 
1 953  GLU n 
1 954  ASN n 
1 955  PHE n 
1 956  SER n 
1 957  ILE n 
1 958  GLU n 
1 959  ASN n 
1 960  VAL n 
1 961  LEU n 
1 962  SER n 
1 963  TYR n 
1 964  ALA n 
1 965  GLN n 
1 966  LYS n 
1 967  LEU n 
1 968  GLU n 
1 969  TYR n 
1 970  LEU n 
1 971  LEU n 
1 972  PRO n 
1 973  GLN n 
1 974  TYR n 
1 975  ARG n 
1 976  ASN n 
1 977  PHE n 
1 978  SER n 
1 979  PHE n 
1 980  SER n 
1 981  LEU n 
1 982  LYS n 
1 983  GLU n 
1 984  LYS n 
1 985  GLU n 
1 986  LEU n 
1 987  ASN n 
1 988  VAL n 
1 989  GLY n 
1 990  ARG n 
1 991  THR n 
1 992  PHE n 
1 993  GLY n 
1 994  LYS n 
1 995  LEU n 
1 996  PRO n 
1 997  TYR n 
1 998  PRO n 
1 999  THR n 
1 1000 ARG n 
1 1001 ASN n 
1 1002 VAL n 
1 1003 GLN n 
1 1004 THR n 
1 1005 LEU n 
1 1006 CYS n 
1 1007 GLU n 
1 1008 ALA n 
1 1009 LEU n 
1 1010 LEU n 
1 1011 ALA n 
1 1012 ASP n 
1 1013 GLY n 
1 1014 LEU n 
1 1015 ALA n 
1 1016 LYS n 
1 1017 ALA n 
1 1018 PHE n 
1 1019 PRO n 
1 1020 SER n 
1 1021 ASN n 
1 1022 MET n 
1 1023 MET n 
1 1024 VAL n 
1 1025 VAL n 
1 1026 THR n 
1 1027 GLU n 
1 1028 ARG n 
1 1029 GLU n 
1 1030 GLN n 
1 1031 LYS n 
1 1032 GLU n 
1 1033 SER n 
1 1034 LEU n 
1 1035 LEU n 
1 1036 HIS n 
1 1037 GLN n 
1 1038 ALA n 
1 1039 SER n 
1 1040 TRP n 
1 1041 HIS n 
1 1042 HIS n 
1 1043 THR n 
1 1044 SER n 
1 1045 ASP n 
1 1046 ASP n 
1 1047 PHE n 
1 1048 GLY n 
1 1049 GLU n 
1 1050 HIS n 
1 1051 ALA n 
1 1052 THR n 
1 1053 VAL n 
1 1054 ARG n 
1 1055 GLY n 
1 1056 SER n 
1 1057 SER n 
1 1058 PHE n 
1 1059 VAL n 
1 1060 THR n 
1 1061 ASP n 
1 1062 LEU n 
1 1063 GLU n 
1 1064 LYS n 
1 1065 TYR n 
1 1066 ASN n 
1 1067 LEU n 
1 1068 ALA n 
1 1069 PHE n 
1 1070 ARG n 
1 1071 TYR n 
1 1072 GLU n 
1 1073 PHE n 
1 1074 THR n 
1 1075 ALA n 
1 1076 PRO n 
1 1077 PHE n 
1 1078 ILE n 
1 1079 GLU n 
1 1080 TYR n 
1 1081 CYS n 
1 1082 ASN n 
1 1083 ARG n 
1 1084 CYS n 
1 1085 TYR n 
1 1086 GLY n 
1 1087 VAL n 
1 1088 LYS n 
1 1089 ASN n 
1 1090 VAL n 
1 1091 PHE n 
1 1092 ASN n 
1 1093 TRP n 
1 1094 MET n 
1 1095 HIS n 
1 1096 TYR n 
1 1097 THR n 
1 1098 ILE n 
1 1099 PRO n 
1 1100 GLN n 
1 1101 CYS n 
1 1102 TYR n 
1 1103 MET n 
1 1104 HIS n 
1 1105 VAL n 
1 1106 SER n 
1 1107 ASP n 
1 1108 TYR n 
1 1109 TYR n 
1 1110 ASN n 
1 1111 PRO n 
1 1112 PRO n 
1 1113 HIS n 
1 1114 ASN n 
1 1115 LEU n 
1 1116 THR n 
1 1117 LEU n 
1 1118 GLU n 
1 1119 ASN n 
1 1120 ARG n 
1 1121 ASP n 
1 1122 ASN n 
1 1123 PRO n 
1 1124 PRO n 
1 1125 GLU n 
1 1126 GLY n 
1 1127 PRO n 
1 1128 SER n 
1 1129 SER n 
1 1130 TYR n 
1 1131 ARG n 
1 1132 GLY n 
1 1133 HIS n 
1 1134 MET n 
1 1135 GLY n 
1 1136 GLY n 
1 1137 ILE n 
1 1138 GLU n 
1 1139 GLY n 
1 1140 LEU n 
1 1141 GLN n 
1 1142 GLN n 
1 1143 LYS n 
1 1144 LEU n 
1 1145 TRP n 
1 1146 THR n 
1 1147 SER n 
1 1148 ILE n 
1 1149 SER n 
1 1150 CYS n 
1 1151 ALA n 
1 1152 GLN n 
1 1153 ILE n 
1 1154 SER n 
1 1155 LEU n 
1 1156 VAL n 
1 1157 GLU n 
1 1158 ILE n 
1 1159 LYS n 
1 1160 THR n 
1 1161 GLY n 
1 1162 PHE n 
1 1163 LYS n 
1 1164 LEU n 
1 1165 ARG n 
1 1166 SER n 
1 1167 ALA n 
1 1168 VAL n 
1 1169 MET n 
1 1170 GLY n 
1 1171 ASP n 
1 1172 ASN n 
1 1173 GLN n 
1 1174 CYS n 
1 1175 ILE n 
1 1176 THR n 
1 1177 VAL n 
1 1178 LEU n 
1 1179 SER n 
1 1180 VAL n 
1 1181 PHE n 
1 1182 PRO n 
1 1183 LEU n 
1 1184 GLU n 
1 1185 THR n 
1 1186 ASP n 
1 1187 ALA n 
1 1188 ASP n 
1 1189 GLU n 
1 1190 GLN n 
1 1191 GLU n 
1 1192 GLN n 
1 1193 SER n 
1 1194 ALA n 
1 1195 GLU n 
1 1196 ASP n 
1 1197 ASN n 
1 1198 ALA n 
1 1199 ALA n 
1 1200 ARG n 
1 1201 VAL n 
1 1202 ALA n 
1 1203 ALA n 
1 1204 SER n 
1 1205 LEU n 
1 1206 ALA n 
1 1207 LYS n 
1 1208 VAL n 
1 1209 THR n 
1 1210 SER n 
1 1211 ALA n 
1 1212 CYS n 
1 1213 GLY n 
1 1214 ILE n 
1 1215 PHE n 
1 1216 LEU n 
1 1217 LYS n 
1 1218 PRO n 
1 1219 ASP n 
1 1220 GLU n 
1 1221 THR n 
1 1222 PHE n 
1 1223 VAL n 
1 1224 HIS n 
1 1225 SER n 
1 1226 GLY n 
1 1227 PHE n 
1 1228 ILE n 
1 1229 TYR n 
1 1230 PHE n 
1 1231 GLY n 
1 1232 LYS n 
1 1233 LYS n 
1 1234 GLN n 
1 1235 TYR n 
1 1236 LEU n 
1 1237 ASN n 
1 1238 GLY n 
1 1239 VAL n 
1 1240 GLN n 
1 1241 LEU n 
1 1242 PRO n 
1 1243 GLN n 
1 1244 SER n 
1 1245 LEU n 
1 1246 LYS n 
1 1247 THR n 
1 1248 ALA n 
1 1249 THR n 
1 1250 ARG n 
1 1251 MET n 
1 1252 ALA n 
1 1253 PRO n 
1 1254 LEU n 
1 1255 SER n 
1 1256 ASP n 
1 1257 ALA n 
1 1258 ILE n 
1 1259 PHE n 
1 1260 ASP n 
1 1261 ASP n 
1 1262 LEU n 
1 1263 GLN n 
1 1264 GLY n 
1 1265 THR n 
1 1266 LEU n 
1 1267 ALA n 
1 1268 SER n 
1 1269 ILE n 
1 1270 GLY n 
1 1271 THR n 
1 1272 ALA n 
1 1273 PHE n 
1 1274 GLU n 
1 1275 ARG n 
1 1276 SER n 
1 1277 ILE n 
1 1278 SER n 
1 1279 GLU n 
1 1280 THR n 
1 1281 ARG n 
1 1282 HIS n 
1 1283 ILE n 
1 1284 PHE n 
1 1285 PRO n 
1 1286 CYS n 
1 1287 ARG n 
1 1288 ILE n 
1 1289 THR n 
1 1290 ALA n 
1 1291 ALA n 
1 1292 PHE n 
1 1293 HIS n 
1 1294 THR n 
1 1295 PHE n 
1 1296 PHE n 
1 1297 SER n 
1 1298 VAL n 
1 1299 ARG n 
1 1300 ILE n 
1 1301 LEU n 
1 1302 GLN n 
1 1303 TYR n 
1 1304 HIS n 
1 1305 HIS n 
1 1306 LEU n 
1 1307 GLY n 
1 1308 PHE n 
1 1309 ASN n 
1 1310 LYS n 
1 1311 GLY n 
1 1312 PHE n 
1 1313 ASP n 
1 1314 LEU n 
1 1315 GLY n 
1 1316 GLN n 
1 1317 LEU n 
1 1318 THR n 
1 1319 LEU n 
1 1320 GLY n 
1 1321 LYS n 
1 1322 PRO n 
1 1323 LEU n 
1 1324 ASP n 
1 1325 PHE n 
1 1326 GLY n 
1 1327 THR n 
1 1328 ILE n 
1 1329 SER n 
1 1330 LEU n 
1 1331 ALA n 
1 1332 LEU n 
1 1333 ALA n 
1 1334 VAL n 
1 1335 PRO n 
1 1336 GLN n 
1 1337 VAL n 
1 1338 LEU n 
1 1339 GLY n 
1 1340 GLY n 
1 1341 LEU n 
1 1342 SER n 
1 1343 PHE n 
1 1344 LEU n 
1 1345 ASN n 
1 1346 PRO n 
1 1347 GLU n 
1 1348 LYS n 
1 1349 CYS n 
1 1350 PHE n 
1 1351 TYR n 
1 1352 ARG n 
1 1353 ASN n 
1 1354 LEU n 
1 1355 GLY n 
1 1356 ASP n 
1 1357 PRO n 
1 1358 VAL n 
1 1359 THR n 
1 1360 SER n 
1 1361 GLY n 
1 1362 LEU n 
1 1363 PHE n 
1 1364 GLN n 
1 1365 LEU n 
1 1366 LYS n 
1 1367 THR n 
1 1368 TYR n 
1 1369 LEU n 
1 1370 ARG n 
1 1371 MET n 
1 1372 ILE n 
1 1373 GLU n 
1 1374 MET n 
1 1375 ASP n 
1 1376 ASP n 
1 1377 LEU n 
1 1378 PHE n 
1 1379 LEU n 
1 1380 PRO n 
1 1381 LEU n 
1 1382 ILE n 
1 1383 ALA n 
1 1384 LYS n 
1 1385 ASN n 
1 1386 PRO n 
1 1387 GLY n 
1 1388 ASN n 
1 1389 CYS n 
1 1390 THR n 
1 1391 ALA n 
1 1392 ILE n 
1 1393 ASP n 
1 1394 PHE n 
1 1395 VAL n 
1 1396 LEU n 
1 1397 ASN n 
1 1398 PRO n 
1 1399 SER n 
1 1400 GLY n 
1 1401 LEU n 
1 1402 ASN n 
1 1403 VAL n 
1 1404 PRO n 
1 1405 GLY n 
1 1406 SER n 
1 1407 GLN n 
1 1408 ASP n 
1 1409 LEU n 
1 1410 THR n 
1 1411 SER n 
1 1412 PHE n 
1 1413 LEU n 
1 1414 ARG n 
1 1415 GLN n 
1 1416 ILE n 
1 1417 VAL n 
1 1418 ARG n 
1 1419 ARG n 
1 1420 THR n 
1 1421 ILE n 
1 1422 THR n 
1 1423 LEU n 
1 1424 SER n 
1 1425 ALA n 
1 1426 LYS n 
1 1427 ASN n 
1 1428 LYS n 
1 1429 LEU n 
1 1430 ILE n 
1 1431 ASN n 
1 1432 THR n 
1 1433 LEU n 
1 1434 PHE n 
1 1435 HIS n 
1 1436 ALA n 
1 1437 SER n 
1 1438 ALA n 
1 1439 ASP n 
1 1440 PHE n 
1 1441 GLU n 
1 1442 ASP n 
1 1443 GLU n 
1 1444 MET n 
1 1445 VAL n 
1 1446 CYS n 
1 1447 LYS n 
1 1448 TRP n 
1 1449 LEU n 
1 1450 LEU n 
1 1451 SER n 
1 1452 SER n 
1 1453 THR n 
1 1454 PRO n 
1 1455 VAL n 
1 1456 MET n 
1 1457 SER n 
1 1458 ARG n 
1 1459 PHE n 
1 1460 ALA n 
1 1461 ALA n 
1 1462 ASP n 
1 1463 ILE n 
1 1464 PHE n 
1 1465 SER n 
1 1466 ARG n 
1 1467 THR n 
1 1468 PRO n 
1 1469 SER n 
1 1470 GLY n 
1 1471 LYS n 
1 1472 ARG n 
1 1473 LEU n 
1 1474 GLN n 
1 1475 ILE n 
1 1476 LEU n 
1 1477 GLY n 
1 1478 TYR n 
1 1479 LEU n 
1 1480 GLU n 
1 1481 GLY n 
1 1482 THR n 
1 1483 ARG n 
1 1484 THR n 
1 1485 LEU n 
1 1486 LEU n 
1 1487 ALA n 
1 1488 SER n 
1 1489 LYS n 
1 1490 ILE n 
1 1491 ILE n 
1 1492 ASN n 
1 1493 ASN n 
1 1494 ASN n 
1 1495 THR n 
1 1496 GLU n 
1 1497 THR n 
1 1498 PRO n 
1 1499 VAL n 
1 1500 LEU n 
1 1501 ASP n 
1 1502 ARG n 
1 1503 LEU n 
1 1504 ARG n 
1 1505 LYS n 
1 1506 ILE n 
1 1507 THR n 
1 1508 LEU n 
1 1509 GLN n 
1 1510 ARG n 
1 1511 TRP n 
1 1512 SER n 
1 1513 LEU n 
1 1514 TRP n 
1 1515 PHE n 
1 1516 SER n 
1 1517 TYR n 
1 1518 LEU n 
1 1519 ASP n 
1 1520 HIS n 
1 1521 CYS n 
1 1522 ASP n 
1 1523 ASN n 
1 1524 ILE n 
1 1525 LEU n 
1 1526 ALA n 
1 1527 GLU n 
1 1528 ALA n 
1 1529 LEU n 
1 1530 THR n 
1 1531 GLN n 
1 1532 ILE n 
1 1533 THR n 
1 1534 CYS n 
1 1535 THR n 
1 1536 VAL n 
1 1537 ASP n 
1 1538 LEU n 
1 1539 ALA n 
1 1540 GLN n 
1 1541 ILE n 
1 1542 LEU n 
1 1543 ARG n 
1 1544 GLU n 
1 1545 TYR n 
1 1546 SER n 
1 1547 TRP n 
1 1548 ALA n 
1 1549 HIS n 
1 1550 ILE n 
1 1551 LEU n 
1 1552 GLU n 
1 1553 GLY n 
1 1554 ARG n 
1 1555 PRO n 
1 1556 LEU n 
1 1557 ILE n 
1 1558 GLY n 
1 1559 ALA n 
1 1560 THR n 
1 1561 LEU n 
1 1562 PRO n 
1 1563 CYS n 
1 1564 MET n 
1 1565 ILE n 
1 1566 GLU n 
1 1567 GLN n 
1 1568 PHE n 
1 1569 LYS n 
1 1570 VAL n 
1 1571 PHE n 
1 1572 TRP n 
1 1573 LEU n 
1 1574 LYS n 
1 1575 PRO n 
1 1576 TYR n 
1 1577 GLU n 
1 1578 GLN n 
1 1579 CYS n 
1 1580 PRO n 
1 1581 GLN n 
1 1582 CYS n 
1 1583 SER n 
1 1584 ASN n 
1 1585 ALA n 
1 1586 LYS n 
1 1587 GLN n 
1 1588 PRO n 
1 1589 GLY n 
1 1590 GLY n 
1 1591 LYS n 
1 1592 PRO n 
1 1593 PHE n 
1 1594 VAL n 
1 1595 SER n 
1 1596 VAL n 
1 1597 ALA n 
1 1598 VAL n 
1 1599 LYS n 
1 1600 LYS n 
1 1601 HIS n 
1 1602 ILE n 
1 1603 VAL n 
1 1604 SER n 
1 1605 ALA n 
1 1606 TRP n 
1 1607 PRO n 
1 1608 ASN n 
1 1609 ALA n 
1 1610 SER n 
1 1611 ARG n 
1 1612 ILE n 
1 1613 SER n 
1 1614 TRP n 
1 1615 THR n 
1 1616 ILE n 
1 1617 GLY n 
1 1618 ASP n 
1 1619 GLY n 
1 1620 ILE n 
1 1621 PRO n 
1 1622 TYR n 
1 1623 ILE n 
1 1624 GLY n 
1 1625 SER n 
1 1626 ARG n 
1 1627 THR n 
1 1628 GLU n 
1 1629 ASP n 
1 1630 LYS n 
1 1631 ILE n 
1 1632 GLY n 
1 1633 GLN n 
1 1634 PRO n 
1 1635 ALA n 
1 1636 ILE n 
1 1637 LYS n 
1 1638 PRO n 
1 1639 LYS n 
1 1640 CYS n 
1 1641 PRO n 
1 1642 SER n 
1 1643 ALA n 
1 1644 ALA n 
1 1645 LEU n 
1 1646 ARG n 
1 1647 GLU n 
1 1648 ALA n 
1 1649 ILE n 
1 1650 GLU n 
1 1651 LEU n 
1 1652 ALA n 
1 1653 SER n 
1 1654 ARG n 
1 1655 LEU n 
1 1656 THR n 
1 1657 TRP n 
1 1658 VAL n 
1 1659 THR n 
1 1660 GLN n 
1 1661 GLY n 
1 1662 SER n 
1 1663 SER n 
1 1664 ASN n 
1 1665 SER n 
1 1666 ASP n 
1 1667 LEU n 
1 1668 LEU n 
1 1669 ILE n 
1 1670 LYS n 
1 1671 PRO n 
1 1672 PHE n 
1 1673 LEU n 
1 1674 GLU n 
1 1675 ALA n 
1 1676 ARG n 
1 1677 VAL n 
1 1678 ASN n 
1 1679 LEU n 
1 1680 SER n 
1 1681 VAL n 
1 1682 GLN n 
1 1683 GLU n 
1 1684 ILE n 
1 1685 LEU n 
1 1686 GLN n 
1 1687 MET n 
1 1688 THR n 
1 1689 PRO n 
1 1690 SER n 
1 1691 HIS n 
1 1692 TYR n 
1 1693 SER n 
1 1694 GLY n 
1 1695 ASN n 
1 1696 ILE n 
1 1697 VAL n 
1 1698 HIS n 
1 1699 ARG n 
1 1700 TYR n 
1 1701 ASN n 
1 1702 ASP n 
1 1703 GLN n 
1 1704 TYR n 
1 1705 SER n 
1 1706 PRO n 
1 1707 HIS n 
1 1708 SER n 
1 1709 PHE n 
1 1710 MET n 
1 1711 ALA n 
1 1712 ASN n 
1 1713 ARG n 
1 1714 MET n 
1 1715 SER n 
1 1716 ASN n 
1 1717 SER n 
1 1718 ALA n 
1 1719 THR n 
1 1720 ARG n 
1 1721 LEU n 
1 1722 ILE n 
1 1723 VAL n 
1 1724 SER n 
1 1725 THR n 
1 1726 ASN n 
1 1727 THR n 
1 1728 LEU n 
1 1729 GLY n 
1 1730 GLU n 
1 1731 PHE n 
1 1732 SER n 
1 1733 GLY n 
1 1734 GLY n 
1 1735 GLY n 
1 1736 GLN n 
1 1737 SER n 
1 1738 ALA n 
1 1739 ARG n 
1 1740 ASP n 
1 1741 SER n 
1 1742 ASN n 
1 1743 ILE n 
1 1744 ILE n 
1 1745 PHE n 
1 1746 GLN n 
1 1747 ASN n 
1 1748 VAL n 
1 1749 ILE n 
1 1750 ASN n 
1 1751 TYR n 
1 1752 ALA n 
1 1753 VAL n 
1 1754 ALA n 
1 1755 LEU n 
1 1756 PHE n 
1 1757 ASP n 
1 1758 ILE n 
1 1759 LYS n 
1 1760 PHE n 
1 1761 ARG n 
1 1762 ASN n 
1 1763 THR n 
1 1764 GLU n 
1 1765 ALA n 
1 1766 THR n 
1 1767 ASP n 
1 1768 ILE n 
1 1769 GLN n 
1 1770 TYR n 
1 1771 ASN n 
1 1772 ARG n 
1 1773 ALA n 
1 1774 HIS n 
1 1775 LEU n 
1 1776 HIS n 
1 1777 LEU n 
1 1778 THR n 
1 1779 LYS n 
1 1780 CYS n 
1 1781 CYS n 
1 1782 THR n 
1 1783 ARG n 
1 1784 GLU n 
1 1785 VAL n 
1 1786 PRO n 
1 1787 ALA n 
1 1788 GLN n 
1 1789 TYR n 
1 1790 LEU n 
1 1791 THR n 
1 1792 TYR n 
1 1793 THR n 
1 1794 SER n 
1 1795 THR n 
1 1796 LEU n 
1 1797 ASP n 
1 1798 LEU n 
1 1799 ASP n 
1 1800 LEU n 
1 1801 THR n 
1 1802 ARG n 
1 1803 TYR n 
1 1804 ARG n 
1 1805 GLU n 
1 1806 ASN n 
1 1807 GLU n 
1 1808 LEU n 
1 1809 ILE n 
1 1810 TYR n 
1 1811 ASP n 
1 1812 SER n 
1 1813 ASN n 
1 1814 PRO n 
1 1815 LEU n 
1 1816 LYS n 
1 1817 GLY n 
1 1818 GLY n 
1 1819 LEU n 
1 1820 ASN n 
1 1821 CYS n 
1 1822 ASN n 
1 1823 ILE n 
1 1824 SER n 
1 1825 PHE n 
1 1826 ASP n 
1 1827 ASN n 
1 1828 PRO n 
1 1829 PHE n 
1 1830 SER n 
1 1831 ARG n 
1 1832 ASP n 
1 1833 TYR n 
1 1834 LYS n 
1 1835 ASP n 
1 1836 ASP n 
1 1837 ASP n 
1 1838 ASP n 
1 1839 LYS n 
2 1    MET n 
2 2    GLY n 
2 3    SER n 
2 4    SER n 
2 5    HIS n 
2 6    HIS n 
2 7    HIS n 
2 8    HIS n 
2 9    HIS n 
2 10   HIS n 
2 11   GLY n 
2 12   THR n 
2 13   LYS n 
2 14   THR n 
2 15   GLU n 
2 16   GLU n 
2 17   GLY n 
2 18   LYS n 
2 19   LEU n 
2 20   VAL n 
2 21   ILE n 
2 22   TRP n 
2 23   ILE n 
2 24   ASN n 
2 25   GLY n 
2 26   ASP n 
2 27   LYS n 
2 28   GLY n 
2 29   TYR n 
2 30   ASN n 
2 31   GLY n 
2 32   LEU n 
2 33   ALA n 
2 34   GLU n 
2 35   VAL n 
2 36   GLY n 
2 37   LYS n 
2 38   LYS n 
2 39   PHE n 
2 40   GLU n 
2 41   LYS n 
2 42   ASP n 
2 43   THR n 
2 44   GLY n 
2 45   ILE n 
2 46   LYS n 
2 47   VAL n 
2 48   THR n 
2 49   VAL n 
2 50   GLU n 
2 51   HIS n 
2 52   PRO n 
2 53   ASP n 
2 54   LYS n 
2 55   LEU n 
2 56   GLU n 
2 57   GLU n 
2 58   LYS n 
2 59   PHE n 
2 60   PRO n 
2 61   GLN n 
2 62   VAL n 
2 63   ALA n 
2 64   ALA n 
2 65   THR n 
2 66   GLY n 
2 67   ASP n 
2 68   GLY n 
2 69   PRO n 
2 70   ASP n 
2 71   ILE n 
2 72   ILE n 
2 73   PHE n 
2 74   TRP n 
2 75   ALA n 
2 76   HIS n 
2 77   ASP n 
2 78   ARG n 
2 79   PHE n 
2 80   GLY n 
2 81   GLY n 
2 82   TYR n 
2 83   ALA n 
2 84   GLN n 
2 85   SER n 
2 86   GLY n 
2 87   LEU n 
2 88   LEU n 
2 89   ALA n 
2 90   GLU n 
2 91   ILE n 
2 92   THR n 
2 93   PRO n 
2 94   ASP n 
2 95   LYS n 
2 96   ALA n 
2 97   PHE n 
2 98   GLN n 
2 99   ASP n 
2 100  LYS n 
2 101  LEU n 
2 102  TYR n 
2 103  PRO n 
2 104  PHE n 
2 105  THR n 
2 106  TRP n 
2 107  ASP n 
2 108  ALA n 
2 109  VAL n 
2 110  ARG n 
2 111  TYR n 
2 112  ASN n 
2 113  GLY n 
2 114  LYS n 
2 115  LEU n 
2 116  ILE n 
2 117  ALA n 
2 118  TYR n 
2 119  PRO n 
2 120  ILE n 
2 121  ALA n 
2 122  VAL n 
2 123  GLU n 
2 124  ALA n 
2 125  LEU n 
2 126  SER n 
2 127  LEU n 
2 128  ILE n 
2 129  TYR n 
2 130  ASN n 
2 131  LYS n 
2 132  ASP n 
2 133  LEU n 
2 134  LEU n 
2 135  PRO n 
2 136  ASN n 
2 137  PRO n 
2 138  PRO n 
2 139  LYS n 
2 140  THR n 
2 141  TRP n 
2 142  GLU n 
2 143  GLU n 
2 144  ILE n 
2 145  PRO n 
2 146  ALA n 
2 147  LEU n 
2 148  ASP n 
2 149  LYS n 
2 150  GLU n 
2 151  LEU n 
2 152  LYS n 
2 153  ALA n 
2 154  LYS n 
2 155  GLY n 
2 156  LYS n 
2 157  SER n 
2 158  ALA n 
2 159  LEU n 
2 160  MET n 
2 161  PHE n 
2 162  ASN n 
2 163  LEU n 
2 164  GLN n 
2 165  GLU n 
2 166  PRO n 
2 167  TYR n 
2 168  PHE n 
2 169  THR n 
2 170  TRP n 
2 171  PRO n 
2 172  LEU n 
2 173  ILE n 
2 174  ALA n 
2 175  ALA n 
2 176  ASP n 
2 177  GLY n 
2 178  GLY n 
2 179  TYR n 
2 180  ALA n 
2 181  PHE n 
2 182  LYS n 
2 183  TYR n 
2 184  GLU n 
2 185  ASN n 
2 186  GLY n 
2 187  LYS n 
2 188  TYR n 
2 189  ASP n 
2 190  ILE n 
2 191  LYS n 
2 192  ASP n 
2 193  VAL n 
2 194  GLY n 
2 195  VAL n 
2 196  ASP n 
2 197  ASN n 
2 198  ALA n 
2 199  GLY n 
2 200  ALA n 
2 201  LYS n 
2 202  ALA n 
2 203  GLY n 
2 204  LEU n 
2 205  THR n 
2 206  PHE n 
2 207  LEU n 
2 208  VAL n 
2 209  ASP n 
2 210  LEU n 
2 211  ILE n 
2 212  LYS n 
2 213  ASN n 
2 214  LYS n 
2 215  HIS n 
2 216  MET n 
2 217  ASN n 
2 218  ALA n 
2 219  ASP n 
2 220  THR n 
2 221  ASP n 
2 222  TYR n 
2 223  SER n 
2 224  ILE n 
2 225  ALA n 
2 226  GLU n 
2 227  ALA n 
2 228  ALA n 
2 229  PHE n 
2 230  ASN n 
2 231  LYS n 
2 232  GLY n 
2 233  GLU n 
2 234  THR n 
2 235  ALA n 
2 236  MET n 
2 237  THR n 
2 238  ILE n 
2 239  ASN n 
2 240  GLY n 
2 241  PRO n 
2 242  TRP n 
2 243  ALA n 
2 244  TRP n 
2 245  SER n 
2 246  ASN n 
2 247  ILE n 
2 248  ASP n 
2 249  THR n 
2 250  SER n 
2 251  LYS n 
2 252  VAL n 
2 253  ASN n 
2 254  TYR n 
2 255  GLY n 
2 256  VAL n 
2 257  THR n 
2 258  VAL n 
2 259  LEU n 
2 260  PRO n 
2 261  THR n 
2 262  PHE n 
2 263  LYS n 
2 264  GLY n 
2 265  GLN n 
2 266  PRO n 
2 267  SER n 
2 268  LYS n 
2 269  PRO n 
2 270  PHE n 
2 271  VAL n 
2 272  GLY n 
2 273  VAL n 
2 274  LEU n 
2 275  SER n 
2 276  ALA n 
2 277  GLY n 
2 278  ILE n 
2 279  ASN n 
2 280  ALA n 
2 281  ALA n 
2 282  SER n 
2 283  PRO n 
2 284  ASN n 
2 285  LYS n 
2 286  GLU n 
2 287  LEU n 
2 288  ALA n 
2 289  LYS n 
2 290  GLU n 
2 291  PHE n 
2 292  LEU n 
2 293  GLU n 
2 294  ASN n 
2 295  TYR n 
2 296  LEU n 
2 297  LEU n 
2 298  THR n 
2 299  ASP n 
2 300  GLU n 
2 301  GLY n 
2 302  LEU n 
2 303  GLU n 
2 304  ALA n 
2 305  VAL n 
2 306  ASN n 
2 307  LYS n 
2 308  ASP n 
2 309  LYS n 
2 310  PRO n 
2 311  LEU n 
2 312  GLY n 
2 313  ALA n 
2 314  VAL n 
2 315  ALA n 
2 316  LEU n 
2 317  LYS n 
2 318  SER n 
2 319  TYR n 
2 320  GLU n 
2 321  GLU n 
2 322  GLU n 
2 323  LEU n 
2 324  ALA n 
2 325  LYS n 
2 326  ASP n 
2 327  PRO n 
2 328  ARG n 
2 329  ILE n 
2 330  ALA n 
2 331  ALA n 
2 332  THR n 
2 333  MET n 
2 334  GLU n 
2 335  ASN n 
2 336  ALA n 
2 337  GLN n 
2 338  LYS n 
2 339  GLY n 
2 340  GLU n 
2 341  ILE n 
2 342  MET n 
2 343  PRO n 
2 344  ASN n 
2 345  ILE n 
2 346  PRO n 
2 347  GLN n 
2 348  MET n 
2 349  SER n 
2 350  ALA n 
2 351  PHE n 
2 352  TRP n 
2 353  TYR n 
2 354  ALA n 
2 355  VAL n 
2 356  ARG n 
2 357  THR n 
2 358  ALA n 
2 359  VAL n 
2 360  ILE n 
2 361  ASN n 
2 362  ALA n 
2 363  ALA n 
2 364  SER n 
2 365  GLY n 
2 366  ARG n 
2 367  GLN n 
2 368  THR n 
2 369  VAL n 
2 370  ASP n 
2 371  GLU n 
2 372  ALA n 
2 373  LEU n 
2 374  LYS n 
2 375  ASP n 
2 376  ALA n 
2 377  GLN n 
2 378  THR n 
2 379  GLY n 
2 380  THR n 
2 381  ASP n 
2 382  TYR n 
2 383  ASP n 
2 384  ILE n 
2 385  PRO n 
2 386  THR n 
2 387  THR n 
2 388  GLU n 
2 389  ASN n 
2 390  LEU n 
2 391  TYR n 
2 392  PHE n 
2 393  GLN n 
2 394  GLY n 
2 395  GLY n 
2 396  SER n 
2 397  ASN n 
2 398  HIS n 
2 399  SER n 
2 400  PHE n 
2 401  GLU n 
2 402  GLU n 
2 403  VAL n 
2 404  VAL n 
2 405  GLN n 
2 406  THR n 
2 407  LEU n 
2 408  ALA n 
2 409  SER n 
2 410  LEU n 
2 411  ALA n 
2 412  THR n 
2 413  VAL n 
2 414  VAL n 
2 415  GLN n 
2 416  GLN n 
2 417  GLN n 
2 418  THR n 
2 419  ILE n 
2 420  ALA n 
2 421  SER n 
2 422  GLU n 
2 423  SER n 
2 424  LEU n 
2 425  GLU n 
2 426  GLN n 
2 427  ARG n 
2 428  ILE n 
2 429  THR n 
2 430  SER n 
2 431  LEU n 
2 432  GLU n 
2 433  ASN n 
2 434  GLY n 
2 435  LEU n 
2 436  LYS n 
2 437  PRO n 
2 438  VAL n 
2 439  TYR n 
2 440  ASP n 
2 441  MET n 
2 442  ALA n 
2 443  LYS n 
2 444  THR n 
2 445  ILE n 
2 446  SER n 
2 447  SER n 
2 448  LEU n 
2 449  ASN n 
2 450  ARG n 
2 451  VAL n 
2 452  CYS n 
2 453  ALA n 
2 454  GLU n 
2 455  MET n 
2 456  VAL n 
2 457  ALA n 
2 458  LYS n 
2 459  TYR n 
2 460  ASP n 
2 461  LEU n 
2 462  LEU n 
2 463  VAL n 
2 464  MET n 
2 465  THR n 
2 466  THR n 
2 467  GLY n 
2 468  ARG n 
2 469  ALA n 
2 470  THR n 
2 471  ALA n 
2 472  THR n 
2 473  ALA n 
2 474  ALA n 
2 475  ALA n 
2 476  THR n 
2 477  GLU n 
2 478  ALA n 
2 479  TYR n 
2 480  TRP n 
2 481  ALA n 
2 482  GLU n 
2 483  HIS n 
2 484  GLY n 
2 485  GLN n 
2 486  PRO n 
2 487  PRO n 
2 488  PRO n 
2 489  GLY n 
2 490  PRO n 
2 491  SER n 
2 492  LEU n 
2 493  TYR n 
2 494  GLU n 
2 495  GLU n 
2 496  SER n 
2 497  ALA n 
2 498  ILE n 
2 499  ARG n 
2 500  GLY n 
2 501  LYS n 
2 502  ILE n 
2 503  GLU n 
2 504  SER n 
2 505  ARG n 
2 506  ASP n 
2 507  GLU n 
2 508  THR n 
2 509  VAL n 
2 510  PRO n 
2 511  GLN n 
2 512  SER n 
2 513  VAL n 
2 514  ARG n 
2 515  GLU n 
2 516  ALA n 
2 517  PHE n 
2 518  ASN n 
2 519  ASN n 
2 520  LEU n 
2 521  ASN n 
2 522  SER n 
2 523  THR n 
2 524  THR n 
2 525  SER n 
2 526  LEU n 
2 527  THR n 
2 528  GLU n 
2 529  GLU n 
2 530  ASN n 
2 531  PHE n 
2 532  GLY n 
2 533  LYS n 
2 534  PRO n 
2 535  ASP n 
2 536  ILE n 
2 537  SER n 
2 538  ALA n 
2 539  LYS n 
2 540  ASP n 
2 541  LEU n 
2 542  ARG n 
2 543  ASN n 
2 544  ILE n 
2 545  MET n 
2 546  TYR n 
2 547  ASP n 
2 548  HIS n 
2 549  LEU n 
2 550  PRO n 
2 551  GLY n 
2 552  PHE n 
2 553  GLY n 
2 554  THR n 
2 555  ALA n 
2 556  PHE n 
2 557  HIS n 
2 558  GLN n 
2 559  LEU n 
2 560  VAL n 
2 561  GLN n 
2 562  VAL n 
2 563  ILE n 
2 564  CYS n 
2 565  LYS n 
2 566  LEU n 
2 567  GLY n 
2 568  LYS n 
2 569  ASP n 
2 570  SER n 
2 571  ASN n 
2 572  SER n 
2 573  LEU n 
2 574  ASP n 
2 575  ILE n 
2 576  ILE n 
2 577  HIS n 
2 578  ALA n 
2 579  GLU n 
2 580  PHE n 
2 581  GLN n 
2 582  ALA n 
2 583  SER n 
2 584  LEU n 
2 585  ALA n 
2 586  GLU n 
2 587  GLY n 
2 588  ASP n 
2 589  SER n 
2 590  PRO n 
2 591  GLN n 
2 592  CYS n 
2 593  ALA n 
2 594  LEU n 
2 595  ILE n 
2 596  GLN n 
2 597  ILE n 
2 598  THR n 
2 599  LYS n 
2 600  ARG n 
2 601  VAL n 
2 602  PRO n 
2 603  ILE n 
2 604  PHE n 
2 605  GLN n 
2 606  ASP n 
2 607  ALA n 
2 608  ALA n 
2 609  PRO n 
2 610  PRO n 
2 611  VAL n 
2 612  ILE n 
2 613  HIS n 
2 614  ILE n 
2 615  ARG n 
2 616  SER n 
2 617  ARG n 
2 618  GLY n 
2 619  ASP n 
2 620  ILE n 
2 621  PRO n 
2 622  ARG n 
2 623  ALA n 
2 624  CYS n 
2 625  GLN n 
2 626  LYS n 
2 627  SER n 
2 628  LEU n 
2 629  ARG n 
2 630  PRO n 
2 631  VAL n 
2 632  PRO n 
2 633  PRO n 
2 634  SER n 
2 635  PRO n 
2 636  LYS n 
2 637  ILE n 
2 638  ASP n 
2 639  ARG n 
2 640  GLY n 
2 641  TRP n 
2 642  VAL n 
2 643  CYS n 
2 644  VAL n 
2 645  PHE n 
2 646  GLN n 
2 647  LEU n 
2 648  GLN n 
2 649  ASP n 
2 650  GLY n 
2 651  LYS n 
2 652  THR n 
2 653  LEU n 
2 654  GLY n 
2 655  LEU n 
2 656  LYS n 
2 657  ILE 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   429  ? ? 'malE, b4034, JW3994' ? ? ? ? ? ? 'Escherichia coli (strain K12)'      83333  ? ? ? 
? ? ? ? ? 'Spodoptera frugiperda' 7108 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
1 2 sample 'Biological sequence' 430 1839 ? ? ?                     ? ? ? ? ? ? 'Ebola virus - Eckron (Zaire, 1976)' 129000 ? ? ? 
? ? ? ? ? 'Spodoptera frugiperda' 7108 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1   396  ? ? 'malE, b4034, JW3994' ? ? ? ? ? ? 'Escherichia coli (strain K12)'      83333  ? ? ? 
? ? ? ? ? 'Spodoptera frugiperda' 7108 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 2 sample 'Biological sequence' 397 657  ? ? VP35                  ? ? ? ? ? ? 'Ebola virus - Eckron (Zaire, 1976)' 129000 ? ? ? 
? ? ? ? ? 'Spodoptera frugiperda' 7108 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
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 
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
ZN  non-polymer         . 'ZINC ION'      ? 'Zn 2'           65.409  
# 
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    -428 ?    ?   ?   A . n 
A 1 2    GLY 2    -427 ?    ?   ?   A . n 
A 1 3    SER 3    -426 ?    ?   ?   A . n 
A 1 4    GLY 4    -425 ?    ?   ?   A . n 
A 1 5    TRP 5    -424 ?    ?   ?   A . n 
A 1 6    SER 6    -423 ?    ?   ?   A . n 
A 1 7    HIS 7    -422 ?    ?   ?   A . n 
A 1 8    PRO 8    -421 ?    ?   ?   A . n 
A 1 9    GLN 9    -420 ?    ?   ?   A . n 
A 1 10   PHE 10   -419 ?    ?   ?   A . n 
A 1 11   GLU 11   -418 ?    ?   ?   A . n 
A 1 12   LYS 12   -417 ?    ?   ?   A . n 
A 1 13   GLY 13   -416 ?    ?   ?   A . n 
A 1 14   GLY 14   -415 ?    ?   ?   A . n 
A 1 15   GLY 15   -414 ?    ?   ?   A . n 
A 1 16   SER 16   -413 ?    ?   ?   A . n 
A 1 17   GLY 17   -412 ?    ?   ?   A . n 
A 1 18   GLY 18   -411 ?    ?   ?   A . n 
A 1 19   GLY 19   -410 ?    ?   ?   A . n 
A 1 20   SER 20   -409 ?    ?   ?   A . n 
A 1 21   GLY 21   -408 ?    ?   ?   A . n 
A 1 22   GLY 22   -407 ?    ?   ?   A . n 
A 1 23   SER 23   -406 ?    ?   ?   A . n 
A 1 24   ALA 24   -405 ?    ?   ?   A . n 
A 1 25   TRP 25   -404 ?    ?   ?   A . n 
A 1 26   SER 26   -403 ?    ?   ?   A . n 
A 1 27   HIS 27   -402 ?    ?   ?   A . n 
A 1 28   PRO 28   -401 ?    ?   ?   A . n 
A 1 29   GLN 29   -400 ?    ?   ?   A . n 
A 1 30   PHE 30   -399 ?    ?   ?   A . n 
A 1 31   GLU 31   -398 ?    ?   ?   A . n 
A 1 32   LYS 32   -397 ?    ?   ?   A . n 
A 1 33   GLY 33   -396 ?    ?   ?   A . n 
A 1 34   SER 34   -395 ?    ?   ?   A . n 
A 1 35   ALA 35   -394 ?    ?   ?   A . n 
A 1 36   SER 36   -393 ?    ?   ?   A . n 
A 1 37   HIS 37   -392 ?    ?   ?   A . n 
A 1 38   HIS 38   -391 ?    ?   ?   A . n 
A 1 39   HIS 39   -390 ?    ?   ?   A . n 
A 1 40   HIS 40   -389 ?    ?   ?   A . n 
A 1 41   HIS 41   -388 ?    ?   ?   A . n 
A 1 42   HIS 42   -387 ?    ?   ?   A . n 
A 1 43   GLY 43   -386 ?    ?   ?   A . n 
A 1 44   THR 44   -385 ?    ?   ?   A . n 
A 1 45   LYS 45   -384 ?    ?   ?   A . n 
A 1 46   THR 46   -383 ?    ?   ?   A . n 
A 1 47   GLU 47   -382 ?    ?   ?   A . n 
A 1 48   GLU 48   -381 ?    ?   ?   A . n 
A 1 49   GLY 49   -380 ?    ?   ?   A . n 
A 1 50   LYS 50   -379 ?    ?   ?   A . n 
A 1 51   LEU 51   -378 ?    ?   ?   A . n 
A 1 52   VAL 52   -377 ?    ?   ?   A . n 
A 1 53   ILE 53   -376 ?    ?   ?   A . n 
A 1 54   TRP 54   -375 ?    ?   ?   A . n 
A 1 55   ILE 55   -374 ?    ?   ?   A . n 
A 1 56   ASN 56   -373 ?    ?   ?   A . n 
A 1 57   GLY 57   -372 ?    ?   ?   A . n 
A 1 58   ASP 58   -371 ?    ?   ?   A . n 
A 1 59   LYS 59   -370 ?    ?   ?   A . n 
A 1 60   GLY 60   -369 ?    ?   ?   A . n 
A 1 61   TYR 61   -368 ?    ?   ?   A . n 
A 1 62   ASN 62   -367 ?    ?   ?   A . n 
A 1 63   GLY 63   -366 ?    ?   ?   A . n 
A 1 64   LEU 64   -365 ?    ?   ?   A . n 
A 1 65   ALA 65   -364 ?    ?   ?   A . n 
A 1 66   GLU 66   -363 ?    ?   ?   A . n 
A 1 67   VAL 67   -362 ?    ?   ?   A . n 
A 1 68   GLY 68   -361 ?    ?   ?   A . n 
A 1 69   LYS 69   -360 ?    ?   ?   A . n 
A 1 70   LYS 70   -359 ?    ?   ?   A . n 
A 1 71   PHE 71   -358 ?    ?   ?   A . n 
A 1 72   GLU 72   -357 ?    ?   ?   A . n 
A 1 73   LYS 73   -356 ?    ?   ?   A . n 
A 1 74   ASP 74   -355 ?    ?   ?   A . n 
A 1 75   THR 75   -354 ?    ?   ?   A . n 
A 1 76   GLY 76   -353 ?    ?   ?   A . n 
A 1 77   ILE 77   -352 ?    ?   ?   A . n 
A 1 78   LYS 78   -351 ?    ?   ?   A . n 
A 1 79   VAL 79   -350 ?    ?   ?   A . n 
A 1 80   THR 80   -349 ?    ?   ?   A . n 
A 1 81   VAL 81   -348 ?    ?   ?   A . n 
A 1 82   GLU 82   -347 ?    ?   ?   A . n 
A 1 83   HIS 83   -346 ?    ?   ?   A . n 
A 1 84   PRO 84   -345 ?    ?   ?   A . n 
A 1 85   ASP 85   -344 ?    ?   ?   A . n 
A 1 86   LYS 86   -343 ?    ?   ?   A . n 
A 1 87   LEU 87   -342 ?    ?   ?   A . n 
A 1 88   GLU 88   -341 ?    ?   ?   A . n 
A 1 89   GLU 89   -340 ?    ?   ?   A . n 
A 1 90   LYS 90   -339 ?    ?   ?   A . n 
A 1 91   PHE 91   -338 ?    ?   ?   A . n 
A 1 92   PRO 92   -337 ?    ?   ?   A . n 
A 1 93   GLN 93   -336 ?    ?   ?   A . n 
A 1 94   VAL 94   -335 ?    ?   ?   A . n 
A 1 95   ALA 95   -334 ?    ?   ?   A . n 
A 1 96   ALA 96   -333 ?    ?   ?   A . n 
A 1 97   THR 97   -332 ?    ?   ?   A . n 
A 1 98   GLY 98   -331 ?    ?   ?   A . n 
A 1 99   ASP 99   -330 ?    ?   ?   A . n 
A 1 100  GLY 100  -329 ?    ?   ?   A . n 
A 1 101  PRO 101  -328 ?    ?   ?   A . n 
A 1 102  ASP 102  -327 ?    ?   ?   A . n 
A 1 103  ILE 103  -326 ?    ?   ?   A . n 
A 1 104  ILE 104  -325 ?    ?   ?   A . n 
A 1 105  PHE 105  -324 ?    ?   ?   A . n 
A 1 106  TRP 106  -323 ?    ?   ?   A . n 
A 1 107  ALA 107  -322 ?    ?   ?   A . n 
A 1 108  HIS 108  -321 ?    ?   ?   A . n 
A 1 109  ASP 109  -320 ?    ?   ?   A . n 
A 1 110  ARG 110  -319 ?    ?   ?   A . n 
A 1 111  PHE 111  -318 ?    ?   ?   A . n 
A 1 112  GLY 112  -317 ?    ?   ?   A . n 
A 1 113  GLY 113  -316 ?    ?   ?   A . n 
A 1 114  TYR 114  -315 ?    ?   ?   A . n 
A 1 115  ALA 115  -314 ?    ?   ?   A . n 
A 1 116  GLN 116  -313 ?    ?   ?   A . n 
A 1 117  SER 117  -312 ?    ?   ?   A . n 
A 1 118  GLY 118  -311 ?    ?   ?   A . n 
A 1 119  LEU 119  -310 ?    ?   ?   A . n 
A 1 120  LEU 120  -309 ?    ?   ?   A . n 
A 1 121  ALA 121  -308 ?    ?   ?   A . n 
A 1 122  GLU 122  -307 ?    ?   ?   A . n 
A 1 123  ILE 123  -306 ?    ?   ?   A . n 
A 1 124  THR 124  -305 ?    ?   ?   A . n 
A 1 125  PRO 125  -304 ?    ?   ?   A . n 
A 1 126  ASP 126  -303 ?    ?   ?   A . n 
A 1 127  LYS 127  -302 ?    ?   ?   A . n 
A 1 128  ALA 128  -301 ?    ?   ?   A . n 
A 1 129  PHE 129  -300 ?    ?   ?   A . n 
A 1 130  GLN 130  -299 ?    ?   ?   A . n 
A 1 131  ASP 131  -298 ?    ?   ?   A . n 
A 1 132  LYS 132  -297 ?    ?   ?   A . n 
A 1 133  LEU 133  -296 ?    ?   ?   A . n 
A 1 134  TYR 134  -295 ?    ?   ?   A . n 
A 1 135  PRO 135  -294 ?    ?   ?   A . n 
A 1 136  PHE 136  -293 ?    ?   ?   A . n 
A 1 137  THR 137  -292 ?    ?   ?   A . n 
A 1 138  TRP 138  -291 ?    ?   ?   A . n 
A 1 139  ASP 139  -290 ?    ?   ?   A . n 
A 1 140  ALA 140  -289 ?    ?   ?   A . n 
A 1 141  VAL 141  -288 ?    ?   ?   A . n 
A 1 142  ARG 142  -287 ?    ?   ?   A . n 
A 1 143  TYR 143  -286 ?    ?   ?   A . n 
A 1 144  ASN 144  -285 ?    ?   ?   A . n 
A 1 145  GLY 145  -284 ?    ?   ?   A . n 
A 1 146  LYS 146  -283 ?    ?   ?   A . n 
A 1 147  LEU 147  -282 ?    ?   ?   A . n 
A 1 148  ILE 148  -281 ?    ?   ?   A . n 
A 1 149  ALA 149  -280 ?    ?   ?   A . n 
A 1 150  TYR 150  -279 ?    ?   ?   A . n 
A 1 151  PRO 151  -278 ?    ?   ?   A . n 
A 1 152  ILE 152  -277 ?    ?   ?   A . n 
A 1 153  ALA 153  -276 ?    ?   ?   A . n 
A 1 154  VAL 154  -275 ?    ?   ?   A . n 
A 1 155  GLU 155  -274 ?    ?   ?   A . n 
A 1 156  ALA 156  -273 ?    ?   ?   A . n 
A 1 157  LEU 157  -272 ?    ?   ?   A . n 
A 1 158  SER 158  -271 ?    ?   ?   A . n 
A 1 159  LEU 159  -270 ?    ?   ?   A . n 
A 1 160  ILE 160  -269 ?    ?   ?   A . n 
A 1 161  TYR 161  -268 ?    ?   ?   A . n 
A 1 162  ASN 162  -267 ?    ?   ?   A . n 
A 1 163  LYS 163  -266 ?    ?   ?   A . n 
A 1 164  ASP 164  -265 ?    ?   ?   A . n 
A 1 165  LEU 165  -264 ?    ?   ?   A . n 
A 1 166  LEU 166  -263 ?    ?   ?   A . n 
A 1 167  PRO 167  -262 ?    ?   ?   A . n 
A 1 168  ASN 168  -261 ?    ?   ?   A . n 
A 1 169  PRO 169  -260 ?    ?   ?   A . n 
A 1 170  PRO 170  -259 ?    ?   ?   A . n 
A 1 171  LYS 171  -258 ?    ?   ?   A . n 
A 1 172  THR 172  -257 ?    ?   ?   A . n 
A 1 173  TRP 173  -256 ?    ?   ?   A . n 
A 1 174  GLU 174  -255 ?    ?   ?   A . n 
A 1 175  GLU 175  -254 ?    ?   ?   A . n 
A 1 176  ILE 176  -253 ?    ?   ?   A . n 
A 1 177  PRO 177  -252 ?    ?   ?   A . n 
A 1 178  ALA 178  -251 ?    ?   ?   A . n 
A 1 179  LEU 179  -250 ?    ?   ?   A . n 
A 1 180  ASP 180  -249 ?    ?   ?   A . n 
A 1 181  LYS 181  -248 ?    ?   ?   A . n 
A 1 182  GLU 182  -247 ?    ?   ?   A . n 
A 1 183  LEU 183  -246 ?    ?   ?   A . n 
A 1 184  LYS 184  -245 ?    ?   ?   A . n 
A 1 185  ALA 185  -244 ?    ?   ?   A . n 
A 1 186  LYS 186  -243 ?    ?   ?   A . n 
A 1 187  GLY 187  -242 ?    ?   ?   A . n 
A 1 188  LYS 188  -241 ?    ?   ?   A . n 
A 1 189  SER 189  -240 ?    ?   ?   A . n 
A 1 190  ALA 190  -239 ?    ?   ?   A . n 
A 1 191  LEU 191  -238 ?    ?   ?   A . n 
A 1 192  MET 192  -237 ?    ?   ?   A . n 
A 1 193  PHE 193  -236 ?    ?   ?   A . n 
A 1 194  ASN 194  -235 ?    ?   ?   A . n 
A 1 195  LEU 195  -234 ?    ?   ?   A . n 
A 1 196  GLN 196  -233 ?    ?   ?   A . n 
A 1 197  GLU 197  -232 ?    ?   ?   A . n 
A 1 198  PRO 198  -231 ?    ?   ?   A . n 
A 1 199  TYR 199  -230 ?    ?   ?   A . n 
A 1 200  PHE 200  -229 ?    ?   ?   A . n 
A 1 201  THR 201  -228 ?    ?   ?   A . n 
A 1 202  TRP 202  -227 ?    ?   ?   A . n 
A 1 203  PRO 203  -226 ?    ?   ?   A . n 
A 1 204  LEU 204  -225 ?    ?   ?   A . n 
A 1 205  ILE 205  -224 ?    ?   ?   A . n 
A 1 206  ALA 206  -223 ?    ?   ?   A . n 
A 1 207  ALA 207  -222 ?    ?   ?   A . n 
A 1 208  ASP 208  -221 ?    ?   ?   A . n 
A 1 209  GLY 209  -220 ?    ?   ?   A . n 
A 1 210  GLY 210  -219 ?    ?   ?   A . n 
A 1 211  TYR 211  -218 ?    ?   ?   A . n 
A 1 212  ALA 212  -217 ?    ?   ?   A . n 
A 1 213  PHE 213  -216 ?    ?   ?   A . n 
A 1 214  LYS 214  -215 ?    ?   ?   A . n 
A 1 215  TYR 215  -214 ?    ?   ?   A . n 
A 1 216  GLU 216  -213 ?    ?   ?   A . n 
A 1 217  ASN 217  -212 ?    ?   ?   A . n 
A 1 218  GLY 218  -211 ?    ?   ?   A . n 
A 1 219  LYS 219  -210 ?    ?   ?   A . n 
A 1 220  TYR 220  -209 ?    ?   ?   A . n 
A 1 221  ASP 221  -208 ?    ?   ?   A . n 
A 1 222  ILE 222  -207 ?    ?   ?   A . n 
A 1 223  LYS 223  -206 ?    ?   ?   A . n 
A 1 224  ASP 224  -205 ?    ?   ?   A . n 
A 1 225  VAL 225  -204 ?    ?   ?   A . n 
A 1 226  GLY 226  -203 ?    ?   ?   A . n 
A 1 227  VAL 227  -202 ?    ?   ?   A . n 
A 1 228  ASP 228  -201 ?    ?   ?   A . n 
A 1 229  ASN 229  -200 ?    ?   ?   A . n 
A 1 230  ALA 230  -199 ?    ?   ?   A . n 
A 1 231  GLY 231  -198 ?    ?   ?   A . n 
A 1 232  ALA 232  -197 ?    ?   ?   A . n 
A 1 233  LYS 233  -196 ?    ?   ?   A . n 
A 1 234  ALA 234  -195 ?    ?   ?   A . n 
A 1 235  GLY 235  -194 ?    ?   ?   A . n 
A 1 236  LEU 236  -193 ?    ?   ?   A . n 
A 1 237  THR 237  -192 ?    ?   ?   A . n 
A 1 238  PHE 238  -191 ?    ?   ?   A . n 
A 1 239  LEU 239  -190 ?    ?   ?   A . n 
A 1 240  VAL 240  -189 ?    ?   ?   A . n 
A 1 241  ASP 241  -188 ?    ?   ?   A . n 
A 1 242  LEU 242  -187 ?    ?   ?   A . n 
A 1 243  ILE 243  -186 ?    ?   ?   A . n 
A 1 244  LYS 244  -185 ?    ?   ?   A . n 
A 1 245  ASN 245  -184 ?    ?   ?   A . n 
A 1 246  LYS 246  -183 ?    ?   ?   A . n 
A 1 247  HIS 247  -182 ?    ?   ?   A . n 
A 1 248  MET 248  -181 ?    ?   ?   A . n 
A 1 249  ASN 249  -180 ?    ?   ?   A . n 
A 1 250  ALA 250  -179 ?    ?   ?   A . n 
A 1 251  ASP 251  -178 ?    ?   ?   A . n 
A 1 252  THR 252  -177 ?    ?   ?   A . n 
A 1 253  ASP 253  -176 ?    ?   ?   A . n 
A 1 254  TYR 254  -175 ?    ?   ?   A . n 
A 1 255  SER 255  -174 ?    ?   ?   A . n 
A 1 256  ILE 256  -173 ?    ?   ?   A . n 
A 1 257  ALA 257  -172 ?    ?   ?   A . n 
A 1 258  GLU 258  -171 ?    ?   ?   A . n 
A 1 259  ALA 259  -170 ?    ?   ?   A . n 
A 1 260  ALA 260  -169 ?    ?   ?   A . n 
A 1 261  PHE 261  -168 ?    ?   ?   A . n 
A 1 262  ASN 262  -167 ?    ?   ?   A . n 
A 1 263  LYS 263  -166 ?    ?   ?   A . n 
A 1 264  GLY 264  -165 ?    ?   ?   A . n 
A 1 265  GLU 265  -164 ?    ?   ?   A . n 
A 1 266  THR 266  -163 ?    ?   ?   A . n 
A 1 267  ALA 267  -162 ?    ?   ?   A . n 
A 1 268  MET 268  -161 ?    ?   ?   A . n 
A 1 269  THR 269  -160 ?    ?   ?   A . n 
A 1 270  ILE 270  -159 ?    ?   ?   A . n 
A 1 271  ASN 271  -158 ?    ?   ?   A . n 
A 1 272  GLY 272  -157 ?    ?   ?   A . n 
A 1 273  PRO 273  -156 ?    ?   ?   A . n 
A 1 274  TRP 274  -155 ?    ?   ?   A . n 
A 1 275  ALA 275  -154 ?    ?   ?   A . n 
A 1 276  TRP 276  -153 ?    ?   ?   A . n 
A 1 277  SER 277  -152 ?    ?   ?   A . n 
A 1 278  ASN 278  -151 ?    ?   ?   A . n 
A 1 279  ILE 279  -150 ?    ?   ?   A . n 
A 1 280  ASP 280  -149 ?    ?   ?   A . n 
A 1 281  THR 281  -148 ?    ?   ?   A . n 
A 1 282  SER 282  -147 ?    ?   ?   A . n 
A 1 283  LYS 283  -146 ?    ?   ?   A . n 
A 1 284  VAL 284  -145 ?    ?   ?   A . n 
A 1 285  ASN 285  -144 ?    ?   ?   A . n 
A 1 286  TYR 286  -143 ?    ?   ?   A . n 
A 1 287  GLY 287  -142 ?    ?   ?   A . n 
A 1 288  VAL 288  -141 ?    ?   ?   A . n 
A 1 289  THR 289  -140 ?    ?   ?   A . n 
A 1 290  VAL 290  -139 ?    ?   ?   A . n 
A 1 291  LEU 291  -138 ?    ?   ?   A . n 
A 1 292  PRO 292  -137 ?    ?   ?   A . n 
A 1 293  THR 293  -136 ?    ?   ?   A . n 
A 1 294  PHE 294  -135 ?    ?   ?   A . n 
A 1 295  LYS 295  -134 ?    ?   ?   A . n 
A 1 296  GLY 296  -133 ?    ?   ?   A . n 
A 1 297  GLN 297  -132 ?    ?   ?   A . n 
A 1 298  PRO 298  -131 ?    ?   ?   A . n 
A 1 299  SER 299  -130 ?    ?   ?   A . n 
A 1 300  LYS 300  -129 ?    ?   ?   A . n 
A 1 301  PRO 301  -128 ?    ?   ?   A . n 
A 1 302  PHE 302  -127 ?    ?   ?   A . n 
A 1 303  VAL 303  -126 ?    ?   ?   A . n 
A 1 304  GLY 304  -125 ?    ?   ?   A . n 
A 1 305  VAL 305  -124 ?    ?   ?   A . n 
A 1 306  LEU 306  -123 ?    ?   ?   A . n 
A 1 307  SER 307  -122 ?    ?   ?   A . n 
A 1 308  ALA 308  -121 ?    ?   ?   A . n 
A 1 309  GLY 309  -120 ?    ?   ?   A . n 
A 1 310  ILE 310  -119 ?    ?   ?   A . n 
A 1 311  ASN 311  -118 ?    ?   ?   A . n 
A 1 312  ALA 312  -117 ?    ?   ?   A . n 
A 1 313  ALA 313  -116 ?    ?   ?   A . n 
A 1 314  SER 314  -115 ?    ?   ?   A . n 
A 1 315  PRO 315  -114 ?    ?   ?   A . n 
A 1 316  ASN 316  -113 ?    ?   ?   A . n 
A 1 317  LYS 317  -112 ?    ?   ?   A . n 
A 1 318  GLU 318  -111 ?    ?   ?   A . n 
A 1 319  LEU 319  -110 ?    ?   ?   A . n 
A 1 320  ALA 320  -109 ?    ?   ?   A . n 
A 1 321  LYS 321  -108 ?    ?   ?   A . n 
A 1 322  GLU 322  -107 ?    ?   ?   A . n 
A 1 323  PHE 323  -106 ?    ?   ?   A . n 
A 1 324  LEU 324  -105 ?    ?   ?   A . n 
A 1 325  GLU 325  -104 ?    ?   ?   A . n 
A 1 326  ASN 326  -103 ?    ?   ?   A . n 
A 1 327  TYR 327  -102 ?    ?   ?   A . n 
A 1 328  LEU 328  -101 ?    ?   ?   A . n 
A 1 329  LEU 329  -100 ?    ?   ?   A . n 
A 1 330  THR 330  -99  ?    ?   ?   A . n 
A 1 331  ASP 331  -98  ?    ?   ?   A . n 
A 1 332  GLU 332  -97  ?    ?   ?   A . n 
A 1 333  GLY 333  -96  ?    ?   ?   A . n 
A 1 334  LEU 334  -95  ?    ?   ?   A . n 
A 1 335  GLU 335  -94  ?    ?   ?   A . n 
A 1 336  ALA 336  -93  ?    ?   ?   A . n 
A 1 337  VAL 337  -92  ?    ?   ?   A . n 
A 1 338  ASN 338  -91  ?    ?   ?   A . n 
A 1 339  LYS 339  -90  ?    ?   ?   A . n 
A 1 340  ASP 340  -89  ?    ?   ?   A . n 
A 1 341  LYS 341  -88  ?    ?   ?   A . n 
A 1 342  PRO 342  -87  ?    ?   ?   A . n 
A 1 343  LEU 343  -86  ?    ?   ?   A . n 
A 1 344  GLY 344  -85  ?    ?   ?   A . n 
A 1 345  ALA 345  -84  ?    ?   ?   A . n 
A 1 346  VAL 346  -83  ?    ?   ?   A . n 
A 1 347  ALA 347  -82  ?    ?   ?   A . n 
A 1 348  LEU 348  -81  ?    ?   ?   A . n 
A 1 349  LYS 349  -80  ?    ?   ?   A . n 
A 1 350  SER 350  -79  ?    ?   ?   A . n 
A 1 351  TYR 351  -78  ?    ?   ?   A . n 
A 1 352  GLU 352  -77  ?    ?   ?   A . n 
A 1 353  GLU 353  -76  ?    ?   ?   A . n 
A 1 354  GLU 354  -75  ?    ?   ?   A . n 
A 1 355  LEU 355  -74  ?    ?   ?   A . n 
A 1 356  ALA 356  -73  ?    ?   ?   A . n 
A 1 357  LYS 357  -72  ?    ?   ?   A . n 
A 1 358  ASP 358  -71  ?    ?   ?   A . n 
A 1 359  PRO 359  -70  ?    ?   ?   A . n 
A 1 360  ARG 360  -69  ?    ?   ?   A . n 
A 1 361  ILE 361  -68  ?    ?   ?   A . n 
A 1 362  ALA 362  -67  ?    ?   ?   A . n 
A 1 363  ALA 363  -66  ?    ?   ?   A . n 
A 1 364  THR 364  -65  ?    ?   ?   A . n 
A 1 365  MET 365  -64  ?    ?   ?   A . n 
A 1 366  GLU 366  -63  ?    ?   ?   A . n 
A 1 367  ASN 367  -62  ?    ?   ?   A . n 
A 1 368  ALA 368  -61  ?    ?   ?   A . n 
A 1 369  GLN 369  -60  ?    ?   ?   A . n 
A 1 370  LYS 370  -59  ?    ?   ?   A . n 
A 1 371  GLY 371  -58  ?    ?   ?   A . n 
A 1 372  GLU 372  -57  ?    ?   ?   A . n 
A 1 373  ILE 373  -56  ?    ?   ?   A . n 
A 1 374  MET 374  -55  ?    ?   ?   A . n 
A 1 375  PRO 375  -54  ?    ?   ?   A . n 
A 1 376  ASN 376  -53  ?    ?   ?   A . n 
A 1 377  ILE 377  -52  ?    ?   ?   A . n 
A 1 378  PRO 378  -51  ?    ?   ?   A . n 
A 1 379  GLN 379  -50  ?    ?   ?   A . n 
A 1 380  MET 380  -49  ?    ?   ?   A . n 
A 1 381  SER 381  -48  ?    ?   ?   A . n 
A 1 382  ALA 382  -47  ?    ?   ?   A . n 
A 1 383  PHE 383  -46  ?    ?   ?   A . n 
A 1 384  TRP 384  -45  ?    ?   ?   A . n 
A 1 385  TYR 385  -44  ?    ?   ?   A . n 
A 1 386  ALA 386  -43  ?    ?   ?   A . n 
A 1 387  VAL 387  -42  ?    ?   ?   A . n 
A 1 388  ARG 388  -41  ?    ?   ?   A . n 
A 1 389  THR 389  -40  ?    ?   ?   A . n 
A 1 390  ALA 390  -39  ?    ?   ?   A . n 
A 1 391  VAL 391  -38  ?    ?   ?   A . n 
A 1 392  ILE 392  -37  ?    ?   ?   A . n 
A 1 393  ASN 393  -36  ?    ?   ?   A . n 
A 1 394  ALA 394  -35  ?    ?   ?   A . n 
A 1 395  ALA 395  -34  ?    ?   ?   A . n 
A 1 396  SER 396  -33  ?    ?   ?   A . n 
A 1 397  GLY 397  -32  ?    ?   ?   A . n 
A 1 398  ARG 398  -31  ?    ?   ?   A . n 
A 1 399  GLN 399  -30  ?    ?   ?   A . n 
A 1 400  THR 400  -29  ?    ?   ?   A . n 
A 1 401  VAL 401  -28  ?    ?   ?   A . n 
A 1 402  ASP 402  -27  ?    ?   ?   A . n 
A 1 403  GLU 403  -26  ?    ?   ?   A . n 
A 1 404  ALA 404  -25  ?    ?   ?   A . n 
A 1 405  LEU 405  -24  ?    ?   ?   A . n 
A 1 406  LYS 406  -23  ?    ?   ?   A . n 
A 1 407  ASP 407  -22  ?    ?   ?   A . n 
A 1 408  ALA 408  -21  ?    ?   ?   A . n 
A 1 409  GLN 409  -20  ?    ?   ?   A . n 
A 1 410  THR 410  -19  ?    ?   ?   A . n 
A 1 411  GLY 411  -18  ?    ?   ?   A . n 
A 1 412  THR 412  -17  ?    ?   ?   A . n 
A 1 413  ASP 413  -16  ?    ?   ?   A . n 
A 1 414  TYR 414  -15  ?    ?   ?   A . n 
A 1 415  ASP 415  -14  ?    ?   ?   A . n 
A 1 416  ILE 416  -13  ?    ?   ?   A . n 
A 1 417  PRO 417  -12  ?    ?   ?   A . n 
A 1 418  THR 418  -11  ?    ?   ?   A . n 
A 1 419  THR 419  -10  ?    ?   ?   A . n 
A 1 420  LEU 420  -9   ?    ?   ?   A . n 
A 1 421  GLU 421  -8   ?    ?   ?   A . n 
A 1 422  VAL 422  -7   ?    ?   ?   A . n 
A 1 423  LEU 423  -6   ?    ?   ?   A . n 
A 1 424  PHE 424  -5   ?    ?   ?   A . n 
A 1 425  GLN 425  -4   ?    ?   ?   A . n 
A 1 426  GLY 426  -3   ?    ?   ?   A . n 
A 1 427  PRO 427  -2   ?    ?   ?   A . n 
A 1 428  GLY 428  -1   ?    ?   ?   A . n 
A 1 429  SER 429  0    ?    ?   ?   A . n 
A 1 430  MET 430  1    ?    ?   ?   A . n 
A 1 431  ALA 431  2    ?    ?   ?   A . n 
A 1 432  THR 432  3    ?    ?   ?   A . n 
A 1 433  GLN 433  4    ?    ?   ?   A . n 
A 1 434  HIS 434  5    ?    ?   ?   A . n 
A 1 435  THR 435  6    6    THR THR A . n 
A 1 436  GLN 436  7    7    GLN GLN A . n 
A 1 437  TYR 437  8    8    TYR TYR A . n 
A 1 438  PRO 438  9    9    PRO PRO A . n 
A 1 439  ASP 439  10   10   ASP ASP A . n 
A 1 440  ALA 440  11   11   ALA ALA A . n 
A 1 441  ARG 441  12   12   ARG ARG A . n 
A 1 442  LEU 442  13   13   LEU LEU A . n 
A 1 443  SER 443  14   14   SER SER A . n 
A 1 444  SER 444  15   15   SER SER A . n 
A 1 445  PRO 445  16   16   PRO PRO A . n 
A 1 446  ILE 446  17   17   ILE ILE A . n 
A 1 447  VAL 447  18   18   VAL VAL A . n 
A 1 448  LEU 448  19   19   LEU LEU A . n 
A 1 449  ASP 449  20   20   ASP ASP A . n 
A 1 450  GLN 450  21   21   GLN GLN A . n 
A 1 451  CYS 451  22   22   CYS CYS A . n 
A 1 452  ASP 452  23   23   ASP ASP A . n 
A 1 453  LEU 453  24   24   LEU LEU A . n 
A 1 454  VAL 454  25   25   VAL VAL A . n 
A 1 455  THR 455  26   26   THR THR A . n 
A 1 456  ARG 456  27   27   ARG ARG A . n 
A 1 457  ALA 457  28   28   ALA ALA A . n 
A 1 458  CYS 458  29   29   CYS CYS A . n 
A 1 459  GLY 459  30   30   GLY GLY A . n 
A 1 460  LEU 460  31   31   LEU LEU A . n 
A 1 461  TYR 461  32   32   TYR TYR A . n 
A 1 462  SER 462  33   33   SER SER A . n 
A 1 463  SER 463  34   34   SER SER A . n 
A 1 464  TYR 464  35   35   TYR TYR A . n 
A 1 465  SER 465  36   36   SER SER A . n 
A 1 466  LEU 466  37   37   LEU LEU A . n 
A 1 467  ASN 467  38   38   ASN ASN A . n 
A 1 468  PRO 468  39   39   PRO PRO A . n 
A 1 469  GLN 469  40   40   GLN GLN A . n 
A 1 470  LEU 470  41   41   LEU LEU A . n 
A 1 471  ARG 471  42   42   ARG ARG A . n 
A 1 472  ASN 472  43   43   ASN ASN A . n 
A 1 473  CYS 473  44   44   CYS CYS A . n 
A 1 474  LYS 474  45   45   LYS LYS A . n 
A 1 475  LEU 475  46   46   LEU LEU A . n 
A 1 476  PRO 476  47   47   PRO PRO A . n 
A 1 477  LYS 477  48   48   LYS LYS A . n 
A 1 478  HIS 478  49   49   HIS HIS A . n 
A 1 479  ILE 479  50   50   ILE ILE A . n 
A 1 480  TYR 480  51   51   TYR TYR A . n 
A 1 481  ARG 481  52   52   ARG ARG A . n 
A 1 482  LEU 482  53   53   LEU LEU A . n 
A 1 483  LYS 483  54   54   LYS LYS A . n 
A 1 484  TYR 484  55   55   TYR TYR A . n 
A 1 485  ASP 485  56   56   ASP ASP A . n 
A 1 486  VAL 486  57   57   VAL VAL A . n 
A 1 487  THR 487  58   58   THR THR A . n 
A 1 488  VAL 488  59   59   VAL VAL A . n 
A 1 489  THR 489  60   60   THR THR A . n 
A 1 490  LYS 490  61   61   LYS LYS A . n 
A 1 491  PHE 491  62   62   PHE PHE A . n 
A 1 492  LEU 492  63   63   LEU LEU A . n 
A 1 493  SER 493  64   64   SER SER A . n 
A 1 494  ASP 494  65   65   ASP ASP A . n 
A 1 495  VAL 495  66   66   VAL VAL A . n 
A 1 496  PRO 496  67   67   PRO PRO A . n 
A 1 497  VAL 497  68   68   VAL VAL A . n 
A 1 498  ALA 498  69   69   ALA ALA A . n 
A 1 499  THR 499  70   70   THR THR A . n 
A 1 500  LEU 500  71   71   LEU LEU A . n 
A 1 501  PRO 501  72   72   PRO PRO A . n 
A 1 502  ILE 502  73   73   ILE ILE A . n 
A 1 503  ASP 503  74   74   ASP ASP A . n 
A 1 504  PHE 504  75   75   PHE PHE A . n 
A 1 505  ILE 505  76   76   ILE ILE A . n 
A 1 506  VAL 506  77   77   VAL VAL A . n 
A 1 507  PRO 507  78   78   PRO PRO A . n 
A 1 508  VAL 508  79   79   VAL VAL A . n 
A 1 509  LEU 509  80   80   LEU LEU A . n 
A 1 510  LEU 510  81   81   LEU LEU A . n 
A 1 511  LYS 511  82   82   LYS LYS A . n 
A 1 512  ALA 512  83   83   ALA ALA A . n 
A 1 513  LEU 513  84   84   LEU LEU A . n 
A 1 514  SER 514  85   85   SER SER A . n 
A 1 515  GLY 515  86   86   GLY GLY A . n 
A 1 516  ASN 516  87   87   ASN ASN A . n 
A 1 517  GLY 517  88   88   GLY GLY A . n 
A 1 518  PHE 518  89   89   PHE PHE A . n 
A 1 519  CYS 519  90   90   CYS CYS A . n 
A 1 520  PRO 520  91   91   PRO PRO A . n 
A 1 521  VAL 521  92   92   VAL VAL A . n 
A 1 522  GLU 522  93   93   GLU GLU A . n 
A 1 523  PRO 523  94   94   PRO PRO A . n 
A 1 524  ARG 524  95   95   ARG ARG A . n 
A 1 525  CYS 525  96   96   CYS CYS A . n 
A 1 526  GLN 526  97   97   GLN GLN A . n 
A 1 527  GLN 527  98   98   GLN GLN A . n 
A 1 528  PHE 528  99   99   PHE PHE A . n 
A 1 529  LEU 529  100  100  LEU LEU A . n 
A 1 530  ASP 530  101  101  ASP ASP A . n 
A 1 531  GLU 531  102  102  GLU GLU A . n 
A 1 532  ILE 532  103  103  ILE ILE A . n 
A 1 533  ILE 533  104  104  ILE ILE A . n 
A 1 534  LYS 534  105  105  LYS LYS A . n 
A 1 535  TYR 535  106  106  TYR TYR A . n 
A 1 536  THR 536  107  107  THR THR A . n 
A 1 537  MET 537  108  108  MET MET A . n 
A 1 538  GLN 538  109  109  GLN GLN A . n 
A 1 539  ASP 539  110  110  ASP ASP A . n 
A 1 540  ALA 540  111  111  ALA ALA A . n 
A 1 541  LEU 541  112  112  LEU LEU A . n 
A 1 542  PHE 542  113  113  PHE PHE A . n 
A 1 543  LEU 543  114  114  LEU LEU A . n 
A 1 544  LYS 544  115  115  LYS LYS A . n 
A 1 545  TYR 545  116  116  TYR TYR A . n 
A 1 546  TYR 546  117  117  TYR TYR A . n 
A 1 547  LEU 547  118  118  LEU LEU A . n 
A 1 548  LYS 548  119  119  LYS LYS A . n 
A 1 549  ASN 549  120  120  ASN ASN A . n 
A 1 550  VAL 550  121  121  VAL VAL A . n 
A 1 551  GLY 551  122  122  GLY GLY A . n 
A 1 552  ALA 552  123  123  ALA ALA A . n 
A 1 553  GLN 553  124  124  GLN GLN A . n 
A 1 554  GLU 554  125  125  GLU GLU A . n 
A 1 555  ASP 555  126  126  ASP ASP A . n 
A 1 556  CYS 556  127  127  CYS CYS A . n 
A 1 557  VAL 557  128  128  VAL VAL A . n 
A 1 558  ASP 558  129  129  ASP ASP A . n 
A 1 559  GLU 559  130  130  GLU GLU A . n 
A 1 560  HIS 560  131  131  HIS HIS A . n 
A 1 561  PHE 561  132  132  PHE PHE A . n 
A 1 562  GLN 562  133  133  GLN GLN A . n 
A 1 563  GLU 563  134  134  GLU GLU A . n 
A 1 564  LYS 564  135  135  LYS LYS A . n 
A 1 565  ILE 565  136  136  ILE ILE A . n 
A 1 566  LEU 566  137  137  LEU LEU A . n 
A 1 567  SER 567  138  138  SER SER A . n 
A 1 568  SER 568  139  139  SER SER A . n 
A 1 569  ILE 569  140  140  ILE ILE A . n 
A 1 570  GLN 570  141  141  GLN GLN A . n 
A 1 571  GLY 571  142  142  GLY GLY A . n 
A 1 572  ASN 572  143  143  ASN ASN A . n 
A 1 573  GLU 573  144  144  GLU GLU A . n 
A 1 574  PHE 574  145  145  PHE PHE A . n 
A 1 575  LEU 575  146  146  LEU LEU A . n 
A 1 576  HIS 576  147  147  HIS HIS A . n 
A 1 577  GLN 577  148  148  GLN GLN A . n 
A 1 578  MET 578  149  149  MET MET A . n 
A 1 579  PHE 579  150  150  PHE PHE A . n 
A 1 580  PHE 580  151  151  PHE PHE A . n 
A 1 581  TRP 581  152  152  TRP TRP A . n 
A 1 582  TYR 582  153  153  TYR TYR A . n 
A 1 583  ASP 583  154  154  ASP ASP A . n 
A 1 584  LEU 584  155  155  LEU LEU A . n 
A 1 585  ALA 585  156  156  ALA ALA A . n 
A 1 586  ILE 586  157  157  ILE ILE A . n 
A 1 587  LEU 587  158  158  LEU LEU A . n 
A 1 588  THR 588  159  159  THR THR A . n 
A 1 589  ARG 589  160  160  ARG ARG A . n 
A 1 590  ARG 590  161  161  ARG ARG A . n 
A 1 591  GLY 591  162  162  GLY GLY A . n 
A 1 592  ARG 592  163  163  ARG ARG A . n 
A 1 593  LEU 593  164  164  LEU LEU A . n 
A 1 594  ASN 594  165  165  ASN ASN A . n 
A 1 595  ARG 595  166  166  ARG ARG A . n 
A 1 596  GLY 596  167  167  GLY GLY A . n 
A 1 597  ASN 597  168  168  ASN ASN A . n 
A 1 598  SER 598  169  169  SER SER A . n 
A 1 599  ARG 599  170  170  ARG ARG A . n 
A 1 600  SER 600  171  171  SER SER A . n 
A 1 601  THR 601  172  172  THR THR A . n 
A 1 602  TRP 602  173  173  TRP TRP A . n 
A 1 603  PHE 603  174  174  PHE PHE A . n 
A 1 604  VAL 604  175  175  VAL VAL A . n 
A 1 605  HIS 605  176  176  HIS HIS A . n 
A 1 606  ASP 606  177  177  ASP ASP A . n 
A 1 607  ASP 607  178  178  ASP ASP A . n 
A 1 608  LEU 608  179  179  LEU LEU A . n 
A 1 609  ILE 609  180  180  ILE ILE A . n 
A 1 610  ASP 610  181  181  ASP ASP A . n 
A 1 611  ILE 611  182  182  ILE ILE A . n 
A 1 612  LEU 612  183  183  LEU LEU A . n 
A 1 613  GLY 613  184  184  GLY GLY A . n 
A 1 614  TYR 614  185  185  TYR TYR A . n 
A 1 615  GLY 615  186  186  GLY GLY A . n 
A 1 616  ASP 616  187  187  ASP ASP A . n 
A 1 617  TYR 617  188  188  TYR TYR A . n 
A 1 618  VAL 618  189  189  VAL VAL A . n 
A 1 619  PHE 619  190  190  PHE PHE A . n 
A 1 620  TRP 620  191  191  TRP TRP A . n 
A 1 621  LYS 621  192  192  LYS LYS A . n 
A 1 622  ILE 622  193  193  ILE ILE A . n 
A 1 623  PRO 623  194  194  PRO PRO A . n 
A 1 624  ILE 624  195  195  ILE ILE A . n 
A 1 625  SER 625  196  196  SER SER A . n 
A 1 626  MET 626  197  197  MET MET A . n 
A 1 627  LEU 627  198  198  LEU LEU A . n 
A 1 628  PRO 628  199  199  PRO PRO A . n 
A 1 629  LEU 629  200  200  LEU LEU A . n 
A 1 630  ASN 630  201  201  ASN ASN A . n 
A 1 631  THR 631  202  202  THR THR A . n 
A 1 632  GLN 632  203  203  GLN GLN A . n 
A 1 633  GLY 633  204  204  GLY GLY A . n 
A 1 634  ILE 634  205  205  ILE ILE A . n 
A 1 635  PRO 635  206  206  PRO PRO A . n 
A 1 636  HIS 636  207  207  HIS HIS A . n 
A 1 637  ALA 637  208  208  ALA ALA A . n 
A 1 638  ALA 638  209  209  ALA ALA A . n 
A 1 639  MET 639  210  210  MET MET A . n 
A 1 640  ASP 640  211  211  ASP ASP A . n 
A 1 641  TRP 641  212  212  TRP TRP A . n 
A 1 642  TYR 642  213  213  TYR TYR A . n 
A 1 643  GLN 643  214  214  GLN GLN A . n 
A 1 644  ALA 644  215  215  ALA ALA A . n 
A 1 645  SER 645  216  216  SER SER A . n 
A 1 646  VAL 646  217  217  VAL VAL A . n 
A 1 647  PHE 647  218  218  PHE PHE A . n 
A 1 648  LYS 648  219  219  LYS LYS A . n 
A 1 649  GLU 649  220  220  GLU GLU A . n 
A 1 650  ALA 650  221  221  ALA ALA A . n 
A 1 651  VAL 651  222  222  VAL VAL A . n 
A 1 652  GLN 652  223  223  GLN GLN A . n 
A 1 653  GLY 653  224  224  GLY GLY A . n 
A 1 654  HIS 654  225  225  HIS HIS A . n 
A 1 655  THR 655  226  226  THR THR A . n 
A 1 656  HIS 656  227  227  HIS HIS A . n 
A 1 657  ILE 657  228  228  ILE ILE A . n 
A 1 658  VAL 658  229  229  VAL VAL A . n 
A 1 659  SER 659  230  230  SER SER A . n 
A 1 660  VAL 660  231  231  VAL VAL A . n 
A 1 661  SER 661  232  232  SER SER A . n 
A 1 662  THR 662  233  233  THR THR A . n 
A 1 663  ALA 663  234  234  ALA ALA A . n 
A 1 664  ASP 664  235  235  ASP ASP A . n 
A 1 665  VAL 665  236  236  VAL VAL A . n 
A 1 666  LEU 666  237  237  LEU LEU A . n 
A 1 667  ILE 667  238  238  ILE ILE A . n 
A 1 668  MET 668  239  239  MET MET A . n 
A 1 669  CYS 669  240  240  CYS CYS A . n 
A 1 670  LYS 670  241  241  LYS LYS A . n 
A 1 671  ASP 671  242  242  ASP ASP A . n 
A 1 672  LEU 672  243  243  LEU LEU A . n 
A 1 673  ILE 673  244  244  ILE ILE A . n 
A 1 674  THR 674  245  245  THR THR A . n 
A 1 675  CYS 675  246  246  CYS CYS A . n 
A 1 676  ARG 676  247  247  ARG ARG A . n 
A 1 677  PHE 677  248  248  PHE PHE A . n 
A 1 678  ASN 678  249  249  ASN ASN A . n 
A 1 679  THR 679  250  250  THR THR A . n 
A 1 680  THR 680  251  251  THR THR A . n 
A 1 681  LEU 681  252  252  LEU LEU A . n 
A 1 682  ILE 682  253  253  ILE ILE A . n 
A 1 683  SER 683  254  254  SER SER A . n 
A 1 684  LYS 684  255  255  LYS LYS A . n 
A 1 685  ILE 685  256  256  ILE ILE A . n 
A 1 686  ALA 686  257  257  ALA ALA A . n 
A 1 687  GLU 687  258  258  GLU GLU A . n 
A 1 688  ILE 688  259  259  ILE ILE A . n 
A 1 689  GLU 689  260  260  GLU GLU A . n 
A 1 690  ASP 690  261  261  ASP ASP A . n 
A 1 691  PRO 691  262  262  PRO PRO A . n 
A 1 692  VAL 692  263  263  VAL VAL A . n 
A 1 693  CYS 693  264  264  CYS CYS A . n 
A 1 694  SER 694  265  265  SER SER A . n 
A 1 695  ASP 695  266  266  ASP ASP A . n 
A 1 696  TYR 696  267  267  TYR TYR A . n 
A 1 697  PRO 697  268  268  PRO PRO A . n 
A 1 698  ASN 698  269  269  ASN ASN A . n 
A 1 699  PHE 699  270  270  PHE PHE A . n 
A 1 700  LYS 700  271  271  LYS LYS A . n 
A 1 701  ILE 701  272  272  ILE ILE A . n 
A 1 702  VAL 702  273  273  VAL VAL A . n 
A 1 703  SER 703  274  274  SER SER A . n 
A 1 704  MET 704  275  275  MET MET A . n 
A 1 705  LEU 705  276  276  LEU LEU A . n 
A 1 706  TYR 706  277  277  TYR TYR A . n 
A 1 707  GLN 707  278  278  GLN GLN A . n 
A 1 708  SER 708  279  279  SER SER A . n 
A 1 709  GLY 709  280  280  GLY GLY A . n 
A 1 710  ASP 710  281  281  ASP ASP A . n 
A 1 711  TYR 711  282  282  TYR TYR A . n 
A 1 712  LEU 712  283  283  LEU LEU A . n 
A 1 713  LEU 713  284  284  LEU LEU A . n 
A 1 714  SER 714  285  285  SER SER A . n 
A 1 715  ILE 715  286  286  ILE ILE A . n 
A 1 716  LEU 716  287  287  LEU LEU A . n 
A 1 717  GLY 717  288  288  GLY GLY A . n 
A 1 718  SER 718  289  289  SER SER A . n 
A 1 719  ASP 719  290  290  ASP ASP A . n 
A 1 720  GLY 720  291  291  GLY GLY A . n 
A 1 721  TYR 721  292  292  TYR TYR A . n 
A 1 722  LYS 722  293  293  LYS LYS A . n 
A 1 723  ILE 723  294  294  ILE ILE A . n 
A 1 724  ILE 724  295  295  ILE ILE A . n 
A 1 725  LYS 725  296  296  LYS LYS A . n 
A 1 726  PHE 726  297  297  PHE PHE A . n 
A 1 727  LEU 727  298  298  LEU LEU A . n 
A 1 728  GLU 728  299  299  GLU GLU A . n 
A 1 729  PRO 729  300  300  PRO PRO A . n 
A 1 730  LEU 730  301  301  LEU LEU A . n 
A 1 731  CYS 731  302  302  CYS CYS A . n 
A 1 732  LEU 732  303  303  LEU LEU A . n 
A 1 733  ALA 733  304  304  ALA ALA A . n 
A 1 734  LYS 734  305  305  LYS LYS A . n 
A 1 735  ILE 735  306  306  ILE ILE A . n 
A 1 736  GLN 736  307  307  GLN GLN A . n 
A 1 737  LEU 737  308  308  LEU LEU A . n 
A 1 738  CYS 738  309  309  CYS CYS A . n 
A 1 739  SER 739  310  310  SER SER A . n 
A 1 740  LYS 740  311  311  LYS LYS A . n 
A 1 741  TYR 741  312  312  TYR TYR A . n 
A 1 742  THR 742  313  313  THR THR A . n 
A 1 743  GLU 743  314  314  GLU GLU A . n 
A 1 744  ARG 744  315  315  ARG ARG A . n 
A 1 745  LYS 745  316  316  LYS LYS A . n 
A 1 746  GLY 746  317  317  GLY GLY A . n 
A 1 747  ARG 747  318  318  ARG ARG A . n 
A 1 748  PHE 748  319  319  PHE PHE A . n 
A 1 749  LEU 749  320  320  LEU LEU A . n 
A 1 750  THR 750  321  321  THR THR A . n 
A 1 751  GLN 751  322  322  GLN GLN A . n 
A 1 752  MET 752  323  323  MET MET A . n 
A 1 753  HIS 753  324  324  HIS HIS A . n 
A 1 754  LEU 754  325  325  LEU LEU A . n 
A 1 755  ALA 755  326  326  ALA ALA A . n 
A 1 756  VAL 756  327  327  VAL VAL A . n 
A 1 757  ASN 757  328  328  ASN ASN A . n 
A 1 758  HIS 758  329  329  HIS HIS A . n 
A 1 759  THR 759  330  330  THR THR A . n 
A 1 760  LEU 760  331  331  LEU LEU A . n 
A 1 761  GLU 761  332  332  GLU GLU A . n 
A 1 762  GLU 762  333  333  GLU GLU A . n 
A 1 763  ILE 763  334  334  ILE ILE A . n 
A 1 764  THR 764  335  335  THR THR A . n 
A 1 765  GLU 765  336  336  GLU GLU A . n 
A 1 766  MET 766  337  337  MET MET A . n 
A 1 767  ARG 767  338  338  ARG ARG A . n 
A 1 768  ALA 768  339  339  ALA ALA A . n 
A 1 769  LEU 769  340  340  LEU LEU A . n 
A 1 770  LYS 770  341  341  LYS LYS A . n 
A 1 771  PRO 771  342  342  PRO PRO A . n 
A 1 772  SER 772  343  343  SER SER A . n 
A 1 773  GLN 773  344  344  GLN GLN A . n 
A 1 774  ALA 774  345  345  ALA ALA A . n 
A 1 775  GLN 775  346  346  GLN GLN A . n 
A 1 776  LYS 776  347  347  LYS LYS A . n 
A 1 777  ILE 777  348  348  ILE ILE A . n 
A 1 778  ARG 778  349  349  ARG ARG A . n 
A 1 779  GLU 779  350  350  GLU GLU A . n 
A 1 780  PHE 780  351  351  PHE PHE A . n 
A 1 781  HIS 781  352  352  HIS HIS A . n 
A 1 782  ARG 782  353  353  ARG ARG A . n 
A 1 783  THR 783  354  354  THR THR A . n 
A 1 784  LEU 784  355  355  LEU LEU A . n 
A 1 785  ILE 785  356  356  ILE ILE A . n 
A 1 786  ARG 786  357  357  ARG ARG A . n 
A 1 787  LEU 787  358  358  LEU LEU A . n 
A 1 788  GLU 788  359  359  GLU GLU A . n 
A 1 789  MET 789  360  360  MET MET A . n 
A 1 790  THR 790  361  361  THR THR A . n 
A 1 791  PRO 791  362  362  PRO PRO A . n 
A 1 792  GLN 792  363  363  GLN GLN A . n 
A 1 793  GLN 793  364  364  GLN GLN A . n 
A 1 794  LEU 794  365  365  LEU LEU A . n 
A 1 795  CYS 795  366  366  CYS CYS A . n 
A 1 796  GLU 796  367  367  GLU GLU A . n 
A 1 797  LEU 797  368  368  LEU LEU A . n 
A 1 798  PHE 798  369  369  PHE PHE A . n 
A 1 799  SER 799  370  370  SER SER A . n 
A 1 800  ILE 800  371  371  ILE ILE A . n 
A 1 801  GLN 801  372  372  GLN GLN A . n 
A 1 802  LYS 802  373  373  LYS LYS A . n 
A 1 803  HIS 803  374  374  HIS HIS A . n 
A 1 804  TRP 804  375  375  TRP TRP A . n 
A 1 805  GLY 805  376  376  GLY GLY A . n 
A 1 806  HIS 806  377  377  HIS HIS A . n 
A 1 807  PRO 807  378  378  PRO PRO A . n 
A 1 808  VAL 808  379  379  VAL VAL A . n 
A 1 809  LEU 809  380  380  LEU LEU A . n 
A 1 810  HIS 810  381  381  HIS HIS A . n 
A 1 811  SER 811  382  382  SER SER A . n 
A 1 812  GLU 812  383  383  GLU GLU A . n 
A 1 813  THR 813  384  384  THR THR A . n 
A 1 814  ALA 814  385  385  ALA ALA A . n 
A 1 815  ILE 815  386  386  ILE ILE A . n 
A 1 816  GLN 816  387  387  GLN GLN A . n 
A 1 817  LYS 817  388  388  LYS LYS A . n 
A 1 818  VAL 818  389  389  VAL VAL A . n 
A 1 819  LYS 819  390  390  LYS LYS A . n 
A 1 820  LYS 820  391  391  LYS LYS A . n 
A 1 821  HIS 821  392  392  HIS HIS A . n 
A 1 822  ALA 822  393  393  ALA ALA A . n 
A 1 823  THR 823  394  394  THR THR A . n 
A 1 824  VAL 824  395  395  VAL VAL A . n 
A 1 825  LEU 825  396  396  LEU LEU A . n 
A 1 826  LYS 826  397  397  LYS LYS A . n 
A 1 827  ALA 827  398  398  ALA ALA A . n 
A 1 828  LEU 828  399  399  LEU LEU A . n 
A 1 829  ARG 829  400  400  ARG ARG A . n 
A 1 830  PRO 830  401  401  PRO PRO A . n 
A 1 831  ILE 831  402  402  ILE ILE A . n 
A 1 832  VAL 832  403  403  VAL VAL A . n 
A 1 833  ILE 833  404  404  ILE ILE A . n 
A 1 834  PHE 834  405  405  PHE PHE A . n 
A 1 835  GLU 835  406  406  GLU GLU A . n 
A 1 836  THR 836  407  407  THR THR A . n 
A 1 837  TYR 837  408  408  TYR TYR A . n 
A 1 838  CYS 838  409  409  CYS CYS A . n 
A 1 839  VAL 839  410  410  VAL VAL A . n 
A 1 840  PHE 840  411  411  PHE PHE A . n 
A 1 841  LYS 841  412  412  LYS LYS A . n 
A 1 842  TYR 842  413  413  TYR TYR A . n 
A 1 843  SER 843  414  414  SER SER A . n 
A 1 844  ILE 844  415  415  ILE ILE A . n 
A 1 845  ALA 845  416  416  ALA ALA A . n 
A 1 846  LYS 846  417  417  LYS LYS A . n 
A 1 847  HIS 847  418  418  HIS HIS A . n 
A 1 848  TYR 848  419  419  TYR TYR A . n 
A 1 849  PHE 849  420  420  PHE PHE A . n 
A 1 850  ASP 850  421  421  ASP ASP A . n 
A 1 851  SER 851  422  422  SER SER A . n 
A 1 852  GLN 852  423  423  GLN GLN A . n 
A 1 853  GLY 853  424  424  GLY GLY A . n 
A 1 854  SER 854  425  425  SER SER A . n 
A 1 855  TRP 855  426  426  TRP TRP A . n 
A 1 856  TYR 856  427  427  TYR TYR A . n 
A 1 857  SER 857  428  428  SER SER A . n 
A 1 858  VAL 858  429  429  VAL VAL A . n 
A 1 859  THR 859  430  430  THR THR A . n 
A 1 860  SER 860  431  431  SER SER A . n 
A 1 861  ASP 861  432  432  ASP ASP A . n 
A 1 862  ARG 862  433  433  ARG ARG A . n 
A 1 863  ASN 863  434  434  ASN ASN A . n 
A 1 864  LEU 864  435  435  LEU LEU A . n 
A 1 865  THR 865  436  436  THR THR A . n 
A 1 866  PRO 866  437  437  PRO PRO A . n 
A 1 867  GLY 867  438  438  GLY GLY A . n 
A 1 868  LEU 868  439  439  LEU LEU A . n 
A 1 869  ASN 869  440  440  ASN ASN A . n 
A 1 870  SER 870  441  441  SER SER A . n 
A 1 871  TYR 871  442  442  TYR TYR A . n 
A 1 872  ILE 872  443  443  ILE ILE A . n 
A 1 873  LYS 873  444  444  LYS LYS A . n 
A 1 874  ARG 874  445  445  ARG ARG A . n 
A 1 875  ASN 875  446  446  ASN ASN A . n 
A 1 876  GLN 876  447  447  GLN GLN A . n 
A 1 877  PHE 877  448  448  PHE PHE A . n 
A 1 878  PRO 878  449  449  PRO PRO A . n 
A 1 879  PRO 879  450  450  PRO PRO A . n 
A 1 880  LEU 880  451  451  LEU LEU A . n 
A 1 881  PRO 881  452  452  PRO PRO A . n 
A 1 882  MET 882  453  453  MET MET A . n 
A 1 883  ILE 883  454  454  ILE ILE A . n 
A 1 884  LYS 884  455  455  LYS LYS A . n 
A 1 885  GLU 885  456  456  GLU GLU A . n 
A 1 886  LEU 886  457  457  LEU LEU A . n 
A 1 887  LEU 887  458  458  LEU LEU A . n 
A 1 888  TRP 888  459  459  TRP TRP A . n 
A 1 889  GLU 889  460  460  GLU GLU A . n 
A 1 890  PHE 890  461  461  PHE PHE A . n 
A 1 891  TYR 891  462  462  TYR TYR A . n 
A 1 892  HIS 892  463  463  HIS HIS A . n 
A 1 893  LEU 893  464  464  LEU LEU A . n 
A 1 894  ASP 894  465  465  ASP ASP A . n 
A 1 895  HIS 895  466  466  HIS HIS A . n 
A 1 896  PRO 896  467  467  PRO PRO A . n 
A 1 897  PRO 897  468  468  PRO PRO A . n 
A 1 898  LEU 898  469  469  LEU LEU A . n 
A 1 899  PHE 899  470  470  PHE PHE A . n 
A 1 900  SER 900  471  471  SER SER A . n 
A 1 901  THR 901  472  472  THR THR A . n 
A 1 902  LYS 902  473  473  LYS LYS A . n 
A 1 903  ILE 903  474  474  ILE ILE A . n 
A 1 904  ILE 904  475  475  ILE ILE A . n 
A 1 905  SER 905  476  476  SER SER A . n 
A 1 906  ASP 906  477  477  ASP ASP A . n 
A 1 907  LEU 907  478  478  LEU LEU A . n 
A 1 908  SER 908  479  479  SER SER A . n 
A 1 909  ILE 909  480  480  ILE ILE A . n 
A 1 910  PHE 910  481  481  PHE PHE A . n 
A 1 911  ILE 911  482  482  ILE ILE A . n 
A 1 912  LYS 912  483  483  LYS LYS A . n 
A 1 913  ASP 913  484  484  ASP ASP A . n 
A 1 914  ARG 914  485  485  ARG ARG A . n 
A 1 915  ALA 915  486  486  ALA ALA A . n 
A 1 916  THR 916  487  487  THR THR A . n 
A 1 917  ALA 917  488  488  ALA ALA A . n 
A 1 918  VAL 918  489  489  VAL VAL A . n 
A 1 919  GLU 919  490  490  GLU GLU A . n 
A 1 920  ARG 920  491  491  ARG ARG A . n 
A 1 921  THR 921  492  492  THR THR A . n 
A 1 922  CYS 922  493  493  CYS CYS A . n 
A 1 923  TRP 923  494  494  TRP TRP A . n 
A 1 924  ASP 924  495  495  ASP ASP A . n 
A 1 925  ALA 925  496  496  ALA ALA A . n 
A 1 926  VAL 926  497  497  VAL VAL A . n 
A 1 927  PHE 927  498  498  PHE PHE A . n 
A 1 928  GLU 928  499  499  GLU GLU A . n 
A 1 929  PRO 929  500  500  PRO PRO A . n 
A 1 930  ASN 930  501  501  ASN ASN A . n 
A 1 931  VAL 931  502  502  VAL VAL A . n 
A 1 932  LEU 932  503  503  LEU LEU A . n 
A 1 933  GLY 933  504  504  GLY GLY A . n 
A 1 934  TYR 934  505  505  TYR TYR A . n 
A 1 935  ASN 935  506  506  ASN ASN A . n 
A 1 936  PRO 936  507  507  PRO PRO A . n 
A 1 937  PRO 937  508  508  PRO PRO A . n 
A 1 938  HIS 938  509  509  HIS HIS A . n 
A 1 939  LYS 939  510  510  LYS LYS A . n 
A 1 940  PHE 940  511  511  PHE PHE A . n 
A 1 941  SER 941  512  512  SER SER A . n 
A 1 942  THR 942  513  513  THR THR A . n 
A 1 943  LYS 943  514  514  LYS LYS A . n 
A 1 944  ARG 944  515  515  ARG ARG A . n 
A 1 945  VAL 945  516  516  VAL VAL A . n 
A 1 946  PRO 946  517  517  PRO PRO A . n 
A 1 947  GLU 947  518  518  GLU GLU A . n 
A 1 948  GLN 948  519  519  GLN GLN A . n 
A 1 949  PHE 949  520  520  PHE PHE A . n 
A 1 950  LEU 950  521  521  LEU LEU A . n 
A 1 951  GLU 951  522  522  GLU GLU A . n 
A 1 952  GLN 952  523  523  GLN GLN A . n 
A 1 953  GLU 953  524  524  GLU GLU A . n 
A 1 954  ASN 954  525  525  ASN ASN A . n 
A 1 955  PHE 955  526  526  PHE PHE A . n 
A 1 956  SER 956  527  527  SER SER A . n 
A 1 957  ILE 957  528  528  ILE ILE A . n 
A 1 958  GLU 958  529  529  GLU GLU A . n 
A 1 959  ASN 959  530  530  ASN ASN A . n 
A 1 960  VAL 960  531  531  VAL VAL A . n 
A 1 961  LEU 961  532  532  LEU LEU A . n 
A 1 962  SER 962  533  533  SER SER A . n 
A 1 963  TYR 963  534  534  TYR TYR A . n 
A 1 964  ALA 964  535  535  ALA ALA A . n 
A 1 965  GLN 965  536  536  GLN GLN A . n 
A 1 966  LYS 966  537  537  LYS LYS A . n 
A 1 967  LEU 967  538  538  LEU LEU A . n 
A 1 968  GLU 968  539  539  GLU GLU A . n 
A 1 969  TYR 969  540  540  TYR TYR A . n 
A 1 970  LEU 970  541  541  LEU LEU A . n 
A 1 971  LEU 971  542  542  LEU LEU A . n 
A 1 972  PRO 972  543  543  PRO PRO A . n 
A 1 973  GLN 973  544  544  GLN GLN A . n 
A 1 974  TYR 974  545  545  TYR TYR A . n 
A 1 975  ARG 975  546  546  ARG ARG A . n 
A 1 976  ASN 976  547  547  ASN ASN A . n 
A 1 977  PHE 977  548  548  PHE PHE A . n 
A 1 978  SER 978  549  549  SER SER A . n 
A 1 979  PHE 979  550  550  PHE PHE A . n 
A 1 980  SER 980  551  551  SER SER A . n 
A 1 981  LEU 981  552  552  LEU LEU A . n 
A 1 982  LYS 982  553  553  LYS LYS A . n 
A 1 983  GLU 983  554  554  GLU GLU A . n 
A 1 984  LYS 984  555  555  LYS LYS A . n 
A 1 985  GLU 985  556  556  GLU GLU A . n 
A 1 986  LEU 986  557  557  LEU LEU A . n 
A 1 987  ASN 987  558  558  ASN ASN A . n 
A 1 988  VAL 988  559  559  VAL VAL A . n 
A 1 989  GLY 989  560  560  GLY GLY A . n 
A 1 990  ARG 990  561  561  ARG ARG A . n 
A 1 991  THR 991  562  562  THR THR A . n 
A 1 992  PHE 992  563  563  PHE PHE A . n 
A 1 993  GLY 993  564  564  GLY GLY A . n 
A 1 994  LYS 994  565  565  LYS LYS A . n 
A 1 995  LEU 995  566  566  LEU LEU A . n 
A 1 996  PRO 996  567  567  PRO PRO A . n 
A 1 997  TYR 997  568  568  TYR TYR A . n 
A 1 998  PRO 998  569  569  PRO PRO A . n 
A 1 999  THR 999  570  570  THR THR A . n 
A 1 1000 ARG 1000 571  571  ARG ARG A . n 
A 1 1001 ASN 1001 572  572  ASN ASN A . n 
A 1 1002 VAL 1002 573  573  VAL VAL A . n 
A 1 1003 GLN 1003 574  574  GLN GLN A . n 
A 1 1004 THR 1004 575  575  THR THR A . n 
A 1 1005 LEU 1005 576  576  LEU LEU A . n 
A 1 1006 CYS 1006 577  577  CYS CYS A . n 
A 1 1007 GLU 1007 578  578  GLU GLU A . n 
A 1 1008 ALA 1008 579  579  ALA ALA A . n 
A 1 1009 LEU 1009 580  580  LEU LEU A . n 
A 1 1010 LEU 1010 581  581  LEU LEU A . n 
A 1 1011 ALA 1011 582  582  ALA ALA A . n 
A 1 1012 ASP 1012 583  583  ASP ASP A . n 
A 1 1013 GLY 1013 584  584  GLY GLY A . n 
A 1 1014 LEU 1014 585  585  LEU LEU A . n 
A 1 1015 ALA 1015 586  586  ALA ALA A . n 
A 1 1016 LYS 1016 587  587  LYS LYS A . n 
A 1 1017 ALA 1017 588  588  ALA ALA A . n 
A 1 1018 PHE 1018 589  589  PHE PHE A . n 
A 1 1019 PRO 1019 590  590  PRO PRO A . n 
A 1 1020 SER 1020 591  591  SER SER A . n 
A 1 1021 ASN 1021 592  592  ASN ASN A . n 
A 1 1022 MET 1022 593  593  MET MET A . n 
A 1 1023 MET 1023 594  594  MET MET A . n 
A 1 1024 VAL 1024 595  595  VAL VAL A . n 
A 1 1025 VAL 1025 596  596  VAL VAL A . n 
A 1 1026 THR 1026 597  597  THR THR A . n 
A 1 1027 GLU 1027 598  598  GLU GLU A . n 
A 1 1028 ARG 1028 599  599  ARG ARG A . n 
A 1 1029 GLU 1029 600  600  GLU GLU A . n 
A 1 1030 GLN 1030 601  601  GLN GLN A . n 
A 1 1031 LYS 1031 602  602  LYS LYS A . n 
A 1 1032 GLU 1032 603  603  GLU GLU A . n 
A 1 1033 SER 1033 604  604  SER SER A . n 
A 1 1034 LEU 1034 605  605  LEU LEU A . n 
A 1 1035 LEU 1035 606  606  LEU LEU A . n 
A 1 1036 HIS 1036 607  607  HIS HIS A . n 
A 1 1037 GLN 1037 608  608  GLN GLN A . n 
A 1 1038 ALA 1038 609  609  ALA ALA A . n 
A 1 1039 SER 1039 610  610  SER SER A . n 
A 1 1040 TRP 1040 611  611  TRP TRP A . n 
A 1 1041 HIS 1041 612  ?    ?   ?   A . n 
A 1 1042 HIS 1042 613  ?    ?   ?   A . n 
A 1 1043 THR 1043 614  ?    ?   ?   A . n 
A 1 1044 SER 1044 615  ?    ?   ?   A . n 
A 1 1045 ASP 1045 616  ?    ?   ?   A . n 
A 1 1046 ASP 1046 617  ?    ?   ?   A . n 
A 1 1047 PHE 1047 618  ?    ?   ?   A . n 
A 1 1048 GLY 1048 619  ?    ?   ?   A . n 
A 1 1049 GLU 1049 620  ?    ?   ?   A . n 
A 1 1050 HIS 1050 621  ?    ?   ?   A . n 
A 1 1051 ALA 1051 622  622  ALA ALA A . n 
A 1 1052 THR 1052 623  623  THR THR A . n 
A 1 1053 VAL 1053 624  624  VAL VAL A . n 
A 1 1054 ARG 1054 625  625  ARG ARG A . n 
A 1 1055 GLY 1055 626  626  GLY GLY A . n 
A 1 1056 SER 1056 627  627  SER SER A . n 
A 1 1057 SER 1057 628  628  SER SER A . n 
A 1 1058 PHE 1058 629  629  PHE PHE A . n 
A 1 1059 VAL 1059 630  630  VAL VAL A . n 
A 1 1060 THR 1060 631  631  THR THR A . n 
A 1 1061 ASP 1061 632  632  ASP ASP A . n 
A 1 1062 LEU 1062 633  633  LEU LEU A . n 
A 1 1063 GLU 1063 634  634  GLU GLU A . n 
A 1 1064 LYS 1064 635  635  LYS LYS A . n 
A 1 1065 TYR 1065 636  636  TYR TYR A . n 
A 1 1066 ASN 1066 637  637  ASN ASN A . n 
A 1 1067 LEU 1067 638  638  LEU LEU A . n 
A 1 1068 ALA 1068 639  639  ALA ALA A . n 
A 1 1069 PHE 1069 640  640  PHE PHE A . n 
A 1 1070 ARG 1070 641  641  ARG ARG A . n 
A 1 1071 TYR 1071 642  642  TYR TYR A . n 
A 1 1072 GLU 1072 643  643  GLU GLU A . n 
A 1 1073 PHE 1073 644  644  PHE PHE A . n 
A 1 1074 THR 1074 645  645  THR THR A . n 
A 1 1075 ALA 1075 646  646  ALA ALA A . n 
A 1 1076 PRO 1076 647  647  PRO PRO A . n 
A 1 1077 PHE 1077 648  648  PHE PHE A . n 
A 1 1078 ILE 1078 649  649  ILE ILE A . n 
A 1 1079 GLU 1079 650  650  GLU GLU A . n 
A 1 1080 TYR 1080 651  651  TYR TYR A . n 
A 1 1081 CYS 1081 652  652  CYS CYS A . n 
A 1 1082 ASN 1082 653  653  ASN ASN A . n 
A 1 1083 ARG 1083 654  654  ARG ARG A . n 
A 1 1084 CYS 1084 655  655  CYS CYS A . n 
A 1 1085 TYR 1085 656  656  TYR TYR A . n 
A 1 1086 GLY 1086 657  657  GLY GLY A . n 
A 1 1087 VAL 1087 658  658  VAL VAL A . n 
A 1 1088 LYS 1088 659  659  LYS LYS A . n 
A 1 1089 ASN 1089 660  660  ASN ASN A . n 
A 1 1090 VAL 1090 661  661  VAL VAL A . n 
A 1 1091 PHE 1091 662  662  PHE PHE A . n 
A 1 1092 ASN 1092 663  663  ASN ASN A . n 
A 1 1093 TRP 1093 664  664  TRP TRP A . n 
A 1 1094 MET 1094 665  665  MET MET A . n 
A 1 1095 HIS 1095 666  666  HIS HIS A . n 
A 1 1096 TYR 1096 667  667  TYR TYR A . n 
A 1 1097 THR 1097 668  668  THR THR A . n 
A 1 1098 ILE 1098 669  669  ILE ILE A . n 
A 1 1099 PRO 1099 670  670  PRO PRO A . n 
A 1 1100 GLN 1100 671  671  GLN GLN A . n 
A 1 1101 CYS 1101 672  672  CYS CYS A . n 
A 1 1102 TYR 1102 673  673  TYR TYR A . n 
A 1 1103 MET 1103 674  674  MET MET A . n 
A 1 1104 HIS 1104 675  675  HIS HIS A . n 
A 1 1105 VAL 1105 676  676  VAL VAL A . n 
A 1 1106 SER 1106 677  677  SER SER A . n 
A 1 1107 ASP 1107 678  678  ASP ASP A . n 
A 1 1108 TYR 1108 679  679  TYR TYR A . n 
A 1 1109 TYR 1109 680  680  TYR TYR A . n 
A 1 1110 ASN 1110 681  681  ASN ASN A . n 
A 1 1111 PRO 1111 682  682  PRO PRO A . n 
A 1 1112 PRO 1112 683  683  PRO PRO A . n 
A 1 1113 HIS 1113 684  684  HIS HIS A . n 
A 1 1114 ASN 1114 685  685  ASN ASN A . n 
A 1 1115 LEU 1115 686  686  LEU LEU A . n 
A 1 1116 THR 1116 687  687  THR THR A . n 
A 1 1117 LEU 1117 688  688  LEU LEU A . n 
A 1 1118 GLU 1118 689  689  GLU GLU A . n 
A 1 1119 ASN 1119 690  690  ASN ASN A . n 
A 1 1120 ARG 1120 691  691  ARG ARG A . n 
A 1 1121 ASP 1121 692  692  ASP ASP A . n 
A 1 1122 ASN 1122 693  693  ASN ASN A . n 
A 1 1123 PRO 1123 694  694  PRO PRO A . n 
A 1 1124 PRO 1124 695  695  PRO PRO A . n 
A 1 1125 GLU 1125 696  696  GLU GLU A . n 
A 1 1126 GLY 1126 697  697  GLY GLY A . n 
A 1 1127 PRO 1127 698  698  PRO PRO A . n 
A 1 1128 SER 1128 699  699  SER SER A . n 
A 1 1129 SER 1129 700  700  SER SER A . n 
A 1 1130 TYR 1130 701  701  TYR TYR A . n 
A 1 1131 ARG 1131 702  702  ARG ARG A . n 
A 1 1132 GLY 1132 703  703  GLY GLY A . n 
A 1 1133 HIS 1133 704  704  HIS HIS A . n 
A 1 1134 MET 1134 705  705  MET MET A . n 
A 1 1135 GLY 1135 706  706  GLY GLY A . n 
A 1 1136 GLY 1136 707  707  GLY GLY A . n 
A 1 1137 ILE 1137 708  708  ILE ILE A . n 
A 1 1138 GLU 1138 709  709  GLU GLU A . n 
A 1 1139 GLY 1139 710  710  GLY GLY A . n 
A 1 1140 LEU 1140 711  711  LEU LEU A . n 
A 1 1141 GLN 1141 712  712  GLN GLN A . n 
A 1 1142 GLN 1142 713  713  GLN GLN A . n 
A 1 1143 LYS 1143 714  714  LYS LYS A . n 
A 1 1144 LEU 1144 715  715  LEU LEU A . n 
A 1 1145 TRP 1145 716  716  TRP TRP A . n 
A 1 1146 THR 1146 717  717  THR THR A . n 
A 1 1147 SER 1147 718  718  SER SER A . n 
A 1 1148 ILE 1148 719  719  ILE ILE A . n 
A 1 1149 SER 1149 720  720  SER SER A . n 
A 1 1150 CYS 1150 721  721  CYS CYS A . n 
A 1 1151 ALA 1151 722  722  ALA ALA A . n 
A 1 1152 GLN 1152 723  723  GLN GLN A . n 
A 1 1153 ILE 1153 724  724  ILE ILE A . n 
A 1 1154 SER 1154 725  725  SER SER A . n 
A 1 1155 LEU 1155 726  726  LEU LEU A . n 
A 1 1156 VAL 1156 727  727  VAL VAL A . n 
A 1 1157 GLU 1157 728  728  GLU GLU A . n 
A 1 1158 ILE 1158 729  729  ILE ILE A . n 
A 1 1159 LYS 1159 730  730  LYS LYS A . n 
A 1 1160 THR 1160 731  731  THR THR A . n 
A 1 1161 GLY 1161 732  732  GLY GLY A . n 
A 1 1162 PHE 1162 733  733  PHE PHE A . n 
A 1 1163 LYS 1163 734  734  LYS LYS A . n 
A 1 1164 LEU 1164 735  735  LEU LEU A . n 
A 1 1165 ARG 1165 736  736  ARG ARG A . n 
A 1 1166 SER 1166 737  737  SER SER A . n 
A 1 1167 ALA 1167 738  738  ALA ALA A . n 
A 1 1168 VAL 1168 739  739  VAL VAL A . n 
A 1 1169 MET 1169 740  740  MET MET A . n 
A 1 1170 GLY 1170 741  741  GLY GLY A . n 
A 1 1171 ASP 1171 742  742  ASP ASP A . n 
A 1 1172 ASN 1172 743  743  ASN ASN A . n 
A 1 1173 GLN 1173 744  744  GLN GLN A . n 
A 1 1174 CYS 1174 745  745  CYS CYS A . n 
A 1 1175 ILE 1175 746  746  ILE ILE A . n 
A 1 1176 THR 1176 747  747  THR THR A . n 
A 1 1177 VAL 1177 748  748  VAL VAL A . n 
A 1 1178 LEU 1178 749  749  LEU LEU A . n 
A 1 1179 SER 1179 750  750  SER SER A . n 
A 1 1180 VAL 1180 751  751  VAL VAL A . n 
A 1 1181 PHE 1181 752  752  PHE PHE A . n 
A 1 1182 PRO 1182 753  753  PRO PRO A . n 
A 1 1183 LEU 1183 754  754  LEU LEU A . n 
A 1 1184 GLU 1184 755  755  GLU GLU A . n 
A 1 1185 THR 1185 756  756  THR THR A . n 
A 1 1186 ASP 1186 757  757  ASP ASP A . n 
A 1 1187 ALA 1187 758  758  ALA ALA A . n 
A 1 1188 ASP 1188 759  759  ASP ASP A . n 
A 1 1189 GLU 1189 760  760  GLU GLU A . n 
A 1 1190 GLN 1190 761  761  GLN GLN A . n 
A 1 1191 GLU 1191 762  762  GLU GLU A . n 
A 1 1192 GLN 1192 763  763  GLN GLN A . n 
A 1 1193 SER 1193 764  764  SER SER A . n 
A 1 1194 ALA 1194 765  765  ALA ALA A . n 
A 1 1195 GLU 1195 766  766  GLU GLU A . n 
A 1 1196 ASP 1196 767  767  ASP ASP A . n 
A 1 1197 ASN 1197 768  768  ASN ASN A . n 
A 1 1198 ALA 1198 769  769  ALA ALA A . n 
A 1 1199 ALA 1199 770  770  ALA ALA A . n 
A 1 1200 ARG 1200 771  771  ARG ARG A . n 
A 1 1201 VAL 1201 772  772  VAL VAL A . n 
A 1 1202 ALA 1202 773  773  ALA ALA A . n 
A 1 1203 ALA 1203 774  774  ALA ALA A . n 
A 1 1204 SER 1204 775  775  SER SER A . n 
A 1 1205 LEU 1205 776  776  LEU LEU A . n 
A 1 1206 ALA 1206 777  777  ALA ALA A . n 
A 1 1207 LYS 1207 778  778  LYS LYS A . n 
A 1 1208 VAL 1208 779  779  VAL VAL A . n 
A 1 1209 THR 1209 780  780  THR THR A . n 
A 1 1210 SER 1210 781  781  SER SER A . n 
A 1 1211 ALA 1211 782  782  ALA ALA A . n 
A 1 1212 CYS 1212 783  783  CYS CYS A . n 
A 1 1213 GLY 1213 784  784  GLY GLY A . n 
A 1 1214 ILE 1214 785  785  ILE ILE A . n 
A 1 1215 PHE 1215 786  786  PHE PHE A . n 
A 1 1216 LEU 1216 787  787  LEU LEU A . n 
A 1 1217 LYS 1217 788  788  LYS LYS A . n 
A 1 1218 PRO 1218 789  789  PRO PRO A . n 
A 1 1219 ASP 1219 790  790  ASP ASP A . n 
A 1 1220 GLU 1220 791  791  GLU GLU A . n 
A 1 1221 THR 1221 792  792  THR THR A . n 
A 1 1222 PHE 1222 793  793  PHE PHE A . n 
A 1 1223 VAL 1223 794  794  VAL VAL A . n 
A 1 1224 HIS 1224 795  795  HIS HIS A . n 
A 1 1225 SER 1225 796  796  SER SER A . n 
A 1 1226 GLY 1226 797  797  GLY GLY A . n 
A 1 1227 PHE 1227 798  798  PHE PHE A . n 
A 1 1228 ILE 1228 799  799  ILE ILE A . n 
A 1 1229 TYR 1229 800  800  TYR TYR A . n 
A 1 1230 PHE 1230 801  801  PHE PHE A . n 
A 1 1231 GLY 1231 802  802  GLY GLY A . n 
A 1 1232 LYS 1232 803  803  LYS LYS A . n 
A 1 1233 LYS 1233 804  804  LYS LYS A . n 
A 1 1234 GLN 1234 805  805  GLN GLN A . n 
A 1 1235 TYR 1235 806  806  TYR TYR A . n 
A 1 1236 LEU 1236 807  807  LEU LEU A . n 
A 1 1237 ASN 1237 808  808  ASN ASN A . n 
A 1 1238 GLY 1238 809  809  GLY GLY A . n 
A 1 1239 VAL 1239 810  810  VAL VAL A . n 
A 1 1240 GLN 1240 811  811  GLN GLN A . n 
A 1 1241 LEU 1241 812  812  LEU LEU A . n 
A 1 1242 PRO 1242 813  813  PRO PRO A . n 
A 1 1243 GLN 1243 814  814  GLN GLN A . n 
A 1 1244 SER 1244 815  815  SER SER A . n 
A 1 1245 LEU 1245 816  816  LEU LEU A . n 
A 1 1246 LYS 1246 817  817  LYS LYS A . n 
A 1 1247 THR 1247 818  818  THR THR A . n 
A 1 1248 ALA 1248 819  819  ALA ALA A . n 
A 1 1249 THR 1249 820  820  THR THR A . n 
A 1 1250 ARG 1250 821  821  ARG ARG A . n 
A 1 1251 MET 1251 822  822  MET MET A . n 
A 1 1252 ALA 1252 823  823  ALA ALA A . n 
A 1 1253 PRO 1253 824  824  PRO PRO A . n 
A 1 1254 LEU 1254 825  825  LEU LEU A . n 
A 1 1255 SER 1255 826  826  SER SER A . n 
A 1 1256 ASP 1256 827  827  ASP ASP A . n 
A 1 1257 ALA 1257 828  828  ALA ALA A . n 
A 1 1258 ILE 1258 829  829  ILE ILE A . n 
A 1 1259 PHE 1259 830  830  PHE PHE A . n 
A 1 1260 ASP 1260 831  831  ASP ASP A . n 
A 1 1261 ASP 1261 832  832  ASP ASP A . n 
A 1 1262 LEU 1262 833  833  LEU LEU A . n 
A 1 1263 GLN 1263 834  834  GLN GLN A . n 
A 1 1264 GLY 1264 835  835  GLY GLY A . n 
A 1 1265 THR 1265 836  836  THR THR A . n 
A 1 1266 LEU 1266 837  837  LEU LEU A . n 
A 1 1267 ALA 1267 838  838  ALA ALA A . n 
A 1 1268 SER 1268 839  839  SER SER A . n 
A 1 1269 ILE 1269 840  840  ILE ILE A . n 
A 1 1270 GLY 1270 841  841  GLY GLY A . n 
A 1 1271 THR 1271 842  842  THR THR A . n 
A 1 1272 ALA 1272 843  843  ALA ALA A . n 
A 1 1273 PHE 1273 844  844  PHE PHE A . n 
A 1 1274 GLU 1274 845  845  GLU GLU A . n 
A 1 1275 ARG 1275 846  846  ARG ARG A . n 
A 1 1276 SER 1276 847  847  SER SER A . n 
A 1 1277 ILE 1277 848  848  ILE ILE A . n 
A 1 1278 SER 1278 849  849  SER SER A . n 
A 1 1279 GLU 1279 850  850  GLU GLU A . n 
A 1 1280 THR 1280 851  851  THR THR A . n 
A 1 1281 ARG 1281 852  852  ARG ARG A . n 
A 1 1282 HIS 1282 853  853  HIS HIS A . n 
A 1 1283 ILE 1283 854  854  ILE ILE A . n 
A 1 1284 PHE 1284 855  855  PHE PHE A . n 
A 1 1285 PRO 1285 856  856  PRO PRO A . n 
A 1 1286 CYS 1286 857  857  CYS CYS A . n 
A 1 1287 ARG 1287 858  858  ARG ARG A . n 
A 1 1288 ILE 1288 859  859  ILE ILE A . n 
A 1 1289 THR 1289 860  860  THR THR A . n 
A 1 1290 ALA 1290 861  861  ALA ALA A . n 
A 1 1291 ALA 1291 862  862  ALA ALA A . n 
A 1 1292 PHE 1292 863  863  PHE PHE A . n 
A 1 1293 HIS 1293 864  864  HIS HIS A . n 
A 1 1294 THR 1294 865  865  THR THR A . n 
A 1 1295 PHE 1295 866  866  PHE PHE A . n 
A 1 1296 PHE 1296 867  867  PHE PHE A . n 
A 1 1297 SER 1297 868  868  SER SER A . n 
A 1 1298 VAL 1298 869  869  VAL VAL A . n 
A 1 1299 ARG 1299 870  870  ARG ARG A . n 
A 1 1300 ILE 1300 871  871  ILE ILE A . n 
A 1 1301 LEU 1301 872  872  LEU LEU A . n 
A 1 1302 GLN 1302 873  873  GLN GLN A . n 
A 1 1303 TYR 1303 874  874  TYR TYR A . n 
A 1 1304 HIS 1304 875  875  HIS HIS A . n 
A 1 1305 HIS 1305 876  876  HIS HIS A . n 
A 1 1306 LEU 1306 877  877  LEU LEU A . n 
A 1 1307 GLY 1307 878  878  GLY GLY A . n 
A 1 1308 PHE 1308 879  879  PHE PHE A . n 
A 1 1309 ASN 1309 880  880  ASN ASN A . n 
A 1 1310 LYS 1310 881  881  LYS LYS A . n 
A 1 1311 GLY 1311 882  882  GLY GLY A . n 
A 1 1312 PHE 1312 883  883  PHE PHE A . n 
A 1 1313 ASP 1313 884  884  ASP ASP A . n 
A 1 1314 LEU 1314 885  885  LEU LEU A . n 
A 1 1315 GLY 1315 886  886  GLY GLY A . n 
A 1 1316 GLN 1316 887  887  GLN GLN A . n 
A 1 1317 LEU 1317 888  888  LEU LEU A . n 
A 1 1318 THR 1318 889  889  THR THR A . n 
A 1 1319 LEU 1319 890  890  LEU LEU A . n 
A 1 1320 GLY 1320 891  891  GLY GLY A . n 
A 1 1321 LYS 1321 892  892  LYS LYS A . n 
A 1 1322 PRO 1322 893  893  PRO PRO A . n 
A 1 1323 LEU 1323 894  894  LEU LEU A . n 
A 1 1324 ASP 1324 895  895  ASP ASP A . n 
A 1 1325 PHE 1325 896  896  PHE PHE A . n 
A 1 1326 GLY 1326 897  897  GLY GLY A . n 
A 1 1327 THR 1327 898  898  THR THR A . n 
A 1 1328 ILE 1328 899  899  ILE ILE A . n 
A 1 1329 SER 1329 900  900  SER SER A . n 
A 1 1330 LEU 1330 901  901  LEU LEU A . n 
A 1 1331 ALA 1331 902  902  ALA ALA A . n 
A 1 1332 LEU 1332 903  903  LEU LEU A . n 
A 1 1333 ALA 1333 904  904  ALA ALA A . n 
A 1 1334 VAL 1334 905  905  VAL VAL A . n 
A 1 1335 PRO 1335 906  906  PRO PRO A . n 
A 1 1336 GLN 1336 907  907  GLN GLN A . n 
A 1 1337 VAL 1337 908  908  VAL VAL A . n 
A 1 1338 LEU 1338 909  909  LEU LEU A . n 
A 1 1339 GLY 1339 910  910  GLY GLY A . n 
A 1 1340 GLY 1340 911  911  GLY GLY A . n 
A 1 1341 LEU 1341 912  912  LEU LEU A . n 
A 1 1342 SER 1342 913  913  SER SER A . n 
A 1 1343 PHE 1343 914  914  PHE PHE A . n 
A 1 1344 LEU 1344 915  915  LEU LEU A . n 
A 1 1345 ASN 1345 916  916  ASN ASN A . n 
A 1 1346 PRO 1346 917  917  PRO PRO A . n 
A 1 1347 GLU 1347 918  918  GLU GLU A . n 
A 1 1348 LYS 1348 919  919  LYS LYS A . n 
A 1 1349 CYS 1349 920  920  CYS CYS A . n 
A 1 1350 PHE 1350 921  921  PHE PHE A . n 
A 1 1351 TYR 1351 922  922  TYR TYR A . n 
A 1 1352 ARG 1352 923  923  ARG ARG A . n 
A 1 1353 ASN 1353 924  924  ASN ASN A . n 
A 1 1354 LEU 1354 925  925  LEU LEU A . n 
A 1 1355 GLY 1355 926  926  GLY GLY A . n 
A 1 1356 ASP 1356 927  927  ASP ASP A . n 
A 1 1357 PRO 1357 928  928  PRO PRO A . n 
A 1 1358 VAL 1358 929  929  VAL VAL A . n 
A 1 1359 THR 1359 930  930  THR THR A . n 
A 1 1360 SER 1360 931  931  SER SER A . n 
A 1 1361 GLY 1361 932  932  GLY GLY A . n 
A 1 1362 LEU 1362 933  933  LEU LEU A . n 
A 1 1363 PHE 1363 934  934  PHE PHE A . n 
A 1 1364 GLN 1364 935  935  GLN GLN A . n 
A 1 1365 LEU 1365 936  936  LEU LEU A . n 
A 1 1366 LYS 1366 937  937  LYS LYS A . n 
A 1 1367 THR 1367 938  938  THR THR A . n 
A 1 1368 TYR 1368 939  939  TYR TYR A . n 
A 1 1369 LEU 1369 940  940  LEU LEU A . n 
A 1 1370 ARG 1370 941  941  ARG ARG A . n 
A 1 1371 MET 1371 942  942  MET MET A . n 
A 1 1372 ILE 1372 943  943  ILE ILE A . n 
A 1 1373 GLU 1373 944  944  GLU GLU A . n 
A 1 1374 MET 1374 945  945  MET MET A . n 
A 1 1375 ASP 1375 946  946  ASP ASP A . n 
A 1 1376 ASP 1376 947  947  ASP ASP A . n 
A 1 1377 LEU 1377 948  948  LEU LEU A . n 
A 1 1378 PHE 1378 949  949  PHE PHE A . n 
A 1 1379 LEU 1379 950  950  LEU LEU A . n 
A 1 1380 PRO 1380 951  951  PRO PRO A . n 
A 1 1381 LEU 1381 952  952  LEU LEU A . n 
A 1 1382 ILE 1382 953  953  ILE ILE A . n 
A 1 1383 ALA 1383 954  954  ALA ALA A . n 
A 1 1384 LYS 1384 955  955  LYS LYS A . n 
A 1 1385 ASN 1385 956  956  ASN ASN A . n 
A 1 1386 PRO 1386 957  957  PRO PRO A . n 
A 1 1387 GLY 1387 958  958  GLY GLY A . n 
A 1 1388 ASN 1388 959  959  ASN ASN A . n 
A 1 1389 CYS 1389 960  960  CYS CYS A . n 
A 1 1390 THR 1390 961  961  THR THR A . n 
A 1 1391 ALA 1391 962  962  ALA ALA A . n 
A 1 1392 ILE 1392 963  963  ILE ILE A . n 
A 1 1393 ASP 1393 964  964  ASP ASP A . n 
A 1 1394 PHE 1394 965  965  PHE PHE A . n 
A 1 1395 VAL 1395 966  966  VAL VAL A . n 
A 1 1396 LEU 1396 967  967  LEU LEU A . n 
A 1 1397 ASN 1397 968  968  ASN ASN A . n 
A 1 1398 PRO 1398 969  969  PRO PRO A . n 
A 1 1399 SER 1399 970  970  SER SER A . n 
A 1 1400 GLY 1400 971  971  GLY GLY A . n 
A 1 1401 LEU 1401 972  972  LEU LEU A . n 
A 1 1402 ASN 1402 973  973  ASN ASN A . n 
A 1 1403 VAL 1403 974  974  VAL VAL A . n 
A 1 1404 PRO 1404 975  975  PRO PRO A . n 
A 1 1405 GLY 1405 976  976  GLY GLY A . n 
A 1 1406 SER 1406 977  977  SER SER A . n 
A 1 1407 GLN 1407 978  978  GLN GLN A . n 
A 1 1408 ASP 1408 979  979  ASP ASP A . n 
A 1 1409 LEU 1409 980  980  LEU LEU A . n 
A 1 1410 THR 1410 981  981  THR THR A . n 
A 1 1411 SER 1411 982  982  SER SER A . n 
A 1 1412 PHE 1412 983  983  PHE PHE A . n 
A 1 1413 LEU 1413 984  984  LEU LEU A . n 
A 1 1414 ARG 1414 985  985  ARG ARG A . n 
A 1 1415 GLN 1415 986  986  GLN GLN A . n 
A 1 1416 ILE 1416 987  987  ILE ILE A . n 
A 1 1417 VAL 1417 988  988  VAL VAL A . n 
A 1 1418 ARG 1418 989  989  ARG ARG A . n 
A 1 1419 ARG 1419 990  990  ARG ARG A . n 
A 1 1420 THR 1420 991  991  THR THR A . n 
A 1 1421 ILE 1421 992  992  ILE ILE A . n 
A 1 1422 THR 1422 993  993  THR THR A . n 
A 1 1423 LEU 1423 994  994  LEU LEU A . n 
A 1 1424 SER 1424 995  995  SER SER A . n 
A 1 1425 ALA 1425 996  996  ALA ALA A . n 
A 1 1426 LYS 1426 997  997  LYS LYS A . n 
A 1 1427 ASN 1427 998  998  ASN ASN A . n 
A 1 1428 LYS 1428 999  999  LYS LYS A . n 
A 1 1429 LEU 1429 1000 1000 LEU LEU A . n 
A 1 1430 ILE 1430 1001 1001 ILE ILE A . n 
A 1 1431 ASN 1431 1002 1002 ASN ASN A . n 
A 1 1432 THR 1432 1003 1003 THR THR A . n 
A 1 1433 LEU 1433 1004 1004 LEU LEU A . n 
A 1 1434 PHE 1434 1005 1005 PHE PHE A . n 
A 1 1435 HIS 1435 1006 1006 HIS HIS A . n 
A 1 1436 ALA 1436 1007 1007 ALA ALA A . n 
A 1 1437 SER 1437 1008 1008 SER SER A . n 
A 1 1438 ALA 1438 1009 1009 ALA ALA A . n 
A 1 1439 ASP 1439 1010 1010 ASP ASP A . n 
A 1 1440 PHE 1440 1011 1011 PHE PHE A . n 
A 1 1441 GLU 1441 1012 1012 GLU GLU A . n 
A 1 1442 ASP 1442 1013 1013 ASP ASP A . n 
A 1 1443 GLU 1443 1014 1014 GLU GLU A . n 
A 1 1444 MET 1444 1015 1015 MET MET A . n 
A 1 1445 VAL 1445 1016 1016 VAL VAL A . n 
A 1 1446 CYS 1446 1017 1017 CYS CYS A . n 
A 1 1447 LYS 1447 1018 1018 LYS LYS A . n 
A 1 1448 TRP 1448 1019 1019 TRP TRP A . n 
A 1 1449 LEU 1449 1020 1020 LEU LEU A . n 
A 1 1450 LEU 1450 1021 1021 LEU LEU A . n 
A 1 1451 SER 1451 1022 1022 SER SER A . n 
A 1 1452 SER 1452 1023 1023 SER SER A . n 
A 1 1453 THR 1453 1024 1024 THR THR A . n 
A 1 1454 PRO 1454 1025 1025 PRO PRO A . n 
A 1 1455 VAL 1455 1026 1026 VAL VAL A . n 
A 1 1456 MET 1456 1027 1027 MET MET A . n 
A 1 1457 SER 1457 1028 1028 SER SER A . n 
A 1 1458 ARG 1458 1029 1029 ARG ARG A . n 
A 1 1459 PHE 1459 1030 1030 PHE PHE A . n 
A 1 1460 ALA 1460 1031 1031 ALA ALA A . n 
A 1 1461 ALA 1461 1032 1032 ALA ALA A . n 
A 1 1462 ASP 1462 1033 1033 ASP ASP A . n 
A 1 1463 ILE 1463 1034 1034 ILE ILE A . n 
A 1 1464 PHE 1464 1035 1035 PHE PHE A . n 
A 1 1465 SER 1465 1036 1036 SER SER A . n 
A 1 1466 ARG 1466 1037 1037 ARG ARG A . n 
A 1 1467 THR 1467 1038 1038 THR THR A . n 
A 1 1468 PRO 1468 1039 1039 PRO PRO A . n 
A 1 1469 SER 1469 1040 1040 SER SER A . n 
A 1 1470 GLY 1470 1041 1041 GLY GLY A . n 
A 1 1471 LYS 1471 1042 1042 LYS LYS A . n 
A 1 1472 ARG 1472 1043 1043 ARG ARG A . n 
A 1 1473 LEU 1473 1044 1044 LEU LEU A . n 
A 1 1474 GLN 1474 1045 1045 GLN GLN A . n 
A 1 1475 ILE 1475 1046 1046 ILE ILE A . n 
A 1 1476 LEU 1476 1047 1047 LEU LEU A . n 
A 1 1477 GLY 1477 1048 1048 GLY GLY A . n 
A 1 1478 TYR 1478 1049 1049 TYR TYR A . n 
A 1 1479 LEU 1479 1050 1050 LEU LEU A . n 
A 1 1480 GLU 1480 1051 1051 GLU GLU A . n 
A 1 1481 GLY 1481 1052 1052 GLY GLY A . n 
A 1 1482 THR 1482 1053 1053 THR THR A . n 
A 1 1483 ARG 1483 1054 1054 ARG ARG A . n 
A 1 1484 THR 1484 1055 1055 THR THR A . n 
A 1 1485 LEU 1485 1056 1056 LEU LEU A . n 
A 1 1486 LEU 1486 1057 1057 LEU LEU A . n 
A 1 1487 ALA 1487 1058 1058 ALA ALA A . n 
A 1 1488 SER 1488 1059 1059 SER SER A . n 
A 1 1489 LYS 1489 1060 1060 LYS LYS A . n 
A 1 1490 ILE 1490 1061 1061 ILE ILE A . n 
A 1 1491 ILE 1491 1062 1062 ILE ILE A . n 
A 1 1492 ASN 1492 1063 1063 ASN ASN A . n 
A 1 1493 ASN 1493 1064 1064 ASN ASN A . n 
A 1 1494 ASN 1494 1065 1065 ASN ASN A . n 
A 1 1495 THR 1495 1066 1066 THR THR A . n 
A 1 1496 GLU 1496 1067 1067 GLU GLU A . n 
A 1 1497 THR 1497 1068 1068 THR THR A . n 
A 1 1498 PRO 1498 1069 1069 PRO PRO A . n 
A 1 1499 VAL 1499 1070 1070 VAL VAL A . n 
A 1 1500 LEU 1500 1071 1071 LEU LEU A . n 
A 1 1501 ASP 1501 1072 1072 ASP ASP A . n 
A 1 1502 ARG 1502 1073 1073 ARG ARG A . n 
A 1 1503 LEU 1503 1074 1074 LEU LEU A . n 
A 1 1504 ARG 1504 1075 1075 ARG ARG A . n 
A 1 1505 LYS 1505 1076 1076 LYS LYS A . n 
A 1 1506 ILE 1506 1077 1077 ILE ILE A . n 
A 1 1507 THR 1507 1078 1078 THR THR A . n 
A 1 1508 LEU 1508 1079 1079 LEU LEU A . n 
A 1 1509 GLN 1509 1080 1080 GLN GLN A . n 
A 1 1510 ARG 1510 1081 1081 ARG ARG A . n 
A 1 1511 TRP 1511 1082 1082 TRP TRP A . n 
A 1 1512 SER 1512 1083 1083 SER SER A . n 
A 1 1513 LEU 1513 1084 1084 LEU LEU A . n 
A 1 1514 TRP 1514 1085 1085 TRP TRP A . n 
A 1 1515 PHE 1515 1086 1086 PHE PHE A . n 
A 1 1516 SER 1516 1087 1087 SER SER A . n 
A 1 1517 TYR 1517 1088 1088 TYR TYR A . n 
A 1 1518 LEU 1518 1089 1089 LEU LEU A . n 
A 1 1519 ASP 1519 1090 1090 ASP ASP A . n 
A 1 1520 HIS 1520 1091 1091 HIS HIS A . n 
A 1 1521 CYS 1521 1092 1092 CYS CYS A . n 
A 1 1522 ASP 1522 1093 1093 ASP ASP A . n 
A 1 1523 ASN 1523 1094 1094 ASN ASN A . n 
A 1 1524 ILE 1524 1095 1095 ILE ILE A . n 
A 1 1525 LEU 1525 1096 1096 LEU LEU A . n 
A 1 1526 ALA 1526 1097 1097 ALA ALA A . n 
A 1 1527 GLU 1527 1098 1098 GLU GLU A . n 
A 1 1528 ALA 1528 1099 1099 ALA ALA A . n 
A 1 1529 LEU 1529 1100 1100 LEU LEU A . n 
A 1 1530 THR 1530 1101 1101 THR THR A . n 
A 1 1531 GLN 1531 1102 1102 GLN GLN A . n 
A 1 1532 ILE 1532 1103 1103 ILE ILE A . n 
A 1 1533 THR 1533 1104 1104 THR THR A . n 
A 1 1534 CYS 1534 1105 1105 CYS CYS A . n 
A 1 1535 THR 1535 1106 1106 THR THR A . n 
A 1 1536 VAL 1536 1107 1107 VAL VAL A . n 
A 1 1537 ASP 1537 1108 1108 ASP ASP A . n 
A 1 1538 LEU 1538 1109 1109 LEU LEU A . n 
A 1 1539 ALA 1539 1110 1110 ALA ALA A . n 
A 1 1540 GLN 1540 1111 1111 GLN GLN A . n 
A 1 1541 ILE 1541 1112 1112 ILE ILE A . n 
A 1 1542 LEU 1542 1113 1113 LEU LEU A . n 
A 1 1543 ARG 1543 1114 1114 ARG ARG A . n 
A 1 1544 GLU 1544 1115 1115 GLU GLU A . n 
A 1 1545 TYR 1545 1116 1116 TYR TYR A . n 
A 1 1546 SER 1546 1117 1117 SER SER A . n 
A 1 1547 TRP 1547 1118 1118 TRP TRP A . n 
A 1 1548 ALA 1548 1119 1119 ALA ALA A . n 
A 1 1549 HIS 1549 1120 1120 HIS HIS A . n 
A 1 1550 ILE 1550 1121 1121 ILE ILE A . n 
A 1 1551 LEU 1551 1122 1122 LEU LEU A . n 
A 1 1552 GLU 1552 1123 1123 GLU GLU A . n 
A 1 1553 GLY 1553 1124 1124 GLY GLY A . n 
A 1 1554 ARG 1554 1125 1125 ARG ARG A . n 
A 1 1555 PRO 1555 1126 1126 PRO PRO A . n 
A 1 1556 LEU 1556 1127 1127 LEU LEU A . n 
A 1 1557 ILE 1557 1128 1128 ILE ILE A . n 
A 1 1558 GLY 1558 1129 1129 GLY GLY A . n 
A 1 1559 ALA 1559 1130 1130 ALA ALA A . n 
A 1 1560 THR 1560 1131 1131 THR THR A . n 
A 1 1561 LEU 1561 1132 1132 LEU LEU A . n 
A 1 1562 PRO 1562 1133 1133 PRO PRO A . n 
A 1 1563 CYS 1563 1134 1134 CYS CYS A . n 
A 1 1564 MET 1564 1135 1135 MET MET A . n 
A 1 1565 ILE 1565 1136 1136 ILE ILE A . n 
A 1 1566 GLU 1566 1137 1137 GLU GLU A . n 
A 1 1567 GLN 1567 1138 1138 GLN GLN A . n 
A 1 1568 PHE 1568 1139 1139 PHE PHE A . n 
A 1 1569 LYS 1569 1140 1140 LYS LYS A . n 
A 1 1570 VAL 1570 1141 1141 VAL VAL A . n 
A 1 1571 PHE 1571 1142 1142 PHE PHE A . n 
A 1 1572 TRP 1572 1143 1143 TRP TRP A . n 
A 1 1573 LEU 1573 1144 1144 LEU LEU A . n 
A 1 1574 LYS 1574 1145 1145 LYS LYS A . n 
A 1 1575 PRO 1575 1146 1146 PRO PRO A . n 
A 1 1576 TYR 1576 1147 1147 TYR TYR A . n 
A 1 1577 GLU 1577 1148 1148 GLU GLU A . n 
A 1 1578 GLN 1578 1149 1149 GLN GLN A . n 
A 1 1579 CYS 1579 1150 1150 CYS CYS A . n 
A 1 1580 PRO 1580 1151 1151 PRO PRO A . n 
A 1 1581 GLN 1581 1152 1152 GLN GLN A . n 
A 1 1582 CYS 1582 1153 1153 CYS CYS A . n 
A 1 1583 SER 1583 1154 1154 SER SER A . n 
A 1 1584 ASN 1584 1155 1155 ASN ASN A . n 
A 1 1585 ALA 1585 1156 1156 ALA ALA A . n 
A 1 1586 LYS 1586 1157 1157 LYS LYS A . n 
A 1 1587 GLN 1587 1158 1158 GLN GLN A . n 
A 1 1588 PRO 1588 1159 1159 PRO PRO A . n 
A 1 1589 GLY 1589 1160 1160 GLY GLY A . n 
A 1 1590 GLY 1590 1161 1161 GLY GLY A . n 
A 1 1591 LYS 1591 1162 1162 LYS LYS A . n 
A 1 1592 PRO 1592 1163 1163 PRO PRO A . n 
A 1 1593 PHE 1593 1164 1164 PHE PHE A . n 
A 1 1594 VAL 1594 1165 1165 VAL VAL A . n 
A 1 1595 SER 1595 1166 1166 SER SER A . n 
A 1 1596 VAL 1596 1167 1167 VAL VAL A . n 
A 1 1597 ALA 1597 1168 1168 ALA ALA A . n 
A 1 1598 VAL 1598 1169 1169 VAL VAL A . n 
A 1 1599 LYS 1599 1170 1170 LYS LYS A . n 
A 1 1600 LYS 1600 1171 1171 LYS LYS A . n 
A 1 1601 HIS 1601 1172 1172 HIS HIS A . n 
A 1 1602 ILE 1602 1173 1173 ILE ILE A . n 
A 1 1603 VAL 1603 1174 1174 VAL VAL A . n 
A 1 1604 SER 1604 1175 1175 SER SER A . n 
A 1 1605 ALA 1605 1176 1176 ALA ALA A . n 
A 1 1606 TRP 1606 1177 1177 TRP TRP A . n 
A 1 1607 PRO 1607 1178 1178 PRO PRO A . n 
A 1 1608 ASN 1608 1179 1179 ASN ASN A . n 
A 1 1609 ALA 1609 1180 1180 ALA ALA A . n 
A 1 1610 SER 1610 1181 1181 SER SER A . n 
A 1 1611 ARG 1611 1182 1182 ARG ARG A . n 
A 1 1612 ILE 1612 1183 1183 ILE ILE A . n 
A 1 1613 SER 1613 1184 1184 SER SER A . n 
A 1 1614 TRP 1614 1185 1185 TRP TRP A . n 
A 1 1615 THR 1615 1186 1186 THR THR A . n 
A 1 1616 ILE 1616 1187 1187 ILE ILE A . n 
A 1 1617 GLY 1617 1188 1188 GLY GLY A . n 
A 1 1618 ASP 1618 1189 1189 ASP ASP A . n 
A 1 1619 GLY 1619 1190 1190 GLY GLY A . n 
A 1 1620 ILE 1620 1191 1191 ILE ILE A . n 
A 1 1621 PRO 1621 1192 1192 PRO PRO A . n 
A 1 1622 TYR 1622 1193 1193 TYR TYR A . n 
A 1 1623 ILE 1623 1194 1194 ILE ILE A . n 
A 1 1624 GLY 1624 1195 ?    ?   ?   A . n 
A 1 1625 SER 1625 1196 ?    ?   ?   A . n 
A 1 1626 ARG 1626 1197 ?    ?   ?   A . n 
A 1 1627 THR 1627 1198 ?    ?   ?   A . n 
A 1 1628 GLU 1628 1199 ?    ?   ?   A . n 
A 1 1629 ASP 1629 1200 ?    ?   ?   A . n 
A 1 1630 LYS 1630 1201 ?    ?   ?   A . n 
A 1 1631 ILE 1631 1202 ?    ?   ?   A . n 
A 1 1632 GLY 1632 1203 ?    ?   ?   A . n 
A 1 1633 GLN 1633 1204 1204 GLN GLN A . n 
A 1 1634 PRO 1634 1205 1205 PRO PRO A . n 
A 1 1635 ALA 1635 1206 1206 ALA ALA A . n 
A 1 1636 ILE 1636 1207 1207 ILE ILE A . n 
A 1 1637 LYS 1637 1208 1208 LYS LYS A . n 
A 1 1638 PRO 1638 1209 1209 PRO PRO A . n 
A 1 1639 LYS 1639 1210 1210 LYS LYS A . n 
A 1 1640 CYS 1640 1211 1211 CYS CYS A . n 
A 1 1641 PRO 1641 1212 1212 PRO PRO A . n 
A 1 1642 SER 1642 1213 1213 SER SER A . n 
A 1 1643 ALA 1643 1214 1214 ALA ALA A . n 
A 1 1644 ALA 1644 1215 1215 ALA ALA A . n 
A 1 1645 LEU 1645 1216 1216 LEU LEU A . n 
A 1 1646 ARG 1646 1217 1217 ARG ARG A . n 
A 1 1647 GLU 1647 1218 1218 GLU GLU A . n 
A 1 1648 ALA 1648 1219 1219 ALA ALA A . n 
A 1 1649 ILE 1649 1220 1220 ILE ILE A . n 
A 1 1650 GLU 1650 1221 1221 GLU GLU A . n 
A 1 1651 LEU 1651 1222 1222 LEU LEU A . n 
A 1 1652 ALA 1652 1223 1223 ALA ALA A . n 
A 1 1653 SER 1653 1224 1224 SER SER A . n 
A 1 1654 ARG 1654 1225 1225 ARG ARG A . n 
A 1 1655 LEU 1655 1226 1226 LEU LEU A . n 
A 1 1656 THR 1656 1227 1227 THR THR A . n 
A 1 1657 TRP 1657 1228 1228 TRP TRP A . n 
A 1 1658 VAL 1658 1229 1229 VAL VAL A . n 
A 1 1659 THR 1659 1230 1230 THR THR A . n 
A 1 1660 GLN 1660 1231 1231 GLN GLN A . n 
A 1 1661 GLY 1661 1232 1232 GLY GLY A . n 
A 1 1662 SER 1662 1233 1233 SER SER A . n 
A 1 1663 SER 1663 1234 1234 SER SER A . n 
A 1 1664 ASN 1664 1235 1235 ASN ASN A . n 
A 1 1665 SER 1665 1236 1236 SER SER A . n 
A 1 1666 ASP 1666 1237 1237 ASP ASP A . n 
A 1 1667 LEU 1667 1238 1238 LEU LEU A . n 
A 1 1668 LEU 1668 1239 1239 LEU LEU A . n 
A 1 1669 ILE 1669 1240 1240 ILE ILE A . n 
A 1 1670 LYS 1670 1241 1241 LYS LYS A . n 
A 1 1671 PRO 1671 1242 1242 PRO PRO A . n 
A 1 1672 PHE 1672 1243 1243 PHE PHE A . n 
A 1 1673 LEU 1673 1244 1244 LEU LEU A . n 
A 1 1674 GLU 1674 1245 1245 GLU GLU A . n 
A 1 1675 ALA 1675 1246 1246 ALA ALA A . n 
A 1 1676 ARG 1676 1247 1247 ARG ARG A . n 
A 1 1677 VAL 1677 1248 1248 VAL VAL A . n 
A 1 1678 ASN 1678 1249 1249 ASN ASN A . n 
A 1 1679 LEU 1679 1250 1250 LEU LEU A . n 
A 1 1680 SER 1680 1251 1251 SER SER A . n 
A 1 1681 VAL 1681 1252 1252 VAL VAL A . n 
A 1 1682 GLN 1682 1253 1253 GLN GLN A . n 
A 1 1683 GLU 1683 1254 1254 GLU GLU A . n 
A 1 1684 ILE 1684 1255 1255 ILE ILE A . n 
A 1 1685 LEU 1685 1256 1256 LEU LEU A . n 
A 1 1686 GLN 1686 1257 1257 GLN GLN A . n 
A 1 1687 MET 1687 1258 1258 MET MET A . n 
A 1 1688 THR 1688 1259 1259 THR THR A . n 
A 1 1689 PRO 1689 1260 1260 PRO PRO A . n 
A 1 1690 SER 1690 1261 1261 SER SER A . n 
A 1 1691 HIS 1691 1262 1262 HIS HIS A . n 
A 1 1692 TYR 1692 1263 1263 TYR TYR A . n 
A 1 1693 SER 1693 1264 1264 SER SER A . n 
A 1 1694 GLY 1694 1265 1265 GLY GLY A . n 
A 1 1695 ASN 1695 1266 1266 ASN ASN A . n 
A 1 1696 ILE 1696 1267 1267 ILE ILE A . n 
A 1 1697 VAL 1697 1268 1268 VAL VAL A . n 
A 1 1698 HIS 1698 1269 1269 HIS HIS A . n 
A 1 1699 ARG 1699 1270 1270 ARG ARG A . n 
A 1 1700 TYR 1700 1271 1271 TYR TYR A . n 
A 1 1701 ASN 1701 1272 1272 ASN ASN A . n 
A 1 1702 ASP 1702 1273 1273 ASP ASP A . n 
A 1 1703 GLN 1703 1274 1274 GLN GLN A . n 
A 1 1704 TYR 1704 1275 1275 TYR TYR A . n 
A 1 1705 SER 1705 1276 1276 SER SER A . n 
A 1 1706 PRO 1706 1277 1277 PRO PRO A . n 
A 1 1707 HIS 1707 1278 1278 HIS HIS A . n 
A 1 1708 SER 1708 1279 1279 SER SER A . n 
A 1 1709 PHE 1709 1280 1280 PHE PHE A . n 
A 1 1710 MET 1710 1281 1281 MET MET A . n 
A 1 1711 ALA 1711 1282 1282 ALA ALA A . n 
A 1 1712 ASN 1712 1283 1283 ASN ASN A . n 
A 1 1713 ARG 1713 1284 1284 ARG ARG A . n 
A 1 1714 MET 1714 1285 1285 MET MET A . n 
A 1 1715 SER 1715 1286 1286 SER SER A . n 
A 1 1716 ASN 1716 1287 1287 ASN ASN A . n 
A 1 1717 SER 1717 1288 1288 SER SER A . n 
A 1 1718 ALA 1718 1289 1289 ALA ALA A . n 
A 1 1719 THR 1719 1290 1290 THR THR A . n 
A 1 1720 ARG 1720 1291 1291 ARG ARG A . n 
A 1 1721 LEU 1721 1292 1292 LEU LEU A . n 
A 1 1722 ILE 1722 1293 1293 ILE ILE A . n 
A 1 1723 VAL 1723 1294 1294 VAL VAL A . n 
A 1 1724 SER 1724 1295 1295 SER SER A . n 
A 1 1725 THR 1725 1296 1296 THR THR A . n 
A 1 1726 ASN 1726 1297 1297 ASN ASN A . n 
A 1 1727 THR 1727 1298 1298 THR THR A . n 
A 1 1728 LEU 1728 1299 1299 LEU LEU A . n 
A 1 1729 GLY 1729 1300 1300 GLY GLY A . n 
A 1 1730 GLU 1730 1301 1301 GLU GLU A . n 
A 1 1731 PHE 1731 1302 1302 PHE PHE A . n 
A 1 1732 SER 1732 1303 1303 SER SER A . n 
A 1 1733 GLY 1733 1304 1304 GLY GLY A . n 
A 1 1734 GLY 1734 1305 ?    ?   ?   A . n 
A 1 1735 GLY 1735 1306 ?    ?   ?   A . n 
A 1 1736 GLN 1736 1307 ?    ?   ?   A . n 
A 1 1737 SER 1737 1308 ?    ?   ?   A . n 
A 1 1738 ALA 1738 1309 1309 ALA ALA A . n 
A 1 1739 ARG 1739 1310 1310 ARG ARG A . n 
A 1 1740 ASP 1740 1311 1311 ASP ASP A . n 
A 1 1741 SER 1741 1312 1312 SER SER A . n 
A 1 1742 ASN 1742 1313 1313 ASN ASN A . n 
A 1 1743 ILE 1743 1314 1314 ILE ILE A . n 
A 1 1744 ILE 1744 1315 1315 ILE ILE A . n 
A 1 1745 PHE 1745 1316 1316 PHE PHE A . n 
A 1 1746 GLN 1746 1317 1317 GLN GLN A . n 
A 1 1747 ASN 1747 1318 1318 ASN ASN A . n 
A 1 1748 VAL 1748 1319 1319 VAL VAL A . n 
A 1 1749 ILE 1749 1320 1320 ILE ILE A . n 
A 1 1750 ASN 1750 1321 1321 ASN ASN A . n 
A 1 1751 TYR 1751 1322 1322 TYR TYR A . n 
A 1 1752 ALA 1752 1323 1323 ALA ALA A . n 
A 1 1753 VAL 1753 1324 1324 VAL VAL A . n 
A 1 1754 ALA 1754 1325 1325 ALA ALA A . n 
A 1 1755 LEU 1755 1326 1326 LEU LEU A . n 
A 1 1756 PHE 1756 1327 1327 PHE PHE A . n 
A 1 1757 ASP 1757 1328 1328 ASP ASP A . n 
A 1 1758 ILE 1758 1329 1329 ILE ILE A . n 
A 1 1759 LYS 1759 1330 1330 LYS LYS A . n 
A 1 1760 PHE 1760 1331 1331 PHE PHE A . n 
A 1 1761 ARG 1761 1332 1332 ARG ARG A . n 
A 1 1762 ASN 1762 1333 1333 ASN ASN A . n 
A 1 1763 THR 1763 1334 1334 THR THR A . n 
A 1 1764 GLU 1764 1335 1335 GLU GLU A . n 
A 1 1765 ALA 1765 1336 1336 ALA ALA A . n 
A 1 1766 THR 1766 1337 1337 THR THR A . n 
A 1 1767 ASP 1767 1338 1338 ASP ASP A . n 
A 1 1768 ILE 1768 1339 1339 ILE ILE A . n 
A 1 1769 GLN 1769 1340 1340 GLN GLN A . n 
A 1 1770 TYR 1770 1341 1341 TYR TYR A . n 
A 1 1771 ASN 1771 1342 1342 ASN ASN A . n 
A 1 1772 ARG 1772 1343 1343 ARG ARG A . n 
A 1 1773 ALA 1773 1344 1344 ALA ALA A . n 
A 1 1774 HIS 1774 1345 1345 HIS HIS A . n 
A 1 1775 LEU 1775 1346 1346 LEU LEU A . n 
A 1 1776 HIS 1776 1347 1347 HIS HIS A . n 
A 1 1777 LEU 1777 1348 1348 LEU LEU A . n 
A 1 1778 THR 1778 1349 1349 THR THR A . n 
A 1 1779 LYS 1779 1350 1350 LYS LYS A . n 
A 1 1780 CYS 1780 1351 1351 CYS CYS A . n 
A 1 1781 CYS 1781 1352 1352 CYS CYS A . n 
A 1 1782 THR 1782 1353 1353 THR THR A . n 
A 1 1783 ARG 1783 1354 1354 ARG ARG A . n 
A 1 1784 GLU 1784 1355 1355 GLU GLU A . n 
A 1 1785 VAL 1785 1356 1356 VAL VAL A . n 
A 1 1786 PRO 1786 1357 1357 PRO PRO A . n 
A 1 1787 ALA 1787 1358 1358 ALA ALA A . n 
A 1 1788 GLN 1788 1359 1359 GLN GLN A . n 
A 1 1789 TYR 1789 1360 1360 TYR TYR A . n 
A 1 1790 LEU 1790 1361 1361 LEU LEU A . n 
A 1 1791 THR 1791 1362 1362 THR THR A . n 
A 1 1792 TYR 1792 1363 1363 TYR TYR A . n 
A 1 1793 THR 1793 1364 1364 THR THR A . n 
A 1 1794 SER 1794 1365 1365 SER SER A . n 
A 1 1795 THR 1795 1366 1366 THR THR A . n 
A 1 1796 LEU 1796 1367 1367 LEU LEU A . n 
A 1 1797 ASP 1797 1368 1368 ASP ASP A . n 
A 1 1798 LEU 1798 1369 1369 LEU LEU A . n 
A 1 1799 ASP 1799 1370 1370 ASP ASP A . n 
A 1 1800 LEU 1800 1371 1371 LEU LEU A . n 
A 1 1801 THR 1801 1372 1372 THR THR A . n 
A 1 1802 ARG 1802 1373 1373 ARG ARG A . n 
A 1 1803 TYR 1803 1374 1374 TYR TYR A . n 
A 1 1804 ARG 1804 1375 1375 ARG ARG A . n 
A 1 1805 GLU 1805 1376 1376 GLU GLU A . n 
A 1 1806 ASN 1806 1377 1377 ASN ASN A . n 
A 1 1807 GLU 1807 1378 1378 GLU GLU A . n 
A 1 1808 LEU 1808 1379 1379 LEU LEU A . n 
A 1 1809 ILE 1809 1380 1380 ILE ILE A . n 
A 1 1810 TYR 1810 1381 1381 TYR TYR A . n 
A 1 1811 ASP 1811 1382 1382 ASP ASP A . n 
A 1 1812 SER 1812 1383 1383 SER SER A . n 
A 1 1813 ASN 1813 1384 1384 ASN ASN A . n 
A 1 1814 PRO 1814 1385 1385 PRO PRO A . n 
A 1 1815 LEU 1815 1386 1386 LEU LEU A . n 
A 1 1816 LYS 1816 1387 1387 LYS LYS A . n 
A 1 1817 GLY 1817 1388 1388 GLY GLY A . n 
A 1 1818 GLY 1818 1389 1389 GLY GLY A . n 
A 1 1819 LEU 1819 1390 1390 LEU LEU A . n 
A 1 1820 ASN 1820 1391 1391 ASN ASN A . n 
A 1 1821 CYS 1821 1392 1392 CYS CYS A . n 
A 1 1822 ASN 1822 1393 1393 ASN ASN A . n 
A 1 1823 ILE 1823 1394 ?    ?   ?   A . n 
A 1 1824 SER 1824 1395 ?    ?   ?   A . n 
A 1 1825 PHE 1825 1396 ?    ?   ?   A . n 
A 1 1826 ASP 1826 1397 ?    ?   ?   A . n 
A 1 1827 ASN 1827 1398 ?    ?   ?   A . n 
A 1 1828 PRO 1828 1399 ?    ?   ?   A . n 
A 1 1829 PHE 1829 1400 ?    ?   ?   A . n 
A 1 1830 SER 1830 1401 ?    ?   ?   A . n 
A 1 1831 ARG 1831 1402 ?    ?   ?   A . n 
A 1 1832 ASP 1832 1403 ?    ?   ?   A . n 
A 1 1833 TYR 1833 1404 ?    ?   ?   A . n 
A 1 1834 LYS 1834 1405 ?    ?   ?   A . n 
A 1 1835 ASP 1835 1406 ?    ?   ?   A . n 
A 1 1836 ASP 1836 1407 ?    ?   ?   A . n 
A 1 1837 ASP 1837 1408 ?    ?   ?   A . n 
A 1 1838 ASP 1838 1409 ?    ?   ?   A . n 
A 1 1839 LYS 1839 1410 ?    ?   ?   A . n 
B 2 1    MET 1    -316 ?    ?   ?   B . n 
B 2 2    GLY 2    -315 ?    ?   ?   B . n 
B 2 3    SER 3    -314 ?    ?   ?   B . n 
B 2 4    SER 4    -313 ?    ?   ?   B . n 
B 2 5    HIS 5    -312 ?    ?   ?   B . n 
B 2 6    HIS 6    -311 ?    ?   ?   B . n 
B 2 7    HIS 7    -310 ?    ?   ?   B . n 
B 2 8    HIS 8    -309 ?    ?   ?   B . n 
B 2 9    HIS 9    -308 ?    ?   ?   B . n 
B 2 10   HIS 10   -307 ?    ?   ?   B . n 
B 2 11   GLY 11   -306 ?    ?   ?   B . n 
B 2 12   THR 12   -305 ?    ?   ?   B . n 
B 2 13   LYS 13   -304 ?    ?   ?   B . n 
B 2 14   THR 14   -303 ?    ?   ?   B . n 
B 2 15   GLU 15   -302 ?    ?   ?   B . n 
B 2 16   GLU 16   -301 ?    ?   ?   B . n 
B 2 17   GLY 17   -300 ?    ?   ?   B . n 
B 2 18   LYS 18   -299 ?    ?   ?   B . n 
B 2 19   LEU 19   -298 ?    ?   ?   B . n 
B 2 20   VAL 20   -297 ?    ?   ?   B . n 
B 2 21   ILE 21   -296 ?    ?   ?   B . n 
B 2 22   TRP 22   -295 ?    ?   ?   B . n 
B 2 23   ILE 23   -294 ?    ?   ?   B . n 
B 2 24   ASN 24   -293 ?    ?   ?   B . n 
B 2 25   GLY 25   -292 ?    ?   ?   B . n 
B 2 26   ASP 26   -291 ?    ?   ?   B . n 
B 2 27   LYS 27   -290 ?    ?   ?   B . n 
B 2 28   GLY 28   -289 ?    ?   ?   B . n 
B 2 29   TYR 29   -288 ?    ?   ?   B . n 
B 2 30   ASN 30   -287 ?    ?   ?   B . n 
B 2 31   GLY 31   -286 ?    ?   ?   B . n 
B 2 32   LEU 32   -285 ?    ?   ?   B . n 
B 2 33   ALA 33   -284 ?    ?   ?   B . n 
B 2 34   GLU 34   -283 ?    ?   ?   B . n 
B 2 35   VAL 35   -282 ?    ?   ?   B . n 
B 2 36   GLY 36   -281 ?    ?   ?   B . n 
B 2 37   LYS 37   -280 ?    ?   ?   B . n 
B 2 38   LYS 38   -279 ?    ?   ?   B . n 
B 2 39   PHE 39   -278 ?    ?   ?   B . n 
B 2 40   GLU 40   -277 ?    ?   ?   B . n 
B 2 41   LYS 41   -276 ?    ?   ?   B . n 
B 2 42   ASP 42   -275 ?    ?   ?   B . n 
B 2 43   THR 43   -274 ?    ?   ?   B . n 
B 2 44   GLY 44   -273 ?    ?   ?   B . n 
B 2 45   ILE 45   -272 ?    ?   ?   B . n 
B 2 46   LYS 46   -271 ?    ?   ?   B . n 
B 2 47   VAL 47   -270 ?    ?   ?   B . n 
B 2 48   THR 48   -269 ?    ?   ?   B . n 
B 2 49   VAL 49   -268 ?    ?   ?   B . n 
B 2 50   GLU 50   -267 ?    ?   ?   B . n 
B 2 51   HIS 51   -266 ?    ?   ?   B . n 
B 2 52   PRO 52   -265 ?    ?   ?   B . n 
B 2 53   ASP 53   -264 ?    ?   ?   B . n 
B 2 54   LYS 54   -263 ?    ?   ?   B . n 
B 2 55   LEU 55   -262 ?    ?   ?   B . n 
B 2 56   GLU 56   -261 ?    ?   ?   B . n 
B 2 57   GLU 57   -260 ?    ?   ?   B . n 
B 2 58   LYS 58   -259 ?    ?   ?   B . n 
B 2 59   PHE 59   -258 ?    ?   ?   B . n 
B 2 60   PRO 60   -257 ?    ?   ?   B . n 
B 2 61   GLN 61   -256 ?    ?   ?   B . n 
B 2 62   VAL 62   -255 ?    ?   ?   B . n 
B 2 63   ALA 63   -254 ?    ?   ?   B . n 
B 2 64   ALA 64   -253 ?    ?   ?   B . n 
B 2 65   THR 65   -252 ?    ?   ?   B . n 
B 2 66   GLY 66   -251 ?    ?   ?   B . n 
B 2 67   ASP 67   -250 ?    ?   ?   B . n 
B 2 68   GLY 68   -249 ?    ?   ?   B . n 
B 2 69   PRO 69   -248 ?    ?   ?   B . n 
B 2 70   ASP 70   -247 ?    ?   ?   B . n 
B 2 71   ILE 71   -246 ?    ?   ?   B . n 
B 2 72   ILE 72   -245 ?    ?   ?   B . n 
B 2 73   PHE 73   -244 ?    ?   ?   B . n 
B 2 74   TRP 74   -243 ?    ?   ?   B . n 
B 2 75   ALA 75   -242 ?    ?   ?   B . n 
B 2 76   HIS 76   -241 ?    ?   ?   B . n 
B 2 77   ASP 77   -240 ?    ?   ?   B . n 
B 2 78   ARG 78   -239 ?    ?   ?   B . n 
B 2 79   PHE 79   -238 ?    ?   ?   B . n 
B 2 80   GLY 80   -237 ?    ?   ?   B . n 
B 2 81   GLY 81   -236 ?    ?   ?   B . n 
B 2 82   TYR 82   -235 ?    ?   ?   B . n 
B 2 83   ALA 83   -234 ?    ?   ?   B . n 
B 2 84   GLN 84   -233 ?    ?   ?   B . n 
B 2 85   SER 85   -232 ?    ?   ?   B . n 
B 2 86   GLY 86   -231 ?    ?   ?   B . n 
B 2 87   LEU 87   -230 ?    ?   ?   B . n 
B 2 88   LEU 88   -229 ?    ?   ?   B . n 
B 2 89   ALA 89   -228 ?    ?   ?   B . n 
B 2 90   GLU 90   -227 ?    ?   ?   B . n 
B 2 91   ILE 91   -226 ?    ?   ?   B . n 
B 2 92   THR 92   -225 ?    ?   ?   B . n 
B 2 93   PRO 93   -224 ?    ?   ?   B . n 
B 2 94   ASP 94   -223 ?    ?   ?   B . n 
B 2 95   LYS 95   -222 ?    ?   ?   B . n 
B 2 96   ALA 96   -221 ?    ?   ?   B . n 
B 2 97   PHE 97   -220 ?    ?   ?   B . n 
B 2 98   GLN 98   -219 ?    ?   ?   B . n 
B 2 99   ASP 99   -218 ?    ?   ?   B . n 
B 2 100  LYS 100  -217 ?    ?   ?   B . n 
B 2 101  LEU 101  -216 ?    ?   ?   B . n 
B 2 102  TYR 102  -215 ?    ?   ?   B . n 
B 2 103  PRO 103  -214 ?    ?   ?   B . n 
B 2 104  PHE 104  -213 ?    ?   ?   B . n 
B 2 105  THR 105  -212 ?    ?   ?   B . n 
B 2 106  TRP 106  -211 ?    ?   ?   B . n 
B 2 107  ASP 107  -210 ?    ?   ?   B . n 
B 2 108  ALA 108  -209 ?    ?   ?   B . n 
B 2 109  VAL 109  -208 ?    ?   ?   B . n 
B 2 110  ARG 110  -207 ?    ?   ?   B . n 
B 2 111  TYR 111  -206 ?    ?   ?   B . n 
B 2 112  ASN 112  -205 ?    ?   ?   B . n 
B 2 113  GLY 113  -204 ?    ?   ?   B . n 
B 2 114  LYS 114  -203 ?    ?   ?   B . n 
B 2 115  LEU 115  -202 ?    ?   ?   B . n 
B 2 116  ILE 116  -201 ?    ?   ?   B . n 
B 2 117  ALA 117  -200 ?    ?   ?   B . n 
B 2 118  TYR 118  -199 ?    ?   ?   B . n 
B 2 119  PRO 119  -198 ?    ?   ?   B . n 
B 2 120  ILE 120  -197 ?    ?   ?   B . n 
B 2 121  ALA 121  -196 ?    ?   ?   B . n 
B 2 122  VAL 122  -195 ?    ?   ?   B . n 
B 2 123  GLU 123  -194 ?    ?   ?   B . n 
B 2 124  ALA 124  -193 ?    ?   ?   B . n 
B 2 125  LEU 125  -192 ?    ?   ?   B . n 
B 2 126  SER 126  -191 ?    ?   ?   B . n 
B 2 127  LEU 127  -190 ?    ?   ?   B . n 
B 2 128  ILE 128  -189 ?    ?   ?   B . n 
B 2 129  TYR 129  -188 ?    ?   ?   B . n 
B 2 130  ASN 130  -187 ?    ?   ?   B . n 
B 2 131  LYS 131  -186 ?    ?   ?   B . n 
B 2 132  ASP 132  -185 ?    ?   ?   B . n 
B 2 133  LEU 133  -184 ?    ?   ?   B . n 
B 2 134  LEU 134  -183 ?    ?   ?   B . n 
B 2 135  PRO 135  -182 ?    ?   ?   B . n 
B 2 136  ASN 136  -181 ?    ?   ?   B . n 
B 2 137  PRO 137  -180 ?    ?   ?   B . n 
B 2 138  PRO 138  -179 ?    ?   ?   B . n 
B 2 139  LYS 139  -178 ?    ?   ?   B . n 
B 2 140  THR 140  -177 ?    ?   ?   B . n 
B 2 141  TRP 141  -176 ?    ?   ?   B . n 
B 2 142  GLU 142  -175 ?    ?   ?   B . n 
B 2 143  GLU 143  -174 ?    ?   ?   B . n 
B 2 144  ILE 144  -173 ?    ?   ?   B . n 
B 2 145  PRO 145  -172 ?    ?   ?   B . n 
B 2 146  ALA 146  -171 ?    ?   ?   B . n 
B 2 147  LEU 147  -170 ?    ?   ?   B . n 
B 2 148  ASP 148  -169 ?    ?   ?   B . n 
B 2 149  LYS 149  -168 ?    ?   ?   B . n 
B 2 150  GLU 150  -167 ?    ?   ?   B . n 
B 2 151  LEU 151  -166 ?    ?   ?   B . n 
B 2 152  LYS 152  -165 ?    ?   ?   B . n 
B 2 153  ALA 153  -164 ?    ?   ?   B . n 
B 2 154  LYS 154  -163 ?    ?   ?   B . n 
B 2 155  GLY 155  -162 ?    ?   ?   B . n 
B 2 156  LYS 156  -161 ?    ?   ?   B . n 
B 2 157  SER 157  -160 ?    ?   ?   B . n 
B 2 158  ALA 158  -159 ?    ?   ?   B . n 
B 2 159  LEU 159  -158 ?    ?   ?   B . n 
B 2 160  MET 160  -157 ?    ?   ?   B . n 
B 2 161  PHE 161  -156 ?    ?   ?   B . n 
B 2 162  ASN 162  -155 ?    ?   ?   B . n 
B 2 163  LEU 163  -154 ?    ?   ?   B . n 
B 2 164  GLN 164  -153 ?    ?   ?   B . n 
B 2 165  GLU 165  -152 ?    ?   ?   B . n 
B 2 166  PRO 166  -151 ?    ?   ?   B . n 
B 2 167  TYR 167  -150 ?    ?   ?   B . n 
B 2 168  PHE 168  -149 ?    ?   ?   B . n 
B 2 169  THR 169  -148 ?    ?   ?   B . n 
B 2 170  TRP 170  -147 ?    ?   ?   B . n 
B 2 171  PRO 171  -146 ?    ?   ?   B . n 
B 2 172  LEU 172  -145 ?    ?   ?   B . n 
B 2 173  ILE 173  -144 ?    ?   ?   B . n 
B 2 174  ALA 174  -143 ?    ?   ?   B . n 
B 2 175  ALA 175  -142 ?    ?   ?   B . n 
B 2 176  ASP 176  -141 ?    ?   ?   B . n 
B 2 177  GLY 177  -140 ?    ?   ?   B . n 
B 2 178  GLY 178  -139 ?    ?   ?   B . n 
B 2 179  TYR 179  -138 ?    ?   ?   B . n 
B 2 180  ALA 180  -137 ?    ?   ?   B . n 
B 2 181  PHE 181  -136 ?    ?   ?   B . n 
B 2 182  LYS 182  -135 ?    ?   ?   B . n 
B 2 183  TYR 183  -134 ?    ?   ?   B . n 
B 2 184  GLU 184  -133 ?    ?   ?   B . n 
B 2 185  ASN 185  -132 ?    ?   ?   B . n 
B 2 186  GLY 186  -131 ?    ?   ?   B . n 
B 2 187  LYS 187  -130 ?    ?   ?   B . n 
B 2 188  TYR 188  -129 ?    ?   ?   B . n 
B 2 189  ASP 189  -128 ?    ?   ?   B . n 
B 2 190  ILE 190  -127 ?    ?   ?   B . n 
B 2 191  LYS 191  -126 ?    ?   ?   B . n 
B 2 192  ASP 192  -125 ?    ?   ?   B . n 
B 2 193  VAL 193  -124 ?    ?   ?   B . n 
B 2 194  GLY 194  -123 ?    ?   ?   B . n 
B 2 195  VAL 195  -122 ?    ?   ?   B . n 
B 2 196  ASP 196  -121 ?    ?   ?   B . n 
B 2 197  ASN 197  -120 ?    ?   ?   B . n 
B 2 198  ALA 198  -119 ?    ?   ?   B . n 
B 2 199  GLY 199  -118 ?    ?   ?   B . n 
B 2 200  ALA 200  -117 ?    ?   ?   B . n 
B 2 201  LYS 201  -116 ?    ?   ?   B . n 
B 2 202  ALA 202  -115 ?    ?   ?   B . n 
B 2 203  GLY 203  -114 ?    ?   ?   B . n 
B 2 204  LEU 204  -113 ?    ?   ?   B . n 
B 2 205  THR 205  -112 ?    ?   ?   B . n 
B 2 206  PHE 206  -111 ?    ?   ?   B . n 
B 2 207  LEU 207  -110 ?    ?   ?   B . n 
B 2 208  VAL 208  -109 ?    ?   ?   B . n 
B 2 209  ASP 209  -108 ?    ?   ?   B . n 
B 2 210  LEU 210  -107 ?    ?   ?   B . n 
B 2 211  ILE 211  -106 ?    ?   ?   B . n 
B 2 212  LYS 212  -105 ?    ?   ?   B . n 
B 2 213  ASN 213  -104 ?    ?   ?   B . n 
B 2 214  LYS 214  -103 ?    ?   ?   B . n 
B 2 215  HIS 215  -102 ?    ?   ?   B . n 
B 2 216  MET 216  -101 ?    ?   ?   B . n 
B 2 217  ASN 217  -100 ?    ?   ?   B . n 
B 2 218  ALA 218  -99  ?    ?   ?   B . n 
B 2 219  ASP 219  -98  ?    ?   ?   B . n 
B 2 220  THR 220  -97  ?    ?   ?   B . n 
B 2 221  ASP 221  -96  ?    ?   ?   B . n 
B 2 222  TYR 222  -95  ?    ?   ?   B . n 
B 2 223  SER 223  -94  ?    ?   ?   B . n 
B 2 224  ILE 224  -93  ?    ?   ?   B . n 
B 2 225  ALA 225  -92  ?    ?   ?   B . n 
B 2 226  GLU 226  -91  ?    ?   ?   B . n 
B 2 227  ALA 227  -90  ?    ?   ?   B . n 
B 2 228  ALA 228  -89  ?    ?   ?   B . n 
B 2 229  PHE 229  -88  ?    ?   ?   B . n 
B 2 230  ASN 230  -87  ?    ?   ?   B . n 
B 2 231  LYS 231  -86  ?    ?   ?   B . n 
B 2 232  GLY 232  -85  ?    ?   ?   B . n 
B 2 233  GLU 233  -84  ?    ?   ?   B . n 
B 2 234  THR 234  -83  ?    ?   ?   B . n 
B 2 235  ALA 235  -82  ?    ?   ?   B . n 
B 2 236  MET 236  -81  ?    ?   ?   B . n 
B 2 237  THR 237  -80  ?    ?   ?   B . n 
B 2 238  ILE 238  -79  ?    ?   ?   B . n 
B 2 239  ASN 239  -78  ?    ?   ?   B . n 
B 2 240  GLY 240  -77  ?    ?   ?   B . n 
B 2 241  PRO 241  -76  ?    ?   ?   B . n 
B 2 242  TRP 242  -75  ?    ?   ?   B . n 
B 2 243  ALA 243  -74  ?    ?   ?   B . n 
B 2 244  TRP 244  -73  ?    ?   ?   B . n 
B 2 245  SER 245  -72  ?    ?   ?   B . n 
B 2 246  ASN 246  -71  ?    ?   ?   B . n 
B 2 247  ILE 247  -70  ?    ?   ?   B . n 
B 2 248  ASP 248  -69  ?    ?   ?   B . n 
B 2 249  THR 249  -68  ?    ?   ?   B . n 
B 2 250  SER 250  -67  ?    ?   ?   B . n 
B 2 251  LYS 251  -66  ?    ?   ?   B . n 
B 2 252  VAL 252  -65  ?    ?   ?   B . n 
B 2 253  ASN 253  -64  ?    ?   ?   B . n 
B 2 254  TYR 254  -63  ?    ?   ?   B . n 
B 2 255  GLY 255  -62  ?    ?   ?   B . n 
B 2 256  VAL 256  -61  ?    ?   ?   B . n 
B 2 257  THR 257  -60  ?    ?   ?   B . n 
B 2 258  VAL 258  -59  ?    ?   ?   B . n 
B 2 259  LEU 259  -58  ?    ?   ?   B . n 
B 2 260  PRO 260  -57  ?    ?   ?   B . n 
B 2 261  THR 261  -56  ?    ?   ?   B . n 
B 2 262  PHE 262  -55  ?    ?   ?   B . n 
B 2 263  LYS 263  -54  ?    ?   ?   B . n 
B 2 264  GLY 264  -53  ?    ?   ?   B . n 
B 2 265  GLN 265  -52  ?    ?   ?   B . n 
B 2 266  PRO 266  -51  ?    ?   ?   B . n 
B 2 267  SER 267  -50  ?    ?   ?   B . n 
B 2 268  LYS 268  -49  ?    ?   ?   B . n 
B 2 269  PRO 269  -48  ?    ?   ?   B . n 
B 2 270  PHE 270  -47  ?    ?   ?   B . n 
B 2 271  VAL 271  -46  ?    ?   ?   B . n 
B 2 272  GLY 272  -45  ?    ?   ?   B . n 
B 2 273  VAL 273  -44  ?    ?   ?   B . n 
B 2 274  LEU 274  -43  ?    ?   ?   B . n 
B 2 275  SER 275  -42  ?    ?   ?   B . n 
B 2 276  ALA 276  -41  ?    ?   ?   B . n 
B 2 277  GLY 277  -40  ?    ?   ?   B . n 
B 2 278  ILE 278  -39  ?    ?   ?   B . n 
B 2 279  ASN 279  -38  ?    ?   ?   B . n 
B 2 280  ALA 280  -37  ?    ?   ?   B . n 
B 2 281  ALA 281  -36  ?    ?   ?   B . n 
B 2 282  SER 282  -35  ?    ?   ?   B . n 
B 2 283  PRO 283  -34  ?    ?   ?   B . n 
B 2 284  ASN 284  -33  ?    ?   ?   B . n 
B 2 285  LYS 285  -32  ?    ?   ?   B . n 
B 2 286  GLU 286  -31  ?    ?   ?   B . n 
B 2 287  LEU 287  -30  ?    ?   ?   B . n 
B 2 288  ALA 288  -29  ?    ?   ?   B . n 
B 2 289  LYS 289  -28  ?    ?   ?   B . n 
B 2 290  GLU 290  -27  ?    ?   ?   B . n 
B 2 291  PHE 291  -26  ?    ?   ?   B . n 
B 2 292  LEU 292  -25  ?    ?   ?   B . n 
B 2 293  GLU 293  -24  ?    ?   ?   B . n 
B 2 294  ASN 294  -23  ?    ?   ?   B . n 
B 2 295  TYR 295  -22  ?    ?   ?   B . n 
B 2 296  LEU 296  -21  ?    ?   ?   B . n 
B 2 297  LEU 297  -20  ?    ?   ?   B . n 
B 2 298  THR 298  -19  ?    ?   ?   B . n 
B 2 299  ASP 299  -18  ?    ?   ?   B . n 
B 2 300  GLU 300  -17  ?    ?   ?   B . n 
B 2 301  GLY 301  -16  ?    ?   ?   B . n 
B 2 302  LEU 302  -15  ?    ?   ?   B . n 
B 2 303  GLU 303  -14  ?    ?   ?   B . n 
B 2 304  ALA 304  -13  ?    ?   ?   B . n 
B 2 305  VAL 305  -12  ?    ?   ?   B . n 
B 2 306  ASN 306  -11  ?    ?   ?   B . n 
B 2 307  LYS 307  -10  ?    ?   ?   B . n 
B 2 308  ASP 308  -9   ?    ?   ?   B . n 
B 2 309  LYS 309  -8   ?    ?   ?   B . n 
B 2 310  PRO 310  -7   ?    ?   ?   B . n 
B 2 311  LEU 311  -6   ?    ?   ?   B . n 
B 2 312  GLY 312  -5   ?    ?   ?   B . n 
B 2 313  ALA 313  -4   ?    ?   ?   B . n 
B 2 314  VAL 314  -3   ?    ?   ?   B . n 
B 2 315  ALA 315  -2   ?    ?   ?   B . n 
B 2 316  LEU 316  -1   ?    ?   ?   B . n 
B 2 317  LYS 317  0    ?    ?   ?   B . n 
B 2 318  SER 318  1    ?    ?   ?   B . n 
B 2 319  TYR 319  2    ?    ?   ?   B . n 
B 2 320  GLU 320  3    ?    ?   ?   B . n 
B 2 321  GLU 321  4    ?    ?   ?   B . n 
B 2 322  GLU 322  5    ?    ?   ?   B . n 
B 2 323  LEU 323  6    ?    ?   ?   B . n 
B 2 324  ALA 324  7    ?    ?   ?   B . n 
B 2 325  LYS 325  8    ?    ?   ?   B . n 
B 2 326  ASP 326  9    ?    ?   ?   B . n 
B 2 327  PRO 327  10   ?    ?   ?   B . n 
B 2 328  ARG 328  11   ?    ?   ?   B . n 
B 2 329  ILE 329  12   ?    ?   ?   B . n 
B 2 330  ALA 330  13   ?    ?   ?   B . n 
B 2 331  ALA 331  14   ?    ?   ?   B . n 
B 2 332  THR 332  15   ?    ?   ?   B . n 
B 2 333  MET 333  16   ?    ?   ?   B . n 
B 2 334  GLU 334  17   ?    ?   ?   B . n 
B 2 335  ASN 335  18   ?    ?   ?   B . n 
B 2 336  ALA 336  19   ?    ?   ?   B . n 
B 2 337  GLN 337  20   ?    ?   ?   B . n 
B 2 338  LYS 338  21   ?    ?   ?   B . n 
B 2 339  GLY 339  22   ?    ?   ?   B . n 
B 2 340  GLU 340  23   ?    ?   ?   B . n 
B 2 341  ILE 341  24   ?    ?   ?   B . n 
B 2 342  MET 342  25   ?    ?   ?   B . n 
B 2 343  PRO 343  26   ?    ?   ?   B . n 
B 2 344  ASN 344  27   ?    ?   ?   B . n 
B 2 345  ILE 345  28   ?    ?   ?   B . n 
B 2 346  PRO 346  29   ?    ?   ?   B . n 
B 2 347  GLN 347  30   ?    ?   ?   B . n 
B 2 348  MET 348  31   ?    ?   ?   B . n 
B 2 349  SER 349  32   ?    ?   ?   B . n 
B 2 350  ALA 350  33   ?    ?   ?   B . n 
B 2 351  PHE 351  34   ?    ?   ?   B . n 
B 2 352  TRP 352  35   ?    ?   ?   B . n 
B 2 353  TYR 353  36   ?    ?   ?   B . n 
B 2 354  ALA 354  37   ?    ?   ?   B . n 
B 2 355  VAL 355  38   ?    ?   ?   B . n 
B 2 356  ARG 356  39   ?    ?   ?   B . n 
B 2 357  THR 357  40   ?    ?   ?   B . n 
B 2 358  ALA 358  41   ?    ?   ?   B . n 
B 2 359  VAL 359  42   ?    ?   ?   B . n 
B 2 360  ILE 360  43   ?    ?   ?   B . n 
B 2 361  ASN 361  44   ?    ?   ?   B . n 
B 2 362  ALA 362  45   ?    ?   ?   B . n 
B 2 363  ALA 363  46   ?    ?   ?   B . n 
B 2 364  SER 364  47   ?    ?   ?   B . n 
B 2 365  GLY 365  48   ?    ?   ?   B . n 
B 2 366  ARG 366  49   ?    ?   ?   B . n 
B 2 367  GLN 367  50   ?    ?   ?   B . n 
B 2 368  THR 368  51   ?    ?   ?   B . n 
B 2 369  VAL 369  52   ?    ?   ?   B . n 
B 2 370  ASP 370  53   ?    ?   ?   B . n 
B 2 371  GLU 371  54   ?    ?   ?   B . n 
B 2 372  ALA 372  55   ?    ?   ?   B . n 
B 2 373  LEU 373  56   ?    ?   ?   B . n 
B 2 374  LYS 374  57   ?    ?   ?   B . n 
B 2 375  ASP 375  58   ?    ?   ?   B . n 
B 2 376  ALA 376  59   ?    ?   ?   B . n 
B 2 377  GLN 377  60   ?    ?   ?   B . n 
B 2 378  THR 378  61   ?    ?   ?   B . n 
B 2 379  GLY 379  62   ?    ?   ?   B . n 
B 2 380  THR 380  63   ?    ?   ?   B . n 
B 2 381  ASP 381  64   ?    ?   ?   B . n 
B 2 382  TYR 382  65   ?    ?   ?   B . n 
B 2 383  ASP 383  66   ?    ?   ?   B . n 
B 2 384  ILE 384  67   ?    ?   ?   B . n 
B 2 385  PRO 385  68   ?    ?   ?   B . n 
B 2 386  THR 386  69   ?    ?   ?   B . n 
B 2 387  THR 387  70   ?    ?   ?   B . n 
B 2 388  GLU 388  71   ?    ?   ?   B . n 
B 2 389  ASN 389  72   ?    ?   ?   B . n 
B 2 390  LEU 390  73   ?    ?   ?   B . n 
B 2 391  TYR 391  74   ?    ?   ?   B . n 
B 2 392  PHE 392  75   ?    ?   ?   B . n 
B 2 393  GLN 393  76   ?    ?   ?   B . n 
B 2 394  GLY 394  77   ?    ?   ?   B . n 
B 2 395  GLY 395  78   ?    ?   ?   B . n 
B 2 396  SER 396  79   ?    ?   ?   B . n 
B 2 397  ASN 397  80   ?    ?   ?   B . n 
B 2 398  HIS 398  81   ?    ?   ?   B . n 
B 2 399  SER 399  82   ?    ?   ?   B . n 
B 2 400  PHE 400  83   ?    ?   ?   B . n 
B 2 401  GLU 401  84   ?    ?   ?   B . n 
B 2 402  GLU 402  85   ?    ?   ?   B . n 
B 2 403  VAL 403  86   ?    ?   ?   B . n 
B 2 404  VAL 404  87   ?    ?   ?   B . n 
B 2 405  GLN 405  88   ?    ?   ?   B . n 
B 2 406  THR 406  89   ?    ?   ?   B . n 
B 2 407  LEU 407  90   ?    ?   ?   B . n 
B 2 408  ALA 408  91   ?    ?   ?   B . n 
B 2 409  SER 409  92   ?    ?   ?   B . n 
B 2 410  LEU 410  93   ?    ?   ?   B . n 
B 2 411  ALA 411  94   ?    ?   ?   B . n 
B 2 412  THR 412  95   ?    ?   ?   B . n 
B 2 413  VAL 413  96   ?    ?   ?   B . n 
B 2 414  VAL 414  97   ?    ?   ?   B . n 
B 2 415  GLN 415  98   ?    ?   ?   B . n 
B 2 416  GLN 416  99   ?    ?   ?   B . n 
B 2 417  GLN 417  100  ?    ?   ?   B . n 
B 2 418  THR 418  101  ?    ?   ?   B . n 
B 2 419  ILE 419  102  ?    ?   ?   B . n 
B 2 420  ALA 420  103  ?    ?   ?   B . n 
B 2 421  SER 421  104  ?    ?   ?   B . n 
B 2 422  GLU 422  105  ?    ?   ?   B . n 
B 2 423  SER 423  106  ?    ?   ?   B . n 
B 2 424  LEU 424  107  ?    ?   ?   B . n 
B 2 425  GLU 425  108  ?    ?   ?   B . n 
B 2 426  GLN 426  109  ?    ?   ?   B . n 
B 2 427  ARG 427  110  ?    ?   ?   B . n 
B 2 428  ILE 428  111  ?    ?   ?   B . n 
B 2 429  THR 429  112  ?    ?   ?   B . n 
B 2 430  SER 430  113  ?    ?   ?   B . n 
B 2 431  LEU 431  114  ?    ?   ?   B . n 
B 2 432  GLU 432  115  ?    ?   ?   B . n 
B 2 433  ASN 433  116  ?    ?   ?   B . n 
B 2 434  GLY 434  117  ?    ?   ?   B . n 
B 2 435  LEU 435  118  ?    ?   ?   B . n 
B 2 436  LYS 436  119  ?    ?   ?   B . n 
B 2 437  PRO 437  120  ?    ?   ?   B . n 
B 2 438  VAL 438  121  ?    ?   ?   B . n 
B 2 439  TYR 439  122  ?    ?   ?   B . n 
B 2 440  ASP 440  123  123  ASP ASP B . n 
B 2 441  MET 441  124  124  MET MET B . n 
B 2 442  ALA 442  125  125  ALA ALA B . n 
B 2 443  LYS 443  126  126  LYS LYS B . n 
B 2 444  THR 444  127  127  THR THR B . n 
B 2 445  ILE 445  128  128  ILE ILE B . n 
B 2 446  SER 446  129  129  SER SER B . n 
B 2 447  SER 447  130  130  SER SER B . n 
B 2 448  LEU 448  131  131  LEU LEU B . n 
B 2 449  ASN 449  132  132  ASN ASN B . n 
B 2 450  ARG 450  133  133  ARG ARG B . n 
B 2 451  VAL 451  134  134  VAL VAL B . n 
B 2 452  CYS 452  135  135  CYS CYS B . n 
B 2 453  ALA 453  136  136  ALA ALA B . n 
B 2 454  GLU 454  137  137  GLU GLU B . n 
B 2 455  MET 455  138  138  MET MET B . n 
B 2 456  VAL 456  139  139  VAL VAL B . n 
B 2 457  ALA 457  140  140  ALA ALA B . n 
B 2 458  LYS 458  141  141  LYS LYS B . n 
B 2 459  TYR 459  142  142  TYR TYR B . n 
B 2 460  ASP 460  143  143  ASP ASP B . n 
B 2 461  LEU 461  144  144  LEU LEU B . n 
B 2 462  LEU 462  145  145  LEU LEU B . n 
B 2 463  VAL 463  146  146  VAL VAL B . n 
B 2 464  MET 464  147  147  MET MET B . n 
B 2 465  THR 465  148  148  THR THR B . n 
B 2 466  THR 466  149  149  THR THR B . n 
B 2 467  GLY 467  150  150  GLY GLY B . n 
B 2 468  ARG 468  151  151  ARG ARG B . n 
B 2 469  ALA 469  152  152  ALA ALA B . n 
B 2 470  THR 470  153  153  THR THR B . n 
B 2 471  ALA 471  154  154  ALA ALA B . n 
B 2 472  THR 472  155  155  THR THR B . n 
B 2 473  ALA 473  156  156  ALA ALA B . n 
B 2 474  ALA 474  157  157  ALA ALA B . n 
B 2 475  ALA 475  158  158  ALA ALA B . n 
B 2 476  THR 476  159  159  THR THR B . n 
B 2 477  GLU 477  160  160  GLU GLU B . n 
B 2 478  ALA 478  161  161  ALA ALA B . n 
B 2 479  TYR 479  162  162  TYR TYR B . n 
B 2 480  TRP 480  163  163  TRP TRP B . n 
B 2 481  ALA 481  164  164  ALA ALA B . n 
B 2 482  GLU 482  165  165  GLU GLU B . n 
B 2 483  HIS 483  166  166  HIS HIS B . n 
B 2 484  GLY 484  167  167  GLY GLY B . n 
B 2 485  GLN 485  168  168  GLN GLN B . n 
B 2 486  PRO 486  169  169  PRO PRO B . n 
B 2 487  PRO 487  170  170  PRO PRO B . n 
B 2 488  PRO 488  171  171  PRO PRO B . n 
B 2 489  GLY 489  172  172  GLY GLY B . n 
B 2 490  PRO 490  173  173  PRO PRO B . n 
B 2 491  SER 491  174  174  SER SER B . n 
B 2 492  LEU 492  175  175  LEU LEU B . n 
B 2 493  TYR 493  176  176  TYR TYR B . n 
B 2 494  GLU 494  177  177  GLU GLU B . n 
B 2 495  GLU 495  178  178  GLU GLU B . n 
B 2 496  SER 496  179  179  SER SER B . n 
B 2 497  ALA 497  180  180  ALA ALA B . n 
B 2 498  ILE 498  181  181  ILE ILE B . n 
B 2 499  ARG 499  182  182  ARG ARG B . n 
B 2 500  GLY 500  183  183  GLY GLY B . n 
B 2 501  LYS 501  184  184  LYS LYS B . n 
B 2 502  ILE 502  185  185  ILE ILE B . n 
B 2 503  GLU 503  186  186  GLU GLU B . n 
B 2 504  SER 504  187  187  SER SER B . n 
B 2 505  ARG 505  188  188  ARG ARG B . n 
B 2 506  ASP 506  189  189  ASP ASP B . n 
B 2 507  GLU 507  190  190  GLU GLU B . n 
B 2 508  THR 508  191  191  THR THR B . n 
B 2 509  VAL 509  192  192  VAL VAL B . n 
B 2 510  PRO 510  193  193  PRO PRO B . n 
B 2 511  GLN 511  194  194  GLN GLN B . n 
B 2 512  SER 512  195  195  SER SER B . n 
B 2 513  VAL 513  196  196  VAL VAL B . n 
B 2 514  ARG 514  197  197  ARG ARG B . n 
B 2 515  GLU 515  198  198  GLU GLU B . n 
B 2 516  ALA 516  199  199  ALA ALA B . n 
B 2 517  PHE 517  200  200  PHE PHE B . n 
B 2 518  ASN 518  201  201  ASN ASN B . n 
B 2 519  ASN 519  202  202  ASN ASN B . n 
B 2 520  LEU 520  203  203  LEU LEU B . n 
B 2 521  ASN 521  204  204  ASN ASN B . n 
B 2 522  SER 522  205  205  SER SER B . n 
B 2 523  THR 523  206  206  THR THR B . n 
B 2 524  THR 524  207  207  THR THR B . n 
B 2 525  SER 525  208  208  SER SER B . n 
B 2 526  LEU 526  209  209  LEU LEU B . n 
B 2 527  THR 527  210  210  THR THR B . n 
B 2 528  GLU 528  211  211  GLU GLU B . n 
B 2 529  GLU 529  212  212  GLU GLU B . n 
B 2 530  ASN 530  213  213  ASN ASN B . n 
B 2 531  PHE 531  214  214  PHE PHE B . n 
B 2 532  GLY 532  215  215  GLY GLY B . n 
B 2 533  LYS 533  216  216  LYS LYS B . n 
B 2 534  PRO 534  217  217  PRO PRO B . n 
B 2 535  ASP 535  218  218  ASP ASP B . n 
B 2 536  ILE 536  219  219  ILE ILE B . n 
B 2 537  SER 537  220  220  SER SER B . n 
B 2 538  ALA 538  221  221  ALA ALA B . n 
B 2 539  LYS 539  222  222  LYS LYS B . n 
B 2 540  ASP 540  223  223  ASP ASP B . n 
B 2 541  LEU 541  224  224  LEU LEU B . n 
B 2 542  ARG 542  225  225  ARG ARG B . n 
B 2 543  ASN 543  226  226  ASN ASN B . n 
B 2 544  ILE 544  227  227  ILE ILE B . n 
B 2 545  MET 545  228  228  MET MET B . n 
B 2 546  TYR 546  229  229  TYR TYR B . n 
B 2 547  ASP 547  230  230  ASP ASP B . n 
B 2 548  HIS 548  231  231  HIS HIS B . n 
B 2 549  LEU 549  232  232  LEU LEU B . n 
B 2 550  PRO 550  233  233  PRO PRO B . n 
B 2 551  GLY 551  234  234  GLY GLY B . n 
B 2 552  PHE 552  235  235  PHE PHE B . n 
B 2 553  GLY 553  236  236  GLY GLY B . n 
B 2 554  THR 554  237  237  THR THR B . n 
B 2 555  ALA 555  238  238  ALA ALA B . n 
B 2 556  PHE 556  239  239  PHE PHE B . n 
B 2 557  HIS 557  240  240  HIS HIS B . n 
B 2 558  GLN 558  241  241  GLN GLN B . n 
B 2 559  LEU 559  242  242  LEU LEU B . n 
B 2 560  VAL 560  243  243  VAL VAL B . n 
B 2 561  GLN 561  244  244  GLN GLN B . n 
B 2 562  VAL 562  245  245  VAL VAL B . n 
B 2 563  ILE 563  246  246  ILE ILE B . n 
B 2 564  CYS 564  247  247  CYS CYS B . n 
B 2 565  LYS 565  248  248  LYS LYS B . n 
B 2 566  LEU 566  249  249  LEU LEU B . n 
B 2 567  GLY 567  250  250  GLY GLY B . n 
B 2 568  LYS 568  251  251  LYS LYS B . n 
B 2 569  ASP 569  252  252  ASP ASP B . n 
B 2 570  SER 570  253  253  SER SER B . n 
B 2 571  ASN 571  254  254  ASN ASN B . n 
B 2 572  SER 572  255  255  SER SER B . n 
B 2 573  LEU 573  256  256  LEU LEU B . n 
B 2 574  ASP 574  257  257  ASP ASP B . n 
B 2 575  ILE 575  258  258  ILE ILE B . n 
B 2 576  ILE 576  259  259  ILE ILE B . n 
B 2 577  HIS 577  260  260  HIS HIS B . n 
B 2 578  ALA 578  261  261  ALA ALA B . n 
B 2 579  GLU 579  262  262  GLU GLU B . n 
B 2 580  PHE 580  263  263  PHE PHE B . n 
B 2 581  GLN 581  264  264  GLN GLN B . n 
B 2 582  ALA 582  265  265  ALA ALA B . n 
B 2 583  SER 583  266  266  SER SER B . n 
B 2 584  LEU 584  267  267  LEU LEU B . n 
B 2 585  ALA 585  268  268  ALA ALA B . n 
B 2 586  GLU 586  269  269  GLU GLU B . n 
B 2 587  GLY 587  270  270  GLY GLY B . n 
B 2 588  ASP 588  271  271  ASP ASP B . n 
B 2 589  SER 589  272  272  SER SER B . n 
B 2 590  PRO 590  273  273  PRO PRO B . n 
B 2 591  GLN 591  274  274  GLN GLN B . n 
B 2 592  CYS 592  275  275  CYS CYS B . n 
B 2 593  ALA 593  276  276  ALA ALA B . n 
B 2 594  LEU 594  277  277  LEU LEU B . n 
B 2 595  ILE 595  278  278  ILE ILE B . n 
B 2 596  GLN 596  279  279  GLN GLN B . n 
B 2 597  ILE 597  280  280  ILE ILE B . n 
B 2 598  THR 598  281  281  THR THR B . n 
B 2 599  LYS 599  282  282  LYS LYS B . n 
B 2 600  ARG 600  283  283  ARG ARG B . n 
B 2 601  VAL 601  284  284  VAL VAL B . n 
B 2 602  PRO 602  285  285  PRO PRO B . n 
B 2 603  ILE 603  286  286  ILE ILE B . n 
B 2 604  PHE 604  287  287  PHE PHE B . n 
B 2 605  GLN 605  288  288  GLN GLN B . n 
B 2 606  ASP 606  289  289  ASP ASP B . n 
B 2 607  ALA 607  290  290  ALA ALA B . n 
B 2 608  ALA 608  291  291  ALA ALA B . n 
B 2 609  PRO 609  292  292  PRO PRO B . n 
B 2 610  PRO 610  293  293  PRO PRO B . n 
B 2 611  VAL 611  294  294  VAL VAL B . n 
B 2 612  ILE 612  295  295  ILE ILE B . n 
B 2 613  HIS 613  296  296  HIS HIS B . n 
B 2 614  ILE 614  297  297  ILE ILE B . n 
B 2 615  ARG 615  298  298  ARG ARG B . n 
B 2 616  SER 616  299  299  SER SER B . n 
B 2 617  ARG 617  300  300  ARG ARG B . n 
B 2 618  GLY 618  301  301  GLY GLY B . n 
B 2 619  ASP 619  302  302  ASP ASP B . n 
B 2 620  ILE 620  303  303  ILE ILE B . n 
B 2 621  PRO 621  304  304  PRO PRO B . n 
B 2 622  ARG 622  305  305  ARG ARG B . n 
B 2 623  ALA 623  306  306  ALA ALA B . n 
B 2 624  CYS 624  307  307  CYS CYS B . n 
B 2 625  GLN 625  308  308  GLN GLN B . n 
B 2 626  LYS 626  309  309  LYS LYS B . n 
B 2 627  SER 627  310  310  SER SER B . n 
B 2 628  LEU 628  311  311  LEU LEU B . n 
B 2 629  ARG 629  312  312  ARG ARG B . n 
B 2 630  PRO 630  313  313  PRO PRO B . n 
B 2 631  VAL 631  314  314  VAL VAL B . n 
B 2 632  PRO 632  315  315  PRO PRO B . n 
B 2 633  PRO 633  316  316  PRO PRO B . n 
B 2 634  SER 634  317  317  SER SER B . n 
B 2 635  PRO 635  318  318  PRO PRO B . n 
B 2 636  LYS 636  319  319  LYS LYS B . n 
B 2 637  ILE 637  320  320  ILE ILE B . n 
B 2 638  ASP 638  321  321  ASP ASP B . n 
B 2 639  ARG 639  322  322  ARG ARG B . n 
B 2 640  GLY 640  323  323  GLY GLY B . n 
B 2 641  TRP 641  324  324  TRP TRP B . n 
B 2 642  VAL 642  325  325  VAL VAL B . n 
B 2 643  CYS 643  326  326  CYS CYS B . n 
B 2 644  VAL 644  327  327  VAL VAL B . n 
B 2 645  PHE 645  328  328  PHE PHE B . n 
B 2 646  GLN 646  329  329  GLN GLN B . n 
B 2 647  LEU 647  330  330  LEU LEU B . n 
B 2 648  GLN 648  331  331  GLN GLN B . n 
B 2 649  ASP 649  332  332  ASP ASP B . n 
B 2 650  GLY 650  333  333  GLY GLY B . n 
B 2 651  LYS 651  334  334  LYS LYS B . n 
B 2 652  THR 652  335  335  THR THR B . n 
B 2 653  LEU 653  336  336  LEU LEU B . n 
B 2 654  GLY 654  337  337  GLY GLY B . n 
B 2 655  LEU 655  338  338  LEU LEU B . n 
B 2 656  LYS 656  339  339  LYS LYS B . n 
B 2 657  ILE 657  340  340  ILE ILE B . n 
C 2 1    MET 1    -316 ?    ?   ?   C . n 
C 2 2    GLY 2    -315 ?    ?   ?   C . n 
C 2 3    SER 3    -314 ?    ?   ?   C . n 
C 2 4    SER 4    -313 ?    ?   ?   C . n 
C 2 5    HIS 5    -312 ?    ?   ?   C . n 
C 2 6    HIS 6    -311 ?    ?   ?   C . n 
C 2 7    HIS 7    -310 ?    ?   ?   C . n 
C 2 8    HIS 8    -309 ?    ?   ?   C . n 
C 2 9    HIS 9    -308 ?    ?   ?   C . n 
C 2 10   HIS 10   -307 ?    ?   ?   C . n 
C 2 11   GLY 11   -306 ?    ?   ?   C . n 
C 2 12   THR 12   -305 ?    ?   ?   C . n 
C 2 13   LYS 13   -304 ?    ?   ?   C . n 
C 2 14   THR 14   -303 ?    ?   ?   C . n 
C 2 15   GLU 15   -302 ?    ?   ?   C . n 
C 2 16   GLU 16   -301 ?    ?   ?   C . n 
C 2 17   GLY 17   -300 ?    ?   ?   C . n 
C 2 18   LYS 18   -299 ?    ?   ?   C . n 
C 2 19   LEU 19   -298 ?    ?   ?   C . n 
C 2 20   VAL 20   -297 ?    ?   ?   C . n 
C 2 21   ILE 21   -296 ?    ?   ?   C . n 
C 2 22   TRP 22   -295 ?    ?   ?   C . n 
C 2 23   ILE 23   -294 ?    ?   ?   C . n 
C 2 24   ASN 24   -293 ?    ?   ?   C . n 
C 2 25   GLY 25   -292 ?    ?   ?   C . n 
C 2 26   ASP 26   -291 ?    ?   ?   C . n 
C 2 27   LYS 27   -290 ?    ?   ?   C . n 
C 2 28   GLY 28   -289 ?    ?   ?   C . n 
C 2 29   TYR 29   -288 ?    ?   ?   C . n 
C 2 30   ASN 30   -287 ?    ?   ?   C . n 
C 2 31   GLY 31   -286 ?    ?   ?   C . n 
C 2 32   LEU 32   -285 ?    ?   ?   C . n 
C 2 33   ALA 33   -284 ?    ?   ?   C . n 
C 2 34   GLU 34   -283 ?    ?   ?   C . n 
C 2 35   VAL 35   -282 ?    ?   ?   C . n 
C 2 36   GLY 36   -281 ?    ?   ?   C . n 
C 2 37   LYS 37   -280 ?    ?   ?   C . n 
C 2 38   LYS 38   -279 ?    ?   ?   C . n 
C 2 39   PHE 39   -278 ?    ?   ?   C . n 
C 2 40   GLU 40   -277 ?    ?   ?   C . n 
C 2 41   LYS 41   -276 ?    ?   ?   C . n 
C 2 42   ASP 42   -275 ?    ?   ?   C . n 
C 2 43   THR 43   -274 ?    ?   ?   C . n 
C 2 44   GLY 44   -273 ?    ?   ?   C . n 
C 2 45   ILE 45   -272 ?    ?   ?   C . n 
C 2 46   LYS 46   -271 ?    ?   ?   C . n 
C 2 47   VAL 47   -270 ?    ?   ?   C . n 
C 2 48   THR 48   -269 ?    ?   ?   C . n 
C 2 49   VAL 49   -268 ?    ?   ?   C . n 
C 2 50   GLU 50   -267 ?    ?   ?   C . n 
C 2 51   HIS 51   -266 ?    ?   ?   C . n 
C 2 52   PRO 52   -265 ?    ?   ?   C . n 
C 2 53   ASP 53   -264 ?    ?   ?   C . n 
C 2 54   LYS 54   -263 ?    ?   ?   C . n 
C 2 55   LEU 55   -262 ?    ?   ?   C . n 
C 2 56   GLU 56   -261 ?    ?   ?   C . n 
C 2 57   GLU 57   -260 ?    ?   ?   C . n 
C 2 58   LYS 58   -259 ?    ?   ?   C . n 
C 2 59   PHE 59   -258 ?    ?   ?   C . n 
C 2 60   PRO 60   -257 ?    ?   ?   C . n 
C 2 61   GLN 61   -256 ?    ?   ?   C . n 
C 2 62   VAL 62   -255 ?    ?   ?   C . n 
C 2 63   ALA 63   -254 ?    ?   ?   C . n 
C 2 64   ALA 64   -253 ?    ?   ?   C . n 
C 2 65   THR 65   -252 ?    ?   ?   C . n 
C 2 66   GLY 66   -251 ?    ?   ?   C . n 
C 2 67   ASP 67   -250 ?    ?   ?   C . n 
C 2 68   GLY 68   -249 ?    ?   ?   C . n 
C 2 69   PRO 69   -248 ?    ?   ?   C . n 
C 2 70   ASP 70   -247 ?    ?   ?   C . n 
C 2 71   ILE 71   -246 ?    ?   ?   C . n 
C 2 72   ILE 72   -245 ?    ?   ?   C . n 
C 2 73   PHE 73   -244 ?    ?   ?   C . n 
C 2 74   TRP 74   -243 ?    ?   ?   C . n 
C 2 75   ALA 75   -242 ?    ?   ?   C . n 
C 2 76   HIS 76   -241 ?    ?   ?   C . n 
C 2 77   ASP 77   -240 ?    ?   ?   C . n 
C 2 78   ARG 78   -239 ?    ?   ?   C . n 
C 2 79   PHE 79   -238 ?    ?   ?   C . n 
C 2 80   GLY 80   -237 ?    ?   ?   C . n 
C 2 81   GLY 81   -236 ?    ?   ?   C . n 
C 2 82   TYR 82   -235 ?    ?   ?   C . n 
C 2 83   ALA 83   -234 ?    ?   ?   C . n 
C 2 84   GLN 84   -233 ?    ?   ?   C . n 
C 2 85   SER 85   -232 ?    ?   ?   C . n 
C 2 86   GLY 86   -231 ?    ?   ?   C . n 
C 2 87   LEU 87   -230 ?    ?   ?   C . n 
C 2 88   LEU 88   -229 ?    ?   ?   C . n 
C 2 89   ALA 89   -228 ?    ?   ?   C . n 
C 2 90   GLU 90   -227 ?    ?   ?   C . n 
C 2 91   ILE 91   -226 ?    ?   ?   C . n 
C 2 92   THR 92   -225 ?    ?   ?   C . n 
C 2 93   PRO 93   -224 ?    ?   ?   C . n 
C 2 94   ASP 94   -223 ?    ?   ?   C . n 
C 2 95   LYS 95   -222 ?    ?   ?   C . n 
C 2 96   ALA 96   -221 ?    ?   ?   C . n 
C 2 97   PHE 97   -220 ?    ?   ?   C . n 
C 2 98   GLN 98   -219 ?    ?   ?   C . n 
C 2 99   ASP 99   -218 ?    ?   ?   C . n 
C 2 100  LYS 100  -217 ?    ?   ?   C . n 
C 2 101  LEU 101  -216 ?    ?   ?   C . n 
C 2 102  TYR 102  -215 ?    ?   ?   C . n 
C 2 103  PRO 103  -214 ?    ?   ?   C . n 
C 2 104  PHE 104  -213 ?    ?   ?   C . n 
C 2 105  THR 105  -212 ?    ?   ?   C . n 
C 2 106  TRP 106  -211 ?    ?   ?   C . n 
C 2 107  ASP 107  -210 ?    ?   ?   C . n 
C 2 108  ALA 108  -209 ?    ?   ?   C . n 
C 2 109  VAL 109  -208 ?    ?   ?   C . n 
C 2 110  ARG 110  -207 ?    ?   ?   C . n 
C 2 111  TYR 111  -206 ?    ?   ?   C . n 
C 2 112  ASN 112  -205 ?    ?   ?   C . n 
C 2 113  GLY 113  -204 ?    ?   ?   C . n 
C 2 114  LYS 114  -203 ?    ?   ?   C . n 
C 2 115  LEU 115  -202 ?    ?   ?   C . n 
C 2 116  ILE 116  -201 ?    ?   ?   C . n 
C 2 117  ALA 117  -200 ?    ?   ?   C . n 
C 2 118  TYR 118  -199 ?    ?   ?   C . n 
C 2 119  PRO 119  -198 ?    ?   ?   C . n 
C 2 120  ILE 120  -197 ?    ?   ?   C . n 
C 2 121  ALA 121  -196 ?    ?   ?   C . n 
C 2 122  VAL 122  -195 ?    ?   ?   C . n 
C 2 123  GLU 123  -194 ?    ?   ?   C . n 
C 2 124  ALA 124  -193 ?    ?   ?   C . n 
C 2 125  LEU 125  -192 ?    ?   ?   C . n 
C 2 126  SER 126  -191 ?    ?   ?   C . n 
C 2 127  LEU 127  -190 ?    ?   ?   C . n 
C 2 128  ILE 128  -189 ?    ?   ?   C . n 
C 2 129  TYR 129  -188 ?    ?   ?   C . n 
C 2 130  ASN 130  -187 ?    ?   ?   C . n 
C 2 131  LYS 131  -186 ?    ?   ?   C . n 
C 2 132  ASP 132  -185 ?    ?   ?   C . n 
C 2 133  LEU 133  -184 ?    ?   ?   C . n 
C 2 134  LEU 134  -183 ?    ?   ?   C . n 
C 2 135  PRO 135  -182 ?    ?   ?   C . n 
C 2 136  ASN 136  -181 ?    ?   ?   C . n 
C 2 137  PRO 137  -180 ?    ?   ?   C . n 
C 2 138  PRO 138  -179 ?    ?   ?   C . n 
C 2 139  LYS 139  -178 ?    ?   ?   C . n 
C 2 140  THR 140  -177 ?    ?   ?   C . n 
C 2 141  TRP 141  -176 ?    ?   ?   C . n 
C 2 142  GLU 142  -175 ?    ?   ?   C . n 
C 2 143  GLU 143  -174 ?    ?   ?   C . n 
C 2 144  ILE 144  -173 ?    ?   ?   C . n 
C 2 145  PRO 145  -172 ?    ?   ?   C . n 
C 2 146  ALA 146  -171 ?    ?   ?   C . n 
C 2 147  LEU 147  -170 ?    ?   ?   C . n 
C 2 148  ASP 148  -169 ?    ?   ?   C . n 
C 2 149  LYS 149  -168 ?    ?   ?   C . n 
C 2 150  GLU 150  -167 ?    ?   ?   C . n 
C 2 151  LEU 151  -166 ?    ?   ?   C . n 
C 2 152  LYS 152  -165 ?    ?   ?   C . n 
C 2 153  ALA 153  -164 ?    ?   ?   C . n 
C 2 154  LYS 154  -163 ?    ?   ?   C . n 
C 2 155  GLY 155  -162 ?    ?   ?   C . n 
C 2 156  LYS 156  -161 ?    ?   ?   C . n 
C 2 157  SER 157  -160 ?    ?   ?   C . n 
C 2 158  ALA 158  -159 ?    ?   ?   C . n 
C 2 159  LEU 159  -158 ?    ?   ?   C . n 
C 2 160  MET 160  -157 ?    ?   ?   C . n 
C 2 161  PHE 161  -156 ?    ?   ?   C . n 
C 2 162  ASN 162  -155 ?    ?   ?   C . n 
C 2 163  LEU 163  -154 ?    ?   ?   C . n 
C 2 164  GLN 164  -153 ?    ?   ?   C . n 
C 2 165  GLU 165  -152 ?    ?   ?   C . n 
C 2 166  PRO 166  -151 ?    ?   ?   C . n 
C 2 167  TYR 167  -150 ?    ?   ?   C . n 
C 2 168  PHE 168  -149 ?    ?   ?   C . n 
C 2 169  THR 169  -148 ?    ?   ?   C . n 
C 2 170  TRP 170  -147 ?    ?   ?   C . n 
C 2 171  PRO 171  -146 ?    ?   ?   C . n 
C 2 172  LEU 172  -145 ?    ?   ?   C . n 
C 2 173  ILE 173  -144 ?    ?   ?   C . n 
C 2 174  ALA 174  -143 ?    ?   ?   C . n 
C 2 175  ALA 175  -142 ?    ?   ?   C . n 
C 2 176  ASP 176  -141 ?    ?   ?   C . n 
C 2 177  GLY 177  -140 ?    ?   ?   C . n 
C 2 178  GLY 178  -139 ?    ?   ?   C . n 
C 2 179  TYR 179  -138 ?    ?   ?   C . n 
C 2 180  ALA 180  -137 ?    ?   ?   C . n 
C 2 181  PHE 181  -136 ?    ?   ?   C . n 
C 2 182  LYS 182  -135 ?    ?   ?   C . n 
C 2 183  TYR 183  -134 ?    ?   ?   C . n 
C 2 184  GLU 184  -133 ?    ?   ?   C . n 
C 2 185  ASN 185  -132 ?    ?   ?   C . n 
C 2 186  GLY 186  -131 ?    ?   ?   C . n 
C 2 187  LYS 187  -130 ?    ?   ?   C . n 
C 2 188  TYR 188  -129 ?    ?   ?   C . n 
C 2 189  ASP 189  -128 ?    ?   ?   C . n 
C 2 190  ILE 190  -127 ?    ?   ?   C . n 
C 2 191  LYS 191  -126 ?    ?   ?   C . n 
C 2 192  ASP 192  -125 ?    ?   ?   C . n 
C 2 193  VAL 193  -124 ?    ?   ?   C . n 
C 2 194  GLY 194  -123 ?    ?   ?   C . n 
C 2 195  VAL 195  -122 ?    ?   ?   C . n 
C 2 196  ASP 196  -121 ?    ?   ?   C . n 
C 2 197  ASN 197  -120 ?    ?   ?   C . n 
C 2 198  ALA 198  -119 ?    ?   ?   C . n 
C 2 199  GLY 199  -118 ?    ?   ?   C . n 
C 2 200  ALA 200  -117 ?    ?   ?   C . n 
C 2 201  LYS 201  -116 ?    ?   ?   C . n 
C 2 202  ALA 202  -115 ?    ?   ?   C . n 
C 2 203  GLY 203  -114 ?    ?   ?   C . n 
C 2 204  LEU 204  -113 ?    ?   ?   C . n 
C 2 205  THR 205  -112 ?    ?   ?   C . n 
C 2 206  PHE 206  -111 ?    ?   ?   C . n 
C 2 207  LEU 207  -110 ?    ?   ?   C . n 
C 2 208  VAL 208  -109 ?    ?   ?   C . n 
C 2 209  ASP 209  -108 ?    ?   ?   C . n 
C 2 210  LEU 210  -107 ?    ?   ?   C . n 
C 2 211  ILE 211  -106 ?    ?   ?   C . n 
C 2 212  LYS 212  -105 ?    ?   ?   C . n 
C 2 213  ASN 213  -104 ?    ?   ?   C . n 
C 2 214  LYS 214  -103 ?    ?   ?   C . n 
C 2 215  HIS 215  -102 ?    ?   ?   C . n 
C 2 216  MET 216  -101 ?    ?   ?   C . n 
C 2 217  ASN 217  -100 ?    ?   ?   C . n 
C 2 218  ALA 218  -99  ?    ?   ?   C . n 
C 2 219  ASP 219  -98  ?    ?   ?   C . n 
C 2 220  THR 220  -97  ?    ?   ?   C . n 
C 2 221  ASP 221  -96  ?    ?   ?   C . n 
C 2 222  TYR 222  -95  ?    ?   ?   C . n 
C 2 223  SER 223  -94  ?    ?   ?   C . n 
C 2 224  ILE 224  -93  ?    ?   ?   C . n 
C 2 225  ALA 225  -92  ?    ?   ?   C . n 
C 2 226  GLU 226  -91  ?    ?   ?   C . n 
C 2 227  ALA 227  -90  ?    ?   ?   C . n 
C 2 228  ALA 228  -89  ?    ?   ?   C . n 
C 2 229  PHE 229  -88  ?    ?   ?   C . n 
C 2 230  ASN 230  -87  ?    ?   ?   C . n 
C 2 231  LYS 231  -86  ?    ?   ?   C . n 
C 2 232  GLY 232  -85  ?    ?   ?   C . n 
C 2 233  GLU 233  -84  ?    ?   ?   C . n 
C 2 234  THR 234  -83  ?    ?   ?   C . n 
C 2 235  ALA 235  -82  ?    ?   ?   C . n 
C 2 236  MET 236  -81  ?    ?   ?   C . n 
C 2 237  THR 237  -80  ?    ?   ?   C . n 
C 2 238  ILE 238  -79  ?    ?   ?   C . n 
C 2 239  ASN 239  -78  ?    ?   ?   C . n 
C 2 240  GLY 240  -77  ?    ?   ?   C . n 
C 2 241  PRO 241  -76  ?    ?   ?   C . n 
C 2 242  TRP 242  -75  ?    ?   ?   C . n 
C 2 243  ALA 243  -74  ?    ?   ?   C . n 
C 2 244  TRP 244  -73  ?    ?   ?   C . n 
C 2 245  SER 245  -72  ?    ?   ?   C . n 
C 2 246  ASN 246  -71  ?    ?   ?   C . n 
C 2 247  ILE 247  -70  ?    ?   ?   C . n 
C 2 248  ASP 248  -69  ?    ?   ?   C . n 
C 2 249  THR 249  -68  ?    ?   ?   C . n 
C 2 250  SER 250  -67  ?    ?   ?   C . n 
C 2 251  LYS 251  -66  ?    ?   ?   C . n 
C 2 252  VAL 252  -65  ?    ?   ?   C . n 
C 2 253  ASN 253  -64  ?    ?   ?   C . n 
C 2 254  TYR 254  -63  ?    ?   ?   C . n 
C 2 255  GLY 255  -62  ?    ?   ?   C . n 
C 2 256  VAL 256  -61  ?    ?   ?   C . n 
C 2 257  THR 257  -60  ?    ?   ?   C . n 
C 2 258  VAL 258  -59  ?    ?   ?   C . n 
C 2 259  LEU 259  -58  ?    ?   ?   C . n 
C 2 260  PRO 260  -57  ?    ?   ?   C . n 
C 2 261  THR 261  -56  ?    ?   ?   C . n 
C 2 262  PHE 262  -55  ?    ?   ?   C . n 
C 2 263  LYS 263  -54  ?    ?   ?   C . n 
C 2 264  GLY 264  -53  ?    ?   ?   C . n 
C 2 265  GLN 265  -52  ?    ?   ?   C . n 
C 2 266  PRO 266  -51  ?    ?   ?   C . n 
C 2 267  SER 267  -50  ?    ?   ?   C . n 
C 2 268  LYS 268  -49  ?    ?   ?   C . n 
C 2 269  PRO 269  -48  ?    ?   ?   C . n 
C 2 270  PHE 270  -47  ?    ?   ?   C . n 
C 2 271  VAL 271  -46  ?    ?   ?   C . n 
C 2 272  GLY 272  -45  ?    ?   ?   C . n 
C 2 273  VAL 273  -44  ?    ?   ?   C . n 
C 2 274  LEU 274  -43  ?    ?   ?   C . n 
C 2 275  SER 275  -42  ?    ?   ?   C . n 
C 2 276  ALA 276  -41  ?    ?   ?   C . n 
C 2 277  GLY 277  -40  ?    ?   ?   C . n 
C 2 278  ILE 278  -39  ?    ?   ?   C . n 
C 2 279  ASN 279  -38  ?    ?   ?   C . n 
C 2 280  ALA 280  -37  ?    ?   ?   C . n 
C 2 281  ALA 281  -36  ?    ?   ?   C . n 
C 2 282  SER 282  -35  ?    ?   ?   C . n 
C 2 283  PRO 283  -34  ?    ?   ?   C . n 
C 2 284  ASN 284  -33  ?    ?   ?   C . n 
C 2 285  LYS 285  -32  ?    ?   ?   C . n 
C 2 286  GLU 286  -31  ?    ?   ?   C . n 
C 2 287  LEU 287  -30  ?    ?   ?   C . n 
C 2 288  ALA 288  -29  ?    ?   ?   C . n 
C 2 289  LYS 289  -28  ?    ?   ?   C . n 
C 2 290  GLU 290  -27  ?    ?   ?   C . n 
C 2 291  PHE 291  -26  ?    ?   ?   C . n 
C 2 292  LEU 292  -25  ?    ?   ?   C . n 
C 2 293  GLU 293  -24  ?    ?   ?   C . n 
C 2 294  ASN 294  -23  ?    ?   ?   C . n 
C 2 295  TYR 295  -22  ?    ?   ?   C . n 
C 2 296  LEU 296  -21  ?    ?   ?   C . n 
C 2 297  LEU 297  -20  ?    ?   ?   C . n 
C 2 298  THR 298  -19  ?    ?   ?   C . n 
C 2 299  ASP 299  -18  ?    ?   ?   C . n 
C 2 300  GLU 300  -17  ?    ?   ?   C . n 
C 2 301  GLY 301  -16  ?    ?   ?   C . n 
C 2 302  LEU 302  -15  ?    ?   ?   C . n 
C 2 303  GLU 303  -14  ?    ?   ?   C . n 
C 2 304  ALA 304  -13  ?    ?   ?   C . n 
C 2 305  VAL 305  -12  ?    ?   ?   C . n 
C 2 306  ASN 306  -11  ?    ?   ?   C . n 
C 2 307  LYS 307  -10  ?    ?   ?   C . n 
C 2 308  ASP 308  -9   ?    ?   ?   C . n 
C 2 309  LYS 309  -8   ?    ?   ?   C . n 
C 2 310  PRO 310  -7   ?    ?   ?   C . n 
C 2 311  LEU 311  -6   ?    ?   ?   C . n 
C 2 312  GLY 312  -5   ?    ?   ?   C . n 
C 2 313  ALA 313  -4   ?    ?   ?   C . n 
C 2 314  VAL 314  -3   ?    ?   ?   C . n 
C 2 315  ALA 315  -2   ?    ?   ?   C . n 
C 2 316  LEU 316  -1   ?    ?   ?   C . n 
C 2 317  LYS 317  0    ?    ?   ?   C . n 
C 2 318  SER 318  1    ?    ?   ?   C . n 
C 2 319  TYR 319  2    ?    ?   ?   C . n 
C 2 320  GLU 320  3    ?    ?   ?   C . n 
C 2 321  GLU 321  4    ?    ?   ?   C . n 
C 2 322  GLU 322  5    ?    ?   ?   C . n 
C 2 323  LEU 323  6    ?    ?   ?   C . n 
C 2 324  ALA 324  7    ?    ?   ?   C . n 
C 2 325  LYS 325  8    ?    ?   ?   C . n 
C 2 326  ASP 326  9    ?    ?   ?   C . n 
C 2 327  PRO 327  10   ?    ?   ?   C . n 
C 2 328  ARG 328  11   ?    ?   ?   C . n 
C 2 329  ILE 329  12   ?    ?   ?   C . n 
C 2 330  ALA 330  13   ?    ?   ?   C . n 
C 2 331  ALA 331  14   ?    ?   ?   C . n 
C 2 332  THR 332  15   ?    ?   ?   C . n 
C 2 333  MET 333  16   ?    ?   ?   C . n 
C 2 334  GLU 334  17   ?    ?   ?   C . n 
C 2 335  ASN 335  18   ?    ?   ?   C . n 
C 2 336  ALA 336  19   ?    ?   ?   C . n 
C 2 337  GLN 337  20   ?    ?   ?   C . n 
C 2 338  LYS 338  21   ?    ?   ?   C . n 
C 2 339  GLY 339  22   ?    ?   ?   C . n 
C 2 340  GLU 340  23   ?    ?   ?   C . n 
C 2 341  ILE 341  24   ?    ?   ?   C . n 
C 2 342  MET 342  25   ?    ?   ?   C . n 
C 2 343  PRO 343  26   ?    ?   ?   C . n 
C 2 344  ASN 344  27   ?    ?   ?   C . n 
C 2 345  ILE 345  28   ?    ?   ?   C . n 
C 2 346  PRO 346  29   ?    ?   ?   C . n 
C 2 347  GLN 347  30   ?    ?   ?   C . n 
C 2 348  MET 348  31   ?    ?   ?   C . n 
C 2 349  SER 349  32   ?    ?   ?   C . n 
C 2 350  ALA 350  33   ?    ?   ?   C . n 
C 2 351  PHE 351  34   ?    ?   ?   C . n 
C 2 352  TRP 352  35   ?    ?   ?   C . n 
C 2 353  TYR 353  36   ?    ?   ?   C . n 
C 2 354  ALA 354  37   ?    ?   ?   C . n 
C 2 355  VAL 355  38   ?    ?   ?   C . n 
C 2 356  ARG 356  39   ?    ?   ?   C . n 
C 2 357  THR 357  40   ?    ?   ?   C . n 
C 2 358  ALA 358  41   ?    ?   ?   C . n 
C 2 359  VAL 359  42   ?    ?   ?   C . n 
C 2 360  ILE 360  43   ?    ?   ?   C . n 
C 2 361  ASN 361  44   ?    ?   ?   C . n 
C 2 362  ALA 362  45   ?    ?   ?   C . n 
C 2 363  ALA 363  46   ?    ?   ?   C . n 
C 2 364  SER 364  47   ?    ?   ?   C . n 
C 2 365  GLY 365  48   ?    ?   ?   C . n 
C 2 366  ARG 366  49   ?    ?   ?   C . n 
C 2 367  GLN 367  50   ?    ?   ?   C . n 
C 2 368  THR 368  51   ?    ?   ?   C . n 
C 2 369  VAL 369  52   ?    ?   ?   C . n 
C 2 370  ASP 370  53   ?    ?   ?   C . n 
C 2 371  GLU 371  54   ?    ?   ?   C . n 
C 2 372  ALA 372  55   ?    ?   ?   C . n 
C 2 373  LEU 373  56   ?    ?   ?   C . n 
C 2 374  LYS 374  57   ?    ?   ?   C . n 
C 2 375  ASP 375  58   ?    ?   ?   C . n 
C 2 376  ALA 376  59   ?    ?   ?   C . n 
C 2 377  GLN 377  60   ?    ?   ?   C . n 
C 2 378  THR 378  61   ?    ?   ?   C . n 
C 2 379  GLY 379  62   ?    ?   ?   C . n 
C 2 380  THR 380  63   ?    ?   ?   C . n 
C 2 381  ASP 381  64   ?    ?   ?   C . n 
C 2 382  TYR 382  65   ?    ?   ?   C . n 
C 2 383  ASP 383  66   ?    ?   ?   C . n 
C 2 384  ILE 384  67   ?    ?   ?   C . n 
C 2 385  PRO 385  68   ?    ?   ?   C . n 
C 2 386  THR 386  69   ?    ?   ?   C . n 
C 2 387  THR 387  70   ?    ?   ?   C . n 
C 2 388  GLU 388  71   ?    ?   ?   C . n 
C 2 389  ASN 389  72   ?    ?   ?   C . n 
C 2 390  LEU 390  73   ?    ?   ?   C . n 
C 2 391  TYR 391  74   ?    ?   ?   C . n 
C 2 392  PHE 392  75   ?    ?   ?   C . n 
C 2 393  GLN 393  76   ?    ?   ?   C . n 
C 2 394  GLY 394  77   ?    ?   ?   C . n 
C 2 395  GLY 395  78   ?    ?   ?   C . n 
C 2 396  SER 396  79   ?    ?   ?   C . n 
C 2 397  ASN 397  80   ?    ?   ?   C . n 
C 2 398  HIS 398  81   ?    ?   ?   C . n 
C 2 399  SER 399  82   ?    ?   ?   C . n 
C 2 400  PHE 400  83   ?    ?   ?   C . n 
C 2 401  GLU 401  84   ?    ?   ?   C . n 
C 2 402  GLU 402  85   ?    ?   ?   C . n 
C 2 403  VAL 403  86   ?    ?   ?   C . n 
C 2 404  VAL 404  87   ?    ?   ?   C . n 
C 2 405  GLN 405  88   ?    ?   ?   C . n 
C 2 406  THR 406  89   ?    ?   ?   C . n 
C 2 407  LEU 407  90   ?    ?   ?   C . n 
C 2 408  ALA 408  91   ?    ?   ?   C . n 
C 2 409  SER 409  92   ?    ?   ?   C . n 
C 2 410  LEU 410  93   ?    ?   ?   C . n 
C 2 411  ALA 411  94   ?    ?   ?   C . n 
C 2 412  THR 412  95   ?    ?   ?   C . n 
C 2 413  VAL 413  96   ?    ?   ?   C . n 
C 2 414  VAL 414  97   ?    ?   ?   C . n 
C 2 415  GLN 415  98   ?    ?   ?   C . n 
C 2 416  GLN 416  99   ?    ?   ?   C . n 
C 2 417  GLN 417  100  ?    ?   ?   C . n 
C 2 418  THR 418  101  ?    ?   ?   C . n 
C 2 419  ILE 419  102  ?    ?   ?   C . n 
C 2 420  ALA 420  103  ?    ?   ?   C . n 
C 2 421  SER 421  104  ?    ?   ?   C . n 
C 2 422  GLU 422  105  ?    ?   ?   C . n 
C 2 423  SER 423  106  ?    ?   ?   C . n 
C 2 424  LEU 424  107  ?    ?   ?   C . n 
C 2 425  GLU 425  108  ?    ?   ?   C . n 
C 2 426  GLN 426  109  ?    ?   ?   C . n 
C 2 427  ARG 427  110  ?    ?   ?   C . n 
C 2 428  ILE 428  111  ?    ?   ?   C . n 
C 2 429  THR 429  112  ?    ?   ?   C . n 
C 2 430  SER 430  113  ?    ?   ?   C . n 
C 2 431  LEU 431  114  ?    ?   ?   C . n 
C 2 432  GLU 432  115  ?    ?   ?   C . n 
C 2 433  ASN 433  116  ?    ?   ?   C . n 
C 2 434  GLY 434  117  ?    ?   ?   C . n 
C 2 435  LEU 435  118  ?    ?   ?   C . n 
C 2 436  LYS 436  119  ?    ?   ?   C . n 
C 2 437  PRO 437  120  ?    ?   ?   C . n 
C 2 438  VAL 438  121  ?    ?   ?   C . n 
C 2 439  TYR 439  122  ?    ?   ?   C . n 
C 2 440  ASP 440  123  ?    ?   ?   C . n 
C 2 441  MET 441  124  124  MET MET C . n 
C 2 442  ALA 442  125  125  ALA ALA C . n 
C 2 443  LYS 443  126  126  LYS LYS C . n 
C 2 444  THR 444  127  127  THR THR C . n 
C 2 445  ILE 445  128  128  ILE ILE C . n 
C 2 446  SER 446  129  129  SER SER C . n 
C 2 447  SER 447  130  130  SER SER C . n 
C 2 448  LEU 448  131  131  LEU LEU C . n 
C 2 449  ASN 449  132  132  ASN ASN C . n 
C 2 450  ARG 450  133  133  ARG ARG C . n 
C 2 451  VAL 451  134  134  VAL VAL C . n 
C 2 452  CYS 452  135  135  CYS CYS C . n 
C 2 453  ALA 453  136  136  ALA ALA C . n 
C 2 454  GLU 454  137  137  GLU GLU C . n 
C 2 455  MET 455  138  138  MET MET C . n 
C 2 456  VAL 456  139  139  VAL VAL C . n 
C 2 457  ALA 457  140  140  ALA ALA C . n 
C 2 458  LYS 458  141  141  LYS LYS C . n 
C 2 459  TYR 459  142  142  TYR TYR C . n 
C 2 460  ASP 460  143  143  ASP ASP C . n 
C 2 461  LEU 461  144  144  LEU LEU C . n 
C 2 462  LEU 462  145  145  LEU LEU C . n 
C 2 463  VAL 463  146  146  VAL VAL C . n 
C 2 464  MET 464  147  147  MET MET C . n 
C 2 465  THR 465  148  148  THR THR C . n 
C 2 466  THR 466  149  149  THR THR C . n 
C 2 467  GLY 467  150  150  GLY GLY C . n 
C 2 468  ARG 468  151  151  ARG ARG C . n 
C 2 469  ALA 469  152  152  ALA ALA C . n 
C 2 470  THR 470  153  153  THR THR C . n 
C 2 471  ALA 471  154  154  ALA ALA C . n 
C 2 472  THR 472  155  155  THR THR C . n 
C 2 473  ALA 473  156  156  ALA ALA C . n 
C 2 474  ALA 474  157  157  ALA ALA C . n 
C 2 475  ALA 475  158  158  ALA ALA C . n 
C 2 476  THR 476  159  159  THR THR C . n 
C 2 477  GLU 477  160  160  GLU GLU C . n 
C 2 478  ALA 478  161  161  ALA ALA C . n 
C 2 479  TYR 479  162  162  TYR TYR C . n 
C 2 480  TRP 480  163  163  TRP TRP C . n 
C 2 481  ALA 481  164  164  ALA ALA C . n 
C 2 482  GLU 482  165  165  GLU GLU C . n 
C 2 483  HIS 483  166  166  HIS HIS C . n 
C 2 484  GLY 484  167  167  GLY GLY C . n 
C 2 485  GLN 485  168  168  GLN GLN C . n 
C 2 486  PRO 486  169  169  PRO PRO C . n 
C 2 487  PRO 487  170  170  PRO PRO C . n 
C 2 488  PRO 488  171  171  PRO PRO C . n 
C 2 489  GLY 489  172  172  GLY GLY C . n 
C 2 490  PRO 490  173  173  PRO PRO C . n 
C 2 491  SER 491  174  174  SER SER C . n 
C 2 492  LEU 492  175  175  LEU LEU C . n 
C 2 493  TYR 493  176  176  TYR TYR C . n 
C 2 494  GLU 494  177  177  GLU GLU C . n 
C 2 495  GLU 495  178  178  GLU GLU C . n 
C 2 496  SER 496  179  179  SER SER C . n 
C 2 497  ALA 497  180  ?    ?   ?   C . n 
C 2 498  ILE 498  181  ?    ?   ?   C . n 
C 2 499  ARG 499  182  ?    ?   ?   C . n 
C 2 500  GLY 500  183  ?    ?   ?   C . n 
C 2 501  LYS 501  184  ?    ?   ?   C . n 
C 2 502  ILE 502  185  ?    ?   ?   C . n 
C 2 503  GLU 503  186  ?    ?   ?   C . n 
C 2 504  SER 504  187  ?    ?   ?   C . n 
C 2 505  ARG 505  188  ?    ?   ?   C . n 
C 2 506  ASP 506  189  ?    ?   ?   C . n 
C 2 507  GLU 507  190  ?    ?   ?   C . n 
C 2 508  THR 508  191  ?    ?   ?   C . n 
C 2 509  VAL 509  192  ?    ?   ?   C . n 
C 2 510  PRO 510  193  ?    ?   ?   C . n 
C 2 511  GLN 511  194  ?    ?   ?   C . n 
C 2 512  SER 512  195  ?    ?   ?   C . n 
C 2 513  VAL 513  196  ?    ?   ?   C . n 
C 2 514  ARG 514  197  ?    ?   ?   C . n 
C 2 515  GLU 515  198  ?    ?   ?   C . n 
C 2 516  ALA 516  199  ?    ?   ?   C . n 
C 2 517  PHE 517  200  ?    ?   ?   C . n 
C 2 518  ASN 518  201  ?    ?   ?   C . n 
C 2 519  ASN 519  202  ?    ?   ?   C . n 
C 2 520  LEU 520  203  ?    ?   ?   C . n 
C 2 521  ASN 521  204  ?    ?   ?   C . n 
C 2 522  SER 522  205  ?    ?   ?   C . n 
C 2 523  THR 523  206  ?    ?   ?   C . n 
C 2 524  THR 524  207  ?    ?   ?   C . n 
C 2 525  SER 525  208  ?    ?   ?   C . n 
C 2 526  LEU 526  209  ?    ?   ?   C . n 
C 2 527  THR 527  210  ?    ?   ?   C . n 
C 2 528  GLU 528  211  ?    ?   ?   C . n 
C 2 529  GLU 529  212  ?    ?   ?   C . n 
C 2 530  ASN 530  213  ?    ?   ?   C . n 
C 2 531  PHE 531  214  ?    ?   ?   C . n 
C 2 532  GLY 532  215  ?    ?   ?   C . n 
C 2 533  LYS 533  216  ?    ?   ?   C . n 
C 2 534  PRO 534  217  ?    ?   ?   C . n 
C 2 535  ASP 535  218  ?    ?   ?   C . n 
C 2 536  ILE 536  219  ?    ?   ?   C . n 
C 2 537  SER 537  220  ?    ?   ?   C . n 
C 2 538  ALA 538  221  ?    ?   ?   C . n 
C 2 539  LYS 539  222  ?    ?   ?   C . n 
C 2 540  ASP 540  223  ?    ?   ?   C . n 
C 2 541  LEU 541  224  ?    ?   ?   C . n 
C 2 542  ARG 542  225  ?    ?   ?   C . n 
C 2 543  ASN 543  226  ?    ?   ?   C . n 
C 2 544  ILE 544  227  ?    ?   ?   C . n 
C 2 545  MET 545  228  ?    ?   ?   C . n 
C 2 546  TYR 546  229  ?    ?   ?   C . n 
C 2 547  ASP 547  230  ?    ?   ?   C . n 
C 2 548  HIS 548  231  ?    ?   ?   C . n 
C 2 549  LEU 549  232  ?    ?   ?   C . n 
C 2 550  PRO 550  233  ?    ?   ?   C . n 
C 2 551  GLY 551  234  ?    ?   ?   C . n 
C 2 552  PHE 552  235  ?    ?   ?   C . n 
C 2 553  GLY 553  236  ?    ?   ?   C . n 
C 2 554  THR 554  237  ?    ?   ?   C . n 
C 2 555  ALA 555  238  ?    ?   ?   C . n 
C 2 556  PHE 556  239  ?    ?   ?   C . n 
C 2 557  HIS 557  240  ?    ?   ?   C . n 
C 2 558  GLN 558  241  ?    ?   ?   C . n 
C 2 559  LEU 559  242  ?    ?   ?   C . n 
C 2 560  VAL 560  243  ?    ?   ?   C . n 
C 2 561  GLN 561  244  ?    ?   ?   C . n 
C 2 562  VAL 562  245  ?    ?   ?   C . n 
C 2 563  ILE 563  246  ?    ?   ?   C . n 
C 2 564  CYS 564  247  ?    ?   ?   C . n 
C 2 565  LYS 565  248  ?    ?   ?   C . n 
C 2 566  LEU 566  249  ?    ?   ?   C . n 
C 2 567  GLY 567  250  ?    ?   ?   C . n 
C 2 568  LYS 568  251  ?    ?   ?   C . n 
C 2 569  ASP 569  252  ?    ?   ?   C . n 
C 2 570  SER 570  253  ?    ?   ?   C . n 
C 2 571  ASN 571  254  ?    ?   ?   C . n 
C 2 572  SER 572  255  ?    ?   ?   C . n 
C 2 573  LEU 573  256  ?    ?   ?   C . n 
C 2 574  ASP 574  257  ?    ?   ?   C . n 
C 2 575  ILE 575  258  ?    ?   ?   C . n 
C 2 576  ILE 576  259  ?    ?   ?   C . n 
C 2 577  HIS 577  260  ?    ?   ?   C . n 
C 2 578  ALA 578  261  ?    ?   ?   C . n 
C 2 579  GLU 579  262  ?    ?   ?   C . n 
C 2 580  PHE 580  263  ?    ?   ?   C . n 
C 2 581  GLN 581  264  ?    ?   ?   C . n 
C 2 582  ALA 582  265  ?    ?   ?   C . n 
C 2 583  SER 583  266  ?    ?   ?   C . n 
C 2 584  LEU 584  267  ?    ?   ?   C . n 
C 2 585  ALA 585  268  ?    ?   ?   C . n 
C 2 586  GLU 586  269  ?    ?   ?   C . n 
C 2 587  GLY 587  270  ?    ?   ?   C . n 
C 2 588  ASP 588  271  ?    ?   ?   C . n 
C 2 589  SER 589  272  ?    ?   ?   C . n 
C 2 590  PRO 590  273  ?    ?   ?   C . n 
C 2 591  GLN 591  274  ?    ?   ?   C . n 
C 2 592  CYS 592  275  ?    ?   ?   C . n 
C 2 593  ALA 593  276  ?    ?   ?   C . n 
C 2 594  LEU 594  277  ?    ?   ?   C . n 
C 2 595  ILE 595  278  ?    ?   ?   C . n 
C 2 596  GLN 596  279  ?    ?   ?   C . n 
C 2 597  ILE 597  280  ?    ?   ?   C . n 
C 2 598  THR 598  281  ?    ?   ?   C . n 
C 2 599  LYS 599  282  ?    ?   ?   C . n 
C 2 600  ARG 600  283  ?    ?   ?   C . n 
C 2 601  VAL 601  284  ?    ?   ?   C . n 
C 2 602  PRO 602  285  ?    ?   ?   C . n 
C 2 603  ILE 603  286  ?    ?   ?   C . n 
C 2 604  PHE 604  287  ?    ?   ?   C . n 
C 2 605  GLN 605  288  ?    ?   ?   C . n 
C 2 606  ASP 606  289  ?    ?   ?   C . n 
C 2 607  ALA 607  290  ?    ?   ?   C . n 
C 2 608  ALA 608  291  ?    ?   ?   C . n 
C 2 609  PRO 609  292  ?    ?   ?   C . n 
C 2 610  PRO 610  293  ?    ?   ?   C . n 
C 2 611  VAL 611  294  ?    ?   ?   C . n 
C 2 612  ILE 612  295  ?    ?   ?   C . n 
C 2 613  HIS 613  296  ?    ?   ?   C . n 
C 2 614  ILE 614  297  ?    ?   ?   C . n 
C 2 615  ARG 615  298  ?    ?   ?   C . n 
C 2 616  SER 616  299  ?    ?   ?   C . n 
C 2 617  ARG 617  300  ?    ?   ?   C . n 
C 2 618  GLY 618  301  ?    ?   ?   C . n 
C 2 619  ASP 619  302  ?    ?   ?   C . n 
C 2 620  ILE 620  303  ?    ?   ?   C . n 
C 2 621  PRO 621  304  ?    ?   ?   C . n 
C 2 622  ARG 622  305  ?    ?   ?   C . n 
C 2 623  ALA 623  306  ?    ?   ?   C . n 
C 2 624  CYS 624  307  ?    ?   ?   C . n 
C 2 625  GLN 625  308  ?    ?   ?   C . n 
C 2 626  LYS 626  309  ?    ?   ?   C . n 
C 2 627  SER 627  310  ?    ?   ?   C . n 
C 2 628  LEU 628  311  ?    ?   ?   C . n 
C 2 629  ARG 629  312  ?    ?   ?   C . n 
C 2 630  PRO 630  313  ?    ?   ?   C . n 
C 2 631  VAL 631  314  ?    ?   ?   C . n 
C 2 632  PRO 632  315  ?    ?   ?   C . n 
C 2 633  PRO 633  316  ?    ?   ?   C . n 
C 2 634  SER 634  317  ?    ?   ?   C . n 
C 2 635  PRO 635  318  ?    ?   ?   C . n 
C 2 636  LYS 636  319  ?    ?   ?   C . n 
C 2 637  ILE 637  320  ?    ?   ?   C . n 
C 2 638  ASP 638  321  ?    ?   ?   C . n 
C 2 639  ARG 639  322  ?    ?   ?   C . n 
C 2 640  GLY 640  323  ?    ?   ?   C . n 
C 2 641  TRP 641  324  ?    ?   ?   C . n 
C 2 642  VAL 642  325  ?    ?   ?   C . n 
C 2 643  CYS 643  326  ?    ?   ?   C . n 
C 2 644  VAL 644  327  ?    ?   ?   C . n 
C 2 645  PHE 645  328  ?    ?   ?   C . n 
C 2 646  GLN 646  329  ?    ?   ?   C . n 
C 2 647  LEU 647  330  ?    ?   ?   C . n 
C 2 648  GLN 648  331  ?    ?   ?   C . n 
C 2 649  ASP 649  332  ?    ?   ?   C . n 
C 2 650  GLY 650  333  ?    ?   ?   C . n 
C 2 651  LYS 651  334  ?    ?   ?   C . n 
C 2 652  THR 652  335  ?    ?   ?   C . n 
C 2 653  LEU 653  336  ?    ?   ?   C . n 
C 2 654  GLY 654  337  ?    ?   ?   C . n 
C 2 655  LEU 655  338  ?    ?   ?   C . n 
C 2 656  LYS 656  339  ?    ?   ?   C . n 
C 2 657  ILE 657  340  ?    ?   ?   C . n 
D 2 1    MET 1    -316 ?    ?   ?   D . n 
D 2 2    GLY 2    -315 ?    ?   ?   D . n 
D 2 3    SER 3    -314 ?    ?   ?   D . n 
D 2 4    SER 4    -313 ?    ?   ?   D . n 
D 2 5    HIS 5    -312 ?    ?   ?   D . n 
D 2 6    HIS 6    -311 ?    ?   ?   D . n 
D 2 7    HIS 7    -310 ?    ?   ?   D . n 
D 2 8    HIS 8    -309 ?    ?   ?   D . n 
D 2 9    HIS 9    -308 ?    ?   ?   D . n 
D 2 10   HIS 10   -307 ?    ?   ?   D . n 
D 2 11   GLY 11   -306 ?    ?   ?   D . n 
D 2 12   THR 12   -305 ?    ?   ?   D . n 
D 2 13   LYS 13   -304 ?    ?   ?   D . n 
D 2 14   THR 14   -303 ?    ?   ?   D . n 
D 2 15   GLU 15   -302 ?    ?   ?   D . n 
D 2 16   GLU 16   -301 ?    ?   ?   D . n 
D 2 17   GLY 17   -300 ?    ?   ?   D . n 
D 2 18   LYS 18   -299 ?    ?   ?   D . n 
D 2 19   LEU 19   -298 ?    ?   ?   D . n 
D 2 20   VAL 20   -297 ?    ?   ?   D . n 
D 2 21   ILE 21   -296 ?    ?   ?   D . n 
D 2 22   TRP 22   -295 ?    ?   ?   D . n 
D 2 23   ILE 23   -294 ?    ?   ?   D . n 
D 2 24   ASN 24   -293 ?    ?   ?   D . n 
D 2 25   GLY 25   -292 ?    ?   ?   D . n 
D 2 26   ASP 26   -291 ?    ?   ?   D . n 
D 2 27   LYS 27   -290 ?    ?   ?   D . n 
D 2 28   GLY 28   -289 ?    ?   ?   D . n 
D 2 29   TYR 29   -288 ?    ?   ?   D . n 
D 2 30   ASN 30   -287 ?    ?   ?   D . n 
D 2 31   GLY 31   -286 ?    ?   ?   D . n 
D 2 32   LEU 32   -285 ?    ?   ?   D . n 
D 2 33   ALA 33   -284 ?    ?   ?   D . n 
D 2 34   GLU 34   -283 ?    ?   ?   D . n 
D 2 35   VAL 35   -282 ?    ?   ?   D . n 
D 2 36   GLY 36   -281 ?    ?   ?   D . n 
D 2 37   LYS 37   -280 ?    ?   ?   D . n 
D 2 38   LYS 38   -279 ?    ?   ?   D . n 
D 2 39   PHE 39   -278 ?    ?   ?   D . n 
D 2 40   GLU 40   -277 ?    ?   ?   D . n 
D 2 41   LYS 41   -276 ?    ?   ?   D . n 
D 2 42   ASP 42   -275 ?    ?   ?   D . n 
D 2 43   THR 43   -274 ?    ?   ?   D . n 
D 2 44   GLY 44   -273 ?    ?   ?   D . n 
D 2 45   ILE 45   -272 ?    ?   ?   D . n 
D 2 46   LYS 46   -271 ?    ?   ?   D . n 
D 2 47   VAL 47   -270 ?    ?   ?   D . n 
D 2 48   THR 48   -269 ?    ?   ?   D . n 
D 2 49   VAL 49   -268 ?    ?   ?   D . n 
D 2 50   GLU 50   -267 ?    ?   ?   D . n 
D 2 51   HIS 51   -266 ?    ?   ?   D . n 
D 2 52   PRO 52   -265 ?    ?   ?   D . n 
D 2 53   ASP 53   -264 ?    ?   ?   D . n 
D 2 54   LYS 54   -263 ?    ?   ?   D . n 
D 2 55   LEU 55   -262 ?    ?   ?   D . n 
D 2 56   GLU 56   -261 ?    ?   ?   D . n 
D 2 57   GLU 57   -260 ?    ?   ?   D . n 
D 2 58   LYS 58   -259 ?    ?   ?   D . n 
D 2 59   PHE 59   -258 ?    ?   ?   D . n 
D 2 60   PRO 60   -257 ?    ?   ?   D . n 
D 2 61   GLN 61   -256 ?    ?   ?   D . n 
D 2 62   VAL 62   -255 ?    ?   ?   D . n 
D 2 63   ALA 63   -254 ?    ?   ?   D . n 
D 2 64   ALA 64   -253 ?    ?   ?   D . n 
D 2 65   THR 65   -252 ?    ?   ?   D . n 
D 2 66   GLY 66   -251 ?    ?   ?   D . n 
D 2 67   ASP 67   -250 ?    ?   ?   D . n 
D 2 68   GLY 68   -249 ?    ?   ?   D . n 
D 2 69   PRO 69   -248 ?    ?   ?   D . n 
D 2 70   ASP 70   -247 ?    ?   ?   D . n 
D 2 71   ILE 71   -246 ?    ?   ?   D . n 
D 2 72   ILE 72   -245 ?    ?   ?   D . n 
D 2 73   PHE 73   -244 ?    ?   ?   D . n 
D 2 74   TRP 74   -243 ?    ?   ?   D . n 
D 2 75   ALA 75   -242 ?    ?   ?   D . n 
D 2 76   HIS 76   -241 ?    ?   ?   D . n 
D 2 77   ASP 77   -240 ?    ?   ?   D . n 
D 2 78   ARG 78   -239 ?    ?   ?   D . n 
D 2 79   PHE 79   -238 ?    ?   ?   D . n 
D 2 80   GLY 80   -237 ?    ?   ?   D . n 
D 2 81   GLY 81   -236 ?    ?   ?   D . n 
D 2 82   TYR 82   -235 ?    ?   ?   D . n 
D 2 83   ALA 83   -234 ?    ?   ?   D . n 
D 2 84   GLN 84   -233 ?    ?   ?   D . n 
D 2 85   SER 85   -232 ?    ?   ?   D . n 
D 2 86   GLY 86   -231 ?    ?   ?   D . n 
D 2 87   LEU 87   -230 ?    ?   ?   D . n 
D 2 88   LEU 88   -229 ?    ?   ?   D . n 
D 2 89   ALA 89   -228 ?    ?   ?   D . n 
D 2 90   GLU 90   -227 ?    ?   ?   D . n 
D 2 91   ILE 91   -226 ?    ?   ?   D . n 
D 2 92   THR 92   -225 ?    ?   ?   D . n 
D 2 93   PRO 93   -224 ?    ?   ?   D . n 
D 2 94   ASP 94   -223 ?    ?   ?   D . n 
D 2 95   LYS 95   -222 ?    ?   ?   D . n 
D 2 96   ALA 96   -221 ?    ?   ?   D . n 
D 2 97   PHE 97   -220 ?    ?   ?   D . n 
D 2 98   GLN 98   -219 ?    ?   ?   D . n 
D 2 99   ASP 99   -218 ?    ?   ?   D . n 
D 2 100  LYS 100  -217 ?    ?   ?   D . n 
D 2 101  LEU 101  -216 ?    ?   ?   D . n 
D 2 102  TYR 102  -215 ?    ?   ?   D . n 
D 2 103  PRO 103  -214 ?    ?   ?   D . n 
D 2 104  PHE 104  -213 ?    ?   ?   D . n 
D 2 105  THR 105  -212 ?    ?   ?   D . n 
D 2 106  TRP 106  -211 ?    ?   ?   D . n 
D 2 107  ASP 107  -210 ?    ?   ?   D . n 
D 2 108  ALA 108  -209 ?    ?   ?   D . n 
D 2 109  VAL 109  -208 ?    ?   ?   D . n 
D 2 110  ARG 110  -207 ?    ?   ?   D . n 
D 2 111  TYR 111  -206 ?    ?   ?   D . n 
D 2 112  ASN 112  -205 ?    ?   ?   D . n 
D 2 113  GLY 113  -204 ?    ?   ?   D . n 
D 2 114  LYS 114  -203 ?    ?   ?   D . n 
D 2 115  LEU 115  -202 ?    ?   ?   D . n 
D 2 116  ILE 116  -201 ?    ?   ?   D . n 
D 2 117  ALA 117  -200 ?    ?   ?   D . n 
D 2 118  TYR 118  -199 ?    ?   ?   D . n 
D 2 119  PRO 119  -198 ?    ?   ?   D . n 
D 2 120  ILE 120  -197 ?    ?   ?   D . n 
D 2 121  ALA 121  -196 ?    ?   ?   D . n 
D 2 122  VAL 122  -195 ?    ?   ?   D . n 
D 2 123  GLU 123  -194 ?    ?   ?   D . n 
D 2 124  ALA 124  -193 ?    ?   ?   D . n 
D 2 125  LEU 125  -192 ?    ?   ?   D . n 
D 2 126  SER 126  -191 ?    ?   ?   D . n 
D 2 127  LEU 127  -190 ?    ?   ?   D . n 
D 2 128  ILE 128  -189 ?    ?   ?   D . n 
D 2 129  TYR 129  -188 ?    ?   ?   D . n 
D 2 130  ASN 130  -187 ?    ?   ?   D . n 
D 2 131  LYS 131  -186 ?    ?   ?   D . n 
D 2 132  ASP 132  -185 ?    ?   ?   D . n 
D 2 133  LEU 133  -184 ?    ?   ?   D . n 
D 2 134  LEU 134  -183 ?    ?   ?   D . n 
D 2 135  PRO 135  -182 ?    ?   ?   D . n 
D 2 136  ASN 136  -181 ?    ?   ?   D . n 
D 2 137  PRO 137  -180 ?    ?   ?   D . n 
D 2 138  PRO 138  -179 ?    ?   ?   D . n 
D 2 139  LYS 139  -178 ?    ?   ?   D . n 
D 2 140  THR 140  -177 ?    ?   ?   D . n 
D 2 141  TRP 141  -176 ?    ?   ?   D . n 
D 2 142  GLU 142  -175 ?    ?   ?   D . n 
D 2 143  GLU 143  -174 ?    ?   ?   D . n 
D 2 144  ILE 144  -173 ?    ?   ?   D . n 
D 2 145  PRO 145  -172 ?    ?   ?   D . n 
D 2 146  ALA 146  -171 ?    ?   ?   D . n 
D 2 147  LEU 147  -170 ?    ?   ?   D . n 
D 2 148  ASP 148  -169 ?    ?   ?   D . n 
D 2 149  LYS 149  -168 ?    ?   ?   D . n 
D 2 150  GLU 150  -167 ?    ?   ?   D . n 
D 2 151  LEU 151  -166 ?    ?   ?   D . n 
D 2 152  LYS 152  -165 ?    ?   ?   D . n 
D 2 153  ALA 153  -164 ?    ?   ?   D . n 
D 2 154  LYS 154  -163 ?    ?   ?   D . n 
D 2 155  GLY 155  -162 ?    ?   ?   D . n 
D 2 156  LYS 156  -161 ?    ?   ?   D . n 
D 2 157  SER 157  -160 ?    ?   ?   D . n 
D 2 158  ALA 158  -159 ?    ?   ?   D . n 
D 2 159  LEU 159  -158 ?    ?   ?   D . n 
D 2 160  MET 160  -157 ?    ?   ?   D . n 
D 2 161  PHE 161  -156 ?    ?   ?   D . n 
D 2 162  ASN 162  -155 ?    ?   ?   D . n 
D 2 163  LEU 163  -154 ?    ?   ?   D . n 
D 2 164  GLN 164  -153 ?    ?   ?   D . n 
D 2 165  GLU 165  -152 ?    ?   ?   D . n 
D 2 166  PRO 166  -151 ?    ?   ?   D . n 
D 2 167  TYR 167  -150 ?    ?   ?   D . n 
D 2 168  PHE 168  -149 ?    ?   ?   D . n 
D 2 169  THR 169  -148 ?    ?   ?   D . n 
D 2 170  TRP 170  -147 ?    ?   ?   D . n 
D 2 171  PRO 171  -146 ?    ?   ?   D . n 
D 2 172  LEU 172  -145 ?    ?   ?   D . n 
D 2 173  ILE 173  -144 ?    ?   ?   D . n 
D 2 174  ALA 174  -143 ?    ?   ?   D . n 
D 2 175  ALA 175  -142 ?    ?   ?   D . n 
D 2 176  ASP 176  -141 ?    ?   ?   D . n 
D 2 177  GLY 177  -140 ?    ?   ?   D . n 
D 2 178  GLY 178  -139 ?    ?   ?   D . n 
D 2 179  TYR 179  -138 ?    ?   ?   D . n 
D 2 180  ALA 180  -137 ?    ?   ?   D . n 
D 2 181  PHE 181  -136 ?    ?   ?   D . n 
D 2 182  LYS 182  -135 ?    ?   ?   D . n 
D 2 183  TYR 183  -134 ?    ?   ?   D . n 
D 2 184  GLU 184  -133 ?    ?   ?   D . n 
D 2 185  ASN 185  -132 ?    ?   ?   D . n 
D 2 186  GLY 186  -131 ?    ?   ?   D . n 
D 2 187  LYS 187  -130 ?    ?   ?   D . n 
D 2 188  TYR 188  -129 ?    ?   ?   D . n 
D 2 189  ASP 189  -128 ?    ?   ?   D . n 
D 2 190  ILE 190  -127 ?    ?   ?   D . n 
D 2 191  LYS 191  -126 ?    ?   ?   D . n 
D 2 192  ASP 192  -125 ?    ?   ?   D . n 
D 2 193  VAL 193  -124 ?    ?   ?   D . n 
D 2 194  GLY 194  -123 ?    ?   ?   D . n 
D 2 195  VAL 195  -122 ?    ?   ?   D . n 
D 2 196  ASP 196  -121 ?    ?   ?   D . n 
D 2 197  ASN 197  -120 ?    ?   ?   D . n 
D 2 198  ALA 198  -119 ?    ?   ?   D . n 
D 2 199  GLY 199  -118 ?    ?   ?   D . n 
D 2 200  ALA 200  -117 ?    ?   ?   D . n 
D 2 201  LYS 201  -116 ?    ?   ?   D . n 
D 2 202  ALA 202  -115 ?    ?   ?   D . n 
D 2 203  GLY 203  -114 ?    ?   ?   D . n 
D 2 204  LEU 204  -113 ?    ?   ?   D . n 
D 2 205  THR 205  -112 ?    ?   ?   D . n 
D 2 206  PHE 206  -111 ?    ?   ?   D . n 
D 2 207  LEU 207  -110 ?    ?   ?   D . n 
D 2 208  VAL 208  -109 ?    ?   ?   D . n 
D 2 209  ASP 209  -108 ?    ?   ?   D . n 
D 2 210  LEU 210  -107 ?    ?   ?   D . n 
D 2 211  ILE 211  -106 ?    ?   ?   D . n 
D 2 212  LYS 212  -105 ?    ?   ?   D . n 
D 2 213  ASN 213  -104 ?    ?   ?   D . n 
D 2 214  LYS 214  -103 ?    ?   ?   D . n 
D 2 215  HIS 215  -102 ?    ?   ?   D . n 
D 2 216  MET 216  -101 ?    ?   ?   D . n 
D 2 217  ASN 217  -100 ?    ?   ?   D . n 
D 2 218  ALA 218  -99  ?    ?   ?   D . n 
D 2 219  ASP 219  -98  ?    ?   ?   D . n 
D 2 220  THR 220  -97  ?    ?   ?   D . n 
D 2 221  ASP 221  -96  ?    ?   ?   D . n 
D 2 222  TYR 222  -95  ?    ?   ?   D . n 
D 2 223  SER 223  -94  ?    ?   ?   D . n 
D 2 224  ILE 224  -93  ?    ?   ?   D . n 
D 2 225  ALA 225  -92  ?    ?   ?   D . n 
D 2 226  GLU 226  -91  ?    ?   ?   D . n 
D 2 227  ALA 227  -90  ?    ?   ?   D . n 
D 2 228  ALA 228  -89  ?    ?   ?   D . n 
D 2 229  PHE 229  -88  ?    ?   ?   D . n 
D 2 230  ASN 230  -87  ?    ?   ?   D . n 
D 2 231  LYS 231  -86  ?    ?   ?   D . n 
D 2 232  GLY 232  -85  ?    ?   ?   D . n 
D 2 233  GLU 233  -84  ?    ?   ?   D . n 
D 2 234  THR 234  -83  ?    ?   ?   D . n 
D 2 235  ALA 235  -82  ?    ?   ?   D . n 
D 2 236  MET 236  -81  ?    ?   ?   D . n 
D 2 237  THR 237  -80  ?    ?   ?   D . n 
D 2 238  ILE 238  -79  ?    ?   ?   D . n 
D 2 239  ASN 239  -78  ?    ?   ?   D . n 
D 2 240  GLY 240  -77  ?    ?   ?   D . n 
D 2 241  PRO 241  -76  ?    ?   ?   D . n 
D 2 242  TRP 242  -75  ?    ?   ?   D . n 
D 2 243  ALA 243  -74  ?    ?   ?   D . n 
D 2 244  TRP 244  -73  ?    ?   ?   D . n 
D 2 245  SER 245  -72  ?    ?   ?   D . n 
D 2 246  ASN 246  -71  ?    ?   ?   D . n 
D 2 247  ILE 247  -70  ?    ?   ?   D . n 
D 2 248  ASP 248  -69  ?    ?   ?   D . n 
D 2 249  THR 249  -68  ?    ?   ?   D . n 
D 2 250  SER 250  -67  ?    ?   ?   D . n 
D 2 251  LYS 251  -66  ?    ?   ?   D . n 
D 2 252  VAL 252  -65  ?    ?   ?   D . n 
D 2 253  ASN 253  -64  ?    ?   ?   D . n 
D 2 254  TYR 254  -63  ?    ?   ?   D . n 
D 2 255  GLY 255  -62  ?    ?   ?   D . n 
D 2 256  VAL 256  -61  ?    ?   ?   D . n 
D 2 257  THR 257  -60  ?    ?   ?   D . n 
D 2 258  VAL 258  -59  ?    ?   ?   D . n 
D 2 259  LEU 259  -58  ?    ?   ?   D . n 
D 2 260  PRO 260  -57  ?    ?   ?   D . n 
D 2 261  THR 261  -56  ?    ?   ?   D . n 
D 2 262  PHE 262  -55  ?    ?   ?   D . n 
D 2 263  LYS 263  -54  ?    ?   ?   D . n 
D 2 264  GLY 264  -53  ?    ?   ?   D . n 
D 2 265  GLN 265  -52  ?    ?   ?   D . n 
D 2 266  PRO 266  -51  ?    ?   ?   D . n 
D 2 267  SER 267  -50  ?    ?   ?   D . n 
D 2 268  LYS 268  -49  ?    ?   ?   D . n 
D 2 269  PRO 269  -48  ?    ?   ?   D . n 
D 2 270  PHE 270  -47  ?    ?   ?   D . n 
D 2 271  VAL 271  -46  ?    ?   ?   D . n 
D 2 272  GLY 272  -45  ?    ?   ?   D . n 
D 2 273  VAL 273  -44  ?    ?   ?   D . n 
D 2 274  LEU 274  -43  ?    ?   ?   D . n 
D 2 275  SER 275  -42  ?    ?   ?   D . n 
D 2 276  ALA 276  -41  ?    ?   ?   D . n 
D 2 277  GLY 277  -40  ?    ?   ?   D . n 
D 2 278  ILE 278  -39  ?    ?   ?   D . n 
D 2 279  ASN 279  -38  ?    ?   ?   D . n 
D 2 280  ALA 280  -37  ?    ?   ?   D . n 
D 2 281  ALA 281  -36  ?    ?   ?   D . n 
D 2 282  SER 282  -35  ?    ?   ?   D . n 
D 2 283  PRO 283  -34  ?    ?   ?   D . n 
D 2 284  ASN 284  -33  ?    ?   ?   D . n 
D 2 285  LYS 285  -32  ?    ?   ?   D . n 
D 2 286  GLU 286  -31  ?    ?   ?   D . n 
D 2 287  LEU 287  -30  ?    ?   ?   D . n 
D 2 288  ALA 288  -29  ?    ?   ?   D . n 
D 2 289  LYS 289  -28  ?    ?   ?   D . n 
D 2 290  GLU 290  -27  ?    ?   ?   D . n 
D 2 291  PHE 291  -26  ?    ?   ?   D . n 
D 2 292  LEU 292  -25  ?    ?   ?   D . n 
D 2 293  GLU 293  -24  ?    ?   ?   D . n 
D 2 294  ASN 294  -23  ?    ?   ?   D . n 
D 2 295  TYR 295  -22  ?    ?   ?   D . n 
D 2 296  LEU 296  -21  ?    ?   ?   D . n 
D 2 297  LEU 297  -20  ?    ?   ?   D . n 
D 2 298  THR 298  -19  ?    ?   ?   D . n 
D 2 299  ASP 299  -18  ?    ?   ?   D . n 
D 2 300  GLU 300  -17  ?    ?   ?   D . n 
D 2 301  GLY 301  -16  ?    ?   ?   D . n 
D 2 302  LEU 302  -15  ?    ?   ?   D . n 
D 2 303  GLU 303  -14  ?    ?   ?   D . n 
D 2 304  ALA 304  -13  ?    ?   ?   D . n 
D 2 305  VAL 305  -12  ?    ?   ?   D . n 
D 2 306  ASN 306  -11  ?    ?   ?   D . n 
D 2 307  LYS 307  -10  ?    ?   ?   D . n 
D 2 308  ASP 308  -9   ?    ?   ?   D . n 
D 2 309  LYS 309  -8   ?    ?   ?   D . n 
D 2 310  PRO 310  -7   ?    ?   ?   D . n 
D 2 311  LEU 311  -6   ?    ?   ?   D . n 
D 2 312  GLY 312  -5   ?    ?   ?   D . n 
D 2 313  ALA 313  -4   ?    ?   ?   D . n 
D 2 314  VAL 314  -3   ?    ?   ?   D . n 
D 2 315  ALA 315  -2   ?    ?   ?   D . n 
D 2 316  LEU 316  -1   ?    ?   ?   D . n 
D 2 317  LYS 317  0    ?    ?   ?   D . n 
D 2 318  SER 318  1    ?    ?   ?   D . n 
D 2 319  TYR 319  2    ?    ?   ?   D . n 
D 2 320  GLU 320  3    ?    ?   ?   D . n 
D 2 321  GLU 321  4    ?    ?   ?   D . n 
D 2 322  GLU 322  5    ?    ?   ?   D . n 
D 2 323  LEU 323  6    ?    ?   ?   D . n 
D 2 324  ALA 324  7    ?    ?   ?   D . n 
D 2 325  LYS 325  8    ?    ?   ?   D . n 
D 2 326  ASP 326  9    ?    ?   ?   D . n 
D 2 327  PRO 327  10   ?    ?   ?   D . n 
D 2 328  ARG 328  11   ?    ?   ?   D . n 
D 2 329  ILE 329  12   ?    ?   ?   D . n 
D 2 330  ALA 330  13   ?    ?   ?   D . n 
D 2 331  ALA 331  14   ?    ?   ?   D . n 
D 2 332  THR 332  15   ?    ?   ?   D . n 
D 2 333  MET 333  16   ?    ?   ?   D . n 
D 2 334  GLU 334  17   ?    ?   ?   D . n 
D 2 335  ASN 335  18   ?    ?   ?   D . n 
D 2 336  ALA 336  19   ?    ?   ?   D . n 
D 2 337  GLN 337  20   ?    ?   ?   D . n 
D 2 338  LYS 338  21   ?    ?   ?   D . n 
D 2 339  GLY 339  22   ?    ?   ?   D . n 
D 2 340  GLU 340  23   ?    ?   ?   D . n 
D 2 341  ILE 341  24   ?    ?   ?   D . n 
D 2 342  MET 342  25   ?    ?   ?   D . n 
D 2 343  PRO 343  26   ?    ?   ?   D . n 
D 2 344  ASN 344  27   ?    ?   ?   D . n 
D 2 345  ILE 345  28   ?    ?   ?   D . n 
D 2 346  PRO 346  29   ?    ?   ?   D . n 
D 2 347  GLN 347  30   ?    ?   ?   D . n 
D 2 348  MET 348  31   ?    ?   ?   D . n 
D 2 349  SER 349  32   ?    ?   ?   D . n 
D 2 350  ALA 350  33   ?    ?   ?   D . n 
D 2 351  PHE 351  34   ?    ?   ?   D . n 
D 2 352  TRP 352  35   ?    ?   ?   D . n 
D 2 353  TYR 353  36   ?    ?   ?   D . n 
D 2 354  ALA 354  37   ?    ?   ?   D . n 
D 2 355  VAL 355  38   ?    ?   ?   D . n 
D 2 356  ARG 356  39   ?    ?   ?   D . n 
D 2 357  THR 357  40   ?    ?   ?   D . n 
D 2 358  ALA 358  41   ?    ?   ?   D . n 
D 2 359  VAL 359  42   ?    ?   ?   D . n 
D 2 360  ILE 360  43   ?    ?   ?   D . n 
D 2 361  ASN 361  44   ?    ?   ?   D . n 
D 2 362  ALA 362  45   ?    ?   ?   D . n 
D 2 363  ALA 363  46   ?    ?   ?   D . n 
D 2 364  SER 364  47   ?    ?   ?   D . n 
D 2 365  GLY 365  48   ?    ?   ?   D . n 
D 2 366  ARG 366  49   ?    ?   ?   D . n 
D 2 367  GLN 367  50   ?    ?   ?   D . n 
D 2 368  THR 368  51   ?    ?   ?   D . n 
D 2 369  VAL 369  52   ?    ?   ?   D . n 
D 2 370  ASP 370  53   ?    ?   ?   D . n 
D 2 371  GLU 371  54   ?    ?   ?   D . n 
D 2 372  ALA 372  55   ?    ?   ?   D . n 
D 2 373  LEU 373  56   ?    ?   ?   D . n 
D 2 374  LYS 374  57   ?    ?   ?   D . n 
D 2 375  ASP 375  58   ?    ?   ?   D . n 
D 2 376  ALA 376  59   ?    ?   ?   D . n 
D 2 377  GLN 377  60   ?    ?   ?   D . n 
D 2 378  THR 378  61   ?    ?   ?   D . n 
D 2 379  GLY 379  62   ?    ?   ?   D . n 
D 2 380  THR 380  63   ?    ?   ?   D . n 
D 2 381  ASP 381  64   ?    ?   ?   D . n 
D 2 382  TYR 382  65   ?    ?   ?   D . n 
D 2 383  ASP 383  66   ?    ?   ?   D . n 
D 2 384  ILE 384  67   ?    ?   ?   D . n 
D 2 385  PRO 385  68   ?    ?   ?   D . n 
D 2 386  THR 386  69   ?    ?   ?   D . n 
D 2 387  THR 387  70   ?    ?   ?   D . n 
D 2 388  GLU 388  71   ?    ?   ?   D . n 
D 2 389  ASN 389  72   ?    ?   ?   D . n 
D 2 390  LEU 390  73   ?    ?   ?   D . n 
D 2 391  TYR 391  74   ?    ?   ?   D . n 
D 2 392  PHE 392  75   ?    ?   ?   D . n 
D 2 393  GLN 393  76   ?    ?   ?   D . n 
D 2 394  GLY 394  77   ?    ?   ?   D . n 
D 2 395  GLY 395  78   ?    ?   ?   D . n 
D 2 396  SER 396  79   ?    ?   ?   D . n 
D 2 397  ASN 397  80   ?    ?   ?   D . n 
D 2 398  HIS 398  81   ?    ?   ?   D . n 
D 2 399  SER 399  82   ?    ?   ?   D . n 
D 2 400  PHE 400  83   ?    ?   ?   D . n 
D 2 401  GLU 401  84   ?    ?   ?   D . n 
D 2 402  GLU 402  85   ?    ?   ?   D . n 
D 2 403  VAL 403  86   ?    ?   ?   D . n 
D 2 404  VAL 404  87   ?    ?   ?   D . n 
D 2 405  GLN 405  88   ?    ?   ?   D . n 
D 2 406  THR 406  89   ?    ?   ?   D . n 
D 2 407  LEU 407  90   ?    ?   ?   D . n 
D 2 408  ALA 408  91   ?    ?   ?   D . n 
D 2 409  SER 409  92   ?    ?   ?   D . n 
D 2 410  LEU 410  93   ?    ?   ?   D . n 
D 2 411  ALA 411  94   ?    ?   ?   D . n 
D 2 412  THR 412  95   ?    ?   ?   D . n 
D 2 413  VAL 413  96   ?    ?   ?   D . n 
D 2 414  VAL 414  97   ?    ?   ?   D . n 
D 2 415  GLN 415  98   ?    ?   ?   D . n 
D 2 416  GLN 416  99   ?    ?   ?   D . n 
D 2 417  GLN 417  100  ?    ?   ?   D . n 
D 2 418  THR 418  101  ?    ?   ?   D . n 
D 2 419  ILE 419  102  ?    ?   ?   D . n 
D 2 420  ALA 420  103  ?    ?   ?   D . n 
D 2 421  SER 421  104  ?    ?   ?   D . n 
D 2 422  GLU 422  105  ?    ?   ?   D . n 
D 2 423  SER 423  106  ?    ?   ?   D . n 
D 2 424  LEU 424  107  ?    ?   ?   D . n 
D 2 425  GLU 425  108  ?    ?   ?   D . n 
D 2 426  GLN 426  109  ?    ?   ?   D . n 
D 2 427  ARG 427  110  ?    ?   ?   D . n 
D 2 428  ILE 428  111  ?    ?   ?   D . n 
D 2 429  THR 429  112  ?    ?   ?   D . n 
D 2 430  SER 430  113  ?    ?   ?   D . n 
D 2 431  LEU 431  114  ?    ?   ?   D . n 
D 2 432  GLU 432  115  ?    ?   ?   D . n 
D 2 433  ASN 433  116  ?    ?   ?   D . n 
D 2 434  GLY 434  117  ?    ?   ?   D . n 
D 2 435  LEU 435  118  ?    ?   ?   D . n 
D 2 436  LYS 436  119  ?    ?   ?   D . n 
D 2 437  PRO 437  120  120  PRO PRO D . n 
D 2 438  VAL 438  121  121  VAL VAL D . n 
D 2 439  TYR 439  122  122  TYR TYR D . n 
D 2 440  ASP 440  123  123  ASP ASP D . n 
D 2 441  MET 441  124  124  MET MET D . n 
D 2 442  ALA 442  125  125  ALA ALA D . n 
D 2 443  LYS 443  126  126  LYS LYS D . n 
D 2 444  THR 444  127  127  THR THR D . n 
D 2 445  ILE 445  128  128  ILE ILE D . n 
D 2 446  SER 446  129  129  SER SER D . n 
D 2 447  SER 447  130  130  SER SER D . n 
D 2 448  LEU 448  131  131  LEU LEU D . n 
D 2 449  ASN 449  132  132  ASN ASN D . n 
D 2 450  ARG 450  133  133  ARG ARG D . n 
D 2 451  VAL 451  134  134  VAL VAL D . n 
D 2 452  CYS 452  135  135  CYS CYS D . n 
D 2 453  ALA 453  136  136  ALA ALA D . n 
D 2 454  GLU 454  137  137  GLU GLU D . n 
D 2 455  MET 455  138  138  MET MET D . n 
D 2 456  VAL 456  139  139  VAL VAL D . n 
D 2 457  ALA 457  140  140  ALA ALA D . n 
D 2 458  LYS 458  141  141  LYS LYS D . n 
D 2 459  TYR 459  142  142  TYR TYR D . n 
D 2 460  ASP 460  143  143  ASP ASP D . n 
D 2 461  LEU 461  144  144  LEU LEU D . n 
D 2 462  LEU 462  145  145  LEU LEU D . n 
D 2 463  VAL 463  146  146  VAL VAL D . n 
D 2 464  MET 464  147  147  MET MET D . n 
D 2 465  THR 465  148  148  THR THR D . n 
D 2 466  THR 466  149  149  THR THR D . n 
D 2 467  GLY 467  150  ?    ?   ?   D . n 
D 2 468  ARG 468  151  ?    ?   ?   D . n 
D 2 469  ALA 469  152  ?    ?   ?   D . n 
D 2 470  THR 470  153  ?    ?   ?   D . n 
D 2 471  ALA 471  154  ?    ?   ?   D . n 
D 2 472  THR 472  155  ?    ?   ?   D . n 
D 2 473  ALA 473  156  ?    ?   ?   D . n 
D 2 474  ALA 474  157  ?    ?   ?   D . n 
D 2 475  ALA 475  158  ?    ?   ?   D . n 
D 2 476  THR 476  159  ?    ?   ?   D . n 
D 2 477  GLU 477  160  ?    ?   ?   D . n 
D 2 478  ALA 478  161  ?    ?   ?   D . n 
D 2 479  TYR 479  162  ?    ?   ?   D . n 
D 2 480  TRP 480  163  ?    ?   ?   D . n 
D 2 481  ALA 481  164  ?    ?   ?   D . n 
D 2 482  GLU 482  165  ?    ?   ?   D . n 
D 2 483  HIS 483  166  ?    ?   ?   D . n 
D 2 484  GLY 484  167  ?    ?   ?   D . n 
D 2 485  GLN 485  168  ?    ?   ?   D . n 
D 2 486  PRO 486  169  ?    ?   ?   D . n 
D 2 487  PRO 487  170  ?    ?   ?   D . n 
D 2 488  PRO 488  171  ?    ?   ?   D . n 
D 2 489  GLY 489  172  ?    ?   ?   D . n 
D 2 490  PRO 490  173  ?    ?   ?   D . n 
D 2 491  SER 491  174  ?    ?   ?   D . n 
D 2 492  LEU 492  175  ?    ?   ?   D . n 
D 2 493  TYR 493  176  ?    ?   ?   D . n 
D 2 494  GLU 494  177  ?    ?   ?   D . n 
D 2 495  GLU 495  178  ?    ?   ?   D . n 
D 2 496  SER 496  179  ?    ?   ?   D . n 
D 2 497  ALA 497  180  ?    ?   ?   D . n 
D 2 498  ILE 498  181  ?    ?   ?   D . n 
D 2 499  ARG 499  182  ?    ?   ?   D . n 
D 2 500  GLY 500  183  ?    ?   ?   D . n 
D 2 501  LYS 501  184  ?    ?   ?   D . n 
D 2 502  ILE 502  185  ?    ?   ?   D . n 
D 2 503  GLU 503  186  ?    ?   ?   D . n 
D 2 504  SER 504  187  ?    ?   ?   D . n 
D 2 505  ARG 505  188  ?    ?   ?   D . n 
D 2 506  ASP 506  189  ?    ?   ?   D . n 
D 2 507  GLU 507  190  ?    ?   ?   D . n 
D 2 508  THR 508  191  ?    ?   ?   D . n 
D 2 509  VAL 509  192  ?    ?   ?   D . n 
D 2 510  PRO 510  193  ?    ?   ?   D . n 
D 2 511  GLN 511  194  ?    ?   ?   D . n 
D 2 512  SER 512  195  ?    ?   ?   D . n 
D 2 513  VAL 513  196  ?    ?   ?   D . n 
D 2 514  ARG 514  197  ?    ?   ?   D . n 
D 2 515  GLU 515  198  ?    ?   ?   D . n 
D 2 516  ALA 516  199  ?    ?   ?   D . n 
D 2 517  PHE 517  200  ?    ?   ?   D . n 
D 2 518  ASN 518  201  ?    ?   ?   D . n 
D 2 519  ASN 519  202  ?    ?   ?   D . n 
D 2 520  LEU 520  203  ?    ?   ?   D . n 
D 2 521  ASN 521  204  ?    ?   ?   D . n 
D 2 522  SER 522  205  ?    ?   ?   D . n 
D 2 523  THR 523  206  ?    ?   ?   D . n 
D 2 524  THR 524  207  ?    ?   ?   D . n 
D 2 525  SER 525  208  ?    ?   ?   D . n 
D 2 526  LEU 526  209  ?    ?   ?   D . n 
D 2 527  THR 527  210  ?    ?   ?   D . n 
D 2 528  GLU 528  211  ?    ?   ?   D . n 
D 2 529  GLU 529  212  ?    ?   ?   D . n 
D 2 530  ASN 530  213  ?    ?   ?   D . n 
D 2 531  PHE 531  214  ?    ?   ?   D . n 
D 2 532  GLY 532  215  ?    ?   ?   D . n 
D 2 533  LYS 533  216  ?    ?   ?   D . n 
D 2 534  PRO 534  217  ?    ?   ?   D . n 
D 2 535  ASP 535  218  ?    ?   ?   D . n 
D 2 536  ILE 536  219  ?    ?   ?   D . n 
D 2 537  SER 537  220  ?    ?   ?   D . n 
D 2 538  ALA 538  221  ?    ?   ?   D . n 
D 2 539  LYS 539  222  ?    ?   ?   D . n 
D 2 540  ASP 540  223  ?    ?   ?   D . n 
D 2 541  LEU 541  224  ?    ?   ?   D . n 
D 2 542  ARG 542  225  ?    ?   ?   D . n 
D 2 543  ASN 543  226  ?    ?   ?   D . n 
D 2 544  ILE 544  227  ?    ?   ?   D . n 
D 2 545  MET 545  228  ?    ?   ?   D . n 
D 2 546  TYR 546  229  ?    ?   ?   D . n 
D 2 547  ASP 547  230  ?    ?   ?   D . n 
D 2 548  HIS 548  231  ?    ?   ?   D . n 
D 2 549  LEU 549  232  ?    ?   ?   D . n 
D 2 550  PRO 550  233  ?    ?   ?   D . n 
D 2 551  GLY 551  234  ?    ?   ?   D . n 
D 2 552  PHE 552  235  ?    ?   ?   D . n 
D 2 553  GLY 553  236  ?    ?   ?   D . n 
D 2 554  THR 554  237  ?    ?   ?   D . n 
D 2 555  ALA 555  238  ?    ?   ?   D . n 
D 2 556  PHE 556  239  ?    ?   ?   D . n 
D 2 557  HIS 557  240  ?    ?   ?   D . n 
D 2 558  GLN 558  241  ?    ?   ?   D . n 
D 2 559  LEU 559  242  ?    ?   ?   D . n 
D 2 560  VAL 560  243  ?    ?   ?   D . n 
D 2 561  GLN 561  244  ?    ?   ?   D . n 
D 2 562  VAL 562  245  ?    ?   ?   D . n 
D 2 563  ILE 563  246  ?    ?   ?   D . n 
D 2 564  CYS 564  247  ?    ?   ?   D . n 
D 2 565  LYS 565  248  ?    ?   ?   D . n 
D 2 566  LEU 566  249  ?    ?   ?   D . n 
D 2 567  GLY 567  250  ?    ?   ?   D . n 
D 2 568  LYS 568  251  ?    ?   ?   D . n 
D 2 569  ASP 569  252  ?    ?   ?   D . n 
D 2 570  SER 570  253  ?    ?   ?   D . n 
D 2 571  ASN 571  254  ?    ?   ?   D . n 
D 2 572  SER 572  255  ?    ?   ?   D . n 
D 2 573  LEU 573  256  ?    ?   ?   D . n 
D 2 574  ASP 574  257  ?    ?   ?   D . n 
D 2 575  ILE 575  258  ?    ?   ?   D . n 
D 2 576  ILE 576  259  ?    ?   ?   D . n 
D 2 577  HIS 577  260  ?    ?   ?   D . n 
D 2 578  ALA 578  261  ?    ?   ?   D . n 
D 2 579  GLU 579  262  ?    ?   ?   D . n 
D 2 580  PHE 580  263  ?    ?   ?   D . n 
D 2 581  GLN 581  264  ?    ?   ?   D . n 
D 2 582  ALA 582  265  ?    ?   ?   D . n 
D 2 583  SER 583  266  ?    ?   ?   D . n 
D 2 584  LEU 584  267  ?    ?   ?   D . n 
D 2 585  ALA 585  268  ?    ?   ?   D . n 
D 2 586  GLU 586  269  ?    ?   ?   D . n 
D 2 587  GLY 587  270  ?    ?   ?   D . n 
D 2 588  ASP 588  271  ?    ?   ?   D . n 
D 2 589  SER 589  272  ?    ?   ?   D . n 
D 2 590  PRO 590  273  ?    ?   ?   D . n 
D 2 591  GLN 591  274  ?    ?   ?   D . n 
D 2 592  CYS 592  275  ?    ?   ?   D . n 
D 2 593  ALA 593  276  ?    ?   ?   D . n 
D 2 594  LEU 594  277  ?    ?   ?   D . n 
D 2 595  ILE 595  278  ?    ?   ?   D . n 
D 2 596  GLN 596  279  ?    ?   ?   D . n 
D 2 597  ILE 597  280  ?    ?   ?   D . n 
D 2 598  THR 598  281  ?    ?   ?   D . n 
D 2 599  LYS 599  282  ?    ?   ?   D . n 
D 2 600  ARG 600  283  ?    ?   ?   D . n 
D 2 601  VAL 601  284  ?    ?   ?   D . n 
D 2 602  PRO 602  285  ?    ?   ?   D . n 
D 2 603  ILE 603  286  ?    ?   ?   D . n 
D 2 604  PHE 604  287  ?    ?   ?   D . n 
D 2 605  GLN 605  288  ?    ?   ?   D . n 
D 2 606  ASP 606  289  ?    ?   ?   D . n 
D 2 607  ALA 607  290  ?    ?   ?   D . n 
D 2 608  ALA 608  291  ?    ?   ?   D . n 
D 2 609  PRO 609  292  ?    ?   ?   D . n 
D 2 610  PRO 610  293  ?    ?   ?   D . n 
D 2 611  VAL 611  294  ?    ?   ?   D . n 
D 2 612  ILE 612  295  ?    ?   ?   D . n 
D 2 613  HIS 613  296  ?    ?   ?   D . n 
D 2 614  ILE 614  297  ?    ?   ?   D . n 
D 2 615  ARG 615  298  ?    ?   ?   D . n 
D 2 616  SER 616  299  ?    ?   ?   D . n 
D 2 617  ARG 617  300  ?    ?   ?   D . n 
D 2 618  GLY 618  301  ?    ?   ?   D . n 
D 2 619  ASP 619  302  ?    ?   ?   D . n 
D 2 620  ILE 620  303  ?    ?   ?   D . n 
D 2 621  PRO 621  304  ?    ?   ?   D . n 
D 2 622  ARG 622  305  ?    ?   ?   D . n 
D 2 623  ALA 623  306  ?    ?   ?   D . n 
D 2 624  CYS 624  307  ?    ?   ?   D . n 
D 2 625  GLN 625  308  ?    ?   ?   D . n 
D 2 626  LYS 626  309  ?    ?   ?   D . n 
D 2 627  SER 627  310  ?    ?   ?   D . n 
D 2 628  LEU 628  311  ?    ?   ?   D . n 
D 2 629  ARG 629  312  ?    ?   ?   D . n 
D 2 630  PRO 630  313  ?    ?   ?   D . n 
D 2 631  VAL 631  314  ?    ?   ?   D . n 
D 2 632  PRO 632  315  ?    ?   ?   D . n 
D 2 633  PRO 633  316  ?    ?   ?   D . n 
D 2 634  SER 634  317  ?    ?   ?   D . n 
D 2 635  PRO 635  318  ?    ?   ?   D . n 
D 2 636  LYS 636  319  ?    ?   ?   D . n 
D 2 637  ILE 637  320  ?    ?   ?   D . n 
D 2 638  ASP 638  321  ?    ?   ?   D . n 
D 2 639  ARG 639  322  ?    ?   ?   D . n 
D 2 640  GLY 640  323  ?    ?   ?   D . n 
D 2 641  TRP 641  324  ?    ?   ?   D . n 
D 2 642  VAL 642  325  ?    ?   ?   D . n 
D 2 643  CYS 643  326  ?    ?   ?   D . n 
D 2 644  VAL 644  327  ?    ?   ?   D . n 
D 2 645  PHE 645  328  ?    ?   ?   D . n 
D 2 646  GLN 646  329  ?    ?   ?   D . n 
D 2 647  LEU 647  330  ?    ?   ?   D . n 
D 2 648  GLN 648  331  ?    ?   ?   D . n 
D 2 649  ASP 649  332  ?    ?   ?   D . n 
D 2 650  GLY 650  333  ?    ?   ?   D . n 
D 2 651  LYS 651  334  ?    ?   ?   D . n 
D 2 652  THR 652  335  ?    ?   ?   D . n 
D 2 653  LEU 653  336  ?    ?   ?   D . n 
D 2 654  GLY 654  337  ?    ?   ?   D . n 
D 2 655  LEU 655  338  ?    ?   ?   D . n 
D 2 656  LYS 656  339  ?    ?   ?   D . n 
D 2 657  ILE 657  340  ?    ?   ?   D . n 
E 2 1    MET 1    -316 ?    ?   ?   E . n 
E 2 2    GLY 2    -315 ?    ?   ?   E . n 
E 2 3    SER 3    -314 ?    ?   ?   E . n 
E 2 4    SER 4    -313 ?    ?   ?   E . n 
E 2 5    HIS 5    -312 ?    ?   ?   E . n 
E 2 6    HIS 6    -311 ?    ?   ?   E . n 
E 2 7    HIS 7    -310 ?    ?   ?   E . n 
E 2 8    HIS 8    -309 ?    ?   ?   E . n 
E 2 9    HIS 9    -308 ?    ?   ?   E . n 
E 2 10   HIS 10   -307 ?    ?   ?   E . n 
E 2 11   GLY 11   -306 ?    ?   ?   E . n 
E 2 12   THR 12   -305 ?    ?   ?   E . n 
E 2 13   LYS 13   -304 ?    ?   ?   E . n 
E 2 14   THR 14   -303 ?    ?   ?   E . n 
E 2 15   GLU 15   -302 ?    ?   ?   E . n 
E 2 16   GLU 16   -301 ?    ?   ?   E . n 
E 2 17   GLY 17   -300 ?    ?   ?   E . n 
E 2 18   LYS 18   -299 ?    ?   ?   E . n 
E 2 19   LEU 19   -298 ?    ?   ?   E . n 
E 2 20   VAL 20   -297 ?    ?   ?   E . n 
E 2 21   ILE 21   -296 ?    ?   ?   E . n 
E 2 22   TRP 22   -295 ?    ?   ?   E . n 
E 2 23   ILE 23   -294 ?    ?   ?   E . n 
E 2 24   ASN 24   -293 ?    ?   ?   E . n 
E 2 25   GLY 25   -292 ?    ?   ?   E . n 
E 2 26   ASP 26   -291 ?    ?   ?   E . n 
E 2 27   LYS 27   -290 ?    ?   ?   E . n 
E 2 28   GLY 28   -289 ?    ?   ?   E . n 
E 2 29   TYR 29   -288 ?    ?   ?   E . n 
E 2 30   ASN 30   -287 ?    ?   ?   E . n 
E 2 31   GLY 31   -286 ?    ?   ?   E . n 
E 2 32   LEU 32   -285 ?    ?   ?   E . n 
E 2 33   ALA 33   -284 ?    ?   ?   E . n 
E 2 34   GLU 34   -283 ?    ?   ?   E . n 
E 2 35   VAL 35   -282 ?    ?   ?   E . n 
E 2 36   GLY 36   -281 ?    ?   ?   E . n 
E 2 37   LYS 37   -280 ?    ?   ?   E . n 
E 2 38   LYS 38   -279 ?    ?   ?   E . n 
E 2 39   PHE 39   -278 ?    ?   ?   E . n 
E 2 40   GLU 40   -277 ?    ?   ?   E . n 
E 2 41   LYS 41   -276 ?    ?   ?   E . n 
E 2 42   ASP 42   -275 ?    ?   ?   E . n 
E 2 43   THR 43   -274 ?    ?   ?   E . n 
E 2 44   GLY 44   -273 ?    ?   ?   E . n 
E 2 45   ILE 45   -272 ?    ?   ?   E . n 
E 2 46   LYS 46   -271 ?    ?   ?   E . n 
E 2 47   VAL 47   -270 ?    ?   ?   E . n 
E 2 48   THR 48   -269 ?    ?   ?   E . n 
E 2 49   VAL 49   -268 ?    ?   ?   E . n 
E 2 50   GLU 50   -267 ?    ?   ?   E . n 
E 2 51   HIS 51   -266 ?    ?   ?   E . n 
E 2 52   PRO 52   -265 ?    ?   ?   E . n 
E 2 53   ASP 53   -264 ?    ?   ?   E . n 
E 2 54   LYS 54   -263 ?    ?   ?   E . n 
E 2 55   LEU 55   -262 ?    ?   ?   E . n 
E 2 56   GLU 56   -261 ?    ?   ?   E . n 
E 2 57   GLU 57   -260 ?    ?   ?   E . n 
E 2 58   LYS 58   -259 ?    ?   ?   E . n 
E 2 59   PHE 59   -258 ?    ?   ?   E . n 
E 2 60   PRO 60   -257 ?    ?   ?   E . n 
E 2 61   GLN 61   -256 ?    ?   ?   E . n 
E 2 62   VAL 62   -255 ?    ?   ?   E . n 
E 2 63   ALA 63   -254 ?    ?   ?   E . n 
E 2 64   ALA 64   -253 ?    ?   ?   E . n 
E 2 65   THR 65   -252 ?    ?   ?   E . n 
E 2 66   GLY 66   -251 ?    ?   ?   E . n 
E 2 67   ASP 67   -250 ?    ?   ?   E . n 
E 2 68   GLY 68   -249 ?    ?   ?   E . n 
E 2 69   PRO 69   -248 ?    ?   ?   E . n 
E 2 70   ASP 70   -247 ?    ?   ?   E . n 
E 2 71   ILE 71   -246 ?    ?   ?   E . n 
E 2 72   ILE 72   -245 ?    ?   ?   E . n 
E 2 73   PHE 73   -244 ?    ?   ?   E . n 
E 2 74   TRP 74   -243 ?    ?   ?   E . n 
E 2 75   ALA 75   -242 ?    ?   ?   E . n 
E 2 76   HIS 76   -241 ?    ?   ?   E . n 
E 2 77   ASP 77   -240 ?    ?   ?   E . n 
E 2 78   ARG 78   -239 ?    ?   ?   E . n 
E 2 79   PHE 79   -238 ?    ?   ?   E . n 
E 2 80   GLY 80   -237 ?    ?   ?   E . n 
E 2 81   GLY 81   -236 ?    ?   ?   E . n 
E 2 82   TYR 82   -235 ?    ?   ?   E . n 
E 2 83   ALA 83   -234 ?    ?   ?   E . n 
E 2 84   GLN 84   -233 ?    ?   ?   E . n 
E 2 85   SER 85   -232 ?    ?   ?   E . n 
E 2 86   GLY 86   -231 ?    ?   ?   E . n 
E 2 87   LEU 87   -230 ?    ?   ?   E . n 
E 2 88   LEU 88   -229 ?    ?   ?   E . n 
E 2 89   ALA 89   -228 ?    ?   ?   E . n 
E 2 90   GLU 90   -227 ?    ?   ?   E . n 
E 2 91   ILE 91   -226 ?    ?   ?   E . n 
E 2 92   THR 92   -225 ?    ?   ?   E . n 
E 2 93   PRO 93   -224 ?    ?   ?   E . n 
E 2 94   ASP 94   -223 ?    ?   ?   E . n 
E 2 95   LYS 95   -222 ?    ?   ?   E . n 
E 2 96   ALA 96   -221 ?    ?   ?   E . n 
E 2 97   PHE 97   -220 ?    ?   ?   E . n 
E 2 98   GLN 98   -219 ?    ?   ?   E . n 
E 2 99   ASP 99   -218 ?    ?   ?   E . n 
E 2 100  LYS 100  -217 ?    ?   ?   E . n 
E 2 101  LEU 101  -216 ?    ?   ?   E . n 
E 2 102  TYR 102  -215 ?    ?   ?   E . n 
E 2 103  PRO 103  -214 ?    ?   ?   E . n 
E 2 104  PHE 104  -213 ?    ?   ?   E . n 
E 2 105  THR 105  -212 ?    ?   ?   E . n 
E 2 106  TRP 106  -211 ?    ?   ?   E . n 
E 2 107  ASP 107  -210 ?    ?   ?   E . n 
E 2 108  ALA 108  -209 ?    ?   ?   E . n 
E 2 109  VAL 109  -208 ?    ?   ?   E . n 
E 2 110  ARG 110  -207 ?    ?   ?   E . n 
E 2 111  TYR 111  -206 ?    ?   ?   E . n 
E 2 112  ASN 112  -205 ?    ?   ?   E . n 
E 2 113  GLY 113  -204 ?    ?   ?   E . n 
E 2 114  LYS 114  -203 ?    ?   ?   E . n 
E 2 115  LEU 115  -202 ?    ?   ?   E . n 
E 2 116  ILE 116  -201 ?    ?   ?   E . n 
E 2 117  ALA 117  -200 ?    ?   ?   E . n 
E 2 118  TYR 118  -199 ?    ?   ?   E . n 
E 2 119  PRO 119  -198 ?    ?   ?   E . n 
E 2 120  ILE 120  -197 ?    ?   ?   E . n 
E 2 121  ALA 121  -196 ?    ?   ?   E . n 
E 2 122  VAL 122  -195 ?    ?   ?   E . n 
E 2 123  GLU 123  -194 ?    ?   ?   E . n 
E 2 124  ALA 124  -193 ?    ?   ?   E . n 
E 2 125  LEU 125  -192 ?    ?   ?   E . n 
E 2 126  SER 126  -191 ?    ?   ?   E . n 
E 2 127  LEU 127  -190 ?    ?   ?   E . n 
E 2 128  ILE 128  -189 ?    ?   ?   E . n 
E 2 129  TYR 129  -188 ?    ?   ?   E . n 
E 2 130  ASN 130  -187 ?    ?   ?   E . n 
E 2 131  LYS 131  -186 ?    ?   ?   E . n 
E 2 132  ASP 132  -185 ?    ?   ?   E . n 
E 2 133  LEU 133  -184 ?    ?   ?   E . n 
E 2 134  LEU 134  -183 ?    ?   ?   E . n 
E 2 135  PRO 135  -182 ?    ?   ?   E . n 
E 2 136  ASN 136  -181 ?    ?   ?   E . n 
E 2 137  PRO 137  -180 ?    ?   ?   E . n 
E 2 138  PRO 138  -179 ?    ?   ?   E . n 
E 2 139  LYS 139  -178 ?    ?   ?   E . n 
E 2 140  THR 140  -177 ?    ?   ?   E . n 
E 2 141  TRP 141  -176 ?    ?   ?   E . n 
E 2 142  GLU 142  -175 ?    ?   ?   E . n 
E 2 143  GLU 143  -174 ?    ?   ?   E . n 
E 2 144  ILE 144  -173 ?    ?   ?   E . n 
E 2 145  PRO 145  -172 ?    ?   ?   E . n 
E 2 146  ALA 146  -171 ?    ?   ?   E . n 
E 2 147  LEU 147  -170 ?    ?   ?   E . n 
E 2 148  ASP 148  -169 ?    ?   ?   E . n 
E 2 149  LYS 149  -168 ?    ?   ?   E . n 
E 2 150  GLU 150  -167 ?    ?   ?   E . n 
E 2 151  LEU 151  -166 ?    ?   ?   E . n 
E 2 152  LYS 152  -165 ?    ?   ?   E . n 
E 2 153  ALA 153  -164 ?    ?   ?   E . n 
E 2 154  LYS 154  -163 ?    ?   ?   E . n 
E 2 155  GLY 155  -162 ?    ?   ?   E . n 
E 2 156  LYS 156  -161 ?    ?   ?   E . n 
E 2 157  SER 157  -160 ?    ?   ?   E . n 
E 2 158  ALA 158  -159 ?    ?   ?   E . n 
E 2 159  LEU 159  -158 ?    ?   ?   E . n 
E 2 160  MET 160  -157 ?    ?   ?   E . n 
E 2 161  PHE 161  -156 ?    ?   ?   E . n 
E 2 162  ASN 162  -155 ?    ?   ?   E . n 
E 2 163  LEU 163  -154 ?    ?   ?   E . n 
E 2 164  GLN 164  -153 ?    ?   ?   E . n 
E 2 165  GLU 165  -152 ?    ?   ?   E . n 
E 2 166  PRO 166  -151 ?    ?   ?   E . n 
E 2 167  TYR 167  -150 ?    ?   ?   E . n 
E 2 168  PHE 168  -149 ?    ?   ?   E . n 
E 2 169  THR 169  -148 ?    ?   ?   E . n 
E 2 170  TRP 170  -147 ?    ?   ?   E . n 
E 2 171  PRO 171  -146 ?    ?   ?   E . n 
E 2 172  LEU 172  -145 ?    ?   ?   E . n 
E 2 173  ILE 173  -144 ?    ?   ?   E . n 
E 2 174  ALA 174  -143 ?    ?   ?   E . n 
E 2 175  ALA 175  -142 ?    ?   ?   E . n 
E 2 176  ASP 176  -141 ?    ?   ?   E . n 
E 2 177  GLY 177  -140 ?    ?   ?   E . n 
E 2 178  GLY 178  -139 ?    ?   ?   E . n 
E 2 179  TYR 179  -138 ?    ?   ?   E . n 
E 2 180  ALA 180  -137 ?    ?   ?   E . n 
E 2 181  PHE 181  -136 ?    ?   ?   E . n 
E 2 182  LYS 182  -135 ?    ?   ?   E . n 
E 2 183  TYR 183  -134 ?    ?   ?   E . n 
E 2 184  GLU 184  -133 ?    ?   ?   E . n 
E 2 185  ASN 185  -132 ?    ?   ?   E . n 
E 2 186  GLY 186  -131 ?    ?   ?   E . n 
E 2 187  LYS 187  -130 ?    ?   ?   E . n 
E 2 188  TYR 188  -129 ?    ?   ?   E . n 
E 2 189  ASP 189  -128 ?    ?   ?   E . n 
E 2 190  ILE 190  -127 ?    ?   ?   E . n 
E 2 191  LYS 191  -126 ?    ?   ?   E . n 
E 2 192  ASP 192  -125 ?    ?   ?   E . n 
E 2 193  VAL 193  -124 ?    ?   ?   E . n 
E 2 194  GLY 194  -123 ?    ?   ?   E . n 
E 2 195  VAL 195  -122 ?    ?   ?   E . n 
E 2 196  ASP 196  -121 ?    ?   ?   E . n 
E 2 197  ASN 197  -120 ?    ?   ?   E . n 
E 2 198  ALA 198  -119 ?    ?   ?   E . n 
E 2 199  GLY 199  -118 ?    ?   ?   E . n 
E 2 200  ALA 200  -117 ?    ?   ?   E . n 
E 2 201  LYS 201  -116 ?    ?   ?   E . n 
E 2 202  ALA 202  -115 ?    ?   ?   E . n 
E 2 203  GLY 203  -114 ?    ?   ?   E . n 
E 2 204  LEU 204  -113 ?    ?   ?   E . n 
E 2 205  THR 205  -112 ?    ?   ?   E . n 
E 2 206  PHE 206  -111 ?    ?   ?   E . n 
E 2 207  LEU 207  -110 ?    ?   ?   E . n 
E 2 208  VAL 208  -109 ?    ?   ?   E . n 
E 2 209  ASP 209  -108 ?    ?   ?   E . n 
E 2 210  LEU 210  -107 ?    ?   ?   E . n 
E 2 211  ILE 211  -106 ?    ?   ?   E . n 
E 2 212  LYS 212  -105 ?    ?   ?   E . n 
E 2 213  ASN 213  -104 ?    ?   ?   E . n 
E 2 214  LYS 214  -103 ?    ?   ?   E . n 
E 2 215  HIS 215  -102 ?    ?   ?   E . n 
E 2 216  MET 216  -101 ?    ?   ?   E . n 
E 2 217  ASN 217  -100 ?    ?   ?   E . n 
E 2 218  ALA 218  -99  ?    ?   ?   E . n 
E 2 219  ASP 219  -98  ?    ?   ?   E . n 
E 2 220  THR 220  -97  ?    ?   ?   E . n 
E 2 221  ASP 221  -96  ?    ?   ?   E . n 
E 2 222  TYR 222  -95  ?    ?   ?   E . n 
E 2 223  SER 223  -94  ?    ?   ?   E . n 
E 2 224  ILE 224  -93  ?    ?   ?   E . n 
E 2 225  ALA 225  -92  ?    ?   ?   E . n 
E 2 226  GLU 226  -91  ?    ?   ?   E . n 
E 2 227  ALA 227  -90  ?    ?   ?   E . n 
E 2 228  ALA 228  -89  ?    ?   ?   E . n 
E 2 229  PHE 229  -88  ?    ?   ?   E . n 
E 2 230  ASN 230  -87  ?    ?   ?   E . n 
E 2 231  LYS 231  -86  ?    ?   ?   E . n 
E 2 232  GLY 232  -85  ?    ?   ?   E . n 
E 2 233  GLU 233  -84  ?    ?   ?   E . n 
E 2 234  THR 234  -83  ?    ?   ?   E . n 
E 2 235  ALA 235  -82  ?    ?   ?   E . n 
E 2 236  MET 236  -81  ?    ?   ?   E . n 
E 2 237  THR 237  -80  ?    ?   ?   E . n 
E 2 238  ILE 238  -79  ?    ?   ?   E . n 
E 2 239  ASN 239  -78  ?    ?   ?   E . n 
E 2 240  GLY 240  -77  ?    ?   ?   E . n 
E 2 241  PRO 241  -76  ?    ?   ?   E . n 
E 2 242  TRP 242  -75  ?    ?   ?   E . n 
E 2 243  ALA 243  -74  ?    ?   ?   E . n 
E 2 244  TRP 244  -73  ?    ?   ?   E . n 
E 2 245  SER 245  -72  ?    ?   ?   E . n 
E 2 246  ASN 246  -71  ?    ?   ?   E . n 
E 2 247  ILE 247  -70  ?    ?   ?   E . n 
E 2 248  ASP 248  -69  ?    ?   ?   E . n 
E 2 249  THR 249  -68  ?    ?   ?   E . n 
E 2 250  SER 250  -67  ?    ?   ?   E . n 
E 2 251  LYS 251  -66  ?    ?   ?   E . n 
E 2 252  VAL 252  -65  ?    ?   ?   E . n 
E 2 253  ASN 253  -64  ?    ?   ?   E . n 
E 2 254  TYR 254  -63  ?    ?   ?   E . n 
E 2 255  GLY 255  -62  ?    ?   ?   E . n 
E 2 256  VAL 256  -61  ?    ?   ?   E . n 
E 2 257  THR 257  -60  ?    ?   ?   E . n 
E 2 258  VAL 258  -59  ?    ?   ?   E . n 
E 2 259  LEU 259  -58  ?    ?   ?   E . n 
E 2 260  PRO 260  -57  ?    ?   ?   E . n 
E 2 261  THR 261  -56  ?    ?   ?   E . n 
E 2 262  PHE 262  -55  ?    ?   ?   E . n 
E 2 263  LYS 263  -54  ?    ?   ?   E . n 
E 2 264  GLY 264  -53  ?    ?   ?   E . n 
E 2 265  GLN 265  -52  ?    ?   ?   E . n 
E 2 266  PRO 266  -51  ?    ?   ?   E . n 
E 2 267  SER 267  -50  ?    ?   ?   E . n 
E 2 268  LYS 268  -49  ?    ?   ?   E . n 
E 2 269  PRO 269  -48  ?    ?   ?   E . n 
E 2 270  PHE 270  -47  ?    ?   ?   E . n 
E 2 271  VAL 271  -46  ?    ?   ?   E . n 
E 2 272  GLY 272  -45  ?    ?   ?   E . n 
E 2 273  VAL 273  -44  ?    ?   ?   E . n 
E 2 274  LEU 274  -43  ?    ?   ?   E . n 
E 2 275  SER 275  -42  ?    ?   ?   E . n 
E 2 276  ALA 276  -41  ?    ?   ?   E . n 
E 2 277  GLY 277  -40  ?    ?   ?   E . n 
E 2 278  ILE 278  -39  ?    ?   ?   E . n 
E 2 279  ASN 279  -38  ?    ?   ?   E . n 
E 2 280  ALA 280  -37  ?    ?   ?   E . n 
E 2 281  ALA 281  -36  ?    ?   ?   E . n 
E 2 282  SER 282  -35  ?    ?   ?   E . n 
E 2 283  PRO 283  -34  ?    ?   ?   E . n 
E 2 284  ASN 284  -33  ?    ?   ?   E . n 
E 2 285  LYS 285  -32  ?    ?   ?   E . n 
E 2 286  GLU 286  -31  ?    ?   ?   E . n 
E 2 287  LEU 287  -30  ?    ?   ?   E . n 
E 2 288  ALA 288  -29  ?    ?   ?   E . n 
E 2 289  LYS 289  -28  ?    ?   ?   E . n 
E 2 290  GLU 290  -27  ?    ?   ?   E . n 
E 2 291  PHE 291  -26  ?    ?   ?   E . n 
E 2 292  LEU 292  -25  ?    ?   ?   E . n 
E 2 293  GLU 293  -24  ?    ?   ?   E . n 
E 2 294  ASN 294  -23  ?    ?   ?   E . n 
E 2 295  TYR 295  -22  ?    ?   ?   E . n 
E 2 296  LEU 296  -21  ?    ?   ?   E . n 
E 2 297  LEU 297  -20  ?    ?   ?   E . n 
E 2 298  THR 298  -19  ?    ?   ?   E . n 
E 2 299  ASP 299  -18  ?    ?   ?   E . n 
E 2 300  GLU 300  -17  ?    ?   ?   E . n 
E 2 301  GLY 301  -16  ?    ?   ?   E . n 
E 2 302  LEU 302  -15  ?    ?   ?   E . n 
E 2 303  GLU 303  -14  ?    ?   ?   E . n 
E 2 304  ALA 304  -13  ?    ?   ?   E . n 
E 2 305  VAL 305  -12  ?    ?   ?   E . n 
E 2 306  ASN 306  -11  ?    ?   ?   E . n 
E 2 307  LYS 307  -10  ?    ?   ?   E . n 
E 2 308  ASP 308  -9   ?    ?   ?   E . n 
E 2 309  LYS 309  -8   ?    ?   ?   E . n 
E 2 310  PRO 310  -7   ?    ?   ?   E . n 
E 2 311  LEU 311  -6   ?    ?   ?   E . n 
E 2 312  GLY 312  -5   ?    ?   ?   E . n 
E 2 313  ALA 313  -4   ?    ?   ?   E . n 
E 2 314  VAL 314  -3   ?    ?   ?   E . n 
E 2 315  ALA 315  -2   ?    ?   ?   E . n 
E 2 316  LEU 316  -1   ?    ?   ?   E . n 
E 2 317  LYS 317  0    ?    ?   ?   E . n 
E 2 318  SER 318  1    ?    ?   ?   E . n 
E 2 319  TYR 319  2    ?    ?   ?   E . n 
E 2 320  GLU 320  3    ?    ?   ?   E . n 
E 2 321  GLU 321  4    ?    ?   ?   E . n 
E 2 322  GLU 322  5    ?    ?   ?   E . n 
E 2 323  LEU 323  6    ?    ?   ?   E . n 
E 2 324  ALA 324  7    ?    ?   ?   E . n 
E 2 325  LYS 325  8    ?    ?   ?   E . n 
E 2 326  ASP 326  9    ?    ?   ?   E . n 
E 2 327  PRO 327  10   ?    ?   ?   E . n 
E 2 328  ARG 328  11   ?    ?   ?   E . n 
E 2 329  ILE 329  12   ?    ?   ?   E . n 
E 2 330  ALA 330  13   ?    ?   ?   E . n 
E 2 331  ALA 331  14   ?    ?   ?   E . n 
E 2 332  THR 332  15   ?    ?   ?   E . n 
E 2 333  MET 333  16   ?    ?   ?   E . n 
E 2 334  GLU 334  17   ?    ?   ?   E . n 
E 2 335  ASN 335  18   ?    ?   ?   E . n 
E 2 336  ALA 336  19   ?    ?   ?   E . n 
E 2 337  GLN 337  20   ?    ?   ?   E . n 
E 2 338  LYS 338  21   ?    ?   ?   E . n 
E 2 339  GLY 339  22   ?    ?   ?   E . n 
E 2 340  GLU 340  23   ?    ?   ?   E . n 
E 2 341  ILE 341  24   ?    ?   ?   E . n 
E 2 342  MET 342  25   ?    ?   ?   E . n 
E 2 343  PRO 343  26   ?    ?   ?   E . n 
E 2 344  ASN 344  27   ?    ?   ?   E . n 
E 2 345  ILE 345  28   ?    ?   ?   E . n 
E 2 346  PRO 346  29   ?    ?   ?   E . n 
E 2 347  GLN 347  30   ?    ?   ?   E . n 
E 2 348  MET 348  31   ?    ?   ?   E . n 
E 2 349  SER 349  32   ?    ?   ?   E . n 
E 2 350  ALA 350  33   ?    ?   ?   E . n 
E 2 351  PHE 351  34   ?    ?   ?   E . n 
E 2 352  TRP 352  35   ?    ?   ?   E . n 
E 2 353  TYR 353  36   ?    ?   ?   E . n 
E 2 354  ALA 354  37   ?    ?   ?   E . n 
E 2 355  VAL 355  38   ?    ?   ?   E . n 
E 2 356  ARG 356  39   ?    ?   ?   E . n 
E 2 357  THR 357  40   ?    ?   ?   E . n 
E 2 358  ALA 358  41   ?    ?   ?   E . n 
E 2 359  VAL 359  42   ?    ?   ?   E . n 
E 2 360  ILE 360  43   ?    ?   ?   E . n 
E 2 361  ASN 361  44   ?    ?   ?   E . n 
E 2 362  ALA 362  45   ?    ?   ?   E . n 
E 2 363  ALA 363  46   ?    ?   ?   E . n 
E 2 364  SER 364  47   ?    ?   ?   E . n 
E 2 365  GLY 365  48   ?    ?   ?   E . n 
E 2 366  ARG 366  49   ?    ?   ?   E . n 
E 2 367  GLN 367  50   ?    ?   ?   E . n 
E 2 368  THR 368  51   ?    ?   ?   E . n 
E 2 369  VAL 369  52   ?    ?   ?   E . n 
E 2 370  ASP 370  53   ?    ?   ?   E . n 
E 2 371  GLU 371  54   ?    ?   ?   E . n 
E 2 372  ALA 372  55   ?    ?   ?   E . n 
E 2 373  LEU 373  56   ?    ?   ?   E . n 
E 2 374  LYS 374  57   ?    ?   ?   E . n 
E 2 375  ASP 375  58   ?    ?   ?   E . n 
E 2 376  ALA 376  59   ?    ?   ?   E . n 
E 2 377  GLN 377  60   ?    ?   ?   E . n 
E 2 378  THR 378  61   ?    ?   ?   E . n 
E 2 379  GLY 379  62   ?    ?   ?   E . n 
E 2 380  THR 380  63   ?    ?   ?   E . n 
E 2 381  ASP 381  64   ?    ?   ?   E . n 
E 2 382  TYR 382  65   ?    ?   ?   E . n 
E 2 383  ASP 383  66   ?    ?   ?   E . n 
E 2 384  ILE 384  67   ?    ?   ?   E . n 
E 2 385  PRO 385  68   ?    ?   ?   E . n 
E 2 386  THR 386  69   ?    ?   ?   E . n 
E 2 387  THR 387  70   ?    ?   ?   E . n 
E 2 388  GLU 388  71   ?    ?   ?   E . n 
E 2 389  ASN 389  72   ?    ?   ?   E . n 
E 2 390  LEU 390  73   ?    ?   ?   E . n 
E 2 391  TYR 391  74   ?    ?   ?   E . n 
E 2 392  PHE 392  75   ?    ?   ?   E . n 
E 2 393  GLN 393  76   ?    ?   ?   E . n 
E 2 394  GLY 394  77   ?    ?   ?   E . n 
E 2 395  GLY 395  78   ?    ?   ?   E . n 
E 2 396  SER 396  79   ?    ?   ?   E . n 
E 2 397  ASN 397  80   ?    ?   ?   E . n 
E 2 398  HIS 398  81   ?    ?   ?   E . n 
E 2 399  SER 399  82   ?    ?   ?   E . n 
E 2 400  PHE 400  83   ?    ?   ?   E . n 
E 2 401  GLU 401  84   ?    ?   ?   E . n 
E 2 402  GLU 402  85   ?    ?   ?   E . n 
E 2 403  VAL 403  86   ?    ?   ?   E . n 
E 2 404  VAL 404  87   ?    ?   ?   E . n 
E 2 405  GLN 405  88   ?    ?   ?   E . n 
E 2 406  THR 406  89   ?    ?   ?   E . n 
E 2 407  LEU 407  90   ?    ?   ?   E . n 
E 2 408  ALA 408  91   ?    ?   ?   E . n 
E 2 409  SER 409  92   ?    ?   ?   E . n 
E 2 410  LEU 410  93   ?    ?   ?   E . n 
E 2 411  ALA 411  94   ?    ?   ?   E . n 
E 2 412  THR 412  95   ?    ?   ?   E . n 
E 2 413  VAL 413  96   ?    ?   ?   E . n 
E 2 414  VAL 414  97   ?    ?   ?   E . n 
E 2 415  GLN 415  98   ?    ?   ?   E . n 
E 2 416  GLN 416  99   ?    ?   ?   E . n 
E 2 417  GLN 417  100  ?    ?   ?   E . n 
E 2 418  THR 418  101  ?    ?   ?   E . n 
E 2 419  ILE 419  102  ?    ?   ?   E . n 
E 2 420  ALA 420  103  ?    ?   ?   E . n 
E 2 421  SER 421  104  ?    ?   ?   E . n 
E 2 422  GLU 422  105  ?    ?   ?   E . n 
E 2 423  SER 423  106  ?    ?   ?   E . n 
E 2 424  LEU 424  107  ?    ?   ?   E . n 
E 2 425  GLU 425  108  ?    ?   ?   E . n 
E 2 426  GLN 426  109  ?    ?   ?   E . n 
E 2 427  ARG 427  110  ?    ?   ?   E . n 
E 2 428  ILE 428  111  ?    ?   ?   E . n 
E 2 429  THR 429  112  ?    ?   ?   E . n 
E 2 430  SER 430  113  ?    ?   ?   E . n 
E 2 431  LEU 431  114  ?    ?   ?   E . n 
E 2 432  GLU 432  115  ?    ?   ?   E . n 
E 2 433  ASN 433  116  ?    ?   ?   E . n 
E 2 434  GLY 434  117  ?    ?   ?   E . n 
E 2 435  LEU 435  118  ?    ?   ?   E . n 
E 2 436  LYS 436  119  ?    ?   ?   E . n 
E 2 437  PRO 437  120  ?    ?   ?   E . n 
E 2 438  VAL 438  121  ?    ?   ?   E . n 
E 2 439  TYR 439  122  ?    ?   ?   E . n 
E 2 440  ASP 440  123  123  ASP ASP E . n 
E 2 441  MET 441  124  124  MET MET E . n 
E 2 442  ALA 442  125  125  ALA ALA E . n 
E 2 443  LYS 443  126  126  LYS LYS E . n 
E 2 444  THR 444  127  127  THR THR E . n 
E 2 445  ILE 445  128  128  ILE ILE E . n 
E 2 446  SER 446  129  129  SER SER E . n 
E 2 447  SER 447  130  130  SER SER E . n 
E 2 448  LEU 448  131  131  LEU LEU E . n 
E 2 449  ASN 449  132  132  ASN ASN E . n 
E 2 450  ARG 450  133  133  ARG ARG E . n 
E 2 451  VAL 451  134  134  VAL VAL E . n 
E 2 452  CYS 452  135  135  CYS CYS E . n 
E 2 453  ALA 453  136  136  ALA ALA E . n 
E 2 454  GLU 454  137  137  GLU GLU E . n 
E 2 455  MET 455  138  138  MET MET E . n 
E 2 456  VAL 456  139  139  VAL VAL E . n 
E 2 457  ALA 457  140  140  ALA ALA E . n 
E 2 458  LYS 458  141  141  LYS LYS E . n 
E 2 459  TYR 459  142  142  TYR TYR E . n 
E 2 460  ASP 460  143  143  ASP ASP E . n 
E 2 461  LEU 461  144  144  LEU LEU E . n 
E 2 462  LEU 462  145  145  LEU LEU E . n 
E 2 463  VAL 463  146  146  VAL VAL E . n 
E 2 464  MET 464  147  ?    ?   ?   E . n 
E 2 465  THR 465  148  ?    ?   ?   E . n 
E 2 466  THR 466  149  ?    ?   ?   E . n 
E 2 467  GLY 467  150  ?    ?   ?   E . n 
E 2 468  ARG 468  151  ?    ?   ?   E . n 
E 2 469  ALA 469  152  ?    ?   ?   E . n 
E 2 470  THR 470  153  ?    ?   ?   E . n 
E 2 471  ALA 471  154  ?    ?   ?   E . n 
E 2 472  THR 472  155  ?    ?   ?   E . n 
E 2 473  ALA 473  156  ?    ?   ?   E . n 
E 2 474  ALA 474  157  ?    ?   ?   E . n 
E 2 475  ALA 475  158  ?    ?   ?   E . n 
E 2 476  THR 476  159  ?    ?   ?   E . n 
E 2 477  GLU 477  160  ?    ?   ?   E . n 
E 2 478  ALA 478  161  ?    ?   ?   E . n 
E 2 479  TYR 479  162  ?    ?   ?   E . n 
E 2 480  TRP 480  163  ?    ?   ?   E . n 
E 2 481  ALA 481  164  ?    ?   ?   E . n 
E 2 482  GLU 482  165  ?    ?   ?   E . n 
E 2 483  HIS 483  166  ?    ?   ?   E . n 
E 2 484  GLY 484  167  ?    ?   ?   E . n 
E 2 485  GLN 485  168  ?    ?   ?   E . n 
E 2 486  PRO 486  169  ?    ?   ?   E . n 
E 2 487  PRO 487  170  ?    ?   ?   E . n 
E 2 488  PRO 488  171  ?    ?   ?   E . n 
E 2 489  GLY 489  172  ?    ?   ?   E . n 
E 2 490  PRO 490  173  ?    ?   ?   E . n 
E 2 491  SER 491  174  ?    ?   ?   E . n 
E 2 492  LEU 492  175  ?    ?   ?   E . n 
E 2 493  TYR 493  176  ?    ?   ?   E . n 
E 2 494  GLU 494  177  ?    ?   ?   E . n 
E 2 495  GLU 495  178  ?    ?   ?   E . n 
E 2 496  SER 496  179  ?    ?   ?   E . n 
E 2 497  ALA 497  180  ?    ?   ?   E . n 
E 2 498  ILE 498  181  ?    ?   ?   E . n 
E 2 499  ARG 499  182  ?    ?   ?   E . n 
E 2 500  GLY 500  183  ?    ?   ?   E . n 
E 2 501  LYS 501  184  ?    ?   ?   E . n 
E 2 502  ILE 502  185  ?    ?   ?   E . n 
E 2 503  GLU 503  186  ?    ?   ?   E . n 
E 2 504  SER 504  187  ?    ?   ?   E . n 
E 2 505  ARG 505  188  ?    ?   ?   E . n 
E 2 506  ASP 506  189  ?    ?   ?   E . n 
E 2 507  GLU 507  190  ?    ?   ?   E . n 
E 2 508  THR 508  191  ?    ?   ?   E . n 
E 2 509  VAL 509  192  ?    ?   ?   E . n 
E 2 510  PRO 510  193  ?    ?   ?   E . n 
E 2 511  GLN 511  194  ?    ?   ?   E . n 
E 2 512  SER 512  195  ?    ?   ?   E . n 
E 2 513  VAL 513  196  ?    ?   ?   E . n 
E 2 514  ARG 514  197  ?    ?   ?   E . n 
E 2 515  GLU 515  198  ?    ?   ?   E . n 
E 2 516  ALA 516  199  ?    ?   ?   E . n 
E 2 517  PHE 517  200  ?    ?   ?   E . n 
E 2 518  ASN 518  201  ?    ?   ?   E . n 
E 2 519  ASN 519  202  ?    ?   ?   E . n 
E 2 520  LEU 520  203  ?    ?   ?   E . n 
E 2 521  ASN 521  204  ?    ?   ?   E . n 
E 2 522  SER 522  205  ?    ?   ?   E . n 
E 2 523  THR 523  206  ?    ?   ?   E . n 
E 2 524  THR 524  207  ?    ?   ?   E . n 
E 2 525  SER 525  208  ?    ?   ?   E . n 
E 2 526  LEU 526  209  ?    ?   ?   E . n 
E 2 527  THR 527  210  ?    ?   ?   E . n 
E 2 528  GLU 528  211  ?    ?   ?   E . n 
E 2 529  GLU 529  212  ?    ?   ?   E . n 
E 2 530  ASN 530  213  ?    ?   ?   E . n 
E 2 531  PHE 531  214  ?    ?   ?   E . n 
E 2 532  GLY 532  215  ?    ?   ?   E . n 
E 2 533  LYS 533  216  ?    ?   ?   E . n 
E 2 534  PRO 534  217  ?    ?   ?   E . n 
E 2 535  ASP 535  218  ?    ?   ?   E . n 
E 2 536  ILE 536  219  ?    ?   ?   E . n 
E 2 537  SER 537  220  ?    ?   ?   E . n 
E 2 538  ALA 538  221  ?    ?   ?   E . n 
E 2 539  LYS 539  222  ?    ?   ?   E . n 
E 2 540  ASP 540  223  ?    ?   ?   E . n 
E 2 541  LEU 541  224  ?    ?   ?   E . n 
E 2 542  ARG 542  225  ?    ?   ?   E . n 
E 2 543  ASN 543  226  ?    ?   ?   E . n 
E 2 544  ILE 544  227  ?    ?   ?   E . n 
E 2 545  MET 545  228  ?    ?   ?   E . n 
E 2 546  TYR 546  229  ?    ?   ?   E . n 
E 2 547  ASP 547  230  ?    ?   ?   E . n 
E 2 548  HIS 548  231  ?    ?   ?   E . n 
E 2 549  LEU 549  232  ?    ?   ?   E . n 
E 2 550  PRO 550  233  ?    ?   ?   E . n 
E 2 551  GLY 551  234  ?    ?   ?   E . n 
E 2 552  PHE 552  235  ?    ?   ?   E . n 
E 2 553  GLY 553  236  ?    ?   ?   E . n 
E 2 554  THR 554  237  ?    ?   ?   E . n 
E 2 555  ALA 555  238  ?    ?   ?   E . n 
E 2 556  PHE 556  239  ?    ?   ?   E . n 
E 2 557  HIS 557  240  ?    ?   ?   E . n 
E 2 558  GLN 558  241  ?    ?   ?   E . n 
E 2 559  LEU 559  242  ?    ?   ?   E . n 
E 2 560  VAL 560  243  ?    ?   ?   E . n 
E 2 561  GLN 561  244  ?    ?   ?   E . n 
E 2 562  VAL 562  245  ?    ?   ?   E . n 
E 2 563  ILE 563  246  ?    ?   ?   E . n 
E 2 564  CYS 564  247  ?    ?   ?   E . n 
E 2 565  LYS 565  248  ?    ?   ?   E . n 
E 2 566  LEU 566  249  ?    ?   ?   E . n 
E 2 567  GLY 567  250  ?    ?   ?   E . n 
E 2 568  LYS 568  251  ?    ?   ?   E . n 
E 2 569  ASP 569  252  ?    ?   ?   E . n 
E 2 570  SER 570  253  ?    ?   ?   E . n 
E 2 571  ASN 571  254  ?    ?   ?   E . n 
E 2 572  SER 572  255  ?    ?   ?   E . n 
E 2 573  LEU 573  256  ?    ?   ?   E . n 
E 2 574  ASP 574  257  ?    ?   ?   E . n 
E 2 575  ILE 575  258  ?    ?   ?   E . n 
E 2 576  ILE 576  259  ?    ?   ?   E . n 
E 2 577  HIS 577  260  ?    ?   ?   E . n 
E 2 578  ALA 578  261  ?    ?   ?   E . n 
E 2 579  GLU 579  262  ?    ?   ?   E . n 
E 2 580  PHE 580  263  ?    ?   ?   E . n 
E 2 581  GLN 581  264  ?    ?   ?   E . n 
E 2 582  ALA 582  265  ?    ?   ?   E . n 
E 2 583  SER 583  266  ?    ?   ?   E . n 
E 2 584  LEU 584  267  ?    ?   ?   E . n 
E 2 585  ALA 585  268  ?    ?   ?   E . n 
E 2 586  GLU 586  269  ?    ?   ?   E . n 
E 2 587  GLY 587  270  ?    ?   ?   E . n 
E 2 588  ASP 588  271  ?    ?   ?   E . n 
E 2 589  SER 589  272  ?    ?   ?   E . n 
E 2 590  PRO 590  273  ?    ?   ?   E . n 
E 2 591  GLN 591  274  ?    ?   ?   E . n 
E 2 592  CYS 592  275  ?    ?   ?   E . n 
E 2 593  ALA 593  276  ?    ?   ?   E . n 
E 2 594  LEU 594  277  ?    ?   ?   E . n 
E 2 595  ILE 595  278  ?    ?   ?   E . n 
E 2 596  GLN 596  279  ?    ?   ?   E . n 
E 2 597  ILE 597  280  ?    ?   ?   E . n 
E 2 598  THR 598  281  ?    ?   ?   E . n 
E 2 599  LYS 599  282  ?    ?   ?   E . n 
E 2 600  ARG 600  283  ?    ?   ?   E . n 
E 2 601  VAL 601  284  ?    ?   ?   E . n 
E 2 602  PRO 602  285  ?    ?   ?   E . n 
E 2 603  ILE 603  286  ?    ?   ?   E . n 
E 2 604  PHE 604  287  ?    ?   ?   E . n 
E 2 605  GLN 605  288  ?    ?   ?   E . n 
E 2 606  ASP 606  289  ?    ?   ?   E . n 
E 2 607  ALA 607  290  ?    ?   ?   E . n 
E 2 608  ALA 608  291  ?    ?   ?   E . n 
E 2 609  PRO 609  292  ?    ?   ?   E . n 
E 2 610  PRO 610  293  ?    ?   ?   E . n 
E 2 611  VAL 611  294  ?    ?   ?   E . n 
E 2 612  ILE 612  295  ?    ?   ?   E . n 
E 2 613  HIS 613  296  ?    ?   ?   E . n 
E 2 614  ILE 614  297  ?    ?   ?   E . n 
E 2 615  ARG 615  298  ?    ?   ?   E . n 
E 2 616  SER 616  299  ?    ?   ?   E . n 
E 2 617  ARG 617  300  ?    ?   ?   E . n 
E 2 618  GLY 618  301  ?    ?   ?   E . n 
E 2 619  ASP 619  302  ?    ?   ?   E . n 
E 2 620  ILE 620  303  ?    ?   ?   E . n 
E 2 621  PRO 621  304  ?    ?   ?   E . n 
E 2 622  ARG 622  305  ?    ?   ?   E . n 
E 2 623  ALA 623  306  ?    ?   ?   E . n 
E 2 624  CYS 624  307  ?    ?   ?   E . n 
E 2 625  GLN 625  308  ?    ?   ?   E . n 
E 2 626  LYS 626  309  ?    ?   ?   E . n 
E 2 627  SER 627  310  ?    ?   ?   E . n 
E 2 628  LEU 628  311  ?    ?   ?   E . n 
E 2 629  ARG 629  312  ?    ?   ?   E . n 
E 2 630  PRO 630  313  ?    ?   ?   E . n 
E 2 631  VAL 631  314  ?    ?   ?   E . n 
E 2 632  PRO 632  315  ?    ?   ?   E . n 
E 2 633  PRO 633  316  ?    ?   ?   E . n 
E 2 634  SER 634  317  ?    ?   ?   E . n 
E 2 635  PRO 635  318  ?    ?   ?   E . n 
E 2 636  LYS 636  319  ?    ?   ?   E . n 
E 2 637  ILE 637  320  ?    ?   ?   E . n 
E 2 638  ASP 638  321  ?    ?   ?   E . n 
E 2 639  ARG 639  322  ?    ?   ?   E . n 
E 2 640  GLY 640  323  ?    ?   ?   E . n 
E 2 641  TRP 641  324  ?    ?   ?   E . n 
E 2 642  VAL 642  325  ?    ?   ?   E . n 
E 2 643  CYS 643  326  ?    ?   ?   E . n 
E 2 644  VAL 644  327  ?    ?   ?   E . n 
E 2 645  PHE 645  328  ?    ?   ?   E . n 
E 2 646  GLN 646  329  ?    ?   ?   E . n 
E 2 647  LEU 647  330  ?    ?   ?   E . n 
E 2 648  GLN 648  331  ?    ?   ?   E . n 
E 2 649  ASP 649  332  ?    ?   ?   E . n 
E 2 650  GLY 650  333  ?    ?   ?   E . n 
E 2 651  LYS 651  334  ?    ?   ?   E . n 
E 2 652  THR 652  335  ?    ?   ?   E . n 
E 2 653  LEU 653  336  ?    ?   ?   E . n 
E 2 654  GLY 654  337  ?    ?   ?   E . n 
E 2 655  LEU 655  338  ?    ?   ?   E . n 
E 2 656  LYS 656  339  ?    ?   ?   E . n 
E 2 657  ILE 657  340  ?    ?   ?   E . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        ZN 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   ZN 
_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        ? 
# 
_pdbx_nonpoly_scheme.asym_id         F 
_pdbx_nonpoly_scheme.entity_id       3 
_pdbx_nonpoly_scheme.mon_id          ZN 
_pdbx_nonpoly_scheme.ndb_seq_num     1 
_pdbx_nonpoly_scheme.pdb_seq_num     1501 
_pdbx_nonpoly_scheme.auth_seq_num    1394 
_pdbx_nonpoly_scheme.pdb_mon_id      ZN 
_pdbx_nonpoly_scheme.auth_mon_id     ZN 
_pdbx_nonpoly_scheme.pdb_strand_id   A 
_pdbx_nonpoly_scheme.pdb_ins_code    . 
# 
_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                     9IP3 
_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                         9IP3 
_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                   9IP3 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9IP3 
_refine.pdbx_refine_id                           'ELECTRON MICROSCOPY' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            3.10 
_refine.ls_d_res_low                             238.08 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     948510 
_refine.ls_number_reflns_R_free                  2064 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.97 
_refine.ls_percent_reflns_R_free                 22 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2456 
_refine.ls_R_factor_R_free                       ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       ? 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.correlation_coeff_I_to_Fcsqd_work        ? 
_refine.correlation_coeff_I_to_Fcsqd_free        ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.72 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.pdbx_method_to_determine_struct          ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 31.36 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.31 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
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' ? 0.013 ? 13782 ? f_bond_d           ? ? 
'ELECTRON MICROSCOPY' ? 1.215 ? 18711 ? f_angle_d          ? ? 
'ELECTRON MICROSCOPY' ? 9.974 ? 1836  ? f_dihedral_angle_d ? ? 
'ELECTRON MICROSCOPY' ? 0.065 ? 2109  ? f_chiral_restr     ? ? 
'ELECTRON MICROSCOPY' ? 0.006 ? 2391  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.correlation_coeff_Fo_to_Fc 
_refine_ls_shell.correlation_coeff_Fo_to_Fc_free 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_work 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_free 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'ELECTRON MICROSCOPY' 3.10 3.17   . . 144 63948 100.00 . . . . 0.4305 . . . . . . . . . . . . . . . 0.4157 
'ELECTRON MICROSCOPY' 3.17 3.25   . . 132 62374 100.00 . . . . 0.4073 . . . . . . . . . . . . . . . 0.3574 
'ELECTRON MICROSCOPY' 3.25 3.34   . . 120 62764 100.00 . . . . 0.3827 . . . . . . . . . . . . . . . 0.4174 
'ELECTRON MICROSCOPY' 3.34 3.44   . . 168 63614 100.00 . . . . 0.3680 . . . . . . . . . . . . . . . 0.3502 
'ELECTRON MICROSCOPY' 3.44 3.55   . . 120 62932 100.00 . . . . 0.3366 . . . . . . . . . . . . . . . 0.3495 
'ELECTRON MICROSCOPY' 3.55 3.68   . . 120 63265 100.00 . . . . 0.3164 . . . . . . . . . . . . . . . 0.3308 
'ELECTRON MICROSCOPY' 3.68 3.82   . . 120 62924 100.00 . . . . 0.2888 . . . . . . . . . . . . . . . 0.2556 
'ELECTRON MICROSCOPY' 3.82 4.00   . . 108 63289 100.00 . . . . 0.2505 . . . . . . . . . . . . . . . 0.2422 
'ELECTRON MICROSCOPY' 4.00 4.21   . . 168 63197 100.00 . . . . 0.2216 . . . . . . . . . . . . . . . 0.2204 
'ELECTRON MICROSCOPY' 4.21 4.47   . . 120 62843 100.00 . . . . 0.2028 . . . . . . . . . . . . . . . 0.2178 
'ELECTRON MICROSCOPY' 4.47 4.82   . . 168 63182 100.00 . . . . 0.1896 . . . . . . . . . . . . . . . 0.2010 
'ELECTRON MICROSCOPY' 4.82 5.30   . . 120 63321 100.00 . . . . 0.1909 . . . . . . . . . . . . . . . 0.2065 
'ELECTRON MICROSCOPY' 5.30 6.07   . . 144 62871 100.00 . . . . 0.2114 . . . . . . . . . . . . . . . 0.2155 
'ELECTRON MICROSCOPY' 6.07 7.64   . . 144 63205 100.00 . . . . 0.2174 . . . . . . . . . . . . . . . 0.2110 
'ELECTRON MICROSCOPY' 7.65 238.08 . . 168 62717 99.00  . . . . 0.1753 . . . . . . . . . . . . . . . 0.1816 
# 
_struct.entry_id                     9IP3 
_struct.title                        
'Cryo-EM structure of the RNA-dependent RNA polymerase complex in a compact conformation from Ebola virus' 
_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        9IP3 
_struct_keywords.text            'RNA-dependent RNA polymerase complex, VIRAL PROTEIN' 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 2 ? 
D N N 2 ? 
E N N 2 ? 
F N N 3 ? 
# 
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 MALE_ECOLI P0AEX9 ? 1 
;EEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPD
KAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIA
ADGGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKVNY
GVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAATME
NAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQT
;
29 
2 UNP L_EBOZM    Q05318 ? 1 
;MATQHTQYPDARLSSPIVLDQCDLVTRACGLYSSYSLNPQLRNCKLPKHIYRLKYDVTVTKFLSDVPVATLPIDFIVPVL
LKALSGNGFCPVEPRCQQFLDEIIKYTMQDALFLKYYLKNVGAQEDCVDEHFQEKILSSIQGNEFLHQMFFWYDLAILTR
RGRLNRGNSRSTWFVHDDLIDILGYGDYVFWKIPISMLPLNTQGIPHAAMDWYQASVFKEAVQGHTHIVSVSTADVLIMC
KDLITCRFNTTLISKIAEIEDPVCSDYPNFKIVSMLYQSGDYLLSILGSDGYKIIKFLEPLCLAKIQLCSKYTERKGRFL
TQMHLAVNHTLEEITEMRALKPSQAQKIREFHRTLIRLEMTPQQLCELFSIQKHWGHPVLHSETAIQKVKKHATVLKALR
PIVIFETYCVFKYSIAKHYFDSQGSWYSVTSDRNLTPGLNSYIKRNQFPPLPMIKELLWEFYHLDHPPLFSTKIISDLSI
FIKDRATAVERTCWDAVFEPNVLGYNPPHKFSTKRVPEQFLEQENFSIENVLSYAQKLEYLLPQYRNFSFSLKEKELNVG
RTFGKLPYPTRNVQTLCEALLADGLAKAFPSNMMVVTEREQKESLLHQASWHHTSDDFGEHATVRGSSFVTDLEKYNLAF
RYEFTAPFIEYCNRCYGVKNVFNWMHYTIPQCYMHVSDYYNPPHNLTLENRDNPPEGPSSYRGHMGGIEGLQQKLWTSIS
CAQISLVEIKTGFKLRSAVMGDNQCITVLSVFPLETDADEQEQSAEDNAARVAASLAKVTSACGIFLKPDETFVHSGFIY
FGKKQYLNGVQLPQSLKTATRMAPLSDAIFDDLQGTLASIGTAFERSISETRHIFPCRITAAFHTFFSVRILQYHHLGFN
KGFDLGQLTLGKPLDFGTISLALAVPQVLGGLSFLNPEKCFYRNLGDPVTSGLFQLKTYLRMIEMDDLFLPLIAKNPGNC
TAIDFVLNPSGLNVPGSQDLTSFLRQIVRRTITLSAKNKLINTLFHASADFEDEMVCKWLLSSTPVMSRFAADIFSRTPS
GKRLQILGYLEGTRTLLASKIINNNTETPVLDRLRKITLQRWSLWFSYLDHCDNILAEALTQITCTVDLAQILREYSWAH
ILEGRPLIGATLPCMIEQFKVFWLKPYEQCPQCSNAKQPGGKPFVSVAVKKHIVSAWPNASRISWTIGDGIPYIGSRTED
KIGQPAIKPKCPSAALREAIELASRLTWVTQGSSNSDLLIKPFLEARVNLSVQEILQMTPSHYSGNIVHRYNDQYSPHSF
MANRMSNSATRLIVSTNTLGEFSGGGQSARDSNIIFQNVINYAVALFDIKFRNTEATDIQYNRAHLHLTKCCTREVPAQY
LTYTSTLDLDLTRYRENELIYDSNPLKGGLNCNISFDNPF
;
1  
3 UNP MALE_ECOLI P0AEX9 ? 2 
;EEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPD
KAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIA
ADGGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKVNY
GVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAATME
NAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQT
;
29 
4 UNP VP35_EBOZM Q05127 ? 2 
;NHSFEEVVQTLASLATVVQQQTIASESLEQRITSLENGLKPVYDMAKTISSLNRVCAEMVAKYDLLVMTTGRATATAAAT
EAYWAEHGQPPPGPSLYEESAIRGKIESRDETVPQSVREAFNNLNSTTSLTEENFGKPDISAKDLRNIMYDHLPGFGTAF
HQLVQVICKLGKDSNSLDIIHAEFQASLAEGDSPQCALIQITKRVPIFQDAAPPVIHIRSRGDIPRACQKSLRPVPPSPK
IDRGWVCVFQLQDGKTLGLKI
;
80 
# 
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 9IP3 A 47  ? 410  ? P0AEX9 29 ? 392  ? -382 -19  
2  2 9IP3 A 430 ? 1829 ? Q05318 1  ? 1400 ? 1    1400 
3  3 9IP3 B 15  ? 378  ? P0AEX9 29 ? 392  ? -302 61   
4  4 9IP3 B 397 ? 657  ? Q05127 80 ? 340  ? 80   340  
5  3 9IP3 C 15  ? 378  ? P0AEX9 29 ? 392  ? -302 61   
6  4 9IP3 C 397 ? 657  ? Q05127 80 ? 340  ? 80   340  
7  3 9IP3 D 15  ? 378  ? P0AEX9 29 ? 392  ? -302 61   
8  4 9IP3 D 397 ? 657  ? Q05127 80 ? 340  ? 80   340  
9  3 9IP3 E 15  ? 378  ? P0AEX9 29 ? 392  ? -302 61   
10 4 9IP3 E 397 ? 657  ? Q05127 80 ? 340  ? 80   340  
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9IP3 MET A 1    ? UNP P0AEX9 ? ? 'initiating methionine' -428 1   
1 9IP3 GLY A 2    ? UNP P0AEX9 ? ? 'expression tag'        -427 2   
1 9IP3 SER A 3    ? UNP P0AEX9 ? ? 'expression tag'        -426 3   
1 9IP3 GLY A 4    ? UNP P0AEX9 ? ? 'expression tag'        -425 4   
1 9IP3 TRP A 5    ? UNP P0AEX9 ? ? 'expression tag'        -424 5   
1 9IP3 SER A 6    ? UNP P0AEX9 ? ? 'expression tag'        -423 6   
1 9IP3 HIS A 7    ? UNP P0AEX9 ? ? 'expression tag'        -422 7   
1 9IP3 PRO A 8    ? UNP P0AEX9 ? ? 'expression tag'        -421 8   
1 9IP3 GLN A 9    ? UNP P0AEX9 ? ? 'expression tag'        -420 9   
1 9IP3 PHE A 10   ? UNP P0AEX9 ? ? 'expression tag'        -419 10  
1 9IP3 GLU A 11   ? UNP P0AEX9 ? ? 'expression tag'        -418 11  
1 9IP3 LYS A 12   ? UNP P0AEX9 ? ? 'expression tag'        -417 12  
1 9IP3 GLY A 13   ? UNP P0AEX9 ? ? 'expression tag'        -416 13  
1 9IP3 GLY A 14   ? UNP P0AEX9 ? ? 'expression tag'        -415 14  
1 9IP3 GLY A 15   ? UNP P0AEX9 ? ? 'expression tag'        -414 15  
1 9IP3 SER A 16   ? UNP P0AEX9 ? ? 'expression tag'        -413 16  
1 9IP3 GLY A 17   ? UNP P0AEX9 ? ? 'expression tag'        -412 17  
1 9IP3 GLY A 18   ? UNP P0AEX9 ? ? 'expression tag'        -411 18  
1 9IP3 GLY A 19   ? UNP P0AEX9 ? ? 'expression tag'        -410 19  
1 9IP3 SER A 20   ? UNP P0AEX9 ? ? 'expression tag'        -409 20  
1 9IP3 GLY A 21   ? UNP P0AEX9 ? ? 'expression tag'        -408 21  
1 9IP3 GLY A 22   ? UNP P0AEX9 ? ? 'expression tag'        -407 22  
1 9IP3 SER A 23   ? UNP P0AEX9 ? ? 'expression tag'        -406 23  
1 9IP3 ALA A 24   ? UNP P0AEX9 ? ? 'expression tag'        -405 24  
1 9IP3 TRP A 25   ? UNP P0AEX9 ? ? 'expression tag'        -404 25  
1 9IP3 SER A 26   ? UNP P0AEX9 ? ? 'expression tag'        -403 26  
1 9IP3 HIS A 27   ? UNP P0AEX9 ? ? 'expression tag'        -402 27  
1 9IP3 PRO A 28   ? UNP P0AEX9 ? ? 'expression tag'        -401 28  
1 9IP3 GLN A 29   ? UNP P0AEX9 ? ? 'expression tag'        -400 29  
1 9IP3 PHE A 30   ? UNP P0AEX9 ? ? 'expression tag'        -399 30  
1 9IP3 GLU A 31   ? UNP P0AEX9 ? ? 'expression tag'        -398 31  
1 9IP3 LYS A 32   ? UNP P0AEX9 ? ? 'expression tag'        -397 32  
1 9IP3 GLY A 33   ? UNP P0AEX9 ? ? 'expression tag'        -396 33  
1 9IP3 SER A 34   ? UNP P0AEX9 ? ? 'expression tag'        -395 34  
1 9IP3 ALA A 35   ? UNP P0AEX9 ? ? 'expression tag'        -394 35  
1 9IP3 SER A 36   ? UNP P0AEX9 ? ? 'expression tag'        -393 36  
1 9IP3 HIS A 37   ? UNP P0AEX9 ? ? 'expression tag'        -392 37  
1 9IP3 HIS A 38   ? UNP P0AEX9 ? ? 'expression tag'        -391 38  
1 9IP3 HIS A 39   ? UNP P0AEX9 ? ? 'expression tag'        -390 39  
1 9IP3 HIS A 40   ? UNP P0AEX9 ? ? 'expression tag'        -389 40  
1 9IP3 HIS A 41   ? UNP P0AEX9 ? ? 'expression tag'        -388 41  
1 9IP3 HIS A 42   ? UNP P0AEX9 ? ? 'expression tag'        -387 42  
1 9IP3 GLY A 43   ? UNP P0AEX9 ? ? 'expression tag'        -386 43  
1 9IP3 THR A 44   ? UNP P0AEX9 ? ? 'expression tag'        -385 44  
1 9IP3 LYS A 45   ? UNP P0AEX9 ? ? 'expression tag'        -384 45  
1 9IP3 THR A 46   ? UNP P0AEX9 ? ? 'expression tag'        -383 46  
1 9IP3 GLY A 411  ? UNP P0AEX9 ? ? linker                  -18  47  
1 9IP3 THR A 412  ? UNP P0AEX9 ? ? linker                  -17  48  
1 9IP3 ASP A 413  ? UNP P0AEX9 ? ? linker                  -16  49  
1 9IP3 TYR A 414  ? UNP P0AEX9 ? ? linker                  -15  50  
1 9IP3 ASP A 415  ? UNP P0AEX9 ? ? linker                  -14  51  
1 9IP3 ILE A 416  ? UNP P0AEX9 ? ? linker                  -13  52  
1 9IP3 PRO A 417  ? UNP P0AEX9 ? ? linker                  -12  53  
1 9IP3 THR A 418  ? UNP P0AEX9 ? ? linker                  -11  54  
1 9IP3 THR A 419  ? UNP P0AEX9 ? ? linker                  -10  55  
1 9IP3 LEU A 420  ? UNP P0AEX9 ? ? linker                  -9   56  
1 9IP3 GLU A 421  ? UNP P0AEX9 ? ? linker                  -8   57  
1 9IP3 VAL A 422  ? UNP P0AEX9 ? ? linker                  -7   58  
1 9IP3 LEU A 423  ? UNP P0AEX9 ? ? linker                  -6   59  
1 9IP3 PHE A 424  ? UNP P0AEX9 ? ? linker                  -5   60  
1 9IP3 GLN A 425  ? UNP P0AEX9 ? ? linker                  -4   61  
1 9IP3 GLY A 426  ? UNP P0AEX9 ? ? linker                  -3   62  
1 9IP3 PRO A 427  ? UNP P0AEX9 ? ? linker                  -2   63  
1 9IP3 GLY A 428  ? UNP P0AEX9 ? ? linker                  -1   64  
1 9IP3 SER A 429  ? UNP P0AEX9 ? ? linker                  0    65  
2 9IP3 SER A 1830 ? UNP Q05318 ? ? 'expression tag'        1401 66  
2 9IP3 ARG A 1831 ? UNP Q05318 ? ? 'expression tag'        1402 67  
2 9IP3 ASP A 1832 ? UNP Q05318 ? ? 'expression tag'        1403 68  
2 9IP3 TYR A 1833 ? UNP Q05318 ? ? 'expression tag'        1404 69  
2 9IP3 LYS A 1834 ? UNP Q05318 ? ? 'expression tag'        1405 70  
2 9IP3 ASP A 1835 ? UNP Q05318 ? ? 'expression tag'        1406 71  
2 9IP3 ASP A 1836 ? UNP Q05318 ? ? 'expression tag'        1407 72  
2 9IP3 ASP A 1837 ? UNP Q05318 ? ? 'expression tag'        1408 73  
2 9IP3 ASP A 1838 ? UNP Q05318 ? ? 'expression tag'        1409 74  
2 9IP3 LYS A 1839 ? UNP Q05318 ? ? 'expression tag'        1410 75  
3 9IP3 MET B 1    ? UNP P0AEX9 ? ? 'initiating methionine' -316 76  
3 9IP3 GLY B 2    ? UNP P0AEX9 ? ? 'expression tag'        -315 77  
3 9IP3 SER B 3    ? UNP P0AEX9 ? ? 'expression tag'        -314 78  
3 9IP3 SER B 4    ? UNP P0AEX9 ? ? 'expression tag'        -313 79  
3 9IP3 HIS B 5    ? UNP P0AEX9 ? ? 'expression tag'        -312 80  
3 9IP3 HIS B 6    ? UNP P0AEX9 ? ? 'expression tag'        -311 81  
3 9IP3 HIS B 7    ? UNP P0AEX9 ? ? 'expression tag'        -310 82  
3 9IP3 HIS B 8    ? UNP P0AEX9 ? ? 'expression tag'        -309 83  
3 9IP3 HIS B 9    ? UNP P0AEX9 ? ? 'expression tag'        -308 84  
3 9IP3 HIS B 10   ? UNP P0AEX9 ? ? 'expression tag'        -307 85  
3 9IP3 GLY B 11   ? UNP P0AEX9 ? ? 'expression tag'        -306 86  
3 9IP3 THR B 12   ? UNP P0AEX9 ? ? 'expression tag'        -305 87  
3 9IP3 LYS B 13   ? UNP P0AEX9 ? ? 'expression tag'        -304 88  
3 9IP3 THR B 14   ? UNP P0AEX9 ? ? 'expression tag'        -303 89  
3 9IP3 GLY B 379  ? UNP P0AEX9 ? ? linker                  62   90  
3 9IP3 THR B 380  ? UNP P0AEX9 ? ? linker                  63   91  
3 9IP3 ASP B 381  ? UNP P0AEX9 ? ? linker                  64   92  
3 9IP3 TYR B 382  ? UNP P0AEX9 ? ? linker                  65   93  
3 9IP3 ASP B 383  ? UNP P0AEX9 ? ? linker                  66   94  
3 9IP3 ILE B 384  ? UNP P0AEX9 ? ? linker                  67   95  
3 9IP3 PRO B 385  ? UNP P0AEX9 ? ? linker                  68   96  
3 9IP3 THR B 386  ? UNP P0AEX9 ? ? linker                  69   97  
3 9IP3 THR B 387  ? UNP P0AEX9 ? ? linker                  70   98  
3 9IP3 GLU B 388  ? UNP P0AEX9 ? ? linker                  71   99  
3 9IP3 ASN B 389  ? UNP P0AEX9 ? ? linker                  72   100 
3 9IP3 LEU B 390  ? UNP P0AEX9 ? ? linker                  73   101 
3 9IP3 TYR B 391  ? UNP P0AEX9 ? ? linker                  74   102 
3 9IP3 PHE B 392  ? UNP P0AEX9 ? ? linker                  75   103 
3 9IP3 GLN B 393  ? UNP P0AEX9 ? ? linker                  76   104 
3 9IP3 GLY B 394  ? UNP P0AEX9 ? ? linker                  77   105 
3 9IP3 GLY B 395  ? UNP P0AEX9 ? ? linker                  78   106 
3 9IP3 SER B 396  ? UNP P0AEX9 ? ? linker                  79   107 
5 9IP3 MET C 1    ? UNP P0AEX9 ? ? 'initiating methionine' -316 108 
5 9IP3 GLY C 2    ? UNP P0AEX9 ? ? 'expression tag'        -315 109 
5 9IP3 SER C 3    ? UNP P0AEX9 ? ? 'expression tag'        -314 110 
5 9IP3 SER C 4    ? UNP P0AEX9 ? ? 'expression tag'        -313 111 
5 9IP3 HIS C 5    ? UNP P0AEX9 ? ? 'expression tag'        -312 112 
5 9IP3 HIS C 6    ? UNP P0AEX9 ? ? 'expression tag'        -311 113 
5 9IP3 HIS C 7    ? UNP P0AEX9 ? ? 'expression tag'        -310 114 
5 9IP3 HIS C 8    ? UNP P0AEX9 ? ? 'expression tag'        -309 115 
5 9IP3 HIS C 9    ? UNP P0AEX9 ? ? 'expression tag'        -308 116 
5 9IP3 HIS C 10   ? UNP P0AEX9 ? ? 'expression tag'        -307 117 
5 9IP3 GLY C 11   ? UNP P0AEX9 ? ? 'expression tag'        -306 118 
5 9IP3 THR C 12   ? UNP P0AEX9 ? ? 'expression tag'        -305 119 
5 9IP3 LYS C 13   ? UNP P0AEX9 ? ? 'expression tag'        -304 120 
5 9IP3 THR C 14   ? UNP P0AEX9 ? ? 'expression tag'        -303 121 
5 9IP3 GLY C 379  ? UNP P0AEX9 ? ? linker                  62   122 
5 9IP3 THR C 380  ? UNP P0AEX9 ? ? linker                  63   123 
5 9IP3 ASP C 381  ? UNP P0AEX9 ? ? linker                  64   124 
5 9IP3 TYR C 382  ? UNP P0AEX9 ? ? linker                  65   125 
5 9IP3 ASP C 383  ? UNP P0AEX9 ? ? linker                  66   126 
5 9IP3 ILE C 384  ? UNP P0AEX9 ? ? linker                  67   127 
5 9IP3 PRO C 385  ? UNP P0AEX9 ? ? linker                  68   128 
5 9IP3 THR C 386  ? UNP P0AEX9 ? ? linker                  69   129 
5 9IP3 THR C 387  ? UNP P0AEX9 ? ? linker                  70   130 
5 9IP3 GLU C 388  ? UNP P0AEX9 ? ? linker                  71   131 
5 9IP3 ASN C 389  ? UNP P0AEX9 ? ? linker                  72   132 
5 9IP3 LEU C 390  ? UNP P0AEX9 ? ? linker                  73   133 
5 9IP3 TYR C 391  ? UNP P0AEX9 ? ? linker                  74   134 
5 9IP3 PHE C 392  ? UNP P0AEX9 ? ? linker                  75   135 
5 9IP3 GLN C 393  ? UNP P0AEX9 ? ? linker                  76   136 
5 9IP3 GLY C 394  ? UNP P0AEX9 ? ? linker                  77   137 
5 9IP3 GLY C 395  ? UNP P0AEX9 ? ? linker                  78   138 
5 9IP3 SER C 396  ? UNP P0AEX9 ? ? linker                  79   139 
7 9IP3 MET D 1    ? UNP P0AEX9 ? ? 'initiating methionine' -316 140 
7 9IP3 GLY D 2    ? UNP P0AEX9 ? ? 'expression tag'        -315 141 
7 9IP3 SER D 3    ? UNP P0AEX9 ? ? 'expression tag'        -314 142 
7 9IP3 SER D 4    ? UNP P0AEX9 ? ? 'expression tag'        -313 143 
7 9IP3 HIS D 5    ? UNP P0AEX9 ? ? 'expression tag'        -312 144 
7 9IP3 HIS D 6    ? UNP P0AEX9 ? ? 'expression tag'        -311 145 
7 9IP3 HIS D 7    ? UNP P0AEX9 ? ? 'expression tag'        -310 146 
7 9IP3 HIS D 8    ? UNP P0AEX9 ? ? 'expression tag'        -309 147 
7 9IP3 HIS D 9    ? UNP P0AEX9 ? ? 'expression tag'        -308 148 
7 9IP3 HIS D 10   ? UNP P0AEX9 ? ? 'expression tag'        -307 149 
7 9IP3 GLY D 11   ? UNP P0AEX9 ? ? 'expression tag'        -306 150 
7 9IP3 THR D 12   ? UNP P0AEX9 ? ? 'expression tag'        -305 151 
7 9IP3 LYS D 13   ? UNP P0AEX9 ? ? 'expression tag'        -304 152 
7 9IP3 THR D 14   ? UNP P0AEX9 ? ? 'expression tag'        -303 153 
7 9IP3 GLY D 379  ? UNP P0AEX9 ? ? linker                  62   154 
7 9IP3 THR D 380  ? UNP P0AEX9 ? ? linker                  63   155 
7 9IP3 ASP D 381  ? UNP P0AEX9 ? ? linker                  64   156 
7 9IP3 TYR D 382  ? UNP P0AEX9 ? ? linker                  65   157 
7 9IP3 ASP D 383  ? UNP P0AEX9 ? ? linker                  66   158 
7 9IP3 ILE D 384  ? UNP P0AEX9 ? ? linker                  67   159 
7 9IP3 PRO D 385  ? UNP P0AEX9 ? ? linker                  68   160 
7 9IP3 THR D 386  ? UNP P0AEX9 ? ? linker                  69   161 
7 9IP3 THR D 387  ? UNP P0AEX9 ? ? linker                  70   162 
7 9IP3 GLU D 388  ? UNP P0AEX9 ? ? linker                  71   163 
7 9IP3 ASN D 389  ? UNP P0AEX9 ? ? linker                  72   164 
7 9IP3 LEU D 390  ? UNP P0AEX9 ? ? linker                  73   165 
7 9IP3 TYR D 391  ? UNP P0AEX9 ? ? linker                  74   166 
7 9IP3 PHE D 392  ? UNP P0AEX9 ? ? linker                  75   167 
7 9IP3 GLN D 393  ? UNP P0AEX9 ? ? linker                  76   168 
7 9IP3 GLY D 394  ? UNP P0AEX9 ? ? linker                  77   169 
7 9IP3 GLY D 395  ? UNP P0AEX9 ? ? linker                  78   170 
7 9IP3 SER D 396  ? UNP P0AEX9 ? ? linker                  79   171 
9 9IP3 MET E 1    ? UNP P0AEX9 ? ? 'initiating methionine' -316 172 
9 9IP3 GLY E 2    ? UNP P0AEX9 ? ? 'expression tag'        -315 173 
9 9IP3 SER E 3    ? UNP P0AEX9 ? ? 'expression tag'        -314 174 
9 9IP3 SER E 4    ? UNP P0AEX9 ? ? 'expression tag'        -313 175 
9 9IP3 HIS E 5    ? UNP P0AEX9 ? ? 'expression tag'        -312 176 
9 9IP3 HIS E 6    ? UNP P0AEX9 ? ? 'expression tag'        -311 177 
9 9IP3 HIS E 7    ? UNP P0AEX9 ? ? 'expression tag'        -310 178 
9 9IP3 HIS E 8    ? UNP P0AEX9 ? ? 'expression tag'        -309 179 
9 9IP3 HIS E 9    ? UNP P0AEX9 ? ? 'expression tag'        -308 180 
9 9IP3 HIS E 10   ? UNP P0AEX9 ? ? 'expression tag'        -307 181 
9 9IP3 GLY E 11   ? UNP P0AEX9 ? ? 'expression tag'        -306 182 
9 9IP3 THR E 12   ? UNP P0AEX9 ? ? 'expression tag'        -305 183 
9 9IP3 LYS E 13   ? UNP P0AEX9 ? ? 'expression tag'        -304 184 
9 9IP3 THR E 14   ? UNP P0AEX9 ? ? 'expression tag'        -303 185 
9 9IP3 GLY E 379  ? UNP P0AEX9 ? ? linker                  62   186 
9 9IP3 THR E 380  ? UNP P0AEX9 ? ? linker                  63   187 
9 9IP3 ASP E 381  ? UNP P0AEX9 ? ? linker                  64   188 
9 9IP3 TYR E 382  ? UNP P0AEX9 ? ? linker                  65   189 
9 9IP3 ASP E 383  ? UNP P0AEX9 ? ? linker                  66   190 
9 9IP3 ILE E 384  ? UNP P0AEX9 ? ? linker                  67   191 
9 9IP3 PRO E 385  ? UNP P0AEX9 ? ? linker                  68   192 
9 9IP3 THR E 386  ? UNP P0AEX9 ? ? linker                  69   193 
9 9IP3 THR E 387  ? UNP P0AEX9 ? ? linker                  70   194 
9 9IP3 GLU E 388  ? UNP P0AEX9 ? ? linker                  71   195 
9 9IP3 ASN E 389  ? UNP P0AEX9 ? ? linker                  72   196 
9 9IP3 LEU E 390  ? UNP P0AEX9 ? ? linker                  73   197 
9 9IP3 TYR E 391  ? UNP P0AEX9 ? ? linker                  74   198 
9 9IP3 PHE E 392  ? UNP P0AEX9 ? ? linker                  75   199 
9 9IP3 GLN E 393  ? UNP P0AEX9 ? ? linker                  76   200 
9 9IP3 GLY E 394  ? UNP P0AEX9 ? ? linker                  77   201 
9 9IP3 GLY E 395  ? UNP P0AEX9 ? ? linker                  78   202 
9 9IP3 SER E 396  ? UNP P0AEX9 ? ? linker                  79   203 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   pentameric 
_pdbx_struct_assembly.oligomeric_count     5 
# 
_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 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'electron microscopy' 
_pdbx_struct_assembly_auth_evidence.details                'not applicable' 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   ? 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 GLN A 450  ? GLY A 459  ? GLN A 21   GLY A 30   1 ? 10 
HELX_P HELX_P2  AA2 PRO A 468  ? CYS A 473  ? PRO A 39   CYS A 44   1 ? 6  
HELX_P HELX_P3  AA3 PRO A 476  ? ARG A 481  ? PRO A 47   ARG A 52   1 ? 6  
HELX_P HELX_P4  AA4 LEU A 482  ? TYR A 484  ? LEU A 53   TYR A 55   5 ? 3  
HELX_P HELX_P5  AA5 ASP A 485  ? LEU A 492  ? ASP A 56   LEU A 63   1 ? 8  
HELX_P HELX_P6  AA6 PRO A 501  ? LEU A 513  ? PRO A 72   LEU A 84   1 ? 13 
HELX_P HELX_P7  AA7 ARG A 524  ? GLY A 551  ? ARG A 95   GLY A 122  1 ? 28 
HELX_P HELX_P8  AA8 HIS A 560  ? ASN A 572  ? HIS A 131  ASN A 143  1 ? 13 
HELX_P HELX_P9  AA9 PHE A 574  ? ASN A 594  ? PHE A 145  ASN A 165  1 ? 21 
HELX_P HELX_P10 AB1 ASN A 597  ? THR A 601  ? ASN A 168  THR A 172  5 ? 5  
HELX_P HELX_P11 AB2 SER A 625  ? LEU A 627  ? SER A 196  LEU A 198  5 ? 3  
HELX_P HELX_P12 AB3 PRO A 635  ? TYR A 642  ? PRO A 206  TYR A 213  1 ? 8  
HELX_P HELX_P13 AB4 VAL A 646  ? VAL A 651  ? VAL A 217  VAL A 222  1 ? 6  
HELX_P HELX_P14 AB5 ALA A 663  ? ASP A 690  ? ALA A 234  ASP A 261  1 ? 28 
HELX_P HELX_P15 AB6 ASN A 698  ? GLY A 717  ? ASN A 269  GLY A 288  1 ? 20 
HELX_P HELX_P16 AB7 GLY A 720  ? LYS A 725  ? GLY A 291  LYS A 296  1 ? 6  
HELX_P HELX_P17 AB8 PHE A 726  ? LEU A 737  ? PHE A 297  LEU A 308  1 ? 12 
HELX_P HELX_P18 AB9 THR A 742  ? GLU A 765  ? THR A 313  GLU A 336  1 ? 24 
HELX_P HELX_P19 AC1 LYS A 770  ? ARG A 778  ? LYS A 341  ARG A 349  1 ? 9  
HELX_P HELX_P20 AC2 ARG A 778  ? LEU A 787  ? ARG A 349  LEU A 358  1 ? 10 
HELX_P HELX_P21 AC3 THR A 790  ? PHE A 798  ? THR A 361  PHE A 369  1 ? 9  
HELX_P HELX_P22 AC4 SER A 799  ? GLY A 805  ? SER A 370  GLY A 376  5 ? 7  
HELX_P HELX_P23 AC5 HIS A 810  ? THR A 823  ? HIS A 381  THR A 394  1 ? 14 
HELX_P HELX_P24 AC6 ARG A 829  ? GLY A 853  ? ARG A 400  GLY A 424  1 ? 25 
HELX_P HELX_P25 AC7 GLY A 867  ? ASN A 875  ? GLY A 438  ASN A 446  1 ? 9  
HELX_P HELX_P26 AC8 MET A 882  ? LEU A 887  ? MET A 453  LEU A 458  1 ? 6  
HELX_P HELX_P27 AC9 TRP A 888  ? LEU A 893  ? TRP A 459  LEU A 464  5 ? 6  
HELX_P HELX_P28 AD1 LEU A 907  ? LYS A 912  ? LEU A 478  LYS A 483  1 ? 6  
HELX_P HELX_P29 AD2 GLU A 919  ? PHE A 927  ? GLU A 490  PHE A 498  5 ? 9  
HELX_P HELX_P30 AD3 GLU A 928  ? GLY A 933  ? GLU A 499  GLY A 504  1 ? 6  
HELX_P HELX_P31 AD4 ARG A 944  ? GLN A 952  ? ARG A 515  GLN A 523  1 ? 9  
HELX_P HELX_P32 AD5 SER A 956  ? LYS A 966  ? SER A 527  LYS A 537  1 ? 11 
HELX_P HELX_P33 AD6 LEU A 967  ? ARG A 975  ? LEU A 538  ARG A 546  5 ? 9  
HELX_P HELX_P34 AD7 PRO A 996  ? GLY A 1013 ? PRO A 567  GLY A 584  1 ? 18 
HELX_P HELX_P35 AD8 LEU A 1014 ? PHE A 1018 ? LEU A 585  PHE A 589  5 ? 5  
HELX_P HELX_P36 AD9 GLN A 1030 ? ALA A 1038 ? GLN A 601  ALA A 609  1 ? 9  
HELX_P HELX_P37 AE1 LYS A 1064 ? PHE A 1069 ? LYS A 635  PHE A 640  1 ? 6  
HELX_P HELX_P38 AE2 ARG A 1070 ? TYR A 1085 ? ARG A 641  TYR A 656  1 ? 16 
HELX_P HELX_P39 AE3 ASN A 1092 ? ILE A 1098 ? ASN A 663  ILE A 669  1 ? 7  
HELX_P HELX_P40 AE4 PRO A 1099 ? CYS A 1101 ? PRO A 670  CYS A 672  5 ? 3  
HELX_P HELX_P41 AE5 GLN A 1141 ? GLY A 1161 ? GLN A 712  GLY A 732  1 ? 21 
HELX_P HELX_P42 AE6 ASP A 1186 ? GLY A 1213 ? ASP A 757  GLY A 784  1 ? 28 
HELX_P HELX_P43 AE7 SER A 1244 ? THR A 1249 ? SER A 815  THR A 820  1 ? 6  
HELX_P HELX_P44 AE8 ASP A 1261 ? GLU A 1279 ? ASP A 832  GLU A 850  1 ? 19 
HELX_P HELX_P45 AE9 ILE A 1283 ? HIS A 1304 ? ILE A 854  HIS A 875  1 ? 22 
HELX_P HELX_P46 AF1 ASP A 1313 ? GLY A 1320 ? ASP A 884  GLY A 891  1 ? 8  
HELX_P HELX_P47 AF2 ASP A 1324 ? LEU A 1332 ? ASP A 895  LEU A 903  1 ? 9  
HELX_P HELX_P48 AF3 ASN A 1345 ? PHE A 1350 ? ASN A 916  PHE A 921  5 ? 6  
HELX_P HELX_P49 AF4 ASP A 1356 ? ILE A 1372 ? ASP A 927  ILE A 943  1 ? 17 
HELX_P HELX_P50 AF5 MET A 1374 ? ASP A 1376 ? MET A 945  ASP A 947  5 ? 3  
HELX_P HELX_P51 AF6 LEU A 1377 ? ALA A 1383 ? LEU A 948  ALA A 954  1 ? 7  
HELX_P HELX_P52 AF7 THR A 1390 ? ASN A 1397 ? THR A 961  ASN A 968  1 ? 8  
HELX_P HELX_P53 AF8 LEU A 1409 ? ALA A 1425 ? LEU A 980  ALA A 996  1 ? 17 
HELX_P HELX_P54 AF9 ASN A 1427 ? THR A 1432 ? ASN A 998  THR A 1003 1 ? 6  
HELX_P HELX_P55 AG1 SER A 1437 ? LEU A 1450 ? SER A 1008 LEU A 1021 1 ? 14 
HELX_P HELX_P56 AG2 MET A 1456 ? SER A 1465 ? MET A 1027 SER A 1036 1 ? 10 
HELX_P HELX_P57 AG3 THR A 1467 ? GLY A 1477 ? THR A 1038 GLY A 1048 1 ? 11 
HELX_P HELX_P58 AG4 GLY A 1481 ? SER A 1488 ? GLY A 1052 SER A 1059 1 ? 8  
HELX_P HELX_P59 AG5 PRO A 1498 ? SER A 1516 ? PRO A 1069 SER A 1087 1 ? 19 
HELX_P HELX_P60 AG6 ASP A 1522 ? LEU A 1529 ? ASP A 1093 LEU A 1100 1 ? 8  
HELX_P HELX_P61 AG7 CYS A 1534 ? TRP A 1547 ? CYS A 1105 TRP A 1118 1 ? 14 
HELX_P HELX_P62 AG8 TRP A 1547 ? GLU A 1552 ? TRP A 1118 GLU A 1123 1 ? 6  
HELX_P HELX_P63 AG9 CYS A 1563 ? GLN A 1567 ? CYS A 1134 GLN A 1138 1 ? 5  
HELX_P HELX_P64 AH1 CYS A 1579 ? ALA A 1585 ? CYS A 1150 ALA A 1156 1 ? 7  
HELX_P HELX_P65 AH2 ARG A 1611 ? SER A 1613 ? ARG A 1182 SER A 1184 5 ? 3  
HELX_P HELX_P66 AH3 SER A 1642 ? THR A 1659 ? SER A 1213 THR A 1230 1 ? 18 
HELX_P HELX_P67 AH4 ASN A 1664 ? ALA A 1675 ? ASN A 1235 ALA A 1246 1 ? 12 
HELX_P HELX_P68 AH5 SER A 1680 ? THR A 1688 ? SER A 1251 THR A 1259 1 ? 9  
HELX_P HELX_P69 AH6 ASN A 1695 ? GLN A 1703 ? ASN A 1266 GLN A 1274 1 ? 9  
HELX_P HELX_P70 AH7 THR A 1725 ? SER A 1732 ? THR A 1296 SER A 1303 5 ? 8  
HELX_P HELX_P71 AH8 ILE A 1744 ? PHE A 1760 ? ILE A 1315 PHE A 1331 1 ? 17 
HELX_P HELX_P72 AH9 GLU A 1764 ? ILE A 1768 ? GLU A 1335 ILE A 1339 5 ? 5  
HELX_P HELX_P73 AI1 LYS A 1779 ? THR A 1782 ? LYS A 1350 THR A 1353 5 ? 4  
HELX_P HELX_P74 AI2 ASP A 1799 ? GLU A 1805 ? ASP A 1370 GLU A 1376 5 ? 7  
HELX_P HELX_P75 AI3 MET B 441  ? THR B 466  ? MET B 124  THR B 149  1 ? 26 
HELX_P HELX_P76 AI4 THR B 472  ? HIS B 483  ? THR B 155  HIS B 166  1 ? 12 
HELX_P HELX_P77 AI5 GLU B 495  ? GLY B 500  ? GLU B 178  GLY B 183  1 ? 6  
HELX_P HELX_P78 AI6 PRO B 510  ? THR B 523  ? PRO B 193  THR B 206  1 ? 14 
HELX_P HELX_P79 AI7 THR B 524  ? LEU B 526  ? THR B 207  LEU B 209  5 ? 3  
HELX_P HELX_P80 AI8 SER B 537  ? LEU B 549  ? SER B 220  LEU B 232  1 ? 13 
HELX_P HELX_P81 AI9 THR B 554  ? ASN B 571  ? THR B 237  ASN B 254  1 ? 18 
HELX_P HELX_P82 AJ1 SER B 572  ? GLU B 586  ? SER B 255  GLU B 269  1 ? 15 
HELX_P HELX_P83 AJ2 SER B 589  ? VAL B 601  ? SER B 272  VAL B 284  1 ? 13 
HELX_P HELX_P84 AJ3 PRO B 602  ? GLN B 605  ? PRO B 285  GLN B 288  5 ? 4  
HELX_P HELX_P85 AJ4 PRO B 621  ? GLN B 625  ? PRO B 304  GLN B 308  5 ? 5  
HELX_P HELX_P86 AJ5 ALA C 442  ? LEU C 461  ? ALA C 125  LEU C 144  1 ? 20 
HELX_P HELX_P87 AJ6 ALA C 469  ? GLY C 484  ? ALA C 152  GLY C 167  1 ? 16 
HELX_P HELX_P88 AJ7 VAL D 438  ? VAL D 463  ? VAL D 121  VAL D 146  1 ? 26 
HELX_P HELX_P89 AJ8 MET E 441  ? ARG E 450  ? MET E 124  ARG E 133  1 ? 10 
HELX_P HELX_P90 AJ9 VAL E 451  ? VAL E 463  ? VAL E 134  VAL E 146  1 ? 13 
# 
_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 
disulf1 disulf ? ? A CYS 1534 SG  ? ? ? 1_555 A CYS 1781 SG ? ? A CYS 1105 A CYS 1352 1_555 ? ? ? ? ? ? ? 2.046 ? ? 
metalc1 metalc ? ? A CYS 1579 SG  ? ? ? 1_555 F ZN  .    ZN ? ? A CYS 1150 A ZN  1501 1_555 ? ? ? ? ? ? ? 2.227 ? ? 
metalc2 metalc ? ? A CYS 1582 SG  ? ? ? 1_555 F ZN  .    ZN ? ? A CYS 1153 A ZN  1501 1_555 ? ? ? ? ? ? ? 2.275 ? ? 
metalc3 metalc ? ? A HIS 1774 ND1 ? ? ? 1_555 F ZN  .    ZN ? ? A HIS 1345 A ZN  1501 1_555 ? ? ? ? ? ? ? 1.893 ? ? 
metalc4 metalc ? ? A HIS 1776 NE2 ? ? ? 1_555 F ZN  .    ZN ? ? A HIS 1347 A ZN  1501 1_555 ? ? ? ? ? ? ? 1.978 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
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 SG  ? A CYS 1579 ? A CYS 1150 ? 1_555 ZN ? F ZN . ? A ZN 1501 ? 1_555 SG  ? A CYS 1582 ? A CYS 1153 ? 1_555 112.7 ? 
2 SG  ? A CYS 1579 ? A CYS 1150 ? 1_555 ZN ? F ZN . ? A ZN 1501 ? 1_555 ND1 ? A HIS 1774 ? A HIS 1345 ? 1_555 97.1  ? 
3 SG  ? A CYS 1582 ? A CYS 1153 ? 1_555 ZN ? F ZN . ? A ZN 1501 ? 1_555 ND1 ? A HIS 1774 ? A HIS 1345 ? 1_555 119.0 ? 
4 SG  ? A CYS 1579 ? A CYS 1150 ? 1_555 ZN ? F ZN . ? A ZN 1501 ? 1_555 NE2 ? A HIS 1776 ? A HIS 1347 ? 1_555 89.9  ? 
5 SG  ? A CYS 1582 ? A CYS 1153 ? 1_555 ZN ? F ZN . ? A ZN 1501 ? 1_555 NE2 ? A HIS 1776 ? A HIS 1347 ? 1_555 117.5 ? 
6 ND1 ? A HIS 1774 ? A HIS 1345 ? 1_555 ZN ? F ZN . ? A ZN 1501 ? 1_555 NE2 ? A HIS 1776 ? A HIS 1347 ? 1_555 114.2 ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      CYS 
_pdbx_modification_feature.label_asym_id                      A 
_pdbx_modification_feature.label_seq_id                       1534 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     CYS 
_pdbx_modification_feature.modified_residue_label_asym_id     A 
_pdbx_modification_feature.modified_residue_label_seq_id      1781 
_pdbx_modification_feature.modified_residue_label_alt_id      ? 
_pdbx_modification_feature.auth_comp_id                       CYS 
_pdbx_modification_feature.auth_asym_id                       A 
_pdbx_modification_feature.auth_seq_id                        1105 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      CYS 
_pdbx_modification_feature.modified_residue_auth_asym_id      A 
_pdbx_modification_feature.modified_residue_auth_seq_id       1352 
_pdbx_modification_feature.modified_residue_PDB_ins_code      ? 
_pdbx_modification_feature.modified_residue_symmetry          1_555 
_pdbx_modification_feature.comp_id_linking_atom               SG 
_pdbx_modification_feature.modified_residue_id_linking_atom   SG 
_pdbx_modification_feature.modified_residue_id                . 
_pdbx_modification_feature.ref_pcm_id                         . 
_pdbx_modification_feature.ref_comp_id                        . 
_pdbx_modification_feature.type                               None 
_pdbx_modification_feature.category                           'Disulfide bridge' 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 GLU 522  A . ? GLU 93   A PRO 523  A ? PRO 94   A 1 -0.08 
2 TRP 1606 A . ? TRP 1177 A PRO 1607 A ? PRO 1178 A 1 6.20  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 3 ? 
AA3 ? 2 ? 
AA4 ? 4 ? 
AA5 ? 3 ? 
AA6 ? 4 ? 
AA7 ? 2 ? 
AA8 ? 2 ? 
AA9 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA3 1 2 ? parallel      
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AA9 2 3 ? 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 TYR A 617  ? PRO A 623  ? TYR A 188  PRO A 194  
AA1 2 HIS A 656  ? THR A 662  ? HIS A 227  THR A 233  
AA2 1 ALA A 827  ? LEU A 828  ? ALA A 398  LEU A 399  
AA2 2 LEU C 462  ? THR C 465  ? LEU C 145  THR C 148  
AA2 3 SER B 491  ? GLU B 494  ? SER B 174  GLU B 177  
AA3 1 SER A 978  ? PHE A 979  ? SER A 549  PHE A 550  
AA3 2 HIS A 1104 ? VAL A 1105 ? HIS A 675  VAL A 676  
AA4 1 LYS A 1163 ? MET A 1169 ? LYS A 734  MET A 740  
AA4 2 ASN A 1172 ? PHE A 1181 ? ASN A 743  PHE A 752  
AA4 3 THR A 1052 ? ASP A 1061 ? THR A 623  ASP A 632  
AA4 4 PHE A 1222 ? HIS A 1224 ? PHE A 793  HIS A 795  
AA5 1 PHE A 1227 ? ILE A 1228 ? PHE A 798  ILE A 799  
AA5 2 TYR A 1235 ? LEU A 1236 ? TYR A 806  LEU A 807  
AA5 3 VAL A 1239 ? GLN A 1240 ? VAL A 810  GLN A 811  
AA6 1 PHE A 1568 ? LEU A 1573 ? PHE A 1139 LEU A 1144 
AA6 2 ARG A 1772 ? LEU A 1777 ? ARG A 1343 LEU A 1348 
AA6 3 PHE A 1593 ? VAL A 1598 ? PHE A 1164 VAL A 1169 
AA6 4 LEU A 1721 ? SER A 1724 ? LEU A 1292 SER A 1295 
AA7 1 SER A 1604 ? ALA A 1605 ? SER A 1175 ALA A 1176 
AA7 2 THR A 1615 ? ILE A 1616 ? THR A 1186 ILE A 1187 
AA8 1 LYS A 1637 ? PRO A 1638 ? LYS A 1208 PRO A 1209 
AA8 2 LEU A 1819 ? ASN A 1820 ? LEU A 1390 ASN A 1391 
AA9 1 LEU B 628  ? PRO B 630  ? LEU B 311  PRO B 313  
AA9 2 THR B 652  ? LEU B 655  ? THR B 335  LEU B 338  
AA9 3 VAL B 644  ? GLN B 646  ? VAL B 327  GLN B 329  
# 
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 VAL A 618  ? N VAL A 189  O SER A 661  ? O SER A 232  
AA2 1 2 N LEU A 828  ? N LEU A 399  O MET C 464  ? O MET C 147  
AA2 2 3 O VAL C 463  ? O VAL C 146  N TYR B 493  ? N TYR B 176  
AA3 1 2 N PHE A 979  ? N PHE A 550  O HIS A 1104 ? O HIS A 675  
AA4 1 2 N ALA A 1167 ? N ALA A 738  O CYS A 1174 ? O CYS A 745  
AA4 2 3 O VAL A 1177 ? O VAL A 748  N SER A 1056 ? N SER A 627  
AA4 3 4 N SER A 1057 ? N SER A 628  O HIS A 1224 ? O HIS A 795  
AA5 1 2 N ILE A 1228 ? N ILE A 799  O TYR A 1235 ? O TYR A 806  
AA5 2 3 N LEU A 1236 ? N LEU A 807  O VAL A 1239 ? O VAL A 810  
AA6 1 2 N PHE A 1571 ? N PHE A 1142 O HIS A 1774 ? O HIS A 1345 
AA6 2 3 O ALA A 1773 ? O ALA A 1344 N VAL A 1596 ? N VAL A 1167 
AA6 3 4 N SER A 1595 ? N SER A 1166 O SER A 1724 ? O SER A 1295 
AA7 1 2 N SER A 1604 ? N SER A 1175 O ILE A 1616 ? O ILE A 1187 
AA8 1 2 N LYS A 1637 ? N LYS A 1208 O ASN A 1820 ? O ASN A 1391 
AA9 1 2 N ARG B 629  ? N ARG B 312  O GLY B 654  ? O GLY B 337  
AA9 2 3 O LEU B 653  ? O LEU B 336  N PHE B 645  ? N PHE B 328  
# 
_pdbx_entry_details.entry_id                   9IP3 
_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_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1 1 CB  A TRP 1085 ? ? CG  A TRP 1085 ? ? 1.366 1.498 -0.132 0.018 N 
2 1 CG  A TYR 1381 ? ? CD2 A TYR 1381 ? ? 1.497 1.387 0.110  0.013 N 
3 1 CE1 A TYR 1381 ? ? CZ  A TYR 1381 ? ? 1.465 1.381 0.084  0.013 N 
4 1 CB  B TRP 163  ? ? CG  B TRP 163  ? ? 1.389 1.498 -0.109 0.018 N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 CA A LEU 972  ? ? CB A LEU 972  ? ? CG  A LEU 972  ? ? 100.28 115.30 -15.02 2.30 N 
2 1 CB A LEU 1326 ? ? CG A LEU 1326 ? ? CD2 A LEU 1326 ? ? 98.57  111.00 -12.43 1.70 N 
3 1 CB A TYR 1381 ? ? CG A TYR 1381 ? ? CD2 A TYR 1381 ? ? 124.85 121.00 3.85   0.60 N 
4 1 CB A TYR 1381 ? ? CG A TYR 1381 ? ? CD1 A TYR 1381 ? ? 116.58 121.00 -4.42  0.60 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ASP A 65   ? ? -96.52  32.36   
2  1 SER A 216  ? ? 65.34   -0.90   
3  1 GLN A 223  ? ? -96.09  -63.69  
4  1 LEU A 308  ? ? -66.35  1.24    
5  1 SER A 370  ? ? -93.99  49.07   
6  1 ARG A 485  ? ? -174.68 -174.53 
7  1 ASN A 681  ? ? -152.04 83.20   
8  1 ARG A 702  ? ? -94.21  -64.22  
9  1 PHE A 830  ? ? 55.24   -127.10 
10 1 GLU A 850  ? ? -107.41 42.43   
11 1 ASP A 884  ? ? -68.86  97.47   
12 1 ALA A 954  ? ? -59.64  106.23  
13 1 LEU A 980  ? ? -68.60  7.01    
14 1 PHE A 1005 ? ? -102.40 66.94   
15 1 ALA A 1058 ? ? -142.09 12.96   
16 1 LYS A 1157 ? ? -66.14  -77.71  
17 1 GLN A 1158 ? ? -96.87  -62.29  
18 1 THR A 1230 ? ? -97.82  36.42   
19 1 MET A 1285 ? ? -38.64  137.23  
20 1 LEU A 1371 ? ? -65.92  1.11    
21 1 TYR A 1374 ? ? -79.86  24.17   
22 1 LYS B 184  ? ? 55.38   5.35    
23 1 THR B 210  ? ? -126.20 -164.75 
24 1 ASP B 289  ? ? -142.25 10.79   
25 1 ASP B 332  ? ? -93.85  50.64   
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9IP3 
_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                    9IP3 
_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                  3.1 
_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               77587 
_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       '25 mM HEPES, 300 mM NaCl, 1 mM TCEP, 6 mM MgCl2' 
_em_buffer.pH            7.5 
# 
_em_entity_assembly.id                   1 
_em_entity_assembly.parent_id            0 
_em_entity_assembly.source               RECOMBINANT 
_em_entity_assembly.type                 COMPLEX 
_em_entity_assembly.name                 'Ternary complex of L-VP35 core region from Ebola virus' 
_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                        9IP3 
_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             1000 
_em_imaging.nominal_defocus_max             1500 
_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_imaging.objective_aperture              ? 
_em_imaging.microscope_serial_number        ? 
_em_imaging.microscope_version              ? 
# 
_em_vitrification.entry_id              9IP3 
_em_vitrification.id                    1 
_em_vitrification.specimen_id           1 
_em_vitrification.cryogen_name          ETHANE 
_em_vitrification.humidity              ? 
_em_vitrification.temp                  ? 
_em_vitrification.chamber_temperature   ? 
_em_vitrification.instrument            ? 
_em_vitrification.method                ? 
_em_vitrification.time_resolved_state   ? 
_em_vitrification.citation_id           ? 
_em_vitrification.details               ? 
# 
_em_experiment.entry_id                9IP3 
_em_experiment.id                      1 
_em_experiment.reconstruction_method   'SINGLE PARTICLE' 
_em_experiment.aggregation_state       PARTICLE 
_em_experiment.entity_assembly_id      1 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1    1 Y 1 A MET -428 ? A MET 1    
2    1 Y 1 A GLY -427 ? A GLY 2    
3    1 Y 1 A SER -426 ? A SER 3    
4    1 Y 1 A GLY -425 ? A GLY 4    
5    1 Y 1 A TRP -424 ? A TRP 5    
6    1 Y 1 A SER -423 ? A SER 6    
7    1 Y 1 A HIS -422 ? A HIS 7    
8    1 Y 1 A PRO -421 ? A PRO 8    
9    1 Y 1 A GLN -420 ? A GLN 9    
10   1 Y 1 A PHE -419 ? A PHE 10   
11   1 Y 1 A GLU -418 ? A GLU 11   
12   1 Y 1 A LYS -417 ? A LYS 12   
13   1 Y 1 A GLY -416 ? A GLY 13   
14   1 Y 1 A GLY -415 ? A GLY 14   
15   1 Y 1 A GLY -414 ? A GLY 15   
16   1 Y 1 A SER -413 ? A SER 16   
17   1 Y 1 A GLY -412 ? A GLY 17   
18   1 Y 1 A GLY -411 ? A GLY 18   
19   1 Y 1 A GLY -410 ? A GLY 19   
20   1 Y 1 A SER -409 ? A SER 20   
21   1 Y 1 A GLY -408 ? A GLY 21   
22   1 Y 1 A GLY -407 ? A GLY 22   
23   1 Y 1 A SER -406 ? A SER 23   
24   1 Y 1 A ALA -405 ? A ALA 24   
25   1 Y 1 A TRP -404 ? A TRP 25   
26   1 Y 1 A SER -403 ? A SER 26   
27   1 Y 1 A HIS -402 ? A HIS 27   
28   1 Y 1 A PRO -401 ? A PRO 28   
29   1 Y 1 A GLN -400 ? A GLN 29   
30   1 Y 1 A PHE -399 ? A PHE 30   
31   1 Y 1 A GLU -398 ? A GLU 31   
32   1 Y 1 A LYS -397 ? A LYS 32   
33   1 Y 1 A GLY -396 ? A GLY 33   
34   1 Y 1 A SER -395 ? A SER 34   
35   1 Y 1 A ALA -394 ? A ALA 35   
36   1 Y 1 A SER -393 ? A SER 36   
37   1 Y 1 A HIS -392 ? A HIS 37   
38   1 Y 1 A HIS -391 ? A HIS 38   
39   1 Y 1 A HIS -390 ? A HIS 39   
40   1 Y 1 A HIS -389 ? A HIS 40   
41   1 Y 1 A HIS -388 ? A HIS 41   
42   1 Y 1 A HIS -387 ? A HIS 42   
43   1 Y 1 A GLY -386 ? A GLY 43   
44   1 Y 1 A THR -385 ? A THR 44   
45   1 Y 1 A LYS -384 ? A LYS 45   
46   1 Y 1 A THR -383 ? A THR 46   
47   1 Y 1 A GLU -382 ? A GLU 47   
48   1 Y 1 A GLU -381 ? A GLU 48   
49   1 Y 1 A GLY -380 ? A GLY 49   
50   1 Y 1 A LYS -379 ? A LYS 50   
51   1 Y 1 A LEU -378 ? A LEU 51   
52   1 Y 1 A VAL -377 ? A VAL 52   
53   1 Y 1 A ILE -376 ? A ILE 53   
54   1 Y 1 A TRP -375 ? A TRP 54   
55   1 Y 1 A ILE -374 ? A ILE 55   
56   1 Y 1 A ASN -373 ? A ASN 56   
57   1 Y 1 A GLY -372 ? A GLY 57   
58   1 Y 1 A ASP -371 ? A ASP 58   
59   1 Y 1 A LYS -370 ? A LYS 59   
60   1 Y 1 A GLY -369 ? A GLY 60   
61   1 Y 1 A TYR -368 ? A TYR 61   
62   1 Y 1 A ASN -367 ? A ASN 62   
63   1 Y 1 A GLY -366 ? A GLY 63   
64   1 Y 1 A LEU -365 ? A LEU 64   
65   1 Y 1 A ALA -364 ? A ALA 65   
66   1 Y 1 A GLU -363 ? A GLU 66   
67   1 Y 1 A VAL -362 ? A VAL 67   
68   1 Y 1 A GLY -361 ? A GLY 68   
69   1 Y 1 A LYS -360 ? A LYS 69   
70   1 Y 1 A LYS -359 ? A LYS 70   
71   1 Y 1 A PHE -358 ? A PHE 71   
72   1 Y 1 A GLU -357 ? A GLU 72   
73   1 Y 1 A LYS -356 ? A LYS 73   
74   1 Y 1 A ASP -355 ? A ASP 74   
75   1 Y 1 A THR -354 ? A THR 75   
76   1 Y 1 A GLY -353 ? A GLY 76   
77   1 Y 1 A ILE -352 ? A ILE 77   
78   1 Y 1 A LYS -351 ? A LYS 78   
79   1 Y 1 A VAL -350 ? A VAL 79   
80   1 Y 1 A THR -349 ? A THR 80   
81   1 Y 1 A VAL -348 ? A VAL 81   
82   1 Y 1 A GLU -347 ? A GLU 82   
83   1 Y 1 A HIS -346 ? A HIS 83   
84   1 Y 1 A PRO -345 ? A PRO 84   
85   1 Y 1 A ASP -344 ? A ASP 85   
86   1 Y 1 A LYS -343 ? A LYS 86   
87   1 Y 1 A LEU -342 ? A LEU 87   
88   1 Y 1 A GLU -341 ? A GLU 88   
89   1 Y 1 A GLU -340 ? A GLU 89   
90   1 Y 1 A LYS -339 ? A LYS 90   
91   1 Y 1 A PHE -338 ? A PHE 91   
92   1 Y 1 A PRO -337 ? A PRO 92   
93   1 Y 1 A GLN -336 ? A GLN 93   
94   1 Y 1 A VAL -335 ? A VAL 94   
95   1 Y 1 A ALA -334 ? A ALA 95   
96   1 Y 1 A ALA -333 ? A ALA 96   
97   1 Y 1 A THR -332 ? A THR 97   
98   1 Y 1 A GLY -331 ? A GLY 98   
99   1 Y 1 A ASP -330 ? A ASP 99   
100  1 Y 1 A GLY -329 ? A GLY 100  
101  1 Y 1 A PRO -328 ? A PRO 101  
102  1 Y 1 A ASP -327 ? A ASP 102  
103  1 Y 1 A ILE -326 ? A ILE 103  
104  1 Y 1 A ILE -325 ? A ILE 104  
105  1 Y 1 A PHE -324 ? A PHE 105  
106  1 Y 1 A TRP -323 ? A TRP 106  
107  1 Y 1 A ALA -322 ? A ALA 107  
108  1 Y 1 A HIS -321 ? A HIS 108  
109  1 Y 1 A ASP -320 ? A ASP 109  
110  1 Y 1 A ARG -319 ? A ARG 110  
111  1 Y 1 A PHE -318 ? A PHE 111  
112  1 Y 1 A GLY -317 ? A GLY 112  
113  1 Y 1 A GLY -316 ? A GLY 113  
114  1 Y 1 A TYR -315 ? A TYR 114  
115  1 Y 1 A ALA -314 ? A ALA 115  
116  1 Y 1 A GLN -313 ? A GLN 116  
117  1 Y 1 A SER -312 ? A SER 117  
118  1 Y 1 A GLY -311 ? A GLY 118  
119  1 Y 1 A LEU -310 ? A LEU 119  
120  1 Y 1 A LEU -309 ? A LEU 120  
121  1 Y 1 A ALA -308 ? A ALA 121  
122  1 Y 1 A GLU -307 ? A GLU 122  
123  1 Y 1 A ILE -306 ? A ILE 123  
124  1 Y 1 A THR -305 ? A THR 124  
125  1 Y 1 A PRO -304 ? A PRO 125  
126  1 Y 1 A ASP -303 ? A ASP 126  
127  1 Y 1 A LYS -302 ? A LYS 127  
128  1 Y 1 A ALA -301 ? A ALA 128  
129  1 Y 1 A PHE -300 ? A PHE 129  
130  1 Y 1 A GLN -299 ? A GLN 130  
131  1 Y 1 A ASP -298 ? A ASP 131  
132  1 Y 1 A LYS -297 ? A LYS 132  
133  1 Y 1 A LEU -296 ? A LEU 133  
134  1 Y 1 A TYR -295 ? A TYR 134  
135  1 Y 1 A PRO -294 ? A PRO 135  
136  1 Y 1 A PHE -293 ? A PHE 136  
137  1 Y 1 A THR -292 ? A THR 137  
138  1 Y 1 A TRP -291 ? A TRP 138  
139  1 Y 1 A ASP -290 ? A ASP 139  
140  1 Y 1 A ALA -289 ? A ALA 140  
141  1 Y 1 A VAL -288 ? A VAL 141  
142  1 Y 1 A ARG -287 ? A ARG 142  
143  1 Y 1 A TYR -286 ? A TYR 143  
144  1 Y 1 A ASN -285 ? A ASN 144  
145  1 Y 1 A GLY -284 ? A GLY 145  
146  1 Y 1 A LYS -283 ? A LYS 146  
147  1 Y 1 A LEU -282 ? A LEU 147  
148  1 Y 1 A ILE -281 ? A ILE 148  
149  1 Y 1 A ALA -280 ? A ALA 149  
150  1 Y 1 A TYR -279 ? A TYR 150  
151  1 Y 1 A PRO -278 ? A PRO 151  
152  1 Y 1 A ILE -277 ? A ILE 152  
153  1 Y 1 A ALA -276 ? A ALA 153  
154  1 Y 1 A VAL -275 ? A VAL 154  
155  1 Y 1 A GLU -274 ? A GLU 155  
156  1 Y 1 A ALA -273 ? A ALA 156  
157  1 Y 1 A LEU -272 ? A LEU 157  
158  1 Y 1 A SER -271 ? A SER 158  
159  1 Y 1 A LEU -270 ? A LEU 159  
160  1 Y 1 A ILE -269 ? A ILE 160  
161  1 Y 1 A TYR -268 ? A TYR 161  
162  1 Y 1 A ASN -267 ? A ASN 162  
163  1 Y 1 A LYS -266 ? A LYS 163  
164  1 Y 1 A ASP -265 ? A ASP 164  
165  1 Y 1 A LEU -264 ? A LEU 165  
166  1 Y 1 A LEU -263 ? A LEU 166  
167  1 Y 1 A PRO -262 ? A PRO 167  
168  1 Y 1 A ASN -261 ? A ASN 168  
169  1 Y 1 A PRO -260 ? A PRO 169  
170  1 Y 1 A PRO -259 ? A PRO 170  
171  1 Y 1 A LYS -258 ? A LYS 171  
172  1 Y 1 A THR -257 ? A THR 172  
173  1 Y 1 A TRP -256 ? A TRP 173  
174  1 Y 1 A GLU -255 ? A GLU 174  
175  1 Y 1 A GLU -254 ? A GLU 175  
176  1 Y 1 A ILE -253 ? A ILE 176  
177  1 Y 1 A PRO -252 ? A PRO 177  
178  1 Y 1 A ALA -251 ? A ALA 178  
179  1 Y 1 A LEU -250 ? A LEU 179  
180  1 Y 1 A ASP -249 ? A ASP 180  
181  1 Y 1 A LYS -248 ? A LYS 181  
182  1 Y 1 A GLU -247 ? A GLU 182  
183  1 Y 1 A LEU -246 ? A LEU 183  
184  1 Y 1 A LYS -245 ? A LYS 184  
185  1 Y 1 A ALA -244 ? A ALA 185  
186  1 Y 1 A LYS -243 ? A LYS 186  
187  1 Y 1 A GLY -242 ? A GLY 187  
188  1 Y 1 A LYS -241 ? A LYS 188  
189  1 Y 1 A SER -240 ? A SER 189  
190  1 Y 1 A ALA -239 ? A ALA 190  
191  1 Y 1 A LEU -238 ? A LEU 191  
192  1 Y 1 A MET -237 ? A MET 192  
193  1 Y 1 A PHE -236 ? A PHE 193  
194  1 Y 1 A ASN -235 ? A ASN 194  
195  1 Y 1 A LEU -234 ? A LEU 195  
196  1 Y 1 A GLN -233 ? A GLN 196  
197  1 Y 1 A GLU -232 ? A GLU 197  
198  1 Y 1 A PRO -231 ? A PRO 198  
199  1 Y 1 A TYR -230 ? A TYR 199  
200  1 Y 1 A PHE -229 ? A PHE 200  
201  1 Y 1 A THR -228 ? A THR 201  
202  1 Y 1 A TRP -227 ? A TRP 202  
203  1 Y 1 A PRO -226 ? A PRO 203  
204  1 Y 1 A LEU -225 ? A LEU 204  
205  1 Y 1 A ILE -224 ? A ILE 205  
206  1 Y 1 A ALA -223 ? A ALA 206  
207  1 Y 1 A ALA -222 ? A ALA 207  
208  1 Y 1 A ASP -221 ? A ASP 208  
209  1 Y 1 A GLY -220 ? A GLY 209  
210  1 Y 1 A GLY -219 ? A GLY 210  
211  1 Y 1 A TYR -218 ? A TYR 211  
212  1 Y 1 A ALA -217 ? A ALA 212  
213  1 Y 1 A PHE -216 ? A PHE 213  
214  1 Y 1 A LYS -215 ? A LYS 214  
215  1 Y 1 A TYR -214 ? A TYR 215  
216  1 Y 1 A GLU -213 ? A GLU 216  
217  1 Y 1 A ASN -212 ? A ASN 217  
218  1 Y 1 A GLY -211 ? A GLY 218  
219  1 Y 1 A LYS -210 ? A LYS 219  
220  1 Y 1 A TYR -209 ? A TYR 220  
221  1 Y 1 A ASP -208 ? A ASP 221  
222  1 Y 1 A ILE -207 ? A ILE 222  
223  1 Y 1 A LYS -206 ? A LYS 223  
224  1 Y 1 A ASP -205 ? A ASP 224  
225  1 Y 1 A VAL -204 ? A VAL 225  
226  1 Y 1 A GLY -203 ? A GLY 226  
227  1 Y 1 A VAL -202 ? A VAL 227  
228  1 Y 1 A ASP -201 ? A ASP 228  
229  1 Y 1 A ASN -200 ? A ASN 229  
230  1 Y 1 A ALA -199 ? A ALA 230  
231  1 Y 1 A GLY -198 ? A GLY 231  
232  1 Y 1 A ALA -197 ? A ALA 232  
233  1 Y 1 A LYS -196 ? A LYS 233  
234  1 Y 1 A ALA -195 ? A ALA 234  
235  1 Y 1 A GLY -194 ? A GLY 235  
236  1 Y 1 A LEU -193 ? A LEU 236  
237  1 Y 1 A THR -192 ? A THR 237  
238  1 Y 1 A PHE -191 ? A PHE 238  
239  1 Y 1 A LEU -190 ? A LEU 239  
240  1 Y 1 A VAL -189 ? A VAL 240  
241  1 Y 1 A ASP -188 ? A ASP 241  
242  1 Y 1 A LEU -187 ? A LEU 242  
243  1 Y 1 A ILE -186 ? A ILE 243  
244  1 Y 1 A LYS -185 ? A LYS 244  
245  1 Y 1 A ASN -184 ? A ASN 245  
246  1 Y 1 A LYS -183 ? A LYS 246  
247  1 Y 1 A HIS -182 ? A HIS 247  
248  1 Y 1 A MET -181 ? A MET 248  
249  1 Y 1 A ASN -180 ? A ASN 249  
250  1 Y 1 A ALA -179 ? A ALA 250  
251  1 Y 1 A ASP -178 ? A ASP 251  
252  1 Y 1 A THR -177 ? A THR 252  
253  1 Y 1 A ASP -176 ? A ASP 253  
254  1 Y 1 A TYR -175 ? A TYR 254  
255  1 Y 1 A SER -174 ? A SER 255  
256  1 Y 1 A ILE -173 ? A ILE 256  
257  1 Y 1 A ALA -172 ? A ALA 257  
258  1 Y 1 A GLU -171 ? A GLU 258  
259  1 Y 1 A ALA -170 ? A ALA 259  
260  1 Y 1 A ALA -169 ? A ALA 260  
261  1 Y 1 A PHE -168 ? A PHE 261  
262  1 Y 1 A ASN -167 ? A ASN 262  
263  1 Y 1 A LYS -166 ? A LYS 263  
264  1 Y 1 A GLY -165 ? A GLY 264  
265  1 Y 1 A GLU -164 ? A GLU 265  
266  1 Y 1 A THR -163 ? A THR 266  
267  1 Y 1 A ALA -162 ? A ALA 267  
268  1 Y 1 A MET -161 ? A MET 268  
269  1 Y 1 A THR -160 ? A THR 269  
270  1 Y 1 A ILE -159 ? A ILE 270  
271  1 Y 1 A ASN -158 ? A ASN 271  
272  1 Y 1 A GLY -157 ? A GLY 272  
273  1 Y 1 A PRO -156 ? A PRO 273  
274  1 Y 1 A TRP -155 ? A TRP 274  
275  1 Y 1 A ALA -154 ? A ALA 275  
276  1 Y 1 A TRP -153 ? A TRP 276  
277  1 Y 1 A SER -152 ? A SER 277  
278  1 Y 1 A ASN -151 ? A ASN 278  
279  1 Y 1 A ILE -150 ? A ILE 279  
280  1 Y 1 A ASP -149 ? A ASP 280  
281  1 Y 1 A THR -148 ? A THR 281  
282  1 Y 1 A SER -147 ? A SER 282  
283  1 Y 1 A LYS -146 ? A LYS 283  
284  1 Y 1 A VAL -145 ? A VAL 284  
285  1 Y 1 A ASN -144 ? A ASN 285  
286  1 Y 1 A TYR -143 ? A TYR 286  
287  1 Y 1 A GLY -142 ? A GLY 287  
288  1 Y 1 A VAL -141 ? A VAL 288  
289  1 Y 1 A THR -140 ? A THR 289  
290  1 Y 1 A VAL -139 ? A VAL 290  
291  1 Y 1 A LEU -138 ? A LEU 291  
292  1 Y 1 A PRO -137 ? A PRO 292  
293  1 Y 1 A THR -136 ? A THR 293  
294  1 Y 1 A PHE -135 ? A PHE 294  
295  1 Y 1 A LYS -134 ? A LYS 295  
296  1 Y 1 A GLY -133 ? A GLY 296  
297  1 Y 1 A GLN -132 ? A GLN 297  
298  1 Y 1 A PRO -131 ? A PRO 298  
299  1 Y 1 A SER -130 ? A SER 299  
300  1 Y 1 A LYS -129 ? A LYS 300  
301  1 Y 1 A PRO -128 ? A PRO 301  
302  1 Y 1 A PHE -127 ? A PHE 302  
303  1 Y 1 A VAL -126 ? A VAL 303  
304  1 Y 1 A GLY -125 ? A GLY 304  
305  1 Y 1 A VAL -124 ? A VAL 305  
306  1 Y 1 A LEU -123 ? A LEU 306  
307  1 Y 1 A SER -122 ? A SER 307  
308  1 Y 1 A ALA -121 ? A ALA 308  
309  1 Y 1 A GLY -120 ? A GLY 309  
310  1 Y 1 A ILE -119 ? A ILE 310  
311  1 Y 1 A ASN -118 ? A ASN 311  
312  1 Y 1 A ALA -117 ? A ALA 312  
313  1 Y 1 A ALA -116 ? A ALA 313  
314  1 Y 1 A SER -115 ? A SER 314  
315  1 Y 1 A PRO -114 ? A PRO 315  
316  1 Y 1 A ASN -113 ? A ASN 316  
317  1 Y 1 A LYS -112 ? A LYS 317  
318  1 Y 1 A GLU -111 ? A GLU 318  
319  1 Y 1 A LEU -110 ? A LEU 319  
320  1 Y 1 A ALA -109 ? A ALA 320  
321  1 Y 1 A LYS -108 ? A LYS 321  
322  1 Y 1 A GLU -107 ? A GLU 322  
323  1 Y 1 A PHE -106 ? A PHE 323  
324  1 Y 1 A LEU -105 ? A LEU 324  
325  1 Y 1 A GLU -104 ? A GLU 325  
326  1 Y 1 A ASN -103 ? A ASN 326  
327  1 Y 1 A TYR -102 ? A TYR 327  
328  1 Y 1 A LEU -101 ? A LEU 328  
329  1 Y 1 A LEU -100 ? A LEU 329  
330  1 Y 1 A THR -99  ? A THR 330  
331  1 Y 1 A ASP -98  ? A ASP 331  
332  1 Y 1 A GLU -97  ? A GLU 332  
333  1 Y 1 A GLY -96  ? A GLY 333  
334  1 Y 1 A LEU -95  ? A LEU 334  
335  1 Y 1 A GLU -94  ? A GLU 335  
336  1 Y 1 A ALA -93  ? A ALA 336  
337  1 Y 1 A VAL -92  ? A VAL 337  
338  1 Y 1 A ASN -91  ? A ASN 338  
339  1 Y 1 A LYS -90  ? A LYS 339  
340  1 Y 1 A ASP -89  ? A ASP 340  
341  1 Y 1 A LYS -88  ? A LYS 341  
342  1 Y 1 A PRO -87  ? A PRO 342  
343  1 Y 1 A LEU -86  ? A LEU 343  
344  1 Y 1 A GLY -85  ? A GLY 344  
345  1 Y 1 A ALA -84  ? A ALA 345  
346  1 Y 1 A VAL -83  ? A VAL 346  
347  1 Y 1 A ALA -82  ? A ALA 347  
348  1 Y 1 A LEU -81  ? A LEU 348  
349  1 Y 1 A LYS -80  ? A LYS 349  
350  1 Y 1 A SER -79  ? A SER 350  
351  1 Y 1 A TYR -78  ? A TYR 351  
352  1 Y 1 A GLU -77  ? A GLU 352  
353  1 Y 1 A GLU -76  ? A GLU 353  
354  1 Y 1 A GLU -75  ? A GLU 354  
355  1 Y 1 A LEU -74  ? A LEU 355  
356  1 Y 1 A ALA -73  ? A ALA 356  
357  1 Y 1 A LYS -72  ? A LYS 357  
358  1 Y 1 A ASP -71  ? A ASP 358  
359  1 Y 1 A PRO -70  ? A PRO 359  
360  1 Y 1 A ARG -69  ? A ARG 360  
361  1 Y 1 A ILE -68  ? A ILE 361  
362  1 Y 1 A ALA -67  ? A ALA 362  
363  1 Y 1 A ALA -66  ? A ALA 363  
364  1 Y 1 A THR -65  ? A THR 364  
365  1 Y 1 A MET -64  ? A MET 365  
366  1 Y 1 A GLU -63  ? A GLU 366  
367  1 Y 1 A ASN -62  ? A ASN 367  
368  1 Y 1 A ALA -61  ? A ALA 368  
369  1 Y 1 A GLN -60  ? A GLN 369  
370  1 Y 1 A LYS -59  ? A LYS 370  
371  1 Y 1 A GLY -58  ? A GLY 371  
372  1 Y 1 A GLU -57  ? A GLU 372  
373  1 Y 1 A ILE -56  ? A ILE 373  
374  1 Y 1 A MET -55  ? A MET 374  
375  1 Y 1 A PRO -54  ? A PRO 375  
376  1 Y 1 A ASN -53  ? A ASN 376  
377  1 Y 1 A ILE -52  ? A ILE 377  
378  1 Y 1 A PRO -51  ? A PRO 378  
379  1 Y 1 A GLN -50  ? A GLN 379  
380  1 Y 1 A MET -49  ? A MET 380  
381  1 Y 1 A SER -48  ? A SER 381  
382  1 Y 1 A ALA -47  ? A ALA 382  
383  1 Y 1 A PHE -46  ? A PHE 383  
384  1 Y 1 A TRP -45  ? A TRP 384  
385  1 Y 1 A TYR -44  ? A TYR 385  
386  1 Y 1 A ALA -43  ? A ALA 386  
387  1 Y 1 A VAL -42  ? A VAL 387  
388  1 Y 1 A ARG -41  ? A ARG 388  
389  1 Y 1 A THR -40  ? A THR 389  
390  1 Y 1 A ALA -39  ? A ALA 390  
391  1 Y 1 A VAL -38  ? A VAL 391  
392  1 Y 1 A ILE -37  ? A ILE 392  
393  1 Y 1 A ASN -36  ? A ASN 393  
394  1 Y 1 A ALA -35  ? A ALA 394  
395  1 Y 1 A ALA -34  ? A ALA 395  
396  1 Y 1 A SER -33  ? A SER 396  
397  1 Y 1 A GLY -32  ? A GLY 397  
398  1 Y 1 A ARG -31  ? A ARG 398  
399  1 Y 1 A GLN -30  ? A GLN 399  
400  1 Y 1 A THR -29  ? A THR 400  
401  1 Y 1 A VAL -28  ? A VAL 401  
402  1 Y 1 A ASP -27  ? A ASP 402  
403  1 Y 1 A GLU -26  ? A GLU 403  
404  1 Y 1 A ALA -25  ? A ALA 404  
405  1 Y 1 A LEU -24  ? A LEU 405  
406  1 Y 1 A LYS -23  ? A LYS 406  
407  1 Y 1 A ASP -22  ? A ASP 407  
408  1 Y 1 A ALA -21  ? A ALA 408  
409  1 Y 1 A GLN -20  ? A GLN 409  
410  1 Y 1 A THR -19  ? A THR 410  
411  1 Y 1 A GLY -18  ? A GLY 411  
412  1 Y 1 A THR -17  ? A THR 412  
413  1 Y 1 A ASP -16  ? A ASP 413  
414  1 Y 1 A TYR -15  ? A TYR 414  
415  1 Y 1 A ASP -14  ? A ASP 415  
416  1 Y 1 A ILE -13  ? A ILE 416  
417  1 Y 1 A PRO -12  ? A PRO 417  
418  1 Y 1 A THR -11  ? A THR 418  
419  1 Y 1 A THR -10  ? A THR 419  
420  1 Y 1 A LEU -9   ? A LEU 420  
421  1 Y 1 A GLU -8   ? A GLU 421  
422  1 Y 1 A VAL -7   ? A VAL 422  
423  1 Y 1 A LEU -6   ? A LEU 423  
424  1 Y 1 A PHE -5   ? A PHE 424  
425  1 Y 1 A GLN -4   ? A GLN 425  
426  1 Y 1 A GLY -3   ? A GLY 426  
427  1 Y 1 A PRO -2   ? A PRO 427  
428  1 Y 1 A GLY -1   ? A GLY 428  
429  1 Y 1 A SER 0    ? A SER 429  
430  1 Y 1 A MET 1    ? A MET 430  
431  1 Y 1 A ALA 2    ? A ALA 431  
432  1 Y 1 A THR 3    ? A THR 432  
433  1 Y 1 A GLN 4    ? A GLN 433  
434  1 Y 1 A HIS 5    ? A HIS 434  
435  1 Y 1 A HIS 612  ? A HIS 1041 
436  1 Y 1 A HIS 613  ? A HIS 1042 
437  1 Y 1 A THR 614  ? A THR 1043 
438  1 Y 1 A SER 615  ? A SER 1044 
439  1 Y 1 A ASP 616  ? A ASP 1045 
440  1 Y 1 A ASP 617  ? A ASP 1046 
441  1 Y 1 A PHE 618  ? A PHE 1047 
442  1 Y 1 A GLY 619  ? A GLY 1048 
443  1 Y 1 A GLU 620  ? A GLU 1049 
444  1 Y 1 A HIS 621  ? A HIS 1050 
445  1 Y 1 A GLY 1195 ? A GLY 1624 
446  1 Y 1 A SER 1196 ? A SER 1625 
447  1 Y 1 A ARG 1197 ? A ARG 1626 
448  1 Y 1 A THR 1198 ? A THR 1627 
449  1 Y 1 A GLU 1199 ? A GLU 1628 
450  1 Y 1 A ASP 1200 ? A ASP 1629 
451  1 Y 1 A LYS 1201 ? A LYS 1630 
452  1 Y 1 A ILE 1202 ? A ILE 1631 
453  1 Y 1 A GLY 1203 ? A GLY 1632 
454  1 Y 1 A GLY 1305 ? A GLY 1734 
455  1 Y 1 A GLY 1306 ? A GLY 1735 
456  1 Y 1 A GLN 1307 ? A GLN 1736 
457  1 Y 1 A SER 1308 ? A SER 1737 
458  1 Y 1 A ILE 1394 ? A ILE 1823 
459  1 Y 1 A SER 1395 ? A SER 1824 
460  1 Y 1 A PHE 1396 ? A PHE 1825 
461  1 Y 1 A ASP 1397 ? A ASP 1826 
462  1 Y 1 A ASN 1398 ? A ASN 1827 
463  1 Y 1 A PRO 1399 ? A PRO 1828 
464  1 Y 1 A PHE 1400 ? A PHE 1829 
465  1 Y 1 A SER 1401 ? A SER 1830 
466  1 Y 1 A ARG 1402 ? A ARG 1831 
467  1 Y 1 A ASP 1403 ? A ASP 1832 
468  1 Y 1 A TYR 1404 ? A TYR 1833 
469  1 Y 1 A LYS 1405 ? A LYS 1834 
470  1 Y 1 A ASP 1406 ? A ASP 1835 
471  1 Y 1 A ASP 1407 ? A ASP 1836 
472  1 Y 1 A ASP 1408 ? A ASP 1837 
473  1 Y 1 A ASP 1409 ? A ASP 1838 
474  1 Y 1 A LYS 1410 ? A LYS 1839 
475  1 Y 1 B MET -316 ? B MET 1    
476  1 Y 1 B GLY -315 ? B GLY 2    
477  1 Y 1 B SER -314 ? B SER 3    
478  1 Y 1 B SER -313 ? B SER 4    
479  1 Y 1 B HIS -312 ? B HIS 5    
480  1 Y 1 B HIS -311 ? B HIS 6    
481  1 Y 1 B HIS -310 ? B HIS 7    
482  1 Y 1 B HIS -309 ? B HIS 8    
483  1 Y 1 B HIS -308 ? B HIS 9    
484  1 Y 1 B HIS -307 ? B HIS 10   
485  1 Y 1 B GLY -306 ? B GLY 11   
486  1 Y 1 B THR -305 ? B THR 12   
487  1 Y 1 B LYS -304 ? B LYS 13   
488  1 Y 1 B THR -303 ? B THR 14   
489  1 Y 1 B GLU -302 ? B GLU 15   
490  1 Y 1 B GLU -301 ? B GLU 16   
491  1 Y 1 B GLY -300 ? B GLY 17   
492  1 Y 1 B LYS -299 ? B LYS 18   
493  1 Y 1 B LEU -298 ? B LEU 19   
494  1 Y 1 B VAL -297 ? B VAL 20   
495  1 Y 1 B ILE -296 ? B ILE 21   
496  1 Y 1 B TRP -295 ? B TRP 22   
497  1 Y 1 B ILE -294 ? B ILE 23   
498  1 Y 1 B ASN -293 ? B ASN 24   
499  1 Y 1 B GLY -292 ? B GLY 25   
500  1 Y 1 B ASP -291 ? B ASP 26   
501  1 Y 1 B LYS -290 ? B LYS 27   
502  1 Y 1 B GLY -289 ? B GLY 28   
503  1 Y 1 B TYR -288 ? B TYR 29   
504  1 Y 1 B ASN -287 ? B ASN 30   
505  1 Y 1 B GLY -286 ? B GLY 31   
506  1 Y 1 B LEU -285 ? B LEU 32   
507  1 Y 1 B ALA -284 ? B ALA 33   
508  1 Y 1 B GLU -283 ? B GLU 34   
509  1 Y 1 B VAL -282 ? B VAL 35   
510  1 Y 1 B GLY -281 ? B GLY 36   
511  1 Y 1 B LYS -280 ? B LYS 37   
512  1 Y 1 B LYS -279 ? B LYS 38   
513  1 Y 1 B PHE -278 ? B PHE 39   
514  1 Y 1 B GLU -277 ? B GLU 40   
515  1 Y 1 B LYS -276 ? B LYS 41   
516  1 Y 1 B ASP -275 ? B ASP 42   
517  1 Y 1 B THR -274 ? B THR 43   
518  1 Y 1 B GLY -273 ? B GLY 44   
519  1 Y 1 B ILE -272 ? B ILE 45   
520  1 Y 1 B LYS -271 ? B LYS 46   
521  1 Y 1 B VAL -270 ? B VAL 47   
522  1 Y 1 B THR -269 ? B THR 48   
523  1 Y 1 B VAL -268 ? B VAL 49   
524  1 Y 1 B GLU -267 ? B GLU 50   
525  1 Y 1 B HIS -266 ? B HIS 51   
526  1 Y 1 B PRO -265 ? B PRO 52   
527  1 Y 1 B ASP -264 ? B ASP 53   
528  1 Y 1 B LYS -263 ? B LYS 54   
529  1 Y 1 B LEU -262 ? B LEU 55   
530  1 Y 1 B GLU -261 ? B GLU 56   
531  1 Y 1 B GLU -260 ? B GLU 57   
532  1 Y 1 B LYS -259 ? B LYS 58   
533  1 Y 1 B PHE -258 ? B PHE 59   
534  1 Y 1 B PRO -257 ? B PRO 60   
535  1 Y 1 B GLN -256 ? B GLN 61   
536  1 Y 1 B VAL -255 ? B VAL 62   
537  1 Y 1 B ALA -254 ? B ALA 63   
538  1 Y 1 B ALA -253 ? B ALA 64   
539  1 Y 1 B THR -252 ? B THR 65   
540  1 Y 1 B GLY -251 ? B GLY 66   
541  1 Y 1 B ASP -250 ? B ASP 67   
542  1 Y 1 B GLY -249 ? B GLY 68   
543  1 Y 1 B PRO -248 ? B PRO 69   
544  1 Y 1 B ASP -247 ? B ASP 70   
545  1 Y 1 B ILE -246 ? B ILE 71   
546  1 Y 1 B ILE -245 ? B ILE 72   
547  1 Y 1 B PHE -244 ? B PHE 73   
548  1 Y 1 B TRP -243 ? B TRP 74   
549  1 Y 1 B ALA -242 ? B ALA 75   
550  1 Y 1 B HIS -241 ? B HIS 76   
551  1 Y 1 B ASP -240 ? B ASP 77   
552  1 Y 1 B ARG -239 ? B ARG 78   
553  1 Y 1 B PHE -238 ? B PHE 79   
554  1 Y 1 B GLY -237 ? B GLY 80   
555  1 Y 1 B GLY -236 ? B GLY 81   
556  1 Y 1 B TYR -235 ? B TYR 82   
557  1 Y 1 B ALA -234 ? B ALA 83   
558  1 Y 1 B GLN -233 ? B GLN 84   
559  1 Y 1 B SER -232 ? B SER 85   
560  1 Y 1 B GLY -231 ? B GLY 86   
561  1 Y 1 B LEU -230 ? B LEU 87   
562  1 Y 1 B LEU -229 ? B LEU 88   
563  1 Y 1 B ALA -228 ? B ALA 89   
564  1 Y 1 B GLU -227 ? B GLU 90   
565  1 Y 1 B ILE -226 ? B ILE 91   
566  1 Y 1 B THR -225 ? B THR 92   
567  1 Y 1 B PRO -224 ? B PRO 93   
568  1 Y 1 B ASP -223 ? B ASP 94   
569  1 Y 1 B LYS -222 ? B LYS 95   
570  1 Y 1 B ALA -221 ? B ALA 96   
571  1 Y 1 B PHE -220 ? B PHE 97   
572  1 Y 1 B GLN -219 ? B GLN 98   
573  1 Y 1 B ASP -218 ? B ASP 99   
574  1 Y 1 B LYS -217 ? B LYS 100  
575  1 Y 1 B LEU -216 ? B LEU 101  
576  1 Y 1 B TYR -215 ? B TYR 102  
577  1 Y 1 B PRO -214 ? B PRO 103  
578  1 Y 1 B PHE -213 ? B PHE 104  
579  1 Y 1 B THR -212 ? B THR 105  
580  1 Y 1 B TRP -211 ? B TRP 106  
581  1 Y 1 B ASP -210 ? B ASP 107  
582  1 Y 1 B ALA -209 ? B ALA 108  
583  1 Y 1 B VAL -208 ? B VAL 109  
584  1 Y 1 B ARG -207 ? B ARG 110  
585  1 Y 1 B TYR -206 ? B TYR 111  
586  1 Y 1 B ASN -205 ? B ASN 112  
587  1 Y 1 B GLY -204 ? B GLY 113  
588  1 Y 1 B LYS -203 ? B LYS 114  
589  1 Y 1 B LEU -202 ? B LEU 115  
590  1 Y 1 B ILE -201 ? B ILE 116  
591  1 Y 1 B ALA -200 ? B ALA 117  
592  1 Y 1 B TYR -199 ? B TYR 118  
593  1 Y 1 B PRO -198 ? B PRO 119  
594  1 Y 1 B ILE -197 ? B ILE 120  
595  1 Y 1 B ALA -196 ? B ALA 121  
596  1 Y 1 B VAL -195 ? B VAL 122  
597  1 Y 1 B GLU -194 ? B GLU 123  
598  1 Y 1 B ALA -193 ? B ALA 124  
599  1 Y 1 B LEU -192 ? B LEU 125  
600  1 Y 1 B SER -191 ? B SER 126  
601  1 Y 1 B LEU -190 ? B LEU 127  
602  1 Y 1 B ILE -189 ? B ILE 128  
603  1 Y 1 B TYR -188 ? B TYR 129  
604  1 Y 1 B ASN -187 ? B ASN 130  
605  1 Y 1 B LYS -186 ? B LYS 131  
606  1 Y 1 B ASP -185 ? B ASP 132  
607  1 Y 1 B LEU -184 ? B LEU 133  
608  1 Y 1 B LEU -183 ? B LEU 134  
609  1 Y 1 B PRO -182 ? B PRO 135  
610  1 Y 1 B ASN -181 ? B ASN 136  
611  1 Y 1 B PRO -180 ? B PRO 137  
612  1 Y 1 B PRO -179 ? B PRO 138  
613  1 Y 1 B LYS -178 ? B LYS 139  
614  1 Y 1 B THR -177 ? B THR 140  
615  1 Y 1 B TRP -176 ? B TRP 141  
616  1 Y 1 B GLU -175 ? B GLU 142  
617  1 Y 1 B GLU -174 ? B GLU 143  
618  1 Y 1 B ILE -173 ? B ILE 144  
619  1 Y 1 B PRO -172 ? B PRO 145  
620  1 Y 1 B ALA -171 ? B ALA 146  
621  1 Y 1 B LEU -170 ? B LEU 147  
622  1 Y 1 B ASP -169 ? B ASP 148  
623  1 Y 1 B LYS -168 ? B LYS 149  
624  1 Y 1 B GLU -167 ? B GLU 150  
625  1 Y 1 B LEU -166 ? B LEU 151  
626  1 Y 1 B LYS -165 ? B LYS 152  
627  1 Y 1 B ALA -164 ? B ALA 153  
628  1 Y 1 B LYS -163 ? B LYS 154  
629  1 Y 1 B GLY -162 ? B GLY 155  
630  1 Y 1 B LYS -161 ? B LYS 156  
631  1 Y 1 B SER -160 ? B SER 157  
632  1 Y 1 B ALA -159 ? B ALA 158  
633  1 Y 1 B LEU -158 ? B LEU 159  
634  1 Y 1 B MET -157 ? B MET 160  
635  1 Y 1 B PHE -156 ? B PHE 161  
636  1 Y 1 B ASN -155 ? B ASN 162  
637  1 Y 1 B LEU -154 ? B LEU 163  
638  1 Y 1 B GLN -153 ? B GLN 164  
639  1 Y 1 B GLU -152 ? B GLU 165  
640  1 Y 1 B PRO -151 ? B PRO 166  
641  1 Y 1 B TYR -150 ? B TYR 167  
642  1 Y 1 B PHE -149 ? B PHE 168  
643  1 Y 1 B THR -148 ? B THR 169  
644  1 Y 1 B TRP -147 ? B TRP 170  
645  1 Y 1 B PRO -146 ? B PRO 171  
646  1 Y 1 B LEU -145 ? B LEU 172  
647  1 Y 1 B ILE -144 ? B ILE 173  
648  1 Y 1 B ALA -143 ? B ALA 174  
649  1 Y 1 B ALA -142 ? B ALA 175  
650  1 Y 1 B ASP -141 ? B ASP 176  
651  1 Y 1 B GLY -140 ? B GLY 177  
652  1 Y 1 B GLY -139 ? B GLY 178  
653  1 Y 1 B TYR -138 ? B TYR 179  
654  1 Y 1 B ALA -137 ? B ALA 180  
655  1 Y 1 B PHE -136 ? B PHE 181  
656  1 Y 1 B LYS -135 ? B LYS 182  
657  1 Y 1 B TYR -134 ? B TYR 183  
658  1 Y 1 B GLU -133 ? B GLU 184  
659  1 Y 1 B ASN -132 ? B ASN 185  
660  1 Y 1 B GLY -131 ? B GLY 186  
661  1 Y 1 B LYS -130 ? B LYS 187  
662  1 Y 1 B TYR -129 ? B TYR 188  
663  1 Y 1 B ASP -128 ? B ASP 189  
664  1 Y 1 B ILE -127 ? B ILE 190  
665  1 Y 1 B LYS -126 ? B LYS 191  
666  1 Y 1 B ASP -125 ? B ASP 192  
667  1 Y 1 B VAL -124 ? B VAL 193  
668  1 Y 1 B GLY -123 ? B GLY 194  
669  1 Y 1 B VAL -122 ? B VAL 195  
670  1 Y 1 B ASP -121 ? B ASP 196  
671  1 Y 1 B ASN -120 ? B ASN 197  
672  1 Y 1 B ALA -119 ? B ALA 198  
673  1 Y 1 B GLY -118 ? B GLY 199  
674  1 Y 1 B ALA -117 ? B ALA 200  
675  1 Y 1 B LYS -116 ? B LYS 201  
676  1 Y 1 B ALA -115 ? B ALA 202  
677  1 Y 1 B GLY -114 ? B GLY 203  
678  1 Y 1 B LEU -113 ? B LEU 204  
679  1 Y 1 B THR -112 ? B THR 205  
680  1 Y 1 B PHE -111 ? B PHE 206  
681  1 Y 1 B LEU -110 ? B LEU 207  
682  1 Y 1 B VAL -109 ? B VAL 208  
683  1 Y 1 B ASP -108 ? B ASP 209  
684  1 Y 1 B LEU -107 ? B LEU 210  
685  1 Y 1 B ILE -106 ? B ILE 211  
686  1 Y 1 B LYS -105 ? B LYS 212  
687  1 Y 1 B ASN -104 ? B ASN 213  
688  1 Y 1 B LYS -103 ? B LYS 214  
689  1 Y 1 B HIS -102 ? B HIS 215  
690  1 Y 1 B MET -101 ? B MET 216  
691  1 Y 1 B ASN -100 ? B ASN 217  
692  1 Y 1 B ALA -99  ? B ALA 218  
693  1 Y 1 B ASP -98  ? B ASP 219  
694  1 Y 1 B THR -97  ? B THR 220  
695  1 Y 1 B ASP -96  ? B ASP 221  
696  1 Y 1 B TYR -95  ? B TYR 222  
697  1 Y 1 B SER -94  ? B SER 223  
698  1 Y 1 B ILE -93  ? B ILE 224  
699  1 Y 1 B ALA -92  ? B ALA 225  
700  1 Y 1 B GLU -91  ? B GLU 226  
701  1 Y 1 B ALA -90  ? B ALA 227  
702  1 Y 1 B ALA -89  ? B ALA 228  
703  1 Y 1 B PHE -88  ? B PHE 229  
704  1 Y 1 B ASN -87  ? B ASN 230  
705  1 Y 1 B LYS -86  ? B LYS 231  
706  1 Y 1 B GLY -85  ? B GLY 232  
707  1 Y 1 B GLU -84  ? B GLU 233  
708  1 Y 1 B THR -83  ? B THR 234  
709  1 Y 1 B ALA -82  ? B ALA 235  
710  1 Y 1 B MET -81  ? B MET 236  
711  1 Y 1 B THR -80  ? B THR 237  
712  1 Y 1 B ILE -79  ? B ILE 238  
713  1 Y 1 B ASN -78  ? B ASN 239  
714  1 Y 1 B GLY -77  ? B GLY 240  
715  1 Y 1 B PRO -76  ? B PRO 241  
716  1 Y 1 B TRP -75  ? B TRP 242  
717  1 Y 1 B ALA -74  ? B ALA 243  
718  1 Y 1 B TRP -73  ? B TRP 244  
719  1 Y 1 B SER -72  ? B SER 245  
720  1 Y 1 B ASN -71  ? B ASN 246  
721  1 Y 1 B ILE -70  ? B ILE 247  
722  1 Y 1 B ASP -69  ? B ASP 248  
723  1 Y 1 B THR -68  ? B THR 249  
724  1 Y 1 B SER -67  ? B SER 250  
725  1 Y 1 B LYS -66  ? B LYS 251  
726  1 Y 1 B VAL -65  ? B VAL 252  
727  1 Y 1 B ASN -64  ? B ASN 253  
728  1 Y 1 B TYR -63  ? B TYR 254  
729  1 Y 1 B GLY -62  ? B GLY 255  
730  1 Y 1 B VAL -61  ? B VAL 256  
731  1 Y 1 B THR -60  ? B THR 257  
732  1 Y 1 B VAL -59  ? B VAL 258  
733  1 Y 1 B LEU -58  ? B LEU 259  
734  1 Y 1 B PRO -57  ? B PRO 260  
735  1 Y 1 B THR -56  ? B THR 261  
736  1 Y 1 B PHE -55  ? B PHE 262  
737  1 Y 1 B LYS -54  ? B LYS 263  
738  1 Y 1 B GLY -53  ? B GLY 264  
739  1 Y 1 B GLN -52  ? B GLN 265  
740  1 Y 1 B PRO -51  ? B PRO 266  
741  1 Y 1 B SER -50  ? B SER 267  
742  1 Y 1 B LYS -49  ? B LYS 268  
743  1 Y 1 B PRO -48  ? B PRO 269  
744  1 Y 1 B PHE -47  ? B PHE 270  
745  1 Y 1 B VAL -46  ? B VAL 271  
746  1 Y 1 B GLY -45  ? B GLY 272  
747  1 Y 1 B VAL -44  ? B VAL 273  
748  1 Y 1 B LEU -43  ? B LEU 274  
749  1 Y 1 B SER -42  ? B SER 275  
750  1 Y 1 B ALA -41  ? B ALA 276  
751  1 Y 1 B GLY -40  ? B GLY 277  
752  1 Y 1 B ILE -39  ? B ILE 278  
753  1 Y 1 B ASN -38  ? B ASN 279  
754  1 Y 1 B ALA -37  ? B ALA 280  
755  1 Y 1 B ALA -36  ? B ALA 281  
756  1 Y 1 B SER -35  ? B SER 282  
757  1 Y 1 B PRO -34  ? B PRO 283  
758  1 Y 1 B ASN -33  ? B ASN 284  
759  1 Y 1 B LYS -32  ? B LYS 285  
760  1 Y 1 B GLU -31  ? B GLU 286  
761  1 Y 1 B LEU -30  ? B LEU 287  
762  1 Y 1 B ALA -29  ? B ALA 288  
763  1 Y 1 B LYS -28  ? B LYS 289  
764  1 Y 1 B GLU -27  ? B GLU 290  
765  1 Y 1 B PHE -26  ? B PHE 291  
766  1 Y 1 B LEU -25  ? B LEU 292  
767  1 Y 1 B GLU -24  ? B GLU 293  
768  1 Y 1 B ASN -23  ? B ASN 294  
769  1 Y 1 B TYR -22  ? B TYR 295  
770  1 Y 1 B LEU -21  ? B LEU 296  
771  1 Y 1 B LEU -20  ? B LEU 297  
772  1 Y 1 B THR -19  ? B THR 298  
773  1 Y 1 B ASP -18  ? B ASP 299  
774  1 Y 1 B GLU -17  ? B GLU 300  
775  1 Y 1 B GLY -16  ? B GLY 301  
776  1 Y 1 B LEU -15  ? B LEU 302  
777  1 Y 1 B GLU -14  ? B GLU 303  
778  1 Y 1 B ALA -13  ? B ALA 304  
779  1 Y 1 B VAL -12  ? B VAL 305  
780  1 Y 1 B ASN -11  ? B ASN 306  
781  1 Y 1 B LYS -10  ? B LYS 307  
782  1 Y 1 B ASP -9   ? B ASP 308  
783  1 Y 1 B LYS -8   ? B LYS 309  
784  1 Y 1 B PRO -7   ? B PRO 310  
785  1 Y 1 B LEU -6   ? B LEU 311  
786  1 Y 1 B GLY -5   ? B GLY 312  
787  1 Y 1 B ALA -4   ? B ALA 313  
788  1 Y 1 B VAL -3   ? B VAL 314  
789  1 Y 1 B ALA -2   ? B ALA 315  
790  1 Y 1 B LEU -1   ? B LEU 316  
791  1 Y 1 B LYS 0    ? B LYS 317  
792  1 Y 1 B SER 1    ? B SER 318  
793  1 Y 1 B TYR 2    ? B TYR 319  
794  1 Y 1 B GLU 3    ? B GLU 320  
795  1 Y 1 B GLU 4    ? B GLU 321  
796  1 Y 1 B GLU 5    ? B GLU 322  
797  1 Y 1 B LEU 6    ? B LEU 323  
798  1 Y 1 B ALA 7    ? B ALA 324  
799  1 Y 1 B LYS 8    ? B LYS 325  
800  1 Y 1 B ASP 9    ? B ASP 326  
801  1 Y 1 B PRO 10   ? B PRO 327  
802  1 Y 1 B ARG 11   ? B ARG 328  
803  1 Y 1 B ILE 12   ? B ILE 329  
804  1 Y 1 B ALA 13   ? B ALA 330  
805  1 Y 1 B ALA 14   ? B ALA 331  
806  1 Y 1 B THR 15   ? B THR 332  
807  1 Y 1 B MET 16   ? B MET 333  
808  1 Y 1 B GLU 17   ? B GLU 334  
809  1 Y 1 B ASN 18   ? B ASN 335  
810  1 Y 1 B ALA 19   ? B ALA 336  
811  1 Y 1 B GLN 20   ? B GLN 337  
812  1 Y 1 B LYS 21   ? B LYS 338  
813  1 Y 1 B GLY 22   ? B GLY 339  
814  1 Y 1 B GLU 23   ? B GLU 340  
815  1 Y 1 B ILE 24   ? B ILE 341  
816  1 Y 1 B MET 25   ? B MET 342  
817  1 Y 1 B PRO 26   ? B PRO 343  
818  1 Y 1 B ASN 27   ? B ASN 344  
819  1 Y 1 B ILE 28   ? B ILE 345  
820  1 Y 1 B PRO 29   ? B PRO 346  
821  1 Y 1 B GLN 30   ? B GLN 347  
822  1 Y 1 B MET 31   ? B MET 348  
823  1 Y 1 B SER 32   ? B SER 349  
824  1 Y 1 B ALA 33   ? B ALA 350  
825  1 Y 1 B PHE 34   ? B PHE 351  
826  1 Y 1 B TRP 35   ? B TRP 352  
827  1 Y 1 B TYR 36   ? B TYR 353  
828  1 Y 1 B ALA 37   ? B ALA 354  
829  1 Y 1 B VAL 38   ? B VAL 355  
830  1 Y 1 B ARG 39   ? B ARG 356  
831  1 Y 1 B THR 40   ? B THR 357  
832  1 Y 1 B ALA 41   ? B ALA 358  
833  1 Y 1 B VAL 42   ? B VAL 359  
834  1 Y 1 B ILE 43   ? B ILE 360  
835  1 Y 1 B ASN 44   ? B ASN 361  
836  1 Y 1 B ALA 45   ? B ALA 362  
837  1 Y 1 B ALA 46   ? B ALA 363  
838  1 Y 1 B SER 47   ? B SER 364  
839  1 Y 1 B GLY 48   ? B GLY 365  
840  1 Y 1 B ARG 49   ? B ARG 366  
841  1 Y 1 B GLN 50   ? B GLN 367  
842  1 Y 1 B THR 51   ? B THR 368  
843  1 Y 1 B VAL 52   ? B VAL 369  
844  1 Y 1 B ASP 53   ? B ASP 370  
845  1 Y 1 B GLU 54   ? B GLU 371  
846  1 Y 1 B ALA 55   ? B ALA 372  
847  1 Y 1 B LEU 56   ? B LEU 373  
848  1 Y 1 B LYS 57   ? B LYS 374  
849  1 Y 1 B ASP 58   ? B ASP 375  
850  1 Y 1 B ALA 59   ? B ALA 376  
851  1 Y 1 B GLN 60   ? B GLN 377  
852  1 Y 1 B THR 61   ? B THR 378  
853  1 Y 1 B GLY 62   ? B GLY 379  
854  1 Y 1 B THR 63   ? B THR 380  
855  1 Y 1 B ASP 64   ? B ASP 381  
856  1 Y 1 B TYR 65   ? B TYR 382  
857  1 Y 1 B ASP 66   ? B ASP 383  
858  1 Y 1 B ILE 67   ? B ILE 384  
859  1 Y 1 B PRO 68   ? B PRO 385  
860  1 Y 1 B THR 69   ? B THR 386  
861  1 Y 1 B THR 70   ? B THR 387  
862  1 Y 1 B GLU 71   ? B GLU 388  
863  1 Y 1 B ASN 72   ? B ASN 389  
864  1 Y 1 B LEU 73   ? B LEU 390  
865  1 Y 1 B TYR 74   ? B TYR 391  
866  1 Y 1 B PHE 75   ? B PHE 392  
867  1 Y 1 B GLN 76   ? B GLN 393  
868  1 Y 1 B GLY 77   ? B GLY 394  
869  1 Y 1 B GLY 78   ? B GLY 395  
870  1 Y 1 B SER 79   ? B SER 396  
871  1 Y 1 B ASN 80   ? B ASN 397  
872  1 Y 1 B HIS 81   ? B HIS 398  
873  1 Y 1 B SER 82   ? B SER 399  
874  1 Y 1 B PHE 83   ? B PHE 400  
875  1 Y 1 B GLU 84   ? B GLU 401  
876  1 Y 1 B GLU 85   ? B GLU 402  
877  1 Y 1 B VAL 86   ? B VAL 403  
878  1 Y 1 B VAL 87   ? B VAL 404  
879  1 Y 1 B GLN 88   ? B GLN 405  
880  1 Y 1 B THR 89   ? B THR 406  
881  1 Y 1 B LEU 90   ? B LEU 407  
882  1 Y 1 B ALA 91   ? B ALA 408  
883  1 Y 1 B SER 92   ? B SER 409  
884  1 Y 1 B LEU 93   ? B LEU 410  
885  1 Y 1 B ALA 94   ? B ALA 411  
886  1 Y 1 B THR 95   ? B THR 412  
887  1 Y 1 B VAL 96   ? B VAL 413  
888  1 Y 1 B VAL 97   ? B VAL 414  
889  1 Y 1 B GLN 98   ? B GLN 415  
890  1 Y 1 B GLN 99   ? B GLN 416  
891  1 Y 1 B GLN 100  ? B GLN 417  
892  1 Y 1 B THR 101  ? B THR 418  
893  1 Y 1 B ILE 102  ? B ILE 419  
894  1 Y 1 B ALA 103  ? B ALA 420  
895  1 Y 1 B SER 104  ? B SER 421  
896  1 Y 1 B GLU 105  ? B GLU 422  
897  1 Y 1 B SER 106  ? B SER 423  
898  1 Y 1 B LEU 107  ? B LEU 424  
899  1 Y 1 B GLU 108  ? B GLU 425  
900  1 Y 1 B GLN 109  ? B GLN 426  
901  1 Y 1 B ARG 110  ? B ARG 427  
902  1 Y 1 B ILE 111  ? B ILE 428  
903  1 Y 1 B THR 112  ? B THR 429  
904  1 Y 1 B SER 113  ? B SER 430  
905  1 Y 1 B LEU 114  ? B LEU 431  
906  1 Y 1 B GLU 115  ? B GLU 432  
907  1 Y 1 B ASN 116  ? B ASN 433  
908  1 Y 1 B GLY 117  ? B GLY 434  
909  1 Y 1 B LEU 118  ? B LEU 435  
910  1 Y 1 B LYS 119  ? B LYS 436  
911  1 Y 1 B PRO 120  ? B PRO 437  
912  1 Y 1 B VAL 121  ? B VAL 438  
913  1 Y 1 B TYR 122  ? B TYR 439  
914  1 Y 1 C MET -316 ? C MET 1    
915  1 Y 1 C GLY -315 ? C GLY 2    
916  1 Y 1 C SER -314 ? C SER 3    
917  1 Y 1 C SER -313 ? C SER 4    
918  1 Y 1 C HIS -312 ? C HIS 5    
919  1 Y 1 C HIS -311 ? C HIS 6    
920  1 Y 1 C HIS -310 ? C HIS 7    
921  1 Y 1 C HIS -309 ? C HIS 8    
922  1 Y 1 C HIS -308 ? C HIS 9    
923  1 Y 1 C HIS -307 ? C HIS 10   
924  1 Y 1 C GLY -306 ? C GLY 11   
925  1 Y 1 C THR -305 ? C THR 12   
926  1 Y 1 C LYS -304 ? C LYS 13   
927  1 Y 1 C THR -303 ? C THR 14   
928  1 Y 1 C GLU -302 ? C GLU 15   
929  1 Y 1 C GLU -301 ? C GLU 16   
930  1 Y 1 C GLY -300 ? C GLY 17   
931  1 Y 1 C LYS -299 ? C LYS 18   
932  1 Y 1 C LEU -298 ? C LEU 19   
933  1 Y 1 C VAL -297 ? C VAL 20   
934  1 Y 1 C ILE -296 ? C ILE 21   
935  1 Y 1 C TRP -295 ? C TRP 22   
936  1 Y 1 C ILE -294 ? C ILE 23   
937  1 Y 1 C ASN -293 ? C ASN 24   
938  1 Y 1 C GLY -292 ? C GLY 25   
939  1 Y 1 C ASP -291 ? C ASP 26   
940  1 Y 1 C LYS -290 ? C LYS 27   
941  1 Y 1 C GLY -289 ? C GLY 28   
942  1 Y 1 C TYR -288 ? C TYR 29   
943  1 Y 1 C ASN -287 ? C ASN 30   
944  1 Y 1 C GLY -286 ? C GLY 31   
945  1 Y 1 C LEU -285 ? C LEU 32   
946  1 Y 1 C ALA -284 ? C ALA 33   
947  1 Y 1 C GLU -283 ? C GLU 34   
948  1 Y 1 C VAL -282 ? C VAL 35   
949  1 Y 1 C GLY -281 ? C GLY 36   
950  1 Y 1 C LYS -280 ? C LYS 37   
951  1 Y 1 C LYS -279 ? C LYS 38   
952  1 Y 1 C PHE -278 ? C PHE 39   
953  1 Y 1 C GLU -277 ? C GLU 40   
954  1 Y 1 C LYS -276 ? C LYS 41   
955  1 Y 1 C ASP -275 ? C ASP 42   
956  1 Y 1 C THR -274 ? C THR 43   
957  1 Y 1 C GLY -273 ? C GLY 44   
958  1 Y 1 C ILE -272 ? C ILE 45   
959  1 Y 1 C LYS -271 ? C LYS 46   
960  1 Y 1 C VAL -270 ? C VAL 47   
961  1 Y 1 C THR -269 ? C THR 48   
962  1 Y 1 C VAL -268 ? C VAL 49   
963  1 Y 1 C GLU -267 ? C GLU 50   
964  1 Y 1 C HIS -266 ? C HIS 51   
965  1 Y 1 C PRO -265 ? C PRO 52   
966  1 Y 1 C ASP -264 ? C ASP 53   
967  1 Y 1 C LYS -263 ? C LYS 54   
968  1 Y 1 C LEU -262 ? C LEU 55   
969  1 Y 1 C GLU -261 ? C GLU 56   
970  1 Y 1 C GLU -260 ? C GLU 57   
971  1 Y 1 C LYS -259 ? C LYS 58   
972  1 Y 1 C PHE -258 ? C PHE 59   
973  1 Y 1 C PRO -257 ? C PRO 60   
974  1 Y 1 C GLN -256 ? C GLN 61   
975  1 Y 1 C VAL -255 ? C VAL 62   
976  1 Y 1 C ALA -254 ? C ALA 63   
977  1 Y 1 C ALA -253 ? C ALA 64   
978  1 Y 1 C THR -252 ? C THR 65   
979  1 Y 1 C GLY -251 ? C GLY 66   
980  1 Y 1 C ASP -250 ? C ASP 67   
981  1 Y 1 C GLY -249 ? C GLY 68   
982  1 Y 1 C PRO -248 ? C PRO 69   
983  1 Y 1 C ASP -247 ? C ASP 70   
984  1 Y 1 C ILE -246 ? C ILE 71   
985  1 Y 1 C ILE -245 ? C ILE 72   
986  1 Y 1 C PHE -244 ? C PHE 73   
987  1 Y 1 C TRP -243 ? C TRP 74   
988  1 Y 1 C ALA -242 ? C ALA 75   
989  1 Y 1 C HIS -241 ? C HIS 76   
990  1 Y 1 C ASP -240 ? C ASP 77   
991  1 Y 1 C ARG -239 ? C ARG 78   
992  1 Y 1 C PHE -238 ? C PHE 79   
993  1 Y 1 C GLY -237 ? C GLY 80   
994  1 Y 1 C GLY -236 ? C GLY 81   
995  1 Y 1 C TYR -235 ? C TYR 82   
996  1 Y 1 C ALA -234 ? C ALA 83   
997  1 Y 1 C GLN -233 ? C GLN 84   
998  1 Y 1 C SER -232 ? C SER 85   
999  1 Y 1 C GLY -231 ? C GLY 86   
1000 1 Y 1 C LEU -230 ? C LEU 87   
1001 1 Y 1 C LEU -229 ? C LEU 88   
1002 1 Y 1 C ALA -228 ? C ALA 89   
1003 1 Y 1 C GLU -227 ? C GLU 90   
1004 1 Y 1 C ILE -226 ? C ILE 91   
1005 1 Y 1 C THR -225 ? C THR 92   
1006 1 Y 1 C PRO -224 ? C PRO 93   
1007 1 Y 1 C ASP -223 ? C ASP 94   
1008 1 Y 1 C LYS -222 ? C LYS 95   
1009 1 Y 1 C ALA -221 ? C ALA 96   
1010 1 Y 1 C PHE -220 ? C PHE 97   
1011 1 Y 1 C GLN -219 ? C GLN 98   
1012 1 Y 1 C ASP -218 ? C ASP 99   
1013 1 Y 1 C LYS -217 ? C LYS 100  
1014 1 Y 1 C LEU -216 ? C LEU 101  
1015 1 Y 1 C TYR -215 ? C TYR 102  
1016 1 Y 1 C PRO -214 ? C PRO 103  
1017 1 Y 1 C PHE -213 ? C PHE 104  
1018 1 Y 1 C THR -212 ? C THR 105  
1019 1 Y 1 C TRP -211 ? C TRP 106  
1020 1 Y 1 C ASP -210 ? C ASP 107  
1021 1 Y 1 C ALA -209 ? C ALA 108  
1022 1 Y 1 C VAL -208 ? C VAL 109  
1023 1 Y 1 C ARG -207 ? C ARG 110  
1024 1 Y 1 C TYR -206 ? C TYR 111  
1025 1 Y 1 C ASN -205 ? C ASN 112  
1026 1 Y 1 C GLY -204 ? C GLY 113  
1027 1 Y 1 C LYS -203 ? C LYS 114  
1028 1 Y 1 C LEU -202 ? C LEU 115  
1029 1 Y 1 C ILE -201 ? C ILE 116  
1030 1 Y 1 C ALA -200 ? C ALA 117  
1031 1 Y 1 C TYR -199 ? C TYR 118  
1032 1 Y 1 C PRO -198 ? C PRO 119  
1033 1 Y 1 C ILE -197 ? C ILE 120  
1034 1 Y 1 C ALA -196 ? C ALA 121  
1035 1 Y 1 C VAL -195 ? C VAL 122  
1036 1 Y 1 C GLU -194 ? C GLU 123  
1037 1 Y 1 C ALA -193 ? C ALA 124  
1038 1 Y 1 C LEU -192 ? C LEU 125  
1039 1 Y 1 C SER -191 ? C SER 126  
1040 1 Y 1 C LEU -190 ? C LEU 127  
1041 1 Y 1 C ILE -189 ? C ILE 128  
1042 1 Y 1 C TYR -188 ? C TYR 129  
1043 1 Y 1 C ASN -187 ? C ASN 130  
1044 1 Y 1 C LYS -186 ? C LYS 131  
1045 1 Y 1 C ASP -185 ? C ASP 132  
1046 1 Y 1 C LEU -184 ? C LEU 133  
1047 1 Y 1 C LEU -183 ? C LEU 134  
1048 1 Y 1 C PRO -182 ? C PRO 135  
1049 1 Y 1 C ASN -181 ? C ASN 136  
1050 1 Y 1 C PRO -180 ? C PRO 137  
1051 1 Y 1 C PRO -179 ? C PRO 138  
1052 1 Y 1 C LYS -178 ? C LYS 139  
1053 1 Y 1 C THR -177 ? C THR 140  
1054 1 Y 1 C TRP -176 ? C TRP 141  
1055 1 Y 1 C GLU -175 ? C GLU 142  
1056 1 Y 1 C GLU -174 ? C GLU 143  
1057 1 Y 1 C ILE -173 ? C ILE 144  
1058 1 Y 1 C PRO -172 ? C PRO 145  
1059 1 Y 1 C ALA -171 ? C ALA 146  
1060 1 Y 1 C LEU -170 ? C LEU 147  
1061 1 Y 1 C ASP -169 ? C ASP 148  
1062 1 Y 1 C LYS -168 ? C LYS 149  
1063 1 Y 1 C GLU -167 ? C GLU 150  
1064 1 Y 1 C LEU -166 ? C LEU 151  
1065 1 Y 1 C LYS -165 ? C LYS 152  
1066 1 Y 1 C ALA -164 ? C ALA 153  
1067 1 Y 1 C LYS -163 ? C LYS 154  
1068 1 Y 1 C GLY -162 ? C GLY 155  
1069 1 Y 1 C LYS -161 ? C LYS 156  
1070 1 Y 1 C SER -160 ? C SER 157  
1071 1 Y 1 C ALA -159 ? C ALA 158  
1072 1 Y 1 C LEU -158 ? C LEU 159  
1073 1 Y 1 C MET -157 ? C MET 160  
1074 1 Y 1 C PHE -156 ? C PHE 161  
1075 1 Y 1 C ASN -155 ? C ASN 162  
1076 1 Y 1 C LEU -154 ? C LEU 163  
1077 1 Y 1 C GLN -153 ? C GLN 164  
1078 1 Y 1 C GLU -152 ? C GLU 165  
1079 1 Y 1 C PRO -151 ? C PRO 166  
1080 1 Y 1 C TYR -150 ? C TYR 167  
1081 1 Y 1 C PHE -149 ? C PHE 168  
1082 1 Y 1 C THR -148 ? C THR 169  
1083 1 Y 1 C TRP -147 ? C TRP 170  
1084 1 Y 1 C PRO -146 ? C PRO 171  
1085 1 Y 1 C LEU -145 ? C LEU 172  
1086 1 Y 1 C ILE -144 ? C ILE 173  
1087 1 Y 1 C ALA -143 ? C ALA 174  
1088 1 Y 1 C ALA -142 ? C ALA 175  
1089 1 Y 1 C ASP -141 ? C ASP 176  
1090 1 Y 1 C GLY -140 ? C GLY 177  
1091 1 Y 1 C GLY -139 ? C GLY 178  
1092 1 Y 1 C TYR -138 ? C TYR 179  
1093 1 Y 1 C ALA -137 ? C ALA 180  
1094 1 Y 1 C PHE -136 ? C PHE 181  
1095 1 Y 1 C LYS -135 ? C LYS 182  
1096 1 Y 1 C TYR -134 ? C TYR 183  
1097 1 Y 1 C GLU -133 ? C GLU 184  
1098 1 Y 1 C ASN -132 ? C ASN 185  
1099 1 Y 1 C GLY -131 ? C GLY 186  
1100 1 Y 1 C LYS -130 ? C LYS 187  
1101 1 Y 1 C TYR -129 ? C TYR 188  
1102 1 Y 1 C ASP -128 ? C ASP 189  
1103 1 Y 1 C ILE -127 ? C ILE 190  
1104 1 Y 1 C LYS -126 ? C LYS 191  
1105 1 Y 1 C ASP -125 ? C ASP 192  
1106 1 Y 1 C VAL -124 ? C VAL 193  
1107 1 Y 1 C GLY -123 ? C GLY 194  
1108 1 Y 1 C VAL -122 ? C VAL 195  
1109 1 Y 1 C ASP -121 ? C ASP 196  
1110 1 Y 1 C ASN -120 ? C ASN 197  
1111 1 Y 1 C ALA -119 ? C ALA 198  
1112 1 Y 1 C GLY -118 ? C GLY 199  
1113 1 Y 1 C ALA -117 ? C ALA 200  
1114 1 Y 1 C LYS -116 ? C LYS 201  
1115 1 Y 1 C ALA -115 ? C ALA 202  
1116 1 Y 1 C GLY -114 ? C GLY 203  
1117 1 Y 1 C LEU -113 ? C LEU 204  
1118 1 Y 1 C THR -112 ? C THR 205  
1119 1 Y 1 C PHE -111 ? C PHE 206  
1120 1 Y 1 C LEU -110 ? C LEU 207  
1121 1 Y 1 C VAL -109 ? C VAL 208  
1122 1 Y 1 C ASP -108 ? C ASP 209  
1123 1 Y 1 C LEU -107 ? C LEU 210  
1124 1 Y 1 C ILE -106 ? C ILE 211  
1125 1 Y 1 C LYS -105 ? C LYS 212  
1126 1 Y 1 C ASN -104 ? C ASN 213  
1127 1 Y 1 C LYS -103 ? C LYS 214  
1128 1 Y 1 C HIS -102 ? C HIS 215  
1129 1 Y 1 C MET -101 ? C MET 216  
1130 1 Y 1 C ASN -100 ? C ASN 217  
1131 1 Y 1 C ALA -99  ? C ALA 218  
1132 1 Y 1 C ASP -98  ? C ASP 219  
1133 1 Y 1 C THR -97  ? C THR 220  
1134 1 Y 1 C ASP -96  ? C ASP 221  
1135 1 Y 1 C TYR -95  ? C TYR 222  
1136 1 Y 1 C SER -94  ? C SER 223  
1137 1 Y 1 C ILE -93  ? C ILE 224  
1138 1 Y 1 C ALA -92  ? C ALA 225  
1139 1 Y 1 C GLU -91  ? C GLU 226  
1140 1 Y 1 C ALA -90  ? C ALA 227  
1141 1 Y 1 C ALA -89  ? C ALA 228  
1142 1 Y 1 C PHE -88  ? C PHE 229  
1143 1 Y 1 C ASN -87  ? C ASN 230  
1144 1 Y 1 C LYS -86  ? C LYS 231  
1145 1 Y 1 C GLY -85  ? C GLY 232  
1146 1 Y 1 C GLU -84  ? C GLU 233  
1147 1 Y 1 C THR -83  ? C THR 234  
1148 1 Y 1 C ALA -82  ? C ALA 235  
1149 1 Y 1 C MET -81  ? C MET 236  
1150 1 Y 1 C THR -80  ? C THR 237  
1151 1 Y 1 C ILE -79  ? C ILE 238  
1152 1 Y 1 C ASN -78  ? C ASN 239  
1153 1 Y 1 C GLY -77  ? C GLY 240  
1154 1 Y 1 C PRO -76  ? C PRO 241  
1155 1 Y 1 C TRP -75  ? C TRP 242  
1156 1 Y 1 C ALA -74  ? C ALA 243  
1157 1 Y 1 C TRP -73  ? C TRP 244  
1158 1 Y 1 C SER -72  ? C SER 245  
1159 1 Y 1 C ASN -71  ? C ASN 246  
1160 1 Y 1 C ILE -70  ? C ILE 247  
1161 1 Y 1 C ASP -69  ? C ASP 248  
1162 1 Y 1 C THR -68  ? C THR 249  
1163 1 Y 1 C SER -67  ? C SER 250  
1164 1 Y 1 C LYS -66  ? C LYS 251  
1165 1 Y 1 C VAL -65  ? C VAL 252  
1166 1 Y 1 C ASN -64  ? C ASN 253  
1167 1 Y 1 C TYR -63  ? C TYR 254  
1168 1 Y 1 C GLY -62  ? C GLY 255  
1169 1 Y 1 C VAL -61  ? C VAL 256  
1170 1 Y 1 C THR -60  ? C THR 257  
1171 1 Y 1 C VAL -59  ? C VAL 258  
1172 1 Y 1 C LEU -58  ? C LEU 259  
1173 1 Y 1 C PRO -57  ? C PRO 260  
1174 1 Y 1 C THR -56  ? C THR 261  
1175 1 Y 1 C PHE -55  ? C PHE 262  
1176 1 Y 1 C LYS -54  ? C LYS 263  
1177 1 Y 1 C GLY -53  ? C GLY 264  
1178 1 Y 1 C GLN -52  ? C GLN 265  
1179 1 Y 1 C PRO -51  ? C PRO 266  
1180 1 Y 1 C SER -50  ? C SER 267  
1181 1 Y 1 C LYS -49  ? C LYS 268  
1182 1 Y 1 C PRO -48  ? C PRO 269  
1183 1 Y 1 C PHE -47  ? C PHE 270  
1184 1 Y 1 C VAL -46  ? C VAL 271  
1185 1 Y 1 C GLY -45  ? C GLY 272  
1186 1 Y 1 C VAL -44  ? C VAL 273  
1187 1 Y 1 C LEU -43  ? C LEU 274  
1188 1 Y 1 C SER -42  ? C SER 275  
1189 1 Y 1 C ALA -41  ? C ALA 276  
1190 1 Y 1 C GLY -40  ? C GLY 277  
1191 1 Y 1 C ILE -39  ? C ILE 278  
1192 1 Y 1 C ASN -38  ? C ASN 279  
1193 1 Y 1 C ALA -37  ? C ALA 280  
1194 1 Y 1 C ALA -36  ? C ALA 281  
1195 1 Y 1 C SER -35  ? C SER 282  
1196 1 Y 1 C PRO -34  ? C PRO 283  
1197 1 Y 1 C ASN -33  ? C ASN 284  
1198 1 Y 1 C LYS -32  ? C LYS 285  
1199 1 Y 1 C GLU -31  ? C GLU 286  
1200 1 Y 1 C LEU -30  ? C LEU 287  
1201 1 Y 1 C ALA -29  ? C ALA 288  
1202 1 Y 1 C LYS -28  ? C LYS 289  
1203 1 Y 1 C GLU -27  ? C GLU 290  
1204 1 Y 1 C PHE -26  ? C PHE 291  
1205 1 Y 1 C LEU -25  ? C LEU 292  
1206 1 Y 1 C GLU -24  ? C GLU 293  
1207 1 Y 1 C ASN -23  ? C ASN 294  
1208 1 Y 1 C TYR -22  ? C TYR 295  
1209 1 Y 1 C LEU -21  ? C LEU 296  
1210 1 Y 1 C LEU -20  ? C LEU 297  
1211 1 Y 1 C THR -19  ? C THR 298  
1212 1 Y 1 C ASP -18  ? C ASP 299  
1213 1 Y 1 C GLU -17  ? C GLU 300  
1214 1 Y 1 C GLY -16  ? C GLY 301  
1215 1 Y 1 C LEU -15  ? C LEU 302  
1216 1 Y 1 C GLU -14  ? C GLU 303  
1217 1 Y 1 C ALA -13  ? C ALA 304  
1218 1 Y 1 C VAL -12  ? C VAL 305  
1219 1 Y 1 C ASN -11  ? C ASN 306  
1220 1 Y 1 C LYS -10  ? C LYS 307  
1221 1 Y 1 C ASP -9   ? C ASP 308  
1222 1 Y 1 C LYS -8   ? C LYS 309  
1223 1 Y 1 C PRO -7   ? C PRO 310  
1224 1 Y 1 C LEU -6   ? C LEU 311  
1225 1 Y 1 C GLY -5   ? C GLY 312  
1226 1 Y 1 C ALA -4   ? C ALA 313  
1227 1 Y 1 C VAL -3   ? C VAL 314  
1228 1 Y 1 C ALA -2   ? C ALA 315  
1229 1 Y 1 C LEU -1   ? C LEU 316  
1230 1 Y 1 C LYS 0    ? C LYS 317  
1231 1 Y 1 C SER 1    ? C SER 318  
1232 1 Y 1 C TYR 2    ? C TYR 319  
1233 1 Y 1 C GLU 3    ? C GLU 320  
1234 1 Y 1 C GLU 4    ? C GLU 321  
1235 1 Y 1 C GLU 5    ? C GLU 322  
1236 1 Y 1 C LEU 6    ? C LEU 323  
1237 1 Y 1 C ALA 7    ? C ALA 324  
1238 1 Y 1 C LYS 8    ? C LYS 325  
1239 1 Y 1 C ASP 9    ? C ASP 326  
1240 1 Y 1 C PRO 10   ? C PRO 327  
1241 1 Y 1 C ARG 11   ? C ARG 328  
1242 1 Y 1 C ILE 12   ? C ILE 329  
1243 1 Y 1 C ALA 13   ? C ALA 330  
1244 1 Y 1 C ALA 14   ? C ALA 331  
1245 1 Y 1 C THR 15   ? C THR 332  
1246 1 Y 1 C MET 16   ? C MET 333  
1247 1 Y 1 C GLU 17   ? C GLU 334  
1248 1 Y 1 C ASN 18   ? C ASN 335  
1249 1 Y 1 C ALA 19   ? C ALA 336  
1250 1 Y 1 C GLN 20   ? C GLN 337  
1251 1 Y 1 C LYS 21   ? C LYS 338  
1252 1 Y 1 C GLY 22   ? C GLY 339  
1253 1 Y 1 C GLU 23   ? C GLU 340  
1254 1 Y 1 C ILE 24   ? C ILE 341  
1255 1 Y 1 C MET 25   ? C MET 342  
1256 1 Y 1 C PRO 26   ? C PRO 343  
1257 1 Y 1 C ASN 27   ? C ASN 344  
1258 1 Y 1 C ILE 28   ? C ILE 345  
1259 1 Y 1 C PRO 29   ? C PRO 346  
1260 1 Y 1 C GLN 30   ? C GLN 347  
1261 1 Y 1 C MET 31   ? C MET 348  
1262 1 Y 1 C SER 32   ? C SER 349  
1263 1 Y 1 C ALA 33   ? C ALA 350  
1264 1 Y 1 C PHE 34   ? C PHE 351  
1265 1 Y 1 C TRP 35   ? C TRP 352  
1266 1 Y 1 C TYR 36   ? C TYR 353  
1267 1 Y 1 C ALA 37   ? C ALA 354  
1268 1 Y 1 C VAL 38   ? C VAL 355  
1269 1 Y 1 C ARG 39   ? C ARG 356  
1270 1 Y 1 C THR 40   ? C THR 357  
1271 1 Y 1 C ALA 41   ? C ALA 358  
1272 1 Y 1 C VAL 42   ? C VAL 359  
1273 1 Y 1 C ILE 43   ? C ILE 360  
1274 1 Y 1 C ASN 44   ? C ASN 361  
1275 1 Y 1 C ALA 45   ? C ALA 362  
1276 1 Y 1 C ALA 46   ? C ALA 363  
1277 1 Y 1 C SER 47   ? C SER 364  
1278 1 Y 1 C GLY 48   ? C GLY 365  
1279 1 Y 1 C ARG 49   ? C ARG 366  
1280 1 Y 1 C GLN 50   ? C GLN 367  
1281 1 Y 1 C THR 51   ? C THR 368  
1282 1 Y 1 C VAL 52   ? C VAL 369  
1283 1 Y 1 C ASP 53   ? C ASP 370  
1284 1 Y 1 C GLU 54   ? C GLU 371  
1285 1 Y 1 C ALA 55   ? C ALA 372  
1286 1 Y 1 C LEU 56   ? C LEU 373  
1287 1 Y 1 C LYS 57   ? C LYS 374  
1288 1 Y 1 C ASP 58   ? C ASP 375  
1289 1 Y 1 C ALA 59   ? C ALA 376  
1290 1 Y 1 C GLN 60   ? C GLN 377  
1291 1 Y 1 C THR 61   ? C THR 378  
1292 1 Y 1 C GLY 62   ? C GLY 379  
1293 1 Y 1 C THR 63   ? C THR 380  
1294 1 Y 1 C ASP 64   ? C ASP 381  
1295 1 Y 1 C TYR 65   ? C TYR 382  
1296 1 Y 1 C ASP 66   ? C ASP 383  
1297 1 Y 1 C ILE 67   ? C ILE 384  
1298 1 Y 1 C PRO 68   ? C PRO 385  
1299 1 Y 1 C THR 69   ? C THR 386  
1300 1 Y 1 C THR 70   ? C THR 387  
1301 1 Y 1 C GLU 71   ? C GLU 388  
1302 1 Y 1 C ASN 72   ? C ASN 389  
1303 1 Y 1 C LEU 73   ? C LEU 390  
1304 1 Y 1 C TYR 74   ? C TYR 391  
1305 1 Y 1 C PHE 75   ? C PHE 392  
1306 1 Y 1 C GLN 76   ? C GLN 393  
1307 1 Y 1 C GLY 77   ? C GLY 394  
1308 1 Y 1 C GLY 78   ? C GLY 395  
1309 1 Y 1 C SER 79   ? C SER 396  
1310 1 Y 1 C ASN 80   ? C ASN 397  
1311 1 Y 1 C HIS 81   ? C HIS 398  
1312 1 Y 1 C SER 82   ? C SER 399  
1313 1 Y 1 C PHE 83   ? C PHE 400  
1314 1 Y 1 C GLU 84   ? C GLU 401  
1315 1 Y 1 C GLU 85   ? C GLU 402  
1316 1 Y 1 C VAL 86   ? C VAL 403  
1317 1 Y 1 C VAL 87   ? C VAL 404  
1318 1 Y 1 C GLN 88   ? C GLN 405  
1319 1 Y 1 C THR 89   ? C THR 406  
1320 1 Y 1 C LEU 90   ? C LEU 407  
1321 1 Y 1 C ALA 91   ? C ALA 408  
1322 1 Y 1 C SER 92   ? C SER 409  
1323 1 Y 1 C LEU 93   ? C LEU 410  
1324 1 Y 1 C ALA 94   ? C ALA 411  
1325 1 Y 1 C THR 95   ? C THR 412  
1326 1 Y 1 C VAL 96   ? C VAL 413  
1327 1 Y 1 C VAL 97   ? C VAL 414  
1328 1 Y 1 C GLN 98   ? C GLN 415  
1329 1 Y 1 C GLN 99   ? C GLN 416  
1330 1 Y 1 C GLN 100  ? C GLN 417  
1331 1 Y 1 C THR 101  ? C THR 418  
1332 1 Y 1 C ILE 102  ? C ILE 419  
1333 1 Y 1 C ALA 103  ? C ALA 420  
1334 1 Y 1 C SER 104  ? C SER 421  
1335 1 Y 1 C GLU 105  ? C GLU 422  
1336 1 Y 1 C SER 106  ? C SER 423  
1337 1 Y 1 C LEU 107  ? C LEU 424  
1338 1 Y 1 C GLU 108  ? C GLU 425  
1339 1 Y 1 C GLN 109  ? C GLN 426  
1340 1 Y 1 C ARG 110  ? C ARG 427  
1341 1 Y 1 C ILE 111  ? C ILE 428  
1342 1 Y 1 C THR 112  ? C THR 429  
1343 1 Y 1 C SER 113  ? C SER 430  
1344 1 Y 1 C LEU 114  ? C LEU 431  
1345 1 Y 1 C GLU 115  ? C GLU 432  
1346 1 Y 1 C ASN 116  ? C ASN 433  
1347 1 Y 1 C GLY 117  ? C GLY 434  
1348 1 Y 1 C LEU 118  ? C LEU 435  
1349 1 Y 1 C LYS 119  ? C LYS 436  
1350 1 Y 1 C PRO 120  ? C PRO 437  
1351 1 Y 1 C VAL 121  ? C VAL 438  
1352 1 Y 1 C TYR 122  ? C TYR 439  
1353 1 Y 1 C ASP 123  ? C ASP 440  
1354 1 Y 1 C ALA 180  ? C ALA 497  
1355 1 Y 1 C ILE 181  ? C ILE 498  
1356 1 Y 1 C ARG 182  ? C ARG 499  
1357 1 Y 1 C GLY 183  ? C GLY 500  
1358 1 Y 1 C LYS 184  ? C LYS 501  
1359 1 Y 1 C ILE 185  ? C ILE 502  
1360 1 Y 1 C GLU 186  ? C GLU 503  
1361 1 Y 1 C SER 187  ? C SER 504  
1362 1 Y 1 C ARG 188  ? C ARG 505  
1363 1 Y 1 C ASP 189  ? C ASP 506  
1364 1 Y 1 C GLU 190  ? C GLU 507  
1365 1 Y 1 C THR 191  ? C THR 508  
1366 1 Y 1 C VAL 192  ? C VAL 509  
1367 1 Y 1 C PRO 193  ? C PRO 510  
1368 1 Y 1 C GLN 194  ? C GLN 511  
1369 1 Y 1 C SER 195  ? C SER 512  
1370 1 Y 1 C VAL 196  ? C VAL 513  
1371 1 Y 1 C ARG 197  ? C ARG 514  
1372 1 Y 1 C GLU 198  ? C GLU 515  
1373 1 Y 1 C ALA 199  ? C ALA 516  
1374 1 Y 1 C PHE 200  ? C PHE 517  
1375 1 Y 1 C ASN 201  ? C ASN 518  
1376 1 Y 1 C ASN 202  ? C ASN 519  
1377 1 Y 1 C LEU 203  ? C LEU 520  
1378 1 Y 1 C ASN 204  ? C ASN 521  
1379 1 Y 1 C SER 205  ? C SER 522  
1380 1 Y 1 C THR 206  ? C THR 523  
1381 1 Y 1 C THR 207  ? C THR 524  
1382 1 Y 1 C SER 208  ? C SER 525  
1383 1 Y 1 C LEU 209  ? C LEU 526  
1384 1 Y 1 C THR 210  ? C THR 527  
1385 1 Y 1 C GLU 211  ? C GLU 528  
1386 1 Y 1 C GLU 212  ? C GLU 529  
1387 1 Y 1 C ASN 213  ? C ASN 530  
1388 1 Y 1 C PHE 214  ? C PHE 531  
1389 1 Y 1 C GLY 215  ? C GLY 532  
1390 1 Y 1 C LYS 216  ? C LYS 533  
1391 1 Y 1 C PRO 217  ? C PRO 534  
1392 1 Y 1 C ASP 218  ? C ASP 535  
1393 1 Y 1 C ILE 219  ? C ILE 536  
1394 1 Y 1 C SER 220  ? C SER 537  
1395 1 Y 1 C ALA 221  ? C ALA 538  
1396 1 Y 1 C LYS 222  ? C LYS 539  
1397 1 Y 1 C ASP 223  ? C ASP 540  
1398 1 Y 1 C LEU 224  ? C LEU 541  
1399 1 Y 1 C ARG 225  ? C ARG 542  
1400 1 Y 1 C ASN 226  ? C ASN 543  
1401 1 Y 1 C ILE 227  ? C ILE 544  
1402 1 Y 1 C MET 228  ? C MET 545  
1403 1 Y 1 C TYR 229  ? C TYR 546  
1404 1 Y 1 C ASP 230  ? C ASP 547  
1405 1 Y 1 C HIS 231  ? C HIS 548  
1406 1 Y 1 C LEU 232  ? C LEU 549  
1407 1 Y 1 C PRO 233  ? C PRO 550  
1408 1 Y 1 C GLY 234  ? C GLY 551  
1409 1 Y 1 C PHE 235  ? C PHE 552  
1410 1 Y 1 C GLY 236  ? C GLY 553  
1411 1 Y 1 C THR 237  ? C THR 554  
1412 1 Y 1 C ALA 238  ? C ALA 555  
1413 1 Y 1 C PHE 239  ? C PHE 556  
1414 1 Y 1 C HIS 240  ? C HIS 557  
1415 1 Y 1 C GLN 241  ? C GLN 558  
1416 1 Y 1 C LEU 242  ? C LEU 559  
1417 1 Y 1 C VAL 243  ? C VAL 560  
1418 1 Y 1 C GLN 244  ? C GLN 561  
1419 1 Y 1 C VAL 245  ? C VAL 562  
1420 1 Y 1 C ILE 246  ? C ILE 563  
1421 1 Y 1 C CYS 247  ? C CYS 564  
1422 1 Y 1 C LYS 248  ? C LYS 565  
1423 1 Y 1 C LEU 249  ? C LEU 566  
1424 1 Y 1 C GLY 250  ? C GLY 567  
1425 1 Y 1 C LYS 251  ? C LYS 568  
1426 1 Y 1 C ASP 252  ? C ASP 569  
1427 1 Y 1 C SER 253  ? C SER 570  
1428 1 Y 1 C ASN 254  ? C ASN 571  
1429 1 Y 1 C SER 255  ? C SER 572  
1430 1 Y 1 C LEU 256  ? C LEU 573  
1431 1 Y 1 C ASP 257  ? C ASP 574  
1432 1 Y 1 C ILE 258  ? C ILE 575  
1433 1 Y 1 C ILE 259  ? C ILE 576  
1434 1 Y 1 C HIS 260  ? C HIS 577  
1435 1 Y 1 C ALA 261  ? C ALA 578  
1436 1 Y 1 C GLU 262  ? C GLU 579  
1437 1 Y 1 C PHE 263  ? C PHE 580  
1438 1 Y 1 C GLN 264  ? C GLN 581  
1439 1 Y 1 C ALA 265  ? C ALA 582  
1440 1 Y 1 C SER 266  ? C SER 583  
1441 1 Y 1 C LEU 267  ? C LEU 584  
1442 1 Y 1 C ALA 268  ? C ALA 585  
1443 1 Y 1 C GLU 269  ? C GLU 586  
1444 1 Y 1 C GLY 270  ? C GLY 587  
1445 1 Y 1 C ASP 271  ? C ASP 588  
1446 1 Y 1 C SER 272  ? C SER 589  
1447 1 Y 1 C PRO 273  ? C PRO 590  
1448 1 Y 1 C GLN 274  ? C GLN 591  
1449 1 Y 1 C CYS 275  ? C CYS 592  
1450 1 Y 1 C ALA 276  ? C ALA 593  
1451 1 Y 1 C LEU 277  ? C LEU 594  
1452 1 Y 1 C ILE 278  ? C ILE 595  
1453 1 Y 1 C GLN 279  ? C GLN 596  
1454 1 Y 1 C ILE 280  ? C ILE 597  
1455 1 Y 1 C THR 281  ? C THR 598  
1456 1 Y 1 C LYS 282  ? C LYS 599  
1457 1 Y 1 C ARG 283  ? C ARG 600  
1458 1 Y 1 C VAL 284  ? C VAL 601  
1459 1 Y 1 C PRO 285  ? C PRO 602  
1460 1 Y 1 C ILE 286  ? C ILE 603  
1461 1 Y 1 C PHE 287  ? C PHE 604  
1462 1 Y 1 C GLN 288  ? C GLN 605  
1463 1 Y 1 C ASP 289  ? C ASP 606  
1464 1 Y 1 C ALA 290  ? C ALA 607  
1465 1 Y 1 C ALA 291  ? C ALA 608  
1466 1 Y 1 C PRO 292  ? C PRO 609  
1467 1 Y 1 C PRO 293  ? C PRO 610  
1468 1 Y 1 C VAL 294  ? C VAL 611  
1469 1 Y 1 C ILE 295  ? C ILE 612  
1470 1 Y 1 C HIS 296  ? C HIS 613  
1471 1 Y 1 C ILE 297  ? C ILE 614  
1472 1 Y 1 C ARG 298  ? C ARG 615  
1473 1 Y 1 C SER 299  ? C SER 616  
1474 1 Y 1 C ARG 300  ? C ARG 617  
1475 1 Y 1 C GLY 301  ? C GLY 618  
1476 1 Y 1 C ASP 302  ? C ASP 619  
1477 1 Y 1 C ILE 303  ? C ILE 620  
1478 1 Y 1 C PRO 304  ? C PRO 621  
1479 1 Y 1 C ARG 305  ? C ARG 622  
1480 1 Y 1 C ALA 306  ? C ALA 623  
1481 1 Y 1 C CYS 307  ? C CYS 624  
1482 1 Y 1 C GLN 308  ? C GLN 625  
1483 1 Y 1 C LYS 309  ? C LYS 626  
1484 1 Y 1 C SER 310  ? C SER 627  
1485 1 Y 1 C LEU 311  ? C LEU 628  
1486 1 Y 1 C ARG 312  ? C ARG 629  
1487 1 Y 1 C PRO 313  ? C PRO 630  
1488 1 Y 1 C VAL 314  ? C VAL 631  
1489 1 Y 1 C PRO 315  ? C PRO 632  
1490 1 Y 1 C PRO 316  ? C PRO 633  
1491 1 Y 1 C SER 317  ? C SER 634  
1492 1 Y 1 C PRO 318  ? C PRO 635  
1493 1 Y 1 C LYS 319  ? C LYS 636  
1494 1 Y 1 C ILE 320  ? C ILE 637  
1495 1 Y 1 C ASP 321  ? C ASP 638  
1496 1 Y 1 C ARG 322  ? C ARG 639  
1497 1 Y 1 C GLY 323  ? C GLY 640  
1498 1 Y 1 C TRP 324  ? C TRP 641  
1499 1 Y 1 C VAL 325  ? C VAL 642  
1500 1 Y 1 C CYS 326  ? C CYS 643  
1501 1 Y 1 C VAL 327  ? C VAL 644  
1502 1 Y 1 C PHE 328  ? C PHE 645  
1503 1 Y 1 C GLN 329  ? C GLN 646  
1504 1 Y 1 C LEU 330  ? C LEU 647  
1505 1 Y 1 C GLN 331  ? C GLN 648  
1506 1 Y 1 C ASP 332  ? C ASP 649  
1507 1 Y 1 C GLY 333  ? C GLY 650  
1508 1 Y 1 C LYS 334  ? C LYS 651  
1509 1 Y 1 C THR 335  ? C THR 652  
1510 1 Y 1 C LEU 336  ? C LEU 653  
1511 1 Y 1 C GLY 337  ? C GLY 654  
1512 1 Y 1 C LEU 338  ? C LEU 655  
1513 1 Y 1 C LYS 339  ? C LYS 656  
1514 1 Y 1 C ILE 340  ? C ILE 657  
1515 1 Y 1 D MET -316 ? D MET 1    
1516 1 Y 1 D GLY -315 ? D GLY 2    
1517 1 Y 1 D SER -314 ? D SER 3    
1518 1 Y 1 D SER -313 ? D SER 4    
1519 1 Y 1 D HIS -312 ? D HIS 5    
1520 1 Y 1 D HIS -311 ? D HIS 6    
1521 1 Y 1 D HIS -310 ? D HIS 7    
1522 1 Y 1 D HIS -309 ? D HIS 8    
1523 1 Y 1 D HIS -308 ? D HIS 9    
1524 1 Y 1 D HIS -307 ? D HIS 10   
1525 1 Y 1 D GLY -306 ? D GLY 11   
1526 1 Y 1 D THR -305 ? D THR 12   
1527 1 Y 1 D LYS -304 ? D LYS 13   
1528 1 Y 1 D THR -303 ? D THR 14   
1529 1 Y 1 D GLU -302 ? D GLU 15   
1530 1 Y 1 D GLU -301 ? D GLU 16   
1531 1 Y 1 D GLY -300 ? D GLY 17   
1532 1 Y 1 D LYS -299 ? D LYS 18   
1533 1 Y 1 D LEU -298 ? D LEU 19   
1534 1 Y 1 D VAL -297 ? D VAL 20   
1535 1 Y 1 D ILE -296 ? D ILE 21   
1536 1 Y 1 D TRP -295 ? D TRP 22   
1537 1 Y 1 D ILE -294 ? D ILE 23   
1538 1 Y 1 D ASN -293 ? D ASN 24   
1539 1 Y 1 D GLY -292 ? D GLY 25   
1540 1 Y 1 D ASP -291 ? D ASP 26   
1541 1 Y 1 D LYS -290 ? D LYS 27   
1542 1 Y 1 D GLY -289 ? D GLY 28   
1543 1 Y 1 D TYR -288 ? D TYR 29   
1544 1 Y 1 D ASN -287 ? D ASN 30   
1545 1 Y 1 D GLY -286 ? D GLY 31   
1546 1 Y 1 D LEU -285 ? D LEU 32   
1547 1 Y 1 D ALA -284 ? D ALA 33   
1548 1 Y 1 D GLU -283 ? D GLU 34   
1549 1 Y 1 D VAL -282 ? D VAL 35   
1550 1 Y 1 D GLY -281 ? D GLY 36   
1551 1 Y 1 D LYS -280 ? D LYS 37   
1552 1 Y 1 D LYS -279 ? D LYS 38   
1553 1 Y 1 D PHE -278 ? D PHE 39   
1554 1 Y 1 D GLU -277 ? D GLU 40   
1555 1 Y 1 D LYS -276 ? D LYS 41   
1556 1 Y 1 D ASP -275 ? D ASP 42   
1557 1 Y 1 D THR -274 ? D THR 43   
1558 1 Y 1 D GLY -273 ? D GLY 44   
1559 1 Y 1 D ILE -272 ? D ILE 45   
1560 1 Y 1 D LYS -271 ? D LYS 46   
1561 1 Y 1 D VAL -270 ? D VAL 47   
1562 1 Y 1 D THR -269 ? D THR 48   
1563 1 Y 1 D VAL -268 ? D VAL 49   
1564 1 Y 1 D GLU -267 ? D GLU 50   
1565 1 Y 1 D HIS -266 ? D HIS 51   
1566 1 Y 1 D PRO -265 ? D PRO 52   
1567 1 Y 1 D ASP -264 ? D ASP 53   
1568 1 Y 1 D LYS -263 ? D LYS 54   
1569 1 Y 1 D LEU -262 ? D LEU 55   
1570 1 Y 1 D GLU -261 ? D GLU 56   
1571 1 Y 1 D GLU -260 ? D GLU 57   
1572 1 Y 1 D LYS -259 ? D LYS 58   
1573 1 Y 1 D PHE -258 ? D PHE 59   
1574 1 Y 1 D PRO -257 ? D PRO 60   
1575 1 Y 1 D GLN -256 ? D GLN 61   
1576 1 Y 1 D VAL -255 ? D VAL 62   
1577 1 Y 1 D ALA -254 ? D ALA 63   
1578 1 Y 1 D ALA -253 ? D ALA 64   
1579 1 Y 1 D THR -252 ? D THR 65   
1580 1 Y 1 D GLY -251 ? D GLY 66   
1581 1 Y 1 D ASP -250 ? D ASP 67   
1582 1 Y 1 D GLY -249 ? D GLY 68   
1583 1 Y 1 D PRO -248 ? D PRO 69   
1584 1 Y 1 D ASP -247 ? D ASP 70   
1585 1 Y 1 D ILE -246 ? D ILE 71   
1586 1 Y 1 D ILE -245 ? D ILE 72   
1587 1 Y 1 D PHE -244 ? D PHE 73   
1588 1 Y 1 D TRP -243 ? D TRP 74   
1589 1 Y 1 D ALA -242 ? D ALA 75   
1590 1 Y 1 D HIS -241 ? D HIS 76   
1591 1 Y 1 D ASP -240 ? D ASP 77   
1592 1 Y 1 D ARG -239 ? D ARG 78   
1593 1 Y 1 D PHE -238 ? D PHE 79   
1594 1 Y 1 D GLY -237 ? D GLY 80   
1595 1 Y 1 D GLY -236 ? D GLY 81   
1596 1 Y 1 D TYR -235 ? D TYR 82   
1597 1 Y 1 D ALA -234 ? D ALA 83   
1598 1 Y 1 D GLN -233 ? D GLN 84   
1599 1 Y 1 D SER -232 ? D SER 85   
1600 1 Y 1 D GLY -231 ? D GLY 86   
1601 1 Y 1 D LEU -230 ? D LEU 87   
1602 1 Y 1 D LEU -229 ? D LEU 88   
1603 1 Y 1 D ALA -228 ? D ALA 89   
1604 1 Y 1 D GLU -227 ? D GLU 90   
1605 1 Y 1 D ILE -226 ? D ILE 91   
1606 1 Y 1 D THR -225 ? D THR 92   
1607 1 Y 1 D PRO -224 ? D PRO 93   
1608 1 Y 1 D ASP -223 ? D ASP 94   
1609 1 Y 1 D LYS -222 ? D LYS 95   
1610 1 Y 1 D ALA -221 ? D ALA 96   
1611 1 Y 1 D PHE -220 ? D PHE 97   
1612 1 Y 1 D GLN -219 ? D GLN 98   
1613 1 Y 1 D ASP -218 ? D ASP 99   
1614 1 Y 1 D LYS -217 ? D LYS 100  
1615 1 Y 1 D LEU -216 ? D LEU 101  
1616 1 Y 1 D TYR -215 ? D TYR 102  
1617 1 Y 1 D PRO -214 ? D PRO 103  
1618 1 Y 1 D PHE -213 ? D PHE 104  
1619 1 Y 1 D THR -212 ? D THR 105  
1620 1 Y 1 D TRP -211 ? D TRP 106  
1621 1 Y 1 D ASP -210 ? D ASP 107  
1622 1 Y 1 D ALA -209 ? D ALA 108  
1623 1 Y 1 D VAL -208 ? D VAL 109  
1624 1 Y 1 D ARG -207 ? D ARG 110  
1625 1 Y 1 D TYR -206 ? D TYR 111  
1626 1 Y 1 D ASN -205 ? D ASN 112  
1627 1 Y 1 D GLY -204 ? D GLY 113  
1628 1 Y 1 D LYS -203 ? D LYS 114  
1629 1 Y 1 D LEU -202 ? D LEU 115  
1630 1 Y 1 D ILE -201 ? D ILE 116  
1631 1 Y 1 D ALA -200 ? D ALA 117  
1632 1 Y 1 D TYR -199 ? D TYR 118  
1633 1 Y 1 D PRO -198 ? D PRO 119  
1634 1 Y 1 D ILE -197 ? D ILE 120  
1635 1 Y 1 D ALA -196 ? D ALA 121  
1636 1 Y 1 D VAL -195 ? D VAL 122  
1637 1 Y 1 D GLU -194 ? D GLU 123  
1638 1 Y 1 D ALA -193 ? D ALA 124  
1639 1 Y 1 D LEU -192 ? D LEU 125  
1640 1 Y 1 D SER -191 ? D SER 126  
1641 1 Y 1 D LEU -190 ? D LEU 127  
1642 1 Y 1 D ILE -189 ? D ILE 128  
1643 1 Y 1 D TYR -188 ? D TYR 129  
1644 1 Y 1 D ASN -187 ? D ASN 130  
1645 1 Y 1 D LYS -186 ? D LYS 131  
1646 1 Y 1 D ASP -185 ? D ASP 132  
1647 1 Y 1 D LEU -184 ? D LEU 133  
1648 1 Y 1 D LEU -183 ? D LEU 134  
1649 1 Y 1 D PRO -182 ? D PRO 135  
1650 1 Y 1 D ASN -181 ? D ASN 136  
1651 1 Y 1 D PRO -180 ? D PRO 137  
1652 1 Y 1 D PRO -179 ? D PRO 138  
1653 1 Y 1 D LYS -178 ? D LYS 139  
1654 1 Y 1 D THR -177 ? D THR 140  
1655 1 Y 1 D TRP -176 ? D TRP 141  
1656 1 Y 1 D GLU -175 ? D GLU 142  
1657 1 Y 1 D GLU -174 ? D GLU 143  
1658 1 Y 1 D ILE -173 ? D ILE 144  
1659 1 Y 1 D PRO -172 ? D PRO 145  
1660 1 Y 1 D ALA -171 ? D ALA 146  
1661 1 Y 1 D LEU -170 ? D LEU 147  
1662 1 Y 1 D ASP -169 ? D ASP 148  
1663 1 Y 1 D LYS -168 ? D LYS 149  
1664 1 Y 1 D GLU -167 ? D GLU 150  
1665 1 Y 1 D LEU -166 ? D LEU 151  
1666 1 Y 1 D LYS -165 ? D LYS 152  
1667 1 Y 1 D ALA -164 ? D ALA 153  
1668 1 Y 1 D LYS -163 ? D LYS 154  
1669 1 Y 1 D GLY -162 ? D GLY 155  
1670 1 Y 1 D LYS -161 ? D LYS 156  
1671 1 Y 1 D SER -160 ? D SER 157  
1672 1 Y 1 D ALA -159 ? D ALA 158  
1673 1 Y 1 D LEU -158 ? D LEU 159  
1674 1 Y 1 D MET -157 ? D MET 160  
1675 1 Y 1 D PHE -156 ? D PHE 161  
1676 1 Y 1 D ASN -155 ? D ASN 162  
1677 1 Y 1 D LEU -154 ? D LEU 163  
1678 1 Y 1 D GLN -153 ? D GLN 164  
1679 1 Y 1 D GLU -152 ? D GLU 165  
1680 1 Y 1 D PRO -151 ? D PRO 166  
1681 1 Y 1 D TYR -150 ? D TYR 167  
1682 1 Y 1 D PHE -149 ? D PHE 168  
1683 1 Y 1 D THR -148 ? D THR 169  
1684 1 Y 1 D TRP -147 ? D TRP 170  
1685 1 Y 1 D PRO -146 ? D PRO 171  
1686 1 Y 1 D LEU -145 ? D LEU 172  
1687 1 Y 1 D ILE -144 ? D ILE 173  
1688 1 Y 1 D ALA -143 ? D ALA 174  
1689 1 Y 1 D ALA -142 ? D ALA 175  
1690 1 Y 1 D ASP -141 ? D ASP 176  
1691 1 Y 1 D GLY -140 ? D GLY 177  
1692 1 Y 1 D GLY -139 ? D GLY 178  
1693 1 Y 1 D TYR -138 ? D TYR 179  
1694 1 Y 1 D ALA -137 ? D ALA 180  
1695 1 Y 1 D PHE -136 ? D PHE 181  
1696 1 Y 1 D LYS -135 ? D LYS 182  
1697 1 Y 1 D TYR -134 ? D TYR 183  
1698 1 Y 1 D GLU -133 ? D GLU 184  
1699 1 Y 1 D ASN -132 ? D ASN 185  
1700 1 Y 1 D GLY -131 ? D GLY 186  
1701 1 Y 1 D LYS -130 ? D LYS 187  
1702 1 Y 1 D TYR -129 ? D TYR 188  
1703 1 Y 1 D ASP -128 ? D ASP 189  
1704 1 Y 1 D ILE -127 ? D ILE 190  
1705 1 Y 1 D LYS -126 ? D LYS 191  
1706 1 Y 1 D ASP -125 ? D ASP 192  
1707 1 Y 1 D VAL -124 ? D VAL 193  
1708 1 Y 1 D GLY -123 ? D GLY 194  
1709 1 Y 1 D VAL -122 ? D VAL 195  
1710 1 Y 1 D ASP -121 ? D ASP 196  
1711 1 Y 1 D ASN -120 ? D ASN 197  
1712 1 Y 1 D ALA -119 ? D ALA 198  
1713 1 Y 1 D GLY -118 ? D GLY 199  
1714 1 Y 1 D ALA -117 ? D ALA 200  
1715 1 Y 1 D LYS -116 ? D LYS 201  
1716 1 Y 1 D ALA -115 ? D ALA 202  
1717 1 Y 1 D GLY -114 ? D GLY 203  
1718 1 Y 1 D LEU -113 ? D LEU 204  
1719 1 Y 1 D THR -112 ? D THR 205  
1720 1 Y 1 D PHE -111 ? D PHE 206  
1721 1 Y 1 D LEU -110 ? D LEU 207  
1722 1 Y 1 D VAL -109 ? D VAL 208  
1723 1 Y 1 D ASP -108 ? D ASP 209  
1724 1 Y 1 D LEU -107 ? D LEU 210  
1725 1 Y 1 D ILE -106 ? D ILE 211  
1726 1 Y 1 D LYS -105 ? D LYS 212  
1727 1 Y 1 D ASN -104 ? D ASN 213  
1728 1 Y 1 D LYS -103 ? D LYS 214  
1729 1 Y 1 D HIS -102 ? D HIS 215  
1730 1 Y 1 D MET -101 ? D MET 216  
1731 1 Y 1 D ASN -100 ? D ASN 217  
1732 1 Y 1 D ALA -99  ? D ALA 218  
1733 1 Y 1 D ASP -98  ? D ASP 219  
1734 1 Y 1 D THR -97  ? D THR 220  
1735 1 Y 1 D ASP -96  ? D ASP 221  
1736 1 Y 1 D TYR -95  ? D TYR 222  
1737 1 Y 1 D SER -94  ? D SER 223  
1738 1 Y 1 D ILE -93  ? D ILE 224  
1739 1 Y 1 D ALA -92  ? D ALA 225  
1740 1 Y 1 D GLU -91  ? D GLU 226  
1741 1 Y 1 D ALA -90  ? D ALA 227  
1742 1 Y 1 D ALA -89  ? D ALA 228  
1743 1 Y 1 D PHE -88  ? D PHE 229  
1744 1 Y 1 D ASN -87  ? D ASN 230  
1745 1 Y 1 D LYS -86  ? D LYS 231  
1746 1 Y 1 D GLY -85  ? D GLY 232  
1747 1 Y 1 D GLU -84  ? D GLU 233  
1748 1 Y 1 D THR -83  ? D THR 234  
1749 1 Y 1 D ALA -82  ? D ALA 235  
1750 1 Y 1 D MET -81  ? D MET 236  
1751 1 Y 1 D THR -80  ? D THR 237  
1752 1 Y 1 D ILE -79  ? D ILE 238  
1753 1 Y 1 D ASN -78  ? D ASN 239  
1754 1 Y 1 D GLY -77  ? D GLY 240  
1755 1 Y 1 D PRO -76  ? D PRO 241  
1756 1 Y 1 D TRP -75  ? D TRP 242  
1757 1 Y 1 D ALA -74  ? D ALA 243  
1758 1 Y 1 D TRP -73  ? D TRP 244  
1759 1 Y 1 D SER -72  ? D SER 245  
1760 1 Y 1 D ASN -71  ? D ASN 246  
1761 1 Y 1 D ILE -70  ? D ILE 247  
1762 1 Y 1 D ASP -69  ? D ASP 248  
1763 1 Y 1 D THR -68  ? D THR 249  
1764 1 Y 1 D SER -67  ? D SER 250  
1765 1 Y 1 D LYS -66  ? D LYS 251  
1766 1 Y 1 D VAL -65  ? D VAL 252  
1767 1 Y 1 D ASN -64  ? D ASN 253  
1768 1 Y 1 D TYR -63  ? D TYR 254  
1769 1 Y 1 D GLY -62  ? D GLY 255  
1770 1 Y 1 D VAL -61  ? D VAL 256  
1771 1 Y 1 D THR -60  ? D THR 257  
1772 1 Y 1 D VAL -59  ? D VAL 258  
1773 1 Y 1 D LEU -58  ? D LEU 259  
1774 1 Y 1 D PRO -57  ? D PRO 260  
1775 1 Y 1 D THR -56  ? D THR 261  
1776 1 Y 1 D PHE -55  ? D PHE 262  
1777 1 Y 1 D LYS -54  ? D LYS 263  
1778 1 Y 1 D GLY -53  ? D GLY 264  
1779 1 Y 1 D GLN -52  ? D GLN 265  
1780 1 Y 1 D PRO -51  ? D PRO 266  
1781 1 Y 1 D SER -50  ? D SER 267  
1782 1 Y 1 D LYS -49  ? D LYS 268  
1783 1 Y 1 D PRO -48  ? D PRO 269  
1784 1 Y 1 D PHE -47  ? D PHE 270  
1785 1 Y 1 D VAL -46  ? D VAL 271  
1786 1 Y 1 D GLY -45  ? D GLY 272  
1787 1 Y 1 D VAL -44  ? D VAL 273  
1788 1 Y 1 D LEU -43  ? D LEU 274  
1789 1 Y 1 D SER -42  ? D SER 275  
1790 1 Y 1 D ALA -41  ? D ALA 276  
1791 1 Y 1 D GLY -40  ? D GLY 277  
1792 1 Y 1 D ILE -39  ? D ILE 278  
1793 1 Y 1 D ASN -38  ? D ASN 279  
1794 1 Y 1 D ALA -37  ? D ALA 280  
1795 1 Y 1 D ALA -36  ? D ALA 281  
1796 1 Y 1 D SER -35  ? D SER 282  
1797 1 Y 1 D PRO -34  ? D PRO 283  
1798 1 Y 1 D ASN -33  ? D ASN 284  
1799 1 Y 1 D LYS -32  ? D LYS 285  
1800 1 Y 1 D GLU -31  ? D GLU 286  
1801 1 Y 1 D LEU -30  ? D LEU 287  
1802 1 Y 1 D ALA -29  ? D ALA 288  
1803 1 Y 1 D LYS -28  ? D LYS 289  
1804 1 Y 1 D GLU -27  ? D GLU 290  
1805 1 Y 1 D PHE -26  ? D PHE 291  
1806 1 Y 1 D LEU -25  ? D LEU 292  
1807 1 Y 1 D GLU -24  ? D GLU 293  
1808 1 Y 1 D ASN -23  ? D ASN 294  
1809 1 Y 1 D TYR -22  ? D TYR 295  
1810 1 Y 1 D LEU -21  ? D LEU 296  
1811 1 Y 1 D LEU -20  ? D LEU 297  
1812 1 Y 1 D THR -19  ? D THR 298  
1813 1 Y 1 D ASP -18  ? D ASP 299  
1814 1 Y 1 D GLU -17  ? D GLU 300  
1815 1 Y 1 D GLY -16  ? D GLY 301  
1816 1 Y 1 D LEU -15  ? D LEU 302  
1817 1 Y 1 D GLU -14  ? D GLU 303  
1818 1 Y 1 D ALA -13  ? D ALA 304  
1819 1 Y 1 D VAL -12  ? D VAL 305  
1820 1 Y 1 D ASN -11  ? D ASN 306  
1821 1 Y 1 D LYS -10  ? D LYS 307  
1822 1 Y 1 D ASP -9   ? D ASP 308  
1823 1 Y 1 D LYS -8   ? D LYS 309  
1824 1 Y 1 D PRO -7   ? D PRO 310  
1825 1 Y 1 D LEU -6   ? D LEU 311  
1826 1 Y 1 D GLY -5   ? D GLY 312  
1827 1 Y 1 D ALA -4   ? D ALA 313  
1828 1 Y 1 D VAL -3   ? D VAL 314  
1829 1 Y 1 D ALA -2   ? D ALA 315  
1830 1 Y 1 D LEU -1   ? D LEU 316  
1831 1 Y 1 D LYS 0    ? D LYS 317  
1832 1 Y 1 D SER 1    ? D SER 318  
1833 1 Y 1 D TYR 2    ? D TYR 319  
1834 1 Y 1 D GLU 3    ? D GLU 320  
1835 1 Y 1 D GLU 4    ? D GLU 321  
1836 1 Y 1 D GLU 5    ? D GLU 322  
1837 1 Y 1 D LEU 6    ? D LEU 323  
1838 1 Y 1 D ALA 7    ? D ALA 324  
1839 1 Y 1 D LYS 8    ? D LYS 325  
1840 1 Y 1 D ASP 9    ? D ASP 326  
1841 1 Y 1 D PRO 10   ? D PRO 327  
1842 1 Y 1 D ARG 11   ? D ARG 328  
1843 1 Y 1 D ILE 12   ? D ILE 329  
1844 1 Y 1 D ALA 13   ? D ALA 330  
1845 1 Y 1 D ALA 14   ? D ALA 331  
1846 1 Y 1 D THR 15   ? D THR 332  
1847 1 Y 1 D MET 16   ? D MET 333  
1848 1 Y 1 D GLU 17   ? D GLU 334  
1849 1 Y 1 D ASN 18   ? D ASN 335  
1850 1 Y 1 D ALA 19   ? D ALA 336  
1851 1 Y 1 D GLN 20   ? D GLN 337  
1852 1 Y 1 D LYS 21   ? D LYS 338  
1853 1 Y 1 D GLY 22   ? D GLY 339  
1854 1 Y 1 D GLU 23   ? D GLU 340  
1855 1 Y 1 D ILE 24   ? D ILE 341  
1856 1 Y 1 D MET 25   ? D MET 342  
1857 1 Y 1 D PRO 26   ? D PRO 343  
1858 1 Y 1 D ASN 27   ? D ASN 344  
1859 1 Y 1 D ILE 28   ? D ILE 345  
1860 1 Y 1 D PRO 29   ? D PRO 346  
1861 1 Y 1 D GLN 30   ? D GLN 347  
1862 1 Y 1 D MET 31   ? D MET 348  
1863 1 Y 1 D SER 32   ? D SER 349  
1864 1 Y 1 D ALA 33   ? D ALA 350  
1865 1 Y 1 D PHE 34   ? D PHE 351  
1866 1 Y 1 D TRP 35   ? D TRP 352  
1867 1 Y 1 D TYR 36   ? D TYR 353  
1868 1 Y 1 D ALA 37   ? D ALA 354  
1869 1 Y 1 D VAL 38   ? D VAL 355  
1870 1 Y 1 D ARG 39   ? D ARG 356  
1871 1 Y 1 D THR 40   ? D THR 357  
1872 1 Y 1 D ALA 41   ? D ALA 358  
1873 1 Y 1 D VAL 42   ? D VAL 359  
1874 1 Y 1 D ILE 43   ? D ILE 360  
1875 1 Y 1 D ASN 44   ? D ASN 361  
1876 1 Y 1 D ALA 45   ? D ALA 362  
1877 1 Y 1 D ALA 46   ? D ALA 363  
1878 1 Y 1 D SER 47   ? D SER 364  
1879 1 Y 1 D GLY 48   ? D GLY 365  
1880 1 Y 1 D ARG 49   ? D ARG 366  
1881 1 Y 1 D GLN 50   ? D GLN 367  
1882 1 Y 1 D THR 51   ? D THR 368  
1883 1 Y 1 D VAL 52   ? D VAL 369  
1884 1 Y 1 D ASP 53   ? D ASP 370  
1885 1 Y 1 D GLU 54   ? D GLU 371  
1886 1 Y 1 D ALA 55   ? D ALA 372  
1887 1 Y 1 D LEU 56   ? D LEU 373  
1888 1 Y 1 D LYS 57   ? D LYS 374  
1889 1 Y 1 D ASP 58   ? D ASP 375  
1890 1 Y 1 D ALA 59   ? D ALA 376  
1891 1 Y 1 D GLN 60   ? D GLN 377  
1892 1 Y 1 D THR 61   ? D THR 378  
1893 1 Y 1 D GLY 62   ? D GLY 379  
1894 1 Y 1 D THR 63   ? D THR 380  
1895 1 Y 1 D ASP 64   ? D ASP 381  
1896 1 Y 1 D TYR 65   ? D TYR 382  
1897 1 Y 1 D ASP 66   ? D ASP 383  
1898 1 Y 1 D ILE 67   ? D ILE 384  
1899 1 Y 1 D PRO 68   ? D PRO 385  
1900 1 Y 1 D THR 69   ? D THR 386  
1901 1 Y 1 D THR 70   ? D THR 387  
1902 1 Y 1 D GLU 71   ? D GLU 388  
1903 1 Y 1 D ASN 72   ? D ASN 389  
1904 1 Y 1 D LEU 73   ? D LEU 390  
1905 1 Y 1 D TYR 74   ? D TYR 391  
1906 1 Y 1 D PHE 75   ? D PHE 392  
1907 1 Y 1 D GLN 76   ? D GLN 393  
1908 1 Y 1 D GLY 77   ? D GLY 394  
1909 1 Y 1 D GLY 78   ? D GLY 395  
1910 1 Y 1 D SER 79   ? D SER 396  
1911 1 Y 1 D ASN 80   ? D ASN 397  
1912 1 Y 1 D HIS 81   ? D HIS 398  
1913 1 Y 1 D SER 82   ? D SER 399  
1914 1 Y 1 D PHE 83   ? D PHE 400  
1915 1 Y 1 D GLU 84   ? D GLU 401  
1916 1 Y 1 D GLU 85   ? D GLU 402  
1917 1 Y 1 D VAL 86   ? D VAL 403  
1918 1 Y 1 D VAL 87   ? D VAL 404  
1919 1 Y 1 D GLN 88   ? D GLN 405  
1920 1 Y 1 D THR 89   ? D THR 406  
1921 1 Y 1 D LEU 90   ? D LEU 407  
1922 1 Y 1 D ALA 91   ? D ALA 408  
1923 1 Y 1 D SER 92   ? D SER 409  
1924 1 Y 1 D LEU 93   ? D LEU 410  
1925 1 Y 1 D ALA 94   ? D ALA 411  
1926 1 Y 1 D THR 95   ? D THR 412  
1927 1 Y 1 D VAL 96   ? D VAL 413  
1928 1 Y 1 D VAL 97   ? D VAL 414  
1929 1 Y 1 D GLN 98   ? D GLN 415  
1930 1 Y 1 D GLN 99   ? D GLN 416  
1931 1 Y 1 D GLN 100  ? D GLN 417  
1932 1 Y 1 D THR 101  ? D THR 418  
1933 1 Y 1 D ILE 102  ? D ILE 419  
1934 1 Y 1 D ALA 103  ? D ALA 420  
1935 1 Y 1 D SER 104  ? D SER 421  
1936 1 Y 1 D GLU 105  ? D GLU 422  
1937 1 Y 1 D SER 106  ? D SER 423  
1938 1 Y 1 D LEU 107  ? D LEU 424  
1939 1 Y 1 D GLU 108  ? D GLU 425  
1940 1 Y 1 D GLN 109  ? D GLN 426  
1941 1 Y 1 D ARG 110  ? D ARG 427  
1942 1 Y 1 D ILE 111  ? D ILE 428  
1943 1 Y 1 D THR 112  ? D THR 429  
1944 1 Y 1 D SER 113  ? D SER 430  
1945 1 Y 1 D LEU 114  ? D LEU 431  
1946 1 Y 1 D GLU 115  ? D GLU 432  
1947 1 Y 1 D ASN 116  ? D ASN 433  
1948 1 Y 1 D GLY 117  ? D GLY 434  
1949 1 Y 1 D LEU 118  ? D LEU 435  
1950 1 Y 1 D LYS 119  ? D LYS 436  
1951 1 Y 1 D GLY 150  ? D GLY 467  
1952 1 Y 1 D ARG 151  ? D ARG 468  
1953 1 Y 1 D ALA 152  ? D ALA 469  
1954 1 Y 1 D THR 153  ? D THR 470  
1955 1 Y 1 D ALA 154  ? D ALA 471  
1956 1 Y 1 D THR 155  ? D THR 472  
1957 1 Y 1 D ALA 156  ? D ALA 473  
1958 1 Y 1 D ALA 157  ? D ALA 474  
1959 1 Y 1 D ALA 158  ? D ALA 475  
1960 1 Y 1 D THR 159  ? D THR 476  
1961 1 Y 1 D GLU 160  ? D GLU 477  
1962 1 Y 1 D ALA 161  ? D ALA 478  
1963 1 Y 1 D TYR 162  ? D TYR 479  
1964 1 Y 1 D TRP 163  ? D TRP 480  
1965 1 Y 1 D ALA 164  ? D ALA 481  
1966 1 Y 1 D GLU 165  ? D GLU 482  
1967 1 Y 1 D HIS 166  ? D HIS 483  
1968 1 Y 1 D GLY 167  ? D GLY 484  
1969 1 Y 1 D GLN 168  ? D GLN 485  
1970 1 Y 1 D PRO 169  ? D PRO 486  
1971 1 Y 1 D PRO 170  ? D PRO 487  
1972 1 Y 1 D PRO 171  ? D PRO 488  
1973 1 Y 1 D GLY 172  ? D GLY 489  
1974 1 Y 1 D PRO 173  ? D PRO 490  
1975 1 Y 1 D SER 174  ? D SER 491  
1976 1 Y 1 D LEU 175  ? D LEU 492  
1977 1 Y 1 D TYR 176  ? D TYR 493  
1978 1 Y 1 D GLU 177  ? D GLU 494  
1979 1 Y 1 D GLU 178  ? D GLU 495  
1980 1 Y 1 D SER 179  ? D SER 496  
1981 1 Y 1 D ALA 180  ? D ALA 497  
1982 1 Y 1 D ILE 181  ? D ILE 498  
1983 1 Y 1 D ARG 182  ? D ARG 499  
1984 1 Y 1 D GLY 183  ? D GLY 500  
1985 1 Y 1 D LYS 184  ? D LYS 501  
1986 1 Y 1 D ILE 185  ? D ILE 502  
1987 1 Y 1 D GLU 186  ? D GLU 503  
1988 1 Y 1 D SER 187  ? D SER 504  
1989 1 Y 1 D ARG 188  ? D ARG 505  
1990 1 Y 1 D ASP 189  ? D ASP 506  
1991 1 Y 1 D GLU 190  ? D GLU 507  
1992 1 Y 1 D THR 191  ? D THR 508  
1993 1 Y 1 D VAL 192  ? D VAL 509  
1994 1 Y 1 D PRO 193  ? D PRO 510  
1995 1 Y 1 D GLN 194  ? D GLN 511  
1996 1 Y 1 D SER 195  ? D SER 512  
1997 1 Y 1 D VAL 196  ? D VAL 513  
1998 1 Y 1 D ARG 197  ? D ARG 514  
1999 1 Y 1 D GLU 198  ? D GLU 515  
2000 1 Y 1 D ALA 199  ? D ALA 516  
2001 1 Y 1 D PHE 200  ? D PHE 517  
2002 1 Y 1 D ASN 201  ? D ASN 518  
2003 1 Y 1 D ASN 202  ? D ASN 519  
2004 1 Y 1 D LEU 203  ? D LEU 520  
2005 1 Y 1 D ASN 204  ? D ASN 521  
2006 1 Y 1 D SER 205  ? D SER 522  
2007 1 Y 1 D THR 206  ? D THR 523  
2008 1 Y 1 D THR 207  ? D THR 524  
2009 1 Y 1 D SER 208  ? D SER 525  
2010 1 Y 1 D LEU 209  ? D LEU 526  
2011 1 Y 1 D THR 210  ? D THR 527  
2012 1 Y 1 D GLU 211  ? D GLU 528  
2013 1 Y 1 D GLU 212  ? D GLU 529  
2014 1 Y 1 D ASN 213  ? D ASN 530  
2015 1 Y 1 D PHE 214  ? D PHE 531  
2016 1 Y 1 D GLY 215  ? D GLY 532  
2017 1 Y 1 D LYS 216  ? D LYS 533  
2018 1 Y 1 D PRO 217  ? D PRO 534  
2019 1 Y 1 D ASP 218  ? D ASP 535  
2020 1 Y 1 D ILE 219  ? D ILE 536  
2021 1 Y 1 D SER 220  ? D SER 537  
2022 1 Y 1 D ALA 221  ? D ALA 538  
2023 1 Y 1 D LYS 222  ? D LYS 539  
2024 1 Y 1 D ASP 223  ? D ASP 540  
2025 1 Y 1 D LEU 224  ? D LEU 541  
2026 1 Y 1 D ARG 225  ? D ARG 542  
2027 1 Y 1 D ASN 226  ? D ASN 543  
2028 1 Y 1 D ILE 227  ? D ILE 544  
2029 1 Y 1 D MET 228  ? D MET 545  
2030 1 Y 1 D TYR 229  ? D TYR 546  
2031 1 Y 1 D ASP 230  ? D ASP 547  
2032 1 Y 1 D HIS 231  ? D HIS 548  
2033 1 Y 1 D LEU 232  ? D LEU 549  
2034 1 Y 1 D PRO 233  ? D PRO 550  
2035 1 Y 1 D GLY 234  ? D GLY 551  
2036 1 Y 1 D PHE 235  ? D PHE 552  
2037 1 Y 1 D GLY 236  ? D GLY 553  
2038 1 Y 1 D THR 237  ? D THR 554  
2039 1 Y 1 D ALA 238  ? D ALA 555  
2040 1 Y 1 D PHE 239  ? D PHE 556  
2041 1 Y 1 D HIS 240  ? D HIS 557  
2042 1 Y 1 D GLN 241  ? D GLN 558  
2043 1 Y 1 D LEU 242  ? D LEU 559  
2044 1 Y 1 D VAL 243  ? D VAL 560  
2045 1 Y 1 D GLN 244  ? D GLN 561  
2046 1 Y 1 D VAL 245  ? D VAL 562  
2047 1 Y 1 D ILE 246  ? D ILE 563  
2048 1 Y 1 D CYS 247  ? D CYS 564  
2049 1 Y 1 D LYS 248  ? D LYS 565  
2050 1 Y 1 D LEU 249  ? D LEU 566  
2051 1 Y 1 D GLY 250  ? D GLY 567  
2052 1 Y 1 D LYS 251  ? D LYS 568  
2053 1 Y 1 D ASP 252  ? D ASP 569  
2054 1 Y 1 D SER 253  ? D SER 570  
2055 1 Y 1 D ASN 254  ? D ASN 571  
2056 1 Y 1 D SER 255  ? D SER 572  
2057 1 Y 1 D LEU 256  ? D LEU 573  
2058 1 Y 1 D ASP 257  ? D ASP 574  
2059 1 Y 1 D ILE 258  ? D ILE 575  
2060 1 Y 1 D ILE 259  ? D ILE 576  
2061 1 Y 1 D HIS 260  ? D HIS 577  
2062 1 Y 1 D ALA 261  ? D ALA 578  
2063 1 Y 1 D GLU 262  ? D GLU 579  
2064 1 Y 1 D PHE 263  ? D PHE 580  
2065 1 Y 1 D GLN 264  ? D GLN 581  
2066 1 Y 1 D ALA 265  ? D ALA 582  
2067 1 Y 1 D SER 266  ? D SER 583  
2068 1 Y 1 D LEU 267  ? D LEU 584  
2069 1 Y 1 D ALA 268  ? D ALA 585  
2070 1 Y 1 D GLU 269  ? D GLU 586  
2071 1 Y 1 D GLY 270  ? D GLY 587  
2072 1 Y 1 D ASP 271  ? D ASP 588  
2073 1 Y 1 D SER 272  ? D SER 589  
2074 1 Y 1 D PRO 273  ? D PRO 590  
2075 1 Y 1 D GLN 274  ? D GLN 591  
2076 1 Y 1 D CYS 275  ? D CYS 592  
2077 1 Y 1 D ALA 276  ? D ALA 593  
2078 1 Y 1 D LEU 277  ? D LEU 594  
2079 1 Y 1 D ILE 278  ? D ILE 595  
2080 1 Y 1 D GLN 279  ? D GLN 596  
2081 1 Y 1 D ILE 280  ? D ILE 597  
2082 1 Y 1 D THR 281  ? D THR 598  
2083 1 Y 1 D LYS 282  ? D LYS 599  
2084 1 Y 1 D ARG 283  ? D ARG 600  
2085 1 Y 1 D VAL 284  ? D VAL 601  
2086 1 Y 1 D PRO 285  ? D PRO 602  
2087 1 Y 1 D ILE 286  ? D ILE 603  
2088 1 Y 1 D PHE 287  ? D PHE 604  
2089 1 Y 1 D GLN 288  ? D GLN 605  
2090 1 Y 1 D ASP 289  ? D ASP 606  
2091 1 Y 1 D ALA 290  ? D ALA 607  
2092 1 Y 1 D ALA 291  ? D ALA 608  
2093 1 Y 1 D PRO 292  ? D PRO 609  
2094 1 Y 1 D PRO 293  ? D PRO 610  
2095 1 Y 1 D VAL 294  ? D VAL 611  
2096 1 Y 1 D ILE 295  ? D ILE 612  
2097 1 Y 1 D HIS 296  ? D HIS 613  
2098 1 Y 1 D ILE 297  ? D ILE 614  
2099 1 Y 1 D ARG 298  ? D ARG 615  
2100 1 Y 1 D SER 299  ? D SER 616  
2101 1 Y 1 D ARG 300  ? D ARG 617  
2102 1 Y 1 D GLY 301  ? D GLY 618  
2103 1 Y 1 D ASP 302  ? D ASP 619  
2104 1 Y 1 D ILE 303  ? D ILE 620  
2105 1 Y 1 D PRO 304  ? D PRO 621  
2106 1 Y 1 D ARG 305  ? D ARG 622  
2107 1 Y 1 D ALA 306  ? D ALA 623  
2108 1 Y 1 D CYS 307  ? D CYS 624  
2109 1 Y 1 D GLN 308  ? D GLN 625  
2110 1 Y 1 D LYS 309  ? D LYS 626  
2111 1 Y 1 D SER 310  ? D SER 627  
2112 1 Y 1 D LEU 311  ? D LEU 628  
2113 1 Y 1 D ARG 312  ? D ARG 629  
2114 1 Y 1 D PRO 313  ? D PRO 630  
2115 1 Y 1 D VAL 314  ? D VAL 631  
2116 1 Y 1 D PRO 315  ? D PRO 632  
2117 1 Y 1 D PRO 316  ? D PRO 633  
2118 1 Y 1 D SER 317  ? D SER 634  
2119 1 Y 1 D PRO 318  ? D PRO 635  
2120 1 Y 1 D LYS 319  ? D LYS 636  
2121 1 Y 1 D ILE 320  ? D ILE 637  
2122 1 Y 1 D ASP 321  ? D ASP 638  
2123 1 Y 1 D ARG 322  ? D ARG 639  
2124 1 Y 1 D GLY 323  ? D GLY 640  
2125 1 Y 1 D TRP 324  ? D TRP 641  
2126 1 Y 1 D VAL 325  ? D VAL 642  
2127 1 Y 1 D CYS 326  ? D CYS 643  
2128 1 Y 1 D VAL 327  ? D VAL 644  
2129 1 Y 1 D PHE 328  ? D PHE 645  
2130 1 Y 1 D GLN 329  ? D GLN 646  
2131 1 Y 1 D LEU 330  ? D LEU 647  
2132 1 Y 1 D GLN 331  ? D GLN 648  
2133 1 Y 1 D ASP 332  ? D ASP 649  
2134 1 Y 1 D GLY 333  ? D GLY 650  
2135 1 Y 1 D LYS 334  ? D LYS 651  
2136 1 Y 1 D THR 335  ? D THR 652  
2137 1 Y 1 D LEU 336  ? D LEU 653  
2138 1 Y 1 D GLY 337  ? D GLY 654  
2139 1 Y 1 D LEU 338  ? D LEU 655  
2140 1 Y 1 D LYS 339  ? D LYS 656  
2141 1 Y 1 D ILE 340  ? D ILE 657  
2142 1 Y 1 E MET -316 ? E MET 1    
2143 1 Y 1 E GLY -315 ? E GLY 2    
2144 1 Y 1 E SER -314 ? E SER 3    
2145 1 Y 1 E SER -313 ? E SER 4    
2146 1 Y 1 E HIS -312 ? E HIS 5    
2147 1 Y 1 E HIS -311 ? E HIS 6    
2148 1 Y 1 E HIS -310 ? E HIS 7    
2149 1 Y 1 E HIS -309 ? E HIS 8    
2150 1 Y 1 E HIS -308 ? E HIS 9    
2151 1 Y 1 E HIS -307 ? E HIS 10   
2152 1 Y 1 E GLY -306 ? E GLY 11   
2153 1 Y 1 E THR -305 ? E THR 12   
2154 1 Y 1 E LYS -304 ? E LYS 13   
2155 1 Y 1 E THR -303 ? E THR 14   
2156 1 Y 1 E GLU -302 ? E GLU 15   
2157 1 Y 1 E GLU -301 ? E GLU 16   
2158 1 Y 1 E GLY -300 ? E GLY 17   
2159 1 Y 1 E LYS -299 ? E LYS 18   
2160 1 Y 1 E LEU -298 ? E LEU 19   
2161 1 Y 1 E VAL -297 ? E VAL 20   
2162 1 Y 1 E ILE -296 ? E ILE 21   
2163 1 Y 1 E TRP -295 ? E TRP 22   
2164 1 Y 1 E ILE -294 ? E ILE 23   
2165 1 Y 1 E ASN -293 ? E ASN 24   
2166 1 Y 1 E GLY -292 ? E GLY 25   
2167 1 Y 1 E ASP -291 ? E ASP 26   
2168 1 Y 1 E LYS -290 ? E LYS 27   
2169 1 Y 1 E GLY -289 ? E GLY 28   
2170 1 Y 1 E TYR -288 ? E TYR 29   
2171 1 Y 1 E ASN -287 ? E ASN 30   
2172 1 Y 1 E GLY -286 ? E GLY 31   
2173 1 Y 1 E LEU -285 ? E LEU 32   
2174 1 Y 1 E ALA -284 ? E ALA 33   
2175 1 Y 1 E GLU -283 ? E GLU 34   
2176 1 Y 1 E VAL -282 ? E VAL 35   
2177 1 Y 1 E GLY -281 ? E GLY 36   
2178 1 Y 1 E LYS -280 ? E LYS 37   
2179 1 Y 1 E LYS -279 ? E LYS 38   
2180 1 Y 1 E PHE -278 ? E PHE 39   
2181 1 Y 1 E GLU -277 ? E GLU 40   
2182 1 Y 1 E LYS -276 ? E LYS 41   
2183 1 Y 1 E ASP -275 ? E ASP 42   
2184 1 Y 1 E THR -274 ? E THR 43   
2185 1 Y 1 E GLY -273 ? E GLY 44   
2186 1 Y 1 E ILE -272 ? E ILE 45   
2187 1 Y 1 E LYS -271 ? E LYS 46   
2188 1 Y 1 E VAL -270 ? E VAL 47   
2189 1 Y 1 E THR -269 ? E THR 48   
2190 1 Y 1 E VAL -268 ? E VAL 49   
2191 1 Y 1 E GLU -267 ? E GLU 50   
2192 1 Y 1 E HIS -266 ? E HIS 51   
2193 1 Y 1 E PRO -265 ? E PRO 52   
2194 1 Y 1 E ASP -264 ? E ASP 53   
2195 1 Y 1 E LYS -263 ? E LYS 54   
2196 1 Y 1 E LEU -262 ? E LEU 55   
2197 1 Y 1 E GLU -261 ? E GLU 56   
2198 1 Y 1 E GLU -260 ? E GLU 57   
2199 1 Y 1 E LYS -259 ? E LYS 58   
2200 1 Y 1 E PHE -258 ? E PHE 59   
2201 1 Y 1 E PRO -257 ? E PRO 60   
2202 1 Y 1 E GLN -256 ? E GLN 61   
2203 1 Y 1 E VAL -255 ? E VAL 62   
2204 1 Y 1 E ALA -254 ? E ALA 63   
2205 1 Y 1 E ALA -253 ? E ALA 64   
2206 1 Y 1 E THR -252 ? E THR 65   
2207 1 Y 1 E GLY -251 ? E GLY 66   
2208 1 Y 1 E ASP -250 ? E ASP 67   
2209 1 Y 1 E GLY -249 ? E GLY 68   
2210 1 Y 1 E PRO -248 ? E PRO 69   
2211 1 Y 1 E ASP -247 ? E ASP 70   
2212 1 Y 1 E ILE -246 ? E ILE 71   
2213 1 Y 1 E ILE -245 ? E ILE 72   
2214 1 Y 1 E PHE -244 ? E PHE 73   
2215 1 Y 1 E TRP -243 ? E TRP 74   
2216 1 Y 1 E ALA -242 ? E ALA 75   
2217 1 Y 1 E HIS -241 ? E HIS 76   
2218 1 Y 1 E ASP -240 ? E ASP 77   
2219 1 Y 1 E ARG -239 ? E ARG 78   
2220 1 Y 1 E PHE -238 ? E PHE 79   
2221 1 Y 1 E GLY -237 ? E GLY 80   
2222 1 Y 1 E GLY -236 ? E GLY 81   
2223 1 Y 1 E TYR -235 ? E TYR 82   
2224 1 Y 1 E ALA -234 ? E ALA 83   
2225 1 Y 1 E GLN -233 ? E GLN 84   
2226 1 Y 1 E SER -232 ? E SER 85   
2227 1 Y 1 E GLY -231 ? E GLY 86   
2228 1 Y 1 E LEU -230 ? E LEU 87   
2229 1 Y 1 E LEU -229 ? E LEU 88   
2230 1 Y 1 E ALA -228 ? E ALA 89   
2231 1 Y 1 E GLU -227 ? E GLU 90   
2232 1 Y 1 E ILE -226 ? E ILE 91   
2233 1 Y 1 E THR -225 ? E THR 92   
2234 1 Y 1 E PRO -224 ? E PRO 93   
2235 1 Y 1 E ASP -223 ? E ASP 94   
2236 1 Y 1 E LYS -222 ? E LYS 95   
2237 1 Y 1 E ALA -221 ? E ALA 96   
2238 1 Y 1 E PHE -220 ? E PHE 97   
2239 1 Y 1 E GLN -219 ? E GLN 98   
2240 1 Y 1 E ASP -218 ? E ASP 99   
2241 1 Y 1 E LYS -217 ? E LYS 100  
2242 1 Y 1 E LEU -216 ? E LEU 101  
2243 1 Y 1 E TYR -215 ? E TYR 102  
2244 1 Y 1 E PRO -214 ? E PRO 103  
2245 1 Y 1 E PHE -213 ? E PHE 104  
2246 1 Y 1 E THR -212 ? E THR 105  
2247 1 Y 1 E TRP -211 ? E TRP 106  
2248 1 Y 1 E ASP -210 ? E ASP 107  
2249 1 Y 1 E ALA -209 ? E ALA 108  
2250 1 Y 1 E VAL -208 ? E VAL 109  
2251 1 Y 1 E ARG -207 ? E ARG 110  
2252 1 Y 1 E TYR -206 ? E TYR 111  
2253 1 Y 1 E ASN -205 ? E ASN 112  
2254 1 Y 1 E GLY -204 ? E GLY 113  
2255 1 Y 1 E LYS -203 ? E LYS 114  
2256 1 Y 1 E LEU -202 ? E LEU 115  
2257 1 Y 1 E ILE -201 ? E ILE 116  
2258 1 Y 1 E ALA -200 ? E ALA 117  
2259 1 Y 1 E TYR -199 ? E TYR 118  
2260 1 Y 1 E PRO -198 ? E PRO 119  
2261 1 Y 1 E ILE -197 ? E ILE 120  
2262 1 Y 1 E ALA -196 ? E ALA 121  
2263 1 Y 1 E VAL -195 ? E VAL 122  
2264 1 Y 1 E GLU -194 ? E GLU 123  
2265 1 Y 1 E ALA -193 ? E ALA 124  
2266 1 Y 1 E LEU -192 ? E LEU 125  
2267 1 Y 1 E SER -191 ? E SER 126  
2268 1 Y 1 E LEU -190 ? E LEU 127  
2269 1 Y 1 E ILE -189 ? E ILE 128  
2270 1 Y 1 E TYR -188 ? E TYR 129  
2271 1 Y 1 E ASN -187 ? E ASN 130  
2272 1 Y 1 E LYS -186 ? E LYS 131  
2273 1 Y 1 E ASP -185 ? E ASP 132  
2274 1 Y 1 E LEU -184 ? E LEU 133  
2275 1 Y 1 E LEU -183 ? E LEU 134  
2276 1 Y 1 E PRO -182 ? E PRO 135  
2277 1 Y 1 E ASN -181 ? E ASN 136  
2278 1 Y 1 E PRO -180 ? E PRO 137  
2279 1 Y 1 E PRO -179 ? E PRO 138  
2280 1 Y 1 E LYS -178 ? E LYS 139  
2281 1 Y 1 E THR -177 ? E THR 140  
2282 1 Y 1 E TRP -176 ? E TRP 141  
2283 1 Y 1 E GLU -175 ? E GLU 142  
2284 1 Y 1 E GLU -174 ? E GLU 143  
2285 1 Y 1 E ILE -173 ? E ILE 144  
2286 1 Y 1 E PRO -172 ? E PRO 145  
2287 1 Y 1 E ALA -171 ? E ALA 146  
2288 1 Y 1 E LEU -170 ? E LEU 147  
2289 1 Y 1 E ASP -169 ? E ASP 148  
2290 1 Y 1 E LYS -168 ? E LYS 149  
2291 1 Y 1 E GLU -167 ? E GLU 150  
2292 1 Y 1 E LEU -166 ? E LEU 151  
2293 1 Y 1 E LYS -165 ? E LYS 152  
2294 1 Y 1 E ALA -164 ? E ALA 153  
2295 1 Y 1 E LYS -163 ? E LYS 154  
2296 1 Y 1 E GLY -162 ? E GLY 155  
2297 1 Y 1 E LYS -161 ? E LYS 156  
2298 1 Y 1 E SER -160 ? E SER 157  
2299 1 Y 1 E ALA -159 ? E ALA 158  
2300 1 Y 1 E LEU -158 ? E LEU 159  
2301 1 Y 1 E MET -157 ? E MET 160  
2302 1 Y 1 E PHE -156 ? E PHE 161  
2303 1 Y 1 E ASN -155 ? E ASN 162  
2304 1 Y 1 E LEU -154 ? E LEU 163  
2305 1 Y 1 E GLN -153 ? E GLN 164  
2306 1 Y 1 E GLU -152 ? E GLU 165  
2307 1 Y 1 E PRO -151 ? E PRO 166  
2308 1 Y 1 E TYR -150 ? E TYR 167  
2309 1 Y 1 E PHE -149 ? E PHE 168  
2310 1 Y 1 E THR -148 ? E THR 169  
2311 1 Y 1 E TRP -147 ? E TRP 170  
2312 1 Y 1 E PRO -146 ? E PRO 171  
2313 1 Y 1 E LEU -145 ? E LEU 172  
2314 1 Y 1 E ILE -144 ? E ILE 173  
2315 1 Y 1 E ALA -143 ? E ALA 174  
2316 1 Y 1 E ALA -142 ? E ALA 175  
2317 1 Y 1 E ASP -141 ? E ASP 176  
2318 1 Y 1 E GLY -140 ? E GLY 177  
2319 1 Y 1 E GLY -139 ? E GLY 178  
2320 1 Y 1 E TYR -138 ? E TYR 179  
2321 1 Y 1 E ALA -137 ? E ALA 180  
2322 1 Y 1 E PHE -136 ? E PHE 181  
2323 1 Y 1 E LYS -135 ? E LYS 182  
2324 1 Y 1 E TYR -134 ? E TYR 183  
2325 1 Y 1 E GLU -133 ? E GLU 184  
2326 1 Y 1 E ASN -132 ? E ASN 185  
2327 1 Y 1 E GLY -131 ? E GLY 186  
2328 1 Y 1 E LYS -130 ? E LYS 187  
2329 1 Y 1 E TYR -129 ? E TYR 188  
2330 1 Y 1 E ASP -128 ? E ASP 189  
2331 1 Y 1 E ILE -127 ? E ILE 190  
2332 1 Y 1 E LYS -126 ? E LYS 191  
2333 1 Y 1 E ASP -125 ? E ASP 192  
2334 1 Y 1 E VAL -124 ? E VAL 193  
2335 1 Y 1 E GLY -123 ? E GLY 194  
2336 1 Y 1 E VAL -122 ? E VAL 195  
2337 1 Y 1 E ASP -121 ? E ASP 196  
2338 1 Y 1 E ASN -120 ? E ASN 197  
2339 1 Y 1 E ALA -119 ? E ALA 198  
2340 1 Y 1 E GLY -118 ? E GLY 199  
2341 1 Y 1 E ALA -117 ? E ALA 200  
2342 1 Y 1 E LYS -116 ? E LYS 201  
2343 1 Y 1 E ALA -115 ? E ALA 202  
2344 1 Y 1 E GLY -114 ? E GLY 203  
2345 1 Y 1 E LEU -113 ? E LEU 204  
2346 1 Y 1 E THR -112 ? E THR 205  
2347 1 Y 1 E PHE -111 ? E PHE 206  
2348 1 Y 1 E LEU -110 ? E LEU 207  
2349 1 Y 1 E VAL -109 ? E VAL 208  
2350 1 Y 1 E ASP -108 ? E ASP 209  
2351 1 Y 1 E LEU -107 ? E LEU 210  
2352 1 Y 1 E ILE -106 ? E ILE 211  
2353 1 Y 1 E LYS -105 ? E LYS 212  
2354 1 Y 1 E ASN -104 ? E ASN 213  
2355 1 Y 1 E LYS -103 ? E LYS 214  
2356 1 Y 1 E HIS -102 ? E HIS 215  
2357 1 Y 1 E MET -101 ? E MET 216  
2358 1 Y 1 E ASN -100 ? E ASN 217  
2359 1 Y 1 E ALA -99  ? E ALA 218  
2360 1 Y 1 E ASP -98  ? E ASP 219  
2361 1 Y 1 E THR -97  ? E THR 220  
2362 1 Y 1 E ASP -96  ? E ASP 221  
2363 1 Y 1 E TYR -95  ? E TYR 222  
2364 1 Y 1 E SER -94  ? E SER 223  
2365 1 Y 1 E ILE -93  ? E ILE 224  
2366 1 Y 1 E ALA -92  ? E ALA 225  
2367 1 Y 1 E GLU -91  ? E GLU 226  
2368 1 Y 1 E ALA -90  ? E ALA 227  
2369 1 Y 1 E ALA -89  ? E ALA 228  
2370 1 Y 1 E PHE -88  ? E PHE 229  
2371 1 Y 1 E ASN -87  ? E ASN 230  
2372 1 Y 1 E LYS -86  ? E LYS 231  
2373 1 Y 1 E GLY -85  ? E GLY 232  
2374 1 Y 1 E GLU -84  ? E GLU 233  
2375 1 Y 1 E THR -83  ? E THR 234  
2376 1 Y 1 E ALA -82  ? E ALA 235  
2377 1 Y 1 E MET -81  ? E MET 236  
2378 1 Y 1 E THR -80  ? E THR 237  
2379 1 Y 1 E ILE -79  ? E ILE 238  
2380 1 Y 1 E ASN -78  ? E ASN 239  
2381 1 Y 1 E GLY -77  ? E GLY 240  
2382 1 Y 1 E PRO -76  ? E PRO 241  
2383 1 Y 1 E TRP -75  ? E TRP 242  
2384 1 Y 1 E ALA -74  ? E ALA 243  
2385 1 Y 1 E TRP -73  ? E TRP 244  
2386 1 Y 1 E SER -72  ? E SER 245  
2387 1 Y 1 E ASN -71  ? E ASN 246  
2388 1 Y 1 E ILE -70  ? E ILE 247  
2389 1 Y 1 E ASP -69  ? E ASP 248  
2390 1 Y 1 E THR -68  ? E THR 249  
2391 1 Y 1 E SER -67  ? E SER 250  
2392 1 Y 1 E LYS -66  ? E LYS 251  
2393 1 Y 1 E VAL -65  ? E VAL 252  
2394 1 Y 1 E ASN -64  ? E ASN 253  
2395 1 Y 1 E TYR -63  ? E TYR 254  
2396 1 Y 1 E GLY -62  ? E GLY 255  
2397 1 Y 1 E VAL -61  ? E VAL 256  
2398 1 Y 1 E THR -60  ? E THR 257  
2399 1 Y 1 E VAL -59  ? E VAL 258  
2400 1 Y 1 E LEU -58  ? E LEU 259  
2401 1 Y 1 E PRO -57  ? E PRO 260  
2402 1 Y 1 E THR -56  ? E THR 261  
2403 1 Y 1 E PHE -55  ? E PHE 262  
2404 1 Y 1 E LYS -54  ? E LYS 263  
2405 1 Y 1 E GLY -53  ? E GLY 264  
2406 1 Y 1 E GLN -52  ? E GLN 265  
2407 1 Y 1 E PRO -51  ? E PRO 266  
2408 1 Y 1 E SER -50  ? E SER 267  
2409 1 Y 1 E LYS -49  ? E LYS 268  
2410 1 Y 1 E PRO -48  ? E PRO 269  
2411 1 Y 1 E PHE -47  ? E PHE 270  
2412 1 Y 1 E VAL -46  ? E VAL 271  
2413 1 Y 1 E GLY -45  ? E GLY 272  
2414 1 Y 1 E VAL -44  ? E VAL 273  
2415 1 Y 1 E LEU -43  ? E LEU 274  
2416 1 Y 1 E SER -42  ? E SER 275  
2417 1 Y 1 E ALA -41  ? E ALA 276  
2418 1 Y 1 E GLY -40  ? E GLY 277  
2419 1 Y 1 E ILE -39  ? E ILE 278  
2420 1 Y 1 E ASN -38  ? E ASN 279  
2421 1 Y 1 E ALA -37  ? E ALA 280  
2422 1 Y 1 E ALA -36  ? E ALA 281  
2423 1 Y 1 E SER -35  ? E SER 282  
2424 1 Y 1 E PRO -34  ? E PRO 283  
2425 1 Y 1 E ASN -33  ? E ASN 284  
2426 1 Y 1 E LYS -32  ? E LYS 285  
2427 1 Y 1 E GLU -31  ? E GLU 286  
2428 1 Y 1 E LEU -30  ? E LEU 287  
2429 1 Y 1 E ALA -29  ? E ALA 288  
2430 1 Y 1 E LYS -28  ? E LYS 289  
2431 1 Y 1 E GLU -27  ? E GLU 290  
2432 1 Y 1 E PHE -26  ? E PHE 291  
2433 1 Y 1 E LEU -25  ? E LEU 292  
2434 1 Y 1 E GLU -24  ? E GLU 293  
2435 1 Y 1 E ASN -23  ? E ASN 294  
2436 1 Y 1 E TYR -22  ? E TYR 295  
2437 1 Y 1 E LEU -21  ? E LEU 296  
2438 1 Y 1 E LEU -20  ? E LEU 297  
2439 1 Y 1 E THR -19  ? E THR 298  
2440 1 Y 1 E ASP -18  ? E ASP 299  
2441 1 Y 1 E GLU -17  ? E GLU 300  
2442 1 Y 1 E GLY -16  ? E GLY 301  
2443 1 Y 1 E LEU -15  ? E LEU 302  
2444 1 Y 1 E GLU -14  ? E GLU 303  
2445 1 Y 1 E ALA -13  ? E ALA 304  
2446 1 Y 1 E VAL -12  ? E VAL 305  
2447 1 Y 1 E ASN -11  ? E ASN 306  
2448 1 Y 1 E LYS -10  ? E LYS 307  
2449 1 Y 1 E ASP -9   ? E ASP 308  
2450 1 Y 1 E LYS -8   ? E LYS 309  
2451 1 Y 1 E PRO -7   ? E PRO 310  
2452 1 Y 1 E LEU -6   ? E LEU 311  
2453 1 Y 1 E GLY -5   ? E GLY 312  
2454 1 Y 1 E ALA -4   ? E ALA 313  
2455 1 Y 1 E VAL -3   ? E VAL 314  
2456 1 Y 1 E ALA -2   ? E ALA 315  
2457 1 Y 1 E LEU -1   ? E LEU 316  
2458 1 Y 1 E LYS 0    ? E LYS 317  
2459 1 Y 1 E SER 1    ? E SER 318  
2460 1 Y 1 E TYR 2    ? E TYR 319  
2461 1 Y 1 E GLU 3    ? E GLU 320  
2462 1 Y 1 E GLU 4    ? E GLU 321  
2463 1 Y 1 E GLU 5    ? E GLU 322  
2464 1 Y 1 E LEU 6    ? E LEU 323  
2465 1 Y 1 E ALA 7    ? E ALA 324  
2466 1 Y 1 E LYS 8    ? E LYS 325  
2467 1 Y 1 E ASP 9    ? E ASP 326  
2468 1 Y 1 E PRO 10   ? E PRO 327  
2469 1 Y 1 E ARG 11   ? E ARG 328  
2470 1 Y 1 E ILE 12   ? E ILE 329  
2471 1 Y 1 E ALA 13   ? E ALA 330  
2472 1 Y 1 E ALA 14   ? E ALA 331  
2473 1 Y 1 E THR 15   ? E THR 332  
2474 1 Y 1 E MET 16   ? E MET 333  
2475 1 Y 1 E GLU 17   ? E GLU 334  
2476 1 Y 1 E ASN 18   ? E ASN 335  
2477 1 Y 1 E ALA 19   ? E ALA 336  
2478 1 Y 1 E GLN 20   ? E GLN 337  
2479 1 Y 1 E LYS 21   ? E LYS 338  
2480 1 Y 1 E GLY 22   ? E GLY 339  
2481 1 Y 1 E GLU 23   ? E GLU 340  
2482 1 Y 1 E ILE 24   ? E ILE 341  
2483 1 Y 1 E MET 25   ? E MET 342  
2484 1 Y 1 E PRO 26   ? E PRO 343  
2485 1 Y 1 E ASN 27   ? E ASN 344  
2486 1 Y 1 E ILE 28   ? E ILE 345  
2487 1 Y 1 E PRO 29   ? E PRO 346  
2488 1 Y 1 E GLN 30   ? E GLN 347  
2489 1 Y 1 E MET 31   ? E MET 348  
2490 1 Y 1 E SER 32   ? E SER 349  
2491 1 Y 1 E ALA 33   ? E ALA 350  
2492 1 Y 1 E PHE 34   ? E PHE 351  
2493 1 Y 1 E TRP 35   ? E TRP 352  
2494 1 Y 1 E TYR 36   ? E TYR 353  
2495 1 Y 1 E ALA 37   ? E ALA 354  
2496 1 Y 1 E VAL 38   ? E VAL 355  
2497 1 Y 1 E ARG 39   ? E ARG 356  
2498 1 Y 1 E THR 40   ? E THR 357  
2499 1 Y 1 E ALA 41   ? E ALA 358  
2500 1 Y 1 E VAL 42   ? E VAL 359  
2501 1 Y 1 E ILE 43   ? E ILE 360  
2502 1 Y 1 E ASN 44   ? E ASN 361  
2503 1 Y 1 E ALA 45   ? E ALA 362  
2504 1 Y 1 E ALA 46   ? E ALA 363  
2505 1 Y 1 E SER 47   ? E SER 364  
2506 1 Y 1 E GLY 48   ? E GLY 365  
2507 1 Y 1 E ARG 49   ? E ARG 366  
2508 1 Y 1 E GLN 50   ? E GLN 367  
2509 1 Y 1 E THR 51   ? E THR 368  
2510 1 Y 1 E VAL 52   ? E VAL 369  
2511 1 Y 1 E ASP 53   ? E ASP 370  
2512 1 Y 1 E GLU 54   ? E GLU 371  
2513 1 Y 1 E ALA 55   ? E ALA 372  
2514 1 Y 1 E LEU 56   ? E LEU 373  
2515 1 Y 1 E LYS 57   ? E LYS 374  
2516 1 Y 1 E ASP 58   ? E ASP 375  
2517 1 Y 1 E ALA 59   ? E ALA 376  
2518 1 Y 1 E GLN 60   ? E GLN 377  
2519 1 Y 1 E THR 61   ? E THR 378  
2520 1 Y 1 E GLY 62   ? E GLY 379  
2521 1 Y 1 E THR 63   ? E THR 380  
2522 1 Y 1 E ASP 64   ? E ASP 381  
2523 1 Y 1 E TYR 65   ? E TYR 382  
2524 1 Y 1 E ASP 66   ? E ASP 383  
2525 1 Y 1 E ILE 67   ? E ILE 384  
2526 1 Y 1 E PRO 68   ? E PRO 385  
2527 1 Y 1 E THR 69   ? E THR 386  
2528 1 Y 1 E THR 70   ? E THR 387  
2529 1 Y 1 E GLU 71   ? E GLU 388  
2530 1 Y 1 E ASN 72   ? E ASN 389  
2531 1 Y 1 E LEU 73   ? E LEU 390  
2532 1 Y 1 E TYR 74   ? E TYR 391  
2533 1 Y 1 E PHE 75   ? E PHE 392  
2534 1 Y 1 E GLN 76   ? E GLN 393  
2535 1 Y 1 E GLY 77   ? E GLY 394  
2536 1 Y 1 E GLY 78   ? E GLY 395  
2537 1 Y 1 E SER 79   ? E SER 396  
2538 1 Y 1 E ASN 80   ? E ASN 397  
2539 1 Y 1 E HIS 81   ? E HIS 398  
2540 1 Y 1 E SER 82   ? E SER 399  
2541 1 Y 1 E PHE 83   ? E PHE 400  
2542 1 Y 1 E GLU 84   ? E GLU 401  
2543 1 Y 1 E GLU 85   ? E GLU 402  
2544 1 Y 1 E VAL 86   ? E VAL 403  
2545 1 Y 1 E VAL 87   ? E VAL 404  
2546 1 Y 1 E GLN 88   ? E GLN 405  
2547 1 Y 1 E THR 89   ? E THR 406  
2548 1 Y 1 E LEU 90   ? E LEU 407  
2549 1 Y 1 E ALA 91   ? E ALA 408  
2550 1 Y 1 E SER 92   ? E SER 409  
2551 1 Y 1 E LEU 93   ? E LEU 410  
2552 1 Y 1 E ALA 94   ? E ALA 411  
2553 1 Y 1 E THR 95   ? E THR 412  
2554 1 Y 1 E VAL 96   ? E VAL 413  
2555 1 Y 1 E VAL 97   ? E VAL 414  
2556 1 Y 1 E GLN 98   ? E GLN 415  
2557 1 Y 1 E GLN 99   ? E GLN 416  
2558 1 Y 1 E GLN 100  ? E GLN 417  
2559 1 Y 1 E THR 101  ? E THR 418  
2560 1 Y 1 E ILE 102  ? E ILE 419  
2561 1 Y 1 E ALA 103  ? E ALA 420  
2562 1 Y 1 E SER 104  ? E SER 421  
2563 1 Y 1 E GLU 105  ? E GLU 422  
2564 1 Y 1 E SER 106  ? E SER 423  
2565 1 Y 1 E LEU 107  ? E LEU 424  
2566 1 Y 1 E GLU 108  ? E GLU 425  
2567 1 Y 1 E GLN 109  ? E GLN 426  
2568 1 Y 1 E ARG 110  ? E ARG 427  
2569 1 Y 1 E ILE 111  ? E ILE 428  
2570 1 Y 1 E THR 112  ? E THR 429  
2571 1 Y 1 E SER 113  ? E SER 430  
2572 1 Y 1 E LEU 114  ? E LEU 431  
2573 1 Y 1 E GLU 115  ? E GLU 432  
2574 1 Y 1 E ASN 116  ? E ASN 433  
2575 1 Y 1 E GLY 117  ? E GLY 434  
2576 1 Y 1 E LEU 118  ? E LEU 435  
2577 1 Y 1 E LYS 119  ? E LYS 436  
2578 1 Y 1 E PRO 120  ? E PRO 437  
2579 1 Y 1 E VAL 121  ? E VAL 438  
2580 1 Y 1 E TYR 122  ? E TYR 439  
2581 1 Y 1 E MET 147  ? E MET 464  
2582 1 Y 1 E THR 148  ? E THR 465  
2583 1 Y 1 E THR 149  ? E THR 466  
2584 1 Y 1 E GLY 150  ? E GLY 467  
2585 1 Y 1 E ARG 151  ? E ARG 468  
2586 1 Y 1 E ALA 152  ? E ALA 469  
2587 1 Y 1 E THR 153  ? E THR 470  
2588 1 Y 1 E ALA 154  ? E ALA 471  
2589 1 Y 1 E THR 155  ? E THR 472  
2590 1 Y 1 E ALA 156  ? E ALA 473  
2591 1 Y 1 E ALA 157  ? E ALA 474  
2592 1 Y 1 E ALA 158  ? E ALA 475  
2593 1 Y 1 E THR 159  ? E THR 476  
2594 1 Y 1 E GLU 160  ? E GLU 477  
2595 1 Y 1 E ALA 161  ? E ALA 478  
2596 1 Y 1 E TYR 162  ? E TYR 479  
2597 1 Y 1 E TRP 163  ? E TRP 480  
2598 1 Y 1 E ALA 164  ? E ALA 481  
2599 1 Y 1 E GLU 165  ? E GLU 482  
2600 1 Y 1 E HIS 166  ? E HIS 483  
2601 1 Y 1 E GLY 167  ? E GLY 484  
2602 1 Y 1 E GLN 168  ? E GLN 485  
2603 1 Y 1 E PRO 169  ? E PRO 486  
2604 1 Y 1 E PRO 170  ? E PRO 487  
2605 1 Y 1 E PRO 171  ? E PRO 488  
2606 1 Y 1 E GLY 172  ? E GLY 489  
2607 1 Y 1 E PRO 173  ? E PRO 490  
2608 1 Y 1 E SER 174  ? E SER 491  
2609 1 Y 1 E LEU 175  ? E LEU 492  
2610 1 Y 1 E TYR 176  ? E TYR 493  
2611 1 Y 1 E GLU 177  ? E GLU 494  
2612 1 Y 1 E GLU 178  ? E GLU 495  
2613 1 Y 1 E SER 179  ? E SER 496  
2614 1 Y 1 E ALA 180  ? E ALA 497  
2615 1 Y 1 E ILE 181  ? E ILE 498  
2616 1 Y 1 E ARG 182  ? E ARG 499  
2617 1 Y 1 E GLY 183  ? E GLY 500  
2618 1 Y 1 E LYS 184  ? E LYS 501  
2619 1 Y 1 E ILE 185  ? E ILE 502  
2620 1 Y 1 E GLU 186  ? E GLU 503  
2621 1 Y 1 E SER 187  ? E SER 504  
2622 1 Y 1 E ARG 188  ? E ARG 505  
2623 1 Y 1 E ASP 189  ? E ASP 506  
2624 1 Y 1 E GLU 190  ? E GLU 507  
2625 1 Y 1 E THR 191  ? E THR 508  
2626 1 Y 1 E VAL 192  ? E VAL 509  
2627 1 Y 1 E PRO 193  ? E PRO 510  
2628 1 Y 1 E GLN 194  ? E GLN 511  
2629 1 Y 1 E SER 195  ? E SER 512  
2630 1 Y 1 E VAL 196  ? E VAL 513  
2631 1 Y 1 E ARG 197  ? E ARG 514  
2632 1 Y 1 E GLU 198  ? E GLU 515  
2633 1 Y 1 E ALA 199  ? E ALA 516  
2634 1 Y 1 E PHE 200  ? E PHE 517  
2635 1 Y 1 E ASN 201  ? E ASN 518  
2636 1 Y 1 E ASN 202  ? E ASN 519  
2637 1 Y 1 E LEU 203  ? E LEU 520  
2638 1 Y 1 E ASN 204  ? E ASN 521  
2639 1 Y 1 E SER 205  ? E SER 522  
2640 1 Y 1 E THR 206  ? E THR 523  
2641 1 Y 1 E THR 207  ? E THR 524  
2642 1 Y 1 E SER 208  ? E SER 525  
2643 1 Y 1 E LEU 209  ? E LEU 526  
2644 1 Y 1 E THR 210  ? E THR 527  
2645 1 Y 1 E GLU 211  ? E GLU 528  
2646 1 Y 1 E GLU 212  ? E GLU 529  
2647 1 Y 1 E ASN 213  ? E ASN 530  
2648 1 Y 1 E PHE 214  ? E PHE 531  
2649 1 Y 1 E GLY 215  ? E GLY 532  
2650 1 Y 1 E LYS 216  ? E LYS 533  
2651 1 Y 1 E PRO 217  ? E PRO 534  
2652 1 Y 1 E ASP 218  ? E ASP 535  
2653 1 Y 1 E ILE 219  ? E ILE 536  
2654 1 Y 1 E SER 220  ? E SER 537  
2655 1 Y 1 E ALA 221  ? E ALA 538  
2656 1 Y 1 E LYS 222  ? E LYS 539  
2657 1 Y 1 E ASP 223  ? E ASP 540  
2658 1 Y 1 E LEU 224  ? E LEU 541  
2659 1 Y 1 E ARG 225  ? E ARG 542  
2660 1 Y 1 E ASN 226  ? E ASN 543  
2661 1 Y 1 E ILE 227  ? E ILE 544  
2662 1 Y 1 E MET 228  ? E MET 545  
2663 1 Y 1 E TYR 229  ? E TYR 546  
2664 1 Y 1 E ASP 230  ? E ASP 547  
2665 1 Y 1 E HIS 231  ? E HIS 548  
2666 1 Y 1 E LEU 232  ? E LEU 549  
2667 1 Y 1 E PRO 233  ? E PRO 550  
2668 1 Y 1 E GLY 234  ? E GLY 551  
2669 1 Y 1 E PHE 235  ? E PHE 552  
2670 1 Y 1 E GLY 236  ? E GLY 553  
2671 1 Y 1 E THR 237  ? E THR 554  
2672 1 Y 1 E ALA 238  ? E ALA 555  
2673 1 Y 1 E PHE 239  ? E PHE 556  
2674 1 Y 1 E HIS 240  ? E HIS 557  
2675 1 Y 1 E GLN 241  ? E GLN 558  
2676 1 Y 1 E LEU 242  ? E LEU 559  
2677 1 Y 1 E VAL 243  ? E VAL 560  
2678 1 Y 1 E GLN 244  ? E GLN 561  
2679 1 Y 1 E VAL 245  ? E VAL 562  
2680 1 Y 1 E ILE 246  ? E ILE 563  
2681 1 Y 1 E CYS 247  ? E CYS 564  
2682 1 Y 1 E LYS 248  ? E LYS 565  
2683 1 Y 1 E LEU 249  ? E LEU 566  
2684 1 Y 1 E GLY 250  ? E GLY 567  
2685 1 Y 1 E LYS 251  ? E LYS 568  
2686 1 Y 1 E ASP 252  ? E ASP 569  
2687 1 Y 1 E SER 253  ? E SER 570  
2688 1 Y 1 E ASN 254  ? E ASN 571  
2689 1 Y 1 E SER 255  ? E SER 572  
2690 1 Y 1 E LEU 256  ? E LEU 573  
2691 1 Y 1 E ASP 257  ? E ASP 574  
2692 1 Y 1 E ILE 258  ? E ILE 575  
2693 1 Y 1 E ILE 259  ? E ILE 576  
2694 1 Y 1 E HIS 260  ? E HIS 577  
2695 1 Y 1 E ALA 261  ? E ALA 578  
2696 1 Y 1 E GLU 262  ? E GLU 579  
2697 1 Y 1 E PHE 263  ? E PHE 580  
2698 1 Y 1 E GLN 264  ? E GLN 581  
2699 1 Y 1 E ALA 265  ? E ALA 582  
2700 1 Y 1 E SER 266  ? E SER 583  
2701 1 Y 1 E LEU 267  ? E LEU 584  
2702 1 Y 1 E ALA 268  ? E ALA 585  
2703 1 Y 1 E GLU 269  ? E GLU 586  
2704 1 Y 1 E GLY 270  ? E GLY 587  
2705 1 Y 1 E ASP 271  ? E ASP 588  
2706 1 Y 1 E SER 272  ? E SER 589  
2707 1 Y 1 E PRO 273  ? E PRO 590  
2708 1 Y 1 E GLN 274  ? E GLN 591  
2709 1 Y 1 E CYS 275  ? E CYS 592  
2710 1 Y 1 E ALA 276  ? E ALA 593  
2711 1 Y 1 E LEU 277  ? E LEU 594  
2712 1 Y 1 E ILE 278  ? E ILE 595  
2713 1 Y 1 E GLN 279  ? E GLN 596  
2714 1 Y 1 E ILE 280  ? E ILE 597  
2715 1 Y 1 E THR 281  ? E THR 598  
2716 1 Y 1 E LYS 282  ? E LYS 599  
2717 1 Y 1 E ARG 283  ? E ARG 600  
2718 1 Y 1 E VAL 284  ? E VAL 601  
2719 1 Y 1 E PRO 285  ? E PRO 602  
2720 1 Y 1 E ILE 286  ? E ILE 603  
2721 1 Y 1 E PHE 287  ? E PHE 604  
2722 1 Y 1 E GLN 288  ? E GLN 605  
2723 1 Y 1 E ASP 289  ? E ASP 606  
2724 1 Y 1 E ALA 290  ? E ALA 607  
2725 1 Y 1 E ALA 291  ? E ALA 608  
2726 1 Y 1 E PRO 292  ? E PRO 609  
2727 1 Y 1 E PRO 293  ? E PRO 610  
2728 1 Y 1 E VAL 294  ? E VAL 611  
2729 1 Y 1 E ILE 295  ? E ILE 612  
2730 1 Y 1 E HIS 296  ? E HIS 613  
2731 1 Y 1 E ILE 297  ? E ILE 614  
2732 1 Y 1 E ARG 298  ? E ARG 615  
2733 1 Y 1 E SER 299  ? E SER 616  
2734 1 Y 1 E ARG 300  ? E ARG 617  
2735 1 Y 1 E GLY 301  ? E GLY 618  
2736 1 Y 1 E ASP 302  ? E ASP 619  
2737 1 Y 1 E ILE 303  ? E ILE 620  
2738 1 Y 1 E PRO 304  ? E PRO 621  
2739 1 Y 1 E ARG 305  ? E ARG 622  
2740 1 Y 1 E ALA 306  ? E ALA 623  
2741 1 Y 1 E CYS 307  ? E CYS 624  
2742 1 Y 1 E GLN 308  ? E GLN 625  
2743 1 Y 1 E LYS 309  ? E LYS 626  
2744 1 Y 1 E SER 310  ? E SER 627  
2745 1 Y 1 E LEU 311  ? E LEU 628  
2746 1 Y 1 E ARG 312  ? E ARG 629  
2747 1 Y 1 E PRO 313  ? E PRO 630  
2748 1 Y 1 E VAL 314  ? E VAL 631  
2749 1 Y 1 E PRO 315  ? E PRO 632  
2750 1 Y 1 E PRO 316  ? E PRO 633  
2751 1 Y 1 E SER 317  ? E SER 634  
2752 1 Y 1 E PRO 318  ? E PRO 635  
2753 1 Y 1 E LYS 319  ? E LYS 636  
2754 1 Y 1 E ILE 320  ? E ILE 637  
2755 1 Y 1 E ASP 321  ? E ASP 638  
2756 1 Y 1 E ARG 322  ? E ARG 639  
2757 1 Y 1 E GLY 323  ? E GLY 640  
2758 1 Y 1 E TRP 324  ? E TRP 641  
2759 1 Y 1 E VAL 325  ? E VAL 642  
2760 1 Y 1 E CYS 326  ? E CYS 643  
2761 1 Y 1 E VAL 327  ? E VAL 644  
2762 1 Y 1 E PHE 328  ? E PHE 645  
2763 1 Y 1 E GLN 329  ? E GLN 646  
2764 1 Y 1 E LEU 330  ? E LEU 647  
2765 1 Y 1 E GLN 331  ? E GLN 648  
2766 1 Y 1 E ASP 332  ? E ASP 649  
2767 1 Y 1 E GLY 333  ? E GLY 650  
2768 1 Y 1 E LYS 334  ? E LYS 651  
2769 1 Y 1 E THR 335  ? E THR 652  
2770 1 Y 1 E LEU 336  ? E LEU 653  
2771 1 Y 1 E GLY 337  ? E GLY 654  
2772 1 Y 1 E LEU 338  ? E LEU 655  
2773 1 Y 1 E LYS 339  ? E LYS 656  
2774 1 Y 1 E ILE 340  ? E ILE 657  
# 
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  
CYS N    N  N N 74  
CYS CA   C  N R 75  
CYS C    C  N N 76  
CYS O    O  N N 77  
CYS CB   C  N N 78  
CYS SG   S  N N 79  
CYS OXT  O  N N 80  
CYS H    H  N N 81  
CYS H2   H  N N 82  
CYS HA   H  N N 83  
CYS HB2  H  N N 84  
CYS HB3  H  N N 85  
CYS HG   H  N N 86  
CYS HXT  H  N N 87  
GLN N    N  N N 88  
GLN CA   C  N S 89  
GLN C    C  N N 90  
GLN O    O  N N 91  
GLN CB   C  N N 92  
GLN CG   C  N N 93  
GLN CD   C  N N 94  
GLN OE1  O  N N 95  
GLN NE2  N  N N 96  
GLN OXT  O  N N 97  
GLN H    H  N N 98  
GLN H2   H  N N 99  
GLN HA   H  N N 100 
GLN HB2  H  N N 101 
GLN HB3  H  N N 102 
GLN HG2  H  N N 103 
GLN HG3  H  N N 104 
GLN HE21 H  N N 105 
GLN HE22 H  N N 106 
GLN HXT  H  N N 107 
GLU N    N  N N 108 
GLU CA   C  N S 109 
GLU C    C  N N 110 
GLU O    O  N N 111 
GLU CB   C  N N 112 
GLU CG   C  N N 113 
GLU CD   C  N N 114 
GLU OE1  O  N N 115 
GLU OE2  O  N N 116 
GLU OXT  O  N N 117 
GLU H    H  N N 118 
GLU H2   H  N N 119 
GLU HA   H  N N 120 
GLU HB2  H  N N 121 
GLU HB3  H  N N 122 
GLU HG2  H  N N 123 
GLU HG3  H  N N 124 
GLU HE2  H  N N 125 
GLU HXT  H  N N 126 
GLY N    N  N N 127 
GLY CA   C  N N 128 
GLY C    C  N N 129 
GLY O    O  N N 130 
GLY OXT  O  N N 131 
GLY H    H  N N 132 
GLY H2   H  N N 133 
GLY HA2  H  N N 134 
GLY HA3  H  N N 135 
GLY HXT  H  N N 136 
HIS N    N  N N 137 
HIS CA   C  N S 138 
HIS C    C  N N 139 
HIS O    O  N N 140 
HIS CB   C  N N 141 
HIS CG   C  Y N 142 
HIS ND1  N  Y N 143 
HIS CD2  C  Y N 144 
HIS CE1  C  Y N 145 
HIS NE2  N  Y N 146 
HIS OXT  O  N N 147 
HIS H    H  N N 148 
HIS H2   H  N N 149 
HIS HA   H  N N 150 
HIS HB2  H  N N 151 
HIS HB3  H  N N 152 
HIS HD1  H  N N 153 
HIS HD2  H  N N 154 
HIS HE1  H  N N 155 
HIS HE2  H  N N 156 
HIS HXT  H  N N 157 
ILE N    N  N N 158 
ILE CA   C  N S 159 
ILE C    C  N N 160 
ILE O    O  N N 161 
ILE CB   C  N S 162 
ILE CG1  C  N N 163 
ILE CG2  C  N N 164 
ILE CD1  C  N N 165 
ILE OXT  O  N N 166 
ILE H    H  N N 167 
ILE H2   H  N N 168 
ILE HA   H  N N 169 
ILE HB   H  N N 170 
ILE HG12 H  N N 171 
ILE HG13 H  N N 172 
ILE HG21 H  N N 173 
ILE HG22 H  N N 174 
ILE HG23 H  N N 175 
ILE HD11 H  N N 176 
ILE HD12 H  N N 177 
ILE HD13 H  N N 178 
ILE HXT  H  N N 179 
LEU N    N  N N 180 
LEU CA   C  N S 181 
LEU C    C  N N 182 
LEU O    O  N N 183 
LEU CB   C  N N 184 
LEU CG   C  N N 185 
LEU CD1  C  N N 186 
LEU CD2  C  N N 187 
LEU OXT  O  N N 188 
LEU H    H  N N 189 
LEU H2   H  N N 190 
LEU HA   H  N N 191 
LEU HB2  H  N N 192 
LEU HB3  H  N N 193 
LEU HG   H  N N 194 
LEU HD11 H  N N 195 
LEU HD12 H  N N 196 
LEU HD13 H  N N 197 
LEU HD21 H  N N 198 
LEU HD22 H  N N 199 
LEU HD23 H  N N 200 
LEU HXT  H  N N 201 
LYS N    N  N N 202 
LYS CA   C  N S 203 
LYS C    C  N N 204 
LYS O    O  N N 205 
LYS CB   C  N N 206 
LYS CG   C  N N 207 
LYS CD   C  N N 208 
LYS CE   C  N N 209 
LYS NZ   N  N N 210 
LYS OXT  O  N N 211 
LYS H    H  N N 212 
LYS H2   H  N N 213 
LYS HA   H  N N 214 
LYS HB2  H  N N 215 
LYS HB3  H  N N 216 
LYS HG2  H  N N 217 
LYS HG3  H  N N 218 
LYS HD2  H  N N 219 
LYS HD3  H  N N 220 
LYS HE2  H  N N 221 
LYS HE3  H  N N 222 
LYS HZ1  H  N N 223 
LYS HZ2  H  N N 224 
LYS HZ3  H  N N 225 
LYS HXT  H  N N 226 
MET N    N  N N 227 
MET CA   C  N S 228 
MET C    C  N N 229 
MET O    O  N N 230 
MET CB   C  N N 231 
MET CG   C  N N 232 
MET SD   S  N N 233 
MET CE   C  N N 234 
MET OXT  O  N N 235 
MET H    H  N N 236 
MET H2   H  N N 237 
MET HA   H  N N 238 
MET HB2  H  N N 239 
MET HB3  H  N N 240 
MET HG2  H  N N 241 
MET HG3  H  N N 242 
MET HE1  H  N N 243 
MET HE2  H  N N 244 
MET HE3  H  N N 245 
MET HXT  H  N N 246 
PHE N    N  N N 247 
PHE CA   C  N S 248 
PHE C    C  N N 249 
PHE O    O  N N 250 
PHE CB   C  N N 251 
PHE CG   C  Y N 252 
PHE CD1  C  Y N 253 
PHE CD2  C  Y N 254 
PHE CE1  C  Y N 255 
PHE CE2  C  Y N 256 
PHE CZ   C  Y N 257 
PHE OXT  O  N N 258 
PHE H    H  N N 259 
PHE H2   H  N N 260 
PHE HA   H  N N 261 
PHE HB2  H  N N 262 
PHE HB3  H  N N 263 
PHE HD1  H  N N 264 
PHE HD2  H  N N 265 
PHE HE1  H  N N 266 
PHE HE2  H  N N 267 
PHE HZ   H  N N 268 
PHE HXT  H  N N 269 
PRO N    N  N N 270 
PRO CA   C  N S 271 
PRO C    C  N N 272 
PRO O    O  N N 273 
PRO CB   C  N N 274 
PRO CG   C  N N 275 
PRO CD   C  N N 276 
PRO OXT  O  N N 277 
PRO H    H  N N 278 
PRO HA   H  N N 279 
PRO HB2  H  N N 280 
PRO HB3  H  N N 281 
PRO HG2  H  N N 282 
PRO HG3  H  N N 283 
PRO HD2  H  N N 284 
PRO HD3  H  N N 285 
PRO HXT  H  N N 286 
SER N    N  N N 287 
SER CA   C  N S 288 
SER C    C  N N 289 
SER O    O  N N 290 
SER CB   C  N N 291 
SER OG   O  N N 292 
SER OXT  O  N N 293 
SER H    H  N N 294 
SER H2   H  N N 295 
SER HA   H  N N 296 
SER HB2  H  N N 297 
SER HB3  H  N N 298 
SER HG   H  N N 299 
SER HXT  H  N N 300 
THR N    N  N N 301 
THR CA   C  N S 302 
THR C    C  N N 303 
THR O    O  N N 304 
THR CB   C  N R 305 
THR OG1  O  N N 306 
THR CG2  C  N N 307 
THR OXT  O  N N 308 
THR H    H  N N 309 
THR H2   H  N N 310 
THR HA   H  N N 311 
THR HB   H  N N 312 
THR HG1  H  N N 313 
THR HG21 H  N N 314 
THR HG22 H  N N 315 
THR HG23 H  N N 316 
THR HXT  H  N N 317 
TRP N    N  N N 318 
TRP CA   C  N S 319 
TRP C    C  N N 320 
TRP O    O  N N 321 
TRP CB   C  N N 322 
TRP CG   C  Y N 323 
TRP CD1  C  Y N 324 
TRP CD2  C  Y N 325 
TRP NE1  N  Y N 326 
TRP CE2  C  Y N 327 
TRP CE3  C  Y N 328 
TRP CZ2  C  Y N 329 
TRP CZ3  C  Y N 330 
TRP CH2  C  Y N 331 
TRP OXT  O  N N 332 
TRP H    H  N N 333 
TRP H2   H  N N 334 
TRP HA   H  N N 335 
TRP HB2  H  N N 336 
TRP HB3  H  N N 337 
TRP HD1  H  N N 338 
TRP HE1  H  N N 339 
TRP HE3  H  N N 340 
TRP HZ2  H  N N 341 
TRP HZ3  H  N N 342 
TRP HH2  H  N N 343 
TRP HXT  H  N N 344 
TYR N    N  N N 345 
TYR CA   C  N S 346 
TYR C    C  N N 347 
TYR O    O  N N 348 
TYR CB   C  N N 349 
TYR CG   C  Y N 350 
TYR CD1  C  Y N 351 
TYR CD2  C  Y N 352 
TYR CE1  C  Y N 353 
TYR CE2  C  Y N 354 
TYR CZ   C  Y N 355 
TYR OH   O  N N 356 
TYR OXT  O  N N 357 
TYR H    H  N N 358 
TYR H2   H  N N 359 
TYR HA   H  N N 360 
TYR HB2  H  N N 361 
TYR HB3  H  N N 362 
TYR HD1  H  N N 363 
TYR HD2  H  N N 364 
TYR HE1  H  N N 365 
TYR HE2  H  N N 366 
TYR HH   H  N N 367 
TYR HXT  H  N N 368 
VAL N    N  N N 369 
VAL CA   C  N S 370 
VAL C    C  N N 371 
VAL O    O  N N 372 
VAL CB   C  N N 373 
VAL CG1  C  N N 374 
VAL CG2  C  N N 375 
VAL OXT  O  N N 376 
VAL H    H  N N 377 
VAL H2   H  N N 378 
VAL HA   H  N N 379 
VAL HB   H  N N 380 
VAL HG11 H  N N 381 
VAL HG12 H  N N 382 
VAL HG13 H  N N 383 
VAL HG21 H  N N 384 
VAL HG22 H  N N 385 
VAL HG23 H  N N 386 
VAL HXT  H  N N 387 
ZN  ZN   ZN N N 388 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
ILE N   CA   sing N N 150 
ILE N   H    sing N N 151 
ILE N   H2   sing N N 152 
ILE CA  C    sing N N 153 
ILE CA  CB   sing N N 154 
ILE CA  HA   sing N N 155 
ILE C   O    doub N N 156 
ILE C   OXT  sing N N 157 
ILE CB  CG1  sing N N 158 
ILE CB  CG2  sing N N 159 
ILE CB  HB   sing N N 160 
ILE CG1 CD1  sing N N 161 
ILE CG1 HG12 sing N N 162 
ILE CG1 HG13 sing N N 163 
ILE CG2 HG21 sing N N 164 
ILE CG2 HG22 sing N N 165 
ILE CG2 HG23 sing N N 166 
ILE CD1 HD11 sing N N 167 
ILE CD1 HD12 sing N N 168 
ILE CD1 HD13 sing N N 169 
ILE OXT HXT  sing N N 170 
LEU N   CA   sing N N 171 
LEU N   H    sing N N 172 
LEU N   H2   sing N N 173 
LEU CA  C    sing N N 174 
LEU CA  CB   sing N N 175 
LEU CA  HA   sing N N 176 
LEU C   O    doub N N 177 
LEU C   OXT  sing N N 178 
LEU CB  CG   sing N N 179 
LEU CB  HB2  sing N N 180 
LEU CB  HB3  sing N N 181 
LEU CG  CD1  sing N N 182 
LEU CG  CD2  sing N N 183 
LEU CG  HG   sing N N 184 
LEU CD1 HD11 sing N N 185 
LEU CD1 HD12 sing N N 186 
LEU CD1 HD13 sing N N 187 
LEU CD2 HD21 sing N N 188 
LEU CD2 HD22 sing N N 189 
LEU CD2 HD23 sing N N 190 
LEU OXT HXT  sing N N 191 
LYS N   CA   sing N N 192 
LYS N   H    sing N N 193 
LYS N   H2   sing N N 194 
LYS CA  C    sing N N 195 
LYS CA  CB   sing N N 196 
LYS CA  HA   sing N N 197 
LYS C   O    doub N N 198 
LYS C   OXT  sing N N 199 
LYS CB  CG   sing N N 200 
LYS CB  HB2  sing N N 201 
LYS CB  HB3  sing N N 202 
LYS CG  CD   sing N N 203 
LYS CG  HG2  sing N N 204 
LYS CG  HG3  sing N N 205 
LYS CD  CE   sing N N 206 
LYS CD  HD2  sing N N 207 
LYS CD  HD3  sing N N 208 
LYS CE  NZ   sing N N 209 
LYS CE  HE2  sing N N 210 
LYS CE  HE3  sing N N 211 
LYS NZ  HZ1  sing N N 212 
LYS NZ  HZ2  sing N N 213 
LYS NZ  HZ3  sing N N 214 
LYS OXT HXT  sing N N 215 
MET N   CA   sing N N 216 
MET N   H    sing N N 217 
MET N   H2   sing N N 218 
MET CA  C    sing N N 219 
MET CA  CB   sing N N 220 
MET CA  HA   sing N N 221 
MET C   O    doub N N 222 
MET C   OXT  sing N N 223 
MET CB  CG   sing N N 224 
MET CB  HB2  sing N N 225 
MET CB  HB3  sing N N 226 
MET CG  SD   sing N N 227 
MET CG  HG2  sing N N 228 
MET CG  HG3  sing N N 229 
MET SD  CE   sing N N 230 
MET CE  HE1  sing N N 231 
MET CE  HE2  sing N N 232 
MET CE  HE3  sing N N 233 
MET OXT HXT  sing N N 234 
PHE N   CA   sing N N 235 
PHE N   H    sing N N 236 
PHE N   H2   sing N N 237 
PHE CA  C    sing N N 238 
PHE CA  CB   sing N N 239 
PHE CA  HA   sing N N 240 
PHE C   O    doub N N 241 
PHE C   OXT  sing N N 242 
PHE CB  CG   sing N N 243 
PHE CB  HB2  sing N N 244 
PHE CB  HB3  sing N N 245 
PHE CG  CD1  doub Y N 246 
PHE CG  CD2  sing Y N 247 
PHE CD1 CE1  sing Y N 248 
PHE CD1 HD1  sing N N 249 
PHE CD2 CE2  doub Y N 250 
PHE CD2 HD2  sing N N 251 
PHE CE1 CZ   doub Y N 252 
PHE CE1 HE1  sing N N 253 
PHE CE2 CZ   sing Y N 254 
PHE CE2 HE2  sing N N 255 
PHE CZ  HZ   sing N N 256 
PHE OXT HXT  sing N N 257 
PRO N   CA   sing N N 258 
PRO N   CD   sing N N 259 
PRO N   H    sing N N 260 
PRO CA  C    sing N N 261 
PRO CA  CB   sing N N 262 
PRO CA  HA   sing N N 263 
PRO C   O    doub N N 264 
PRO C   OXT  sing N N 265 
PRO CB  CG   sing N N 266 
PRO CB  HB2  sing N N 267 
PRO CB  HB3  sing N N 268 
PRO CG  CD   sing N N 269 
PRO CG  HG2  sing N N 270 
PRO CG  HG3  sing N N 271 
PRO CD  HD2  sing N N 272 
PRO CD  HD3  sing N N 273 
PRO OXT HXT  sing N N 274 
SER N   CA   sing N N 275 
SER N   H    sing N N 276 
SER N   H2   sing N N 277 
SER CA  C    sing N N 278 
SER CA  CB   sing N N 279 
SER CA  HA   sing N N 280 
SER C   O    doub N N 281 
SER C   OXT  sing N N 282 
SER CB  OG   sing N N 283 
SER CB  HB2  sing N N 284 
SER CB  HB3  sing N N 285 
SER OG  HG   sing N N 286 
SER OXT HXT  sing N N 287 
THR N   CA   sing N N 288 
THR N   H    sing N N 289 
THR N   H2   sing N N 290 
THR CA  C    sing N N 291 
THR CA  CB   sing N N 292 
THR CA  HA   sing N N 293 
THR C   O    doub N N 294 
THR C   OXT  sing N N 295 
THR CB  OG1  sing N N 296 
THR CB  CG2  sing N N 297 
THR CB  HB   sing N N 298 
THR OG1 HG1  sing N N 299 
THR CG2 HG21 sing N N 300 
THR CG2 HG22 sing N N 301 
THR CG2 HG23 sing N N 302 
THR OXT HXT  sing N N 303 
TRP N   CA   sing N N 304 
TRP N   H    sing N N 305 
TRP N   H2   sing N N 306 
TRP CA  C    sing N N 307 
TRP CA  CB   sing N N 308 
TRP CA  HA   sing N N 309 
TRP C   O    doub N N 310 
TRP C   OXT  sing N N 311 
TRP CB  CG   sing N N 312 
TRP CB  HB2  sing N N 313 
TRP CB  HB3  sing N N 314 
TRP CG  CD1  doub Y N 315 
TRP CG  CD2  sing Y N 316 
TRP CD1 NE1  sing Y N 317 
TRP CD1 HD1  sing N N 318 
TRP CD2 CE2  doub Y N 319 
TRP CD2 CE3  sing Y N 320 
TRP NE1 CE2  sing Y N 321 
TRP NE1 HE1  sing N N 322 
TRP CE2 CZ2  sing Y N 323 
TRP CE3 CZ3  doub Y N 324 
TRP CE3 HE3  sing N N 325 
TRP CZ2 CH2  doub Y N 326 
TRP CZ2 HZ2  sing N N 327 
TRP CZ3 CH2  sing Y N 328 
TRP CZ3 HZ3  sing N N 329 
TRP CH2 HH2  sing N N 330 
TRP OXT HXT  sing N N 331 
TYR N   CA   sing N N 332 
TYR N   H    sing N N 333 
TYR N   H2   sing N N 334 
TYR CA  C    sing N N 335 
TYR CA  CB   sing N N 336 
TYR CA  HA   sing N N 337 
TYR C   O    doub N N 338 
TYR C   OXT  sing N N 339 
TYR CB  CG   sing N N 340 
TYR CB  HB2  sing N N 341 
TYR CB  HB3  sing N N 342 
TYR CG  CD1  doub Y N 343 
TYR CG  CD2  sing Y N 344 
TYR CD1 CE1  sing Y N 345 
TYR CD1 HD1  sing N N 346 
TYR CD2 CE2  doub Y N 347 
TYR CD2 HD2  sing N N 348 
TYR CE1 CZ   doub Y N 349 
TYR CE1 HE1  sing N N 350 
TYR CE2 CZ   sing Y N 351 
TYR CE2 HE2  sing N N 352 
TYR CZ  OH   sing N N 353 
TYR OH  HH   sing N N 354 
TYR OXT HXT  sing N N 355 
VAL N   CA   sing N N 356 
VAL N   H    sing N N 357 
VAL N   H2   sing N N 358 
VAL CA  C    sing N N 359 
VAL CA  CB   sing N N 360 
VAL CA  HA   sing N N 361 
VAL C   O    doub N N 362 
VAL C   OXT  sing N N 363 
VAL CB  CG1  sing N N 364 
VAL CB  CG2  sing N N 365 
VAL CB  HB   sing N N 366 
VAL CG1 HG11 sing N N 367 
VAL CG1 HG12 sing N N 368 
VAL CG1 HG13 sing N N 369 
VAL CG2 HG21 sing N N 370 
VAL CG2 HG22 sing N N 371 
VAL CG2 HG23 sing N N 372 
VAL OXT HXT  sing N N 373 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2024-07-10 
_em_admin.deposition_site    PDBJ 
_em_admin.entry_id           9IP3 
_em_admin.last_update        2025-04-16 
_em_admin.map_release_date   2025-04-09 
_em_admin.title              
'Cryo-EM structure of the RNA-dependent RNA polymerase complex in a compact conformation from Ebola virus' 
# 
_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                0.5 
# 
_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          129000 
_em_entity_assembly_naturalsource.organism             'Ebola virus - Eckron (Zaire, 1976)' 
_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          7108 
_em_entity_assembly_recombinant.organism             'Spodoptera frugiperda' 
_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         50 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       ? 
_em_image_recording.film_or_detector_model              'FEI FALCON IV (4k 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 ? ? ? ? 
'VOLUME SELECTION'              ? 14 1 1 1 ? ? 
'SERIES ALIGNMENT'              ? 15 1 1 1 ? ? 
'MOLECULAR REPLACEMENT'         ? 16 1 1 1 ? ? 
'LATTICE DISTORTION CORRECTION' ? 17 1 1 1 ? ? 
'SYMMETRY DETERMINATION'        ? 18 1 1 1 ? ? 
'CRYSTALLOGRAPHY MERGING'       ? 19 1 1 1 ? ? 
# 
_em_specimen.concentration           1.2 
_em_specimen.details                 'This sample is monodisperse.' 
_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 
# 
_pdbx_audit_support.funding_organization   'National Natural Science Foundation of China (NSFC)' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           32371344 
_pdbx_audit_support.ordinal                1 
# 
_atom_sites.entry_id                    9IP3 
_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  
N  
O  
S  
ZN 
# 
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   . THR A 1 435  ? 90.041  116.537 105.238 1.00 116.64 ? 6    THR A N   1 
ATOM   2     C  CA  . THR A 1 435  ? 91.127  117.479 105.504 1.00 115.21 ? 6    THR A CA  1 
ATOM   3     C  C   . THR A 1 435  ? 92.235  116.806 106.317 1.00 104.23 ? 6    THR A C   1 
ATOM   4     O  O   . THR A 1 435  ? 92.287  116.938 107.546 1.00 102.45 ? 6    THR A O   1 
ATOM   5     C  CB  . THR A 1 435  ? 90.621  118.751 106.250 1.00 119.34 ? 6    THR A CB  1 
ATOM   6     O  OG1 . THR A 1 435  ? 90.155  118.403 107.562 1.00 114.67 ? 6    THR A OG1 1 
ATOM   7     C  CG2 . THR A 1 435  ? 89.489  119.435 105.460 1.00 118.67 ? 6    THR A CG2 1 
ATOM   8     N  N   . GLN A 1 436  ? 93.118  116.080 105.630 1.00 99.15  ? 7    GLN A N   1 
ATOM   9     C  CA  . GLN A 1 436  ? 94.162  115.350 106.333 1.00 87.92  ? 7    GLN A CA  1 
ATOM   10    C  C   . GLN A 1 436  ? 95.303  115.047 105.379 1.00 60.11  ? 7    GLN A C   1 
ATOM   11    O  O   . GLN A 1 436  ? 95.165  115.138 104.156 1.00 61.61  ? 7    GLN A O   1 
ATOM   12    C  CB  . GLN A 1 436  ? 93.609  114.069 106.964 1.00 80.35  ? 7    GLN A CB  1 
ATOM   13    C  CG  . GLN A 1 436  ? 94.462  113.527 108.073 1.00 75.47  ? 7    GLN A CG  1 
ATOM   14    C  CD  . GLN A 1 436  ? 93.799  112.378 108.772 1.00 86.40  ? 7    GLN A CD  1 
ATOM   15    O  OE1 . GLN A 1 436  ? 92.693  111.974 108.406 1.00 88.14  ? 7    GLN A OE1 1 
ATOM   16    N  NE2 . GLN A 1 436  ? 94.459  111.846 109.797 1.00 88.84  ? 7    GLN A NE2 1 
ATOM   17    N  N   . TYR A 1 437  ? 96.427  114.718 105.959 1.00 45.72  ? 8    TYR A N   1 
ATOM   18    C  CA  . TYR A 1 437  ? 97.595  114.454 105.156 1.00 42.30  ? 8    TYR A CA  1 
ATOM   19    C  C   . TYR A 1 437  ? 98.566  113.590 105.924 1.00 49.06  ? 8    TYR A C   1 
ATOM   20    O  O   . TYR A 1 437  ? 99.230  114.082 106.843 1.00 60.07  ? 8    TYR A O   1 
ATOM   21    C  CB  . TYR A 1 437  ? 98.264  115.757 104.770 1.00 55.34  ? 8    TYR A CB  1 
ATOM   22    C  CG  . TYR A 1 437  ? 99.031  115.668 103.489 1.00 43.64  ? 8    TYR A CG  1 
ATOM   23    C  CD1 . TYR A 1 437  ? 98.422  115.959 102.294 1.00 45.96  ? 8    TYR A CD1 1 
ATOM   24    C  CD2 . TYR A 1 437  ? 100.360 115.348 103.485 1.00 32.78  ? 8    TYR A CD2 1 
ATOM   25    C  CE1 . TYR A 1 437  ? 99.094  115.902 101.164 1.00 36.30  ? 8    TYR A CE1 1 
ATOM   26    C  CE2 . TYR A 1 437  ? 101.038 115.295 102.350 1.00 31.03  ? 8    TYR A CE2 1 
ATOM   27    C  CZ  . TYR A 1 437  ? 100.399 115.575 101.192 1.00 32.35  ? 8    TYR A CZ  1 
ATOM   28    O  OH  . TYR A 1 437  ? 101.066 115.521 100.003 1.00 51.77  ? 8    TYR A OH  1 
ATOM   29    N  N   . PRO A 1 438  ? 98.691  112.313 105.578 1.00 45.62  ? 9    PRO A N   1 
ATOM   30    C  CA  . PRO A 1 438  ? 99.648  111.445 106.283 1.00 46.36  ? 9    PRO A CA  1 
ATOM   31    C  C   . PRO A 1 438  ? 101.089 111.856 106.010 1.00 47.98  ? 9    PRO A C   1 
ATOM   32    O  O   . PRO A 1 438  ? 101.493 112.056 104.864 1.00 50.28  ? 9    PRO A O   1 
ATOM   33    C  CB  . PRO A 1 438  ? 99.343  110.052 105.728 1.00 46.07  ? 9    PRO A CB  1 
ATOM   34    C  CG  . PRO A 1 438  ? 98.723  110.312 104.398 1.00 52.49  ? 9    PRO A CG  1 
ATOM   35    C  CD  . PRO A 1 438  ? 97.938  111.597 104.542 1.00 52.51  ? 9    PRO A CD  1 
ATOM   36    N  N   . ASP A 1 439  ? 101.860 111.981 107.083 1.00 57.09  ? 10   ASP A N   1 
ATOM   37    C  CA  . ASP A 1 439  ? 103.250 112.379 106.967 1.00 58.35  ? 10   ASP A CA  1 
ATOM   38    C  C   . ASP A 1 439  ? 104.055 111.305 106.243 1.00 55.44  ? 10   ASP A C   1 
ATOM   39    O  O   . ASP A 1 439  ? 103.748 110.107 106.301 1.00 54.12  ? 10   ASP A O   1 
ATOM   40    C  CB  . ASP A 1 439  ? 103.837 112.692 108.358 1.00 70.27  ? 10   ASP A CB  1 
ATOM   41    C  CG  . ASP A 1 439  ? 103.491 111.630 109.426 1.00 74.37  ? 10   ASP A CG  1 
ATOM   42    O  OD1 . ASP A 1 439  ? 102.722 110.679 109.137 1.00 67.48  ? 10   ASP A OD1 1 
ATOM   43    O  OD2 . ASP A 1 439  ? 103.990 111.768 110.573 1.00 73.63  ? 10   ASP A OD2 1 
ATOM   44    N  N   . ALA A 1 440  ? 105.071 111.762 105.510 1.00 58.62  ? 11   ALA A N   1 
ATOM   45    C  CA  . ALA A 1 440  ? 105.879 110.850 104.708 1.00 59.26  ? 11   ALA A CA  1 
ATOM   46    C  C   . ALA A 1 440  ? 106.843 110.042 105.572 1.00 61.41  ? 11   ALA A C   1 
ATOM   47    O  O   . ALA A 1 440  ? 106.980 108.827 105.380 1.00 59.88  ? 11   ALA A O   1 
ATOM   48    C  CB  . ALA A 1 440  ? 106.632 111.640 103.635 1.00 63.82  ? 11   ALA A CB  1 
ATOM   49    N  N   . ARG A 1 441  ? 107.506 110.693 106.531 1.00 63.96  ? 12   ARG A N   1 
ATOM   50    C  CA  . ARG A 1 441  ? 108.496 110.065 107.399 1.00 58.34  ? 12   ARG A CA  1 
ATOM   51    C  C   . ARG A 1 441  ? 107.906 109.831 108.781 1.00 51.26  ? 12   ARG A C   1 
ATOM   52    O  O   . ARG A 1 441  ? 106.857 110.370 109.139 1.00 57.52  ? 12   ARG A O   1 
ATOM   53    C  CB  . ARG A 1 441  ? 109.757 110.927 107.537 1.00 63.78  ? 12   ARG A CB  1 
ATOM   54    C  CG  . ARG A 1 441  ? 110.258 111.550 106.245 1.00 67.79  ? 12   ARG A CG  1 
ATOM   55    C  CD  . ARG A 1 441  ? 111.779 111.630 106.203 1.00 70.18  ? 12   ARG A CD  1 
ATOM   56    N  NE  . ARG A 1 441  ? 112.314 110.265 106.129 1.00 80.32  ? 12   ARG A NE  1 
ATOM   57    C  CZ  . ARG A 1 441  ? 113.600 109.950 105.987 1.00 82.46  ? 12   ARG A CZ  1 
ATOM   58    N  NH1 . ARG A 1 441  ? 114.508 110.912 105.880 1.00 77.05  ? 12   ARG A NH1 1 
ATOM   59    N  NH2 . ARG A 1 441  ? 113.977 108.671 105.924 1.00 72.62  ? 12   ARG A NH2 1 
ATOM   60    N  N   . LEU A 1 442  ? 108.600 109.019 109.565 1.00 48.38  ? 13   LEU A N   1 
ATOM   61    C  CA  . LEU A 1 442  ? 108.178 108.777 110.934 1.00 47.36  ? 13   LEU A CA  1 
ATOM   62    C  C   . LEU A 1 442  ? 108.350 110.065 111.727 1.00 65.52  ? 13   LEU A C   1 
ATOM   63    O  O   . LEU A 1 442  ? 109.466 110.586 111.810 1.00 72.82  ? 13   LEU A O   1 
ATOM   64    C  CB  . LEU A 1 442  ? 109.023 107.676 111.554 1.00 51.05  ? 13   LEU A CB  1 
ATOM   65    C  CG  . LEU A 1 442  ? 108.599 107.354 112.980 1.00 59.93  ? 13   LEU A CG  1 
ATOM   66    C  CD1 . LEU A 1 442  ? 107.211 106.733 112.897 1.00 57.67  ? 13   LEU A CD1 1 
ATOM   67    C  CD2 . LEU A 1 442  ? 109.592 106.463 113.723 1.00 59.08  ? 13   LEU A CD2 1 
ATOM   68    N  N   . SER A 1 443  ? 107.262 110.595 112.312 1.00 63.42  ? 14   SER A N   1 
ATOM   69    C  CA  . SER A 1 443  ? 107.369 111.785 113.160 1.00 56.60  ? 14   SER A CA  1 
ATOM   70    C  C   . SER A 1 443  ? 106.601 111.690 114.470 1.00 47.95  ? 14   SER A C   1 
ATOM   71    O  O   . SER A 1 443  ? 106.573 112.668 115.222 1.00 53.83  ? 14   SER A O   1 
ATOM   72    C  CB  . SER A 1 443  ? 106.914 113.047 112.401 1.00 64.21  ? 14   SER A CB  1 
ATOM   73    O  OG  . SER A 1 443  ? 107.788 113.360 111.326 1.00 62.30  ? 14   SER A OG  1 
ATOM   74    N  N   . SER A 1 444  ? 106.005 110.550 114.776 1.00 51.40  ? 15   SER A N   1 
ATOM   75    C  CA  . SER A 1 444  ? 105.224 110.371 115.987 1.00 51.05  ? 15   SER A CA  1 
ATOM   76    C  C   . SER A 1 444  ? 105.756 109.176 116.760 1.00 40.85  ? 15   SER A C   1 
ATOM   77    O  O   . SER A 1 444  ? 106.361 108.275 116.174 1.00 48.98  ? 15   SER A O   1 
ATOM   78    C  CB  . SER A 1 444  ? 103.740 110.149 115.658 1.00 58.51  ? 15   SER A CB  1 
ATOM   79    O  OG  . SER A 1 444  ? 103.568 109.002 114.841 1.00 57.77  ? 15   SER A OG  1 
ATOM   80    N  N   . PRO A 1 445  ? 105.581 109.152 118.068 1.00 31.33  ? 16   PRO A N   1 
ATOM   81    C  CA  . PRO A 1 445  ? 106.136 108.047 118.834 1.00 28.51  ? 16   PRO A CA  1 
ATOM   82    C  C   . PRO A 1 445  ? 105.371 106.798 118.501 1.00 34.53  ? 16   PRO A C   1 
ATOM   83    O  O   . PRO A 1 445  ? 104.158 106.823 118.293 1.00 40.33  ? 16   PRO A O   1 
ATOM   84    C  CB  . PRO A 1 445  ? 105.904 108.459 120.283 1.00 38.14  ? 16   PRO A CB  1 
ATOM   85    C  CG  . PRO A 1 445  ? 104.762 109.383 120.215 1.00 40.22  ? 16   PRO A CG  1 
ATOM   86    C  CD  . PRO A 1 445  ? 104.912 110.127 118.935 1.00 40.54  ? 16   PRO A CD  1 
ATOM   87    N  N   . ILE A 1 446  ? 106.096 105.691 118.436 1.00 32.50  ? 17   ILE A N   1 
ATOM   88    C  CA  . ILE A 1 446  ? 105.459 104.443 118.075 1.00 26.18  ? 17   ILE A CA  1 
ATOM   89    C  C   . ILE A 1 446  ? 104.641 104.066 119.295 1.00 27.64  ? 17   ILE A C   1 
ATOM   90    O  O   . ILE A 1 446  ? 105.181 103.568 120.275 1.00 40.07  ? 17   ILE A O   1 
ATOM   91    C  CB  . ILE A 1 446  ? 106.479 103.366 117.721 1.00 28.61  ? 17   ILE A CB  1 
ATOM   92    C  CG1 . ILE A 1 446  ? 107.381 103.894 116.633 1.00 36.69  ? 17   ILE A CG1 1 
ATOM   93    C  CG2 . ILE A 1 446  ? 105.779 102.143 117.183 1.00 36.90  ? 17   ILE A CG2 1 
ATOM   94    C  CD1 . ILE A 1 446  ? 106.625 104.130 115.344 1.00 46.24  ? 17   ILE A CD1 1 
ATOM   95    N  N   . VAL A 1 447  ? 103.361 104.363 119.278 1.00 19.15  ? 18   VAL A N   1 
ATOM   96    C  CA  . VAL A 1 447  ? 102.501 103.951 120.360 1.00 22.62  ? 18   VAL A CA  1 
ATOM   97    C  C   . VAL A 1 447  ? 101.444 103.050 119.764 1.00 30.27  ? 18   VAL A C   1 
ATOM   98    O  O   . VAL A 1 447  ? 100.720 103.452 118.845 1.00 33.31  ? 18   VAL A O   1 
ATOM   99    C  CB  . VAL A 1 447  ? 101.899 105.154 121.086 1.00 39.60  ? 18   VAL A CB  1 
ATOM   100   C  CG1 . VAL A 1 447  ? 101.188 104.713 122.367 1.00 44.75  ? 18   VAL A CG1 1 
ATOM   101   C  CG2 . VAL A 1 447  ? 103.019 106.129 121.415 1.00 44.65  ? 18   VAL A CG2 1 
ATOM   102   N  N   . LEU A 1 448  ? 101.366 101.826 120.264 1.00 26.43  ? 19   LEU A N   1 
ATOM   103   C  CA  . LEU A 1 448  ? 100.505 100.845 119.643 1.00 24.36  ? 19   LEU A CA  1 
ATOM   104   C  C   . LEU A 1 448  ? 99.264  100.550 120.460 1.00 36.87  ? 19   LEU A C   1 
ATOM   105   O  O   . LEU A 1 448  ? 98.615  99.524  120.227 1.00 46.52  ? 19   LEU A O   1 
ATOM   106   C  CB  . LEU A 1 448  ? 101.274 99.557  119.398 1.00 29.07  ? 19   LEU A CB  1 
ATOM   107   C  CG  . LEU A 1 448  ? 102.450 99.785  118.490 1.00 33.30  ? 19   LEU A CG  1 
ATOM   108   C  CD1 . LEU A 1 448  ? 103.078 98.463  118.089 1.00 35.67  ? 19   LEU A CD1 1 
ATOM   109   C  CD2 . LEU A 1 448  ? 101.918 100.539 117.297 1.00 41.75  ? 19   LEU A CD2 1 
ATOM   110   N  N   . ASP A 1 449  ? 98.909  101.401 121.422 1.00 35.58  ? 20   ASP A N   1 
ATOM   111   C  CA  . ASP A 1 449  ? 97.722  101.081 122.217 1.00 42.31  ? 20   ASP A CA  1 
ATOM   112   C  C   . ASP A 1 449  ? 96.470  101.023 121.351 1.00 42.84  ? 20   ASP A C   1 
ATOM   113   O  O   . ASP A 1 449  ? 95.555  100.248 121.641 1.00 46.15  ? 20   ASP A O   1 
ATOM   114   C  CB  . ASP A 1 449  ? 97.513  102.074 123.378 1.00 60.18  ? 20   ASP A CB  1 
ATOM   115   C  CG  . ASP A 1 449  ? 98.730  102.174 124.338 1.00 67.12  ? 20   ASP A CG  1 
ATOM   116   O  OD1 . ASP A 1 449  ? 99.124  103.311 124.711 1.00 58.29  ? 20   ASP A OD1 1 
ATOM   117   O  OD2 . ASP A 1 449  ? 99.264  101.114 124.751 1.00 59.14  ? 20   ASP A OD2 1 
ATOM   118   N  N   . GLN A 1 450  ? 96.410  101.817 120.286 1.00 39.38  ? 21   GLN A N   1 
ATOM   119   C  CA  . GLN A 1 450  ? 95.233  101.787 119.433 1.00 33.15  ? 21   GLN A CA  1 
ATOM   120   C  C   . GLN A 1 450  ? 95.095  100.450 118.736 1.00 32.86  ? 21   GLN A C   1 
ATOM   121   O  O   . GLN A 1 450  ? 93.977  99.981  118.503 1.00 42.81  ? 21   GLN A O   1 
ATOM   122   C  CB  . GLN A 1 450  ? 95.313  102.906 118.423 1.00 34.93  ? 21   GLN A CB  1 
ATOM   123   C  CG  . GLN A 1 450  ? 96.658  102.945 117.805 1.00 39.35  ? 21   GLN A CG  1 
ATOM   124   C  CD  . GLN A 1 450  ? 96.818  104.099 116.868 1.00 47.90  ? 21   GLN A CD  1 
ATOM   125   O  OE1 . GLN A 1 450  ? 95.837  104.702 116.432 1.00 52.83  ? 21   GLN A OE1 1 
ATOM   126   N  NE2 . GLN A 1 450  ? 98.062  104.434 116.556 1.00 48.15  ? 21   GLN A NE2 1 
ATOM   127   N  N   . CYS A 1 451  ? 96.208  99.807  118.401 1.00 27.48  ? 22   CYS A N   1 
ATOM   128   C  CA  . CYS A 1 451  ? 96.073  98.535  117.711 1.00 27.71  ? 22   CYS A CA  1 
ATOM   129   C  C   . CYS A 1 451  ? 95.320  97.537  118.552 1.00 32.66  ? 22   CYS A C   1 
ATOM   130   O  O   . CYS A 1 451  ? 94.658  96.647  118.011 1.00 47.02  ? 22   CYS A O   1 
ATOM   131   C  CB  . CYS A 1 451  ? 97.425  97.966  117.330 1.00 36.65  ? 22   CYS A CB  1 
ATOM   132   S  SG  . CYS A 1 451  ? 98.345  99.081  116.269 1.00 65.44  ? 22   CYS A SG  1 
ATOM   133   N  N   . ASP A 1 452  ? 95.350  97.702  119.865 1.00 34.71  ? 23   ASP A N   1 
ATOM   134   C  CA  . ASP A 1 452  ? 94.638  96.770  120.723 1.00 37.69  ? 23   ASP A CA  1 
ATOM   135   C  C   . ASP A 1 452  ? 93.134  96.766  120.440 1.00 43.21  ? 23   ASP A C   1 
ATOM   136   O  O   . ASP A 1 452  ? 92.492  95.716  120.577 1.00 50.59  ? 23   ASP A O   1 
ATOM   137   C  CB  . ASP A 1 452  ? 94.905  97.109  122.191 1.00 50.27  ? 23   ASP A CB  1 
ATOM   138   C  CG  . ASP A 1 452  ? 94.543  95.972  123.132 1.00 55.17  ? 23   ASP A CG  1 
ATOM   139   O  OD1 . ASP A 1 452  ? 95.485  95.317  123.631 1.00 56.07  ? 23   ASP A OD1 1 
ATOM   140   O  OD2 . ASP A 1 452  ? 93.338  95.715  123.356 1.00 57.14  ? 23   ASP A OD2 1 
ATOM   141   N  N   . LEU A 1 453  ? 92.541  97.911  120.050 1.00 39.96  ? 24   LEU A N   1 
ATOM   142   C  CA  . LEU A 1 453  ? 91.122  97.872  119.683 1.00 33.45  ? 24   LEU A CA  1 
ATOM   143   C  C   . LEU A 1 453  ? 90.934  97.204  118.334 1.00 40.72  ? 24   LEU A C   1 
ATOM   144   O  O   . LEU A 1 453  ? 89.978  96.444  118.149 1.00 47.47  ? 24   LEU A O   1 
ATOM   145   C  CB  . LEU A 1 453  ? 90.493  99.256  119.634 1.00 29.72  ? 24   LEU A CB  1 
ATOM   146   C  CG  . LEU A 1 453  ? 90.934  100.198 120.725 1.00 45.20  ? 24   LEU A CG  1 
ATOM   147   C  CD1 . LEU A 1 453  ? 90.298  101.562 120.508 1.00 50.19  ? 24   LEU A CD1 1 
ATOM   148   C  CD2 . LEU A 1 453  ? 90.633  99.603  122.086 1.00 49.96  ? 24   LEU A CD2 1 
ATOM   149   N  N   . VAL A 1 454  ? 91.836  97.468  117.381 1.00 36.89  ? 25   VAL A N   1 
ATOM   150   C  CA  . VAL A 1 454  ? 91.692  96.869  116.059 1.00 27.04  ? 25   VAL A CA  1 
ATOM   151   C  C   . VAL A 1 454  ? 91.567  95.369  116.179 1.00 35.60  ? 25   VAL A C   1 
ATOM   152   O  O   . VAL A 1 454  ? 90.610  94.772  115.675 1.00 51.01  ? 25   VAL A O   1 
ATOM   153   C  CB  . VAL A 1 454  ? 92.866  97.250  115.150 1.00 26.39  ? 25   VAL A CB  1 
ATOM   154   C  CG1 . VAL A 1 454  ? 92.838  96.407  113.938 1.00 32.53  ? 25   VAL A CG1 1 
ATOM   155   C  CG2 . VAL A 1 454  ? 92.685  98.669  114.705 1.00 41.77  ? 25   VAL A CG2 1 
ATOM   156   N  N   . THR A 1 455  ? 92.479  94.741  116.906 1.00 31.34  ? 26   THR A N   1 
ATOM   157   C  CA  . THR A 1 455  ? 92.421  93.293  116.978 1.00 37.93  ? 26   THR A CA  1 
ATOM   158   C  C   . THR A 1 455  ? 91.109  92.823  117.600 1.00 43.81  ? 26   THR A C   1 
ATOM   159   O  O   . THR A 1 455  ? 90.595  91.756  117.235 1.00 52.02  ? 26   THR A O   1 
ATOM   160   C  CB  . THR A 1 455  ? 93.623  92.749  117.752 1.00 51.19  ? 26   THR A CB  1 
ATOM   161   O  OG1 . THR A 1 455  ? 93.423  92.935  119.163 1.00 54.92  ? 26   THR A OG1 1 
ATOM   162   C  CG2 . THR A 1 455  ? 94.911  93.457  117.319 1.00 49.43  ? 26   THR A CG2 1 
ATOM   163   N  N   . ARG A 1 456  ? 90.531  93.609  118.506 1.00 36.84  ? 27   ARG A N   1 
ATOM   164   C  CA  . ARG A 1 456  ? 89.289  93.175  119.129 1.00 35.89  ? 27   ARG A CA  1 
ATOM   165   C  C   . ARG A 1 456  ? 88.126  93.264  118.159 1.00 34.22  ? 27   ARG A C   1 
ATOM   166   O  O   . ARG A 1 456  ? 87.181  92.477  118.242 1.00 37.85  ? 27   ARG A O   1 
ATOM   167   C  CB  . ARG A 1 456  ? 89.033  94.003  120.377 1.00 37.90  ? 27   ARG A CB  1 
ATOM   168   C  CG  . ARG A 1 456  ? 87.986  93.445  121.240 1.00 39.62  ? 27   ARG A CG  1 
ATOM   169   C  CD  . ARG A 1 456  ? 88.206  93.994  122.611 1.00 43.70  ? 27   ARG A CD  1 
ATOM   170   N  NE  . ARG A 1 456  ? 88.277  95.431  122.569 1.00 35.02  ? 27   ARG A NE  1 
ATOM   171   C  CZ  . ARG A 1 456  ? 87.212  96.191  122.730 1.00 42.05  ? 27   ARG A CZ  1 
ATOM   172   N  NH1 . ARG A 1 456  ? 86.029  95.624  122.919 1.00 41.18  ? 27   ARG A NH1 1 
ATOM   173   N  NH2 . ARG A 1 456  ? 87.326  97.511  122.688 1.00 53.29  ? 27   ARG A NH2 1 
ATOM   174   N  N   . ALA A 1 457  ? 88.179  94.211  117.237 1.00 37.12  ? 28   ALA A N   1 
ATOM   175   C  CA  . ALA A 1 457  ? 87.127  94.300  116.245 1.00 37.96  ? 28   ALA A CA  1 
ATOM   176   C  C   . ALA A 1 457  ? 87.261  93.188  115.224 1.00 44.47  ? 28   ALA A C   1 
ATOM   177   O  O   . ALA A 1 457  ? 86.258  92.599  114.808 1.00 57.56  ? 28   ALA A O   1 
ATOM   178   C  CB  . ALA A 1 457  ? 87.164  95.662  115.559 1.00 44.90  ? 28   ALA A CB  1 
ATOM   179   N  N   . CYS A 1 458  ? 88.485  92.882  114.806 1.00 37.55  ? 29   CYS A N   1 
ATOM   180   C  CA  . CYS A 1 458  ? 88.644  91.847  113.796 1.00 41.80  ? 29   CYS A CA  1 
ATOM   181   C  C   . CYS A 1 458  ? 88.376  90.446  114.329 1.00 51.90  ? 29   CYS A C   1 
ATOM   182   O  O   . CYS A 1 458  ? 88.321  89.500  113.535 1.00 53.15  ? 29   CYS A O   1 
ATOM   183   C  CB  . CYS A 1 458  ? 90.042  91.909  113.187 1.00 43.70  ? 29   CYS A CB  1 
ATOM   184   S  SG  . CYS A 1 458  ? 90.355  93.411  112.246 1.00 63.44  ? 29   CYS A SG  1 
ATOM   185   N  N   . GLY A 1 459  ? 88.200  90.282  115.636 1.00 47.22  ? 30   GLY A N   1 
ATOM   186   C  CA  . GLY A 1 459  ? 88.143  88.963  116.213 1.00 41.36  ? 30   GLY A CA  1 
ATOM   187   C  C   . GLY A 1 459  ? 89.474  88.445  116.700 1.00 43.46  ? 30   GLY A C   1 
ATOM   188   O  O   . GLY A 1 459  ? 89.505  87.399  117.359 1.00 49.00  ? 30   GLY A O   1 
ATOM   189   N  N   . LEU A 1 460  ? 90.567  89.153  116.423 1.00 36.26  ? 31   LEU A N   1 
ATOM   190   C  CA  . LEU A 1 460  ? 91.887  88.763  116.898 1.00 35.58  ? 31   LEU A CA  1 
ATOM   191   C  C   . LEU A 1 460  ? 92.038  89.049  118.401 1.00 45.67  ? 31   LEU A C   1 
ATOM   192   O  O   . LEU A 1 460  ? 91.082  89.395  119.103 1.00 44.33  ? 31   LEU A O   1 
ATOM   193   C  CB  . LEU A 1 460  ? 92.961  89.468  116.082 1.00 37.16  ? 31   LEU A CB  1 
ATOM   194   C  CG  . LEU A 1 460  ? 92.855  89.365  114.571 1.00 41.78  ? 31   LEU A CG  1 
ATOM   195   C  CD1 . LEU A 1 460  ? 93.796  90.362  113.879 1.00 40.03  ? 31   LEU A CD1 1 
ATOM   196   C  CD2 . LEU A 1 460  ? 93.207  87.935  114.190 1.00 43.96  ? 31   LEU A CD2 1 
ATOM   197   N  N   . TYR A 1 461  ? 93.259  88.874  118.916 1.00 46.59  ? 32   TYR A N   1 
ATOM   198   C  CA  . TYR A 1 461  ? 93.618  89.173  120.297 1.00 40.92  ? 32   TYR A CA  1 
ATOM   199   C  C   . TYR A 1 461  ? 95.027  89.742  120.328 1.00 42.53  ? 32   TYR A C   1 
ATOM   200   O  O   . TYR A 1 461  ? 95.923  89.211  119.665 1.00 45.47  ? 32   TYR A O   1 
ATOM   201   C  CB  . TYR A 1 461  ? 93.568  87.928  121.179 1.00 38.28  ? 32   TYR A CB  1 
ATOM   202   C  CG  . TYR A 1 461  ? 94.107  88.197  122.559 1.00 37.14  ? 32   TYR A CG  1 
ATOM   203   C  CD1 . TYR A 1 461  ? 93.314  88.793  123.524 1.00 52.00  ? 32   TYR A CD1 1 
ATOM   204   C  CD2 . TYR A 1 461  ? 95.403  87.888  122.885 1.00 35.70  ? 32   TYR A CD2 1 
ATOM   205   C  CE1 . TYR A 1 461  ? 93.788  89.053  124.779 1.00 48.93  ? 32   TYR A CE1 1 
ATOM   206   C  CE2 . TYR A 1 461  ? 95.893  88.148  124.132 1.00 47.72  ? 32   TYR A CE2 1 
ATOM   207   C  CZ  . TYR A 1 461  ? 95.078  88.733  125.078 1.00 51.45  ? 32   TYR A CZ  1 
ATOM   208   O  OH  . TYR A 1 461  ? 95.554  89.000  126.336 1.00 59.97  ? 32   TYR A OH  1 
ATOM   209   N  N   . SER A 1 462  ? 95.228  90.801  121.104 1.00 48.79  ? 33   SER A N   1 
ATOM   210   C  CA  . SER A 1 462  ? 96.555  91.378  121.291 1.00 50.76  ? 33   SER A CA  1 
ATOM   211   C  C   . SER A 1 462  ? 96.566  92.110  122.620 1.00 52.23  ? 33   SER A C   1 
ATOM   212   O  O   . SER A 1 462  ? 95.515  92.486  123.142 1.00 60.83  ? 33   SER A O   1 
ATOM   213   C  CB  . SER A 1 462  ? 96.928  92.344  120.159 1.00 50.08  ? 33   SER A CB  1 
ATOM   214   O  OG  . SER A 1 462  ? 96.992  91.674  118.911 1.00 52.41  ? 33   SER A OG  1 
ATOM   215   N  N   . SER A 1 463  ? 97.750  92.323  123.175 1.00 41.17  ? 34   SER A N   1 
ATOM   216   C  CA  . SER A 1 463  ? 97.801  93.024  124.448 1.00 39.23  ? 34   SER A CA  1 
ATOM   217   C  C   . SER A 1 463  ? 98.910  94.064  124.457 1.00 41.29  ? 34   SER A C   1 
ATOM   218   O  O   . SER A 1 463  ? 99.704  94.153  125.396 1.00 43.26  ? 34   SER A O   1 
ATOM   219   C  CB  . SER A 1 463  ? 97.933  92.019  125.569 1.00 43.14  ? 34   SER A CB  1 
ATOM   220   O  OG  . SER A 1 463  ? 99.153  91.331  125.439 1.00 54.63  ? 34   SER A OG  1 
ATOM   221   N  N   . TYR A 1 464  ? 98.965  94.879  123.396 1.00 39.91  ? 35   TYR A N   1 
ATOM   222   C  CA  . TYR A 1 464  ? 99.945  95.956  123.337 1.00 29.07  ? 35   TYR A CA  1 
ATOM   223   C  C   . TYR A 1 464  ? 99.838  96.848  124.561 1.00 38.99  ? 35   TYR A C   1 
ATOM   224   O  O   . TYR A 1 464  ? 100.849 97.202  125.173 1.00 49.12  ? 35   TYR A O   1 
ATOM   225   C  CB  . TYR A 1 464  ? 99.737  96.804  122.098 1.00 23.68  ? 35   TYR A CB  1 
ATOM   226   C  CG  . TYR A 1 464  ? 100.007 96.077  120.850 1.00 26.29  ? 35   TYR A CG  1 
ATOM   227   C  CD1 . TYR A 1 464  ? 98.984  95.497  120.149 1.00 34.79  ? 35   TYR A CD1 1 
ATOM   228   C  CD2 . TYR A 1 464  ? 101.292 95.924  120.385 1.00 34.72  ? 35   TYR A CD2 1 
ATOM   229   C  CE1 . TYR A 1 464  ? 99.221  94.802  118.997 1.00 37.13  ? 35   TYR A CE1 1 
ATOM   230   C  CE2 . TYR A 1 464  ? 101.543 95.235  119.230 1.00 33.21  ? 35   TYR A CE2 1 
ATOM   231   C  CZ  . TYR A 1 464  ? 100.501 94.670  118.542 1.00 33.26  ? 35   TYR A CZ  1 
ATOM   232   O  OH  . TYR A 1 464  ? 100.733 93.962  117.383 1.00 40.32  ? 35   TYR A OH  1 
ATOM   233   N  N   . SER A 1 465  ? 98.624  97.236  124.930 1.00 30.87  ? 36   SER A N   1 
ATOM   234   C  CA  . SER A 1 465  ? 98.464  98.291  125.909 1.00 26.41  ? 36   SER A CA  1 
ATOM   235   C  C   . SER A 1 465  ? 98.485  97.699  127.300 1.00 41.50  ? 36   SER A C   1 
ATOM   236   O  O   . SER A 1 465  ? 97.889  96.648  127.546 1.00 45.59  ? 36   SER A O   1 
ATOM   237   C  CB  . SER A 1 465  ? 97.160  99.049  125.701 1.00 38.86  ? 36   SER A CB  1 
ATOM   238   O  OG  . SER A 1 465  ? 96.052  98.176  125.780 1.00 43.18  ? 36   SER A OG  1 
ATOM   239   N  N   . LEU A 1 466  ? 99.182  98.380  128.211 1.00 43.64  ? 37   LEU A N   1 
ATOM   240   C  CA  . LEU A 1 466  ? 99.177  98.019  129.618 1.00 29.03  ? 37   LEU A CA  1 
ATOM   241   C  C   . LEU A 1 466  ? 97.959  98.515  130.320 1.00 30.96  ? 37   LEU A C   1 
ATOM   242   O  O   . LEU A 1 466  ? 97.920  98.499  131.549 1.00 40.14  ? 37   LEU A O   1 
ATOM   243   C  CB  . LEU A 1 466  ? 100.401 98.572  130.331 1.00 32.38  ? 37   LEU A CB  1 
ATOM   244   C  CG  . LEU A 1 466  ? 101.722 98.254  129.631 1.00 50.61  ? 37   LEU A CG  1 
ATOM   245   C  CD1 . LEU A 1 466  ? 102.940 98.821  130.415 1.00 50.97  ? 37   LEU A CD1 1 
ATOM   246   C  CD2 . LEU A 1 466  ? 101.851 96.743  129.345 1.00 46.33  ? 37   LEU A CD2 1 
ATOM   247   N  N   . ASN A 1 467  ? 96.982  98.992  129.590 1.00 27.16  ? 38   ASN A N   1 
ATOM   248   C  CA  . ASN A 1 467  ? 95.873  99.619  130.234 1.00 25.56  ? 38   ASN A CA  1 
ATOM   249   C  C   . ASN A 1 467  ? 94.707  98.659  130.190 1.00 28.58  ? 38   ASN A C   1 
ATOM   250   O  O   . ASN A 1 467  ? 94.281  98.291  129.091 1.00 41.89  ? 38   ASN A O   1 
ATOM   251   C  CB  . ASN A 1 467  ? 95.518  100.906 129.527 1.00 32.31  ? 38   ASN A CB  1 
ATOM   252   C  CG  . ASN A 1 467  ? 94.586  101.747 130.337 1.00 42.12  ? 38   ASN A CG  1 
ATOM   253   O  OD1 . ASN A 1 467  ? 94.496  101.583 131.556 1.00 41.50  ? 38   ASN A OD1 1 
ATOM   254   N  ND2 . ASN A 1 467  ? 93.833  102.623 129.668 1.00 45.02  ? 38   ASN A ND2 1 
ATOM   255   N  N   . PRO A 1 468  ? 94.164  98.209  131.314 1.00 27.73  ? 39   PRO A N   1 
ATOM   256   C  CA  . PRO A 1 468  ? 93.044  97.267  131.243 1.00 26.76  ? 39   PRO A CA  1 
ATOM   257   C  C   . PRO A 1 468  ? 91.827  97.860  130.622 1.00 32.22  ? 39   PRO A C   1 
ATOM   258   O  O   . PRO A 1 468  ? 90.920  97.112  130.250 1.00 43.07  ? 39   PRO A O   1 
ATOM   259   C  CB  . PRO A 1 468  ? 92.772  96.917  132.707 1.00 35.14  ? 39   PRO A CB  1 
ATOM   260   C  CG  . PRO A 1 468  ? 93.992  97.282  133.429 1.00 41.37  ? 39   PRO A CG  1 
ATOM   261   C  CD  . PRO A 1 468  ? 94.560  98.472  132.698 1.00 42.21  ? 39   PRO A CD  1 
ATOM   262   N  N   . GLN A 1 469  ? 91.755  99.183  130.529 1.00 36.87  ? 40   GLN A N   1 
ATOM   263   C  CA  . GLN A 1 469  ? 90.594  99.807  129.911 1.00 39.64  ? 40   GLN A CA  1 
ATOM   264   C  C   . GLN A 1 469  ? 90.466  99.394  128.453 1.00 40.97  ? 40   GLN A C   1 
ATOM   265   O  O   . GLN A 1 469  ? 89.352  99.187  127.966 1.00 53.34  ? 40   GLN A O   1 
ATOM   266   C  CB  . GLN A 1 469  ? 90.682  101.331 130.036 1.00 47.10  ? 40   GLN A CB  1 
ATOM   267   C  CG  . GLN A 1 469  ? 89.560  102.106 129.363 1.00 37.41  ? 40   GLN A CG  1 
ATOM   268   C  CD  . GLN A 1 469  ? 88.255  101.940 130.104 1.00 39.91  ? 40   GLN A CD  1 
ATOM   269   O  OE1 . GLN A 1 469  ? 88.241  101.662 131.302 1.00 44.45  ? 40   GLN A OE1 1 
ATOM   270   N  NE2 . GLN A 1 469  ? 87.147  102.107 129.397 1.00 48.48  ? 40   GLN A NE2 1 
ATOM   271   N  N   . LEU A 1 470  ? 91.582  99.253  127.736 1.00 30.13  ? 41   LEU A N   1 
ATOM   272   C  CA  . LEU A 1 470  ? 91.443  98.946  126.320 1.00 27.88  ? 41   LEU A CA  1 
ATOM   273   C  C   . LEU A 1 470  ? 90.965  97.531  126.049 1.00 36.38  ? 41   LEU A C   1 
ATOM   274   O  O   . LEU A 1 470  ? 90.621  97.226  124.906 1.00 40.48  ? 41   LEU A O   1 
ATOM   275   C  CB  . LEU A 1 470  ? 92.733  99.173  125.587 1.00 25.86  ? 41   LEU A CB  1 
ATOM   276   C  CG  . LEU A 1 470  ? 92.859  100.644 125.273 1.00 33.27  ? 41   LEU A CG  1 
ATOM   277   C  CD1 . LEU A 1 470  ? 93.082  101.466 126.520 1.00 40.13  ? 41   LEU A CD1 1 
ATOM   278   C  CD2 . LEU A 1 470  ? 93.997  100.828 124.330 1.00 43.74  ? 41   LEU A CD2 1 
ATOM   279   N  N   . ARG A 1 471  ? 90.933  96.661  127.054 1.00 44.66  ? 42   ARG A N   1 
ATOM   280   C  CA  . ARG A 1 471  ? 90.377  95.326  126.854 1.00 45.42  ? 42   ARG A CA  1 
ATOM   281   C  C   . ARG A 1 471  ? 88.877  95.374  126.639 1.00 46.07  ? 42   ARG A C   1 
ATOM   282   O  O   . ARG A 1 471  ? 88.357  94.736  125.717 1.00 53.65  ? 42   ARG A O   1 
ATOM   283   C  CB  . ARG A 1 471  ? 90.699  94.438  128.057 1.00 58.49  ? 42   ARG A CB  1 
ATOM   284   C  CG  . ARG A 1 471  ? 92.161  93.972  128.118 1.00 68.64  ? 42   ARG A CG  1 
ATOM   285   C  CD  . ARG A 1 471  ? 92.339  92.604  127.432 1.00 76.09  ? 42   ARG A CD  1 
ATOM   286   N  NE  . ARG A 1 471  ? 92.038  92.656  125.996 1.00 80.29  ? 42   ARG A NE  1 
ATOM   287   C  CZ  . ARG A 1 471  ? 92.947  92.794  125.030 1.00 81.12  ? 42   ARG A CZ  1 
ATOM   288   N  NH1 . ARG A 1 471  ? 94.242  92.880  125.336 1.00 74.80  ? 42   ARG A NH1 1 
ATOM   289   N  NH2 . ARG A 1 471  ? 92.560  92.842  123.752 1.00 72.46  ? 42   ARG A NH2 1 
ATOM   290   N  N   . ASN A 1 472  ? 88.163  96.126  127.474 1.00 44.52  ? 43   ASN A N   1 
ATOM   291   C  CA  . ASN A 1 472  ? 86.706  96.076  127.508 1.00 50.27  ? 43   ASN A CA  1 
ATOM   292   C  C   . ASN A 1 472  ? 86.064  97.435  127.263 1.00 49.25  ? 43   ASN A C   1 
ATOM   293   O  O   . ASN A 1 472  ? 84.935  97.668  127.701 1.00 53.43  ? 43   ASN A O   1 
ATOM   294   C  CB  . ASN A 1 472  ? 86.237  95.523  128.850 1.00 62.70  ? 43   ASN A CB  1 
ATOM   295   C  CG  . ASN A 1 472  ? 86.931  96.197  130.024 1.00 70.26  ? 43   ASN A CG  1 
ATOM   296   O  OD1 . ASN A 1 472  ? 87.416  97.328  129.909 1.00 59.95  ? 43   ASN A OD1 1 
ATOM   297   N  ND2 . ASN A 1 472  ? 86.990  95.502  131.159 1.00 74.42  ? 43   ASN A ND2 1 
ATOM   298   N  N   . CYS A 1 473  ? 86.759  98.347  126.604 1.00 44.50  ? 44   CYS A N   1 
ATOM   299   C  CA  . CYS A 1 473  ? 86.138  99.616  126.278 1.00 42.13  ? 44   CYS A CA  1 
ATOM   300   C  C   . CYS A 1 473  ? 85.264  99.466  125.043 1.00 44.40  ? 44   CYS A C   1 
ATOM   301   O  O   . CYS A 1 473  ? 85.358  98.492  124.299 1.00 51.21  ? 44   CYS A O   1 
ATOM   302   C  CB  . CYS A 1 473  ? 87.190  100.684 126.020 1.00 54.39  ? 44   CYS A CB  1 
ATOM   303   S  SG  . CYS A 1 473  ? 88.011  100.465 124.408 1.00 71.95  ? 44   CYS A SG  1 
ATOM   304   N  N   . LYS A 1 474  ? 84.411  100.452 124.821 1.00 46.46  ? 45   LYS A N   1 
ATOM   305   C  CA  . LYS A 1 474  ? 83.550  100.409 123.654 1.00 40.75  ? 45   LYS A CA  1 
ATOM   306   C  C   . LYS A 1 474  ? 84.360  100.726 122.409 1.00 42.95  ? 45   LYS A C   1 
ATOM   307   O  O   . LYS A 1 474  ? 85.139  101.682 122.393 1.00 50.24  ? 45   LYS A O   1 
ATOM   308   C  CB  . LYS A 1 474  ? 82.414  101.399 123.817 1.00 56.80  ? 45   LYS A CB  1 
ATOM   309   C  CG  . LYS A 1 474  ? 81.326  101.256 122.790 1.00 68.27  ? 45   LYS A CG  1 
ATOM   310   C  CD  . LYS A 1 474  ? 80.215  102.270 123.067 1.00 84.13  ? 45   LYS A CD  1 
ATOM   311   C  CE  . LYS A 1 474  ? 79.021  102.062 122.146 1.00 90.25  ? 45   LYS A CE  1 
ATOM   312   N  NZ  . LYS A 1 474  ? 79.401  102.145 120.703 1.00 85.13  ? 45   LYS A NZ  1 
ATOM   313   N  N   . LEU A 1 475  ? 84.186  99.917  121.371 1.00 43.63  ? 46   LEU A N   1 
ATOM   314   C  CA  . LEU A 1 475  ? 84.976  100.070 120.157 1.00 40.60  ? 46   LEU A CA  1 
ATOM   315   C  C   . LEU A 1 475  ? 84.645  101.381 119.461 1.00 37.22  ? 46   LEU A C   1 
ATOM   316   O  O   . LEU A 1 475  ? 83.479  101.764 119.388 1.00 54.15  ? 46   LEU A O   1 
ATOM   317   C  CB  . LEU A 1 475  ? 84.708  98.914  119.212 1.00 46.67  ? 46   LEU A CB  1 
ATOM   318   C  CG  . LEU A 1 475  ? 85.629  97.741  119.493 1.00 51.83  ? 46   LEU A CG  1 
ATOM   319   C  CD1 . LEU A 1 475  ? 85.247  96.525  118.643 1.00 52.47  ? 46   LEU A CD1 1 
ATOM   320   C  CD2 . LEU A 1 475  ? 87.043  98.224  119.183 1.00 50.92  ? 46   LEU A CD2 1 
ATOM   321   N  N   . PRO A 1 476  ? 85.637  102.100 118.968 1.00 32.36  ? 47   PRO A N   1 
ATOM   322   C  CA  . PRO A 1 476  ? 85.345  103.287 118.172 1.00 36.61  ? 47   PRO A CA  1 
ATOM   323   C  C   . PRO A 1 476  ? 84.565  102.879 116.944 1.00 55.22  ? 47   PRO A C   1 
ATOM   324   O  O   . PRO A 1 476  ? 84.814  101.820 116.365 1.00 62.25  ? 47   PRO A O   1 
ATOM   325   C  CB  . PRO A 1 476  ? 86.730  103.825 117.803 1.00 41.53  ? 47   PRO A CB  1 
ATOM   326   C  CG  . PRO A 1 476  ? 87.616  103.292 118.834 1.00 55.41  ? 47   PRO A CG  1 
ATOM   327   C  CD  . PRO A 1 476  ? 87.071  101.928 119.191 1.00 51.81  ? 47   PRO A CD  1 
ATOM   328   N  N   . LYS A 1 477  ? 83.601  103.719 116.547 1.00 64.16  ? 48   LYS A N   1 
ATOM   329   C  CA  . LYS A 1 477  ? 82.774  103.390 115.385 1.00 65.38  ? 48   LYS A CA  1 
ATOM   330   C  C   . LYS A 1 477  ? 83.582  103.374 114.102 1.00 49.99  ? 48   LYS A C   1 
ATOM   331   O  O   . LYS A 1 477  ? 83.192  102.715 113.134 1.00 54.92  ? 48   LYS A O   1 
ATOM   332   C  CB  . LYS A 1 477  ? 81.598  104.370 115.243 1.00 79.45  ? 48   LYS A CB  1 
ATOM   333   C  CG  . LYS A 1 477  ? 80.778  104.586 116.524 1.00 91.69  ? 48   LYS A CG  1 
ATOM   334   C  CD  . LYS A 1 477  ? 80.303  103.249 117.138 1.00 95.65  ? 48   LYS A CD  1 
ATOM   335   C  CE  . LYS A 1 477  ? 79.302  102.489 116.250 1.00 91.00  ? 48   LYS A CE  1 
ATOM   336   N  NZ  . LYS A 1 477  ? 78.861  101.196 116.875 1.00 80.89  ? 48   LYS A NZ  1 
ATOM   337   N  N   . HIS A 1 478  ? 84.704  104.067 114.084 1.00 51.00  ? 49   HIS A N   1 
ATOM   338   C  CA  . HIS A 1 478  ? 85.550  104.022 112.912 1.00 58.38  ? 49   HIS A CA  1 
ATOM   339   C  C   . HIS A 1 478  ? 86.015  102.604 112.612 1.00 54.95  ? 49   HIS A C   1 
ATOM   340   O  O   . HIS A 1 478  ? 85.977  102.165 111.459 1.00 62.37  ? 49   HIS A O   1 
ATOM   341   C  CB  . HIS A 1 478  ? 86.744  104.941 113.121 1.00 69.04  ? 49   HIS A CB  1 
ATOM   342   C  CG  . HIS A 1 478  ? 87.718  104.870 112.005 1.00 77.07  ? 49   HIS A CG  1 
ATOM   343   N  ND1 . HIS A 1 478  ? 88.762  103.971 111.990 1.00 77.92  ? 49   HIS A ND1 1 
ATOM   344   C  CD2 . HIS A 1 478  ? 87.763  105.527 110.823 1.00 95.49  ? 49   HIS A CD2 1 
ATOM   345   C  CE1 . HIS A 1 478  ? 89.433  104.103 110.860 1.00 93.70  ? 49   HIS A CE1 1 
ATOM   346   N  NE2 . HIS A 1 478  ? 88.847  105.040 110.134 1.00 104.05 ? 49   HIS A NE2 1 
ATOM   347   N  N   . ILE A 1 479  ? 86.466  101.873 113.636 1.00 59.24  ? 50   ILE A N   1 
ATOM   348   C  CA  . ILE A 1 479  ? 87.043  100.541 113.449 1.00 55.41  ? 50   ILE A CA  1 
ATOM   349   C  C   . ILE A 1 479  ? 86.108  99.433  113.862 1.00 48.48  ? 50   ILE A C   1 
ATOM   350   O  O   . ILE A 1 479  ? 86.454  98.254  113.694 1.00 58.20  ? 50   ILE A O   1 
ATOM   351   C  CB  . ILE A 1 479  ? 88.359  100.351 114.234 1.00 60.88  ? 50   ILE A CB  1 
ATOM   352   C  CG1 . ILE A 1 479  ? 88.109  100.551 115.735 1.00 63.26  ? 50   ILE A CG1 1 
ATOM   353   C  CG2 . ILE A 1 479  ? 89.450  101.260 113.697 1.00 72.48  ? 50   ILE A CG2 1 
ATOM   354   C  CD1 . ILE A 1 479  ? 89.361  100.478 116.591 1.00 59.14  ? 50   ILE A CD1 1 
ATOM   355   N  N   . TYR A 1 480  ? 84.964  99.752  114.432 1.00 44.09  ? 51   TYR A N   1 
ATOM   356   C  CA  . TYR A 1 480  ? 84.002  98.703  114.644 1.00 38.97  ? 51   TYR A CA  1 
ATOM   357   C  C   . TYR A 1 480  ? 83.554  98.118  113.329 1.00 45.85  ? 51   TYR A C   1 
ATOM   358   O  O   . TYR A 1 480  ? 83.113  96.969  113.291 1.00 59.59  ? 51   TYR A O   1 
ATOM   359   C  CB  . TYR A 1 480  ? 82.818  99.248  115.414 1.00 51.88  ? 51   TYR A CB  1 
ATOM   360   C  CG  . TYR A 1 480  ? 81.657  98.307  115.491 1.00 59.16  ? 51   TYR A CG  1 
ATOM   361   C  CD1 . TYR A 1 480  ? 81.635  97.278  116.417 1.00 62.13  ? 51   TYR A CD1 1 
ATOM   362   C  CD2 . TYR A 1 480  ? 80.559  98.467  114.661 1.00 69.78  ? 51   TYR A CD2 1 
ATOM   363   C  CE1 . TYR A 1 480  ? 80.559  96.421  116.500 1.00 69.70  ? 51   TYR A CE1 1 
ATOM   364   C  CE2 . TYR A 1 480  ? 79.474  97.613  114.736 1.00 72.07  ? 51   TYR A CE2 1 
ATOM   365   C  CZ  . TYR A 1 480  ? 79.478  96.593  115.657 1.00 73.00  ? 51   TYR A CZ  1 
ATOM   366   O  OH  . TYR A 1 480  ? 78.398  95.741  115.733 1.00 74.37  ? 51   TYR A OH  1 
ATOM   367   N  N   . ARG A 1 481  ? 83.686  98.864  112.244 1.00 45.64  ? 52   ARG A N   1 
ATOM   368   C  CA  . ARG A 1 481  ? 83.175  98.370  110.982 1.00 50.58  ? 52   ARG A CA  1 
ATOM   369   C  C   . ARG A 1 481  ? 84.060  97.300  110.367 1.00 55.71  ? 52   ARG A C   1 
ATOM   370   O  O   . ARG A 1 481  ? 83.641  96.671  109.389 1.00 65.07  ? 52   ARG A O   1 
ATOM   371   C  CB  . ARG A 1 481  ? 82.994  99.518  109.984 1.00 60.72  ? 52   ARG A CB  1 
ATOM   372   C  CG  . ARG A 1 481  ? 84.290  100.157 109.496 1.00 70.90  ? 52   ARG A CG  1 
ATOM   373   C  CD  . ARG A 1 481  ? 84.051  101.049 108.258 1.00 83.29  ? 52   ARG A CD  1 
ATOM   374   N  NE  . ARG A 1 481  ? 85.299  101.612 107.732 1.00 93.19  ? 52   ARG A NE  1 
ATOM   375   C  CZ  . ARG A 1 481  ? 85.415  102.289 106.586 1.00 102.08 ? 52   ARG A CZ  1 
ATOM   376   N  NH1 . ARG A 1 481  ? 84.355  102.500 105.809 1.00 100.08 ? 52   ARG A NH1 1 
ATOM   377   N  NH2 . ARG A 1 481  ? 86.606  102.745 106.207 1.00 100.23 ? 52   ARG A NH2 1 
ATOM   378   N  N   . LEU A 1 482  ? 85.258  97.068  110.903 1.00 48.77  ? 53   LEU A N   1 
ATOM   379   C  CA  . LEU A 1 482  ? 86.107  96.031  110.334 1.00 42.91  ? 53   LEU A CA  1 
ATOM   380   C  C   . LEU A 1 482  ? 85.397  94.692  110.317 1.00 54.48  ? 53   LEU A C   1 
ATOM   381   O  O   . LEU A 1 482  ? 85.652  93.863  109.436 1.00 60.89  ? 53   LEU A O   1 
ATOM   382   C  CB  . LEU A 1 482  ? 87.388  95.902  111.128 1.00 40.32  ? 53   LEU A CB  1 
ATOM   383   C  CG  . LEU A 1 482  ? 88.339  97.002  110.766 1.00 43.19  ? 53   LEU A CG  1 
ATOM   384   C  CD1 . LEU A 1 482  ? 89.477  97.007  111.766 1.00 52.24  ? 53   LEU A CD1 1 
ATOM   385   C  CD2 . LEU A 1 482  ? 88.799  96.715  109.386 1.00 50.84  ? 53   LEU A CD2 1 
ATOM   386   N  N   . LYS A 1 483  ? 84.509  94.454  111.281 1.00 49.75  ? 54   LYS A N   1 
ATOM   387   C  CA  . LYS A 1 483  ? 83.804  93.190  111.258 1.00 57.08  ? 54   LYS A CA  1 
ATOM   388   C  C   . LYS A 1 483  ? 82.836  93.115  110.086 1.00 57.49  ? 54   LYS A C   1 
ATOM   389   O  O   . LYS A 1 483  ? 82.517  92.011  109.635 1.00 63.16  ? 54   LYS A O   1 
ATOM   390   C  CB  . LYS A 1 483  ? 83.085  92.942  112.590 1.00 66.88  ? 54   LYS A CB  1 
ATOM   391   C  CG  . LYS A 1 483  ? 82.051  93.990  112.969 1.00 80.14  ? 54   LYS A CG  1 
ATOM   392   C  CD  . LYS A 1 483  ? 81.366  93.662  114.301 1.00 85.12  ? 54   LYS A CD  1 
ATOM   393   C  CE  . LYS A 1 483  ? 80.646  92.317  114.238 1.00 86.04  ? 54   LYS A CE  1 
ATOM   394   N  NZ  . LYS A 1 483  ? 79.894  92.004  115.487 1.00 88.61  ? 54   LYS A NZ  1 
ATOM   395   N  N   . TYR A 1 484  ? 82.380  94.249  109.565 1.00 53.56  ? 55   TYR A N   1 
ATOM   396   C  CA  . TYR A 1 484  ? 81.538  94.213  108.378 1.00 55.95  ? 55   TYR A CA  1 
ATOM   397   C  C   . TYR A 1 484  ? 82.350  94.171  107.106 1.00 49.54  ? 55   TYR A C   1 
ATOM   398   O  O   . TYR A 1 484  ? 81.785  93.961  106.032 1.00 57.97  ? 55   TYR A O   1 
ATOM   399   C  CB  . TYR A 1 484  ? 80.617  95.428  108.313 1.00 60.55  ? 55   TYR A CB  1 
ATOM   400   C  CG  . TYR A 1 484  ? 79.594  95.432  109.399 1.00 62.30  ? 55   TYR A CG  1 
ATOM   401   C  CD1 . TYR A 1 484  ? 79.328  94.278  110.127 1.00 66.23  ? 55   TYR A CD1 1 
ATOM   402   C  CD2 . TYR A 1 484  ? 78.915  96.592  109.720 1.00 68.53  ? 55   TYR A CD2 1 
ATOM   403   C  CE1 . TYR A 1 484  ? 78.412  94.280  111.149 1.00 74.00  ? 55   TYR A CE1 1 
ATOM   404   C  CE2 . TYR A 1 484  ? 77.989  96.609  110.735 1.00 78.63  ? 55   TYR A CE2 1 
ATOM   405   C  CZ  . TYR A 1 484  ? 77.739  95.450  111.449 1.00 83.64  ? 55   TYR A CZ  1 
ATOM   406   O  OH  . TYR A 1 484  ? 76.807  95.470  112.463 1.00 86.34  ? 55   TYR A OH  1 
ATOM   407   N  N   . ASP A 1 485  ? 83.647  94.390  107.199 1.00 44.27  ? 56   ASP A N   1 
ATOM   408   C  CA  . ASP A 1 485  ? 84.477  94.329  106.017 1.00 43.49  ? 56   ASP A CA  1 
ATOM   409   C  C   . ASP A 1 485  ? 84.573  92.892  105.528 1.00 52.17  ? 56   ASP A C   1 
ATOM   410   O  O   . ASP A 1 485  ? 84.683  91.959  106.327 1.00 57.27  ? 56   ASP A O   1 
ATOM   411   C  CB  . ASP A 1 485  ? 85.863  94.854  106.336 1.00 53.79  ? 56   ASP A CB  1 
ATOM   412   C  CG  . ASP A 1 485  ? 86.634  95.231  105.097 1.00 67.41  ? 56   ASP A CG  1 
ATOM   413   O  OD1 . ASP A 1 485  ? 86.474  94.542  104.059 1.00 66.52  ? 56   ASP A OD1 1 
ATOM   414   O  OD2 . ASP A 1 485  ? 87.417  96.211  105.166 1.00 65.25  ? 56   ASP A OD2 1 
ATOM   415   N  N   . VAL A 1 486  ? 84.529  92.711  104.208 1.00 52.41  ? 57   VAL A N   1 
ATOM   416   C  CA  . VAL A 1 486  ? 84.764  91.394  103.617 1.00 50.62  ? 57   VAL A CA  1 
ATOM   417   C  C   . VAL A 1 486  ? 86.249  91.133  103.393 1.00 54.17  ? 57   VAL A C   1 
ATOM   418   O  O   . VAL A 1 486  ? 86.727  90.023  103.648 1.00 62.50  ? 57   VAL A O   1 
ATOM   419   C  CB  . VAL A 1 486  ? 83.975  91.236  102.305 1.00 63.03  ? 57   VAL A CB  1 
ATOM   420   C  CG1 . VAL A 1 486  ? 84.419  92.280  101.271 1.00 69.14  ? 57   VAL A CG1 1 
ATOM   421   C  CG2 . VAL A 1 486  ? 84.184  89.822  101.749 1.00 66.39  ? 57   VAL A CG2 1 
ATOM   422   N  N   . THR A 1 487  ? 86.997  92.146  102.948 1.00 49.82  ? 58   THR A N   1 
ATOM   423   C  CA  . THR A 1 487  ? 88.414  91.962  102.663 1.00 44.79  ? 58   THR A CA  1 
ATOM   424   C  C   . THR A 1 487  ? 89.172  91.552  103.928 1.00 50.68  ? 58   THR A C   1 
ATOM   425   O  O   . THR A 1 487  ? 90.018  90.648  103.892 1.00 57.79  ? 58   THR A O   1 
ATOM   426   C  CB  . THR A 1 487  ? 88.981  93.249  102.068 1.00 43.93  ? 58   THR A CB  1 
ATOM   427   O  OG1 . THR A 1 487  ? 88.177  93.642  100.951 1.00 50.34  ? 58   THR A OG1 1 
ATOM   428   C  CG2 . THR A 1 487  ? 90.364  93.010  101.534 1.00 42.15  ? 58   THR A CG2 1 
ATOM   429   N  N   . VAL A 1 488  ? 88.846  92.158  105.069 1.00 47.46  ? 59   VAL A N   1 
ATOM   430   C  CA  . VAL A 1 488  ? 89.547  91.816  106.303 1.00 44.75  ? 59   VAL A CA  1 
ATOM   431   C  C   . VAL A 1 488  ? 89.189  90.409  106.765 1.00 49.22  ? 59   VAL A C   1 
ATOM   432   O  O   . VAL A 1 488  ? 90.058  89.652  107.221 1.00 60.52  ? 59   VAL A O   1 
ATOM   433   C  CB  . VAL A 1 488  ? 89.255  92.862  107.390 1.00 58.31  ? 59   VAL A CB  1 
ATOM   434   C  CG1 . VAL A 1 488  ? 90.006  92.518  108.667 1.00 60.03  ? 59   VAL A CG1 1 
ATOM   435   C  CG2 . VAL A 1 488  ? 89.671  94.248  106.901 1.00 61.35  ? 59   VAL A CG2 1 
ATOM   436   N  N   . THR A 1 489  ? 87.916  90.033  106.675 1.00 43.06  ? 60   THR A N   1 
ATOM   437   C  CA  . THR A 1 489  ? 87.539  88.688  107.085 1.00 34.82  ? 60   THR A CA  1 
ATOM   438   C  C   . THR A 1 489  ? 88.209  87.640  106.219 1.00 45.56  ? 60   THR A C   1 
ATOM   439   O  O   . THR A 1 489  ? 88.708  86.628  106.729 1.00 57.17  ? 60   THR A O   1 
ATOM   440   C  CB  . THR A 1 489  ? 86.038  88.515  107.017 1.00 44.26  ? 60   THR A CB  1 
ATOM   441   O  OG1 . THR A 1 489  ? 85.425  89.425  107.937 1.00 57.96  ? 60   THR A OG1 1 
ATOM   442   C  CG2 . THR A 1 489  ? 85.663  87.078  107.379 1.00 46.12  ? 60   THR A CG2 1 
ATOM   443   N  N   . LYS A 1 490  ? 88.240  87.859  104.906 1.00 45.15  ? 61   LYS A N   1 
ATOM   444   C  CA  . LYS A 1 490  ? 88.880  86.881  104.034 1.00 46.84  ? 61   LYS A CA  1 
ATOM   445   C  C   . LYS A 1 490  ? 90.381  86.843  104.255 1.00 45.89  ? 61   LYS A C   1 
ATOM   446   O  O   . LYS A 1 490  ? 91.014  85.805  104.044 1.00 54.14  ? 61   LYS A O   1 
ATOM   447   C  CB  . LYS A 1 490  ? 88.575  87.197  102.578 1.00 59.26  ? 61   LYS A CB  1 
ATOM   448   C  CG  . LYS A 1 490  ? 89.087  86.153  101.603 1.00 81.24  ? 61   LYS A CG  1 
ATOM   449   C  CD  . LYS A 1 490  ? 88.698  86.515  100.164 1.00 104.10 ? 61   LYS A CD  1 
ATOM   450   C  CE  . LYS A 1 490  ? 87.170  86.513  99.938  1.00 105.76 ? 61   LYS A CE  1 
ATOM   451   N  NZ  . LYS A 1 490  ? 86.510  85.177  100.125 1.00 99.82  ? 61   LYS A NZ  1 
ATOM   452   N  N   . PHE A 1 491  ? 90.964  87.958  104.682 1.00 45.64  ? 62   PHE A N   1 
ATOM   453   C  CA  . PHE A 1 491  ? 92.389  87.979  104.979 1.00 39.84  ? 62   PHE A CA  1 
ATOM   454   C  C   . PHE A 1 491  ? 92.719  87.161  106.210 1.00 41.03  ? 62   PHE A C   1 
ATOM   455   O  O   . PHE A 1 491  ? 93.631  86.330  106.188 1.00 52.18  ? 62   PHE A O   1 
ATOM   456   C  CB  . PHE A 1 491  ? 92.832  89.410  105.181 1.00 44.57  ? 62   PHE A CB  1 
ATOM   457   C  CG  . PHE A 1 491  ? 94.269  89.556  105.399 1.00 31.62  ? 62   PHE A CG  1 
ATOM   458   C  CD1 . PHE A 1 491  ? 95.135  89.351  104.371 1.00 31.96  ? 62   PHE A CD1 1 
ATOM   459   C  CD2 . PHE A 1 491  ? 94.750  89.947  106.618 1.00 43.45  ? 62   PHE A CD2 1 
ATOM   460   C  CE1 . PHE A 1 491  ? 96.469  89.510  104.535 1.00 40.51  ? 62   PHE A CE1 1 
ATOM   461   C  CE2 . PHE A 1 491  ? 96.102  90.114  106.809 1.00 52.44  ? 62   PHE A CE2 1 
ATOM   462   C  CZ  . PHE A 1 491  ? 96.970  89.896  105.754 1.00 50.21  ? 62   PHE A CZ  1 
ATOM   463   N  N   . LEU A 1 492  ? 91.993  87.381  107.300 1.00 43.22  ? 63   LEU A N   1 
ATOM   464   C  CA  . LEU A 1 492  ? 92.298  86.683  108.542 1.00 55.08  ? 63   LEU A CA  1 
ATOM   465   C  C   . LEU A 1 492  ? 91.470  85.392  108.751 1.00 69.24  ? 63   LEU A C   1 
ATOM   466   O  O   . LEU A 1 492  ? 91.403  84.896  109.885 1.00 71.03  ? 63   LEU A O   1 
ATOM   467   C  CB  . LEU A 1 492  ? 92.143  87.627  109.746 1.00 52.38  ? 63   LEU A CB  1 
ATOM   468   C  CG  . LEU A 1 492  ? 90.826  88.350  110.044 1.00 51.04  ? 63   LEU A CG  1 
ATOM   469   C  CD1 . LEU A 1 492  ? 89.877  87.504  110.864 1.00 54.56  ? 63   LEU A CD1 1 
ATOM   470   C  CD2 . LEU A 1 492  ? 91.134  89.632  110.792 1.00 54.27  ? 63   LEU A CD2 1 
ATOM   471   N  N   . SER A 1 493  ? 90.856  84.826  107.697 1.00 61.60  ? 64   SER A N   1 
ATOM   472   C  CA  . SER A 1 493  ? 90.113  83.575  107.874 1.00 52.04  ? 64   SER A CA  1 
ATOM   473   C  C   . SER A 1 493  ? 91.029  82.422  108.258 1.00 52.02  ? 64   SER A C   1 
ATOM   474   O  O   . SER A 1 493  ? 90.666  81.594  109.099 1.00 63.02  ? 64   SER A O   1 
ATOM   475   C  CB  . SER A 1 493  ? 89.355  83.204  106.605 1.00 60.03  ? 64   SER A CB  1 
ATOM   476   O  OG  . SER A 1 493  ? 90.272  82.903  105.568 1.00 62.59  ? 64   SER A OG  1 
ATOM   477   N  N   . ASP A 1 494  ? 92.213  82.339  107.647 1.00 51.04  ? 65   ASP A N   1 
ATOM   478   C  CA  . ASP A 1 494  ? 93.154  81.241  107.871 1.00 57.14  ? 65   ASP A CA  1 
ATOM   479   C  C   . ASP A 1 494  ? 94.237  81.568  108.905 1.00 61.77  ? 65   ASP A C   1 
ATOM   480   O  O   . ASP A 1 494  ? 95.367  81.076  108.797 1.00 58.30  ? 65   ASP A O   1 
ATOM   481   C  CB  . ASP A 1 494  ? 93.806  80.843  106.550 1.00 66.48  ? 65   ASP A CB  1 
ATOM   482   C  CG  . ASP A 1 494  ? 94.587  81.999  105.916 1.00 78.04  ? 65   ASP A CG  1 
ATOM   483   O  OD1 . ASP A 1 494  ? 94.226  83.177  106.164 1.00 69.86  ? 65   ASP A OD1 1 
ATOM   484   O  OD2 . ASP A 1 494  ? 95.565  81.738  105.178 1.00 77.88  ? 65   ASP A OD2 1 
ATOM   485   N  N   . VAL A 1 495  ? 93.910  82.383  109.907 1.00 64.66  ? 66   VAL A N   1 
ATOM   486   C  CA  . VAL A 1 495  ? 94.836  82.846  110.948 1.00 59.18  ? 66   VAL A CA  1 
ATOM   487   C  C   . VAL A 1 495  ? 94.222  82.589  112.321 1.00 55.26  ? 66   VAL A C   1 
ATOM   488   O  O   . VAL A 1 495  ? 93.007  82.766  112.499 1.00 58.04  ? 66   VAL A O   1 
ATOM   489   C  CB  . VAL A 1 495  ? 95.173  84.343  110.776 1.00 66.09  ? 66   VAL A CB  1 
ATOM   490   C  CG1 . VAL A 1 495  ? 96.245  84.769  111.757 1.00 65.38  ? 66   VAL A CG1 1 
ATOM   491   C  CG2 . VAL A 1 495  ? 95.657  84.642  109.343 1.00 64.71  ? 66   VAL A CG2 1 
ATOM   492   N  N   . PRO A 1 496  ? 95.002  82.189  113.316 1.00 43.85  ? 67   PRO A N   1 
ATOM   493   C  CA  . PRO A 1 496  ? 94.427  81.927  114.629 1.00 41.05  ? 67   PRO A CA  1 
ATOM   494   C  C   . PRO A 1 496  ? 94.043  83.230  115.282 1.00 36.67  ? 67   PRO A C   1 
ATOM   495   O  O   . PRO A 1 496  ? 94.463  84.309  114.869 1.00 46.27  ? 67   PRO A O   1 
ATOM   496   C  CB  . PRO A 1 496  ? 95.565  81.268  115.395 1.00 55.29  ? 67   PRO A CB  1 
ATOM   497   C  CG  . PRO A 1 496  ? 96.790  81.816  114.736 1.00 54.07  ? 67   PRO A CG  1 
ATOM   498   C  CD  . PRO A 1 496  ? 96.447  81.928  113.299 1.00 51.78  ? 67   PRO A CD  1 
ATOM   499   N  N   . VAL A 1 497  ? 93.254  83.110  116.343 1.00 31.76  ? 68   VAL A N   1 
ATOM   500   C  CA  . VAL A 1 497  ? 92.864  84.295  117.079 1.00 24.41  ? 68   VAL A CA  1 
ATOM   501   C  C   . VAL A 1 497  ? 94.071  84.991  117.667 1.00 35.37  ? 68   VAL A C   1 
ATOM   502   O  O   . VAL A 1 497  ? 94.082  86.219  117.791 1.00 46.02  ? 68   VAL A O   1 
ATOM   503   C  CB  . VAL A 1 497  ? 91.853  83.929  118.156 1.00 36.96  ? 68   VAL A CB  1 
ATOM   504   C  CG1 . VAL A 1 497  ? 91.403  85.182  118.888 1.00 45.21  ? 68   VAL A CG1 1 
ATOM   505   C  CG2 . VAL A 1 497  ? 90.666  83.250  117.495 1.00 53.17  ? 68   VAL A CG2 1 
ATOM   506   N  N   . ALA A 1 498  ? 95.115  84.252  118.004 1.00 34.59  ? 69   ALA A N   1 
ATOM   507   C  CA  . ALA A 1 498  ? 96.286  84.895  118.587 1.00 38.73  ? 69   ALA A CA  1 
ATOM   508   C  C   . ALA A 1 498  ? 97.059  85.699  117.545 1.00 29.44  ? 69   ALA A C   1 
ATOM   509   O  O   . ALA A 1 498  ? 97.078  85.368  116.361 1.00 41.75  ? 69   ALA A O   1 
ATOM   510   C  CB  . ALA A 1 498  ? 97.202  83.847  119.224 1.00 53.59  ? 69   ALA A CB  1 
ATOM   511   N  N   . THR A 1 499  ? 97.680  86.772  117.989 1.00 21.99  ? 70   THR A N   1 
ATOM   512   C  CA  . THR A 1 499  ? 98.575  87.526  117.155 1.00 20.99  ? 70   THR A CA  1 
ATOM   513   C  C   . THR A 1 499  ? 99.854  87.736  117.921 1.00 32.44  ? 70   THR A C   1 
ATOM   514   O  O   . THR A 1 499  ? 99.996  87.300  119.060 1.00 46.38  ? 70   THR A O   1 
ATOM   515   C  CB  . THR A 1 499  ? 98.025  88.891  116.836 1.00 29.75  ? 70   THR A CB  1 
ATOM   516   O  OG1 . THR A 1 499  ? 98.060  89.642  118.042 1.00 41.77  ? 70   THR A OG1 1 
ATOM   517   C  CG2 . THR A 1 499  ? 96.597  88.775  116.409 1.00 43.14  ? 70   THR A CG2 1 
ATOM   518   N  N   . LEU A 1 500  ? 100.770 88.477  117.336 1.00 28.89  ? 71   LEU A N   1 
ATOM   519   C  CA  . LEU A 1 500  ? 102.018 88.679  118.041 1.00 30.25  ? 71   LEU A CA  1 
ATOM   520   C  C   . LEU A 1 500  ? 102.402 90.140  118.005 1.00 35.99  ? 71   LEU A C   1 
ATOM   521   O  O   . LEU A 1 500  ? 102.102 90.841  117.034 1.00 43.01  ? 71   LEU A O   1 
ATOM   522   C  CB  . LEU A 1 500  ? 103.139 87.849  117.402 1.00 40.17  ? 71   LEU A CB  1 
ATOM   523   C  CG  . LEU A 1 500  ? 102.986 86.335  117.415 1.00 44.60  ? 71   LEU A CG  1 
ATOM   524   C  CD1 . LEU A 1 500  ? 104.195 85.711  116.771 1.00 43.85  ? 71   LEU A CD1 1 
ATOM   525   C  CD2 . LEU A 1 500  ? 102.862 85.859  118.838 1.00 51.75  ? 71   LEU A CD2 1 
ATOM   526   N  N   . PRO A 1 501  ? 103.072 90.620  119.040 1.00 34.49  ? 72   PRO A N   1 
ATOM   527   C  CA  . PRO A 1 501  ? 103.490 92.014  119.036 1.00 34.47  ? 72   PRO A CA  1 
ATOM   528   C  C   . PRO A 1 501  ? 104.436 92.309  117.887 1.00 29.27  ? 72   PRO A C   1 
ATOM   529   O  O   . PRO A 1 501  ? 105.262 91.476  117.501 1.00 33.62  ? 72   PRO A O   1 
ATOM   530   C  CB  . PRO A 1 501  ? 104.143 92.206  120.403 1.00 39.31  ? 72   PRO A CB  1 
ATOM   531   C  CG  . PRO A 1 501  ? 104.446 90.840  120.863 1.00 40.59  ? 72   PRO A CG  1 
ATOM   532   C  CD  . PRO A 1 501  ? 103.389 89.957  120.294 1.00 41.33  ? 72   PRO A CD  1 
ATOM   533   N  N   . ILE A 1 502  ? 104.256 93.492  117.280 1.00 31.22  ? 73   ILE A N   1 
ATOM   534   C  CA  . ILE A 1 502  ? 105.055 93.833  116.094 1.00 26.34  ? 73   ILE A CA  1 
ATOM   535   C  C   . ILE A 1 502  ? 106.479 94.210  116.460 1.00 34.52  ? 73   ILE A C   1 
ATOM   536   O  O   . ILE A 1 502  ? 107.319 94.292  115.592 1.00 46.87  ? 73   ILE A O   1 
ATOM   537   C  CB  . ILE A 1 502  ? 104.396 94.978  115.299 1.00 36.40  ? 73   ILE A CB  1 
ATOM   538   C  CG1 . ILE A 1 502  ? 105.035 95.049  113.964 1.00 40.14  ? 73   ILE A CG1 1 
ATOM   539   C  CG2 . ILE A 1 502  ? 104.857 96.313  115.907 1.00 49.30  ? 73   ILE A CG2 1 
ATOM   540   C  CD1 . ILE A 1 502  ? 104.782 93.924  113.125 1.00 46.82  ? 73   ILE A CD1 1 
ATOM   541   N  N   . ASP A 1 503  ? 106.734 94.382  117.733 1.00 37.64  ? 74   ASP A N   1 
ATOM   542   C  CA  . ASP A 1 503  ? 108.096 94.505  118.221 1.00 49.68  ? 74   ASP A CA  1 
ATOM   543   C  C   . ASP A 1 503  ? 109.012 93.340  117.780 1.00 43.59  ? 74   ASP A C   1 
ATOM   544   O  O   . ASP A 1 503  ? 110.160 93.535  117.317 1.00 42.99  ? 74   ASP A O   1 
ATOM   545   C  CB  . ASP A 1 503  ? 108.097 94.545  119.754 1.00 58.51  ? 74   ASP A CB  1 
ATOM   546   C  CG  . ASP A 1 503  ? 107.542 95.834  120.310 1.00 69.24  ? 74   ASP A CG  1 
ATOM   547   O  OD1 . ASP A 1 503  ? 108.080 96.896  119.920 1.00 65.93  ? 74   ASP A OD1 1 
ATOM   548   O  OD2 . ASP A 1 503  ? 106.584 95.803  121.119 1.00 68.77  ? 74   ASP A OD2 1 
ATOM   549   N  N   . PHE A 1 504  ? 108.515 92.129  117.922 1.00 33.76  ? 75   PHE A N   1 
ATOM   550   C  CA  . PHE A 1 504  ? 109.274 90.950  117.593 1.00 25.92  ? 75   PHE A CA  1 
ATOM   551   C  C   . PHE A 1 504  ? 109.211 90.629  116.125 1.00 38.75  ? 75   PHE A C   1 
ATOM   552   O  O   . PHE A 1 504  ? 110.085 89.914  115.624 1.00 48.69  ? 75   PHE A O   1 
ATOM   553   C  CB  . PHE A 1 504  ? 108.765 89.783  118.399 1.00 26.44  ? 75   PHE A CB  1 
ATOM   554   C  CG  . PHE A 1 504  ? 108.889 90.004  119.836 1.00 31.39  ? 75   PHE A CG  1 
ATOM   555   C  CD1 . PHE A 1 504  ? 107.999 90.819  120.500 1.00 37.56  ? 75   PHE A CD1 1 
ATOM   556   C  CD2 . PHE A 1 504  ? 109.858 89.363  120.548 1.00 42.37  ? 75   PHE A CD2 1 
ATOM   557   C  CE1 . PHE A 1 504  ? 108.119 91.048  121.845 1.00 37.26  ? 75   PHE A CE1 1 
ATOM   558   C  CE2 . PHE A 1 504  ? 109.974 89.559  121.897 1.00 46.54  ? 75   PHE A CE2 1 
ATOM   559   C  CZ  . PHE A 1 504  ? 109.097 90.405  122.549 1.00 41.94  ? 75   PHE A CZ  1 
ATOM   560   N  N   . ILE A 1 505  ? 108.206 91.130  115.419 1.00 34.75  ? 76   ILE A N   1 
ATOM   561   C  CA  . ILE A 1 505  ? 108.094 90.799  114.011 1.00 27.06  ? 76   ILE A CA  1 
ATOM   562   C  C   . ILE A 1 505  ? 108.809 91.805  113.140 1.00 27.15  ? 76   ILE A C   1 
ATOM   563   O  O   . ILE A 1 505  ? 109.037 91.534  111.958 1.00 40.57  ? 76   ILE A O   1 
ATOM   564   C  CB  . ILE A 1 505  ? 106.641 90.696  113.531 1.00 31.62  ? 76   ILE A CB  1 
ATOM   565   C  CG1 . ILE A 1 505  ? 105.767 90.016  114.580 1.00 40.82  ? 76   ILE A CG1 1 
ATOM   566   C  CG2 . ILE A 1 505  ? 106.570 89.863  112.285 1.00 48.25  ? 76   ILE A CG2 1 
ATOM   567   C  CD1 . ILE A 1 505  ? 106.227 88.620  114.933 1.00 44.03  ? 76   ILE A CD1 1 
ATOM   568   N  N   . VAL A 1 506  ? 109.140 92.972  113.658 1.00 29.17  ? 77   VAL A N   1 
ATOM   569   C  CA  . VAL A 1 506  ? 109.790 93.963  112.822 1.00 28.01  ? 77   VAL A CA  1 
ATOM   570   C  C   . VAL A 1 506  ? 111.084 93.413  112.273 1.00 28.79  ? 77   VAL A C   1 
ATOM   571   O  O   . VAL A 1 506  ? 111.330 93.574  111.073 1.00 46.89  ? 77   VAL A O   1 
ATOM   572   C  CB  . VAL A 1 506  ? 109.946 95.292  113.575 1.00 46.77  ? 77   VAL A CB  1 
ATOM   573   C  CG1 . VAL A 1 506  ? 111.040 96.135  112.931 1.00 56.50  ? 77   VAL A CG1 1 
ATOM   574   C  CG2 . VAL A 1 506  ? 108.625 96.097  113.498 1.00 52.42  ? 77   VAL A CG2 1 
ATOM   575   N  N   . PRO A 1 507  ? 111.926 92.738  113.041 1.00 28.20  ? 78   PRO A N   1 
ATOM   576   C  CA  . PRO A 1 507  ? 113.160 92.184  112.457 1.00 36.86  ? 78   PRO A CA  1 
ATOM   577   C  C   . PRO A 1 507  ? 112.913 91.109  111.422 1.00 39.17  ? 78   PRO A C   1 
ATOM   578   O  O   . PRO A 1 507  ? 113.709 90.965  110.484 1.00 44.51  ? 78   PRO A O   1 
ATOM   579   C  CB  . PRO A 1 507  ? 113.889 91.593  113.660 1.00 43.25  ? 78   PRO A CB  1 
ATOM   580   C  CG  . PRO A 1 507  ? 112.831 91.400  114.656 1.00 47.32  ? 78   PRO A CG  1 
ATOM   581   C  CD  . PRO A 1 507  ? 111.873 92.529  114.479 1.00 39.05  ? 78   PRO A CD  1 
ATOM   582   N  N   . VAL A 1 508  ? 111.850 90.325  111.583 1.00 35.90  ? 79   VAL A N   1 
ATOM   583   C  CA  . VAL A 1 508  ? 111.490 89.346  110.563 1.00 29.30  ? 79   VAL A CA  1 
ATOM   584   C  C   . VAL A 1 508  ? 111.136 90.044  109.251 1.00 33.61  ? 79   VAL A C   1 
ATOM   585   O  O   . VAL A 1 508  ? 111.647 89.695  108.184 1.00 45.76  ? 79   VAL A O   1 
ATOM   586   C  CB  . VAL A 1 508  ? 110.333 88.474  111.067 1.00 33.04  ? 79   VAL A CB  1 
ATOM   587   C  CG1 . VAL A 1 508  ? 109.857 87.558  109.966 1.00 59.28  ? 79   VAL A CG1 1 
ATOM   588   C  CG2 . VAL A 1 508  ? 110.755 87.691  112.301 1.00 39.93  ? 79   VAL A CG2 1 
ATOM   589   N  N   . LEU A 1 509  ? 110.256 91.044  109.311 1.00 36.51  ? 80   LEU A N   1 
ATOM   590   C  CA  . LEU A 1 509  ? 109.877 91.757  108.098 1.00 37.72  ? 80   LEU A CA  1 
ATOM   591   C  C   . LEU A 1 509  ? 111.099 92.361  107.434 1.00 41.69  ? 80   LEU A C   1 
ATOM   592   O  O   . LEU A 1 509  ? 111.192 92.391  106.203 1.00 52.28  ? 80   LEU A O   1 
ATOM   593   C  CB  . LEU A 1 509  ? 108.846 92.855  108.394 1.00 27.23  ? 80   LEU A CB  1 
ATOM   594   C  CG  . LEU A 1 509  ? 107.604 92.414  109.157 1.00 28.01  ? 80   LEU A CG  1 
ATOM   595   C  CD1 . LEU A 1 509  ? 106.846 93.621  109.584 1.00 41.95  ? 80   LEU A CD1 1 
ATOM   596   C  CD2 . LEU A 1 509  ? 106.722 91.480  108.358 1.00 36.01  ? 80   LEU A CD2 1 
ATOM   597   N  N   . LEU A 1 510  ? 112.051 92.848  108.225 1.00 37.07  ? 81   LEU A N   1 
ATOM   598   C  CA  . LEU A 1 510  ? 113.191 93.511  107.612 1.00 42.38  ? 81   LEU A CA  1 
ATOM   599   C  C   . LEU A 1 510  ? 114.080 92.554  106.842 1.00 54.04  ? 81   LEU A C   1 
ATOM   600   O  O   . LEU A 1 510  ? 114.929 93.019  106.075 1.00 63.49  ? 81   LEU A O   1 
ATOM   601   C  CB  . LEU A 1 510  ? 114.018 94.270  108.655 1.00 46.07  ? 81   LEU A CB  1 
ATOM   602   C  CG  . LEU A 1 510  ? 113.698 95.760  108.868 1.00 51.40  ? 81   LEU A CG  1 
ATOM   603   C  CD1 . LEU A 1 510  ? 112.261 96.014  109.291 1.00 54.03  ? 81   LEU A CD1 1 
ATOM   604   C  CD2 . LEU A 1 510  ? 114.674 96.398  109.872 1.00 53.05  ? 81   LEU A CD2 1 
ATOM   605   N  N   . LYS A 1 511  ? 113.898 91.248  107.007 1.00 52.51  ? 82   LYS A N   1 
ATOM   606   C  CA  . LYS A 1 511  ? 114.623 90.238  106.236 1.00 53.70  ? 82   LYS A CA  1 
ATOM   607   C  C   . LYS A 1 511  ? 113.729 89.429  105.303 1.00 51.64  ? 82   LYS A C   1 
ATOM   608   O  O   . LYS A 1 511  ? 114.129 89.138  104.174 1.00 54.36  ? 82   LYS A O   1 
ATOM   609   C  CB  . LYS A 1 511  ? 115.363 89.292  107.191 1.00 55.57  ? 82   LYS A CB  1 
ATOM   610   C  CG  . LYS A 1 511  ? 116.150 88.176  106.537 1.00 66.94  ? 82   LYS A CG  1 
ATOM   611   C  CD  . LYS A 1 511  ? 116.883 87.367  107.608 1.00 76.43  ? 82   LYS A CD  1 
ATOM   612   C  CE  . LYS A 1 511  ? 115.908 86.827  108.666 1.00 79.68  ? 82   LYS A CE  1 
ATOM   613   N  NZ  . LYS A 1 511  ? 114.813 85.953  108.126 1.00 72.44  ? 82   LYS A NZ  1 
ATOM   614   N  N   . ALA A 1 512  ? 112.520 89.062  105.739 1.00 49.43  ? 83   ALA A N   1 
ATOM   615   C  CA  . ALA A 1 512  ? 111.641 88.253  104.902 1.00 44.11  ? 83   ALA A CA  1 
ATOM   616   C  C   . ALA A 1 512  ? 111.121 89.049  103.721 1.00 44.48  ? 83   ALA A C   1 
ATOM   617   O  O   . ALA A 1 512  ? 111.026 88.521  102.611 1.00 55.82  ? 83   ALA A O   1 
ATOM   618   C  CB  . ALA A 1 512  ? 110.472 87.704  105.720 1.00 51.22  ? 83   ALA A CB  1 
ATOM   619   N  N   . LEU A 1 513  ? 110.762 90.308  103.935 1.00 46.26  ? 84   LEU A N   1 
ATOM   620   C  CA  . LEU A 1 513  ? 110.165 91.089  102.859 1.00 51.53  ? 84   LEU A CA  1 
ATOM   621   C  C   . LEU A 1 513  ? 111.198 91.390  101.781 1.00 54.47  ? 84   LEU A C   1 
ATOM   622   O  O   . LEU A 1 513  ? 112.351 91.724  102.073 1.00 54.81  ? 84   LEU A O   1 
ATOM   623   C  CB  . LEU A 1 513  ? 109.558 92.381  103.411 1.00 45.80  ? 84   LEU A CB  1 
ATOM   624   C  CG  . LEU A 1 513  ? 108.178 92.131  104.030 1.00 47.25  ? 84   LEU A CG  1 
ATOM   625   C  CD1 . LEU A 1 513  ? 107.564 93.375  104.601 1.00 49.41  ? 84   LEU A CD1 1 
ATOM   626   C  CD2 . LEU A 1 513  ? 107.254 91.579  102.979 1.00 51.69  ? 84   LEU A CD2 1 
ATOM   627   N  N   . SER A 1 514  ? 110.775 91.236  100.526 1.00 52.25  ? 85   SER A N   1 
ATOM   628   C  CA  . SER A 1 514  ? 111.571 91.553  99.346  1.00 49.55  ? 85   SER A CA  1 
ATOM   629   C  C   . SER A 1 514  ? 110.637 92.166  98.310  1.00 52.89  ? 85   SER A C   1 
ATOM   630   O  O   . SER A 1 514  ? 109.465 92.433  98.589  1.00 60.70  ? 85   SER A O   1 
ATOM   631   C  CB  . SER A 1 514  ? 112.269 90.303  98.807  1.00 63.63  ? 85   SER A CB  1 
ATOM   632   O  OG  . SER A 1 514  ? 111.304 89.340  98.414  1.00 69.53  ? 85   SER A OG  1 
ATOM   633   N  N   . GLY A 1 515  ? 111.135 92.381  97.099  1.00 57.75  ? 86   GLY A N   1 
ATOM   634   C  CA  . GLY A 1 515  ? 110.312 92.925  96.038  1.00 67.18  ? 86   GLY A CA  1 
ATOM   635   C  C   . GLY A 1 515  ? 109.715 91.938  95.048  1.00 70.19  ? 86   GLY A C   1 
ATOM   636   O  O   . GLY A 1 515  ? 109.144 92.373  94.041  1.00 72.77  ? 86   GLY A O   1 
ATOM   637   N  N   . ASN A 1 516  ? 109.811 90.631  95.291  1.00 65.56  ? 87   ASN A N   1 
ATOM   638   C  CA  . ASN A 1 516  ? 109.501 89.675  94.236  1.00 63.08  ? 87   ASN A CA  1 
ATOM   639   C  C   . ASN A 1 516  ? 108.016 89.421  94.050  1.00 65.59  ? 87   ASN A C   1 
ATOM   640   O  O   . ASN A 1 516  ? 107.636 88.827  93.037  1.00 69.68  ? 87   ASN A O   1 
ATOM   641   C  CB  . ASN A 1 516  ? 110.201 88.337  94.495  1.00 75.98  ? 87   ASN A CB  1 
ATOM   642   C  CG  . ASN A 1 516  ? 111.713 88.480  94.636  1.00 83.62  ? 87   ASN A CG  1 
ATOM   643   O  OD1 . ASN A 1 516  ? 112.332 89.326  93.981  1.00 80.85  ? 87   ASN A OD1 1 
ATOM   644   N  ND2 . ASN A 1 516  ? 112.314 87.644  95.487  1.00 74.51  ? 87   ASN A ND2 1 
ATOM   645   N  N   . GLY A 1 517  ? 107.164 89.838  94.981  1.00 70.05  ? 88   GLY A N   1 
ATOM   646   C  CA  . GLY A 1 517  ? 105.745 89.563  94.878  1.00 71.27  ? 88   GLY A CA  1 
ATOM   647   C  C   . GLY A 1 517  ? 104.995 90.611  94.070  1.00 65.20  ? 88   GLY A C   1 
ATOM   648   O  O   . GLY A 1 517  ? 105.575 91.510  93.463  1.00 69.48  ? 88   GLY A O   1 
ATOM   649   N  N   . PHE A 1 518  ? 103.670 90.483  94.073  1.00 56.65  ? 89   PHE A N   1 
ATOM   650   C  CA  . PHE A 1 518  ? 102.816 91.457  93.413  1.00 60.17  ? 89   PHE A CA  1 
ATOM   651   C  C   . PHE A 1 518  ? 102.286 92.479  94.407  1.00 66.19  ? 89   PHE A C   1 
ATOM   652   O  O   . PHE A 1 518  ? 101.723 92.107  95.441  1.00 67.90  ? 89   PHE A O   1 
ATOM   653   C  CB  . PHE A 1 518  ? 101.648 90.771  92.721  1.00 73.97  ? 89   PHE A CB  1 
ATOM   654   C  CG  . PHE A 1 518  ? 100.721 91.732  92.026  1.00 91.80  ? 89   PHE A CG  1 
ATOM   655   C  CD1 . PHE A 1 518  ? 101.081 92.300  90.803  1.00 98.64  ? 89   PHE A CD1 1 
ATOM   656   C  CD2 . PHE A 1 518  ? 99.482  92.062  92.577  1.00 95.66  ? 89   PHE A CD2 1 
ATOM   657   C  CE1 . PHE A 1 518  ? 100.230 93.192  90.141  1.00 99.83  ? 89   PHE A CE1 1 
ATOM   658   C  CE2 . PHE A 1 518  ? 98.620  92.955  91.921  1.00 97.42  ? 89   PHE A CE2 1 
ATOM   659   C  CZ  . PHE A 1 518  ? 98.998  93.519  90.701  1.00 99.54  ? 89   PHE A CZ  1 
ATOM   660   N  N   . CYS A 1 519  ? 102.438 93.765  94.074  1.00 69.53  ? 90   CYS A N   1 
ATOM   661   C  CA  . CYS A 1 519  ? 101.996 94.885  94.903  1.00 65.14  ? 90   CYS A CA  1 
ATOM   662   C  C   . CYS A 1 519  ? 101.080 95.811  94.107  1.00 66.19  ? 90   CYS A C   1 
ATOM   663   O  O   . CYS A 1 519  ? 101.387 96.121  92.946  1.00 75.28  ? 90   CYS A O   1 
ATOM   664   C  CB  . CYS A 1 519  ? 103.211 95.669  95.428  1.00 65.67  ? 90   CYS A CB  1 
ATOM   665   S  SG  . CYS A 1 519  ? 102.822 97.027  96.583  1.00 78.27  ? 90   CYS A SG  1 
ATOM   666   N  N   . PRO A 1 520  ? 99.952  96.265  94.668  1.00 44.28  ? 91   PRO A N   1 
ATOM   667   C  CA  . PRO A 1 520  ? 99.004  97.084  93.893  1.00 42.33  ? 91   PRO A CA  1 
ATOM   668   C  C   . PRO A 1 520  ? 99.432  98.545  93.781  1.00 49.64  ? 91   PRO A C   1 
ATOM   669   O  O   . PRO A 1 520  ? 98.722  99.473  94.192  1.00 57.81  ? 91   PRO A O   1 
ATOM   670   C  CB  . PRO A 1 520  ? 97.704  96.913  94.684  1.00 40.93  ? 91   PRO A CB  1 
ATOM   671   C  CG  . PRO A 1 520  ? 98.132  96.706  96.054  1.00 42.51  ? 91   PRO A CG  1 
ATOM   672   C  CD  . PRO A 1 520  ? 99.395  95.888  95.967  1.00 45.19  ? 91   PRO A CD  1 
ATOM   673   N  N   . VAL A 1 521  ? 100.608 98.755  93.202  1.00 42.09  ? 92   VAL A N   1 
ATOM   674   C  CA  . VAL A 1 521  ? 101.178 100.068 92.952  1.00 26.21  ? 92   VAL A CA  1 
ATOM   675   C  C   . VAL A 1 521  ? 101.709 100.063 91.541  1.00 37.65  ? 92   VAL A C   1 
ATOM   676   O  O   . VAL A 1 521  ? 102.523 99.203  91.186  1.00 46.94  ? 92   VAL A O   1 
ATOM   677   C  CB  . VAL A 1 521  ? 102.306 100.398 93.927  1.00 36.93  ? 92   VAL A CB  1 
ATOM   678   C  CG1 . VAL A 1 521  ? 103.085 101.553 93.399  1.00 45.60  ? 92   VAL A CG1 1 
ATOM   679   C  CG2 . VAL A 1 521  ? 101.727 100.758 95.253  1.00 46.07  ? 92   VAL A CG2 1 
ATOM   680   N  N   . GLU A 1 522  ? 101.262 101.011 90.731  1.00 39.78  ? 93   GLU A N   1 
ATOM   681   C  CA  . GLU A 1 522  ? 101.800 101.086 89.398  1.00 38.56  ? 93   GLU A CA  1 
ATOM   682   C  C   . GLU A 1 522  ? 102.016 102.543 89.049  1.00 34.48  ? 93   GLU A C   1 
ATOM   683   O  O   . GLU A 1 522  ? 101.108 103.363 89.238  1.00 47.14  ? 93   GLU A O   1 
ATOM   684   C  CB  . GLU A 1 522  ? 100.891 100.421 88.375  1.00 45.45  ? 93   GLU A CB  1 
ATOM   685   C  CG  . GLU A 1 522  ? 99.466  100.905 88.448  1.00 60.00  ? 93   GLU A CG  1 
ATOM   686   C  CD  . GLU A 1 522  ? 98.603  100.377 87.306  1.00 83.34  ? 93   GLU A CD  1 
ATOM   687   O  OE1 . GLU A 1 522  ? 99.054  99.454  86.586  1.00 76.96  ? 93   GLU A OE1 1 
ATOM   688   O  OE2 . GLU A 1 522  ? 97.470  100.889 87.132  1.00 84.79  ? 93   GLU A OE2 1 
ATOM   689   N  N   . PRO A 1 523  ? 103.178 102.894 88.545  1.00 27.96  ? 94   PRO A N   1 
ATOM   690   C  CA  . PRO A 1 523  ? 104.284 101.986 88.295  1.00 33.42  ? 94   PRO A CA  1 
ATOM   691   C  C   . PRO A 1 523  ? 105.037 101.647 89.541  1.00 42.70  ? 94   PRO A C   1 
ATOM   692   O  O   . PRO A 1 523  ? 105.155 102.514 90.402  1.00 45.68  ? 94   PRO A O   1 
ATOM   693   C  CB  . PRO A 1 523  ? 105.177 102.784 87.381  1.00 41.69  ? 94   PRO A CB  1 
ATOM   694   C  CG  . PRO A 1 523  ? 104.937 104.176 87.790  1.00 40.82  ? 94   PRO A CG  1 
ATOM   695   C  CD  . PRO A 1 523  ? 103.492 104.262 88.137  1.00 36.87  ? 94   PRO A CD  1 
ATOM   696   N  N   . ARG A 1 524  ? 105.566 100.426 89.623  1.00 43.83  ? 95   ARG A N   1 
ATOM   697   C  CA  . ARG A 1 524  ? 106.338 100.024 90.790  1.00 40.13  ? 95   ARG A CA  1 
ATOM   698   C  C   . ARG A 1 524  ? 107.572 100.894 90.903  1.00 40.12  ? 95   ARG A C   1 
ATOM   699   O  O   . ARG A 1 524  ? 108.123 101.355 89.902  1.00 48.25  ? 95   ARG A O   1 
ATOM   700   C  CB  . ARG A 1 524  ? 106.771 98.564  90.685  1.00 55.04  ? 95   ARG A CB  1 
ATOM   701   C  CG  . ARG A 1 524  ? 105.649 97.556  90.816  1.00 63.15  ? 95   ARG A CG  1 
ATOM   702   C  CD  . ARG A 1 524  ? 105.181 97.501  92.247  1.00 61.00  ? 95   ARG A CD  1 
ATOM   703   N  NE  . ARG A 1 524  ? 106.273 97.138  93.137  1.00 63.42  ? 95   ARG A NE  1 
ATOM   704   C  CZ  . ARG A 1 524  ? 106.542 95.891  93.506  1.00 76.53  ? 95   ARG A CZ  1 
ATOM   705   N  NH1 . ARG A 1 524  ? 105.787 94.894  93.056  1.00 80.09  ? 95   ARG A NH1 1 
ATOM   706   N  NH2 . ARG A 1 524  ? 107.557 95.639  94.330  1.00 74.15  ? 95   ARG A NH2 1 
ATOM   707   N  N   . CYS A 1 525  ? 108.002 101.141 92.131  1.00 40.80  ? 96   CYS A N   1 
ATOM   708   C  CA  . CYS A 1 525  ? 109.226 101.905 92.272  1.00 41.98  ? 96   CYS A CA  1 
ATOM   709   C  C   . CYS A 1 525  ? 110.429 101.150 91.726  1.00 38.23  ? 96   CYS A C   1 
ATOM   710   O  O   . CYS A 1 525  ? 111.471 101.767 91.488  1.00 46.70  ? 96   CYS A O   1 
ATOM   711   C  CB  . CYS A 1 525  ? 109.435 102.315 93.736  1.00 42.65  ? 96   CYS A CB  1 
ATOM   712   S  SG  . CYS A 1 525  ? 108.200 103.545 94.313  1.00 61.76  ? 96   CYS A SG  1 
ATOM   713   N  N   . GLN A 1 526  ? 110.313 99.846  91.499  1.00 36.08  ? 97   GLN A N   1 
ATOM   714   C  CA  . GLN A 1 526  ? 111.469 99.115  90.999  1.00 38.43  ? 97   GLN A CA  1 
ATOM   715   C  C   . GLN A 1 526  ? 111.769 99.468  89.559  1.00 49.74  ? 97   GLN A C   1 
ATOM   716   O  O   . GLN A 1 526  ? 112.929 99.404  89.137  1.00 56.38  ? 97   GLN A O   1 
ATOM   717   C  CB  . GLN A 1 526  ? 111.262 97.615  91.134  1.00 41.69  ? 97   GLN A CB  1 
ATOM   718   C  CG  . GLN A 1 526  ? 110.904 97.207  92.541  1.00 62.69  ? 97   GLN A CG  1 
ATOM   719   C  CD  . GLN A 1 526  ? 110.501 95.741  92.669  1.00 81.52  ? 97   GLN A CD  1 
ATOM   720   O  OE1 . GLN A 1 526  ? 110.235 95.262  93.777  1.00 74.39  ? 97   GLN A OE1 1 
ATOM   721   N  NE2 . GLN A 1 526  ? 110.434 95.030  91.539  1.00 75.01  ? 97   GLN A NE2 1 
ATOM   722   N  N   . GLN A 1 527  ? 110.749 99.829  88.787  1.00 49.17  ? 98   GLN A N   1 
ATOM   723   C  CA  . GLN A 1 527  ? 110.990 100.158 87.390  1.00 46.67  ? 98   GLN A CA  1 
ATOM   724   C  C   . GLN A 1 527  ? 111.903 101.368 87.274  1.00 41.68  ? 98   GLN A C   1 
ATOM   725   O  O   . GLN A 1 527  ? 112.797 101.407 86.421  1.00 44.28  ? 98   GLN A O   1 
ATOM   726   C  CB  . GLN A 1 527  ? 109.671 100.423 86.692  1.00 44.95  ? 98   GLN A CB  1 
ATOM   727   C  CG  . GLN A 1 527  ? 109.822 100.760 85.244  1.00 70.45  ? 98   GLN A CG  1 
ATOM   728   C  CD  . GLN A 1 527  ? 108.565 101.402 84.696  1.00 88.29  ? 98   GLN A CD  1 
ATOM   729   O  OE1 . GLN A 1 527  ? 107.612 101.657 85.441  1.00 76.49  ? 98   GLN A OE1 1 
ATOM   730   N  NE2 . GLN A 1 527  ? 108.543 101.653 83.389  1.00 98.03  ? 98   GLN A NE2 1 
ATOM   731   N  N   . PHE A 1 528  ? 111.709 102.354 88.141  1.00 35.19  ? 99   PHE A N   1 
ATOM   732   C  CA  . PHE A 1 528  ? 112.547 103.528 88.067  1.00 32.46  ? 99   PHE A CA  1 
ATOM   733   C  C   . PHE A 1 528  ? 114.004 103.176 88.201  1.00 32.41  ? 99   PHE A C   1 
ATOM   734   O  O   . PHE A 1 528  ? 114.844 103.919 87.695  1.00 47.06  ? 99   PHE A O   1 
ATOM   735   C  CB  . PHE A 1 528  ? 112.183 104.534 89.155  1.00 37.60  ? 99   PHE A CB  1 
ATOM   736   C  CG  . PHE A 1 528  ? 110.720 104.812 89.255  1.00 36.61  ? 99   PHE A CG  1 
ATOM   737   C  CD1 . PHE A 1 528  ? 109.952 104.915 88.116  1.00 34.69  ? 99   PHE A CD1 1 
ATOM   738   C  CD2 . PHE A 1 528  ? 110.120 104.984 90.483  1.00 33.76  ? 99   PHE A CD2 1 
ATOM   739   C  CE1 . PHE A 1 528  ? 108.630 105.171 88.190  1.00 32.55  ? 99   PHE A CE1 1 
ATOM   740   C  CE2 . PHE A 1 528  ? 108.789 105.243 90.563  1.00 37.07  ? 99   PHE A CE2 1 
ATOM   741   C  CZ  . PHE A 1 528  ? 108.042 105.336 89.410  1.00 37.44  ? 99   PHE A CZ  1 
ATOM   742   N  N   . LEU A 1 529  ? 114.325 102.063 88.844  1.00 29.67  ? 100  LEU A N   1 
ATOM   743   C  CA  . LEU A 1 529  ? 115.714 101.806 89.183  1.00 30.02  ? 100  LEU A CA  1 
ATOM   744   C  C   . LEU A 1 529  ? 116.608 101.969 87.974  1.00 31.61  ? 100  LEU A C   1 
ATOM   745   O  O   . LEU A 1 529  ? 117.600 102.702 88.015  1.00 43.37  ? 100  LEU A O   1 
ATOM   746   C  CB  . LEU A 1 529  ? 115.861 100.408 89.778  1.00 39.28  ? 100  LEU A CB  1 
ATOM   747   C  CG  . LEU A 1 529  ? 117.301 99.953  90.030  1.00 52.00  ? 100  LEU A CG  1 
ATOM   748   C  CD1 . LEU A 1 529  ? 117.943 100.791 91.133  1.00 58.71  ? 100  LEU A CD1 1 
ATOM   749   C  CD2 . LEU A 1 529  ? 117.360 98.467  90.415  1.00 57.99  ? 100  LEU A CD2 1 
ATOM   750   N  N   . ASP A 1 530  ? 116.213 101.372 86.858  1.00 42.40  ? 101  ASP A N   1 
ATOM   751   C  CA  . ASP A 1 530  ? 117.071 101.321 85.677  1.00 51.93  ? 101  ASP A CA  1 
ATOM   752   C  C   . ASP A 1 530  ? 117.512 102.715 85.222  1.00 44.11  ? 101  ASP A C   1 
ATOM   753   O  O   . ASP A 1 530  ? 118.619 102.875 84.694  1.00 45.60  ? 101  ASP A O   1 
ATOM   754   C  CB  . ASP A 1 530  ? 116.325 100.584 84.552  1.00 70.81  ? 101  ASP A CB  1 
ATOM   755   C  CG  . ASP A 1 530  ? 117.223 100.229 83.366  1.00 81.95  ? 101  ASP A CG  1 
ATOM   756   O  OD1 . ASP A 1 530  ? 118.462 100.178 83.544  1.00 73.33  ? 101  ASP A OD1 1 
ATOM   757   O  OD2 . ASP A 1 530  ? 116.676 99.991  82.258  1.00 76.39  ? 101  ASP A OD2 1 
ATOM   758   N  N   . GLU A 1 531  ? 116.679 103.734 85.420  1.00 38.36  ? 102  GLU A N   1 
ATOM   759   C  CA  . GLU A 1 531  ? 117.083 105.075 85.035  1.00 34.72  ? 102  GLU A CA  1 
ATOM   760   C  C   . GLU A 1 531  ? 117.607 105.887 86.201  1.00 39.81  ? 102  GLU A C   1 
ATOM   761   O  O   . GLU A 1 531  ? 118.444 106.768 85.986  1.00 45.67  ? 102  GLU A O   1 
ATOM   762   C  CB  . GLU A 1 531  ? 115.929 105.839 84.369  1.00 49.09  ? 102  GLU A CB  1 
ATOM   763   C  CG  . GLU A 1 531  ? 114.597 105.833 85.131  1.00 54.62  ? 102  GLU A CG  1 
ATOM   764   C  CD  . GLU A 1 531  ? 113.431 106.429 84.320  1.00 58.90  ? 102  GLU A CD  1 
ATOM   765   O  OE1 . GLU A 1 531  ? 113.628 106.746 83.121  1.00 56.04  ? 102  GLU A OE1 1 
ATOM   766   O  OE2 . GLU A 1 531  ? 112.319 106.582 84.888  1.00 54.37  ? 102  GLU A OE2 1 
ATOM   767   N  N   . ILE A 1 532  ? 117.168 105.603 87.432  1.00 37.09  ? 103  ILE A N   1 
ATOM   768   C  CA  . ILE A 1 532  ? 117.781 106.253 88.587  1.00 26.30  ? 103  ILE A CA  1 
ATOM   769   C  C   . ILE A 1 532  ? 119.271 106.027 88.564  1.00 25.82  ? 103  ILE A C   1 
ATOM   770   O  O   . ILE A 1 532  ? 120.062 106.963 88.703  1.00 34.51  ? 103  ILE A O   1 
ATOM   771   C  CB  . ILE A 1 532  ? 117.198 105.718 89.893  1.00 26.12  ? 103  ILE A CB  1 
ATOM   772   C  CG1 . ILE A 1 532  ? 115.760 106.149 90.060  1.00 32.57  ? 103  ILE A CG1 1 
ATOM   773   C  CG2 . ILE A 1 532  ? 118.033 106.203 91.039  1.00 31.74  ? 103  ILE A CG2 1 
ATOM   774   C  CD1 . ILE A 1 532  ? 115.217 105.689 91.361  1.00 35.02  ? 103  ILE A CD1 1 
ATOM   775   N  N   . ILE A 1 533  ? 119.675 104.781 88.358  1.00 28.01  ? 104  ILE A N   1 
ATOM   776   C  CA  . ILE A 1 533  ? 121.090 104.501 88.235  1.00 25.50  ? 104  ILE A CA  1 
ATOM   777   C  C   . ILE A 1 533  ? 121.669 105.259 87.073  1.00 28.77  ? 104  ILE A C   1 
ATOM   778   O  O   . ILE A 1 533  ? 122.712 105.911 87.203  1.00 44.47  ? 104  ILE A O   1 
ATOM   779   C  CB  . ILE A 1 533  ? 121.344 103.002 88.107  1.00 30.11  ? 104  ILE A CB  1 
ATOM   780   C  CG1 . ILE A 1 533  ? 120.715 102.290 89.310  1.00 35.11  ? 104  ILE A CG1 1 
ATOM   781   C  CG2 . ILE A 1 533  ? 122.840 102.776 88.004  1.00 48.82  ? 104  ILE A CG2 1 
ATOM   782   C  CD1 . ILE A 1 533  ? 120.932 100.805 89.329  1.00 47.14  ? 104  ILE A CD1 1 
ATOM   783   N  N   . LYS A 1 534  ? 120.975 105.265 85.946  1.00 28.40  ? 105  LYS A N   1 
ATOM   784   C  CA  . LYS A 1 534  ? 121.506 106.018 84.820  1.00 34.67  ? 105  LYS A CA  1 
ATOM   785   C  C   . LYS A 1 534  ? 121.726 107.477 85.196  1.00 32.81  ? 105  LYS A C   1 
ATOM   786   O  O   . LYS A 1 534  ? 122.688 108.101 84.729  1.00 38.19  ? 105  LYS A O   1 
ATOM   787   C  CB  . LYS A 1 534  ? 120.562 105.889 83.626  1.00 49.16  ? 105  LYS A CB  1 
ATOM   788   C  CG  . LYS A 1 534  ? 121.023 106.580 82.348  1.00 53.93  ? 105  LYS A CG  1 
ATOM   789   C  CD  . LYS A 1 534  ? 119.946 106.422 81.281  1.00 57.62  ? 105  LYS A CD  1 
ATOM   790   C  CE  . LYS A 1 534  ? 120.321 107.093 79.981  1.00 64.41  ? 105  LYS A CE  1 
ATOM   791   N  NZ  . LYS A 1 534  ? 119.212 106.974 78.987  1.00 63.51  ? 105  LYS A NZ  1 
ATOM   792   N  N   . TYR A 1 535  ? 120.883 108.023 86.077  1.00 32.14  ? 106  TYR A N   1 
ATOM   793   C  CA  . TYR A 1 535  ? 121.092 109.393 86.527  1.00 28.70  ? 106  TYR A CA  1 
ATOM   794   C  C   . TYR A 1 535  ? 122.224 109.457 87.526  1.00 29.83  ? 106  TYR A C   1 
ATOM   795   O  O   . TYR A 1 535  ? 123.123 110.291 87.398  1.00 38.82  ? 106  TYR A O   1 
ATOM   796   C  CB  . TYR A 1 535  ? 119.836 109.958 87.163  1.00 30.73  ? 106  TYR A CB  1 
ATOM   797   C  CG  . TYR A 1 535  ? 120.007 111.370 87.622  1.00 25.02  ? 106  TYR A CG  1 
ATOM   798   C  CD1 . TYR A 1 535  ? 120.216 112.381 86.709  1.00 33.73  ? 106  TYR A CD1 1 
ATOM   799   C  CD2 . TYR A 1 535  ? 119.974 111.687 88.948  1.00 26.84  ? 106  TYR A CD2 1 
ATOM   800   C  CE1 . TYR A 1 535  ? 120.367 113.671 87.099  1.00 34.59  ? 106  TYR A CE1 1 
ATOM   801   C  CE2 . TYR A 1 535  ? 120.126 112.981 89.361  1.00 33.78  ? 106  TYR A CE2 1 
ATOM   802   C  CZ  . TYR A 1 535  ? 120.327 113.971 88.430  1.00 36.73  ? 106  TYR A CZ  1 
ATOM   803   O  OH  . TYR A 1 535  ? 120.483 115.277 88.837  1.00 44.37  ? 106  TYR A OH  1 
ATOM   804   N  N   . THR A 1 536  ? 122.202 108.570 88.522  1.00 28.89  ? 107  THR A N   1 
ATOM   805   C  CA  . THR A 1 536  ? 123.232 108.601 89.547  1.00 19.66  ? 107  THR A CA  1 
ATOM   806   C  C   . THR A 1 536  ? 124.584 108.567 88.921  1.00 23.93  ? 107  THR A C   1 
ATOM   807   O  O   . THR A 1 536  ? 125.411 109.449 89.161  1.00 38.93  ? 107  THR A O   1 
ATOM   808   C  CB  . THR A 1 536  ? 123.125 107.417 90.475  1.00 24.99  ? 107  THR A CB  1 
ATOM   809   O  OG1 . THR A 1 536  ? 121.862 107.438 91.151  1.00 36.82  ? 107  THR A OG1 1 
ATOM   810   C  CG2 . THR A 1 536  ? 124.248 107.471 91.451  1.00 31.56  ? 107  THR A CG2 1 
ATOM   811   N  N   . MET A 1 537  ? 124.816 107.588 88.064  1.00 26.61  ? 108  MET A N   1 
ATOM   812   C  CA  . MET A 1 537  ? 126.107 107.538 87.410  1.00 37.98  ? 108  MET A CA  1 
ATOM   813   C  C   . MET A 1 537  ? 126.367 108.839 86.687  1.00 39.84  ? 108  MET A C   1 
ATOM   814   O  O   . MET A 1 537  ? 127.402 109.485 86.911  1.00 48.74  ? 108  MET A O   1 
ATOM   815   C  CB  . MET A 1 537  ? 126.193 106.358 86.465  1.00 42.20  ? 108  MET A CB  1 
ATOM   816   C  CG  . MET A 1 537  ? 126.160 105.053 87.204  1.00 48.47  ? 108  MET A CG  1 
ATOM   817   S  SD  . MET A 1 537  ? 126.901 103.790 86.178  1.00 85.46  ? 108  MET A SD  1 
ATOM   818   C  CE  . MET A 1 537  ? 125.967 104.012 84.653  1.00 73.05  ? 108  MET A CE  1 
ATOM   819   N  N   . GLN A 1 538  ? 125.397 109.307 85.906  1.00 29.00  ? 109  GLN A N   1 
ATOM   820   C  CA  . GLN A 1 538  ? 125.652 110.547 85.185  1.00 31.10  ? 109  GLN A CA  1 
ATOM   821   C  C   . GLN A 1 538  ? 125.983 111.671 86.136  1.00 30.03  ? 109  GLN A C   1 
ATOM   822   O  O   . GLN A 1 538  ? 126.930 112.428 85.895  1.00 41.76  ? 109  GLN A O   1 
ATOM   823   C  CB  . GLN A 1 538  ? 124.479 110.950 84.327  1.00 40.16  ? 109  GLN A CB  1 
ATOM   824   C  CG  . GLN A 1 538  ? 124.801 112.166 83.538  1.00 38.29  ? 109  GLN A CG  1 
ATOM   825   C  CD  . GLN A 1 538  ? 123.698 112.471 82.579  1.00 58.12  ? 109  GLN A CD  1 
ATOM   826   O  OE1 . GLN A 1 538  ? 122.516 112.422 82.941  1.00 57.38  ? 109  GLN A OE1 1 
ATOM   827   N  NE2 . GLN A 1 538  ? 124.061 112.768 81.333  1.00 60.74  ? 109  GLN A NE2 1 
ATOM   828   N  N   . ASP A 1 539  ? 125.268 111.766 87.258  1.00 30.56  ? 110  ASP A N   1 
ATOM   829   C  CA  . ASP A 1 539  ? 125.596 112.842 88.187  1.00 29.17  ? 110  ASP A CA  1 
ATOM   830   C  C   . ASP A 1 539  ? 126.988 112.671 88.762  1.00 29.81  ? 110  ASP A C   1 
ATOM   831   O  O   . ASP A 1 539  ? 127.776 113.625 88.779  1.00 32.43  ? 110  ASP A O   1 
ATOM   832   C  CB  . ASP A 1 539  ? 124.598 112.943 89.314  1.00 24.69  ? 110  ASP A CB  1 
ATOM   833   C  CG  . ASP A 1 539  ? 124.894 114.119 90.183  1.00 37.65  ? 110  ASP A CG  1 
ATOM   834   O  OD1 . ASP A 1 539  ? 124.823 115.257 89.660  1.00 37.18  ? 110  ASP A OD1 1 
ATOM   835   O  OD2 . ASP A 1 539  ? 125.213 113.910 91.377  1.00 41.90  ? 110  ASP A OD2 1 
ATOM   836   N  N   . ALA A 1 540  ? 127.329 111.458 89.192  1.00 29.14  ? 111  ALA A N   1 
ATOM   837   C  CA  . ALA A 1 540  ? 128.694 111.218 89.620  1.00 26.42  ? 111  ALA A CA  1 
ATOM   838   C  C   . ALA A 1 540  ? 129.640 111.715 88.555  1.00 26.80  ? 111  ALA A C   1 
ATOM   839   O  O   . ALA A 1 540  ? 130.595 112.440 88.846  1.00 40.52  ? 111  ALA A O   1 
ATOM   840   C  CB  . ALA A 1 540  ? 128.929 109.733 89.883  1.00 35.99  ? 111  ALA A CB  1 
ATOM   841   N  N   . LEU A 1 541  ? 129.336 111.411 87.300  1.00 25.64  ? 112  LEU A N   1 
ATOM   842   C  CA  . LEU A 1 541  ? 130.247 111.797 86.240  1.00 28.91  ? 112  LEU A CA  1 
ATOM   843   C  C   . LEU A 1 541  ? 130.393 113.308 86.193  1.00 29.79  ? 112  LEU A C   1 
ATOM   844   O  O   . LEU A 1 541  ? 131.514 113.832 86.189  1.00 38.90  ? 112  LEU A O   1 
ATOM   845   C  CB  . LEU A 1 541  ? 129.764 111.250 84.907  1.00 42.09  ? 112  LEU A CB  1 
ATOM   846   C  CG  . LEU A 1 541  ? 130.715 111.519 83.744  1.00 59.52  ? 112  LEU A CG  1 
ATOM   847   C  CD1 . LEU A 1 541  ? 132.050 110.794 83.994  1.00 56.43  ? 112  LEU A CD1 1 
ATOM   848   C  CD2 . LEU A 1 541  ? 130.086 111.115 82.391  1.00 60.62  ? 112  LEU A CD2 1 
ATOM   849   N  N   . PHE A 1 542  ? 129.274 114.029 86.250  1.00 30.12  ? 113  PHE A N   1 
ATOM   850   C  CA  . PHE A 1 542  ? 129.340 115.487 86.332  1.00 31.54  ? 113  PHE A CA  1 
ATOM   851   C  C   . PHE A 1 542  ? 130.251 115.933 87.458  1.00 30.74  ? 113  PHE A C   1 
ATOM   852   O  O   . PHE A 1 542  ? 131.126 116.784 87.262  1.00 34.67  ? 113  PHE A O   1 
ATOM   853   C  CB  . PHE A 1 542  ? 127.944 116.067 86.523  1.00 36.97  ? 113  PHE A CB  1 
ATOM   854   C  CG  . PHE A 1 542  ? 127.924 117.532 86.817  1.00 28.46  ? 113  PHE A CG  1 
ATOM   855   C  CD1 . PHE A 1 542  ? 128.647 118.410 86.056  1.00 30.34  ? 113  PHE A CD1 1 
ATOM   856   C  CD2 . PHE A 1 542  ? 127.113 118.023 87.821  1.00 29.68  ? 113  PHE A CD2 1 
ATOM   857   C  CE1 . PHE A 1 542  ? 128.596 119.757 86.321  1.00 36.20  ? 113  PHE A CE1 1 
ATOM   858   C  CE2 . PHE A 1 542  ? 127.049 119.349 88.083  1.00 30.33  ? 113  PHE A CE2 1 
ATOM   859   C  CZ  . PHE A 1 542  ? 127.786 120.227 87.334  1.00 33.41  ? 113  PHE A CZ  1 
ATOM   860   N  N   . LEU A 1 543  ? 130.064 115.361 88.646  1.00 31.52  ? 114  LEU A N   1 
ATOM   861   C  CA  . LEU A 1 543  ? 130.891 115.786 89.756  1.00 24.11  ? 114  LEU A CA  1 
ATOM   862   C  C   . LEU A 1 543  ? 132.325 115.624 89.376  1.00 23.01  ? 114  LEU A C   1 
ATOM   863   O  O   . LEU A 1 543  ? 133.095 116.588 89.419  1.00 39.69  ? 114  LEU A O   1 
ATOM   864   C  CB  . LEU A 1 543  ? 130.595 114.999 91.019  1.00 25.16  ? 114  LEU A CB  1 
ATOM   865   C  CG  . LEU A 1 543  ? 131.471 115.564 92.110  1.00 24.91  ? 114  LEU A CG  1 
ATOM   866   C  CD1 . LEU A 1 543  ? 131.155 117.028 92.175  1.00 25.06  ? 114  LEU A CD1 1 
ATOM   867   C  CD2 . LEU A 1 543  ? 131.062 114.933 93.406  1.00 34.65  ? 114  LEU A CD2 1 
ATOM   868   N  N   . LYS A 1 544  ? 132.677 114.458 88.863  1.00 20.59  ? 115  LYS A N   1 
ATOM   869   C  CA  . LYS A 1 544  ? 134.064 114.287 88.492  1.00 28.99  ? 115  LYS A CA  1 
ATOM   870   C  C   . LYS A 1 544  ? 134.478 115.339 87.476  1.00 31.69  ? 115  LYS A C   1 
ATOM   871   O  O   . LYS A 1 544  ? 135.521 115.988 87.635  1.00 41.60  ? 115  LYS A O   1 
ATOM   872   C  CB  . LYS A 1 544  ? 134.308 112.891 87.965  1.00 36.46  ? 115  LYS A CB  1 
ATOM   873   C  CG  . LYS A 1 544  ? 135.779 112.629 87.814  1.00 50.78  ? 115  LYS A CG  1 
ATOM   874   C  CD  . LYS A 1 544  ? 136.039 111.155 87.527  1.00 71.63  ? 115  LYS A CD  1 
ATOM   875   C  CE  . LYS A 1 544  ? 135.480 110.253 88.637  1.00 69.89  ? 115  LYS A CE  1 
ATOM   876   N  NZ  . LYS A 1 544  ? 136.082 110.536 89.983  1.00 60.32  ? 115  LYS A NZ  1 
ATOM   877   N  N   . TYR A 1 545  ? 133.623 115.607 86.497  1.00 24.63  ? 116  TYR A N   1 
ATOM   878   C  CA  . TYR A 1 545  ? 133.978 116.593 85.489  1.00 23.89  ? 116  TYR A CA  1 
ATOM   879   C  C   . TYR A 1 545  ? 134.203 117.941 86.119  1.00 19.95  ? 116  TYR A C   1 
ATOM   880   O  O   . TYR A 1 545  ? 135.223 118.587 85.872  1.00 33.71  ? 116  TYR A O   1 
ATOM   881   C  CB  . TYR A 1 545  ? 132.889 116.665 84.432  1.00 34.74  ? 116  TYR A CB  1 
ATOM   882   C  CG  . TYR A 1 545  ? 133.183 117.597 83.294  1.00 31.79  ? 116  TYR A CG  1 
ATOM   883   C  CD1 . TYR A 1 545  ? 133.951 117.187 82.219  1.00 30.30  ? 116  TYR A CD1 1 
ATOM   884   C  CD2 . TYR A 1 545  ? 132.624 118.854 83.258  1.00 35.41  ? 116  TYR A CD2 1 
ATOM   885   C  CE1 . TYR A 1 545  ? 134.199 118.022 81.171  1.00 34.10  ? 116  TYR A CE1 1 
ATOM   886   C  CE2 . TYR A 1 545  ? 132.861 119.699 82.210  1.00 36.82  ? 116  TYR A CE2 1 
ATOM   887   C  CZ  . TYR A 1 545  ? 133.647 119.284 81.169  1.00 43.62  ? 116  TYR A CZ  1 
ATOM   888   O  OH  . TYR A 1 545  ? 133.873 120.151 80.120  1.00 53.07  ? 116  TYR A OH  1 
ATOM   889   N  N   . TYR A 1 546  ? 133.310 118.346 86.991  1.00 19.84  ? 117  TYR A N   1 
ATOM   890   C  CA  . TYR A 1 546  ? 133.502 119.610 87.665  1.00 20.26  ? 117  TYR A CA  1 
ATOM   891   C  C   . TYR A 1 546  ? 134.873 119.657 88.283  1.00 24.64  ? 117  TYR A C   1 
ATOM   892   O  O   . TYR A 1 546  ? 135.659 120.562 88.002  1.00 35.68  ? 117  TYR A O   1 
ATOM   893   C  CB  . TYR A 1 546  ? 132.460 119.740 88.737  1.00 27.94  ? 117  TYR A CB  1 
ATOM   894   C  CG  . TYR A 1 546  ? 132.124 121.116 89.159  1.00 33.62  ? 117  TYR A CG  1 
ATOM   895   C  CD1 . TYR A 1 546  ? 132.826 121.747 90.154  1.00 36.64  ? 117  TYR A CD1 1 
ATOM   896   C  CD2 . TYR A 1 546  ? 131.034 121.765 88.607  1.00 45.92  ? 117  TYR A CD2 1 
ATOM   897   C  CE1 . TYR A 1 546  ? 132.471 123.009 90.569  1.00 41.05  ? 117  TYR A CE1 1 
ATOM   898   C  CE2 . TYR A 1 546  ? 130.668 123.025 89.013  1.00 41.49  ? 117  TYR A CE2 1 
ATOM   899   C  CZ  . TYR A 1 546  ? 131.392 123.642 89.994  1.00 41.23  ? 117  TYR A CZ  1 
ATOM   900   O  OH  . TYR A 1 546  ? 131.028 124.908 90.398  1.00 47.84  ? 117  TYR A OH  1 
ATOM   901   N  N   . LEU A 1 547  ? 135.222 118.629 89.052  1.00 24.91  ? 118  LEU A N   1 
ATOM   902   C  CA  . LEU A 1 547  ? 136.499 118.661 89.746  1.00 22.55  ? 118  LEU A CA  1 
ATOM   903   C  C   . LEU A 1 547  ? 137.655 118.717 88.763  1.00 29.08  ? 118  LEU A C   1 
ATOM   904   O  O   . LEU A 1 547  ? 138.610 119.474 88.971  1.00 40.77  ? 118  LEU A O   1 
ATOM   905   C  CB  . LEU A 1 547  ? 136.613 117.475 90.685  1.00 22.27  ? 118  LEU A CB  1 
ATOM   906   C  CG  . LEU A 1 547  ? 135.541 117.380 91.774  1.00 21.56  ? 118  LEU A CG  1 
ATOM   907   C  CD1 . LEU A 1 547  ? 135.801 116.194 92.670  1.00 31.15  ? 118  LEU A CD1 1 
ATOM   908   C  CD2 . LEU A 1 547  ? 135.559 118.620 92.616  1.00 23.03  ? 118  LEU A CD2 1 
ATOM   909   N  N   . LYS A 1 548  ? 137.550 118.003 87.640  1.00 30.19  ? 119  LYS A N   1 
ATOM   910   C  CA  . LYS A 1 548  ? 138.614 118.061 86.635  1.00 38.26  ? 119  LYS A CA  1 
ATOM   911   C  C   . LYS A 1 548  ? 138.897 119.488 86.157  1.00 45.22  ? 119  LYS A C   1 
ATOM   912   O  O   . LYS A 1 548  ? 140.047 119.804 85.824  1.00 46.37  ? 119  LYS A O   1 
ATOM   913   C  CB  . LYS A 1 548  ? 138.267 117.205 85.416  1.00 43.33  ? 119  LYS A CB  1 
ATOM   914   C  CG  . LYS A 1 548  ? 139.393 117.123 84.372  1.00 47.46  ? 119  LYS A CG  1 
ATOM   915   C  CD  . LYS A 1 548  ? 139.349 115.821 83.581  1.00 55.23  ? 119  LYS A CD  1 
ATOM   916   C  CE  . LYS A 1 548  ? 139.606 114.633 84.485  1.00 69.10  ? 119  LYS A CE  1 
ATOM   917   N  NZ  . LYS A 1 548  ? 140.963 114.700 85.095  1.00 70.20  ? 119  LYS A NZ  1 
ATOM   918   N  N   . ASN A 1 549  ? 137.887 120.362 86.079  1.00 37.42  ? 120  ASN A N   1 
ATOM   919   C  CA  . ASN A 1 549  ? 138.262 121.686 85.612  1.00 38.95  ? 120  ASN A CA  1 
ATOM   920   C  C   . ASN A 1 549  ? 138.570 122.641 86.761  1.00 49.93  ? 120  ASN A C   1 
ATOM   921   O  O   . ASN A 1 549  ? 139.104 123.728 86.512  1.00 54.33  ? 120  ASN A O   1 
ATOM   922   C  CB  . ASN A 1 549  ? 137.200 122.293 84.671  1.00 43.96  ? 120  ASN A CB  1 
ATOM   923   C  CG  . ASN A 1 549  ? 135.913 122.742 85.381  1.00 56.54  ? 120  ASN A CG  1 
ATOM   924   O  OD1 . ASN A 1 549  ? 135.879 122.965 86.591  1.00 51.59  ? 120  ASN A OD1 1 
ATOM   925   N  ND2 . ASN A 1 549  ? 134.843 122.908 84.596  1.00 61.32  ? 120  ASN A ND2 1 
ATOM   926   N  N   . VAL A 1 550  ? 138.265 122.278 88.007  1.00 37.27  ? 121  VAL A N   1 
ATOM   927   C  CA  . VAL A 1 550  ? 138.611 123.187 89.084  1.00 26.16  ? 121  VAL A CA  1 
ATOM   928   C  C   . VAL A 1 550  ? 140.035 122.952 89.512  1.00 30.79  ? 121  VAL A C   1 
ATOM   929   O  O   . VAL A 1 550  ? 140.666 123.855 90.071  1.00 42.85  ? 121  VAL A O   1 
ATOM   930   C  CB  . VAL A 1 550  ? 137.663 123.041 90.280  1.00 35.74  ? 121  VAL A CB  1 
ATOM   931   C  CG1 . VAL A 1 550  ? 137.976 124.072 91.323  1.00 46.81  ? 121  VAL A CG1 1 
ATOM   932   C  CG2 . VAL A 1 550  ? 136.247 123.236 89.836  1.00 45.18  ? 121  VAL A CG2 1 
ATOM   933   N  N   . GLY A 1 551  ? 140.582 121.789 89.217  1.00 37.82  ? 122  GLY A N   1 
ATOM   934   C  CA  . GLY A 1 551  ? 141.910 121.450 89.662  1.00 47.85  ? 122  GLY A CA  1 
ATOM   935   C  C   . GLY A 1 551  ? 141.965 120.572 90.890  1.00 49.57  ? 122  GLY A C   1 
ATOM   936   O  O   . GLY A 1 551  ? 143.044 120.435 91.481  1.00 50.26  ? 122  GLY A O   1 
ATOM   937   N  N   . ALA A 1 552  ? 140.852 119.963 91.288  1.00 36.70  ? 123  ALA A N   1 
ATOM   938   C  CA  . ALA A 1 552  ? 140.803 119.151 92.493  1.00 33.73  ? 123  ALA A CA  1 
ATOM   939   C  C   . ALA A 1 552  ? 140.564 117.682 92.176  1.00 37.08  ? 123  ALA A C   1 
ATOM   940   O  O   . ALA A 1 552  ? 139.819 116.998 92.882  1.00 40.10  ? 123  ALA A O   1 
ATOM   941   C  CB  . ALA A 1 552  ? 139.731 119.676 93.442  1.00 40.63  ? 123  ALA A CB  1 
ATOM   942   N  N   . GLN A 1 553  ? 141.188 117.163 91.118  1.00 41.02  ? 124  GLN A N   1 
ATOM   943   C  CA  . GLN A 1 553  ? 141.010 115.756 90.773  1.00 43.21  ? 124  GLN A CA  1 
ATOM   944   C  C   . GLN A 1 553  ? 142.113 114.930 91.401  1.00 49.13  ? 124  GLN A C   1 
ATOM   945   O  O   . GLN A 1 553  ? 143.281 115.328 91.405  1.00 54.43  ? 124  GLN A O   1 
ATOM   946   C  CB  . GLN A 1 553  ? 140.995 115.513 89.258  1.00 44.40  ? 124  GLN A CB  1 
ATOM   947   C  CG  . GLN A 1 553  ? 142.317 115.691 88.550  1.00 44.68  ? 124  GLN A CG  1 
ATOM   948   C  CD  . GLN A 1 553  ? 142.636 117.150 88.293  1.00 59.56  ? 124  GLN A CD  1 
ATOM   949   O  OE1 . GLN A 1 553  ? 142.277 118.030 89.084  1.00 57.62  ? 124  GLN A OE1 1 
ATOM   950   N  NE2 . GLN A 1 553  ? 143.303 117.422 87.173  1.00 64.66  ? 124  GLN A NE2 1 
ATOM   951   N  N   . GLU A 1 554  ? 141.728 113.782 91.945  1.00 50.86  ? 125  GLU A N   1 
ATOM   952   C  CA  . GLU A 1 554  ? 142.704 112.858 92.492  1.00 49.92  ? 125  GLU A CA  1 
ATOM   953   C  C   . GLU A 1 554  ? 143.699 112.437 91.421  1.00 56.37  ? 125  GLU A C   1 
ATOM   954   O  O   . GLU A 1 554  ? 143.331 112.194 90.269  1.00 64.44  ? 125  GLU A O   1 
ATOM   955   C  CB  . GLU A 1 554  ? 141.989 111.641 93.051  1.00 60.58  ? 125  GLU A CB  1 
ATOM   956   C  CG  . GLU A 1 554  ? 141.418 111.869 94.442  1.00 72.60  ? 125  GLU A CG  1 
ATOM   957   C  CD  . GLU A 1 554  ? 140.563 110.695 94.934  1.00 82.27  ? 125  GLU A CD  1 
ATOM   958   O  OE1 . GLU A 1 554  ? 139.339 110.691 94.650  1.00 78.86  ? 125  GLU A OE1 1 
ATOM   959   O  OE2 . GLU A 1 554  ? 141.113 109.766 95.578  1.00 67.10  ? 125  GLU A OE2 1 
ATOM   960   N  N   . ASP A 1 555  ? 144.969 112.358 91.805  1.00 53.12  ? 126  ASP A N   1 
ATOM   961   C  CA  . ASP A 1 555  ? 145.994 111.927 90.861  1.00 58.69  ? 126  ASP A CA  1 
ATOM   962   C  C   . ASP A 1 555  ? 145.762 110.490 90.406  1.00 72.28  ? 126  ASP A C   1 
ATOM   963   O  O   . ASP A 1 555  ? 145.852 110.180 89.212  1.00 76.68  ? 126  ASP A O   1 
ATOM   964   C  CB  . ASP A 1 555  ? 147.365 112.077 91.504  1.00 69.04  ? 126  ASP A CB  1 
ATOM   965   C  CG  . ASP A 1 555  ? 147.702 113.531 91.797  1.00 84.99  ? 126  ASP A CG  1 
ATOM   966   O  OD1 . ASP A 1 555  ? 147.233 114.404 91.030  1.00 81.01  ? 126  ASP A OD1 1 
ATOM   967   O  OD2 . ASP A 1 555  ? 148.409 113.806 92.798  1.00 80.97  ? 126  ASP A OD2 1 
ATOM   968   N  N   . CYS A 1 556  ? 145.463 109.595 91.349  1.00 79.40  ? 127  CYS A N   1 
ATOM   969   C  CA  . CYS A 1 556  ? 145.166 108.198 91.042  1.00 80.23  ? 127  CYS A CA  1 
ATOM   970   C  C   . CYS A 1 556  ? 143.731 108.086 90.538  1.00 85.23  ? 127  CYS A C   1 
ATOM   971   O  O   . CYS A 1 556  ? 142.785 108.474 91.238  1.00 83.87  ? 127  CYS A O   1 
ATOM   972   C  CB  . CYS A 1 556  ? 145.367 107.323 92.280  1.00 87.02  ? 127  CYS A CB  1 
ATOM   973   S  SG  . CYS A 1 556  ? 144.533 107.952 93.786  1.00 103.76 ? 127  CYS A SG  1 
ATOM   974   N  N   . VAL A 1 557  ? 143.564 107.550 89.332  1.00 89.60  ? 128  VAL A N   1 
ATOM   975   C  CA  . VAL A 1 557  ? 142.268 107.497 88.660  1.00 89.83  ? 128  VAL A CA  1 
ATOM   976   C  C   . VAL A 1 557  ? 141.823 106.039 88.592  1.00 87.64  ? 128  VAL A C   1 
ATOM   977   O  O   . VAL A 1 557  ? 142.515 105.201 87.996  1.00 85.34  ? 128  VAL A O   1 
ATOM   978   C  CB  . VAL A 1 557  ? 142.335 108.131 87.257  1.00 97.91  ? 128  VAL A CB  1 
ATOM   979   C  CG1 . VAL A 1 557  ? 140.965 108.074 86.556  1.00 94.75  ? 128  VAL A CG1 1 
ATOM   980   C  CG2 . VAL A 1 557  ? 142.873 109.589 87.327  1.00 85.71  ? 128  VAL A CG2 1 
ATOM   981   N  N   . ASP A 1 558  ? 140.668 105.736 89.202  1.00 88.93  ? 129  ASP A N   1 
ATOM   982   C  CA  . ASP A 1 558  ? 140.090 104.390 89.153  1.00 84.07  ? 129  ASP A CA  1 
ATOM   983   C  C   . ASP A 1 558  ? 139.451 104.203 87.780  1.00 77.36  ? 129  ASP A C   1 
ATOM   984   O  O   . ASP A 1 558  ? 138.432 104.828 87.463  1.00 78.25  ? 129  ASP A O   1 
ATOM   985   C  CB  . ASP A 1 558  ? 139.083 104.177 90.288  1.00 75.27  ? 129  ASP A CB  1 
ATOM   986   C  CG  . ASP A 1 558  ? 138.800 102.682 90.578  1.00 71.12  ? 129  ASP A CG  1 
ATOM   987   O  OD1 . ASP A 1 558  ? 138.768 101.867 89.626  1.00 74.98  ? 129  ASP A OD1 1 
ATOM   988   O  OD2 . ASP A 1 558  ? 138.615 102.323 91.764  1.00 63.21  ? 129  ASP A OD2 1 
ATOM   989   N  N   . GLU A 1 559  ? 140.064 103.354 86.958  1.00 73.68  ? 130  GLU A N   1 
ATOM   990   C  CA  . GLU A 1 559  ? 139.615 103.218 85.584  1.00 75.02  ? 130  GLU A CA  1 
ATOM   991   C  C   . GLU A 1 559  ? 138.183 102.719 85.516  1.00 76.49  ? 130  GLU A C   1 
ATOM   992   O  O   . GLU A 1 559  ? 137.451 103.061 84.580  1.00 83.56  ? 130  GLU A O   1 
ATOM   993   C  CB  . GLU A 1 559  ? 140.560 102.284 84.820  1.00 90.43  ? 130  GLU A CB  1 
ATOM   994   C  CG  . GLU A 1 559  ? 140.816 100.915 85.485  1.00 92.02  ? 130  GLU A CG  1 
ATOM   995   C  CD  . GLU A 1 559  ? 141.854 100.064 84.731  1.00 97.94  ? 130  GLU A CD  1 
ATOM   996   O  OE1 . GLU A 1 559  ? 142.391 100.533 83.700  1.00 97.10  ? 130  GLU A OE1 1 
ATOM   997   O  OE2 . GLU A 1 559  ? 142.125 98.920  85.166  1.00 93.03  ? 130  GLU A OE2 1 
ATOM   998   N  N   . HIS A 1 560  ? 137.755 101.934 86.502  1.00 67.40  ? 131  HIS A N   1 
ATOM   999   C  CA  . HIS A 1 560  ? 136.417 101.368 86.507  1.00 61.55  ? 131  HIS A CA  1 
ATOM   1000  C  C   . HIS A 1 560  ? 135.501 102.082 87.481  1.00 56.78  ? 131  HIS A C   1 
ATOM   1001  O  O   . HIS A 1 560  ? 134.658 101.451 88.115  1.00 66.20  ? 131  HIS A O   1 
ATOM   1002  C  CB  . HIS A 1 560  ? 136.472 99.871  86.807  1.00 69.61  ? 131  HIS A CB  1 
ATOM   1003  C  CG  . HIS A 1 560  ? 137.326 99.095  85.848  1.00 84.40  ? 131  HIS A CG  1 
ATOM   1004  N  ND1 . HIS A 1 560  ? 137.623 99.550  84.580  1.00 86.10  ? 131  HIS A ND1 1 
ATOM   1005  C  CD2 . HIS A 1 560  ? 137.932 97.889  85.964  1.00 90.75  ? 131  HIS A CD2 1 
ATOM   1006  C  CE1 . HIS A 1 560  ? 138.373 98.658  83.957  1.00 87.66  ? 131  HIS A CE1 1 
ATOM   1007  N  NE2 . HIS A 1 560  ? 138.579 97.643  84.776  1.00 88.96  ? 131  HIS A NE2 1 
ATOM   1008  N  N   . PHE A 1 561  ? 135.629 103.397 87.596  1.00 52.29  ? 132  PHE A N   1 
ATOM   1009  C  CA  . PHE A 1 561  ? 134.900 104.076 88.650  1.00 45.87  ? 132  PHE A CA  1 
ATOM   1010  C  C   . PHE A 1 561  ? 133.409 103.993 88.418  1.00 49.57  ? 132  PHE A C   1 
ATOM   1011  O  O   . PHE A 1 561  ? 132.651 103.621 89.324  1.00 59.70  ? 132  PHE A O   1 
ATOM   1012  C  CB  . PHE A 1 561  ? 135.325 105.523 88.759  1.00 60.15  ? 132  PHE A CB  1 
ATOM   1013  C  CG  . PHE A 1 561  ? 134.770 106.197 89.970  1.00 64.01  ? 132  PHE A CG  1 
ATOM   1014  C  CD1 . PHE A 1 561  ? 135.243 105.864 91.233  1.00 69.69  ? 132  PHE A CD1 1 
ATOM   1015  C  CD2 . PHE A 1 561  ? 133.782 107.154 89.860  1.00 62.10  ? 132  PHE A CD2 1 
ATOM   1016  C  CE1 . PHE A 1 561  ? 134.740 106.478 92.372  1.00 69.00  ? 132  PHE A CE1 1 
ATOM   1017  C  CE2 . PHE A 1 561  ? 133.275 107.778 90.996  1.00 65.22  ? 132  PHE A CE2 1 
ATOM   1018  C  CZ  . PHE A 1 561  ? 133.753 107.435 92.254  1.00 69.76  ? 132  PHE A CZ  1 
ATOM   1019  N  N   . GLN A 1 562  ? 132.965 104.312 87.201  1.00 49.73  ? 133  GLN A N   1 
ATOM   1020  C  CA  . GLN A 1 562  ? 131.548 104.153 86.894  1.00 57.65  ? 133  GLN A CA  1 
ATOM   1021  C  C   . GLN A 1 562  ? 131.116 102.707 87.091  1.00 54.57  ? 133  GLN A C   1 
ATOM   1022  O  O   . GLN A 1 562  ? 130.024 102.439 87.605  1.00 55.28  ? 133  GLN A O   1 
ATOM   1023  C  CB  . GLN A 1 562  ? 131.244 104.620 85.464  1.00 55.83  ? 133  GLN A CB  1 
ATOM   1024  C  CG  . GLN A 1 562  ? 131.358 106.123 85.264  1.00 65.17  ? 133  GLN A CG  1 
ATOM   1025  C  CD  . GLN A 1 562  ? 130.273 106.937 86.003  1.00 66.62  ? 133  GLN A CD  1 
ATOM   1026  O  OE1 . GLN A 1 562  ? 129.294 106.390 86.533  1.00 57.15  ? 133  GLN A OE1 1 
ATOM   1027  N  NE2 . GLN A 1 562  ? 130.459 108.258 86.036  1.00 60.71  ? 133  GLN A NE2 1 
ATOM   1028  N  N   . GLU A 1 563  ? 131.956 101.759 86.696  1.00 56.26  ? 134  GLU A N   1 
ATOM   1029  C  CA  . GLU A 1 563  ? 131.543 100.372 86.792  1.00 52.19  ? 134  GLU A CA  1 
ATOM   1030  C  C   . GLU A 1 563  ? 131.329 100.027 88.249  1.00 44.38  ? 134  GLU A C   1 
ATOM   1031  O  O   . GLU A 1 563  ? 130.368 99.347  88.609  1.00 49.02  ? 134  GLU A O   1 
ATOM   1032  C  CB  . GLU A 1 563  ? 132.616 99.476  86.184  1.00 63.00  ? 134  GLU A CB  1 
ATOM   1033  C  CG  . GLU A 1 563  ? 132.527 99.254  84.681  1.00 75.66  ? 134  GLU A CG  1 
ATOM   1034  C  CD  . GLU A 1 563  ? 132.792 100.543 83.811  1.00 86.79  ? 134  GLU A CD  1 
ATOM   1035  O  OE1 . GLU A 1 563  ? 133.033 101.653 84.429  1.00 77.42  ? 134  GLU A OE1 1 
ATOM   1036  O  OE2 . GLU A 1 563  ? 132.852 100.413 82.557  1.00 88.73  ? 134  GLU A OE2 1 
ATOM   1037  N  N   . LYS A 1 564  ? 132.262 100.451 89.094  1.00 41.73  ? 135  LYS A N   1 
ATOM   1038  C  CA  . LYS A 1 564  ? 132.167 100.143 90.506  1.00 40.73  ? 135  LYS A CA  1 
ATOM   1039  C  C   . LYS A 1 564  ? 130.904 100.736 91.079  1.00 45.70  ? 135  LYS A C   1 
ATOM   1040  O  O   . LYS A 1 564  ? 130.241 100.105 91.897  1.00 54.75  ? 135  LYS A O   1 
ATOM   1041  C  CB  . LYS A 1 564  ? 133.372 100.694 91.262  1.00 50.58  ? 135  LYS A CB  1 
ATOM   1042  C  CG  . LYS A 1 564  ? 134.694 100.038 90.904  1.00 59.68  ? 135  LYS A CG  1 
ATOM   1043  C  CD  . LYS A 1 564  ? 134.886 98.627  91.415  1.00 64.27  ? 135  LYS A CD  1 
ATOM   1044  C  CE  . LYS A 1 564  ? 136.312 98.178  91.071  1.00 72.00  ? 135  LYS A CE  1 
ATOM   1045  N  NZ  . LYS A 1 564  ? 137.360 99.151  91.529  1.00 69.62  ? 135  LYS A NZ  1 
ATOM   1046  N  N   . ILE A 1 565  ? 130.582 101.973 90.705  1.00 48.56  ? 136  ILE A N   1 
ATOM   1047  C  CA  . ILE A 1 565  ? 129.344 102.576 91.187  1.00 41.20  ? 136  ILE A CA  1 
ATOM   1048  C  C   . ILE A 1 565  ? 128.161 101.734 90.777  1.00 48.38  ? 136  ILE A C   1 
ATOM   1049  O  O   . ILE A 1 565  ? 127.245 101.497 91.570  1.00 57.14  ? 136  ILE A O   1 
ATOM   1050  C  CB  . ILE A 1 565  ? 129.191 104.010 90.660  1.00 49.27  ? 136  ILE A CB  1 
ATOM   1051  C  CG1 . ILE A 1 565  ? 130.197 104.938 91.341  1.00 64.73  ? 136  ILE A CG1 1 
ATOM   1052  C  CG2 . ILE A 1 565  ? 127.760 104.487 90.833  1.00 51.47  ? 136  ILE A CG2 1 
ATOM   1053  C  CD1 . ILE A 1 565  ? 130.100 106.382 90.869  1.00 69.86  ? 136  ILE A CD1 1 
ATOM   1054  N  N   . LEU A 1 566  ? 128.150 101.280 89.526  1.00 53.50  ? 137  LEU A N   1 
ATOM   1055  C  CA  . LEU A 1 566  ? 127.019 100.496 89.044  1.00 50.23  ? 137  LEU A CA  1 
ATOM   1056  C  C   . LEU A 1 566  ? 126.907 99.187  89.815  1.00 46.35  ? 137  LEU A C   1 
ATOM   1057  O  O   . LEU A 1 566  ? 125.825 98.822  90.287  1.00 51.28  ? 137  LEU A O   1 
ATOM   1058  C  CB  . LEU A 1 566  ? 127.159 100.251 87.543  1.00 49.29  ? 137  LEU A CB  1 
ATOM   1059  C  CG  . LEU A 1 566  ? 126.134 99.298  86.952  1.00 54.36  ? 137  LEU A CG  1 
ATOM   1060  C  CD1 . LEU A 1 566  ? 124.750 99.863  87.214  1.00 55.96  ? 137  LEU A CD1 1 
ATOM   1061  C  CD2 . LEU A 1 566  ? 126.380 99.124  85.454  1.00 56.16  ? 137  LEU A CD2 1 
ATOM   1062  N  N   . SER A 1 567  ? 128.030 98.489  89.997  1.00 45.16  ? 138  SER A N   1 
ATOM   1063  C  CA  . SER A 1 567  ? 128.007 97.253  90.773  1.00 44.45  ? 138  SER A CA  1 
ATOM   1064  C  C   . SER A 1 567  ? 127.549 97.524  92.195  1.00 38.98  ? 138  SER A C   1 
ATOM   1065  O  O   . SER A 1 567  ? 126.654 96.846  92.706  1.00 46.54  ? 138  SER A O   1 
ATOM   1066  C  CB  . SER A 1 567  ? 129.386 96.590  90.775  1.00 44.86  ? 138  SER A CB  1 
ATOM   1067  O  OG  . SER A 1 567  ? 129.800 96.247  89.463  1.00 48.74  ? 138  SER A OG  1 
ATOM   1068  N  N   . SER A 1 568  ? 128.114 98.547  92.825  1.00 36.04  ? 139  SER A N   1 
ATOM   1069  C  CA  . SER A 1 568  ? 127.775 98.856  94.199  1.00 34.84  ? 139  SER A CA  1 
ATOM   1070  C  C   . SER A 1 568  ? 126.296 99.132  94.338  1.00 40.44  ? 139  SER A C   1 
ATOM   1071  O  O   . SER A 1 568  ? 125.658 98.668  95.288  1.00 51.96  ? 139  SER A O   1 
ATOM   1072  C  CB  . SER A 1 568  ? 128.575 100.062 94.694  1.00 44.01  ? 139  SER A CB  1 
ATOM   1073  O  OG  . SER A 1 568  ? 129.979 99.874  94.578  1.00 48.00  ? 139  SER A OG  1 
ATOM   1074  N  N   . ILE A 1 569  ? 125.723 99.891  93.417  1.00 40.27  ? 140  ILE A N   1 
ATOM   1075  C  CA  . ILE A 1 569  ? 124.313 100.200 93.569  1.00 41.19  ? 140  ILE A CA  1 
ATOM   1076  C  C   . ILE A 1 569  ? 123.477 98.955  93.311  1.00 45.60  ? 140  ILE A C   1 
ATOM   1077  O  O   . ILE A 1 569  ? 122.484 98.710  94.006  1.00 48.40  ? 140  ILE A O   1 
ATOM   1078  C  CB  . ILE A 1 569  ? 123.908 101.373 92.662  1.00 51.43  ? 140  ILE A CB  1 
ATOM   1079  C  CG1 . ILE A 1 569  ? 124.684 102.639 93.040  1.00 56.37  ? 140  ILE A CG1 1 
ATOM   1080  C  CG2 . ILE A 1 569  ? 122.402 101.647 92.769  1.00 57.92  ? 140  ILE A CG2 1 
ATOM   1081  C  CD1 . ILE A 1 569  ? 124.337 103.849 92.153  1.00 63.33  ? 140  ILE A CD1 1 
ATOM   1082  N  N   . GLN A 1 570  ? 123.865 98.139  92.323  1.00 46.72  ? 141  GLN A N   1 
ATOM   1083  C  CA  . GLN A 1 570  ? 123.072 96.953  92.005  1.00 44.89  ? 141  GLN A CA  1 
ATOM   1084  C  C   . GLN A 1 570  ? 123.158 95.919  93.117  1.00 45.90  ? 141  GLN A C   1 
ATOM   1085  O  O   . GLN A 1 570  ? 122.141 95.363  93.542  1.00 49.39  ? 141  GLN A O   1 
ATOM   1086  C  CB  . GLN A 1 570  ? 123.526 96.324  90.687  1.00 48.81  ? 141  GLN A CB  1 
ATOM   1087  C  CG  . GLN A 1 570  ? 123.234 97.133  89.411  1.00 56.37  ? 141  GLN A CG  1 
ATOM   1088  C  CD  . GLN A 1 570  ? 121.798 97.002  88.934  1.00 66.52  ? 141  GLN A CD  1 
ATOM   1089  O  OE1 . GLN A 1 570  ? 120.976 96.335  89.570  1.00 67.95  ? 141  GLN A OE1 1 
ATOM   1090  N  NE2 . GLN A 1 570  ? 121.495 97.620  87.791  1.00 62.99  ? 141  GLN A NE2 1 
ATOM   1091  N  N   . GLY A 1 571  ? 124.351 95.654  93.607  1.00 44.11  ? 142  GLY A N   1 
ATOM   1092  C  CA  . GLY A 1 571  ? 124.472 94.581  94.562  1.00 45.87  ? 142  GLY A CA  1 
ATOM   1093  C  C   . GLY A 1 571  ? 124.137 94.947  95.979  1.00 43.14  ? 142  GLY A C   1 
ATOM   1094  O  O   . GLY A 1 571  ? 124.195 94.081  96.858  1.00 49.32  ? 142  GLY A O   1 
ATOM   1095  N  N   . ASN A 1 572  ? 123.810 96.210  96.230  1.00 38.16  ? 143  ASN A N   1 
ATOM   1096  C  CA  . ASN A 1 572  ? 123.369 96.622  97.548  1.00 30.44  ? 143  ASN A CA  1 
ATOM   1097  C  C   . ASN A 1 572  ? 122.261 95.699  98.017  1.00 37.09  ? 143  ASN A C   1 
ATOM   1098  O  O   . ASN A 1 572  ? 121.396 95.303  97.232  1.00 42.58  ? 143  ASN A O   1 
ATOM   1099  C  CB  . ASN A 1 572  ? 122.868 98.049  97.489  1.00 29.02  ? 143  ASN A CB  1 
ATOM   1100  C  CG  . ASN A 1 572  ? 122.871 98.684  98.805  1.00 29.52  ? 143  ASN A CG  1 
ATOM   1101  O  OD1 . ASN A 1 572  ? 121.996 98.414  99.628  1.00 34.58  ? 143  ASN A OD1 1 
ATOM   1102  N  ND2 . ASN A 1 572  ? 123.869 99.526  99.055  1.00 35.00  ? 143  ASN A ND2 1 
ATOM   1103  N  N   . GLU A 1 573  ? 122.309 95.302  99.277  1.00 29.22  ? 144  GLU A N   1 
ATOM   1104  C  CA  . GLU A 1 573  ? 121.377 94.268  99.664  1.00 26.19  ? 144  GLU A CA  1 
ATOM   1105  C  C   . GLU A 1 573  ? 120.041 94.811  100.128 1.00 37.08  ? 144  GLU A C   1 
ATOM   1106  O  O   . GLU A 1 573  ? 119.104 94.028  100.299 1.00 50.26  ? 144  GLU A O   1 
ATOM   1107  C  CB  . GLU A 1 573  ? 121.946 93.408  100.765 1.00 38.43  ? 144  GLU A CB  1 
ATOM   1108  C  CG  . GLU A 1 573  ? 122.156 94.156  102.061 1.00 57.97  ? 144  GLU A CG  1 
ATOM   1109  C  CD  . GLU A 1 573  ? 122.459 93.214  103.252 1.00 71.17  ? 144  GLU A CD  1 
ATOM   1110  O  OE1 . GLU A 1 573  ? 122.440 91.971  103.071 1.00 67.56  ? 144  GLU A OE1 1 
ATOM   1111  O  OE2 . GLU A 1 573  ? 122.707 93.720  104.375 1.00 67.10  ? 144  GLU A OE2 1 
ATOM   1112  N  N   . PHE A 1 574  ? 119.907 96.111  100.334 1.00 35.07  ? 145  PHE A N   1 
ATOM   1113  C  CA  . PHE A 1 574  ? 118.612 96.671  100.694 1.00 37.06  ? 145  PHE A CA  1 
ATOM   1114  C  C   . PHE A 1 574  ? 117.988 97.442  99.551  1.00 34.52  ? 145  PHE A C   1 
ATOM   1115  O  O   . PHE A 1 574  ? 117.078 98.240  99.782  1.00 36.38  ? 145  PHE A O   1 
ATOM   1116  C  CB  . PHE A 1 574  ? 118.738 97.586  101.907 1.00 44.55  ? 145  PHE A CB  1 
ATOM   1117  C  CG  . PHE A 1 574  ? 119.279 96.898  103.111 1.00 42.50  ? 145  PHE A CG  1 
ATOM   1118  C  CD1 . PHE A 1 574  ? 118.485 96.052  103.858 1.00 50.34  ? 145  PHE A CD1 1 
ATOM   1119  C  CD2 . PHE A 1 574  ? 120.598 97.075  103.474 1.00 47.26  ? 145  PHE A CD2 1 
ATOM   1120  C  CE1 . PHE A 1 574  ? 118.990 95.413  104.966 1.00 50.85  ? 145  PHE A CE1 1 
ATOM   1121  C  CE2 . PHE A 1 574  ? 121.115 96.442  104.581 1.00 51.89  ? 145  PHE A CE2 1 
ATOM   1122  C  CZ  . PHE A 1 574  ? 120.309 95.606  105.330 1.00 49.58  ? 145  PHE A CZ  1 
ATOM   1123  N  N   . LEU A 1 575  ? 118.495 97.264  98.334  1.00 34.36  ? 146  LEU A N   1 
ATOM   1124  C  CA  . LEU A 1 575  ? 117.929 97.971  97.199  1.00 24.67  ? 146  LEU A CA  1 
ATOM   1125  C  C   . LEU A 1 575  ? 116.492 97.530  96.977  1.00 34.37  ? 146  LEU A C   1 
ATOM   1126  O  O   . LEU A 1 575  ? 115.550 98.319  97.136  1.00 47.21  ? 146  LEU A O   1 
ATOM   1127  C  CB  . LEU A 1 575  ? 118.782 97.722  95.967  1.00 23.46  ? 146  LEU A CB  1 
ATOM   1128  C  CG  . LEU A 1 575  ? 118.340 98.488  94.740  1.00 34.23  ? 146  LEU A CG  1 
ATOM   1129  C  CD1 . LEU A 1 575  ? 118.506 99.942  95.070  1.00 34.58  ? 146  LEU A CD1 1 
ATOM   1130  C  CD2 . LEU A 1 575  ? 119.186 98.123  93.523  1.00 46.80  ? 146  LEU A CD2 1 
ATOM   1131  N  N   . HIS A 1 576  ? 116.291 96.258  96.650  1.00 32.72  ? 147  HIS A N   1 
ATOM   1132  C  CA  . HIS A 1 576  ? 114.935 95.829  96.352  1.00 31.14  ? 147  HIS A CA  1 
ATOM   1133  C  C   . HIS A 1 576  ? 114.052 95.918  97.565  1.00 27.52  ? 147  HIS A C   1 
ATOM   1134  O  O   . HIS A 1 576  ? 112.856 96.201  97.443  1.00 40.43  ? 147  HIS A O   1 
ATOM   1135  C  CB  . HIS A 1 576  ? 114.939 94.438  95.760  1.00 37.21  ? 147  HIS A CB  1 
ATOM   1136  C  CG  . HIS A 1 576  ? 115.419 94.422  94.345  1.00 56.13  ? 147  HIS A CG  1 
ATOM   1137  N  ND1 . HIS A 1 576  ? 116.501 95.164  93.919  1.00 59.99  ? 147  HIS A ND1 1 
ATOM   1138  C  CD2 . HIS A 1 576  ? 114.938 93.795  93.244  1.00 82.03  ? 147  HIS A CD2 1 
ATOM   1139  C  CE1 . HIS A 1 576  ? 116.679 94.979  92.622  1.00 60.06  ? 147  HIS A CE1 1 
ATOM   1140  N  NE2 . HIS A 1 576  ? 115.745 94.151  92.188  1.00 75.05  ? 147  HIS A NE2 1 
ATOM   1141  N  N   . GLN A 1 577  ? 114.619 95.772  98.737  1.00 23.55  ? 148  GLN A N   1 
ATOM   1142  C  CA  . GLN A 1 577  ? 113.785 95.943  99.905  1.00 33.14  ? 148  GLN A CA  1 
ATOM   1143  C  C   . GLN A 1 577  ? 113.360 97.397  100.058 1.00 32.47  ? 148  GLN A C   1 
ATOM   1144  O  O   . GLN A 1 577  ? 112.219 97.673  100.440 1.00 40.62  ? 148  GLN A O   1 
ATOM   1145  C  CB  . GLN A 1 577  ? 114.522 95.468  101.141 1.00 47.06  ? 148  GLN A CB  1 
ATOM   1146  C  CG  . GLN A 1 577  ? 114.910 94.021  101.053 1.00 51.95  ? 148  GLN A CG  1 
ATOM   1147  C  CD  . GLN A 1 577  ? 115.028 93.398  102.411 1.00 62.38  ? 148  GLN A CD  1 
ATOM   1148  O  OE1 . GLN A 1 577  ? 114.301 93.771  103.337 1.00 59.95  ? 148  GLN A OE1 1 
ATOM   1149  N  NE2 . GLN A 1 577  ? 115.991 92.496  102.569 1.00 59.87  ? 148  GLN A NE2 1 
ATOM   1150  N  N   . MET A 1 578  ? 114.262 98.341  99.779  1.00 28.67  ? 149  MET A N   1 
ATOM   1151  C  CA  . MET A 1 578  ? 113.906 99.752  99.919  1.00 29.02  ? 149  MET A CA  1 
ATOM   1152  C  C   . MET A 1 578  ? 112.785 100.133 98.971  1.00 42.59  ? 149  MET A C   1 
ATOM   1153  O  O   . MET A 1 578  ? 111.836 100.832 99.358  1.00 45.94  ? 149  MET A O   1 
ATOM   1154  C  CB  . MET A 1 578  ? 115.096 100.658 99.633  1.00 29.62  ? 149  MET A CB  1 
ATOM   1155  C  CG  . MET A 1 578  ? 114.798 102.087 99.975  1.00 30.59  ? 149  MET A CG  1 
ATOM   1156  S  SD  . MET A 1 578  ? 116.099 103.173 99.419  1.00 37.59  ? 149  MET A SD  1 
ATOM   1157  C  CE  . MET A 1 578  ? 115.979 102.884 97.662  1.00 43.32  ? 149  MET A CE  1 
ATOM   1158  N  N   . PHE A 1 579  ? 112.885 99.705  97.714  1.00 37.18  ? 150  PHE A N   1 
ATOM   1159  C  CA  . PHE A 1 579  ? 111.796 99.979  96.792  1.00 26.92  ? 150  PHE A CA  1 
ATOM   1160  C  C   . PHE A 1 579  ? 110.501 99.337  97.257  1.00 27.66  ? 150  PHE A C   1 
ATOM   1161  O  O   . PHE A 1 579  ? 109.435 99.962  97.198  1.00 43.51  ? 150  PHE A O   1 
ATOM   1162  C  CB  . PHE A 1 579  ? 112.178 99.512  95.410  1.00 30.97  ? 150  PHE A CB  1 
ATOM   1163  C  CG  . PHE A 1 579  ? 113.183 100.370 94.776  1.00 23.28  ? 150  PHE A CG  1 
ATOM   1164  C  CD1 . PHE A 1 579  ? 113.118 101.712 94.916  1.00 30.78  ? 150  PHE A CD1 1 
ATOM   1165  C  CD2 . PHE A 1 579  ? 114.206 99.837  94.070  1.00 33.41  ? 150  PHE A CD2 1 
ATOM   1166  C  CE1 . PHE A 1 579  ? 114.048 102.518 94.314  1.00 37.01  ? 150  PHE A CE1 1 
ATOM   1167  C  CE2 . PHE A 1 579  ? 115.143 100.634 93.484  1.00 36.71  ? 150  PHE A CE2 1 
ATOM   1168  C  CZ  . PHE A 1 579  ? 115.069 101.969 93.605  1.00 28.39  ? 150  PHE A CZ  1 
ATOM   1169  N  N   . PHE A 1 580  ? 110.560 98.114  97.747  1.00 20.88  ? 151  PHE A N   1 
ATOM   1170  C  CA  . PHE A 1 580  ? 109.322 97.533  98.209  1.00 22.11  ? 151  PHE A CA  1 
ATOM   1171  C  C   . PHE A 1 580  ? 108.731 98.329  99.363  1.00 37.04  ? 151  PHE A C   1 
ATOM   1172  O  O   . PHE A 1 580  ? 107.508 98.508  99.445  1.00 49.97  ? 151  PHE A O   1 
ATOM   1173  C  CB  . PHE A 1 580  ? 109.544 96.104  98.618  1.00 31.18  ? 151  PHE A CB  1 
ATOM   1174  C  CG  . PHE A 1 580  ? 108.306 95.431  99.055  1.00 36.53  ? 151  PHE A CG  1 
ATOM   1175  C  CD1 . PHE A 1 580  ? 107.351 95.089  98.127  1.00 47.29  ? 151  PHE A CD1 1 
ATOM   1176  C  CD2 . PHE A 1 580  ? 108.112 95.085  100.369 1.00 39.70  ? 151  PHE A CD2 1 
ATOM   1177  C  CE1 . PHE A 1 580  ? 106.201 94.448  98.501  1.00 52.83  ? 151  PHE A CE1 1 
ATOM   1178  C  CE2 . PHE A 1 580  ? 106.969 94.429  100.751 1.00 50.78  ? 151  PHE A CE2 1 
ATOM   1179  C  CZ  . PHE A 1 580  ? 106.007 94.110  99.811  1.00 52.53  ? 151  PHE A CZ  1 
ATOM   1180  N  N   . TRP A 1 581  ? 109.571 98.814  100.275 1.00 37.76  ? 152  TRP A N   1 
ATOM   1181  C  CA  . TRP A 1 581  ? 109.056 99.534  101.439 1.00 29.53  ? 152  TRP A CA  1 
ATOM   1182  C  C   . TRP A 1 581  ? 108.526 100.892 101.061 1.00 35.80  ? 152  TRP A C   1 
ATOM   1183  O  O   . TRP A 1 581  ? 107.636 101.414 101.742 1.00 45.24  ? 152  TRP A O   1 
ATOM   1184  C  CB  . TRP A 1 581  ? 110.135 99.669  102.487 1.00 34.82  ? 152  TRP A CB  1 
ATOM   1185  C  CG  . TRP A 1 581  ? 110.211 98.440  103.285 1.00 34.31  ? 152  TRP A CG  1 
ATOM   1186  C  CD1 . TRP A 1 581  ? 111.156 97.462  103.212 1.00 33.62  ? 152  TRP A CD1 1 
ATOM   1187  C  CD2 . TRP A 1 581  ? 109.319 98.064  104.309 1.00 26.56  ? 152  TRP A CD2 1 
ATOM   1188  N  NE1 . TRP A 1 581  ? 110.884 96.486  104.116 1.00 38.40  ? 152  TRP A NE1 1 
ATOM   1189  C  CE2 . TRP A 1 581  ? 109.759 96.840  104.811 1.00 32.37  ? 152  TRP A CE2 1 
ATOM   1190  C  CE3 . TRP A 1 581  ? 108.192 98.655  104.861 1.00 38.94  ? 152  TRP A CE3 1 
ATOM   1191  C  CZ2 . TRP A 1 581  ? 109.112 96.188  105.839 1.00 49.22  ? 152  TRP A CZ2 1 
ATOM   1192  C  CZ3 . TRP A 1 581  ? 107.541 98.008  105.873 1.00 46.36  ? 152  TRP A CZ3 1 
ATOM   1193  C  CH2 . TRP A 1 581  ? 107.999 96.781  106.355 1.00 49.25  ? 152  TRP A CH2 1 
ATOM   1194  N  N   . TYR A 1 582  ? 109.039 101.479 99.972  1.00 42.10  ? 153  TYR A N   1 
ATOM   1195  C  CA  . TYR A 1 582  ? 108.417 102.700 99.458  1.00 42.40  ? 153  TYR A CA  1 
ATOM   1196  C  C   . TYR A 1 582  ? 107.063 102.407 98.836  1.00 37.49  ? 153  TYR A C   1 
ATOM   1197  O  O   . TYR A 1 582  ? 106.142 103.217 98.949  1.00 45.23  ? 153  TYR A O   1 
ATOM   1198  C  CB  . TYR A 1 582  ? 109.329 103.434 98.468  1.00 35.42  ? 153  TYR A CB  1 
ATOM   1199  C  CG  . TYR A 1 582  ? 110.264 104.334 99.206  1.00 35.19  ? 153  TYR A CG  1 
ATOM   1200  C  CD1 . TYR A 1 582  ? 109.783 105.400 99.958  1.00 44.02  ? 153  TYR A CD1 1 
ATOM   1201  C  CD2 . TYR A 1 582  ? 111.612 104.069 99.236  1.00 41.15  ? 153  TYR A CD2 1 
ATOM   1202  C  CE1 . TYR A 1 582  ? 110.640 106.208 100.691 1.00 41.01  ? 153  TYR A CE1 1 
ATOM   1203  C  CE2 . TYR A 1 582  ? 112.484 104.870 99.957  1.00 48.06  ? 153  TYR A CE2 1 
ATOM   1204  C  CZ  . TYR A 1 582  ? 111.992 105.932 100.685 1.00 48.17  ? 153  TYR A CZ  1 
ATOM   1205  O  OH  . TYR A 1 582  ? 112.870 106.717 101.400 1.00 52.03  ? 153  TYR A OH  1 
ATOM   1206  N  N   . ASP A 1 583  ? 106.909 101.268 98.181  1.00 32.40  ? 154  ASP A N   1 
ATOM   1207  C  CA  . ASP A 1 583  ? 105.572 100.943 97.702  1.00 34.96  ? 154  ASP A CA  1 
ATOM   1208  C  C   . ASP A 1 583  ? 104.610 100.785 98.854  1.00 29.94  ? 154  ASP A C   1 
ATOM   1209  O  O   . ASP A 1 583  ? 103.470 101.260 98.789  1.00 42.83  ? 154  ASP A O   1 
ATOM   1210  C  CB  . ASP A 1 583  ? 105.579 99.670  96.870  1.00 54.35  ? 154  ASP A CB  1 
ATOM   1211  C  CG  . ASP A 1 583  ? 106.441 99.800  95.638  1.00 66.30  ? 154  ASP A CG  1 
ATOM   1212  O  OD1 . ASP A 1 583  ? 106.991 100.911 95.416  1.00 58.29  ? 154  ASP A OD1 1 
ATOM   1213  O  OD2 . ASP A 1 583  ? 106.587 98.789  94.907  1.00 66.36  ? 154  ASP A OD2 1 
ATOM   1214  N  N   . LEU A 1 584  ? 105.032 100.105 99.906  1.00 27.71  ? 155  LEU A N   1 
ATOM   1215  C  CA  . LEU A 1 584  ? 104.128 99.958  101.039 1.00 37.41  ? 155  LEU A CA  1 
ATOM   1216  C  C   . LEU A 1 584  ? 103.815 101.316 101.676 1.00 41.84  ? 155  LEU A C   1 
ATOM   1217  O  O   . LEU A 1 584  ? 102.677 101.567 102.087 1.00 42.33  ? 155  LEU A O   1 
ATOM   1218  C  CB  . LEU A 1 584  ? 104.700 98.993  102.081 1.00 42.08  ? 155  LEU A CB  1 
ATOM   1219  C  CG  . LEU A 1 584  ? 104.879 97.519  101.724 1.00 46.64  ? 155  LEU A CG  1 
ATOM   1220  C  CD1 . LEU A 1 584  ? 105.390 96.753  102.943 1.00 44.47  ? 155  LEU A CD1 1 
ATOM   1221  C  CD2 . LEU A 1 584  ? 103.567 96.924  101.206 1.00 54.02  ? 155  LEU A CD2 1 
ATOM   1222  N  N   . ALA A 1 585  ? 104.807 102.204 101.775 1.00 36.14  ? 156  ALA A N   1 
ATOM   1223  C  CA  . ALA A 1 585  ? 104.533 103.527 102.309 1.00 26.62  ? 156  ALA A CA  1 
ATOM   1224  C  C   . ALA A 1 585  ? 103.571 104.302 101.408 1.00 41.92  ? 156  ALA A C   1 
ATOM   1225  O  O   . ALA A 1 585  ? 102.677 104.978 101.910 1.00 47.31  ? 156  ALA A O   1 
ATOM   1226  C  CB  . ALA A 1 585  ? 105.834 104.299 102.498 1.00 42.37  ? 156  ALA A CB  1 
ATOM   1227  N  N   . ILE A 1 586  ? 103.738 104.226 100.076 1.00 42.76  ? 157  ILE A N   1 
ATOM   1228  C  CA  . ILE A 1 586  ? 102.801 104.864 99.139  1.00 24.13  ? 157  ILE A CA  1 
ATOM   1229  C  C   . ILE A 1 586  ? 101.391 104.379 99.386  1.00 25.39  ? 157  ILE A C   1 
ATOM   1230  O  O   . ILE A 1 586  ? 100.447 105.168 99.532  1.00 33.33  ? 157  ILE A O   1 
ATOM   1231  C  CB  . ILE A 1 586  ? 103.192 104.549 97.694  1.00 16.38  ? 157  ILE A CB  1 
ATOM   1232  C  CG1 . ILE A 1 586  ? 104.456 105.267 97.313  1.00 22.29  ? 157  ILE A CG1 1 
ATOM   1233  C  CG2 . ILE A 1 586  ? 102.085 104.927 96.824  1.00 23.39  ? 157  ILE A CG2 1 
ATOM   1234  C  CD1 . ILE A 1 586  ? 104.280 106.741 97.427  1.00 37.61  ? 157  ILE A CD1 1 
ATOM   1235  N  N   . LEU A 1 587  ? 101.233 103.066 99.407  1.00 22.74  ? 158  LEU A N   1 
ATOM   1236  C  CA  . LEU A 1 587  ? 99.935  102.498 99.661  1.00 20.49  ? 158  LEU A CA  1 
ATOM   1237  C  C   . LEU A 1 587  ? 99.387  102.974 100.973 1.00 24.78  ? 158  LEU A C   1 
ATOM   1238  O  O   . LEU A 1 587  ? 98.216  103.335 101.054 1.00 36.38  ? 158  LEU A O   1 
ATOM   1239  C  CB  . LEU A 1 587  ? 100.026 100.994 99.670  1.00 33.11  ? 158  LEU A CB  1 
ATOM   1240  C  CG  . LEU A 1 587  ? 99.994  100.492 98.254  1.00 35.35  ? 158  LEU A CG  1 
ATOM   1241  C  CD1 . LEU A 1 587  ? 100.198 98.999  98.248  1.00 40.63  ? 158  LEU A CD1 1 
ATOM   1242  C  CD2 . LEU A 1 587  ? 98.634  100.852 97.696  1.00 42.35  ? 158  LEU A CD2 1 
ATOM   1243  N  N   . THR A 1 588  ? 100.192 102.982 102.021 1.00 26.54  ? 159  THR A N   1 
ATOM   1244  C  CA  . THR A 1 588  ? 99.594  103.341 103.301 1.00 34.34  ? 159  THR A CA  1 
ATOM   1245  C  C   . THR A 1 588  ? 99.359  104.835 103.431 1.00 44.77  ? 159  THR A C   1 
ATOM   1246  O  O   . THR A 1 588  ? 98.502  105.239 104.223 1.00 50.03  ? 159  THR A O   1 
ATOM   1247  C  CB  . THR A 1 588  ? 100.421 102.865 104.496 1.00 46.31  ? 159  THR A CB  1 
ATOM   1248  O  OG1 . THR A 1 588  ? 99.632  103.013 105.684 1.00 41.83  ? 159  THR A OG1 1 
ATOM   1249  C  CG2 . THR A 1 588  ? 101.695 103.688 104.650 1.00 56.07  ? 159  THR A CG2 1 
ATOM   1250  N  N   . ARG A 1 589  ? 100.050 105.658 102.631 1.00 43.03  ? 160  ARG A N   1 
ATOM   1251  C  CA  . ARG A 1 589  ? 99.760  107.087 102.615 1.00 36.30  ? 160  ARG A CA  1 
ATOM   1252  C  C   . ARG A 1 589  ? 98.402  107.331 101.975 1.00 33.81  ? 160  ARG A C   1 
ATOM   1253  O  O   . ARG A 1 589  ? 97.493  107.880 102.606 1.00 39.58  ? 160  ARG A O   1 
ATOM   1254  C  CB  . ARG A 1 589  ? 100.846 107.834 101.857 1.00 32.48  ? 160  ARG A CB  1 
ATOM   1255  C  CG  . ARG A 1 589  ? 102.167 107.768 102.509 1.00 29.80  ? 160  ARG A CG  1 
ATOM   1256  C  CD  . ARG A 1 589  ? 102.372 108.949 103.338 1.00 46.21  ? 160  ARG A CD  1 
ATOM   1257  N  NE  . ARG A 1 589  ? 102.363 110.174 102.561 1.00 47.32  ? 160  ARG A NE  1 
ATOM   1258  C  CZ  . ARG A 1 589  ? 103.342 110.545 101.756 1.00 43.15  ? 160  ARG A CZ  1 
ATOM   1259  N  NH1 . ARG A 1 589  ? 104.404 109.765 101.599 1.00 41.14  ? 160  ARG A NH1 1 
ATOM   1260  N  NH2 . ARG A 1 589  ? 103.252 111.701 101.114 1.00 51.75  ? 160  ARG A NH2 1 
ATOM   1261  N  N   . ARG A 1 590  ? 98.234  106.861 100.742 1.00 31.63  ? 161  ARG A N   1 
ATOM   1262  C  CA  . ARG A 1 590  ? 96.920  106.887 100.122 1.00 26.80  ? 161  ARG A CA  1 
ATOM   1263  C  C   . ARG A 1 590  ? 95.869  106.332 101.043 1.00 28.08  ? 161  ARG A C   1 
ATOM   1264  O  O   . ARG A 1 590  ? 94.756  106.849 101.104 1.00 45.14  ? 161  ARG A O   1 
ATOM   1265  C  CB  . ARG A 1 590  ? 96.929  106.056 98.862  1.00 34.00  ? 161  ARG A CB  1 
ATOM   1266  C  CG  . ARG A 1 590  ? 95.622  106.069 98.208  1.00 44.64  ? 161  ARG A CG  1 
ATOM   1267  C  CD  . ARG A 1 590  ? 95.276  107.454 97.824  1.00 56.30  ? 161  ARG A CD  1 
ATOM   1268  N  NE  . ARG A 1 590  ? 96.295  107.958 96.912  1.00 51.80  ? 161  ARG A NE  1 
ATOM   1269  C  CZ  . ARG A 1 590  ? 96.295  109.178 96.382  1.00 49.93  ? 161  ARG A CZ  1 
ATOM   1270  N  NH1 . ARG A 1 590  ? 95.302  110.036 96.644  1.00 42.19  ? 161  ARG A NH1 1 
ATOM   1271  N  NH2 . ARG A 1 590  ? 97.281  109.522 95.563  1.00 40.89  ? 161  ARG A NH2 1 
ATOM   1272  N  N   . GLY A 1 591  ? 96.192  105.259 101.750 1.00 30.58  ? 162  GLY A N   1 
ATOM   1273  C  CA  . GLY A 1 591  ? 95.215  104.654 102.619 1.00 33.09  ? 162  GLY A CA  1 
ATOM   1274  C  C   . GLY A 1 591  ? 94.830  105.586 103.737 1.00 39.09  ? 162  GLY A C   1 
ATOM   1275  O  O   . GLY A 1 591  ? 93.658  105.695 104.084 1.00 59.29  ? 162  GLY A O   1 
ATOM   1276  N  N   . ARG A 1 592  ? 95.802  106.276 104.314 1.00 33.06  ? 163  ARG A N   1 
ATOM   1277  C  CA  . ARG A 1 592  ? 95.481  107.157 105.428 1.00 42.88  ? 163  ARG A CA  1 
ATOM   1278  C  C   . ARG A 1 592  ? 94.683  108.368 104.958 1.00 52.64  ? 163  ARG A C   1 
ATOM   1279  O  O   . ARG A 1 592  ? 93.764  108.821 105.652 1.00 59.15  ? 163  ARG A O   1 
ATOM   1280  C  CB  . ARG A 1 592  ? 96.770  107.587 106.133 1.00 54.25  ? 163  ARG A CB  1 
ATOM   1281  C  CG  . ARG A 1 592  ? 97.509  106.470 106.872 1.00 51.27  ? 163  ARG A CG  1 
ATOM   1282  C  CD  . ARG A 1 592  ? 98.683  107.021 107.651 1.00 40.50  ? 163  ARG A CD  1 
ATOM   1283  N  NE  . ARG A 1 592  ? 98.345  107.287 109.029 1.00 46.95  ? 163  ARG A NE  1 
ATOM   1284  C  CZ  . ARG A 1 592  ? 99.187  107.848 109.881 1.00 64.92  ? 163  ARG A CZ  1 
ATOM   1285  N  NH1 . ARG A 1 592  ? 100.400 108.199 109.466 1.00 64.99  ? 163  ARG A NH1 1 
ATOM   1286  N  NH2 . ARG A 1 592  ? 98.822  108.062 111.140 1.00 69.08  ? 163  ARG A NH2 1 
ATOM   1287  N  N   . LEU A 1 593  ? 95.022  108.906 103.781 1.00 56.28  ? 164  LEU A N   1 
ATOM   1288  C  CA  . LEU A 1 593  ? 94.365  110.118 103.295 1.00 45.26  ? 164  LEU A CA  1 
ATOM   1289  C  C   . LEU A 1 593  ? 92.872  109.914 103.177 1.00 51.95  ? 164  LEU A C   1 
ATOM   1290  O  O   . LEU A 1 593  ? 92.087  110.816 103.488 1.00 66.98  ? 164  LEU A O   1 
ATOM   1291  C  CB  . LEU A 1 593  ? 94.966  110.542 101.960 1.00 41.27  ? 164  LEU A CB  1 
ATOM   1292  C  CG  . LEU A 1 593  ? 94.675  111.958 101.487 1.00 59.55  ? 164  LEU A CG  1 
ATOM   1293  C  CD1 . LEU A 1 593  ? 95.807  112.477 100.615 1.00 59.73  ? 164  LEU A CD1 1 
ATOM   1294  C  CD2 . LEU A 1 593  ? 93.383  111.939 100.676 1.00 68.72  ? 164  LEU A CD2 1 
ATOM   1295  N  N   . ASN A 1 594  ? 92.457  108.730 102.768 1.00 52.86  ? 165  ASN A N   1 
ATOM   1296  C  CA  . ASN A 1 594  ? 91.036  108.474 102.615 1.00 73.65  ? 165  ASN A CA  1 
ATOM   1297  C  C   . ASN A 1 594  ? 90.601  107.352 103.554 1.00 86.70  ? 165  ASN A C   1 
ATOM   1298  O  O   . ASN A 1 594  ? 89.927  106.403 103.137 1.00 96.37  ? 165  ASN A O   1 
ATOM   1299  C  CB  . ASN A 1 594  ? 90.695  108.168 101.147 1.00 81.30  ? 165  ASN A CB  1 
ATOM   1300  C  CG  . ASN A 1 594  ? 91.631  107.145 100.516 1.00 84.25  ? 165  ASN A CG  1 
ATOM   1301  O  OD1 . ASN A 1 594  ? 91.948  106.107 101.112 1.00 85.59  ? 165  ASN A OD1 1 
ATOM   1302  N  ND2 . ASN A 1 594  ? 92.069  107.431 99.294  1.00 82.77  ? 165  ASN A ND2 1 
ATOM   1303  N  N   . ARG A 1 595  ? 90.994  107.461 104.832 1.00 86.77  ? 166  ARG A N   1 
ATOM   1304  C  CA  . ARG A 1 595  ? 90.774  106.392 105.814 1.00 99.02  ? 166  ARG A CA  1 
ATOM   1305  C  C   . ARG A 1 595  ? 89.294  106.037 105.991 1.00 111.99 ? 166  ARG A C   1 
ATOM   1306  O  O   . ARG A 1 595  ? 88.970  104.878 106.292 1.00 108.07 ? 166  ARG A O   1 
ATOM   1307  C  CB  . ARG A 1 595  ? 91.376  106.800 107.165 1.00 101.76 ? 166  ARG A CB  1 
ATOM   1308  C  CG  . ARG A 1 595  ? 91.320  105.746 108.285 1.00 93.56  ? 166  ARG A CG  1 
ATOM   1309  C  CD  . ARG A 1 595  ? 92.025  106.283 109.546 1.00 97.50  ? 166  ARG A CD  1 
ATOM   1310  N  NE  . ARG A 1 595  ? 91.886  107.747 109.650 1.00 108.54 ? 166  ARG A NE  1 
ATOM   1311  C  CZ  . ARG A 1 595  ? 90.944  108.394 110.343 1.00 109.25 ? 166  ARG A CZ  1 
ATOM   1312  N  NH1 . ARG A 1 595  ? 90.026  107.724 111.033 1.00 102.06 ? 166  ARG A NH1 1 
ATOM   1313  N  NH2 . ARG A 1 595  ? 90.919  109.722 110.346 1.00 98.26  ? 166  ARG A NH2 1 
ATOM   1314  N  N   . GLY A 1 596  ? 88.387  107.018 105.843 1.00 111.90 ? 167  GLY A N   1 
ATOM   1315  C  CA  . GLY A 1 596  ? 86.953  106.760 105.939 1.00 115.32 ? 167  GLY A CA  1 
ATOM   1316  C  C   . GLY A 1 596  ? 86.301  106.210 104.677 1.00 118.71 ? 167  GLY A C   1 
ATOM   1317  O  O   . GLY A 1 596  ? 85.195  105.663 104.757 1.00 116.25 ? 167  GLY A O   1 
ATOM   1318  N  N   . ASN A 1 597  ? 86.956  106.346 103.519 1.00 118.23 ? 168  ASN A N   1 
ATOM   1319  C  CA  . ASN A 1 597  ? 86.439  105.888 102.231 1.00 123.48 ? 168  ASN A CA  1 
ATOM   1320  C  C   . ASN A 1 597  ? 86.757  104.395 102.020 1.00 120.86 ? 168  ASN A C   1 
ATOM   1321  O  O   . ASN A 1 597  ? 87.443  103.757 102.829 1.00 115.44 ? 168  ASN A O   1 
ATOM   1322  C  CB  . ASN A 1 597  ? 87.025  106.735 101.086 1.00 120.95 ? 168  ASN A CB  1 
ATOM   1323  C  CG  . ASN A 1 597  ? 86.544  108.204 101.099 1.00 113.05 ? 168  ASN A CG  1 
ATOM   1324  O  OD1 . ASN A 1 597  ? 85.436  108.515 101.550 1.00 110.38 ? 168  ASN A OD1 1 
ATOM   1325  N  ND2 . ASN A 1 597  ? 87.382  109.103 100.573 1.00 98.13  ? 168  ASN A ND2 1 
ATOM   1326  N  N   . SER A 1 598  ? 86.246  103.833 100.910 1.00 120.50 ? 169  SER A N   1 
ATOM   1327  C  CA  . SER A 1 598  ? 86.445  102.410 100.611 1.00 120.67 ? 169  SER A CA  1 
ATOM   1328  C  C   . SER A 1 598  ? 87.866  102.092 100.131 1.00 112.08 ? 169  SER A C   1 
ATOM   1329  O  O   . SER A 1 598  ? 88.288  100.929 100.208 1.00 99.73  ? 169  SER A O   1 
ATOM   1330  C  CB  . SER A 1 598  ? 85.415  101.941 99.569  1.00 115.77 ? 169  SER A CB  1 
ATOM   1331  O  OG  . SER A 1 598  ? 85.560  100.560 99.256  1.00 106.82 ? 169  SER A OG  1 
ATOM   1332  N  N   . ARG A 1 599  ? 88.616  103.099 99.657  1.00 112.34 ? 170  ARG A N   1 
ATOM   1333  C  CA  . ARG A 1 599  ? 89.972  102.944 99.121  1.00 108.07 ? 170  ARG A CA  1 
ATOM   1334  C  C   . ARG A 1 599  ? 91.021  102.669 100.204 1.00 95.30  ? 170  ARG A C   1 
ATOM   1335  O  O   . ARG A 1 599  ? 92.193  102.463 99.855  1.00 88.58  ? 170  ARG A O   1 
ATOM   1336  C  CB  . ARG A 1 599  ? 90.367  104.203 98.316  1.00 109.53 ? 170  ARG A CB  1 
ATOM   1337  C  CG  . ARG A 1 599  ? 91.405  104.001 97.173  1.00 104.10 ? 170  ARG A CG  1 
ATOM   1338  C  CD  . ARG A 1 599  ? 91.935  105.349 96.611  1.00 100.51 ? 170  ARG A CD  1 
ATOM   1339  N  NE  . ARG A 1 599  ? 90.874  106.268 96.177  1.00 113.38 ? 170  ARG A NE  1 
ATOM   1340  C  CZ  . ARG A 1 599  ? 91.070  107.516 95.736  1.00 111.21 ? 170  ARG A CZ  1 
ATOM   1341  N  NH1 . ARG A 1 599  ? 92.297  108.037 95.685  1.00 90.22  ? 170  ARG A NH1 1 
ATOM   1342  N  NH2 . ARG A 1 599  ? 90.028  108.258 95.364  1.00 105.13 ? 170  ARG A NH2 1 
ATOM   1343  N  N   . SER A 1 600  ? 90.644  102.668 101.493 1.00 89.68  ? 171  SER A N   1 
ATOM   1344  C  CA  . SER A 1 600  ? 91.633  102.471 102.555 1.00 84.82  ? 171  SER A CA  1 
ATOM   1345  C  C   . SER A 1 600  ? 92.304  101.100 102.454 1.00 76.58  ? 171  SER A C   1 
ATOM   1346  O  O   . SER A 1 600  ? 93.532  100.995 102.582 1.00 66.59  ? 171  SER A O   1 
ATOM   1347  C  CB  . SER A 1 600  ? 90.987  102.650 103.939 1.00 83.57  ? 171  SER A CB  1 
ATOM   1348  O  OG  . SER A 1 600  ? 89.961  101.692 104.192 1.00 75.31  ? 171  SER A OG  1 
ATOM   1349  N  N   . THR A 1 601  ? 91.527  100.041 102.221 1.00 63.21  ? 172  THR A N   1 
ATOM   1350  C  CA  . THR A 1 601  ? 92.102  98.711  102.273 1.00 35.07  ? 172  THR A CA  1 
ATOM   1351  C  C   . THR A 1 601  ? 92.993  98.491  101.086 1.00 24.66  ? 172  THR A C   1 
ATOM   1352  O  O   . THR A 1 601  ? 92.694  98.916  99.975  1.00 39.89  ? 172  THR A O   1 
ATOM   1353  C  CB  . THR A 1 601  ? 91.025  97.646  102.302 1.00 52.26  ? 172  THR A CB  1 
ATOM   1354  O  OG1 . THR A 1 601  ? 90.059  97.976  103.309 1.00 62.39  ? 172  THR A OG1 1 
ATOM   1355  C  CG2 . THR A 1 601  ? 91.650  96.301  102.651 1.00 53.27  ? 172  THR A CG2 1 
ATOM   1356  N  N   . TRP A 1 602  ? 94.101  97.839  101.334 1.00 24.98  ? 173  TRP A N   1 
ATOM   1357  C  CA  . TRP A 1 602  ? 95.001  97.462  100.271 1.00 33.29  ? 173  TRP A CA  1 
ATOM   1358  C  C   . TRP A 1 602  ? 95.653  96.163  100.685 1.00 38.94  ? 173  TRP A C   1 
ATOM   1359  O  O   . TRP A 1 602  ? 95.775  95.868  101.878 1.00 45.24  ? 173  TRP A O   1 
ATOM   1360  C  CB  . TRP A 1 602  ? 96.044  98.536  100.023 1.00 41.43  ? 173  TRP A CB  1 
ATOM   1361  C  CG  . TRP A 1 602  ? 96.660  98.960  101.276 1.00 37.52  ? 173  TRP A CG  1 
ATOM   1362  C  CD1 . TRP A 1 602  ? 96.156  99.844  102.167 1.00 42.61  ? 173  TRP A CD1 1 
ATOM   1363  C  CD2 . TRP A 1 602  ? 97.917  98.542  101.789 1.00 33.46  ? 173  TRP A CD2 1 
ATOM   1364  N  NE1 . TRP A 1 602  ? 97.014  99.994  103.226 1.00 40.33  ? 173  TRP A NE1 1 
ATOM   1365  C  CE2 . TRP A 1 602  ? 98.107  99.203  103.014 1.00 33.95  ? 173  TRP A CE2 1 
ATOM   1366  C  CE3 . TRP A 1 602  ? 98.904  97.672  101.331 1.00 41.36  ? 173  TRP A CE3 1 
ATOM   1367  C  CZ2 . TRP A 1 602  ? 99.234  99.022  103.790 1.00 42.68  ? 173  TRP A CZ2 1 
ATOM   1368  C  CZ3 . TRP A 1 602  ? 100.035 97.491  102.101 1.00 42.56  ? 173  TRP A CZ3 1 
ATOM   1369  C  CH2 . TRP A 1 602  ? 100.190 98.162  103.320 1.00 47.42  ? 173  TRP A CH2 1 
ATOM   1370  N  N   . PHE A 1 603  ? 96.045  95.374  99.701  1.00 35.37  ? 174  PHE A N   1 
ATOM   1371  C  CA  . PHE A 1 603  ? 96.525  94.031  99.964  1.00 29.93  ? 174  PHE A CA  1 
ATOM   1372  C  C   . PHE A 1 603  ? 97.789  93.790  99.180  1.00 26.02  ? 174  PHE A C   1 
ATOM   1373  O  O   . PHE A 1 603  ? 97.831  94.033  97.976  1.00 39.72  ? 174  PHE A O   1 
ATOM   1374  C  CB  . PHE A 1 603  ? 95.492  93.006  99.567  1.00 37.74  ? 174  PHE A CB  1 
ATOM   1375  C  CG  . PHE A 1 603  ? 95.937  91.615  99.766  1.00 41.36  ? 174  PHE A CG  1 
ATOM   1376  C  CD1 . PHE A 1 603  ? 95.778  90.987  100.990 1.00 44.06  ? 174  PHE A CD1 1 
ATOM   1377  C  CD2 . PHE A 1 603  ? 96.578  90.937  98.742  1.00 51.80  ? 174  PHE A CD2 1 
ATOM   1378  C  CE1 . PHE A 1 603  ? 96.208  89.667  101.173 1.00 52.52  ? 174  PHE A CE1 1 
ATOM   1379  C  CE2 . PHE A 1 603  ? 97.019  89.623  98.913  1.00 58.30  ? 174  PHE A CE2 1 
ATOM   1380  C  CZ  . PHE A 1 603  ? 96.836  88.985  100.132 1.00 55.19  ? 174  PHE A CZ  1 
ATOM   1381  N  N   . VAL A 1 604  ? 98.798  93.281  99.842  1.00 27.16  ? 175  VAL A N   1 
ATOM   1382  C  CA  . VAL A 1 604  ? 100.049 92.974  99.192  1.00 26.12  ? 175  VAL A CA  1 
ATOM   1383  C  C   . VAL A 1 604  ? 100.445 91.569  99.570  1.00 35.23  ? 175  VAL A C   1 
ATOM   1384  O  O   . VAL A 1 604  ? 100.387 91.193  100.745 1.00 46.31  ? 175  VAL A O   1 
ATOM   1385  C  CB  . VAL A 1 604  ? 101.144 93.950  99.605  1.00 43.51  ? 175  VAL A CB  1 
ATOM   1386  C  CG1 . VAL A 1 604  ? 102.431 93.597  98.879  1.00 52.60  ? 175  VAL A CG1 1 
ATOM   1387  C  CG2 . VAL A 1 604  ? 100.680 95.349  99.327  1.00 47.66  ? 175  VAL A CG2 1 
ATOM   1388  N  N   . HIS A 1 605  ? 100.836 90.796  98.592  1.00 38.94  ? 176  HIS A N   1 
ATOM   1389  C  CA  . HIS A 1 605  ? 101.205 89.414  98.814  1.00 39.38  ? 176  HIS A CA  1 
ATOM   1390  C  C   . HIS A 1 605  ? 102.631 89.240  98.361  1.00 44.58  ? 176  HIS A C   1 
ATOM   1391  O  O   . HIS A 1 605  ? 102.890 89.123  97.160  1.00 56.98  ? 176  HIS A O   1 
ATOM   1392  C  CB  . HIS A 1 605  ? 100.288 88.477  98.053  1.00 46.80  ? 176  HIS A CB  1 
ATOM   1393  C  CG  . HIS A 1 605  ? 100.711 87.054  98.129  1.00 52.28  ? 176  HIS A CG  1 
ATOM   1394  N  ND1 . HIS A 1 605  ? 100.681 86.331  99.301  1.00 59.40  ? 176  HIS A ND1 1 
ATOM   1395  C  CD2 . HIS A 1 605  ? 101.175 86.213  97.176  1.00 60.98  ? 176  HIS A CD2 1 
ATOM   1396  C  CE1 . HIS A 1 605  ? 101.114 85.103  99.069  1.00 65.20  ? 176  HIS A CE1 1 
ATOM   1397  N  NE2 . HIS A 1 605  ? 101.417 85.004  97.786  1.00 67.84  ? 176  HIS A NE2 1 
ATOM   1398  N  N   . ASP A 1 606  ? 103.547 89.210  99.308  1.00 50.99  ? 177  ASP A N   1 
ATOM   1399  C  CA  . ASP A 1 606  ? 104.929 88.917  98.976  1.00 54.09  ? 177  ASP A CA  1 
ATOM   1400  C  C   . ASP A 1 606  ? 105.125 87.407  98.881  1.00 61.12  ? 177  ASP A C   1 
ATOM   1401  O  O   . ASP A 1 606  ? 104.165 86.631  98.847  1.00 65.02  ? 177  ASP A O   1 
ATOM   1402  C  CB  . ASP A 1 606  ? 105.881 89.539  99.985  1.00 56.69  ? 177  ASP A CB  1 
ATOM   1403  C  CG  . ASP A 1 606  ? 107.284 89.664  99.430  1.00 65.95  ? 177  ASP A CG  1 
ATOM   1404  O  OD1 . ASP A 1 606  ? 107.435 90.247  98.333  1.00 66.11  ? 177  ASP A OD1 1 
ATOM   1405  O  OD2 . ASP A 1 606  ? 108.231 89.147  100.070 1.00 65.19  ? 177  ASP A OD2 1 
ATOM   1406  N  N   . ASP A 1 607  ? 106.383 86.977  98.820  1.00 57.31  ? 178  ASP A N   1 
ATOM   1407  C  CA  . ASP A 1 607  ? 106.663 85.555  98.706  1.00 57.69  ? 178  ASP A CA  1 
ATOM   1408  C  C   . ASP A 1 607  ? 106.027 84.780  99.852  1.00 58.12  ? 178  ASP A C   1 
ATOM   1409  O  O   . ASP A 1 607  ? 105.406 83.735  99.630  1.00 62.62  ? 178  ASP A O   1 
ATOM   1410  C  CB  . ASP A 1 607  ? 108.176 85.324  98.656  1.00 75.88  ? 178  ASP A CB  1 
ATOM   1411  C  CG  . ASP A 1 607  ? 108.851 86.047  97.477  1.00 86.03  ? 178  ASP A CG  1 
ATOM   1412  O  OD1 . ASP A 1 607  ? 108.190 86.247  96.427  1.00 80.61  ? 178  ASP A OD1 1 
ATOM   1413  O  OD2 . ASP A 1 607  ? 110.051 86.397  97.594  1.00 81.88  ? 178  ASP A OD2 1 
ATOM   1414  N  N   . LEU A 1 608  ? 106.130 85.295  101.078 1.00 57.69  ? 179  LEU A N   1 
ATOM   1415  C  CA  . LEU A 1 608  ? 105.603 84.588  102.237 1.00 51.83  ? 179  LEU A CA  1 
ATOM   1416  C  C   . LEU A 1 608  ? 104.877 85.477  103.241 1.00 43.92  ? 179  LEU A C   1 
ATOM   1417  O  O   . LEU A 1 608  ? 104.354 84.952  104.227 1.00 48.25  ? 179  LEU A O   1 
ATOM   1418  C  CB  . LEU A 1 608  ? 106.747 83.818  102.935 1.00 64.74  ? 179  LEU A CB  1 
ATOM   1419  C  CG  . LEU A 1 608  ? 107.869 84.540  103.714 1.00 78.40  ? 179  LEU A CG  1 
ATOM   1420  C  CD1 . LEU A 1 608  ? 108.730 83.540  104.542 1.00 70.65  ? 179  LEU A CD1 1 
ATOM   1421  C  CD2 . LEU A 1 608  ? 108.760 85.443  102.817 1.00 73.67  ? 179  LEU A CD2 1 
ATOM   1422  N  N   . ILE A 1 609  ? 104.797 86.784  103.012 1.00 44.00  ? 180  ILE A N   1 
ATOM   1423  C  CA  . ILE A 1 609  ? 104.195 87.737  103.939 1.00 44.99  ? 180  ILE A CA  1 
ATOM   1424  C  C   . ILE A 1 609  ? 102.970 88.373  103.286 1.00 47.41  ? 180  ILE A C   1 
ATOM   1425  O  O   . ILE A 1 609  ? 103.026 88.772  102.118 1.00 56.27  ? 180  ILE A O   1 
ATOM   1426  C  CB  . ILE A 1 609  ? 105.214 88.831  104.327 1.00 53.71  ? 180  ILE A CB  1 
ATOM   1427  C  CG1 . ILE A 1 609  ? 106.538 88.214  104.757 1.00 60.19  ? 180  ILE A CG1 1 
ATOM   1428  C  CG2 . ILE A 1 609  ? 104.671 89.747  105.444 1.00 56.74  ? 180  ILE A CG2 1 
ATOM   1429  C  CD1 . ILE A 1 609  ? 106.432 87.449  106.065 1.00 69.19  ? 180  ILE A CD1 1 
ATOM   1430  N  N   . ASP A 1 610  ? 101.875 88.499  104.030 1.00 31.23  ? 181  ASP A N   1 
ATOM   1431  C  CA  . ASP A 1 610  ? 100.696 89.188  103.532 1.00 24.96  ? 181  ASP A CA  1 
ATOM   1432  C  C   . ASP A 1 610  ? 100.442 90.413  104.372 1.00 27.87  ? 181  ASP A C   1 
ATOM   1433  O  O   . ASP A 1 610  ? 100.419 90.332  105.598 1.00 40.42  ? 181  ASP A O   1 
ATOM   1434  C  CB  . ASP A 1 610  ? 99.488  88.297  103.572 1.00 40.87  ? 181  ASP A CB  1 
ATOM   1435  C  CG  . ASP A 1 610  ? 99.647  87.111  102.687 1.00 59.13  ? 181  ASP A CG  1 
ATOM   1436  O  OD1 . ASP A 1 610  ? 100.754 86.968  102.123 1.00 57.50  ? 181  ASP A OD1 1 
ATOM   1437  O  OD2 . ASP A 1 610  ? 98.679  86.326  102.538 1.00 60.29  ? 181  ASP A OD2 1 
ATOM   1438  N  N   . ILE A 1 611  ? 100.244 91.534  103.724 1.00 24.04  ? 182  ILE A N   1 
ATOM   1439  C  CA  . ILE A 1 611  ? 100.427 92.774  104.437 1.00 22.61  ? 182  ILE A CA  1 
ATOM   1440  C  C   . ILE A 1 611  ? 99.146  93.555  104.315 1.00 21.20  ? 182  ILE A C   1 
ATOM   1441  O  O   . ILE A 1 611  ? 99.170  94.776  104.185 1.00 32.51  ? 182  ILE A O   1 
ATOM   1442  C  CB  . ILE A 1 611  ? 101.635 93.550  103.881 1.00 37.86  ? 182  ILE A CB  1 
ATOM   1443  C  CG1 . ILE A 1 611  ? 102.864 92.650  103.908 1.00 49.53  ? 182  ILE A CG1 1 
ATOM   1444  C  CG2 . ILE A 1 611  ? 102.014 94.749  104.756 1.00 43.08  ? 182  ILE A CG2 1 
ATOM   1445  C  CD1 . ILE A 1 611  ? 104.078 93.255  103.238 1.00 58.07  ? 182  ILE A CD1 1 
ATOM   1446  N  N   . LEU A 1 612  ? 98.018  92.879  104.314 1.00 24.15  ? 183  LEU A N   1 
ATOM   1447  C  CA  . LEU A 1 612  ? 96.777  93.613  104.117 1.00 27.20  ? 183  LEU A CA  1 
ATOM   1448  C  C   . LEU A 1 612  ? 96.670  94.763  105.081 1.00 21.52  ? 183  LEU A C   1 
ATOM   1449  O  O   . LEU A 1 612  ? 96.999  94.632  106.257 1.00 36.50  ? 183  LEU A O   1 
ATOM   1450  C  CB  . LEU A 1 612  ? 95.569  92.731  104.322 1.00 48.07  ? 183  LEU A CB  1 
ATOM   1451  C  CG  . LEU A 1 612  ? 94.282  93.547  104.161 1.00 50.92  ? 183  LEU A CG  1 
ATOM   1452  C  CD1 . LEU A 1 612  ? 93.278  92.707  103.394 1.00 57.21  ? 183  LEU A CD1 1 
ATOM   1453  C  CD2 . LEU A 1 612  ? 93.693  93.947  105.512 1.00 48.20  ? 183  LEU A CD2 1 
ATOM   1454  N  N   . GLY A 1 613  ? 96.196  95.887  104.593 1.00 27.45  ? 184  GLY A N   1 
ATOM   1455  C  CA  . GLY A 1 613  ? 96.253  97.074  105.419 1.00 34.03  ? 184  GLY A CA  1 
ATOM   1456  C  C   . GLY A 1 613  ? 95.008  97.928  105.354 1.00 37.18  ? 184  GLY A C   1 
ATOM   1457  O  O   . GLY A 1 613  ? 94.450  98.144  104.274 1.00 47.62  ? 184  GLY A O   1 
ATOM   1458  N  N   . TYR A 1 614  ? 94.571  98.424  106.491 1.00 29.88  ? 185  TYR A N   1 
ATOM   1459  C  CA  . TYR A 1 614  ? 93.401  99.275  106.601 1.00 25.46  ? 185  TYR A CA  1 
ATOM   1460  C  C   . TYR A 1 614  ? 93.837  100.725 106.536 1.00 30.10  ? 185  TYR A C   1 
ATOM   1461  O  O   . TYR A 1 614  ? 94.960  101.023 106.128 1.00 36.97  ? 185  TYR A O   1 
ATOM   1462  C  CB  . TYR A 1 614  ? 92.698  98.998  107.897 1.00 33.65  ? 185  TYR A CB  1 
ATOM   1463  C  CG  . TYR A 1 614  ? 91.267  99.307  107.853 1.00 27.92  ? 185  TYR A CG  1 
ATOM   1464  C  CD1 . TYR A 1 614  ? 90.717  100.107 108.814 1.00 47.44  ? 185  TYR A CD1 1 
ATOM   1465  C  CD2 . TYR A 1 614  ? 90.458  98.761  106.910 1.00 35.53  ? 185  TYR A CD2 1 
ATOM   1466  C  CE1 . TYR A 1 614  ? 89.415  100.381 108.824 1.00 53.59  ? 185  TYR A CE1 1 
ATOM   1467  C  CE2 . TYR A 1 614  ? 89.132  99.026  106.907 1.00 46.26  ? 185  TYR A CE2 1 
ATOM   1468  C  CZ  . TYR A 1 614  ? 88.619  99.841  107.877 1.00 47.44  ? 185  TYR A CZ  1 
ATOM   1469  O  OH  . TYR A 1 614  ? 87.289  100.136 107.906 1.00 64.74  ? 185  TYR A OH  1 
ATOM   1470  N  N   . GLY A 1 615  ? 92.968  101.634 106.941 1.00 38.01  ? 186  GLY A N   1 
ATOM   1471  C  CA  . GLY A 1 615  ? 93.342  103.029 106.913 1.00 48.24  ? 186  GLY A CA  1 
ATOM   1472  C  C   . GLY A 1 615  ? 94.715  103.317 107.493 1.00 41.99  ? 186  GLY A C   1 
ATOM   1473  O  O   . GLY A 1 615  ? 95.657  103.607 106.745 1.00 44.07  ? 186  GLY A O   1 
ATOM   1474  N  N   . ASP A 1 616  ? 94.862  103.200 108.809 1.00 37.03  ? 187  ASP A N   1 
ATOM   1475  C  CA  . ASP A 1 616  ? 96.161  103.382 109.443 1.00 33.32  ? 187  ASP A CA  1 
ATOM   1476  C  C   . ASP A 1 616  ? 96.470  102.219 110.362 1.00 35.53  ? 187  ASP A C   1 
ATOM   1477  O  O   . ASP A 1 616  ? 97.199  102.379 111.339 1.00 45.39  ? 187  ASP A O   1 
ATOM   1478  C  CB  . ASP A 1 616  ? 96.212  104.682 110.223 1.00 46.18  ? 187  ASP A CB  1 
ATOM   1479  C  CG  . ASP A 1 616  ? 95.011  104.836 111.108 1.00 61.77  ? 187  ASP A CG  1 
ATOM   1480  O  OD1 . ASP A 1 616  ? 94.078  104.018 110.930 1.00 59.82  ? 187  ASP A OD1 1 
ATOM   1481  O  OD2 . ASP A 1 616  ? 94.977  105.756 111.958 1.00 66.42  ? 187  ASP A OD2 1 
ATOM   1482  N  N   . TYR A 1 617  ? 95.896  101.070 110.081 1.00 31.93  ? 188  TYR A N   1 
ATOM   1483  C  CA  . TYR A 1 617  ? 96.294  99.832  110.698 1.00 26.22  ? 188  TYR A CA  1 
ATOM   1484  C  C   . TYR A 1 617  ? 96.797  98.894  109.622 1.00 35.03  ? 188  TYR A C   1 
ATOM   1485  O  O   . TYR A 1 617  ? 96.122  98.696  108.608 1.00 43.73  ? 188  TYR A O   1 
ATOM   1486  C  CB  . TYR A 1 617  ? 95.121  99.231  111.395 1.00 26.69  ? 188  TYR A CB  1 
ATOM   1487  C  CG  . TYR A 1 617  ? 94.628  100.186 112.337 1.00 22.59  ? 188  TYR A CG  1 
ATOM   1488  C  CD1 . TYR A 1 617  ? 93.520  100.911 112.067 1.00 37.27  ? 188  TYR A CD1 1 
ATOM   1489  C  CD2 . TYR A 1 617  ? 95.341  100.447 113.467 1.00 33.06  ? 188  TYR A CD2 1 
ATOM   1490  C  CE1 . TYR A 1 617  ? 93.070  101.837 112.961 1.00 55.53  ? 188  TYR A CE1 1 
ATOM   1491  C  CE2 . TYR A 1 617  ? 94.927  101.358 114.372 1.00 41.40  ? 188  TYR A CE2 1 
ATOM   1492  C  CZ  . TYR A 1 617  ? 93.786  102.063 114.121 1.00 48.52  ? 188  TYR A CZ  1 
ATOM   1493  O  OH  . TYR A 1 617  ? 93.349  103.003 115.030 1.00 53.78  ? 188  TYR A OH  1 
ATOM   1494  N  N   . VAL A 1 618  ? 97.954  98.294  109.844 1.00 28.91  ? 189  VAL A N   1 
ATOM   1495  C  CA  . VAL A 1 618  ? 98.520  97.345  108.902 1.00 23.69  ? 189  VAL A CA  1 
ATOM   1496  C  C   . VAL A 1 618  ? 98.513  95.976  109.540 1.00 29.84  ? 189  VAL A C   1 
ATOM   1497  O  O   . VAL A 1 618  ? 99.172  95.773  110.565 1.00 40.83  ? 189  VAL A O   1 
ATOM   1498  C  CB  . VAL A 1 618  ? 99.948  97.724  108.530 1.00 28.88  ? 189  VAL A CB  1 
ATOM   1499  C  CG1 . VAL A 1 618  ? 100.443 96.788  107.461 1.00 38.99  ? 189  VAL A CG1 1 
ATOM   1500  C  CG2 . VAL A 1 618  ? 100.003 99.173  108.093 1.00 43.13  ? 189  VAL A CG2 1 
ATOM   1501  N  N   . PHE A 1 619  ? 97.829  95.024  108.926 1.00 25.06  ? 190  PHE A N   1 
ATOM   1502  C  CA  . PHE A 1 619  ? 97.900  93.638  109.372 1.00 24.91  ? 190  PHE A CA  1 
ATOM   1503  C  C   . PHE A 1 619  ? 99.039  92.941  108.644 1.00 39.71  ? 190  PHE A C   1 
ATOM   1504  O  O   . PHE A 1 619  ? 99.158  93.065  107.421 1.00 46.75  ? 190  PHE A O   1 
ATOM   1505  C  CB  . PHE A 1 619  ? 96.598  92.926  109.080 1.00 20.43  ? 190  PHE A CB  1 
ATOM   1506  C  CG  . PHE A 1 619  ? 95.447  93.582  109.674 1.00 24.58  ? 190  PHE A CG  1 
ATOM   1507  C  CD1 . PHE A 1 619  ? 94.862  94.654  109.043 1.00 31.97  ? 190  PHE A CD1 1 
ATOM   1508  C  CD2 . PHE A 1 619  ? 94.916  93.123  110.860 1.00 36.09  ? 190  PHE A CD2 1 
ATOM   1509  C  CE1 . PHE A 1 619  ? 93.772  95.298  109.595 1.00 37.87  ? 190  PHE A CE1 1 
ATOM   1510  C  CE2 . PHE A 1 619  ? 93.823  93.744  111.427 1.00 40.92  ? 190  PHE A CE2 1 
ATOM   1511  C  CZ  . PHE A 1 619  ? 93.243  94.843  110.787 1.00 45.06  ? 190  PHE A CZ  1 
ATOM   1512  N  N   . TRP A 1 620  ? 99.886  92.220  109.370 1.00 29.46  ? 191  TRP A N   1 
ATOM   1513  C  CA  . TRP A 1 620  ? 100.933 91.459  108.712 1.00 29.07  ? 191  TRP A CA  1 
ATOM   1514  C  C   . TRP A 1 620  ? 100.679 89.979  108.943 1.00 44.10  ? 191  TRP A C   1 
ATOM   1515  O  O   . TRP A 1 620  ? 100.538 89.553  110.091 1.00 50.78  ? 191  TRP A O   1 
ATOM   1516  C  CB  . TRP A 1 620  ? 102.306 91.820  109.241 1.00 31.63  ? 191  TRP A CB  1 
ATOM   1517  C  CG  . TRP A 1 620  ? 102.562 93.251  109.380 1.00 30.37  ? 191  TRP A CG  1 
ATOM   1518  C  CD1 . TRP A 1 620  ? 102.104 94.044  110.361 1.00 36.84  ? 191  TRP A CD1 1 
ATOM   1519  C  CD2 . TRP A 1 620  ? 103.419 94.056  108.586 1.00 30.09  ? 191  TRP A CD2 1 
ATOM   1520  N  NE1 . TRP A 1 620  ? 102.590 95.307  110.223 1.00 35.65  ? 191  TRP A NE1 1 
ATOM   1521  C  CE2 . TRP A 1 620  ? 103.406 95.340  109.134 1.00 27.57  ? 191  TRP A CE2 1 
ATOM   1522  C  CE3 . TRP A 1 620  ? 104.188 93.818  107.452 1.00 52.81  ? 191  TRP A CE3 1 
ATOM   1523  C  CZ2 . TRP A 1 620  ? 104.122 96.395  108.594 1.00 41.49  ? 191  TRP A CZ2 1 
ATOM   1524  C  CZ3 . TRP A 1 620  ? 104.913 94.875  106.909 1.00 52.74  ? 191  TRP A CZ3 1 
ATOM   1525  C  CH2 . TRP A 1 620  ? 104.868 96.147  107.482 1.00 43.29  ? 191  TRP A CH2 1 
ATOM   1526  N  N   . LYS A 1 621  ? 100.640 89.195  107.871 1.00 40.86  ? 192  LYS A N   1 
ATOM   1527  C  CA  . LYS A 1 621  ? 100.464 87.758  107.986 1.00 35.04  ? 192  LYS A CA  1 
ATOM   1528  C  C   . LYS A 1 621  ? 101.818 87.109  107.755 1.00 41.31  ? 192  LYS A C   1 
ATOM   1529  O  O   . LYS A 1 621  ? 102.359 87.190  106.652 1.00 51.36  ? 192  LYS A O   1 
ATOM   1530  C  CB  . LYS A 1 621  ? 99.443  87.246  106.979 1.00 33.23  ? 192  LYS A CB  1 
ATOM   1531  C  CG  . LYS A 1 621  ? 98.736  86.064  107.544 1.00 42.23  ? 192  LYS A CG  1 
ATOM   1532  C  CD  . LYS A 1 621  ? 97.900  85.327  106.552 1.00 46.80  ? 192  LYS A CD  1 
ATOM   1533  C  CE  . LYS A 1 621  ? 96.820  86.171  105.970 1.00 40.96  ? 192  LYS A CE  1 
ATOM   1534  N  NZ  . LYS A 1 621  ? 95.979  85.327  105.071 1.00 48.09  ? 192  LYS A NZ  1 
ATOM   1535  N  N   . ILE A 1 622  ? 102.366 86.467  108.780 1.00 43.16  ? 193  ILE A N   1 
ATOM   1536  C  CA  . ILE A 1 622  ? 103.731 85.939  108.715 1.00 47.86  ? 193  ILE A CA  1 
ATOM   1537  C  C   . ILE A 1 622  ? 103.732 84.444  108.998 1.00 48.35  ? 193  ILE A C   1 
ATOM   1538  O  O   . ILE A 1 622  ? 102.872 83.956  109.747 1.00 56.50  ? 193  ILE A O   1 
ATOM   1539  C  CB  . ILE A 1 622  ? 104.671 86.634  109.718 1.00 57.22  ? 193  ILE A CB  1 
ATOM   1540  C  CG1 . ILE A 1 622  ? 104.206 86.385  111.144 1.00 55.44  ? 193  ILE A CG1 1 
ATOM   1541  C  CG2 . ILE A 1 622  ? 104.715 88.134  109.502 1.00 58.67  ? 193  ILE A CG2 1 
ATOM   1542  C  CD1 . ILE A 1 622  ? 105.304 86.597  112.147 1.00 61.29  ? 193  ILE A CD1 1 
ATOM   1543  N  N   . PRO A 1 623  ? 104.691 83.688  108.465 1.00 39.64  ? 194  PRO A N   1 
ATOM   1544  C  CA  . PRO A 1 623  ? 104.747 82.255  108.763 1.00 41.02  ? 194  PRO A CA  1 
ATOM   1545  C  C   . PRO A 1 623  ? 105.264 82.023  110.174 1.00 50.29  ? 194  PRO A C   1 
ATOM   1546  O  O   . PRO A 1 623  ? 106.265 82.615  110.585 1.00 56.87  ? 194  PRO A O   1 
ATOM   1547  C  CB  . PRO A 1 623  ? 105.736 81.721  107.725 1.00 47.92  ? 194  PRO A CB  1 
ATOM   1548  C  CG  . PRO A 1 623  ? 105.842 82.782  106.704 1.00 45.89  ? 194  PRO A CG  1 
ATOM   1549  C  CD  . PRO A 1 623  ? 105.662 84.060  107.433 1.00 41.34  ? 194  PRO A CD  1 
ATOM   1550  N  N   . ILE A 1 624  ? 104.583 81.150  110.920 1.00 40.52  ? 195  ILE A N   1 
ATOM   1551  C  CA  . ILE A 1 624  ? 105.069 80.846  112.256 1.00 33.03  ? 195  ILE A CA  1 
ATOM   1552  C  C   . ILE A 1 624  ? 106.470 80.285  112.183 1.00 44.68  ? 195  ILE A C   1 
ATOM   1553  O  O   . ILE A 1 624  ? 107.292 80.522  113.077 1.00 54.19  ? 195  ILE A O   1 
ATOM   1554  C  CB  . ILE A 1 624  ? 104.128 79.872  112.968 1.00 36.89  ? 195  ILE A CB  1 
ATOM   1555  C  CG1 . ILE A 1 624  ? 102.821 80.563  113.284 1.00 51.54  ? 195  ILE A CG1 1 
ATOM   1556  C  CG2 . ILE A 1 624  ? 104.743 79.399  114.272 1.00 45.17  ? 195  ILE A CG2 1 
ATOM   1557  C  CD1 . ILE A 1 624  ? 102.985 81.612  114.354 1.00 59.93  ? 195  ILE A CD1 1 
ATOM   1558  N  N   . SER A 1 625  ? 106.783 79.567  111.110 1.00 40.86  ? 196  SER A N   1 
ATOM   1559  C  CA  . SER A 1 625  ? 108.038 78.836  111.091 1.00 46.07  ? 196  SER A CA  1 
ATOM   1560  C  C   . SER A 1 625  ? 109.224 79.764  111.291 1.00 51.43  ? 196  SER A C   1 
ATOM   1561  O  O   . SER A 1 625  ? 110.243 79.345  111.854 1.00 60.07  ? 196  SER A O   1 
ATOM   1562  C  CB  . SER A 1 625  ? 108.192 78.058  109.785 1.00 53.14  ? 196  SER A CB  1 
ATOM   1563  O  OG  . SER A 1 625  ? 108.274 78.937  108.675 1.00 52.99  ? 196  SER A OG  1 
ATOM   1564  N  N   . MET A 1 626  ? 109.118 81.024  110.879 1.00 42.66  ? 197  MET A N   1 
ATOM   1565  C  CA  . MET A 1 626  ? 110.299 81.872  110.901 1.00 44.70  ? 197  MET A CA  1 
ATOM   1566  C  C   . MET A 1 626  ? 110.397 82.720  112.160 1.00 49.31  ? 197  MET A C   1 
ATOM   1567  O  O   . MET A 1 626  ? 111.141 83.706  112.167 1.00 57.64  ? 197  MET A O   1 
ATOM   1568  C  CB  . MET A 1 626  ? 110.354 82.757  109.659 1.00 41.75  ? 197  MET A CB  1 
ATOM   1569  C  CG  . MET A 1 626  ? 109.291 83.802  109.588 1.00 47.14  ? 197  MET A CG  1 
ATOM   1570  S  SD  . MET A 1 626  ? 109.386 84.613  107.983 1.00 58.97  ? 197  MET A SD  1 
ATOM   1571  C  CE  . MET A 1 626  ? 111.161 84.754  107.787 1.00 51.15  ? 197  MET A CE  1 
ATOM   1572  N  N   . LEU A 1 627  ? 109.664 82.371  113.220 1.00 46.40  ? 198  LEU A N   1 
ATOM   1573  C  CA  . LEU A 1 627  ? 109.841 83.012  114.529 1.00 46.98  ? 198  LEU A CA  1 
ATOM   1574  C  C   . LEU A 1 627  ? 110.828 82.207  115.374 1.00 55.06  ? 198  LEU A C   1 
ATOM   1575  O  O   . LEU A 1 627  ? 110.677 80.981  115.483 1.00 56.89  ? 198  LEU A O   1 
ATOM   1576  C  CB  . LEU A 1 627  ? 108.523 83.094  115.271 1.00 41.17  ? 198  LEU A CB  1 
ATOM   1577  C  CG  . LEU A 1 627  ? 107.552 83.950  114.487 1.00 53.10  ? 198  LEU A CG  1 
ATOM   1578  C  CD1 . LEU A 1 627  ? 106.118 83.641  114.908 1.00 54.41  ? 198  LEU A CD1 1 
ATOM   1579  C  CD2 . LEU A 1 627  ? 107.919 85.409  114.657 1.00 62.81  ? 198  LEU A CD2 1 
ATOM   1580  N  N   . PRO A 1 628  ? 111.844 82.826  115.984 1.00 45.28  ? 199  PRO A N   1 
ATOM   1581  C  CA  . PRO A 1 628  ? 112.685 82.074  116.924 1.00 37.46  ? 199  PRO A CA  1 
ATOM   1582  C  C   . PRO A 1 628  ? 111.861 81.552  118.093 1.00 41.02  ? 199  PRO A C   1 
ATOM   1583  O  O   . PRO A 1 628  ? 110.983 82.247  118.608 1.00 45.57  ? 199  PRO A O   1 
ATOM   1584  C  CB  . PRO A 1 628  ? 113.718 83.108  117.377 1.00 39.71  ? 199  PRO A CB  1 
ATOM   1585  C  CG  . PRO A 1 628  ? 113.761 84.117  116.278 1.00 42.52  ? 199  PRO A CG  1 
ATOM   1586  C  CD  . PRO A 1 628  ? 112.350 84.193  115.774 1.00 49.28  ? 199  PRO A CD  1 
ATOM   1587  N  N   . LEU A 1 629  ? 112.158 80.327  118.524 1.00 33.17  ? 200  LEU A N   1 
ATOM   1588  C  CA  . LEU A 1 629  ? 111.429 79.707  119.620 1.00 27.69  ? 200  LEU A CA  1 
ATOM   1589  C  C   . LEU A 1 629  ? 112.178 79.852  120.928 1.00 32.72  ? 200  LEU A C   1 
ATOM   1590  O  O   . LEU A 1 629  ? 113.350 80.215  120.973 1.00 38.38  ? 200  LEU A O   1 
ATOM   1591  C  CB  . LEU A 1 629  ? 111.188 78.239  119.342 1.00 36.56  ? 200  LEU A CB  1 
ATOM   1592  C  CG  . LEU A 1 629  ? 110.225 78.070  118.187 1.00 45.29  ? 200  LEU A CG  1 
ATOM   1593  C  CD1 . LEU A 1 629  ? 110.166 76.615  117.759 1.00 52.55  ? 200  LEU A CD1 1 
ATOM   1594  C  CD2 . LEU A 1 629  ? 108.847 78.558  118.624 1.00 49.43  ? 200  LEU A CD2 1 
ATOM   1595  N  N   . ASN A 1 630  ? 111.476 79.574  122.003 1.00 33.62  ? 201  ASN A N   1 
ATOM   1596  C  CA  . ASN A 1 630  ? 112.048 79.570  123.337 1.00 37.04  ? 201  ASN A CA  1 
ATOM   1597  C  C   . ASN A 1 630  ? 112.124 78.125  123.820 1.00 40.14  ? 201  ASN A C   1 
ATOM   1598  O  O   . ASN A 1 630  ? 111.802 77.192  123.083 1.00 46.77  ? 201  ASN A O   1 
ATOM   1599  C  CB  . ASN A 1 630  ? 111.233 80.485  124.259 1.00 36.28  ? 201  ASN A CB  1 
ATOM   1600  C  CG  . ASN A 1 630  ? 109.923 79.870  124.707 1.00 51.41  ? 201  ASN A CG  1 
ATOM   1601  O  OD1 . ASN A 1 630  ? 109.412 78.938  124.087 1.00 57.76  ? 201  ASN A OD1 1 
ATOM   1602  N  ND2 . ASN A 1 630  ? 109.334 80.429  125.754 1.00 52.00  ? 201  ASN A ND2 1 
ATOM   1603  N  N   . THR A 1 631  ? 112.565 77.917  125.056 1.00 34.93  ? 202  THR A N   1 
ATOM   1604  C  CA  . THR A 1 631  ? 112.641 76.535  125.509 1.00 37.15  ? 202  THR A CA  1 
ATOM   1605  C  C   . THR A 1 631  ? 111.264 75.925  125.638 1.00 42.75  ? 202  THR A C   1 
ATOM   1606  O  O   . THR A 1 631  ? 111.092 74.730  125.389 1.00 53.48  ? 202  THR A O   1 
ATOM   1607  C  CB  . THR A 1 631  ? 113.338 76.427  126.851 1.00 47.06  ? 202  THR A CB  1 
ATOM   1608  O  OG1 . THR A 1 631  ? 112.448 76.891  127.875 1.00 50.30  ? 202  THR A OG1 1 
ATOM   1609  C  CG2 . THR A 1 631  ? 114.604 77.282  126.844 1.00 55.14  ? 202  THR A CG2 1 
ATOM   1610  N  N   . GLN A 1 632  ? 110.276 76.713  126.042 1.00 43.56  ? 203  GLN A N   1 
ATOM   1611  C  CA  . GLN A 1 632  ? 108.954 76.144  126.243 1.00 46.84  ? 203  GLN A CA  1 
ATOM   1612  C  C   . GLN A 1 632  ? 108.287 75.732  124.942 1.00 49.68  ? 203  GLN A C   1 
ATOM   1613  O  O   . GLN A 1 632  ? 107.248 75.067  124.989 1.00 58.92  ? 203  GLN A O   1 
ATOM   1614  C  CB  . GLN A 1 632  ? 108.064 77.131  126.981 1.00 51.17  ? 203  GLN A CB  1 
ATOM   1615  C  CG  . GLN A 1 632  ? 108.484 77.350  128.422 1.00 59.51  ? 203  GLN A CG  1 
ATOM   1616  C  CD  . GLN A 1 632  ? 107.513 78.252  129.163 1.00 74.85  ? 203  GLN A CD  1 
ATOM   1617  O  OE1 . GLN A 1 632  ? 107.024 79.242  128.609 1.00 72.71  ? 203  GLN A OE1 1 
ATOM   1618  N  NE2 . GLN A 1 632  ? 107.225 77.916  130.417 1.00 75.74  ? 203  GLN A NE2 1 
ATOM   1619  N  N   . GLY A 1 633  ? 108.836 76.114  123.793 1.00 43.14  ? 204  GLY A N   1 
ATOM   1620  C  CA  . GLY A 1 633  ? 108.270 75.727  122.516 1.00 51.21  ? 204  GLY A CA  1 
ATOM   1621  C  C   . GLY A 1 633  ? 107.326 76.722  121.865 1.00 49.93  ? 204  GLY A C   1 
ATOM   1622  O  O   . GLY A 1 633  ? 106.653 76.362  120.895 1.00 53.30  ? 204  GLY A O   1 
ATOM   1623  N  N   . ILE A 1 634  ? 107.239 77.946  122.369 1.00 38.74  ? 205  ILE A N   1 
ATOM   1624  C  CA  . ILE A 1 634  ? 106.435 78.976  121.733 1.00 27.79  ? 205  ILE A CA  1 
ATOM   1625  C  C   . ILE A 1 634  ? 107.366 80.080  121.268 1.00 30.67  ? 205  ILE A C   1 
ATOM   1626  O  O   . ILE A 1 634  ? 108.453 80.238  121.827 1.00 43.44  ? 205  ILE A O   1 
ATOM   1627  C  CB  . ILE A 1 634  ? 105.410 79.544  122.706 1.00 45.01  ? 205  ILE A CB  1 
ATOM   1628  C  CG1 . ILE A 1 634  ? 106.139 80.195  123.882 1.00 50.63  ? 205  ILE A CG1 1 
ATOM   1629  C  CG2 . ILE A 1 634  ? 104.498 78.424  123.198 1.00 59.33  ? 205  ILE A CG2 1 
ATOM   1630  C  CD1 . ILE A 1 634  ? 105.211 80.764  124.947 1.00 55.23  ? 205  ILE A CD1 1 
ATOM   1631  N  N   . PRO A 1 635  ? 106.996 80.870  120.280 1.00 31.02  ? 206  PRO A N   1 
ATOM   1632  C  CA  . PRO A 1 635  ? 107.892 81.932  119.827 1.00 31.04  ? 206  PRO A CA  1 
ATOM   1633  C  C   . PRO A 1 635  ? 108.138 82.915  120.946 1.00 35.68  ? 206  PRO A C   1 
ATOM   1634  O  O   . PRO A 1 635  ? 107.299 83.089  121.830 1.00 43.97  ? 206  PRO A O   1 
ATOM   1635  C  CB  . PRO A 1 635  ? 107.117 82.592  118.682 1.00 44.73  ? 206  PRO A CB  1 
ATOM   1636  C  CG  . PRO A 1 635  ? 106.145 81.548  118.224 1.00 55.52  ? 206  PRO A CG  1 
ATOM   1637  C  CD  . PRO A 1 635  ? 105.780 80.783  119.465 1.00 48.96  ? 206  PRO A CD  1 
ATOM   1638  N  N   . HIS A 1 636  ? 109.302 83.565  120.903 1.00 32.27  ? 207  HIS A N   1 
ATOM   1639  C  CA  . HIS A 1 636  ? 109.613 84.557  121.924 1.00 34.65  ? 207  HIS A CA  1 
ATOM   1640  C  C   . HIS A 1 636  ? 108.584 85.675  121.962 1.00 30.65  ? 207  HIS A C   1 
ATOM   1641  O  O   . HIS A 1 636  ? 108.385 86.288  123.011 1.00 37.32  ? 207  HIS A O   1 
ATOM   1642  C  CB  . HIS A 1 636  ? 111.017 85.117  121.696 1.00 41.67  ? 207  HIS A CB  1 
ATOM   1643  C  CG  . HIS A 1 636  ? 112.106 84.143  122.024 1.00 38.58  ? 207  HIS A CG  1 
ATOM   1644  N  ND1 . HIS A 1 636  ? 112.472 83.851  123.319 1.00 31.73  ? 207  HIS A ND1 1 
ATOM   1645  C  CD2 . HIS A 1 636  ? 112.885 83.371  121.228 1.00 38.78  ? 207  HIS A CD2 1 
ATOM   1646  C  CE1 . HIS A 1 636  ? 113.436 82.949  123.305 1.00 34.64  ? 207  HIS A CE1 1 
ATOM   1647  N  NE2 . HIS A 1 636  ? 113.702 82.637  122.049 1.00 34.98  ? 207  HIS A NE2 1 
ATOM   1648  N  N   . ALA A 1 637  ? 107.906 85.934  120.854 1.00 32.75  ? 208  ALA A N   1 
ATOM   1649  C  CA  . ALA A 1 637  ? 106.838 86.919  120.882 1.00 39.79  ? 208  ALA A CA  1 
ATOM   1650  C  C   . ALA A 1 637  ? 105.693 86.456  121.760 1.00 29.65  ? 208  ALA A C   1 
ATOM   1651  O  O   . ALA A 1 637  ? 105.014 87.274  122.384 1.00 42.66  ? 208  ALA A O   1 
ATOM   1652  C  CB  . ALA A 1 637  ? 106.331 87.198  119.459 1.00 42.08  ? 208  ALA A CB  1 
ATOM   1653  N  N   . ALA A 1 638  ? 105.446 85.174  121.808 1.00 24.67  ? 209  ALA A N   1 
ATOM   1654  C  CA  . ALA A 1 638  ? 104.280 84.768  122.555 1.00 38.05  ? 209  ALA A CA  1 
ATOM   1655  C  C   . ALA A 1 638  ? 104.520 84.802  124.051 1.00 46.48  ? 209  ALA A C   1 
ATOM   1656  O  O   . ALA A 1 638  ? 103.553 84.795  124.820 1.00 53.53  ? 209  ALA A O   1 
ATOM   1657  C  CB  . ALA A 1 638  ? 103.846 83.364  122.135 1.00 51.44  ? 209  ALA A CB  1 
ATOM   1658  N  N   . MET A 1 639  ? 105.773 84.833  124.483 1.00 42.49  ? 210  MET A N   1 
ATOM   1659  C  CA  . MET A 1 639  ? 106.033 84.751  125.910 1.00 42.80  ? 210  MET A CA  1 
ATOM   1660  C  C   . MET A 1 639  ? 105.398 85.916  126.641 1.00 38.57  ? 210  MET A C   1 
ATOM   1661  O  O   . MET A 1 639  ? 104.810 85.737  127.709 1.00 48.71  ? 210  MET A O   1 
ATOM   1662  C  CB  . MET A 1 639  ? 107.535 84.707  126.159 1.00 47.78  ? 210  MET A CB  1 
ATOM   1663  C  CG  . MET A 1 639  ? 107.917 84.722  127.603 1.00 53.93  ? 210  MET A CG  1 
ATOM   1664  S  SD  . MET A 1 639  ? 109.703 84.595  127.716 1.00 84.69  ? 210  MET A SD  1 
ATOM   1665  C  CE  . MET A 1 639  ? 109.922 83.038  126.881 1.00 63.93  ? 210  MET A CE  1 
ATOM   1666  N  N   . ASP A 1 640  ? 105.478 87.113  126.076 1.00 39.10  ? 211  ASP A N   1 
ATOM   1667  C  CA  . ASP A 1 640  ? 104.925 88.253  126.789 1.00 51.86  ? 211  ASP A CA  1 
ATOM   1668  C  C   . ASP A 1 640  ? 103.428 88.093  127.032 1.00 51.51  ? 211  ASP A C   1 
ATOM   1669  O  O   . ASP A 1 640  ? 102.938 88.416  128.118 1.00 60.27  ? 211  ASP A O   1 
ATOM   1670  C  CB  . ASP A 1 640  ? 105.210 89.568  126.046 1.00 63.72  ? 211  ASP A CB  1 
ATOM   1671  C  CG  . ASP A 1 640  ? 106.684 89.999  126.135 1.00 68.06  ? 211  ASP A CG  1 
ATOM   1672  O  OD1 . ASP A 1 640  ? 107.345 90.133  125.081 1.00 66.62  ? 211  ASP A OD1 1 
ATOM   1673  O  OD2 . ASP A 1 640  ? 107.189 90.184  127.268 1.00 65.91  ? 211  ASP A OD2 1 
ATOM   1674  N  N   . TRP A 1 641  ? 102.684 87.594  126.060 1.00 38.96  ? 212  TRP A N   1 
ATOM   1675  C  CA  . TRP A 1 641  ? 101.239 87.709  126.148 1.00 32.50  ? 212  TRP A CA  1 
ATOM   1676  C  C   . TRP A 1 641  ? 100.542 86.422  126.521 1.00 41.82  ? 212  TRP A C   1 
ATOM   1677  O  O   . TRP A 1 641  ? 99.589  86.449  127.299 1.00 47.08  ? 212  TRP A O   1 
ATOM   1678  C  CB  . TRP A 1 641  ? 100.684 88.161  124.819 1.00 44.71  ? 212  TRP A CB  1 
ATOM   1679  C  CG  . TRP A 1 641  ? 101.148 89.465  124.402 1.00 44.03  ? 212  TRP A CG  1 
ATOM   1680  C  CD1 . TRP A 1 641  ? 101.986 90.287  125.073 1.00 52.79  ? 212  TRP A CD1 1 
ATOM   1681  C  CD2 . TRP A 1 641  ? 100.847 90.110  123.159 1.00 48.43  ? 212  TRP A CD2 1 
ATOM   1682  N  NE1 . TRP A 1 641  ? 102.208 91.435  124.341 1.00 59.02  ? 212  TRP A NE1 1 
ATOM   1683  C  CE2 . TRP A 1 641  ? 101.523 91.341  123.156 1.00 50.43  ? 212  TRP A CE2 1 
ATOM   1684  C  CE3 . TRP A 1 641  ? 100.062 89.762  122.048 1.00 49.80  ? 212  TRP A CE3 1 
ATOM   1685  C  CZ2 . TRP A 1 641  ? 101.434 92.233  122.099 1.00 48.00  ? 212  TRP A CZ2 1 
ATOM   1686  C  CZ3 . TRP A 1 641  ? 99.985  90.635  120.993 1.00 48.02  ? 212  TRP A CZ3 1 
ATOM   1687  C  CH2 . TRP A 1 641  ? 100.667 91.861  121.023 1.00 49.70  ? 212  TRP A CH2 1 
ATOM   1688  N  N   . TYR A 1 642  ? 100.975 85.302  125.954 1.00 42.92  ? 213  TYR A N   1 
ATOM   1689  C  CA  . TYR A 1 642  ? 100.311 84.015  126.099 1.00 39.16  ? 213  TYR A CA  1 
ATOM   1690  C  C   . TYR A 1 642  ? 101.121 83.100  126.993 1.00 43.47  ? 213  TYR A C   1 
ATOM   1691  O  O   . TYR A 1 642  ? 102.322 82.913  126.770 1.00 50.10  ? 213  TYR A O   1 
ATOM   1692  C  CB  . TYR A 1 642  ? 100.152 83.327  124.749 1.00 45.85  ? 213  TYR A CB  1 
ATOM   1693  C  CG  . TYR A 1 642  ? 99.582  84.216  123.697 1.00 47.60  ? 213  TYR A CG  1 
ATOM   1694  C  CD1 . TYR A 1 642  ? 100.408 84.937  122.856 1.00 45.78  ? 213  TYR A CD1 1 
ATOM   1695  C  CD2 . TYR A 1 642  ? 98.212  84.359  123.567 1.00 47.50  ? 213  TYR A CD2 1 
ATOM   1696  C  CE1 . TYR A 1 642  ? 99.887  85.752  121.900 1.00 44.40  ? 213  TYR A CE1 1 
ATOM   1697  C  CE2 . TYR A 1 642  ? 97.682  85.172  122.621 1.00 46.04  ? 213  TYR A CE2 1 
ATOM   1698  C  CZ  . TYR A 1 642  ? 98.523  85.871  121.789 1.00 46.99  ? 213  TYR A CZ  1 
ATOM   1699  O  OH  . TYR A 1 642  ? 97.989  86.697  120.827 1.00 55.02  ? 213  TYR A OH  1 
ATOM   1700  N  N   . GLN A 1 643  ? 100.463 82.493  127.966 1.00 45.07  ? 214  GLN A N   1 
ATOM   1701  C  CA  . GLN A 1 643  ? 101.103 81.400  128.674 1.00 50.62  ? 214  GLN A CA  1 
ATOM   1702  C  C   . GLN A 1 643  ? 101.278 80.226  127.718 1.00 54.26  ? 214  GLN A C   1 
ATOM   1703  O  O   . GLN A 1 643  ? 100.392 79.944  126.909 1.00 62.73  ? 214  GLN A O   1 
ATOM   1704  C  CB  . GLN A 1 643  ? 100.261 81.008  129.874 1.00 52.23  ? 214  GLN A CB  1 
ATOM   1705  C  CG  . GLN A 1 643  ? 100.838 79.883  130.674 1.00 68.93  ? 214  GLN A CG  1 
ATOM   1706  C  CD  . GLN A 1 643  ? 99.839  79.348  131.672 1.00 83.38  ? 214  GLN A CD  1 
ATOM   1707  O  OE1 . GLN A 1 643  ? 98.657  79.695  131.625 1.00 80.70  ? 214  GLN A OE1 1 
ATOM   1708  N  NE2 . GLN A 1 643  ? 100.309 78.514  132.599 1.00 84.60  ? 214  GLN A NE2 1 
ATOM   1709  N  N   . ALA A 1 644  ? 102.433 79.558  127.774 1.00 51.39  ? 215  ALA A N   1 
ATOM   1710  C  CA  . ALA A 1 644  ? 102.654 78.411  126.897 1.00 48.85  ? 215  ALA A CA  1 
ATOM   1711  C  C   . ALA A 1 644  ? 101.543 77.388  127.103 1.00 56.73  ? 215  ALA A C   1 
ATOM   1712  O  O   . ALA A 1 644  ? 100.826 77.412  128.109 1.00 65.34  ? 215  ALA A O   1 
ATOM   1713  C  CB  . ALA A 1 644  ? 104.015 77.769  127.170 1.00 63.98  ? 215  ALA A CB  1 
ATOM   1714  N  N   . SER A 1 645  ? 101.380 76.496  126.129 1.00 53.01  ? 216  SER A N   1 
ATOM   1715  C  CA  . SER A 1 645  ? 100.286 75.518  126.069 1.00 60.74  ? 216  SER A CA  1 
ATOM   1716  C  C   . SER A 1 645  ? 98.944  76.194  125.903 1.00 55.90  ? 216  SER A C   1 
ATOM   1717  O  O   . SER A 1 645  ? 97.911  75.513  125.902 1.00 59.75  ? 216  SER A O   1 
ATOM   1718  C  CB  . SER A 1 645  ? 100.177 74.614  127.306 1.00 70.25  ? 216  SER A CB  1 
ATOM   1719  O  OG  . SER A 1 645  ? 99.680  75.347  128.417 1.00 65.10  ? 216  SER A OG  1 
ATOM   1720  N  N   . VAL A 1 646  ? 98.920  77.518  125.854 1.00 50.81  ? 217  VAL A N   1 
ATOM   1721  C  CA  . VAL A 1 646  ? 97.785  78.256  125.352 1.00 46.20  ? 217  VAL A CA  1 
ATOM   1722  C  C   . VAL A 1 646  ? 98.093  78.894  124.007 1.00 51.95  ? 217  VAL A C   1 
ATOM   1723  O  O   . VAL A 1 646  ? 97.175  79.081  123.202 1.00 60.91  ? 217  VAL A O   1 
ATOM   1724  C  CB  . VAL A 1 646  ? 97.333  79.318  126.372 1.00 51.59  ? 217  VAL A CB  1 
ATOM   1725  C  CG1 . VAL A 1 646  ? 96.080  80.025  125.918 1.00 50.23  ? 217  VAL A CG1 1 
ATOM   1726  C  CG2 . VAL A 1 646  ? 97.101  78.657  127.726 1.00 61.10  ? 217  VAL A CG2 1 
ATOM   1727  N  N   . PHE A 1 647  ? 99.363  79.206  123.725 1.00 55.37  ? 218  PHE A N   1 
ATOM   1728  C  CA  . PHE A 1 647  ? 99.709  79.686  122.391 1.00 50.00  ? 218  PHE A CA  1 
ATOM   1729  C  C   . PHE A 1 647  ? 99.747  78.548  121.388 1.00 57.72  ? 218  PHE A C   1 
ATOM   1730  O  O   . PHE A 1 647  ? 99.330  78.715  120.234 1.00 64.22  ? 218  PHE A O   1 
ATOM   1731  C  CB  . PHE A 1 647  ? 101.050 80.387  122.374 1.00 37.74  ? 218  PHE A CB  1 
ATOM   1732  C  CG  . PHE A 1 647  ? 101.410 80.884  121.034 1.00 30.21  ? 218  PHE A CG  1 
ATOM   1733  C  CD1 . PHE A 1 647  ? 100.974 82.119  120.628 1.00 44.69  ? 218  PHE A CD1 1 
ATOM   1734  C  CD2 . PHE A 1 647  ? 102.165 80.135  120.176 1.00 39.00  ? 218  PHE A CD2 1 
ATOM   1735  C  CE1 . PHE A 1 647  ? 101.292 82.612  119.392 1.00 51.13  ? 218  PHE A CE1 1 
ATOM   1736  C  CE2 . PHE A 1 647  ? 102.488 80.624  118.917 1.00 51.68  ? 218  PHE A CE2 1 
ATOM   1737  C  CZ  . PHE A 1 647  ? 102.057 81.870  118.534 1.00 52.45  ? 218  PHE A CZ  1 
ATOM   1738  N  N   . LYS A 1 648  ? 100.289 77.399  121.788 1.00 52.92  ? 219  LYS A N   1 
ATOM   1739  C  CA  . LYS A 1 648  ? 100.344 76.283  120.859 1.00 51.66  ? 219  LYS A CA  1 
ATOM   1740  C  C   . LYS A 1 648  ? 98.981  75.614  120.679 1.00 57.43  ? 219  LYS A C   1 
ATOM   1741  O  O   . LYS A 1 648  ? 98.794  74.875  119.706 1.00 63.81  ? 219  LYS A O   1 
ATOM   1742  C  CB  . LYS A 1 648  ? 101.389 75.273  121.313 1.00 51.16  ? 219  LYS A CB  1 
ATOM   1743  C  CG  . LYS A 1 648  ? 101.133 74.750  122.690 1.00 61.91  ? 219  LYS A CG  1 
ATOM   1744  C  CD  . LYS A 1 648  ? 102.196 73.762  123.115 1.00 62.39  ? 219  LYS A CD  1 
ATOM   1745  C  CE  . LYS A 1 648  ? 103.572 74.397  123.088 1.00 62.00  ? 219  LYS A CE  1 
ATOM   1746  N  NZ  . LYS A 1 648  ? 104.595 73.390  123.489 1.00 63.20  ? 219  LYS A NZ  1 
ATOM   1747  N  N   . GLU A 1 649  ? 98.019  75.847  121.578 1.00 51.34  ? 220  GLU A N   1 
ATOM   1748  C  CA  . GLU A 1 649  ? 96.677  75.335  121.312 1.00 54.29  ? 220  GLU A CA  1 
ATOM   1749  C  C   . GLU A 1 649  ? 95.876  76.296  120.452 1.00 49.15  ? 220  GLU A C   1 
ATOM   1750  O  O   . GLU A 1 649  ? 95.013  75.862  119.683 1.00 56.03  ? 220  GLU A O   1 
ATOM   1751  C  CB  . GLU A 1 649  ? 95.941  75.048  122.621 1.00 69.82  ? 220  GLU A CB  1 
ATOM   1752  C  CG  . GLU A 1 649  ? 95.350  76.286  123.308 1.00 78.52  ? 220  GLU A CG  1 
ATOM   1753  C  CD  . GLU A 1 649  ? 94.486  75.946  124.532 1.00 84.26  ? 220  GLU A CD  1 
ATOM   1754  O  OE1 . GLU A 1 649  ? 94.461  74.758  124.937 1.00 79.40  ? 220  GLU A OE1 1 
ATOM   1755  O  OE2 . GLU A 1 649  ? 93.848  76.870  125.095 1.00 75.19  ? 220  GLU A OE2 1 
ATOM   1756  N  N   . ALA A 1 650  ? 96.142  77.594  120.568 1.00 47.94  ? 221  ALA A N   1 
ATOM   1757  C  CA  . ALA A 1 650  ? 95.546  78.547  119.642 1.00 49.72  ? 221  ALA A CA  1 
ATOM   1758  C  C   . ALA A 1 650  ? 96.144  78.390  118.255 1.00 46.75  ? 221  ALA A C   1 
ATOM   1759  O  O   . ALA A 1 650  ? 95.416  78.335  117.260 1.00 55.02  ? 221  ALA A O   1 
ATOM   1760  C  CB  . ALA A 1 650  ? 95.735  79.976  120.150 1.00 53.84  ? 221  ALA A CB  1 
ATOM   1761  N  N   . VAL A 1 651  ? 97.468  78.313  118.168 1.00 41.01  ? 222  VAL A N   1 
ATOM   1762  C  CA  . VAL A 1 651  ? 98.142  78.112  116.879 1.00 44.61  ? 222  VAL A CA  1 
ATOM   1763  C  C   . VAL A 1 651  ? 98.312  76.609  116.707 1.00 54.76  ? 222  VAL A C   1 
ATOM   1764  O  O   . VAL A 1 651  ? 99.394  76.043  116.875 1.00 59.54  ? 222  VAL A O   1 
ATOM   1765  C  CB  . VAL A 1 651  ? 99.472  78.854  116.811 1.00 51.60  ? 222  VAL A CB  1 
ATOM   1766  C  CG1 . VAL A 1 651  ? 100.041 78.784  115.390 1.00 61.18  ? 222  VAL A CG1 1 
ATOM   1767  C  CG2 . VAL A 1 651  ? 99.279  80.295  117.255 1.00 62.24  ? 222  VAL A CG2 1 
ATOM   1768  N  N   . GLN A 1 652  ? 97.229  75.945  116.304 1.00 57.53  ? 223  GLN A N   1 
ATOM   1769  C  CA  . GLN A 1 652  ? 97.249  74.489  116.268 1.00 62.53  ? 223  GLN A CA  1 
ATOM   1770  C  C   . GLN A 1 652  ? 97.585  73.975  114.876 1.00 62.12  ? 223  GLN A C   1 
ATOM   1771  O  O   . GLN A 1 652  ? 98.619  73.331  114.675 1.00 68.53  ? 223  GLN A O   1 
ATOM   1772  C  CB  . GLN A 1 652  ? 95.904  73.902  116.728 1.00 71.63  ? 223  GLN A CB  1 
ATOM   1773  C  CG  . GLN A 1 652  ? 95.921  72.364  116.918 1.00 75.64  ? 223  GLN A CG  1 
ATOM   1774  C  CD  . GLN A 1 652  ? 96.946  71.915  117.974 1.00 84.36  ? 223  GLN A CD  1 
ATOM   1775  O  OE1 . GLN A 1 652  ? 96.923  72.388  119.119 1.00 75.55  ? 223  GLN A OE1 1 
ATOM   1776  N  NE2 . GLN A 1 652  ? 97.854  71.016  117.588 1.00 85.85  ? 223  GLN A NE2 1 
ATOM   1777  N  N   . GLY A 1 653  ? 96.729  74.254  113.906 1.00 58.74  ? 224  GLY A N   1 
ATOM   1778  C  CA  . GLY A 1 653  ? 97.004  73.814  112.558 1.00 57.92  ? 224  GLY A CA  1 
ATOM   1779  C  C   . GLY A 1 653  ? 97.480  74.970  111.713 1.00 60.37  ? 224  GLY A C   1 
ATOM   1780  O  O   . GLY A 1 653  ? 97.927  74.781  110.578 1.00 63.95  ? 224  GLY A O   1 
ATOM   1781  N  N   . HIS A 1 654  ? 97.391  76.178  112.253 1.00 57.26  ? 225  HIS A N   1 
ATOM   1782  C  CA  . HIS A 1 654  ? 97.700  77.337  111.439 1.00 48.58  ? 225  HIS A CA  1 
ATOM   1783  C  C   . HIS A 1 654  ? 99.187  77.437  111.212 1.00 34.92  ? 225  HIS A C   1 
ATOM   1784  O  O   . HIS A 1 654  ? 99.999  77.121  112.079 1.00 40.30  ? 225  HIS A O   1 
ATOM   1785  C  CB  . HIS A 1 654  ? 97.197  78.629  112.069 1.00 51.69  ? 225  HIS A CB  1 
ATOM   1786  C  CG  . HIS A 1 654  ? 95.733  78.624  112.349 1.00 52.85  ? 225  HIS A CG  1 
ATOM   1787  N  ND1 . HIS A 1 654  ? 95.201  78.091  113.504 1.00 60.66  ? 225  HIS A ND1 1 
ATOM   1788  C  CD2 . HIS A 1 654  ? 94.680  79.007  111.590 1.00 57.60  ? 225  HIS A CD2 1 
ATOM   1789  C  CE1 . HIS A 1 654  ? 93.884  78.198  113.470 1.00 65.72  ? 225  HIS A CE1 1 
ATOM   1790  N  NE2 . HIS A 1 654  ? 93.541  78.745  112.316 1.00 65.45  ? 225  HIS A NE2 1 
ATOM   1791  N  N   . THR A 1 655  ? 99.530  77.880  110.034 1.00 33.76  ? 226  THR A N   1 
ATOM   1792  C  CA  . THR A 1 655  ? 100.901 78.107  109.696 1.00 34.79  ? 226  THR A CA  1 
ATOM   1793  C  C   . THR A 1 655  ? 101.206 79.571  109.584 1.00 38.91  ? 226  THR A C   1 
ATOM   1794  O  O   . THR A 1 655  ? 102.381 79.941  109.590 1.00 49.26  ? 226  THR A O   1 
ATOM   1795  C  CB  . THR A 1 655  ? 101.223 77.441  108.365 1.00 59.27  ? 226  THR A CB  1 
ATOM   1796  O  OG1 . THR A 1 655  ? 100.336 77.966  107.368 1.00 58.76  ? 226  THR A OG1 1 
ATOM   1797  C  CG2 . THR A 1 655  ? 101.028 75.917  108.476 1.00 71.67  ? 226  THR A CG2 1 
ATOM   1798  N  N   . HIS A 1 656  ? 100.193 80.406  109.469 1.00 39.12  ? 227  HIS A N   1 
ATOM   1799  C  CA  . HIS A 1 656  ? 100.391 81.839  109.408 1.00 43.86  ? 227  HIS A CA  1 
ATOM   1800  C  C   . HIS A 1 656  ? 99.672  82.527  110.552 1.00 49.68  ? 227  HIS A C   1 
ATOM   1801  O  O   . HIS A 1 656  ? 98.569  82.131  110.939 1.00 56.15  ? 227  HIS A O   1 
ATOM   1802  C  CB  . HIS A 1 656  ? 99.900  82.397  108.082 1.00 47.56  ? 227  HIS A CB  1 
ATOM   1803  C  CG  . HIS A 1 656  ? 100.743 81.991  106.918 1.00 48.55  ? 227  HIS A CG  1 
ATOM   1804  N  ND1 . HIS A 1 656  ? 101.001 80.673  106.605 1.00 54.56  ? 227  HIS A ND1 1 
ATOM   1805  C  CD2 . HIS A 1 656  ? 101.410 82.734  106.001 1.00 52.92  ? 227  HIS A CD2 1 
ATOM   1806  C  CE1 . HIS A 1 656  ? 101.780 80.622  105.538 1.00 56.97  ? 227  HIS A CE1 1 
ATOM   1807  N  NE2 . HIS A 1 656  ? 102.043 81.858  105.152 1.00 54.45  ? 227  HIS A NE2 1 
ATOM   1808  N  N   . ILE A 1 657  ? 100.302 83.576  111.060 1.00 41.24  ? 228  ILE A N   1 
ATOM   1809  C  CA  . ILE A 1 657  ? 99.782  84.334  112.184 1.00 40.49  ? 228  ILE A CA  1 
ATOM   1810  C  C   . ILE A 1 657  ? 99.860  85.823  111.855 1.00 56.52  ? 228  ILE A C   1 
ATOM   1811  O  O   . ILE A 1 657  ? 100.749 86.260  111.119 1.00 58.84  ? 228  ILE A O   1 
ATOM   1812  C  CB  . ILE A 1 657  ? 100.558 83.998  113.452 1.00 37.10  ? 228  ILE A CB  1 
ATOM   1813  C  CG1 . ILE A 1 657  ? 99.735  84.280  114.699 1.00 52.52  ? 228  ILE A CG1 1 
ATOM   1814  C  CG2 . ILE A 1 657  ? 101.843 84.789  113.492 1.00 45.57  ? 228  ILE A CG2 1 
ATOM   1815  C  CD1 . ILE A 1 657  ? 100.469 83.895  115.999 1.00 55.08  ? 228  ILE A CD1 1 
ATOM   1816  N  N   . VAL A 1 658  ? 98.904  86.612  112.376 1.00 50.95  ? 229  VAL A N   1 
ATOM   1817  C  CA  . VAL A 1 658  ? 98.817  88.041  112.040 1.00 36.09  ? 229  VAL A CA  1 
ATOM   1818  C  C   . VAL A 1 658  ? 99.413  88.823  113.195 1.00 40.05  ? 229  VAL A C   1 
ATOM   1819  O  O   . VAL A 1 658  ? 99.638  88.292  114.282 1.00 52.25  ? 229  VAL A O   1 
ATOM   1820  C  CB  . VAL A 1 658  ? 97.413  88.567  111.771 1.00 45.51  ? 229  VAL A CB  1 
ATOM   1821  C  CG1 . VAL A 1 658  ? 96.799  87.834  110.567 1.00 57.90  ? 229  VAL A CG1 1 
ATOM   1822  C  CG2 . VAL A 1 658  ? 96.556  88.356  113.062 1.00 50.92  ? 229  VAL A CG2 1 
ATOM   1823  N  N   . SER A 1 659  ? 99.715  90.107  112.941 1.00 34.71  ? 230  SER A N   1 
ATOM   1824  C  CA  . SER A 1 659  ? 100.315 91.000  113.942 1.00 35.97  ? 230  SER A CA  1 
ATOM   1825  C  C   . SER A 1 659  ? 99.926  92.441  113.591 1.00 39.08  ? 230  SER A C   1 
ATOM   1826  O  O   . SER A 1 659  ? 100.533 93.050  112.707 1.00 43.74  ? 230  SER A O   1 
ATOM   1827  C  CB  . SER A 1 659  ? 101.829 90.809  114.000 1.00 38.10  ? 230  SER A CB  1 
ATOM   1828  O  OG  . SER A 1 659  ? 102.406 91.018  112.729 1.00 42.74  ? 230  SER A OG  1 
ATOM   1829  N  N   . VAL A 1 660  ? 98.878  92.949  114.228 1.00 26.49  ? 231  VAL A N   1 
ATOM   1830  C  CA  . VAL A 1 660  ? 98.319  94.252  113.887 1.00 18.96  ? 231  VAL A CA  1 
ATOM   1831  C  C   . VAL A 1 660  ? 99.237  95.359  114.357 1.00 35.78  ? 231  VAL A C   1 
ATOM   1832  O  O   . VAL A 1 660  ? 99.607  95.400  115.533 1.00 50.98  ? 231  VAL A O   1 
ATOM   1833  C  CB  . VAL A 1 660  ? 96.960  94.411  114.541 1.00 27.10  ? 231  VAL A CB  1 
ATOM   1834  C  CG1 . VAL A 1 660  ? 96.398  95.770  114.218 1.00 33.89  ? 231  VAL A CG1 1 
ATOM   1835  C  CG2 . VAL A 1 660  ? 96.080  93.275  114.062 1.00 44.59  ? 231  VAL A CG2 1 
ATOM   1836  N  N   . SER A 1 661  ? 99.583  96.286  113.468 1.00 33.03  ? 232  SER A N   1 
ATOM   1837  C  CA  . SER A 1 661  ? 100.471 97.378  113.850 1.00 34.02  ? 232  SER A CA  1 
ATOM   1838  C  C   . SER A 1 661  ? 100.020 98.657  113.173 1.00 33.76  ? 232  SER A C   1 
ATOM   1839  O  O   . SER A 1 661  ? 99.364  98.626  112.130 1.00 43.32  ? 232  SER A O   1 
ATOM   1840  C  CB  . SER A 1 661  ? 101.928 97.094  113.478 1.00 43.71  ? 232  SER A CB  1 
ATOM   1841  O  OG  . SER A 1 661  ? 102.077 96.968  112.074 1.00 44.23  ? 232  SER A OG  1 
ATOM   1842  N  N   . THR A 1 662  ? 100.371 99.788  113.771 1.00 32.14  ? 233  THR A N   1 
ATOM   1843  C  CA  . THR A 1 662  ? 99.932  101.046 113.202 1.00 29.44  ? 233  THR A CA  1 
ATOM   1844  C  C   . THR A 1 662  ? 100.751 101.355 111.965 1.00 32.06  ? 233  THR A C   1 
ATOM   1845  O  O   . THR A 1 662  ? 101.850 100.840 111.781 1.00 47.56  ? 233  THR A O   1 
ATOM   1846  C  CB  . THR A 1 662  ? 100.058 102.169 114.215 1.00 44.67  ? 233  THR A CB  1 
ATOM   1847  O  OG1 . THR A 1 662  ? 99.481  101.741 115.451 1.00 46.58  ? 233  THR A OG1 1 
ATOM   1848  C  CG2 . THR A 1 662  ? 99.296  103.386 113.739 1.00 55.01  ? 233  THR A CG2 1 
ATOM   1849  N  N   . ALA A 1 663  ? 100.192 102.175 111.089 1.00 30.16  ? 234  ALA A N   1 
ATOM   1850  C  CA  . ALA A 1 663  ? 100.906 102.504 109.875 1.00 27.66  ? 234  ALA A CA  1 
ATOM   1851  C  C   . ALA A 1 663  ? 102.229 103.152 110.186 1.00 40.61  ? 234  ALA A C   1 
ATOM   1852  O  O   . ALA A 1 663  ? 103.135 103.116 109.348 1.00 54.99  ? 234  ALA A O   1 
ATOM   1853  C  CB  . ALA A 1 663  ? 100.074 103.440 109.006 1.00 47.95  ? 234  ALA A CB  1 
ATOM   1854  N  N   . ASP A 1 664  ? 102.371 103.732 111.375 1.00 42.28  ? 235  ASP A N   1 
ATOM   1855  C  CA  . ASP A 1 664  ? 103.649 104.334 111.738 1.00 49.28  ? 235  ASP A CA  1 
ATOM   1856  C  C   . ASP A 1 664  ? 104.773 103.305 111.785 1.00 49.65  ? 235  ASP A C   1 
ATOM   1857  O  O   . ASP A 1 664  ? 105.930 103.646 111.516 1.00 54.48  ? 235  ASP A O   1 
ATOM   1858  C  CB  . ASP A 1 664  ? 103.543 105.050 113.083 1.00 61.64  ? 235  ASP A CB  1 
ATOM   1859  C  CG  . ASP A 1 664  ? 102.609 106.247 113.029 1.00 80.92  ? 235  ASP A CG  1 
ATOM   1860  O  OD1 . ASP A 1 664  ? 102.474 106.851 111.937 1.00 77.17  ? 235  ASP A OD1 1 
ATOM   1861  O  OD2 . ASP A 1 664  ? 102.025 106.595 114.080 1.00 78.79  ? 235  ASP A OD2 1 
ATOM   1862  N  N   . VAL A 1 665  ? 104.473 102.056 112.146 1.00 44.82  ? 236  VAL A N   1 
ATOM   1863  C  CA  . VAL A 1 665  ? 105.510 101.036 112.111 1.00 32.14  ? 236  VAL A CA  1 
ATOM   1864  C  C   . VAL A 1 665  ? 105.895 100.736 110.679 1.00 33.29  ? 236  VAL A C   1 
ATOM   1865  O  O   . VAL A 1 665  ? 107.076 100.549 110.381 1.00 46.85  ? 236  VAL A O   1 
ATOM   1866  C  CB  . VAL A 1 665  ? 105.093 99.771  112.878 1.00 36.33  ? 236  VAL A CB  1 
ATOM   1867  C  CG1 . VAL A 1 665  ? 106.157 98.709  112.744 1.00 47.92  ? 236  VAL A CG1 1 
ATOM   1868  C  CG2 . VAL A 1 665  ? 104.933 100.096 114.358 1.00 39.22  ? 236  VAL A CG2 1 
ATOM   1869  N  N   . LEU A 1 666  ? 104.933 100.705 109.763 1.00 31.72  ? 237  LEU A N   1 
ATOM   1870  C  CA  . LEU A 1 666  ? 105.318 100.550 108.364 1.00 34.55  ? 237  LEU A CA  1 
ATOM   1871  C  C   . LEU A 1 666  ? 106.209 101.707 107.921 1.00 48.83  ? 237  LEU A C   1 
ATOM   1872  O  O   . LEU A 1 666  ? 107.206 101.500 107.209 1.00 52.11  ? 237  LEU A O   1 
ATOM   1873  C  CB  . LEU A 1 666  ? 104.087 100.447 107.480 1.00 34.56  ? 237  LEU A CB  1 
ATOM   1874  C  CG  . LEU A 1 666  ? 104.379 99.908  106.091 1.00 44.07  ? 237  LEU A CG  1 
ATOM   1875  C  CD1 . LEU A 1 666  ? 103.132 99.203  105.584 1.00 46.77  ? 237  LEU A CD1 1 
ATOM   1876  C  CD2 . LEU A 1 666  ? 104.799 101.028 105.123 1.00 49.15  ? 237  LEU A CD2 1 
ATOM   1877  N  N   . ILE A 1 667  ? 105.885 102.928 108.368 1.00 48.92  ? 238  ILE A N   1 
ATOM   1878  C  CA  . ILE A 1 667  ? 106.684 104.109 108.026 1.00 46.43  ? 238  ILE A CA  1 
ATOM   1879  C  C   . ILE A 1 667  ? 108.115 103.983 108.572 1.00 45.63  ? 238  ILE A C   1 
ATOM   1880  O  O   . ILE A 1 667  ? 109.094 104.241 107.859 1.00 45.79  ? 238  ILE A O   1 
ATOM   1881  C  CB  . ILE A 1 667  ? 105.993 105.391 108.538 1.00 47.15  ? 238  ILE A CB  1 
ATOM   1882  C  CG1 . ILE A 1 667  ? 104.582 105.541 107.955 1.00 44.18  ? 238  ILE A CG1 1 
ATOM   1883  C  CG2 . ILE A 1 667  ? 106.833 106.612 108.209 1.00 57.05  ? 238  ILE A CG2 1 
ATOM   1884  C  CD1 . ILE A 1 667  ? 104.535 105.578 106.432 1.00 53.87  ? 238  ILE A CD1 1 
ATOM   1885  N  N   . MET A 1 668  ? 108.263 103.599 109.847 1.00 43.52  ? 239  MET A N   1 
ATOM   1886  C  CA  . MET A 1 668  ? 109.615 103.491 110.389 1.00 40.95  ? 239  MET A CA  1 
ATOM   1887  C  C   . MET A 1 668  ? 110.366 102.317 109.790 1.00 40.48  ? 239  MET A C   1 
ATOM   1888  O  O   . MET A 1 668  ? 111.592 102.356 109.741 1.00 48.21  ? 239  MET A O   1 
ATOM   1889  C  CB  . MET A 1 668  ? 109.665 103.367 111.924 1.00 37.51  ? 239  MET A CB  1 
ATOM   1890  C  CG  . MET A 1 668  ? 109.212 102.026 112.444 1.00 43.99  ? 239  MET A CG  1 
ATOM   1891  S  SD  . MET A 1 668  ? 109.379 101.692 114.211 1.00 54.65  ? 239  MET A SD  1 
ATOM   1892  C  CE  . MET A 1 668  ? 110.979 100.983 114.233 1.00 40.08  ? 239  MET A CE  1 
ATOM   1893  N  N   . CYS A 1 669  ? 109.698 101.244 109.387 1.00 34.63  ? 240  CYS A N   1 
ATOM   1894  C  CA  . CYS A 1 669  ? 110.476 100.204 108.736 1.00 26.80  ? 240  CYS A CA  1 
ATOM   1895  C  C   . CYS A 1 669  ? 110.951 100.694 107.394 1.00 31.77  ? 240  CYS A C   1 
ATOM   1896  O  O   . CYS A 1 669  ? 112.063 100.374 106.968 1.00 43.70  ? 240  CYS A O   1 
ATOM   1897  C  CB  . CYS A 1 669  ? 109.691 98.917  108.571 1.00 30.24  ? 240  CYS A CB  1 
ATOM   1898  S  SG  . CYS A 1 669  ? 109.340 98.097  110.128 1.00 59.57  ? 240  CYS A SG  1 
ATOM   1899  N  N   . LYS A 1 670  ? 110.143 101.495 106.719 1.00 32.84  ? 241  LYS A N   1 
ATOM   1900  C  CA  . LYS A 1 670  ? 110.637 102.123 105.499 1.00 39.75  ? 241  LYS A CA  1 
ATOM   1901  C  C   . LYS A 1 670  ? 111.842 103.020 105.784 1.00 44.16  ? 241  LYS A C   1 
ATOM   1902  O  O   . LYS A 1 670  ? 112.822 103.022 105.024 1.00 44.88  ? 241  LYS A O   1 
ATOM   1903  C  CB  . LYS A 1 670  ? 109.490 102.875 104.814 1.00 52.66  ? 241  LYS A CB  1 
ATOM   1904  C  CG  . LYS A 1 670  ? 109.834 103.716 103.576 1.00 50.89  ? 241  LYS A CG  1 
ATOM   1905  C  CD  . LYS A 1 670  ? 110.004 105.162 104.030 1.00 53.46  ? 241  LYS A CD  1 
ATOM   1906  C  CE  . LYS A 1 670  ? 108.626 105.739 104.437 1.00 55.39  ? 241  LYS A CE  1 
ATOM   1907  N  NZ  . LYS A 1 670  ? 108.676 107.157 104.886 1.00 58.64  ? 241  LYS A NZ  1 
ATOM   1908  N  N   . ASP A 1 671  ? 111.799 103.770 106.886 1.00 45.56  ? 242  ASP A N   1 
ATOM   1909  C  CA  . ASP A 1 671  ? 112.927 104.630 107.243 1.00 35.84  ? 242  ASP A CA  1 
ATOM   1910  C  C   . ASP A 1 671  ? 114.160 103.809 107.605 1.00 37.86  ? 242  ASP A C   1 
ATOM   1911  O  O   . ASP A 1 671  ? 115.284 104.157 107.223 1.00 43.89  ? 242  ASP A O   1 
ATOM   1912  C  CB  . ASP A 1 671  ? 112.528 105.534 108.387 1.00 34.57  ? 242  ASP A CB  1 
ATOM   1913  C  CG  . ASP A 1 671  ? 111.354 106.392 108.024 1.00 55.08  ? 242  ASP A CG  1 
ATOM   1914  O  OD1 . ASP A 1 671  ? 111.129 106.606 106.809 1.00 52.57  ? 242  ASP A OD1 1 
ATOM   1915  O  OD2 . ASP A 1 671  ? 110.653 106.856 108.946 1.00 61.24  ? 242  ASP A OD2 1 
ATOM   1916  N  N   . LEU A 1 672  ? 113.975 102.715 108.337 1.00 32.05  ? 243  LEU A N   1 
ATOM   1917  C  CA  . LEU A 1 672  ? 115.093 101.829 108.580 1.00 22.12  ? 243  LEU A CA  1 
ATOM   1918  C  C   . LEU A 1 672  ? 115.691 101.372 107.278 1.00 32.92  ? 243  LEU A C   1 
ATOM   1919  O  O   . LEU A 1 672  ? 116.909 101.401 107.109 1.00 41.00  ? 243  LEU A O   1 
ATOM   1920  C  CB  . LEU A 1 672  ? 114.686 100.592 109.345 1.00 23.49  ? 243  LEU A CB  1 
ATOM   1921  C  CG  . LEU A 1 672  ? 114.296 100.893 110.746 1.00 34.78  ? 243  LEU A CG  1 
ATOM   1922  C  CD1 . LEU A 1 672  ? 114.334 99.562  111.499 1.00 40.36  ? 243  LEU A CD1 1 
ATOM   1923  C  CD2 . LEU A 1 672  ? 115.230 101.984 111.313 1.00 44.70  ? 243  LEU A CD2 1 
ATOM   1924  N  N   . ILE A 1 673  ? 114.864 100.865 106.371 1.00 27.03  ? 244  ILE A N   1 
ATOM   1925  C  CA  . ILE A 1 673  ? 115.453 100.217 105.222 1.00 19.89  ? 244  ILE A CA  1 
ATOM   1926  C  C   . ILE A 1 673  ? 116.138 101.239 104.341 1.00 27.12  ? 244  ILE A C   1 
ATOM   1927  O  O   . ILE A 1 673  ? 117.204 100.973 103.783 1.00 35.35  ? 244  ILE A O   1 
ATOM   1928  C  CB  . ILE A 1 673  ? 114.423 99.398  104.459 1.00 25.72  ? 244  ILE A CB  1 
ATOM   1929  C  CG1 . ILE A 1 673  ? 113.904 98.315  105.375 1.00 31.66  ? 244  ILE A CG1 1 
ATOM   1930  C  CG2 . ILE A 1 673  ? 115.113 98.723  103.336 1.00 34.64  ? 244  ILE A CG2 1 
ATOM   1931  C  CD1 . ILE A 1 673  ? 114.965 97.311  105.705 1.00 41.41  ? 244  ILE A CD1 1 
ATOM   1932  N  N   . THR A 1 674  ? 115.583 102.438 104.227 1.00 28.14  ? 245  THR A N   1 
ATOM   1933  C  CA  . THR A 1 674  ? 116.297 103.411 103.412 1.00 29.20  ? 245  THR A CA  1 
ATOM   1934  C  C   . THR A 1 674  ? 117.578 103.900 104.100 1.00 35.79  ? 245  THR A C   1 
ATOM   1935  O  O   . THR A 1 674  ? 118.564 104.179 103.407 1.00 37.45  ? 245  THR A O   1 
ATOM   1936  C  CB  . THR A 1 674  ? 115.376 104.577 103.007 1.00 40.81  ? 245  THR A CB  1 
ATOM   1937  O  OG1 . THR A 1 674  ? 116.064 105.412 102.068 1.00 44.28  ? 245  THR A OG1 1 
ATOM   1938  C  CG2 . THR A 1 674  ? 114.934 105.436 104.200 1.00 49.88  ? 245  THR A CG2 1 
ATOM   1939  N  N   . CYS A 1 675  ? 117.606 103.989 105.448 1.00 38.02  ? 246  CYS A N   1 
ATOM   1940  C  CA  . CYS A 1 675  ? 118.852 104.326 106.148 1.00 30.87  ? 246  CYS A CA  1 
ATOM   1941  C  C   . CYS A 1 675  ? 119.889 103.231 105.975 1.00 31.75  ? 246  CYS A C   1 
ATOM   1942  O  O   . CYS A 1 675  ? 121.070 103.514 105.748 1.00 36.70  ? 246  CYS A O   1 
ATOM   1943  C  CB  . CYS A 1 675  ? 118.615 104.546 107.641 1.00 24.11  ? 246  CYS A CB  1 
ATOM   1944  S  SG  . CYS A 1 675  ? 117.713 106.037 108.044 1.00 42.70  ? 246  CYS A SG  1 
ATOM   1945  N  N   . ARG A 1 676  ? 119.474 101.979 106.108 1.00 27.04  ? 247  ARG A N   1 
ATOM   1946  C  CA  . ARG A 1 676  ? 120.388 100.885 105.878 1.00 21.43  ? 247  ARG A CA  1 
ATOM   1947  C  C   . ARG A 1 676  ? 120.912 100.922 104.465 1.00 26.37  ? 247  ARG A C   1 
ATOM   1948  O  O   . ARG A 1 676  ? 122.107 100.697 104.238 1.00 35.73  ? 247  ARG A O   1 
ATOM   1949  C  CB  . ARG A 1 676  ? 119.693 99.570  106.169 1.00 27.43  ? 247  ARG A CB  1 
ATOM   1950  C  CG  . ARG A 1 676  ? 119.392 99.385  107.617 1.00 29.35  ? 247  ARG A CG  1 
ATOM   1951  C  CD  . ARG A 1 676  ? 118.796 98.048  107.824 1.00 28.41  ? 247  ARG A CD  1 
ATOM   1952  N  NE  . ARG A 1 676  ? 118.631 97.814  109.229 1.00 21.27  ? 247  ARG A NE  1 
ATOM   1953  C  CZ  . ARG A 1 676  ? 118.234 96.659  109.706 1.00 23.06  ? 247  ARG A CZ  1 
ATOM   1954  N  NH1 . ARG A 1 676  ? 117.951 95.678  108.872 1.00 27.81  ? 247  ARG A NH1 1 
ATOM   1955  N  NH2 . ARG A 1 676  ? 118.124 96.492  111.005 1.00 31.72  ? 247  ARG A NH2 1 
ATOM   1956  N  N   . PHE A 1 677  ? 120.045 101.213 103.500 1.00 23.30  ? 248  PHE A N   1 
ATOM   1957  C  CA  . PHE A 1 677  ? 120.501 101.277 102.123 1.00 22.48  ? 248  PHE A CA  1 
ATOM   1958  C  C   . PHE A 1 677  ? 121.539 102.378 101.943 1.00 27.64  ? 248  PHE A C   1 
ATOM   1959  O  O   . PHE A 1 677  ? 122.617 102.145 101.387 1.00 33.33  ? 248  PHE A O   1 
ATOM   1960  C  CB  . PHE A 1 677  ? 119.309 101.451 101.179 1.00 28.32  ? 248  PHE A CB  1 
ATOM   1961  C  CG  . PHE A 1 677  ? 119.689 101.894 99.810  1.00 25.08  ? 248  PHE A CG  1 
ATOM   1962  C  CD1 . PHE A 1 677  ? 120.219 101.003 98.910  1.00 34.51  ? 248  PHE A CD1 1 
ATOM   1963  C  CD2 . PHE A 1 677  ? 119.453 103.181 99.401  1.00 27.23  ? 248  PHE A CD2 1 
ATOM   1964  C  CE1 . PHE A 1 677  ? 120.585 101.404 97.639  1.00 34.79  ? 248  PHE A CE1 1 
ATOM   1965  C  CE2 . PHE A 1 677  ? 119.794 103.596 98.129  1.00 34.17  ? 248  PHE A CE2 1 
ATOM   1966  C  CZ  . PHE A 1 677  ? 120.364 102.704 97.244  1.00 35.41  ? 248  PHE A CZ  1 
ATOM   1967  N  N   . ASN A 1 678  ? 121.253 103.580 102.433 1.00 32.15  ? 249  ASN A N   1 
ATOM   1968  C  CA  . ASN A 1 678  ? 122.223 104.660 102.300 1.00 25.05  ? 249  ASN A CA  1 
ATOM   1969  C  C   . ASN A 1 678  ? 123.544 104.259 102.927 1.00 29.54  ? 249  ASN A C   1 
ATOM   1970  O  O   . ASN A 1 678  ? 124.598 104.465 102.333 1.00 34.94  ? 249  ASN A O   1 
ATOM   1971  C  CB  . ASN A 1 678  ? 121.699 105.929 102.969 1.00 26.79  ? 249  ASN A CB  1 
ATOM   1972  C  CG  . ASN A 1 678  ? 120.450 106.436 102.319 1.00 29.23  ? 249  ASN A CG  1 
ATOM   1973  O  OD1 . ASN A 1 678  ? 120.223 106.205 101.128 1.00 33.30  ? 249  ASN A OD1 1 
ATOM   1974  N  ND2 . ASN A 1 678  ? 119.613 107.110 103.089 1.00 30.61  ? 249  ASN A ND2 1 
ATOM   1975  N  N   . THR A 1 679  ? 123.501 103.686 104.142 1.00 29.89  ? 250  THR A N   1 
ATOM   1976  C  CA  . THR A 1 679  ? 124.722 103.356 104.876 1.00 22.86  ? 250  THR A CA  1 
ATOM   1977  C  C   . THR A 1 679  ? 125.560 102.325 104.132 1.00 27.01  ? 250  THR A C   1 
ATOM   1978  O  O   . THR A 1 679  ? 126.785 102.469 104.022 1.00 33.36  ? 250  THR A O   1 
ATOM   1979  C  CB  . THR A 1 679  ? 124.384 102.847 106.268 1.00 18.67  ? 250  THR A CB  1 
ATOM   1980  O  OG1 . THR A 1 679  ? 123.613 103.829 106.956 1.00 25.69  ? 250  THR A OG1 1 
ATOM   1981  C  CG2 . THR A 1 679  ? 125.632 102.581 107.040 1.00 30.48  ? 250  THR A CG2 1 
ATOM   1982  N  N   . THR A 1 680  ? 124.923 101.294 103.586 1.00 23.24  ? 251  THR A N   1 
ATOM   1983  C  CA  . THR A 1 680  ? 125.705 100.294 102.877 1.00 19.66  ? 251  THR A CA  1 
ATOM   1984  C  C   . THR A 1 680  ? 126.194 100.830 101.534 1.00 24.51  ? 251  THR A C   1 
ATOM   1985  O  O   . THR A 1 680  ? 127.320 100.531 101.123 1.00 41.30  ? 251  THR A O   1 
ATOM   1986  C  CB  . THR A 1 680  ? 124.904 99.009  102.687 1.00 26.62  ? 251  THR A CB  1 
ATOM   1987  O  OG1 . THR A 1 680  ? 123.716 99.288  101.947 1.00 31.96  ? 251  THR A OG1 1 
ATOM   1988  C  CG2 . THR A 1 680  ? 124.480 98.420  104.042 1.00 23.21  ? 251  THR A CG2 1 
ATOM   1989  N  N   . LEU A 1 681  ? 125.398 101.643 100.842 1.00 22.51  ? 252  LEU A N   1 
ATOM   1990  C  CA  . LEU A 1 681  ? 125.889 102.267 99.611  1.00 21.84  ? 252  LEU A CA  1 
ATOM   1991  C  C   . LEU A 1 681  ? 127.044 103.211 99.878  1.00 27.15  ? 252  LEU A C   1 
ATOM   1992  O  O   . LEU A 1 681  ? 127.998 103.266 99.101  1.00 36.26  ? 252  LEU A O   1 
ATOM   1993  C  CB  . LEU A 1 681  ? 124.776 103.034 98.915  1.00 28.87  ? 252  LEU A CB  1 
ATOM   1994  C  CG  . LEU A 1 681  ? 125.200 103.739 97.640  1.00 32.80  ? 252  LEU A CG  1 
ATOM   1995  C  CD1 . LEU A 1 681  ? 125.847 102.761 96.686  1.00 45.26  ? 252  LEU A CD1 1 
ATOM   1996  C  CD2 . LEU A 1 681  ? 123.963 104.361 96.997  1.00 36.81  ? 252  LEU A CD2 1 
ATOM   1997  N  N   . ILE A 1 682  ? 126.956 103.982 100.955 1.00 25.54  ? 253  ILE A N   1 
ATOM   1998  C  CA  . ILE A 1 682  ? 127.986 104.946 101.298 1.00 17.67  ? 253  ILE A CA  1 
ATOM   1999  C  C   . ILE A 1 682  ? 129.283 104.229 101.615 1.00 29.47  ? 253  ILE A C   1 
ATOM   2000  O  O   . ILE A 1 682  ? 130.354 104.598 101.116 1.00 37.11  ? 253  ILE A O   1 
ATOM   2001  C  CB  . ILE A 1 682  ? 127.514 105.791 102.481 1.00 18.70  ? 253  ILE A CB  1 
ATOM   2002  C  CG1 . ILE A 1 682  ? 126.495 106.810 102.010 1.00 27.13  ? 253  ILE A CG1 1 
ATOM   2003  C  CG2 . ILE A 1 682  ? 128.676 106.477 103.121 1.00 34.79  ? 253  ILE A CG2 1 
ATOM   2004  C  CD1 . ILE A 1 682  ? 125.867 107.601 103.138 1.00 30.95  ? 253  ILE A CD1 1 
ATOM   2005  N  N   . SER A 1 683  ? 129.206 103.184 102.449 1.00 31.20  ? 254  SER A N   1 
ATOM   2006  C  CA  . SER A 1 683  ? 130.401 102.406 102.770 1.00 30.03  ? 254  SER A CA  1 
ATOM   2007  C  C   . SER A 1 683  ? 130.992 101.776 101.521 1.00 32.44  ? 254  SER A C   1 
ATOM   2008  O  O   . SER A 1 683  ? 132.218 101.769 101.338 1.00 44.94  ? 254  SER A O   1 
ATOM   2009  C  CB  . SER A 1 683  ? 130.081 101.318 103.794 1.00 28.36  ? 254  SER A CB  1 
ATOM   2010  O  OG  . SER A 1 683  ? 129.573 101.891 104.986 1.00 37.43  ? 254  SER A OG  1 
ATOM   2011  N  N   . LYS A 1 684  ? 130.149 101.252 100.643 1.00 24.08  ? 255  LYS A N   1 
ATOM   2012  C  CA  . LYS A 1 684  ? 130.706 100.606 99.482  1.00 21.55  ? 255  LYS A CA  1 
ATOM   2013  C  C   . LYS A 1 684  ? 131.356 101.618 98.542  1.00 38.09  ? 255  LYS A C   1 
ATOM   2014  O  O   . LYS A 1 684  ? 132.456 101.371 98.025  1.00 52.65  ? 255  LYS A O   1 
ATOM   2015  C  CB  . LYS A 1 684  ? 129.638 99.839  98.766  1.00 26.05  ? 255  LYS A CB  1 
ATOM   2016  C  CG  . LYS A 1 684  ? 130.160 98.594  98.197  1.00 41.13  ? 255  LYS A CG  1 
ATOM   2017  C  CD  . LYS A 1 684  ? 128.973 97.772  97.760  1.00 63.71  ? 255  LYS A CD  1 
ATOM   2018  C  CE  . LYS A 1 684  ? 127.977 97.523  98.898  1.00 62.33  ? 255  LYS A CE  1 
ATOM   2019  N  NZ  . LYS A 1 684  ? 126.815 96.709  98.382  1.00 58.22  ? 255  LYS A NZ  1 
ATOM   2020  N  N   . ILE A 1 685  ? 130.722 102.776 98.316  1.00 31.40  ? 256  ILE A N   1 
ATOM   2021  C  CA  . ILE A 1 685  ? 131.332 103.763 97.420  1.00 29.24  ? 256  ILE A CA  1 
ATOM   2022  C  C   . ILE A 1 685  ? 132.602 104.345 98.032  1.00 39.27  ? 256  ILE A C   1 
ATOM   2023  O  O   . ILE A 1 685  ? 133.535 104.720 97.308  1.00 48.94  ? 256  ILE A O   1 
ATOM   2024  C  CB  . ILE A 1 685  ? 130.345 104.880 97.058  1.00 38.01  ? 256  ILE A CB  1 
ATOM   2025  C  CG1 . ILE A 1 685  ? 129.131 104.305 96.344  1.00 43.74  ? 256  ILE A CG1 1 
ATOM   2026  C  CG2 . ILE A 1 685  ? 131.018 105.917 96.151  1.00 46.70  ? 256  ILE A CG2 1 
ATOM   2027  C  CD1 . ILE A 1 685  ? 129.490 103.562 95.093  1.00 56.10  ? 256  ILE A CD1 1 
ATOM   2028  N  N   . ALA A 1 686  ? 132.672 104.448 99.357  1.00 35.45  ? 257  ALA A N   1 
ATOM   2029  C  CA  . ALA A 1 686  ? 133.928 104.850 99.971  1.00 35.80  ? 257  ALA A CA  1 
ATOM   2030  C  C   . ALA A 1 686  ? 135.022 103.827 99.695  1.00 29.26  ? 257  ALA A C   1 
ATOM   2031  O  O   . ALA A 1 686  ? 136.156 104.192 99.383  1.00 38.66  ? 257  ALA A O   1 
ATOM   2032  C  CB  . ALA A 1 686  ? 133.736 105.046 101.471 1.00 41.57  ? 257  ALA A CB  1 
ATOM   2033  N  N   . GLU A 1 687  ? 134.712 102.543 99.813  1.00 33.78  ? 258  GLU A N   1 
ATOM   2034  C  CA  . GLU A 1 687  ? 135.722 101.554 99.456  1.00 34.33  ? 258  GLU A CA  1 
ATOM   2035  C  C   . GLU A 1 687  ? 136.160 101.725 98.027  1.00 32.31  ? 258  GLU A C   1 
ATOM   2036  O  O   . GLU A 1 687  ? 137.302 101.414 97.688  1.00 43.51  ? 258  GLU A O   1 
ATOM   2037  C  CB  . GLU A 1 687  ? 135.203 100.132 99.658  1.00 41.99  ? 258  GLU A CB  1 
ATOM   2038  C  CG  . GLU A 1 687  ? 134.847 99.833  101.111 1.00 57.86  ? 258  GLU A CG  1 
ATOM   2039  C  CD  . GLU A 1 687  ? 134.803 98.340  101.426 1.00 72.89  ? 258  GLU A CD  1 
ATOM   2040  O  OE1 . GLU A 1 687  ? 135.830 97.652  101.221 1.00 71.77  ? 258  GLU A OE1 1 
ATOM   2041  O  OE2 . GLU A 1 687  ? 133.758 97.860  101.924 1.00 63.07  ? 258  GLU A OE2 1 
ATOM   2042  N  N   . ILE A 1 688  ? 135.260 102.193 97.171  1.00 38.55  ? 259  ILE A N   1 
ATOM   2043  C  CA  . ILE A 1 688  ? 135.617 102.388 95.766  1.00 41.26  ? 259  ILE A CA  1 
ATOM   2044  C  C   . ILE A 1 688  ? 136.574 103.564 95.606  1.00 39.36  ? 259  ILE A C   1 
ATOM   2045  O  O   . ILE A 1 688  ? 137.531 103.501 94.827  1.00 50.40  ? 259  ILE A O   1 
ATOM   2046  C  CB  . ILE A 1 688  ? 134.357 102.593 94.908  1.00 53.54  ? 259  ILE A CB  1 
ATOM   2047  C  CG1 . ILE A 1 688  ? 133.461 101.315 94.868  1.00 62.25  ? 259  ILE A CG1 1 
ATOM   2048  C  CG2 . ILE A 1 688  ? 134.752 103.150 93.532  1.00 61.70  ? 259  ILE A CG2 1 
ATOM   2049  C  CD1 . ILE A 1 688  ? 134.172 99.948  94.631  1.00 64.02  ? 259  ILE A CD1 1 
ATOM   2050  N  N   . GLU A 1 689  ? 136.322 104.664 96.315  1.00 48.36  ? 260  GLU A N   1 
ATOM   2051  C  CA  . GLU A 1 689  ? 137.184 105.835 96.176  1.00 49.42  ? 260  GLU A CA  1 
ATOM   2052  C  C   . GLU A 1 689  ? 138.437 105.766 97.048  1.00 51.53  ? 260  GLU A C   1 
ATOM   2053  O  O   . GLU A 1 689  ? 139.378 106.525 96.795  1.00 55.49  ? 260  GLU A O   1 
ATOM   2054  C  CB  . GLU A 1 689  ? 136.410 107.138 96.479  1.00 51.19  ? 260  GLU A CB  1 
ATOM   2055  C  CG  . GLU A 1 689  ? 136.223 107.537 97.972  1.00 44.78  ? 260  GLU A CG  1 
ATOM   2056  C  CD  . GLU A 1 689  ? 135.716 108.994 98.151  1.00 47.05  ? 260  GLU A CD  1 
ATOM   2057  O  OE1 . GLU A 1 689  ? 135.052 109.525 97.237  1.00 43.78  ? 260  GLU A OE1 1 
ATOM   2058  O  OE2 . GLU A 1 689  ? 136.007 109.626 99.196  1.00 42.91  ? 260  GLU A OE2 1 
ATOM   2059  N  N   . ASP A 1 690  ? 138.480 104.878 98.051  1.00 51.35  ? 261  ASP A N   1 
ATOM   2060  C  CA  . ASP A 1 690  ? 139.622 104.757 98.968  1.00 45.59  ? 261  ASP A CA  1 
ATOM   2061  C  C   . ASP A 1 690  ? 139.838 103.305 99.400  1.00 49.81  ? 261  ASP A C   1 
ATOM   2062  O  O   . ASP A 1 690  ? 139.429 102.897 100.497 1.00 44.74  ? 261  ASP A O   1 
ATOM   2063  C  CB  . ASP A 1 690  ? 139.426 105.648 100.193 1.00 51.23  ? 261  ASP A CB  1 
ATOM   2064  C  CG  . ASP A 1 690  ? 140.728 105.871 100.962 1.00 67.32  ? 261  ASP A CG  1 
ATOM   2065  O  OD1 . ASP A 1 690  ? 141.775 105.316 100.522 1.00 59.27  ? 261  ASP A OD1 1 
ATOM   2066  O  OD2 . ASP A 1 690  ? 140.707 106.602 101.993 1.00 61.04  ? 261  ASP A OD2 1 
ATOM   2067  N  N   . PRO A 1 691  ? 140.487 102.491 98.555  1.00 48.43  ? 262  PRO A N   1 
ATOM   2068  C  CA  . PRO A 1 691  ? 140.567 101.053 98.851  1.00 35.92  ? 262  PRO A CA  1 
ATOM   2069  C  C   . PRO A 1 691  ? 141.313 100.754 100.131 1.00 42.59  ? 262  PRO A C   1 
ATOM   2070  O  O   . PRO A 1 691  ? 140.968 99.800  100.839 1.00 46.12  ? 262  PRO A O   1 
ATOM   2071  C  CB  . PRO A 1 691  ? 141.311 100.487 97.632  1.00 42.55  ? 262  PRO A CB  1 
ATOM   2072  C  CG  . PRO A 1 691  ? 141.146 101.498 96.549  1.00 43.71  ? 262  PRO A CG  1 
ATOM   2073  C  CD  . PRO A 1 691  ? 141.127 102.822 97.267  1.00 51.23  ? 262  PRO A CD  1 
ATOM   2074  N  N   . VAL A 1 692  ? 142.326 101.556 100.453 1.00 48.88  ? 263  VAL A N   1 
ATOM   2075  C  CA  . VAL A 1 692  ? 143.224 101.243 101.564 1.00 46.61  ? 263  VAL A CA  1 
ATOM   2076  C  C   . VAL A 1 692  ? 142.493 101.326 102.899 1.00 48.50  ? 263  VAL A C   1 
ATOM   2077  O  O   . VAL A 1 692  ? 142.408 100.337 103.634 1.00 52.30  ? 263  VAL A O   1 
ATOM   2078  C  CB  . VAL A 1 692  ? 144.444 102.175 101.542 1.00 57.27  ? 263  VAL A CB  1 
ATOM   2079  C  CG1 . VAL A 1 692  ? 145.356 101.867 102.733 1.00 62.56  ? 263  VAL A CG1 1 
ATOM   2080  C  CG2 . VAL A 1 692  ? 145.182 102.059 100.196 1.00 54.78  ? 263  VAL A CG2 1 
ATOM   2081  N  N   . CYS A 1 693  ? 141.962 102.507 103.241 1.00 44.22  ? 264  CYS A N   1 
ATOM   2082  C  CA  . CYS A 1 693  ? 141.252 102.668 104.510 1.00 33.13  ? 264  CYS A CA  1 
ATOM   2083  C  C   . CYS A 1 693  ? 140.175 103.741 104.370 1.00 35.15  ? 264  CYS A C   1 
ATOM   2084  O  O   . CYS A 1 693  ? 140.462 104.927 104.548 1.00 41.98  ? 264  CYS A O   1 
ATOM   2085  C  CB  . CYS A 1 693  ? 142.227 103.026 105.610 1.00 40.55  ? 264  CYS A CB  1 
ATOM   2086  S  SG  . CYS A 1 693  ? 141.380 103.347 107.178 1.00 75.42  ? 264  CYS A SG  1 
ATOM   2087  N  N   . SER A 1 694  ? 138.942 103.326 104.097 1.00 32.63  ? 265  SER A N   1 
ATOM   2088  C  CA  . SER A 1 694  ? 137.841 104.271 103.984 1.00 30.55  ? 265  SER A CA  1 
ATOM   2089  C  C   . SER A 1 694  ? 137.331 104.640 105.362 1.00 28.85  ? 265  SER A C   1 
ATOM   2090  O  O   . SER A 1 694  ? 137.311 103.818 106.278 1.00 36.00  ? 265  SER A O   1 
ATOM   2091  C  CB  . SER A 1 694  ? 136.670 103.684 103.206 1.00 43.10  ? 265  SER A CB  1 
ATOM   2092  O  OG  . SER A 1 694  ? 136.158 102.524 103.850 1.00 40.99  ? 265  SER A OG  1 
ATOM   2093  N  N   . ASP A 1 695  ? 136.873 105.868 105.502 1.00 26.48  ? 266  ASP A N   1 
ATOM   2094  C  CA  . ASP A 1 695  ? 136.456 106.256 106.828 1.00 21.92  ? 266  ASP A CA  1 
ATOM   2095  C  C   . ASP A 1 695  ? 135.128 105.659 107.216 1.00 32.15  ? 266  ASP A C   1 
ATOM   2096  O  O   . ASP A 1 695  ? 134.772 105.719 108.395 1.00 39.88  ? 266  ASP A O   1 
ATOM   2097  C  CB  . ASP A 1 695  ? 136.390 107.757 106.925 1.00 25.16  ? 266  ASP A CB  1 
ATOM   2098  C  CG  . ASP A 1 695  ? 137.743 108.341 106.958 1.00 41.03  ? 266  ASP A CG  1 
ATOM   2099  O  OD1 . ASP A 1 695  ? 138.696 107.543 106.761 1.00 34.78  ? 266  ASP A OD1 1 
ATOM   2100  O  OD2 . ASP A 1 695  ? 137.871 109.571 107.186 1.00 43.81  ? 266  ASP A OD2 1 
ATOM   2101  N  N   . TYR A 1 696  ? 134.413 105.096 106.310 1.00 27.67  ? 267  TYR A N   1 
ATOM   2102  C  CA  . TYR A 1 696  ? 133.187 104.540 106.839 1.00 23.96  ? 267  TYR A CA  1 
ATOM   2103  C  C   . TYR A 1 696  ? 133.441 103.119 107.299 1.00 27.25  ? 267  TYR A C   1 
ATOM   2104  O  O   . TYR A 1 696  ? 134.429 102.497 106.902 1.00 36.39  ? 267  TYR A O   1 
ATOM   2105  C  CB  . TYR A 1 696  ? 132.100 104.590 105.775 1.00 39.64  ? 267  TYR A CB  1 
ATOM   2106  C  CG  . TYR A 1 696  ? 131.765 106.001 105.325 1.00 41.30  ? 267  TYR A CG  1 
ATOM   2107  C  CD1 . TYR A 1 696  ? 130.817 106.760 106.000 1.00 44.83  ? 267  TYR A CD1 1 
ATOM   2108  C  CD2 . TYR A 1 696  ? 132.366 106.556 104.199 1.00 37.83  ? 267  TYR A CD2 1 
ATOM   2109  C  CE1 . TYR A 1 696  ? 130.519 108.064 105.592 1.00 45.93  ? 267  TYR A CE1 1 
ATOM   2110  C  CE2 . TYR A 1 696  ? 132.070 107.842 103.777 1.00 39.74  ? 267  TYR A CE2 1 
ATOM   2111  C  CZ  . TYR A 1 696  ? 131.146 108.597 104.475 1.00 46.09  ? 267  TYR A CZ  1 
ATOM   2112  O  OH  . TYR A 1 696  ? 130.843 109.883 104.059 1.00 44.71  ? 267  TYR A OH  1 
ATOM   2113  N  N   . PRO A 1 697  ? 132.606 102.587 108.175 1.00 20.45  ? 268  PRO A N   1 
ATOM   2114  C  CA  . PRO A 1 697  ? 132.796 101.202 108.605 1.00 21.79  ? 268  PRO A CA  1 
ATOM   2115  C  C   . PRO A 1 697  ? 132.576 100.301 107.416 1.00 31.01  ? 268  PRO A C   1 
ATOM   2116  O  O   . PRO A 1 697  ? 131.708 100.572 106.588 1.00 41.44  ? 268  PRO A O   1 
ATOM   2117  C  CB  . PRO A 1 697  ? 131.695 101.000 109.639 1.00 32.85  ? 268  PRO A CB  1 
ATOM   2118  C  CG  . PRO A 1 697  ? 131.325 102.371 110.062 1.00 35.55  ? 268  PRO A CG  1 
ATOM   2119  C  CD  . PRO A 1 697  ? 131.478 103.226 108.853 1.00 28.22  ? 268  PRO A CD  1 
ATOM   2120  N  N   . ASN A 1 698  ? 133.345 99.220  107.329 1.00 30.51  ? 269  ASN A N   1 
ATOM   2121  C  CA  . ASN A 1 698  ? 133.168 98.304  106.209 1.00 21.86  ? 269  ASN A CA  1 
ATOM   2122  C  C   . ASN A 1 698  ? 131.738 97.790  106.168 1.00 34.47  ? 269  ASN A C   1 
ATOM   2123  O  O   . ASN A 1 698  ? 131.198 97.366  107.192 1.00 41.96  ? 269  ASN A O   1 
ATOM   2124  C  CB  . ASN A 1 698  ? 134.125 97.139  106.326 1.00 24.43  ? 269  ASN A CB  1 
ATOM   2125  C  CG  . ASN A 1 698  ? 134.158 96.329  105.078 1.00 41.44  ? 269  ASN A CG  1 
ATOM   2126  O  OD1 . ASN A 1 698  ? 133.412 95.361  104.932 1.00 45.10  ? 269  ASN A OD1 1 
ATOM   2127  N  ND2 . ASN A 1 698  ? 134.997 96.731  104.139 1.00 48.64  ? 269  ASN A ND2 1 
ATOM   2128  N  N   . PHE A 1 699  ? 131.125 97.818  104.978 1.00 37.50  ? 270  PHE A N   1 
ATOM   2129  C  CA  . PHE A 1 699  ? 129.687 97.566  104.873 1.00 31.53  ? 270  PHE A CA  1 
ATOM   2130  C  C   . PHE A 1 699  ? 129.323 96.155  105.301 1.00 33.20  ? 270  PHE A C   1 
ATOM   2131  O  O   . PHE A 1 699  ? 128.186 95.916  105.714 1.00 39.53  ? 270  PHE A O   1 
ATOM   2132  C  CB  . PHE A 1 699  ? 129.209 97.794  103.447 1.00 32.57  ? 270  PHE A CB  1 
ATOM   2133  C  CG  . PHE A 1 699  ? 129.580 96.699  102.520 1.00 32.64  ? 270  PHE A CG  1 
ATOM   2134  C  CD1 . PHE A 1 699  ? 130.864 96.598  102.049 1.00 43.80  ? 270  PHE A CD1 1 
ATOM   2135  C  CD2 . PHE A 1 699  ? 128.642 95.802  102.074 1.00 43.07  ? 270  PHE A CD2 1 
ATOM   2136  C  CE1 . PHE A 1 699  ? 131.234 95.587  101.179 1.00 53.64  ? 270  PHE A CE1 1 
ATOM   2137  C  CE2 . PHE A 1 699  ? 128.988 94.788  101.191 1.00 50.38  ? 270  PHE A CE2 1 
ATOM   2138  C  CZ  . PHE A 1 699  ? 130.290 94.680  100.741 1.00 56.74  ? 270  PHE A CZ  1 
ATOM   2139  N  N   . LYS A 1 700  ? 130.259 95.205  105.198 1.00 37.56  ? 271  LYS A N   1 
ATOM   2140  C  CA  . LYS A 1 700  ? 130.016 93.858  105.720 1.00 34.60  ? 271  LYS A CA  1 
ATOM   2141  C  C   . LYS A 1 700  ? 129.846 93.861  107.233 1.00 30.28  ? 271  LYS A C   1 
ATOM   2142  O  O   . LYS A 1 700  ? 128.936 93.217  107.756 1.00 39.16  ? 271  LYS A O   1 
ATOM   2143  C  CB  . LYS A 1 700  ? 131.155 92.920  105.332 1.00 39.00  ? 271  LYS A CB  1 
ATOM   2144  C  CG  . LYS A 1 700  ? 130.984 91.518  105.879 1.00 52.84  ? 271  LYS A CG  1 
ATOM   2145  C  CD  . LYS A 1 700  ? 132.168 90.615  105.487 1.00 77.52  ? 271  LYS A CD  1 
ATOM   2146  C  CE  . LYS A 1 700  ? 131.991 89.136  105.919 1.00 92.77  ? 271  LYS A CE  1 
ATOM   2147  N  NZ  . LYS A 1 700  ? 130.789 88.428  105.362 1.00 76.68  ? 271  LYS A NZ  1 
ATOM   2148  N  N   . ILE A 1 701  ? 130.727 94.550  107.955 1.00 30.25  ? 272  ILE A N   1 
ATOM   2149  C  CA  . ILE A 1 701  ? 130.587 94.619  109.401 1.00 25.02  ? 272  ILE A CA  1 
ATOM   2150  C  C   . ILE A 1 701  ? 129.291 95.306  109.764 1.00 30.71  ? 272  ILE A C   1 
ATOM   2151  O  O   . ILE A 1 701  ? 128.580 94.873  110.671 1.00 45.11  ? 272  ILE A O   1 
ATOM   2152  C  CB  . ILE A 1 701  ? 131.777 95.353  110.035 1.00 32.46  ? 272  ILE A CB  1 
ATOM   2153  C  CG1 . ILE A 1 701  ? 133.092 94.613  109.798 1.00 36.20  ? 272  ILE A CG1 1 
ATOM   2154  C  CG2 . ILE A 1 701  ? 131.516 95.602  111.519 1.00 48.10  ? 272  ILE A CG2 1 
ATOM   2155  C  CD1 . ILE A 1 701  ? 134.286 95.315  110.472 1.00 45.58  ? 272  ILE A CD1 1 
ATOM   2156  N  N   . VAL A 1 702  ? 128.985 96.414  109.105 1.00 31.24  ? 273  VAL A N   1 
ATOM   2157  C  CA  . VAL A 1 702  ? 127.735 97.091  109.403 1.00 27.99  ? 273  VAL A CA  1 
ATOM   2158  C  C   . VAL A 1 702  ? 126.564 96.162  109.152 1.00 37.48  ? 273  VAL A C   1 
ATOM   2159  O  O   . VAL A 1 702  ? 125.606 96.136  109.932 1.00 45.79  ? 273  VAL A O   1 
ATOM   2160  C  CB  . VAL A 1 702  ? 127.607 98.389  108.590 1.00 36.92  ? 273  VAL A CB  1 
ATOM   2161  C  CG1 . VAL A 1 702  ? 126.448 99.173  109.084 1.00 43.71  ? 273  VAL A CG1 1 
ATOM   2162  C  CG2 . VAL A 1 702  ? 128.835 99.236  108.773 1.00 42.15  ? 273  VAL A CG2 1 
ATOM   2163  N  N   . SER A 1 703  ? 126.606 95.390  108.060 1.00 38.77  ? 274  SER A N   1 
ATOM   2164  C  CA  . SER A 1 703  ? 125.511 94.465  107.773 1.00 29.37  ? 274  SER A CA  1 
ATOM   2165  C  C   . SER A 1 703  ? 125.400 93.396  108.839 1.00 35.98  ? 274  SER A C   1 
ATOM   2166  O  O   . SER A 1 703  ? 124.294 93.012  109.238 1.00 47.63  ? 274  SER A O   1 
ATOM   2167  C  CB  . SER A 1 703  ? 125.700 93.802  106.427 1.00 35.51  ? 274  SER A CB  1 
ATOM   2168  O  OG  . SER A 1 703  ? 124.641 92.882  106.232 1.00 52.76  ? 274  SER A OG  1 
ATOM   2169  N  N   . MET A 1 704  ? 126.535 92.892  109.297 1.00 36.54  ? 275  MET A N   1 
ATOM   2170  C  CA  . MET A 1 704  ? 126.515 91.938  110.389 1.00 33.77  ? 275  MET A CA  1 
ATOM   2171  C  C   . MET A 1 704  ? 125.927 92.581  111.636 1.00 28.82  ? 275  MET A C   1 
ATOM   2172  O  O   . MET A 1 704  ? 125.174 91.940  112.366 1.00 40.33  ? 275  MET A O   1 
ATOM   2173  C  CB  . MET A 1 704  ? 127.929 91.425  110.643 1.00 40.89  ? 275  MET A CB  1 
ATOM   2174  C  CG  . MET A 1 704  ? 128.044 90.334  111.677 1.00 58.43  ? 275  MET A CG  1 
ATOM   2175  S  SD  . MET A 1 704  ? 129.718 89.642  111.801 1.00 100.60 ? 275  MET A SD  1 
ATOM   2176  C  CE  . MET A 1 704  ? 130.689 91.105  112.215 1.00 67.15  ? 275  MET A CE  1 
ATOM   2177  N  N   . LEU A 1 705  ? 126.257 93.844  111.898 1.00 27.34  ? 276  LEU A N   1 
ATOM   2178  C  CA  . LEU A 1 705  ? 125.668 94.542  113.038 1.00 33.04  ? 276  LEU A CA  1 
ATOM   2179  C  C   . LEU A 1 705  ? 124.166 94.638  112.895 1.00 34.67  ? 276  LEU A C   1 
ATOM   2180  O  O   . LEU A 1 705  ? 123.429 94.500  113.874 1.00 39.46  ? 276  LEU A O   1 
ATOM   2181  C  CB  . LEU A 1 705  ? 126.254 95.946  113.195 1.00 33.13  ? 276  LEU A CB  1 
ATOM   2182  C  CG  . LEU A 1 705  ? 127.561 95.963  113.974 1.00 50.95  ? 276  LEU A CG  1 
ATOM   2183  C  CD1 . LEU A 1 705  ? 128.188 97.354  114.024 1.00 53.76  ? 276  LEU A CD1 1 
ATOM   2184  C  CD2 . LEU A 1 705  ? 127.246 95.461  115.381 1.00 51.25  ? 276  LEU A CD2 1 
ATOM   2185  N  N   . TYR A 1 706  ? 123.699 94.899  111.687 1.00 29.81  ? 277  TYR A N   1 
ATOM   2186  C  CA  . TYR A 1 706  ? 122.271 94.965  111.464 1.00 26.05  ? 277  TYR A CA  1 
ATOM   2187  C  C   . TYR A 1 706  ? 121.628 93.623  111.778 1.00 34.19  ? 277  TYR A C   1 
ATOM   2188  O  O   . TYR A 1 706  ? 120.594 93.561  112.448 1.00 41.16  ? 277  TYR A O   1 
ATOM   2189  C  CB  . TYR A 1 706  ? 121.996 95.370  110.016 1.00 37.59  ? 277  TYR A CB  1 
ATOM   2190  C  CG  . TYR A 1 706  ? 122.385 96.801  109.643 1.00 35.86  ? 277  TYR A CG  1 
ATOM   2191  C  CD1 . TYR A 1 706  ? 122.446 97.813  110.595 1.00 37.44  ? 277  TYR A CD1 1 
ATOM   2192  C  CD2 . TYR A 1 706  ? 122.696 97.126  108.341 1.00 29.29  ? 277  TYR A CD2 1 
ATOM   2193  C  CE1 . TYR A 1 706  ? 122.798 99.087  110.241 1.00 28.14  ? 277  TYR A CE1 1 
ATOM   2194  C  CE2 . TYR A 1 706  ? 123.044 98.387  107.995 1.00 23.63  ? 277  TYR A CE2 1 
ATOM   2195  C  CZ  . TYR A 1 706  ? 123.095 99.355  108.933 1.00 22.07  ? 277  TYR A CZ  1 
ATOM   2196  O  OH  . TYR A 1 706  ? 123.460 100.619 108.551 1.00 29.45  ? 277  TYR A OH  1 
ATOM   2197  N  N   . GLN A 1 707  ? 122.230 92.532  111.297 1.00 35.19  ? 278  GLN A N   1 
ATOM   2198  C  CA  . GLN A 1 707  ? 121.645 91.209  111.522 1.00 33.40  ? 278  GLN A CA  1 
ATOM   2199  C  C   . GLN A 1 707  ? 121.673 90.828  112.992 1.00 33.87  ? 278  GLN A C   1 
ATOM   2200  O  O   . GLN A 1 707  ? 120.706 90.264  113.509 1.00 42.16  ? 278  GLN A O   1 
ATOM   2201  C  CB  . GLN A 1 707  ? 122.378 90.147  110.713 1.00 45.16  ? 278  GLN A CB  1 
ATOM   2202  C  CG  . GLN A 1 707  ? 122.286 90.298  109.213 1.00 55.52  ? 278  GLN A CG  1 
ATOM   2203  C  CD  . GLN A 1 707  ? 122.792 89.051  108.488 1.00 78.94  ? 278  GLN A CD  1 
ATOM   2204  O  OE1 . GLN A 1 707  ? 122.939 87.980  109.091 1.00 71.97  ? 278  GLN A OE1 1 
ATOM   2205  N  NE2 . GLN A 1 707  ? 123.061 89.186  107.188 1.00 83.70  ? 278  GLN A NE2 1 
ATOM   2206  N  N   . SER A 1 708  ? 122.783 91.091  113.673 1.00 32.06  ? 279  SER A N   1 
ATOM   2207  C  CA  . SER A 1 708  ? 122.842 90.838  115.103 1.00 27.49  ? 279  SER A CA  1 
ATOM   2208  C  C   . SER A 1 708  ? 121.772 91.625  115.825 1.00 29.77  ? 279  SER A C   1 
ATOM   2209  O  O   . SER A 1 708  ? 121.055 91.086  116.670 1.00 41.92  ? 279  SER A O   1 
ATOM   2210  C  CB  . SER A 1 708  ? 124.213 91.206  115.656 1.00 29.66  ? 279  SER A CB  1 
ATOM   2211  O  OG  . SER A 1 708  ? 125.239 90.506  114.980 1.00 41.07  ? 279  SER A OG  1 
ATOM   2212  N  N   . GLY A 1 709  ? 121.647 92.905  115.508 1.00 33.59  ? 280  GLY A N   1 
ATOM   2213  C  CA  . GLY A 1 709  ? 120.678 93.723  116.204 1.00 36.64  ? 280  GLY A CA  1 
ATOM   2214  C  C   . GLY A 1 709  ? 119.266 93.245  115.963 1.00 32.28  ? 280  GLY A C   1 
ATOM   2215  O  O   . GLY A 1 709  ? 118.448 93.211  116.881 1.00 44.27  ? 280  GLY A O   1 
ATOM   2216  N  N   . ASP A 1 710  ? 118.966 92.852  114.735 1.00 30.87  ? 281  ASP A N   1 
ATOM   2217  C  CA  . ASP A 1 710  ? 117.629 92.353  114.454 1.00 36.45  ? 281  ASP A CA  1 
ATOM   2218  C  C   . ASP A 1 710  ? 117.378 91.025  115.150 1.00 40.56  ? 281  ASP A C   1 
ATOM   2219  O  O   . ASP A 1 710  ? 116.269 90.763  115.621 1.00 43.90  ? 281  ASP A O   1 
ATOM   2220  C  CB  . ASP A 1 710  ? 117.426 92.216  112.947 1.00 52.23  ? 281  ASP A CB  1 
ATOM   2221  C  CG  . ASP A 1 710  ? 117.258 93.572  112.258 1.00 61.94  ? 281  ASP A CG  1 
ATOM   2222  O  OD1 . ASP A 1 710  ? 117.233 94.593  112.988 1.00 52.25  ? 281  ASP A OD1 1 
ATOM   2223  O  OD2 . ASP A 1 710  ? 117.156 93.619  110.999 1.00 60.76  ? 281  ASP A OD2 1 
ATOM   2224  N  N   . TYR A 1 711  ? 118.375 90.157  115.196 1.00 40.57  ? 282  TYR A N   1 
ATOM   2225  C  CA  . TYR A 1 711  ? 118.194 88.907  115.909 1.00 37.62  ? 282  TYR A CA  1 
ATOM   2226  C  C   . TYR A 1 711  ? 117.892 89.183  117.371 1.00 27.20  ? 282  TYR A C   1 
ATOM   2227  O  O   . TYR A 1 711  ? 116.946 88.634  117.953 1.00 37.15  ? 282  TYR A O   1 
ATOM   2228  C  CB  . TYR A 1 711  ? 119.450 88.046  115.695 1.00 39.04  ? 282  TYR A CB  1 
ATOM   2229  C  CG  . TYR A 1 711  ? 119.393 86.735  116.395 1.00 46.79  ? 282  TYR A CG  1 
ATOM   2230  C  CD1 . TYR A 1 711  ? 118.656 85.682  115.882 1.00 47.86  ? 282  TYR A CD1 1 
ATOM   2231  C  CD2 . TYR A 1 711  ? 120.119 86.532  117.552 1.00 55.52  ? 282  TYR A CD2 1 
ATOM   2232  C  CE1 . TYR A 1 711  ? 118.594 84.477  116.541 1.00 50.42  ? 282  TYR A CE1 1 
ATOM   2233  C  CE2 . TYR A 1 711  ? 120.084 85.321  118.210 1.00 54.69  ? 282  TYR A CE2 1 
ATOM   2234  C  CZ  . TYR A 1 711  ? 119.319 84.300  117.700 1.00 51.17  ? 282  TYR A CZ  1 
ATOM   2235  O  OH  . TYR A 1 711  ? 119.287 83.101  118.372 1.00 56.89  ? 282  TYR A OH  1 
ATOM   2236  N  N   . LEU A 1 712  ? 118.651 90.084  117.949 1.00 30.29  ? 283  LEU A N   1 
ATOM   2237  C  CA  . LEU A 1 712  ? 118.452 90.452  119.330 1.00 28.72  ? 283  LEU A CA  1 
ATOM   2238  C  C   . LEU A 1 712  ? 117.066 90.990  119.526 1.00 28.58  ? 283  LEU A C   1 
ATOM   2239  O  O   . LEU A 1 712  ? 116.409 90.684  120.522 1.00 41.09  ? 283  LEU A O   1 
ATOM   2240  C  CB  . LEU A 1 712  ? 119.487 91.500  119.718 1.00 35.21  ? 283  LEU A CB  1 
ATOM   2241  C  CG  . LEU A 1 712  ? 119.649 91.863  121.175 1.00 37.33  ? 283  LEU A CG  1 
ATOM   2242  C  CD1 . LEU A 1 712  ? 121.121 92.025  121.487 1.00 44.99  ? 283  LEU A CD1 1 
ATOM   2243  C  CD2 . LEU A 1 712  ? 118.930 93.166  121.379 1.00 44.82  ? 283  LEU A CD2 1 
ATOM   2244  N  N   . LEU A 1 713  ? 116.607 91.806  118.593 1.00 34.80  ? 284  LEU A N   1 
ATOM   2245  C  CA  . LEU A 1 713  ? 115.271 92.357  118.729 1.00 37.21  ? 284  LEU A CA  1 
ATOM   2246  C  C   . LEU A 1 713  ? 114.221 91.257  118.576 1.00 42.98  ? 284  LEU A C   1 
ATOM   2247  O  O   . LEU A 1 713  ? 113.207 91.285  119.278 1.00 45.63  ? 284  LEU A O   1 
ATOM   2248  C  CB  . LEU A 1 713  ? 115.042 93.485  117.717 1.00 37.91  ? 284  LEU A CB  1 
ATOM   2249  C  CG  . LEU A 1 713  ? 115.821 94.795  117.914 1.00 36.75  ? 284  LEU A CG  1 
ATOM   2250  C  CD1 . LEU A 1 713  ? 115.443 95.872  116.868 1.00 33.67  ? 284  LEU A CD1 1 
ATOM   2251  C  CD2 . LEU A 1 713  ? 115.659 95.314  119.323 1.00 43.90  ? 284  LEU A CD2 1 
ATOM   2252  N  N   . SER A 1 714  ? 114.465 90.253  117.711 1.00 33.61  ? 285  SER A N   1 
ATOM   2253  C  CA  . SER A 1 714  ? 113.436 89.244  117.473 1.00 26.52  ? 285  SER A CA  1 
ATOM   2254  C  C   . SER A 1 714  ? 113.288 88.337  118.679 1.00 36.45  ? 285  SER A C   1 
ATOM   2255  O  O   . SER A 1 714  ? 112.231 87.725  118.874 1.00 41.99  ? 285  SER A O   1 
ATOM   2256  C  CB  . SER A 1 714  ? 113.745 88.398  116.247 1.00 27.23  ? 285  SER A CB  1 
ATOM   2257  O  OG  . SER A 1 714  ? 114.913 87.632  116.438 1.00 37.08  ? 285  SER A OG  1 
ATOM   2258  N  N   . ILE A 1 715  ? 114.337 88.228  119.482 1.00 38.12  ? 286  ILE A N   1 
ATOM   2259  C  CA  . ILE A 1 715  ? 114.256 87.438  120.704 1.00 26.71  ? 286  ILE A CA  1 
ATOM   2260  C  C   . ILE A 1 715  ? 113.768 88.258  121.874 1.00 23.02  ? 286  ILE A C   1 
ATOM   2261  O  O   . ILE A 1 715  ? 112.990 87.777  122.686 1.00 37.02  ? 286  ILE A O   1 
ATOM   2262  C  CB  . ILE A 1 715  ? 115.614 86.830  121.006 1.00 28.02  ? 286  ILE A CB  1 
ATOM   2263  C  CG1 . ILE A 1 715  ? 115.987 85.895  119.870 1.00 38.08  ? 286  ILE A CG1 1 
ATOM   2264  C  CG2 . ILE A 1 715  ? 115.554 86.098  122.316 1.00 36.93  ? 286  ILE A CG2 1 
ATOM   2265  C  CD1 . ILE A 1 715  ? 117.304 85.260  120.085 1.00 51.06  ? 286  ILE A CD1 1 
ATOM   2266  N  N   . LEU A 1 716  ? 114.186 89.499  121.995 1.00 25.88  ? 287  LEU A N   1 
ATOM   2267  C  CA  . LEU A 1 716  ? 113.881 90.269  123.186 1.00 33.80  ? 287  LEU A CA  1 
ATOM   2268  C  C   . LEU A 1 716  ? 112.631 91.128  123.051 1.00 39.52  ? 287  LEU A C   1 
ATOM   2269  O  O   . LEU A 1 716  ? 111.792 91.121  123.953 1.00 46.27  ? 287  LEU A O   1 
ATOM   2270  C  CB  . LEU A 1 716  ? 115.077 91.157  123.533 1.00 41.09  ? 287  LEU A CB  1 
ATOM   2271  C  CG  . LEU A 1 716  ? 116.313 90.318  123.811 1.00 36.51  ? 287  LEU A CG  1 
ATOM   2272  C  CD1 . LEU A 1 716  ? 117.521 91.172  124.237 1.00 33.31  ? 287  LEU A CD1 1 
ATOM   2273  C  CD2 . LEU A 1 716  ? 115.928 89.310  124.878 1.00 42.39  ? 287  LEU A CD2 1 
ATOM   2274  N  N   . GLY A 1 717  ? 112.494 91.890  121.967 1.00 37.47  ? 288  GLY A N   1 
ATOM   2275  C  CA  . GLY A 1 717  ? 111.353 92.767  121.823 1.00 43.83  ? 288  GLY A CA  1 
ATOM   2276  C  C   . GLY A 1 717  ? 111.743 94.229  121.818 1.00 47.73  ? 288  GLY A C   1 
ATOM   2277  O  O   . GLY A 1 717  ? 112.839 94.573  121.360 1.00 43.73  ? 288  GLY A O   1 
ATOM   2278  N  N   . SER A 1 718  ? 110.855 95.106  122.310 1.00 47.21  ? 289  SER A N   1 
ATOM   2279  C  CA  . SER A 1 718  ? 111.244 96.498  122.480 1.00 44.46  ? 289  SER A CA  1 
ATOM   2280  C  C   . SER A 1 718  ? 112.387 96.631  123.471 1.00 44.73  ? 289  SER A C   1 
ATOM   2281  O  O   . SER A 1 718  ? 113.157 97.593  123.390 1.00 49.46  ? 289  SER A O   1 
ATOM   2282  C  CB  . SER A 1 718  ? 110.071 97.337  122.961 1.00 43.06  ? 289  SER A CB  1 
ATOM   2283  O  OG  . SER A 1 718  ? 109.678 96.908  124.251 1.00 50.19  ? 289  SER A OG  1 
ATOM   2284  N  N   . ASP A 1 719  ? 112.521 95.682  124.395 1.00 42.15  ? 290  ASP A N   1 
ATOM   2285  C  CA  . ASP A 1 719  ? 113.635 95.731  125.330 1.00 41.59  ? 290  ASP A CA  1 
ATOM   2286  C  C   . ASP A 1 719  ? 114.965 95.626  124.613 1.00 37.02  ? 290  ASP A C   1 
ATOM   2287  O  O   . ASP A 1 719  ? 115.970 96.163  125.088 1.00 41.77  ? 290  ASP A O   1 
ATOM   2288  C  CB  . ASP A 1 719  ? 113.498 94.612  126.352 1.00 49.96  ? 290  ASP A CB  1 
ATOM   2289  C  CG  . ASP A 1 719  ? 112.159 94.647  127.033 1.00 66.03  ? 290  ASP A CG  1 
ATOM   2290  O  OD1 . ASP A 1 719  ? 111.386 95.592  126.727 1.00 61.87  ? 290  ASP A OD1 1 
ATOM   2291  O  OD2 . ASP A 1 719  ? 111.865 93.748  127.852 1.00 74.22  ? 290  ASP A OD2 1 
ATOM   2292  N  N   . GLY A 1 720  ? 114.997 94.953  123.471 1.00 35.90  ? 291  GLY A N   1 
ATOM   2293  C  CA  . GLY A 1 720  ? 116.260 94.819  122.799 1.00 29.70  ? 291  GLY A CA  1 
ATOM   2294  C  C   . GLY A 1 720  ? 116.897 96.154  122.556 1.00 27.92  ? 291  GLY A C   1 
ATOM   2295  O  O   . GLY A 1 720  ? 118.122 96.246  122.419 1.00 35.06  ? 291  GLY A O   1 
ATOM   2296  N  N   . TYR A 1 721  ? 116.101 97.210  122.536 1.00 26.93  ? 292  TYR A N   1 
ATOM   2297  C  CA  . TYR A 1 721  ? 116.730 98.488  122.326 1.00 26.19  ? 292  TYR A CA  1 
ATOM   2298  C  C   . TYR A 1 721  ? 117.561 98.866  123.523 1.00 32.09  ? 292  TYR A C   1 
ATOM   2299  O  O   . TYR A 1 721  ? 118.482 99.670  123.381 1.00 44.53  ? 292  TYR A O   1 
ATOM   2300  C  CB  . TYR A 1 721  ? 115.698 99.560  122.005 1.00 32.65  ? 292  TYR A CB  1 
ATOM   2301  C  CG  . TYR A 1 721  ? 115.105 99.300  120.644 1.00 31.76  ? 292  TYR A CG  1 
ATOM   2302  C  CD1 . TYR A 1 721  ? 115.815 99.587  119.497 1.00 34.81  ? 292  TYR A CD1 1 
ATOM   2303  C  CD2 . TYR A 1 721  ? 113.850 98.732  120.515 1.00 31.55  ? 292  TYR A CD2 1 
ATOM   2304  C  CE1 . TYR A 1 721  ? 115.284 99.328  118.263 1.00 34.39  ? 292  TYR A CE1 1 
ATOM   2305  C  CE2 . TYR A 1 721  ? 113.313 98.468  119.295 1.00 32.92  ? 292  TYR A CE2 1 
ATOM   2306  C  CZ  . TYR A 1 721  ? 114.028 98.769  118.169 1.00 35.81  ? 292  TYR A CZ  1 
ATOM   2307  O  OH  . TYR A 1 721  ? 113.482 98.507  116.929 1.00 42.70  ? 292  TYR A OH  1 
ATOM   2308  N  N   . LYS A 1 722  ? 117.321 98.260  124.682 1.00 29.73  ? 293  LYS A N   1 
ATOM   2309  C  CA  . LYS A 1 722  ? 118.198 98.570  125.798 1.00 24.89  ? 293  LYS A CA  1 
ATOM   2310  C  C   . LYS A 1 722  ? 119.580 97.984  125.604 1.00 25.88  ? 293  LYS A C   1 
ATOM   2311  O  O   . LYS A 1 722  ? 120.465 98.246  126.423 1.00 33.24  ? 293  LYS A O   1 
ATOM   2312  C  CB  . LYS A 1 722  ? 117.599 98.089  127.114 1.00 27.24  ? 293  LYS A CB  1 
ATOM   2313  C  CG  . LYS A 1 722  ? 116.592 99.073  127.651 1.00 34.12  ? 293  LYS A CG  1 
ATOM   2314  C  CD  . LYS A 1 722  ? 116.005 98.580  128.935 1.00 34.68  ? 293  LYS A CD  1 
ATOM   2315  C  CE  . LYS A 1 722  ? 115.018 97.482  128.699 1.00 39.79  ? 293  LYS A CE  1 
ATOM   2316  N  NZ  . LYS A 1 722  ? 114.407 97.147  130.013 1.00 51.84  ? 293  LYS A NZ  1 
ATOM   2317  N  N   . ILE A 1 723  ? 119.785 97.182  124.565 1.00 28.38  ? 294  ILE A N   1 
ATOM   2318  C  CA  . ILE A 1 723  ? 121.118 96.763  124.181 1.00 23.02  ? 294  ILE A CA  1 
ATOM   2319  C  C   . ILE A 1 723  ? 121.596 97.484  122.936 1.00 25.98  ? 294  ILE A C   1 
ATOM   2320  O  O   . ILE A 1 723  ? 122.778 97.826  122.847 1.00 31.77  ? 294  ILE A O   1 
ATOM   2321  C  CB  . ILE A 1 723  ? 121.152 95.250  123.961 1.00 21.59  ? 294  ILE A CB  1 
ATOM   2322  C  CG1 . ILE A 1 723  ? 120.735 94.585  125.243 1.00 25.96  ? 294  ILE A CG1 1 
ATOM   2323  C  CG2 . ILE A 1 723  ? 122.510 94.861  123.515 1.00 22.53  ? 294  ILE A CG2 1 
ATOM   2324  C  CD1 . ILE A 1 723  ? 121.667 94.975  126.359 1.00 32.79  ? 294  ILE A CD1 1 
ATOM   2325  N  N   . ILE A 1 724  ? 120.702 97.762  121.993 1.00 27.59  ? 295  ILE A N   1 
ATOM   2326  C  CA  . ILE A 1 724  ? 121.120 98.486  120.802 1.00 22.54  ? 295  ILE A CA  1 
ATOM   2327  C  C   . ILE A 1 724  ? 121.606 99.850  121.224 1.00 23.15  ? 295  ILE A C   1 
ATOM   2328  O  O   . ILE A 1 724  ? 122.498 100.425 120.604 1.00 32.64  ? 295  ILE A O   1 
ATOM   2329  C  CB  . ILE A 1 724  ? 119.960 98.646  119.811 1.00 28.77  ? 295  ILE A CB  1 
ATOM   2330  C  CG1 . ILE A 1 724  ? 119.400 97.288  119.358 1.00 34.87  ? 295  ILE A CG1 1 
ATOM   2331  C  CG2 . ILE A 1 724  ? 120.467 99.349  118.563 1.00 28.61  ? 295  ILE A CG2 1 
ATOM   2332  C  CD1 . ILE A 1 724  ? 120.374 96.372  118.626 1.00 46.66  ? 295  ILE A CD1 1 
ATOM   2333  N  N   . LYS A 1 725  ? 121.010 100.399 122.275 1.00 25.24  ? 296  LYS A N   1 
ATOM   2334  C  CA  . LYS A 1 725  ? 121.360 101.715 122.744 1.00 24.55  ? 296  LYS A CA  1 
ATOM   2335  C  C   . LYS A 1 725  ? 122.819 101.804 123.113 1.00 27.75  ? 296  LYS A C   1 
ATOM   2336  O  O   . LYS A 1 725  ? 123.390 102.890 123.073 1.00 33.93  ? 296  LYS A O   1 
ATOM   2337  C  CB  . LYS A 1 725  ? 120.469 102.056 123.927 1.00 29.50  ? 296  LYS A CB  1 
ATOM   2338  C  CG  . LYS A 1 725  ? 120.653 103.464 124.387 1.00 44.01  ? 296  LYS A CG  1 
ATOM   2339  C  CD  . LYS A 1 725  ? 120.035 103.753 125.740 1.00 46.46  ? 296  LYS A CD  1 
ATOM   2340  C  CE  . LYS A 1 725  ? 118.570 103.365 125.740 1.00 50.15  ? 296  LYS A CE  1 
ATOM   2341  N  NZ  . LYS A 1 725  ? 117.982 103.613 127.079 1.00 56.31  ? 296  LYS A NZ  1 
ATOM   2342  N  N   . PHE A 1 726  ? 123.447 100.701 123.434 1.00 25.47  ? 297  PHE A N   1 
ATOM   2343  C  CA  . PHE A 1 726  ? 124.843 100.786 123.791 1.00 22.75  ? 297  PHE A CA  1 
ATOM   2344  C  C   . PHE A 1 726  ? 125.730 100.802 122.613 1.00 24.18  ? 297  PHE A C   1 
ATOM   2345  O  O   . PHE A 1 726  ? 126.900 100.444 122.755 1.00 30.03  ? 297  PHE A O   1 
ATOM   2346  C  CB  . PHE A 1 726  ? 125.240 99.609  124.659 1.00 26.76  ? 297  PHE A CB  1 
ATOM   2347  C  CG  . PHE A 1 726  ? 124.747 99.712  126.034 1.00 24.25  ? 297  PHE A CG  1 
ATOM   2348  C  CD1 . PHE A 1 726  ? 125.279 100.624 126.892 1.00 28.76  ? 297  PHE A CD1 1 
ATOM   2349  C  CD2 . PHE A 1 726  ? 123.746 98.881  126.478 1.00 30.42  ? 297  PHE A CD2 1 
ATOM   2350  C  CE1 . PHE A 1 726  ? 124.816 100.720 128.180 1.00 36.82  ? 297  PHE A CE1 1 
ATOM   2351  C  CE2 . PHE A 1 726  ? 123.272 98.965  127.773 1.00 33.45  ? 297  PHE A CE2 1 
ATOM   2352  C  CZ  . PHE A 1 726  ? 123.810 99.888  128.625 1.00 35.42  ? 297  PHE A CZ  1 
ATOM   2353  N  N   . LEU A 1 727  ? 125.218 101.105 121.429 1.00 24.27  ? 298  LEU A N   1 
ATOM   2354  C  CA  . LEU A 1 727  ? 126.117 101.219 120.290 1.00 26.75  ? 298  LEU A CA  1 
ATOM   2355  C  C   . LEU A 1 727  ? 126.948 102.496 120.381 1.00 37.59  ? 298  LEU A C   1 
ATOM   2356  O  O   . LEU A 1 727  ? 128.174 102.465 120.218 1.00 43.22  ? 298  LEU A O   1 
ATOM   2357  C  CB  . LEU A 1 727  ? 125.339 101.173 118.985 1.00 25.09  ? 298  LEU A CB  1 
ATOM   2358  C  CG  . LEU A 1 727  ? 126.214 101.251 117.742 1.00 27.73  ? 298  LEU A CG  1 
ATOM   2359  C  CD1 . LEU A 1 727  ? 125.737 100.240 116.713 1.00 35.93  ? 298  LEU A CD1 1 
ATOM   2360  C  CD2 . LEU A 1 727  ? 126.174 102.654 117.161 1.00 35.13  ? 298  LEU A CD2 1 
ATOM   2361  N  N   . GLU A 1 728  ? 126.302 103.631 120.659 1.00 37.74  ? 299  GLU A N   1 
ATOM   2362  C  CA  . GLU A 1 728  ? 127.034 104.895 120.748 1.00 36.13  ? 299  GLU A CA  1 
ATOM   2363  C  C   . GLU A 1 728  ? 128.044 104.914 121.887 1.00 33.40  ? 299  GLU A C   1 
ATOM   2364  O  O   . GLU A 1 728  ? 129.181 105.356 121.662 1.00 40.39  ? 299  GLU A O   1 
ATOM   2365  C  CB  . GLU A 1 728  ? 126.053 106.071 120.889 1.00 51.95  ? 299  GLU A CB  1 
ATOM   2366  C  CG  . GLU A 1 728  ? 125.179 106.377 119.648 1.00 61.82  ? 299  GLU A CG  1 
ATOM   2367  C  CD  . GLU A 1 728  ? 124.202 107.572 119.850 1.00 69.26  ? 299  GLU A CD  1 
ATOM   2368  O  OE1 . GLU A 1 728  ? 123.416 107.870 118.916 1.00 57.90  ? 299  GLU A OE1 1 
ATOM   2369  O  OE2 . GLU A 1 728  ? 124.234 108.219 120.928 1.00 68.87  ? 299  GLU A OE2 1 
ATOM   2370  N  N   . PRO A 1 729  ? 127.713 104.533 123.110 1.00 20.75  ? 300  PRO A N   1 
ATOM   2371  C  CA  . PRO A 1 729  ? 128.738 104.562 124.133 1.00 19.72  ? 300  PRO A CA  1 
ATOM   2372  C  C   . PRO A 1 729  ? 129.854 103.603 123.838 1.00 29.39  ? 300  PRO A C   1 
ATOM   2373  O  O   . PRO A 1 729  ? 131.014 103.876 124.166 1.00 36.88  ? 300  PRO A O   1 
ATOM   2374  C  CB  . PRO A 1 729  ? 127.976 104.167 125.387 1.00 26.34  ? 300  PRO A CB  1 
ATOM   2375  C  CG  . PRO A 1 729  ? 126.628 104.522 125.095 1.00 27.43  ? 300  PRO A CG  1 
ATOM   2376  C  CD  . PRO A 1 729  ? 126.415 104.212 123.689 1.00 25.79  ? 300  PRO A CD  1 
ATOM   2377  N  N   . LEU A 1 730  ? 129.556 102.478 123.213 1.00 25.86  ? 301  LEU A N   1 
ATOM   2378  C  CA  . LEU A 1 730  ? 130.641 101.567 122.904 1.00 21.49  ? 301  LEU A CA  1 
ATOM   2379  C  C   . LEU A 1 730  ? 131.488 102.114 121.775 1.00 24.40  ? 301  LEU A C   1 
ATOM   2380  O  O   . LEU A 1 730  ? 132.703 101.923 121.778 1.00 43.13  ? 301  LEU A O   1 
ATOM   2381  C  CB  . LEU A 1 730  ? 130.087 100.190 122.580 1.00 24.85  ? 301  LEU A CB  1 
ATOM   2382  C  CG  . LEU A 1 730  ? 129.663 99.542  123.892 1.00 19.39  ? 301  LEU A CG  1 
ATOM   2383  C  CD1 . LEU A 1 730  ? 129.022 98.205  123.675 1.00 26.12  ? 301  LEU A CD1 1 
ATOM   2384  C  CD2 . LEU A 1 730  ? 130.875 99.413  124.718 1.00 28.98  ? 301  LEU A CD2 1 
ATOM   2385  N  N   . CYS A 1 731  ? 130.898 102.836 120.833 1.00 22.52  ? 302  CYS A N   1 
ATOM   2386  C  CA  . CYS A 1 731  ? 131.722 103.503 119.832 1.00 31.70  ? 302  CYS A CA  1 
ATOM   2387  C  C   . CYS A 1 731  ? 132.572 104.616 120.437 1.00 38.96  ? 302  CYS A C   1 
ATOM   2388  O  O   . CYS A 1 731  ? 133.724 104.798 120.036 1.00 44.66  ? 302  CYS A O   1 
ATOM   2389  C  CB  . CYS A 1 731  ? 130.860 104.050 118.696 1.00 38.24  ? 302  CYS A CB  1 
ATOM   2390  S  SG  . CYS A 1 731  ? 130.229 102.735 117.614 1.00 69.84  ? 302  CYS A SG  1 
ATOM   2391  N  N   . LEU A 1 732  ? 132.032 105.382 121.389 1.00 36.44  ? 303  LEU A N   1 
ATOM   2392  C  CA  . LEU A 1 732  ? 132.846 106.421 122.017 1.00 35.63  ? 303  LEU A CA  1 
ATOM   2393  C  C   . LEU A 1 732  ? 133.991 105.804 122.824 1.00 37.37  ? 303  LEU A C   1 
ATOM   2394  O  O   . LEU A 1 732  ? 135.131 106.293 122.777 1.00 45.98  ? 303  LEU A O   1 
ATOM   2395  C  CB  . LEU A 1 732  ? 131.976 107.325 122.887 1.00 34.86  ? 303  LEU A CB  1 
ATOM   2396  C  CG  . LEU A 1 732  ? 130.939 108.071 122.035 1.00 42.53  ? 303  LEU A CG  1 
ATOM   2397  C  CD1 . LEU A 1 732  ? 130.000 108.967 122.859 1.00 47.34  ? 303  LEU A CD1 1 
ATOM   2398  C  CD2 . LEU A 1 732  ? 131.586 108.851 120.892 1.00 51.62  ? 303  LEU A CD2 1 
ATOM   2399  N  N   . ALA A 1 733  ? 133.724 104.715 123.540 1.00 26.32  ? 304  ALA A N   1 
ATOM   2400  C  CA  . ALA A 1 733  ? 134.805 103.999 124.197 1.00 26.33  ? 304  ALA A CA  1 
ATOM   2401  C  C   . ALA A 1 733  ? 135.849 103.566 123.199 1.00 24.79  ? 304  ALA A C   1 
ATOM   2402  O  O   . ALA A 1 733  ? 137.047 103.777 123.407 1.00 40.04  ? 304  ALA A O   1 
ATOM   2403  C  CB  . ALA A 1 733  ? 134.274 102.766 124.919 1.00 40.35  ? 304  ALA A CB  1 
ATOM   2404  N  N   . LYS A 1 734  ? 135.422 102.921 122.129 1.00 21.28  ? 305  LYS A N   1 
ATOM   2405  C  CA  . LYS A 1 734  ? 136.395 102.380 121.207 1.00 24.29  ? 305  LYS A CA  1 
ATOM   2406  C  C   . LYS A 1 734  ? 137.203 103.490 120.533 1.00 38.11  ? 305  LYS A C   1 
ATOM   2407  O  O   . LYS A 1 734  ? 138.367 103.274 120.179 1.00 46.52  ? 305  LYS A O   1 
ATOM   2408  C  CB  . LYS A 1 734  ? 135.695 101.490 120.171 1.00 41.54  ? 305  LYS A CB  1 
ATOM   2409  C  CG  . LYS A 1 734  ? 135.000 100.223 120.725 1.00 34.95  ? 305  LYS A CG  1 
ATOM   2410  C  CD  . LYS A 1 734  ? 136.042 99.282  121.259 1.00 41.04  ? 305  LYS A CD  1 
ATOM   2411  C  CE  . LYS A 1 734  ? 136.939 98.788  120.134 1.00 42.60  ? 305  LYS A CE  1 
ATOM   2412  N  NZ  . LYS A 1 734  ? 137.991 97.861  120.647 1.00 43.86  ? 305  LYS A NZ  1 
ATOM   2413  N  N   . ILE A 1 735  ? 136.621 104.683 120.358 1.00 41.66  ? 306  ILE A N   1 
ATOM   2414  C  CA  . ILE A 1 735  ? 137.384 105.821 119.834 1.00 35.82  ? 306  ILE A CA  1 
ATOM   2415  C  C   . ILE A 1 735  ? 138.446 106.238 120.834 1.00 36.44  ? 306  ILE A C   1 
ATOM   2416  O  O   . ILE A 1 735  ? 139.621 106.404 120.497 1.00 42.05  ? 306  ILE A O   1 
ATOM   2417  C  CB  . ILE A 1 735  ? 136.449 107.009 119.543 1.00 40.20  ? 306  ILE A CB  1 
ATOM   2418  C  CG1 . ILE A 1 735  ? 135.499 106.715 118.375 1.00 43.89  ? 306  ILE A CG1 1 
ATOM   2419  C  CG2 . ILE A 1 735  ? 137.288 108.273 119.280 1.00 43.43  ? 306  ILE A CG2 1 
ATOM   2420  C  CD1 . ILE A 1 735  ? 134.368 107.769 118.176 1.00 49.78  ? 306  ILE A CD1 1 
ATOM   2421  N  N   . GLN A 1 736  ? 138.034 106.430 122.081 1.00 34.85  ? 307  GLN A N   1 
ATOM   2422  C  CA  . GLN A 1 736  ? 138.959 106.922 123.081 1.00 32.18  ? 307  GLN A CA  1 
ATOM   2423  C  C   . GLN A 1 736  ? 140.133 105.969 123.221 1.00 27.70  ? 307  GLN A C   1 
ATOM   2424  O  O   . GLN A 1 736  ? 141.280 106.397 123.326 1.00 39.51  ? 307  GLN A O   1 
ATOM   2425  C  CB  . GLN A 1 736  ? 138.211 107.096 124.399 1.00 38.86  ? 307  GLN A CB  1 
ATOM   2426  C  CG  . GLN A 1 736  ? 138.889 107.953 125.419 1.00 45.54  ? 307  GLN A CG  1 
ATOM   2427  C  CD  . GLN A 1 736  ? 137.972 108.266 126.582 1.00 40.69  ? 307  GLN A CD  1 
ATOM   2428  O  OE1 . GLN A 1 736  ? 136.777 107.994 126.525 1.00 39.74  ? 307  GLN A OE1 1 
ATOM   2429  N  NE2 . GLN A 1 736  ? 138.526 108.849 127.639 1.00 45.34  ? 307  GLN A NE2 1 
ATOM   2430  N  N   . LEU A 1 737  ? 139.876 104.676 123.183 1.00 30.90  ? 308  LEU A N   1 
ATOM   2431  C  CA  . LEU A 1 737  ? 141.012 103.777 123.302 1.00 26.87  ? 308  LEU A CA  1 
ATOM   2432  C  C   . LEU A 1 737  ? 141.948 103.850 122.149 1.00 28.55  ? 308  LEU A C   1 
ATOM   2433  O  O   . LEU A 1 737  ? 142.907 103.086 122.146 1.00 39.06  ? 308  LEU A O   1 
ATOM   2434  C  CB  . LEU A 1 737  ? 140.602 102.312 123.442 1.00 30.05  ? 308  LEU A CB  1 
ATOM   2435  C  CG  . LEU A 1 737  ? 140.255 101.748 124.820 1.00 45.57  ? 308  LEU A CG  1 
ATOM   2436  C  CD1 . LEU A 1 737  ? 138.981 102.331 125.385 1.00 44.12  ? 308  LEU A CD1 1 
ATOM   2437  C  CD2 . LEU A 1 737  ? 140.191 100.210 124.785 1.00 47.95  ? 308  LEU A CD2 1 
ATOM   2438  N  N   . CYS A 1 738  ? 141.720 104.692 121.161 1.00 33.85  ? 309  CYS A N   1 
ATOM   2439  C  CA  . CYS A 1 738  ? 142.622 104.730 120.016 1.00 47.03  ? 309  CYS A CA  1 
ATOM   2440  C  C   . CYS A 1 738  ? 143.777 105.697 120.221 1.00 45.74  ? 309  CYS A C   1 
ATOM   2441  O  O   . CYS A 1 738  ? 144.606 105.857 119.320 1.00 45.28  ? 309  CYS A O   1 
ATOM   2442  C  CB  . CYS A 1 738  ? 141.854 105.104 118.739 1.00 56.68  ? 309  CYS A CB  1 
ATOM   2443  S  SG  . CYS A 1 738  ? 140.644 103.814 118.186 1.00 72.17  ? 309  CYS A SG  1 
ATOM   2444  N  N   . SER A 1 739  ? 143.834 106.350 121.373 1.00 47.88  ? 310  SER A N   1 
ATOM   2445  C  CA  . SER A 1 739  ? 144.939 107.212 121.742 1.00 52.62  ? 310  SER A CA  1 
ATOM   2446  C  C   . SER A 1 739  ? 145.854 106.451 122.698 1.00 50.58  ? 310  SER A C   1 
ATOM   2447  O  O   . SER A 1 739  ? 145.642 105.269 122.984 1.00 51.49  ? 310  SER A O   1 
ATOM   2448  C  CB  . SER A 1 739  ? 144.427 108.508 122.379 1.00 58.72  ? 310  SER A CB  1 
ATOM   2449  O  OG  . SER A 1 739  ? 143.698 108.238 123.567 1.00 56.75  ? 310  SER A OG  1 
ATOM   2450  N  N   . LYS A 1 740  ? 146.886 107.129 123.196 1.00 48.92  ? 311  LYS A N   1 
ATOM   2451  C  CA  . LYS A 1 740  ? 147.788 106.493 124.135 1.00 42.47  ? 311  LYS A CA  1 
ATOM   2452  C  C   . LYS A 1 740  ? 146.980 105.976 125.301 1.00 48.19  ? 311  LYS A C   1 
ATOM   2453  O  O   . LYS A 1 740  ? 146.082 106.660 125.793 1.00 60.73  ? 311  LYS A O   1 
ATOM   2454  C  CB  . LYS A 1 740  ? 148.837 107.480 124.619 1.00 58.85  ? 311  LYS A CB  1 
ATOM   2455  C  CG  . LYS A 1 740  ? 149.817 106.880 125.615 1.00 74.80  ? 311  LYS A CG  1 
ATOM   2456  C  CD  . LYS A 1 740  ? 150.772 107.952 126.157 1.00 91.72  ? 311  LYS A CD  1 
ATOM   2457  C  CE  . LYS A 1 740  ? 151.784 107.390 127.172 1.00 101.94 ? 311  LYS A CE  1 
ATOM   2458  N  NZ  . LYS A 1 740  ? 151.152 106.760 128.373 1.00 93.84  ? 311  LYS A NZ  1 
ATOM   2459  N  N   . TYR A 1 741  ? 147.259 104.752 125.710 1.00 52.88  ? 312  TYR A N   1 
ATOM   2460  C  CA  . TYR A 1 741  ? 146.437 104.093 126.714 1.00 51.53  ? 312  TYR A CA  1 
ATOM   2461  C  C   . TYR A 1 741  ? 146.817 104.541 128.119 1.00 65.98  ? 312  TYR A C   1 
ATOM   2462  O  O   . TYR A 1 741  ? 147.936 104.286 128.582 1.00 63.55  ? 312  TYR A O   1 
ATOM   2463  C  CB  . TYR A 1 741  ? 146.581 102.593 126.594 1.00 52.38  ? 312  TYR A CB  1 
ATOM   2464  C  CG  . TYR A 1 741  ? 145.651 101.856 127.489 1.00 65.29  ? 312  TYR A CG  1 
ATOM   2465  C  CD1 . TYR A 1 741  ? 144.361 101.559 127.088 1.00 71.35  ? 312  TYR A CD1 1 
ATOM   2466  C  CD2 . TYR A 1 741  ? 146.061 101.456 128.757 1.00 75.89  ? 312  TYR A CD2 1 
ATOM   2467  C  CE1 . TYR A 1 741  ? 143.497 100.856 127.922 1.00 80.65  ? 312  TYR A CE1 1 
ATOM   2468  C  CE2 . TYR A 1 741  ? 145.212 100.760 129.604 1.00 80.73  ? 312  TYR A CE2 1 
ATOM   2469  C  CZ  . TYR A 1 741  ? 143.927 100.462 129.182 1.00 84.72  ? 312  TYR A CZ  1 
ATOM   2470  O  OH  . TYR A 1 741  ? 143.072 99.772  130.021 1.00 82.75  ? 312  TYR A OH  1 
ATOM   2471  N  N   . THR A 1 742  ? 145.858 105.181 128.800 1.00 73.67  ? 313  THR A N   1 
ATOM   2472  C  CA  . THR A 1 742  ? 145.953 105.631 130.186 1.00 66.78  ? 313  THR A CA  1 
ATOM   2473  C  C   . THR A 1 742  ? 144.874 104.917 130.996 1.00 62.21  ? 313  THR A C   1 
ATOM   2474  O  O   . THR A 1 742  ? 143.784 104.634 130.488 1.00 61.33  ? 313  THR A O   1 
ATOM   2475  C  CB  . THR A 1 742  ? 145.753 107.151 130.296 1.00 60.26  ? 313  THR A CB  1 
ATOM   2476  O  OG1 . THR A 1 742  ? 146.660 107.820 129.415 1.00 63.05  ? 313  THR A OG1 1 
ATOM   2477  C  CG2 . THR A 1 742  ? 146.038 107.617 131.698 1.00 65.85  ? 313  THR A CG2 1 
ATOM   2478  N  N   . GLU A 1 743  ? 145.170 104.642 132.266 1.00 63.08  ? 314  GLU A N   1 
ATOM   2479  C  CA  . GLU A 1 743  ? 144.329 103.720 133.017 1.00 60.00  ? 314  GLU A CA  1 
ATOM   2480  C  C   . GLU A 1 743  ? 142.866 104.105 132.902 1.00 56.17  ? 314  GLU A C   1 
ATOM   2481  O  O   . GLU A 1 743  ? 142.001 103.234 132.779 1.00 63.94  ? 314  GLU A O   1 
ATOM   2482  C  CB  . GLU A 1 743  ? 144.754 103.668 134.489 1.00 71.61  ? 314  GLU A CB  1 
ATOM   2483  C  CG  . GLU A 1 743  ? 144.484 104.956 135.283 1.00 77.37  ? 314  GLU A CG  1 
ATOM   2484  C  CD  . GLU A 1 743  ? 145.567 106.023 135.103 1.00 87.34  ? 314  GLU A CD  1 
ATOM   2485  O  OE1 . GLU A 1 743  ? 146.561 105.757 134.384 1.00 84.06  ? 314  GLU A OE1 1 
ATOM   2486  O  OE2 . GLU A 1 743  ? 145.407 107.141 135.655 1.00 80.03  ? 314  GLU A OE2 1 
ATOM   2487  N  N   . ARG A 1 744  ? 142.565 105.400 132.894 1.00 56.99  ? 315  ARG A N   1 
ATOM   2488  C  CA  . ARG A 1 744  ? 141.168 105.799 132.809 1.00 59.08  ? 315  ARG A CA  1 
ATOM   2489  C  C   . ARG A 1 744  ? 140.641 105.767 131.382 1.00 60.61  ? 315  ARG A C   1 
ATOM   2490  O  O   . ARG A 1 744  ? 139.455 106.049 131.177 1.00 57.37  ? 315  ARG A O   1 
ATOM   2491  C  CB  . ARG A 1 744  ? 140.946 107.202 133.378 1.00 54.98  ? 315  ARG A CB  1 
ATOM   2492  C  CG  . ARG A 1 744  ? 141.509 107.434 134.751 1.00 56.10  ? 315  ARG A CG  1 
ATOM   2493  C  CD  . ARG A 1 744  ? 141.272 108.862 135.193 1.00 53.34  ? 315  ARG A CD  1 
ATOM   2494  N  NE  . ARG A 1 744  ? 142.196 109.222 136.255 1.00 55.99  ? 315  ARG A NE  1 
ATOM   2495  C  CZ  . ARG A 1 744  ? 141.960 109.002 137.540 1.00 56.68  ? 315  ARG A CZ  1 
ATOM   2496  N  NH1 . ARG A 1 744  ? 140.846 108.388 137.908 1.00 59.83  ? 315  ARG A NH1 1 
ATOM   2497  N  NH2 . ARG A 1 744  ? 142.853 109.363 138.453 1.00 61.05  ? 315  ARG A NH2 1 
ATOM   2498  N  N   . LYS A 1 745  ? 141.485 105.480 130.387 1.00 54.81  ? 316  LYS A N   1 
ATOM   2499  C  CA  . LYS A 1 745  ? 140.964 105.365 129.029 1.00 51.40  ? 316  LYS A CA  1 
ATOM   2500  C  C   . LYS A 1 745  ? 140.149 104.096 128.883 1.00 48.22  ? 316  LYS A C   1 
ATOM   2501  O  O   . LYS A 1 745  ? 139.030 104.118 128.362 1.00 53.88  ? 316  LYS A O   1 
ATOM   2502  C  CB  . LYS A 1 745  ? 142.099 105.386 127.999 1.00 65.23  ? 316  LYS A CB  1 
ATOM   2503  C  CG  . LYS A 1 745  ? 142.833 106.736 127.858 1.00 66.60  ? 316  LYS A CG  1 
ATOM   2504  C  CD  . LYS A 1 745  ? 142.130 107.734 126.936 1.00 61.45  ? 316  LYS A CD  1 
ATOM   2505  C  CE  . LYS A 1 745  ? 142.921 109.052 126.814 1.00 64.10  ? 316  LYS A CE  1 
ATOM   2506  N  NZ  . LYS A 1 745  ? 144.347 108.894 126.381 1.00 68.37  ? 316  LYS A NZ  1 
ATOM   2507  N  N   . GLY A 1 746  ? 140.686 102.982 129.358 1.00 51.11  ? 317  GLY A N   1 
ATOM   2508  C  CA  . GLY A 1 746  ? 139.954 101.745 129.246 1.00 51.79  ? 317  GLY A CA  1 
ATOM   2509  C  C   . GLY A 1 746  ? 138.777 101.654 130.184 1.00 41.28  ? 317  GLY A C   1 
ATOM   2510  O  O   . GLY A 1 746  ? 137.918 100.794 130.009 1.00 45.43  ? 317  GLY A O   1 
ATOM   2511  N  N   . ARG A 1 747  ? 138.712 102.531 131.173 1.00 35.89  ? 318  ARG A N   1 
ATOM   2512  C  CA  . ARG A 1 747  ? 137.626 102.474 132.126 1.00 32.56  ? 318  ARG A CA  1 
ATOM   2513  C  C   . ARG A 1 747  ? 136.306 102.873 131.510 1.00 35.66  ? 318  ARG A C   1 
ATOM   2514  O  O   . ARG A 1 747  ? 135.265 102.384 131.964 1.00 47.14  ? 318  ARG A O   1 
ATOM   2515  C  CB  . ARG A 1 747  ? 138.037 103.300 133.322 1.00 40.40  ? 318  ARG A CB  1 
ATOM   2516  C  CG  . ARG A 1 747  ? 138.853 102.427 134.203 1.00 58.23  ? 318  ARG A CG  1 
ATOM   2517  C  CD  . ARG A 1 747  ? 139.678 103.131 135.288 1.00 71.57  ? 318  ARG A CD  1 
ATOM   2518  N  NE  . ARG A 1 747  ? 138.988 103.725 136.408 1.00 75.81  ? 318  ARG A NE  1 
ATOM   2519  C  CZ  . ARG A 1 747  ? 139.686 104.437 137.309 1.00 75.03  ? 318  ARG A CZ  1 
ATOM   2520  N  NH1 . ARG A 1 747  ? 139.123 105.050 138.355 1.00 70.53  ? 318  ARG A NH1 1 
ATOM   2521  N  NH2 . ARG A 1 747  ? 141.022 104.588 137.162 1.00 75.41  ? 318  ARG A NH2 1 
ATOM   2522  N  N   . PHE A 1 748  ? 136.326 103.654 130.435 1.00 38.18  ? 319  PHE A N   1 
ATOM   2523  C  CA  . PHE A 1 748  ? 135.098 103.919 129.707 1.00 39.88  ? 319  PHE A CA  1 
ATOM   2524  C  C   . PHE A 1 748  ? 134.560 102.592 129.154 1.00 40.93  ? 319  PHE A C   1 
ATOM   2525  O  O   . PHE A 1 748  ? 133.453 102.168 129.491 1.00 44.77  ? 319  PHE A O   1 
ATOM   2526  C  CB  . PHE A 1 748  ? 135.382 104.845 128.519 1.00 45.94  ? 319  PHE A CB  1 
ATOM   2527  C  CG  . PHE A 1 748  ? 134.165 105.517 127.910 1.00 49.19  ? 319  PHE A CG  1 
ATOM   2528  C  CD1 . PHE A 1 748  ? 133.903 106.883 128.136 1.00 60.99  ? 319  PHE A CD1 1 
ATOM   2529  C  CD2 . PHE A 1 748  ? 133.130 104.722 127.436 1.00 53.08  ? 319  PHE A CD2 1 
ATOM   2530  C  CE1 . PHE A 1 748  ? 132.788 107.486 127.561 1.00 60.00  ? 319  PHE A CE1 1 
ATOM   2531  C  CE2 . PHE A 1 748  ? 131.969 105.265 126.953 1.00 48.64  ? 319  PHE A CE2 1 
ATOM   2532  C  CZ  . PHE A 1 748  ? 131.796 106.675 127.009 1.00 54.29  ? 319  PHE A CZ  1 
ATOM   2533  N  N   . LEU A 1 749  ? 135.347 101.928 128.288 1.00 36.29  ? 320  LEU A N   1 
ATOM   2534  C  CA  . LEU A 1 749  ? 134.934 100.663 127.678 1.00 30.37  ? 320  LEU A CA  1 
ATOM   2535  C  C   . LEU A 1 749  ? 134.615 99.596  128.718 1.00 40.12  ? 320  LEU A C   1 
ATOM   2536  O  O   . LEU A 1 749  ? 133.684 98.819  128.520 1.00 43.53  ? 320  LEU A O   1 
ATOM   2537  C  CB  . LEU A 1 749  ? 136.004 100.149 126.729 1.00 25.13  ? 320  LEU A CB  1 
ATOM   2538  C  CG  . LEU A 1 749  ? 135.629 98.847  126.065 1.00 25.16  ? 320  LEU A CG  1 
ATOM   2539  C  CD1 . LEU A 1 749  ? 134.340 99.070  125.359 1.00 34.74  ? 320  LEU A CD1 1 
ATOM   2540  C  CD2 . LEU A 1 749  ? 136.725 98.507  125.098 1.00 35.51  ? 320  LEU A CD2 1 
ATOM   2541  N  N   . THR A 1 750  ? 135.376 99.508  129.811 1.00 32.60  ? 321  THR A N   1 
ATOM   2542  C  CA  . THR A 1 750  ? 135.038 98.531  130.836 1.00 21.46  ? 321  THR A CA  1 
ATOM   2543  C  C   . THR A 1 750  ? 133.708 98.838  131.473 1.00 26.92  ? 321  THR A C   1 
ATOM   2544  O  O   . THR A 1 750  ? 132.897 97.935  131.674 1.00 40.33  ? 321  THR A O   1 
ATOM   2545  C  CB  . THR A 1 750  ? 136.087 98.469  131.914 1.00 34.05  ? 321  THR A CB  1 
ATOM   2546  O  OG1 . THR A 1 750  ? 137.301 97.954  131.357 1.00 48.16  ? 321  THR A OG1 1 
ATOM   2547  C  CG2 . THR A 1 750  ? 135.602 97.582  133.041 1.00 46.36  ? 321  THR A CG2 1 
ATOM   2548  N  N   . GLN A 1 751  ? 133.442 100.099 131.798 1.00 29.52  ? 322  GLN A N   1 
ATOM   2549  C  CA  . GLN A 1 751  ? 132.135 100.406 132.369 1.00 29.57  ? 322  GLN A CA  1 
ATOM   2550  C  C   . GLN A 1 751  ? 131.021 100.145 131.376 1.00 38.03  ? 322  GLN A C   1 
ATOM   2551  O  O   . GLN A 1 751  ? 129.977 99.613  131.753 1.00 46.48  ? 322  GLN A O   1 
ATOM   2552  C  CB  . GLN A 1 751  ? 132.053 101.839 132.857 1.00 36.74  ? 322  GLN A CB  1 
ATOM   2553  C  CG  . GLN A 1 751  ? 132.840 102.041 134.107 1.00 47.00  ? 322  GLN A CG  1 
ATOM   2554  C  CD  . GLN A 1 751  ? 132.102 101.536 135.306 1.00 54.69  ? 322  GLN A CD  1 
ATOM   2555  O  OE1 . GLN A 1 751  ? 131.530 100.449 135.280 1.00 52.38  ? 322  GLN A OE1 1 
ATOM   2556  N  NE2 . GLN A 1 751  ? 132.090 102.329 136.371 1.00 67.12  ? 322  GLN A NE2 1 
ATOM   2557  N  N   . MET A 1 752  ? 131.211 100.508 130.104 1.00 36.77  ? 323  MET A N   1 
ATOM   2558  C  CA  . MET A 1 752  ? 130.170 100.230 129.112 1.00 33.67  ? 323  MET A CA  1 
ATOM   2559  C  C   . MET A 1 752  ? 130.002 98.740  128.883 1.00 35.20  ? 323  MET A C   1 
ATOM   2560  O  O   . MET A 1 752  ? 128.878 98.257  128.730 1.00 42.70  ? 323  MET A O   1 
ATOM   2561  C  CB  . MET A 1 752  ? 130.443 100.926 127.783 1.00 37.07  ? 323  MET A CB  1 
ATOM   2562  C  CG  . MET A 1 752  ? 130.388 102.426 127.872 1.00 42.92  ? 323  MET A CG  1 
ATOM   2563  S  SD  . MET A 1 752  ? 129.299 102.961 129.221 1.00 49.31  ? 323  MET A SD  1 
ATOM   2564  C  CE  . MET A 1 752  ? 127.670 102.563 128.650 1.00 36.92  ? 323  MET A CE  1 
ATOM   2565  N  N   . HIS A 1 753  ? 131.093 97.996  128.857 1.00 24.50  ? 324  HIS A N   1 
ATOM   2566  C  CA  . HIS A 1 753  ? 130.992 96.566  128.674 1.00 23.82  ? 324  HIS A CA  1 
ATOM   2567  C  C   . HIS A 1 753  ? 130.306 95.900  129.851 1.00 31.45  ? 324  HIS A C   1 
ATOM   2568  O  O   . HIS A 1 753  ? 129.450 95.027  129.668 1.00 39.57  ? 324  HIS A O   1 
ATOM   2569  C  CB  . HIS A 1 753  ? 132.370 96.003  128.486 1.00 32.70  ? 324  HIS A CB  1 
ATOM   2570  C  CG  . HIS A 1 753  ? 132.359 94.612  127.998 1.00 31.18  ? 324  HIS A CG  1 
ATOM   2571  N  ND1 . HIS A 1 753  ? 133.506 93.946  127.622 1.00 40.93  ? 324  HIS A ND1 1 
ATOM   2572  C  CD2 . HIS A 1 753  ? 131.339 93.743  127.844 1.00 36.45  ? 324  HIS A CD2 1 
ATOM   2573  C  CE1 . HIS A 1 753  ? 133.189 92.721  127.246 1.00 54.39  ? 324  HIS A CE1 1 
ATOM   2574  N  NE2 . HIS A 1 753  ? 131.880 92.572  127.371 1.00 55.00  ? 324  HIS A NE2 1 
ATOM   2575  N  N   . LEU A 1 754  ? 130.662 96.294  131.070 1.00 29.91  ? 325  LEU A N   1 
ATOM   2576  C  CA  . LEU A 1 754  ? 129.943 95.810  132.238 1.00 28.91  ? 325  LEU A CA  1 
ATOM   2577  C  C   . LEU A 1 754  ? 128.477 96.205  132.167 1.00 31.11  ? 325  LEU A C   1 
ATOM   2578  O  O   . LEU A 1 754  ? 127.594 95.403  132.482 1.00 38.38  ? 325  LEU A O   1 
ATOM   2579  C  CB  . LEU A 1 754  ? 130.572 96.375  133.506 1.00 36.81  ? 325  LEU A CB  1 
ATOM   2580  C  CG  . LEU A 1 754  ? 131.943 95.828  133.883 1.00 42.74  ? 325  LEU A CG  1 
ATOM   2581  C  CD1 . LEU A 1 754  ? 132.539 96.591  135.075 1.00 45.86  ? 325  LEU A CD1 1 
ATOM   2582  C  CD2 . LEU A 1 754  ? 131.769 94.369  134.211 1.00 52.33  ? 325  LEU A CD2 1 
ATOM   2583  N  N   . ALA A 1 755  ? 128.196 97.434  131.770 1.00 21.51  ? 326  ALA A N   1 
ATOM   2584  C  CA  . ALA A 1 755  ? 126.814 97.841  131.693 1.00 19.44  ? 326  ALA A CA  1 
ATOM   2585  C  C   . ALA A 1 755  ? 126.076 96.988  130.697 1.00 26.84  ? 326  ALA A C   1 
ATOM   2586  O  O   . ALA A 1 755  ? 124.948 96.577  130.962 1.00 38.26  ? 326  ALA A O   1 
ATOM   2587  C  CB  . ALA A 1 755  ? 126.710 99.311  131.310 1.00 32.17  ? 326  ALA A CB  1 
ATOM   2588  N  N   . VAL A 1 756  ? 126.689 96.708  129.542 1.00 25.44  ? 327  VAL A N   1 
ATOM   2589  C  CA  . VAL A 1 756  ? 126.014 95.915  128.515 1.00 19.61  ? 327  VAL A CA  1 
ATOM   2590  C  C   . VAL A 1 756  ? 125.721 94.530  129.034 1.00 28.75  ? 327  VAL A C   1 
ATOM   2591  O  O   . VAL A 1 756  ? 124.628 94.003  128.833 1.00 36.61  ? 327  VAL A O   1 
ATOM   2592  C  CB  . VAL A 1 756  ? 126.843 95.818  127.237 1.00 19.28  ? 327  VAL A CB  1 
ATOM   2593  C  CG1 . VAL A 1 756  ? 126.253 94.749  126.395 1.00 22.92  ? 327  VAL A CG1 1 
ATOM   2594  C  CG2 . VAL A 1 756  ? 126.776 97.087  126.497 1.00 33.88  ? 327  VAL A CG2 1 
ATOM   2595  N  N   . ASN A 1 757  ? 126.699 93.907  129.695 1.00 29.19  ? 328  ASN A N   1 
ATOM   2596  C  CA  . ASN A 1 757  ? 126.455 92.582  130.244 1.00 20.27  ? 328  ASN A CA  1 
ATOM   2597  C  C   . ASN A 1 757  ? 125.376 92.612  131.288 1.00 23.25  ? 328  ASN A C   1 
ATOM   2598  O  O   . ASN A 1 757  ? 124.500 91.748  131.294 1.00 39.30  ? 328  ASN A O   1 
ATOM   2599  C  CB  . ASN A 1 757  ? 127.710 91.999  130.838 1.00 25.24  ? 328  ASN A CB  1 
ATOM   2600  C  CG  . ASN A 1 757  ? 128.625 91.483  129.789 1.00 43.18  ? 328  ASN A CG  1 
ATOM   2601  O  OD1 . ASN A 1 757  ? 128.170 91.054  128.724 1.00 45.42  ? 328  ASN A OD1 1 
ATOM   2602  N  ND2 . ASN A 1 757  ? 129.930 91.538  130.050 1.00 48.33  ? 328  ASN A ND2 1 
ATOM   2603  N  N   . HIS A 1 758  ? 125.412 93.575  132.190 1.00 20.25  ? 329  HIS A N   1 
ATOM   2604  C  CA  . HIS A 1 758  ? 124.368 93.586  133.197 1.00 26.18  ? 329  HIS A CA  1 
ATOM   2605  C  C   . HIS A 1 758  ? 123.005 93.773  132.557 1.00 29.94  ? 329  HIS A C   1 
ATOM   2606  O  O   . HIS A 1 758  ? 122.042 93.097  132.929 1.00 40.89  ? 329  HIS A O   1 
ATOM   2607  C  CB  . HIS A 1 758  ? 124.634 94.655  134.247 1.00 33.85  ? 329  HIS A CB  1 
ATOM   2608  C  CG  . HIS A 1 758  ? 125.661 94.238  135.242 1.00 40.42  ? 329  HIS A CG  1 
ATOM   2609  N  ND1 . HIS A 1 758  ? 126.752 95.017  135.563 1.00 46.75  ? 329  HIS A ND1 1 
ATOM   2610  C  CD2 . HIS A 1 758  ? 125.807 93.082  135.930 1.00 45.25  ? 329  HIS A CD2 1 
ATOM   2611  C  CE1 . HIS A 1 758  ? 127.504 94.376  136.441 1.00 54.24  ? 329  HIS A CE1 1 
ATOM   2612  N  NE2 . HIS A 1 758  ? 126.954 93.197  136.679 1.00 53.02  ? 329  HIS A NE2 1 
ATOM   2613  N  N   . THR A 1 759  ? 122.904 94.655  131.572 1.00 26.23  ? 330  THR A N   1 
ATOM   2614  C  CA  . THR A 1 759  ? 121.624 94.849  130.919 1.00 23.46  ? 330  THR A CA  1 
ATOM   2615  C  C   . THR A 1 759  ? 121.201 93.581  130.209 1.00 30.14  ? 330  THR A C   1 
ATOM   2616  O  O   . THR A 1 759  ? 120.026 93.189  130.260 1.00 43.55  ? 330  THR A O   1 
ATOM   2617  C  CB  . THR A 1 759  ? 121.690 95.996  129.922 1.00 25.85  ? 330  THR A CB  1 
ATOM   2618  O  OG1 . THR A 1 759  ? 122.199 97.169  130.561 1.00 31.62  ? 330  THR A OG1 1 
ATOM   2619  C  CG2 . THR A 1 759  ? 120.291 96.315  129.425 1.00 38.41  ? 330  THR A CG2 1 
ATOM   2620  N  N   . LEU A 1 760  ? 122.145 92.912  129.559 1.00 25.67  ? 331  LEU A N   1 
ATOM   2621  C  CA  . LEU A 1 760  ? 121.787 91.736  128.789 1.00 26.93  ? 331  LEU A CA  1 
ATOM   2622  C  C   . LEU A 1 760  ? 121.328 90.617  129.709 1.00 32.98  ? 331  LEU A C   1 
ATOM   2623  O  O   . LEU A 1 760  ? 120.404 89.867  129.377 1.00 43.17  ? 331  LEU A O   1 
ATOM   2624  C  CB  . LEU A 1 760  ? 122.959 91.294  127.926 1.00 23.31  ? 331  LEU A CB  1 
ATOM   2625  C  CG  . LEU A 1 760  ? 122.532 90.258  126.906 1.00 27.56  ? 331  LEU A CG  1 
ATOM   2626  C  CD1 . LEU A 1 760  ? 121.380 90.830  126.116 1.00 33.05  ? 331  LEU A CD1 1 
ATOM   2627  C  CD2 . LEU A 1 760  ? 123.680 89.942  125.984 1.00 40.09  ? 331  LEU A CD2 1 
ATOM   2628  N  N   . GLU A 1 761  ? 121.937 90.506  130.882 1.00 30.69  ? 332  GLU A N   1 
ATOM   2629  C  CA  . GLU A 1 761  ? 121.493 89.497  131.832 1.00 34.17  ? 332  GLU A CA  1 
ATOM   2630  C  C   . GLU A 1 761  ? 120.127 89.843  132.401 1.00 35.90  ? 332  GLU A C   1 
ATOM   2631  O  O   . GLU A 1 761  ? 119.295 88.955  132.602 1.00 49.94  ? 332  GLU A O   1 
ATOM   2632  C  CB  . GLU A 1 761  ? 122.508 89.347  132.965 1.00 45.53  ? 332  GLU A CB  1 
ATOM   2633  C  CG  . GLU A 1 761  ? 123.846 88.734  132.542 1.00 56.09  ? 332  GLU A CG  1 
ATOM   2634  C  CD  . GLU A 1 761  ? 123.798 87.210  132.443 1.00 78.19  ? 332  GLU A CD  1 
ATOM   2635  O  OE1 . GLU A 1 761  ? 122.685 86.659  132.267 1.00 72.98  ? 332  GLU A OE1 1 
ATOM   2636  O  OE2 . GLU A 1 761  ? 124.871 86.561  132.538 1.00 76.94  ? 332  GLU A OE2 1 
ATOM   2637  N  N   . GLU A 1 762  ? 119.881 91.118  132.692 1.00 33.18  ? 333  GLU A N   1 
ATOM   2638  C  CA  . GLU A 1 762  ? 118.621 91.476  133.331 1.00 31.80  ? 333  GLU A CA  1 
ATOM   2639  C  C   . GLU A 1 762  ? 117.449 91.288  132.394 1.00 41.55  ? 333  GLU A C   1 
ATOM   2640  O  O   . GLU A 1 762  ? 116.380 90.846  132.825 1.00 50.25  ? 333  GLU A O   1 
ATOM   2641  C  CB  . GLU A 1 762  ? 118.642 92.914  133.810 1.00 49.15  ? 333  GLU A CB  1 
ATOM   2642  C  CG  . GLU A 1 762  ? 119.523 93.133  135.026 1.00 73.40  ? 333  GLU A CG  1 
ATOM   2643  C  CD  . GLU A 1 762  ? 119.491 94.582  135.508 1.00 89.42  ? 333  GLU A CD  1 
ATOM   2644  O  OE1 . GLU A 1 762  ? 118.773 95.401  134.884 1.00 77.44  ? 333  GLU A OE1 1 
ATOM   2645  O  OE2 . GLU A 1 762  ? 120.196 94.905  136.495 1.00 83.96  ? 333  GLU A OE2 1 
ATOM   2646  N  N   . ILE A 1 763  ? 117.605 91.635  131.112 1.00 39.47  ? 334  ILE A N   1 
ATOM   2647  C  CA  . ILE A 1 763  ? 116.463 91.468  130.211 1.00 34.20  ? 334  ILE A CA  1 
ATOM   2648  C  C   . ILE A 1 763  ? 116.295 90.051  129.686 1.00 40.34  ? 334  ILE A C   1 
ATOM   2649  O  O   . ILE A 1 763  ? 115.234 89.734  129.142 1.00 47.95  ? 334  ILE A O   1 
ATOM   2650  C  CB  . ILE A 1 763  ? 116.519 92.415  129.001 1.00 37.44  ? 334  ILE A CB  1 
ATOM   2651  C  CG1 . ILE A 1 763  ? 117.742 92.124  128.145 1.00 38.72  ? 334  ILE A CG1 1 
ATOM   2652  C  CG2 . ILE A 1 763  ? 116.495 93.871  129.447 1.00 48.74  ? 334  ILE A CG2 1 
ATOM   2653  C  CD1 . ILE A 1 763  ? 118.005 93.216  127.122 1.00 44.26  ? 334  ILE A CD1 1 
ATOM   2654  N  N   . THR A 1 764  ? 117.292 89.183  129.822 1.00 38.58  ? 335  THR A N   1 
ATOM   2655  C  CA  . THR A 1 764  ? 117.150 87.809  129.375 1.00 32.47  ? 335  THR A CA  1 
ATOM   2656  C  C   . THR A 1 764  ? 117.024 86.831  130.519 1.00 35.68  ? 335  THR A C   1 
ATOM   2657  O  O   . THR A 1 764  ? 117.011 85.621  130.282 1.00 43.39  ? 335  THR A O   1 
ATOM   2658  C  CB  . THR A 1 764  ? 118.340 87.392  128.523 1.00 29.71  ? 335  THR A CB  1 
ATOM   2659  O  OG1 . THR A 1 764  ? 119.533 87.552  129.290 1.00 34.78  ? 335  THR A OG1 1 
ATOM   2660  C  CG2 . THR A 1 764  ? 118.431 88.254  127.297 1.00 40.30  ? 335  THR A CG2 1 
ATOM   2661  N  N   . GLU A 1 765  ? 116.961 87.303  131.753 1.00 37.94  ? 336  GLU A N   1 
ATOM   2662  C  CA  . GLU A 1 765  ? 116.968 86.353  132.853 1.00 51.31  ? 336  GLU A CA  1 
ATOM   2663  C  C   . GLU A 1 765  ? 115.689 85.527  132.845 1.00 57.49  ? 336  GLU A C   1 
ATOM   2664  O  O   . GLU A 1 765  ? 115.735 84.292  132.844 1.00 58.20  ? 336  GLU A O   1 
ATOM   2665  C  CB  . GLU A 1 765  ? 117.157 87.095  134.184 1.00 66.45  ? 336  GLU A CB  1 
ATOM   2666  C  CG  . GLU A 1 765  ? 117.182 86.199  135.436 1.00 83.59  ? 336  GLU A CG  1 
ATOM   2667  C  CD  . GLU A 1 765  ? 118.374 85.221  135.464 1.00 95.84  ? 336  GLU A CD  1 
ATOM   2668  O  OE1 . GLU A 1 765  ? 119.448 85.554  134.908 1.00 86.41  ? 336  GLU A OE1 1 
ATOM   2669  O  OE2 . GLU A 1 765  ? 118.232 84.116  136.045 1.00 94.83  ? 336  GLU A OE2 1 
ATOM   2670  N  N   . MET A 1 766  ? 114.540 86.194  132.768 1.00 56.53  ? 337  MET A N   1 
ATOM   2671  C  CA  . MET A 1 766  ? 113.239 85.551  132.874 1.00 42.59  ? 337  MET A CA  1 
ATOM   2672  C  C   . MET A 1 766  ? 112.715 85.034  131.546 1.00 43.76  ? 337  MET A C   1 
ATOM   2673  O  O   . MET A 1 766  ? 111.643 84.430  131.518 1.00 51.79  ? 337  MET A O   1 
ATOM   2674  C  CB  . MET A 1 766  ? 112.245 86.540  133.459 1.00 50.11  ? 337  MET A CB  1 
ATOM   2675  C  CG  . MET A 1 766  ? 112.653 87.037  134.832 1.00 63.85  ? 337  MET A CG  1 
ATOM   2676  S  SD  . MET A 1 766  ? 112.826 85.688  136.021 1.00 119.79 ? 337  MET A SD  1 
ATOM   2677  C  CE  . MET A 1 766  ? 111.149 85.028  136.080 1.00 83.92  ? 337  MET A CE  1 
ATOM   2678  N  N   . ARG A 1 767  ? 113.434 85.262  130.451 1.00 48.28  ? 338  ARG A N   1 
ATOM   2679  C  CA  . ARG A 1 767  ? 113.017 84.844  129.117 1.00 41.17  ? 338  ARG A CA  1 
ATOM   2680  C  C   . ARG A 1 767  ? 113.749 83.559  128.795 1.00 46.19  ? 338  ARG A C   1 
ATOM   2681  O  O   . ARG A 1 767  ? 114.982 83.541  128.756 1.00 50.88  ? 338  ARG A O   1 
ATOM   2682  C  CB  . ARG A 1 767  ? 113.359 85.904  128.078 1.00 33.54  ? 338  ARG A CB  1 
ATOM   2683  C  CG  . ARG A 1 767  ? 112.866 87.241  128.504 1.00 45.88  ? 338  ARG A CG  1 
ATOM   2684  C  CD  . ARG A 1 767  ? 112.922 88.216  127.388 1.00 48.58  ? 338  ARG A CD  1 
ATOM   2685  N  NE  . ARG A 1 767  ? 112.029 87.776  126.335 1.00 47.77  ? 338  ARG A NE  1 
ATOM   2686  C  CZ  . ARG A 1 767  ? 110.736 88.056  126.313 1.00 43.98  ? 338  ARG A CZ  1 
ATOM   2687  N  NH1 . ARG A 1 767  ? 110.199 88.760  127.297 1.00 41.55  ? 338  ARG A NH1 1 
ATOM   2688  N  NH2 . ARG A 1 767  ? 109.987 87.617  125.314 1.00 49.18  ? 338  ARG A NH2 1 
ATOM   2689  N  N   . ALA A 1 768  ? 113.009 82.488  128.585 1.00 40.53  ? 339  ALA A N   1 
ATOM   2690  C  CA  . ALA A 1 768  ? 113.666 81.217  128.331 1.00 34.93  ? 339  ALA A CA  1 
ATOM   2691  C  C   . ALA A 1 768  ? 114.317 81.287  126.969 1.00 27.92  ? 339  ALA A C   1 
ATOM   2692  O  O   . ALA A 1 768  ? 113.629 81.337  125.953 1.00 45.35  ? 339  ALA A O   1 
ATOM   2693  C  CB  . ALA A 1 768  ? 112.659 80.076  128.388 1.00 48.99  ? 339  ALA A CB  1 
ATOM   2694  N  N   . LEU A 1 769  ? 115.624 81.317  126.918 1.00 25.12  ? 340  LEU A N   1 
ATOM   2695  C  CA  . LEU A 1 769  ? 116.300 81.248  125.638 1.00 31.33  ? 340  LEU A CA  1 
ATOM   2696  C  C   . LEU A 1 769  ? 116.970 79.891  125.519 1.00 31.15  ? 340  LEU A C   1 
ATOM   2697  O  O   . LEU A 1 769  ? 117.588 79.405  126.471 1.00 35.38  ? 340  LEU A O   1 
ATOM   2698  C  CB  . LEU A 1 769  ? 117.345 82.363  125.482 1.00 39.22  ? 340  LEU A CB  1 
ATOM   2699  C  CG  . LEU A 1 769  ? 116.926 83.718  124.889 1.00 43.54  ? 340  LEU A CG  1 
ATOM   2700  C  CD1 . LEU A 1 769  ? 116.032 84.508  125.863 1.00 48.76  ? 340  LEU A CD1 1 
ATOM   2701  C  CD2 . LEU A 1 769  ? 118.143 84.554  124.428 1.00 42.12  ? 340  LEU A CD2 1 
ATOM   2702  N  N   . LYS A 1 770  ? 116.869 79.283  124.355 1.00 29.74  ? 341  LYS A N   1 
ATOM   2703  C  CA  . LYS A 1 770  ? 117.649 78.087  124.146 1.00 31.63  ? 341  LYS A CA  1 
ATOM   2704  C  C   . LYS A 1 770  ? 119.133 78.441  124.236 1.00 31.46  ? 341  LYS A C   1 
ATOM   2705  O  O   . LYS A 1 770  ? 119.507 79.601  124.059 1.00 39.16  ? 341  LYS A O   1 
ATOM   2706  C  CB  . LYS A 1 770  ? 117.305 77.472  122.794 1.00 40.29  ? 341  LYS A CB  1 
ATOM   2707  C  CG  . LYS A 1 770  ? 115.843 77.054  122.691 1.00 45.52  ? 341  LYS A CG  1 
ATOM   2708  C  CD  . LYS A 1 770  ? 115.578 76.287  121.410 1.00 45.56  ? 341  LYS A CD  1 
ATOM   2709  C  CE  . LYS A 1 770  ? 115.921 77.160  120.222 1.00 56.04  ? 341  LYS A CE  1 
ATOM   2710  N  NZ  . LYS A 1 770  ? 115.709 76.450  118.939 1.00 67.37  ? 341  LYS A NZ  1 
ATOM   2711  N  N   . PRO A 1 771  ? 119.993 77.477  124.571 1.00 27.40  ? 342  PRO A N   1 
ATOM   2712  C  CA  . PRO A 1 771  ? 121.428 77.782  124.661 1.00 26.00  ? 342  PRO A CA  1 
ATOM   2713  C  C   . PRO A 1 771  ? 122.012 78.302  123.365 1.00 34.08  ? 342  PRO A C   1 
ATOM   2714  O  O   . PRO A 1 771  ? 122.866 79.196  123.387 1.00 39.43  ? 342  PRO A O   1 
ATOM   2715  C  CB  . PRO A 1 771  ? 122.046 76.438  125.036 1.00 35.73  ? 342  PRO A CB  1 
ATOM   2716  C  CG  . PRO A 1 771  ? 120.964 75.708  125.707 1.00 47.37  ? 342  PRO A CG  1 
ATOM   2717  C  CD  . PRO A 1 771  ? 119.699 76.109  125.004 1.00 39.95  ? 342  PRO A CD  1 
ATOM   2718  N  N   . SER A 1 772  ? 121.584 77.763  122.228 1.00 32.47  ? 343  SER A N   1 
ATOM   2719  C  CA  . SER A 1 772  ? 121.985 78.350  120.958 1.00 26.93  ? 343  SER A CA  1 
ATOM   2720  C  C   . SER A 1 772  ? 121.672 79.826  120.927 1.00 27.70  ? 343  SER A C   1 
ATOM   2721  O  O   . SER A 1 772  ? 122.522 80.640  120.568 1.00 42.45  ? 343  SER A O   1 
ATOM   2722  C  CB  . SER A 1 772  ? 121.267 77.665  119.804 1.00 38.70  ? 343  SER A CB  1 
ATOM   2723  O  OG  . SER A 1 772  ? 121.561 78.336  118.592 1.00 45.50  ? 343  SER A OG  1 
ATOM   2724  N  N   . GLN A 1 773  ? 120.447 80.188  121.294 1.00 30.70  ? 344  GLN A N   1 
ATOM   2725  C  CA  . GLN A 1 773  ? 120.051 81.589  121.260 1.00 33.62  ? 344  GLN A CA  1 
ATOM   2726  C  C   . GLN A 1 773  ? 120.869 82.434  122.233 1.00 39.75  ? 344  GLN A C   1 
ATOM   2727  O  O   . GLN A 1 773  ? 121.243 83.565  121.907 1.00 49.79  ? 344  GLN A O   1 
ATOM   2728  C  CB  . GLN A 1 773  ? 118.563 81.719  121.550 1.00 31.45  ? 344  GLN A CB  1 
ATOM   2729  C  CG  . GLN A 1 773  ? 117.719 81.077  120.498 1.00 37.02  ? 344  GLN A CG  1 
ATOM   2730  C  CD  . GLN A 1 773  ? 116.241 81.199  120.790 1.00 41.68  ? 344  GLN A CD  1 
ATOM   2731  O  OE1 . GLN A 1 773  ? 115.845 81.664  121.859 1.00 41.31  ? 344  GLN A OE1 1 
ATOM   2732  N  NE2 . GLN A 1 773  ? 115.412 80.834  119.818 1.00 47.27  ? 344  GLN A NE2 1 
ATOM   2733  N  N   . ALA A 1 774  ? 121.166 81.915  123.425 1.00 34.35  ? 345  ALA A N   1 
ATOM   2734  C  CA  . ALA A 1 774  ? 121.963 82.694  124.370 1.00 31.96  ? 345  ALA A CA  1 
ATOM   2735  C  C   . ALA A 1 774  ? 123.322 83.041  123.783 1.00 29.75  ? 345  ALA A C   1 
ATOM   2736  O  O   . ALA A 1 774  ? 123.792 84.173  123.912 1.00 38.10  ? 345  ALA A O   1 
ATOM   2737  C  CB  . ALA A 1 774  ? 122.139 81.928  125.682 1.00 40.55  ? 345  ALA A CB  1 
ATOM   2738  N  N   . GLN A 1 775  ? 123.960 82.089  123.122 1.00 34.11  ? 346  GLN A N   1 
ATOM   2739  C  CA  . GLN A 1 775  ? 125.261 82.366  122.534 1.00 40.07  ? 346  GLN A CA  1 
ATOM   2740  C  C   . GLN A 1 775  ? 125.157 83.335  121.369 1.00 39.68  ? 346  GLN A C   1 
ATOM   2741  O  O   . GLN A 1 775  ? 126.088 84.106  121.115 1.00 44.63  ? 346  GLN A O   1 
ATOM   2742  C  CB  . GLN A 1 775  ? 125.919 81.052  122.092 1.00 48.29  ? 346  GLN A CB  1 
ATOM   2743  C  CG  . GLN A 1 775  ? 127.314 81.220  121.518 1.00 65.03  ? 346  GLN A CG  1 
ATOM   2744  C  CD  . GLN A 1 775  ? 128.281 81.892  122.497 1.00 84.19  ? 346  GLN A CD  1 
ATOM   2745  O  OE1 . GLN A 1 775  ? 128.861 82.946  122.197 1.00 76.91  ? 346  GLN A OE1 1 
ATOM   2746  N  NE2 . GLN A 1 775  ? 128.455 81.286  123.670 1.00 79.53  ? 346  GLN A NE2 1 
ATOM   2747  N  N   . LYS A 1 776  ? 124.035 83.323  120.669 1.00 42.79  ? 347  LYS A N   1 
ATOM   2748  C  CA  . LYS A 1 776  ? 123.894 84.100  119.448 1.00 48.54  ? 347  LYS A CA  1 
ATOM   2749  C  C   . LYS A 1 776  ? 123.238 85.457  119.672 1.00 40.53  ? 347  LYS A C   1 
ATOM   2750  O  O   . LYS A 1 776  ? 123.403 86.350  118.835 1.00 49.56  ? 347  LYS A O   1 
ATOM   2751  C  CB  . LYS A 1 776  ? 123.072 83.312  118.419 1.00 56.87  ? 347  LYS A CB  1 
ATOM   2752  C  CG  . LYS A 1 776  ? 123.271 83.727  116.959 1.00 65.48  ? 347  LYS A CG  1 
ATOM   2753  C  CD  . LYS A 1 776  ? 122.397 82.876  116.004 1.00 70.11  ? 347  LYS A CD  1 
ATOM   2754  C  CE  . LYS A 1 776  ? 122.647 81.367  116.129 1.00 70.47  ? 347  LYS A CE  1 
ATOM   2755  N  NZ  . LYS A 1 776  ? 124.078 80.988  115.922 1.00 70.06  ? 347  LYS A NZ  1 
ATOM   2756  N  N   . ILE A 1 777  ? 122.489 85.638  120.759 1.00 31.94  ? 348  ILE A N   1 
ATOM   2757  C  CA  . ILE A 1 777  ? 121.934 86.950  121.024 1.00 26.04  ? 348  ILE A CA  1 
ATOM   2758  C  C   . ILE A 1 777  ? 123.038 87.897  121.400 1.00 34.08  ? 348  ILE A C   1 
ATOM   2759  O  O   . ILE A 1 777  ? 122.855 89.115  121.346 1.00 42.63  ? 348  ILE A O   1 
ATOM   2760  C  CB  . ILE A 1 777  ? 120.918 86.929  122.160 1.00 28.92  ? 348  ILE A CB  1 
ATOM   2761  C  CG1 . ILE A 1 777  ? 120.159 88.221  122.226 1.00 31.83  ? 348  ILE A CG1 1 
ATOM   2762  C  CG2 . ILE A 1 777  ? 121.625 86.928  123.473 1.00 35.91  ? 348  ILE A CG2 1 
ATOM   2763  C  CD1 . ILE A 1 777  ? 119.087 88.154  123.249 1.00 39.23  ? 348  ILE A CD1 1 
ATOM   2764  N  N   . ARG A 1 778  ? 124.198 87.375  121.774 1.00 34.63  ? 349  ARG A N   1 
ATOM   2765  C  CA  . ARG A 1 778  ? 125.294 88.227  122.201 1.00 32.29  ? 349  ARG A CA  1 
ATOM   2766  C  C   . ARG A 1 778  ? 126.191 88.672  121.067 1.00 29.18  ? 349  ARG A C   1 
ATOM   2767  O  O   . ARG A 1 778  ? 127.157 89.383  121.323 1.00 41.16  ? 349  ARG A O   1 
ATOM   2768  C  CB  . ARG A 1 778  ? 126.134 87.514  123.257 1.00 42.97  ? 349  ARG A CB  1 
ATOM   2769  C  CG  . ARG A 1 778  ? 125.288 86.858  124.352 1.00 48.94  ? 349  ARG A CG  1 
ATOM   2770  C  CD  . ARG A 1 778  ? 126.142 86.180  125.423 1.00 44.50  ? 349  ARG A CD  1 
ATOM   2771  N  NE  . ARG A 1 778  ? 126.692 87.190  126.314 1.00 47.04  ? 349  ARG A NE  1 
ATOM   2772  C  CZ  . ARG A 1 778  ? 126.078 87.586  127.418 1.00 50.85  ? 349  ARG A CZ  1 
ATOM   2773  N  NH1 . ARG A 1 778  ? 124.916 87.032  127.747 1.00 46.49  ? 349  ARG A NH1 1 
ATOM   2774  N  NH2 . ARG A 1 778  ? 126.618 88.525  128.188 1.00 52.07  ? 349  ARG A NH2 1 
ATOM   2775  N  N   . GLU A 1 779  ? 125.912 88.282  119.830 1.00 31.13  ? 350  GLU A N   1 
ATOM   2776  C  CA  . GLU A 1 779  ? 126.802 88.658  118.741 1.00 30.74  ? 350  GLU A CA  1 
ATOM   2777  C  C   . GLU A 1 779  ? 126.833 90.160  118.532 1.00 38.18  ? 350  GLU A C   1 
ATOM   2778  O  O   . GLU A 1 779  ? 127.820 90.693  118.010 1.00 43.78  ? 350  GLU A O   1 
ATOM   2779  C  CB  . GLU A 1 779  ? 126.363 87.995  117.457 1.00 34.42  ? 350  GLU A CB  1 
ATOM   2780  C  CG  . GLU A 1 779  ? 126.450 86.503  117.548 1.00 58.53  ? 350  GLU A CG  1 
ATOM   2781  C  CD  . GLU A 1 779  ? 126.284 85.847  116.196 1.00 76.61  ? 350  GLU A CD  1 
ATOM   2782  O  OE1 . GLU A 1 779  ? 125.947 86.576  115.232 1.00 73.68  ? 350  GLU A OE1 1 
ATOM   2783  O  OE2 . GLU A 1 779  ? 126.456 84.606  116.100 1.00 75.21  ? 350  GLU A OE2 1 
ATOM   2784  N  N   . PHE A 1 780  ? 125.770 90.862  118.923 1.00 34.46  ? 351  PHE A N   1 
ATOM   2785  C  CA  . PHE A 1 780  ? 125.700 92.291  118.655 1.00 29.73  ? 351  PHE A CA  1 
ATOM   2786  C  C   . PHE A 1 780  ? 126.810 93.032  119.387 1.00 33.00  ? 351  PHE A C   1 
ATOM   2787  O  O   . PHE A 1 780  ? 127.743 93.565  118.771 1.00 40.80  ? 351  PHE A O   1 
ATOM   2788  C  CB  . PHE A 1 780  ? 124.320 92.817  119.061 1.00 40.81  ? 351  PHE A CB  1 
ATOM   2789  C  CG  . PHE A 1 780  ? 124.192 94.312  118.990 1.00 38.86  ? 351  PHE A CG  1 
ATOM   2790  C  CD1 . PHE A 1 780  ? 124.137 94.950  117.764 1.00 40.84  ? 351  PHE A CD1 1 
ATOM   2791  C  CD2 . PHE A 1 780  ? 124.086 95.071  120.136 1.00 43.38  ? 351  PHE A CD2 1 
ATOM   2792  C  CE1 . PHE A 1 780  ? 124.022 96.306  117.678 1.00 41.33  ? 351  PHE A CE1 1 
ATOM   2793  C  CE2 . PHE A 1 780  ? 123.963 96.448  120.060 1.00 43.84  ? 351  PHE A CE2 1 
ATOM   2794  C  CZ  . PHE A 1 780  ? 123.934 97.065  118.827 1.00 41.48  ? 351  PHE A CZ  1 
ATOM   2795  N  N   . HIS A 1 781  ? 126.763 93.028  120.716 1.00 33.75  ? 352  HIS A N   1 
ATOM   2796  C  CA  . HIS A 1 781  ? 127.787 93.749  121.444 1.00 26.58  ? 352  HIS A CA  1 
ATOM   2797  C  C   . HIS A 1 781  ? 129.111 93.029  121.411 1.00 26.44  ? 352  HIS A C   1 
ATOM   2798  O  O   . HIS A 1 781  ? 130.147 93.659  121.622 1.00 37.61  ? 352  HIS A O   1 
ATOM   2799  C  CB  . HIS A 1 781  ? 127.357 93.984  122.876 1.00 32.16  ? 352  HIS A CB  1 
ATOM   2800  C  CG  . HIS A 1 781  ? 127.551 92.804  123.769 1.00 32.93  ? 352  HIS A CG  1 
ATOM   2801  N  ND1 . HIS A 1 781  ? 126.577 91.848  123.960 1.00 40.40  ? 352  HIS A ND1 1 
ATOM   2802  C  CD2 . HIS A 1 781  ? 128.589 92.446  124.562 1.00 40.35  ? 352  HIS A CD2 1 
ATOM   2803  C  CE1 . HIS A 1 781  ? 127.009 90.945  124.823 1.00 48.99  ? 352  HIS A CE1 1 
ATOM   2804  N  NE2 . HIS A 1 781  ? 128.228 91.285  125.205 1.00 48.32  ? 352  HIS A NE2 1 
ATOM   2805  N  N   . ARG A 1 782  ? 129.115 91.735  121.138 1.00 28.83  ? 353  ARG A N   1 
ATOM   2806  C  CA  . ARG A 1 782  ? 130.391 91.057  120.990 1.00 26.69  ? 353  ARG A CA  1 
ATOM   2807  C  C   . ARG A 1 782  ? 131.154 91.607  119.798 1.00 27.04  ? 353  ARG A C   1 
ATOM   2808  O  O   . ARG A 1 782  ? 132.352 91.902  119.900 1.00 38.69  ? 353  ARG A O   1 
ATOM   2809  C  CB  . ARG A 1 782  ? 130.170 89.568  120.852 1.00 34.03  ? 353  ARG A CB  1 
ATOM   2810  C  CG  . ARG A 1 782  ? 131.424 88.774  121.003 1.00 52.28  ? 353  ARG A CG  1 
ATOM   2811  C  CD  . ARG A 1 782  ? 131.108 87.346  121.381 1.00 49.65  ? 353  ARG A CD  1 
ATOM   2812  N  NE  . ARG A 1 782  ? 130.443 87.265  122.669 1.00 49.64  ? 353  ARG A NE  1 
ATOM   2813  C  CZ  . ARG A 1 782  ? 130.017 86.123  123.194 1.00 58.87  ? 353  ARG A CZ  1 
ATOM   2814  N  NH1 . ARG A 1 782  ? 130.186 84.989  122.524 1.00 56.37  ? 353  ARG A NH1 1 
ATOM   2815  N  NH2 . ARG A 1 782  ? 129.419 86.110  124.382 1.00 64.30  ? 353  ARG A NH2 1 
ATOM   2816  N  N   . THR A 1 783  ? 130.472 91.808  118.672 1.00 31.25  ? 354  THR A N   1 
ATOM   2817  C  CA  . THR A 1 783  ? 131.105 92.511  117.558 1.00 29.43  ? 354  THR A CA  1 
ATOM   2818  C  C   . THR A 1 783  ? 131.463 93.936  117.930 1.00 30.89  ? 354  THR A C   1 
ATOM   2819  O  O   . THR A 1 783  ? 132.516 94.431  117.531 1.00 38.58  ? 354  THR A O   1 
ATOM   2820  C  CB  . THR A 1 783  ? 130.202 92.517  116.324 1.00 33.15  ? 354  THR A CB  1 
ATOM   2821  O  OG1 . THR A 1 783  ? 129.989 91.174  115.865 1.00 37.72  ? 354  THR A OG1 1 
ATOM   2822  C  CG2 . THR A 1 783  ? 130.802 93.372  115.214 1.00 38.12  ? 354  THR A CG2 1 
ATOM   2823  N  N   . LEU A 1 784  ? 130.601 94.624  118.683 1.00 37.58  ? 355  LEU A N   1 
ATOM   2824  C  CA  . LEU A 1 784  ? 130.897 96.024  119.013 1.00 34.30  ? 355  LEU A CA  1 
ATOM   2825  C  C   . LEU A 1 784  ? 132.152 96.160  119.861 1.00 32.54  ? 355  LEU A C   1 
ATOM   2826  O  O   . LEU A 1 784  ? 132.781 97.220  119.888 1.00 37.89  ? 355  LEU A O   1 
ATOM   2827  C  CB  . LEU A 1 784  ? 129.746 96.655  119.766 1.00 26.17  ? 355  LEU A CB  1 
ATOM   2828  C  CG  . LEU A 1 784  ? 128.682 97.195  118.856 1.00 35.69  ? 355  LEU A CG  1 
ATOM   2829  C  CD1 . LEU A 1 784  ? 127.586 97.792  119.735 1.00 48.55  ? 355  LEU A CD1 1 
ATOM   2830  C  CD2 . LEU A 1 784  ? 129.310 98.224  117.935 1.00 45.52  ? 355  LEU A CD2 1 
ATOM   2831  N  N   . ILE A 1 785  ? 132.497 95.130  120.605 1.00 30.41  ? 356  ILE A N   1 
ATOM   2832  C  CA  . ILE A 1 785  ? 133.689 95.194  121.417 1.00 24.73  ? 356  ILE A CA  1 
ATOM   2833  C  C   . ILE A 1 785  ? 134.902 94.761  120.638 1.00 29.71  ? 356  ILE A C   1 
ATOM   2834  O  O   . ILE A 1 785  ? 135.948 95.408  120.684 1.00 40.32  ? 356  ILE A O   1 
ATOM   2835  C  CB  . ILE A 1 785  ? 133.499 94.325  122.659 1.00 30.12  ? 356  ILE A CB  1 
ATOM   2836  C  CG1 . ILE A 1 785  ? 132.390 94.905  123.509 1.00 40.23  ? 356  ILE A CG1 1 
ATOM   2837  C  CG2 . ILE A 1 785  ? 134.751 94.279  123.464 1.00 43.36  ? 356  ILE A CG2 1 
ATOM   2838  C  CD1 . ILE A 1 785  ? 131.879 93.946  124.506 1.00 45.09  ? 356  ILE A CD1 1 
ATOM   2839  N  N   . ARG A 1 786  ? 134.786 93.657  119.922 1.00 26.52  ? 357  ARG A N   1 
ATOM   2840  C  CA  . ARG A 1 786  ? 135.956 93.110  119.266 1.00 25.04  ? 357  ARG A CA  1 
ATOM   2841  C  C   . ARG A 1 786  ? 136.481 94.020  118.159 1.00 42.51  ? 357  ARG A C   1 
ATOM   2842  O  O   . ARG A 1 786  ? 137.700 94.104  117.948 1.00 48.42  ? 357  ARG A O   1 
ATOM   2843  C  CB  . ARG A 1 786  ? 135.584 91.771  118.693 1.00 34.22  ? 357  ARG A CB  1 
ATOM   2844  C  CG  . ARG A 1 786  ? 135.701 90.702  119.710 1.00 42.48  ? 357  ARG A CG  1 
ATOM   2845  C  CD  . ARG A 1 786  ? 134.772 89.644  119.275 1.00 41.72  ? 357  ARG A CD  1 
ATOM   2846  N  NE  . ARG A 1 786  ? 134.969 88.433  120.030 1.00 56.06  ? 357  ARG A NE  1 
ATOM   2847  C  CZ  . ARG A 1 786  ? 134.385 87.295  119.664 1.00 67.08  ? 357  ARG A CZ  1 
ATOM   2848  N  NH1 . ARG A 1 786  ? 133.638 87.267  118.539 1.00 67.18  ? 357  ARG A NH1 1 
ATOM   2849  N  NH2 . ARG A 1 786  ? 134.535 86.181  120.385 1.00 66.82  ? 357  ARG A NH2 1 
ATOM   2850  N  N   . LEU A 1 787  ? 135.590 94.712  117.451 1.00 46.31  ? 358  LEU A N   1 
ATOM   2851  C  CA  . LEU A 1 787  ? 135.947 95.230  116.142 1.00 39.65  ? 358  LEU A CA  1 
ATOM   2852  C  C   . LEU A 1 787  ? 136.951 96.342  116.309 1.00 28.73  ? 358  LEU A C   1 
ATOM   2853  O  O   . LEU A 1 787  ? 136.815 97.208  117.172 1.00 33.80  ? 358  LEU A O   1 
ATOM   2854  C  CB  . LEU A 1 787  ? 134.720 95.717  115.370 1.00 44.61  ? 358  LEU A CB  1 
ATOM   2855  C  CG  . LEU A 1 787  ? 134.033 97.061  115.600 1.00 47.45  ? 358  LEU A CG  1 
ATOM   2856  C  CD1 . LEU A 1 787  ? 132.924 97.269  114.548 1.00 56.93  ? 358  LEU A CD1 1 
ATOM   2857  C  CD2 . LEU A 1 787  ? 133.520 97.217  116.988 1.00 43.95  ? 358  LEU A CD2 1 
ATOM   2858  N  N   . GLU A 1 788  ? 137.993 96.261  115.523 1.00 32.92  ? 359  GLU A N   1 
ATOM   2859  C  CA  . GLU A 1 788  ? 139.083 97.203  115.565 1.00 41.63  ? 359  GLU A CA  1 
ATOM   2860  C  C   . GLU A 1 788  ? 139.003 98.065  114.319 1.00 37.65  ? 359  GLU A C   1 
ATOM   2861  O  O   . GLU A 1 788  ? 138.990 97.550  113.198 1.00 43.17  ? 359  GLU A O   1 
ATOM   2862  C  CB  . GLU A 1 788  ? 140.400 96.436  115.708 1.00 63.57  ? 359  GLU A CB  1 
ATOM   2863  C  CG  . GLU A 1 788  ? 140.681 95.348  114.643 1.00 74.75  ? 359  GLU A CG  1 
ATOM   2864  C  CD  . GLU A 1 788  ? 141.390 95.849  113.384 1.00 90.68  ? 359  GLU A CD  1 
ATOM   2865  O  OE1 . GLU A 1 788  ? 142.004 96.944  113.426 1.00 87.88  ? 359  GLU A OE1 1 
ATOM   2866  O  OE2 . GLU A 1 788  ? 141.367 95.122  112.360 1.00 77.82  ? 359  GLU A OE2 1 
ATOM   2867  N  N   . MET A 1 789  ? 138.878 99.363  114.515 1.00 27.83  ? 360  MET A N   1 
ATOM   2868  C  CA  . MET A 1 789  ? 138.664 100.242 113.393 1.00 29.49  ? 360  MET A CA  1 
ATOM   2869  C  C   . MET A 1 789  ? 139.380 101.527 113.729 1.00 34.89  ? 360  MET A C   1 
ATOM   2870  O  O   . MET A 1 789  ? 139.684 101.782 114.896 1.00 40.66  ? 360  MET A O   1 
ATOM   2871  C  CB  . MET A 1 789  ? 137.171 100.495 113.148 1.00 33.47  ? 360  MET A CB  1 
ATOM   2872  C  CG  . MET A 1 789  ? 136.376 99.229  112.795 1.00 46.46  ? 360  MET A CG  1 
ATOM   2873  S  SD  . MET A 1 789  ? 134.665 99.459  112.239 1.00 52.79  ? 360  MET A SD  1 
ATOM   2874  C  CE  . MET A 1 789  ? 133.971 100.423 113.574 1.00 40.93  ? 360  MET A CE  1 
ATOM   2875  N  N   . THR A 1 790  ? 139.654 102.339 112.709 1.00 26.79  ? 361  THR A N   1 
ATOM   2876  C  CA  . THR A 1 790  ? 140.251 103.640 112.956 1.00 22.40  ? 361  THR A CA  1 
ATOM   2877  C  C   . THR A 1 790  ? 139.258 104.514 113.719 1.00 26.02  ? 361  THR A C   1 
ATOM   2878  O  O   . THR A 1 790  ? 138.061 104.228 113.730 1.00 34.88  ? 361  THR A O   1 
ATOM   2879  C  CB  . THR A 1 790  ? 140.629 104.270 111.637 1.00 30.66  ? 361  THR A CB  1 
ATOM   2880  O  OG1 . THR A 1 790  ? 139.436 104.475 110.879 1.00 36.36  ? 361  THR A OG1 1 
ATOM   2881  C  CG2 . THR A 1 790  ? 141.529 103.323 110.862 1.00 38.44  ? 361  THR A CG2 1 
ATOM   2882  N  N   . PRO A 1 791  ? 139.721 105.550 114.412 1.00 19.62  ? 362  PRO A N   1 
ATOM   2883  C  CA  . PRO A 1 791  ? 138.760 106.363 115.146 1.00 17.20  ? 362  PRO A CA  1 
ATOM   2884  C  C   . PRO A 1 791  ? 137.688 106.892 114.234 1.00 35.21  ? 362  PRO A C   1 
ATOM   2885  O  O   . PRO A 1 791  ? 136.511 106.815 114.605 1.00 40.64  ? 362  PRO A O   1 
ATOM   2886  C  CB  . PRO A 1 791  ? 139.610 107.498 115.707 1.00 27.85  ? 362  PRO A CB  1 
ATOM   2887  C  CG  . PRO A 1 791  ? 140.954 106.964 115.772 1.00 31.67  ? 362  PRO A CG  1 
ATOM   2888  C  CD  . PRO A 1 791  ? 141.090 106.029 114.610 1.00 32.19  ? 362  PRO A CD  1 
ATOM   2889  N  N   . GLN A 1 792  ? 138.053 107.365 113.019 1.00 31.03  ? 363  GLN A N   1 
ATOM   2890  C  CA  . GLN A 1 792  ? 137.064 107.903 112.079 1.00 21.70  ? 363  GLN A CA  1 
ATOM   2891  C  C   . GLN A 1 792  ? 135.976 106.888 111.753 1.00 28.96  ? 363  GLN A C   1 
ATOM   2892  O  O   . GLN A 1 792  ? 134.784 107.229 111.740 1.00 37.02  ? 363  GLN A O   1 
ATOM   2893  C  CB  . GLN A 1 792  ? 137.720 108.355 110.789 1.00 23.05  ? 363  GLN A CB  1 
ATOM   2894  C  CG  . GLN A 1 792  ? 138.653 109.474 110.943 1.00 25.71  ? 363  GLN A CG  1 
ATOM   2895  C  CD  . GLN A 1 792  ? 139.932 109.039 111.487 1.00 29.84  ? 363  GLN A CD  1 
ATOM   2896  O  OE1 . GLN A 1 792  ? 140.227 107.850 111.503 1.00 33.61  ? 363  GLN A OE1 1 
ATOM   2897  N  NE2 . GLN A 1 792  ? 140.725 109.990 111.965 1.00 39.20  ? 363  GLN A NE2 1 
ATOM   2898  N  N   . GLN A 1 793  ? 136.363 105.639 111.477 1.00 27.41  ? 364  GLN A N   1 
ATOM   2899  C  CA  . GLN A 1 793  ? 135.374 104.600 111.218 1.00 25.01  ? 364  GLN A CA  1 
ATOM   2900  C  C   . GLN A 1 793  ? 134.443 104.437 112.397 1.00 24.34  ? 364  GLN A C   1 
ATOM   2901  O  O   . GLN A 1 793  ? 133.229 104.306 112.226 1.00 29.78  ? 364  GLN A O   1 
ATOM   2902  C  CB  . GLN A 1 793  ? 136.075 103.288 110.919 1.00 23.57  ? 364  GLN A CB  1 
ATOM   2903  C  CG  . GLN A 1 793  ? 136.850 103.365 109.654 1.00 29.04  ? 364  GLN A CG  1 
ATOM   2904  C  CD  . GLN A 1 793  ? 137.474 102.053 109.286 1.00 40.37  ? 364  GLN A CD  1 
ATOM   2905  O  OE1 . GLN A 1 793  ? 137.093 101.001 109.803 1.00 48.32  ? 364  GLN A OE1 1 
ATOM   2906  N  NE2 . GLN A 1 793  ? 138.479 102.104 108.424 1.00 42.38  ? 364  GLN A NE2 1 
ATOM   2907  N  N   . LEU A 1 794  ? 134.988 104.434 113.599 1.00 24.32  ? 365  LEU A N   1 
ATOM   2908  C  CA  . LEU A 1 794  ? 134.119 104.294 114.745 1.00 28.77  ? 365  LEU A CA  1 
ATOM   2909  C  C   . LEU A 1 794  ? 133.181 105.488 114.878 1.00 32.94  ? 365  LEU A C   1 
ATOM   2910  O  O   . LEU A 1 794  ? 132.039 105.326 115.313 1.00 38.76  ? 365  LEU A O   1 
ATOM   2911  C  CB  . LEU A 1 794  ? 134.959 104.089 116.006 1.00 34.30  ? 365  LEU A CB  1 
ATOM   2912  C  CG  . LEU A 1 794  ? 135.586 102.703 116.111 1.00 36.16  ? 365  LEU A CG  1 
ATOM   2913  C  CD1 . LEU A 1 794  ? 136.847 102.723 116.953 1.00 40.87  ? 365  LEU A CD1 1 
ATOM   2914  C  CD2 . LEU A 1 794  ? 134.567 101.755 116.725 1.00 39.61  ? 365  LEU A CD2 1 
ATOM   2915  N  N   . CYS A 1 795  ? 133.616 106.689 114.499 1.00 35.14  ? 366  CYS A N   1 
ATOM   2916  C  CA  . CYS A 1 795  ? 132.751 107.853 114.695 1.00 32.76  ? 366  CYS A CA  1 
ATOM   2917  C  C   . CYS A 1 795  ? 131.640 107.899 113.653 1.00 35.77  ? 366  CYS A C   1 
ATOM   2918  O  O   . CYS A 1 795  ? 130.589 108.516 113.884 1.00 36.10  ? 366  CYS A O   1 
ATOM   2919  C  CB  . CYS A 1 795  ? 133.573 109.140 114.663 1.00 26.89  ? 366  CYS A CB  1 
ATOM   2920  S  SG  . CYS A 1 795  ? 132.614 110.569 115.214 1.00 50.54  ? 366  CYS A SG  1 
ATOM   2921  N  N   . GLU A 1 796  ? 131.873 107.271 112.499 1.00 36.39  ? 367  GLU A N   1 
ATOM   2922  C  CA  . GLU A 1 796  ? 130.803 107.064 111.528 1.00 26.87  ? 367  GLU A CA  1 
ATOM   2923  C  C   . GLU A 1 796  ? 129.837 105.977 111.989 1.00 32.08  ? 367  GLU A C   1 
ATOM   2924  O  O   . GLU A 1 796  ? 128.616 106.160 111.940 1.00 42.00  ? 367  GLU A O   1 
ATOM   2925  C  CB  . GLU A 1 796  ? 131.412 106.704 110.194 1.00 28.12  ? 367  GLU A CB  1 
ATOM   2926  C  CG  . GLU A 1 796  ? 132.217 107.845 109.635 1.00 36.74  ? 367  GLU A CG  1 
ATOM   2927  C  CD  . GLU A 1 796  ? 131.348 108.841 108.893 1.00 51.05  ? 367  GLU A CD  1 
ATOM   2928  O  OE1 . GLU A 1 796  ? 130.099 108.734 109.004 1.00 47.31  ? 367  GLU A OE1 1 
ATOM   2929  O  OE2 . GLU A 1 796  ? 131.909 109.726 108.192 1.00 45.94  ? 367  GLU A OE2 1 
ATOM   2930  N  N   . LEU A 1 797  ? 130.359 104.845 112.456 1.00 30.91  ? 368  LEU A N   1 
ATOM   2931  C  CA  . LEU A 1 797  ? 129.492 103.816 113.024 1.00 26.92  ? 368  LEU A CA  1 
ATOM   2932  C  C   . LEU A 1 797  ? 128.664 104.365 114.165 1.00 25.02  ? 368  LEU A C   1 
ATOM   2933  O  O   . LEU A 1 797  ? 127.564 103.883 114.422 1.00 32.97  ? 368  LEU A O   1 
ATOM   2934  C  CB  . LEU A 1 797  ? 130.333 102.645 113.517 1.00 26.61  ? 368  LEU A CB  1 
ATOM   2935  C  CG  . LEU A 1 797  ? 129.620 101.364 113.891 1.00 35.80  ? 368  LEU A CG  1 
ATOM   2936  C  CD1 . LEU A 1 797  ? 129.120 100.659 112.644 1.00 48.60  ? 368  LEU A CD1 1 
ATOM   2937  C  CD2 . LEU A 1 797  ? 130.586 100.456 114.674 1.00 52.73  ? 368  LEU A CD2 1 
ATOM   2938  N  N   . PHE A 1 798  ? 129.181 105.362 114.863 1.00 28.38  ? 369  PHE A N   1 
ATOM   2939  C  CA  . PHE A 1 798  ? 128.454 105.933 115.980 1.00 27.12  ? 369  PHE A CA  1 
ATOM   2940  C  C   . PHE A 1 798  ? 127.089 106.387 115.537 1.00 29.00  ? 369  PHE A C   1 
ATOM   2941  O  O   . PHE A 1 798  ? 126.123 106.268 116.291 1.00 38.03  ? 369  PHE A O   1 
ATOM   2942  C  CB  . PHE A 1 798  ? 129.257 107.099 116.547 1.00 38.53  ? 369  PHE A CB  1 
ATOM   2943  C  CG  . PHE A 1 798  ? 128.474 108.051 117.382 1.00 36.71  ? 369  PHE A CG  1 
ATOM   2944  C  CD1 . PHE A 1 798  ? 128.395 107.887 118.750 1.00 38.66  ? 369  PHE A CD1 1 
ATOM   2945  C  CD2 . PHE A 1 798  ? 127.816 109.123 116.798 1.00 56.88  ? 369  PHE A CD2 1 
ATOM   2946  C  CE1 . PHE A 1 798  ? 127.685 108.791 119.532 1.00 47.78  ? 369  PHE A CE1 1 
ATOM   2947  C  CE2 . PHE A 1 798  ? 127.085 110.026 117.567 1.00 62.69  ? 369  PHE A CE2 1 
ATOM   2948  C  CZ  . PHE A 1 798  ? 127.017 109.859 118.937 1.00 55.89  ? 369  PHE A CZ  1 
ATOM   2949  N  N   . SER A 1 799  ? 126.987 106.909 114.317 1.00 35.81  ? 370  SER A N   1 
ATOM   2950  C  CA  . SER A 1 799  ? 125.740 107.478 113.794 1.00 35.70  ? 370  SER A CA  1 
ATOM   2951  C  C   . SER A 1 799  ? 124.957 106.452 113.005 1.00 28.33  ? 370  SER A C   1 
ATOM   2952  O  O   . SER A 1 799  ? 124.528 106.716 111.887 1.00 28.10  ? 370  SER A O   1 
ATOM   2953  C  CB  . SER A 1 799  ? 126.029 108.680 112.910 1.00 38.50  ? 370  SER A CB  1 
ATOM   2954  O  OG  . SER A 1 799  ? 126.818 108.297 111.793 1.00 32.22  ? 370  SER A OG  1 
ATOM   2955  N  N   . ILE A 1 800  ? 124.766 105.267 113.568 1.00 29.93  ? 371  ILE A N   1 
ATOM   2956  C  CA  . ILE A 1 800  ? 123.821 104.324 112.996 1.00 24.03  ? 371  ILE A CA  1 
ATOM   2957  C  C   . ILE A 1 800  ? 122.961 103.844 114.138 1.00 19.85  ? 371  ILE A C   1 
ATOM   2958  O  O   . ILE A 1 800  ? 122.359 102.771 114.071 1.00 28.11  ? 371  ILE A O   1 
ATOM   2959  C  CB  . ILE A 1 800  ? 124.495 103.140 112.286 1.00 24.43  ? 371  ILE A CB  1 
ATOM   2960  C  CG1 . ILE A 1 800  ? 125.069 102.143 113.290 1.00 29.52  ? 371  ILE A CG1 1 
ATOM   2961  C  CG2 . ILE A 1 800  ? 125.585 103.630 111.340 1.00 34.73  ? 371  ILE A CG2 1 
ATOM   2962  C  CD1 . ILE A 1 800  ? 125.345 100.785 112.668 1.00 35.87  ? 371  ILE A CD1 1 
ATOM   2963  N  N   . GLN A 1 801  ? 122.894 104.608 115.204 1.00 17.85  ? 372  GLN A N   1 
ATOM   2964  C  CA  . GLN A 1 801  ? 122.223 103.997 116.320 1.00 24.48  ? 372  GLN A CA  1 
ATOM   2965  C  C   . GLN A 1 801  ? 120.744 103.830 116.057 1.00 31.35  ? 372  GLN A C   1 
ATOM   2966  O  O   . GLN A 1 801  ? 120.139 102.874 116.554 1.00 41.74  ? 372  GLN A O   1 
ATOM   2967  C  CB  . GLN A 1 801  ? 122.460 104.751 117.608 1.00 30.66  ? 372  GLN A CB  1 
ATOM   2968  C  CG  . GLN A 1 801  ? 121.890 103.930 118.725 1.00 32.18  ? 372  GLN A CG  1 
ATOM   2969  C  CD  . GLN A 1 801  ? 122.515 104.211 120.054 1.00 49.30  ? 372  GLN A CD  1 
ATOM   2970  O  OE1 . GLN A 1 801  ? 123.572 103.652 120.364 1.00 48.69  ? 372  GLN A OE1 1 
ATOM   2971  N  NE2 . GLN A 1 801  ? 121.898 105.089 120.850 1.00 52.86  ? 372  GLN A NE2 1 
ATOM   2972  N  N   . LYS A 1 802  ? 120.144 104.668 115.232 1.00 25.81  ? 373  LYS A N   1 
ATOM   2973  C  CA  . LYS A 1 802  ? 118.703 104.519 115.074 1.00 28.63  ? 373  LYS A CA  1 
ATOM   2974  C  C   . LYS A 1 802  ? 118.333 103.623 113.899 1.00 30.91  ? 373  LYS A C   1 
ATOM   2975  O  O   . LYS A 1 802  ? 117.174 103.627 113.475 1.00 39.44  ? 373  LYS A O   1 
ATOM   2976  C  CB  . LYS A 1 802  ? 118.033 105.876 114.901 1.00 37.07  ? 373  LYS A CB  1 
ATOM   2977  C  CG  . LYS A 1 802  ? 118.145 106.724 116.129 1.00 43.78  ? 373  LYS A CG  1 
ATOM   2978  C  CD  . LYS A 1 802  ? 117.477 108.045 115.910 1.00 52.71  ? 373  LYS A CD  1 
ATOM   2979  C  CE  . LYS A 1 802  ? 117.676 108.920 117.129 1.00 76.15  ? 373  LYS A CE  1 
ATOM   2980  N  NZ  . LYS A 1 802  ? 117.076 108.365 118.370 1.00 64.98  ? 373  LYS A NZ  1 
ATOM   2981  N  N   . HIS A 1 803  ? 119.275 102.895 113.333 1.00 19.04  ? 374  HIS A N   1 
ATOM   2982  C  CA  . HIS A 1 803  ? 118.891 102.122 112.184 1.00 7.76   ? 374  HIS A CA  1 
ATOM   2983  C  C   . HIS A 1 803  ? 118.165 100.853 112.556 1.00 23.68  ? 374  HIS A C   1 
ATOM   2984  O  O   . HIS A 1 803  ? 117.725 100.144 111.649 1.00 36.18  ? 374  HIS A O   1 
ATOM   2985  C  CB  . HIS A 1 803  ? 120.104 101.815 111.360 1.00 8.53   ? 374  HIS A CB  1 
ATOM   2986  C  CG  . HIS A 1 803  ? 120.662 103.023 110.734 1.00 14.64  ? 374  HIS A CG  1 
ATOM   2987  N  ND1 . HIS A 1 803  ? 121.761 103.009 109.911 1.00 21.94  ? 374  HIS A ND1 1 
ATOM   2988  C  CD2 . HIS A 1 803  ? 120.246 104.307 110.789 1.00 23.43  ? 374  HIS A CD2 1 
ATOM   2989  C  CE1 . HIS A 1 803  ? 122.020 104.242 109.507 1.00 25.72  ? 374  HIS A CE1 1 
ATOM   2990  N  NE2 . HIS A 1 803  ? 121.111 105.047 110.022 1.00 27.83  ? 374  HIS A NE2 1 
ATOM   2991  N  N   . TRP A 1 804  ? 118.021 100.522 113.841 1.00 25.70  ? 375  TRP A N   1 
ATOM   2992  C  CA  . TRP A 1 804  ? 117.261 99.336  114.208 1.00 21.73  ? 375  TRP A CA  1 
ATOM   2993  C  C   . TRP A 1 804  ? 115.842 99.670  114.591 1.00 22.59  ? 375  TRP A C   1 
ATOM   2994  O  O   . TRP A 1 804  ? 115.040 98.757  114.801 1.00 35.16  ? 375  TRP A O   1 
ATOM   2995  C  CB  . TRP A 1 804  ? 117.946 98.573  115.340 1.00 19.96  ? 375  TRP A CB  1 
ATOM   2996  C  CG  . TRP A 1 804  ? 119.130 97.898  114.850 1.00 18.88  ? 375  TRP A CG  1 
ATOM   2997  C  CD1 . TRP A 1 804  ? 119.192 96.670  114.301 1.00 27.52  ? 375  TRP A CD1 1 
ATOM   2998  C  CD2 . TRP A 1 804  ? 120.443 98.418  114.814 1.00 15.63  ? 375  TRP A CD2 1 
ATOM   2999  N  NE1 . TRP A 1 804  ? 120.478 96.376  113.932 1.00 25.78  ? 375  TRP A NE1 1 
ATOM   3000  C  CE2 . TRP A 1 804  ? 121.261 97.447  114.242 1.00 21.77  ? 375  TRP A CE2 1 
ATOM   3001  C  CE3 . TRP A 1 804  ? 121.005 99.609  115.211 1.00 19.20  ? 375  TRP A CE3 1 
ATOM   3002  C  CZ2 . TRP A 1 804  ? 122.607 97.633  114.064 1.00 35.48  ? 375  TRP A CZ2 1 
ATOM   3003  C  CZ3 . TRP A 1 804  ? 122.341 99.792  115.040 1.00 26.45  ? 375  TRP A CZ3 1 
ATOM   3004  C  CH2 . TRP A 1 804  ? 123.131 98.818  114.471 1.00 31.90  ? 375  TRP A CH2 1 
ATOM   3005  N  N   . GLY A 1 805  ? 115.494 100.916 114.634 1.00 14.94  ? 376  GLY A N   1 
ATOM   3006  C  CA  . GLY A 1 805  ? 114.122 101.137 114.973 1.00 18.61  ? 376  GLY A CA  1 
ATOM   3007  C  C   . GLY A 1 805  ? 113.991 102.139 116.092 1.00 31.69  ? 376  GLY A C   1 
ATOM   3008  O  O   . GLY A 1 805  ? 114.887 102.952 116.334 1.00 38.85  ? 376  GLY A O   1 
ATOM   3009  N  N   . HIS A 1 806  ? 112.834 102.110 116.754 1.00 34.32  ? 377  HIS A N   1 
ATOM   3010  C  CA  . HIS A 1 806  ? 112.557 102.868 117.956 1.00 27.45  ? 377  HIS A CA  1 
ATOM   3011  C  C   . HIS A 1 806  ? 111.542 102.072 118.751 1.00 25.68  ? 377  HIS A C   1 
ATOM   3012  O  O   . HIS A 1 806  ? 110.580 101.557 118.174 1.00 36.96  ? 377  HIS A O   1 
ATOM   3013  C  CB  . HIS A 1 806  ? 112.006 104.239 117.645 1.00 29.70  ? 377  HIS A CB  1 
ATOM   3014  C  CG  . HIS A 1 806  ? 112.825 104.969 116.648 1.00 37.40  ? 377  HIS A CG  1 
ATOM   3015  N  ND1 . HIS A 1 806  ? 114.127 105.341 116.894 1.00 46.83  ? 377  HIS A ND1 1 
ATOM   3016  C  CD2 . HIS A 1 806  ? 112.530 105.424 115.411 1.00 44.70  ? 377  HIS A CD2 1 
ATOM   3017  C  CE1 . HIS A 1 806  ? 114.613 105.968 115.838 1.00 47.91  ? 377  HIS A CE1 1 
ATOM   3018  N  NE2 . HIS A 1 806  ? 113.660 106.040 114.926 1.00 48.96  ? 377  HIS A NE2 1 
ATOM   3019  N  N   . PRO A 1 807  ? 111.709 101.971 120.039 1.00 12.51  ? 378  PRO A N   1 
ATOM   3020  C  CA  . PRO A 1 807  ? 110.911 101.043 120.797 1.00 15.38  ? 378  PRO A CA  1 
ATOM   3021  C  C   . PRO A 1 807  ? 109.494 101.526 120.823 1.00 27.83  ? 378  PRO A C   1 
ATOM   3022  O  O   . PRO A 1 807  ? 109.240 102.728 120.749 1.00 34.24  ? 378  PRO A O   1 
ATOM   3023  C  CB  . PRO A 1 807  ? 111.505 101.137 122.182 1.00 25.89  ? 378  PRO A CB  1 
ATOM   3024  C  CG  . PRO A 1 807  ? 111.975 102.495 122.220 1.00 25.70  ? 378  PRO A CG  1 
ATOM   3025  C  CD  . PRO A 1 807  ? 112.476 102.834 120.900 1.00 23.23  ? 378  PRO A CD  1 
ATOM   3026  N  N   . VAL A 1 808  ? 108.566 100.584 120.976 1.00 29.31  ? 379  VAL A N   1 
ATOM   3027  C  CA  . VAL A 1 808  ? 107.161 100.929 121.147 1.00 26.21  ? 379  VAL A CA  1 
ATOM   3028  C  C   . VAL A 1 808  ? 106.920 101.559 122.514 1.00 31.84  ? 379  VAL A C   1 
ATOM   3029  O  O   . VAL A 1 808  ? 106.839 100.857 123.529 1.00 37.54  ? 379  VAL A O   1 
ATOM   3030  C  CB  . VAL A 1 808  ? 106.288 99.685  120.964 1.00 38.14  ? 379  VAL A CB  1 
ATOM   3031  C  CG1 . VAL A 1 808  ? 104.841 99.971  121.404 1.00 43.03  ? 379  VAL A CG1 1 
ATOM   3032  C  CG2 . VAL A 1 808  ? 106.334 99.283  119.509 1.00 49.59  ? 379  VAL A CG2 1 
ATOM   3033  N  N   . LEU A 1 809  ? 106.778 102.879 122.556 1.00 25.01  ? 380  LEU A N   1 
ATOM   3034  C  CA  . LEU A 1 809  ? 106.655 103.551 123.835 1.00 18.82  ? 380  LEU A CA  1 
ATOM   3035  C  C   . LEU A 1 809  ? 105.352 103.199 124.501 1.00 26.77  ? 380  LEU A C   1 
ATOM   3036  O  O   . LEU A 1 809  ? 104.309 103.106 123.856 1.00 36.91  ? 380  LEU A O   1 
ATOM   3037  C  CB  . LEU A 1 809  ? 106.712 105.043 123.666 1.00 21.84  ? 380  LEU A CB  1 
ATOM   3038  C  CG  . LEU A 1 809  ? 107.970 105.411 122.935 1.00 33.13  ? 380  LEU A CG  1 
ATOM   3039  C  CD1 . LEU A 1 809  ? 108.069 106.906 122.974 1.00 43.82  ? 380  LEU A CD1 1 
ATOM   3040  C  CD2 . LEU A 1 809  ? 109.191 104.765 123.596 1.00 44.36  ? 380  LEU A CD2 1 
ATOM   3041  N  N   . HIS A 1 810  ? 105.396 103.031 125.799 1.00 24.72  ? 381  HIS A N   1 
ATOM   3042  C  CA  . HIS A 1 810  ? 104.160 102.961 126.542 1.00 27.39  ? 381  HIS A CA  1 
ATOM   3043  C  C   . HIS A 1 810  ? 104.009 104.213 127.376 1.00 33.41  ? 381  HIS A C   1 
ATOM   3044  O  O   . HIS A 1 810  ? 104.994 104.802 127.832 1.00 38.53  ? 381  HIS A O   1 
ATOM   3045  C  CB  . HIS A 1 810  ? 104.125 101.748 127.432 1.00 30.44  ? 381  HIS A CB  1 
ATOM   3046  C  CG  . HIS A 1 810  ? 103.994 100.497 126.667 1.00 30.45  ? 381  HIS A CG  1 
ATOM   3047  N  ND1 . HIS A 1 810  ? 105.072 99.693  126.380 1.00 35.91  ? 381  HIS A ND1 1 
ATOM   3048  C  CD2 . HIS A 1 810  ? 102.920 99.925  126.084 1.00 36.91  ? 381  HIS A CD2 1 
ATOM   3049  C  CE1 . HIS A 1 810  ? 104.661 98.658  125.672 1.00 41.24  ? 381  HIS A CE1 1 
ATOM   3050  N  NE2 . HIS A 1 810  ? 103.359 98.774  125.480 1.00 44.71  ? 381  HIS A NE2 1 
ATOM   3051  N  N   . SER A 1 811  ? 102.763 104.626 127.562 1.00 35.15  ? 382  SER A N   1 
ATOM   3052  C  CA  . SER A 1 811  ? 102.526 105.717 128.487 1.00 32.50  ? 382  SER A CA  1 
ATOM   3053  C  C   . SER A 1 811  ? 102.935 105.313 129.891 1.00 29.00  ? 382  SER A C   1 
ATOM   3054  O  O   . SER A 1 811  ? 103.494 106.124 130.633 1.00 38.95  ? 382  SER A O   1 
ATOM   3055  C  CB  . SER A 1 811  ? 101.060 106.139 128.441 1.00 46.90  ? 382  SER A CB  1 
ATOM   3056  O  OG  . SER A 1 811  ? 100.832 107.219 129.338 1.00 48.13  ? 382  SER A OG  1 
ATOM   3057  N  N   . GLU A 1 812  ? 102.689 104.061 130.271 1.00 26.08  ? 383  GLU A N   1 
ATOM   3058  C  CA  . GLU A 1 812  ? 102.995 103.662 131.634 1.00 24.34  ? 383  GLU A CA  1 
ATOM   3059  C  C   . GLU A 1 812  ? 104.489 103.621 131.883 1.00 29.21  ? 383  GLU A C   1 
ATOM   3060  O  O   . GLU A 1 812  ? 104.961 104.122 132.905 1.00 39.73  ? 383  GLU A O   1 
ATOM   3061  C  CB  . GLU A 1 812  ? 102.379 102.317 131.973 1.00 39.31  ? 383  GLU A CB  1 
ATOM   3062  C  CG  . GLU A 1 812  ? 100.859 102.346 132.045 1.00 50.84  ? 383  GLU A CG  1 
ATOM   3063  C  CD  . GLU A 1 812  ? 100.191 102.280 130.668 1.00 58.27  ? 383  GLU A CD  1 
ATOM   3064  O  OE1 . GLU A 1 812  ? 100.865 101.870 129.688 1.00 51.12  ? 383  GLU A OE1 1 
ATOM   3065  O  OE2 . GLU A 1 812  ? 99.000  102.668 130.562 1.00 53.99  ? 383  GLU A OE2 1 
ATOM   3066  N  N   . THR A 1 813  ? 105.260 103.028 130.983 1.00 28.41  ? 384  THR A N   1 
ATOM   3067  C  CA  . THR A 1 813  ? 106.683 102.957 131.291 1.00 28.74  ? 384  THR A CA  1 
ATOM   3068  C  C   . THR A 1 813  ? 107.380 104.314 131.204 1.00 33.06  ? 384  THR A C   1 
ATOM   3069  O  O   . THR A 1 813  ? 108.526 104.419 131.649 1.00 41.51  ? 384  THR A O   1 
ATOM   3070  C  CB  . THR A 1 813  ? 107.403 101.972 130.365 1.00 39.03  ? 384  THR A CB  1 
ATOM   3071  O  OG1 . THR A 1 813  ? 107.387 102.456 129.014 1.00 39.47  ? 384  THR A OG1 1 
ATOM   3072  C  CG2 . THR A 1 813  ? 106.708 100.627 130.402 1.00 42.95  ? 384  THR A CG2 1 
ATOM   3073  N  N   . ALA A 1 814  ? 106.748 105.343 130.638 1.00 29.11  ? 385  ALA A N   1 
ATOM   3074  C  CA  . ALA A 1 814  ? 107.361 106.662 130.532 1.00 27.38  ? 385  ALA A CA  1 
ATOM   3075  C  C   . ALA A 1 814  ? 106.934 107.613 131.637 1.00 37.00  ? 385  ALA A C   1 
ATOM   3076  O  O   . ALA A 1 814  ? 107.422 108.746 131.676 1.00 44.45  ? 385  ALA A O   1 
ATOM   3077  C  CB  . ALA A 1 814  ? 107.041 107.307 129.181 1.00 34.51  ? 385  ALA A CB  1 
ATOM   3078  N  N   . ILE A 1 815  ? 106.017 107.204 132.511 1.00 32.36  ? 386  ILE A N   1 
ATOM   3079  C  CA  . ILE A 1 815  ? 105.619 108.016 133.653 1.00 22.29  ? 386  ILE A CA  1 
ATOM   3080  C  C   . ILE A 1 815  ? 106.290 107.485 134.895 1.00 32.95  ? 386  ILE A C   1 
ATOM   3081  O  O   . ILE A 1 815  ? 106.619 108.248 135.804 1.00 42.85  ? 386  ILE A O   1 
ATOM   3082  C  CB  . ILE A 1 815  ? 104.109 108.030 133.823 1.00 20.10  ? 386  ILE A CB  1 
ATOM   3083  C  CG1 . ILE A 1 815  ? 103.557 108.933 132.765 1.00 33.03  ? 386  ILE A CG1 1 
ATOM   3084  C  CG2 . ILE A 1 815  ? 103.755 108.556 135.158 1.00 26.65  ? 386  ILE A CG2 1 
ATOM   3085  C  CD1 . ILE A 1 815  ? 104.051 110.324 132.981 1.00 38.78  ? 386  ILE A CD1 1 
ATOM   3086  N  N   . GLN A 1 816  ? 106.513 106.178 134.943 1.00 30.18  ? 387  GLN A N   1 
ATOM   3087  C  CA  . GLN A 1 816  ? 107.294 105.639 136.041 1.00 30.59  ? 387  GLN A CA  1 
ATOM   3088  C  C   . GLN A 1 816  ? 108.676 106.268 136.077 1.00 34.98  ? 387  GLN A C   1 
ATOM   3089  O  O   . GLN A 1 816  ? 109.169 106.647 137.153 1.00 46.49  ? 387  GLN A O   1 
ATOM   3090  C  CB  . GLN A 1 816  ? 107.401 104.133 135.900 1.00 41.74  ? 387  GLN A CB  1 
ATOM   3091  C  CG  . GLN A 1 816  ? 106.049 103.509 135.723 1.00 43.64  ? 387  GLN A CG  1 
ATOM   3092  C  CD  . GLN A 1 816  ? 105.261 103.500 136.993 1.00 47.84  ? 387  GLN A CD  1 
ATOM   3093  O  OE1 . GLN A 1 816  ? 105.763 103.869 138.056 1.00 55.90  ? 387  GLN A OE1 1 
ATOM   3094  N  NE2 . GLN A 1 816  ? 104.010 103.076 136.900 1.00 47.91  ? 387  GLN A NE2 1 
ATOM   3095  N  N   . LYS A 1 817  ? 109.300 106.431 134.912 1.00 24.78  ? 388  LYS A N   1 
ATOM   3096  C  CA  . LYS A 1 817  ? 110.631 107.015 134.885 1.00 27.82  ? 388  LYS A CA  1 
ATOM   3097  C  C   . LYS A 1 817  ? 110.654 108.383 135.528 1.00 33.74  ? 388  LYS A C   1 
ATOM   3098  O  O   . LYS A 1 817  ? 111.518 108.662 136.360 1.00 44.33  ? 388  LYS A O   1 
ATOM   3099  C  CB  . LYS A 1 817  ? 111.136 107.134 133.468 1.00 38.02  ? 388  LYS A CB  1 
ATOM   3100  C  CG  . LYS A 1 817  ? 111.676 105.855 132.909 1.00 46.84  ? 388  LYS A CG  1 
ATOM   3101  C  CD  . LYS A 1 817  ? 111.997 106.081 131.453 1.00 46.75  ? 388  LYS A CD  1 
ATOM   3102  C  CE  . LYS A 1 817  ? 112.805 107.390 131.291 1.00 56.32  ? 388  LYS A CE  1 
ATOM   3103  N  NZ  . LYS A 1 817  ? 114.112 107.438 132.026 1.00 50.96  ? 388  LYS A NZ  1 
ATOM   3104  N  N   . VAL A 1 818  ? 109.734 109.268 135.142 1.00 34.60  ? 389  VAL A N   1 
ATOM   3105  C  CA  . VAL A 1 818  ? 109.773 110.607 135.725 1.00 36.29  ? 389  VAL A CA  1 
ATOM   3106  C  C   . VAL A 1 818  ? 109.312 110.583 137.173 1.00 33.36  ? 389  VAL A C   1 
ATOM   3107  O  O   . VAL A 1 818  ? 109.783 111.379 137.992 1.00 43.67  ? 389  VAL A O   1 
ATOM   3108  C  CB  . VAL A 1 818  ? 108.957 111.619 134.897 1.00 46.06  ? 389  VAL A CB  1 
ATOM   3109  C  CG1 . VAL A 1 818  ? 109.542 111.766 133.492 1.00 50.24  ? 389  VAL A CG1 1 
ATOM   3110  C  CG2 . VAL A 1 818  ? 107.504 111.195 134.820 1.00 49.95  ? 389  VAL A CG2 1 
ATOM   3111  N  N   . LYS A 1 819  ? 108.394 109.694 137.523 1.00 31.09  ? 390  LYS A N   1 
ATOM   3112  C  CA  . LYS A 1 819  ? 107.884 109.701 138.882 1.00 28.94  ? 390  LYS A CA  1 
ATOM   3113  C  C   . LYS A 1 819  ? 108.977 109.355 139.870 1.00 28.81  ? 390  LYS A C   1 
ATOM   3114  O  O   . LYS A 1 819  ? 109.111 110.006 140.909 1.00 38.75  ? 390  LYS A O   1 
ATOM   3115  C  CB  . LYS A 1 819  ? 106.721 108.735 138.997 1.00 34.19  ? 390  LYS A CB  1 
ATOM   3116  C  CG  . LYS A 1 819  ? 106.147 108.648 140.350 1.00 36.93  ? 390  LYS A CG  1 
ATOM   3117  C  CD  . LYS A 1 819  ? 104.956 107.720 140.314 1.00 40.96  ? 390  LYS A CD  1 
ATOM   3118  C  CE  . LYS A 1 819  ? 104.400 107.568 141.707 1.00 54.86  ? 390  LYS A CE  1 
ATOM   3119  N  NZ  . LYS A 1 819  ? 104.010 108.896 142.288 1.00 50.67  ? 390  LYS A NZ  1 
ATOM   3120  N  N   . LYS A 1 820  ? 109.803 108.376 139.552 1.00 31.79  ? 391  LYS A N   1 
ATOM   3121  C  CA  . LYS A 1 820  ? 110.813 107.988 140.534 1.00 40.09  ? 391  LYS A CA  1 
ATOM   3122  C  C   . LYS A 1 820  ? 111.890 109.044 140.736 1.00 30.45  ? 391  LYS A C   1 
ATOM   3123  O  O   . LYS A 1 820  ? 112.524 109.069 141.791 1.00 35.87  ? 391  LYS A O   1 
ATOM   3124  C  CB  . LYS A 1 820  ? 111.439 106.653 140.118 1.00 63.05  ? 391  LYS A CB  1 
ATOM   3125  C  CG  . LYS A 1 820  ? 112.585 106.738 139.080 1.00 65.03  ? 391  LYS A CG  1 
ATOM   3126  C  CD  . LYS A 1 820  ? 113.227 105.336 138.794 1.00 79.23  ? 391  LYS A CD  1 
ATOM   3127  C  CE  . LYS A 1 820  ? 113.694 104.557 140.048 1.00 89.65  ? 391  LYS A CE  1 
ATOM   3128  N  NZ  . LYS A 1 820  ? 114.696 105.296 140.876 1.00 72.28  ? 391  LYS A NZ  1 
ATOM   3129  N  N   . HIS A 1 821  ? 112.115 109.912 139.772 1.00 26.63  ? 392  HIS A N   1 
ATOM   3130  C  CA  . HIS A 1 821  ? 113.158 110.891 139.940 1.00 21.18  ? 392  HIS A CA  1 
ATOM   3131  C  C   . HIS A 1 821  ? 112.628 112.237 140.349 1.00 28.75  ? 392  HIS A C   1 
ATOM   3132  O  O   . HIS A 1 821  ? 113.409 113.090 140.779 1.00 33.77  ? 392  HIS A O   1 
ATOM   3133  C  CB  . HIS A 1 821  ? 113.913 111.081 138.653 1.00 24.64  ? 392  HIS A CB  1 
ATOM   3134  C  CG  . HIS A 1 821  ? 114.722 109.901 138.272 1.00 40.70  ? 392  HIS A CG  1 
ATOM   3135  N  ND1 . HIS A 1 821  ? 115.820 109.497 138.996 1.00 50.37  ? 392  HIS A ND1 1 
ATOM   3136  C  CD2 . HIS A 1 821  ? 114.640 109.069 137.209 1.00 46.86  ? 392  HIS A CD2 1 
ATOM   3137  C  CE1 . HIS A 1 821  ? 116.362 108.442 138.413 1.00 53.49  ? 392  HIS A CE1 1 
ATOM   3138  N  NE2 . HIS A 1 821  ? 115.664 108.162 137.327 1.00 50.32  ? 392  HIS A NE2 1 
ATOM   3139  N  N   . ALA A 1 822  ? 111.335 112.461 140.187 1.00 30.30  ? 393  ALA A N   1 
ATOM   3140  C  CA  . ALA A 1 822  ? 110.747 113.745 140.504 1.00 26.34  ? 393  ALA A CA  1 
ATOM   3141  C  C   . ALA A 1 822  ? 110.000 113.739 141.824 1.00 27.61  ? 393  ALA A C   1 
ATOM   3142  O  O   . ALA A 1 822  ? 109.713 114.810 142.365 1.00 35.72  ? 393  ALA A O   1 
ATOM   3143  C  CB  . ALA A 1 822  ? 109.802 114.177 139.380 1.00 30.53  ? 393  ALA A CB  1 
ATOM   3144  N  N   . THR A 1 823  ? 109.698 112.580 142.368 1.00 27.26  ? 394  THR A N   1 
ATOM   3145  C  CA  . THR A 1 823  ? 109.072 112.528 143.669 1.00 28.78  ? 394  THR A CA  1 
ATOM   3146  C  C   . THR A 1 823  ? 110.049 112.159 144.792 1.00 28.28  ? 394  THR A C   1 
ATOM   3147  O  O   . THR A 1 823  ? 109.701 112.305 145.967 1.00 35.06  ? 394  THR A O   1 
ATOM   3148  C  CB  . THR A 1 823  ? 107.902 111.544 143.596 1.00 43.78  ? 394  THR A CB  1 
ATOM   3149  O  OG1 . THR A 1 823  ? 107.065 111.917 142.489 1.00 40.35  ? 394  THR A OG1 1 
ATOM   3150  C  CG2 . THR A 1 823  ? 107.050 111.562 144.881 1.00 56.46  ? 394  THR A CG2 1 
ATOM   3151  N  N   . VAL A 1 824  ? 111.278 111.747 144.480 1.00 25.25  ? 395  VAL A N   1 
ATOM   3152  C  CA  . VAL A 1 824  ? 112.175 111.270 145.526 1.00 23.12  ? 395  VAL A CA  1 
ATOM   3153  C  C   . VAL A 1 824  ? 112.604 112.431 146.412 1.00 30.61  ? 395  VAL A C   1 
ATOM   3154  O  O   . VAL A 1 824  ? 112.813 113.551 145.943 1.00 37.77  ? 395  VAL A O   1 
ATOM   3155  C  CB  . VAL A 1 824  ? 113.398 110.565 144.917 1.00 26.71  ? 395  VAL A CB  1 
ATOM   3156  C  CG1 . VAL A 1 824  ? 114.172 111.544 144.049 1.00 29.20  ? 395  VAL A CG1 1 
ATOM   3157  C  CG2 . VAL A 1 824  ? 114.281 110.013 146.012 1.00 34.39  ? 395  VAL A CG2 1 
ATOM   3158  N  N   . LEU A 1 825  ? 112.692 112.171 147.713 1.00 34.21  ? 396  LEU A N   1 
ATOM   3159  C  CA  . LEU A 1 825  ? 113.216 113.122 148.679 1.00 29.62  ? 396  LEU A CA  1 
ATOM   3160  C  C   . LEU A 1 825  ? 114.742 113.193 148.529 1.00 30.32  ? 396  LEU A C   1 
ATOM   3161  O  O   . LEU A 1 825  ? 115.403 112.171 148.355 1.00 41.88  ? 396  LEU A O   1 
ATOM   3162  C  CB  . LEU A 1 825  ? 112.882 112.668 150.069 1.00 28.31  ? 396  LEU A CB  1 
ATOM   3163  C  CG  . LEU A 1 825  ? 113.200 113.673 151.129 1.00 39.62  ? 396  LEU A CG  1 
ATOM   3164  C  CD1 . LEU A 1 825  ? 112.357 113.490 152.462 1.00 54.29  ? 396  LEU A CD1 1 
ATOM   3165  C  CD2 . LEU A 1 825  ? 114.716 113.245 151.540 1.00 41.56  ? 396  LEU A CD2 1 
ATOM   3166  N  N   . LYS A 1 826  ? 115.315 114.395 148.679 1.00 20.28  ? 397  LYS A N   1 
ATOM   3167  C  CA  . LYS A 1 826  ? 116.752 114.604 148.512 1.00 24.21  ? 397  LYS A CA  1 
ATOM   3168  C  C   . LYS A 1 826  ? 117.348 115.291 149.735 1.00 39.77  ? 397  LYS A C   1 
ATOM   3169  O  O   . LYS A 1 826  ? 116.739 116.207 150.301 1.00 46.52  ? 397  LYS A O   1 
ATOM   3170  C  CB  . LYS A 1 826  ? 117.022 115.449 147.294 1.00 22.56  ? 397  LYS A CB  1 
ATOM   3171  C  CG  . LYS A 1 826  ? 116.651 114.761 146.074 1.00 25.34  ? 397  LYS A CG  1 
ATOM   3172  C  CD  . LYS A 1 826  ? 116.939 115.559 144.866 1.00 28.79  ? 397  LYS A CD  1 
ATOM   3173  C  CE  . LYS A 1 826  ? 116.656 114.677 143.641 1.00 39.68  ? 397  LYS A CE  1 
ATOM   3174  N  NZ  . LYS A 1 826  ? 117.497 113.422 143.582 1.00 40.59  ? 397  LYS A NZ  1 
ATOM   3175  N  N   . ALA A 1 827  ? 118.553 114.885 150.109 1.00 33.82  ? 398  ALA A N   1 
ATOM   3176  C  CA  . ALA A 1 827  ? 119.293 115.526 151.175 1.00 25.56  ? 398  ALA A CA  1 
ATOM   3177  C  C   . ALA A 1 827  ? 120.247 116.530 150.563 1.00 36.39  ? 398  ALA A C   1 
ATOM   3178  O  O   . ALA A 1 827  ? 121.046 116.172 149.694 1.00 40.30  ? 398  ALA A O   1 
ATOM   3179  C  CB  . ALA A 1 827  ? 120.081 114.504 151.984 1.00 39.78  ? 398  ALA A CB  1 
ATOM   3180  N  N   . LEU A 1 828  ? 120.164 117.781 151.021 1.00 45.88  ? 399  LEU A N   1 
ATOM   3181  C  CA  . LEU A 1 828  ? 120.980 118.894 150.535 1.00 43.24  ? 399  LEU A CA  1 
ATOM   3182  C  C   . LEU A 1 828  ? 121.827 119.480 151.664 1.00 47.32  ? 399  LEU A C   1 
ATOM   3183  O  O   . LEU A 1 828  ? 121.326 119.697 152.774 1.00 49.21  ? 399  LEU A O   1 
ATOM   3184  C  CB  . LEU A 1 828  ? 120.102 120.019 149.977 1.00 40.43  ? 399  LEU A CB  1 
ATOM   3185  C  CG  . LEU A 1 828  ? 119.029 119.689 148.944 1.00 46.13  ? 399  LEU A CG  1 
ATOM   3186  C  CD1 . LEU A 1 828  ? 118.204 120.922 148.569 1.00 51.90  ? 399  LEU A CD1 1 
ATOM   3187  C  CD2 . LEU A 1 828  ? 119.672 119.132 147.732 1.00 46.65  ? 399  LEU A CD2 1 
ATOM   3188  N  N   . ARG A 1 829  ? 123.095 119.776 151.385 1.00 35.60  ? 400  ARG A N   1 
ATOM   3189  C  CA  . ARG A 1 829  ? 123.909 120.492 152.355 1.00 27.24  ? 400  ARG A CA  1 
ATOM   3190  C  C   . ARG A 1 829  ? 123.761 121.983 152.134 1.00 36.28  ? 400  ARG A C   1 
ATOM   3191  O  O   . ARG A 1 829  ? 124.181 122.479 151.081 1.00 42.98  ? 400  ARG A O   1 
ATOM   3192  C  CB  . ARG A 1 829  ? 125.356 120.140 152.205 1.00 32.86  ? 400  ARG A CB  1 
ATOM   3193  C  CG  . ARG A 1 829  ? 125.656 118.704 152.319 1.00 49.43  ? 400  ARG A CG  1 
ATOM   3194  C  CD  . ARG A 1 829  ? 127.142 118.597 152.416 1.00 47.71  ? 400  ARG A CD  1 
ATOM   3195  N  NE  . ARG A 1 829  ? 127.598 117.354 151.862 1.00 36.91  ? 400  ARG A NE  1 
ATOM   3196  C  CZ  . ARG A 1 829  ? 127.668 116.271 152.595 1.00 40.70  ? 400  ARG A CZ  1 
ATOM   3197  N  NH1 . ARG A 1 829  ? 127.280 116.343 153.855 1.00 41.01  ? 400  ARG A NH1 1 
ATOM   3198  N  NH2 . ARG A 1 829  ? 128.102 115.135 152.073 1.00 52.57  ? 400  ARG A NH2 1 
ATOM   3199  N  N   . PRO A 1 830  ? 123.205 122.733 153.075 1.00 22.91  ? 401  PRO A N   1 
ATOM   3200  C  CA  . PRO A 1 830  ? 122.993 124.142 152.808 1.00 19.37  ? 401  PRO A CA  1 
ATOM   3201  C  C   . PRO A 1 830  ? 124.272 124.822 152.516 1.00 20.57  ? 401  PRO A C   1 
ATOM   3202  O  O   . PRO A 1 830  ? 124.309 125.718 151.676 1.00 30.28  ? 401  PRO A O   1 
ATOM   3203  C  CB  . PRO A 1 830  ? 122.398 124.669 154.099 1.00 27.16  ? 401  PRO A CB  1 
ATOM   3204  C  CG  . PRO A 1 830  ? 121.851 123.536 154.731 1.00 41.76  ? 401  PRO A CG  1 
ATOM   3205  C  CD  . PRO A 1 830  ? 122.730 122.377 154.398 1.00 34.69  ? 401  PRO A CD  1 
ATOM   3206  N  N   . ILE A 1 831  ? 125.338 124.438 153.189 1.00 20.89  ? 402  ILE A N   1 
ATOM   3207  C  CA  . ILE A 1 831  ? 126.574 125.147 152.924 1.00 21.41  ? 402  ILE A CA  1 
ATOM   3208  C  C   . ILE A 1 831  ? 126.919 125.101 151.468 1.00 28.28  ? 402  ILE A C   1 
ATOM   3209  O  O   . ILE A 1 831  ? 127.452 126.072 150.929 1.00 42.89  ? 402  ILE A O   1 
ATOM   3210  C  CB  . ILE A 1 831  ? 127.734 124.627 153.763 1.00 32.91  ? 402  ILE A CB  1 
ATOM   3211  C  CG1 . ILE A 1 831  ? 128.940 125.457 153.392 1.00 29.33  ? 402  ILE A CG1 1 
ATOM   3212  C  CG2 . ILE A 1 831  ? 128.006 123.171 153.456 1.00 47.52  ? 402  ILE A CG2 1 
ATOM   3213  C  CD1 . ILE A 1 831  ? 128.767 126.871 153.662 1.00 42.85  ? 402  ILE A CD1 1 
ATOM   3214  N  N   . VAL A 1 832  ? 126.629 123.995 150.790 1.00 28.69  ? 403  VAL A N   1 
ATOM   3215  C  CA  . VAL A 1 832  ? 126.963 123.986 149.372 1.00 29.39  ? 403  VAL A CA  1 
ATOM   3216  C  C   . VAL A 1 832  ? 125.952 124.813 148.600 1.00 33.44  ? 403  VAL A C   1 
ATOM   3217  O  O   . VAL A 1 832  ? 126.316 125.541 147.667 1.00 44.89  ? 403  VAL A O   1 
ATOM   3218  C  CB  . VAL A 1 832  ? 127.109 122.558 148.820 1.00 36.70  ? 403  VAL A CB  1 
ATOM   3219  C  CG1 . VAL A 1 832  ? 127.339 122.592 147.335 1.00 36.81  ? 403  VAL A CG1 1 
ATOM   3220  C  CG2 . VAL A 1 832  ? 128.313 121.866 149.471 1.00 41.09  ? 403  VAL A CG2 1 
ATOM   3221  N  N   . ILE A 1 833  ? 124.682 124.774 149.000 1.00 27.71  ? 404  ILE A N   1 
ATOM   3222  C  CA  . ILE A 1 833  ? 123.706 125.618 148.318 1.00 23.68  ? 404  ILE A CA  1 
ATOM   3223  C  C   . ILE A 1 833  ? 124.034 127.079 148.527 1.00 28.02  ? 404  ILE A C   1 
ATOM   3224  O  O   . ILE A 1 833  ? 123.879 127.906 147.624 1.00 34.73  ? 404  ILE A O   1 
ATOM   3225  C  CB  . ILE A 1 833  ? 122.301 125.303 148.796 1.00 20.24  ? 404  ILE A CB  1 
ATOM   3226  C  CG1 . ILE A 1 833  ? 122.000 123.860 148.457 1.00 34.71  ? 404  ILE A CG1 1 
ATOM   3227  C  CG2 . ILE A 1 833  ? 121.353 126.234 148.157 1.00 26.46  ? 404  ILE A CG2 1 
ATOM   3228  C  CD1 . ILE A 1 833  ? 120.548 123.504 148.646 1.00 47.07  ? 404  ILE A CD1 1 
ATOM   3229  N  N   . PHE A 1 834  ? 124.492 127.426 149.716 1.00 28.64  ? 405  PHE A N   1 
ATOM   3230  C  CA  . PHE A 1 834  ? 124.923 128.793 149.912 1.00 28.59  ? 405  PHE A CA  1 
ATOM   3231  C  C   . PHE A 1 834  ? 126.083 129.128 148.997 1.00 28.15  ? 405  PHE A C   1 
ATOM   3232  O  O   . PHE A 1 834  ? 126.111 130.197 148.387 1.00 35.60  ? 405  PHE A O   1 
ATOM   3233  C  CB  . PHE A 1 834  ? 125.343 129.023 151.349 1.00 30.10  ? 405  PHE A CB  1 
ATOM   3234  C  CG  . PHE A 1 834  ? 125.888 130.363 151.562 1.00 27.83  ? 405  PHE A CG  1 
ATOM   3235  C  CD1 . PHE A 1 834  ? 127.239 130.575 151.617 1.00 42.21  ? 405  PHE A CD1 1 
ATOM   3236  C  CD2 . PHE A 1 834  ? 125.049 131.419 151.718 1.00 39.07  ? 405  PHE A CD2 1 
ATOM   3237  C  CE1 . PHE A 1 834  ? 127.748 131.842 151.804 1.00 47.56  ? 405  PHE A CE1 1 
ATOM   3238  C  CE2 . PHE A 1 834  ? 125.542 132.685 151.915 1.00 51.35  ? 405  PHE A CE2 1 
ATOM   3239  C  CZ  . PHE A 1 834  ? 126.898 132.898 151.963 1.00 48.68  ? 405  PHE A CZ  1 
ATOM   3240  N  N   . GLU A 1 835  ? 127.064 128.249 148.908 1.00 23.79  ? 406  GLU A N   1 
ATOM   3241  C  CA  . GLU A 1 835  ? 128.212 128.607 148.106 1.00 25.92  ? 406  GLU A CA  1 
ATOM   3242  C  C   . GLU A 1 835  ? 127.856 128.660 146.631 1.00 34.55  ? 406  GLU A C   1 
ATOM   3243  O  O   . GLU A 1 835  ? 128.390 129.497 145.891 1.00 41.83  ? 406  GLU A O   1 
ATOM   3244  C  CB  . GLU A 1 835  ? 129.353 127.639 148.350 1.00 30.21  ? 406  GLU A CB  1 
ATOM   3245  C  CG  . GLU A 1 835  ? 129.785 127.612 149.792 1.00 41.20  ? 406  GLU A CG  1 
ATOM   3246  C  CD  . GLU A 1 835  ? 130.681 128.786 150.136 1.00 61.28  ? 406  GLU A CD  1 
ATOM   3247  O  OE1 . GLU A 1 835  ? 131.783 128.551 150.688 1.00 63.58  ? 406  GLU A OE1 1 
ATOM   3248  O  OE2 . GLU A 1 835  ? 130.300 129.946 149.836 1.00 54.54  ? 406  GLU A OE2 1 
ATOM   3249  N  N   . THR A 1 836  ? 126.958 127.795 146.178 1.00 30.43  ? 407  THR A N   1 
ATOM   3250  C  CA  . THR A 1 836  ? 126.579 127.864 144.776 1.00 25.59  ? 407  THR A CA  1 
ATOM   3251  C  C   . THR A 1 836  ? 125.856 129.166 144.481 1.00 36.80  ? 407  THR A C   1 
ATOM   3252  O  O   . THR A 1 836  ? 126.113 129.791 143.451 1.00 46.35  ? 407  THR A O   1 
ATOM   3253  C  CB  . THR A 1 836  ? 125.711 126.670 144.384 1.00 36.70  ? 407  THR A CB  1 
ATOM   3254  O  OG1 . THR A 1 836  ? 126.395 125.443 144.695 1.00 38.00  ? 407  THR A OG1 1 
ATOM   3255  C  CG2 . THR A 1 836  ? 125.428 126.709 142.897 1.00 44.64  ? 407  THR A CG2 1 
ATOM   3256  N  N   . TYR A 1 837  ? 124.970 129.612 145.383 1.00 35.01  ? 408  TYR A N   1 
ATOM   3257  C  CA  . TYR A 1 837  ? 124.251 130.872 145.172 1.00 23.89  ? 408  TYR A CA  1 
ATOM   3258  C  C   . TYR A 1 837  ? 125.190 132.061 145.157 1.00 31.42  ? 408  TYR A C   1 
ATOM   3259  O  O   . TYR A 1 837  ? 125.022 132.986 144.355 1.00 39.51  ? 408  TYR A O   1 
ATOM   3260  C  CB  . TYR A 1 837  ? 123.237 131.070 146.271 1.00 30.75  ? 408  TYR A CB  1 
ATOM   3261  C  CG  . TYR A 1 837  ? 122.448 132.344 146.175 1.00 39.58  ? 408  TYR A CG  1 
ATOM   3262  C  CD1 . TYR A 1 837  ? 121.643 132.592 145.067 1.00 49.91  ? 408  TYR A CD1 1 
ATOM   3263  C  CD2 . TYR A 1 837  ? 122.417 133.254 147.223 1.00 34.82  ? 408  TYR A CD2 1 
ATOM   3264  C  CE1 . TYR A 1 837  ? 120.860 133.742 144.983 1.00 46.97  ? 408  TYR A CE1 1 
ATOM   3265  C  CE2 . TYR A 1 837  ? 121.639 134.400 147.146 1.00 38.13  ? 408  TYR A CE2 1 
ATOM   3266  C  CZ  . TYR A 1 837  ? 120.867 134.637 146.027 1.00 44.77  ? 408  TYR A CZ  1 
ATOM   3267  O  OH  . TYR A 1 837  ? 120.101 135.776 145.947 1.00 48.93  ? 408  TYR A OH  1 
ATOM   3268  N  N   . CYS A 1 838  ? 126.157 132.083 146.068 1.00 28.26  ? 409  CYS A N   1 
ATOM   3269  C  CA  . CYS A 1 838  ? 127.097 133.183 146.066 1.00 20.59  ? 409  CYS A CA  1 
ATOM   3270  C  C   . CYS A 1 838  ? 127.916 133.176 144.812 1.00 22.98  ? 409  CYS A C   1 
ATOM   3271  O  O   . CYS A 1 838  ? 128.195 134.230 144.257 1.00 36.34  ? 409  CYS A O   1 
ATOM   3272  C  CB  . CYS A 1 838  ? 127.982 133.114 147.272 1.00 23.62  ? 409  CYS A CB  1 
ATOM   3273  S  SG  . CYS A 1 838  ? 127.030 133.628 148.644 1.00 41.95  ? 409  CYS A SG  1 
ATOM   3274  N  N   . VAL A 1 839  ? 128.297 132.009 144.325 1.00 20.66  ? 410  VAL A N   1 
ATOM   3275  C  CA  . VAL A 1 839  ? 129.017 132.049 143.069 1.00 21.82  ? 410  VAL A CA  1 
ATOM   3276  C  C   . VAL A 1 839  ? 128.103 132.446 141.928 1.00 30.13  ? 410  VAL A C   1 
ATOM   3277  O  O   . VAL A 1 839  ? 128.549 133.061 140.958 1.00 42.97  ? 410  VAL A O   1 
ATOM   3278  C  CB  . VAL A 1 839  ? 129.717 130.720 142.817 1.00 32.83  ? 410  VAL A CB  1 
ATOM   3279  C  CG1 . VAL A 1 839  ? 130.360 130.728 141.466 1.00 36.90  ? 410  VAL A CG1 1 
ATOM   3280  C  CG2 . VAL A 1 839  ? 130.802 130.567 143.858 1.00 40.15  ? 410  VAL A CG2 1 
ATOM   3281  N  N   . PHE A 1 840  ? 126.818 132.143 142.024 1.00 28.02  ? 411  PHE A N   1 
ATOM   3282  C  CA  . PHE A 1 840  ? 125.853 132.610 141.029 1.00 31.46  ? 411  PHE A CA  1 
ATOM   3283  C  C   . PHE A 1 840  ? 125.852 134.136 140.958 1.00 37.68  ? 411  PHE A C   1 
ATOM   3284  O  O   . PHE A 1 840  ? 126.051 134.734 139.885 1.00 46.46  ? 411  PHE A O   1 
ATOM   3285  C  CB  . PHE A 1 840  ? 124.482 132.055 141.418 1.00 31.80  ? 411  PHE A CB  1 
ATOM   3286  C  CG  . PHE A 1 840  ? 123.369 132.370 140.484 1.00 25.78  ? 411  PHE A CG  1 
ATOM   3287  C  CD1 . PHE A 1 840  ? 123.221 131.673 139.318 1.00 32.64  ? 411  PHE A CD1 1 
ATOM   3288  C  CD2 . PHE A 1 840  ? 122.397 133.277 140.843 1.00 35.02  ? 411  PHE A CD2 1 
ATOM   3289  C  CE1 . PHE A 1 840  ? 122.150 131.915 138.475 1.00 40.56  ? 411  PHE A CE1 1 
ATOM   3290  C  CE2 . PHE A 1 840  ? 121.318 133.532 140.014 1.00 41.71  ? 411  PHE A CE2 1 
ATOM   3291  C  CZ  . PHE A 1 840  ? 121.197 132.847 138.822 1.00 43.60  ? 411  PHE A CZ  1 
ATOM   3292  N  N   . LYS A 1 841  ? 125.695 134.783 142.111 1.00 34.26  ? 412  LYS A N   1 
ATOM   3293  C  CA  . LYS A 1 841  ? 125.773 136.237 142.148 1.00 29.89  ? 412  LYS A CA  1 
ATOM   3294  C  C   . LYS A 1 841  ? 127.125 136.705 141.682 1.00 27.68  ? 412  LYS A C   1 
ATOM   3295  O  O   . LYS A 1 841  ? 127.238 137.742 141.034 1.00 43.90  ? 412  LYS A O   1 
ATOM   3296  C  CB  . LYS A 1 841  ? 125.527 136.768 143.550 1.00 31.17  ? 412  LYS A CB  1 
ATOM   3297  C  CG  . LYS A 1 841  ? 124.176 136.401 144.090 1.00 44.99  ? 412  LYS A CG  1 
ATOM   3298  C  CD  . LYS A 1 841  ? 123.934 137.031 145.455 1.00 48.99  ? 412  LYS A CD  1 
ATOM   3299  C  CE  . LYS A 1 841  ? 123.772 138.536 145.318 1.00 53.67  ? 412  LYS A CE  1 
ATOM   3300  N  NZ  . LYS A 1 841  ? 122.382 138.910 144.893 1.00 60.74  ? 412  LYS A NZ  1 
ATOM   3301  N  N   . TYR A 1 842  ? 128.167 135.987 142.040 1.00 29.26  ? 413  TYR A N   1 
ATOM   3302  C  CA  . TYR A 1 842  ? 129.483 136.444 141.665 1.00 33.89  ? 413  TYR A CA  1 
ATOM   3303  C  C   . TYR A 1 842  ? 129.607 136.455 140.170 1.00 38.23  ? 413  TYR A C   1 
ATOM   3304  O  O   . TYR A 1 842  ? 130.197 137.376 139.600 1.00 56.54  ? 413  TYR A O   1 
ATOM   3305  C  CB  . TYR A 1 842  ? 130.563 135.561 142.271 1.00 44.19  ? 413  TYR A CB  1 
ATOM   3306  C  CG  . TYR A 1 842  ? 131.828 135.512 141.451 1.00 44.58  ? 413  TYR A CG  1 
ATOM   3307  C  CD1 . TYR A 1 842  ? 132.745 136.539 141.501 1.00 49.83  ? 413  TYR A CD1 1 
ATOM   3308  C  CD2 . TYR A 1 842  ? 132.102 134.432 140.623 1.00 51.68  ? 413  TYR A CD2 1 
ATOM   3309  C  CE1 . TYR A 1 842  ? 133.904 136.493 140.753 1.00 57.80  ? 413  TYR A CE1 1 
ATOM   3310  C  CE2 . TYR A 1 842  ? 133.256 134.379 139.872 1.00 50.27  ? 413  TYR A CE2 1 
ATOM   3311  C  CZ  . TYR A 1 842  ? 134.151 135.412 139.942 1.00 54.49  ? 413  TYR A CZ  1 
ATOM   3312  O  OH  . TYR A 1 842  ? 135.302 135.367 139.195 1.00 65.97  ? 413  TYR A OH  1 
ATOM   3313  N  N   . SER A 1 843  ? 129.044 135.458 139.508 1.00 33.67  ? 414  SER A N   1 
ATOM   3314  C  CA  . SER A 1 843  ? 129.248 135.397 138.066 1.00 48.58  ? 414  SER A CA  1 
ATOM   3315  C  C   . SER A 1 843  ? 128.388 136.440 137.354 1.00 51.71  ? 414  SER A C   1 
ATOM   3316  O  O   . SER A 1 843  ? 128.788 136.962 136.303 1.00 53.24  ? 414  SER A O   1 
ATOM   3317  C  CB  . SER A 1 843  ? 128.984 133.980 137.541 1.00 53.98  ? 414  SER A CB  1 
ATOM   3318  O  OG  . SER A 1 843  ? 129.314 133.884 136.165 1.00 53.00  ? 414  SER A OG  1 
ATOM   3319  N  N   . ILE A 1 844  ? 127.232 136.799 137.934 1.00 51.08  ? 415  ILE A N   1 
ATOM   3320  C  CA  . ILE A 1 844  ? 126.424 137.882 137.353 1.00 43.92  ? 415  ILE A CA  1 
ATOM   3321  C  C   . ILE A 1 844  ? 127.085 139.243 137.578 1.00 44.30  ? 415  ILE A C   1 
ATOM   3322  O  O   . ILE A 1 844  ? 127.107 140.089 136.677 1.00 53.94  ? 415  ILE A O   1 
ATOM   3323  C  CB  . ILE A 1 844  ? 124.997 137.831 137.910 1.00 35.72  ? 415  ILE A CB  1 
ATOM   3324  C  CG1 . ILE A 1 844  ? 124.335 136.536 137.436 1.00 43.13  ? 415  ILE A CG1 1 
ATOM   3325  C  CG2 . ILE A 1 844  ? 124.211 139.039 137.446 1.00 44.23  ? 415  ILE A CG2 1 
ATOM   3326  C  CD1 . ILE A 1 844  ? 123.006 136.252 138.100 1.00 51.78  ? 415  ILE A CD1 1 
ATOM   3327  N  N   . ALA A 1 845  ? 127.627 139.481 138.769 1.00 32.62  ? 416  ALA A N   1 
ATOM   3328  C  CA  . ALA A 1 845  ? 128.381 140.701 138.990 1.00 28.73  ? 416  ALA A CA  1 
ATOM   3329  C  C   . ALA A 1 845  ? 129.547 140.790 138.040 1.00 32.10  ? 416  ALA A C   1 
ATOM   3330  O  O   . ALA A 1 845  ? 129.850 141.867 137.526 1.00 47.17  ? 416  ALA A O   1 
ATOM   3331  C  CB  . ALA A 1 845  ? 128.893 140.766 140.416 1.00 40.54  ? 416  ALA A CB  1 
ATOM   3332  N  N   . LYS A 1 846  ? 130.225 139.675 137.799 1.00 35.70  ? 417  LYS A N   1 
ATOM   3333  C  CA  . LYS A 1 846  ? 131.372 139.703 136.898 1.00 46.42  ? 417  LYS A CA  1 
ATOM   3334  C  C   . LYS A 1 846  ? 130.954 139.988 135.461 1.00 53.73  ? 417  LYS A C   1 
ATOM   3335  O  O   . LYS A 1 846  ? 131.638 140.733 134.752 1.00 63.47  ? 417  LYS A O   1 
ATOM   3336  C  CB  . LYS A 1 846  ? 132.150 138.387 136.976 1.00 53.91  ? 417  LYS A CB  1 
ATOM   3337  C  CG  . LYS A 1 846  ? 133.331 138.288 136.011 1.00 62.63  ? 417  LYS A CG  1 
ATOM   3338  C  CD  . LYS A 1 846  ? 134.050 136.946 136.142 1.00 73.01  ? 417  LYS A CD  1 
ATOM   3339  C  CE  . LYS A 1 846  ? 135.202 136.842 135.153 1.00 83.57  ? 417  LYS A CE  1 
ATOM   3340  N  NZ  . LYS A 1 846  ? 136.204 137.926 135.360 1.00 89.47  ? 417  LYS A NZ  1 
ATOM   3341  N  N   . HIS A 1 847  ? 129.856 139.392 134.999 1.00 52.46  ? 418  HIS A N   1 
ATOM   3342  C  CA  . HIS A 1 847  ? 129.384 139.676 133.645 1.00 50.53  ? 418  HIS A CA  1 
ATOM   3343  C  C   . HIS A 1 847  ? 128.951 141.123 133.493 1.00 57.68  ? 418  HIS A C   1 
ATOM   3344  O  O   . HIS A 1 847  ? 129.174 141.736 132.443 1.00 62.57  ? 418  HIS A O   1 
ATOM   3345  C  CB  . HIS A 1 847  ? 128.215 138.773 133.294 1.00 63.00  ? 418  HIS A CB  1 
ATOM   3346  C  CG  . HIS A 1 847  ? 127.529 139.151 132.022 1.00 63.97  ? 418  HIS A CG  1 
ATOM   3347  N  ND1 . HIS A 1 847  ? 128.103 138.958 130.783 1.00 65.30  ? 418  HIS A ND1 1 
ATOM   3348  C  CD2 . HIS A 1 847  ? 126.328 139.736 131.799 1.00 62.87  ? 418  HIS A CD2 1 
ATOM   3349  C  CE1 . HIS A 1 847  ? 127.274 139.390 129.848 1.00 72.41  ? 418  HIS A CE1 1 
ATOM   3350  N  NE2 . HIS A 1 847  ? 126.190 139.867 130.438 1.00 69.90  ? 418  HIS A NE2 1 
ATOM   3351  N  N   . TYR A 1 848  ? 128.275 141.669 134.508 1.00 56.01  ? 419  TYR A N   1 
ATOM   3352  C  CA  . TYR A 1 848  ? 127.881 143.070 134.455 1.00 49.76  ? 419  TYR A CA  1 
ATOM   3353  C  C   . TYR A 1 848  ? 129.093 143.973 134.437 1.00 42.78  ? 419  TYR A C   1 
ATOM   3354  O  O   . TYR A 1 848  ? 129.156 144.931 133.666 1.00 55.35  ? 419  TYR A O   1 
ATOM   3355  C  CB  . TYR A 1 848  ? 126.992 143.414 135.637 1.00 52.08  ? 419  TYR A CB  1 
ATOM   3356  C  CG  . TYR A 1 848  ? 126.455 144.821 135.579 1.00 59.75  ? 419  TYR A CG  1 
ATOM   3357  C  CD1 . TYR A 1 848  ? 127.138 145.884 136.176 1.00 59.99  ? 419  TYR A CD1 1 
ATOM   3358  C  CD2 . TYR A 1 848  ? 125.281 145.100 134.883 1.00 56.80  ? 419  TYR A CD2 1 
ATOM   3359  C  CE1 . TYR A 1 848  ? 126.636 147.181 136.112 1.00 54.78  ? 419  TYR A CE1 1 
ATOM   3360  C  CE2 . TYR A 1 848  ? 124.777 146.385 134.812 1.00 57.37  ? 419  TYR A CE2 1 
ATOM   3361  C  CZ  . TYR A 1 848  ? 125.457 147.422 135.430 1.00 62.62  ? 419  TYR A CZ  1 
ATOM   3362  O  OH  . TYR A 1 848  ? 124.951 148.702 135.352 1.00 74.35  ? 419  TYR A OH  1 
ATOM   3363  N  N   . PHE A 1 849  ? 130.078 143.664 135.257 1.00 42.68  ? 420  PHE A N   1 
ATOM   3364  C  CA  . PHE A 1 849  ? 131.268 144.485 135.284 1.00 45.71  ? 420  PHE A CA  1 
ATOM   3365  C  C   . PHE A 1 849  ? 131.943 144.549 133.920 1.00 59.54  ? 420  PHE A C   1 
ATOM   3366  O  O   . PHE A 1 849  ? 132.344 145.631 133.480 1.00 70.88  ? 420  PHE A O   1 
ATOM   3367  C  CB  . PHE A 1 849  ? 132.226 143.956 136.331 1.00 52.46  ? 420  PHE A CB  1 
ATOM   3368  C  CG  . PHE A 1 849  ? 133.417 144.806 136.509 1.00 55.40  ? 420  PHE A CG  1 
ATOM   3369  C  CD1 . PHE A 1 849  ? 134.595 144.520 135.843 1.00 64.92  ? 420  PHE A CD1 1 
ATOM   3370  C  CD2 . PHE A 1 849  ? 133.350 145.930 137.299 1.00 62.59  ? 420  PHE A CD2 1 
ATOM   3371  C  CE1 . PHE A 1 849  ? 135.707 145.325 135.999 1.00 71.32  ? 420  PHE A CE1 1 
ATOM   3372  C  CE2 . PHE A 1 849  ? 134.449 146.746 137.463 1.00 72.66  ? 420  PHE A CE2 1 
ATOM   3373  C  CZ  . PHE A 1 849  ? 135.634 146.444 136.809 1.00 78.43  ? 420  PHE A CZ  1 
ATOM   3374  N  N   . ASP A 1 850  ? 132.082 143.413 133.229 1.00 59.44  ? 421  ASP A N   1 
ATOM   3375  C  CA  . ASP A 1 850  ? 132.856 143.407 131.982 1.00 61.99  ? 421  ASP A CA  1 
ATOM   3376  C  C   . ASP A 1 850  ? 132.149 144.167 130.868 1.00 56.52  ? 421  ASP A C   1 
ATOM   3377  O  O   . ASP A 1 850  ? 132.796 144.876 130.088 1.00 58.61  ? 421  ASP A O   1 
ATOM   3378  C  CB  . ASP A 1 850  ? 133.152 141.975 131.535 1.00 72.73  ? 421  ASP A CB  1 
ATOM   3379  C  CG  . ASP A 1 850  ? 134.181 141.278 132.425 1.00 86.28  ? 421  ASP A CG  1 
ATOM   3380  O  OD1 . ASP A 1 850  ? 134.752 141.940 133.324 1.00 73.83  ? 421  ASP A OD1 1 
ATOM   3381  O  OD2 . ASP A 1 850  ? 134.406 140.058 132.230 1.00 90.08  ? 421  ASP A OD2 1 
ATOM   3382  N  N   . SER A 1 851  ? 130.831 144.028 130.769 1.00 58.68  ? 422  SER A N   1 
ATOM   3383  C  CA  . SER A 1 851  ? 130.108 144.668 129.677 1.00 65.23  ? 422  SER A CA  1 
ATOM   3384  C  C   . SER A 1 851  ? 129.925 146.154 129.948 1.00 64.37  ? 422  SER A C   1 
ATOM   3385  O  O   . SER A 1 851  ? 130.372 147.002 129.167 1.00 66.52  ? 422  SER A O   1 
ATOM   3386  C  CB  . SER A 1 851  ? 128.744 143.992 129.479 1.00 71.54  ? 422  SER A CB  1 
ATOM   3387  O  OG  . SER A 1 851  ? 128.880 142.616 129.149 1.00 65.15  ? 422  SER A OG  1 
ATOM   3388  N  N   . GLN A 1 852  ? 129.283 146.479 131.061 1.00 59.33  ? 423  GLN A N   1 
ATOM   3389  C  CA  . GLN A 1 852  ? 129.012 147.856 131.414 1.00 56.63  ? 423  GLN A CA  1 
ATOM   3390  C  C   . GLN A 1 852  ? 130.250 148.585 131.886 1.00 51.96  ? 423  GLN A C   1 
ATOM   3391  O  O   . GLN A 1 852  ? 130.197 149.797 132.099 1.00 61.10  ? 423  GLN A O   1 
ATOM   3392  C  CB  . GLN A 1 852  ? 127.963 147.908 132.508 1.00 65.09  ? 423  GLN A CB  1 
ATOM   3393  C  CG  . GLN A 1 852  ? 126.602 147.527 132.016 1.00 68.18  ? 423  GLN A CG  1 
ATOM   3394  C  CD  . GLN A 1 852  ? 126.056 148.538 131.060 1.00 82.31  ? 423  GLN A CD  1 
ATOM   3395  O  OE1 . GLN A 1 852  ? 125.581 149.599 131.463 1.00 86.65  ? 423  GLN A OE1 1 
ATOM   3396  N  NE2 . GLN A 1 852  ? 126.114 148.218 129.774 1.00 87.41  ? 423  GLN A NE2 1 
ATOM   3397  N  N   . GLY A 1 853  ? 131.344 147.886 132.092 1.00 47.13  ? 424  GLY A N   1 
ATOM   3398  C  CA  . GLY A 1 853  ? 132.561 148.571 132.409 1.00 59.03  ? 424  GLY A CA  1 
ATOM   3399  C  C   . GLY A 1 853  ? 132.681 149.054 133.834 1.00 61.45  ? 424  GLY A C   1 
ATOM   3400  O  O   . GLY A 1 853  ? 133.771 149.494 134.223 1.00 66.72  ? 424  GLY A O   1 
ATOM   3401  N  N   . SER A 1 854  ? 131.625 148.985 134.642 1.00 49.63  ? 425  SER A N   1 
ATOM   3402  C  CA  . SER A 1 854  ? 131.813 149.267 136.059 1.00 58.69  ? 425  SER A CA  1 
ATOM   3403  C  C   . SER A 1 854  ? 130.765 148.545 136.883 1.00 57.40  ? 425  SER A C   1 
ATOM   3404  O  O   . SER A 1 854  ? 129.815 147.966 136.351 1.00 56.76  ? 425  SER A O   1 
ATOM   3405  C  CB  . SER A 1 854  ? 131.795 150.767 136.355 1.00 65.56  ? 425  SER A CB  1 
ATOM   3406  O  OG  . SER A 1 854  ? 132.949 151.393 135.812 1.00 68.23  ? 425  SER A OG  1 
ATOM   3407  N  N   . TRP A 1 855  ? 130.970 148.574 138.199 1.00 45.74  ? 426  TRP A N   1 
ATOM   3408  C  CA  . TRP A 1 855  ? 130.045 147.936 139.104 1.00 35.03  ? 426  TRP A CA  1 
ATOM   3409  C  C   . TRP A 1 855  ? 128.650 148.472 138.890 1.00 47.81  ? 426  TRP A C   1 
ATOM   3410  O  O   . TRP A 1 855  ? 128.453 149.582 138.394 1.00 54.40  ? 426  TRP A O   1 
ATOM   3411  C  CB  . TRP A 1 855  ? 130.446 148.178 140.539 1.00 40.26  ? 426  TRP A CB  1 
ATOM   3412  C  CG  . TRP A 1 855  ? 131.396 147.181 141.007 1.00 58.46  ? 426  TRP A CG  1 
ATOM   3413  C  CD1 . TRP A 1 855  ? 132.706 147.085 140.671 1.00 66.64  ? 426  TRP A CD1 1 
ATOM   3414  C  CD2 . TRP A 1 855  ? 131.122 146.091 141.895 1.00 60.07  ? 426  TRP A CD2 1 
ATOM   3415  N  NE1 . TRP A 1 855  ? 133.278 146.003 141.303 1.00 67.61  ? 426  TRP A NE1 1 
ATOM   3416  C  CE2 . TRP A 1 855  ? 132.324 145.376 142.060 1.00 64.40  ? 426  TRP A CE2 1 
ATOM   3417  C  CE3 . TRP A 1 855  ? 129.976 145.651 142.566 1.00 65.72  ? 426  TRP A CE3 1 
ATOM   3418  C  CZ2 . TRP A 1 855  ? 132.417 144.242 142.871 1.00 78.86  ? 426  TRP A CZ2 1 
ATOM   3419  C  CZ3 . TRP A 1 855  ? 130.065 144.525 143.369 1.00 72.23  ? 426  TRP A CZ3 1 
ATOM   3420  C  CH2 . TRP A 1 855  ? 131.279 143.834 143.517 1.00 81.74  ? 426  TRP A CH2 1 
ATOM   3421  N  N   . TYR A 1 856  ? 127.667 147.654 139.243 1.00 46.27  ? 427  TYR A N   1 
ATOM   3422  C  CA  . TYR A 1 856  ? 126.318 148.173 139.284 1.00 40.35  ? 427  TYR A CA  1 
ATOM   3423  C  C   . TYR A 1 856  ? 126.116 148.920 140.593 1.00 41.82  ? 427  TYR A C   1 
ATOM   3424  O  O   . TYR A 1 856  ? 126.846 148.728 141.569 1.00 45.24  ? 427  TYR A O   1 
ATOM   3425  C  CB  . TYR A 1 856  ? 125.313 147.056 139.156 1.00 40.46  ? 427  TYR A CB  1 
ATOM   3426  C  CG  . TYR A 1 856  ? 125.690 145.857 139.982 1.00 51.08  ? 427  TYR A CG  1 
ATOM   3427  C  CD1 . TYR A 1 856  ? 125.472 145.844 141.349 1.00 56.63  ? 427  TYR A CD1 1 
ATOM   3428  C  CD2 . TYR A 1 856  ? 126.236 144.730 139.405 1.00 55.78  ? 427  TYR A CD2 1 
ATOM   3429  C  CE1 . TYR A 1 856  ? 125.795 144.753 142.121 1.00 50.27  ? 427  TYR A CE1 1 
ATOM   3430  C  CE2 . TYR A 1 856  ? 126.564 143.622 140.178 1.00 56.03  ? 427  TYR A CE2 1 
ATOM   3431  C  CZ  . TYR A 1 856  ? 126.339 143.647 141.535 1.00 46.74  ? 427  TYR A CZ  1 
ATOM   3432  O  OH  . TYR A 1 856  ? 126.663 142.561 142.312 1.00 52.17  ? 427  TYR A OH  1 
ATOM   3433  N  N   . SER A 1 857  ? 125.122 149.790 140.601 1.00 40.27  ? 428  SER A N   1 
ATOM   3434  C  CA  . SER A 1 857  ? 124.914 150.676 141.739 1.00 47.46  ? 428  SER A CA  1 
ATOM   3435  C  C   . SER A 1 857  ? 124.486 149.857 142.949 1.00 48.45  ? 428  SER A C   1 
ATOM   3436  O  O   . SER A 1 857  ? 123.359 149.358 143.013 1.00 53.68  ? 428  SER A O   1 
ATOM   3437  C  CB  . SER A 1 857  ? 123.867 151.724 141.389 1.00 58.09  ? 428  SER A CB  1 
ATOM   3438  O  OG  . SER A 1 857  ? 122.682 151.090 140.929 1.00 58.20  ? 428  SER A OG  1 
ATOM   3439  N  N   . VAL A 1 858  ? 125.376 149.723 143.923 1.00 44.90  ? 429  VAL A N   1 
ATOM   3440  C  CA  . VAL A 1 858  ? 125.129 148.819 145.033 1.00 40.22  ? 429  VAL A CA  1 
ATOM   3441  C  C   . VAL A 1 858  ? 124.256 149.549 146.037 1.00 38.12  ? 429  VAL A C   1 
ATOM   3442  O  O   . VAL A 1 858  ? 124.739 150.354 146.825 1.00 53.13  ? 429  VAL A O   1 
ATOM   3443  C  CB  . VAL A 1 858  ? 126.428 148.349 145.673 1.00 56.03  ? 429  VAL A CB  1 
ATOM   3444  C  CG1 . VAL A 1 858  ? 126.110 147.469 146.852 1.00 68.13  ? 429  VAL A CG1 1 
ATOM   3445  C  CG2 . VAL A 1 858  ? 127.266 147.627 144.646 1.00 58.30  ? 429  VAL A CG2 1 
ATOM   3446  N  N   . THR A 1 859  ? 122.985 149.240 146.045 1.00 42.01  ? 430  THR A N   1 
ATOM   3447  C  CA  . THR A 1 859  ? 122.092 149.913 146.966 1.00 57.70  ? 430  THR A CA  1 
ATOM   3448  C  C   . THR A 1 859  ? 122.068 149.270 148.346 1.00 57.88  ? 430  THR A C   1 
ATOM   3449  O  O   . THR A 1 859  ? 121.334 149.744 149.220 1.00 64.04  ? 430  THR A O   1 
ATOM   3450  C  CB  . THR A 1 859  ? 120.664 149.963 146.388 1.00 76.22  ? 430  THR A CB  1 
ATOM   3451  O  OG1 . THR A 1 859  ? 120.154 148.627 146.213 1.00 70.17  ? 430  THR A OG1 1 
ATOM   3452  C  CG2 . THR A 1 859  ? 120.635 150.732 145.044 1.00 67.07  ? 430  THR A CG2 1 
ATOM   3453  N  N   . SER A 1 860  ? 122.836 148.214 148.577 1.00 56.10  ? 431  SER A N   1 
ATOM   3454  C  CA  . SER A 1 860  ? 122.757 147.561 149.874 1.00 60.21  ? 431  SER A CA  1 
ATOM   3455  C  C   . SER A 1 860  ? 123.648 148.280 150.874 1.00 56.23  ? 431  SER A C   1 
ATOM   3456  O  O   . SER A 1 860  ? 124.389 149.204 150.535 1.00 64.66  ? 431  SER A O   1 
ATOM   3457  C  CB  . SER A 1 860  ? 123.167 146.095 149.784 1.00 69.76  ? 431  SER A CB  1 
ATOM   3458  O  OG  . SER A 1 860  ? 124.544 145.965 149.460 1.00 68.64  ? 431  SER A OG  1 
ATOM   3459  N  N   . ASP A 1 861  ? 123.586 147.838 152.121 1.00 51.71  ? 432  ASP A N   1 
ATOM   3460  C  CA  . ASP A 1 861  ? 124.435 148.422 153.139 1.00 57.87  ? 432  ASP A CA  1 
ATOM   3461  C  C   . ASP A 1 861  ? 125.896 148.126 152.825 1.00 66.94  ? 432  ASP A C   1 
ATOM   3462  O  O   . ASP A 1 861  ? 126.246 147.019 152.411 1.00 70.58  ? 432  ASP A O   1 
ATOM   3463  C  CB  . ASP A 1 861  ? 124.052 147.874 154.501 1.00 66.44  ? 432  ASP A CB  1 
ATOM   3464  C  CG  . ASP A 1 861  ? 122.583 148.011 154.767 1.00 76.71  ? 432  ASP A CG  1 
ATOM   3465  O  OD1 . ASP A 1 861  ? 122.008 149.034 154.341 1.00 81.05  ? 432  ASP A OD1 1 
ATOM   3466  O  OD2 . ASP A 1 861  ? 121.994 147.090 155.369 1.00 80.29  ? 432  ASP A OD2 1 
ATOM   3467  N  N   . ARG A 1 862  ? 126.747 149.139 152.979 1.00 65.95  ? 433  ARG A N   1 
ATOM   3468  C  CA  . ARG A 1 862  ? 128.173 148.950 152.771 1.00 59.86  ? 433  ARG A CA  1 
ATOM   3469  C  C   . ARG A 1 862  ? 128.834 148.256 153.940 1.00 58.35  ? 433  ARG A C   1 
ATOM   3470  O  O   . ARG A 1 862  ? 129.930 147.707 153.785 1.00 66.53  ? 433  ARG A O   1 
ATOM   3471  C  CB  . ARG A 1 862  ? 128.862 150.291 152.539 1.00 69.75  ? 433  ARG A CB  1 
ATOM   3472  C  CG  . ARG A 1 862  ? 128.472 150.947 151.238 1.00 76.88  ? 433  ARG A CG  1 
ATOM   3473  C  CD  . ARG A 1 862  ? 128.640 149.971 150.073 1.00 86.58  ? 433  ARG A CD  1 
ATOM   3474  N  NE  . ARG A 1 862  ? 128.410 150.616 148.776 1.00 98.68  ? 433  ARG A NE  1 
ATOM   3475  C  CZ  . ARG A 1 862  ? 129.373 151.054 147.960 1.00 99.68  ? 433  ARG A CZ  1 
ATOM   3476  N  NH1 . ARG A 1 862  ? 130.655 150.920 148.298 1.00 90.36  ? 433  ARG A NH1 1 
ATOM   3477  N  NH2 . ARG A 1 862  ? 129.054 151.632 146.803 1.00 91.49  ? 433  ARG A NH2 1 
ATOM   3478  N  N   . ASN A 1 863  ? 128.212 148.289 155.110 1.00 50.70  ? 434  ASN A N   1 
ATOM   3479  C  CA  . ASN A 1 863  ? 128.766 147.547 156.224 1.00 52.30  ? 434  ASN A CA  1 
ATOM   3480  C  C   . ASN A 1 863  ? 128.717 146.040 155.974 1.00 77.22  ? 434  ASN A C   1 
ATOM   3481  O  O   . ASN A 1 863  ? 129.656 145.318 156.332 1.00 78.90  ? 434  ASN A O   1 
ATOM   3482  C  CB  . ASN A 1 863  ? 128.024 147.891 157.498 1.00 64.35  ? 434  ASN A CB  1 
ATOM   3483  C  CG  . ASN A 1 863  ? 128.343 146.920 158.606 1.00 82.31  ? 434  ASN A CG  1 
ATOM   3484  O  OD1 . ASN A 1 863  ? 129.436 146.952 159.172 1.00 86.82  ? 434  ASN A OD1 1 
ATOM   3485  N  ND2 . ASN A 1 863  ? 127.409 146.014 158.895 1.00 81.02  ? 434  ASN A ND2 1 
ATOM   3486  N  N   . LEU A 1 864  ? 127.628 145.541 155.362 1.00 78.66  ? 435  LEU A N   1 
ATOM   3487  C  CA  . LEU A 1 864  ? 127.423 144.094 155.206 1.00 70.49  ? 435  LEU A CA  1 
ATOM   3488  C  C   . LEU A 1 864  ? 128.470 143.429 154.327 1.00 57.48  ? 435  LEU A C   1 
ATOM   3489  O  O   . LEU A 1 864  ? 128.590 142.201 154.338 1.00 65.57  ? 435  LEU A O   1 
ATOM   3490  C  CB  . LEU A 1 864  ? 126.040 143.798 154.617 1.00 72.97  ? 435  LEU A CB  1 
ATOM   3491  C  CG  . LEU A 1 864  ? 124.808 144.238 155.411 1.00 83.38  ? 435  LEU A CG  1 
ATOM   3492  C  CD1 . LEU A 1 864  ? 123.516 143.926 154.629 1.00 81.22  ? 435  LEU A CD1 1 
ATOM   3493  C  CD2 . LEU A 1 864  ? 124.813 143.574 156.801 1.00 82.39  ? 435  LEU A CD2 1 
ATOM   3494  N  N   . THR A 1 865  ? 129.212 144.198 153.565 1.00 47.38  ? 436  THR A N   1 
ATOM   3495  C  CA  . THR A 1 865  ? 130.195 143.665 152.643 1.00 52.43  ? 436  THR A CA  1 
ATOM   3496  C  C   . THR A 1 865  ? 131.514 144.359 152.947 1.00 62.17  ? 436  THR A C   1 
ATOM   3497  O  O   . THR A 1 865  ? 131.963 145.235 152.196 1.00 69.55  ? 436  THR A O   1 
ATOM   3498  C  CB  . THR A 1 865  ? 129.728 143.884 151.207 1.00 65.30  ? 436  THR A CB  1 
ATOM   3499  O  OG1 . THR A 1 865  ? 129.511 145.285 150.988 1.00 67.14  ? 436  THR A OG1 1 
ATOM   3500  C  CG2 . THR A 1 865  ? 128.425 143.150 150.953 1.00 62.58  ? 436  THR A CG2 1 
ATOM   3501  N  N   . PRO A 1 866  ? 132.157 144.006 154.053 1.00 58.57  ? 437  PRO A N   1 
ATOM   3502  C  CA  . PRO A 1 866  ? 133.390 144.706 154.432 1.00 54.64  ? 437  PRO A CA  1 
ATOM   3503  C  C   . PRO A 1 866  ? 134.484 144.589 153.410 1.00 48.52  ? 437  PRO A C   1 
ATOM   3504  O  O   . PRO A 1 866  ? 135.278 145.519 153.255 1.00 61.24  ? 437  PRO A O   1 
ATOM   3505  C  CB  . PRO A 1 866  ? 133.796 144.020 155.741 1.00 71.47  ? 437  PRO A CB  1 
ATOM   3506  C  CG  . PRO A 1 866  ? 132.548 143.369 156.241 1.00 78.55  ? 437  PRO A CG  1 
ATOM   3507  C  CD  . PRO A 1 866  ? 131.790 142.961 155.016 1.00 71.04  ? 437  PRO A CD  1 
ATOM   3508  N  N   . GLY A 1 867  ? 134.576 143.477 152.719 1.00 48.06  ? 438  GLY A N   1 
ATOM   3509  C  CA  . GLY A 1 867  ? 135.671 143.349 151.796 1.00 56.70  ? 438  GLY A CA  1 
ATOM   3510  C  C   . GLY A 1 867  ? 135.267 143.855 150.438 1.00 54.85  ? 438  GLY A C   1 
ATOM   3511  O  O   . GLY A 1 867  ? 136.030 144.548 149.767 1.00 62.46  ? 438  GLY A O   1 
ATOM   3512  N  N   . LEU A 1 868  ? 134.052 143.537 150.033 1.00 53.42  ? 439  LEU A N   1 
ATOM   3513  C  CA  . LEU A 1 868  ? 133.641 143.890 148.688 1.00 62.59  ? 439  LEU A CA  1 
ATOM   3514  C  C   . LEU A 1 868  ? 133.560 145.401 148.489 1.00 73.17  ? 439  LEU A C   1 
ATOM   3515  O  O   . LEU A 1 868  ? 133.844 145.893 147.385 1.00 77.63  ? 439  LEU A O   1 
ATOM   3516  C  CB  . LEU A 1 868  ? 132.290 143.257 148.371 1.00 69.73  ? 439  LEU A CB  1 
ATOM   3517  C  CG  . LEU A 1 868  ? 132.327 141.819 147.887 1.00 64.54  ? 439  LEU A CG  1 
ATOM   3518  C  CD1 . LEU A 1 868  ? 130.905 141.357 147.669 1.00 64.16  ? 439  LEU A CD1 1 
ATOM   3519  C  CD2 . LEU A 1 868  ? 133.153 141.720 146.612 1.00 76.24  ? 439  LEU A CD2 1 
ATOM   3520  N  N   . ASN A 1 869  ? 133.153 146.151 149.520 1.00 67.18  ? 440  ASN A N   1 
ATOM   3521  C  CA  . ASN A 1 869  ? 132.920 147.577 149.316 1.00 64.22  ? 440  ASN A CA  1 
ATOM   3522  C  C   . ASN A 1 869  ? 134.203 148.283 148.936 1.00 59.90  ? 440  ASN A C   1 
ATOM   3523  O  O   . ASN A 1 869  ? 134.169 149.282 148.214 1.00 69.13  ? 440  ASN A O   1 
ATOM   3524  C  CB  . ASN A 1 869  ? 132.320 148.228 150.561 1.00 71.09  ? 440  ASN A CB  1 
ATOM   3525  C  CG  . ASN A 1 869  ? 133.192 148.058 151.791 1.00 76.78  ? 440  ASN A CG  1 
ATOM   3526  O  OD1 . ASN A 1 869  ? 134.398 147.808 151.688 1.00 75.11  ? 440  ASN A OD1 1 
ATOM   3527  N  ND2 . ASN A 1 869  ? 132.588 148.209 152.971 1.00 72.86  ? 440  ASN A ND2 1 
ATOM   3528  N  N   . SER A 1 870  ? 135.340 147.777 149.404 1.00 52.19  ? 441  SER A N   1 
ATOM   3529  C  CA  . SER A 1 870  ? 136.603 148.375 149.008 1.00 62.65  ? 441  SER A CA  1 
ATOM   3530  C  C   . SER A 1 870  ? 136.849 148.216 147.506 1.00 64.50  ? 441  SER A C   1 
ATOM   3531  O  O   . SER A 1 870  ? 137.250 149.174 146.828 1.00 71.39  ? 441  SER A O   1 
ATOM   3532  C  CB  . SER A 1 870  ? 137.733 147.771 149.838 1.00 65.71  ? 441  SER A CB  1 
ATOM   3533  O  OG  . SER A 1 870  ? 137.779 146.369 149.675 1.00 68.95  ? 441  SER A OG  1 
ATOM   3534  N  N   . TYR A 1 871  ? 136.588 147.031 146.958 1.00 60.61  ? 442  TYR A N   1 
ATOM   3535  C  CA  . TYR A 1 871  ? 136.743 146.854 145.519 1.00 60.56  ? 442  TYR A CA  1 
ATOM   3536  C  C   . TYR A 1 871  ? 135.770 147.737 144.760 1.00 60.86  ? 442  TYR A C   1 
ATOM   3537  O  O   . TYR A 1 871  ? 136.151 148.391 143.783 1.00 68.62  ? 442  TYR A O   1 
ATOM   3538  C  CB  . TYR A 1 871  ? 136.544 145.384 145.133 1.00 75.92  ? 442  TYR A CB  1 
ATOM   3539  C  CG  . TYR A 1 871  ? 137.630 144.455 145.642 1.00 78.38  ? 442  TYR A CG  1 
ATOM   3540  C  CD1 . TYR A 1 871  ? 138.740 144.152 144.865 1.00 73.76  ? 442  TYR A CD1 1 
ATOM   3541  C  CD2 . TYR A 1 871  ? 137.549 143.897 146.914 1.00 82.61  ? 442  TYR A CD2 1 
ATOM   3542  C  CE1 . TYR A 1 871  ? 139.729 143.310 145.342 1.00 81.19  ? 442  TYR A CE1 1 
ATOM   3543  C  CE2 . TYR A 1 871  ? 138.533 143.065 147.397 1.00 78.03  ? 442  TYR A CE2 1 
ATOM   3544  C  CZ  . TYR A 1 871  ? 139.617 142.773 146.612 1.00 79.33  ? 442  TYR A CZ  1 
ATOM   3545  O  OH  . TYR A 1 871  ? 140.589 141.939 147.106 1.00 84.83  ? 442  TYR A OH  1 
ATOM   3546  N  N   . ILE A 1 872  ? 134.517 147.799 145.211 1.00 59.10  ? 443  ILE A N   1 
ATOM   3547  C  CA  . ILE A 1 872  ? 133.546 148.660 144.543 1.00 60.38  ? 443  ILE A CA  1 
ATOM   3548  C  C   . ILE A 1 872  ? 134.031 150.114 144.543 1.00 65.61  ? 443  ILE A C   1 
ATOM   3549  O  O   . ILE A 1 872  ? 133.927 150.820 143.531 1.00 66.15  ? 443  ILE A O   1 
ATOM   3550  C  CB  . ILE A 1 872  ? 132.167 148.509 145.208 1.00 64.74  ? 443  ILE A CB  1 
ATOM   3551  C  CG1 . ILE A 1 872  ? 131.706 147.060 145.126 1.00 63.71  ? 443  ILE A CG1 1 
ATOM   3552  C  CG2 . ILE A 1 872  ? 131.122 149.402 144.527 1.00 73.71  ? 443  ILE A CG2 1 
ATOM   3553  C  CD1 . ILE A 1 872  ? 130.476 146.762 145.989 1.00 72.99  ? 443  ILE A CD1 1 
ATOM   3554  N  N   . LYS A 1 873  ? 134.583 150.581 145.667 1.00 66.39  ? 444  LYS A N   1 
ATOM   3555  C  CA  . LYS A 1 873  ? 135.074 151.954 145.731 1.00 60.00  ? 444  LYS A CA  1 
ATOM   3556  C  C   . LYS A 1 873  ? 136.196 152.176 144.744 1.00 53.60  ? 444  LYS A C   1 
ATOM   3557  O  O   . LYS A 1 873  ? 136.200 153.165 144.003 1.00 63.35  ? 444  LYS A O   1 
ATOM   3558  C  CB  . LYS A 1 873  ? 135.545 152.295 147.143 1.00 64.91  ? 444  LYS A CB  1 
ATOM   3559  C  CG  . LYS A 1 873  ? 134.401 152.461 148.134 1.00 74.58  ? 444  LYS A CG  1 
ATOM   3560  C  CD  . LYS A 1 873  ? 134.884 152.498 149.585 1.00 80.81  ? 444  LYS A CD  1 
ATOM   3561  C  CE  . LYS A 1 873  ? 135.921 153.600 149.850 1.00 89.51  ? 444  LYS A CE  1 
ATOM   3562  N  NZ  . LYS A 1 873  ? 135.417 154.984 149.560 1.00 82.93  ? 444  LYS A NZ  1 
ATOM   3563  N  N   . ARG A 1 874  ? 137.149 151.262 144.702 1.00 54.72  ? 445  ARG A N   1 
ATOM   3564  C  CA  . ARG A 1 874  ? 138.164 151.419 143.680 1.00 61.05  ? 445  ARG A CA  1 
ATOM   3565  C  C   . ARG A 1 874  ? 137.591 151.141 142.305 1.00 66.09  ? 445  ARG A C   1 
ATOM   3566  O  O   . ARG A 1 874  ? 138.271 151.332 141.306 1.00 70.55  ? 445  ARG A O   1 
ATOM   3567  C  CB  . ARG A 1 874  ? 139.339 150.498 143.983 1.00 72.30  ? 445  ARG A CB  1 
ATOM   3568  C  CG  . ARG A 1 874  ? 140.380 151.112 144.937 1.00 78.24  ? 445  ARG A CG  1 
ATOM   3569  C  CD  . ARG A 1 874  ? 141.559 150.165 145.200 1.00 85.35  ? 445  ARG A CD  1 
ATOM   3570  N  NE  . ARG A 1 874  ? 141.114 148.957 145.921 1.00 94.66  ? 445  ARG A NE  1 
ATOM   3571  C  CZ  . ARG A 1 874  ? 140.947 148.852 147.245 1.00 93.81  ? 445  ARG A CZ  1 
ATOM   3572  N  NH1 . ARG A 1 874  ? 141.158 149.889 148.051 1.00 88.76  ? 445  ARG A NH1 1 
ATOM   3573  N  NH2 . ARG A 1 874  ? 140.530 147.701 147.765 1.00 87.96  ? 445  ARG A NH2 1 
ATOM   3574  N  N   . ASN A 1 875  ? 136.354 150.672 142.231 1.00 63.15  ? 446  ASN A N   1 
ATOM   3575  C  CA  . ASN A 1 875  ? 135.638 150.377 140.969 1.00 63.85  ? 446  ASN A CA  1 
ATOM   3576  C  C   . ASN A 1 875  ? 136.384 149.289 140.143 1.00 73.29  ? 446  ASN A C   1 
ATOM   3577  O  O   . ASN A 1 875  ? 136.386 149.319 138.908 1.00 73.20  ? 446  ASN A O   1 
ATOM   3578  C  CB  . ASN A 1 875  ? 135.431 151.677 140.123 1.00 68.16  ? 446  ASN A CB  1 
ATOM   3579  C  CG  . ASN A 1 875  ? 134.458 151.534 138.879 1.00 88.07  ? 446  ASN A CG  1 
ATOM   3580  O  OD1 . ASN A 1 875  ? 133.974 150.452 138.535 1.00 79.76  ? 446  ASN A OD1 1 
ATOM   3581  N  ND2 . ASN A 1 875  ? 134.284 152.675 138.163 1.00 85.59  ? 446  ASN A ND2 1 
ATOM   3582  N  N   . GLN A 1 876  ? 137.044 148.305 140.778 1.00 73.60  ? 447  GLN A N   1 
ATOM   3583  C  CA  . GLN A 1 876  ? 137.722 147.230 140.045 1.00 66.75  ? 447  GLN A CA  1 
ATOM   3584  C  C   . GLN A 1 876  ? 137.245 145.878 140.568 1.00 65.97  ? 447  GLN A C   1 
ATOM   3585  O  O   . GLN A 1 876  ? 136.869 145.739 141.740 1.00 66.28  ? 447  GLN A O   1 
ATOM   3586  C  CB  . GLN A 1 876  ? 139.224 147.372 140.166 1.00 62.46  ? 447  GLN A CB  1 
ATOM   3587  C  CG  . GLN A 1 876  ? 139.611 147.496 141.585 1.00 79.51  ? 447  GLN A CG  1 
ATOM   3588  C  CD  . GLN A 1 876  ? 141.013 147.973 141.724 1.00 92.20  ? 447  GLN A CD  1 
ATOM   3589  O  OE1 . GLN A 1 876  ? 141.539 148.651 140.834 1.00 87.08  ? 447  GLN A OE1 1 
ATOM   3590  N  NE2 . GLN A 1 876  ? 141.652 147.604 142.818 1.00 91.53  ? 447  GLN A NE2 1 
ATOM   3591  N  N   . PHE A 1 877  ? 137.234 144.886 139.675 1.00 70.09  ? 448  PHE A N   1 
ATOM   3592  C  CA  . PHE A 1 877  ? 136.580 143.652 140.105 1.00 68.99  ? 448  PHE A CA  1 
ATOM   3593  C  C   . PHE A 1 877  ? 137.606 142.735 140.755 1.00 62.61  ? 448  PHE A C   1 
ATOM   3594  O  O   . PHE A 1 877  ? 138.730 142.616 140.260 1.00 67.85  ? 448  PHE A O   1 
ATOM   3595  C  CB  . PHE A 1 877  ? 135.933 142.924 138.924 1.00 73.48  ? 448  PHE A CB  1 
ATOM   3596  C  CG  . PHE A 1 877  ? 134.802 141.995 139.312 1.00 72.99  ? 448  PHE A CG  1 
ATOM   3597  C  CD1 . PHE A 1 877  ? 133.557 142.507 139.699 1.00 63.55  ? 448  PHE A CD1 1 
ATOM   3598  C  CD2 . PHE A 1 877  ? 134.989 140.620 139.322 1.00 78.58  ? 448  PHE A CD2 1 
ATOM   3599  C  CE1 . PHE A 1 877  ? 132.514 141.670 140.050 1.00 57.75  ? 448  PHE A CE1 1 
ATOM   3600  C  CE2 . PHE A 1 877  ? 133.954 139.779 139.684 1.00 75.00  ? 448  PHE A CE2 1 
ATOM   3601  C  CZ  . PHE A 1 877  ? 132.710 140.315 140.052 1.00 63.98  ? 448  PHE A CZ  1 
ATOM   3602  N  N   . PRO A 1 878  ? 137.247 142.101 141.863 1.00 66.50  ? 449  PRO A N   1 
ATOM   3603  C  CA  . PRO A 1 878  ? 138.207 141.273 142.589 1.00 71.82  ? 449  PRO A CA  1 
ATOM   3604  C  C   . PRO A 1 878  ? 138.675 140.104 141.741 1.00 67.18  ? 449  PRO A C   1 
ATOM   3605  O  O   . PRO A 1 878  ? 137.904 139.549 140.946 1.00 72.48  ? 449  PRO A O   1 
ATOM   3606  C  CB  . PRO A 1 878  ? 137.409 140.810 143.819 1.00 80.52  ? 449  PRO A CB  1 
ATOM   3607  C  CG  . PRO A 1 878  ? 135.973 140.830 143.356 1.00 80.44  ? 449  PRO A CG  1 
ATOM   3608  C  CD  . PRO A 1 878  ? 135.893 142.030 142.442 1.00 76.08  ? 449  PRO A CD  1 
ATOM   3609  N  N   . PRO A 1 879  ? 139.936 139.713 141.869 1.00 64.33  ? 450  PRO A N   1 
ATOM   3610  C  CA  . PRO A 1 879  ? 140.461 138.629 141.040 1.00 56.12  ? 450  PRO A CA  1 
ATOM   3611  C  C   . PRO A 1 879  ? 139.891 137.304 141.500 1.00 67.22  ? 450  PRO A C   1 
ATOM   3612  O  O   . PRO A 1 879  ? 139.319 137.187 142.583 1.00 73.25  ? 450  PRO A O   1 
ATOM   3613  C  CB  . PRO A 1 879  ? 141.966 138.690 141.290 1.00 71.66  ? 450  PRO A CB  1 
ATOM   3614  C  CG  . PRO A 1 879  ? 142.076 139.242 142.685 1.00 79.02  ? 450  PRO A CG  1 
ATOM   3615  C  CD  . PRO A 1 879  ? 140.943 140.230 142.811 1.00 77.34  ? 450  PRO A CD  1 
ATOM   3616  N  N   . LEU A 1 880  ? 140.071 136.291 140.656 1.00 71.97  ? 451  LEU A N   1 
ATOM   3617  C  CA  . LEU A 1 880  ? 139.569 134.949 140.959 1.00 68.39  ? 451  LEU A CA  1 
ATOM   3618  C  C   . LEU A 1 880  ? 140.186 134.292 142.193 1.00 63.54  ? 451  LEU A C   1 
ATOM   3619  O  O   . LEU A 1 880  ? 139.461 133.550 142.880 1.00 63.72  ? 451  LEU A O   1 
ATOM   3620  C  CB  . LEU A 1 880  ? 139.760 134.057 139.731 1.00 75.38  ? 451  LEU A CB  1 
ATOM   3621  C  CG  . LEU A 1 880  ? 138.958 132.757 139.669 1.00 80.60  ? 451  LEU A CG  1 
ATOM   3622  C  CD1 . LEU A 1 880  ? 137.471 133.056 139.633 1.00 75.36  ? 451  LEU A CD1 1 
ATOM   3623  C  CD2 . LEU A 1 880  ? 139.357 131.956 138.432 1.00 83.81  ? 451  LEU A CD2 1 
ATOM   3624  N  N   . PRO A 1 881  ? 141.484 134.437 142.491 1.00 65.37  ? 452  PRO A N   1 
ATOM   3625  C  CA  . PRO A 1 881  ? 142.013 133.793 143.704 1.00 70.44  ? 452  PRO A CA  1 
ATOM   3626  C  C   . PRO A 1 881  ? 141.377 134.281 144.984 1.00 70.20  ? 452  PRO A C   1 
ATOM   3627  O  O   . PRO A 1 881  ? 141.196 133.492 145.920 1.00 74.33  ? 452  PRO A O   1 
ATOM   3628  C  CB  . PRO A 1 881  ? 143.508 134.147 143.672 1.00 76.70  ? 452  PRO A CB  1 
ATOM   3629  C  CG  . PRO A 1 881  ? 143.595 135.348 142.815 1.00 74.63  ? 452  PRO A CG  1 
ATOM   3630  C  CD  . PRO A 1 881  ? 142.554 135.134 141.760 1.00 74.61  ? 452  PRO A CD  1 
ATOM   3631  N  N   . MET A 1 882  ? 141.049 135.564 145.068 1.00 70.17  ? 453  MET A N   1 
ATOM   3632  C  CA  . MET A 1 882  ? 140.600 136.136 146.329 1.00 75.11  ? 453  MET A CA  1 
ATOM   3633  C  C   . MET A 1 882  ? 139.099 136.016 146.531 1.00 65.79  ? 453  MET A C   1 
ATOM   3634  O  O   . MET A 1 882  ? 138.597 136.381 147.599 1.00 71.22  ? 453  MET A O   1 
ATOM   3635  C  CB  . MET A 1 882  ? 141.031 137.602 146.424 1.00 87.78  ? 453  MET A CB  1 
ATOM   3636  C  CG  . MET A 1 882  ? 141.159 138.115 147.854 1.00 98.77  ? 453  MET A CG  1 
ATOM   3637  S  SD  . MET A 1 882  ? 141.926 139.753 147.935 1.00 139.32 ? 453  MET A SD  1 
ATOM   3638  C  CE  . MET A 1 882  ? 143.579 139.399 147.326 1.00 97.65  ? 453  MET A CE  1 
ATOM   3639  N  N   . ILE A 1 883  ? 138.378 135.493 145.542 1.00 58.13  ? 454  ILE A N   1 
ATOM   3640  C  CA  . ILE A 1 883  ? 136.963 135.242 145.711 1.00 50.53  ? 454  ILE A CA  1 
ATOM   3641  C  C   . ILE A 1 883  ? 136.700 134.285 146.848 1.00 52.47  ? 454  ILE A C   1 
ATOM   3642  O  O   . ILE A 1 883  ? 135.603 134.278 147.406 1.00 64.01  ? 454  ILE A O   1 
ATOM   3643  C  CB  . ILE A 1 883  ? 136.373 134.715 144.394 1.00 64.29  ? 454  ILE A CB  1 
ATOM   3644  C  CG1 . ILE A 1 883  ? 136.608 135.741 143.296 1.00 73.75  ? 454  ILE A CG1 1 
ATOM   3645  C  CG2 . ILE A 1 883  ? 134.884 134.445 144.517 1.00 71.52  ? 454  ILE A CG2 1 
ATOM   3646  C  CD1 . ILE A 1 883  ? 136.035 137.121 143.665 1.00 77.28  ? 454  ILE A CD1 1 
ATOM   3647  N  N   . LYS A 1 884  ? 137.678 133.479 147.225 1.00 54.49  ? 455  LYS A N   1 
ATOM   3648  C  CA  . LYS A 1 884  ? 137.376 132.417 148.168 1.00 60.29  ? 455  LYS A CA  1 
ATOM   3649  C  C   . LYS A 1 884  ? 136.937 132.985 149.508 1.00 54.47  ? 455  LYS A C   1 
ATOM   3650  O  O   . LYS A 1 884  ? 135.947 132.528 150.087 1.00 58.35  ? 455  LYS A O   1 
ATOM   3651  C  CB  . LYS A 1 884  ? 138.588 131.500 148.313 1.00 69.45  ? 455  LYS A CB  1 
ATOM   3652  C  CG  . LYS A 1 884  ? 138.297 130.187 149.031 1.00 77.67  ? 455  LYS A CG  1 
ATOM   3653  C  CD  . LYS A 1 884  ? 139.518 129.261 148.991 1.00 89.25  ? 455  LYS A CD  1 
ATOM   3654  C  CE  . LYS A 1 884  ? 139.244 127.903 149.639 1.00 89.13  ? 455  LYS A CE  1 
ATOM   3655  N  NZ  . LYS A 1 884  ? 140.440 127.008 149.582 1.00 90.45  ? 455  LYS A NZ  1 
ATOM   3656  N  N   . GLU A 1 885  ? 137.635 134.009 149.997 1.00 56.85  ? 456  GLU A N   1 
ATOM   3657  C  CA  . GLU A 1 885  ? 137.319 134.586 151.302 1.00 64.31  ? 456  GLU A CA  1 
ATOM   3658  C  C   . GLU A 1 885  ? 136.144 135.553 151.248 1.00 62.40  ? 456  GLU A C   1 
ATOM   3659  O  O   . GLU A 1 885  ? 135.385 135.655 152.216 1.00 59.28  ? 456  GLU A O   1 
ATOM   3660  C  CB  . GLU A 1 885  ? 138.534 135.327 151.857 1.00 80.46  ? 456  GLU A CB  1 
ATOM   3661  C  CG  . GLU A 1 885  ? 139.687 134.440 152.294 1.00 83.43  ? 456  GLU A CG  1 
ATOM   3662  C  CD  . GLU A 1 885  ? 140.485 133.895 151.121 1.00 85.28  ? 456  GLU A CD  1 
ATOM   3663  O  OE1 . GLU A 1 885  ? 140.276 134.374 149.980 1.00 77.47  ? 456  GLU A OE1 1 
ATOM   3664  O  OE2 . GLU A 1 885  ? 141.333 133.000 151.346 1.00 89.69  ? 456  GLU A OE2 1 
ATOM   3665  N  N   . LEU A 1 886  ? 136.010 136.283 150.143 1.00 63.63  ? 457  LEU A N   1 
ATOM   3666  C  CA  . LEU A 1 886  ? 134.939 137.238 149.912 1.00 57.68  ? 457  LEU A CA  1 
ATOM   3667  C  C   . LEU A 1 886  ? 133.676 136.572 149.391 1.00 65.04  ? 457  LEU A C   1 
ATOM   3668  O  O   . LEU A 1 886  ? 132.711 137.272 149.064 1.00 66.39  ? 457  LEU A O   1 
ATOM   3669  C  CB  . LEU A 1 886  ? 135.375 138.283 148.883 1.00 58.95  ? 457  LEU A CB  1 
ATOM   3670  C  CG  . LEU A 1 886  ? 136.648 139.062 149.190 1.00 76.26  ? 457  LEU A CG  1 
ATOM   3671  C  CD1 . LEU A 1 886  ? 136.969 139.982 148.006 1.00 77.11  ? 457  LEU A CD1 1 
ATOM   3672  C  CD2 . LEU A 1 886  ? 136.563 139.820 150.528 1.00 75.92  ? 457  LEU A CD2 1 
ATOM   3673  N  N   . LEU A 1 887  ? 133.668 135.246 149.263 1.00 61.35  ? 458  LEU A N   1 
ATOM   3674  C  CA  . LEU A 1 887  ? 132.557 134.604 148.584 1.00 42.42  ? 458  LEU A CA  1 
ATOM   3675  C  C   . LEU A 1 887  ? 131.269 134.874 149.309 1.00 44.65  ? 458  LEU A C   1 
ATOM   3676  O  O   . LEU A 1 887  ? 130.243 135.136 148.676 1.00 57.39  ? 458  LEU A O   1 
ATOM   3677  C  CB  . LEU A 1 887  ? 132.793 133.107 148.459 1.00 48.26  ? 458  LEU A CB  1 
ATOM   3678  C  CG  . LEU A 1 887  ? 131.858 132.481 147.434 1.00 54.04  ? 458  LEU A CG  1 
ATOM   3679  C  CD1 . LEU A 1 887  ? 131.890 133.323 146.168 1.00 53.12  ? 458  LEU A CD1 1 
ATOM   3680  C  CD2 . LEU A 1 887  ? 132.255 131.022 147.127 1.00 53.77  ? 458  LEU A CD2 1 
ATOM   3681  N  N   . TRP A 1 888  ? 131.291 134.834 150.634 1.00 42.76  ? 459  TRP A N   1 
ATOM   3682  C  CA  . TRP A 1 888  ? 130.028 135.009 151.332 1.00 56.55  ? 459  TRP A CA  1 
ATOM   3683  C  C   . TRP A 1 888  ? 129.519 136.438 151.205 1.00 60.17  ? 459  TRP A C   1 
ATOM   3684  O  O   . TRP A 1 888  ? 128.301 136.671 151.196 1.00 55.94  ? 459  TRP A O   1 
ATOM   3685  C  CB  . TRP A 1 888  ? 130.179 134.626 152.788 1.00 59.36  ? 459  TRP A CB  1 
ATOM   3686  C  CG  . TRP A 1 888  ? 131.172 135.451 153.429 1.00 60.74  ? 459  TRP A CG  1 
ATOM   3687  C  CD1 . TRP A 1 888  ? 132.496 135.177 153.554 1.00 70.92  ? 459  TRP A CD1 1 
ATOM   3688  C  CD2 . TRP A 1 888  ? 130.949 136.705 154.076 1.00 57.28  ? 459  TRP A CD2 1 
ATOM   3689  N  NE1 . TRP A 1 888  ? 133.123 136.191 154.236 1.00 76.57  ? 459  TRP A NE1 1 
ATOM   3690  C  CE2 . TRP A 1 888  ? 132.191 137.142 154.568 1.00 69.84  ? 459  TRP A CE2 1 
ATOM   3691  C  CE3 . TRP A 1 888  ? 129.822 137.502 154.286 1.00 55.85  ? 459  TRP A CE3 1 
ATOM   3692  C  CZ2 . TRP A 1 888  ? 132.339 138.345 155.260 1.00 78.89  ? 459  TRP A CZ2 1 
ATOM   3693  C  CZ3 . TRP A 1 888  ? 129.968 138.694 154.966 1.00 57.22  ? 459  TRP A CZ3 1 
ATOM   3694  C  CH2 . TRP A 1 888  ? 131.215 139.105 155.449 1.00 66.43  ? 459  TRP A CH2 1 
ATOM   3695  N  N   . GLU A 1 889  ? 130.431 137.403 151.092 1.00 58.67  ? 460  GLU A N   1 
ATOM   3696  C  CA  . GLU A 1 889  ? 129.990 138.784 151.001 1.00 52.83  ? 460  GLU A CA  1 
ATOM   3697  C  C   . GLU A 1 889  ? 129.024 138.961 149.856 1.00 44.73  ? 460  GLU A C   1 
ATOM   3698  O  O   . GLU A 1 889  ? 128.079 139.746 149.963 1.00 53.50  ? 460  GLU A O   1 
ATOM   3699  C  CB  . GLU A 1 889  ? 131.181 139.727 150.830 1.00 61.23  ? 460  GLU A CB  1 
ATOM   3700  C  CG  . GLU A 1 889  ? 132.140 139.740 152.023 1.00 72.82  ? 460  GLU A CG  1 
ATOM   3701  C  CD  . GLU A 1 889  ? 133.240 140.816 151.927 1.00 84.00  ? 460  GLU A CD  1 
ATOM   3702  O  OE1 . GLU A 1 889  ? 133.319 141.521 150.891 1.00 77.41  ? 460  GLU A OE1 1 
ATOM   3703  O  OE2 . GLU A 1 889  ? 134.035 140.947 152.894 1.00 82.68  ? 460  GLU A OE2 1 
ATOM   3704  N  N   . PHE A 1 890  ? 129.223 138.232 148.767 1.00 39.17  ? 461  PHE A N   1 
ATOM   3705  C  CA  . PHE A 1 890  ? 128.387 138.472 147.607 1.00 36.63  ? 461  PHE A CA  1 
ATOM   3706  C  C   . PHE A 1 890  ? 126.928 138.305 147.935 1.00 42.96  ? 461  PHE A C   1 
ATOM   3707  O  O   . PHE A 1 890  ? 126.073 138.872 147.250 1.00 52.28  ? 461  PHE A O   1 
ATOM   3708  C  CB  . PHE A 1 890  ? 128.744 137.532 146.491 1.00 37.46  ? 461  PHE A CB  1 
ATOM   3709  C  CG  . PHE A 1 890  ? 129.757 138.060 145.591 1.00 36.01  ? 461  PHE A CG  1 
ATOM   3710  C  CD1 . PHE A 1 890  ? 129.403 138.948 144.605 1.00 43.11  ? 461  PHE A CD1 1 
ATOM   3711  C  CD2 . PHE A 1 890  ? 131.069 137.648 145.699 1.00 52.42  ? 461  PHE A CD2 1 
ATOM   3712  C  CE1 . PHE A 1 890  ? 130.348 139.435 143.727 1.00 60.23  ? 461  PHE A CE1 1 
ATOM   3713  C  CE2 . PHE A 1 890  ? 132.034 138.129 144.834 1.00 64.80  ? 461  PHE A CE2 1 
ATOM   3714  C  CZ  . PHE A 1 890  ? 131.673 139.030 143.843 1.00 67.74  ? 461  PHE A CZ  1 
ATOM   3715  N  N   . TYR A 1 891  ? 126.614 137.525 148.959 1.00 42.11  ? 462  TYR A N   1 
ATOM   3716  C  CA  . TYR A 1 891  ? 125.211 137.327 149.269 1.00 43.06  ? 462  TYR A CA  1 
ATOM   3717  C  C   . TYR A 1 891  ? 124.529 138.646 149.559 1.00 51.90  ? 462  TYR A C   1 
ATOM   3718  O  O   . TYR A 1 891  ? 123.342 138.810 149.258 1.00 58.92  ? 462  TYR A O   1 
ATOM   3719  C  CB  . TYR A 1 891  ? 125.054 136.413 150.471 1.00 48.01  ? 462  TYR A CB  1 
ATOM   3720  C  CG  . TYR A 1 891  ? 123.621 136.186 150.767 1.00 40.31  ? 462  TYR A CG  1 
ATOM   3721  C  CD1 . TYR A 1 891  ? 122.945 137.005 151.649 1.00 45.68  ? 462  TYR A CD1 1 
ATOM   3722  C  CD2 . TYR A 1 891  ? 122.942 135.148 150.175 1.00 53.90  ? 462  TYR A CD2 1 
ATOM   3723  C  CE1 . TYR A 1 891  ? 121.623 136.825 151.912 1.00 53.24  ? 462  TYR A CE1 1 
ATOM   3724  C  CE2 . TYR A 1 891  ? 121.610 134.939 150.441 1.00 65.64  ? 462  TYR A CE2 1 
ATOM   3725  C  CZ  . TYR A 1 891  ? 120.952 135.785 151.311 1.00 66.02  ? 462  TYR A CZ  1 
ATOM   3726  O  OH  . TYR A 1 891  ? 119.614 135.580 151.576 1.00 72.92  ? 462  TYR A OH  1 
ATOM   3727  N  N   . HIS A 1 892  ? 125.264 139.593 150.143 1.00 52.07  ? 463  HIS A N   1 
ATOM   3728  C  CA  . HIS A 1 892  ? 124.711 140.838 150.650 1.00 43.04  ? 463  HIS A CA  1 
ATOM   3729  C  C   . HIS A 1 892  ? 124.623 141.941 149.613 1.00 46.07  ? 463  HIS A C   1 
ATOM   3730  O  O   . HIS A 1 892  ? 124.005 142.970 149.899 1.00 54.81  ? 463  HIS A O   1 
ATOM   3731  C  CB  . HIS A 1 892  ? 125.544 141.334 151.811 1.00 43.64  ? 463  HIS A CB  1 
ATOM   3732  C  CG  . HIS A 1 892  ? 125.383 140.524 153.050 1.00 47.27  ? 463  HIS A CG  1 
ATOM   3733  N  ND1 . HIS A 1 892  ? 124.193 140.456 153.737 1.00 48.99  ? 463  HIS A ND1 1 
ATOM   3734  C  CD2 . HIS A 1 892  ? 126.269 139.777 153.749 1.00 53.16  ? 463  HIS A CD2 1 
ATOM   3735  C  CE1 . HIS A 1 892  ? 124.348 139.690 154.801 1.00 55.05  ? 463  HIS A CE1 1 
ATOM   3736  N  NE2 . HIS A 1 892  ? 125.598 139.267 154.833 1.00 55.85  ? 463  HIS A NE2 1 
ATOM   3737  N  N   . LEU A 1 893  ? 125.219 141.774 148.437 1.00 45.48  ? 464  LEU A N   1 
ATOM   3738  C  CA  . LEU A 1 893  ? 125.068 142.781 147.394 1.00 44.77  ? 464  LEU A CA  1 
ATOM   3739  C  C   . LEU A 1 893  ? 123.621 142.872 146.951 1.00 56.94  ? 464  LEU A C   1 
ATOM   3740  O  O   . LEU A 1 893  ? 122.972 141.853 146.694 1.00 61.48  ? 464  LEU A O   1 
ATOM   3741  C  CB  . LEU A 1 893  ? 125.913 142.446 146.186 1.00 37.69  ? 464  LEU A CB  1 
ATOM   3742  C  CG  . LEU A 1 893  ? 127.370 142.525 146.538 1.00 51.09  ? 464  LEU A CG  1 
ATOM   3743  C  CD1 . LEU A 1 893  ? 128.112 142.281 145.262 1.00 61.05  ? 464  LEU A CD1 1 
ATOM   3744  C  CD2 . LEU A 1 893  ? 127.704 143.873 147.154 1.00 60.06  ? 464  LEU A CD2 1 
ATOM   3745  N  N   . ASP A 1 894  ? 123.124 144.094 146.833 1.00 54.51  ? 465  ASP A N   1 
ATOM   3746  C  CA  . ASP A 1 894  ? 121.806 144.345 146.280 1.00 51.03  ? 465  ASP A CA  1 
ATOM   3747  C  C   . ASP A 1 894  ? 121.952 145.426 145.221 1.00 52.51  ? 465  ASP A C   1 
ATOM   3748  O  O   . ASP A 1 894  ? 122.962 146.132 145.172 1.00 60.11  ? 465  ASP A O   1 
ATOM   3749  C  CB  . ASP A 1 894  ? 120.821 144.768 147.371 1.00 58.78  ? 465  ASP A CB  1 
ATOM   3750  C  CG  . ASP A 1 894  ? 119.370 144.601 146.952 1.00 71.92  ? 465  ASP A CG  1 
ATOM   3751  O  OD1 . ASP A 1 894  ? 119.115 144.184 145.799 1.00 69.19  ? 465  ASP A OD1 1 
ATOM   3752  O  OD2 . ASP A 1 894  ? 118.481 144.868 147.789 1.00 76.31  ? 465  ASP A OD2 1 
ATOM   3753  N  N   . HIS A 1 895  ? 120.949 145.557 144.368 1.00 48.01  ? 466  HIS A N   1 
ATOM   3754  C  CA  . HIS A 1 895  ? 121.033 146.493 143.259 1.00 44.40  ? 466  HIS A CA  1 
ATOM   3755  C  C   . HIS A 1 895  ? 119.671 146.563 142.572 1.00 52.65  ? 466  HIS A C   1 
ATOM   3756  O  O   . HIS A 1 895  ? 118.845 145.660 142.732 1.00 58.10  ? 466  HIS A O   1 
ATOM   3757  C  CB  . HIS A 1 895  ? 122.125 146.069 142.278 1.00 44.73  ? 466  HIS A CB  1 
ATOM   3758  C  CG  . HIS A 1 895  ? 122.028 144.640 141.889 1.00 48.13  ? 466  HIS A CG  1 
ATOM   3759  N  ND1 . HIS A 1 895  ? 121.103 144.180 140.980 1.00 49.43  ? 466  HIS A ND1 1 
ATOM   3760  C  CD2 . HIS A 1 895  ? 122.699 143.552 142.331 1.00 59.28  ? 466  HIS A CD2 1 
ATOM   3761  C  CE1 . HIS A 1 895  ? 121.220 142.870 140.863 1.00 56.85  ? 466  HIS A CE1 1 
ATOM   3762  N  NE2 . HIS A 1 895  ? 122.190 142.465 141.664 1.00 61.39  ? 466  HIS A NE2 1 
ATOM   3763  N  N   . PRO A 1 896  ? 119.413 147.625 141.826 1.00 40.79  ? 467  PRO A N   1 
ATOM   3764  C  CA  . PRO A 1 896  ? 118.152 147.743 141.106 1.00 33.20  ? 467  PRO A CA  1 
ATOM   3765  C  C   . PRO A 1 896  ? 118.116 146.763 139.957 1.00 36.31  ? 467  PRO A C   1 
ATOM   3766  O  O   . PRO A 1 896  ? 119.152 146.199 139.586 1.00 51.82  ? 467  PRO A O   1 
ATOM   3767  C  CB  . PRO A 1 896  ? 118.198 149.168 140.563 1.00 52.45  ? 467  PRO A CB  1 
ATOM   3768  C  CG  . PRO A 1 896  ? 119.667 149.448 140.465 1.00 55.32  ? 467  PRO A CG  1 
ATOM   3769  C  CD  . PRO A 1 896  ? 120.277 148.790 141.632 1.00 45.46  ? 467  PRO A CD  1 
ATOM   3770  N  N   . PRO A 1 897  ? 116.965 146.582 139.338 1.00 36.29  ? 468  PRO A N   1 
ATOM   3771  C  CA  . PRO A 1 897  ? 116.845 145.667 138.189 1.00 36.77  ? 468  PRO A CA  1 
ATOM   3772  C  C   . PRO A 1 897  ? 117.955 145.802 137.173 1.00 27.01  ? 468  PRO A C   1 
ATOM   3773  O  O   . PRO A 1 897  ? 118.276 146.894 136.735 1.00 36.91  ? 468  PRO A O   1 
ATOM   3774  C  CB  . PRO A 1 897  ? 115.503 146.064 137.571 1.00 52.68  ? 468  PRO A CB  1 
ATOM   3775  C  CG  . PRO A 1 897  ? 114.757 146.854 138.690 1.00 61.99  ? 468  PRO A CG  1 
ATOM   3776  C  CD  . PRO A 1 897  ? 115.670 147.019 139.871 1.00 46.74  ? 468  PRO A CD  1 
ATOM   3777  N  N   . LEU A 1 898  ? 118.539 144.675 136.795 1.00 29.07  ? 469  LEU A N   1 
ATOM   3778  C  CA  . LEU A 1 898  ? 119.684 144.695 135.907 1.00 31.61  ? 469  LEU A CA  1 
ATOM   3779  C  C   . LEU A 1 898  ? 119.370 144.243 134.503 1.00 39.65  ? 469  LEU A C   1 
ATOM   3780  O  O   . LEU A 1 898  ? 120.302 144.020 133.730 1.00 47.39  ? 469  LEU A O   1 
ATOM   3781  C  CB  . LEU A 1 898  ? 120.822 143.834 136.433 1.00 38.57  ? 469  LEU A CB  1 
ATOM   3782  C  CG  . LEU A 1 898  ? 121.433 144.250 137.763 1.00 48.00  ? 469  LEU A CG  1 
ATOM   3783  C  CD1 . LEU A 1 898  ? 122.642 143.373 138.081 1.00 55.17  ? 469  LEU A CD1 1 
ATOM   3784  C  CD2 . LEU A 1 898  ? 121.809 145.724 137.746 1.00 54.17  ? 469  LEU A CD2 1 
ATOM   3785  N  N   . PHE A 1 899  ? 118.099 144.077 134.153 1.00 46.38  ? 470  PHE A N   1 
ATOM   3786  C  CA  . PHE A 1 899  ? 117.733 143.722 132.783 1.00 53.17  ? 470  PHE A CA  1 
ATOM   3787  C  C   . PHE A 1 899  ? 116.320 144.194 132.503 1.00 51.23  ? 470  PHE A C   1 
ATOM   3788  O  O   . PHE A 1 899  ? 115.528 144.439 133.416 1.00 54.09  ? 470  PHE A O   1 
ATOM   3789  C  CB  . PHE A 1 899  ? 117.826 142.213 132.513 1.00 59.87  ? 470  PHE A CB  1 
ATOM   3790  C  CG  . PHE A 1 899  ? 119.214 141.647 132.696 1.00 64.92  ? 470  PHE A CG  1 
ATOM   3791  C  CD1 . PHE A 1 899  ? 120.173 141.802 131.703 1.00 69.58  ? 470  PHE A CD1 1 
ATOM   3792  C  CD2 . PHE A 1 899  ? 119.570 140.981 133.868 1.00 58.03  ? 470  PHE A CD2 1 
ATOM   3793  C  CE1 . PHE A 1 899  ? 121.461 141.291 131.870 1.00 71.28  ? 470  PHE A CE1 1 
ATOM   3794  C  CE2 . PHE A 1 899  ? 120.858 140.471 134.037 1.00 58.52  ? 470  PHE A CE2 1 
ATOM   3795  C  CZ  . PHE A 1 899  ? 121.801 140.622 133.037 1.00 61.97  ? 470  PHE A CZ  1 
ATOM   3796  N  N   . SER A 1 900  ? 116.007 144.316 131.230 1.00 47.85  ? 471  SER A N   1 
ATOM   3797  C  CA  . SER A 1 900  ? 114.723 144.894 130.902 1.00 55.27  ? 471  SER A CA  1 
ATOM   3798  C  C   . SER A 1 900  ? 113.683 143.800 130.780 1.00 54.65  ? 471  SER A C   1 
ATOM   3799  O  O   . SER A 1 900  ? 113.989 142.634 130.530 1.00 58.55  ? 471  SER A O   1 
ATOM   3800  C  CB  . SER A 1 900  ? 114.794 145.705 129.608 1.00 76.54  ? 471  SER A CB  1 
ATOM   3801  O  OG  . SER A 1 900  ? 113.535 146.287 129.294 1.00 76.96  ? 471  SER A OG  1 
ATOM   3802  N  N   . THR A 1 901  ? 112.442 144.193 130.980 1.00 57.85  ? 472  THR A N   1 
ATOM   3803  C  CA  . THR A 1 901  ? 111.331 143.272 130.879 1.00 61.61  ? 472  THR A CA  1 
ATOM   3804  C  C   . THR A 1 901  ? 110.764 143.219 129.475 1.00 66.73  ? 472  THR A C   1 
ATOM   3805  O  O   . THR A 1 901  ? 109.814 142.463 129.229 1.00 68.85  ? 472  THR A O   1 
ATOM   3806  C  CB  . THR A 1 901  ? 110.243 143.680 131.864 1.00 69.17  ? 472  THR A CB  1 
ATOM   3807  O  OG1 . THR A 1 901  ? 109.834 145.025 131.578 1.00 70.10  ? 472  THR A OG1 1 
ATOM   3808  C  CG2 . THR A 1 901  ? 110.786 143.606 133.292 1.00 65.62  ? 472  THR A CG2 1 
ATOM   3809  N  N   . LYS A 1 902  ? 111.329 143.995 128.549 1.00 62.98  ? 473  LYS A N   1 
ATOM   3810  C  CA  . LYS A 1 902  ? 110.890 144.020 127.153 1.00 60.61  ? 473  LYS A CA  1 
ATOM   3811  C  C   . LYS A 1 902  ? 112.110 143.889 126.258 1.00 45.94  ? 473  LYS A C   1 
ATOM   3812  O  O   . LYS A 1 902  ? 112.703 144.894 125.861 1.00 55.39  ? 473  LYS A O   1 
ATOM   3813  C  CB  . LYS A 1 902  ? 110.119 145.291 126.862 1.00 72.57  ? 473  LYS A CB  1 
ATOM   3814  C  CG  . LYS A 1 902  ? 110.709 146.533 127.519 1.00 77.57  ? 473  LYS A CG  1 
ATOM   3815  C  CD  . LYS A 1 902  ? 109.893 147.764 127.180 1.00 85.71  ? 473  LYS A CD  1 
ATOM   3816  C  CE  . LYS A 1 902  ? 110.491 149.011 127.815 1.00 95.00  ? 473  LYS A CE  1 
ATOM   3817  N  NZ  . LYS A 1 902  ? 110.619 148.905 129.295 1.00 95.04  ? 473  LYS A NZ  1 
ATOM   3818  N  N   . ILE A 1 903  ? 112.485 142.649 125.951 1.00 44.53  ? 474  ILE A N   1 
ATOM   3819  C  CA  . ILE A 1 903  ? 113.647 142.386 125.121 1.00 46.96  ? 474  ILE A CA  1 
ATOM   3820  C  C   . ILE A 1 903  ? 113.308 141.474 123.961 1.00 59.07  ? 474  ILE A C   1 
ATOM   3821  O  O   . ILE A 1 903  ? 114.178 141.190 123.137 1.00 65.73  ? 474  ILE A O   1 
ATOM   3822  C  CB  . ILE A 1 903  ? 114.810 141.781 125.947 1.00 70.33  ? 474  ILE A CB  1 
ATOM   3823  C  CG1 . ILE A 1 903  ? 115.055 142.580 127.227 1.00 78.62  ? 474  ILE A CG1 1 
ATOM   3824  C  CG2 . ILE A 1 903  ? 116.130 141.891 125.200 1.00 73.22  ? 474  ILE A CG2 1 
ATOM   3825  C  CD1 . ILE A 1 903  ? 116.080 141.988 128.191 1.00 76.89  ? 474  ILE A CD1 1 
ATOM   3826  N  N   . ILE A 1 904  ? 112.074 140.996 123.867 1.00 68.15  ? 475  ILE A N   1 
ATOM   3827  C  CA  . ILE A 1 904  ? 111.743 140.073 122.783 1.00 79.57  ? 475  ILE A CA  1 
ATOM   3828  C  C   . ILE A 1 904  ? 111.616 140.848 121.474 1.00 77.44  ? 475  ILE A C   1 
ATOM   3829  O  O   . ILE A 1 904  ? 110.995 141.915 121.412 1.00 76.45  ? 475  ILE A O   1 
ATOM   3830  C  CB  . ILE A 1 904  ? 110.454 139.269 123.051 1.00 84.25  ? 475  ILE A CB  1 
ATOM   3831  C  CG1 . ILE A 1 904  ? 109.270 140.224 123.120 1.00 80.34  ? 475  ILE A CG1 1 
ATOM   3832  C  CG2 . ILE A 1 904  ? 110.592 138.490 124.362 1.00 83.15  ? 475  ILE A CG2 1 
ATOM   3833  C  CD1 . ILE A 1 904  ? 107.953 139.573 122.785 1.00 83.42  ? 475  ILE A CD1 1 
ATOM   3834  N  N   . SER A 1 905  ? 112.206 140.307 120.413 1.00 79.44  ? 476  SER A N   1 
ATOM   3835  C  CA  . SER A 1 905  ? 112.160 140.927 119.094 1.00 81.07  ? 476  SER A CA  1 
ATOM   3836  C  C   . SER A 1 905  ? 111.468 140.048 118.067 1.00 85.39  ? 476  SER A C   1 
ATOM   3837  O  O   . SER A 1 905  ? 110.745 140.551 117.196 1.00 86.32  ? 476  SER A O   1 
ATOM   3838  C  CB  . SER A 1 905  ? 113.590 141.273 118.622 1.00 87.88  ? 476  SER A CB  1 
ATOM   3839  O  OG  . SER A 1 905  ? 114.414 140.115 118.596 1.00 87.89  ? 476  SER A OG  1 
ATOM   3840  N  N   . ASP A 1 906  ? 111.644 138.739 118.169 1.00 84.66  ? 477  ASP A N   1 
ATOM   3841  C  CA  . ASP A 1 906  ? 110.986 137.798 117.273 1.00 84.85  ? 477  ASP A CA  1 
ATOM   3842  C  C   . ASP A 1 906  ? 109.668 137.399 117.919 1.00 74.00  ? 477  ASP A C   1 
ATOM   3843  O  O   . ASP A 1 906  ? 109.626 136.510 118.770 1.00 76.70  ? 477  ASP A O   1 
ATOM   3844  C  CB  . ASP A 1 906  ? 111.881 136.591 117.013 1.00 96.83  ? 477  ASP A CB  1 
ATOM   3845  C  CG  . ASP A 1 906  ? 113.185 136.969 116.312 1.00 107.59 ? 477  ASP A CG  1 
ATOM   3846  O  OD1 . ASP A 1 906  ? 113.382 138.170 116.006 1.00 97.85  ? 477  ASP A OD1 1 
ATOM   3847  O  OD2 . ASP A 1 906  ? 114.007 136.059 116.056 1.00 106.95 ? 477  ASP A OD2 1 
ATOM   3848  N  N   . LEU A 1 907  ? 108.583 138.057 117.518 1.00 68.27  ? 478  LEU A N   1 
ATOM   3849  C  CA  . LEU A 1 907  ? 107.274 137.694 118.042 1.00 64.03  ? 478  LEU A CA  1 
ATOM   3850  C  C   . LEU A 1 907  ? 106.849 136.299 117.612 1.00 69.65  ? 478  LEU A C   1 
ATOM   3851  O  O   . LEU A 1 907  ? 105.873 135.766 118.158 1.00 70.82  ? 478  LEU A O   1 
ATOM   3852  C  CB  . LEU A 1 907  ? 106.220 138.688 117.575 1.00 77.94  ? 478  LEU A CB  1 
ATOM   3853  C  CG  . LEU A 1 907  ? 106.363 140.146 118.014 1.00 87.23  ? 478  LEU A CG  1 
ATOM   3854  C  CD1 . LEU A 1 907  ? 105.351 141.050 117.253 1.00 87.36  ? 478  LEU A CD1 1 
ATOM   3855  C  CD2 . LEU A 1 907  ? 106.259 140.281 119.543 1.00 82.55  ? 478  LEU A CD2 1 
ATOM   3856  N  N   . SER A 1 908  ? 107.553 135.703 116.642 1.00 70.78  ? 479  SER A N   1 
ATOM   3857  C  CA  . SER A 1 908  ? 107.220 134.371 116.151 1.00 64.92  ? 479  SER A CA  1 
ATOM   3858  C  C   . SER A 1 908  ? 107.317 133.307 117.236 1.00 66.49  ? 479  SER A C   1 
ATOM   3859  O  O   . SER A 1 908  ? 106.735 132.231 117.082 1.00 65.78  ? 479  SER A O   1 
ATOM   3860  C  CB  . SER A 1 908  ? 108.139 134.006 114.990 1.00 65.55  ? 479  SER A CB  1 
ATOM   3861  O  OG  . SER A 1 908  ? 108.086 135.001 113.979 1.00 66.33  ? 479  SER A OG  1 
ATOM   3862  N  N   . ILE A 1 909  ? 108.041 133.577 118.327 1.00 72.25  ? 480  ILE A N   1 
ATOM   3863  C  CA  . ILE A 1 909  ? 108.094 132.614 119.421 1.00 66.36  ? 480  ILE A CA  1 
ATOM   3864  C  C   . ILE A 1 909  ? 106.710 132.420 120.002 1.00 55.83  ? 480  ILE A C   1 
ATOM   3865  O  O   . ILE A 1 909  ? 106.363 131.321 120.444 1.00 62.96  ? 480  ILE A O   1 
ATOM   3866  C  CB  . ILE A 1 909  ? 109.094 133.046 120.515 1.00 66.23  ? 480  ILE A CB  1 
ATOM   3867  C  CG1 . ILE A 1 909  ? 108.691 134.382 121.136 1.00 60.89  ? 480  ILE A CG1 1 
ATOM   3868  C  CG2 . ILE A 1 909  ? 110.536 133.110 119.955 1.00 64.30  ? 480  ILE A CG2 1 
ATOM   3869  C  CD1 . ILE A 1 909  ? 109.651 134.853 122.239 1.00 68.26  ? 480  ILE A CD1 1 
ATOM   3870  N  N   . PHE A 1 910  ? 105.900 133.466 120.011 1.00 53.43  ? 481  PHE A N   1 
ATOM   3871  C  CA  . PHE A 1 910  ? 104.578 133.326 120.588 1.00 56.44  ? 481  PHE A CA  1 
ATOM   3872  C  C   . PHE A 1 910  ? 103.580 132.712 119.619 1.00 59.34  ? 481  PHE A C   1 
ATOM   3873  O  O   . PHE A 1 910  ? 102.514 132.269 120.058 1.00 62.06  ? 481  PHE A O   1 
ATOM   3874  C  CB  . PHE A 1 910  ? 104.097 134.686 121.086 1.00 60.02  ? 481  PHE A CB  1 
ATOM   3875  C  CG  . PHE A 1 910  ? 104.866 135.194 122.272 1.00 51.24  ? 481  PHE A CG  1 
ATOM   3876  C  CD1 . PHE A 1 910  ? 105.976 135.982 122.106 1.00 53.54  ? 481  PHE A CD1 1 
ATOM   3877  C  CD2 . PHE A 1 910  ? 104.458 134.890 123.548 1.00 50.79  ? 481  PHE A CD2 1 
ATOM   3878  C  CE1 . PHE A 1 910  ? 106.677 136.436 123.187 1.00 57.46  ? 481  PHE A CE1 1 
ATOM   3879  C  CE2 . PHE A 1 910  ? 105.151 135.347 124.633 1.00 52.28  ? 481  PHE A CE2 1 
ATOM   3880  C  CZ  . PHE A 1 910  ? 106.265 136.121 124.454 1.00 54.93  ? 481  PHE A CZ  1 
ATOM   3881  N  N   . ILE A 1 911  ? 103.913 132.657 118.329 1.00 62.22  ? 482  ILE A N   1 
ATOM   3882  C  CA  . ILE A 1 911  ? 103.102 131.989 117.310 1.00 58.26  ? 482  ILE A CA  1 
ATOM   3883  C  C   . ILE A 1 911  ? 103.733 130.687 116.835 1.00 58.33  ? 482  ILE A C   1 
ATOM   3884  O  O   . ILE A 1 911  ? 103.041 129.884 116.189 1.00 62.52  ? 482  ILE A O   1 
ATOM   3885  C  CB  . ILE A 1 911  ? 102.838 132.925 116.100 1.00 71.09  ? 482  ILE A CB  1 
ATOM   3886  C  CG1 . ILE A 1 911  ? 101.615 132.511 115.258 1.00 70.09  ? 482  ILE A CG1 1 
ATOM   3887  C  CG2 . ILE A 1 911  ? 104.071 133.052 115.190 1.00 75.19  ? 482  ILE A CG2 1 
ATOM   3888  C  CD1 . ILE A 1 911  ? 100.278 132.757 115.906 1.00 69.01  ? 482  ILE A CD1 1 
ATOM   3889  N  N   . LYS A 1 912  ? 105.013 130.451 117.145 1.00 67.81  ? 483  LYS A N   1 
ATOM   3890  C  CA  . LYS A 1 912  ? 105.741 129.291 116.645 1.00 62.53  ? 483  LYS A CA  1 
ATOM   3891  C  C   . LYS A 1 912  ? 104.926 128.039 116.904 1.00 67.21  ? 483  LYS A C   1 
ATOM   3892  O  O   . LYS A 1 912  ? 104.495 127.794 118.031 1.00 73.93  ? 483  LYS A O   1 
ATOM   3893  C  CB  . LYS A 1 912  ? 107.107 129.191 117.338 1.00 57.66  ? 483  LYS A CB  1 
ATOM   3894  C  CG  . LYS A 1 912  ? 108.017 128.101 116.810 1.00 67.31  ? 483  LYS A CG  1 
ATOM   3895  C  CD  . LYS A 1 912  ? 107.927 126.829 117.657 1.00 86.81  ? 483  LYS A CD  1 
ATOM   3896  C  CE  . LYS A 1 912  ? 108.271 127.097 119.119 1.00 94.01  ? 483  LYS A CE  1 
ATOM   3897  N  NZ  . LYS A 1 912  ? 108.037 125.893 119.978 1.00 88.24  ? 483  LYS A NZ  1 
ATOM   3898  N  N   . ASP A 1 913  ? 104.708 127.256 115.852 1.00 75.34  ? 484  ASP A N   1 
ATOM   3899  C  CA  . ASP A 1 913  ? 103.741 126.165 115.905 1.00 77.62  ? 484  ASP A CA  1 
ATOM   3900  C  C   . ASP A 1 913  ? 104.192 125.047 116.847 1.00 84.42  ? 484  ASP A C   1 
ATOM   3901  O  O   . ASP A 1 913  ? 105.358 124.637 116.842 1.00 87.88  ? 484  ASP A O   1 
ATOM   3902  C  CB  . ASP A 1 913  ? 103.515 125.610 114.502 1.00 85.50  ? 484  ASP A CB  1 
ATOM   3903  C  CG  . ASP A 1 913  ? 102.137 125.005 114.333 1.00 96.16  ? 484  ASP A CG  1 
ATOM   3904  O  OD1 . ASP A 1 913  ? 101.576 124.536 115.348 1.00 92.72  ? 484  ASP A OD1 1 
ATOM   3905  O  OD2 . ASP A 1 913  ? 101.612 125.005 113.193 1.00 95.96  ? 484  ASP A OD2 1 
ATOM   3906  N  N   . ARG A 1 914  ? 103.249 124.555 117.653 1.00 83.54  ? 485  ARG A N   1 
ATOM   3907  C  CA  . ARG A 1 914  ? 103.469 123.527 118.675 1.00 83.69  ? 485  ARG A CA  1 
ATOM   3908  C  C   . ARG A 1 914  ? 102.107 123.162 119.272 1.00 79.93  ? 485  ARG A C   1 
ATOM   3909  O  O   . ARG A 1 914  ? 101.059 123.614 118.798 1.00 79.58  ? 485  ARG A O   1 
ATOM   3910  C  CB  . ARG A 1 914  ? 104.454 123.997 119.754 1.00 80.14  ? 485  ARG A CB  1 
ATOM   3911  C  CG  . ARG A 1 914  ? 103.935 125.172 120.570 1.00 79.51  ? 485  ARG A CG  1 
ATOM   3912  C  CD  . ARG A 1 914  ? 104.861 125.550 121.719 1.00 90.84  ? 485  ARG A CD  1 
ATOM   3913  N  NE  . ARG A 1 914  ? 104.431 126.811 122.336 1.00 95.63  ? 485  ARG A NE  1 
ATOM   3914  C  CZ  . ARG A 1 914  ? 104.947 128.011 122.058 1.00 100.35 ? 485  ARG A CZ  1 
ATOM   3915  N  NH1 . ARG A 1 914  ? 105.953 128.132 121.188 1.00 91.88  ? 485  ARG A NH1 1 
ATOM   3916  N  NH2 . ARG A 1 914  ? 104.470 129.095 122.670 1.00 87.59  ? 485  ARG A NH2 1 
ATOM   3917  N  N   . ALA A 1 915  ? 102.125 122.319 120.301 1.00 71.44  ? 486  ALA A N   1 
ATOM   3918  C  CA  . ALA A 1 915  ? 100.927 121.999 121.063 1.00 60.20  ? 486  ALA A CA  1 
ATOM   3919  C  C   . ALA A 1 915  ? 101.084 122.453 122.510 1.00 49.37  ? 486  ALA A C   1 
ATOM   3920  O  O   . ALA A 1 915  ? 102.196 122.571 123.035 1.00 49.83  ? 486  ALA A O   1 
ATOM   3921  C  CB  . ALA A 1 915  ? 100.617 120.498 121.009 1.00 62.81  ? 486  ALA A CB  1 
ATOM   3922  N  N   . THR A 1 916  ? 99.954  122.727 123.140 1.00 37.73  ? 487  THR A N   1 
ATOM   3923  C  CA  . THR A 1 916  ? 99.912  123.160 124.521 1.00 27.12  ? 487  THR A CA  1 
ATOM   3924  C  C   . THR A 1 916  ? 98.795  122.410 125.218 1.00 23.78  ? 487  THR A C   1 
ATOM   3925  O  O   . THR A 1 916  ? 97.816  122.010 124.591 1.00 37.60  ? 487  THR A O   1 
ATOM   3926  C  CB  . THR A 1 916  ? 99.654  124.643 124.611 1.00 39.37  ? 487  THR A CB  1 
ATOM   3927  O  OG1 . THR A 1 916  ? 98.399  124.936 123.979 1.00 45.33  ? 487  THR A OG1 1 
ATOM   3928  C  CG2 . THR A 1 916  ? 100.759 125.415 123.888 1.00 51.38  ? 487  THR A CG2 1 
ATOM   3929  N  N   . ALA A 1 917  ? 98.932  122.214 126.507 1.00 17.49  ? 488  ALA A N   1 
ATOM   3930  C  CA  . ALA A 1 917  ? 97.918  121.439 127.180 1.00 16.59  ? 488  ALA A CA  1 
ATOM   3931  C  C   . ALA A 1 917  ? 96.622  122.205 127.195 1.00 15.27  ? 488  ALA A C   1 
ATOM   3932  O  O   . ALA A 1 917  ? 96.607  123.426 127.261 1.00 23.49  ? 488  ALA A O   1 
ATOM   3933  C  CB  . ALA A 1 917  ? 98.341  121.124 128.597 1.00 30.45  ? 488  ALA A CB  1 
ATOM   3934  N  N   . VAL A 1 918  ? 95.531  121.487 127.111 1.00 15.30  ? 489  VAL A N   1 
ATOM   3935  C  CA  . VAL A 1 918  ? 94.274  122.122 127.310 1.00 15.30  ? 489  VAL A CA  1 
ATOM   3936  C  C   . VAL A 1 918  ? 94.116  122.439 128.775 1.00 21.22  ? 489  VAL A C   1 
ATOM   3937  O  O   . VAL A 1 918  ? 94.676  121.767 129.644 1.00 29.33  ? 489  VAL A O   1 
ATOM   3938  C  CB  . VAL A 1 918  ? 93.162  121.188 126.854 1.00 31.28  ? 489  VAL A CB  1 
ATOM   3939  C  CG1 . VAL A 1 918  ? 93.148  121.128 125.356 1.00 61.03  ? 489  VAL A CG1 1 
ATOM   3940  C  CG2 . VAL A 1 918  ? 93.384  119.825 127.468 1.00 33.53  ? 489  VAL A CG2 1 
ATOM   3941  N  N   . GLU A 1 919  ? 93.280  123.431 129.055 1.00 25.15  ? 490  GLU A N   1 
ATOM   3942  C  CA  . GLU A 1 919  ? 93.069  123.917 130.411 1.00 22.46  ? 490  GLU A CA  1 
ATOM   3943  C  C   . GLU A 1 919  ? 92.521  122.817 131.301 1.00 25.81  ? 490  GLU A C   1 
ATOM   3944  O  O   . GLU A 1 919  ? 92.022  121.801 130.827 1.00 37.81  ? 490  GLU A O   1 
ATOM   3945  C  CB  . GLU A 1 919  ? 92.075  125.049 130.387 1.00 46.42  ? 490  GLU A CB  1 
ATOM   3946  C  CG  . GLU A 1 919  ? 92.596  126.279 129.661 1.00 68.35  ? 490  GLU A CG  1 
ATOM   3947  C  CD  . GLU A 1 919  ? 91.513  127.340 129.463 1.00 82.97  ? 490  GLU A CD  1 
ATOM   3948  O  OE1 . GLU A 1 919  ? 91.527  128.001 128.400 1.00 76.65  ? 490  GLU A OE1 1 
ATOM   3949  O  OE2 . GLU A 1 919  ? 90.640  127.500 130.349 1.00 73.97  ? 490  GLU A OE2 1 
ATOM   3950  N  N   . ARG A 1 920  ? 92.600  123.035 132.613 1.00 26.56  ? 491  ARG A N   1 
ATOM   3951  C  CA  . ARG A 1 920  ? 92.242  121.992 133.576 1.00 31.09  ? 491  ARG A CA  1 
ATOM   3952  C  C   . ARG A 1 920  ? 90.772  121.605 133.511 1.00 40.60  ? 491  ARG A C   1 
ATOM   3953  O  O   . ARG A 1 920  ? 90.430  120.445 133.766 1.00 43.85  ? 491  ARG A O   1 
ATOM   3954  C  CB  . ARG A 1 920  ? 92.565  122.454 134.992 1.00 39.24  ? 491  ARG A CB  1 
ATOM   3955  C  CG  . ARG A 1 920  ? 92.687  121.348 136.030 1.00 42.55  ? 491  ARG A CG  1 
ATOM   3956  C  CD  . ARG A 1 920  ? 91.412  121.156 136.866 1.00 36.16  ? 491  ARG A CD  1 
ATOM   3957  N  NE  . ARG A 1 920  ? 91.712  120.189 137.912 1.00 52.80  ? 491  ARG A NE  1 
ATOM   3958  C  CZ  . ARG A 1 920  ? 91.719  118.871 137.725 1.00 67.05  ? 491  ARG A CZ  1 
ATOM   3959  N  NH1 . ARG A 1 920  ? 91.389  118.371 136.537 1.00 58.51  ? 491  ARG A NH1 1 
ATOM   3960  N  NH2 . ARG A 1 920  ? 92.038  118.048 138.726 1.00 65.80  ? 491  ARG A NH2 1 
ATOM   3961  N  N   . THR A 1 921  ? 89.887  122.552 133.219 1.00 35.39  ? 492  THR A N   1 
ATOM   3962  C  CA  . THR A 1 921  ? 88.480  122.209 133.220 1.00 24.76  ? 492  THR A CA  1 
ATOM   3963  C  C   . THR A 1 921  ? 88.167  121.183 132.152 1.00 35.30  ? 492  THR A C   1 
ATOM   3964  O  O   . THR A 1 921  ? 87.252  120.374 132.322 1.00 49.48  ? 492  THR A O   1 
ATOM   3965  C  CB  . THR A 1 921  ? 87.648  123.463 133.026 1.00 36.19  ? 492  THR A CB  1 
ATOM   3966  O  OG1 . THR A 1 921  ? 88.107  124.480 133.927 1.00 34.20  ? 492  THR A OG1 1 
ATOM   3967  C  CG2 . THR A 1 921  ? 86.176  123.174 133.291 1.00 57.28  ? 492  THR A CG2 1 
ATOM   3968  N  N   . CYS A 1 922  ? 88.929  121.166 131.073 1.00 33.82  ? 493  CYS A N   1 
ATOM   3969  C  CA  . CYS A 1 922  ? 88.703  120.254 129.961 1.00 32.57  ? 493  CYS A CA  1 
ATOM   3970  C  C   . CYS A 1 922  ? 89.936  119.399 129.689 1.00 39.02  ? 493  CYS A C   1 
ATOM   3971  O  O   . CYS A 1 922  ? 90.271  119.113 128.536 1.00 45.37  ? 493  CYS A O   1 
ATOM   3972  C  CB  . CYS A 1 922  ? 88.313  121.034 128.710 1.00 50.46  ? 493  CYS A CB  1 
ATOM   3973  S  SG  . CYS A 1 922  ? 89.531  122.330 128.258 1.00 70.77  ? 493  CYS A SG  1 
ATOM   3974  N  N   . TRP A 1 923  ? 90.632  118.976 130.750 1.00 36.76  ? 494  TRP A N   1 
ATOM   3975  C  CA  . TRP A 1 923  ? 91.900  118.265 130.576 1.00 32.34  ? 494  TRP A CA  1 
ATOM   3976  C  C   . TRP A 1 923  ? 91.724  116.932 129.878 1.00 34.25  ? 494  TRP A C   1 
ATOM   3977  O  O   . TRP A 1 923  ? 92.595  116.521 129.103 1.00 41.23  ? 494  TRP A O   1 
ATOM   3978  C  CB  . TRP A 1 923  ? 92.585  118.076 131.925 1.00 34.06  ? 494  TRP A CB  1 
ATOM   3979  C  CG  . TRP A 1 923  ? 91.885  117.120 132.819 1.00 35.43  ? 494  TRP A CG  1 
ATOM   3980  C  CD1 . TRP A 1 923  ? 90.832  117.394 133.632 1.00 43.65  ? 494  TRP A CD1 1 
ATOM   3981  C  CD2 . TRP A 1 923  ? 92.170  115.733 132.993 1.00 35.78  ? 494  TRP A CD2 1 
ATOM   3982  N  NE1 . TRP A 1 923  ? 90.451  116.270 134.311 1.00 39.47  ? 494  TRP A NE1 1 
ATOM   3983  C  CE2 . TRP A 1 923  ? 91.258  115.236 133.931 1.00 29.98  ? 494  TRP A CE2 1 
ATOM   3984  C  CE3 . TRP A 1 923  ? 93.115  114.863 132.444 1.00 49.41  ? 494  TRP A CE3 1 
ATOM   3985  C  CZ2 . TRP A 1 923  ? 91.249  113.917 134.326 1.00 39.97  ? 494  TRP A CZ2 1 
ATOM   3986  C  CZ3 . TRP A 1 923  ? 93.108  113.542 132.847 1.00 43.49  ? 494  TRP A CZ3 1 
ATOM   3987  C  CH2 . TRP A 1 923  ? 92.179  113.084 133.778 1.00 40.84  ? 494  TRP A CH2 1 
ATOM   3988  N  N   . ASP A 1 924  ? 90.623  116.246 130.133 1.00 34.31  ? 495  ASP A N   1 
ATOM   3989  C  CA  . ASP A 1 924  ? 90.398  114.939 129.559 1.00 28.01  ? 495  ASP A CA  1 
ATOM   3990  C  C   . ASP A 1 924  ? 89.790  115.029 128.213 1.00 25.99  ? 495  ASP A C   1 
ATOM   3991  O  O   . ASP A 1 924  ? 89.305  114.025 127.701 1.00 40.89  ? 495  ASP A O   1 
ATOM   3992  C  CB  . ASP A 1 924  ? 89.467  114.150 130.426 1.00 35.31  ? 495  ASP A CB  1 
ATOM   3993  C  CG  . ASP A 1 924  ? 88.150  114.809 130.506 1.00 45.54  ? 495  ASP A CG  1 
ATOM   3994  O  OD1 . ASP A 1 924  ? 88.151  116.058 130.555 1.00 43.52  ? 495  ASP A OD1 1 
ATOM   3995  O  OD2 . ASP A 1 924  ? 87.120  114.106 130.516 1.00 60.00  ? 495  ASP A OD2 1 
ATOM   3996  N  N   . ALA A 1 925  ? 89.742  116.204 127.647 1.00 27.91  ? 496  ALA A N   1 
ATOM   3997  C  CA  . ALA A 1 925  ? 89.258  116.244 126.295 1.00 31.84  ? 496  ALA A CA  1 
ATOM   3998  C  C   . ALA A 1 925  ? 90.235  115.624 125.331 1.00 27.61  ? 496  ALA A C   1 
ATOM   3999  O  O   . ALA A 1 925  ? 89.841  115.323 124.207 1.00 43.50  ? 496  ALA A O   1 
ATOM   4000  C  CB  . ALA A 1 925  ? 88.967  117.678 125.874 1.00 48.11  ? 496  ALA A CB  1 
ATOM   4001  N  N   . VAL A 1 926  ? 91.486  115.413 125.721 1.00 23.80  ? 497  VAL A N   1 
ATOM   4002  C  CA  . VAL A 1 926  ? 92.423  114.912 124.727 1.00 31.87  ? 497  VAL A CA  1 
ATOM   4003  C  C   . VAL A 1 926  ? 92.247  113.430 124.441 1.00 38.92  ? 497  VAL A C   1 
ATOM   4004  O  O   . VAL A 1 926  ? 92.620  112.982 123.360 1.00 46.27  ? 497  VAL A O   1 
ATOM   4005  C  CB  . VAL A 1 926  ? 93.886  115.160 125.118 1.00 47.17  ? 497  VAL A CB  1 
ATOM   4006  C  CG1 . VAL A 1 926  ? 94.199  116.659 125.104 1.00 56.32  ? 497  VAL A CG1 1 
ATOM   4007  C  CG2 . VAL A 1 926  ? 94.194  114.552 126.492 1.00 54.80  ? 497  VAL A CG2 1 
ATOM   4008  N  N   . PHE A 1 927  ? 91.695  112.654 125.362 1.00 38.69  ? 498  PHE A N   1 
ATOM   4009  C  CA  . PHE A 1 927  ? 91.486  111.232 125.133 1.00 37.17  ? 498  PHE A CA  1 
ATOM   4010  C  C   . PHE A 1 927  ? 90.193  110.989 124.388 1.00 48.32  ? 498  PHE A C   1 
ATOM   4011  O  O   . PHE A 1 927  ? 89.190  111.662 124.646 1.00 55.57  ? 498  PHE A O   1 
ATOM   4012  C  CB  . PHE A 1 927  ? 91.449  110.503 126.461 1.00 42.99  ? 498  PHE A CB  1 
ATOM   4013  C  CG  . PHE A 1 927  ? 92.438  111.029 127.432 1.00 43.72  ? 498  PHE A CG  1 
ATOM   4014  C  CD1 . PHE A 1 927  ? 93.796  110.851 127.210 1.00 46.02  ? 498  PHE A CD1 1 
ATOM   4015  C  CD2 . PHE A 1 927  ? 92.028  111.744 128.538 1.00 49.44  ? 498  PHE A CD2 1 
ATOM   4016  C  CE1 . PHE A 1 927  ? 94.744  111.342 128.102 1.00 50.61  ? 498  PHE A CE1 1 
ATOM   4017  C  CE2 . PHE A 1 927  ? 92.960  112.254 129.439 1.00 53.80  ? 498  PHE A CE2 1 
ATOM   4018  C  CZ  . PHE A 1 927  ? 94.327  112.051 129.221 1.00 55.96  ? 498  PHE A CZ  1 
ATOM   4019  N  N   . GLU A 1 928  ? 90.201  109.999 123.468 1.00 47.55  ? 499  GLU A N   1 
ATOM   4020  C  CA  . GLU A 1 928  ? 89.020  109.926 122.622 1.00 44.81  ? 499  GLU A CA  1 
ATOM   4021  C  C   . GLU A 1 928  ? 87.875  109.256 123.366 1.00 33.82  ? 499  GLU A C   1 
ATOM   4022  O  O   . GLU A 1 928  ? 88.097  108.323 124.129 1.00 51.44  ? 499  GLU A O   1 
ATOM   4023  C  CB  . GLU A 1 928  ? 89.310  109.155 121.369 1.00 44.38  ? 499  GLU A CB  1 
ATOM   4024  C  CG  . GLU A 1 928  ? 89.590  107.731 121.573 1.00 52.56  ? 499  GLU A CG  1 
ATOM   4025  C  CD  . GLU A 1 928  ? 88.284  106.953 121.466 1.00 66.99  ? 499  GLU A CD  1 
ATOM   4026  O  OE1 . GLU A 1 928  ? 87.304  107.538 120.928 1.00 61.02  ? 499  GLU A OE1 1 
ATOM   4027  O  OE2 . GLU A 1 928  ? 88.256  105.749 121.809 1.00 65.16  ? 499  GLU A OE2 1 
ATOM   4028  N  N   . PRO A 1 929  ? 86.644  109.691 123.136 1.00 31.23  ? 500  PRO A N   1 
ATOM   4029  C  CA  . PRO A 1 929  ? 85.568  109.392 124.096 1.00 41.49  ? 500  PRO A CA  1 
ATOM   4030  C  C   . PRO A 1 929  ? 85.250  107.916 124.277 1.00 53.09  ? 500  PRO A C   1 
ATOM   4031  O  O   . PRO A 1 929  ? 84.853  107.515 125.383 1.00 52.77  ? 500  PRO A O   1 
ATOM   4032  C  CB  . PRO A 1 929  ? 84.365  110.149 123.520 1.00 56.02  ? 500  PRO A CB  1 
ATOM   4033  C  CG  . PRO A 1 929  ? 84.966  111.222 122.676 1.00 60.11  ? 500  PRO A CG  1 
ATOM   4034  C  CD  . PRO A 1 929  ? 86.204  110.600 122.078 1.00 49.77  ? 500  PRO A CD  1 
ATOM   4035  N  N   . ASN A 1 930  ? 85.395  107.096 123.231 1.00 55.51  ? 501  ASN A N   1 
ATOM   4036  C  CA  . ASN A 1 930  ? 85.079  105.671 123.350 1.00 54.68  ? 501  ASN A CA  1 
ATOM   4037  C  C   . ASN A 1 930  ? 86.057  104.942 124.281 1.00 56.78  ? 501  ASN A C   1 
ATOM   4038  O  O   . ASN A 1 930  ? 85.629  104.172 125.151 1.00 59.05  ? 501  ASN A O   1 
ATOM   4039  C  CB  . ASN A 1 930  ? 85.052  105.027 121.961 1.00 57.06  ? 501  ASN A CB  1 
ATOM   4040  C  CG  . ASN A 1 930  ? 83.962  105.613 121.064 1.00 59.17  ? 501  ASN A CG  1 
ATOM   4041  O  OD1 . ASN A 1 930  ? 84.251  106.228 120.028 1.00 59.15  ? 501  ASN A OD1 1 
ATOM   4042  N  ND2 . ASN A 1 930  ? 82.703  105.382 121.435 1.00 55.83  ? 501  ASN A ND2 1 
ATOM   4043  N  N   . VAL A 1 931  ? 87.372  105.154 124.112 1.00 44.68  ? 502  VAL A N   1 
ATOM   4044  C  CA  . VAL A 1 931  ? 88.324  104.547 125.042 1.00 35.08  ? 502  VAL A CA  1 
ATOM   4045  C  C   . VAL A 1 931  ? 88.211  105.188 126.407 1.00 42.10  ? 502  VAL A C   1 
ATOM   4046  O  O   . VAL A 1 931  ? 88.390  104.523 127.436 1.00 47.97  ? 502  VAL A O   1 
ATOM   4047  C  CB  . VAL A 1 931  ? 89.760  104.630 124.521 1.00 36.92  ? 502  VAL A CB  1 
ATOM   4048  C  CG1 . VAL A 1 931  ? 90.725  104.261 125.629 1.00 42.46  ? 502  VAL A CG1 1 
ATOM   4049  C  CG2 . VAL A 1 931  ? 89.937  103.664 123.380 1.00 49.72  ? 502  VAL A CG2 1 
ATOM   4050  N  N   . LEU A 1 932  ? 87.906  106.480 126.445 1.00 43.18  ? 503  LEU A N   1 
ATOM   4051  C  CA  . LEU A 1 932  ? 87.730  107.163 127.714 1.00 36.54  ? 503  LEU A CA  1 
ATOM   4052  C  C   . LEU A 1 932  ? 86.537  106.616 128.460 1.00 33.97  ? 503  LEU A C   1 
ATOM   4053  O  O   . LEU A 1 932  ? 86.545  106.569 129.690 1.00 42.35  ? 503  LEU A O   1 
ATOM   4054  C  CB  . LEU A 1 932  ? 87.568  108.654 127.468 1.00 47.36  ? 503  LEU A CB  1 
ATOM   4055  C  CG  . LEU A 1 932  ? 87.651  109.580 128.669 1.00 58.76  ? 503  LEU A CG  1 
ATOM   4056  C  CD1 . LEU A 1 932  ? 88.967  109.317 129.383 1.00 58.34  ? 503  LEU A CD1 1 
ATOM   4057  C  CD2 . LEU A 1 932  ? 87.553  111.047 128.216 1.00 58.45  ? 503  LEU A CD2 1 
ATOM   4058  N  N   . GLY A 1 933  ? 85.517  106.176 127.746 1.00 35.58  ? 504  GLY A N   1 
ATOM   4059  C  CA  . GLY A 1 933  ? 84.394  105.543 128.396 1.00 40.46  ? 504  GLY A CA  1 
ATOM   4060  C  C   . GLY A 1 933  ? 83.295  106.475 128.855 1.00 47.54  ? 504  GLY A C   1 
ATOM   4061  O  O   . GLY A 1 933  ? 82.313  106.002 129.440 1.00 50.09  ? 504  GLY A O   1 
ATOM   4062  N  N   . TYR A 1 934  ? 83.427  107.777 128.626 1.00 46.70  ? 505  TYR A N   1 
ATOM   4063  C  CA  . TYR A 1 934  ? 82.370  108.743 128.900 1.00 45.57  ? 505  TYR A CA  1 
ATOM   4064  C  C   . TYR A 1 934  ? 82.647  109.972 128.055 1.00 54.47  ? 505  TYR A C   1 
ATOM   4065  O  O   . TYR A 1 934  ? 83.790  110.232 127.669 1.00 59.47  ? 505  TYR A O   1 
ATOM   4066  C  CB  . TYR A 1 934  ? 82.299  109.126 130.379 1.00 50.74  ? 505  TYR A CB  1 
ATOM   4067  C  CG  . TYR A 1 934  ? 83.587  109.742 130.864 1.00 58.39  ? 505  TYR A CG  1 
ATOM   4068  C  CD1 . TYR A 1 934  ? 83.801  111.116 130.807 1.00 64.78  ? 505  TYR A CD1 1 
ATOM   4069  C  CD2 . TYR A 1 934  ? 84.610  108.944 131.365 1.00 63.26  ? 505  TYR A CD2 1 
ATOM   4070  C  CE1 . TYR A 1 934  ? 85.016  111.683 131.240 1.00 63.64  ? 505  TYR A CE1 1 
ATOM   4071  C  CE2 . TYR A 1 934  ? 85.821  109.495 131.800 1.00 63.31  ? 505  TYR A CE2 1 
ATOM   4072  C  CZ  . TYR A 1 934  ? 86.021  110.862 131.737 1.00 61.93  ? 505  TYR A CZ  1 
ATOM   4073  O  OH  . TYR A 1 934  ? 87.223  111.394 132.171 1.00 58.46  ? 505  TYR A OH  1 
ATOM   4074  N  N   . ASN A 1 935  ? 81.602  110.730 127.783 1.00 53.95  ? 506  ASN A N   1 
ATOM   4075  C  CA  . ASN A 1 935  ? 82.025  111.849 126.948 1.00 52.27  ? 506  ASN A CA  1 
ATOM   4076  C  C   . ASN A 1 935  ? 82.535  112.989 127.817 1.00 53.43  ? 506  ASN A C   1 
ATOM   4077  O  O   . ASN A 1 935  ? 81.974  113.251 128.886 1.00 58.58  ? 506  ASN A O   1 
ATOM   4078  C  CB  . ASN A 1 935  ? 80.871  112.333 126.099 1.00 61.92  ? 506  ASN A CB  1 
ATOM   4079  C  CG  . ASN A 1 935  ? 79.594  112.451 126.903 1.00 72.17  ? 506  ASN A CG  1 
ATOM   4080  O  OD1 . ASN A 1 935  ? 79.594  112.237 128.124 1.00 65.67  ? 506  ASN A OD1 1 
ATOM   4081  N  ND2 . ASN A 1 935  ? 78.495  112.786 126.230 1.00 71.57  ? 506  ASN A ND2 1 
ATOM   4082  N  N   . PRO A 1 936  ? 83.602  113.658 127.394 1.00 51.06  ? 507  PRO A N   1 
ATOM   4083  C  CA  . PRO A 1 936  ? 84.202  114.717 128.226 1.00 50.42  ? 507  PRO A CA  1 
ATOM   4084  C  C   . PRO A 1 936  ? 83.236  115.874 128.403 1.00 53.82  ? 507  PRO A C   1 
ATOM   4085  O  O   . PRO A 1 936  ? 82.765  116.447 127.411 1.00 62.60  ? 507  PRO A O   1 
ATOM   4086  C  CB  . PRO A 1 936  ? 85.439  115.138 127.418 1.00 52.09  ? 507  PRO A CB  1 
ATOM   4087  C  CG  . PRO A 1 936  ? 85.756  113.944 126.543 1.00 50.07  ? 507  PRO A CG  1 
ATOM   4088  C  CD  . PRO A 1 936  ? 84.414  113.340 126.207 1.00 50.31  ? 507  PRO A CD  1 
ATOM   4089  N  N   . PRO A 1 937  ? 82.904  116.243 129.642 1.00 44.04  ? 508  PRO A N   1 
ATOM   4090  C  CA  . PRO A 1 937  ? 81.819  117.216 129.842 1.00 43.53  ? 508  PRO A CA  1 
ATOM   4091  C  C   . PRO A 1 937  ? 82.076  118.555 129.201 1.00 58.67  ? 508  PRO A C   1 
ATOM   4092  O  O   . PRO A 1 937  ? 81.117  119.218 128.783 1.00 68.47  ? 508  PRO A O   1 
ATOM   4093  C  CB  . PRO A 1 937  ? 81.721  117.340 131.364 1.00 50.55  ? 508  PRO A CB  1 
ATOM   4094  C  CG  . PRO A 1 937  ? 82.375  116.133 131.888 1.00 64.86  ? 508  PRO A CG  1 
ATOM   4095  C  CD  . PRO A 1 937  ? 83.448  115.757 130.910 1.00 54.99  ? 508  PRO A CD  1 
ATOM   4096  N  N   . HIS A 1 938  ? 83.327  118.984 129.104 1.00 55.50  ? 509  HIS A N   1 
ATOM   4097  C  CA  . HIS A 1 938  ? 83.649  120.277 128.515 1.00 53.81  ? 509  HIS A CA  1 
ATOM   4098  C  C   . HIS A 1 938  ? 84.568  120.059 127.336 1.00 44.11  ? 509  HIS A C   1 
ATOM   4099  O  O   . HIS A 1 938  ? 85.661  119.508 127.483 1.00 52.88  ? 509  HIS A O   1 
ATOM   4100  C  CB  . HIS A 1 938  ? 84.290  121.222 129.534 1.00 66.37  ? 509  HIS A CB  1 
ATOM   4101  C  CG  . HIS A 1 938  ? 83.478  121.414 130.787 1.00 85.25  ? 509  HIS A CG  1 
ATOM   4102  N  ND1 . HIS A 1 938  ? 82.539  122.420 130.920 1.00 86.12  ? 509  HIS A ND1 1 
ATOM   4103  C  CD2 . HIS A 1 938  ? 83.461  120.730 131.959 1.00 85.55  ? 509  HIS A CD2 1 
ATOM   4104  C  CE1 . HIS A 1 938  ? 81.988  122.352 132.121 1.00 89.07  ? 509  HIS A CE1 1 
ATOM   4105  N  NE2 . HIS A 1 938  ? 82.527  121.333 132.769 1.00 89.93  ? 509  HIS A NE2 1 
ATOM   4106  N  N   . LYS A 1 939  ? 84.116  120.470 126.172 1.00 52.52  ? 510  LYS A N   1 
ATOM   4107  C  CA  . LYS A 1 939  ? 84.996  120.390 125.035 1.00 57.11  ? 510  LYS A CA  1 
ATOM   4108  C  C   . LYS A 1 939  ? 86.045  121.473 125.152 1.00 49.10  ? 510  LYS A C   1 
ATOM   4109  O  O   . LYS A 1 939  ? 85.979  122.351 126.013 1.00 51.24  ? 510  LYS A O   1 
ATOM   4110  C  CB  . LYS A 1 939  ? 84.218  120.537 123.729 1.00 64.57  ? 510  LYS A CB  1 
ATOM   4111  C  CG  . LYS A 1 939  ? 83.605  119.236 123.226 1.00 56.02  ? 510  LYS A CG  1 
ATOM   4112  C  CD  . LYS A 1 939  ? 84.716  118.302 122.824 1.00 65.12  ? 510  LYS A CD  1 
ATOM   4113  C  CE  . LYS A 1 939  ? 85.631  118.965 121.799 1.00 80.19  ? 510  LYS A CE  1 
ATOM   4114  N  NZ  . LYS A 1 939  ? 86.784  118.108 121.382 1.00 83.65  ? 510  LYS A NZ  1 
ATOM   4115  N  N   . PHE A 1 940  ? 87.029  121.394 124.277 1.00 58.46  ? 511  PHE A N   1 
ATOM   4116  C  CA  . PHE A 1 940  ? 88.079  122.393 124.182 1.00 73.85  ? 511  PHE A CA  1 
ATOM   4117  C  C   . PHE A 1 940  ? 88.026  123.028 122.801 1.00 85.59  ? 511  PHE A C   1 
ATOM   4118  O  O   . PHE A 1 940  ? 87.729  122.351 121.811 1.00 87.50  ? 511  PHE A O   1 
ATOM   4119  C  CB  . PHE A 1 940  ? 89.479  121.783 124.452 1.00 82.94  ? 511  PHE A CB  1 
ATOM   4120  C  CG  . PHE A 1 940  ? 90.014  120.916 123.324 1.00 88.71  ? 511  PHE A CG  1 
ATOM   4121  C  CD1 . PHE A 1 940  ? 89.536  119.624 123.128 1.00 89.66  ? 511  PHE A CD1 1 
ATOM   4122  C  CD2 . PHE A 1 940  ? 90.973  121.402 122.447 1.00 88.85  ? 511  PHE A CD2 1 
ATOM   4123  C  CE1 . PHE A 1 940  ? 90.018  118.828 122.092 1.00 90.57  ? 511  PHE A CE1 1 
ATOM   4124  C  CE2 . PHE A 1 940  ? 91.454  120.613 121.405 1.00 93.28  ? 511  PHE A CE2 1 
ATOM   4125  C  CZ  . PHE A 1 940  ? 90.976  119.325 121.230 1.00 96.86  ? 511  PHE A CZ  1 
ATOM   4126  N  N   . SER A 1 941  ? 88.291  124.339 122.743 1.00 92.17  ? 512  SER A N   1 
ATOM   4127  C  CA  . SER A 1 941  ? 88.220  125.064 121.472 1.00 103.57 ? 512  SER A CA  1 
ATOM   4128  C  C   . SER A 1 941  ? 89.325  124.621 120.512 1.00 95.79  ? 512  SER A C   1 
ATOM   4129  O  O   . SER A 1 941  ? 89.066  124.327 119.338 1.00 94.67  ? 512  SER A O   1 
ATOM   4130  C  CB  . SER A 1 941  ? 88.292  126.577 121.727 1.00 102.42 ? 512  SER A CB  1 
ATOM   4131  O  OG  . SER A 1 941  ? 88.216  127.319 120.518 1.00 93.98  ? 512  SER A OG  1 
ATOM   4132  N  N   . THR A 1 942  ? 90.563  124.580 120.994 1.00 89.28  ? 513  THR A N   1 
ATOM   4133  C  CA  . THR A 1 942  ? 91.737  124.188 120.225 1.00 84.79  ? 513  THR A CA  1 
ATOM   4134  C  C   . THR A 1 942  ? 92.903  124.002 121.172 1.00 89.61  ? 513  THR A C   1 
ATOM   4135  O  O   . THR A 1 942  ? 92.996  124.666 122.212 1.00 89.76  ? 513  THR A O   1 
ATOM   4136  C  CB  . THR A 1 942  ? 92.133  125.221 119.174 1.00 88.54  ? 513  THR A CB  1 
ATOM   4137  O  OG1 . THR A 1 942  ? 93.287  124.744 118.468 1.00 80.40  ? 513  THR A OG1 1 
ATOM   4138  C  CG2 . THR A 1 942  ? 92.468  126.550 119.850 1.00 90.47  ? 513  THR A CG2 1 
ATOM   4139  N  N   . LYS A 1 943  ? 93.798  123.102 120.790 1.00 88.52  ? 514  LYS A N   1 
ATOM   4140  C  CA  . LYS A 1 943  ? 95.030  122.875 121.524 1.00 84.31  ? 514  LYS A CA  1 
ATOM   4141  C  C   . LYS A 1 943  ? 96.221  123.431 120.761 1.00 80.54  ? 514  LYS A C   1 
ATOM   4142  O  O   . LYS A 1 943  ? 97.368  123.241 121.179 1.00 77.42  ? 514  LYS A O   1 
ATOM   4143  C  CB  . LYS A 1 943  ? 95.188  121.374 121.824 1.00 88.05  ? 514  LYS A CB  1 
ATOM   4144  C  CG  . LYS A 1 943  ? 95.394  120.483 120.575 1.00 101.82 ? 514  LYS A CG  1 
ATOM   4145  C  CD  . LYS A 1 943  ? 95.653  118.988 120.907 1.00 112.62 ? 514  LYS A CD  1 
ATOM   4146  C  CE  . LYS A 1 943  ? 94.441  118.298 121.574 1.00 99.70  ? 514  LYS A CE  1 
ATOM   4147  N  NZ  . LYS A 1 943  ? 94.656  116.837 121.828 1.00 81.96  ? 514  LYS A NZ  1 
ATOM   4148  N  N   . ARG A 1 944  ? 95.978  124.133 119.665 1.00 66.19  ? 515  ARG A N   1 
ATOM   4149  C  CA  . ARG A 1 944  ? 97.067  124.622 118.847 1.00 61.54  ? 515  ARG A CA  1 
ATOM   4150  C  C   . ARG A 1 944  ? 97.474  126.001 119.327 1.00 53.41  ? 515  ARG A C   1 
ATOM   4151  O  O   . ARG A 1 944  ? 96.623  126.793 119.736 1.00 61.67  ? 515  ARG A O   1 
ATOM   4152  C  CB  . ARG A 1 944  ? 96.629  124.654 117.391 1.00 73.83  ? 515  ARG A CB  1 
ATOM   4153  C  CG  . ARG A 1 944  ? 96.231  123.264 116.906 1.00 91.83  ? 515  ARG A CG  1 
ATOM   4154  C  CD  . ARG A 1 944  ? 97.346  122.209 117.072 1.00 92.72  ? 515  ARG A CD  1 
ATOM   4155  N  NE  . ARG A 1 944  ? 98.556  122.546 116.311 1.00 87.88  ? 515  ARG A NE  1 
ATOM   4156  C  CZ  . ARG A 1 944  ? 99.675  121.827 116.316 1.00 86.29  ? 515  ARG A CZ  1 
ATOM   4157  N  NH1 . ARG A 1 944  ? 99.763  120.737 117.066 1.00 88.57  ? 515  ARG A NH1 1 
ATOM   4158  N  NH2 . ARG A 1 944  ? 100.708 122.202 115.575 1.00 86.64  ? 515  ARG A NH2 1 
ATOM   4159  N  N   . VAL A 1 945  ? 98.777  126.272 119.311 1.00 50.37  ? 516  VAL A N   1 
ATOM   4160  C  CA  . VAL A 1 945  ? 99.290  127.566 119.759 1.00 49.38  ? 516  VAL A CA  1 
ATOM   4161  C  C   . VAL A 1 945  ? 99.012  128.696 118.770 1.00 54.95  ? 516  VAL A C   1 
ATOM   4162  O  O   . VAL A 1 945  ? 98.834  129.837 119.219 1.00 59.28  ? 516  VAL A O   1 
ATOM   4163  C  CB  . VAL A 1 945  ? 100.803 127.537 120.036 1.00 66.70  ? 516  VAL A CB  1 
ATOM   4164  C  CG1 . VAL A 1 945  ? 101.612 127.444 118.767 1.00 70.03  ? 516  VAL A CG1 1 
ATOM   4165  C  CG2 . VAL A 1 945  ? 101.228 128.781 120.810 1.00 67.60  ? 516  VAL A CG2 1 
ATOM   4166  N  N   . PRO A 1 946  ? 98.994  128.494 117.443 1.00 48.25  ? 517  PRO A N   1 
ATOM   4167  C  CA  . PRO A 1 946  ? 98.739  129.660 116.598 1.00 38.42  ? 517  PRO A CA  1 
ATOM   4168  C  C   . PRO A 1 946  ? 97.322  130.146 116.698 1.00 38.76  ? 517  PRO A C   1 
ATOM   4169  O  O   . PRO A 1 946  ? 97.102  131.360 116.785 1.00 53.63  ? 517  PRO A O   1 
ATOM   4170  C  CB  . PRO A 1 946  ? 99.062  129.163 115.197 1.00 47.90  ? 517  PRO A CB  1 
ATOM   4171  C  CG  . PRO A 1 946  ? 98.752  127.779 115.231 1.00 56.59  ? 517  PRO A CG  1 
ATOM   4172  C  CD  . PRO A 1 946  ? 99.144  127.299 116.596 1.00 61.77  ? 517  PRO A CD  1 
ATOM   4173  N  N   . GLU A 1 947  ? 96.348  129.248 116.693 1.00 37.64  ? 518  GLU A N   1 
ATOM   4174  C  CA  . GLU A 1 947  ? 94.985  129.711 116.874 1.00 44.66  ? 518  GLU A CA  1 
ATOM   4175  C  C   . GLU A 1 947  ? 94.803  130.344 118.245 1.00 47.15  ? 518  GLU A C   1 
ATOM   4176  O  O   . GLU A 1 947  ? 94.082  131.335 118.378 1.00 55.74  ? 518  GLU A O   1 
ATOM   4177  C  CB  . GLU A 1 947  ? 93.991  128.575 116.668 1.00 65.42  ? 518  GLU A CB  1 
ATOM   4178  C  CG  . GLU A 1 947  ? 92.520  129.038 116.740 1.00 89.52  ? 518  GLU A CG  1 
ATOM   4179  C  CD  . GLU A 1 947  ? 91.504  127.915 116.486 1.00 108.87 ? 518  GLU A CD  1 
ATOM   4180  O  OE1 . GLU A 1 947  ? 91.921  126.770 116.194 1.00 109.35 ? 518  GLU A OE1 1 
ATOM   4181  O  OE2 . GLU A 1 947  ? 90.285  128.178 116.592 1.00 103.60 ? 518  GLU A OE2 1 
ATOM   4182  N  N   . GLN A 1 948  ? 95.450  129.798 119.277 1.00 46.08  ? 519  GLN A N   1 
ATOM   4183  C  CA  . GLN A 1 948  ? 95.345  130.405 120.603 1.00 51.19  ? 519  GLN A CA  1 
ATOM   4184  C  C   . GLN A 1 948  ? 95.937  131.815 120.618 1.00 54.24  ? 519  GLN A C   1 
ATOM   4185  O  O   . GLN A 1 948  ? 95.348  132.737 121.195 1.00 58.76  ? 519  GLN A O   1 
ATOM   4186  C  CB  . GLN A 1 948  ? 96.042  129.536 121.658 1.00 57.14  ? 519  GLN A CB  1 
ATOM   4187  C  CG  . GLN A 1 948  ? 95.282  128.289 122.094 1.00 61.35  ? 519  GLN A CG  1 
ATOM   4188  C  CD  . GLN A 1 948  ? 94.193  128.589 123.097 1.00 68.42  ? 519  GLN A CD  1 
ATOM   4189  O  OE1 . GLN A 1 948  ? 93.900  129.753 123.383 1.00 66.09  ? 519  GLN A OE1 1 
ATOM   4190  N  NE2 . GLN A 1 948  ? 93.583  127.537 123.643 1.00 73.79  ? 519  GLN A NE2 1 
ATOM   4191  N  N   . PHE A 1 949  ? 97.108  132.001 120.002 1.00 43.81  ? 520  PHE A N   1 
ATOM   4192  C  CA  . PHE A 1 949  ? 97.722  133.322 119.952 1.00 34.42  ? 520  PHE A CA  1 
ATOM   4193  C  C   . PHE A 1 949  ? 96.855  134.301 119.212 1.00 35.52  ? 520  PHE A C   1 
ATOM   4194  O  O   . PHE A 1 949  ? 96.766  135.471 119.585 1.00 47.56  ? 520  PHE A O   1 
ATOM   4195  C  CB  . PHE A 1 949  ? 99.050  133.255 119.250 1.00 41.09  ? 520  PHE A CB  1 
ATOM   4196  C  CG  . PHE A 1 949  ? 99.733  134.571 119.134 1.00 42.03  ? 520  PHE A CG  1 
ATOM   4197  C  CD1 . PHE A 1 949  ? 100.537 135.035 120.145 1.00 55.74  ? 520  PHE A CD1 1 
ATOM   4198  C  CD2 . PHE A 1 949  ? 99.602  135.331 118.005 1.00 48.77  ? 520  PHE A CD2 1 
ATOM   4199  C  CE1 . PHE A 1 949  ? 101.198 136.239 120.028 1.00 53.62  ? 520  PHE A CE1 1 
ATOM   4200  C  CE2 . PHE A 1 949  ? 100.261 136.535 117.885 1.00 56.85  ? 520  PHE A CE2 1 
ATOM   4201  C  CZ  . PHE A 1 949  ? 101.061 136.986 118.899 1.00 52.07  ? 520  PHE A CZ  1 
ATOM   4202  N  N   . LEU A 1 950  ? 96.268  133.868 118.119 1.00 34.62  ? 521  LEU A N   1 
ATOM   4203  C  CA  . LEU A 1 950  ? 95.384  134.777 117.450 1.00 30.87  ? 521  LEU A CA  1 
ATOM   4204  C  C   . LEU A 1 950  ? 94.114  134.994 118.236 1.00 37.44  ? 521  LEU A C   1 
ATOM   4205  O  O   . LEU A 1 950  ? 93.466  136.026 118.058 1.00 53.84  ? 521  LEU A O   1 
ATOM   4206  C  CB  . LEU A 1 950  ? 95.067  134.269 116.060 1.00 38.61  ? 521  LEU A CB  1 
ATOM   4207  C  CG  . LEU A 1 950  ? 96.298  134.198 115.164 1.00 42.71  ? 521  LEU A CG  1 
ATOM   4208  C  CD1 . LEU A 1 950  ? 95.890  133.863 113.727 1.00 51.96  ? 521  LEU A CD1 1 
ATOM   4209  C  CD2 . LEU A 1 950  ? 97.072  135.498 115.228 1.00 41.71  ? 521  LEU A CD2 1 
ATOM   4210  N  N   . GLU A 1 951  ? 93.732  134.081 119.103 1.00 36.76  ? 522  GLU A N   1 
ATOM   4211  C  CA  . GLU A 1 951  ? 92.469  134.293 119.792 1.00 44.30  ? 522  GLU A CA  1 
ATOM   4212  C  C   . GLU A 1 951  ? 92.602  135.146 121.040 1.00 53.72  ? 522  GLU A C   1 
ATOM   4213  O  O   . GLU A 1 951  ? 91.581  135.509 121.634 1.00 59.92  ? 522  GLU A O   1 
ATOM   4214  C  CB  . GLU A 1 951  ? 91.826  132.963 120.175 1.00 51.52  ? 522  GLU A CB  1 
ATOM   4215  C  CG  . GLU A 1 951  ? 91.131  132.275 119.018 1.00 72.02  ? 522  GLU A CG  1 
ATOM   4216  C  CD  . GLU A 1 951  ? 89.688  132.740 118.843 1.00 92.16  ? 522  GLU A CD  1 
ATOM   4217  O  OE1 . GLU A 1 951  ? 88.997  132.947 119.871 1.00 86.14  ? 522  GLU A OE1 1 
ATOM   4218  O  OE2 . GLU A 1 951  ? 89.244  132.902 117.681 1.00 91.62  ? 522  GLU A OE2 1 
ATOM   4219  N  N   . GLN A 1 952  ? 93.819  135.477 121.452 1.00 49.31  ? 523  GLN A N   1 
ATOM   4220  C  CA  . GLN A 1 952  ? 94.035  136.173 122.712 1.00 45.09  ? 523  GLN A CA  1 
ATOM   4221  C  C   . GLN A 1 952  ? 93.946  137.669 122.454 1.00 53.20  ? 523  GLN A C   1 
ATOM   4222  O  O   . GLN A 1 952  ? 94.844  138.252 121.840 1.00 53.12  ? 523  GLN A O   1 
ATOM   4223  C  CB  . GLN A 1 952  ? 95.384  135.802 123.312 1.00 47.51  ? 523  GLN A CB  1 
ATOM   4224  C  CG  . GLN A 1 952  ? 95.536  136.296 124.738 1.00 59.98  ? 523  GLN A CG  1 
ATOM   4225  C  CD  . GLN A 1 952  ? 96.808  135.800 125.414 1.00 61.85  ? 523  GLN A CD  1 
ATOM   4226  O  OE1 . GLN A 1 952  ? 97.830  135.575 124.759 1.00 63.03  ? 523  GLN A OE1 1 
ATOM   4227  N  NE2 . GLN A 1 952  ? 96.747  135.619 126.734 1.00 59.61  ? 523  GLN A NE2 1 
ATOM   4228  N  N   . GLU A 1 953  ? 92.866  138.296 122.928 1.00 58.10  ? 524  GLU A N   1 
ATOM   4229  C  CA  . GLU A 1 953  ? 92.674  139.722 122.678 1.00 50.53  ? 524  GLU A CA  1 
ATOM   4230  C  C   . GLU A 1 953  ? 93.707  140.540 123.418 1.00 45.43  ? 524  GLU A C   1 
ATOM   4231  O  O   . GLU A 1 953  ? 94.622  141.113 122.816 1.00 46.46  ? 524  GLU A O   1 
ATOM   4232  C  CB  . GLU A 1 953  ? 91.271  140.140 123.109 1.00 58.31  ? 524  GLU A CB  1 
ATOM   4233  C  CG  . GLU A 1 953  ? 90.185  139.599 122.182 1.00 79.26  ? 524  GLU A CG  1 
ATOM   4234  C  CD  . GLU A 1 953  ? 88.771  139.852 122.685 1.00 86.13  ? 524  GLU A CD  1 
ATOM   4235  O  OE1 . GLU A 1 953  ? 88.088  138.866 123.054 1.00 84.38  ? 524  GLU A OE1 1 
ATOM   4236  O  OE2 . GLU A 1 953  ? 88.347  141.031 122.707 1.00 79.93  ? 524  GLU A OE2 1 
ATOM   4237  N  N   . ASN A 1 954  ? 93.622  140.539 124.740 1.00 51.45  ? 525  ASN A N   1 
ATOM   4238  C  CA  . ASN A 1 954  ? 94.514  141.352 125.554 1.00 61.01  ? 525  ASN A CA  1 
ATOM   4239  C  C   . ASN A 1 954  ? 95.880  140.672 125.641 1.00 54.44  ? 525  ASN A C   1 
ATOM   4240  O  O   . ASN A 1 954  ? 96.325  140.209 126.694 1.00 58.72  ? 525  ASN A O   1 
ATOM   4241  C  CB  . ASN A 1 954  ? 93.897  141.580 126.929 1.00 65.10  ? 525  ASN A CB  1 
ATOM   4242  C  CG  . ASN A 1 954  ? 93.401  140.288 127.570 1.00 69.12  ? 525  ASN A CG  1 
ATOM   4243  O  OD1 . ASN A 1 954  ? 93.662  139.186 127.070 1.00 62.55  ? 525  ASN A OD1 1 
ATOM   4244  N  ND2 . ASN A 1 954  ? 92.686  140.419 128.686 1.00 74.43  ? 525  ASN A ND2 1 
ATOM   4245  N  N   . PHE A 1 955  ? 96.558  140.608 124.507 1.00 35.09  ? 526  PHE A N   1 
ATOM   4246  C  CA  . PHE A 1 955  ? 97.878  140.029 124.507 1.00 27.53  ? 526  PHE A CA  1 
ATOM   4247  C  C   . PHE A 1 955  ? 98.890  141.139 124.471 1.00 27.86  ? 526  PHE A C   1 
ATOM   4248  O  O   . PHE A 1 955  ? 98.824  142.000 123.598 1.00 43.11  ? 526  PHE A O   1 
ATOM   4249  C  CB  . PHE A 1 955  ? 98.106  139.130 123.316 1.00 37.97  ? 526  PHE A CB  1 
ATOM   4250  C  CG  . PHE A 1 955  ? 99.535  138.728 123.163 1.00 43.87  ? 526  PHE A CG  1 
ATOM   4251  C  CD1 . PHE A 1 955  ? 100.041 137.665 123.882 1.00 48.94  ? 526  PHE A CD1 1 
ATOM   4252  C  CD2 . PHE A 1 955  ? 100.388 139.435 122.344 1.00 46.91  ? 526  PHE A CD2 1 
ATOM   4253  C  CE1 . PHE A 1 955  ? 101.358 137.295 123.760 1.00 50.71  ? 526  PHE A CE1 1 
ATOM   4254  C  CE2 . PHE A 1 955  ? 101.709 139.078 122.225 1.00 43.66  ? 526  PHE A CE2 1 
ATOM   4255  C  CZ  . PHE A 1 955  ? 102.195 138.008 122.931 1.00 49.06  ? 526  PHE A CZ  1 
ATOM   4256  N  N   . SER A 1 956  ? 99.831  141.109 125.392 1.00 27.29  ? 527  SER A N   1 
ATOM   4257  C  CA  . SER A 1 956  ? 100.981 141.987 125.284 1.00 35.38  ? 527  SER A CA  1 
ATOM   4258  C  C   . SER A 1 956  ? 102.012 141.510 126.284 1.00 52.55  ? 527  SER A C   1 
ATOM   4259  O  O   . SER A 1 956  ? 101.689 140.765 127.210 1.00 57.99  ? 527  SER A O   1 
ATOM   4260  C  CB  . SER A 1 956  ? 100.615 143.432 125.563 1.00 44.34  ? 527  SER A CB  1 
ATOM   4261  O  OG  . SER A 1 956  ? 100.199 143.561 126.907 1.00 49.79  ? 527  SER A OG  1 
ATOM   4262  N  N   . ILE A 1 957  ? 103.254 141.963 126.117 1.00 47.11  ? 528  ILE A N   1 
ATOM   4263  C  CA  . ILE A 1 957  ? 104.312 141.439 126.972 1.00 36.47  ? 528  ILE A CA  1 
ATOM   4264  C  C   . ILE A 1 957  ? 104.124 141.879 128.412 1.00 39.76  ? 528  ILE A C   1 
ATOM   4265  O  O   . ILE A 1 957  ? 104.284 141.082 129.343 1.00 51.79  ? 528  ILE A O   1 
ATOM   4266  C  CB  . ILE A 1 957  ? 105.677 141.842 126.438 1.00 41.63  ? 528  ILE A CB  1 
ATOM   4267  C  CG1 . ILE A 1 957  ? 105.810 141.182 125.082 1.00 50.92  ? 528  ILE A CG1 1 
ATOM   4268  C  CG2 . ILE A 1 957  ? 106.744 141.382 127.420 1.00 51.98  ? 528  ILE A CG2 1 
ATOM   4269  C  CD1 . ILE A 1 957  ? 105.440 139.720 125.131 1.00 55.55  ? 528  ILE A CD1 1 
ATOM   4270  N  N   . GLU A 1 958  ? 103.784 143.139 128.633 1.00 41.16  ? 529  GLU A N   1 
ATOM   4271  C  CA  . GLU A 1 958  ? 103.469 143.525 129.997 1.00 40.03  ? 529  GLU A CA  1 
ATOM   4272  C  C   . GLU A 1 958  ? 102.253 142.777 130.497 1.00 41.71  ? 529  GLU A C   1 
ATOM   4273  O  O   . GLU A 1 958  ? 102.092 142.597 131.704 1.00 49.74  ? 529  GLU A O   1 
ATOM   4274  C  CB  . GLU A 1 958  ? 103.232 145.024 130.094 1.00 59.19  ? 529  GLU A CB  1 
ATOM   4275  C  CG  . GLU A 1 958  ? 102.026 145.508 129.286 1.00 73.65  ? 529  GLU A CG  1 
ATOM   4276  C  CD  . GLU A 1 958  ? 102.384 145.872 127.838 1.00 77.37  ? 529  GLU A CD  1 
ATOM   4277  O  OE1 . GLU A 1 958  ? 103.547 145.626 127.427 1.00 68.11  ? 529  GLU A OE1 1 
ATOM   4278  O  OE2 . GLU A 1 958  ? 101.505 146.410 127.117 1.00 67.56  ? 529  GLU A OE2 1 
ATOM   4279  N  N   . ASN A 1 959  ? 101.395 142.307 129.598 1.00 41.28  ? 530  ASN A N   1 
ATOM   4280  C  CA  . ASN A 1 959  ? 100.245 141.542 130.059 1.00 41.42  ? 530  ASN A CA  1 
ATOM   4281  C  C   . ASN A 1 959  ? 100.614 140.101 130.390 1.00 40.20  ? 530  ASN A C   1 
ATOM   4282  O  O   . ASN A 1 959  ? 100.045 139.523 131.320 1.00 49.83  ? 530  ASN A O   1 
ATOM   4283  C  CB  . ASN A 1 959  ? 99.140  141.564 129.017 1.00 51.28  ? 530  ASN A CB  1 
ATOM   4284  C  CG  . ASN A 1 959  ? 97.782  141.359 129.624 1.00 57.66  ? 530  ASN A CG  1 
ATOM   4285  O  OD1 . ASN A 1 959  ? 97.416  140.243 129.991 1.00 58.81  ? 530  ASN A OD1 1 
ATOM   4286  N  ND2 . ASN A 1 959  ? 97.004  142.439 129.710 1.00 57.47  ? 530  ASN A ND2 1 
ATOM   4287  N  N   . VAL A 1 960  ? 101.567 139.513 129.665 1.00 33.46  ? 531  VAL A N   1 
ATOM   4288  C  CA  . VAL A 1 960  ? 102.156 138.250 130.099 1.00 27.14  ? 531  VAL A CA  1 
ATOM   4289  C  C   . VAL A 1 960  ? 102.760 138.406 131.482 1.00 38.41  ? 531  VAL A C   1 
ATOM   4290  O  O   . VAL A 1 960  ? 102.574 137.557 132.362 1.00 47.25  ? 531  VAL A O   1 
ATOM   4291  C  CB  . VAL A 1 960  ? 103.222 137.777 129.092 1.00 36.75  ? 531  VAL A CB  1 
ATOM   4292  C  CG1 . VAL A 1 960  ? 103.811 136.455 129.520 1.00 42.35  ? 531  VAL A CG1 1 
ATOM   4293  C  CG2 . VAL A 1 960  ? 102.638 137.639 127.691 1.00 48.47  ? 531  VAL A CG2 1 
ATOM   4294  N  N   . LEU A 1 961  ? 103.509 139.484 131.695 1.00 42.03  ? 532  LEU A N   1 
ATOM   4295  C  CA  . LEU A 1 961  ? 104.089 139.705 133.012 1.00 38.31  ? 532  LEU A CA  1 
ATOM   4296  C  C   . LEU A 1 961  ? 103.014 139.886 134.071 1.00 39.39  ? 532  LEU A C   1 
ATOM   4297  O  O   . LEU A 1 961  ? 103.185 139.434 135.199 1.00 50.71  ? 532  LEU A O   1 
ATOM   4298  C  CB  . LEU A 1 961  ? 105.022 140.913 133.006 1.00 41.49  ? 532  LEU A CB  1 
ATOM   4299  C  CG  . LEU A 1 961  ? 106.452 140.683 132.522 1.00 55.71  ? 532  LEU A CG  1 
ATOM   4300  C  CD1 . LEU A 1 961  ? 107.326 141.884 132.890 1.00 60.19  ? 532  LEU A CD1 1 
ATOM   4301  C  CD2 . LEU A 1 961  ? 107.010 139.397 133.123 1.00 56.52  ? 532  LEU A CD2 1 
ATOM   4302  N  N   . SER A 1 962  ? 101.931 140.590 133.764 1.00 36.19  ? 533  SER A N   1 
ATOM   4303  C  CA  . SER A 1 962  ? 100.903 140.752 134.784 1.00 37.97  ? 533  SER A CA  1 
ATOM   4304  C  C   . SER A 1 962  ? 100.205 139.437 135.066 1.00 45.32  ? 533  SER A C   1 
ATOM   4305  O  O   . SER A 1 962  ? 99.685  139.235 136.167 1.00 55.66  ? 533  SER A O   1 
ATOM   4306  C  CB  . SER A 1 962  ? 99.873  141.799 134.373 1.00 50.29  ? 533  SER A CB  1 
ATOM   4307  O  OG  . SER A 1 962  ? 100.470 143.070 134.172 1.00 54.93  ? 533  SER A OG  1 
ATOM   4308  N  N   . TYR A 1 963  ? 100.146 138.552 134.074 1.00 43.39  ? 534  TYR A N   1 
ATOM   4309  C  CA  . TYR A 1 963  ? 99.684  137.188 134.316 1.00 45.83  ? 534  TYR A CA  1 
ATOM   4310  C  C   . TYR A 1 963  ? 100.618 136.447 135.260 1.00 52.17  ? 534  TYR A C   1 
ATOM   4311  O  O   . TYR A 1 963  ? 100.163 135.717 136.150 1.00 53.31  ? 534  TYR A O   1 
ATOM   4312  C  CB  . TYR A 1 963  ? 99.564  136.451 132.981 1.00 56.52  ? 534  TYR A CB  1 
ATOM   4313  C  CG  . TYR A 1 963  ? 99.168  134.998 133.075 1.00 53.59  ? 534  TYR A CG  1 
ATOM   4314  C  CD1 . TYR A 1 963  ? 97.838  134.620 133.008 1.00 56.06  ? 534  TYR A CD1 1 
ATOM   4315  C  CD2 . TYR A 1 963  ? 100.135 134.001 133.146 1.00 48.20  ? 534  TYR A CD2 1 
ATOM   4316  C  CE1 . TYR A 1 963  ? 97.479  133.300 133.076 1.00 52.91  ? 534  TYR A CE1 1 
ATOM   4317  C  CE2 . TYR A 1 963  ? 99.790  132.679 133.206 1.00 45.25  ? 534  TYR A CE2 1 
ATOM   4318  C  CZ  . TYR A 1 963  ? 98.461  132.332 133.175 1.00 48.12  ? 534  TYR A CZ  1 
ATOM   4319  O  OH  . TYR A 1 963  ? 98.095  131.009 133.237 1.00 47.36  ? 534  TYR A OH  1 
ATOM   4320  N  N   . ALA A 1 964  ? 101.931 136.606 135.065 1.00 51.01  ? 535  ALA A N   1 
ATOM   4321  C  CA  . ALA A 1 964  ? 102.896 135.920 135.921 1.00 43.90  ? 535  ALA A CA  1 
ATOM   4322  C  C   . ALA A 1 964  ? 102.888 136.519 137.326 1.00 34.08  ? 535  ALA A C   1 
ATOM   4323  O  O   . ALA A 1 964  ? 102.522 135.854 138.298 1.00 39.05  ? 535  ALA A O   1 
ATOM   4324  C  CB  . ALA A 1 964  ? 104.292 135.973 135.289 1.00 37.50  ? 535  ALA A CB  1 
ATOM   4325  N  N   . GLN A 1 965  ? 103.232 137.793 137.440 1.00 31.55  ? 536  GLN A N   1 
ATOM   4326  C  CA  . GLN A 1 965  ? 103.392 138.395 138.748 1.00 28.02  ? 536  GLN A CA  1 
ATOM   4327  C  C   . GLN A 1 965  ? 102.159 138.216 139.565 1.00 28.17  ? 536  GLN A C   1 
ATOM   4328  O  O   . GLN A 1 965  ? 102.233 138.043 140.780 1.00 41.40  ? 536  GLN A O   1 
ATOM   4329  C  CB  . GLN A 1 965  ? 103.683 139.876 138.629 1.00 32.38  ? 536  GLN A CB  1 
ATOM   4330  C  CG  . GLN A 1 965  ? 104.919 140.148 137.840 1.00 36.21  ? 536  GLN A CG  1 
ATOM   4331  C  CD  . GLN A 1 965  ? 105.201 141.606 137.749 1.00 37.72  ? 536  GLN A CD  1 
ATOM   4332  O  OE1 . GLN A 1 965  ? 104.825 142.370 138.640 1.00 34.48  ? 536  GLN A OE1 1 
ATOM   4333  N  NE2 . GLN A 1 965  ? 105.818 142.024 136.647 1.00 42.69  ? 536  GLN A NE2 1 
ATOM   4334  N  N   . LYS A 1 966  ? 101.023 138.253 138.935 1.00 30.90  ? 537  LYS A N   1 
ATOM   4335  C  CA  . LYS A 1 966  ? 99.856  138.103 139.763 1.00 47.51  ? 537  LYS A CA  1 
ATOM   4336  C  C   . LYS A 1 966  ? 99.556  136.654 140.068 1.00 52.74  ? 537  LYS A C   1 
ATOM   4337  O  O   . LYS A 1 966  ? 98.478  136.356 140.601 1.00 58.60  ? 537  LYS A O   1 
ATOM   4338  C  CB  . LYS A 1 966  ? 98.648  138.796 139.131 1.00 58.74  ? 537  LYS A CB  1 
ATOM   4339  C  CG  . LYS A 1 966  ? 98.792  140.313 139.051 1.00 57.21  ? 537  LYS A CG  1 
ATOM   4340  C  CD  . LYS A 1 966  ? 97.560  140.936 138.414 1.00 66.32  ? 537  LYS A CD  1 
ATOM   4341  C  CE  . LYS A 1 966  ? 97.499  142.440 138.646 1.00 75.26  ? 537  LYS A CE  1 
ATOM   4342  N  NZ  . LYS A 1 966  ? 98.771  143.134 138.270 1.00 67.50  ? 537  LYS A NZ  1 
ATOM   4343  N  N   . LEU A 1 967  ? 100.483 135.751 139.756 1.00 50.74  ? 538  LEU A N   1 
ATOM   4344  C  CA  . LEU A 1 967  ? 100.326 134.335 140.081 1.00 52.14  ? 538  LEU A CA  1 
ATOM   4345  C  C   . LEU A 1 967  ? 99.110  133.742 139.380 1.00 45.31  ? 538  LEU A C   1 
ATOM   4346  O  O   . LEU A 1 967  ? 98.459  132.832 139.894 1.00 53.93  ? 538  LEU A O   1 
ATOM   4347  C  CB  . LEU A 1 967  ? 100.239 134.149 141.598 1.00 48.12  ? 538  LEU A CB  1 
ATOM   4348  C  CG  . LEU A 1 967  ? 101.590 134.492 142.227 1.00 52.19  ? 538  LEU A CG  1 
ATOM   4349  C  CD1 . LEU A 1 967  ? 101.387 134.766 143.677 1.00 55.54  ? 538  LEU A CD1 1 
ATOM   4350  C  CD2 . LEU A 1 967  ? 102.574 133.324 142.080 1.00 55.52  ? 538  LEU A CD2 1 
ATOM   4351  N  N   . GLU A 1 968  ? 98.772  134.260 138.207 1.00 42.42  ? 539  GLU A N   1 
ATOM   4352  C  CA  . GLU A 1 968  ? 97.614  133.710 137.536 1.00 46.50  ? 539  GLU A CA  1 
ATOM   4353  C  C   . GLU A 1 968  ? 97.862  132.283 137.091 1.00 48.79  ? 539  GLU A C   1 
ATOM   4354  O  O   . GLU A 1 968  ? 96.900  131.548 136.847 1.00 55.57  ? 539  GLU A O   1 
ATOM   4355  C  CB  . GLU A 1 968  ? 97.202  134.586 136.346 1.00 60.79  ? 539  GLU A CB  1 
ATOM   4356  C  CG  . GLU A 1 968  ? 96.983  136.092 136.676 1.00 71.13  ? 539  GLU A CG  1 
ATOM   4357  C  CD  . GLU A 1 968  ? 95.683  136.375 137.463 1.00 76.78  ? 539  GLU A CD  1 
ATOM   4358  O  OE1 . GLU A 1 968  ? 94.636  135.761 137.144 1.00 70.59  ? 539  GLU A OE1 1 
ATOM   4359  O  OE2 . GLU A 1 968  ? 95.717  137.189 138.422 1.00 68.18  ? 539  GLU A OE2 1 
ATOM   4360  N  N   . TYR A 1 969  ? 99.114  131.848 137.018 1.00 35.31  ? 540  TYR A N   1 
ATOM   4361  C  CA  . TYR A 1 969  ? 99.294  130.464 136.631 1.00 30.94  ? 540  TYR A CA  1 
ATOM   4362  C  C   . TYR A 1 969  ? 98.888  129.493 137.720 1.00 29.60  ? 540  TYR A C   1 
ATOM   4363  O  O   . TYR A 1 969  ? 98.839  128.291 137.463 1.00 41.20  ? 540  TYR A O   1 
ATOM   4364  C  CB  . TYR A 1 969  ? 100.721 130.229 136.212 1.00 36.11  ? 540  TYR A CB  1 
ATOM   4365  C  CG  . TYR A 1 969  ? 101.697 130.872 137.130 1.00 36.71  ? 540  TYR A CG  1 
ATOM   4366  C  CD1 . TYR A 1 969  ? 101.907 130.380 138.395 1.00 39.49  ? 540  TYR A CD1 1 
ATOM   4367  C  CD2 . TYR A 1 969  ? 102.434 131.971 136.717 1.00 39.39  ? 540  TYR A CD2 1 
ATOM   4368  C  CE1 . TYR A 1 969  ? 102.815 130.975 139.231 1.00 37.16  ? 540  TYR A CE1 1 
ATOM   4369  C  CE2 . TYR A 1 969  ? 103.340 132.564 137.538 1.00 31.50  ? 540  TYR A CE2 1 
ATOM   4370  C  CZ  . TYR A 1 969  ? 103.524 132.061 138.792 1.00 28.92  ? 540  TYR A CZ  1 
ATOM   4371  O  OH  . TYR A 1 969  ? 104.432 132.648 139.624 1.00 38.44  ? 540  TYR A OH  1 
ATOM   4372  N  N   . LEU A 1 970  ? 98.572  129.961 138.904 1.00 27.74  ? 541  LEU A N   1 
ATOM   4373  C  CA  . LEU A 1 970  ? 98.042  129.071 139.913 1.00 27.82  ? 541  LEU A CA  1 
ATOM   4374  C  C   . LEU A 1 970  ? 96.537  129.019 139.888 1.00 34.75  ? 541  LEU A C   1 
ATOM   4375  O  O   . LEU A 1 970  ? 95.938  128.416 140.781 1.00 48.60  ? 541  LEU A O   1 
ATOM   4376  C  CB  . LEU A 1 970  ? 98.500  129.498 141.304 1.00 35.61  ? 541  LEU A CB  1 
ATOM   4377  C  CG  . LEU A 1 970  ? 100.005 129.348 141.535 1.00 44.13  ? 541  LEU A CG  1 
ATOM   4378  C  CD1 . LEU A 1 970  ? 100.385 129.806 142.937 1.00 53.99  ? 541  LEU A CD1 1 
ATOM   4379  C  CD2 . LEU A 1 970  ? 100.466 127.923 141.284 1.00 48.05  ? 541  LEU A CD2 1 
ATOM   4380  N  N   . LEU A 1 971  ? 95.902  129.654 138.922 1.00 33.76  ? 542  LEU A N   1 
ATOM   4381  C  CA  . LEU A 1 971  ? 94.455  129.609 138.888 1.00 36.54  ? 542  LEU A CA  1 
ATOM   4382  C  C   . LEU A 1 971  ? 93.998  128.189 138.587 1.00 39.65  ? 542  LEU A C   1 
ATOM   4383  O  O   . LEU A 1 971  ? 94.720  127.427 137.939 1.00 49.23  ? 542  LEU A O   1 
ATOM   4384  C  CB  . LEU A 1 971  ? 93.906  130.551 137.829 1.00 40.04  ? 542  LEU A CB  1 
ATOM   4385  C  CG  . LEU A 1 971  ? 94.043  132.032 138.153 1.00 48.93  ? 542  LEU A CG  1 
ATOM   4386  C  CD1 . LEU A 1 971  ? 93.402  132.832 137.025 1.00 53.98  ? 542  LEU A CD1 1 
ATOM   4387  C  CD2 . LEU A 1 971  ? 93.488  132.385 139.550 1.00 44.73  ? 542  LEU A CD2 1 
ATOM   4388  N  N   . PRO A 1 972  ? 92.801  127.815 139.027 1.00 31.48  ? 543  PRO A N   1 
ATOM   4389  C  CA  . PRO A 1 972  ? 92.350  126.436 138.816 1.00 33.91  ? 543  PRO A CA  1 
ATOM   4390  C  C   . PRO A 1 972  ? 92.379  126.025 137.368 1.00 40.64  ? 543  PRO A C   1 
ATOM   4391  O  O   . PRO A 1 972  ? 92.761  124.894 137.052 1.00 46.34  ? 543  PRO A O   1 
ATOM   4392  C  CB  . PRO A 1 972  ? 90.914  126.454 139.329 1.00 41.97  ? 543  PRO A CB  1 
ATOM   4393  C  CG  . PRO A 1 972  ? 90.862  127.601 140.234 1.00 52.94  ? 543  PRO A CG  1 
ATOM   4394  C  CD  . PRO A 1 972  ? 91.790  128.626 139.701 1.00 41.81  ? 543  PRO A CD  1 
ATOM   4395  N  N   . GLN A 1 973  ? 92.001  126.911 136.463 1.00 37.78  ? 544  GLN A N   1 
ATOM   4396  C  CA  . GLN A 1 973  ? 91.936  126.452 135.095 1.00 34.87  ? 544  GLN A CA  1 
ATOM   4397  C  C   . GLN A 1 973  ? 93.309  126.272 134.493 1.00 33.38  ? 544  GLN A C   1 
ATOM   4398  O  O   . GLN A 1 973  ? 93.423  125.619 133.453 1.00 49.69  ? 544  GLN A O   1 
ATOM   4399  C  CB  . GLN A 1 973  ? 91.140  127.410 134.220 1.00 44.40  ? 544  GLN A CB  1 
ATOM   4400  C  CG  . GLN A 1 973  ? 91.766  128.772 134.104 1.00 49.79  ? 544  GLN A CG  1 
ATOM   4401  C  CD  . GLN A 1 973  ? 91.040  129.795 134.962 1.00 61.21  ? 544  GLN A CD  1 
ATOM   4402  O  OE1 . GLN A 1 973  ? 90.693  129.517 136.119 1.00 59.61  ? 544  GLN A OE1 1 
ATOM   4403  N  NE2 . GLN A 1 973  ? 90.812  130.987 134.408 1.00 65.84  ? 544  GLN A NE2 1 
ATOM   4404  N  N   . TYR A 1 974  ? 94.355  126.817 135.083 1.00 24.08  ? 545  TYR A N   1 
ATOM   4405  C  CA  . TYR A 1 974  ? 95.646  126.659 134.443 1.00 27.89  ? 545  TYR A CA  1 
ATOM   4406  C  C   . TYR A 1 974  ? 96.544  125.674 135.164 1.00 39.25  ? 545  TYR A C   1 
ATOM   4407  O  O   . TYR A 1 974  ? 97.716  125.537 134.798 1.00 46.23  ? 545  TYR A O   1 
ATOM   4408  C  CB  . TYR A 1 974  ? 96.348  127.999 134.322 1.00 41.24  ? 545  TYR A CB  1 
ATOM   4409  C  CG  . TYR A 1 974  ? 95.519  129.090 133.668 1.00 45.02  ? 545  TYR A CG  1 
ATOM   4410  C  CD1 . TYR A 1 974  ? 95.218  129.063 132.315 1.00 41.11  ? 545  TYR A CD1 1 
ATOM   4411  C  CD2 . TYR A 1 974  ? 95.029  130.153 134.428 1.00 50.03  ? 545  TYR A CD2 1 
ATOM   4412  C  CE1 . TYR A 1 974  ? 94.455  130.075 131.743 1.00 47.40  ? 545  TYR A CE1 1 
ATOM   4413  C  CE2 . TYR A 1 974  ? 94.273  131.163 133.867 1.00 47.17  ? 545  TYR A CE2 1 
ATOM   4414  C  CZ  . TYR A 1 974  ? 93.991  131.121 132.530 1.00 46.13  ? 545  TYR A CZ  1 
ATOM   4415  O  OH  . TYR A 1 974  ? 93.238  132.138 131.994 1.00 56.38  ? 545  TYR A OH  1 
ATOM   4416  N  N   . ARG A 1 975  ? 96.038  124.984 136.182 1.00 37.69  ? 546  ARG A N   1 
ATOM   4417  C  CA  . ARG A 1 975  ? 96.779  123.889 136.802 1.00 32.80  ? 546  ARG A CA  1 
ATOM   4418  C  C   . ARG A 1 975  ? 96.565  122.624 135.967 1.00 40.84  ? 546  ARG A C   1 
ATOM   4419  O  O   . ARG A 1 975  ? 95.811  121.719 136.330 1.00 39.92  ? 546  ARG A O   1 
ATOM   4420  C  CB  . ARG A 1 975  ? 96.303  123.685 138.220 1.00 28.51  ? 546  ARG A CB  1 
ATOM   4421  C  CG  . ARG A 1 975  ? 96.650  124.766 139.140 1.00 34.25  ? 546  ARG A CG  1 
ATOM   4422  C  CD  . ARG A 1 975  ? 96.009  124.417 140.437 1.00 32.94  ? 546  ARG A CD  1 
ATOM   4423  N  NE  . ARG A 1 975  ? 95.960  125.575 141.296 1.00 36.23  ? 546  ARG A NE  1 
ATOM   4424  C  CZ  . ARG A 1 975  ? 95.237  125.627 142.397 1.00 41.48  ? 546  ARG A CZ  1 
ATOM   4425  N  NH1 . ARG A 1 975  ? 94.488  124.595 142.728 1.00 45.76  ? 546  ARG A NH1 1 
ATOM   4426  N  NH2 . ARG A 1 975  ? 95.220  126.729 143.130 1.00 50.32  ? 546  ARG A NH2 1 
ATOM   4427  N  N   . ASN A 1 976  ? 97.194  122.599 134.790 1.00 36.40  ? 547  ASN A N   1 
ATOM   4428  C  CA  . ASN A 1 976  ? 97.184  121.415 133.946 1.00 22.54  ? 547  ASN A CA  1 
ATOM   4429  C  C   . ASN A 1 976  ? 98.550  121.203 133.349 1.00 23.53  ? 547  ASN A C   1 
ATOM   4430  O  O   . ASN A 1 976  ? 99.276  122.159 133.084 1.00 36.22  ? 547  ASN A O   1 
ATOM   4431  C  CB  . ASN A 1 976  ? 96.233  121.513 132.796 1.00 26.07  ? 547  ASN A CB  1 
ATOM   4432  C  CG  . ASN A 1 976  ? 96.174  120.246 132.023 1.00 31.48  ? 547  ASN A CG  1 
ATOM   4433  O  OD1 . ASN A 1 976  ? 96.693  120.157 130.917 1.00 32.65  ? 547  ASN A OD1 1 
ATOM   4434  N  ND2 . ASN A 1 976  ? 95.557  119.231 132.606 1.00 35.37  ? 547  ASN A ND2 1 
ATOM   4435  N  N   . PHE A 1 977  ? 98.880  119.949 133.099 1.00 21.20  ? 548  PHE A N   1 
ATOM   4436  C  CA  . PHE A 1 977  ? 100.183 119.636 132.553 1.00 18.60  ? 548  PHE A CA  1 
ATOM   4437  C  C   . PHE A 1 977  ? 100.186 118.254 131.972 1.00 24.80  ? 548  PHE A C   1 
ATOM   4438  O  O   . PHE A 1 977  ? 99.708  117.324 132.615 1.00 36.42  ? 548  PHE A O   1 
ATOM   4439  C  CB  . PHE A 1 977  ? 101.228 119.677 133.609 1.00 17.77  ? 548  PHE A CB  1 
ATOM   4440  C  CG  . PHE A 1 977  ? 102.557 119.468 133.081 1.00 24.74  ? 548  PHE A CG  1 
ATOM   4441  C  CD1 . PHE A 1 977  ? 103.075 118.199 132.996 1.00 35.35  ? 548  PHE A CD1 1 
ATOM   4442  C  CD2 . PHE A 1 977  ? 103.320 120.531 132.663 1.00 38.93  ? 548  PHE A CD2 1 
ATOM   4443  C  CE1 . PHE A 1 977  ? 104.355 117.978 132.522 1.00 41.81  ? 548  PHE A CE1 1 
ATOM   4444  C  CE2 . PHE A 1 977  ? 104.615 120.325 132.180 1.00 47.06  ? 548  PHE A CE2 1 
ATOM   4445  C  CZ  . PHE A 1 977  ? 105.129 119.038 132.118 1.00 42.54  ? 548  PHE A CZ  1 
ATOM   4446  N  N   . SER A 1 978  ? 100.789 118.089 130.809 1.00 20.04  ? 549  SER A N   1 
ATOM   4447  C  CA  . SER A 1 978  ? 100.569 116.826 130.126 1.00 21.57  ? 549  SER A CA  1 
ATOM   4448  C  C   . SER A 1 978  ? 101.761 116.450 129.279 1.00 25.45  ? 549  SER A C   1 
ATOM   4449  O  O   . SER A 1 978  ? 102.134 117.194 128.370 1.00 39.53  ? 549  SER A O   1 
ATOM   4450  C  CB  . SER A 1 978  ? 99.319  116.912 129.257 1.00 29.57  ? 549  SER A CB  1 
ATOM   4451  O  OG  . SER A 1 978  ? 99.486  117.893 128.250 1.00 34.45  ? 549  SER A OG  1 
ATOM   4452  N  N   . PHE A 1 979  ? 102.328 115.291 129.541 1.00 25.05  ? 550  PHE A N   1 
ATOM   4453  C  CA  . PHE A 1 979  ? 103.524 114.930 128.815 1.00 24.66  ? 550  PHE A CA  1 
ATOM   4454  C  C   . PHE A 1 979  ? 103.157 114.465 127.424 1.00 19.34  ? 550  PHE A C   1 
ATOM   4455  O  O   . PHE A 1 979  ? 101.994 114.326 127.063 1.00 28.17  ? 550  PHE A O   1 
ATOM   4456  C  CB  . PHE A 1 979  ? 104.276 113.811 129.519 1.00 37.62  ? 550  PHE A CB  1 
ATOM   4457  C  CG  . PHE A 1 979  ? 104.846 114.205 130.840 1.00 30.13  ? 550  PHE A CG  1 
ATOM   4458  C  CD1 . PHE A 1 979  ? 105.952 115.015 130.918 1.00 39.88  ? 550  PHE A CD1 1 
ATOM   4459  C  CD2 . PHE A 1 979  ? 104.295 113.716 132.001 1.00 28.11  ? 550  PHE A CD2 1 
ATOM   4460  C  CE1 . PHE A 1 979  ? 106.482 115.363 132.143 1.00 44.08  ? 550  PHE A CE1 1 
ATOM   4461  C  CE2 . PHE A 1 979  ? 104.811 114.044 133.213 1.00 33.18  ? 550  PHE A CE2 1 
ATOM   4462  C  CZ  . PHE A 1 979  ? 105.910 114.868 133.292 1.00 40.94  ? 550  PHE A CZ  1 
ATOM   4463  N  N   . SER A 1 980  ? 104.172 114.194 126.648 1.00 19.21  ? 551  SER A N   1 
ATOM   4464  C  CA  . SER A 1 980  ? 103.938 113.674 125.325 1.00 20.76  ? 551  SER A CA  1 
ATOM   4465  C  C   . SER A 1 980  ? 105.195 112.927 124.914 1.00 38.05  ? 551  SER A C   1 
ATOM   4466  O  O   . SER A 1 980  ? 106.285 113.508 124.915 1.00 44.73  ? 551  SER A O   1 
ATOM   4467  C  CB  . SER A 1 980  ? 103.645 114.815 124.376 1.00 29.23  ? 551  SER A CB  1 
ATOM   4468  O  OG  . SER A 1 980  ? 102.558 115.554 124.880 1.00 35.20  ? 551  SER A OG  1 
ATOM   4469  N  N   . LEU A 1 981  ? 105.062 111.653 124.586 1.00 29.54  ? 552  LEU A N   1 
ATOM   4470  C  CA  . LEU A 1 981  ? 106.243 110.861 124.323 1.00 19.89  ? 552  LEU A CA  1 
ATOM   4471  C  C   . LEU A 1 981  ? 107.017 111.469 123.178 1.00 19.77  ? 552  LEU A C   1 
ATOM   4472  O  O   . LEU A 1 981  ? 106.451 111.797 122.140 1.00 32.79  ? 552  LEU A O   1 
ATOM   4473  C  CB  . LEU A 1 981  ? 105.810 109.448 123.994 1.00 35.54  ? 552  LEU A CB  1 
ATOM   4474  C  CG  . LEU A 1 981  ? 104.740 108.914 124.968 1.00 42.36  ? 552  LEU A CG  1 
ATOM   4475  C  CD1 . LEU A 1 981  ? 104.224 107.537 124.538 1.00 44.28  ? 552  LEU A CD1 1 
ATOM   4476  C  CD2 . LEU A 1 981  ? 105.257 108.832 126.408 1.00 35.66  ? 552  LEU A CD2 1 
ATOM   4477  N  N   . LYS A 1 982  ? 108.301 111.661 123.382 1.00 24.69  ? 553  LYS A N   1 
ATOM   4478  C  CA  . LYS A 1 982  ? 109.173 112.056 122.289 1.00 35.94  ? 553  LYS A CA  1 
ATOM   4479  C  C   . LYS A 1 982  ? 109.392 110.912 121.311 1.00 42.33  ? 553  LYS A C   1 
ATOM   4480  O  O   . LYS A 1 982  ? 109.543 109.755 121.708 1.00 43.98  ? 553  LYS A O   1 
ATOM   4481  C  CB  . LYS A 1 982  ? 110.524 112.492 122.820 1.00 48.41  ? 553  LYS A CB  1 
ATOM   4482  C  CG  . LYS A 1 982  ? 110.523 113.827 123.469 1.00 52.55  ? 553  LYS A CG  1 
ATOM   4483  C  CD  . LYS A 1 982  ? 111.956 114.252 123.736 1.00 63.72  ? 553  LYS A CD  1 
ATOM   4484  C  CE  . LYS A 1 982  ? 111.987 115.596 124.448 1.00 77.11  ? 553  LYS A CE  1 
ATOM   4485  N  NZ  . LYS A 1 982  ? 111.457 115.509 125.841 1.00 71.86  ? 553  LYS A NZ  1 
ATOM   4486  N  N   . GLU A 1 983  ? 109.467 111.255 120.030 1.00 38.75  ? 554  GLU A N   1 
ATOM   4487  C  CA  . GLU A 1 983  ? 109.654 110.280 118.973 1.00 34.64  ? 554  GLU A CA  1 
ATOM   4488  C  C   . GLU A 1 983  ? 111.121 110.144 118.617 1.00 40.09  ? 554  GLU A C   1 
ATOM   4489  O  O   . GLU A 1 983  ? 111.943 111.001 118.938 1.00 52.11  ? 554  GLU A O   1 
ATOM   4490  C  CB  . GLU A 1 983  ? 108.864 110.663 117.722 1.00 50.79  ? 554  GLU A CB  1 
ATOM   4491  C  CG  . GLU A 1 983  ? 109.176 112.053 117.123 1.00 63.23  ? 554  GLU A CG  1 
ATOM   4492  C  CD  . GLU A 1 983  ? 108.430 113.226 117.804 1.00 68.60  ? 554  GLU A CD  1 
ATOM   4493  O  OE1 . GLU A 1 983  ? 108.579 114.388 117.343 1.00 64.65  ? 554  GLU A OE1 1 
ATOM   4494  O  OE2 . GLU A 1 983  ? 107.710 112.992 118.806 1.00 61.79  ? 554  GLU A OE2 1 
ATOM   4495  N  N   . LYS A 1 984  ? 111.435 109.050 117.924 1.00 46.01  ? 555  LYS A N   1 
ATOM   4496  C  CA  . LYS A 1 984  ? 112.799 108.722 117.512 1.00 49.53  ? 555  LYS A CA  1 
ATOM   4497  C  C   . LYS A 1 984  ? 113.761 108.713 118.694 1.00 50.26  ? 555  LYS A C   1 
ATOM   4498  O  O   . LYS A 1 984  ? 114.808 109.361 118.684 1.00 60.48  ? 555  LYS A O   1 
ATOM   4499  C  CB  . LYS A 1 984  ? 113.306 109.678 116.434 1.00 67.08  ? 555  LYS A CB  1 
ATOM   4500  C  CG  . LYS A 1 984  ? 112.557 109.633 115.117 1.00 74.17  ? 555  LYS A CG  1 
ATOM   4501  C  CD  . LYS A 1 984  ? 113.398 110.326 114.054 1.00 82.05  ? 555  LYS A CD  1 
ATOM   4502  C  CE  . LYS A 1 984  ? 112.661 110.416 112.740 1.00 83.11  ? 555  LYS A CE  1 
ATOM   4503  N  NZ  . LYS A 1 984  ? 111.493 111.321 112.870 1.00 81.26  ? 555  LYS A NZ  1 
ATOM   4504  N  N   . GLU A 1 985  ? 113.396 107.968 119.727 1.00 50.59  ? 556  GLU A N   1 
ATOM   4505  C  CA  . GLU A 1 985  ? 114.197 107.856 120.938 1.00 54.08  ? 556  GLU A CA  1 
ATOM   4506  C  C   . GLU A 1 985  ? 114.394 106.376 121.224 1.00 61.66  ? 556  GLU A C   1 
ATOM   4507  O  O   . GLU A 1 985  ? 113.407 105.635 121.307 1.00 57.05  ? 556  GLU A O   1 
ATOM   4508  C  CB  . GLU A 1 985  ? 113.492 108.534 122.124 1.00 60.01  ? 556  GLU A CB  1 
ATOM   4509  C  CG  . GLU A 1 985  ? 113.233 110.028 121.967 1.00 68.01  ? 556  GLU A CG  1 
ATOM   4510  C  CD  . GLU A 1 985  ? 114.486 110.870 122.209 1.00 79.98  ? 556  GLU A CD  1 
ATOM   4511  O  OE1 . GLU A 1 985  ? 115.536 110.302 122.595 1.00 77.05  ? 556  GLU A OE1 1 
ATOM   4512  O  OE2 . GLU A 1 985  ? 114.423 112.108 122.021 1.00 79.60  ? 556  GLU A OE2 1 
ATOM   4513  N  N   . LEU A 1 986  ? 115.652 105.938 121.386 1.00 51.43  ? 557  LEU A N   1 
ATOM   4514  C  CA  . LEU A 1 986  ? 115.857 104.541 121.754 1.00 39.08  ? 557  LEU A CA  1 
ATOM   4515  C  C   . LEU A 1 986  ? 115.537 104.213 123.200 1.00 48.73  ? 557  LEU A C   1 
ATOM   4516  O  O   . LEU A 1 986  ? 115.315 103.033 123.504 1.00 48.82  ? 557  LEU A O   1 
ATOM   4517  C  CB  . LEU A 1 986  ? 117.266 104.088 121.437 1.00 28.76  ? 557  LEU A CB  1 
ATOM   4518  C  CG  . LEU A 1 986  ? 117.325 104.072 119.943 1.00 40.59  ? 557  LEU A CG  1 
ATOM   4519  C  CD1 . LEU A 1 986  ? 118.655 103.535 119.564 1.00 52.74  ? 557  LEU A CD1 1 
ATOM   4520  C  CD2 . LEU A 1 986  ? 116.231 103.113 119.496 1.00 39.81  ? 557  LEU A CD2 1 
ATOM   4521  N  N   . ASN A 1 987  ? 115.490 105.198 124.090 1.00 41.64  ? 558  ASN A N   1 
ATOM   4522  C  CA  . ASN A 1 987  ? 115.220 104.884 125.474 1.00 34.84  ? 558  ASN A CA  1 
ATOM   4523  C  C   . ASN A 1 987  ? 113.740 104.670 125.647 1.00 39.66  ? 558  ASN A C   1 
ATOM   4524  O  O   . ASN A 1 987  ? 112.924 105.239 124.922 1.00 45.31  ? 558  ASN A O   1 
ATOM   4525  C  CB  . ASN A 1 987  ? 115.639 106.006 126.381 1.00 41.68  ? 558  ASN A CB  1 
ATOM   4526  C  CG  . ASN A 1 987  ? 114.982 107.273 126.001 1.00 51.95  ? 558  ASN A CG  1 
ATOM   4527  O  OD1 . ASN A 1 987  ? 114.612 107.455 124.844 1.00 50.47  ? 558  ASN A OD1 1 
ATOM   4528  N  ND2 . ASN A 1 987  ? 114.839 108.182 126.956 1.00 66.16  ? 558  ASN A ND2 1 
ATOM   4529  N  N   . VAL A 1 988  ? 113.398 103.816 126.602 1.00 51.29  ? 559  VAL A N   1 
ATOM   4530  C  CA  . VAL A 1 988  ? 112.030 103.684 127.084 1.00 47.27  ? 559  VAL A CA  1 
ATOM   4531  C  C   . VAL A 1 988  ? 111.497 105.092 127.311 1.00 48.58  ? 559  VAL A C   1 
ATOM   4532  O  O   . VAL A 1 988  ? 112.256 105.999 127.683 1.00 50.40  ? 559  VAL A O   1 
ATOM   4533  C  CB  . VAL A 1 988  ? 112.006 102.793 128.339 1.00 53.51  ? 559  VAL A CB  1 
ATOM   4534  C  CG1 . VAL A 1 988  ? 112.921 103.360 129.432 1.00 54.18  ? 559  VAL A CG1 1 
ATOM   4535  C  CG2 . VAL A 1 988  ? 110.589 102.642 128.839 1.00 62.01  ? 559  VAL A CG2 1 
ATOM   4536  N  N   . GLY A 1 989  ? 110.213 105.296 127.030 1.00 45.26  ? 560  GLY A N   1 
ATOM   4537  C  CA  . GLY A 1 989  ? 109.688 106.621 126.716 1.00 59.44  ? 560  GLY A CA  1 
ATOM   4538  C  C   . GLY A 1 989  ? 110.237 107.837 127.457 1.00 55.20  ? 560  GLY A C   1 
ATOM   4539  O  O   . GLY A 1 989  ? 110.190 107.909 128.691 1.00 51.88  ? 560  GLY A O   1 
ATOM   4540  N  N   . ARG A 1 990  ? 110.763 108.803 126.710 1.00 43.37  ? 561  ARG A N   1 
ATOM   4541  C  CA  . ARG A 1 990  ? 111.190 110.069 127.268 1.00 40.88  ? 561  ARG A CA  1 
ATOM   4542  C  C   . ARG A 1 990  ? 110.199 111.137 126.822 1.00 48.26  ? 561  ARG A C   1 
ATOM   4543  O  O   . ARG A 1 990  ? 109.808 111.164 125.651 1.00 55.67  ? 561  ARG A O   1 
ATOM   4544  C  CB  . ARG A 1 990  ? 112.591 110.404 126.798 1.00 46.00  ? 561  ARG A CB  1 
ATOM   4545  C  CG  . ARG A 1 990  ? 113.256 111.446 127.632 1.00 55.79  ? 561  ARG A CG  1 
ATOM   4546  C  CD  . ARG A 1 990  ? 114.657 111.605 127.169 1.00 66.14  ? 561  ARG A CD  1 
ATOM   4547  N  NE  . ARG A 1 990  ? 114.669 112.246 125.857 1.00 82.02  ? 561  ARG A NE  1 
ATOM   4548  C  CZ  . ARG A 1 990  ? 115.760 112.413 125.110 1.00 98.47  ? 561  ARG A CZ  1 
ATOM   4549  N  NH1 . ARG A 1 990  ? 116.939 111.966 125.538 1.00 100.61 ? 561  ARG A NH1 1 
ATOM   4550  N  NH2 . ARG A 1 990  ? 115.678 113.026 123.930 1.00 90.54  ? 561  ARG A NH2 1 
ATOM   4551  N  N   . THR A 1 991  ? 109.781 112.011 127.749 1.00 44.03  ? 562  THR A N   1 
ATOM   4552  C  CA  . THR A 1 991  ? 108.616 112.878 127.562 1.00 38.13  ? 562  THR A CA  1 
ATOM   4553  C  C   . THR A 1 991  ? 108.995 114.359 127.563 1.00 45.03  ? 562  THR A C   1 
ATOM   4554  O  O   . THR A 1 991  ? 109.983 114.757 128.185 1.00 55.74  ? 562  THR A O   1 
ATOM   4555  C  CB  . THR A 1 991  ? 107.569 112.632 128.673 1.00 41.00  ? 562  THR A CB  1 
ATOM   4556  O  OG1 . THR A 1 991  ? 108.157 112.893 129.955 1.00 44.80  ? 562  THR A OG1 1 
ATOM   4557  C  CG2 . THR A 1 991  ? 107.066 111.176 128.653 1.00 48.53  ? 562  THR A CG2 1 
ATOM   4558  N  N   . PHE A 1 992  ? 108.195 115.188 126.880 1.00 39.83  ? 563  PHE A N   1 
ATOM   4559  C  CA  . PHE A 1 992  ? 108.341 116.639 126.954 1.00 35.93  ? 563  PHE A CA  1 
ATOM   4560  C  C   . PHE A 1 992  ? 107.038 117.294 127.361 1.00 25.69  ? 563  PHE A C   1 
ATOM   4561  O  O   . PHE A 1 992  ? 105.972 116.954 126.845 1.00 31.38  ? 563  PHE A O   1 
ATOM   4562  C  CB  . PHE A 1 992  ? 108.799 117.240 125.639 1.00 43.67  ? 563  PHE A CB  1 
ATOM   4563  C  CG  . PHE A 1 992  ? 107.765 117.228 124.558 1.00 41.22  ? 563  PHE A CG  1 
ATOM   4564  C  CD1 . PHE A 1 992  ? 107.607 116.119 123.750 1.00 49.09  ? 563  PHE A CD1 1 
ATOM   4565  C  CD2 . PHE A 1 992  ? 106.976 118.343 124.319 1.00 47.04  ? 563  PHE A CD2 1 
ATOM   4566  C  CE1 . PHE A 1 992  ? 106.663 116.106 122.725 1.00 47.38  ? 563  PHE A CE1 1 
ATOM   4567  C  CE2 . PHE A 1 992  ? 106.027 118.344 123.303 1.00 49.02  ? 563  PHE A CE2 1 
ATOM   4568  C  CZ  . PHE A 1 992  ? 105.873 117.218 122.502 1.00 46.79  ? 563  PHE A CZ  1 
ATOM   4569  N  N   . GLY A 1 993  ? 107.136 118.266 128.250 1.00 23.77  ? 564  GLY A N   1 
ATOM   4570  C  CA  . GLY A 1 993  ? 105.946 118.815 128.854 1.00 31.27  ? 564  GLY A CA  1 
ATOM   4571  C  C   . GLY A 1 993  ? 105.145 119.723 127.932 1.00 31.27  ? 564  GLY A C   1 
ATOM   4572  O  O   . GLY A 1 993  ? 105.655 120.325 126.997 1.00 37.87  ? 564  GLY A O   1 
ATOM   4573  N  N   . LYS A 1 994  ? 103.862 119.821 128.215 1.00 19.76  ? 565  LYS A N   1 
ATOM   4574  C  CA  . LYS A 1 994  ? 102.996 120.792 127.590 1.00 14.82  ? 565  LYS A CA  1 
ATOM   4575  C  C   . LYS A 1 994  ? 102.175 121.454 128.681 1.00 29.19  ? 565  LYS A C   1 
ATOM   4576  O  O   . LYS A 1 994  ? 101.647 120.764 129.555 1.00 36.94  ? 565  LYS A O   1 
ATOM   4577  C  CB  . LYS A 1 994  ? 102.079 120.140 126.629 1.00 21.00  ? 565  LYS A CB  1 
ATOM   4578  C  CG  . LYS A 1 994  ? 102.776 119.401 125.533 1.00 31.62  ? 565  LYS A CG  1 
ATOM   4579  C  CD  . LYS A 1 994  ? 101.784 119.063 124.402 1.00 40.47  ? 565  LYS A CD  1 
ATOM   4580  C  CE  . LYS A 1 994  ? 100.481 118.395 124.886 1.00 35.21  ? 565  LYS A CE  1 
ATOM   4581  N  NZ  . LYS A 1 994  ? 100.698 117.137 125.653 1.00 35.30  ? 565  LYS A NZ  1 
ATOM   4582  N  N   . LEU A 1 995  ? 102.029 122.778 128.618 1.00 33.09  ? 566  LEU A N   1 
ATOM   4583  C  CA  . LEU A 1 995  ? 101.370 123.623 129.613 1.00 26.92  ? 566  LEU A CA  1 
ATOM   4584  C  C   . LEU A 1 995  ? 100.201 124.374 128.987 1.00 26.05  ? 566  LEU A C   1 
ATOM   4585  O  O   . LEU A 1 995  ? 100.091 124.438 127.759 1.00 31.20  ? 566  LEU A O   1 
ATOM   4586  C  CB  . LEU A 1 995  ? 102.364 124.640 130.173 1.00 32.35  ? 566  LEU A CB  1 
ATOM   4587  C  CG  . LEU A 1 995  ? 103.439 124.033 131.061 1.00 46.74  ? 566  LEU A CG  1 
ATOM   4588  C  CD1 . LEU A 1 995  ? 104.737 124.826 130.904 1.00 48.25  ? 566  LEU A CD1 1 
ATOM   4589  C  CD2 . LEU A 1 995  ? 102.953 124.040 132.516 1.00 51.91  ? 566  LEU A CD2 1 
ATOM   4590  N  N   . PRO A 1 996  ? 99.294  124.921 129.787 1.00 19.55  ? 567  PRO A N   1 
ATOM   4591  C  CA  . PRO A 1 996  ? 98.179  125.656 129.205 1.00 17.66  ? 567  PRO A CA  1 
ATOM   4592  C  C   . PRO A 1 996  ? 98.699  126.913 128.566 1.00 30.91  ? 567  PRO A C   1 
ATOM   4593  O  O   . PRO A 1 996  ? 99.665  127.502 129.048 1.00 40.06  ? 567  PRO A O   1 
ATOM   4594  C  CB  . PRO A 1 996  ? 97.299  125.980 130.399 1.00 25.96  ? 567  PRO A CB  1 
ATOM   4595  C  CG  . PRO A 1 996  ? 97.617  124.955 131.378 1.00 33.07  ? 567  PRO A CG  1 
ATOM   4596  C  CD  . PRO A 1 996  ? 99.085  124.685 131.211 1.00 32.35  ? 567  PRO A CD  1 
ATOM   4597  N  N   . TYR A 1 997  ? 98.037  127.337 127.487 1.00 33.02  ? 568  TYR A N   1 
ATOM   4598  C  CA  . TYR A 1 997  ? 98.593  128.384 126.633 1.00 28.66  ? 568  TYR A CA  1 
ATOM   4599  C  C   . TYR A 1 997  ? 99.097  129.586 127.406 1.00 27.94  ? 568  TYR A C   1 
ATOM   4600  O  O   . TYR A 1 997  ? 100.161 130.111 127.045 1.00 40.75  ? 568  TYR A O   1 
ATOM   4601  C  CB  . TYR A 1 997  ? 97.572  128.845 125.581 1.00 41.04  ? 568  TYR A CB  1 
ATOM   4602  C  CG  . TYR A 1 997  ? 98.033  130.083 124.835 1.00 45.60  ? 568  TYR A CG  1 
ATOM   4603  C  CD1 . TYR A 1 997  ? 99.138  130.035 124.002 1.00 54.52  ? 568  TYR A CD1 1 
ATOM   4604  C  CD2 . TYR A 1 997  ? 97.370  131.295 124.960 1.00 53.09  ? 568  TYR A CD2 1 
ATOM   4605  C  CE1 . TYR A 1 997  ? 99.586  131.164 123.317 1.00 53.90  ? 568  TYR A CE1 1 
ATOM   4606  C  CE2 . TYR A 1 997  ? 97.809  132.431 124.271 1.00 56.94  ? 568  TYR A CE2 1 
ATOM   4607  C  CZ  . TYR A 1 997  ? 98.924  132.349 123.447 1.00 53.71  ? 568  TYR A CZ  1 
ATOM   4608  O  OH  . TYR A 1 997  ? 99.396  133.443 122.751 1.00 58.50  ? 568  TYR A OH  1 
ATOM   4609  N  N   . PRO A 1 998  ? 98.439  130.061 128.449 1.00 18.49  ? 569  PRO A N   1 
ATOM   4610  C  CA  . PRO A 1 998  ? 98.992  131.221 129.125 1.00 22.70  ? 569  PRO A CA  1 
ATOM   4611  C  C   . PRO A 1 998  ? 100.240 130.886 129.922 1.00 47.05  ? 569  PRO A C   1 
ATOM   4612  O  O   . PRO A 1 998  ? 101.212 131.664 129.905 1.00 52.71  ? 569  PRO A O   1 
ATOM   4613  C  CB  . PRO A 1 998  ? 97.850  131.666 130.020 1.00 28.51  ? 569  PRO A CB  1 
ATOM   4614  C  CG  . PRO A 1 998  ? 96.679  131.131 129.389 1.00 36.87  ? 569  PRO A CG  1 
ATOM   4615  C  CD  . PRO A 1 998  ? 97.071  129.813 128.873 1.00 24.64  ? 569  PRO A CD  1 
ATOM   4616  N  N   . THR A 1 999  ? 100.262 129.747 130.631 1.00 41.88  ? 570  THR A N   1 
ATOM   4617  C  CA  . THR A 1 999  ? 101.510 129.360 131.283 1.00 27.89  ? 570  THR A CA  1 
ATOM   4618  C  C   . THR A 1 999  ? 102.590 129.165 130.236 1.00 25.85  ? 570  THR A C   1 
ATOM   4619  O  O   . THR A 1 999  ? 103.755 129.456 130.494 1.00 39.94  ? 570  THR A O   1 
ATOM   4620  C  CB  . THR A 1 999  ? 101.342 128.089 132.128 1.00 33.64  ? 570  THR A CB  1 
ATOM   4621  O  OG1 . THR A 1 999  ? 100.145 128.155 132.915 1.00 35.88  ? 570  THR A OG1 1 
ATOM   4622  C  CG2 . THR A 1 999  ? 102.504 127.964 133.103 1.00 39.29  ? 570  THR A CG2 1 
ATOM   4623  N  N   . ARG A 1 1000 ? 102.214 128.717 129.041 1.00 25.75  ? 571  ARG A N   1 
ATOM   4624  C  CA  . ARG A 1 1000 ? 103.182 128.564 127.971 1.00 25.53  ? 571  ARG A CA  1 
ATOM   4625  C  C   . ARG A 1 1000 ? 103.765 129.896 127.559 1.00 38.30  ? 571  ARG A C   1 
ATOM   4626  O  O   . ARG A 1 1000 ? 104.967 129.990 127.286 1.00 52.22  ? 571  ARG A O   1 
ATOM   4627  C  CB  . ARG A 1 1000 ? 102.546 127.907 126.769 1.00 34.38  ? 571  ARG A CB  1 
ATOM   4628  C  CG  . ARG A 1 1000 ? 103.495 127.818 125.605 1.00 48.43  ? 571  ARG A CG  1 
ATOM   4629  C  CD  . ARG A 1 1000 ? 104.729 126.974 125.954 1.00 65.07  ? 571  ARG A CD  1 
ATOM   4630  N  NE  . ARG A 1 1000 ? 105.893 127.316 125.122 1.00 75.73  ? 571  ARG A NE  1 
ATOM   4631  C  CZ  . ARG A 1 1000 ? 107.031 126.617 125.063 1.00 77.88  ? 571  ARG A CZ  1 
ATOM   4632  N  NH1 . ARG A 1 1000 ? 107.183 125.507 125.782 1.00 70.64  ? 571  ARG A NH1 1 
ATOM   4633  N  NH2 . ARG A 1 1000 ? 108.018 127.022 124.269 1.00 78.40  ? 571  ARG A NH2 1 
ATOM   4634  N  N   . ASN A 1 1001 ? 102.937 130.937 127.483 1.00 36.95  ? 572  ASN A N   1 
ATOM   4635  C  CA  . ASN A 1 1001 ? 103.485 132.264 127.220 1.00 35.52  ? 572  ASN A CA  1 
ATOM   4636  C  C   . ASN A 1 1001 ? 104.432 132.696 128.330 1.00 41.60  ? 572  ASN A C   1 
ATOM   4637  O  O   . ASN A 1 1001 ? 105.470 133.306 128.055 1.00 48.12  ? 572  ASN A O   1 
ATOM   4638  C  CB  . ASN A 1 1001 ? 102.380 133.295 127.050 1.00 40.25  ? 572  ASN A CB  1 
ATOM   4639  C  CG  . ASN A 1 1001 ? 101.603 133.114 125.753 1.00 59.38  ? 572  ASN A CG  1 
ATOM   4640  O  OD1 . ASN A 1 1001 ? 102.085 132.473 124.815 1.00 61.90  ? 572  ASN A OD1 1 
ATOM   4641  N  ND2 . ASN A 1 1001 ? 100.404 133.705 125.683 1.00 58.21  ? 572  ASN A ND2 1 
ATOM   4642  N  N   . VAL A 1 1002 ? 104.102 132.393 129.588 1.00 31.77  ? 573  VAL A N   1 
ATOM   4643  C  CA  . VAL A 1 1002 ? 105.024 132.762 130.659 1.00 24.39  ? 573  VAL A CA  1 
ATOM   4644  C  C   . VAL A 1 1002 ? 106.347 132.046 130.494 1.00 31.56  ? 573  VAL A C   1 
ATOM   4645  O  O   . VAL A 1 1002 ? 107.416 132.621 130.718 1.00 42.97  ? 573  VAL A O   1 
ATOM   4646  C  CB  . VAL A 1 1002 ? 104.426 132.489 132.041 1.00 34.46  ? 573  VAL A CB  1 
ATOM   4647  C  CG1 . VAL A 1 1002 ? 105.506 132.632 133.092 1.00 33.69  ? 573  VAL A CG1 1 
ATOM   4648  C  CG2 . VAL A 1 1002 ? 103.356 133.505 132.335 1.00 48.01  ? 573  VAL A CG2 1 
ATOM   4649  N  N   . GLN A 1 1003 ? 106.305 130.781 130.113 1.00 36.89  ? 574  GLN A N   1 
ATOM   4650  C  CA  . GLN A 1 1003 ? 107.552 130.057 129.909 1.00 37.86  ? 574  GLN A CA  1 
ATOM   4651  C  C   . GLN A 1 1003 ? 108.349 130.643 128.766 1.00 39.50  ? 574  GLN A C   1 
ATOM   4652  O  O   . GLN A 1 1003 ? 109.568 130.799 128.871 1.00 53.27  ? 574  GLN A O   1 
ATOM   4653  C  CB  . GLN A 1 1003 ? 107.288 128.594 129.632 1.00 40.76  ? 574  GLN A CB  1 
ATOM   4654  C  CG  . GLN A 1 1003 ? 108.521 127.884 129.173 1.00 44.48  ? 574  GLN A CG  1 
ATOM   4655  C  CD  . GLN A 1 1003 ? 108.183 126.529 128.628 1.00 60.73  ? 574  GLN A CD  1 
ATOM   4656  O  OE1 . GLN A 1 1003 ? 107.017 126.122 128.638 1.00 60.17  ? 574  GLN A OE1 1 
ATOM   4657  N  NE2 . GLN A 1 1003 ? 109.193 125.812 128.148 1.00 65.42  ? 574  GLN A NE2 1 
ATOM   4658  N  N   . THR A 1 1004 ? 107.689 130.973 127.665 1.00 35.12  ? 575  THR A N   1 
ATOM   4659  C  CA  . THR A 1 1004 ? 108.437 131.527 126.550 1.00 36.07  ? 575  THR A CA  1 
ATOM   4660  C  C   . THR A 1 1004 ? 109.028 132.875 126.915 1.00 34.57  ? 575  THR A C   1 
ATOM   4661  O  O   . THR A 1 1004 ? 110.149 133.199 126.514 1.00 41.69  ? 575  THR A O   1 
ATOM   4662  C  CB  . THR A 1 1004 ? 107.555 131.657 125.321 1.00 50.85  ? 575  THR A CB  1 
ATOM   4663  O  OG1 . THR A 1 1004 ? 106.875 130.420 125.100 1.00 59.07  ? 575  THR A OG1 1 
ATOM   4664  C  CG2 . THR A 1 1004 ? 108.414 131.940 124.108 1.00 67.15  ? 575  THR A CG2 1 
ATOM   4665  N  N   . LEU A 1 1005 ? 108.293 133.676 127.670 1.00 32.86  ? 576  LEU A N   1 
ATOM   4666  C  CA  . LEU A 1 1005 ? 108.844 134.951 128.088 1.00 28.35  ? 576  LEU A CA  1 
ATOM   4667  C  C   . LEU A 1 1005 ? 110.042 134.749 128.990 1.00 42.17  ? 576  LEU A C   1 
ATOM   4668  O  O   . LEU A 1 1005 ? 111.029 135.470 128.861 1.00 54.01  ? 576  LEU A O   1 
ATOM   4669  C  CB  . LEU A 1 1005 ? 107.793 135.797 128.799 1.00 39.78  ? 576  LEU A CB  1 
ATOM   4670  C  CG  . LEU A 1 1005 ? 108.260 137.197 129.223 1.00 50.24  ? 576  LEU A CG  1 
ATOM   4671  C  CD1 . LEU A 1 1005 ? 108.689 137.976 127.981 1.00 61.41  ? 576  LEU A CD1 1 
ATOM   4672  C  CD2 . LEU A 1 1005 ? 107.207 137.987 130.037 1.00 45.95  ? 576  LEU A CD2 1 
ATOM   4673  N  N   . CYS A 1 1006 ? 109.976 133.799 129.938 1.00 45.36  ? 577  CYS A N   1 
ATOM   4674  C  CA  . CYS A 1 1006 ? 111.108 133.598 130.853 1.00 38.02  ? 577  CYS A CA  1 
ATOM   4675  C  C   . CYS A 1 1006 ? 112.325 133.102 130.106 1.00 36.42  ? 577  CYS A C   1 
ATOM   4676  O  O   . CYS A 1 1006 ? 113.453 133.481 130.424 1.00 45.36  ? 577  CYS A O   1 
ATOM   4677  C  CB  . CYS A 1 1006 ? 110.760 132.621 131.971 1.00 37.69  ? 577  CYS A CB  1 
ATOM   4678  S  SG  . CYS A 1 1006 ? 109.558 133.277 133.133 1.00 57.94  ? 577  CYS A SG  1 
ATOM   4679  N  N   . GLU A 1 1007 ? 112.115 132.259 129.108 1.00 37.46  ? 578  GLU A N   1 
ATOM   4680  C  CA  . GLU A 1 1007 ? 113.242 131.791 128.326 1.00 36.58  ? 578  GLU A CA  1 
ATOM   4681  C  C   . GLU A 1 1007 ? 113.813 132.915 127.487 1.00 42.78  ? 578  GLU A C   1 
ATOM   4682  O  O   . GLU A 1 1007 ? 115.034 133.033 127.351 1.00 57.17  ? 578  GLU A O   1 
ATOM   4683  C  CB  . GLU A 1 1007 ? 112.826 130.630 127.431 1.00 51.08  ? 578  GLU A CB  1 
ATOM   4684  C  CG  . GLU A 1 1007 ? 112.250 129.436 128.209 1.00 72.94  ? 578  GLU A CG  1 
ATOM   4685  C  CD  . GLU A 1 1007 ? 113.046 129.085 129.480 1.00 80.15  ? 578  GLU A CD  1 
ATOM   4686  O  OE1 . GLU A 1 1007 ? 114.291 128.961 129.412 1.00 68.21  ? 578  GLU A OE1 1 
ATOM   4687  O  OE2 . GLU A 1 1007 ? 112.407 128.938 130.557 1.00 69.67  ? 578  GLU A OE2 1 
ATOM   4688  N  N   . ALA A 1 1008 ? 112.952 133.745 126.903 1.00 40.59  ? 579  ALA A N   1 
ATOM   4689  C  CA  . ALA A 1 1008 ? 113.451 134.862 126.115 1.00 43.22  ? 579  ALA A CA  1 
ATOM   4690  C  C   . ALA A 1 1008 ? 114.161 135.863 126.999 1.00 44.53  ? 579  ALA A C   1 
ATOM   4691  O  O   . ALA A 1 1008 ? 115.223 136.376 126.635 1.00 57.48  ? 579  ALA A O   1 
ATOM   4692  C  CB  . ALA A 1 1008 ? 112.307 135.536 125.360 1.00 59.06  ? 579  ALA A CB  1 
ATOM   4693  N  N   . LEU A 1 1009 ? 113.600 136.134 128.172 1.00 33.26  ? 580  LEU A N   1 
ATOM   4694  C  CA  . LEU A 1 1009 ? 114.223 137.068 129.084 1.00 32.00  ? 580  LEU A CA  1 
ATOM   4695  C  C   . LEU A 1 1009 ? 115.604 136.594 129.517 1.00 51.19  ? 580  LEU A C   1 
ATOM   4696  O  O   . LEU A 1 1009 ? 116.563 137.372 129.490 1.00 59.48  ? 580  LEU A O   1 
ATOM   4697  C  CB  . LEU A 1 1009 ? 113.343 137.275 130.293 1.00 34.80  ? 580  LEU A CB  1 
ATOM   4698  C  CG  . LEU A 1 1009 ? 112.162 138.148 129.948 1.00 50.50  ? 580  LEU A CG  1 
ATOM   4699  C  CD1 . LEU A 1 1009 ? 111.322 138.367 131.208 1.00 57.62  ? 580  LEU A CD1 1 
ATOM   4700  C  CD2 . LEU A 1 1009 ? 112.643 139.464 129.328 1.00 57.54  ? 580  LEU A CD2 1 
ATOM   4701  N  N   . LEU A 1 1010 ? 115.736 135.328 129.918 1.00 47.04  ? 581  LEU A N   1 
ATOM   4702  C  CA  . LEU A 1 1010 ? 117.032 134.851 130.391 1.00 36.02  ? 581  LEU A CA  1 
ATOM   4703  C  C   . LEU A 1 1010 ? 118.054 134.849 129.271 1.00 40.49  ? 581  LEU A C   1 
ATOM   4704  O  O   . LEU A 1 1010 ? 119.184 135.302 129.459 1.00 56.52  ? 581  LEU A O   1 
ATOM   4705  C  CB  . LEU A 1 1010 ? 116.901 133.457 130.997 1.00 42.26  ? 581  LEU A CB  1 
ATOM   4706  C  CG  . LEU A 1 1010 ? 116.106 133.385 132.313 1.00 46.50  ? 581  LEU A CG  1 
ATOM   4707  C  CD1 . LEU A 1 1010 ? 115.847 131.941 132.781 1.00 37.58  ? 581  LEU A CD1 1 
ATOM   4708  C  CD2 . LEU A 1 1010 ? 116.788 134.193 133.415 1.00 45.51  ? 581  LEU A CD2 1 
ATOM   4709  N  N   . ALA A 1 1011 ? 117.679 134.368 128.091 1.00 43.65  ? 582  ALA A N   1 
ATOM   4710  C  CA  . ALA A 1 1011 ? 118.660 134.245 127.016 1.00 55.94  ? 582  ALA A CA  1 
ATOM   4711  C  C   . ALA A 1 1011 ? 119.267 135.597 126.645 1.00 61.99  ? 582  ALA A C   1 
ATOM   4712  O  O   . ALA A 1 1011 ? 120.484 135.698 126.444 1.00 66.16  ? 582  ALA A O   1 
ATOM   4713  C  CB  . ALA A 1 1011 ? 118.023 133.591 125.788 1.00 64.39  ? 582  ALA A CB  1 
ATOM   4714  N  N   . ASP A 1 1012 ? 118.443 136.650 126.548 1.00 57.19  ? 583  ASP A N   1 
ATOM   4715  C  CA  . ASP A 1 1012 ? 118.960 137.968 126.172 1.00 59.75  ? 583  ASP A CA  1 
ATOM   4716  C  C   . ASP A 1 1012 ? 119.636 138.702 127.326 1.00 59.59  ? 583  ASP A C   1 
ATOM   4717  O  O   . ASP A 1 1012 ? 120.449 139.597 127.079 1.00 64.34  ? 583  ASP A O   1 
ATOM   4718  C  CB  . ASP A 1 1012 ? 117.843 138.857 125.593 1.00 75.90  ? 583  ASP A CB  1 
ATOM   4719  C  CG  . ASP A 1 1012 ? 117.148 138.241 124.346 1.00 86.85  ? 583  ASP A CG  1 
ATOM   4720  O  OD1 . ASP A 1 1012 ? 117.818 137.530 123.560 1.00 81.23  ? 583  ASP A OD1 1 
ATOM   4721  O  OD2 . ASP A 1 1012 ? 115.935 138.507 124.133 1.00 72.42  ? 583  ASP A OD2 1 
ATOM   4722  N  N   . GLY A 1 1013 ? 119.327 138.345 128.570 1.00 59.73  ? 584  GLY A N   1 
ATOM   4723  C  CA  . GLY A 1 1013 ? 119.857 139.007 129.749 1.00 51.06  ? 584  GLY A CA  1 
ATOM   4724  C  C   . GLY A 1 1013 ? 120.801 138.152 130.586 1.00 59.99  ? 584  GLY A C   1 
ATOM   4725  O  O   . GLY A 1 1013 ? 121.999 138.062 130.292 1.00 64.66  ? 584  GLY A O   1 
ATOM   4726  N  N   . LEU A 1 1014 ? 120.252 137.522 131.642 1.00 61.44  ? 585  LEU A N   1 
ATOM   4727  C  CA  . LEU A 1 1014 ? 121.044 136.872 132.694 1.00 53.34  ? 585  LEU A CA  1 
ATOM   4728  C  C   . LEU A 1 1014 ? 121.853 135.688 132.189 1.00 44.34  ? 585  LEU A C   1 
ATOM   4729  O  O   . LEU A 1 1014 ? 123.001 135.496 132.596 1.00 51.92  ? 585  LEU A O   1 
ATOM   4730  C  CB  . LEU A 1 1014 ? 120.129 136.392 133.814 1.00 51.10  ? 585  LEU A CB  1 
ATOM   4731  C  CG  . LEU A 1 1014 ? 120.908 136.155 135.093 1.00 55.60  ? 585  LEU A CG  1 
ATOM   4732  C  CD1 . LEU A 1 1014 ? 121.642 137.444 135.344 1.00 60.39  ? 585  LEU A CD1 1 
ATOM   4733  C  CD2 . LEU A 1 1014 ? 119.992 135.790 136.269 1.00 59.98  ? 585  LEU A CD2 1 
ATOM   4734  N  N   . ALA A 1 1015 ? 121.257 134.850 131.356 1.00 44.42  ? 586  ALA A N   1 
ATOM   4735  C  CA  . ALA A 1 1015 ? 121.959 133.657 130.932 1.00 45.52  ? 586  ALA A CA  1 
ATOM   4736  C  C   . ALA A 1 1015 ? 123.215 134.006 130.183 1.00 42.67  ? 586  ALA A C   1 
ATOM   4737  O  O   . ALA A 1 1015 ? 124.104 133.161 130.076 1.00 55.54  ? 586  ALA A O   1 
ATOM   4738  C  CB  . ALA A 1 1015 ? 121.065 132.770 130.055 1.00 60.91  ? 586  ALA A CB  1 
ATOM   4739  N  N   . LYS A 1 1016 ? 123.318 135.223 129.663 1.00 41.85  ? 587  LYS A N   1 
ATOM   4740  C  CA  . LYS A 1 1016 ? 124.598 135.606 129.092 1.00 54.08  ? 587  LYS A CA  1 
ATOM   4741  C  C   . LYS A 1 1016 ? 125.696 135.726 130.147 1.00 63.20  ? 587  LYS A C   1 
ATOM   4742  O  O   . LYS A 1 1016 ? 126.871 135.812 129.769 1.00 68.18  ? 587  LYS A O   1 
ATOM   4743  C  CB  . LYS A 1 1016 ? 124.491 136.919 128.316 1.00 62.68  ? 587  LYS A CB  1 
ATOM   4744  C  CG  . LYS A 1 1016 ? 123.864 136.799 126.939 1.00 67.45  ? 587  LYS A CG  1 
ATOM   4745  C  CD  . LYS A 1 1016 ? 123.799 138.175 126.256 1.00 74.66  ? 587  LYS A CD  1 
ATOM   4746  C  CE  . LYS A 1 1016 ? 123.397 138.071 124.782 1.00 76.69  ? 587  LYS A CE  1 
ATOM   4747  N  NZ  . LYS A 1 1016 ? 122.117 137.322 124.582 1.00 74.71  ? 587  LYS A NZ  1 
ATOM   4748  N  N   . ALA A 1 1017 ? 125.359 135.729 131.448 1.00 53.39  ? 588  ALA A N   1 
ATOM   4749  C  CA  . ALA A 1 1017 ? 126.383 135.743 132.497 1.00 49.83  ? 588  ALA A CA  1 
ATOM   4750  C  C   . ALA A 1 1017 ? 127.061 134.384 132.704 1.00 52.14  ? 588  ALA A C   1 
ATOM   4751  O  O   . ALA A 1 1017 ? 128.086 134.322 133.389 1.00 55.82  ? 588  ALA A O   1 
ATOM   4752  C  CB  . ALA A 1 1017 ? 125.779 136.231 133.817 1.00 55.01  ? 588  ALA A CB  1 
ATOM   4753  N  N   . PHE A 1 1018 ? 126.514 133.305 132.147 1.00 48.51  ? 589  PHE A N   1 
ATOM   4754  C  CA  . PHE A 1 1018 ? 127.089 131.966 132.238 1.00 37.52  ? 589  PHE A CA  1 
ATOM   4755  C  C   . PHE A 1 1018 ? 127.213 131.414 130.835 1.00 45.32  ? 589  PHE A C   1 
ATOM   4756  O  O   . PHE A 1 1018 ? 126.444 130.538 130.426 1.00 47.68  ? 589  PHE A O   1 
ATOM   4757  C  CB  . PHE A 1 1018 ? 126.231 131.062 133.099 1.00 31.04  ? 589  PHE A CB  1 
ATOM   4758  C  CG  . PHE A 1 1018 ? 125.828 131.691 134.360 1.00 40.21  ? 589  PHE A CG  1 
ATOM   4759  C  CD1 . PHE A 1 1018 ? 124.693 132.477 134.430 1.00 51.00  ? 589  PHE A CD1 1 
ATOM   4760  C  CD2 . PHE A 1 1018 ? 126.589 131.506 135.503 1.00 46.59  ? 589  PHE A CD2 1 
ATOM   4761  C  CE1 . PHE A 1 1018 ? 124.316 133.092 135.636 1.00 54.34  ? 589  PHE A CE1 1 
ATOM   4762  C  CE2 . PHE A 1 1018 ? 126.225 132.093 136.714 1.00 49.01  ? 589  PHE A CE2 1 
ATOM   4763  C  CZ  . PHE A 1 1018 ? 125.088 132.895 136.782 1.00 53.33  ? 589  PHE A CZ  1 
ATOM   4764  N  N   . PRO A 1 1019 ? 128.161 131.894 130.082 1.00 49.10  ? 590  PRO A N   1 
ATOM   4765  C  CA  . PRO A 1 1019 ? 128.236 131.510 128.677 1.00 54.01  ? 590  PRO A CA  1 
ATOM   4766  C  C   . PRO A 1 1019 ? 128.669 130.070 128.553 1.00 63.78  ? 590  PRO A C   1 
ATOM   4767  O  O   . PRO A 1 1019 ? 129.840 129.738 128.764 1.00 73.63  ? 590  PRO A O   1 
ATOM   4768  C  CB  . PRO A 1 1019 ? 129.289 132.465 128.109 1.00 64.19  ? 590  PRO A CB  1 
ATOM   4769  C  CG  . PRO A 1 1019 ? 130.150 132.800 129.279 1.00 58.41  ? 590  PRO A CG  1 
ATOM   4770  C  CD  . PRO A 1 1019 ? 129.233 132.822 130.466 1.00 54.39  ? 590  PRO A CD  1 
ATOM   4771  N  N   . SER A 1 1020 ? 127.732 129.200 128.223 1.00 70.17  ? 591  SER A N   1 
ATOM   4772  C  CA  . SER A 1 1020 ? 128.034 127.783 128.110 1.00 82.10  ? 591  SER A CA  1 
ATOM   4773  C  C   . SER A 1 1020 ? 128.316 127.355 126.679 1.00 77.17  ? 591  SER A C   1 
ATOM   4774  O  O   . SER A 1 1020 ? 128.546 126.170 126.430 1.00 78.94  ? 591  SER A O   1 
ATOM   4775  C  CB  . SER A 1 1020 ? 126.884 126.949 128.706 1.00 86.56  ? 591  SER A CB  1 
ATOM   4776  O  OG  . SER A 1 1020 ? 125.644 127.207 128.055 1.00 84.60  ? 591  SER A OG  1 
ATOM   4777  N  N   . ASN A 1 1021 ? 128.301 128.276 125.736 1.00 77.89  ? 592  ASN A N   1 
ATOM   4778  C  CA  . ASN A 1 1021 ? 128.610 127.908 124.369 1.00 92.94  ? 592  ASN A CA  1 
ATOM   4779  C  C   . ASN A 1 1021 ? 130.114 127.919 124.115 1.00 99.50  ? 592  ASN A C   1 
ATOM   4780  O  O   . ASN A 1 1021 ? 130.543 127.671 122.980 1.00 99.70  ? 592  ASN A O   1 
ATOM   4781  C  CB  . ASN A 1 1021 ? 127.873 128.852 123.395 1.00 105.69 ? 592  ASN A CB  1 
ATOM   4782  C  CG  . ASN A 1 1021 ? 127.782 128.293 121.967 1.00 109.86 ? 592  ASN A CG  1 
ATOM   4783  O  OD1 . ASN A 1 1021 ? 127.811 127.077 121.760 1.00 105.44 ? 592  ASN A OD1 1 
ATOM   4784  N  ND2 . ASN A 1 1021 ? 127.662 129.187 120.983 1.00 100.32 ? 592  ASN A ND2 1 
ATOM   4785  N  N   . MET A 1 1022 ? 130.921 128.183 125.146 1.00 90.05  ? 593  MET A N   1 
ATOM   4786  C  CA  . MET A 1 1022 ? 132.358 128.369 124.966 1.00 85.51  ? 593  MET A CA  1 
ATOM   4787  C  C   . MET A 1 1022 ? 132.973 127.045 124.568 1.00 84.94  ? 593  MET A C   1 
ATOM   4788  O  O   . MET A 1 1022 ? 133.201 126.176 125.411 1.00 90.90  ? 593  MET A O   1 
ATOM   4789  C  CB  . MET A 1 1022 ? 132.999 128.887 126.242 1.00 88.17  ? 593  MET A CB  1 
ATOM   4790  C  CG  . MET A 1 1022 ? 132.337 130.127 126.768 1.00 100.14 ? 593  MET A CG  1 
ATOM   4791  S  SD  . MET A 1 1022 ? 133.084 130.660 128.315 1.00 124.86 ? 593  MET A SD  1 
ATOM   4792  C  CE  . MET A 1 1022 ? 134.754 130.991 127.748 1.00 110.82 ? 593  MET A CE  1 
ATOM   4793  N  N   . MET A 1 1023 ? 133.246 126.887 123.282 1.00 81.16  ? 594  MET A N   1 
ATOM   4794  C  CA  . MET A 1 1023 ? 133.835 125.658 122.780 1.00 86.96  ? 594  MET A CA  1 
ATOM   4795  C  C   . MET A 1 1023 ? 135.345 125.719 122.953 1.00 88.03  ? 594  MET A C   1 
ATOM   4796  O  O   . MET A 1 1023 ? 135.981 126.707 122.569 1.00 93.13  ? 594  MET A O   1 
ATOM   4797  C  CB  . MET A 1 1023 ? 133.460 125.441 121.314 1.00 99.73  ? 594  MET A CB  1 
ATOM   4798  C  CG  . MET A 1 1023 ? 131.949 125.341 121.037 1.00 111.14 ? 594  MET A CG  1 
ATOM   4799  S  SD  . MET A 1 1023 ? 131.107 123.873 121.718 1.00 123.63 ? 594  MET A SD  1 
ATOM   4800  C  CE  . MET A 1 1023 ? 130.209 124.551 123.124 1.00 100.77 ? 594  MET A CE  1 
ATOM   4801  N  N   . VAL A 1 1024 ? 135.912 124.669 123.539 1.00 85.43  ? 595  VAL A N   1 
ATOM   4802  C  CA  . VAL A 1 1024 ? 137.334 124.617 123.853 1.00 90.14  ? 595  VAL A CA  1 
ATOM   4803  C  C   . VAL A 1 1024 ? 137.909 123.331 123.268 1.00 82.84  ? 595  VAL A C   1 
ATOM   4804  O  O   . VAL A 1 1024 ? 137.495 122.230 123.654 1.00 83.42  ? 595  VAL A O   1 
ATOM   4805  C  CB  . VAL A 1 1024 ? 137.590 124.699 125.374 1.00 94.57  ? 595  VAL A CB  1 
ATOM   4806  C  CG1 . VAL A 1 1024 ? 139.083 124.492 125.707 1.00 89.98  ? 595  VAL A CG1 1 
ATOM   4807  C  CG2 . VAL A 1 1024 ? 137.082 126.042 125.944 1.00 90.56  ? 595  VAL A CG2 1 
ATOM   4808  N  N   . VAL A 1 1025 ? 138.840 123.471 122.326 1.00 77.74  ? 596  VAL A N   1 
ATOM   4809  C  CA  . VAL A 1 1025 ? 139.693 122.376 121.872 1.00 72.60  ? 596  VAL A CA  1 
ATOM   4810  C  C   . VAL A 1 1025 ? 141.126 122.819 122.102 1.00 75.57  ? 596  VAL A C   1 
ATOM   4811  O  O   . VAL A 1 1025 ? 141.610 123.748 121.443 1.00 83.40  ? 596  VAL A O   1 
ATOM   4812  C  CB  . VAL A 1 1025 ? 139.458 122.016 120.402 1.00 77.39  ? 596  VAL A CB  1 
ATOM   4813  C  CG1 . VAL A 1 1025 ? 140.310 120.811 120.025 1.00 73.35  ? 596  VAL A CG1 1 
ATOM   4814  C  CG2 . VAL A 1 1025 ? 137.970 121.726 120.145 1.00 76.28  ? 596  VAL A CG2 1 
ATOM   4815  N  N   . THR A 1 1026 ? 141.810 122.156 123.029 1.00 70.44  ? 597  THR A N   1 
ATOM   4816  C  CA  . THR A 1 1026 ? 143.067 122.697 123.516 1.00 69.64  ? 597  THR A CA  1 
ATOM   4817  C  C   . THR A 1 1026 ? 144.174 122.607 122.472 1.00 76.98  ? 597  THR A C   1 
ATOM   4818  O  O   . THR A 1 1026 ? 145.048 123.481 122.426 1.00 88.47  ? 597  THR A O   1 
ATOM   4819  C  CB  . THR A 1 1026 ? 143.469 121.987 124.807 1.00 74.91  ? 597  THR A CB  1 
ATOM   4820  O  OG1 . THR A 1 1026 ? 143.618 120.580 124.562 1.00 74.95  ? 597  THR A OG1 1 
ATOM   4821  C  CG2 . THR A 1 1026 ? 142.414 122.233 125.909 1.00 68.41  ? 597  THR A CG2 1 
ATOM   4822  N  N   . GLU A 1 1027 ? 144.150 121.585 121.616 1.00 74.96  ? 598  GLU A N   1 
ATOM   4823  C  CA  . GLU A 1 1027 ? 145.275 121.355 120.707 1.00 83.94  ? 598  GLU A CA  1 
ATOM   4824  C  C   . GLU A 1 1027 ? 145.403 122.440 119.639 1.00 85.21  ? 598  GLU A C   1 
ATOM   4825  O  O   . GLU A 1 1027 ? 146.513 122.713 119.162 1.00 83.58  ? 598  GLU A O   1 
ATOM   4826  C  CB  . GLU A 1 1027 ? 145.145 119.978 120.041 1.00 86.74  ? 598  GLU A CB  1 
ATOM   4827  C  CG  . GLU A 1 1027 ? 145.361 118.763 120.978 1.00 87.96  ? 598  GLU A CG  1 
ATOM   4828  C  CD  . GLU A 1 1027 ? 144.167 118.466 121.915 1.00 86.97  ? 598  GLU A CD  1 
ATOM   4829  O  OE1 . GLU A 1 1027 ? 143.073 119.035 121.697 1.00 85.96  ? 598  GLU A OE1 1 
ATOM   4830  O  OE2 . GLU A 1 1027 ? 144.321 117.655 122.864 1.00 75.61  ? 598  GLU A OE2 1 
ATOM   4831  N  N   . ARG A 1 1028 ? 144.286 123.053 119.241 1.00 86.85  ? 599  ARG A N   1 
ATOM   4832  C  CA  . ARG A 1 1028 ? 144.305 124.015 118.144 1.00 86.61  ? 599  ARG A CA  1 
ATOM   4833  C  C   . ARG A 1 1028 ? 144.671 125.419 118.611 1.00 93.87  ? 599  ARG A C   1 
ATOM   4834  O  O   . ARG A 1 1028 ? 145.281 126.180 117.850 1.00 94.07  ? 599  ARG A O   1 
ATOM   4835  C  CB  . ARG A 1 1028 ? 142.938 124.036 117.455 1.00 89.49  ? 599  ARG A CB  1 
ATOM   4836  C  CG  . ARG A 1 1028 ? 142.207 122.681 117.470 1.00 88.48  ? 599  ARG A CG  1 
ATOM   4837  C  CD  . ARG A 1 1028 ? 140.887 122.718 116.679 1.00 81.41  ? 599  ARG A CD  1 
ATOM   4838  N  NE  . ARG A 1 1028 ? 141.090 122.543 115.241 1.00 81.89  ? 599  ARG A NE  1 
ATOM   4839  C  CZ  . ARG A 1 1028 ? 141.009 121.378 114.602 1.00 70.92  ? 599  ARG A CZ  1 
ATOM   4840  N  NH1 . ARG A 1 1028 ? 140.711 120.274 115.278 1.00 62.10  ? 599  ARG A NH1 1 
ATOM   4841  N  NH2 . ARG A 1 1028 ? 141.213 121.318 113.286 1.00 58.23  ? 599  ARG A NH2 1 
ATOM   4842  N  N   . GLU A 1 1029 ? 144.308 125.774 119.845 1.00 95.54  ? 600  GLU A N   1 
ATOM   4843  C  CA  . GLU A 1 1029 ? 144.474 127.138 120.333 1.00 104.50 ? 600  GLU A CA  1 
ATOM   4844  C  C   . GLU A 1 1029 ? 145.953 127.488 120.520 1.00 107.12 ? 600  GLU A C   1 
ATOM   4845  O  O   . GLU A 1 1029 ? 146.786 126.630 120.831 1.00 108.33 ? 600  GLU A O   1 
ATOM   4846  C  CB  . GLU A 1 1029 ? 143.706 127.322 121.649 1.00 101.87 ? 600  GLU A CB  1 
ATOM   4847  C  CG  . GLU A 1 1029 ? 142.175 127.209 121.513 1.00 103.70 ? 600  GLU A CG  1 
ATOM   4848  C  CD  . GLU A 1 1029 ? 141.439 127.416 122.837 1.00 105.39 ? 600  GLU A CD  1 
ATOM   4849  O  OE1 . GLU A 1 1029 ? 140.322 126.874 122.998 1.00 93.47  ? 600  GLU A OE1 1 
ATOM   4850  O  OE2 . GLU A 1 1029 ? 141.981 128.130 123.712 1.00 109.44 ? 600  GLU A OE2 1 
ATOM   4851  N  N   . GLN A 1 1030 ? 146.269 128.771 120.325 1.00 98.99  ? 601  GLN A N   1 
ATOM   4852  C  CA  . GLN A 1 1030 ? 147.630 129.268 120.500 1.00 92.47  ? 601  GLN A CA  1 
ATOM   4853  C  C   . GLN A 1 1030 ? 148.115 129.022 121.924 1.00 99.25  ? 601  GLN A C   1 
ATOM   4854  O  O   . GLN A 1 1030 ? 147.344 129.099 122.884 1.00 107.89 ? 601  GLN A O   1 
ATOM   4855  C  CB  . GLN A 1 1030 ? 147.677 130.766 120.201 1.00 101.81 ? 601  GLN A CB  1 
ATOM   4856  C  CG  . GLN A 1 1030 ? 149.058 131.405 120.345 1.00 110.32 ? 601  GLN A CG  1 
ATOM   4857  C  CD  . GLN A 1 1030 ? 149.022 132.925 120.208 1.00 113.16 ? 601  GLN A CD  1 
ATOM   4858  O  OE1 . GLN A 1 1030 ? 147.983 133.509 119.880 1.00 107.96 ? 601  GLN A OE1 1 
ATOM   4859  N  NE2 . GLN A 1 1030 ? 150.155 133.573 120.480 1.00 111.26 ? 601  GLN A NE2 1 
ATOM   4860  N  N   . LYS A 1 1031 ? 149.410 128.733 122.068 1.00 94.43  ? 602  LYS A N   1 
ATOM   4861  C  CA  . LYS A 1 1031 ? 149.943 128.431 123.397 1.00 101.72 ? 602  LYS A CA  1 
ATOM   4862  C  C   . LYS A 1 1031 ? 149.821 129.616 124.357 1.00 98.73  ? 602  LYS A C   1 
ATOM   4863  O  O   . LYS A 1 1031 ? 149.421 129.443 125.515 1.00 96.19  ? 602  LYS A O   1 
ATOM   4864  C  CB  . LYS A 1 1031 ? 151.397 127.968 123.290 1.00 109.71 ? 602  LYS A CB  1 
ATOM   4865  C  CG  . LYS A 1 1031 ? 151.558 126.469 123.023 1.00 114.68 ? 602  LYS A CG  1 
ATOM   4866  C  CD  . LYS A 1 1031 ? 150.932 125.645 124.163 1.00 111.84 ? 602  LYS A CD  1 
ATOM   4867  C  CE  . LYS A 1 1031 ? 151.137 124.141 123.974 1.00 104.13 ? 602  LYS A CE  1 
ATOM   4868  N  NZ  . LYS A 1 1031 ? 150.508 123.342 125.069 1.00 86.74  ? 602  LYS A NZ  1 
ATOM   4869  N  N   . GLU A 1 1032 ? 150.162 130.823 123.901 1.00 102.81 ? 603  GLU A N   1 
ATOM   4870  C  CA  . GLU A 1 1032 ? 150.211 131.973 124.805 1.00 105.35 ? 603  GLU A CA  1 
ATOM   4871  C  C   . GLU A 1 1032 ? 148.828 132.317 125.346 1.00 89.09  ? 603  GLU A C   1 
ATOM   4872  O  O   . GLU A 1 1032 ? 148.653 132.531 126.552 1.00 93.56  ? 603  GLU A O   1 
ATOM   4873  C  CB  . GLU A 1 1032 ? 150.823 133.184 124.086 1.00 114.24 ? 603  GLU A CB  1 
ATOM   4874  C  CG  . GLU A 1 1032 ? 152.315 133.045 123.712 1.00 120.09 ? 603  GLU A CG  1 
ATOM   4875  C  CD  . GLU A 1 1032 ? 153.235 132.847 124.923 1.00 125.02 ? 603  GLU A CD  1 
ATOM   4876  O  OE1 . GLU A 1 1032 ? 152.987 133.474 125.981 1.00 122.22 ? 603  GLU A OE1 1 
ATOM   4877  O  OE2 . GLU A 1 1032 ? 154.201 132.056 124.819 1.00 124.23 ? 603  GLU A OE2 1 
ATOM   4878  N  N   . SER A 1 1033 ? 147.842 132.411 124.461 1.00 88.53  ? 604  SER A N   1 
ATOM   4879  C  CA  . SER A 1 1033 ? 146.503 132.735 124.917 1.00 81.78  ? 604  SER A CA  1 
ATOM   4880  C  C   . SER A 1 1033 ? 146.004 131.666 125.860 1.00 78.22  ? 604  SER A C   1 
ATOM   4881  O  O   . SER A 1 1033 ? 145.308 131.967 126.832 1.00 88.12  ? 604  SER A O   1 
ATOM   4882  C  CB  . SER A 1 1033 ? 145.552 132.889 123.731 1.00 94.57  ? 604  SER A CB  1 
ATOM   4883  O  OG  . SER A 1 1033 ? 145.420 131.671 123.017 1.00 96.92  ? 604  SER A OG  1 
ATOM   4884  N  N   . LEU A 1 1034 ? 146.361 130.409 125.594 1.00 85.48  ? 605  LEU A N   1 
ATOM   4885  C  CA  . LEU A 1 1034 ? 145.955 129.329 126.487 1.00 98.69  ? 605  LEU A CA  1 
ATOM   4886  C  C   . LEU A 1 1034 ? 146.575 129.491 127.871 1.00 106.12 ? 605  LEU A C   1 
ATOM   4887  O  O   . LEU A 1 1034 ? 145.891 129.329 128.892 1.00 105.25 ? 605  LEU A O   1 
ATOM   4888  C  CB  . LEU A 1 1034 ? 146.314 127.960 125.892 1.00 103.79 ? 605  LEU A CB  1 
ATOM   4889  C  CG  . LEU A 1 1034 ? 145.320 127.229 124.970 1.00 111.05 ? 605  LEU A CG  1 
ATOM   4890  C  CD1 . LEU A 1 1034 ? 145.995 126.050 124.239 1.00 104.98 ? 605  LEU A CD1 1 
ATOM   4891  C  CD2 . LEU A 1 1034 ? 144.082 126.753 125.751 1.00 104.06 ? 605  LEU A CD2 1 
ATOM   4892  N  N   . LEU A 1 1035 ? 147.874 129.809 127.930 1.00 102.37 ? 606  LEU A N   1 
ATOM   4893  C  CA  . LEU A 1 1035 ? 148.534 129.931 129.230 1.00 98.55  ? 606  LEU A CA  1 
ATOM   4894  C  C   . LEU A 1 1035 ? 147.963 131.101 130.028 1.00 94.64  ? 606  LEU A C   1 
ATOM   4895  O  O   . LEU A 1 1035 ? 147.695 130.969 131.226 1.00 97.75  ? 606  LEU A O   1 
ATOM   4896  C  CB  . LEU A 1 1035 ? 150.049 130.077 129.042 1.00 103.00 ? 606  LEU A CB  1 
ATOM   4897  C  CG  . LEU A 1 1035 ? 150.934 130.143 130.297 1.00 106.79 ? 606  LEU A CG  1 
ATOM   4898  C  CD1 . LEU A 1 1035 ? 150.699 128.909 131.179 1.00 101.70 ? 606  LEU A CD1 1 
ATOM   4899  C  CD2 . LEU A 1 1035 ? 152.432 130.312 129.957 1.00 100.09 ? 606  LEU A CD2 1 
ATOM   4900  N  N   . HIS A 1 1036 ? 147.749 132.249 129.376 1.00 99.48  ? 607  HIS A N   1 
ATOM   4901  C  CA  . HIS A 1 1036 ? 147.151 133.386 130.076 1.00 101.32 ? 607  HIS A CA  1 
ATOM   4902  C  C   . HIS A 1 1036 ? 145.685 133.141 130.372 1.00 93.29  ? 607  HIS A C   1 
ATOM   4903  O  O   . HIS A 1 1036 ? 145.098 133.856 131.188 1.00 95.79  ? 607  HIS A O   1 
ATOM   4904  C  CB  . HIS A 1 1036 ? 147.295 134.679 129.261 1.00 106.42 ? 607  HIS A CB  1 
ATOM   4905  C  CG  . HIS A 1 1036 ? 146.970 135.932 130.029 1.00 112.95 ? 607  HIS A CG  1 
ATOM   4906  N  ND1 . HIS A 1 1036 ? 145.679 136.385 130.211 1.00 107.24 ? 607  HIS A ND1 1 
ATOM   4907  C  CD2 . HIS A 1 1036 ? 147.775 136.842 130.633 1.00 111.35 ? 607  HIS A CD2 1 
ATOM   4908  C  CE1 . HIS A 1 1036 ? 145.702 137.508 130.910 1.00 106.03 ? 607  HIS A CE1 1 
ATOM   4909  N  NE2 . HIS A 1 1036 ? 146.961 137.808 131.176 1.00 107.56 ? 607  HIS A NE2 1 
ATOM   4910  N  N   . GLN A 1 1037 ? 145.082 132.164 129.705 1.00 90.75  ? 608  GLN A N   1 
ATOM   4911  C  CA  . GLN A 1 1037 ? 143.709 131.812 130.008 1.00 95.75  ? 608  GLN A CA  1 
ATOM   4912  C  C   . GLN A 1 1037 ? 143.625 130.915 131.226 1.00 96.32  ? 608  GLN A C   1 
ATOM   4913  O  O   . GLN A 1 1037 ? 142.627 130.958 131.954 1.00 101.86 ? 608  GLN A O   1 
ATOM   4914  C  CB  . GLN A 1 1037 ? 143.056 131.131 128.806 1.00 105.83 ? 608  GLN A CB  1 
ATOM   4915  C  CG  . GLN A 1 1037 ? 141.590 130.765 129.032 1.00 108.82 ? 608  GLN A CG  1 
ATOM   4916  C  CD  . GLN A 1 1037 ? 140.742 131.979 129.403 1.00 108.50 ? 608  GLN A CD  1 
ATOM   4917  O  OE1 . GLN A 1 1037 ? 140.116 132.015 130.467 1.00 107.81 ? 608  GLN A OE1 1 
ATOM   4918  N  NE2 . GLN A 1 1037 ? 140.726 132.983 128.527 1.00 105.68 ? 608  GLN A NE2 1 
ATOM   4919  N  N   . ALA A 1 1038 ? 144.653 130.109 131.475 1.00 96.90  ? 609  ALA A N   1 
ATOM   4920  C  CA  . ALA A 1 1038 ? 144.672 129.227 132.635 1.00 107.15 ? 609  ALA A CA  1 
ATOM   4921  C  C   . ALA A 1 1038 ? 145.545 129.766 133.779 1.00 111.44 ? 609  ALA A C   1 
ATOM   4922  O  O   . ALA A 1 1038 ? 145.923 129.001 134.675 1.00 107.63 ? 609  ALA A O   1 
ATOM   4923  C  CB  . ALA A 1 1038 ? 145.126 127.824 132.218 1.00 97.72  ? 609  ALA A CB  1 
ATOM   4924  N  N   . SER A 1 1039 ? 145.858 131.070 133.771 1.00 112.68 ? 610  SER A N   1 
ATOM   4925  C  CA  . SER A 1 1039 ? 146.742 131.655 134.783 1.00 116.98 ? 610  SER A CA  1 
ATOM   4926  C  C   . SER A 1 1039 ? 146.143 131.621 136.186 1.00 119.42 ? 610  SER A C   1 
ATOM   4927  O  O   . SER A 1 1039 ? 146.901 131.673 137.164 1.00 121.72 ? 610  SER A O   1 
ATOM   4928  C  CB  . SER A 1 1039 ? 147.101 133.106 134.410 1.00 120.22 ? 610  SER A CB  1 
ATOM   4929  O  OG  . SER A 1 1039 ? 147.942 133.717 135.385 1.00 114.64 ? 610  SER A OG  1 
ATOM   4930  N  N   . TRP A 1 1040 ? 144.816 131.547 136.306 1.00 115.09 ? 611  TRP A N   1 
ATOM   4931  C  CA  . TRP A 1 1040 ? 144.124 131.517 137.604 1.00 117.58 ? 611  TRP A CA  1 
ATOM   4932  C  C   . TRP A 1 1040 ? 144.439 132.760 138.451 1.00 116.57 ? 611  TRP A C   1 
ATOM   4933  O  O   . TRP A 1 1040 ? 143.960 133.860 138.170 1.00 113.10 ? 611  TRP A O   1 
ATOM   4934  C  CB  . TRP A 1 1040 ? 144.483 130.229 138.381 1.00 118.29 ? 611  TRP A CB  1 
ATOM   4935  C  CG  . TRP A 1 1040 ? 144.156 130.258 139.875 1.00 119.60 ? 611  TRP A CG  1 
ATOM   4936  C  CD1 . TRP A 1 1040 ? 145.006 130.582 140.905 1.00 118.12 ? 611  TRP A CD1 1 
ATOM   4937  C  CD2 . TRP A 1 1040 ? 142.892 129.939 140.488 1.00 108.95 ? 611  TRP A CD2 1 
ATOM   4938  N  NE1 . TRP A 1 1040 ? 144.347 130.491 142.113 1.00 108.12 ? 611  TRP A NE1 1 
ATOM   4939  C  CE2 . TRP A 1 1040 ? 143.052 130.099 141.888 1.00 106.69 ? 611  TRP A CE2 1 
ATOM   4940  C  CE3 . TRP A 1 1040 ? 141.641 129.539 139.988 1.00 97.02  ? 611  TRP A CE3 1 
ATOM   4941  C  CZ2 . TRP A 1 1040 ? 142.006 129.870 142.796 1.00 97.52  ? 611  TRP A CZ2 1 
ATOM   4942  C  CZ3 . TRP A 1 1040 ? 140.598 129.314 140.891 1.00 89.03  ? 611  TRP A CZ3 1 
ATOM   4943  C  CH2 . TRP A 1 1040 ? 140.791 129.480 142.281 1.00 92.32  ? 611  TRP A CH2 1 
ATOM   4944  N  N   . ALA A 1 1051 ? 155.614 128.286 130.854 1.00 100.86 ? 622  ALA A N   1 
ATOM   4945  C  CA  . ALA A 1 1051 ? 154.959 127.063 131.321 1.00 97.37  ? 622  ALA A CA  1 
ATOM   4946  C  C   . ALA A 1 1051 ? 154.052 126.472 130.233 1.00 85.41  ? 622  ALA A C   1 
ATOM   4947  O  O   . ALA A 1 1051 ? 153.936 127.040 129.150 1.00 86.35  ? 622  ALA A O   1 
ATOM   4948  C  CB  . ALA A 1 1051 ? 154.162 127.345 132.596 1.00 95.21  ? 622  ALA A CB  1 
ATOM   4949  N  N   . THR A 1 1052 ? 153.415 125.333 130.520 1.00 83.47  ? 623  THR A N   1 
ATOM   4950  C  CA  . THR A 1 1052 ? 152.493 124.692 129.586 1.00 79.52  ? 623  THR A CA  1 
ATOM   4951  C  C   . THR A 1 1052 ? 151.126 124.513 130.229 1.00 75.47  ? 623  THR A C   1 
ATOM   4952  O  O   . THR A 1 1052 ? 150.977 124.564 131.454 1.00 77.93  ? 623  THR A O   1 
ATOM   4953  C  CB  . THR A 1 1052 ? 152.984 123.315 129.111 1.00 83.86  ? 623  THR A CB  1 
ATOM   4954  O  OG1 . THR A 1 1052 ? 151.983 122.722 128.271 1.00 77.35  ? 623  THR A OG1 1 
ATOM   4955  C  CG2 . THR A 1 1052 ? 153.232 122.398 130.300 1.00 83.42  ? 623  THR A CG2 1 
ATOM   4956  N  N   . VAL A 1 1053 ? 150.122 124.294 129.390 1.00 66.31  ? 624  VAL A N   1 
ATOM   4957  C  CA  . VAL A 1 1053 ? 148.751 124.169 129.852 1.00 60.39  ? 624  VAL A CA  1 
ATOM   4958  C  C   . VAL A 1 1053 ? 148.093 122.987 129.165 1.00 58.19  ? 624  VAL A C   1 
ATOM   4959  O  O   . VAL A 1 1053 ? 148.186 122.841 127.943 1.00 66.20  ? 624  VAL A O   1 
ATOM   4960  C  CB  . VAL A 1 1053 ? 147.968 125.469 129.618 1.00 76.91  ? 624  VAL A CB  1 
ATOM   4961  C  CG1 . VAL A 1 1053 ? 148.037 125.865 128.156 1.00 84.45  ? 624  VAL A CG1 1 
ATOM   4962  C  CG2 . VAL A 1 1053 ? 146.523 125.280 130.061 1.00 80.80  ? 624  VAL A CG2 1 
ATOM   4963  N  N   . ARG A 1 1054 ? 147.448 122.132 129.955 1.00 57.63  ? 625  ARG A N   1 
ATOM   4964  C  CA  . ARG A 1 1054 ? 146.853 120.912 129.434 1.00 53.49  ? 625  ARG A CA  1 
ATOM   4965  C  C   . ARG A 1 1054 ? 145.417 120.786 129.907 1.00 49.89  ? 625  ARG A C   1 
ATOM   4966  O  O   . ARG A 1 1054 ? 145.105 121.059 131.072 1.00 55.00  ? 625  ARG A O   1 
ATOM   4967  C  CB  . ARG A 1 1054 ? 147.641 119.678 129.860 1.00 62.92  ? 625  ARG A CB  1 
ATOM   4968  C  CG  . ARG A 1 1054 ? 147.134 118.408 129.197 1.00 74.43  ? 625  ARG A CG  1 
ATOM   4969  C  CD  . ARG A 1 1054 ? 147.185 118.518 127.678 1.00 79.09  ? 625  ARG A CD  1 
ATOM   4970  N  NE  . ARG A 1 1054 ? 148.531 118.279 127.164 1.00 78.67  ? 625  ARG A NE  1 
ATOM   4971  C  CZ  . ARG A 1 1054 ? 148.951 117.099 126.724 1.00 81.37  ? 625  ARG A CZ  1 
ATOM   4972  N  NH1 . ARG A 1 1054 ? 148.132 116.053 126.740 1.00 74.30  ? 625  ARG A NH1 1 
ATOM   4973  N  NH2 . ARG A 1 1054 ? 150.190 116.965 126.276 1.00 89.29  ? 625  ARG A NH2 1 
ATOM   4974  N  N   . GLY A 1 1055 ? 144.550 120.365 129.001 1.00 43.45  ? 626  GLY A N   1 
ATOM   4975  C  CA  . GLY A 1 1055 ? 143.142 120.371 129.299 1.00 41.94  ? 626  GLY A CA  1 
ATOM   4976  C  C   . GLY A 1 1055 ? 142.516 119.019 129.130 1.00 33.70  ? 626  GLY A C   1 
ATOM   4977  O  O   . GLY A 1 1055 ? 142.720 118.346 128.121 1.00 43.58  ? 626  GLY A O   1 
ATOM   4978  N  N   . SER A 1 1056 ? 141.757 118.606 130.113 1.00 27.54  ? 627  SER A N   1 
ATOM   4979  C  CA  . SER A 1 1056 ? 141.126 117.311 130.028 1.00 27.54  ? 627  SER A CA  1 
ATOM   4980  C  C   . SER A 1 1056 ? 139.766 117.441 130.646 1.00 28.98  ? 627  SER A C   1 
ATOM   4981  O  O   . SER A 1 1056 ? 139.594 118.181 131.607 1.00 41.92  ? 627  SER A O   1 
ATOM   4982  C  CB  . SER A 1 1056 ? 141.923 116.261 130.753 1.00 42.71  ? 627  SER A CB  1 
ATOM   4983  O  OG  . SER A 1 1056 ? 142.320 116.784 132.010 1.00 48.48  ? 627  SER A OG  1 
ATOM   4984  N  N   . SER A 1 1057 ? 138.801 116.760 130.096 1.00 25.90  ? 628  SER A N   1 
ATOM   4985  C  CA  . SER A 1 1057 ? 137.438 117.104 130.409 1.00 26.81  ? 628  SER A CA  1 
ATOM   4986  C  C   . SER A 1 1057 ? 136.752 115.936 131.052 1.00 23.80  ? 628  SER A C   1 
ATOM   4987  O  O   . SER A 1 1057 ? 137.331 114.879 131.257 1.00 37.58  ? 628  SER A O   1 
ATOM   4988  C  CB  . SER A 1 1057 ? 136.683 117.509 129.151 1.00 41.64  ? 628  SER A CB  1 
ATOM   4989  O  OG  . SER A 1 1057 ? 136.622 116.415 128.249 1.00 41.43  ? 628  SER A OG  1 
ATOM   4990  N  N   . PHE A 1 1058 ? 135.500 116.131 131.359 1.00 20.71  ? 629  PHE A N   1 
ATOM   4991  C  CA  . PHE A 1 1058 ? 134.716 114.976 131.680 1.00 20.71  ? 629  PHE A CA  1 
ATOM   4992  C  C   . PHE A 1 1058 ? 133.293 115.347 131.425 1.00 31.58  ? 629  PHE A C   1 
ATOM   4993  O  O   . PHE A 1 1058 ? 132.867 116.433 131.816 1.00 44.85  ? 629  PHE A O   1 
ATOM   4994  C  CB  . PHE A 1 1058 ? 134.904 114.537 133.112 1.00 32.47  ? 629  PHE A CB  1 
ATOM   4995  C  CG  . PHE A 1 1058 ? 134.509 115.553 134.114 1.00 34.44  ? 629  PHE A CG  1 
ATOM   4996  C  CD1 . PHE A 1 1058 ? 135.375 116.567 134.467 1.00 42.70  ? 629  PHE A CD1 1 
ATOM   4997  C  CD2 . PHE A 1 1058 ? 133.252 115.514 134.689 1.00 37.30  ? 629  PHE A CD2 1 
ATOM   4998  C  CE1 . PHE A 1 1058 ? 135.005 117.511 135.414 1.00 47.53  ? 629  PHE A CE1 1 
ATOM   4999  C  CE2 . PHE A 1 1058 ? 132.866 116.454 135.624 1.00 41.75  ? 629  PHE A CE2 1 
ATOM   5000  C  CZ  . PHE A 1 1058 ? 133.741 117.456 135.989 1.00 47.16  ? 629  PHE A CZ  1 
ATOM   5001  N  N   . VAL A 1 1059 ? 132.574 114.478 130.751 1.00 32.11  ? 630  VAL A N   1 
ATOM   5002  C  CA  . VAL A 1 1059 ? 131.275 114.826 130.206 1.00 37.97  ? 630  VAL A CA  1 
ATOM   5003  C  C   . VAL A 1 1059 ? 130.205 114.170 131.046 1.00 40.02  ? 630  VAL A C   1 
ATOM   5004  O  O   . VAL A 1 1059 ? 130.254 112.960 131.294 1.00 53.15  ? 630  VAL A O   1 
ATOM   5005  C  CB  . VAL A 1 1059 ? 131.157 114.401 128.737 1.00 53.69  ? 630  VAL A CB  1 
ATOM   5006  C  CG1 . VAL A 1 1059 ? 129.772 114.723 128.205 1.00 56.24  ? 630  VAL A CG1 1 
ATOM   5007  C  CG2 . VAL A 1 1059 ? 132.240 115.090 127.913 1.00 61.63  ? 630  VAL A CG2 1 
ATOM   5008  N  N   . THR A 1 1060 ? 129.251 114.961 131.496 1.00 37.64  ? 631  THR A N   1 
ATOM   5009  C  CA  . THR A 1 1060 ? 128.163 114.472 132.314 1.00 45.12  ? 631  THR A CA  1 
ATOM   5010  C  C   . THR A 1 1060 ? 126.881 114.665 131.537 1.00 58.42  ? 631  THR A C   1 
ATOM   5011  O  O   . THR A 1 1060 ? 126.858 115.348 130.513 1.00 64.75  ? 631  THR A O   1 
ATOM   5012  C  CB  . THR A 1 1060 ? 128.074 115.229 133.638 1.00 55.76  ? 631  THR A CB  1 
ATOM   5013  O  OG1 . THR A 1 1060 ? 127.550 116.542 133.392 1.00 57.58  ? 631  THR A OG1 1 
ATOM   5014  C  CG2 . THR A 1 1060 ? 129.468 115.362 134.260 1.00 58.90  ? 631  THR A CG2 1 
ATOM   5015  N  N   . ASP A 1 1061 ? 125.799 114.090 132.046 1.00 61.58  ? 632  ASP A N   1 
ATOM   5016  C  CA  . ASP A 1 1061 ? 124.503 114.171 131.382 1.00 58.18  ? 632  ASP A CA  1 
ATOM   5017  C  C   . ASP A 1 1061 ? 123.637 115.196 132.114 1.00 57.85  ? 632  ASP A C   1 
ATOM   5018  O  O   . ASP A 1 1061 ? 123.006 114.880 133.123 1.00 64.64  ? 632  ASP A O   1 
ATOM   5019  C  CB  . ASP A 1 1061 ? 123.852 112.795 131.331 1.00 67.62  ? 632  ASP A CB  1 
ATOM   5020  C  CG  . ASP A 1 1061 ? 122.875 112.658 130.170 1.00 85.30  ? 632  ASP A CG  1 
ATOM   5021  O  OD1 . ASP A 1 1061 ? 122.279 113.686 129.772 1.00 84.82  ? 632  ASP A OD1 1 
ATOM   5022  O  OD2 . ASP A 1 1061 ? 122.705 111.532 129.648 1.00 80.91  ? 632  ASP A OD2 1 
ATOM   5023  N  N   . LEU A 1 1062 ? 123.600 116.428 131.589 1.00 63.99  ? 633  LEU A N   1 
ATOM   5024  C  CA  . LEU A 1 1062 ? 122.774 117.504 132.140 1.00 64.36  ? 633  LEU A CA  1 
ATOM   5025  C  C   . LEU A 1 1062 ? 121.278 117.240 131.993 1.00 67.79  ? 633  LEU A C   1 
ATOM   5026  O  O   . LEU A 1 1062 ? 120.483 117.926 132.645 1.00 65.95  ? 633  LEU A O   1 
ATOM   5027  C  CB  . LEU A 1 1062 ? 123.136 118.850 131.475 1.00 68.87  ? 633  LEU A CB  1 
ATOM   5028  C  CG  . LEU A 1 1062 ? 122.544 120.175 132.024 1.00 88.42  ? 633  LEU A CG  1 
ATOM   5029  C  CD1 . LEU A 1 1062 ? 123.583 121.326 132.107 1.00 84.41  ? 633  LEU A CD1 1 
ATOM   5030  C  CD2 . LEU A 1 1062 ? 121.277 120.638 131.240 1.00 84.16  ? 633  LEU A CD2 1 
ATOM   5031  N  N   . GLU A 1 1063 ? 120.875 116.270 131.162 1.00 73.80  ? 634  GLU A N   1 
ATOM   5032  C  CA  . GLU A 1 1063 ? 119.451 115.987 130.968 1.00 74.15  ? 634  GLU A CA  1 
ATOM   5033  C  C   . GLU A 1 1063 ? 118.794 115.499 132.254 1.00 67.84  ? 634  GLU A C   1 
ATOM   5034  O  O   . GLU A 1 1063 ? 117.662 115.889 132.569 1.00 62.61  ? 634  GLU A O   1 
ATOM   5035  C  CB  . GLU A 1 1063 ? 119.261 114.953 129.853 1.00 85.31  ? 634  GLU A CB  1 
ATOM   5036  C  CG  . GLU A 1 1063 ? 117.785 114.674 129.509 1.00 96.97  ? 634  GLU A CG  1 
ATOM   5037  C  CD  . GLU A 1 1063 ? 117.605 113.746 128.307 1.00 97.39  ? 634  GLU A CD  1 
ATOM   5038  O  OE1 . GLU A 1 1063 ? 118.319 112.715 128.215 1.00 93.85  ? 634  GLU A OE1 1 
ATOM   5039  O  OE2 . GLU A 1 1063 ? 116.740 114.063 127.456 1.00 91.01  ? 634  GLU A OE2 1 
ATOM   5040  N  N   . LYS A 1 1064 ? 119.487 114.639 133.003 1.00 60.67  ? 635  LYS A N   1 
ATOM   5041  C  CA  . LYS A 1 1064 ? 118.951 114.083 134.235 1.00 48.17  ? 635  LYS A CA  1 
ATOM   5042  C  C   . LYS A 1 1064 ? 119.003 115.048 135.405 1.00 39.42  ? 635  LYS A C   1 
ATOM   5043  O  O   . LYS A 1 1064 ? 118.451 114.744 136.466 1.00 40.81  ? 635  LYS A O   1 
ATOM   5044  C  CB  . LYS A 1 1064 ? 119.707 112.819 134.581 1.00 64.20  ? 635  LYS A CB  1 
ATOM   5045  C  CG  . LYS A 1 1064 ? 119.008 111.598 134.036 1.00 83.05  ? 635  LYS A CG  1 
ATOM   5046  C  CD  . LYS A 1 1064 ? 119.141 111.469 132.513 1.00 84.97  ? 635  LYS A CD  1 
ATOM   5047  C  CE  . LYS A 1 1064 ? 120.533 110.979 132.112 1.00 87.43  ? 635  LYS A CE  1 
ATOM   5048  N  NZ  . LYS A 1 1064 ? 120.608 110.659 130.654 1.00 84.17  ? 635  LYS A NZ  1 
ATOM   5049  N  N   . TYR A 1 1065 ? 119.656 116.191 135.247 1.00 41.59  ? 636  TYR A N   1 
ATOM   5050  C  CA  . TYR A 1 1065 ? 119.552 117.219 136.265 1.00 42.05  ? 636  TYR A CA  1 
ATOM   5051  C  C   . TYR A 1 1065 ? 118.097 117.643 136.434 1.00 36.77  ? 636  TYR A C   1 
ATOM   5052  O  O   . TYR A 1 1065 ? 117.627 117.840 137.558 1.00 39.34  ? 636  TYR A O   1 
ATOM   5053  C  CB  . TYR A 1 1065 ? 120.434 118.421 135.886 1.00 53.93  ? 636  TYR A CB  1 
ATOM   5054  C  CG  . TYR A 1 1065 ? 121.946 118.265 136.128 1.00 65.57  ? 636  TYR A CG  1 
ATOM   5055  C  CD1 . TYR A 1 1065 ? 122.631 117.115 135.708 1.00 69.77  ? 636  TYR A CD1 1 
ATOM   5056  C  CD2 . TYR A 1 1065 ? 122.703 119.294 136.711 1.00 68.79  ? 636  TYR A CD2 1 
ATOM   5057  C  CE1 . TYR A 1 1065 ? 124.023 116.968 135.909 1.00 72.13  ? 636  TYR A CE1 1 
ATOM   5058  C  CE2 . TYR A 1 1065 ? 124.100 119.159 136.913 1.00 70.57  ? 636  TYR A CE2 1 
ATOM   5059  C  CZ  . TYR A 1 1065 ? 124.749 117.994 136.509 1.00 80.92  ? 636  TYR A CZ  1 
ATOM   5060  O  OH  . TYR A 1 1065 ? 126.112 117.847 136.703 1.00 74.30  ? 636  TYR A OH  1 
ATOM   5061  N  N   . ASN A 1 1066 ? 117.360 117.749 135.333 1.00 30.57  ? 637  ASN A N   1 
ATOM   5062  C  CA  . ASN A 1 1066 ? 116.079 118.425 135.388 1.00 21.45  ? 637  ASN A CA  1 
ATOM   5063  C  C   . ASN A 1 1066 ? 115.163 117.774 136.371 1.00 22.32  ? 637  ASN A C   1 
ATOM   5064  O  O   . ASN A 1 1066 ? 114.483 118.458 137.135 1.00 36.57  ? 637  ASN A O   1 
ATOM   5065  C  CB  . ASN A 1 1066 ? 115.421 118.450 134.025 1.00 36.07  ? 637  ASN A CB  1 
ATOM   5066  C  CG  . ASN A 1 1066 ? 116.281 119.134 132.993 1.00 57.04  ? 637  ASN A CG  1 
ATOM   5067  O  OD1 . ASN A 1 1066 ? 117.449 119.444 133.249 1.00 55.40  ? 637  ASN A OD1 1 
ATOM   5068  N  ND2 . ASN A 1 1066 ? 115.711 119.385 131.813 1.00 63.51  ? 637  ASN A ND2 1 
ATOM   5069  N  N   . LEU A 1 1067 ? 115.127 116.465 136.395 1.00 24.06  ? 638  LEU A N   1 
ATOM   5070  C  CA  . LEU A 1 1067 ? 114.201 115.864 137.331 1.00 27.67  ? 638  LEU A CA  1 
ATOM   5071  C  C   . LEU A 1 1067 ? 114.677 116.007 138.768 1.00 28.11  ? 638  LEU A C   1 
ATOM   5072  O  O   . LEU A 1 1067 ? 113.873 115.893 139.696 1.00 32.65  ? 638  LEU A O   1 
ATOM   5073  C  CB  . LEU A 1 1067 ? 113.988 114.397 136.985 1.00 36.96  ? 638  LEU A CB  1 
ATOM   5074  C  CG  . LEU A 1 1067 ? 113.297 114.171 135.640 1.00 34.77  ? 638  LEU A CG  1 
ATOM   5075  C  CD1 . LEU A 1 1067 ? 113.175 112.670 135.405 1.00 37.55  ? 638  LEU A CD1 1 
ATOM   5076  C  CD2 . LEU A 1 1067 ? 111.933 114.850 135.601 1.00 30.66  ? 638  LEU A CD2 1 
ATOM   5077  N  N   . ALA A 1 1068 ? 115.951 116.268 138.976 1.00 28.97  ? 639  ALA A N   1 
ATOM   5078  C  CA  . ALA A 1 1068 ? 116.481 116.312 140.322 1.00 26.98  ? 639  ALA A CA  1 
ATOM   5079  C  C   . ALA A 1 1068 ? 116.478 117.700 140.923 1.00 24.10  ? 639  ALA A C   1 
ATOM   5080  O  O   . ALA A 1 1068 ? 116.894 117.851 142.073 1.00 33.88  ? 639  ALA A O   1 
ATOM   5081  C  CB  . ALA A 1 1068 ? 117.910 115.759 140.350 1.00 38.85  ? 639  ALA A CB  1 
ATOM   5082  N  N   . PHE A 1 1069 ? 116.056 118.720 140.203 1.00 19.01  ? 640  PHE A N   1 
ATOM   5083  C  CA  . PHE A 1 1069 ? 116.064 120.024 140.830 1.00 18.12  ? 640  PHE A CA  1 
ATOM   5084  C  C   . PHE A 1 1069 ? 115.016 120.076 141.905 1.00 17.56  ? 640  PHE A C   1 
ATOM   5085  O  O   . PHE A 1 1069 ? 113.986 119.416 141.826 1.00 27.49  ? 640  PHE A O   1 
ATOM   5086  C  CB  . PHE A 1 1069 ? 115.834 121.098 139.815 1.00 21.29  ? 640  PHE A CB  1 
ATOM   5087  C  CG  . PHE A 1 1069 ? 117.088 121.610 139.265 1.00 24.89  ? 640  PHE A CG  1 
ATOM   5088  C  CD1 . PHE A 1 1069 ? 117.810 122.547 139.944 1.00 31.08  ? 640  PHE A CD1 1 
ATOM   5089  C  CD2 . PHE A 1 1069 ? 117.609 121.077 138.113 1.00 31.44  ? 640  PHE A CD2 1 
ATOM   5090  C  CE1 . PHE A 1 1069 ? 118.997 123.014 139.436 1.00 41.23  ? 640  PHE A CE1 1 
ATOM   5091  C  CE2 . PHE A 1 1069 ? 118.806 121.526 137.606 1.00 35.81  ? 640  PHE A CE2 1 
ATOM   5092  C  CZ  . PHE A 1 1069 ? 119.501 122.496 138.268 1.00 39.01  ? 640  PHE A CZ  1 
ATOM   5093  N  N   . ARG A 1 1070 ? 115.296 120.801 142.925 1.00 10.44  ? 641  ARG A N   1 
ATOM   5094  C  CA  . ARG A 1 1070 ? 114.336 120.909 143.974 1.00 14.50  ? 641  ARG A CA  1 
ATOM   5095  C  C   . ARG A 1 1070 ? 114.192 122.358 144.357 1.00 26.04  ? 641  ARG A C   1 
ATOM   5096  O  O   . ARG A 1 1070 ? 115.146 123.127 144.252 1.00 35.52  ? 641  ARG A O   1 
ATOM   5097  C  CB  . ARG A 1 1070 ? 114.760 120.110 145.139 1.00 26.50  ? 641  ARG A CB  1 
ATOM   5098  C  CG  . ARG A 1 1070 ? 114.765 118.619 144.942 1.00 38.91  ? 641  ARG A CG  1 
ATOM   5099  C  CD  . ARG A 1 1070 ? 113.338 118.132 144.649 1.00 33.14  ? 641  ARG A CD  1 
ATOM   5100  N  NE  . ARG A 1 1070 ? 113.256 116.678 144.572 1.00 23.94  ? 641  ARG A NE  1 
ATOM   5101  C  CZ  . ARG A 1 1070 ? 113.434 115.979 143.463 1.00 25.83  ? 641  ARG A CZ  1 
ATOM   5102  N  NH1 . ARG A 1 1070 ? 113.720 116.609 142.339 1.00 31.67  ? 641  ARG A NH1 1 
ATOM   5103  N  NH2 . ARG A 1 1070 ? 113.348 114.656 143.487 1.00 29.39  ? 641  ARG A NH2 1 
ATOM   5104  N  N   . TYR A 1 1071 ? 113.011 122.733 144.840 1.00 22.89  ? 642  TYR A N   1 
ATOM   5105  C  CA  . TYR A 1 1071 ? 112.838 124.134 145.188 1.00 25.34  ? 642  TYR A CA  1 
ATOM   5106  C  C   . TYR A 1 1071 ? 113.697 124.549 146.376 1.00 32.77  ? 642  TYR A C   1 
ATOM   5107  O  O   . TYR A 1 1071 ? 114.146 125.694 146.434 1.00 38.20  ? 642  TYR A O   1 
ATOM   5108  C  CB  . TYR A 1 1071 ? 111.390 124.458 145.472 1.00 31.70  ? 642  TYR A CB  1 
ATOM   5109  C  CG  . TYR A 1 1071 ? 111.144 125.945 145.474 1.00 26.34  ? 642  TYR A CG  1 
ATOM   5110  C  CD1 . TYR A 1 1071 ? 111.493 126.714 144.379 1.00 27.63  ? 642  TYR A CD1 1 
ATOM   5111  C  CD2 . TYR A 1 1071 ? 110.507 126.557 146.520 1.00 28.46  ? 642  TYR A CD2 1 
ATOM   5112  C  CE1 . TYR A 1 1071 ? 111.263 128.045 144.344 1.00 20.94  ? 642  TYR A CE1 1 
ATOM   5113  C  CE2 . TYR A 1 1071 ? 110.262 127.889 146.486 1.00 33.76  ? 642  TYR A CE2 1 
ATOM   5114  C  CZ  . TYR A 1 1071 ? 110.643 128.630 145.392 1.00 25.91  ? 642  TYR A CZ  1 
ATOM   5115  O  OH  . TYR A 1 1071 ? 110.401 129.981 145.369 1.00 37.40  ? 642  TYR A OH  1 
ATOM   5116  N  N   . GLU A 1 1072 ? 113.961 123.657 147.321 1.00 31.90  ? 643  GLU A N   1 
ATOM   5117  C  CA  . GLU A 1 1072 ? 114.861 124.039 148.397 1.00 21.77  ? 643  GLU A CA  1 
ATOM   5118  C  C   . GLU A 1 1072 ? 116.202 124.369 147.852 1.00 17.71  ? 643  GLU A C   1 
ATOM   5119  O  O   . GLU A 1 1072 ? 116.969 125.089 148.474 1.00 32.90  ? 643  GLU A O   1 
ATOM   5120  C  CB  . GLU A 1 1072 ? 114.998 122.909 149.384 1.00 29.97  ? 643  GLU A CB  1 
ATOM   5121  C  CG  . GLU A 1 1072 ? 113.715 122.690 150.157 1.00 44.60  ? 643  GLU A CG  1 
ATOM   5122  C  CD  . GLU A 1 1072 ? 112.703 121.825 149.372 1.00 53.86  ? 643  GLU A CD  1 
ATOM   5123  O  OE1 . GLU A 1 1072 ? 112.824 121.721 148.125 1.00 47.62  ? 643  GLU A OE1 1 
ATOM   5124  O  OE2 . GLU A 1 1072 ? 111.796 121.223 149.992 1.00 50.32  ? 643  GLU A OE2 1 
ATOM   5125  N  N   . PHE A 1 1073 ? 116.503 123.859 146.701 1.00 18.93  ? 644  PHE A N   1 
ATOM   5126  C  CA  . PHE A 1 1073 ? 117.751 124.218 146.097 1.00 25.90  ? 644  PHE A CA  1 
ATOM   5127  C  C   . PHE A 1 1073 ? 117.636 125.414 145.182 1.00 34.77  ? 644  PHE A C   1 
ATOM   5128  O  O   . PHE A 1 1073 ? 118.542 126.252 145.176 1.00 39.65  ? 644  PHE A O   1 
ATOM   5129  C  CB  . PHE A 1 1073 ? 118.314 123.035 145.319 1.00 30.37  ? 644  PHE A CB  1 
ATOM   5130  C  CG  . PHE A 1 1073 ? 119.450 123.407 144.500 1.00 28.00  ? 644  PHE A CG  1 
ATOM   5131  C  CD1 . PHE A 1 1073 ? 120.582 123.912 145.091 1.00 40.35  ? 644  PHE A CD1 1 
ATOM   5132  C  CD2 . PHE A 1 1073 ? 119.397 123.282 143.145 1.00 27.53  ? 644  PHE A CD2 1 
ATOM   5133  C  CE1 . PHE A 1 1073 ? 121.654 124.301 144.335 1.00 41.93  ? 644  PHE A CE1 1 
ATOM   5134  C  CE2 . PHE A 1 1073 ? 120.467 123.652 142.379 1.00 37.36  ? 644  PHE A CE2 1 
ATOM   5135  C  CZ  . PHE A 1 1073 ? 121.602 124.160 142.974 1.00 37.92  ? 644  PHE A CZ  1 
ATOM   5136  N  N   . THR A 1 1074 ? 116.533 125.533 144.445 1.00 26.71  ? 645  THR A N   1 
ATOM   5137  C  CA  . THR A 1 1074 ? 116.414 126.498 143.373 1.00 16.99  ? 645  THR A CA  1 
ATOM   5138  C  C   . THR A 1 1074 ? 115.777 127.785 143.848 1.00 20.19  ? 645  THR A C   1 
ATOM   5139  O  O   . THR A 1 1074 ? 115.650 128.723 143.071 1.00 32.58  ? 645  THR A O   1 
ATOM   5140  C  CB  . THR A 1 1074 ? 115.586 125.896 142.254 1.00 27.27  ? 645  THR A CB  1 
ATOM   5141  O  OG1 . THR A 1 1074 ? 116.120 124.613 141.948 1.00 37.20  ? 645  THR A OG1 1 
ATOM   5142  C  CG2 . THR A 1 1074 ? 115.766 126.681 140.960 1.00 44.78  ? 645  THR A CG2 1 
ATOM   5143  N  N   . ALA A 1 1075 ? 115.366 127.875 145.093 1.00 22.12  ? 646  ALA A N   1 
ATOM   5144  C  CA  . ALA A 1 1075 ? 114.720 129.106 145.531 1.00 20.12  ? 646  ALA A CA  1 
ATOM   5145  C  C   . ALA A 1 1075 ? 115.630 130.306 145.447 1.00 20.07  ? 646  ALA A C   1 
ATOM   5146  O  O   . ALA A 1 1075 ? 115.186 131.343 144.940 1.00 38.60  ? 646  ALA A O   1 
ATOM   5147  C  CB  . ALA A 1 1075 ? 114.174 128.955 146.950 1.00 35.30  ? 646  ALA A CB  1 
ATOM   5148  N  N   . PRO A 1 1076 ? 116.858 130.274 145.926 1.00 19.51  ? 647  PRO A N   1 
ATOM   5149  C  CA  . PRO A 1 1076 ? 117.644 131.509 145.913 1.00 22.65  ? 647  PRO A CA  1 
ATOM   5150  C  C   . PRO A 1 1076 ? 117.923 131.988 144.521 1.00 27.31  ? 647  PRO A C   1 
ATOM   5151  O  O   . PRO A 1 1076 ? 117.829 133.186 144.240 1.00 36.35  ? 647  PRO A O   1 
ATOM   5152  C  CB  . PRO A 1 1076 ? 118.939 131.111 146.615 1.00 34.26  ? 647  PRO A CB  1 
ATOM   5153  C  CG  . PRO A 1 1076 ? 118.587 129.939 147.413 1.00 42.71  ? 647  PRO A CG  1 
ATOM   5154  C  CD  . PRO A 1 1076 ? 117.586 129.191 146.581 1.00 35.52  ? 647  PRO A CD  1 
ATOM   5155  N  N   . PHE A 1 1077 ? 118.247 131.070 143.624 1.00 26.13  ? 648  PHE A N   1 
ATOM   5156  C  CA  . PHE A 1 1077 ? 118.523 131.465 142.252 1.00 27.54  ? 648  PHE A CA  1 
ATOM   5157  C  C   . PHE A 1 1077 ? 117.303 132.089 141.609 1.00 28.67  ? 648  PHE A C   1 
ATOM   5158  O  O   . PHE A 1 1077 ? 117.410 133.110 140.924 1.00 40.23  ? 648  PHE A O   1 
ATOM   5159  C  CB  . PHE A 1 1077 ? 119.010 130.252 141.470 1.00 36.63  ? 648  PHE A CB  1 
ATOM   5160  C  CG  . PHE A 1 1077 ? 120.144 129.566 142.147 1.00 27.45  ? 648  PHE A CG  1 
ATOM   5161  C  CD1 . PHE A 1 1077 ? 119.916 128.559 143.028 1.00 25.50  ? 648  PHE A CD1 1 
ATOM   5162  C  CD2 . PHE A 1 1077 ? 121.414 130.027 141.984 1.00 29.02  ? 648  PHE A CD2 1 
ATOM   5163  C  CE1 . PHE A 1 1077 ? 120.936 127.978 143.680 1.00 32.67  ? 648  PHE A CE1 1 
ATOM   5164  C  CE2 . PHE A 1 1077 ? 122.430 129.459 142.628 1.00 34.50  ? 648  PHE A CE2 1 
ATOM   5165  C  CZ  . PHE A 1 1077 ? 122.197 128.422 143.482 1.00 38.96  ? 648  PHE A CZ  1 
ATOM   5166  N  N   . ILE A 1 1078 ? 116.128 131.509 141.836 1.00 31.82  ? 649  ILE A N   1 
ATOM   5167  C  CA  . ILE A 1 1078 ? 114.916 132.039 141.225 1.00 24.50  ? 649  ILE A CA  1 
ATOM   5168  C  C   . ILE A 1 1078 ? 114.561 133.388 141.809 1.00 28.47  ? 649  ILE A C   1 
ATOM   5169  O  O   . ILE A 1 1078 ? 114.232 134.330 141.075 1.00 42.06  ? 649  ILE A O   1 
ATOM   5170  C  CB  . ILE A 1 1078 ? 113.760 131.056 141.383 1.00 24.77  ? 649  ILE A CB  1 
ATOM   5171  C  CG1 . ILE A 1 1078 ? 114.036 129.806 140.552 1.00 35.51  ? 649  ILE A CG1 1 
ATOM   5172  C  CG2 . ILE A 1 1078 ? 112.479 131.740 141.000 1.00 41.99  ? 649  ILE A CG2 1 
ATOM   5173  C  CD1 . ILE A 1 1078 ? 112.910 128.785 140.582 1.00 46.25  ? 649  ILE A CD1 1 
ATOM   5174  N  N   . GLU A 1 1079 ? 114.593 133.507 143.125 1.00 26.14  ? 650  GLU A N   1 
ATOM   5175  C  CA  . GLU A 1 1079 ? 114.349 134.807 143.715 1.00 27.23  ? 650  GLU A CA  1 
ATOM   5176  C  C   . GLU A 1 1079 ? 115.291 135.839 143.130 1.00 30.64  ? 650  GLU A C   1 
ATOM   5177  O  O   . GLU A 1 1079 ? 114.881 136.964 142.814 1.00 39.91  ? 650  GLU A O   1 
ATOM   5178  C  CB  . GLU A 1 1079 ? 114.525 134.731 145.217 1.00 43.68  ? 650  GLU A CB  1 
ATOM   5179  C  CG  . GLU A 1 1079 ? 113.460 133.882 145.875 1.00 58.92  ? 650  GLU A CG  1 
ATOM   5180  C  CD  . GLU A 1 1079 ? 112.217 134.680 146.204 1.00 74.70  ? 650  GLU A CD  1 
ATOM   5181  O  OE1 . GLU A 1 1079 ? 112.174 135.879 145.845 1.00 71.29  ? 650  GLU A OE1 1 
ATOM   5182  O  OE2 . GLU A 1 1079 ? 111.284 134.110 146.812 1.00 77.55  ? 650  GLU A OE2 1 
ATOM   5183  N  N   . TYR A 1 1080 ? 116.546 135.470 142.941 1.00 29.38  ? 651  TYR A N   1 
ATOM   5184  C  CA  . TYR A 1 1080 ? 117.465 136.455 142.419 1.00 30.48  ? 651  TYR A CA  1 
ATOM   5185  C  C   . TYR A 1 1080 ? 117.147 136.782 140.981 1.00 25.05  ? 651  TYR A C   1 
ATOM   5186  O  O   . TYR A 1 1080 ? 117.349 137.916 140.564 1.00 40.86  ? 651  TYR A O   1 
ATOM   5187  C  CB  . TYR A 1 1080 ? 118.913 135.979 142.537 1.00 44.59  ? 651  TYR A CB  1 
ATOM   5188  C  CG  . TYR A 1 1080 ? 119.928 137.036 142.172 1.00 34.27  ? 651  TYR A CG  1 
ATOM   5189  C  CD1 . TYR A 1 1080 ? 119.719 138.349 142.516 1.00 38.52  ? 651  TYR A CD1 1 
ATOM   5190  C  CD2 . TYR A 1 1080 ? 121.096 136.709 141.532 1.00 38.78  ? 651  TYR A CD2 1 
ATOM   5191  C  CE1 . TYR A 1 1080 ? 120.618 139.314 142.212 1.00 47.84  ? 651  TYR A CE1 1 
ATOM   5192  C  CE2 . TYR A 1 1080 ? 122.016 137.671 141.225 1.00 49.32  ? 651  TYR A CE2 1 
ATOM   5193  C  CZ  . TYR A 1 1080 ? 121.771 138.978 141.569 1.00 51.19  ? 651  TYR A CZ  1 
ATOM   5194  O  OH  . TYR A 1 1080 ? 122.686 139.964 141.273 1.00 55.39  ? 651  TYR A OH  1 
ATOM   5195  N  N   . CYS A 1 1081 ? 116.688 135.827 140.194 1.00 21.92  ? 652  CYS A N   1 
ATOM   5196  C  CA  . CYS A 1 1081 ? 116.367 136.198 138.826 1.00 22.80  ? 652  CYS A CA  1 
ATOM   5197  C  C   . CYS A 1 1081 ? 115.209 137.178 138.800 1.00 29.80  ? 652  CYS A C   1 
ATOM   5198  O  O   . CYS A 1 1081 ? 115.197 138.124 138.002 1.00 39.85  ? 652  CYS A O   1 
ATOM   5199  C  CB  . CYS A 1 1081 ? 116.048 134.971 137.993 1.00 35.06  ? 652  CYS A CB  1 
ATOM   5200  S  SG  . CYS A 1 1081 ? 117.476 133.900 137.737 1.00 59.95  ? 652  CYS A SG  1 
ATOM   5201  N  N   . ASN A 1 1082 ? 114.232 136.985 139.677 1.00 29.34  ? 653  ASN A N   1 
ATOM   5202  C  CA  . ASN A 1 1082 ? 113.150 137.952 139.754 1.00 22.63  ? 653  ASN A CA  1 
ATOM   5203  C  C   . ASN A 1 1082 ? 113.697 139.328 140.112 1.00 26.60  ? 653  ASN A C   1 
ATOM   5204  O  O   . ASN A 1 1082 ? 113.412 140.318 139.434 1.00 38.25  ? 653  ASN A O   1 
ATOM   5205  C  CB  . ASN A 1 1082 ? 112.116 137.498 140.778 1.00 26.13  ? 653  ASN A CB  1 
ATOM   5206  C  CG  . ASN A 1 1082 ? 111.412 136.230 140.362 1.00 32.22  ? 653  ASN A CG  1 
ATOM   5207  O  OD1 . ASN A 1 1082 ? 111.322 135.921 139.172 1.00 36.11  ? 653  ASN A OD1 1 
ATOM   5208  N  ND2 . ASN A 1 1082 ? 110.915 135.475 141.342 1.00 31.31  ? 653  ASN A ND2 1 
ATOM   5209  N  N   . ARG A 1 1083 ? 114.529 139.404 141.144 1.00 22.79  ? 654  ARG A N   1 
ATOM   5210  C  CA  . ARG A 1 1083 ? 114.988 140.707 141.605 1.00 20.13  ? 654  ARG A CA  1 
ATOM   5211  C  C   . ARG A 1 1083 ? 115.921 141.363 140.612 1.00 19.82  ? 654  ARG A C   1 
ATOM   5212  O  O   . ARG A 1 1083 ? 116.029 142.586 140.559 1.00 29.36  ? 654  ARG A O   1 
ATOM   5213  C  CB  . ARG A 1 1083 ? 115.691 140.555 142.933 1.00 29.64  ? 654  ARG A CB  1 
ATOM   5214  C  CG  . ARG A 1 1083 ? 116.001 141.878 143.561 1.00 55.22  ? 654  ARG A CG  1 
ATOM   5215  C  CD  . ARG A 1 1083 ? 116.315 141.720 145.038 1.00 71.61  ? 654  ARG A CD  1 
ATOM   5216  N  NE  . ARG A 1 1083 ? 117.532 140.950 145.286 1.00 73.59  ? 654  ARG A NE  1 
ATOM   5217  C  CZ  . ARG A 1 1083 ? 117.552 139.664 145.623 1.00 70.77  ? 654  ARG A CZ  1 
ATOM   5218  N  NH1 . ARG A 1 1083 ? 116.414 138.978 145.714 1.00 62.17  ? 654  ARG A NH1 1 
ATOM   5219  N  NH2 . ARG A 1 1083 ? 118.716 139.059 145.846 1.00 70.24  ? 654  ARG A NH2 1 
ATOM   5220  N  N   . CYS A 1 1084 ? 116.606 140.560 139.838 1.00 31.81  ? 655  CYS A N   1 
ATOM   5221  C  CA  . CYS A 1 1084 ? 117.495 140.989 138.777 1.00 35.09  ? 655  CYS A CA  1 
ATOM   5222  C  C   . CYS A 1 1084 ? 116.735 141.489 137.554 1.00 37.43  ? 655  CYS A C   1 
ATOM   5223  O  O   . CYS A 1 1084 ? 117.264 142.326 136.815 1.00 47.90  ? 655  CYS A O   1 
ATOM   5224  C  CB  . CYS A 1 1084 ? 118.389 139.796 138.408 1.00 29.62  ? 655  CYS A CB  1 
ATOM   5225  S  SG  . CYS A 1 1084 ? 119.767 140.085 137.389 1.00 52.18  ? 655  CYS A SG  1 
ATOM   5226  N  N   . TYR A 1 1085 ? 115.518 141.010 137.322 1.00 23.36  ? 656  TYR A N   1 
ATOM   5227  C  CA  . TYR A 1 1085 ? 114.707 141.531 136.243 1.00 23.67  ? 656  TYR A CA  1 
ATOM   5228  C  C   . TYR A 1 1085 ? 113.636 142.511 136.704 1.00 31.79  ? 656  TYR A C   1 
ATOM   5229  O  O   . TYR A 1 1085 ? 112.801 142.926 135.893 1.00 37.55  ? 656  TYR A O   1 
ATOM   5230  C  CB  . TYR A 1 1085 ? 114.060 140.392 135.496 1.00 28.40  ? 656  TYR A CB  1 
ATOM   5231  C  CG  . TYR A 1 1085 ? 114.928 139.778 134.469 1.00 30.38  ? 656  TYR A CG  1 
ATOM   5232  C  CD1 . TYR A 1 1085 ? 115.865 138.861 134.825 1.00 41.46  ? 656  TYR A CD1 1 
ATOM   5233  C  CD2 . TYR A 1 1085 ? 114.740 140.040 133.128 1.00 35.03  ? 656  TYR A CD2 1 
ATOM   5234  C  CE1 . TYR A 1 1085 ? 116.647 138.259 133.901 1.00 42.95  ? 656  TYR A CE1 1 
ATOM   5235  C  CE2 . TYR A 1 1085 ? 115.512 139.443 132.188 1.00 36.39  ? 656  TYR A CE2 1 
ATOM   5236  C  CZ  . TYR A 1 1085 ? 116.471 138.545 132.589 1.00 41.44  ? 656  TYR A CZ  1 
ATOM   5237  O  OH  . TYR A 1 1085 ? 117.283 137.909 131.688 1.00 53.26  ? 656  TYR A OH  1 
ATOM   5238  N  N   . GLY A 1 1086 ? 113.628 142.888 137.975 1.00 30.53  ? 657  GLY A N   1 
ATOM   5239  C  CA  . GLY A 1 1086 ? 112.619 143.831 138.430 1.00 29.11  ? 657  GLY A CA  1 
ATOM   5240  C  C   . GLY A 1 1086 ? 111.192 143.352 138.273 1.00 28.27  ? 657  GLY A C   1 
ATOM   5241  O  O   . GLY A 1 1086 ? 110.325 144.129 137.858 1.00 37.53  ? 657  GLY A O   1 
ATOM   5242  N  N   . VAL A 1 1087 ? 110.925 142.085 138.584 1.00 25.54  ? 658  VAL A N   1 
ATOM   5243  C  CA  . VAL A 1 1087 ? 109.579 141.524 138.597 1.00 27.43  ? 658  VAL A CA  1 
ATOM   5244  C  C   . VAL A 1 1087 ? 109.400 140.732 139.884 1.00 25.25  ? 658  VAL A C   1 
ATOM   5245  O  O   . VAL A 1 1087 ? 110.298 140.665 140.717 1.00 31.79  ? 658  VAL A O   1 
ATOM   5246  C  CB  . VAL A 1 1087 ? 109.310 140.625 137.381 1.00 39.09  ? 658  VAL A CB  1 
ATOM   5247  C  CG1 . VAL A 1 1087 ? 109.262 141.451 136.108 1.00 47.69  ? 658  VAL A CG1 1 
ATOM   5248  C  CG2 . VAL A 1 1087 ? 110.395 139.544 137.304 1.00 43.56  ? 658  VAL A CG2 1 
ATOM   5249  N  N   . LYS A 1 1088 ? 108.237 140.120 140.041 1.00 23.13  ? 659  LYS A N   1 
ATOM   5250  C  CA  . LYS A 1 1088 ? 107.994 139.294 141.215 1.00 26.04  ? 659  LYS A CA  1 
ATOM   5251  C  C   . LYS A 1 1088 ? 107.243 138.048 140.798 1.00 27.14  ? 659  LYS A C   1 
ATOM   5252  O  O   . LYS A 1 1088 ? 106.168 138.146 140.207 1.00 34.25  ? 659  LYS A O   1 
ATOM   5253  C  CB  . LYS A 1 1088 ? 107.192 140.051 142.259 1.00 39.64  ? 659  LYS A CB  1 
ATOM   5254  C  CG  . LYS A 1 1088 ? 107.901 141.243 142.839 1.00 50.35  ? 659  LYS A CG  1 
ATOM   5255  C  CD  . LYS A 1 1088 ? 107.041 141.898 143.913 1.00 64.01  ? 659  LYS A CD  1 
ATOM   5256  C  CE  . LYS A 1 1088 ? 107.756 143.102 144.516 1.00 81.84  ? 659  LYS A CE  1 
ATOM   5257  N  NZ  . LYS A 1 1088 ? 106.949 143.767 145.579 1.00 81.92  ? 659  LYS A NZ  1 
ATOM   5258  N  N   . ASN A 1 1089 ? 107.796 136.889 141.111 1.00 24.79  ? 660  ASN A N   1 
ATOM   5259  C  CA  . ASN A 1 1089 ? 107.130 135.631 140.853 1.00 25.37  ? 660  ASN A CA  1 
ATOM   5260  C  C   . ASN A 1 1089 ? 107.073 135.325 139.373 1.00 26.75  ? 660  ASN A C   1 
ATOM   5261  O  O   . ASN A 1 1089 ? 106.162 134.643 138.910 1.00 34.09  ? 660  ASN A O   1 
ATOM   5262  C  CB  . ASN A 1 1089 ? 105.716 135.642 141.425 1.00 25.34  ? 660  ASN A CB  1 
ATOM   5263  C  CG  . ASN A 1 1089 ? 105.680 136.201 142.808 1.00 34.01  ? 660  ASN A CG  1 
ATOM   5264  O  OD1 . ASN A 1 1089 ? 106.591 135.976 143.592 1.00 40.00  ? 660  ASN A OD1 1 
ATOM   5265  N  ND2 . ASN A 1 1089 ? 104.656 136.985 143.109 1.00 42.43  ? 660  ASN A ND2 1 
ATOM   5266  N  N   . VAL A 1 1090 ? 108.006 135.818 138.585 1.00 22.31  ? 661  VAL A N   1 
ATOM   5267  C  CA  . VAL A 1 1090 ? 107.866 135.471 137.184 1.00 28.23  ? 661  VAL A CA  1 
ATOM   5268  C  C   . VAL A 1 1090 ? 108.683 134.210 136.927 1.00 33.42  ? 661  VAL A C   1 
ATOM   5269  O  O   . VAL A 1 1090 ? 108.149 133.194 136.465 1.00 30.43  ? 661  VAL A O   1 
ATOM   5270  C  CB  . VAL A 1 1090 ? 108.271 136.645 136.275 1.00 43.63  ? 661  VAL A CB  1 
ATOM   5271  C  CG1 . VAL A 1 1090 ? 108.444 136.190 134.818 1.00 48.62  ? 661  VAL A CG1 1 
ATOM   5272  C  CG2 . VAL A 1 1090 ? 107.222 137.761 136.365 1.00 47.99  ? 661  VAL A CG2 1 
ATOM   5273  N  N   . PHE A 1 1091 ? 109.987 134.248 137.270 1.00 36.59  ? 662  PHE A N   1 
ATOM   5274  C  CA  . PHE A 1 1091 ? 110.930 133.138 137.046 1.00 30.43  ? 662  PHE A CA  1 
ATOM   5275  C  C   . PHE A 1 1091 ? 110.730 132.047 137.962 1.00 33.67  ? 662  PHE A C   1 
ATOM   5276  O  O   . PHE A 1 1091 ? 111.464 131.055 138.030 1.00 42.92  ? 662  PHE A O   1 
ATOM   5277  C  CB  . PHE A 1 1091 ? 112.370 133.634 137.144 1.00 23.31  ? 662  PHE A CB  1 
ATOM   5278  C  CG  . PHE A 1 1091 ? 112.696 134.616 136.113 1.00 28.46  ? 662  PHE A CG  1 
ATOM   5279  C  CD1 . PHE A 1 1091 ? 113.252 134.209 134.929 1.00 39.52  ? 662  PHE A CD1 1 
ATOM   5280  C  CD2 . PHE A 1 1091 ? 112.395 135.947 136.288 1.00 43.08  ? 662  PHE A CD2 1 
ATOM   5281  C  CE1 . PHE A 1 1091 ? 113.536 135.114 133.933 1.00 50.20  ? 662  PHE A CE1 1 
ATOM   5282  C  CE2 . PHE A 1 1091 ? 112.669 136.879 135.294 1.00 52.10  ? 662  PHE A CE2 1 
ATOM   5283  C  CZ  . PHE A 1 1091 ? 113.251 136.457 134.110 1.00 56.47  ? 662  PHE A CZ  1 
ATOM   5284  N  N   . ASN A 1 1092 ? 109.670 132.222 138.707 1.00 29.49  ? 663  ASN A N   1 
ATOM   5285  C  CA  . ASN A 1 1092 ? 109.299 131.313 139.755 1.00 25.62  ? 663  ASN A CA  1 
ATOM   5286  C  C   . ASN A 1 1092 ? 108.246 130.306 139.332 1.00 34.79  ? 663  ASN A C   1 
ATOM   5287  O  O   . ASN A 1 1092 ? 107.895 129.445 140.133 1.00 41.85  ? 663  ASN A O   1 
ATOM   5288  C  CB  . ASN A 1 1092 ? 108.758 132.127 140.913 1.00 30.29  ? 663  ASN A CB  1 
ATOM   5289  C  CG  . ASN A 1 1092 ? 109.271 131.670 142.199 1.00 36.52  ? 663  ASN A CG  1 
ATOM   5290  O  OD1 . ASN A 1 1092 ? 109.461 130.471 142.396 1.00 44.74  ? 663  ASN A OD1 1 
ATOM   5291  N  ND2 . ASN A 1 1092 ? 109.409 132.586 143.142 1.00 38.29  ? 663  ASN A ND2 1 
ATOM   5292  N  N   . TRP A 1 1093 ? 107.743 130.380 138.097 1.00 36.02  ? 664  TRP A N   1 
ATOM   5293  C  CA  . TRP A 1 1093 ? 106.422 129.836 137.786 1.00 24.62  ? 664  TRP A CA  1 
ATOM   5294  C  C   . TRP A 1 1093 ? 106.382 128.330 137.877 1.00 30.01  ? 664  TRP A C   1 
ATOM   5295  O  O   . TRP A 1 1093 ? 105.382 127.771 138.330 1.00 35.90  ? 664  TRP A O   1 
ATOM   5296  C  CB  . TRP A 1 1093 ? 106.021 130.266 136.400 1.00 26.68  ? 664  TRP A CB  1 
ATOM   5297  C  CG  . TRP A 1 1093 ? 106.991 129.811 135.435 1.00 23.42  ? 664  TRP A CG  1 
ATOM   5298  C  CD1 . TRP A 1 1093 ? 108.146 130.418 135.106 1.00 35.54  ? 664  TRP A CD1 1 
ATOM   5299  C  CD2 . TRP A 1 1093 ? 106.858 128.708 134.568 1.00 22.21  ? 664  TRP A CD2 1 
ATOM   5300  N  NE1 . TRP A 1 1093 ? 108.786 129.721 134.117 1.00 35.54  ? 664  TRP A NE1 1 
ATOM   5301  C  CE2 . TRP A 1 1093 ? 107.995 128.668 133.766 1.00 24.03  ? 664  TRP A CE2 1 
ATOM   5302  C  CE3 . TRP A 1 1093 ? 105.886 127.740 134.399 1.00 38.87  ? 664  TRP A CE3 1 
ATOM   5303  C  CZ2 . TRP A 1 1093 ? 108.195 127.700 132.832 1.00 39.26  ? 664  TRP A CZ2 1 
ATOM   5304  C  CZ3 . TRP A 1 1093 ? 106.084 126.774 133.464 1.00 40.37  ? 664  TRP A CZ3 1 
ATOM   5305  C  CH2 . TRP A 1 1093 ? 107.226 126.756 132.690 1.00 42.46  ? 664  TRP A CH2 1 
ATOM   5306  N  N   . MET A 1 1094 ? 107.432 127.646 137.411 1.00 36.49  ? 665  MET A N   1 
ATOM   5307  C  CA  . MET A 1 1094 ? 107.388 126.183 137.371 1.00 34.13  ? 665  MET A CA  1 
ATOM   5308  C  C   . MET A 1 1094 ? 107.299 125.601 138.766 1.00 26.05  ? 665  MET A C   1 
ATOM   5309  O  O   . MET A 1 1094 ? 106.463 124.739 139.041 1.00 36.00  ? 665  MET A O   1 
ATOM   5310  C  CB  . MET A 1 1094 ? 108.615 125.604 136.691 1.00 29.79  ? 665  MET A CB  1 
ATOM   5311  C  CG  . MET A 1 1094 ? 108.653 124.112 136.846 1.00 30.33  ? 665  MET A CG  1 
ATOM   5312  S  SD  . MET A 1 1094 ? 110.274 123.483 136.569 1.00 53.10  ? 665  MET A SD  1 
ATOM   5313  C  CE  . MET A 1 1094 ? 110.571 124.350 135.031 1.00 55.26  ? 665  MET A CE  1 
ATOM   5314  N  N   . HIS A 1 1095 ? 108.148 126.050 139.664 1.00 20.82  ? 666  HIS A N   1 
ATOM   5315  C  CA  . HIS A 1 1095 ? 108.082 125.359 140.920 1.00 18.96  ? 666  HIS A CA  1 
ATOM   5316  C  C   . HIS A 1 1095 ? 106.806 125.678 141.644 1.00 21.16  ? 666  HIS A C   1 
ATOM   5317  O  O   . HIS A 1 1095 ? 106.450 124.933 142.549 1.00 35.05  ? 666  HIS A O   1 
ATOM   5318  C  CB  . HIS A 1 1095 ? 109.299 125.683 141.779 1.00 31.45  ? 666  HIS A CB  1 
ATOM   5319  C  CG  . HIS A 1 1095 ? 110.549 124.977 141.341 1.00 31.85  ? 666  HIS A CG  1 
ATOM   5320  N  ND1 . HIS A 1 1095 ? 110.747 123.625 141.514 1.00 27.00  ? 666  HIS A ND1 1 
ATOM   5321  C  CD2 . HIS A 1 1095 ? 111.668 125.442 140.731 1.00 36.03  ? 666  HIS A CD2 1 
ATOM   5322  C  CE1 . HIS A 1 1095 ? 111.928 123.286 141.024 1.00 29.38  ? 666  HIS A CE1 1 
ATOM   5323  N  NE2 . HIS A 1 1095 ? 112.507 124.371 140.542 1.00 32.66  ? 666  HIS A NE2 1 
ATOM   5324  N  N   . TYR A 1 1096 ? 106.065 126.693 141.207 1.00 18.11  ? 667  TYR A N   1 
ATOM   5325  C  CA  . TYR A 1 1096 ? 104.748 126.943 141.854 1.00 26.78  ? 667  TYR A CA  1 
ATOM   5326  C  C   . TYR A 1 1096 ? 103.653 126.169 141.124 1.00 39.94  ? 667  TYR A C   1 
ATOM   5327  O  O   . TYR A 1 1096 ? 102.706 125.717 141.796 1.00 43.78  ? 667  TYR A O   1 
ATOM   5328  C  CB  . TYR A 1 1096 ? 104.395 128.432 141.875 1.00 37.11  ? 667  TYR A CB  1 
ATOM   5329  C  CG  . TYR A 1 1096 ? 105.254 129.295 142.786 1.00 44.53  ? 667  TYR A CG  1 
ATOM   5330  C  CD1 . TYR A 1 1096 ? 105.916 128.748 143.877 1.00 41.92  ? 667  TYR A CD1 1 
ATOM   5331  C  CD2 . TYR A 1 1096 ? 105.376 130.662 142.570 1.00 51.11  ? 667  TYR A CD2 1 
ATOM   5332  C  CE1 . TYR A 1 1096 ? 106.694 129.532 144.711 1.00 42.61  ? 667  TYR A CE1 1 
ATOM   5333  C  CE2 . TYR A 1 1096 ? 106.145 131.457 143.402 1.00 42.24  ? 667  TYR A CE2 1 
ATOM   5334  C  CZ  . TYR A 1 1096 ? 106.806 130.890 144.476 1.00 49.55  ? 667  TYR A CZ  1 
ATOM   5335  O  OH  . TYR A 1 1096 ? 107.569 131.668 145.298 1.00 54.86  ? 667  TYR A OH  1 
ATOM   5336  N  N   . THR A 1 1097 ? 103.780 125.993 139.806 1.00 36.67  ? 668  THR A N   1 
ATOM   5337  C  CA  . THR A 1 1097 ? 102.694 125.360 139.020 1.00 27.71  ? 668  THR A CA  1 
ATOM   5338  C  C   . THR A 1 1097 ? 102.861 123.858 138.938 1.00 38.29  ? 668  THR A C   1 
ATOM   5339  O  O   . THR A 1 1097 ? 101.937 123.151 139.389 1.00 47.92  ? 668  THR A O   1 
ATOM   5340  C  CB  . THR A 1 1097 ? 102.680 125.976 137.623 1.00 34.47  ? 668  THR A CB  1 
ATOM   5341  O  OG1 . THR A 1 1097 ? 102.747 127.383 137.826 1.00 42.45  ? 668  THR A OG1 1 
ATOM   5342  C  CG2 . THR A 1 1097 ? 101.430 125.613 136.841 1.00 48.24  ? 668  THR A CG2 1 
ATOM   5343  N  N   . ILE A 1 1098 ? 103.983 123.370 138.400 1.00 31.53  ? 669  ILE A N   1 
ATOM   5344  C  CA  . ILE A 1 1098 ? 104.138 121.899 138.160 1.00 20.72  ? 669  ILE A CA  1 
ATOM   5345  C  C   . ILE A 1 1098 ? 103.800 121.095 139.428 1.00 27.58  ? 669  ILE A C   1 
ATOM   5346  O  O   . ILE A 1 1098 ? 102.971 120.168 139.320 1.00 44.35  ? 669  ILE A O   1 
ATOM   5347  C  CB  . ILE A 1 1098 ? 105.540 121.566 137.618 1.00 20.35  ? 669  ILE A CB  1 
ATOM   5348  C  CG1 . ILE A 1 1098 ? 105.849 122.367 136.361 1.00 31.69  ? 669  ILE A CG1 1 
ATOM   5349  C  CG2 . ILE A 1 1098 ? 105.689 120.065 137.379 1.00 37.03  ? 669  ILE A CG2 1 
ATOM   5350  C  CD1 . ILE A 1 1098 ? 104.799 122.237 135.275 1.00 38.45  ? 669  ILE A CD1 1 
ATOM   5351  N  N   . PRO A 1 1099 ? 104.376 121.377 140.615 1.00 20.98  ? 670  PRO A N   1 
ATOM   5352  C  CA  . PRO A 1 1099 ? 104.130 120.560 141.836 1.00 25.78  ? 670  PRO A CA  1 
ATOM   5353  C  C   . PRO A 1 1099 ? 102.639 120.414 142.107 1.00 35.53  ? 670  PRO A C   1 
ATOM   5354  O  O   . PRO A 1 1099 ? 102.250 119.439 142.786 1.00 44.31  ? 670  PRO A O   1 
ATOM   5355  C  CB  . PRO A 1 1099 ? 104.850 121.332 142.932 1.00 40.32  ? 670  PRO A CB  1 
ATOM   5356  C  CG  . PRO A 1 1099 ? 106.021 121.908 142.164 1.00 42.31  ? 670  PRO A CG  1 
ATOM   5357  C  CD  . PRO A 1 1099 ? 105.392 122.432 140.916 1.00 34.52  ? 670  PRO A CD  1 
ATOM   5358  N  N   . GLN A 1 1100 ? 101.823 121.338 141.597 1.00 29.00  ? 671  GLN A N   1 
ATOM   5359  C  CA  . GLN A 1 1100 ? 100.367 121.314 141.897 1.00 25.28  ? 671  GLN A CA  1 
ATOM   5360  C  C   . GLN A 1 1100 ? 99.567  120.969 140.632 1.00 34.97  ? 671  GLN A C   1 
ATOM   5361  O  O   . GLN A 1 1100 ? 98.479  121.551 140.450 1.00 40.72  ? 671  GLN A O   1 
ATOM   5362  C  CB  . GLN A 1 1100 ? 99.975  122.666 142.489 1.00 31.64  ? 671  GLN A CB  1 
ATOM   5363  C  CG  . GLN A 1 1100 ? 100.678 122.964 143.809 1.00 40.66  ? 671  GLN A CG  1 
ATOM   5364  C  CD  . GLN A 1 1100 ? 100.913 124.438 144.040 1.00 49.03  ? 671  GLN A CD  1 
ATOM   5365  O  OE1 . GLN A 1 1100 ? 101.505 124.849 145.044 1.00 54.03  ? 671  GLN A OE1 1 
ATOM   5366  N  NE2 . GLN A 1 1100 ? 100.459 125.251 143.099 1.00 48.63  ? 671  GLN A NE2 1 
ATOM   5367  N  N   . CYS A 1 1101 ? 100.082 120.058 139.802 1.00 31.09  ? 672  CYS A N   1 
ATOM   5368  C  CA  . CYS A 1 1101 ? 99.348  119.621 138.586 1.00 29.07  ? 672  CYS A CA  1 
ATOM   5369  C  C   . CYS A 1 1101 ? 99.075  118.112 138.670 1.00 35.83  ? 672  CYS A C   1 
ATOM   5370  O  O   . CYS A 1 1101 ? 99.548  117.487 139.640 1.00 39.16  ? 672  CYS A O   1 
ATOM   5371  C  CB  . CYS A 1 1101 ? 100.146 119.928 137.326 1.00 32.94  ? 672  CYS A CB  1 
ATOM   5372  S  SG  . CYS A 1 1101 ? 100.351 121.699 137.009 1.00 62.54  ? 672  CYS A SG  1 
ATOM   5373  N  N   . TYR A 1 1102 ? 98.338  117.557 137.704 1.00 32.10  ? 673  TYR A N   1 
ATOM   5374  C  CA  . TYR A 1 1102 ? 98.052  116.119 137.676 1.00 23.45  ? 673  TYR A CA  1 
ATOM   5375  C  C   . TYR A 1 1102 ? 98.795  115.527 136.506 1.00 23.13  ? 673  TYR A C   1 
ATOM   5376  O  O   . TYR A 1 1102 ? 98.267  115.446 135.403 1.00 34.78  ? 673  TYR A O   1 
ATOM   5377  C  CB  . TYR A 1 1102 ? 96.572  115.875 137.508 1.00 26.21  ? 673  TYR A CB  1 
ATOM   5378  C  CG  . TYR A 1 1102 ? 96.190  114.408 137.341 1.00 35.14  ? 673  TYR A CG  1 
ATOM   5379  C  CD1 . TYR A 1 1102 ? 96.171  113.534 138.420 1.00 45.58  ? 673  TYR A CD1 1 
ATOM   5380  C  CD2 . TYR A 1 1102 ? 95.798  113.904 136.107 1.00 41.50  ? 673  TYR A CD2 1 
ATOM   5381  C  CE1 . TYR A 1 1102 ? 95.796  112.183 138.263 1.00 39.39  ? 673  TYR A CE1 1 
ATOM   5382  C  CE2 . TYR A 1 1102 ? 95.426  112.559 135.946 1.00 39.72  ? 673  TYR A CE2 1 
ATOM   5383  C  CZ  . TYR A 1 1102 ? 95.435  111.712 137.025 1.00 33.94  ? 673  TYR A CZ  1 
ATOM   5384  O  OH  . TYR A 1 1102 ? 95.067  110.398 136.865 1.00 39.86  ? 673  TYR A OH  1 
ATOM   5385  N  N   . MET A 1 1103 ? 100.013 115.098 136.743 1.00 18.74  ? 674  MET A N   1 
ATOM   5386  C  CA  . MET A 1 1103 ? 100.879 114.753 135.636 1.00 20.87  ? 674  MET A CA  1 
ATOM   5387  C  C   . MET A 1 1103 ? 100.351 113.518 134.932 1.00 30.30  ? 674  MET A C   1 
ATOM   5388  O  O   . MET A 1 1103 ? 100.068 112.511 135.584 1.00 39.07  ? 674  MET A O   1 
ATOM   5389  C  CB  . MET A 1 1103 ? 102.258 114.494 136.172 1.00 29.37  ? 674  MET A CB  1 
ATOM   5390  C  CG  . MET A 1 1103 ? 102.542 115.407 137.318 1.00 29.29  ? 674  MET A CG  1 
ATOM   5391  S  SD  . MET A 1 1103 ? 102.814 117.009 136.604 1.00 34.25  ? 674  MET A SD  1 
ATOM   5392  C  CE  . MET A 1 1103 ? 104.386 116.679 135.814 1.00 30.83  ? 674  MET A CE  1 
ATOM   5393  N  N   . HIS A 1 1104 ? 100.221 113.576 133.609 1.00 26.65  ? 675  HIS A N   1 
ATOM   5394  C  CA  . HIS A 1 1104 ? 99.766  112.413 132.858 1.00 24.66  ? 675  HIS A CA  1 
ATOM   5395  C  C   . HIS A 1 1104 ? 100.256 112.547 131.453 1.00 24.74  ? 675  HIS A C   1 
ATOM   5396  O  O   . HIS A 1 1104 ? 100.884 113.544 131.101 1.00 37.16  ? 675  HIS A O   1 
ATOM   5397  C  CB  . HIS A 1 1104 ? 98.272  112.335 132.823 1.00 30.19  ? 675  HIS A CB  1 
ATOM   5398  C  CG  . HIS A 1 1104 ? 97.649  113.534 132.208 1.00 27.91  ? 675  HIS A CG  1 
ATOM   5399  N  ND1 . HIS A 1 1104 ? 97.071  114.530 132.958 1.00 29.55  ? 675  HIS A ND1 1 
ATOM   5400  C  CD2 . HIS A 1 1104 ? 97.457  113.873 130.915 1.00 37.25  ? 675  HIS A CD2 1 
ATOM   5401  C  CE1 . HIS A 1 1104 ? 96.577  115.453 132.154 1.00 32.66  ? 675  HIS A CE1 1 
ATOM   5402  N  NE2 . HIS A 1 1104 ? 96.791  115.074 130.908 1.00 37.28  ? 675  HIS A NE2 1 
ATOM   5403  N  N   . VAL A 1 1105 ? 99.926  111.584 130.619 1.00 22.60  ? 676  VAL A N   1 
ATOM   5404  C  CA  . VAL A 1 1105 ? 100.357 111.670 129.237 1.00 29.99  ? 676  VAL A CA  1 
ATOM   5405  C  C   . VAL A 1 1105 ? 99.135  111.844 128.351 1.00 33.50  ? 676  VAL A C   1 
ATOM   5406  O  O   . VAL A 1 1105 ? 98.158  111.093 128.453 1.00 37.14  ? 676  VAL A O   1 
ATOM   5407  C  CB  . VAL A 1 1105 ? 101.222 110.471 128.828 1.00 35.35  ? 676  VAL A CB  1 
ATOM   5408  C  CG1 . VAL A 1 1105 ? 101.494 110.514 127.337 1.00 40.02  ? 676  VAL A CG1 1 
ATOM   5409  C  CG2 . VAL A 1 1105 ? 102.539 110.528 129.579 1.00 33.42  ? 676  VAL A CG2 1 
ATOM   5410  N  N   . SER A 1 1106 ? 99.197  112.856 127.492 1.00 31.51  ? 677  SER A N   1 
ATOM   5411  C  CA  . SER A 1 1106 ? 98.102  113.241 126.618 1.00 30.81  ? 677  SER A CA  1 
ATOM   5412  C  C   . SER A 1 1106 ? 98.041  112.295 125.424 1.00 46.52  ? 677  SER A C   1 
ATOM   5413  O  O   . SER A 1 1106 ? 98.085  112.703 124.261 1.00 45.39  ? 677  SER A O   1 
ATOM   5414  C  CB  . SER A 1 1106 ? 98.318  114.667 126.152 1.00 37.59  ? 677  SER A CB  1 
ATOM   5415  O  OG  . SER A 1 1106 ? 99.530  114.712 125.420 1.00 36.28  ? 677  SER A OG  1 
ATOM   5416  N  N   . ASP A 1 1107 ? 97.955  110.998 125.743 1.00 58.80  ? 678  ASP A N   1 
ATOM   5417  C  CA  . ASP A 1 1107 ? 97.955  109.917 124.754 1.00 56.74  ? 678  ASP A CA  1 
ATOM   5418  C  C   . ASP A 1 1107 ? 96.531  109.655 124.280 1.00 42.53  ? 678  ASP A C   1 
ATOM   5419  O  O   . ASP A 1 1107 ? 95.644  109.369 125.091 1.00 46.71  ? 678  ASP A O   1 
ATOM   5420  C  CB  . ASP A 1 1107 ? 98.551  108.645 125.363 1.00 55.31  ? 678  ASP A CB  1 
ATOM   5421  C  CG  . ASP A 1 1107 ? 99.264  107.782 124.338 1.00 64.18  ? 678  ASP A CG  1 
ATOM   5422  O  OD1 . ASP A 1 1107 ? 99.230  108.144 123.140 1.00 61.94  ? 678  ASP A OD1 1 
ATOM   5423  O  OD2 . ASP A 1 1107 ? 99.851  106.744 124.736 1.00 62.63  ? 678  ASP A OD2 1 
ATOM   5424  N  N   . TYR A 1 1108 ? 96.313  109.745 122.978 1.00 33.19  ? 679  TYR A N   1 
ATOM   5425  C  CA  . TYR A 1 1108 ? 94.940  109.803 122.511 1.00 36.37  ? 679  TYR A CA  1 
ATOM   5426  C  C   . TYR A 1 1108 ? 94.148  108.552 122.870 1.00 39.10  ? 679  TYR A C   1 
ATOM   5427  O  O   . TYR A 1 1108 ? 92.944  108.638 123.139 1.00 47.17  ? 679  TYR A O   1 
ATOM   5428  C  CB  . TYR A 1 1108 ? 94.920  110.065 121.014 1.00 46.46  ? 679  TYR A CB  1 
ATOM   5429  C  CG  . TYR A 1 1108 ? 93.539  110.381 120.482 1.00 47.09  ? 679  TYR A CG  1 
ATOM   5430  C  CD1 . TYR A 1 1108 ? 92.753  111.338 121.070 1.00 38.98  ? 679  TYR A CD1 1 
ATOM   5431  C  CD2 . TYR A 1 1108 ? 93.053  109.745 119.351 1.00 56.00  ? 679  TYR A CD2 1 
ATOM   5432  C  CE1 . TYR A 1 1108 ? 91.515  111.629 120.588 1.00 40.25  ? 679  TYR A CE1 1 
ATOM   5433  C  CE2 . TYR A 1 1108 ? 91.815  110.033 118.855 1.00 50.13  ? 679  TYR A CE2 1 
ATOM   5434  C  CZ  . TYR A 1 1108 ? 91.056  110.985 119.471 1.00 44.15  ? 679  TYR A CZ  1 
ATOM   5435  O  OH  . TYR A 1 1108 ? 89.806  111.271 118.976 1.00 53.12  ? 679  TYR A OH  1 
ATOM   5436  N  N   . TYR A 1 1109 ? 94.787  107.385 122.887 1.00 34.12  ? 680  TYR A N   1 
ATOM   5437  C  CA  . TYR A 1 1109 ? 94.061  106.137 123.094 1.00 35.76  ? 680  TYR A CA  1 
ATOM   5438  C  C   . TYR A 1 1109 ? 94.370  105.454 124.410 1.00 42.84  ? 680  TYR A C   1 
ATOM   5439  O  O   . TYR A 1 1109 ? 94.147  104.243 124.544 1.00 46.74  ? 680  TYR A O   1 
ATOM   5440  C  CB  . TYR A 1 1109 ? 94.337  105.146 121.979 1.00 41.79  ? 680  TYR A CB  1 
ATOM   5441  C  CG  . TYR A 1 1109 ? 93.739  105.529 120.671 1.00 43.93  ? 680  TYR A CG  1 
ATOM   5442  C  CD1 . TYR A 1 1109 ? 92.396  105.291 120.419 1.00 40.70  ? 680  TYR A CD1 1 
ATOM   5443  C  CD2 . TYR A 1 1109 ? 94.515  106.072 119.670 1.00 43.94  ? 680  TYR A CD2 1 
ATOM   5444  C  CE1 . TYR A 1 1109 ? 91.851  105.603 119.225 1.00 46.07  ? 680  TYR A CE1 1 
ATOM   5445  C  CE2 . TYR A 1 1109 ? 93.974  106.388 118.464 1.00 43.48  ? 680  TYR A CE2 1 
ATOM   5446  C  CZ  . TYR A 1 1109 ? 92.647  106.154 118.245 1.00 47.53  ? 680  TYR A CZ  1 
ATOM   5447  O  OH  . TYR A 1 1109 ? 92.121  106.483 117.020 1.00 55.54  ? 680  TYR A OH  1 
ATOM   5448  N  N   . ASN A 1 1110 ? 94.897  106.181 125.374 1.00 37.97  ? 681  ASN A N   1 
ATOM   5449  C  CA  . ASN A 1 1110 ? 95.304  105.593 126.641 1.00 23.69  ? 681  ASN A CA  1 
ATOM   5450  C  C   . ASN A 1 1110 ? 95.188  106.668 127.672 1.00 21.84  ? 681  ASN A C   1 
ATOM   5451  O  O   . ASN A 1 1110 ? 96.152  107.375 127.987 1.00 34.88  ? 681  ASN A O   1 
ATOM   5452  C  CB  . ASN A 1 1110 ? 96.716  105.047 126.570 1.00 35.15  ? 681  ASN A CB  1 
ATOM   5453  C  CG  . ASN A 1 1110 ? 97.064  104.256 127.776 1.00 50.26  ? 681  ASN A CG  1 
ATOM   5454  O  OD1 . ASN A 1 1110 ? 96.195  103.944 128.586 1.00 48.13  ? 681  ASN A OD1 1 
ATOM   5455  N  ND2 . ASN A 1 1110 ? 98.342  103.902 127.913 1.00 54.29  ? 681  ASN A ND2 1 
ATOM   5456  N  N   . PRO A 1 1111 ? 94.005  106.862 128.184 1.00 20.05  ? 682  PRO A N   1 
ATOM   5457  C  CA  . PRO A 1 1111 ? 93.802  107.703 129.350 1.00 42.64  ? 682  PRO A CA  1 
ATOM   5458  C  C   . PRO A 1 1111 ? 94.436  107.107 130.606 1.00 46.74  ? 682  PRO A C   1 
ATOM   5459  O  O   . PRO A 1 1111 ? 94.765  105.909 130.635 1.00 47.31  ? 682  PRO A O   1 
ATOM   5460  C  CB  . PRO A 1 1111 ? 92.271  107.742 129.461 1.00 43.85  ? 682  PRO A CB  1 
ATOM   5461  C  CG  . PRO A 1 1111 ? 91.828  106.448 128.833 1.00 39.49  ? 682  PRO A CG  1 
ATOM   5462  C  CD  . PRO A 1 1111 ? 92.787  106.223 127.705 1.00 30.04  ? 682  PRO A CD  1 
ATOM   5463  N  N   . PRO A 1 1112 ? 94.640  107.913 131.664 1.00 25.05  ? 683  PRO A N   1 
ATOM   5464  C  CA  . PRO A 1 1112 ? 95.128  107.375 132.926 1.00 16.49  ? 683  PRO A CA  1 
ATOM   5465  C  C   . PRO A 1 1112 ? 94.186  106.330 133.451 1.00 24.42  ? 683  PRO A C   1 
ATOM   5466  O  O   . PRO A 1 1112 ? 92.977  106.408 133.257 1.00 36.46  ? 683  PRO A O   1 
ATOM   5467  C  CB  . PRO A 1 1112 ? 95.112  108.581 133.845 1.00 33.10  ? 683  PRO A CB  1 
ATOM   5468  C  CG  . PRO A 1 1112 ? 95.259  109.692 132.976 1.00 39.95  ? 683  PRO A CG  1 
ATOM   5469  C  CD  . PRO A 1 1112 ? 94.521  109.368 131.737 1.00 35.13  ? 683  PRO A CD  1 
ATOM   5470  N  N   . HIS A 1 1113 ? 94.742  105.357 134.135 1.00 23.74  ? 684  HIS A N   1 
ATOM   5471  C  CA  . HIS A 1 1113 ? 93.954  104.195 134.453 1.00 21.74  ? 684  HIS A CA  1 
ATOM   5472  C  C   . HIS A 1 1113 ? 92.801  104.591 135.328 1.00 19.11  ? 684  HIS A C   1 
ATOM   5473  O  O   . HIS A 1 1113 ? 92.822  105.628 135.981 1.00 30.26  ? 684  HIS A O   1 
ATOM   5474  C  CB  . HIS A 1 1113 ? 94.811  103.164 135.141 1.00 31.86  ? 684  HIS A CB  1 
ATOM   5475  C  CG  . HIS A 1 1113 ? 95.911  102.674 134.274 1.00 29.35  ? 684  HIS A CG  1 
ATOM   5476  N  ND1 . HIS A 1 1113 ? 96.425  101.400 134.362 1.00 36.85  ? 684  HIS A ND1 1 
ATOM   5477  C  CD2 . HIS A 1 1113 ? 96.575  103.283 133.264 1.00 34.33  ? 684  HIS A CD2 1 
ATOM   5478  C  CE1 . HIS A 1 1113 ? 97.376  101.252 133.455 1.00 45.61  ? 684  HIS A CE1 1 
ATOM   5479  N  NE2 . HIS A 1 1113 ? 97.488  102.382 132.779 1.00 44.32  ? 684  HIS A NE2 1 
ATOM   5480  N  N   . ASN A 1 1114 ? 91.758  103.790 135.270 1.00 27.86  ? 685  ASN A N   1 
ATOM   5481  C  CA  . ASN A 1 1114 ? 90.635  103.877 136.187 1.00 36.10  ? 685  ASN A CA  1 
ATOM   5482  C  C   . ASN A 1 1114 ? 89.935  105.221 136.116 1.00 47.84  ? 685  ASN A C   1 
ATOM   5483  O  O   . ASN A 1 1114 ? 89.232  105.610 137.058 1.00 53.16  ? 685  ASN A O   1 
ATOM   5484  C  CB  . ASN A 1 1114 ? 91.087  103.592 137.618 1.00 43.62  ? 685  ASN A CB  1 
ATOM   5485  C  CG  . ASN A 1 1114 ? 91.641  102.192 137.771 1.00 52.17  ? 685  ASN A CG  1 
ATOM   5486  O  OD1 . ASN A 1 1114 ? 91.195  101.265 137.089 1.00 50.57  ? 685  ASN A OD1 1 
ATOM   5487  N  ND2 . ASN A 1 1114 ? 92.589  102.017 138.695 1.00 54.71  ? 685  ASN A ND2 1 
ATOM   5488  N  N   . LEU A 1 1115 ? 90.125  105.943 135.018 1.00 43.27  ? 686  LEU A N   1 
ATOM   5489  C  CA  . LEU A 1 1115 ? 89.524  107.256 134.859 1.00 37.82  ? 686  LEU A CA  1 
ATOM   5490  C  C   . LEU A 1 1115 ? 88.083  107.096 134.434 1.00 39.82  ? 686  LEU A C   1 
ATOM   5491  O  O   . LEU A 1 1115 ? 87.795  106.403 133.457 1.00 48.35  ? 686  LEU A O   1 
ATOM   5492  C  CB  . LEU A 1 1115 ? 90.288  108.048 133.816 1.00 36.94  ? 686  LEU A CB  1 
ATOM   5493  C  CG  . LEU A 1 1115 ? 89.890  109.490 133.693 1.00 44.67  ? 686  LEU A CG  1 
ATOM   5494  C  CD1 . LEU A 1 1115 ? 90.249  110.155 134.992 1.00 49.76  ? 686  LEU A CD1 1 
ATOM   5495  C  CD2 . LEU A 1 1115 ? 90.688  110.085 132.551 1.00 47.02  ? 686  LEU A CD2 1 
ATOM   5496  N  N   . THR A 1 1116 ? 87.174  107.717 135.168 1.00 41.34  ? 687  THR A N   1 
ATOM   5497  C  CA  . THR A 1 1116 ? 85.760  107.627 134.842 1.00 50.02  ? 687  THR A CA  1 
ATOM   5498  C  C   . THR A 1 1116 ? 85.141  109.011 134.995 1.00 61.70  ? 687  THR A C   1 
ATOM   5499  O  O   . THR A 1 1116 ? 85.788  109.952 135.466 1.00 62.98  ? 687  THR A O   1 
ATOM   5500  C  CB  . THR A 1 1116 ? 85.031  106.610 135.735 1.00 57.53  ? 687  THR A CB  1 
ATOM   5501  O  OG1 . THR A 1 1116 ? 85.239  106.947 137.111 1.00 61.61  ? 687  THR A OG1 1 
ATOM   5502  C  CG2 . THR A 1 1116 ? 85.573  105.199 135.502 1.00 60.54  ? 687  THR A CG2 1 
ATOM   5503  N  N   . LEU A 1 1117 ? 83.876  109.144 134.576 1.00 66.38  ? 688  LEU A N   1 
ATOM   5504  C  CA  . LEU A 1 1117 ? 83.175  110.418 134.724 1.00 57.66  ? 688  LEU A CA  1 
ATOM   5505  C  C   . LEU A 1 1117 ? 82.890  110.758 136.180 1.00 53.75  ? 688  LEU A C   1 
ATOM   5506  O  O   . LEU A 1 1117 ? 82.695  111.933 136.502 1.00 59.33  ? 688  LEU A O   1 
ATOM   5507  C  CB  . LEU A 1 1117 ? 81.874  110.402 133.930 1.00 56.94  ? 688  LEU A CB  1 
ATOM   5508  C  CG  . LEU A 1 1117 ? 81.126  111.734 133.874 1.00 66.75  ? 688  LEU A CG  1 
ATOM   5509  C  CD1 . LEU A 1 1117 ? 82.019  112.826 133.296 1.00 61.19  ? 688  LEU A CD1 1 
ATOM   5510  C  CD2 . LEU A 1 1117 ? 79.820  111.605 133.073 1.00 74.03  ? 688  LEU A CD2 1 
ATOM   5511  N  N   . GLU A 1 1118 ? 82.870  109.767 137.066 1.00 49.43  ? 689  GLU A N   1 
ATOM   5512  C  CA  . GLU A 1 1118 ? 82.657  110.070 138.472 1.00 48.80  ? 689  GLU A CA  1 
ATOM   5513  C  C   . GLU A 1 1118 ? 83.843  110.823 139.054 1.00 49.72  ? 689  GLU A C   1 
ATOM   5514  O  O   . GLU A 1 1118 ? 83.667  111.846 139.722 1.00 54.19  ? 689  GLU A O   1 
ATOM   5515  C  CB  . GLU A 1 1118 ? 82.388  108.788 139.261 1.00 67.82  ? 689  GLU A CB  1 
ATOM   5516  C  CG  . GLU A 1 1118 ? 81.004  108.139 139.016 1.00 78.93  ? 689  GLU A CG  1 
ATOM   5517  C  CD  . GLU A 1 1118 ? 80.914  107.371 137.688 1.00 89.80  ? 689  GLU A CD  1 
ATOM   5518  O  OE1 . GLU A 1 1118 ? 81.950  107.257 136.988 1.00 81.77  ? 689  GLU A OE1 1 
ATOM   5519  O  OE2 . GLU A 1 1118 ? 79.813  106.866 137.354 1.00 85.52  ? 689  GLU A OE2 1 
ATOM   5520  N  N   . ASN A 1 1119 ? 85.063  110.349 138.807 1.00 48.78  ? 690  ASN A N   1 
ATOM   5521  C  CA  . ASN A 1 1119 ? 86.253  110.977 139.376 1.00 43.74  ? 690  ASN A CA  1 
ATOM   5522  C  C   . ASN A 1 1119 ? 87.024  111.774 138.336 1.00 47.61  ? 690  ASN A C   1 
ATOM   5523  O  O   . ASN A 1 1119 ? 88.255  111.757 138.321 1.00 53.25  ? 690  ASN A O   1 
ATOM   5524  C  CB  . ASN A 1 1119 ? 87.199  109.961 140.018 1.00 46.38  ? 690  ASN A CB  1 
ATOM   5525  C  CG  . ASN A 1 1119 ? 87.665  108.861 139.052 1.00 48.59  ? 690  ASN A CG  1 
ATOM   5526  O  OD1 . ASN A 1 1119 ? 87.965  109.121 137.889 1.00 47.00  ? 690  ASN A OD1 1 
ATOM   5527  N  ND2 . ASN A 1 1119 ? 87.775  107.628 139.559 1.00 51.77  ? 690  ASN A ND2 1 
ATOM   5528  N  N   . ARG A 1 1120 ? 86.330  112.447 137.424 1.00 45.49  ? 691  ARG A N   1 
ATOM   5529  C  CA  . ARG A 1 1120 ? 87.055  113.248 136.448 1.00 38.89  ? 691  ARG A CA  1 
ATOM   5530  C  C   . ARG A 1 1120 ? 87.672  114.477 137.092 1.00 50.68  ? 691  ARG A C   1 
ATOM   5531  O  O   . ARG A 1 1120 ? 88.781  114.882 136.726 1.00 56.65  ? 691  ARG A O   1 
ATOM   5532  C  CB  . ARG A 1 1120 ? 86.140  113.645 135.309 1.00 49.15  ? 691  ARG A CB  1 
ATOM   5533  C  CG  . ARG A 1 1120 ? 86.876  114.214 134.159 1.00 47.26  ? 691  ARG A CG  1 
ATOM   5534  C  CD  . ARG A 1 1120 ? 85.923  114.962 133.316 1.00 41.21  ? 691  ARG A CD  1 
ATOM   5535  N  NE  . ARG A 1 1120 ? 85.736  116.270 133.884 1.00 45.44  ? 691  ARG A NE  1 
ATOM   5536  C  CZ  . ARG A 1 1120 ? 86.451  117.309 133.498 1.00 56.44  ? 691  ARG A CZ  1 
ATOM   5537  N  NH1 . ARG A 1 1120 ? 87.412  117.125 132.603 1.00 47.98  ? 691  ARG A NH1 1 
ATOM   5538  N  NH2 . ARG A 1 1120 ? 86.244  118.506 134.041 1.00 65.76  ? 691  ARG A NH2 1 
ATOM   5539  N  N   . ASP A 1 1121 ? 86.984  115.075 138.066 1.00 52.83  ? 692  ASP A N   1 
ATOM   5540  C  CA  . ASP A 1 1121 ? 87.516  116.269 138.722 1.00 57.13  ? 692  ASP A CA  1 
ATOM   5541  C  C   . ASP A 1 1121 ? 88.762  115.966 139.558 1.00 57.70  ? 692  ASP A C   1 
ATOM   5542  O  O   . ASP A 1 1121 ? 89.694  116.780 139.610 1.00 61.66  ? 692  ASP A O   1 
ATOM   5543  C  CB  . ASP A 1 1121 ? 86.425  116.923 139.571 1.00 62.93  ? 692  ASP A CB  1 
ATOM   5544  C  CG  . ASP A 1 1121 ? 85.200  117.317 138.745 1.00 80.32  ? 692  ASP A CG  1 
ATOM   5545  O  OD1 . ASP A 1 1121 ? 85.359  117.556 137.523 1.00 74.00  ? 692  ASP A OD1 1 
ATOM   5546  O  OD2 . ASP A 1 1121 ? 84.084  117.400 139.310 1.00 83.89  ? 692  ASP A OD2 1 
ATOM   5547  N  N   . ASN A 1 1122 ? 88.808  114.803 140.205 1.00 49.29  ? 693  ASN A N   1 
ATOM   5548  C  CA  . ASN A 1 1122 ? 89.885  114.422 141.117 1.00 46.23  ? 693  ASN A CA  1 
ATOM   5549  C  C   . ASN A 1 1122 ? 90.439  113.081 140.653 1.00 48.44  ? 693  ASN A C   1 
ATOM   5550  O  O   . ASN A 1 1122 ? 90.189  112.045 141.288 1.00 55.62  ? 693  ASN A O   1 
ATOM   5551  C  CB  . ASN A 1 1122 ? 89.373  114.342 142.559 1.00 49.71  ? 693  ASN A CB  1 
ATOM   5552  C  CG  . ASN A 1 1122 ? 90.489  114.202 143.581 1.00 51.09  ? 693  ASN A CG  1 
ATOM   5553  O  OD1 . ASN A 1 1122 ? 91.595  113.753 143.260 1.00 49.11  ? 693  ASN A OD1 1 
ATOM   5554  N  ND2 . ASN A 1 1122 ? 90.200  114.578 144.828 1.00 47.96  ? 693  ASN A ND2 1 
ATOM   5555  N  N   . PRO A 1 1123 ? 91.207  113.060 139.566 1.00 40.16  ? 694  PRO A N   1 
ATOM   5556  C  CA  . PRO A 1 1123 ? 91.561  111.790 138.950 1.00 37.29  ? 694  PRO A CA  1 
ATOM   5557  C  C   . PRO A 1 1123 ? 92.385  110.948 139.934 1.00 41.20  ? 694  PRO A C   1 
ATOM   5558  O  O   . PRO A 1 1123 ? 93.103  111.503 140.775 1.00 54.36  ? 694  PRO A O   1 
ATOM   5559  C  CB  . PRO A 1 1123 ? 92.417  112.199 137.750 1.00 37.16  ? 694  PRO A CB  1 
ATOM   5560  C  CG  . PRO A 1 1123 ? 92.187  113.636 137.569 1.00 46.99  ? 694  PRO A CG  1 
ATOM   5561  C  CD  . PRO A 1 1123 ? 91.890  114.183 138.926 1.00 46.49  ? 694  PRO A CD  1 
ATOM   5562  N  N   . PRO A 1 1124 ? 92.268  109.640 139.850 1.00 31.83  ? 695  PRO A N   1 
ATOM   5563  C  CA  . PRO A 1 1124 ? 93.139  108.799 140.680 1.00 33.33  ? 695  PRO A CA  1 
ATOM   5564  C  C   . PRO A 1 1124 ? 94.531  108.671 140.088 1.00 39.74  ? 695  PRO A C   1 
ATOM   5565  O  O   . PRO A 1 1124 ? 94.707  108.548 138.874 1.00 44.38  ? 695  PRO A O   1 
ATOM   5566  C  CB  . PRO A 1 1124 ? 92.431  107.449 140.667 1.00 47.13  ? 695  PRO A CB  1 
ATOM   5567  C  CG  . PRO A 1 1124 ? 91.754  107.434 139.312 1.00 56.02  ? 695  PRO A CG  1 
ATOM   5568  C  CD  . PRO A 1 1124 ? 91.319  108.864 139.055 1.00 47.64  ? 695  PRO A CD  1 
ATOM   5569  N  N   . GLU A 1 1125 ? 95.524  108.681 140.973 1.00 41.69  ? 696  GLU A N   1 
ATOM   5570  C  CA  . GLU A 1 1125 ? 96.867  108.262 140.608 1.00 38.17  ? 696  GLU A CA  1 
ATOM   5571  C  C   . GLU A 1 1125 ? 96.845  106.817 140.141 1.00 40.19  ? 696  GLU A C   1 
ATOM   5572  O  O   . GLU A 1 1125 ? 96.026  106.013 140.586 1.00 49.52  ? 696  GLU A O   1 
ATOM   5573  C  CB  . GLU A 1 1125 ? 97.800  108.374 141.805 1.00 44.77  ? 696  GLU A CB  1 
ATOM   5574  C  CG  . GLU A 1 1125 ? 98.195  109.801 142.147 1.00 61.80  ? 696  GLU A CG  1 
ATOM   5575  C  CD  . GLU A 1 1125 ? 99.136  109.884 143.362 1.00 73.63  ? 696  GLU A CD  1 
ATOM   5576  O  OE1 . GLU A 1 1125 ? 98.947  110.794 144.211 1.00 64.44  ? 696  GLU A OE1 1 
ATOM   5577  O  OE2 . GLU A 1 1125 ? 100.058 109.040 143.470 1.00 64.47  ? 696  GLU A OE2 1 
ATOM   5578  N  N   . GLY A 1 1126 ? 97.749  106.484 139.238 1.00 37.00  ? 697  GLY A N   1 
ATOM   5579  C  CA  . GLY A 1 1126 ? 97.846  105.133 138.749 1.00 34.54  ? 697  GLY A CA  1 
ATOM   5580  C  C   . GLY A 1 1126 ? 99.182  104.968 138.084 1.00 32.98  ? 697  GLY A C   1 
ATOM   5581  O  O   . GLY A 1 1126 ? 100.048 105.835 138.184 1.00 43.37  ? 697  GLY A O   1 
ATOM   5582  N  N   . PRO A 1 1127 ? 99.389  103.856 137.397 1.00 24.51  ? 698  PRO A N   1 
ATOM   5583  C  CA  . PRO A 1 1127 ? 100.644 103.684 136.660 1.00 25.22  ? 698  PRO A CA  1 
ATOM   5584  C  C   . PRO A 1 1127 ? 100.822 104.659 135.528 1.00 27.93  ? 698  PRO A C   1 
ATOM   5585  O  O   . PRO A 1 1127 ? 101.953 104.872 135.078 1.00 35.44  ? 698  PRO A O   1 
ATOM   5586  C  CB  . PRO A 1 1127 ? 100.561 102.246 136.153 1.00 37.61  ? 698  PRO A CB  1 
ATOM   5587  C  CG  . PRO A 1 1127 ? 99.107  101.948 136.151 1.00 47.76  ? 698  PRO A CG  1 
ATOM   5588  C  CD  . PRO A 1 1127 ? 98.508  102.692 137.294 1.00 37.63  ? 698  PRO A CD  1 
ATOM   5589  N  N   . SER A 1 1128 ? 99.756  105.270 135.050 1.00 34.12  ? 699  SER A N   1 
ATOM   5590  C  CA  . SER A 1 1128 ? 99.893  106.233 133.968 1.00 35.27  ? 699  SER A CA  1 
ATOM   5591  C  C   . SER A 1 1128 ? 100.082 107.657 134.463 1.00 34.71  ? 699  SER A C   1 
ATOM   5592  O  O   . SER A 1 1128 ? 100.715 108.460 133.774 1.00 41.30  ? 699  SER A O   1 
ATOM   5593  C  CB  . SER A 1 1128 ? 98.663  106.168 133.058 1.00 42.01  ? 699  SER A CB  1 
ATOM   5594  O  OG  . SER A 1 1128 ? 98.748  107.091 131.996 1.00 43.33  ? 699  SER A OG  1 
ATOM   5595  N  N   . SER A 1 1129 ? 99.557  107.994 135.639 1.00 31.08  ? 700  SER A N   1 
ATOM   5596  C  CA  . SER A 1 1129 ? 99.527  109.374 136.095 1.00 28.20  ? 700  SER A CA  1 
ATOM   5597  C  C   . SER A 1 1129 ? 99.934  109.462 137.555 1.00 28.20  ? 700  SER A C   1 
ATOM   5598  O  O   . SER A 1 1129 ? 99.652  108.554 138.336 1.00 41.71  ? 700  SER A O   1 
ATOM   5599  C  CB  . SER A 1 1129 ? 98.131  109.936 135.960 1.00 38.77  ? 700  SER A CB  1 
ATOM   5600  O  OG  . SER A 1 1129 ? 97.247  109.165 136.759 1.00 40.12  ? 700  SER A OG  1 
ATOM   5601  N  N   . TYR A 1 1130 ? 100.556 110.570 137.938 1.00 22.16  ? 701  TYR A N   1 
ATOM   5602  C  CA  . TYR A 1 1130 ? 100.970 110.746 139.317 1.00 21.42  ? 701  TYR A CA  1 
ATOM   5603  C  C   . TYR A 1 1130 ? 100.858 112.194 139.693 1.00 24.42  ? 701  TYR A C   1 
ATOM   5604  O  O   . TYR A 1 1130 ? 100.915 113.072 138.838 1.00 33.81  ? 701  TYR A O   1 
ATOM   5605  C  CB  . TYR A 1 1130 ? 102.394 110.323 139.539 1.00 33.89  ? 701  TYR A CB  1 
ATOM   5606  C  CG  . TYR A 1 1130 ? 103.397 111.214 138.860 1.00 30.32  ? 701  TYR A CG  1 
ATOM   5607  C  CD1 . TYR A 1 1130 ? 103.628 111.110 137.494 1.00 33.74  ? 701  TYR A CD1 1 
ATOM   5608  C  CD2 . TYR A 1 1130 ? 104.153 112.115 139.586 1.00 30.60  ? 701  TYR A CD2 1 
ATOM   5609  C  CE1 . TYR A 1 1130 ? 104.564 111.891 136.864 1.00 31.40  ? 701  TYR A CE1 1 
ATOM   5610  C  CE2 . TYR A 1 1130 ? 105.098 112.907 138.964 1.00 29.95  ? 701  TYR A CE2 1 
ATOM   5611  C  CZ  . TYR A 1 1130 ? 105.297 112.789 137.601 1.00 31.77  ? 701  TYR A CZ  1 
ATOM   5612  O  OH  . TYR A 1 1130 ? 106.230 113.568 136.954 1.00 34.97  ? 701  TYR A OH  1 
ATOM   5613  N  N   . ARG A 1 1131 ? 100.741 112.458 140.986 1.00 25.40  ? 702  ARG A N   1 
ATOM   5614  C  CA  . ARG A 1 1131 ? 100.261 113.783 141.340 1.00 23.59  ? 702  ARG A CA  1 
ATOM   5615  C  C   . ARG A 1 1131 ? 101.381 114.773 141.608 1.00 26.49  ? 702  ARG A C   1 
ATOM   5616  O  O   . ARG A 1 1131 ? 101.520 115.773 140.894 1.00 32.45  ? 702  ARG A O   1 
ATOM   5617  C  CB  . ARG A 1 1131 ? 99.337  113.716 142.543 1.00 26.41  ? 702  ARG A CB  1 
ATOM   5618  C  CG  . ARG A 1 1131 ? 98.686  115.031 142.716 1.00 25.78  ? 702  ARG A CG  1 
ATOM   5619  C  CD  . ARG A 1 1131 ? 97.782  115.237 141.557 1.00 30.05  ? 702  ARG A CD  1 
ATOM   5620  N  NE  . ARG A 1 1131 ? 96.791  114.184 141.467 1.00 26.04  ? 702  ARG A NE  1 
ATOM   5621  C  CZ  . ARG A 1 1131 ? 95.620  114.244 142.076 1.00 29.93  ? 702  ARG A CZ  1 
ATOM   5622  N  NH1 . ARG A 1 1131 ? 95.306  115.314 142.791 1.00 28.88  ? 702  ARG A NH1 1 
ATOM   5623  N  NH2 . ARG A 1 1131 ? 94.759  113.249 141.956 1.00 35.91  ? 702  ARG A NH2 1 
ATOM   5624  N  N   . GLY A 1 1132 ? 102.180 114.544 142.637 1.00 31.55  ? 703  GLY A N   1 
ATOM   5625  C  CA  . GLY A 1 1132 ? 103.105 115.564 143.069 1.00 32.74  ? 703  GLY A CA  1 
ATOM   5626  C  C   . GLY A 1 1132 ? 104.403 115.461 142.319 1.00 20.57  ? 703  GLY A C   1 
ATOM   5627  O  O   . GLY A 1 1132 ? 105.035 114.410 142.312 1.00 34.38  ? 703  GLY A O   1 
ATOM   5628  N  N   . HIS A 1 1133 ? 104.821 116.552 141.727 1.00 13.12  ? 704  HIS A N   1 
ATOM   5629  C  CA  . HIS A 1 1133 ? 106.020 116.518 140.919 1.00 16.45  ? 704  HIS A CA  1 
ATOM   5630  C  C   . HIS A 1 1133 ? 106.973 117.532 141.486 1.00 23.69  ? 704  HIS A C   1 
ATOM   5631  O  O   . HIS A 1 1133 ? 107.044 118.665 141.010 1.00 35.24  ? 704  HIS A O   1 
ATOM   5632  C  CB  . HIS A 1 1133 ? 105.695 116.832 139.522 1.00 29.43  ? 704  HIS A CB  1 
ATOM   5633  C  CG  . HIS A 1 1133 ? 106.864 116.736 138.601 1.00 20.76  ? 704  HIS A CG  1 
ATOM   5634  N  ND1 . HIS A 1 1133 ? 107.029 115.709 137.696 1.00 22.38  ? 704  HIS A ND1 1 
ATOM   5635  C  CD2 . HIS A 1 1133 ? 107.913 117.563 138.427 1.00 20.85  ? 704  HIS A CD2 1 
ATOM   5636  C  CE1 . HIS A 1 1133 ? 108.145 115.895 137.022 1.00 22.59  ? 704  HIS A CE1 1 
ATOM   5637  N  NE2 . HIS A 1 1133 ? 108.698 117.017 137.444 1.00 28.30  ? 704  HIS A NE2 1 
ATOM   5638  N  N   . MET A 1 1134 ? 107.707 117.143 142.507 1.00 21.01  ? 705  MET A N   1 
ATOM   5639  C  CA  . MET A 1 1134 ? 108.616 118.075 143.145 1.00 19.52  ? 705  MET A CA  1 
ATOM   5640  C  C   . MET A 1 1134 ? 109.913 118.103 142.355 1.00 23.47  ? 705  MET A C   1 
ATOM   5641  O  O   . MET A 1 1134 ? 110.908 117.482 142.728 1.00 34.62  ? 705  MET A O   1 
ATOM   5642  C  CB  . MET A 1 1134 ? 108.847 117.650 144.580 1.00 23.00  ? 705  MET A CB  1 
ATOM   5643  C  CG  . MET A 1 1134 ? 107.635 117.925 145.396 1.00 43.58  ? 705  MET A CG  1 
ATOM   5644  S  SD  . MET A 1 1134 ? 107.357 119.703 145.292 1.00 90.01  ? 705  MET A SD  1 
ATOM   5645  C  CE  . MET A 1 1134 ? 105.783 119.867 146.143 1.00 70.66  ? 705  MET A CE  1 
ATOM   5646  N  N   . GLY A 1 1135 ? 109.922 118.817 141.241 1.00 16.09  ? 706  GLY A N   1 
ATOM   5647  C  CA  . GLY A 1 1135 ? 111.090 118.718 140.390 1.00 17.21  ? 706  GLY A CA  1 
ATOM   5648  C  C   . GLY A 1 1135 ? 110.973 119.549 139.150 1.00 21.06  ? 706  GLY A C   1 
ATOM   5649  O  O   . GLY A 1 1135 ? 110.100 120.411 139.045 1.00 33.68  ? 706  GLY A O   1 
ATOM   5650  N  N   . GLY A 1 1136 ? 111.864 119.290 138.200 1.00 18.30  ? 707  GLY A N   1 
ATOM   5651  C  CA  . GLY A 1 1136 ? 111.815 119.950 136.920 1.00 25.91  ? 707  GLY A CA  1 
ATOM   5652  C  C   . GLY A 1 1136 ? 111.182 119.079 135.845 1.00 34.31  ? 707  GLY A C   1 
ATOM   5653  O  O   . GLY A 1 1136 ? 110.818 117.929 136.066 1.00 40.39  ? 707  GLY A O   1 
ATOM   5654  N  N   . ILE A 1 1137 ? 111.046 119.672 134.660 1.00 36.82  ? 708  ILE A N   1 
ATOM   5655  C  CA  . ILE A 1 1137 ? 110.611 118.994 133.444 1.00 34.52  ? 708  ILE A CA  1 
ATOM   5656  C  C   . ILE A 1 1137 ? 111.611 119.309 132.348 1.00 46.30  ? 708  ILE A C   1 
ATOM   5657  O  O   . ILE A 1 1137 ? 112.134 120.426 132.274 1.00 55.24  ? 708  ILE A O   1 
ATOM   5658  C  CB  . ILE A 1 1137 ? 109.206 119.440 133.006 1.00 49.77  ? 708  ILE A CB  1 
ATOM   5659  C  CG1 . ILE A 1 1137 ? 108.214 119.290 134.146 1.00 47.64  ? 708  ILE A CG1 1 
ATOM   5660  C  CG2 . ILE A 1 1137 ? 108.748 118.652 131.782 1.00 59.00  ? 708  ILE A CG2 1 
ATOM   5661  C  CD1 . ILE A 1 1137 ? 107.960 117.843 134.459 1.00 43.73  ? 708  ILE A CD1 1 
ATOM   5662  N  N   . GLU A 1 1138 ? 111.866 118.341 131.479 1.00 38.85  ? 709  GLU A N   1 
ATOM   5663  C  CA  . GLU A 1 1138 ? 112.820 118.591 130.414 1.00 46.05  ? 709  GLU A CA  1 
ATOM   5664  C  C   . GLU A 1 1138 ? 112.382 119.777 129.569 1.00 52.43  ? 709  GLU A C   1 
ATOM   5665  O  O   . GLU A 1 1138 ? 111.207 119.918 129.220 1.00 52.41  ? 709  GLU A O   1 
ATOM   5666  C  CB  . GLU A 1 1138 ? 112.989 117.353 129.542 1.00 68.69  ? 709  GLU A CB  1 
ATOM   5667  C  CG  . GLU A 1 1138 ? 114.069 117.496 128.462 1.00 79.75  ? 709  GLU A CG  1 
ATOM   5668  C  CD  . GLU A 1 1138 ? 114.245 116.228 127.617 1.00 93.14  ? 709  GLU A CD  1 
ATOM   5669  O  OE1 . GLU A 1 1138 ? 113.593 115.199 127.919 1.00 87.00  ? 709  GLU A OE1 1 
ATOM   5670  O  OE2 . GLU A 1 1138 ? 115.044 116.258 126.655 1.00 90.67  ? 709  GLU A OE2 1 
ATOM   5671  N  N   . GLY A 1 1139 ? 113.341 120.647 129.267 1.00 62.18  ? 710  GLY A N   1 
ATOM   5672  C  CA  . GLY A 1 1139 ? 113.148 121.812 128.417 1.00 59.70  ? 710  GLY A CA  1 
ATOM   5673  C  C   . GLY A 1 1139 ? 112.711 123.069 129.134 1.00 58.32  ? 710  GLY A C   1 
ATOM   5674  O  O   . GLY A 1 1139 ? 113.213 124.159 128.847 1.00 63.08  ? 710  GLY A O   1 
ATOM   5675  N  N   . LEU A 1 1140 ? 111.778 122.935 130.069 1.00 50.31  ? 711  LEU A N   1 
ATOM   5676  C  CA  . LEU A 1 1140 ? 111.264 124.082 130.801 1.00 45.35  ? 711  LEU A CA  1 
ATOM   5677  C  C   . LEU A 1 1140 ? 112.377 124.667 131.655 1.00 50.81  ? 711  LEU A C   1 
ATOM   5678  O  O   . LEU A 1 1140 ? 113.078 123.925 132.344 1.00 55.93  ? 711  LEU A O   1 
ATOM   5679  C  CB  . LEU A 1 1140 ? 110.111 123.633 131.678 1.00 45.84  ? 711  LEU A CB  1 
ATOM   5680  C  CG  . LEU A 1 1140 ? 108.758 123.392 131.017 1.00 62.60  ? 711  LEU A CG  1 
ATOM   5681  C  CD1 . LEU A 1 1140 ? 108.796 122.215 130.030 1.00 65.43  ? 711  LEU A CD1 1 
ATOM   5682  C  CD2 . LEU A 1 1140 ? 107.738 123.103 132.106 1.00 64.49  ? 711  LEU A CD2 1 
ATOM   5683  N  N   . GLN A 1 1141 ? 112.570 125.984 131.599 1.00 46.42  ? 712  GLN A N   1 
ATOM   5684  C  CA  . GLN A 1 1141 ? 113.658 126.633 132.345 1.00 43.65  ? 712  GLN A CA  1 
ATOM   5685  C  C   . GLN A 1 1141 ? 115.010 125.986 132.058 1.00 36.02  ? 712  GLN A C   1 
ATOM   5686  O  O   . GLN A 1 1141 ? 115.841 125.814 132.948 1.00 39.82  ? 712  GLN A O   1 
ATOM   5687  C  CB  . GLN A 1 1141 ? 113.386 126.630 133.851 1.00 41.91  ? 712  GLN A CB  1 
ATOM   5688  C  CG  . GLN A 1 1141 ? 112.489 127.736 134.356 1.00 44.83  ? 712  GLN A CG  1 
ATOM   5689  C  CD  . GLN A 1 1141 ? 112.335 127.678 135.867 1.00 45.88  ? 712  GLN A CD  1 
ATOM   5690  O  OE1 . GLN A 1 1141 ? 112.793 126.732 136.508 1.00 48.17  ? 712  GLN A OE1 1 
ATOM   5691  N  NE2 . GLN A 1 1141 ? 111.711 128.695 136.446 1.00 40.70  ? 712  GLN A NE2 1 
ATOM   5692  N  N   . GLN A 1 1142 ? 115.229 125.606 130.809 1.00 35.38  ? 713  GLN A N   1 
ATOM   5693  C  CA  . GLN A 1 1142 ? 116.562 125.187 130.426 1.00 33.31  ? 713  GLN A CA  1 
ATOM   5694  C  C   . GLN A 1 1142 ? 117.574 126.298 130.680 1.00 45.25  ? 713  GLN A C   1 
ATOM   5695  O  O   . GLN A 1 1142 ? 118.708 126.032 131.091 1.00 51.76  ? 713  GLN A O   1 
ATOM   5696  C  CB  . GLN A 1 1142 ? 116.574 124.778 128.958 1.00 51.62  ? 713  GLN A CB  1 
ATOM   5697  C  CG  . GLN A 1 1142 ? 117.968 124.526 128.373 1.00 68.09  ? 713  GLN A CG  1 
ATOM   5698  C  CD  . GLN A 1 1142 ? 118.594 123.218 128.847 1.00 84.94  ? 713  GLN A CD  1 
ATOM   5699  O  OE1 . GLN A 1 1142 ? 117.949 122.410 129.529 1.00 76.40  ? 713  GLN A OE1 1 
ATOM   5700  N  NE2 . GLN A 1 1142 ? 119.863 123.004 128.487 1.00 84.40  ? 713  GLN A NE2 1 
ATOM   5701  N  N   . LYS A 1 1143 ? 117.193 127.553 130.430 1.00 46.76  ? 714  LYS A N   1 
ATOM   5702  C  CA  . LYS A 1 1143 ? 118.136 128.649 130.633 1.00 38.19  ? 714  LYS A CA  1 
ATOM   5703  C  C   . LYS A 1 1143 ? 118.468 128.836 132.102 1.00 28.84  ? 714  LYS A C   1 
ATOM   5704  O  O   . LYS A 1 1143 ? 119.586 129.226 132.440 1.00 38.34  ? 714  LYS A O   1 
ATOM   5705  C  CB  . LYS A 1 1143 ? 117.596 129.956 130.055 1.00 48.14  ? 714  LYS A CB  1 
ATOM   5706  C  CG  . LYS A 1 1143 ? 117.596 130.052 128.558 1.00 43.47  ? 714  LYS A CG  1 
ATOM   5707  C  CD  . LYS A 1 1143 ? 119.013 130.028 128.051 1.00 43.10  ? 714  LYS A CD  1 
ATOM   5708  C  CE  . LYS A 1 1143 ? 119.012 130.159 126.545 1.00 65.76  ? 714  LYS A CE  1 
ATOM   5709  N  NZ  . LYS A 1 1143 ? 118.124 129.130 125.929 1.00 72.22  ? 714  LYS A NZ  1 
ATOM   5710  N  N   . LEU A 1 1144 ? 117.513 128.632 132.987 1.00 24.59  ? 715  LEU A N   1 
ATOM   5711  C  CA  . LEU A 1 1144 ? 117.877 128.833 134.374 1.00 20.56  ? 715  LEU A CA  1 
ATOM   5712  C  C   . LEU A 1 1144 ? 118.729 127.698 134.878 1.00 30.95  ? 715  LEU A C   1 
ATOM   5713  O  O   . LEU A 1 1144 ? 119.711 127.922 135.588 1.00 45.55  ? 715  LEU A O   1 
ATOM   5714  C  CB  . LEU A 1 1144 ? 116.644 128.966 135.237 1.00 28.47  ? 715  LEU A CB  1 
ATOM   5715  C  CG  . LEU A 1 1144 ? 116.987 129.006 136.709 1.00 28.14  ? 715  LEU A CG  1 
ATOM   5716  C  CD1 . LEU A 1 1144 ? 117.948 130.126 136.988 1.00 35.05  ? 715  LEU A CD1 1 
ATOM   5717  C  CD2 . LEU A 1 1144 ? 115.708 129.244 137.461 1.00 45.98  ? 715  LEU A CD2 1 
ATOM   5718  N  N   . TRP A 1 1145 ? 118.383 126.474 134.523 1.00 32.14  ? 716  TRP A N   1 
ATOM   5719  C  CA  . TRP A 1 1145 ? 119.103 125.339 135.078 1.00 27.46  ? 716  TRP A CA  1 
ATOM   5720  C  C   . TRP A 1 1145 ? 120.529 125.306 134.588 1.00 27.90  ? 716  TRP A C   1 
ATOM   5721  O  O   . TRP A 1 1145 ? 121.442 125.039 135.370 1.00 42.92  ? 716  TRP A O   1 
ATOM   5722  C  CB  . TRP A 1 1145 ? 118.376 124.068 134.721 1.00 29.94  ? 716  TRP A CB  1 
ATOM   5723  C  CG  . TRP A 1 1145 ? 117.068 124.076 135.375 1.00 31.89  ? 716  TRP A CG  1 
ATOM   5724  C  CD1 . TRP A 1 1145 ? 116.698 124.840 136.430 1.00 43.09  ? 716  TRP A CD1 1 
ATOM   5725  C  CD2 . TRP A 1 1145 ? 115.921 123.350 134.983 1.00 28.29  ? 716  TRP A CD2 1 
ATOM   5726  N  NE1 . TRP A 1 1145 ? 115.392 124.594 136.758 1.00 39.31  ? 716  TRP A NE1 1 
ATOM   5727  C  CE2 . TRP A 1 1145 ? 114.895 123.678 135.879 1.00 27.35  ? 716  TRP A CE2 1 
ATOM   5728  C  CE3 . TRP A 1 1145 ? 115.669 122.425 133.978 1.00 45.83  ? 716  TRP A CE3 1 
ATOM   5729  C  CZ2 . TRP A 1 1145 ? 113.643 123.124 135.804 1.00 39.85  ? 716  TRP A CZ2 1 
ATOM   5730  C  CZ3 . TRP A 1 1145 ? 114.416 121.868 133.897 1.00 51.01  ? 716  TRP A CZ3 1 
ATOM   5731  C  CH2 . TRP A 1 1145 ? 113.410 122.225 134.803 1.00 46.86  ? 716  TRP A CH2 1 
ATOM   5732  N  N   . THR A 1 1146 ? 120.750 125.599 133.317 1.00 23.88  ? 717  THR A N   1 
ATOM   5733  C  CA  . THR A 1 1146 ? 122.121 125.670 132.856 1.00 27.97  ? 717  THR A CA  1 
ATOM   5734  C  C   . THR A 1 1146 ? 122.890 126.754 133.596 1.00 32.30  ? 717  THR A C   1 
ATOM   5735  O  O   . THR A 1 1146 ? 124.101 126.618 133.807 1.00 45.58  ? 717  THR A O   1 
ATOM   5736  C  CB  . THR A 1 1146 ? 122.174 125.917 131.353 1.00 43.92  ? 717  THR A CB  1 
ATOM   5737  O  OG1 . THR A 1 1146 ? 121.334 124.974 130.675 1.00 49.53  ? 717  THR A OG1 1 
ATOM   5738  C  CG2 . THR A 1 1146 ? 123.586 125.708 130.861 1.00 58.42  ? 717  THR A CG2 1 
ATOM   5739  N  N   . SER A 1 1147 ? 122.215 127.813 134.038 1.00 24.44  ? 718  SER A N   1 
ATOM   5740  C  CA  . SER A 1 1147 ? 122.910 128.847 134.802 1.00 24.37  ? 718  SER A CA  1 
ATOM   5741  C  C   . SER A 1 1147 ? 123.311 128.354 136.188 1.00 33.14  ? 718  SER A C   1 
ATOM   5742  O  O   . SER A 1 1147 ? 124.410 128.659 136.665 1.00 41.80  ? 718  SER A O   1 
ATOM   5743  C  CB  . SER A 1 1147 ? 122.050 130.102 134.928 1.00 37.07  ? 718  SER A CB  1 
ATOM   5744  O  OG  . SER A 1 1147 ? 121.770 130.678 133.659 1.00 43.76  ? 718  SER A OG  1 
ATOM   5745  N  N   . ILE A 1 1148 ? 122.447 127.602 136.863 1.00 26.50  ? 719  ILE A N   1 
ATOM   5746  C  CA  . ILE A 1 1148 ? 122.848 127.051 138.145 1.00 19.42  ? 719  ILE A CA  1 
ATOM   5747  C  C   . ILE A 1 1148 ? 123.933 126.019 137.966 1.00 34.19  ? 719  ILE A C   1 
ATOM   5748  O  O   . ILE A 1 1148 ? 124.802 125.857 138.830 1.00 47.54  ? 719  ILE A O   1 
ATOM   5749  C  CB  . ILE A 1 1148 ? 121.662 126.432 138.855 1.00 28.37  ? 719  ILE A CB  1 
ATOM   5750  C  CG1 . ILE A 1 1148 ? 120.575 127.474 139.015 1.00 43.64  ? 719  ILE A CG1 1 
ATOM   5751  C  CG2 . ILE A 1 1148 ? 122.116 125.954 140.178 1.00 36.06  ? 719  ILE A CG2 1 
ATOM   5752  C  CD1 . ILE A 1 1148 ? 119.349 126.938 139.736 1.00 46.44  ? 719  ILE A CD1 1 
ATOM   5753  N  N   . SER A 1 1149 ? 123.888 125.274 136.862 1.00 34.91  ? 720  SER A N   1 
ATOM   5754  C  CA  . SER A 1 1149 ? 124.962 124.332 136.555 1.00 34.51  ? 720  SER A CA  1 
ATOM   5755  C  C   . SER A 1 1149 ? 126.309 125.037 136.395 1.00 39.04  ? 720  SER A C   1 
ATOM   5756  O  O   . SER A 1 1149 ? 127.322 124.582 136.946 1.00 49.81  ? 720  SER A O   1 
ATOM   5757  C  CB  . SER A 1 1149 ? 124.625 123.554 135.289 1.00 49.55  ? 720  SER A CB  1 
ATOM   5758  O  OG  . SER A 1 1149 ? 125.691 122.685 134.960 1.00 65.91  ? 720  SER A OG  1 
ATOM   5759  N  N   . CYS A 1 1150 ? 126.350 126.149 135.653 1.00 31.78  ? 721  CYS A N   1 
ATOM   5760  C  CA  . CYS A 1 1150 ? 127.615 126.877 135.535 1.00 32.19  ? 721  CYS A CA  1 
ATOM   5761  C  C   . CYS A 1 1150 ? 128.018 127.527 136.848 1.00 34.71  ? 721  CYS A C   1 
ATOM   5762  O  O   . CYS A 1 1150 ? 129.211 127.717 137.104 1.00 38.91  ? 721  CYS A O   1 
ATOM   5763  C  CB  . CYS A 1 1150 ? 127.534 127.927 134.449 1.00 32.07  ? 721  CYS A CB  1 
ATOM   5764  S  SG  . CYS A 1 1150 ? 127.290 127.157 132.853 1.00 69.68  ? 721  CYS A SG  1 
ATOM   5765  N  N   . ALA A 1 1151 ? 127.047 127.864 137.693 1.00 34.40  ? 722  ALA A N   1 
ATOM   5766  C  CA  . ALA A 1 1151 ? 127.377 128.319 139.037 1.00 34.43  ? 722  ALA A CA  1 
ATOM   5767  C  C   . ALA A 1 1151 ? 128.081 127.223 139.840 1.00 41.78  ? 722  ALA A C   1 
ATOM   5768  O  O   . ALA A 1 1151 ? 129.075 127.498 140.521 1.00 51.21  ? 722  ALA A O   1 
ATOM   5769  C  CB  . ALA A 1 1151 ? 126.114 128.793 139.755 1.00 30.78  ? 722  ALA A CB  1 
ATOM   5770  N  N   . GLN A 1 1152 ? 127.588 125.977 139.785 1.00 31.66  ? 723  GLN A N   1 
ATOM   5771  C  CA  . GLN A 1 1152 ? 128.269 124.883 140.488 1.00 24.98  ? 723  GLN A CA  1 
ATOM   5772  C  C   . GLN A 1 1152 ? 129.661 124.636 139.916 1.00 29.48  ? 723  GLN A C   1 
ATOM   5773  O  O   . GLN A 1 1152 ? 130.607 124.362 140.665 1.00 35.65  ? 723  GLN A O   1 
ATOM   5774  C  CB  . GLN A 1 1152 ? 127.447 123.611 140.405 1.00 26.87  ? 723  GLN A CB  1 
ATOM   5775  C  CG  . GLN A 1 1152 ? 126.070 123.751 140.974 1.00 34.75  ? 723  GLN A CG  1 
ATOM   5776  C  CD  . GLN A 1 1152 ? 125.219 122.540 140.657 1.00 48.53  ? 723  GLN A CD  1 
ATOM   5777  O  OE1 . GLN A 1 1152 ? 125.568 121.755 139.775 1.00 53.50  ? 723  GLN A OE1 1 
ATOM   5778  N  NE2 . GLN A 1 1152 ? 124.109 122.368 141.373 1.00 47.42  ? 723  GLN A NE2 1 
ATOM   5779  N  N   . ILE A 1 1153 ? 129.805 124.712 138.587 1.00 29.18  ? 724  ILE A N   1 
ATOM   5780  C  CA  . ILE A 1 1153 ? 131.122 124.544 137.969 1.00 25.95  ? 724  ILE A CA  1 
ATOM   5781  C  C   . ILE A 1 1153 ? 132.087 125.622 138.442 1.00 35.88  ? 724  ILE A C   1 
ATOM   5782  O  O   . ILE A 1 1153 ? 133.261 125.345 138.727 1.00 43.73  ? 724  ILE A O   1 
ATOM   5783  C  CB  . ILE A 1 1153 ? 131.018 124.545 136.440 1.00 32.71  ? 724  ILE A CB  1 
ATOM   5784  C  CG1 . ILE A 1 1153 ? 130.117 123.419 135.984 1.00 46.94  ? 724  ILE A CG1 1 
ATOM   5785  C  CG2 . ILE A 1 1153 ? 132.374 124.299 135.842 1.00 40.38  ? 724  ILE A CG2 1 
ATOM   5786  C  CD1 . ILE A 1 1153 ? 130.575 122.103 136.500 1.00 49.92  ? 724  ILE A CD1 1 
ATOM   5787  N  N   . SER A 1 1154 ? 131.626 126.872 138.530 1.00 35.69  ? 725  SER A N   1 
ATOM   5788  C  CA  . SER A 1 1154 ? 132.510 127.915 139.040 1.00 29.01  ? 725  SER A CA  1 
ATOM   5789  C  C   . SER A 1 1154 ? 132.778 127.755 140.528 1.00 31.71  ? 725  SER A C   1 
ATOM   5790  O  O   . SER A 1 1154 ? 133.851 128.144 140.999 1.00 44.64  ? 725  SER A O   1 
ATOM   5791  C  CB  . SER A 1 1154 ? 131.943 129.301 138.765 1.00 34.93  ? 725  SER A CB  1 
ATOM   5792  O  OG  . SER A 1 1154 ? 131.852 129.543 137.376 1.00 45.34  ? 725  SER A OG  1 
ATOM   5793  N  N   . LEU A 1 1155 ? 131.843 127.199 141.293 1.00 22.93  ? 726  LEU A N   1 
ATOM   5794  C  CA  . LEU A 1 1155 ? 132.154 126.950 142.691 1.00 17.74  ? 726  LEU A CA  1 
ATOM   5795  C  C   . LEU A 1 1155 ? 133.276 125.933 142.820 1.00 27.53  ? 726  LEU A C   1 
ATOM   5796  O  O   . LEU A 1 1155 ? 134.191 126.102 143.637 1.00 39.91  ? 726  LEU A O   1 
ATOM   5797  C  CB  . LEU A 1 1155 ? 130.934 126.465 143.422 1.00 21.50  ? 726  LEU A CB  1 
ATOM   5798  C  CG  . LEU A 1 1155 ? 131.346 125.931 144.769 1.00 22.44  ? 726  LEU A CG  1 
ATOM   5799  C  CD1 . LEU A 1 1155 ? 131.971 127.068 145.524 1.00 25.66  ? 726  LEU A CD1 1 
ATOM   5800  C  CD2 . LEU A 1 1155 ? 130.129 125.390 145.494 1.00 37.89  ? 726  LEU A CD2 1 
ATOM   5801  N  N   . VAL A 1 1156 ? 133.238 124.876 142.007 1.00 33.55  ? 727  VAL A N   1 
ATOM   5802  C  CA  . VAL A 1 1156 ? 134.326 123.895 142.029 1.00 27.30  ? 727  VAL A CA  1 
ATOM   5803  C  C   . VAL A 1 1156 ? 135.629 124.530 141.578 1.00 31.98  ? 727  VAL A C   1 
ATOM   5804  O  O   . VAL A 1 1156 ? 136.699 124.198 142.092 1.00 43.27  ? 727  VAL A O   1 
ATOM   5805  C  CB  . VAL A 1 1156 ? 133.995 122.675 141.163 1.00 29.30  ? 727  VAL A CB  1 
ATOM   5806  C  CG1 . VAL A 1 1156 ? 135.175 121.736 141.151 1.00 34.93  ? 727  VAL A CG1 1 
ATOM   5807  C  CG2 . VAL A 1 1156 ? 132.747 121.967 141.697 1.00 41.86  ? 727  VAL A CG2 1 
ATOM   5808  N  N   . GLU A 1 1157 ? 135.570 125.447 140.610 1.00 34.75  ? 728  GLU A N   1 
ATOM   5809  C  CA  . GLU A 1 1157 ? 136.783 126.144 140.176 1.00 31.51  ? 728  GLU A CA  1 
ATOM   5810  C  C   . GLU A 1 1157 ? 137.398 126.987 141.288 1.00 33.31  ? 728  GLU A C   1 
ATOM   5811  O  O   . GLU A 1 1157 ? 138.620 127.012 141.452 1.00 45.49  ? 728  GLU A O   1 
ATOM   5812  C  CB  . GLU A 1 1157 ? 136.479 127.006 138.969 1.00 34.19  ? 728  GLU A CB  1 
ATOM   5813  C  CG  . GLU A 1 1157 ? 137.573 127.973 138.661 1.00 50.44  ? 728  GLU A CG  1 
ATOM   5814  C  CD  . GLU A 1 1157 ? 137.244 128.827 137.448 1.00 72.20  ? 728  GLU A CD  1 
ATOM   5815  O  OE1 . GLU A 1 1157 ? 138.178 129.449 136.890 1.00 73.81  ? 728  GLU A OE1 1 
ATOM   5816  O  OE2 . GLU A 1 1157 ? 136.058 128.843 137.031 1.00 64.47  ? 728  GLU A OE2 1 
ATOM   5817  N  N   . ILE A 1 1158 ? 136.571 127.691 142.052 1.00 37.29  ? 729  ILE A N   1 
ATOM   5818  C  CA  . ILE A 1 1158 ? 137.064 128.461 143.196 1.00 33.70  ? 729  ILE A CA  1 
ATOM   5819  C  C   . ILE A 1 1158 ? 137.704 127.552 144.233 1.00 39.92  ? 729  ILE A C   1 
ATOM   5820  O  O   . ILE A 1 1158 ? 138.788 127.844 144.747 1.00 48.62  ? 729  ILE A O   1 
ATOM   5821  C  CB  . ILE A 1 1158 ? 135.912 129.261 143.822 1.00 42.13  ? 729  ILE A CB  1 
ATOM   5822  C  CG1 . ILE A 1 1158 ? 135.456 130.376 142.869 1.00 57.47  ? 729  ILE A CG1 1 
ATOM   5823  C  CG2 . ILE A 1 1158 ? 136.256 129.692 145.246 1.00 43.28  ? 729  ILE A CG2 1 
ATOM   5824  C  CD1 . ILE A 1 1158 ? 136.513 131.443 142.613 1.00 68.49  ? 729  ILE A CD1 1 
ATOM   5825  N  N   . LYS A 1 1159 ? 137.022 126.453 144.583 1.00 43.81  ? 730  LYS A N   1 
ATOM   5826  C  CA  . LYS A 1 1159 ? 137.513 125.552 145.632 1.00 41.94  ? 730  LYS A CA  1 
ATOM   5827  C  C   . LYS A 1 1159 ? 138.775 124.807 145.199 1.00 45.22  ? 730  LYS A C   1 
ATOM   5828  O  O   . LYS A 1 1159 ? 139.835 124.945 145.820 1.00 50.73  ? 730  LYS A O   1 
ATOM   5829  C  CB  . LYS A 1 1159 ? 136.429 124.550 146.010 1.00 37.55  ? 730  LYS A CB  1 
ATOM   5830  C  CG  . LYS A 1 1159 ? 135.236 125.163 146.678 1.00 46.35  ? 730  LYS A CG  1 
ATOM   5831  C  CD  . LYS A 1 1159 ? 134.511 124.124 147.519 1.00 54.76  ? 730  LYS A CD  1 
ATOM   5832  C  CE  . LYS A 1 1159 ? 134.091 122.936 146.660 1.00 53.72  ? 730  LYS A CE  1 
ATOM   5833  N  NZ  . LYS A 1 1159 ? 133.400 121.909 147.480 1.00 65.77  ? 730  LYS A NZ  1 
ATOM   5834  N  N   . THR A 1 1160 ? 138.672 123.982 144.156 1.00 30.15  ? 731  THR A N   1 
ATOM   5835  C  CA  . THR A 1 1160 ? 139.817 123.194 143.740 1.00 24.49  ? 731  THR A CA  1 
ATOM   5836  C  C   . THR A 1 1160 ? 140.931 124.098 143.270 1.00 29.97  ? 731  THR A C   1 
ATOM   5837  O  O   . THR A 1 1160 ? 142.057 124.029 143.769 1.00 42.83  ? 731  THR A O   1 
ATOM   5838  C  CB  . THR A 1 1160 ? 139.432 122.262 142.611 1.00 37.76  ? 731  THR A CB  1 
ATOM   5839  O  OG1 . THR A 1 1160 ? 139.013 123.045 141.486 1.00 42.61  ? 731  THR A OG1 1 
ATOM   5840  C  CG2 . THR A 1 1160 ? 138.269 121.392 143.043 1.00 39.81  ? 731  THR A CG2 1 
ATOM   5841  N  N   . GLY A 1 1161 ? 140.632 124.982 142.342 1.00 31.09  ? 732  GLY A N   1 
ATOM   5842  C  CA  . GLY A 1 1161 ? 141.613 125.930 141.904 1.00 38.07  ? 732  GLY A CA  1 
ATOM   5843  C  C   . GLY A 1 1161 ? 142.127 125.721 140.516 1.00 42.04  ? 732  GLY A C   1 
ATOM   5844  O  O   . GLY A 1 1161 ? 143.166 126.291 140.176 1.00 58.30  ? 732  GLY A O   1 
ATOM   5845  N  N   . PHE A 1 1162 ? 141.454 124.932 139.696 1.00 43.88  ? 733  PHE A N   1 
ATOM   5846  C  CA  . PHE A 1 1162 ? 141.862 124.767 138.308 1.00 53.48  ? 733  PHE A CA  1 
ATOM   5847  C  C   . PHE A 1 1162 ? 140.955 125.601 137.413 1.00 50.76  ? 733  PHE A C   1 
ATOM   5848  O  O   . PHE A 1 1162 ? 139.863 126.000 137.816 1.00 56.77  ? 733  PHE A O   1 
ATOM   5849  C  CB  . PHE A 1 1162 ? 141.820 123.289 137.903 1.00 53.43  ? 733  PHE A CB  1 
ATOM   5850  C  CG  . PHE A 1 1162 ? 142.649 122.405 138.787 1.00 41.52  ? 733  PHE A CG  1 
ATOM   5851  C  CD1 . PHE A 1 1162 ? 144.018 122.491 138.767 1.00 42.75  ? 733  PHE A CD1 1 
ATOM   5852  C  CD2 . PHE A 1 1162 ? 142.049 121.499 139.641 1.00 41.65  ? 733  PHE A CD2 1 
ATOM   5853  C  CE1 . PHE A 1 1162 ? 144.771 121.699 139.586 1.00 53.19  ? 733  PHE A CE1 1 
ATOM   5854  C  CE2 . PHE A 1 1162 ? 142.789 120.704 140.458 1.00 44.90  ? 733  PHE A CE2 1 
ATOM   5855  C  CZ  . PHE A 1 1162 ? 144.153 120.799 140.434 1.00 53.87  ? 733  PHE A CZ  1 
ATOM   5856  N  N   . LYS A 1 1163 ? 141.407 125.868 136.187 1.00 48.66  ? 734  LYS A N   1 
ATOM   5857  C  CA  . LYS A 1 1163 ? 140.617 126.709 135.285 1.00 50.37  ? 734  LYS A CA  1 
ATOM   5858  C  C   . LYS A 1 1163 ? 139.535 125.878 134.600 1.00 50.98  ? 734  LYS A C   1 
ATOM   5859  O  O   . LYS A 1 1163 ? 139.833 125.071 133.719 1.00 55.28  ? 734  LYS A O   1 
ATOM   5860  C  CB  . LYS A 1 1163 ? 141.516 127.353 134.241 1.00 65.20  ? 734  LYS A CB  1 
ATOM   5861  C  CG  . LYS A 1 1163 ? 140.795 128.359 133.360 1.00 81.95  ? 734  LYS A CG  1 
ATOM   5862  C  CD  . LYS A 1 1163 ? 140.311 129.539 134.166 1.00 87.46  ? 734  LYS A CD  1 
ATOM   5863  C  CE  . LYS A 1 1163 ? 141.482 130.178 134.895 1.00 94.34  ? 734  LYS A CE  1 
ATOM   5864  N  NZ  . LYS A 1 1163 ? 141.091 131.410 135.629 1.00 96.18  ? 734  LYS A NZ  1 
ATOM   5865  N  N   . LEU A 1 1164 ? 138.280 126.075 134.955 1.00 42.48  ? 735  LEU A N   1 
ATOM   5866  C  CA  . LEU A 1 1164 ? 137.236 125.231 134.406 1.00 35.04  ? 735  LEU A CA  1 
ATOM   5867  C  C   . LEU A 1 1164 ? 136.547 125.953 133.263 1.00 50.09  ? 735  LEU A C   1 
ATOM   5868  O  O   . LEU A 1 1164 ? 136.224 127.138 133.378 1.00 64.74  ? 735  LEU A O   1 
ATOM   5869  C  CB  . LEU A 1 1164 ? 136.215 124.851 135.467 1.00 41.27  ? 735  LEU A CB  1 
ATOM   5870  C  CG  . LEU A 1 1164 ? 136.729 124.018 136.630 1.00 43.90  ? 735  LEU A CG  1 
ATOM   5871  C  CD1 . LEU A 1 1164 ? 135.553 123.405 137.379 1.00 41.09  ? 735  LEU A CD1 1 
ATOM   5872  C  CD2 . LEU A 1 1164 ? 137.680 122.961 136.149 1.00 42.48  ? 735  LEU A CD2 1 
ATOM   5873  N  N   . ARG A 1 1165 ? 136.332 125.241 132.165 1.00 45.41  ? 736  ARG A N   1 
ATOM   5874  C  CA  . ARG A 1 1165 ? 135.527 125.716 131.047 1.00 41.40  ? 736  ARG A CA  1 
ATOM   5875  C  C   . ARG A 1 1165 ? 134.299 124.838 130.917 1.00 45.76  ? 736  ARG A C   1 
ATOM   5876  O  O   . ARG A 1 1165 ? 134.421 123.638 130.669 1.00 53.03  ? 736  ARG A O   1 
ATOM   5877  C  CB  . ARG A 1 1165 ? 136.308 125.641 129.754 1.00 57.63  ? 736  ARG A CB  1 
ATOM   5878  C  CG  . ARG A 1 1165 ? 137.197 126.765 129.535 1.00 71.43  ? 736  ARG A CG  1 
ATOM   5879  C  CD  . ARG A 1 1165 ? 136.370 127.950 129.195 1.00 79.84  ? 736  ARG A CD  1 
ATOM   5880  N  NE  . ARG A 1 1165 ? 137.091 128.757 128.230 1.00 98.43  ? 736  ARG A NE  1 
ATOM   5881  C  CZ  . ARG A 1 1165 ? 138.012 129.653 128.561 1.00 110.30 ? 736  ARG A CZ  1 
ATOM   5882  N  NH1 . ARG A 1 1165 ? 138.356 129.817 129.836 1.00 102.76 ? 736  ARG A NH1 1 
ATOM   5883  N  NH2 . ARG A 1 1165 ? 138.621 130.351 127.612 1.00 111.60 ? 736  ARG A NH2 1 
ATOM   5884  N  N   . SER A 1 1166 ? 133.127 125.425 131.034 1.00 53.06  ? 737  SER A N   1 
ATOM   5885  C  CA  . SER A 1 1166 ? 131.894 124.656 130.993 1.00 55.38  ? 737  SER A CA  1 
ATOM   5886  C  C   . SER A 1 1166 ? 131.201 124.893 129.661 1.00 65.60  ? 737  SER A C   1 
ATOM   5887  O  O   . SER A 1 1166 ? 131.030 126.043 129.238 1.00 76.83  ? 737  SER A O   1 
ATOM   5888  C  CB  . SER A 1 1166 ? 130.973 125.034 132.152 1.00 61.34  ? 737  SER A CB  1 
ATOM   5889  O  OG  . SER A 1 1166 ? 129.815 124.221 132.149 1.00 60.27  ? 737  SER A OG  1 
ATOM   5890  N  N   . ALA A 1 1167 ? 130.810 123.809 129.001 1.00 57.62  ? 738  ALA A N   1 
ATOM   5891  C  CA  . ALA A 1 1167 ? 130.156 123.896 127.705 1.00 56.49  ? 738  ALA A CA  1 
ATOM   5892  C  C   . ALA A 1 1167 ? 129.067 122.838 127.621 1.00 57.55  ? 738  ALA A C   1 
ATOM   5893  O  O   . ALA A 1 1167 ? 129.334 121.659 127.868 1.00 62.02  ? 738  ALA A O   1 
ATOM   5894  C  CB  . ALA A 1 1167 ? 131.174 123.720 126.577 1.00 61.62  ? 738  ALA A CB  1 
ATOM   5895  N  N   . VAL A 1 1168 ? 127.848 123.254 127.268 1.00 58.28  ? 739  VAL A N   1 
ATOM   5896  C  CA  . VAL A 1 1168 ? 126.694 122.364 127.189 1.00 45.69  ? 739  VAL A CA  1 
ATOM   5897  C  C   . VAL A 1 1168 ? 126.173 122.356 125.767 1.00 40.92  ? 739  VAL A C   1 
ATOM   5898  O  O   . VAL A 1 1168 ? 126.154 123.390 125.095 1.00 56.42  ? 739  VAL A O   1 
ATOM   5899  C  CB  . VAL A 1 1168 ? 125.571 122.772 128.163 1.00 60.49  ? 739  VAL A CB  1 
ATOM   5900  C  CG1 . VAL A 1 1168 ? 124.903 124.069 127.709 1.00 61.49  ? 739  VAL A CG1 1 
ATOM   5901  C  CG2 . VAL A 1 1168 ? 124.534 121.645 128.267 1.00 65.17  ? 739  VAL A CG2 1 
ATOM   5902  N  N   . MET A 1 1169 ? 125.774 121.182 125.298 1.00 46.92  ? 740  MET A N   1 
ATOM   5903  C  CA  . MET A 1 1169 ? 125.167 121.084 123.981 1.00 51.19  ? 740  MET A CA  1 
ATOM   5904  C  C   . MET A 1 1169 ? 124.233 119.890 123.962 1.00 48.53  ? 740  MET A C   1 
ATOM   5905  O  O   . MET A 1 1169 ? 124.669 118.759 124.177 1.00 51.06  ? 740  MET A O   1 
ATOM   5906  C  CB  . MET A 1 1169 ? 126.219 120.968 122.881 1.00 56.53  ? 740  MET A CB  1 
ATOM   5907  C  CG  . MET A 1 1169 ? 125.607 120.844 121.481 1.00 75.61  ? 740  MET A CG  1 
ATOM   5908  S  SD  . MET A 1 1169 ? 124.449 122.185 121.042 1.00 114.45 ? 740  MET A SD  1 
ATOM   5909  C  CE  . MET A 1 1169 ? 125.465 123.673 121.157 1.00 89.26  ? 740  MET A CE  1 
ATOM   5910  N  N   . GLY A 1 1170 ? 122.961 120.142 123.673 1.00 45.98  ? 741  GLY A N   1 
ATOM   5911  C  CA  . GLY A 1 1170 ? 121.976 119.096 123.767 1.00 45.31  ? 741  GLY A CA  1 
ATOM   5912  C  C   . GLY A 1 1170 ? 121.838 118.684 125.210 1.00 49.83  ? 741  GLY A C   1 
ATOM   5913  O  O   . GLY A 1 1170 ? 121.525 119.513 126.068 1.00 57.51  ? 741  GLY A O   1 
ATOM   5914  N  N   . ASP A 1 1171 ? 122.085 117.411 125.496 1.00 54.68  ? 742  ASP A N   1 
ATOM   5915  C  CA  . ASP A 1 1171 ? 121.911 116.905 126.849 1.00 58.65  ? 742  ASP A CA  1 
ATOM   5916  C  C   . ASP A 1 1171 ? 123.196 116.915 127.664 1.00 66.36  ? 742  ASP A C   1 
ATOM   5917  O  O   . ASP A 1 1171 ? 123.132 117.010 128.893 1.00 74.35  ? 742  ASP A O   1 
ATOM   5918  C  CB  . ASP A 1 1171 ? 121.357 115.478 126.823 1.00 71.27  ? 742  ASP A CB  1 
ATOM   5919  C  CG  . ASP A 1 1171 ? 120.031 115.377 126.075 1.00 91.98  ? 742  ASP A CG  1 
ATOM   5920  O  OD1 . ASP A 1 1171 ? 120.001 114.759 124.983 1.00 91.50  ? 742  ASP A OD1 1 
ATOM   5921  O  OD2 . ASP A 1 1171 ? 119.025 115.945 126.559 1.00 92.60  ? 742  ASP A OD2 1 
ATOM   5922  N  N   . ASN A 1 1172 ? 124.361 116.826 127.030 1.00 56.22  ? 743  ASN A N   1 
ATOM   5923  C  CA  . ASN A 1 1172 ? 125.605 116.653 127.766 1.00 50.49  ? 743  ASN A CA  1 
ATOM   5924  C  C   . ASN A 1 1172 ? 126.234 117.981 128.149 1.00 52.30  ? 743  ASN A C   1 
ATOM   5925  O  O   . ASN A 1 1172 ? 126.117 118.977 127.434 1.00 60.64  ? 743  ASN A O   1 
ATOM   5926  C  CB  . ASN A 1 1172 ? 126.611 115.851 126.948 1.00 57.53  ? 743  ASN A CB  1 
ATOM   5927  C  CG  . ASN A 1 1172 ? 126.027 114.574 126.413 1.00 64.36  ? 743  ASN A CG  1 
ATOM   5928  O  OD1 . ASN A 1 1172 ? 125.031 114.063 126.935 1.00 67.51  ? 743  ASN A OD1 1 
ATOM   5929  N  ND2 . ASN A 1 1172 ? 126.664 114.024 125.383 1.00 69.70  ? 743  ASN A ND2 1 
ATOM   5930  N  N   . GLN A 1 1173 ? 126.914 117.983 129.292 1.00 53.18  ? 744  GLN A N   1 
ATOM   5931  C  CA  . GLN A 1 1173 ? 127.730 119.111 129.715 1.00 46.43  ? 744  GLN A CA  1 
ATOM   5932  C  C   . GLN A 1 1173 ? 129.159 118.649 129.898 1.00 40.12  ? 744  GLN A C   1 
ATOM   5933  O  O   . GLN A 1 1173 ? 129.433 117.756 130.704 1.00 50.72  ? 744  GLN A O   1 
ATOM   5934  C  CB  . GLN A 1 1173 ? 127.216 119.734 131.005 1.00 53.81  ? 744  GLN A CB  1 
ATOM   5935  C  CG  . GLN A 1 1173 ? 128.067 120.905 131.429 1.00 56.22  ? 744  GLN A CG  1 
ATOM   5936  C  CD  . GLN A 1 1173 ? 127.569 121.554 132.701 1.00 62.45  ? 744  GLN A CD  1 
ATOM   5937  O  OE1 . GLN A 1 1173 ? 126.649 121.049 133.345 1.00 70.25  ? 744  GLN A OE1 1 
ATOM   5938  N  NE2 . GLN A 1 1173 ? 128.174 122.681 133.075 1.00 56.58  ? 744  GLN A NE2 1 
ATOM   5939  N  N   . CYS A 1 1174 ? 130.060 119.267 129.168 1.00 39.67  ? 745  CYS A N   1 
ATOM   5940  C  CA  . CYS A 1 1174 ? 131.468 118.927 129.199 1.00 38.10  ? 745  CYS A CA  1 
ATOM   5941  C  C   . CYS A 1 1174 ? 132.212 119.974 130.002 1.00 43.16  ? 745  CYS A C   1 
ATOM   5942  O  O   . CYS A 1 1174 ? 132.145 121.162 129.676 1.00 55.39  ? 745  CYS A O   1 
ATOM   5943  C  CB  . CYS A 1 1174 ? 132.009 118.889 127.778 1.00 49.33  ? 745  CYS A CB  1 
ATOM   5944  S  SG  . CYS A 1 1174 ? 133.744 118.496 127.603 1.00 63.35  ? 745  CYS A SG  1 
ATOM   5945  N  N   . ILE A 1 1175 ? 132.931 119.553 131.028 1.00 29.12  ? 746  ILE A N   1 
ATOM   5946  C  CA  . ILE A 1 1175 ? 133.670 120.494 131.846 1.00 25.05  ? 746  ILE A CA  1 
ATOM   5947  C  C   . ILE A 1 1175 ? 135.142 120.254 131.590 1.00 29.98  ? 746  ILE A C   1 
ATOM   5948  O  O   . ILE A 1 1175 ? 135.704 119.266 132.073 1.00 41.61  ? 746  ILE A O   1 
ATOM   5949  C  CB  . ILE A 1 1175 ? 133.354 120.336 133.331 1.00 30.20  ? 746  ILE A CB  1 
ATOM   5950  C  CG1 . ILE A 1 1175 ? 131.871 120.477 133.616 1.00 39.79  ? 746  ILE A CG1 1 
ATOM   5951  C  CG2 . ILE A 1 1175 ? 134.066 121.392 134.125 1.00 45.56  ? 746  ILE A CG2 1 
ATOM   5952  C  CD1 . ILE A 1 1175 ? 131.175 119.142 133.739 1.00 45.73  ? 746  ILE A CD1 1 
ATOM   5953  N  N   . THR A 1 1176 ? 135.782 121.142 130.847 1.00 29.49  ? 747  THR A N   1 
ATOM   5954  C  CA  . THR A 1 1176 ? 137.200 121.000 130.545 1.00 32.13  ? 747  THR A CA  1 
ATOM   5955  C  C   . THR A 1 1176 ? 138.031 121.629 131.654 1.00 34.11  ? 747  THR A C   1 
ATOM   5956  O  O   . THR A 1 1176 ? 137.938 122.835 131.896 1.00 46.56  ? 747  THR A O   1 
ATOM   5957  C  CB  . THR A 1 1176 ? 137.543 121.651 129.212 1.00 42.12  ? 747  THR A CB  1 
ATOM   5958  O  OG1 . THR A 1 1176 ? 136.730 121.078 128.182 1.00 47.29  ? 747  THR A OG1 1 
ATOM   5959  C  CG2 . THR A 1 1176 ? 139.017 121.417 128.885 1.00 43.86  ? 747  THR A CG2 1 
ATOM   5960  N  N   . VAL A 1 1177 ? 138.830 120.826 132.326 1.00 26.56  ? 748  VAL A N   1 
ATOM   5961  C  CA  . VAL A 1 1177 ? 139.701 121.304 133.373 1.00 26.56  ? 748  VAL A CA  1 
ATOM   5962  C  C   . VAL A 1 1177 ? 141.024 121.624 132.766 1.00 26.56  ? 748  VAL A C   1 
ATOM   5963  O  O   . VAL A 1 1177 ? 141.689 120.733 132.231 1.00 44.34  ? 748  VAL A O   1 
ATOM   5964  C  CB  . VAL A 1 1177 ? 139.909 120.242 134.429 1.00 29.50  ? 748  VAL A CB  1 
ATOM   5965  C  CG1 . VAL A 1 1177 ? 140.717 120.856 135.505 1.00 42.16  ? 748  VAL A CG1 1 
ATOM   5966  C  CG2 . VAL A 1 1177 ? 138.574 119.694 134.878 1.00 41.60  ? 748  VAL A CG2 1 
ATOM   5967  N  N   . LEU A 1 1178 ? 141.429 122.863 132.861 1.00 32.26  ? 749  LEU A N   1 
ATOM   5968  C  CA  . LEU A 1 1178 ? 142.739 123.261 132.397 1.00 43.64  ? 749  LEU A CA  1 
ATOM   5969  C  C   . LEU A 1 1178 ? 143.647 123.357 133.605 1.00 42.56  ? 749  LEU A C   1 
ATOM   5970  O  O   . LEU A 1 1178 ? 143.305 124.017 134.600 1.00 48.78  ? 749  LEU A O   1 
ATOM   5971  C  CB  . LEU A 1 1178 ? 142.696 124.584 131.625 1.00 47.67  ? 749  LEU A CB  1 
ATOM   5972  C  CG  . LEU A 1 1178 ? 142.100 124.604 130.213 1.00 46.92  ? 749  LEU A CG  1 
ATOM   5973  C  CD1 . LEU A 1 1178 ? 140.590 124.516 130.232 1.00 52.30  ? 749  LEU A CD1 1 
ATOM   5974  C  CD2 . LEU A 1 1178 ? 142.529 125.878 129.505 1.00 61.65  ? 749  LEU A CD2 1 
ATOM   5975  N  N   . SER A 1 1179 ? 144.776 122.674 133.522 1.00 35.63  ? 750  SER A N   1 
ATOM   5976  C  CA  . SER A 1 1179 ? 145.760 122.661 134.575 1.00 35.63  ? 750  SER A CA  1 
ATOM   5977  C  C   . SER A 1 1179 ? 147.082 123.102 133.991 1.00 46.66  ? 750  SER A C   1 
ATOM   5978  O  O   . SER A 1 1179 ? 147.446 122.677 132.891 1.00 55.60  ? 750  SER A O   1 
ATOM   5979  C  CB  . SER A 1 1179 ? 145.890 121.292 135.135 1.00 36.75  ? 750  SER A CB  1 
ATOM   5980  O  OG  . SER A 1 1179 ? 146.093 120.396 134.075 1.00 44.14  ? 750  SER A OG  1 
ATOM   5981  N  N   . VAL A 1 1180 ? 147.796 123.956 134.723 1.00 49.33  ? 751  VAL A N   1 
ATOM   5982  C  CA  . VAL A 1 1180 ? 149.088 124.475 134.282 1.00 50.16  ? 751  VAL A CA  1 
ATOM   5983  C  C   . VAL A 1 1180 ? 150.205 123.649 134.887 1.00 54.55  ? 751  VAL A C   1 
ATOM   5984  O  O   . VAL A 1 1180 ? 150.162 123.298 136.070 1.00 61.70  ? 751  VAL A O   1 
ATOM   5985  C  CB  . VAL A 1 1180 ? 149.254 125.956 134.648 1.00 62.15  ? 751  VAL A CB  1 
ATOM   5986  C  CG1 . VAL A 1 1180 ? 148.283 126.801 133.854 1.00 76.27  ? 751  VAL A CG1 1 
ATOM   5987  C  CG2 . VAL A 1 1180 ? 149.035 126.159 136.142 1.00 65.98  ? 751  VAL A CG2 1 
ATOM   5988  N  N   . PHE A 1 1181 ? 151.207 123.346 134.079 1.00 57.14  ? 752  PHE A N   1 
ATOM   5989  C  CA  . PHE A 1 1181 ? 152.393 122.638 134.504 1.00 62.97  ? 752  PHE A CA  1 
ATOM   5990  C  C   . PHE A 1 1181 ? 153.635 123.459 134.218 1.00 78.04  ? 752  PHE A C   1 
ATOM   5991  O  O   . PHE A 1 1181 ? 153.630 124.315 133.324 1.00 87.38  ? 752  PHE A O   1 
ATOM   5992  C  CB  . PHE A 1 1181 ? 152.511 121.296 133.785 1.00 65.59  ? 752  PHE A CB  1 
ATOM   5993  C  CG  . PHE A 1 1181 ? 151.320 120.448 133.937 1.00 62.33  ? 752  PHE A CG  1 
ATOM   5994  C  CD1 . PHE A 1 1181 ? 150.756 120.274 135.183 1.00 69.92  ? 752  PHE A CD1 1 
ATOM   5995  C  CD2 . PHE A 1 1181 ? 150.715 119.887 132.841 1.00 64.25  ? 752  PHE A CD2 1 
ATOM   5996  C  CE1 . PHE A 1 1181 ? 149.636 119.501 135.351 1.00 74.06  ? 752  PHE A CE1 1 
ATOM   5997  C  CE2 . PHE A 1 1181 ? 149.586 119.121 132.987 1.00 68.05  ? 752  PHE A CE2 1 
ATOM   5998  C  CZ  . PHE A 1 1181 ? 149.040 118.927 134.249 1.00 73.88  ? 752  PHE A CZ  1 
ATOM   5999  N  N   . PRO A 1 1182 ? 154.714 123.223 134.960 1.00 78.95  ? 753  PRO A N   1 
ATOM   6000  C  CA  . PRO A 1 1182 ? 156.022 123.746 134.547 1.00 94.72  ? 753  PRO A CA  1 
ATOM   6001  C  C   . PRO A 1 1182 ? 156.448 123.162 133.201 1.00 102.09 ? 753  PRO A C   1 
ATOM   6002  O  O   . PRO A 1 1182 ? 156.104 122.028 132.858 1.00 103.17 ? 753  PRO A O   1 
ATOM   6003  C  CB  . PRO A 1 1182 ? 156.956 123.302 135.680 1.00 98.05  ? 753  PRO A CB  1 
ATOM   6004  C  CG  . PRO A 1 1182 ? 156.044 123.089 136.860 1.00 88.97  ? 753  PRO A CG  1 
ATOM   6005  C  CD  . PRO A 1 1182 ? 154.757 122.581 136.284 1.00 74.76  ? 753  PRO A CD  1 
ATOM   6006  N  N   . LEU A 1 1183 ? 157.195 123.964 132.427 1.00 103.60 ? 754  LEU A N   1 
ATOM   6007  C  CA  . LEU A 1 1183 ? 157.584 123.558 131.072 1.00 109.91 ? 754  LEU A CA  1 
ATOM   6008  C  C   . LEU A 1 1183 ? 158.487 122.326 131.084 1.00 113.41 ? 754  LEU A C   1 
ATOM   6009  O  O   . LEU A 1 1183 ? 158.354 121.439 130.229 1.00 111.31 ? 754  LEU A O   1 
ATOM   6010  C  CB  . LEU A 1 1183 ? 158.273 124.718 130.345 1.00 114.46 ? 754  LEU A CB  1 
ATOM   6011  C  CG  . LEU A 1 1183 ? 158.696 124.467 128.887 1.00 126.12 ? 754  LEU A CG  1 
ATOM   6012  C  CD1 . LEU A 1 1183 ? 157.509 124.033 128.008 1.00 119.61 ? 754  LEU A CD1 1 
ATOM   6013  C  CD2 . LEU A 1 1183 ? 159.412 125.686 128.291 1.00 118.81 ? 754  LEU A CD2 1 
ATOM   6014  N  N   . GLU A 1 1184 ? 159.420 122.259 132.034 1.00 111.88 ? 755  GLU A N   1 
ATOM   6015  C  CA  . GLU A 1 1184 ? 160.343 121.130 132.148 1.00 108.78 ? 755  GLU A CA  1 
ATOM   6016  C  C   . GLU A 1 1184 ? 159.658 119.963 132.868 1.00 116.59 ? 755  GLU A C   1 
ATOM   6017  O  O   . GLU A 1 1184 ? 159.989 119.597 133.999 1.00 113.98 ? 755  GLU A O   1 
ATOM   6018  C  CB  . GLU A 1 1184 ? 161.611 121.571 132.864 1.00 115.88 ? 755  GLU A CB  1 
ATOM   6019  C  CG  . GLU A 1 1184 ? 161.350 122.501 134.054 1.00 120.41 ? 755  GLU A CG  1 
ATOM   6020  C  CD  . GLU A 1 1184 ? 162.629 122.953 134.754 1.00 121.38 ? 755  GLU A CD  1 
ATOM   6021  O  OE1 . GLU A 1 1184 ? 162.584 123.181 135.984 1.00 115.97 ? 755  GLU A OE1 1 
ATOM   6022  O  OE2 . GLU A 1 1184 ? 163.677 123.076 134.078 1.00 116.42 ? 755  GLU A OE2 1 
ATOM   6023  N  N   . THR A 1 1185 ? 158.671 119.376 132.177 1.00 119.29 ? 756  THR A N   1 
ATOM   6024  C  CA  . THR A 1 1185 ? 157.986 118.167 132.632 1.00 119.65 ? 756  THR A CA  1 
ATOM   6025  C  C   . THR A 1 1185 ? 157.807 117.216 131.451 1.00 117.13 ? 756  THR A C   1 
ATOM   6026  O  O   . THR A 1 1185 ? 157.759 117.640 130.291 1.00 111.52 ? 756  THR A O   1 
ATOM   6027  C  CB  . THR A 1 1185 ? 156.611 118.463 133.285 1.00 112.57 ? 756  THR A CB  1 
ATOM   6028  O  OG1 . THR A 1 1185 ? 156.112 117.277 133.922 1.00 105.62 ? 756  THR A OG1 1 
ATOM   6029  C  CG2 . THR A 1 1185 ? 155.589 118.932 132.246 1.00 108.49 ? 756  THR A CG2 1 
ATOM   6030  N  N   . ASP A 1 1186 ? 157.719 115.921 131.760 1.00 117.61 ? 757  ASP A N   1 
ATOM   6031  C  CA  . ASP A 1 1186 ? 157.581 114.896 130.728 1.00 117.37 ? 757  ASP A CA  1 
ATOM   6032  C  C   . ASP A 1 1186 ? 156.194 114.993 130.094 1.00 107.73 ? 757  ASP A C   1 
ATOM   6033  O  O   . ASP A 1 1186 ? 155.188 115.119 130.799 1.00 106.10 ? 757  ASP A O   1 
ATOM   6034  C  CB  . ASP A 1 1186 ? 157.814 113.502 131.341 1.00 121.03 ? 757  ASP A CB  1 
ATOM   6035  C  CG  . ASP A 1 1186 ? 158.063 112.401 130.292 1.00 116.78 ? 757  ASP A CG  1 
ATOM   6036  O  OD1 . ASP A 1 1186 ? 158.108 112.707 129.080 1.00 116.90 ? 757  ASP A OD1 1 
ATOM   6037  O  OD2 . ASP A 1 1186 ? 158.207 111.221 130.691 1.00 110.87 ? 757  ASP A OD2 1 
ATOM   6038  N  N   . ALA A 1 1187 ? 156.142 114.944 128.758 1.00 105.21 ? 758  ALA A N   1 
ATOM   6039  C  CA  . ALA A 1 1187 ? 154.859 115.043 128.061 1.00 106.90 ? 758  ALA A CA  1 
ATOM   6040  C  C   . ALA A 1 1187 ? 153.942 113.870 128.404 1.00 98.77  ? 758  ALA A C   1 
ATOM   6041  O  O   . ALA A 1 1187 ? 152.722 114.039 128.522 1.00 96.35  ? 758  ALA A O   1 
ATOM   6042  C  CB  . ALA A 1 1187 ? 155.085 115.132 126.549 1.00 105.14 ? 758  ALA A CB  1 
ATOM   6043  N  N   . ASP A 1 1188 ? 154.502 112.669 128.538 1.00 102.69 ? 759  ASP A N   1 
ATOM   6044  C  CA  . ASP A 1 1188 ? 153.696 111.539 128.987 1.00 104.36 ? 759  ASP A CA  1 
ATOM   6045  C  C   . ASP A 1 1188 ? 153.231 111.739 130.422 1.00 87.99  ? 759  ASP A C   1 
ATOM   6046  O  O   . ASP A 1 1188 ? 152.091 111.404 130.761 1.00 87.72  ? 759  ASP A O   1 
ATOM   6047  C  CB  . ASP A 1 1188 ? 154.485 110.228 128.853 1.00 120.20 ? 759  ASP A CB  1 
ATOM   6048  C  CG  . ASP A 1 1188 ? 154.873 109.907 127.407 1.00 119.61 ? 759  ASP A CG  1 
ATOM   6049  O  OD1 . ASP A 1 1188 ? 154.005 110.017 126.510 1.00 110.96 ? 759  ASP A OD1 1 
ATOM   6050  O  OD2 . ASP A 1 1188 ? 156.049 109.538 127.175 1.00 118.33 ? 759  ASP A OD2 1 
ATOM   6051  N  N   . GLU A 1 1189 ? 154.104 112.270 131.282 1.00 88.08  ? 760  GLU A N   1 
ATOM   6052  C  CA  . GLU A 1 1189 ? 153.727 112.477 132.677 1.00 92.33  ? 760  GLU A CA  1 
ATOM   6053  C  C   . GLU A 1 1189 ? 152.681 113.579 132.813 1.00 93.97  ? 760  GLU A C   1 
ATOM   6054  O  O   . GLU A 1 1189 ? 151.728 113.443 133.594 1.00 90.32  ? 760  GLU A O   1 
ATOM   6055  C  CB  . GLU A 1 1189 ? 154.965 112.800 133.520 1.00 105.11 ? 760  GLU A CB  1 
ATOM   6056  C  CG  . GLU A 1 1189 ? 154.684 113.364 134.933 1.00 109.85 ? 760  GLU A CG  1 
ATOM   6057  C  CD  . GLU A 1 1189 ? 153.776 112.475 135.784 1.00 109.54 ? 760  GLU A CD  1 
ATOM   6058  O  OE1 . GLU A 1 1189 ? 152.714 112.967 136.239 1.00 99.55  ? 760  GLU A OE1 1 
ATOM   6059  O  OE2 . GLU A 1 1189 ? 154.124 111.292 136.003 1.00 107.01 ? 760  GLU A OE2 1 
ATOM   6060  N  N   . GLN A 1 1190 ? 152.830 114.677 132.062 1.00 95.15  ? 761  GLN A N   1 
ATOM   6061  C  CA  . GLN A 1 1190 ? 151.888 115.784 132.211 1.00 86.85  ? 761  GLN A CA  1 
ATOM   6062  C  C   . GLN A 1 1190 ? 150.490 115.392 131.751 1.00 73.05  ? 761  GLN A C   1 
ATOM   6063  O  O   . GLN A 1 1190 ? 149.506 115.838 132.340 1.00 73.77  ? 761  GLN A O   1 
ATOM   6064  C  CB  . GLN A 1 1190 ? 152.379 117.031 131.460 1.00 85.44  ? 761  GLN A CB  1 
ATOM   6065  C  CG  . GLN A 1 1190 ? 152.180 117.004 129.947 1.00 89.63  ? 761  GLN A CG  1 
ATOM   6066  C  CD  . GLN A 1 1190 ? 152.493 118.336 129.297 1.00 95.72  ? 761  GLN A CD  1 
ATOM   6067  O  OE1 . GLN A 1 1190 ? 153.000 119.251 129.948 1.00 91.82  ? 761  GLN A OE1 1 
ATOM   6068  N  NE2 . GLN A 1 1190 ? 152.186 118.457 128.007 1.00 97.57  ? 761  GLN A NE2 1 
ATOM   6069  N  N   . GLU A 1 1191 ? 150.373 114.575 130.709 1.00 71.06  ? 762  GLU A N   1 
ATOM   6070  C  CA  . GLU A 1 1191 ? 149.047 114.141 130.310 1.00 64.65  ? 762  GLU A CA  1 
ATOM   6071  C  C   . GLU A 1 1191 ? 148.402 113.334 131.410 1.00 54.60  ? 762  GLU A C   1 
ATOM   6072  O  O   . GLU A 1 1191 ? 147.220 113.521 131.718 1.00 68.05  ? 762  GLU A O   1 
ATOM   6073  C  CB  . GLU A 1 1191 ? 149.108 113.308 129.041 1.00 76.98  ? 762  GLU A CB  1 
ATOM   6074  C  CG  . GLU A 1 1191 ? 147.724 112.947 128.514 1.00 79.04  ? 762  GLU A CG  1 
ATOM   6075  C  CD  . GLU A 1 1191 ? 147.215 111.620 129.077 1.00 83.70  ? 762  GLU A CD  1 
ATOM   6076  O  OE1 . GLU A 1 1191 ? 147.995 110.935 129.781 1.00 81.43  ? 762  GLU A OE1 1 
ATOM   6077  O  OE2 . GLU A 1 1191 ? 146.043 111.259 128.804 1.00 78.06  ? 762  GLU A OE2 1 
ATOM   6078  N  N   . GLN A 1 1192 ? 149.147 112.412 131.986 1.00 50.23  ? 763  GLN A N   1 
ATOM   6079  C  CA  . GLN A 1 1192 ? 148.603 111.665 133.095 1.00 50.36  ? 763  GLN A CA  1 
ATOM   6080  C  C   . GLN A 1 1192 ? 148.170 112.600 134.211 1.00 68.21  ? 763  GLN A C   1 
ATOM   6081  O  O   . GLN A 1 1192 ? 147.074 112.446 134.763 1.00 72.56  ? 763  GLN A O   1 
ATOM   6082  C  CB  . GLN A 1 1192 ? 149.629 110.662 133.591 1.00 64.15  ? 763  GLN A CB  1 
ATOM   6083  C  CG  . GLN A 1 1192 ? 149.150 109.900 134.765 1.00 63.55  ? 763  GLN A CG  1 
ATOM   6084  C  CD  . GLN A 1 1192 ? 148.143 108.869 134.370 1.00 77.89  ? 763  GLN A CD  1 
ATOM   6085  O  OE1 . GLN A 1 1192 ? 148.489 107.809 133.846 1.00 79.25  ? 763  GLN A OE1 1 
ATOM   6086  N  NE2 . GLN A 1 1192 ? 146.869 109.183 134.592 1.00 74.20  ? 763  GLN A NE2 1 
ATOM   6087  N  N   . SER A 1 1193 ? 148.996 113.599 134.546 1.00 64.87  ? 764  SER A N   1 
ATOM   6088  C  CA  . SER A 1 1193 ? 148.644 114.463 135.673 1.00 59.18  ? 764  SER A CA  1 
ATOM   6089  C  C   . SER A 1 1193 ? 147.435 115.325 135.344 1.00 47.00  ? 764  SER A C   1 
ATOM   6090  O  O   . SER A 1 1193 ? 146.620 115.616 136.221 1.00 54.77  ? 764  SER A O   1 
ATOM   6091  C  CB  . SER A 1 1193 ? 149.833 115.330 136.096 1.00 68.10  ? 764  SER A CB  1 
ATOM   6092  O  OG  . SER A 1 1193 ? 150.260 116.193 135.059 1.00 72.32  ? 764  SER A OG  1 
ATOM   6093  N  N   . ALA A 1 1194 ? 147.309 115.750 134.093 1.00 47.87  ? 765  ALA A N   1 
ATOM   6094  C  CA  . ALA A 1 1194 ? 146.151 116.528 133.688 1.00 45.41  ? 765  ALA A CA  1 
ATOM   6095  C  C   . ALA A 1 1194 ? 144.893 115.704 133.791 1.00 44.02  ? 765  ALA A C   1 
ATOM   6096  O  O   . ALA A 1 1194 ? 143.863 116.188 134.270 1.00 54.03  ? 765  ALA A O   1 
ATOM   6097  C  CB  . ALA A 1 1194 ? 146.314 117.030 132.262 1.00 54.27  ? 765  ALA A CB  1 
ATOM   6098  N  N   . GLU A 1 1195 ? 144.947 114.462 133.339 1.00 40.32  ? 766  GLU A N   1 
ATOM   6099  C  CA  . GLU A 1 1195 ? 143.788 113.609 133.509 1.00 38.81  ? 766  GLU A CA  1 
ATOM   6100  C  C   . GLU A 1 1195 ? 143.476 113.417 134.978 1.00 40.29  ? 766  GLU A C   1 
ATOM   6101  O  O   . GLU A 1 1195 ? 142.305 113.367 135.367 1.00 50.83  ? 766  GLU A O   1 
ATOM   6102  C  CB  . GLU A 1 1195 ? 144.020 112.273 132.839 1.00 53.90  ? 766  GLU A CB  1 
ATOM   6103  C  CG  . GLU A 1 1195 ? 142.813 111.366 132.879 1.00 63.03  ? 766  GLU A CG  1 
ATOM   6104  C  CD  . GLU A 1 1195 ? 143.010 110.110 132.034 1.00 77.07  ? 766  GLU A CD  1 
ATOM   6105  O  OE1 . GLU A 1 1195 ? 142.948 110.201 130.784 1.00 72.52  ? 766  GLU A OE1 1 
ATOM   6106  O  OE2 . GLU A 1 1195 ? 143.261 109.033 132.622 1.00 72.57  ? 766  GLU A OE2 1 
ATOM   6107  N  N   . ASP A 1 1196 ? 144.502 113.314 135.817 1.00 38.08  ? 767  ASP A N   1 
ATOM   6108  C  CA  . ASP A 1 1196 ? 144.236 113.181 137.244 1.00 43.00  ? 767  ASP A CA  1 
ATOM   6109  C  C   . ASP A 1 1196 ? 143.562 114.427 137.809 1.00 49.75  ? 767  ASP A C   1 
ATOM   6110  O  O   . ASP A 1 1196 ? 142.651 114.323 138.637 1.00 53.17  ? 767  ASP A O   1 
ATOM   6111  C  CB  . ASP A 1 1196 ? 145.520 112.879 138.011 1.00 60.80  ? 767  ASP A CB  1 
ATOM   6112  C  CG  . ASP A 1 1196 ? 146.141 111.545 137.611 1.00 74.85  ? 767  ASP A CG  1 
ATOM   6113  O  OD1 . ASP A 1 1196 ? 145.384 110.647 137.166 1.00 71.53  ? 767  ASP A OD1 1 
ATOM   6114  O  OD2 . ASP A 1 1196 ? 147.375 111.378 137.780 1.00 68.08  ? 767  ASP A OD2 1 
ATOM   6115  N  N   . ASN A 1 1197 ? 144.003 115.612 137.384 1.00 46.62  ? 768  ASN A N   1 
ATOM   6116  C  CA  . ASN A 1 1197 ? 143.355 116.851 137.802 1.00 36.59  ? 768  ASN A CA  1 
ATOM   6117  C  C   . ASN A 1 1197 ? 141.905 116.880 137.356 1.00 40.40  ? 768  ASN A C   1 
ATOM   6118  O  O   . ASN A 1 1197 ? 141.028 117.367 138.079 1.00 45.61  ? 768  ASN A O   1 
ATOM   6119  C  CB  . ASN A 1 1197 ? 144.114 118.031 137.232 1.00 28.79  ? 768  ASN A CB  1 
ATOM   6120  C  CG  . ASN A 1 1197 ? 145.468 118.130 137.814 1.00 40.41  ? 768  ASN A CG  1 
ATOM   6121  O  OD1 . ASN A 1 1197 ? 145.912 117.219 138.511 1.00 44.54  ? 768  ASN A OD1 1 
ATOM   6122  N  ND2 . ASN A 1 1197 ? 146.172 119.203 137.510 1.00 49.54  ? 768  ASN A ND2 1 
ATOM   6123  N  N   . ALA A 1 1198 ? 141.633 116.377 136.159 1.00 38.09  ? 769  ALA A N   1 
ATOM   6124  C  CA  . ALA A 1 1198 ? 140.252 116.321 135.713 1.00 33.32  ? 769  ALA A CA  1 
ATOM   6125  C  C   . ALA A 1 1198 ? 139.453 115.383 136.582 1.00 32.33  ? 769  ALA A C   1 
ATOM   6126  O  O   . ALA A 1 1198 ? 138.296 115.661 136.896 1.00 46.04  ? 769  ALA A O   1 
ATOM   6127  C  CB  . ALA A 1 1198 ? 140.160 115.889 134.254 1.00 40.54  ? 769  ALA A CB  1 
ATOM   6128  N  N   . ALA A 1 1199 ? 140.035 114.268 136.981 1.00 29.98  ? 770  ALA A N   1 
ATOM   6129  C  CA  . ALA A 1 1199 ? 139.256 113.375 137.819 1.00 31.34  ? 770  ALA A CA  1 
ATOM   6130  C  C   . ALA A 1 1199 ? 139.064 113.968 139.199 1.00 37.43  ? 770  ALA A C   1 
ATOM   6131  O  O   . ALA A 1 1199 ? 138.052 113.689 139.851 1.00 49.36  ? 770  ALA A O   1 
ATOM   6132  C  CB  . ALA A 1 1199 ? 139.904 111.996 137.905 1.00 47.48  ? 770  ALA A CB  1 
ATOM   6133  N  N   . ARG A 1 1200 ? 140.006 114.797 139.659 1.00 37.66  ? 771  ARG A N   1 
ATOM   6134  C  CA  . ARG A 1 1200 ? 139.850 115.449 140.964 1.00 40.73  ? 771  ARG A CA  1 
ATOM   6135  C  C   . ARG A 1 1200 ? 138.766 116.513 140.934 1.00 38.25  ? 771  ARG A C   1 
ATOM   6136  O  O   . ARG A 1 1200 ? 137.974 116.633 141.880 1.00 42.92  ? 771  ARG A O   1 
ATOM   6137  C  CB  . ARG A 1 1200 ? 141.164 116.069 141.412 1.00 45.71  ? 771  ARG A CB  1 
ATOM   6138  C  CG  . ARG A 1 1200 ? 141.028 116.873 142.666 1.00 49.26  ? 771  ARG A CG  1 
ATOM   6139  C  CD  . ARG A 1 1200 ? 142.297 116.729 143.464 1.00 67.75  ? 771  ARG A CD  1 
ATOM   6140  N  NE  . ARG A 1 1200 ? 143.474 116.802 142.605 1.00 65.97  ? 771  ARG A NE  1 
ATOM   6141  C  CZ  . ARG A 1 1200 ? 144.200 117.904 142.433 1.00 71.09  ? 771  ARG A CZ  1 
ATOM   6142  N  NH1 . ARG A 1 1200 ? 143.860 119.031 143.054 1.00 67.98  ? 771  ARG A NH1 1 
ATOM   6143  N  NH2 . ARG A 1 1200 ? 145.266 117.880 141.641 1.00 67.61  ? 771  ARG A NH2 1 
ATOM   6144  N  N   . VAL A 1 1201 ? 138.723 117.293 139.852 1.00 38.67  ? 772  VAL A N   1 
ATOM   6145  C  CA  . VAL A 1 1201 ? 137.612 118.209 139.621 1.00 28.50  ? 772  VAL A CA  1 
ATOM   6146  C  C   . VAL A 1 1201 ? 136.306 117.460 139.554 1.00 28.30  ? 772  VAL A C   1 
ATOM   6147  O  O   . VAL A 1 1201 ? 135.295 117.910 140.090 1.00 38.89  ? 772  VAL A O   1 
ATOM   6148  C  CB  . VAL A 1 1201 ? 137.831 119.005 138.336 1.00 28.68  ? 772  VAL A CB  1 
ATOM   6149  C  CG1 . VAL A 1 1201 ? 136.599 119.796 138.039 1.00 38.21  ? 772  VAL A CG1 1 
ATOM   6150  C  CG2 . VAL A 1 1201 ? 138.998 119.933 138.525 1.00 40.76  ? 772  VAL A CG2 1 
ATOM   6151  N  N   . ALA A 1 1202 ? 136.289 116.329 138.869 1.00 30.48  ? 773  ALA A N   1 
ATOM   6152  C  CA  . ALA A 1 1202 ? 135.055 115.567 138.781 1.00 34.60  ? 773  ALA A CA  1 
ATOM   6153  C  C   . ALA A 1 1202 ? 134.616 115.076 140.151 1.00 34.03  ? 773  ALA A C   1 
ATOM   6154  O  O   . ALA A 1 1202 ? 133.423 115.080 140.451 1.00 47.91  ? 773  ALA A O   1 
ATOM   6155  C  CB  . ALA A 1 1202 ? 135.212 114.394 137.806 1.00 46.02  ? 773  ALA A CB  1 
ATOM   6156  N  N   . ALA A 1 1203 ? 135.551 114.650 140.998 1.00 31.42  ? 774  ALA A N   1 
ATOM   6157  C  CA  . ALA A 1 1203 ? 135.160 114.220 142.340 1.00 30.86  ? 774  ALA A CA  1 
ATOM   6158  C  C   . ALA A 1 1203 ? 134.607 115.383 143.160 1.00 37.48  ? 774  ALA A C   1 
ATOM   6159  O  O   . ALA A 1 1203 ? 133.568 115.245 143.826 1.00 45.34  ? 774  ALA A O   1 
ATOM   6160  C  CB  . ALA A 1 1203 ? 136.340 113.576 143.061 1.00 39.88  ? 774  ALA A CB  1 
ATOM   6161  N  N   . SER A 1 1204 ? 135.268 116.542 143.117 1.00 32.11  ? 775  SER A N   1 
ATOM   6162  C  CA  . SER A 1 1204 ? 134.717 117.700 143.815 1.00 25.47  ? 775  SER A CA  1 
ATOM   6163  C  C   . SER A 1 1204 ? 133.347 118.063 143.270 1.00 29.64  ? 775  SER A C   1 
ATOM   6164  O  O   . SER A 1 1204 ? 132.428 118.360 144.037 1.00 37.58  ? 775  SER A O   1 
ATOM   6165  C  CB  . SER A 1 1204 ? 135.651 118.897 143.703 1.00 31.76  ? 775  SER A CB  1 
ATOM   6166  O  OG  . SER A 1 1204 ? 136.885 118.639 144.357 1.00 39.87  ? 775  SER A OG  1 
ATOM   6167  N  N   . LEU A 1 1205 ? 133.192 118.064 141.953 1.00 30.78  ? 776  LEU A N   1 
ATOM   6168  C  CA  . LEU A 1 1205 ? 131.910 118.422 141.377 1.00 26.46  ? 776  LEU A CA  1 
ATOM   6169  C  C   . LEU A 1 1205 ? 130.873 117.393 141.737 1.00 22.25  ? 776  LEU A C   1 
ATOM   6170  O  O   . LEU A 1 1205 ? 129.697 117.722 141.895 1.00 36.46  ? 776  LEU A O   1 
ATOM   6171  C  CB  . LEU A 1 1205 ? 132.030 118.569 139.867 1.00 25.40  ? 776  LEU A CB  1 
ATOM   6172  C  CG  . LEU A 1 1205 ? 130.734 118.933 139.165 1.00 32.28  ? 776  LEU A CG  1 
ATOM   6173  C  CD1 . LEU A 1 1205 ? 130.216 120.280 139.661 1.00 38.66  ? 776  LEU A CD1 1 
ATOM   6174  C  CD2 . LEU A 1 1205 ? 130.987 118.976 137.684 1.00 41.23  ? 776  LEU A CD2 1 
ATOM   6175  N  N   . ALA A 1 1206 ? 131.286 116.163 141.920 1.00 20.54  ? 777  ALA A N   1 
ATOM   6176  C  CA  . ALA A 1 1206 ? 130.337 115.179 142.382 1.00 26.18  ? 777  ALA A CA  1 
ATOM   6177  C  C   . ALA A 1 1206 ? 129.868 115.530 143.768 1.00 25.69  ? 777  ALA A C   1 
ATOM   6178  O  O   . ALA A 1 1206 ? 128.676 115.442 144.058 1.00 35.33  ? 777  ALA A O   1 
ATOM   6179  C  CB  . ALA A 1 1206 ? 130.955 113.784 142.358 1.00 40.11  ? 777  ALA A CB  1 
ATOM   6180  N  N   . LYS A 1 1207 ? 130.779 115.962 144.631 1.00 25.39  ? 778  LYS A N   1 
ATOM   6181  C  CA  . LYS A 1 1207 ? 130.371 116.303 145.997 1.00 30.90  ? 778  LYS A CA  1 
ATOM   6182  C  C   . LYS A 1 1207 ? 129.443 117.520 146.005 1.00 31.54  ? 778  LYS A C   1 
ATOM   6183  O  O   . LYS A 1 1207 ? 128.381 117.515 146.646 1.00 34.50  ? 778  LYS A O   1 
ATOM   6184  C  CB  . LYS A 1 1207 ? 131.610 116.557 146.859 1.00 36.82  ? 778  LYS A CB  1 
ATOM   6185  C  CG  . LYS A 1 1207 ? 132.532 115.335 146.941 1.00 41.44  ? 778  LYS A CG  1 
ATOM   6186  C  CD  . LYS A 1 1207 ? 133.765 115.550 147.816 1.00 35.80  ? 778  LYS A CD  1 
ATOM   6187  C  CE  . LYS A 1 1207 ? 134.614 114.277 147.842 1.00 31.89  ? 778  LYS A CE  1 
ATOM   6188  N  NZ  . LYS A 1 1207 ? 135.831 114.354 148.703 1.00 31.07  ? 778  LYS A NZ  1 
ATOM   6189  N  N   . VAL A 1 1208 ? 129.818 118.553 145.249 1.00 32.59  ? 779  VAL A N   1 
ATOM   6190  C  CA  . VAL A 1 1208 ? 129.025 119.775 145.140 1.00 23.22  ? 779  VAL A CA  1 
ATOM   6191  C  C   . VAL A 1 1208 ? 127.617 119.457 144.676 1.00 24.06  ? 779  VAL A C   1 
ATOM   6192  O  O   . VAL A 1 1208 ? 126.641 119.711 145.389 1.00 30.79  ? 779  VAL A O   1 
ATOM   6193  C  CB  . VAL A 1 1208 ? 129.702 120.755 144.173 1.00 29.14  ? 779  VAL A CB  1 
ATOM   6194  C  CG1 . VAL A 1 1208 ? 128.744 121.862 143.827 1.00 41.55  ? 779  VAL A CG1 1 
ATOM   6195  C  CG2 . VAL A 1 1208 ? 130.975 121.316 144.798 1.00 38.18  ? 779  VAL A CG2 1 
ATOM   6196  N  N   . THR A 1 1209 ? 127.489 118.884 143.472 1.00 24.93  ? 780  THR A N   1 
ATOM   6197  C  CA  . THR A 1 1209 ? 126.157 118.632 142.940 1.00 23.60  ? 780  THR A CA  1 
ATOM   6198  C  C   . THR A 1 1209 ? 125.406 117.626 143.771 1.00 32.03  ? 780  THR A C   1 
ATOM   6199  O  O   . THR A 1 1209 ? 124.178 117.707 143.852 1.00 48.42  ? 780  THR A O   1 
ATOM   6200  C  CB  . THR A 1 1209 ? 126.176 118.077 141.543 1.00 22.71  ? 780  THR A CB  1 
ATOM   6201  O  OG1 . THR A 1 1209 ? 126.981 116.899 141.538 1.00 27.82  ? 780  THR A OG1 1 
ATOM   6202  C  CG2 . THR A 1 1209 ? 126.728 119.088 140.587 1.00 35.22  ? 780  THR A CG2 1 
ATOM   6203  N  N   . SER A 1 1210 ? 126.088 116.646 144.358 1.00 29.95  ? 781  SER A N   1 
ATOM   6204  C  CA  . SER A 1 1210 ? 125.383 115.733 145.237 1.00 27.04  ? 781  SER A CA  1 
ATOM   6205  C  C   . SER A 1 1210 ? 124.722 116.494 146.358 1.00 32.06  ? 781  SER A C   1 
ATOM   6206  O  O   . SER A 1 1210 ? 123.588 116.191 146.743 1.00 43.07  ? 781  SER A O   1 
ATOM   6207  C  CB  . SER A 1 1210 ? 126.338 114.705 145.809 1.00 31.21  ? 781  SER A CB  1 
ATOM   6208  O  OG  . SER A 1 1210 ? 125.651 113.870 146.726 1.00 46.80  ? 781  SER A OG  1 
ATOM   6209  N  N   . ALA A 1 1211 ? 125.410 117.496 146.887 1.00 33.72  ? 782  ALA A N   1 
ATOM   6210  C  CA  . ALA A 1 1211 ? 124.798 118.295 147.935 1.00 39.14  ? 782  ALA A CA  1 
ATOM   6211  C  C   . ALA A 1 1211 ? 123.689 119.176 147.382 1.00 38.48  ? 782  ALA A C   1 
ATOM   6212  O  O   . ALA A 1 1211 ? 122.757 119.527 148.113 1.00 46.20  ? 782  ALA A O   1 
ATOM   6213  C  CB  . ALA A 1 1211 ? 125.864 119.142 148.643 1.00 49.90  ? 782  ALA A CB  1 
ATOM   6214  N  N   . CYS A 1 1212 ? 123.778 119.562 146.116 1.00 33.54  ? 783  CYS A N   1 
ATOM   6215  C  CA  . CYS A 1 1212 ? 122.739 120.402 145.531 1.00 37.09  ? 783  CYS A CA  1 
ATOM   6216  C  C   . CYS A 1 1212 ? 121.494 119.609 145.150 1.00 44.84  ? 783  CYS A C   1 
ATOM   6217  O  O   . CYS A 1 1212 ? 120.479 120.212 144.776 1.00 46.78  ? 783  CYS A O   1 
ATOM   6218  C  CB  . CYS A 1 1212 ? 123.272 121.114 144.284 1.00 39.06  ? 783  CYS A CB  1 
ATOM   6219  S  SG  . CYS A 1 1212 ? 124.577 122.335 144.572 1.00 63.64  ? 783  CYS A SG  1 
ATOM   6220  N  N   . GLY A 1 1213 ? 121.546 118.276 145.243 1.00 39.36  ? 784  GLY A N   1 
ATOM   6221  C  CA  . GLY A 1 1213 ? 120.451 117.412 144.881 1.00 37.59  ? 784  GLY A CA  1 
ATOM   6222  C  C   . GLY A 1 1213 ? 120.650 116.627 143.601 1.00 42.91  ? 784  GLY A C   1 
ATOM   6223  O  O   . GLY A 1 1213 ? 119.924 115.652 143.378 1.00 48.10  ? 784  GLY A O   1 
ATOM   6224  N  N   . ILE A 1 1214 ? 121.602 117.012 142.759 1.00 35.09  ? 785  ILE A N   1 
ATOM   6225  C  CA  . ILE A 1 1214 ? 121.795 116.379 141.460 1.00 34.32  ? 785  ILE A CA  1 
ATOM   6226  C  C   . ILE A 1 1214 ? 122.902 115.348 141.586 1.00 39.67  ? 785  ILE A C   1 
ATOM   6227  O  O   . ILE A 1 1214 ? 124.075 115.709 141.745 1.00 46.36  ? 785  ILE A O   1 
ATOM   6228  C  CB  . ILE A 1 1214 ? 122.157 117.394 140.373 1.00 43.76  ? 785  ILE A CB  1 
ATOM   6229  C  CG1 . ILE A 1 1214 ? 121.008 118.370 140.082 1.00 49.33  ? 785  ILE A CG1 1 
ATOM   6230  C  CG2 . ILE A 1 1214 ? 122.549 116.641 139.134 1.00 54.27  ? 785  ILE A CG2 1 
ATOM   6231  C  CD1 . ILE A 1 1214 ? 121.066 119.662 140.874 1.00 52.66  ? 785  ILE A CD1 1 
ATOM   6232  N  N   . PHE A 1 1215 ? 122.571 114.066 141.485 1.00 41.02  ? 786  PHE A N   1 
ATOM   6233  C  CA  . PHE A 1 1215 ? 123.578 113.034 141.694 1.00 38.47  ? 786  PHE A CA  1 
ATOM   6234  C  C   . PHE A 1 1215 ? 124.266 112.756 140.375 1.00 36.51  ? 786  PHE A C   1 
ATOM   6235  O  O   . PHE A 1 1215 ? 123.662 112.244 139.432 1.00 41.71  ? 786  PHE A O   1 
ATOM   6236  C  CB  . PHE A 1 1215 ? 122.979 111.776 142.301 1.00 33.83  ? 786  PHE A CB  1 
ATOM   6237  C  CG  . PHE A 1 1215 ? 122.495 111.995 143.676 1.00 40.94  ? 786  PHE A CG  1 
ATOM   6238  C  CD1 . PHE A 1 1215 ? 123.382 112.042 144.738 1.00 42.81  ? 786  PHE A CD1 1 
ATOM   6239  C  CD2 . PHE A 1 1215 ? 121.141 112.220 143.912 1.00 55.46  ? 786  PHE A CD2 1 
ATOM   6240  C  CE1 . PHE A 1 1215 ? 122.914 112.294 146.037 1.00 59.07  ? 786  PHE A CE1 1 
ATOM   6241  C  CE2 . PHE A 1 1215 ? 120.658 112.466 145.201 1.00 61.33  ? 786  PHE A CE2 1 
ATOM   6242  C  CZ  . PHE A 1 1215 ? 121.547 112.504 146.268 1.00 63.45  ? 786  PHE A CZ  1 
ATOM   6243  N  N   . LEU A 1 1216 ? 125.534 113.104 140.329 1.00 41.51  ? 787  LEU A N   1 
ATOM   6244  C  CA  . LEU A 1 1216 ? 126.428 112.812 139.225 1.00 41.72  ? 787  LEU A CA  1 
ATOM   6245  C  C   . LEU A 1 1216 ? 126.894 111.379 139.391 1.00 54.87  ? 787  LEU A C   1 
ATOM   6246  O  O   . LEU A 1 1216 ? 127.778 111.098 140.203 1.00 60.02  ? 787  LEU A O   1 
ATOM   6247  C  CB  . LEU A 1 1216 ? 127.614 113.758 139.281 1.00 46.09  ? 787  LEU A CB  1 
ATOM   6248  C  CG  . LEU A 1 1216 ? 128.257 114.054 137.957 1.00 56.67  ? 787  LEU A CG  1 
ATOM   6249  C  CD1 . LEU A 1 1216 ? 127.142 114.632 137.122 1.00 63.10  ? 787  LEU A CD1 1 
ATOM   6250  C  CD2 . LEU A 1 1216 ? 129.398 115.051 138.147 1.00 52.78  ? 787  LEU A CD2 1 
ATOM   6251  N  N   . LYS A 1 1217 ? 126.320 110.464 138.630 1.00 57.68  ? 788  LYS A N   1 
ATOM   6252  C  CA  . LYS A 1 1217 ? 126.708 109.062 138.765 1.00 56.61  ? 788  LYS A CA  1 
ATOM   6253  C  C   . LYS A 1 1217 ? 128.143 108.869 138.295 1.00 52.53  ? 788  LYS A C   1 
ATOM   6254  O  O   . LYS A 1 1217 ? 128.408 109.037 137.100 1.00 62.82  ? 788  LYS A O   1 
ATOM   6255  C  CB  . LYS A 1 1217 ? 125.756 108.182 137.961 1.00 60.74  ? 788  LYS A CB  1 
ATOM   6256  C  CG  . LYS A 1 1217 ? 124.289 108.339 138.364 1.00 63.26  ? 788  LYS A CG  1 
ATOM   6257  C  CD  . LYS A 1 1217 ? 123.405 107.407 137.562 1.00 68.20  ? 788  LYS A CD  1 
ATOM   6258  C  CE  . LYS A 1 1217 ? 123.881 105.961 137.733 1.00 74.83  ? 788  LYS A CE  1 
ATOM   6259  N  NZ  . LYS A 1 1217 ? 123.121 104.975 136.910 1.00 82.51  ? 788  LYS A NZ  1 
ATOM   6260  N  N   . PRO A 1 1218 ? 129.092 108.548 139.173 1.00 37.92  ? 789  PRO A N   1 
ATOM   6261  C  CA  . PRO A 1 1218 ? 130.474 108.400 138.721 1.00 40.08  ? 789  PRO A CA  1 
ATOM   6262  C  C   . PRO A 1 1218 ? 130.696 107.243 137.750 1.00 56.84  ? 789  PRO A C   1 
ATOM   6263  O  O   . PRO A 1 1218 ? 131.701 107.261 137.029 1.00 63.61  ? 789  PRO A O   1 
ATOM   6264  C  CB  . PRO A 1 1218 ? 131.242 108.183 140.024 1.00 54.27  ? 789  PRO A CB  1 
ATOM   6265  C  CG  . PRO A 1 1218 ? 130.258 107.614 140.938 1.00 57.40  ? 789  PRO A CG  1 
ATOM   6266  C  CD  . PRO A 1 1218 ? 128.960 108.267 140.604 1.00 52.52  ? 789  PRO A CD  1 
ATOM   6267  N  N   . ASP A 1 1219 ? 129.823 106.231 137.704 1.00 57.11  ? 790  ASP A N   1 
ATOM   6268  C  CA  . ASP A 1 1219 ? 130.021 105.155 136.729 1.00 55.27  ? 790  ASP A CA  1 
ATOM   6269  C  C   . ASP A 1 1219 ? 129.890 105.655 135.303 1.00 54.45  ? 790  ASP A C   1 
ATOM   6270  O  O   . ASP A 1 1219 ? 130.670 105.265 134.430 1.00 61.41  ? 790  ASP A O   1 
ATOM   6271  C  CB  . ASP A 1 1219 ? 129.027 104.010 136.941 1.00 71.26  ? 790  ASP A CB  1 
ATOM   6272  C  CG  . ASP A 1 1219 ? 129.281 103.236 138.220 1.00 87.50  ? 790  ASP A CG  1 
ATOM   6273  O  OD1 . ASP A 1 1219 ? 130.282 103.541 138.909 1.00 83.58  ? 790  ASP A OD1 1 
ATOM   6274  O  OD2 . ASP A 1 1219 ? 128.491 102.307 138.520 1.00 81.58  ? 790  ASP A OD2 1 
ATOM   6275  N  N   . GLU A 1 1220 ? 128.897 106.496 135.038 1.00 63.83  ? 791  GLU A N   1 
ATOM   6276  C  CA  . GLU A 1 1220 ? 128.544 106.880 133.679 1.00 67.09  ? 791  GLU A CA  1 
ATOM   6277  C  C   . GLU A 1 1220 ? 129.130 108.227 133.263 1.00 67.88  ? 791  GLU A C   1 
ATOM   6278  O  O   . GLU A 1 1220 ? 128.780 108.729 132.189 1.00 71.56  ? 791  GLU A O   1 
ATOM   6279  C  CB  . GLU A 1 1220 ? 127.017 106.890 133.514 1.00 71.31  ? 791  GLU A CB  1 
ATOM   6280  C  CG  . GLU A 1 1220 ? 126.274 107.975 134.316 1.00 74.32  ? 791  GLU A CG  1 
ATOM   6281  C  CD  . GLU A 1 1220 ? 124.764 107.978 134.055 1.00 88.32  ? 791  GLU A CD  1 
ATOM   6282  O  OE1 . GLU A 1 1220 ? 124.279 107.055 133.359 1.00 86.78  ? 791  GLU A OE1 1 
ATOM   6283  O  OE2 . GLU A 1 1220 ? 124.066 108.902 134.540 1.00 84.05  ? 791  GLU A OE2 1 
ATOM   6284  N  N   . THR A 1 1221 ? 129.996 108.830 134.082 1.00 57.95  ? 792  THR A N   1 
ATOM   6285  C  CA  . THR A 1 1221 ? 130.747 110.017 133.689 1.00 48.47  ? 792  THR A CA  1 
ATOM   6286  C  C   . THR A 1 1221 ? 132.206 109.663 133.595 1.00 38.05  ? 792  THR A C   1 
ATOM   6287  O  O   . THR A 1 1221 ? 132.740 108.961 134.453 1.00 52.76  ? 792  THR A O   1 
ATOM   6288  C  CB  . THR A 1 1221 ? 130.597 111.194 134.660 1.00 59.79  ? 792  THR A CB  1 
ATOM   6289  O  OG1 . THR A 1 1221 ? 131.456 112.260 134.226 1.00 53.03  ? 792  THR A OG1 1 
ATOM   6290  C  CG2 . THR A 1 1221 ? 130.967 110.809 136.092 1.00 61.80  ? 792  THR A CG2 1 
ATOM   6291  N  N   . PHE A 1 1222 ? 132.845 110.127 132.562 1.00 30.76  ? 793  PHE A N   1 
ATOM   6292  C  CA  . PHE A 1 1222 ? 134.175 109.637 132.322 1.00 39.10  ? 793  PHE A CA  1 
ATOM   6293  C  C   . PHE A 1 1222 ? 135.125 110.791 132.094 1.00 45.26  ? 793  PHE A C   1 
ATOM   6294  O  O   . PHE A 1 1222 ? 134.740 111.838 131.577 1.00 52.27  ? 793  PHE A O   1 
ATOM   6295  C  CB  . PHE A 1 1222 ? 134.189 108.683 131.154 1.00 51.71  ? 793  PHE A CB  1 
ATOM   6296  C  CG  . PHE A 1 1222 ? 133.112 107.583 131.211 1.00 74.82  ? 793  PHE A CG  1 
ATOM   6297  C  CD1 . PHE A 1 1222 ? 133.395 106.329 131.794 1.00 72.70  ? 793  PHE A CD1 1 
ATOM   6298  C  CD2 . PHE A 1 1222 ? 131.834 107.781 130.664 1.00 80.12  ? 793  PHE A CD2 1 
ATOM   6299  C  CE1 . PHE A 1 1222 ? 132.426 105.290 131.825 1.00 67.44  ? 793  PHE A CE1 1 
ATOM   6300  C  CE2 . PHE A 1 1222 ? 130.853 106.744 130.696 1.00 75.90  ? 793  PHE A CE2 1 
ATOM   6301  C  CZ  . PHE A 1 1222 ? 131.155 105.504 131.283 1.00 71.04  ? 793  PHE A CZ  1 
ATOM   6302  N  N   . VAL A 1 1223 ? 136.368 110.590 132.500 1.00 37.10  ? 794  VAL A N   1 
ATOM   6303  C  CA  . VAL A 1 1223 ? 137.406 111.591 132.364 1.00 23.52  ? 794  VAL A CA  1 
ATOM   6304  C  C   . VAL A 1 1223 ? 138.138 111.360 131.056 1.00 27.90  ? 794  VAL A C   1 
ATOM   6305  O  O   . VAL A 1 1223 ? 138.875 110.384 130.907 1.00 38.56  ? 794  VAL A O   1 
ATOM   6306  C  CB  . VAL A 1 1223 ? 138.368 111.517 133.539 1.00 31.54  ? 794  VAL A CB  1 
ATOM   6307  C  CG1 . VAL A 1 1223 ? 139.474 112.471 133.307 1.00 45.71  ? 794  VAL A CG1 1 
ATOM   6308  C  CG2 . VAL A 1 1223 ? 137.633 111.855 134.805 1.00 42.41  ? 794  VAL A CG2 1 
ATOM   6309  N  N   . HIS A 1 1224 ? 137.970 112.277 130.126 1.00 31.56  ? 795  HIS A N   1 
ATOM   6310  C  CA  . HIS A 1 1224 ? 138.510 112.142 128.786 1.00 36.11  ? 795  HIS A CA  1 
ATOM   6311  C  C   . HIS A 1 1224 ? 139.678 113.097 128.672 1.00 30.58  ? 795  HIS A C   1 
ATOM   6312  O  O   . HIS A 1 1224 ? 139.511 114.302 128.841 1.00 39.32  ? 795  HIS A O   1 
ATOM   6313  C  CB  . HIS A 1 1224 ? 137.465 112.524 127.746 1.00 42.61  ? 795  HIS A CB  1 
ATOM   6314  C  CG  . HIS A 1 1224 ? 136.122 111.930 127.999 1.00 47.17  ? 795  HIS A CG  1 
ATOM   6315  N  ND1 . HIS A 1 1224 ? 135.831 110.600 127.786 1.00 51.88  ? 795  HIS A ND1 1 
ATOM   6316  C  CD2 . HIS A 1 1224 ? 134.991 112.489 128.489 1.00 52.02  ? 795  HIS A CD2 1 
ATOM   6317  C  CE1 . HIS A 1 1224 ? 134.571 110.368 128.114 1.00 52.93  ? 795  HIS A CE1 1 
ATOM   6318  N  NE2 . HIS A 1 1224 ? 134.041 111.496 128.550 1.00 53.55  ? 795  HIS A NE2 1 
ATOM   6319  N  N   . SER A 1 1225 ? 140.829 112.598 128.346 1.00 29.50  ? 796  SER A N   1 
ATOM   6320  C  CA  . SER A 1 1225 ? 141.934 113.507 128.142 1.00 34.86  ? 796  SER A CA  1 
ATOM   6321  C  C   . SER A 1 1225 ? 142.165 113.567 126.636 1.00 41.35  ? 796  SER A C   1 
ATOM   6322  O  O   . SER A 1 1225 ? 142.807 112.693 126.052 1.00 53.34  ? 796  SER A O   1 
ATOM   6323  C  CB  . SER A 1 1225 ? 143.156 113.035 128.914 1.00 53.66  ? 796  SER A CB  1 
ATOM   6324  O  OG  . SER A 1 1225 ? 144.250 113.923 128.750 1.00 57.59  ? 796  SER A OG  1 
ATOM   6325  N  N   . GLY A 1 1226 ? 141.616 114.580 125.997 1.00 35.46  ? 797  GLY A N   1 
ATOM   6326  C  CA  . GLY A 1 1226 ? 141.870 114.790 124.588 1.00 40.77  ? 797  GLY A CA  1 
ATOM   6327  C  C   . GLY A 1 1226 ? 140.730 114.416 123.668 1.00 50.59  ? 797  GLY A C   1 
ATOM   6328  O  O   . GLY A 1 1226 ? 140.758 114.807 122.492 1.00 56.37  ? 797  GLY A O   1 
ATOM   6329  N  N   . PHE A 1 1227 ? 139.729 113.682 124.148 1.00 44.23  ? 798  PHE A N   1 
ATOM   6330  C  CA  . PHE A 1 1227 ? 138.544 113.346 123.350 1.00 38.27  ? 798  PHE A CA  1 
ATOM   6331  C  C   . PHE A 1 1227 ? 137.363 114.244 123.737 1.00 44.27  ? 798  PHE A C   1 
ATOM   6332  O  O   . PHE A 1 1227 ? 136.657 113.983 124.716 1.00 50.13  ? 798  PHE A O   1 
ATOM   6333  C  CB  . PHE A 1 1227 ? 138.215 111.873 123.519 1.00 40.60  ? 798  PHE A CB  1 
ATOM   6334  C  CG  . PHE A 1 1227 ? 137.046 111.416 122.702 1.00 51.72  ? 798  PHE A CG  1 
ATOM   6335  C  CD1 . PHE A 1 1227 ? 136.871 111.856 121.394 1.00 56.66  ? 798  PHE A CD1 1 
ATOM   6336  C  CD2 . PHE A 1 1227 ? 136.128 110.512 123.233 1.00 54.69  ? 798  PHE A CD2 1 
ATOM   6337  C  CE1 . PHE A 1 1227 ? 135.773 111.417 120.629 1.00 55.97  ? 798  PHE A CE1 1 
ATOM   6338  C  CE2 . PHE A 1 1227 ? 135.037 110.064 122.487 1.00 52.45  ? 798  PHE A CE2 1 
ATOM   6339  C  CZ  . PHE A 1 1227 ? 134.860 110.515 121.180 1.00 57.65  ? 798  PHE A CZ  1 
ATOM   6340  N  N   . ILE A 1 1228 ? 137.165 115.307 122.958 1.00 41.98  ? 799  ILE A N   1 
ATOM   6341  C  CA  . ILE A 1 1228 ? 136.070 116.264 123.104 1.00 39.16  ? 799  ILE A CA  1 
ATOM   6342  C  C   . ILE A 1 1228 ? 134.951 115.788 122.189 1.00 46.16  ? 799  ILE A C   1 
ATOM   6343  O  O   . ILE A 1 1228 ? 135.035 115.962 120.969 1.00 53.95  ? 799  ILE A O   1 
ATOM   6344  C  CB  . ILE A 1 1228 ? 136.519 117.679 122.709 1.00 54.05  ? 799  ILE A CB  1 
ATOM   6345  C  CG1 . ILE A 1 1228 ? 137.634 118.213 123.622 1.00 62.50  ? 799  ILE A CG1 1 
ATOM   6346  C  CG2 . ILE A 1 1228 ? 135.339 118.639 122.469 1.00 67.28  ? 799  ILE A CG2 1 
ATOM   6347  C  CD1 . ILE A 1 1228 ? 139.052 117.868 123.155 1.00 59.12  ? 799  ILE A CD1 1 
ATOM   6348  N  N   . TYR A 1 1229 ? 133.902 115.181 122.730 1.00 43.19  ? 800  TYR A N   1 
ATOM   6349  C  CA  . TYR A 1 1229 ? 132.892 114.635 121.837 1.00 47.66  ? 800  TYR A CA  1 
ATOM   6350  C  C   . TYR A 1 1229 ? 131.509 115.189 122.056 1.00 53.00  ? 800  TYR A C   1 
ATOM   6351  O  O   . TYR A 1 1229 ? 130.598 114.849 121.296 1.00 60.65  ? 800  TYR A O   1 
ATOM   6352  C  CB  . TYR A 1 1229 ? 132.823 113.112 121.936 1.00 53.31  ? 800  TYR A CB  1 
ATOM   6353  C  CG  . TYR A 1 1229 ? 132.313 112.635 123.254 1.00 58.68  ? 800  TYR A CG  1 
ATOM   6354  C  CD1 . TYR A 1 1229 ? 133.184 112.450 124.315 1.00 69.77  ? 800  TYR A CD1 1 
ATOM   6355  C  CD2 . TYR A 1 1229 ? 130.969 112.366 123.452 1.00 64.47  ? 800  TYR A CD2 1 
ATOM   6356  C  CE1 . TYR A 1 1229 ? 132.738 112.002 125.545 1.00 78.59  ? 800  TYR A CE1 1 
ATOM   6357  C  CE2 . TYR A 1 1229 ? 130.503 111.922 124.685 1.00 77.57  ? 800  TYR A CE2 1 
ATOM   6358  C  CZ  . TYR A 1 1229 ? 131.396 111.738 125.730 1.00 85.10  ? 800  TYR A CZ  1 
ATOM   6359  O  OH  . TYR A 1 1229 ? 130.961 111.296 126.965 1.00 79.30  ? 800  TYR A OH  1 
ATOM   6360  N  N   . PHE A 1 1230 ? 131.311 116.010 123.066 1.00 59.74  ? 801  PHE A N   1 
ATOM   6361  C  CA  . PHE A 1 1230 ? 130.050 116.714 123.134 1.00 59.89  ? 801  PHE A CA  1 
ATOM   6362  C  C   . PHE A 1 1230 ? 129.953 117.651 121.943 1.00 61.23  ? 801  PHE A C   1 
ATOM   6363  O  O   . PHE A 1 1230 ? 130.932 117.913 121.237 1.00 64.95  ? 801  PHE A O   1 
ATOM   6364  C  CB  . PHE A 1 1230 ? 129.952 117.502 124.433 1.00 65.75  ? 801  PHE A CB  1 
ATOM   6365  C  CG  . PHE A 1 1230 ? 130.712 118.800 124.393 1.00 81.17  ? 801  PHE A CG  1 
ATOM   6366  C  CD1 . PHE A 1 1230 ? 132.110 118.804 124.491 1.00 89.05  ? 801  PHE A CD1 1 
ATOM   6367  C  CD2 . PHE A 1 1230 ? 130.048 120.019 124.276 1.00 81.62  ? 801  PHE A CD2 1 
ATOM   6368  C  CE1 . PHE A 1 1230 ? 132.842 120.009 124.462 1.00 95.38  ? 801  PHE A CE1 1 
ATOM   6369  C  CE2 . PHE A 1 1230 ? 130.765 121.224 124.245 1.00 87.44  ? 801  PHE A CE2 1 
ATOM   6370  C  CZ  . PHE A 1 1230 ? 132.168 121.216 124.340 1.00 97.69  ? 801  PHE A CZ  1 
ATOM   6371  N  N   . GLY A 1 1231 ? 128.761 118.157 121.720 1.00 72.37  ? 802  GLY A N   1 
ATOM   6372  C  CA  . GLY A 1 1231 ? 128.581 119.197 120.735 1.00 78.73  ? 802  GLY A CA  1 
ATOM   6373  C  C   . GLY A 1 1231 ? 128.508 118.681 119.311 1.00 68.91  ? 802  GLY A C   1 
ATOM   6374  O  O   . GLY A 1 1231 ? 128.436 117.479 119.033 1.00 68.72  ? 802  GLY A O   1 
ATOM   6375  N  N   . LYS A 1 1232 ? 128.523 119.632 118.387 1.00 59.77  ? 803  LYS A N   1 
ATOM   6376  C  CA  . LYS A 1 1232 ? 128.287 119.241 117.016 1.00 56.25  ? 803  LYS A CA  1 
ATOM   6377  C  C   . LYS A 1 1232 ? 129.469 118.485 116.458 1.00 53.48  ? 803  LYS A C   1 
ATOM   6378  O  O   . LYS A 1 1232 ? 129.278 117.580 115.640 1.00 60.64  ? 803  LYS A O   1 
ATOM   6379  C  CB  . LYS A 1 1232 ? 127.965 120.462 116.159 1.00 74.62  ? 803  LYS A CB  1 
ATOM   6380  C  CG  . LYS A 1 1232 ? 129.040 121.530 116.161 1.00 82.23  ? 803  LYS A CG  1 
ATOM   6381  C  CD  . LYS A 1 1232 ? 128.566 122.785 115.422 1.00 91.74  ? 803  LYS A CD  1 
ATOM   6382  C  CE  . LYS A 1 1232 ? 127.373 123.427 116.144 1.00 95.52  ? 803  LYS A CE  1 
ATOM   6383  N  NZ  . LYS A 1 1232 ? 126.928 124.722 115.545 1.00 95.11  ? 803  LYS A NZ  1 
ATOM   6384  N  N   . LYS A 1 1233 ? 130.679 118.789 116.902 1.00 41.51  ? 804  LYS A N   1 
ATOM   6385  C  CA  . LYS A 1 1233 ? 131.852 118.193 116.289 1.00 44.26  ? 804  LYS A CA  1 
ATOM   6386  C  C   . LYS A 1 1233 ? 132.681 117.431 117.312 1.00 47.96  ? 804  LYS A C   1 
ATOM   6387  O  O   . LYS A 1 1233 ? 132.991 117.958 118.384 1.00 52.43  ? 804  LYS A O   1 
ATOM   6388  C  CB  . LYS A 1 1233 ? 132.662 119.268 115.582 1.00 45.29  ? 804  LYS A CB  1 
ATOM   6389  C  CG  . LYS A 1 1233 ? 131.809 120.003 114.559 1.00 59.83  ? 804  LYS A CG  1 
ATOM   6390  C  CD  . LYS A 1 1233 ? 132.495 121.232 113.968 1.00 73.87  ? 804  LYS A CD  1 
ATOM   6391  C  CE  . LYS A 1 1233 ? 131.533 122.071 113.113 1.00 74.03  ? 804  LYS A CE  1 
ATOM   6392  N  NZ  . LYS A 1 1233 ? 132.201 123.312 112.613 1.00 75.94  ? 804  LYS A NZ  1 
ATOM   6393  N  N   . GLN A 1 1234 ? 133.029 116.186 116.980 1.00 37.25  ? 805  GLN A N   1 
ATOM   6394  C  CA  . GLN A 1 1234 ? 133.844 115.360 117.854 1.00 29.26  ? 805  GLN A CA  1 
ATOM   6395  C  C   . GLN A 1 1234 ? 135.302 115.516 117.497 1.00 35.41  ? 805  GLN A C   1 
ATOM   6396  O  O   . GLN A 1 1234 ? 135.663 115.448 116.319 1.00 46.01  ? 805  GLN A O   1 
ATOM   6397  C  CB  . GLN A 1 1234 ? 133.477 113.889 117.750 1.00 38.87  ? 805  GLN A CB  1 
ATOM   6398  C  CG  . GLN A 1 1234 ? 132.170 113.510 118.400 1.00 49.63  ? 805  GLN A CG  1 
ATOM   6399  C  CD  . GLN A 1 1234 ? 130.986 113.934 117.585 1.00 63.07  ? 805  GLN A CD  1 
ATOM   6400  O  OE1 . GLN A 1 1234 ? 131.115 114.249 116.401 1.00 67.70  ? 805  GLN A OE1 1 
ATOM   6401  N  NE2 . GLN A 1 1234 ? 129.816 113.948 118.207 1.00 63.76  ? 805  GLN A NE2 1 
ATOM   6402  N  N   . TYR A 1 1235 ? 136.142 115.687 118.506 1.00 29.69  ? 806  TYR A N   1 
ATOM   6403  C  CA  . TYR A 1 1235 ? 137.569 115.807 118.290 1.00 25.81  ? 806  TYR A CA  1 
ATOM   6404  C  C   . TYR A 1 1235 ? 138.293 114.748 119.089 1.00 30.02  ? 806  TYR A C   1 
ATOM   6405  O  O   . TYR A 1 1235 ? 137.955 114.497 120.242 1.00 44.84  ? 806  TYR A O   1 
ATOM   6406  C  CB  . TYR A 1 1235 ? 138.077 117.156 118.703 1.00 33.01  ? 806  TYR A CB  1 
ATOM   6407  C  CG  . TYR A 1 1235 ? 137.498 118.262 117.899 1.00 34.41  ? 806  TYR A CG  1 
ATOM   6408  C  CD1 . TYR A 1 1235 ? 138.059 118.622 116.703 1.00 40.08  ? 806  TYR A CD1 1 
ATOM   6409  C  CD2 . TYR A 1 1235 ? 136.429 118.990 118.367 1.00 38.49  ? 806  TYR A CD2 1 
ATOM   6410  C  CE1 . TYR A 1 1235 ? 137.538 119.634 115.964 1.00 44.08  ? 806  TYR A CE1 1 
ATOM   6411  C  CE2 . TYR A 1 1235 ? 135.910 120.012 117.645 1.00 39.17  ? 806  TYR A CE2 1 
ATOM   6412  C  CZ  . TYR A 1 1235 ? 136.464 120.331 116.440 1.00 41.68  ? 806  TYR A CZ  1 
ATOM   6413  O  OH  . TYR A 1 1235 ? 135.947 121.359 115.688 1.00 52.00  ? 806  TYR A OH  1 
ATOM   6414  N  N   . LEU A 1 1236 ? 139.290 114.137 118.485 1.00 29.93  ? 807  LEU A N   1 
ATOM   6415  C  CA  . LEU A 1 1236 ? 140.194 113.230 119.179 1.00 29.61  ? 807  LEU A CA  1 
ATOM   6416  C  C   . LEU A 1 1236 ? 141.571 113.861 119.186 1.00 36.72  ? 807  LEU A C   1 
ATOM   6417  O  O   . LEU A 1 1236 ? 142.240 113.886 118.149 1.00 51.71  ? 807  LEU A O   1 
ATOM   6418  C  CB  . LEU A 1 1236 ? 140.240 111.878 118.485 1.00 36.20  ? 807  LEU A CB  1 
ATOM   6419  C  CG  . LEU A 1 1236 ? 141.236 110.939 119.153 1.00 42.41  ? 807  LEU A CG  1 
ATOM   6420  C  CD1 . LEU A 1 1236 ? 140.796 110.617 120.564 1.00 52.03  ? 807  LEU A CD1 1 
ATOM   6421  C  CD2 . LEU A 1 1236 ? 141.371 109.658 118.362 1.00 43.18  ? 807  LEU A CD2 1 
ATOM   6422  N  N   . ASN A 1 1237 ? 141.999 114.373 120.329 1.00 35.43  ? 808  ASN A N   1 
ATOM   6423  C  CA  . ASN A 1 1237 ? 143.259 115.109 120.402 1.00 35.94  ? 808  ASN A CA  1 
ATOM   6424  C  C   . ASN A 1 1237 ? 143.315 116.205 119.354 1.00 42.71  ? 808  ASN A C   1 
ATOM   6425  O  O   . ASN A 1 1237 ? 144.367 116.483 118.774 1.00 50.30  ? 808  ASN A O   1 
ATOM   6426  C  CB  . ASN A 1 1237 ? 144.471 114.192 120.257 1.00 33.46  ? 808  ASN A CB  1 
ATOM   6427  C  CG  . ASN A 1 1237 ? 144.567 113.202 121.371 1.00 50.59  ? 808  ASN A CG  1 
ATOM   6428  O  OD1 . ASN A 1 1237 ? 144.668 113.583 122.538 1.00 55.80  ? 808  ASN A OD1 1 
ATOM   6429  N  ND2 . ASN A 1 1237 ? 144.504 111.918 121.040 1.00 57.05  ? 808  ASN A ND2 1 
ATOM   6430  N  N   . GLY A 1 1238 ? 142.171 116.820 119.082 1.00 45.82  ? 809  GLY A N   1 
ATOM   6431  C  CA  . GLY A 1 1238 ? 142.121 117.901 118.119 1.00 53.20  ? 809  GLY A CA  1 
ATOM   6432  C  C   . GLY A 1 1238 ? 142.061 117.493 116.654 1.00 45.83  ? 809  GLY A C   1 
ATOM   6433  O  O   . GLY A 1 1238 ? 141.948 118.370 115.791 1.00 47.85  ? 809  GLY A O   1 
ATOM   6434  N  N   . VAL A 1 1239 ? 142.143 116.216 116.331 1.00 32.51  ? 810  VAL A N   1 
ATOM   6435  C  CA  . VAL A 1 1239 ? 141.869 115.783 114.980 1.00 21.73  ? 810  VAL A CA  1 
ATOM   6436  C  C   . VAL A 1 1239 ? 140.373 115.625 114.882 1.00 33.24  ? 810  VAL A C   1 
ATOM   6437  O  O   . VAL A 1 1239 ? 139.771 114.931 115.708 1.00 41.34  ? 810  VAL A O   1 
ATOM   6438  C  CB  . VAL A 1 1239 ? 142.566 114.468 114.679 1.00 23.10  ? 810  VAL A CB  1 
ATOM   6439  C  CG1 . VAL A 1 1239 ? 142.172 114.016 113.283 1.00 35.63  ? 810  VAL A CG1 1 
ATOM   6440  C  CG2 . VAL A 1 1239 ? 144.018 114.676 114.818 1.00 34.11  ? 810  VAL A CG2 1 
ATOM   6441  N  N   . GLN A 1 1240 ? 139.754 116.284 113.914 1.00 29.06  ? 811  GLN A N   1 
ATOM   6442  C  CA  . GLN A 1 1240 ? 138.308 116.241 113.860 1.00 24.15  ? 811  GLN A CA  1 
ATOM   6443  C  C   . GLN A 1 1240 ? 137.843 114.915 113.292 1.00 26.19  ? 811  GLN A C   1 
ATOM   6444  O  O   . GLN A 1 1240 ? 138.328 114.471 112.250 1.00 35.80  ? 811  GLN A O   1 
ATOM   6445  C  CB  . GLN A 1 1240 ? 137.767 117.400 113.054 1.00 30.47  ? 811  GLN A CB  1 
ATOM   6446  C  CG  . GLN A 1 1240 ? 136.264 117.401 113.026 1.00 41.23  ? 811  GLN A CG  1 
ATOM   6447  C  CD  . GLN A 1 1240 ? 135.724 118.645 112.375 1.00 49.43  ? 811  GLN A CD  1 
ATOM   6448  O  OE1 . GLN A 1 1240 ? 136.461 119.618 112.185 1.00 48.82  ? 811  GLN A OE1 1 
ATOM   6449  N  NE2 . GLN A 1 1240 ? 134.440 118.627 112.014 1.00 53.41  ? 811  GLN A NE2 1 
ATOM   6450  N  N   . LEU A 1 1241 ? 136.983 114.288 113.977 1.00 22.00  ? 812  LEU A N   1 
ATOM   6451  C  CA  . LEU A 1 1241 ? 136.482 113.039 113.458 1.00 22.35  ? 812  LEU A CA  1 
ATOM   6452  C  C   . LEU A 1 1241 ? 135.238 113.293 112.622 1.00 29.52  ? 812  LEU A C   1 
ATOM   6453  O  O   . LEU A 1 1241 ? 134.487 114.233 112.891 1.00 42.73  ? 812  LEU A O   1 
ATOM   6454  C  CB  . LEU A 1 1241 ? 136.122 112.104 114.595 1.00 28.64  ? 812  LEU A CB  1 
ATOM   6455  C  CG  . LEU A 1 1241 ? 137.119 111.899 115.717 1.00 32.03  ? 812  LEU A CG  1 
ATOM   6456  C  CD1 . LEU A 1 1241 ? 136.522 110.916 116.722 1.00 38.47  ? 812  LEU A CD1 1 
ATOM   6457  C  CD2 . LEU A 1 1241 ? 138.443 111.388 115.167 1.00 38.27  ? 812  LEU A CD2 1 
ATOM   6458  N  N   . PRO A 1 1242 ? 134.969 112.477 111.617 1.00 16.65  ? 813  PRO A N   1 
ATOM   6459  C  CA  . PRO A 1 1242 ? 133.786 112.681 110.790 1.00 18.61  ? 813  PRO A CA  1 
ATOM   6460  C  C   . PRO A 1 1242 ? 132.565 112.009 111.373 1.00 27.32  ? 813  PRO A C   1 
ATOM   6461  O  O   . PRO A 1 1242 ? 132.626 110.870 111.836 1.00 40.59  ? 813  PRO A O   1 
ATOM   6462  C  CB  . PRO A 1 1242 ? 134.161 111.965 109.500 1.00 25.90  ? 813  PRO A CB  1 
ATOM   6463  C  CG  . PRO A 1 1242 ? 135.025 110.864 109.975 1.00 25.55  ? 813  PRO A CG  1 
ATOM   6464  C  CD  . PRO A 1 1242 ? 135.794 111.384 111.131 1.00 20.04  ? 813  PRO A CD  1 
ATOM   6465  N  N   . GLN A 1 1243 ? 131.425 112.696 111.314 1.00 29.01  ? 814  GLN A N   1 
ATOM   6466  C  CA  . GLN A 1 1243 ? 130.137 112.038 111.549 1.00 30.44  ? 814  GLN A CA  1 
ATOM   6467  C  C   . GLN A 1 1243 ? 129.292 112.400 110.342 1.00 35.58  ? 814  GLN A C   1 
ATOM   6468  O  O   . GLN A 1 1243 ? 128.436 113.284 110.381 1.00 43.82  ? 814  GLN A O   1 
ATOM   6469  C  CB  . GLN A 1 1243 ? 129.483 112.466 112.880 1.00 45.57  ? 814  GLN A CB  1 
ATOM   6470  C  CG  . GLN A 1 1243 ? 129.216 113.971 113.045 1.00 55.12  ? 814  GLN A CG  1 
ATOM   6471  C  CD  . GLN A 1 1243 ? 130.481 114.796 113.098 1.00 63.83  ? 814  GLN A CD  1 
ATOM   6472  O  OE1 . GLN A 1 1243 ? 131.587 114.244 113.163 1.00 56.15  ? 814  GLN A OE1 1 
ATOM   6473  N  NE2 . GLN A 1 1243 ? 130.336 116.127 113.020 1.00 62.29  ? 814  GLN A NE2 1 
ATOM   6474  N  N   . SER A 1 1244 ? 129.512 111.689 109.248 1.00 32.60  ? 815  SER A N   1 
ATOM   6475  C  CA  . SER A 1 1244 ? 128.756 112.024 108.058 1.00 26.32  ? 815  SER A CA  1 
ATOM   6476  C  C   . SER A 1 1244 ? 127.407 111.347 108.038 1.00 27.61  ? 815  SER A C   1 
ATOM   6477  O  O   . SER A 1 1244 ? 126.425 111.955 107.613 1.00 34.59  ? 815  SER A O   1 
ATOM   6478  C  CB  . SER A 1 1244 ? 129.515 111.623 106.815 1.00 28.40  ? 815  SER A CB  1 
ATOM   6479  O  OG  . SER A 1 1244 ? 128.721 111.930 105.687 1.00 36.61  ? 815  SER A OG  1 
ATOM   6480  N  N   . LEU A 1 1245 ? 127.329 110.107 108.503 1.00 28.63  ? 816  LEU A N   1 
ATOM   6481  C  CA  . LEU A 1 1245 ? 126.113 109.348 108.279 1.00 30.02  ? 816  LEU A CA  1 
ATOM   6482  C  C   . LEU A 1 1245 ? 124.907 109.929 109.000 1.00 33.16  ? 816  LEU A C   1 
ATOM   6483  O  O   . LEU A 1 1245 ? 123.778 109.580 108.640 1.00 41.59  ? 816  LEU A O   1 
ATOM   6484  C  CB  . LEU A 1 1245 ? 126.290 107.875 108.678 1.00 33.98  ? 816  LEU A CB  1 
ATOM   6485  C  CG  . LEU A 1 1245 ? 127.353 107.103 107.896 1.00 34.69  ? 816  LEU A CG  1 
ATOM   6486  C  CD1 . LEU A 1 1245 ? 127.391 105.617 108.269 1.00 36.83  ? 816  LEU A CD1 1 
ATOM   6487  C  CD2 . LEU A 1 1245 ? 127.104 107.279 106.415 1.00 31.41  ? 816  LEU A CD2 1 
ATOM   6488  N  N   . LYS A 1 1246 ? 125.085 110.788 110.000 1.00 25.25  ? 817  LYS A N   1 
ATOM   6489  C  CA  . LYS A 1 1246 ? 123.883 111.212 110.705 1.00 27.72  ? 817  LYS A CA  1 
ATOM   6490  C  C   . LYS A 1 1246 ? 123.012 112.123 109.851 1.00 37.24  ? 817  LYS A C   1 
ATOM   6491  O  O   . LYS A 1 1246 ? 121.819 112.265 110.141 1.00 44.31  ? 817  LYS A O   1 
ATOM   6492  C  CB  . LYS A 1 1246 ? 124.242 111.882 112.024 1.00 37.74  ? 817  LYS A CB  1 
ATOM   6493  C  CG  . LYS A 1 1246 ? 124.854 113.256 111.852 1.00 58.93  ? 817  LYS A CG  1 
ATOM   6494  C  CD  . LYS A 1 1246 ? 125.251 113.887 113.184 1.00 62.62  ? 817  LYS A CD  1 
ATOM   6495  C  CE  . LYS A 1 1246 ? 124.096 113.837 114.169 1.00 69.32  ? 817  LYS A CE  1 
ATOM   6496  N  NZ  . LYS A 1 1246 ? 122.899 114.514 113.589 1.00 68.32  ? 817  LYS A NZ  1 
ATOM   6497  N  N   . THR A 1 1247 ? 123.572 112.731 108.798 1.00 36.38  ? 818  THR A N   1 
ATOM   6498  C  CA  . THR A 1 1247 ? 122.806 113.505 107.823 1.00 32.61  ? 818  THR A CA  1 
ATOM   6499  C  C   . THR A 1 1247 ? 122.739 112.860 106.456 1.00 33.48  ? 818  THR A C   1 
ATOM   6500  O  O   . THR A 1 1247 ? 121.817 113.153 105.691 1.00 39.51  ? 818  THR A O   1 
ATOM   6501  C  CB  . THR A 1 1247 ? 123.407 114.898 107.631 1.00 32.42  ? 818  THR A CB  1 
ATOM   6502  O  OG1 . THR A 1 1247 ? 124.790 114.763 107.283 1.00 35.60  ? 818  THR A OG1 1 
ATOM   6503  C  CG2 . THR A 1 1247 ? 123.269 115.736 108.899 1.00 45.23  ? 818  THR A CG2 1 
ATOM   6504  N  N   . ALA A 1 1248 ? 123.718 112.027 106.116 1.00 28.83  ? 819  ALA A N   1 
ATOM   6505  C  CA  . ALA A 1 1248 ? 123.713 111.403 104.806 1.00 22.76  ? 819  ALA A CA  1 
ATOM   6506  C  C   . ALA A 1 1248 ? 122.693 110.295 104.721 1.00 25.82  ? 819  ALA A C   1 
ATOM   6507  O  O   . ALA A 1 1248 ? 122.202 110.017 103.625 1.00 37.09  ? 819  ALA A O   1 
ATOM   6508  C  CB  . ALA A 1 1248 ? 125.093 110.862 104.463 1.00 29.26  ? 819  ALA A CB  1 
ATOM   6509  N  N   . THR A 1 1249 ? 122.353 109.652 105.842 1.00 25.08  ? 820  THR A N   1 
ATOM   6510  C  CA  . THR A 1 1249 ? 121.356 108.585 105.820 1.00 26.09  ? 820  THR A CA  1 
ATOM   6511  C  C   . THR A 1 1249 ? 119.948 109.094 106.031 1.00 30.91  ? 820  THR A C   1 
ATOM   6512  O  O   . THR A 1 1249 ? 119.007 108.302 106.019 1.00 43.76  ? 820  THR A O   1 
ATOM   6513  C  CB  . THR A 1 1249 ? 121.614 107.523 106.883 1.00 23.08  ? 820  THR A CB  1 
ATOM   6514  O  OG1 . THR A 1 1249 ? 121.629 108.143 108.167 1.00 30.88  ? 820  THR A OG1 1 
ATOM   6515  C  CG2 . THR A 1 1249 ? 122.927 106.859 106.645 1.00 29.21  ? 820  THR A CG2 1 
ATOM   6516  N  N   . ARG A 1 1250 ? 119.766 110.373 106.234 1.00 33.78  ? 821  ARG A N   1 
ATOM   6517  C  CA  . ARG A 1 1250 ? 118.404 110.858 106.287 1.00 41.59  ? 821  ARG A CA  1 
ATOM   6518  C  C   . ARG A 1 1250 ? 117.834 111.205 104.906 1.00 47.22  ? 821  ARG A C   1 
ATOM   6519  O  O   . ARG A 1 1250 ? 116.657 111.568 104.819 1.00 57.90  ? 821  ARG A O   1 
ATOM   6520  C  CB  . ARG A 1 1250 ? 118.357 112.065 107.222 1.00 59.08  ? 821  ARG A CB  1 
ATOM   6521  C  CG  . ARG A 1 1250 ? 118.717 111.717 108.674 1.00 59.71  ? 821  ARG A CG  1 
ATOM   6522  C  CD  . ARG A 1 1250 ? 117.681 110.769 109.293 1.00 71.04  ? 821  ARG A CD  1 
ATOM   6523  N  NE  . ARG A 1 1250 ? 116.339 111.374 109.274 1.00 85.34  ? 821  ARG A NE  1 
ATOM   6524  C  CZ  . ARG A 1 1250 ? 115.217 110.783 109.693 1.00 87.00  ? 821  ARG A CZ  1 
ATOM   6525  N  NH1 . ARG A 1 1250 ? 115.253 109.551 110.198 1.00 84.34  ? 821  ARG A NH1 1 
ATOM   6526  N  NH2 . ARG A 1 1250 ? 114.053 111.431 109.614 1.00 76.38  ? 821  ARG A NH2 1 
ATOM   6527  N  N   . MET A 1 1251 ? 118.618 111.110 103.832 1.00 34.56  ? 822  MET A N   1 
ATOM   6528  C  CA  . MET A 1 1251 ? 118.107 111.438 102.511 1.00 25.49  ? 822  MET A CA  1 
ATOM   6529  C  C   . MET A 1 1251 ? 117.036 110.454 102.094 1.00 39.69  ? 822  MET A C   1 
ATOM   6530  O  O   . MET A 1 1251 ? 117.149 109.252 102.347 1.00 43.82  ? 822  MET A O   1 
ATOM   6531  C  CB  . MET A 1 1251 ? 119.216 111.408 101.497 1.00 21.21  ? 822  MET A CB  1 
ATOM   6532  C  CG  . MET A 1 1251 ? 120.335 112.210 101.936 1.00 27.68  ? 822  MET A CG  1 
ATOM   6533  S  SD  . MET A 1 1251 ? 121.652 112.180 100.740 1.00 32.18  ? 822  MET A SD  1 
ATOM   6534  C  CE  . MET A 1 1251 ? 122.897 113.021 101.725 1.00 39.20  ? 822  MET A CE  1 
ATOM   6535  N  N   . ALA A 1 1252 ? 115.996 110.965 101.440 1.00 37.64  ? 823  ALA A N   1 
ATOM   6536  C  CA  . ALA A 1 1252 ? 114.857 110.124 101.101 1.00 36.52  ? 823  ALA A CA  1 
ATOM   6537  C  C   . ALA A 1 1252 ? 114.020 110.821 100.054 1.00 35.69  ? 823  ALA A C   1 
ATOM   6538  O  O   . ALA A 1 1252 ? 113.926 112.053 100.055 1.00 46.33  ? 823  ALA A O   1 
ATOM   6539  C  CB  . ALA A 1 1252 ? 113.998 109.820 102.334 1.00 47.41  ? 823  ALA A CB  1 
ATOM   6540  N  N   . PRO A 1 1253 ? 113.396 110.066 99.160  1.00 29.59  ? 824  PRO A N   1 
ATOM   6541  C  CA  . PRO A 1 1253 ? 112.544 110.668 98.132  1.00 34.58  ? 824  PRO A CA  1 
ATOM   6542  C  C   . PRO A 1 1253 ? 111.330 111.363 98.688  1.00 37.53  ? 824  PRO A C   1 
ATOM   6543  O  O   . PRO A 1 1253 ? 110.725 112.196 98.002  1.00 42.15  ? 824  PRO A O   1 
ATOM   6544  C  CB  . PRO A 1 1253 ? 112.104 109.464 97.302  1.00 39.60  ? 824  PRO A CB  1 
ATOM   6545  C  CG  . PRO A 1 1253 ? 112.269 108.322 98.226  1.00 43.56  ? 824  PRO A CG  1 
ATOM   6546  C  CD  . PRO A 1 1253 ? 113.469 108.617 99.031  1.00 34.78  ? 824  PRO A CD  1 
ATOM   6547  N  N   . LEU A 1 1254 ? 110.902 111.013 99.873  1.00 28.65  ? 825  LEU A N   1 
ATOM   6548  C  CA  . LEU A 1 1254 ? 109.733 111.648 100.418 1.00 28.04  ? 825  LEU A CA  1 
ATOM   6549  C  C   . LEU A 1 1254 ? 110.208 112.326 101.679 1.00 42.42  ? 825  LEU A C   1 
ATOM   6550  O  O   . LEU A 1 1254 ? 110.844 111.690 102.522 1.00 51.30  ? 825  LEU A O   1 
ATOM   6551  C  CB  . LEU A 1 1254 ? 108.634 110.627 100.696 1.00 43.66  ? 825  LEU A CB  1 
ATOM   6552  C  CG  . LEU A 1 1254 ? 108.234 109.812 99.454  1.00 57.25  ? 825  LEU A CG  1 
ATOM   6553  C  CD1 . LEU A 1 1254 ? 107.081 108.767 99.708  1.00 50.49  ? 825  LEU A CD1 1 
ATOM   6554  C  CD2 . LEU A 1 1254 ? 107.934 110.742 98.264  1.00 51.20  ? 825  LEU A CD2 1 
ATOM   6555  N  N   . SER A 1 1255 ? 109.868 113.592 101.843 1.00 44.22  ? 826  SER A N   1 
ATOM   6556  C  CA  . SER A 1 1255 ? 110.212 114.337 103.042 1.00 40.22  ? 826  SER A CA  1 
ATOM   6557  C  C   . SER A 1 1255 ? 108.996 115.134 103.470 1.00 45.33  ? 826  SER A C   1 
ATOM   6558  O  O   . SER A 1 1255 ? 107.978 115.161 102.779 1.00 51.53  ? 826  SER A O   1 
ATOM   6559  C  CB  . SER A 1 1255 ? 111.365 115.288 102.771 1.00 48.13  ? 826  SER A CB  1 
ATOM   6560  O  OG  . SER A 1 1255 ? 111.471 116.246 103.806 1.00 59.57  ? 826  SER A OG  1 
ATOM   6561  N  N   . ASP A 1 1256 ? 109.070 115.799 104.612 1.00 56.78  ? 827  ASP A N   1 
ATOM   6562  C  CA  . ASP A 1 1256 ? 107.937 116.602 105.057 1.00 62.98  ? 827  ASP A CA  1 
ATOM   6563  C  C   . ASP A 1 1256 ? 107.981 118.025 104.507 1.00 51.65  ? 827  ASP A C   1 
ATOM   6564  O  O   . ASP A 1 1256 ? 108.124 118.987 105.257 1.00 54.77  ? 827  ASP A O   1 
ATOM   6565  C  CB  . ASP A 1 1256 ? 107.848 116.611 106.583 1.00 79.60  ? 827  ASP A CB  1 
ATOM   6566  C  CG  . ASP A 1 1256 ? 107.432 115.267 107.146 1.00 81.39  ? 827  ASP A CG  1 
ATOM   6567  O  OD1 . ASP A 1 1256 ? 107.030 114.391 106.350 1.00 74.89  ? 827  ASP A OD1 1 
ATOM   6568  O  OD2 . ASP A 1 1256 ? 107.506 115.087 108.379 1.00 77.07  ? 827  ASP A OD2 1 
ATOM   6569  N  N   . ALA A 1 1257 ? 107.856 118.143 103.193 1.00 45.73  ? 828  ALA A N   1 
ATOM   6570  C  CA  . ALA A 1 1257 ? 107.857 119.408 102.489 1.00 55.14  ? 828  ALA A CA  1 
ATOM   6571  C  C   . ALA A 1 1257 ? 106.461 119.994 102.525 1.00 69.83  ? 828  ALA A C   1 
ATOM   6572  O  O   . ALA A 1 1257 ? 105.512 119.316 102.903 1.00 70.90  ? 828  ALA A O   1 
ATOM   6573  C  CB  . ALA A 1 1257 ? 108.305 119.204 101.058 1.00 45.87  ? 828  ALA A CB  1 
ATOM   6574  N  N   . ILE A 1 1258 ? 106.312 121.266 102.169 1.00 72.94  ? 829  ILE A N   1 
ATOM   6575  C  CA  . ILE A 1 1258 ? 104.970 121.827 102.122 1.00 72.26  ? 829  ILE A CA  1 
ATOM   6576  C  C   . ILE A 1 1258 ? 104.306 121.065 100.983 1.00 65.47  ? 829  ILE A C   1 
ATOM   6577  O  O   . ILE A 1 1258 ? 104.893 120.938 99.897  1.00 65.85  ? 829  ILE A O   1 
ATOM   6578  C  CB  . ILE A 1 1258 ? 104.979 123.329 101.826 1.00 80.40  ? 829  ILE A CB  1 
ATOM   6579  C  CG1 . ILE A 1 1258 ? 103.600 123.921 102.105 1.00 76.30  ? 829  ILE A CG1 1 
ATOM   6580  C  CG2 . ILE A 1 1258 ? 105.406 123.587 100.389 1.00 76.93  ? 829  ILE A CG2 1 
ATOM   6581  C  CD1 . ILE A 1 1258 ? 103.051 123.550 103.464 1.00 76.54  ? 829  ILE A CD1 1 
ATOM   6582  N  N   . PHE A 1 1259 ? 103.085 120.592 101.231 1.00 64.25  ? 830  PHE A N   1 
ATOM   6583  C  CA  . PHE A 1 1259 ? 102.330 119.757 100.298 1.00 63.34  ? 830  PHE A CA  1 
ATOM   6584  C  C   . PHE A 1 1259 ? 103.259 118.595 100.012 1.00 50.46  ? 830  PHE A C   1 
ATOM   6585  O  O   . PHE A 1 1259 ? 103.688 117.907 100.933 1.00 59.52  ? 830  PHE A O   1 
ATOM   6586  C  CB  . PHE A 1 1259 ? 101.850 120.472 99.035  1.00 70.65  ? 830  PHE A CB  1 
ATOM   6587  C  CG  . PHE A 1 1259 ? 100.631 119.861 98.430  1.00 53.93  ? 830  PHE A CG  1 
ATOM   6588  C  CD1 . PHE A 1 1259 ? 99.536  119.571 99.211  1.00 52.85  ? 830  PHE A CD1 1 
ATOM   6589  C  CD2 . PHE A 1 1259 ? 100.572 119.598 97.089  1.00 43.08  ? 830  PHE A CD2 1 
ATOM   6590  C  CE1 . PHE A 1 1259 ? 98.406  119.020 98.664  1.00 44.36  ? 830  PHE A CE1 1 
ATOM   6591  C  CE2 . PHE A 1 1259 ? 99.447  119.044 96.533  1.00 46.61  ? 830  PHE A CE2 1 
ATOM   6592  C  CZ  . PHE A 1 1259 ? 98.362  118.758 97.322  1.00 45.92  ? 830  PHE A CZ  1 
ATOM   6593  N  N   . ASP A 1 1260 ? 103.518 118.315 98.751  1.00 40.18  ? 831  ASP A N   1 
ATOM   6594  C  CA  . ASP A 1 1260 ? 104.449 117.255 98.423  1.00 37.97  ? 831  ASP A CA  1 
ATOM   6595  C  C   . ASP A 1 1260 ? 105.359 117.824 97.369  1.00 31.80  ? 831  ASP A C   1 
ATOM   6596  O  O   . ASP A 1 1260 ? 105.675 117.162 96.380  1.00 38.44  ? 831  ASP A O   1 
ATOM   6597  C  CB  . ASP A 1 1260 ? 103.728 116.014 97.916  1.00 57.64  ? 831  ASP A CB  1 
ATOM   6598  C  CG  . ASP A 1 1260 ? 104.380 114.737 98.394  1.00 62.56  ? 831  ASP A CG  1 
ATOM   6599  O  OD1 . ASP A 1 1260 ? 105.139 114.804 99.384  1.00 55.30  ? 831  ASP A OD1 1 
ATOM   6600  O  OD2 . ASP A 1 1260 ? 104.133 113.672 97.790  1.00 55.43  ? 831  ASP A OD2 1 
ATOM   6601  N  N   . ASP A 1 1261 ? 105.783 119.062 97.576  1.00 32.89  ? 832  ASP A N   1 
ATOM   6602  C  CA  . ASP A 1 1261 ? 106.589 119.740 96.579  1.00 30.58  ? 832  ASP A CA  1 
ATOM   6603  C  C   . ASP A 1 1261 ? 107.860 118.997 96.273  1.00 28.28  ? 832  ASP A C   1 
ATOM   6604  O  O   . ASP A 1 1261 ? 108.536 118.507 97.166  1.00 40.74  ? 832  ASP A O   1 
ATOM   6605  C  CB  . ASP A 1 1261 ? 106.925 121.149 97.057  1.00 55.47  ? 832  ASP A CB  1 
ATOM   6606  C  CG  . ASP A 1 1261 ? 107.709 121.940 96.031  1.00 69.74  ? 832  ASP A CG  1 
ATOM   6607  O  OD1 . ASP A 1 1261 ? 107.790 121.491 94.869  1.00 54.44  ? 832  ASP A OD1 1 
ATOM   6608  O  OD2 . ASP A 1 1261 ? 108.240 123.014 96.386  1.00 64.53  ? 832  ASP A OD2 1 
ATOM   6609  N  N   . LEU A 1 1262 ? 108.157 118.881 94.986  1.00 26.61  ? 833  LEU A N   1 
ATOM   6610  C  CA  . LEU A 1 1262 ? 109.371 118.232 94.533  1.00 21.16  ? 833  LEU A CA  1 
ATOM   6611  C  C   . LEU A 1 1262 ? 110.559 119.061 94.950  1.00 32.07  ? 833  LEU A C   1 
ATOM   6612  O  O   . LEU A 1 1262 ? 111.577 118.534 95.393  1.00 42.29  ? 833  LEU A O   1 
ATOM   6613  C  CB  . LEU A 1 1262 ? 109.359 118.055 93.025  1.00 19.59  ? 833  LEU A CB  1 
ATOM   6614  C  CG  . LEU A 1 1262 ? 110.507 117.245 92.452  1.00 21.64  ? 833  LEU A CG  1 
ATOM   6615  C  CD1 . LEU A 1 1262 ? 110.575 115.871 93.098  1.00 37.64  ? 833  LEU A CD1 1 
ATOM   6616  C  CD2 . LEU A 1 1262 ? 110.358 117.131 90.949  1.00 28.18  ? 833  LEU A CD2 1 
ATOM   6617  N  N   . GLN A 1 1263 ? 110.413 120.374 94.823  1.00 36.29  ? 834  GLN A N   1 
ATOM   6618  C  CA  . GLN A 1 1263 ? 111.470 121.305 95.159  1.00 30.10  ? 834  GLN A CA  1 
ATOM   6619  C  C   . GLN A 1 1263 ? 111.809 121.210 96.621  1.00 31.00  ? 834  GLN A C   1 
ATOM   6620  O  O   . GLN A 1 1263 ? 112.977 121.225 96.988  1.00 37.99  ? 834  GLN A O   1 
ATOM   6621  C  CB  . GLN A 1 1263 ? 111.045 122.726 94.830  1.00 33.53  ? 834  GLN A CB  1 
ATOM   6622  C  CG  . GLN A 1 1263 ? 112.185 123.717 94.842  1.00 37.81  ? 834  GLN A CG  1 
ATOM   6623  C  CD  . GLN A 1 1263 ? 111.746 125.093 94.407  1.00 52.20  ? 834  GLN A CD  1 
ATOM   6624  O  OE1 . GLN A 1 1263 ? 110.607 125.493 94.638  1.00 54.87  ? 834  GLN A OE1 1 
ATOM   6625  N  NE2 . GLN A 1 1263 ? 112.649 125.829 93.781  1.00 46.48  ? 834  GLN A NE2 1 
ATOM   6626  N  N   . GLY A 1 1264 ? 110.798 121.102 97.465  1.00 30.12  ? 835  GLY A N   1 
ATOM   6627  C  CA  . GLY A 1 1264 ? 111.061 120.984 98.878  1.00 33.64  ? 835  GLY A CA  1 
ATOM   6628  C  C   . GLY A 1 1264 ? 111.826 119.712 99.166  1.00 39.84  ? 835  GLY A C   1 
ATOM   6629  O  O   . GLY A 1 1264 ? 112.771 119.719 99.947  1.00 45.24  ? 835  GLY A O   1 
ATOM   6630  N  N   . THR A 1 1265 ? 111.422 118.615 98.536  1.00 32.77  ? 836  THR A N   1 
ATOM   6631  C  CA  . THR A 1 1265 ? 112.097 117.340 98.737  1.00 28.83  ? 836  THR A CA  1 
ATOM   6632  C  C   . THR A 1 1265 ? 113.521 117.364 98.232  1.00 28.93  ? 836  THR A C   1 
ATOM   6633  O  O   . THR A 1 1265 ? 114.431 116.877 98.891  1.00 38.37  ? 836  THR A O   1 
ATOM   6634  C  CB  . THR A 1 1265 ? 111.358 116.199 98.044  1.00 27.07  ? 836  THR A CB  1 
ATOM   6635  O  OG1 . THR A 1 1265 ? 110.080 116.031 98.657  1.00 34.43  ? 836  THR A OG1 1 
ATOM   6636  C  CG2 . THR A 1 1265 ? 112.143 114.911 98.175  1.00 30.63  ? 836  THR A CG2 1 
ATOM   6637  N  N   . LEU A 1 1266 ? 113.714 117.936 97.056  1.00 24.60  ? 837  LEU A N   1 
ATOM   6638  C  CA  . LEU A 1 1266 ? 115.037 118.037 96.477  1.00 24.92  ? 837  LEU A CA  1 
ATOM   6639  C  C   . LEU A 1 1266 ? 115.917 118.951 97.313  1.00 27.77  ? 837  LEU A C   1 
ATOM   6640  O  O   . LEU A 1 1266 ? 117.098 118.689 97.487  1.00 29.20  ? 837  LEU A O   1 
ATOM   6641  C  CB  . LEU A 1 1266 ? 114.987 118.420 95.003  1.00 15.84  ? 837  LEU A CB  1 
ATOM   6642  C  CG  . LEU A 1 1266 ? 114.303 117.362 94.143  1.00 23.42  ? 837  LEU A CG  1 
ATOM   6643  C  CD1 . LEU A 1 1266 ? 114.408 117.696 92.674  1.00 33.10  ? 837  LEU A CD1 1 
ATOM   6644  C  CD2 . LEU A 1 1266 ? 114.893 115.991 94.414  1.00 33.02  ? 837  LEU A CD2 1 
ATOM   6645  N  N   . ALA A 1 1267 ? 115.340 120.024 97.836  1.00 28.31  ? 838  ALA A N   1 
ATOM   6646  C  CA  . ALA A 1 1267 ? 116.100 120.939 98.668  1.00 30.66  ? 838  ALA A CA  1 
ATOM   6647  C  C   . ALA A 1 1267 ? 116.586 120.232 99.916  1.00 35.04  ? 838  ALA A C   1 
ATOM   6648  O  O   . ALA A 1 1267 ? 117.724 120.429 100.335 1.00 42.53  ? 838  ALA A O   1 
ATOM   6649  C  CB  . ALA A 1 1267 ? 115.269 122.155 99.041  1.00 36.44  ? 838  ALA A CB  1 
ATOM   6650  N  N   . SER A 1 1268 ? 115.734 119.412 100.519 1.00 28.42  ? 839  SER A N   1 
ATOM   6651  C  CA  . SER A 1 1268 ? 116.132 118.685 101.710 1.00 24.06  ? 839  SER A CA  1 
ATOM   6652  C  C   . SER A 1 1268 ? 117.310 117.813 101.360 1.00 29.08  ? 839  SER A C   1 
ATOM   6653  O  O   . SER A 1 1268 ? 118.318 117.826 102.058 1.00 36.63  ? 839  SER A O   1 
ATOM   6654  C  CB  . SER A 1 1268 ? 114.991 117.854 102.261 1.00 30.44  ? 839  SER A CB  1 
ATOM   6655  O  OG  . SER A 1 1268 ? 113.988 118.684 102.809 1.00 39.31  ? 839  SER A OG  1 
ATOM   6656  N  N   . ILE A 1 1269 ? 117.199 117.051 100.279 1.00 27.85  ? 840  ILE A N   1 
ATOM   6657  C  CA  . ILE A 1 1269 ? 118.330 116.222 99.872  1.00 19.55  ? 840  ILE A CA  1 
ATOM   6658  C  C   . ILE A 1 1269 ? 119.570 117.075 99.625  1.00 25.59  ? 840  ILE A C   1 
ATOM   6659  O  O   . ILE A 1 1269 ? 120.688 116.675 99.962  1.00 39.03  ? 840  ILE A O   1 
ATOM   6660  C  CB  . ILE A 1 1269 ? 117.957 115.396 98.640  1.00 15.05  ? 840  ILE A CB  1 
ATOM   6661  C  CG1 . ILE A 1 1269 ? 116.862 114.415 99.013  1.00 18.96  ? 840  ILE A CG1 1 
ATOM   6662  C  CG2 . ILE A 1 1269 ? 119.150 114.689 98.110  1.00 23.33  ? 840  ILE A CG2 1 
ATOM   6663  C  CD1 . ILE A 1 1269 ? 116.490 113.503 97.885  1.00 31.20  ? 840  ILE A CD1 1 
ATOM   6664  N  N   . GLY A 1 1270 ? 119.408 118.255 99.032  1.00 26.34  ? 841  GLY A N   1 
ATOM   6665  C  CA  . GLY A 1 1270 ? 120.561 119.111 98.815  1.00 23.64  ? 841  GLY A CA  1 
ATOM   6666  C  C   . GLY A 1 1270 ? 121.172 119.570 100.116 1.00 26.01  ? 841  GLY A C   1 
ATOM   6667  O  O   . GLY A 1 1270 ? 122.396 119.638 100.247 1.00 37.34  ? 841  GLY A O   1 
ATOM   6668  N  N   . THR A 1 1271 ? 120.334 119.875 101.102 1.00 24.27  ? 842  THR A N   1 
ATOM   6669  C  CA  . THR A 1 1271 ? 120.860 120.289 102.394 1.00 24.69  ? 842  THR A CA  1 
ATOM   6670  C  C   . THR A 1 1271 ? 121.575 119.145 103.079 1.00 27.03  ? 842  THR A C   1 
ATOM   6671  O  O   . THR A 1 1271 ? 122.675 119.327 103.620 1.00 41.92  ? 842  THR A O   1 
ATOM   6672  C  CB  . THR A 1 1271 ? 119.753 120.813 103.294 1.00 26.41  ? 842  THR A CB  1 
ATOM   6673  O  OG1 . THR A 1 1271 ? 119.094 121.910 102.652 1.00 32.07  ? 842  THR A OG1 1 
ATOM   6674  C  CG2 . THR A 1 1271 ? 120.348 121.308 104.588 1.00 37.51  ? 842  THR A CG2 1 
ATOM   6675  N  N   . ALA A 1 1272 ? 120.969 117.962 103.085 1.00 24.40  ? 843  ALA A N   1 
ATOM   6676  C  CA  . ALA A 1 1272 ? 121.659 116.820 103.671 1.00 25.11  ? 843  ALA A CA  1 
ATOM   6677  C  C   . ALA A 1 1272 ? 122.976 116.548 102.952 1.00 26.85  ? 843  ALA A C   1 
ATOM   6678  O  O   . ALA A 1 1272 ? 123.953 116.133 103.583 1.00 36.61  ? 843  ALA A O   1 
ATOM   6679  C  CB  . ALA A 1 1272 ? 120.767 115.585 103.656 1.00 29.20  ? 843  ALA A CB  1 
ATOM   6680  N  N   . PHE A 1 1273 ? 123.050 116.820 101.651 1.00 23.19  ? 844  PHE A N   1 
ATOM   6681  C  CA  . PHE A 1 1273 ? 124.299 116.569 100.946 1.00 21.45  ? 844  PHE A CA  1 
ATOM   6682  C  C   . PHE A 1 1273 ? 125.367 117.584 101.292 1.00 30.32  ? 844  PHE A C   1 
ATOM   6683  O  O   . PHE A 1 1273 ? 126.548 117.228 101.422 1.00 42.44  ? 844  PHE A O   1 
ATOM   6684  C  CB  . PHE A 1 1273 ? 124.088 116.587 99.468  1.00 29.55  ? 844  PHE A CB  1 
ATOM   6685  C  CG  . PHE A 1 1273 ? 125.339 116.791 98.711  1.00 34.80  ? 844  PHE A CG  1 
ATOM   6686  C  CD1 . PHE A 1 1273 ? 126.197 115.738 98.473  1.00 40.74  ? 844  PHE A CD1 1 
ATOM   6687  C  CD2 . PHE A 1 1273 ? 125.650 118.043 98.198  1.00 44.86  ? 844  PHE A CD2 1 
ATOM   6688  C  CE1 . PHE A 1 1273 ? 127.367 115.933 97.736  1.00 45.66  ? 844  PHE A CE1 1 
ATOM   6689  C  CE2 . PHE A 1 1273 ? 126.805 118.253 97.457  1.00 49.05  ? 844  PHE A CE2 1 
ATOM   6690  C  CZ  . PHE A 1 1273 ? 127.667 117.198 97.227  1.00 46.92  ? 844  PHE A CZ  1 
ATOM   6691  N  N   . GLU A 1 1274 ? 124.991 118.853 101.425 1.00 33.32  ? 845  GLU A N   1 
ATOM   6692  C  CA  . GLU A 1 1274 ? 125.967 119.857 101.852 1.00 29.63  ? 845  GLU A CA  1 
ATOM   6693  C  C   . GLU A 1 1274 ? 126.508 119.523 103.221 1.00 27.40  ? 845  GLU A C   1 
ATOM   6694  O  O   . GLU A 1 1274 ? 127.727 119.496 103.432 1.00 40.46  ? 845  GLU A O   1 
ATOM   6695  C  CB  . GLU A 1 1274 ? 125.333 121.233 101.895 1.00 43.84  ? 845  GLU A CB  1 
ATOM   6696  C  CG  . GLU A 1 1274 ? 124.942 121.719 100.520 1.00 63.13  ? 845  GLU A CG  1 
ATOM   6697  C  CD  . GLU A 1 1274 ? 124.213 123.048 100.569 1.00 75.03  ? 845  GLU A CD  1 
ATOM   6698  O  OE1 . GLU A 1 1274 ? 124.196 123.672 101.661 1.00 70.40  ? 845  GLU A OE1 1 
ATOM   6699  O  OE2 . GLU A 1 1274 ? 123.617 123.437 99.534  1.00 69.48  ? 845  GLU A OE2 1 
ATOM   6700  N  N   . ARG A 1 1275 ? 125.616 119.239 104.167 1.00 21.55  ? 846  ARG A N   1 
ATOM   6701  C  CA  . ARG A 1 1275 ? 126.096 118.955 105.506 1.00 21.98  ? 846  ARG A CA  1 
ATOM   6702  C  C   . ARG A 1 1275 ? 126.968 117.706 105.536 1.00 32.21  ? 846  ARG A C   1 
ATOM   6703  O  O   . ARG A 1 1275 ? 128.047 117.702 106.161 1.00 43.32  ? 846  ARG A O   1 
ATOM   6704  C  CB  . ARG A 1 1275 ? 124.935 118.817 106.455 1.00 27.28  ? 846  ARG A CB  1 
ATOM   6705  C  CG  . ARG A 1 1275 ? 124.190 120.089 106.577 1.00 41.13  ? 846  ARG A CG  1 
ATOM   6706  C  CD  . ARG A 1 1275 ? 123.052 119.930 107.565 1.00 61.70  ? 846  ARG A CD  1 
ATOM   6707  N  NE  . ARG A 1 1275 ? 122.331 121.183 107.773 1.00 66.89  ? 846  ARG A NE  1 
ATOM   6708  C  CZ  . ARG A 1 1275 ? 121.290 121.313 108.588 1.00 73.02  ? 846  ARG A CZ  1 
ATOM   6709  N  NH1 . ARG A 1 1275 ? 120.855 120.265 109.279 1.00 77.27  ? 846  ARG A NH1 1 
ATOM   6710  N  NH2 . ARG A 1 1275 ? 120.689 122.490 108.716 1.00 71.29  ? 846  ARG A NH2 1 
ATOM   6711  N  N   . SER A 1 1276 ? 126.555 116.641 104.851 1.00 23.18  ? 847  SER A N   1 
ATOM   6712  C  CA  . SER A 1 1276 ? 127.340 115.426 104.953 1.00 20.11  ? 847  SER A CA  1 
ATOM   6713  C  C   . SER A 1 1276 ? 128.708 115.608 104.338 1.00 24.64  ? 847  SER A C   1 
ATOM   6714  O  O   . SER A 1 1276 ? 129.694 115.114 104.887 1.00 38.62  ? 847  SER A O   1 
ATOM   6715  C  CB  . SER A 1 1276 ? 126.631 114.266 104.299 1.00 30.74  ? 847  SER A CB  1 
ATOM   6716  O  OG  . SER A 1 1276 ? 126.421 114.552 102.935 1.00 36.71  ? 847  SER A OG  1 
ATOM   6717  N  N   . ILE A 1 1277 ? 128.814 116.318 103.215 1.00 24.42  ? 848  ILE A N   1 
ATOM   6718  C  CA  . ILE A 1 1277 ? 130.152 116.641 102.722 1.00 23.41  ? 848  ILE A CA  1 
ATOM   6719  C  C   . ILE A 1 1277 ? 130.960 117.362 103.785 1.00 28.44  ? 848  ILE A C   1 
ATOM   6720  O  O   . ILE A 1 1277 ? 132.138 117.051 103.997 1.00 32.09  ? 848  ILE A O   1 
ATOM   6721  C  CB  . ILE A 1 1277 ? 130.079 117.478 101.446 1.00 21.93  ? 848  ILE A CB  1 
ATOM   6722  C  CG1 . ILE A 1 1277 ? 129.500 116.628 100.347 1.00 35.75  ? 848  ILE A CG1 1 
ATOM   6723  C  CG2 . ILE A 1 1277 ? 131.436 117.947 101.096 1.00 29.34  ? 848  ILE A CG2 1 
ATOM   6724  C  CD1 . ILE A 1 1277 ? 130.256 115.323 100.228 1.00 49.58  ? 848  ILE A CD1 1 
ATOM   6725  N  N   . SER A 1 1278 ? 130.334 118.311 104.500 1.00 33.48  ? 849  SER A N   1 
ATOM   6726  C  CA  . SER A 1 1278 ? 131.092 119.093 105.480 1.00 34.68  ? 849  SER A CA  1 
ATOM   6727  C  C   . SER A 1 1278 ? 131.754 118.216 106.497 1.00 28.77  ? 849  SER A C   1 
ATOM   6728  O  O   . SER A 1 1278 ? 132.865 118.506 106.946 1.00 39.14  ? 849  SER A O   1 
ATOM   6729  C  CB  . SER A 1 1278 ? 130.238 120.138 106.232 1.00 43.11  ? 849  SER A CB  1 
ATOM   6730  O  OG  . SER A 1 1278 ? 129.260 119.590 107.134 1.00 45.09  ? 849  SER A OG  1 
ATOM   6731  N  N   . GLU A 1 1279 ? 131.052 117.232 106.978 1.00 29.12  ? 850  GLU A N   1 
ATOM   6732  C  CA  . GLU A 1 1279 ? 131.562 116.560 108.147 1.00 27.38  ? 850  GLU A CA  1 
ATOM   6733  C  C   . GLU A 1 1279 ? 132.085 115.190 107.784 1.00 27.32  ? 850  GLU A C   1 
ATOM   6734  O  O   . GLU A 1 1279 ? 131.848 114.226 108.497 1.00 36.52  ? 850  GLU A O   1 
ATOM   6735  C  CB  . GLU A 1 1279 ? 130.499 116.527 109.229 1.00 40.05  ? 850  GLU A CB  1 
ATOM   6736  C  CG  . GLU A 1 1279 ? 129.131 116.047 108.723 1.00 58.00  ? 850  GLU A CG  1 
ATOM   6737  C  CD  . GLU A 1 1279 ? 127.943 116.553 109.588 1.00 67.02  ? 850  GLU A CD  1 
ATOM   6738  O  OE1 . GLU A 1 1279 ? 128.203 117.243 110.602 1.00 70.79  ? 850  GLU A OE1 1 
ATOM   6739  O  OE2 . GLU A 1 1279 ? 126.761 116.246 109.267 1.00 52.22  ? 850  GLU A OE2 1 
ATOM   6740  N  N   . THR A 1 1280 ? 132.800 115.094 106.667 1.00 29.99  ? 851  THR A N   1 
ATOM   6741  C  CA  . THR A 1 1280 ? 133.552 113.889 106.343 1.00 22.83  ? 851  THR A CA  1 
ATOM   6742  C  C   . THR A 1 1280 ? 134.513 114.163 105.205 1.00 28.25  ? 851  THR A C   1 
ATOM   6743  O  O   . THR A 1 1280 ? 134.383 115.150 104.480 1.00 39.39  ? 851  THR A O   1 
ATOM   6744  C  CB  . THR A 1 1280 ? 132.662 112.776 105.916 1.00 24.94  ? 851  THR A CB  1 
ATOM   6745  O  OG1 . THR A 1 1280 ? 133.416 111.563 105.982 1.00 36.29  ? 851  THR A OG1 1 
ATOM   6746  C  CG2 . THR A 1 1280 ? 132.255 113.037 104.489 1.00 35.64  ? 851  THR A CG2 1 
ATOM   6747  N  N   . ARG A 1 1281 ? 135.453 113.260 105.026 1.00 23.95  ? 852  ARG A N   1 
ATOM   6748  C  CA  . ARG A 1 1281 ? 136.468 113.494 104.026 1.00 25.83  ? 852  ARG A CA  1 
ATOM   6749  C  C   . ARG A 1 1281 ? 136.185 112.774 102.725 1.00 45.39  ? 852  ARG A C   1 
ATOM   6750  O  O   . ARG A 1 1281 ? 137.077 112.688 101.873 1.00 52.76  ? 852  ARG A O   1 
ATOM   6751  C  CB  . ARG A 1 1281 ? 137.850 113.106 104.546 1.00 33.70  ? 852  ARG A CB  1 
ATOM   6752  C  CG  . ARG A 1 1281 ? 138.164 111.601 104.590 1.00 46.50  ? 852  ARG A CG  1 
ATOM   6753  C  CD  . ARG A 1 1281 ? 139.673 111.323 104.838 1.00 41.35  ? 852  ARG A CD  1 
ATOM   6754  N  NE  . ARG A 1 1281 ? 139.956 109.900 104.933 1.00 32.16  ? 852  ARG A NE  1 
ATOM   6755  C  CZ  . ARG A 1 1281 ? 140.389 109.157 103.932 1.00 28.28  ? 852  ARG A CZ  1 
ATOM   6756  N  NH1 . ARG A 1 1281 ? 140.562 109.690 102.747 1.00 36.44  ? 852  ARG A NH1 1 
ATOM   6757  N  NH2 . ARG A 1 1281 ? 140.616 107.874 104.117 1.00 35.11  ? 852  ARG A NH2 1 
ATOM   6758  N  N   . HIS A 1 1282 ? 134.978 112.257 102.535 1.00 45.51  ? 853  HIS A N   1 
ATOM   6759  C  CA  . HIS A 1 1282 ? 134.640 111.545 101.307 1.00 48.04  ? 853  HIS A CA  1 
ATOM   6760  C  C   . HIS A 1 1282 ? 133.538 112.265 100.528 1.00 50.11  ? 853  HIS A C   1 
ATOM   6761  O  O   . HIS A 1 1282 ? 132.454 112.531 101.068 1.00 43.59  ? 853  HIS A O   1 
ATOM   6762  C  CB  . HIS A 1 1282 ? 134.207 110.120 101.617 1.00 49.57  ? 853  HIS A CB  1 
ATOM   6763  C  CG  . HIS A 1 1282 ? 135.311 109.254 102.116 1.00 41.50  ? 853  HIS A CG  1 
ATOM   6764  N  ND1 . HIS A 1 1282 ? 136.380 108.896 101.326 1.00 42.07  ? 853  HIS A ND1 1 
ATOM   6765  C  CD2 . HIS A 1 1282 ? 135.481 108.618 103.299 1.00 38.47  ? 853  HIS A CD2 1 
ATOM   6766  C  CE1 . HIS A 1 1282 ? 137.178 108.096 102.007 1.00 43.03  ? 853  HIS A CE1 1 
ATOM   6767  N  NE2 . HIS A 1 1282 ? 136.654 107.907 103.206 1.00 46.16  ? 853  HIS A NE2 1 
ATOM   6768  N  N   . ILE A 1 1283 ? 133.805 112.530 99.250  1.00 43.92  ? 854  ILE A N   1 
ATOM   6769  C  CA  . ILE A 1 1283 ? 132.893 113.306 98.425  1.00 27.41  ? 854  ILE A CA  1 
ATOM   6770  C  C   . ILE A 1 1283 ? 131.900 112.412 97.724  1.00 32.48  ? 854  ILE A C   1 
ATOM   6771  O  O   . ILE A 1 1283 ? 130.695 112.671 97.737  1.00 41.81  ? 854  ILE A O   1 
ATOM   6772  C  CB  . ILE A 1 1283 ? 133.673 114.136 97.399  1.00 27.94  ? 854  ILE A CB  1 
ATOM   6773  C  CG1 . ILE A 1 1283 ? 134.688 115.006 98.090  1.00 43.17  ? 854  ILE A CG1 1 
ATOM   6774  C  CG2 . ILE A 1 1283 ? 132.737 115.063 96.701  1.00 41.63  ? 854  ILE A CG2 1 
ATOM   6775  C  CD1 . ILE A 1 1283 ? 135.428 115.871 97.108  1.00 50.37  ? 854  ILE A CD1 1 
ATOM   6776  N  N   . PHE A 1 1284 ? 132.378 111.377 97.093  1.00 30.13  ? 855  PHE A N   1 
ATOM   6777  C  CA  . PHE A 1 1284 ? 131.499 110.656 96.201  1.00 26.86  ? 855  PHE A CA  1 
ATOM   6778  C  C   . PHE A 1 1284 ? 130.460 109.779 96.889  1.00 28.28  ? 855  PHE A C   1 
ATOM   6779  O  O   . PHE A 1 1284 ? 129.416 109.536 96.280  1.00 40.87  ? 855  PHE A O   1 
ATOM   6780  C  CB  . PHE A 1 1284 ? 132.310 109.827 95.238  1.00 33.31  ? 855  PHE A CB  1 
ATOM   6781  C  CG  . PHE A 1 1284 ? 132.803 110.634 94.117  1.00 34.85  ? 855  PHE A CG  1 
ATOM   6782  C  CD1 . PHE A 1 1284 ? 131.957 111.018 93.113  1.00 42.39  ? 855  PHE A CD1 1 
ATOM   6783  C  CD2 . PHE A 1 1284 ? 134.120 111.026 94.076  1.00 41.54  ? 855  PHE A CD2 1 
ATOM   6784  C  CE1 . PHE A 1 1284 ? 132.419 111.786 92.075  1.00 52.03  ? 855  PHE A CE1 1 
ATOM   6785  C  CE2 . PHE A 1 1284 ? 134.603 111.785 93.055  1.00 46.13  ? 855  PHE A CE2 1 
ATOM   6786  C  CZ  . PHE A 1 1284 ? 133.754 112.172 92.043  1.00 54.03  ? 855  PHE A CZ  1 
ATOM   6787  N  N   . PRO A 1 1285 ? 130.681 109.238 98.089  1.00 23.02  ? 856  PRO A N   1 
ATOM   6788  C  CA  . PRO A 1 1285 ? 129.607 108.448 98.689  1.00 22.50  ? 856  PRO A CA  1 
ATOM   6789  C  C   . PRO A 1 1285 ? 128.333 109.243 98.841  1.00 35.11  ? 856  PRO A C   1 
ATOM   6790  O  O   . PRO A 1 1285 ? 127.263 108.797 98.388  1.00 42.73  ? 856  PRO A O   1 
ATOM   6791  C  CB  . PRO A 1 1285 ? 130.179 108.056 100.046 1.00 28.93  ? 856  PRO A CB  1 
ATOM   6792  C  CG  . PRO A 1 1285 ? 131.587 108.018 99.855  1.00 32.31  ? 856  PRO A CG  1 
ATOM   6793  C  CD  . PRO A 1 1285 ? 131.891 109.150 98.913  1.00 35.97  ? 856  PRO A CD  1 
ATOM   6794  N  N   . CYS A 1 1286 ? 128.414 110.432 99.451  1.00 35.02  ? 857  CYS A N   1 
ATOM   6795  C  CA  . CYS A 1 1286 ? 127.208 111.237 99.660  1.00 33.04  ? 857  CYS A CA  1 
ATOM   6796  C  C   . CYS A 1 1286 ? 126.689 111.821 98.357  1.00 32.36  ? 857  CYS A C   1 
ATOM   6797  O  O   . CYS A 1 1286 ? 125.477 111.983 98.194  1.00 38.44  ? 857  CYS A O   1 
ATOM   6798  C  CB  . CYS A 1 1286 ? 127.462 112.362 100.660 1.00 39.69  ? 857  CYS A CB  1 
ATOM   6799  S  SG  . CYS A 1 1286 ? 128.019 111.810 102.323 1.00 72.12  ? 857  CYS A SG  1 
ATOM   6800  N  N   . ARG A 1 1287 ? 127.572 112.147 97.425  1.00 28.15  ? 858  ARG A N   1 
ATOM   6801  C  CA  . ARG A 1 1287 ? 127.085 112.602 96.136  1.00 26.63  ? 858  ARG A CA  1 
ATOM   6802  C  C   . ARG A 1 1287 ? 126.240 111.534 95.478  1.00 28.02  ? 858  ARG A C   1 
ATOM   6803  O  O   . ARG A 1 1287 ? 125.189 111.834 94.902  1.00 35.37  ? 858  ARG A O   1 
ATOM   6804  C  CB  . ARG A 1 1287 ? 128.257 112.980 95.241  1.00 35.61  ? 858  ARG A CB  1 
ATOM   6805  C  CG  . ARG A 1 1287 ? 127.813 113.511 93.932  1.00 33.42  ? 858  ARG A CG  1 
ATOM   6806  C  CD  . ARG A 1 1287 ? 127.299 114.883 94.109  1.00 25.76  ? 858  ARG A CD  1 
ATOM   6807  N  NE  . ARG A 1 1287 ? 127.038 115.438 92.810  1.00 21.94  ? 858  ARG A NE  1 
ATOM   6808  C  CZ  . ARG A 1 1287 ? 126.644 116.675 92.623  1.00 27.63  ? 858  ARG A CZ  1 
ATOM   6809  N  NH1 . ARG A 1 1287 ? 126.451 117.454 93.679  1.00 37.62  ? 858  ARG A NH1 1 
ATOM   6810  N  NH2 . ARG A 1 1287 ? 126.424 117.124 91.393  1.00 32.03  ? 858  ARG A NH2 1 
ATOM   6811  N  N   . ILE A 1 1288 ? 126.677 110.277 95.559  1.00 24.18  ? 859  ILE A N   1 
ATOM   6812  C  CA  . ILE A 1 1288 ? 125.923 109.189 94.960  1.00 16.68  ? 859  ILE A CA  1 
ATOM   6813  C  C   . ILE A 1 1288 ? 124.594 109.006 95.668  1.00 23.85  ? 859  ILE A C   1 
ATOM   6814  O  O   . ILE A 1 1288 ? 123.558 108.817 95.019  1.00 32.54  ? 859  ILE A O   1 
ATOM   6815  C  CB  . ILE A 1 1288 ? 126.745 107.905 94.977  1.00 19.64  ? 859  ILE A CB  1 
ATOM   6816  C  CG1 . ILE A 1 1288 ? 127.877 108.073 93.999  1.00 29.76  ? 859  ILE A CG1 1 
ATOM   6817  C  CG2 . ILE A 1 1288 ? 125.878 106.734 94.586  1.00 34.18  ? 859  ILE A CG2 1 
ATOM   6818  C  CD1 . ILE A 1 1288 ? 127.363 108.272 92.628  1.00 37.96  ? 859  ILE A CD1 1 
ATOM   6819  N  N   . THR A 1 1289 ? 124.582 109.073 96.999  1.00 21.78  ? 860  THR A N   1 
ATOM   6820  C  CA  . THR A 1 1289 ? 123.311 108.896 97.705  1.00 21.25  ? 860  THR A CA  1 
ATOM   6821  C  C   . THR A 1 1289 ? 122.325 110.033 97.403  1.00 26.56  ? 860  THR A C   1 
ATOM   6822  O  O   . THR A 1 1289 ? 121.121 109.794 97.223  1.00 32.85  ? 860  THR A O   1 
ATOM   6823  C  CB  . THR A 1 1289 ? 123.548 108.766 99.207  1.00 27.05  ? 860  THR A CB  1 
ATOM   6824  O  OG1 . THR A 1 1289 ? 124.466 107.697 99.455  1.00 30.02  ? 860  THR A OG1 1 
ATOM   6825  C  CG2 . THR A 1 1289 ? 122.268 108.468 99.929  1.00 34.52  ? 860  THR A CG2 1 
ATOM   6826  N  N   . ALA A 1 1290 ? 122.807 111.270 97.303  1.00 28.48  ? 861  ALA A N   1 
ATOM   6827  C  CA  . ALA A 1 1290 ? 121.900 112.380 96.999  1.00 30.84  ? 861  ALA A CA  1 
ATOM   6828  C  C   . ALA A 1 1290 ? 121.426 112.353 95.545  1.00 22.74  ? 861  ALA A C   1 
ATOM   6829  O  O   . ALA A 1 1290 ? 120.278 112.699 95.269  1.00 29.73  ? 861  ALA A O   1 
ATOM   6830  C  CB  . ALA A 1 1290 ? 122.562 113.727 97.324  1.00 42.44  ? 861  ALA A CB  1 
ATOM   6831  N  N   . ALA A 1 1291 ? 122.278 111.968 94.599  1.00 17.91  ? 862  ALA A N   1 
ATOM   6832  C  CA  . ALA A 1 1291 ? 121.794 111.826 93.235  1.00 16.69  ? 862  ALA A CA  1 
ATOM   6833  C  C   . ALA A 1 1291 ? 120.713 110.771 93.165  1.00 20.10  ? 862  ALA A C   1 
ATOM   6834  O  O   . ALA A 1 1291 ? 119.652 110.981 92.551  1.00 24.43  ? 862  ALA A O   1 
ATOM   6835  C  CB  . ALA A 1 1291 ? 122.939 111.438 92.314  1.00 28.28  ? 862  ALA A CB  1 
ATOM   6836  N  N   . PHE A 1 1292 ? 120.982 109.613 93.775  1.00 20.32  ? 863  PHE A N   1 
ATOM   6837  C  CA  . PHE A 1 1292 ? 120.037 108.509 93.741  1.00 18.82  ? 863  PHE A CA  1 
ATOM   6838  C  C   . PHE A 1 1292 ? 118.693 108.970 94.274  1.00 20.94  ? 863  PHE A C   1 
ATOM   6839  O  O   . PHE A 1 1292 ? 117.655 108.827 93.614  1.00 29.23  ? 863  PHE A O   1 
ATOM   6840  C  CB  . PHE A 1 1292 ? 120.577 107.353 94.580  1.00 21.56  ? 863  PHE A CB  1 
ATOM   6841  C  CG  . PHE A 1 1292 ? 119.828 106.058 94.415  1.00 22.68  ? 863  PHE A CG  1 
ATOM   6842  C  CD1 . PHE A 1 1292 ? 118.654 105.832 95.098  1.00 20.94  ? 863  PHE A CD1 1 
ATOM   6843  C  CD2 . PHE A 1 1292 ? 120.379 105.018 93.683  1.00 26.09  ? 863  PHE A CD2 1 
ATOM   6844  C  CE1 . PHE A 1 1292 ? 117.984 104.649 94.968  1.00 21.35  ? 863  PHE A CE1 1 
ATOM   6845  C  CE2 . PHE A 1 1292 ? 119.720 103.822 93.565  1.00 24.65  ? 863  PHE A CE2 1 
ATOM   6846  C  CZ  . PHE A 1 1292 ? 118.518 103.639 94.210  1.00 25.54  ? 863  PHE A CZ  1 
ATOM   6847  N  N   . HIS A 1 1293 ? 118.695 109.601 95.432  1.00 17.20  ? 864  HIS A N   1 
ATOM   6848  C  CA  . HIS A 1 1293 ? 117.410 109.988 95.973  1.00 19.53  ? 864  HIS A CA  1 
ATOM   6849  C  C   . HIS A 1 1293 ? 116.789 111.198 95.254  1.00 22.42  ? 864  HIS A C   1 
ATOM   6850  O  O   . HIS A 1 1293 ? 115.565 111.341 95.271  1.00 26.69  ? 864  HIS A O   1 
ATOM   6851  C  CB  . HIS A 1 1293 ? 117.567 110.247 97.460  1.00 31.57  ? 864  HIS A CB  1 
ATOM   6852  C  CG  . HIS A 1 1293 ? 117.732 108.998 98.254  1.00 21.27  ? 864  HIS A CG  1 
ATOM   6853  N  ND1 . HIS A 1 1293 ? 116.687 108.152 98.526  1.00 26.57  ? 864  HIS A ND1 1 
ATOM   6854  C  CD2 . HIS A 1 1293 ? 118.822 108.451 98.832  1.00 22.97  ? 864  HIS A CD2 1 
ATOM   6855  C  CE1 . HIS A 1 1293 ? 117.127 107.129 99.233  1.00 30.33  ? 864  HIS A CE1 1 
ATOM   6856  N  NE2 . HIS A 1 1293 ? 118.420 107.288 99.435  1.00 27.90  ? 864  HIS A NE2 1 
ATOM   6857  N  N   . THR A 1 1294 ? 117.579 112.065 94.614  1.00 21.89  ? 865  THR A N   1 
ATOM   6858  C  CA  . THR A 1 1294 ? 116.999 113.155 93.837  1.00 14.54  ? 865  THR A CA  1 
ATOM   6859  C  C   . THR A 1 1294 ? 116.165 112.613 92.700  1.00 20.22  ? 865  THR A C   1 
ATOM   6860  O  O   . THR A 1 1294 ? 114.982 112.960 92.540  1.00 31.52  ? 865  THR A O   1 
ATOM   6861  C  CB  . THR A 1 1294 ? 118.098 114.037 93.258  1.00 19.85  ? 865  THR A CB  1 
ATOM   6862  O  OG1 . THR A 1 1294 ? 118.746 114.768 94.309  1.00 28.42  ? 865  THR A OG1 1 
ATOM   6863  C  CG2 . THR A 1 1294 ? 117.519 115.013 92.269  1.00 34.35  ? 865  THR A CG2 1 
ATOM   6864  N  N   . PHE A 1 1295 ? 116.755 111.746 91.900  1.00 17.97  ? 866  PHE A N   1 
ATOM   6865  C  CA  . PHE A 1 1295 ? 115.947 111.197 90.832  1.00 17.43  ? 866  PHE A CA  1 
ATOM   6866  C  C   . PHE A 1 1295 ? 114.780 110.403 91.359  1.00 16.66  ? 866  PHE A C   1 
ATOM   6867  O  O   . PHE A 1 1295 ? 113.696 110.430 90.770  1.00 27.52  ? 866  PHE A O   1 
ATOM   6868  C  CB  . PHE A 1 1295 ? 116.751 110.304 89.940  1.00 23.48  ? 866  PHE A CB  1 
ATOM   6869  C  CG  . PHE A 1 1295 ? 116.141 110.163 88.610  1.00 29.00  ? 866  PHE A CG  1 
ATOM   6870  C  CD1 . PHE A 1 1295 ? 115.215 109.189 88.370  1.00 30.29  ? 866  PHE A CD1 1 
ATOM   6871  C  CD2 . PHE A 1 1295 ? 116.438 111.072 87.617  1.00 34.03  ? 866  PHE A CD2 1 
ATOM   6872  C  CE1 . PHE A 1 1295 ? 114.649 109.078 87.143  1.00 39.85  ? 866  PHE A CE1 1 
ATOM   6873  C  CE2 . PHE A 1 1295 ? 115.881 110.970 86.398  1.00 32.16  ? 866  PHE A CE2 1 
ATOM   6874  C  CZ  . PHE A 1 1295 ? 114.977 109.975 86.152  1.00 40.20  ? 866  PHE A CZ  1 
ATOM   6875  N  N   . PHE A 1 1296 ? 114.976 109.676 92.436  1.00 17.89  ? 867  PHE A N   1 
ATOM   6876  C  CA  . PHE A 1 1296 ? 113.885 108.850 92.891  1.00 18.00  ? 867  PHE A CA  1 
ATOM   6877  C  C   . PHE A 1 1296 ? 112.748 109.690 93.418  1.00 23.63  ? 867  PHE A C   1 
ATOM   6878  O  O   . PHE A 1 1296 ? 111.590 109.295 93.269  1.00 36.23  ? 867  PHE A O   1 
ATOM   6879  C  CB  . PHE A 1 1296 ? 114.440 107.848 93.890  1.00 26.22  ? 867  PHE A CB  1 
ATOM   6880  C  CG  . PHE A 1 1296 ? 113.445 106.956 94.490  1.00 22.65  ? 867  PHE A CG  1 
ATOM   6881  C  CD1 . PHE A 1 1296 ? 112.644 106.199 93.682  1.00 42.32  ? 867  PHE A CD1 1 
ATOM   6882  C  CD2 . PHE A 1 1296 ? 113.605 106.566 95.791  1.00 22.51  ? 867  PHE A CD2 1 
ATOM   6883  C  CE1 . PHE A 1 1296 ? 111.784 105.283 94.215  1.00 47.94  ? 867  PHE A CE1 1 
ATOM   6884  C  CE2 . PHE A 1 1296 ? 112.798 105.628 96.349  1.00 32.28  ? 867  PHE A CE2 1 
ATOM   6885  C  CZ  . PHE A 1 1296 ? 111.871 104.980 95.570  1.00 43.85  ? 867  PHE A CZ  1 
ATOM   6886  N  N   . SER A 1 1297 ? 113.030 110.873 93.962  1.00 21.38  ? 868  SER A N   1 
ATOM   6887  C  CA  . SER A 1 1297 ? 111.933 111.753 94.341  1.00 17.02  ? 868  SER A CA  1 
ATOM   6888  C  C   . SER A 1 1297 ? 111.180 112.216 93.130  1.00 17.94  ? 868  SER A C   1 
ATOM   6889  O  O   . SER A 1 1297 ? 109.946 112.209 93.125  1.00 24.50  ? 868  SER A O   1 
ATOM   6890  C  CB  . SER A 1 1297 ? 112.437 112.974 95.079  1.00 25.60  ? 868  SER A CB  1 
ATOM   6891  O  OG  . SER A 1 1297 ? 111.336 113.829 95.290  1.00 29.32  ? 868  SER A OG  1 
ATOM   6892  N  N   . VAL A 1 1298 ? 111.909 112.659 92.105  1.00 19.52  ? 869  VAL A N   1 
ATOM   6893  C  CA  . VAL A 1 1298 ? 111.235 113.130 90.900  1.00 15.24  ? 869  VAL A CA  1 
ATOM   6894  C  C   . VAL A 1 1298 ? 110.249 112.090 90.427  1.00 15.71  ? 869  VAL A C   1 
ATOM   6895  O  O   . VAL A 1 1298 ? 109.057 112.362 90.274  1.00 27.41  ? 869  VAL A O   1 
ATOM   6896  C  CB  . VAL A 1 1298 ? 112.237 113.456 89.787  1.00 17.21  ? 869  VAL A CB  1 
ATOM   6897  C  CG1 . VAL A 1 1298 ? 111.481 113.814 88.562  1.00 21.10  ? 869  VAL A CG1 1 
ATOM   6898  C  CG2 . VAL A 1 1298 ? 113.130 114.616 90.192  1.00 34.34  ? 869  VAL A CG2 1 
ATOM   6899  N  N   . ARG A 1 1299 ? 110.714 110.879 90.244  1.00 14.09  ? 870  ARG A N   1 
ATOM   6900  C  CA  . ARG A 1 1299 ? 109.818 109.870 89.731  1.00 15.51  ? 870  ARG A CA  1 
ATOM   6901  C  C   . ARG A 1 1299 ? 108.691 109.578 90.700  1.00 21.73  ? 870  ARG A C   1 
ATOM   6902  O  O   . ARG A 1 1299 ? 107.549 109.370 90.278  1.00 30.08  ? 870  ARG A O   1 
ATOM   6903  C  CB  . ARG A 1 1299 ? 110.578 108.602 89.447  1.00 26.49  ? 870  ARG A CB  1 
ATOM   6904  C  CG  . ARG A 1 1299 ? 111.280 108.708 88.169  1.00 34.13  ? 870  ARG A CG  1 
ATOM   6905  C  CD  . ARG A 1 1299 ? 110.342 109.066 87.086  1.00 30.01  ? 870  ARG A CD  1 
ATOM   6906  N  NE  . ARG A 1 1299 ? 111.102 109.049 85.859  1.00 30.74  ? 870  ARG A NE  1 
ATOM   6907  C  CZ  . ARG A 1 1299 ? 110.575 109.262 84.676  1.00 36.33  ? 870  ARG A CZ  1 
ATOM   6908  N  NH1 . ARG A 1 1299 ? 109.269 109.450 84.578  1.00 40.47  ? 870  ARG A NH1 1 
ATOM   6909  N  NH2 . ARG A 1 1299 ? 111.344 109.248 83.600  1.00 42.70  ? 870  ARG A NH2 1 
ATOM   6910  N  N   . ILE A 1 1300 ? 108.981 109.508 91.994  1.00 17.39  ? 871  ILE A N   1 
ATOM   6911  C  CA  . ILE A 1 1300 ? 107.966 108.981 92.891  1.00 15.80  ? 871  ILE A CA  1 
ATOM   6912  C  C   . ILE A 1 1300 ? 106.847 109.992 93.098  1.00 24.36  ? 871  ILE A C   1 
ATOM   6913  O  O   . ILE A 1 1300 ? 105.695 109.617 93.345  1.00 30.70  ? 871  ILE A O   1 
ATOM   6914  C  CB  . ILE A 1 1300 ? 108.600 108.556 94.216  1.00 21.05  ? 871  ILE A CB  1 
ATOM   6915  C  CG1 . ILE A 1 1300 ? 107.702 107.591 94.951  1.00 32.28  ? 871  ILE A CG1 1 
ATOM   6916  C  CG2 . ILE A 1 1300 ? 108.817 109.743 95.098  1.00 34.15  ? 871  ILE A CG2 1 
ATOM   6917  C  CD1 . ILE A 1 1300 ? 108.341 107.049 96.225  1.00 38.79  ? 871  ILE A CD1 1 
ATOM   6918  N  N   . LEU A 1 1301 ? 107.143 111.280 93.004  1.00 26.22  ? 872  LEU A N   1 
ATOM   6919  C  CA  . LEU A 1 1301 ? 106.075 112.265 93.019  1.00 17.07  ? 872  LEU A CA  1 
ATOM   6920  C  C   . LEU A 1 1301 ? 105.451 112.393 91.655  1.00 22.82  ? 872  LEU A C   1 
ATOM   6921  O  O   . LEU A 1 1301 ? 104.326 112.881 91.555  1.00 34.95  ? 872  LEU A O   1 
ATOM   6922  C  CB  . LEU A 1 1301 ? 106.610 113.630 93.432  1.00 24.10  ? 872  LEU A CB  1 
ATOM   6923  C  CG  . LEU A 1 1301 ? 106.969 113.775 94.917  1.00 38.50  ? 872  LEU A CG  1 
ATOM   6924  C  CD1 . LEU A 1 1301 ? 107.494 115.181 95.201  1.00 41.01  ? 872  LEU A CD1 1 
ATOM   6925  C  CD2 . LEU A 1 1301 ? 105.818 113.414 95.853  1.00 42.64  ? 872  LEU A CD2 1 
ATOM   6926  N  N   . GLN A 1 1302 ? 106.163 111.989 90.601  1.00 22.40  ? 873  GLN A N   1 
ATOM   6927  C  CA  . GLN A 1 1302 ? 105.590 112.104 89.273  1.00 20.80  ? 873  GLN A CA  1 
ATOM   6928  C  C   . GLN A 1 1302 ? 104.351 111.253 89.155  1.00 26.90  ? 873  GLN A C   1 
ATOM   6929  O  O   . GLN A 1 1302 ? 103.322 111.728 88.671  1.00 44.64  ? 873  GLN A O   1 
ATOM   6930  C  CB  . GLN A 1 1302 ? 106.588 111.702 88.209  1.00 26.47  ? 873  GLN A CB  1 
ATOM   6931  C  CG  . GLN A 1 1302 ? 105.983 111.689 86.835  1.00 35.58  ? 873  GLN A CG  1 
ATOM   6932  C  CD  . GLN A 1 1302 ? 106.974 111.274 85.743  1.00 48.14  ? 873  GLN A CD  1 
ATOM   6933  O  OE1 . GLN A 1 1302 ? 108.192 111.308 85.950  1.00 43.86  ? 873  GLN A OE1 1 
ATOM   6934  N  NE2 . GLN A 1 1302 ? 106.450 110.883 84.570  1.00 46.66  ? 873  GLN A NE2 1 
ATOM   6935  N  N   . TYR A 1 1303 ? 104.397 110.021 89.632  1.00 26.04  ? 874  TYR A N   1 
ATOM   6936  C  CA  . TYR A 1 1303 ? 103.249 109.141 89.473  1.00 25.00  ? 874  TYR A CA  1 
ATOM   6937  C  C   . TYR A 1 1303 ? 102.347 109.088 90.689  1.00 25.29  ? 874  TYR A C   1 
ATOM   6938  O  O   . TYR A 1 1303 ? 101.131 109.233 90.562  1.00 33.63  ? 874  TYR A O   1 
ATOM   6939  C  CB  . TYR A 1 1303 ? 103.723 107.742 89.167  1.00 26.31  ? 874  TYR A CB  1 
ATOM   6940  C  CG  . TYR A 1 1303 ? 104.271 107.626 87.796  1.00 31.22  ? 874  TYR A CG  1 
ATOM   6941  C  CD1 . TYR A 1 1303 ? 103.427 107.493 86.713  1.00 43.61  ? 874  TYR A CD1 1 
ATOM   6942  C  CD2 . TYR A 1 1303 ? 105.630 107.610 87.577  1.00 36.71  ? 874  TYR A CD2 1 
ATOM   6943  C  CE1 . TYR A 1 1303 ? 103.923 107.358 85.433  1.00 45.82  ? 874  TYR A CE1 1 
ATOM   6944  C  CE2 . TYR A 1 1303 ? 106.142 107.468 86.305  1.00 39.69  ? 874  TYR A CE2 1 
ATOM   6945  C  CZ  . TYR A 1 1303 ? 105.283 107.348 85.237  1.00 39.68  ? 874  TYR A CZ  1 
ATOM   6946  O  OH  . TYR A 1 1303 ? 105.778 107.223 83.965  1.00 45.24  ? 874  TYR A OH  1 
ATOM   6947  N  N   . HIS A 1 1304 ? 102.926 108.927 91.866  1.00 23.67  ? 875  HIS A N   1 
ATOM   6948  C  CA  . HIS A 1 1304 ? 102.186 108.652 93.087  1.00 23.92  ? 875  HIS A CA  1 
ATOM   6949  C  C   . HIS A 1 1304 ? 102.003 109.887 93.952  1.00 23.65  ? 875  HIS A C   1 
ATOM   6950  O  O   . HIS A 1 1304 ? 102.160 109.816 95.170  1.00 30.99  ? 875  HIS A O   1 
ATOM   6951  C  CB  . HIS A 1 1304 ? 102.908 107.566 93.865  1.00 24.86  ? 875  HIS A CB  1 
ATOM   6952  C  CG  . HIS A 1 1304 ? 103.234 106.375 93.033  1.00 29.77  ? 875  HIS A CG  1 
ATOM   6953  N  ND1 . HIS A 1 1304 ? 104.293 106.356 92.154  1.00 32.73  ? 875  HIS A ND1 1 
ATOM   6954  C  CD2 . HIS A 1 1304 ? 102.656 105.152 92.960  1.00 30.87  ? 875  HIS A CD2 1 
ATOM   6955  C  CE1 . HIS A 1 1304 ? 104.344 105.177 91.562  1.00 36.76  ? 875  HIS A CE1 1 
ATOM   6956  N  NE2 . HIS A 1 1304 ? 103.362 104.429 92.031  1.00 31.53  ? 875  HIS A NE2 1 
ATOM   6957  N  N   . HIS A 1 1305 ? 101.741 111.045 93.380  1.00 23.84  ? 876  HIS A N   1 
ATOM   6958  C  CA  . HIS A 1 1305 ? 101.684 112.221 94.226  1.00 25.59  ? 876  HIS A CA  1 
ATOM   6959  C  C   . HIS A 1 1305 ? 100.544 112.032 95.191  1.00 17.86  ? 876  HIS A C   1 
ATOM   6960  O  O   . HIS A 1 1305 ? 99.528  111.438 94.847  1.00 26.28  ? 876  HIS A O   1 
ATOM   6961  C  CB  . HIS A 1 1305 ? 101.461 113.475 93.406  1.00 30.85  ? 876  HIS A CB  1 
ATOM   6962  C  CG  . HIS A 1 1305 ? 101.888 114.728 94.091  1.00 30.11  ? 876  HIS A CG  1 
ATOM   6963  N  ND1 . HIS A 1 1305 ? 103.064 115.374 93.783  1.00 32.94  ? 876  HIS A ND1 1 
ATOM   6964  C  CD2 . HIS A 1 1305 ? 101.315 115.440 95.090  1.00 37.02  ? 876  HIS A CD2 1 
ATOM   6965  C  CE1 . HIS A 1 1305 ? 103.172 116.459 94.528  1.00 40.40  ? 876  HIS A CE1 1 
ATOM   6966  N  NE2 . HIS A 1 1305 ? 102.121 116.526 95.326  1.00 35.70  ? 876  HIS A NE2 1 
ATOM   6967  N  N   . LEU A 1 1306 ? 100.735 112.445 96.426  1.00 23.10  ? 877  LEU A N   1 
ATOM   6968  C  CA  . LEU A 1 1306 ? 99.662  112.189 97.375  1.00 30.00  ? 877  LEU A CA  1 
ATOM   6969  C  C   . LEU A 1 1306 ? 98.534  113.199 97.249  1.00 41.02  ? 877  LEU A C   1 
ATOM   6970  O  O   . LEU A 1 1306 ? 97.378  112.881 97.560  1.00 46.13  ? 877  LEU A O   1 
ATOM   6971  C  CB  . LEU A 1 1306 ? 100.179 112.173 98.805  1.00 34.45  ? 877  LEU A CB  1 
ATOM   6972  C  CG  . LEU A 1 1306 ? 99.090  111.686 99.766  1.00 37.35  ? 877  LEU A CG  1 
ATOM   6973  C  CD1 . LEU A 1 1306 ? 98.718  110.257 99.482  1.00 41.23  ? 877  LEU A CD1 1 
ATOM   6974  C  CD2 . LEU A 1 1306 ? 99.501  111.843 101.218 1.00 46.08  ? 877  LEU A CD2 1 
ATOM   6975  N  N   . GLY A 1 1307 ? 98.841  114.420 96.819  1.00 43.77  ? 878  GLY A N   1 
ATOM   6976  C  CA  . GLY A 1 1307 ? 97.788  115.401 96.645  1.00 38.62  ? 878  GLY A CA  1 
ATOM   6977  C  C   . GLY A 1 1307 ? 96.831  115.028 95.533  1.00 35.11  ? 878  GLY A C   1 
ATOM   6978  O  O   . GLY A 1 1307 ? 95.615  115.110 95.701  1.00 47.82  ? 878  GLY A O   1 
ATOM   6979  N  N   . PHE A 1 1308 ? 97.356  114.589 94.402  1.00 24.98  ? 879  PHE A N   1 
ATOM   6980  C  CA  . PHE A 1 1308 ? 96.508  114.265 93.276  1.00 27.97  ? 879  PHE A CA  1 
ATOM   6981  C  C   . PHE A 1 1308 ? 95.905  112.878 93.396  1.00 38.25  ? 879  PHE A C   1 
ATOM   6982  O  O   . PHE A 1 1308 ? 96.329  112.055 94.205  1.00 44.85  ? 879  PHE A O   1 
ATOM   6983  C  CB  . PHE A 1 1308 ? 97.296  114.396 92.009  1.00 36.74  ? 879  PHE A CB  1 
ATOM   6984  C  CG  . PHE A 1 1308 ? 97.783  115.767 91.788  1.00 41.81  ? 879  PHE A CG  1 
ATOM   6985  C  CD1 . PHE A 1 1308 ? 99.017  116.157 92.242  1.00 50.33  ? 879  PHE A CD1 1 
ATOM   6986  C  CD2 . PHE A 1 1308 ? 97.015  116.665 91.074  1.00 49.34  ? 879  PHE A CD2 1 
ATOM   6987  C  CE1 . PHE A 1 1308 ? 99.472  117.441 92.027  1.00 51.49  ? 879  PHE A CE1 1 
ATOM   6988  C  CE2 . PHE A 1 1308 ? 97.458  117.941 90.838  1.00 52.41  ? 879  PHE A CE2 1 
ATOM   6989  C  CZ  . PHE A 1 1308 ? 98.693  118.336 91.314  1.00 51.48  ? 879  PHE A CZ  1 
ATOM   6990  N  N   . ASN A 1 1309 ? 94.892  112.618 92.575  1.00 37.67  ? 880  ASN A N   1 
ATOM   6991  C  CA  . ASN A 1 1309 ? 94.196  111.349 92.691  1.00 40.63  ? 880  ASN A CA  1 
ATOM   6992  C  C   . ASN A 1 1309 ? 95.078  110.199 92.226  1.00 46.93  ? 880  ASN A C   1 
ATOM   6993  O  O   . ASN A 1 1309 ? 96.146  110.387 91.642  1.00 45.92  ? 880  ASN A O   1 
ATOM   6994  C  CB  . ASN A 1 1309 ? 92.893  111.369 91.913  1.00 39.55  ? 880  ASN A CB  1 
ATOM   6995  C  CG  . ASN A 1 1309 ? 91.884  112.286 92.541  1.00 48.80  ? 880  ASN A CG  1 
ATOM   6996  O  OD1 . ASN A 1 1309 ? 92.202  113.032 93.472  1.00 41.68  ? 880  ASN A OD1 1 
ATOM   6997  N  ND2 . ASN A 1 1309 ? 90.646  112.229 92.052  1.00 57.91  ? 880  ASN A ND2 1 
ATOM   6998  N  N   . LYS A 1 1310 ? 94.628  108.988 92.536  1.00 44.43  ? 881  LYS A N   1 
ATOM   6999  C  CA  . LYS A 1 1310 ? 95.407  107.813 92.203  1.00 34.23  ? 881  LYS A CA  1 
ATOM   7000  C  C   . LYS A 1 1310 ? 95.623  107.758 90.705  1.00 38.69  ? 881  LYS A C   1 
ATOM   7001  O  O   . LYS A 1 1310 ? 94.736  108.112 89.928  1.00 47.89  ? 881  LYS A O   1 
ATOM   7002  C  CB  . LYS A 1 1310 ? 94.696  106.558 92.680  1.00 44.15  ? 881  LYS A CB  1 
ATOM   7003  C  CG  . LYS A 1 1310 ? 95.562  105.319 92.596  1.00 53.48  ? 881  LYS A CG  1 
ATOM   7004  C  CD  . LYS A 1 1310 ? 94.835  104.098 93.133  1.00 64.47  ? 881  LYS A CD  1 
ATOM   7005  C  CE  . LYS A 1 1310 ? 95.727  102.860 93.107  1.00 72.71  ? 881  LYS A CE  1 
ATOM   7006  N  NZ  . LYS A 1 1310 ? 97.010  103.021 93.860  1.00 73.10  ? 881  LYS A NZ  1 
ATOM   7007  N  N   . GLY A 1 1311 ? 96.819  107.348 90.299  1.00 43.49  ? 882  GLY A N   1 
ATOM   7008  C  CA  . GLY A 1 1311 ? 97.111  107.213 88.879  1.00 46.36  ? 882  GLY A CA  1 
ATOM   7009  C  C   . GLY A 1 1311 ? 97.056  108.525 88.126  1.00 48.77  ? 882  GLY A C   1 
ATOM   7010  O  O   . GLY A 1 1311 ? 96.466  108.598 87.040  1.00 54.77  ? 882  GLY A O   1 
ATOM   7011  N  N   . PHE A 1 1312 ? 97.636  109.564 88.687  1.00 39.00  ? 883  PHE A N   1 
ATOM   7012  C  CA  . PHE A 1 1312 ? 97.624  110.901 88.124  1.00 36.61  ? 883  PHE A CA  1 
ATOM   7013  C  C   . PHE A 1 1312 ? 99.054  111.166 87.717  1.00 32.60  ? 883  PHE A C   1 
ATOM   7014  O  O   . PHE A 1 1312 ? 99.868  111.634 88.507  1.00 41.33  ? 883  PHE A O   1 
ATOM   7015  C  CB  . PHE A 1 1312 ? 97.157  111.866 89.152  1.00 49.88  ? 883  PHE A CB  1 
ATOM   7016  C  CG  . PHE A 1 1312 ? 96.672  113.154 88.624  1.00 46.79  ? 883  PHE A CG  1 
ATOM   7017  C  CD1 . PHE A 1 1312 ? 95.315  113.416 88.539  1.00 47.74  ? 883  PHE A CD1 1 
ATOM   7018  C  CD2 . PHE A 1 1312 ? 97.581  114.155 88.316  1.00 58.02  ? 883  PHE A CD2 1 
ATOM   7019  C  CE1 . PHE A 1 1312 ? 94.865  114.646 88.093  1.00 62.10  ? 883  PHE A CE1 1 
ATOM   7020  C  CE2 . PHE A 1 1312 ? 97.152  115.399 87.878  1.00 67.28  ? 883  PHE A CE2 1 
ATOM   7021  C  CZ  . PHE A 1 1312 ? 95.790  115.648 87.764  1.00 71.98  ? 883  PHE A CZ  1 
ATOM   7022  N  N   . ASP A 1 1313 ? 99.370  110.836 86.496  1.00 35.01  ? 884  ASP A N   1 
ATOM   7023  C  CA  . ASP A 1 1313 ? 100.729 111.031 86.035  1.00 33.35  ? 884  ASP A CA  1 
ATOM   7024  C  C   . ASP A 1 1313 ? 101.017 112.518 85.922  1.00 37.37  ? 884  ASP A C   1 
ATOM   7025  O  O   . ASP A 1 1313 ? 100.698 113.148 84.914  1.00 51.02  ? 884  ASP A O   1 
ATOM   7026  C  CB  . ASP A 1 1313 ? 100.910 110.323 84.706  1.00 42.46  ? 884  ASP A CB  1 
ATOM   7027  C  CG  . ASP A 1 1313 ? 102.335 110.312 84.263  1.00 51.71  ? 884  ASP A CG  1 
ATOM   7028  O  OD1 . ASP A 1 1313 ? 103.170 110.959 84.938  1.00 48.94  ? 884  ASP A OD1 1 
ATOM   7029  O  OD2 . ASP A 1 1313 ? 102.632 109.628 83.259  1.00 57.38  ? 884  ASP A OD2 1 
ATOM   7030  N  N   . LEU A 1 1314 ? 101.650 113.090 86.941  1.00 32.14  ? 885  LEU A N   1 
ATOM   7031  C  CA  . LEU A 1 1314 ? 101.934 114.506 86.857  1.00 28.17  ? 885  LEU A CA  1 
ATOM   7032  C  C   . LEU A 1 1314 ? 102.768 114.817 85.646  1.00 39.39  ? 885  LEU A C   1 
ATOM   7033  O  O   . LEU A 1 1314 ? 102.748 115.956 85.172  1.00 47.34  ? 885  LEU A O   1 
ATOM   7034  C  CB  . LEU A 1 1314 ? 102.679 115.032 88.063  1.00 31.32  ? 885  LEU A CB  1 
ATOM   7035  C  CG  . LEU A 1 1314 ? 101.827 115.399 89.252  1.00 38.23  ? 885  LEU A CG  1 
ATOM   7036  C  CD1 . LEU A 1 1314 ? 100.903 116.496 88.796  1.00 47.32  ? 885  LEU A CD1 1 
ATOM   7037  C  CD2 . LEU A 1 1314 ? 101.076 114.221 89.800  1.00 42.75  ? 885  LEU A CD2 1 
ATOM   7038  N  N   . GLY A 1 1315 ? 103.490 113.834 85.126  1.00 37.75  ? 886  GLY A N   1 
ATOM   7039  C  CA  . GLY A 1 1315 ? 104.256 114.102 83.931  1.00 51.94  ? 886  GLY A CA  1 
ATOM   7040  C  C   . GLY A 1 1315 ? 103.428 114.211 82.675  1.00 52.42  ? 886  GLY A C   1 
ATOM   7041  O  O   . GLY A 1 1315 ? 103.937 114.658 81.643  1.00 54.73  ? 886  GLY A O   1 
ATOM   7042  N  N   . GLN A 1 1316 ? 102.158 113.826 82.746  1.00 50.20  ? 887  GLN A N   1 
ATOM   7043  C  CA  . GLN A 1 1316 ? 101.266 113.811 81.598  1.00 48.24  ? 887  GLN A CA  1 
ATOM   7044  C  C   . GLN A 1 1316 ? 100.362 115.023 81.565  1.00 41.83  ? 887  GLN A C   1 
ATOM   7045  O  O   . GLN A 1 1316 ? 100.121 115.583 80.493  1.00 50.75  ? 887  GLN A O   1 
ATOM   7046  C  CB  . GLN A 1 1316 ? 100.412 112.540 81.626  1.00 57.55  ? 887  GLN A CB  1 
ATOM   7047  C  CG  . GLN A 1 1316 ? 101.069 111.354 80.940  1.00 56.11  ? 887  GLN A CG  1 
ATOM   7048  C  CD  . GLN A 1 1316 ? 101.161 111.528 79.449  1.00 57.78  ? 887  GLN A CD  1 
ATOM   7049  O  OE1 . GLN A 1 1316 ? 102.221 111.326 78.856  1.00 56.94  ? 887  GLN A OE1 1 
ATOM   7050  N  NE2 . GLN A 1 1316 ? 100.036 111.866 78.821  1.00 59.13  ? 887  GLN A NE2 1 
ATOM   7051  N  N   . LEU A 1 1317 ? 99.866  115.448 82.719  1.00 36.62  ? 888  LEU A N   1 
ATOM   7052  C  CA  . LEU A 1 1317 ? 99.020  116.621 82.739  1.00 40.56  ? 888  LEU A CA  1 
ATOM   7053  C  C   . LEU A 1 1317 ? 99.802  117.913 82.584  1.00 48.67  ? 888  LEU A C   1 
ATOM   7054  O  O   . LEU A 1 1317 ? 99.186  118.979 82.493  1.00 53.63  ? 888  LEU A O   1 
ATOM   7055  C  CB  . LEU A 1 1317 ? 98.177  116.652 84.012  1.00 50.91  ? 888  LEU A CB  1 
ATOM   7056  C  CG  . LEU A 1 1317 ? 97.094  115.552 83.901  1.00 70.59  ? 888  LEU A CG  1 
ATOM   7057  C  CD1 . LEU A 1 1317 ? 97.496  114.209 84.564  1.00 63.14  ? 888  LEU A CD1 1 
ATOM   7058  C  CD2 . LEU A 1 1317 ? 95.659  116.004 84.307  1.00 65.27  ? 888  LEU A CD2 1 
ATOM   7059  N  N   . THR A 1 1318 ? 101.128 117.860 82.537  1.00 40.04  ? 889  THR A N   1 
ATOM   7060  C  CA  . THR A 1 1318 ? 101.913 119.044 82.243  1.00 32.78  ? 889  THR A CA  1 
ATOM   7061  C  C   . THR A 1 1318 ? 102.547 118.992 80.870  1.00 37.79  ? 889  THR A C   1 
ATOM   7062  O  O   . THR A 1 1318 ? 102.398 119.922 80.077  1.00 50.75  ? 889  THR A O   1 
ATOM   7063  C  CB  . THR A 1 1318 ? 103.017 119.219 83.272  1.00 43.95  ? 889  THR A CB  1 
ATOM   7064  O  OG1 . THR A 1 1318 ? 103.945 118.135 83.152  1.00 46.70  ? 889  THR A OG1 1 
ATOM   7065  C  CG2 . THR A 1 1318 ? 102.411 119.197 84.671  1.00 51.68  ? 889  THR A CG2 1 
ATOM   7066  N  N   . LEU A 1 1319 ? 103.262 117.924 80.577  1.00 41.30  ? 890  LEU A N   1 
ATOM   7067  C  CA  . LEU A 1 1319 ? 103.998 117.808 79.329  1.00 46.10  ? 890  LEU A CA  1 
ATOM   7068  C  C   . LEU A 1 1319 ? 103.193 117.193 78.203  1.00 43.29  ? 890  LEU A C   1 
ATOM   7069  O  O   . LEU A 1 1319 ? 103.699 117.104 77.081  1.00 45.33  ? 890  LEU A O   1 
ATOM   7070  C  CB  . LEU A 1 1319 ? 105.247 116.963 79.526  1.00 56.55  ? 890  LEU A CB  1 
ATOM   7071  C  CG  . LEU A 1 1319 ? 106.461 117.810 79.874  1.00 69.57  ? 890  LEU A CG  1 
ATOM   7072  C  CD1 . LEU A 1 1319 ? 106.778 118.742 78.684  1.00 65.36  ? 890  LEU A CD1 1 
ATOM   7073  C  CD2 . LEU A 1 1319 ? 106.255 118.578 81.207  1.00 61.85  ? 890  LEU A CD2 1 
ATOM   7074  N  N   . GLY A 1 1320 ? 101.997 116.713 78.470  1.00 41.48  ? 891  GLY A N   1 
ATOM   7075  C  CA  . GLY A 1 1320 ? 101.275 116.112 77.370  1.00 40.34  ? 891  GLY A CA  1 
ATOM   7076  C  C   . GLY A 1 1320 ? 101.866 114.802 76.906  1.00 47.81  ? 891  GLY A C   1 
ATOM   7077  O  O   . GLY A 1 1320 ? 101.137 113.821 76.744  1.00 56.59  ? 891  GLY A O   1 
ATOM   7078  N  N   . LYS A 1 1321 ? 103.173 114.756 76.664  1.00 45.65  ? 892  LYS A N   1 
ATOM   7079  C  CA  . LYS A 1 1321 ? 103.879 113.502 76.423  1.00 50.00  ? 892  LYS A CA  1 
ATOM   7080  C  C   . LYS A 1 1321 ? 104.636 113.127 77.684  1.00 56.05  ? 892  LYS A C   1 
ATOM   7081  O  O   . LYS A 1 1321 ? 104.917 113.986 78.525  1.00 65.99  ? 892  LYS A O   1 
ATOM   7082  C  CB  . LYS A 1 1321 ? 104.870 113.624 75.264  1.00 54.37  ? 892  LYS A CB  1 
ATOM   7083  C  CG  . LYS A 1 1321 ? 106.000 114.575 75.600  1.00 62.01  ? 892  LYS A CG  1 
ATOM   7084  C  CD  . LYS A 1 1321 ? 107.056 114.634 74.515  1.00 69.83  ? 892  LYS A CD  1 
ATOM   7085  C  CE  . LYS A 1 1321 ? 108.186 115.576 74.922  1.00 80.42  ? 892  LYS A CE  1 
ATOM   7086  N  NZ  . LYS A 1 1321 ? 107.707 116.980 75.109  1.00 78.77  ? 892  LYS A NZ  1 
ATOM   7087  N  N   . PRO A 1 1322 ? 104.961 111.860 77.870  1.00 40.59  ? 893  PRO A N   1 
ATOM   7088  C  CA  . PRO A 1 1322 ? 105.595 111.444 79.132  1.00 51.09  ? 893  PRO A CA  1 
ATOM   7089  C  C   . PRO A 1 1322 ? 106.992 112.044 79.337  1.00 63.33  ? 893  PRO A C   1 
ATOM   7090  O  O   . PRO A 1 1322 ? 107.782 112.160 78.396  1.00 61.65  ? 893  PRO A O   1 
ATOM   7091  C  CB  . PRO A 1 1322 ? 105.642 109.918 79.008  1.00 57.29  ? 893  PRO A CB  1 
ATOM   7092  C  CG  . PRO A 1 1322 ? 104.604 109.597 77.937  1.00 59.89  ? 893  PRO A CG  1 
ATOM   7093  C  CD  . PRO A 1 1322 ? 104.627 110.738 76.992  1.00 42.75  ? 893  PRO A CD  1 
ATOM   7094  N  N   . LEU A 1 1323 ? 107.292 112.419 80.596  1.00 60.14  ? 894  LEU A N   1 
ATOM   7095  C  CA  . LEU A 1 1323 ? 108.623 112.908 80.963  1.00 42.57  ? 894  LEU A CA  1 
ATOM   7096  C  C   . LEU A 1 1323 ? 109.644 111.831 80.724  1.00 39.09  ? 894  LEU A C   1 
ATOM   7097  O  O   . LEU A 1 1323 ? 109.512 110.713 81.223  1.00 53.30  ? 894  LEU A O   1 
ATOM   7098  C  CB  . LEU A 1 1323 ? 108.691 113.270 82.441  1.00 46.07  ? 894  LEU A CB  1 
ATOM   7099  C  CG  . LEU A 1 1323 ? 107.928 114.484 82.942  1.00 63.83  ? 894  LEU A CG  1 
ATOM   7100  C  CD1 . LEU A 1 1323 ? 108.056 114.630 84.476  1.00 56.95  ? 894  LEU A CD1 1 
ATOM   7101  C  CD2 . LEU A 1 1323 ? 108.432 115.718 82.204  1.00 71.99  ? 894  LEU A CD2 1 
ATOM   7102  N  N   . ASP A 1 1324 ? 110.674 112.153 80.024  1.00 32.48  ? 895  ASP A N   1 
ATOM   7103  C  CA  . ASP A 1 1324 ? 111.678 111.134 79.818  1.00 41.70  ? 895  ASP A CA  1 
ATOM   7104  C  C   . ASP A 1 1324 ? 112.881 111.399 80.722  1.00 44.46  ? 895  ASP A C   1 
ATOM   7105  O  O   . ASP A 1 1324 ? 112.896 112.338 81.522  1.00 48.62  ? 895  ASP A O   1 
ATOM   7106  C  CB  . ASP A 1 1324 ? 112.008 111.073 78.329  1.00 53.44  ? 895  ASP A CB  1 
ATOM   7107  C  CG  . ASP A 1 1324 ? 112.383 112.437 77.775  1.00 67.75  ? 895  ASP A CG  1 
ATOM   7108  O  OD1 . ASP A 1 1324 ? 112.165 113.442 78.505  1.00 60.82  ? 895  ASP A OD1 1 
ATOM   7109  O  OD2 . ASP A 1 1324 ? 112.855 112.522 76.616  1.00 65.15  ? 895  ASP A OD2 1 
ATOM   7110  N  N   . PHE A 1 1325 ? 113.873 110.518 80.639  1.00 41.49  ? 896  PHE A N   1 
ATOM   7111  C  CA  . PHE A 1 1325 ? 115.125 110.791 81.324  1.00 33.95  ? 896  PHE A CA  1 
ATOM   7112  C  C   . PHE A 1 1325 ? 115.679 112.139 80.912  1.00 36.68  ? 896  PHE A C   1 
ATOM   7113  O  O   . PHE A 1 1325 ? 116.231 112.868 81.739  1.00 45.30  ? 896  PHE A O   1 
ATOM   7114  C  CB  . PHE A 1 1325 ? 116.141 109.711 81.004  1.00 50.63  ? 896  PHE A CB  1 
ATOM   7115  C  CG  . PHE A 1 1325 ? 117.470 109.930 81.645  1.00 53.86  ? 896  PHE A CG  1 
ATOM   7116  C  CD1 . PHE A 1 1325 ? 117.683 109.581 82.966  1.00 55.95  ? 896  PHE A CD1 1 
ATOM   7117  C  CD2 . PHE A 1 1325 ? 118.509 110.509 80.931  1.00 56.05  ? 896  PHE A CD2 1 
ATOM   7118  C  CE1 . PHE A 1 1325 ? 118.926 109.790 83.570  1.00 58.76  ? 896  PHE A CE1 1 
ATOM   7119  C  CE2 . PHE A 1 1325 ? 119.758 110.729 81.527  1.00 65.21  ? 896  PHE A CE2 1 
ATOM   7120  C  CZ  . PHE A 1 1325 ? 119.970 110.368 82.846  1.00 60.40  ? 896  PHE A CZ  1 
ATOM   7121  N  N   . GLY A 1 1326 ? 115.543 112.488 79.636  1.00 34.72  ? 897  GLY A N   1 
ATOM   7122  C  CA  . GLY A 1 1326 ? 116.141 113.718 79.163  1.00 30.42  ? 897  GLY A CA  1 
ATOM   7123  C  C   . GLY A 1 1326 ? 115.583 114.935 79.868  1.00 33.14  ? 897  GLY A C   1 
ATOM   7124  O  O   . GLY A 1 1326 ? 116.338 115.793 80.327  1.00 40.03  ? 897  GLY A O   1 
ATOM   7125  N  N   . THR A 1 1327 ? 114.257 115.019 79.989  1.00 29.50  ? 898  THR A N   1 
ATOM   7126  C  CA  . THR A 1 1327 ? 113.667 116.228 80.556  1.00 25.53  ? 898  THR A CA  1 
ATOM   7127  C  C   . THR A 1 1327 ? 113.964 116.349 82.034  1.00 32.32  ? 898  THR A C   1 
ATOM   7128  O  O   . THR A 1 1327 ? 114.259 117.443 82.527  1.00 39.75  ? 898  THR A O   1 
ATOM   7129  C  CB  . THR A 1 1327 ? 112.166 116.255 80.357  1.00 34.43  ? 898  THR A CB  1 
ATOM   7130  O  OG1 . THR A 1 1327 ? 111.864 116.174 78.959  1.00 46.37  ? 898  THR A OG1 1 
ATOM   7131  C  CG2 . THR A 1 1327 ? 111.584 117.535 80.959  1.00 36.79  ? 898  THR A CG2 1 
ATOM   7132  N  N   . ILE A 1 1328 ? 113.868 115.251 82.765  1.00 27.29  ? 899  ILE A N   1 
ATOM   7133  C  CA  . ILE A 1 1328 ? 114.189 115.314 84.174  1.00 19.63  ? 899  ILE A CA  1 
ATOM   7134  C  C   . ILE A 1 1328 ? 115.640 115.690 84.373  1.00 22.69  ? 899  ILE A C   1 
ATOM   7135  O  O   . ILE A 1 1328 ? 115.962 116.575 85.170  1.00 32.54  ? 899  ILE A O   1 
ATOM   7136  C  CB  . ILE A 1 1328 ? 113.873 113.981 84.828  1.00 21.59  ? 899  ILE A CB  1 
ATOM   7137  C  CG1 . ILE A 1 1328 ? 112.390 113.733 84.710  1.00 32.07  ? 899  ILE A CG1 1 
ATOM   7138  C  CG2 . ILE A 1 1328 ? 114.276 114.045 86.255  1.00 38.12  ? 899  ILE A CG2 1 
ATOM   7139  C  CD1 . ILE A 1 1328 ? 111.950 112.449 85.348  1.00 44.59  ? 899  ILE A CD1 1 
ATOM   7140  N  N   . SER A 1 1329 ? 116.538 115.052 83.644  1.00 24.75  ? 900  SER A N   1 
ATOM   7141  C  CA  . SER A 1 1329 ? 117.949 115.298 83.889  1.00 27.05  ? 900  SER A CA  1 
ATOM   7142  C  C   . SER A 1 1329 ? 118.323 116.740 83.583  1.00 29.06  ? 900  SER A C   1 
ATOM   7143  O  O   . SER A 1 1329 ? 119.267 117.275 84.178  1.00 36.26  ? 900  SER A O   1 
ATOM   7144  C  CB  . SER A 1 1329 ? 118.801 114.336 83.060  1.00 41.95  ? 900  SER A CB  1 
ATOM   7145  O  OG  . SER A 1 1329 ? 120.177 114.570 83.279  1.00 45.95  ? 900  SER A OG  1 
ATOM   7146  N  N   . LEU A 1 1330 ? 117.615 117.385 82.658  1.00 28.72  ? 901  LEU A N   1 
ATOM   7147  C  CA  . LEU A 1 1330 ? 117.886 118.794 82.393  1.00 27.51  ? 901  LEU A CA  1 
ATOM   7148  C  C   . LEU A 1 1330 ? 117.172 119.726 83.363  1.00 32.37  ? 901  LEU A C   1 
ATOM   7149  O  O   . LEU A 1 1330 ? 117.663 120.827 83.619  1.00 40.59  ? 901  LEU A O   1 
ATOM   7150  C  CB  . LEU A 1 1330 ? 117.515 119.155 80.964  1.00 33.54  ? 901  LEU A CB  1 
ATOM   7151  C  CG  . LEU A 1 1330 ? 118.029 120.546 80.576  1.00 55.79  ? 901  LEU A CG  1 
ATOM   7152  C  CD1 . LEU A 1 1330 ? 119.558 120.581 80.570  1.00 58.65  ? 901  LEU A CD1 1 
ATOM   7153  C  CD2 . LEU A 1 1330 ? 117.449 121.011 79.220  1.00 68.31  ? 901  LEU A CD2 1 
ATOM   7154  N  N   . ALA A 1 1331 ? 116.029 119.328 83.911  1.00 26.11  ? 902  ALA A N   1 
ATOM   7155  C  CA  . ALA A 1 1331 ? 115.439 120.125 84.972  1.00 21.19  ? 902  ALA A CA  1 
ATOM   7156  C  C   . ALA A 1 1331 ? 116.164 119.949 86.290  1.00 23.78  ? 902  ALA A C   1 
ATOM   7157  O  O   . ALA A 1 1331 ? 115.969 120.766 87.191  1.00 32.32  ? 902  ALA A O   1 
ATOM   7158  C  CB  . ALA A 1 1331 ? 113.971 119.772 85.175  1.00 34.12  ? 902  ALA A CB  1 
ATOM   7159  N  N   . LEU A 1 1332 ? 116.973 118.903 86.444  1.00 24.86  ? 903  LEU A N   1 
ATOM   7160  C  CA  . LEU A 1 1332 ? 117.819 118.774 87.626  1.00 24.60  ? 903  LEU A CA  1 
ATOM   7161  C  C   . LEU A 1 1332 ? 119.191 119.398 87.441  1.00 29.23  ? 903  LEU A C   1 
ATOM   7162  O  O   . LEU A 1 1332 ? 120.002 119.315 88.363  1.00 35.05  ? 903  LEU A O   1 
ATOM   7163  C  CB  . LEU A 1 1332 ? 117.988 117.308 88.035  1.00 20.78  ? 903  LEU A CB  1 
ATOM   7164  C  CG  . LEU A 1 1332 ? 116.670 116.682 88.478  1.00 32.66  ? 903  LEU A CG  1 
ATOM   7165  C  CD1 . LEU A 1 1332 ? 116.790 115.209 88.820  1.00 39.47  ? 903  LEU A CD1 1 
ATOM   7166  C  CD2 . LEU A 1 1332 ? 116.227 117.414 89.691  1.00 32.45  ? 903  LEU A CD2 1 
ATOM   7167  N  N   . ALA A 1 1333 ? 119.483 120.008 86.289  1.00 23.86  ? 904  ALA A N   1 
ATOM   7168  C  CA  . ALA A 1 1333 ? 120.756 120.691 86.095  1.00 22.28  ? 904  ALA A CA  1 
ATOM   7169  C  C   . ALA A 1 1333 ? 120.635 122.196 86.155  1.00 24.80  ? 904  ALA A C   1 
ATOM   7170  O  O   . ALA A 1 1333 ? 121.665 122.873 86.146  1.00 28.85  ? 904  ALA A O   1 
ATOM   7171  C  CB  . ALA A 1 1333 ? 121.396 120.307 84.757  1.00 31.09  ? 904  ALA A CB  1 
ATOM   7172  N  N   . VAL A 1 1334 ? 119.416 122.729 86.238  1.00 28.49  ? 905  VAL A N   1 
ATOM   7173  C  CA  . VAL A 1 1334 ? 119.184 124.169 86.320  1.00 22.90  ? 905  VAL A CA  1 
ATOM   7174  C  C   . VAL A 1 1334 ? 119.071 124.545 87.794  1.00 16.02  ? 905  VAL A C   1 
ATOM   7175  O  O   . VAL A 1 1334 ? 118.059 124.211 88.424  1.00 24.16  ? 905  VAL A O   1 
ATOM   7176  C  CB  . VAL A 1 1334 ? 117.914 124.576 85.565  1.00 26.68  ? 905  VAL A CB  1 
ATOM   7177  C  CG1 . VAL A 1 1334 ? 117.839 126.093 85.465  1.00 37.77  ? 905  VAL A CG1 1 
ATOM   7178  C  CG2 . VAL A 1 1334 ? 117.909 123.963 84.164  1.00 37.45  ? 905  VAL A CG2 1 
ATOM   7179  N  N   . PRO A 1 1335 ? 120.030 125.260 88.351  1.00 11.95  ? 906  PRO A N   1 
ATOM   7180  C  CA  . PRO A 1 1335 ? 120.016 125.520 89.777  1.00 13.41  ? 906  PRO A CA  1 
ATOM   7181  C  C   . PRO A 1 1335 ? 118.772 126.277 90.122  1.00 18.01  ? 906  PRO A C   1 
ATOM   7182  O  O   . PRO A 1 1335 ? 118.205 126.980 89.293  1.00 28.12  ? 906  PRO A O   1 
ATOM   7183  C  CB  . PRO A 1 1335 ? 121.233 126.406 89.986  1.00 24.29  ? 906  PRO A CB  1 
ATOM   7184  C  CG  . PRO A 1 1335 ? 122.103 126.090 88.882  1.00 26.87  ? 906  PRO A CG  1 
ATOM   7185  C  CD  . PRO A 1 1335 ? 121.207 125.849 87.719  1.00 25.98  ? 906  PRO A CD  1 
ATOM   7186  N  N   . GLN A 1 1336 ? 118.364 126.146 91.373  1.00 21.68  ? 907  GLN A N   1 
ATOM   7187  C  CA  . GLN A 1 1336 ? 117.055 126.639 91.766  1.00 22.76  ? 907  GLN A CA  1 
ATOM   7188  C  C   . GLN A 1 1336 ? 116.912 128.133 91.539  1.00 29.44  ? 907  GLN A C   1 
ATOM   7189  O  O   . GLN A 1 1336 ? 115.808 128.608 91.251  1.00 37.35  ? 907  GLN A O   1 
ATOM   7190  C  CB  . GLN A 1 1336 ? 116.807 126.327 93.229  1.00 27.40  ? 907  GLN A CB  1 
ATOM   7191  C  CG  . GLN A 1 1336 ? 115.569 126.950 93.716  1.00 29.06  ? 907  GLN A CG  1 
ATOM   7192  C  CD  . GLN A 1 1336 ? 115.894 128.163 94.475  1.00 32.01  ? 907  GLN A CD  1 
ATOM   7193  O  OE1 . GLN A 1 1336 ? 117.047 128.369 94.828  1.00 35.40  ? 907  GLN A OE1 1 
ATOM   7194  N  NE2 . GLN A 1 1336 ? 114.911 129.033 94.670  1.00 39.72  ? 907  GLN A NE2 1 
ATOM   7195  N  N   . VAL A 1 1337 ? 117.999 128.897 91.647  1.00 25.63  ? 908  VAL A N   1 
ATOM   7196  C  CA  . VAL A 1 1337 ? 117.835 130.337 91.554  1.00 17.30  ? 908  VAL A CA  1 
ATOM   7197  C  C   . VAL A 1 1337 ? 117.614 130.762 90.113  1.00 20.09  ? 908  VAL A C   1 
ATOM   7198  O  O   . VAL A 1 1337 ? 116.933 131.757 89.858  1.00 37.14  ? 908  VAL A O   1 
ATOM   7199  C  CB  . VAL A 1 1337 ? 119.030 131.060 92.174  1.00 23.22  ? 908  VAL A CB  1 
ATOM   7200  C  CG1 . VAL A 1 1337 ? 120.263 130.870 91.310  1.00 32.82  ? 908  VAL A CG1 1 
ATOM   7201  C  CG2 . VAL A 1 1337 ? 118.701 132.530 92.404  1.00 30.94  ? 908  VAL A CG2 1 
ATOM   7202  N  N   . LEU A 1 1338 ? 118.159 130.042 89.144  1.00 18.32  ? 909  LEU A N   1 
ATOM   7203  C  CA  . LEU A 1 1338 ? 117.711 130.283 87.782  1.00 14.19  ? 909  LEU A CA  1 
ATOM   7204  C  C   . LEU A 1 1338 ? 116.313 129.777 87.538  1.00 24.68  ? 909  LEU A C   1 
ATOM   7205  O  O   . LEU A 1 1338 ? 115.695 130.170 86.546  1.00 40.94  ? 909  LEU A O   1 
ATOM   7206  C  CB  . LEU A 1 1338 ? 118.583 129.588 86.797  1.00 12.07  ? 909  LEU A CB  1 
ATOM   7207  C  CG  . LEU A 1 1338 ? 119.940 130.048 87.102  1.00 17.59  ? 909  LEU A CG  1 
ATOM   7208  C  CD1 . LEU A 1 1338 ? 120.781 129.340 86.083  1.00 28.03  ? 909  LEU A CD1 1 
ATOM   7209  C  CD2 . LEU A 1 1338 ? 119.888 131.536 86.920  1.00 24.71  ? 909  LEU A CD2 1 
ATOM   7210  N  N   . GLY A 1 1339 ? 115.810 128.897 88.382  1.00 21.15  ? 910  GLY A N   1 
ATOM   7211  C  CA  . GLY A 1 1339 ? 114.477 128.378 88.180  1.00 28.01  ? 910  GLY A CA  1 
ATOM   7212  C  C   . GLY A 1 1339 ? 114.566 126.976 87.645  1.00 29.17  ? 910  GLY A C   1 
ATOM   7213  O  O   . GLY A 1 1339 ? 114.766 126.760 86.447  1.00 34.35  ? 910  GLY A O   1 
ATOM   7214  N  N   . GLY A 1 1340 ? 114.421 126.009 88.539  1.00 30.04  ? 911  GLY A N   1 
ATOM   7215  C  CA  . GLY A 1 1340 ? 114.722 124.631 88.197  1.00 37.12  ? 911  GLY A CA  1 
ATOM   7216  C  C   . GLY A 1 1340 ? 114.780 123.809 89.467  1.00 38.62  ? 911  GLY A C   1 
ATOM   7217  O  O   . GLY A 1 1340 ? 114.281 124.239 90.507  1.00 41.62  ? 911  GLY A O   1 
ATOM   7218  N  N   . LEU A 1 1341 ? 115.393 122.633 89.384  1.00 21.00  ? 912  LEU A N   1 
ATOM   7219  C  CA  . LEU A 1 1341 ? 115.412 121.779 90.553  1.00 16.76  ? 912  LEU A CA  1 
ATOM   7220  C  C   . LEU A 1 1341 ? 116.814 121.355 90.975  1.00 36.92  ? 912  LEU A C   1 
ATOM   7221  O  O   . LEU A 1 1341 ? 116.948 120.459 91.815  1.00 39.22  ? 912  LEU A O   1 
ATOM   7222  C  CB  . LEU A 1 1341 ? 114.593 120.545 90.300  1.00 13.52  ? 912  LEU A CB  1 
ATOM   7223  C  CG  . LEU A 1 1341 ? 113.187 120.940 90.086  1.00 21.56  ? 912  LEU A CG  1 
ATOM   7224  C  CD1 . LEU A 1 1341 ? 112.406 119.656 89.822  1.00 32.31  ? 912  LEU A CD1 1 
ATOM   7225  C  CD2 . LEU A 1 1341 ? 112.786 121.606 91.358  1.00 31.46  ? 912  LEU A CD2 1 
ATOM   7226  N  N   . SER A 1 1342 ? 117.864 121.940 90.426  1.00 26.11  ? 913  SER A N   1 
ATOM   7227  C  CA  . SER A 1 1342 ? 119.199 121.537 90.850  1.00 19.22  ? 913  SER A CA  1 
ATOM   7228  C  C   . SER A 1 1342 ? 119.535 122.188 92.177  1.00 28.77  ? 913  SER A C   1 
ATOM   7229  O  O   . SER A 1 1342 ? 119.932 123.350 92.228  1.00 33.23  ? 913  SER A O   1 
ATOM   7230  C  CB  . SER A 1 1342 ? 120.229 121.918 89.805  1.00 32.70  ? 913  SER A CB  1 
ATOM   7231  O  OG  . SER A 1 1342 ? 121.507 121.874 90.418  1.00 34.03  ? 913  SER A OG  1 
ATOM   7232  N  N   . PHE A 1 1343 ? 119.403 121.437 93.268  1.00 28.73  ? 914  PHE A N   1 
ATOM   7233  C  CA  . PHE A 1 1343 ? 119.911 121.888 94.558  1.00 21.10  ? 914  PHE A CA  1 
ATOM   7234  C  C   . PHE A 1 1343 ? 121.240 121.261 94.960  1.00 27.21  ? 914  PHE A C   1 
ATOM   7235  O  O   . PHE A 1 1343 ? 121.731 121.543 96.053  1.00 32.81  ? 914  PHE A O   1 
ATOM   7236  C  CB  . PHE A 1 1343 ? 118.913 121.589 95.617  1.00 17.44  ? 914  PHE A CB  1 
ATOM   7237  C  CG  . PHE A 1 1343 ? 117.720 122.408 95.518  1.00 21.90  ? 914  PHE A CG  1 
ATOM   7238  C  CD1 . PHE A 1 1343 ? 116.647 121.994 94.785  1.00 26.56  ? 914  PHE A CD1 1 
ATOM   7239  C  CD2 . PHE A 1 1343 ? 117.662 123.614 96.158  1.00 35.38  ? 914  PHE A CD2 1 
ATOM   7240  C  CE1 . PHE A 1 1343 ? 115.496 122.767 94.713  1.00 33.31  ? 914  PHE A CE1 1 
ATOM   7241  C  CE2 . PHE A 1 1343 ? 116.526 124.399 96.101  1.00 38.14  ? 914  PHE A CE2 1 
ATOM   7242  C  CZ  . PHE A 1 1343 ? 115.439 123.971 95.373  1.00 35.92  ? 914  PHE A CZ  1 
ATOM   7243  N  N   . LEU A 1 1344 ? 121.813 120.391 94.130  1.00 31.44  ? 915  LEU A N   1 
ATOM   7244  C  CA  . LEU A 1 1344 ? 123.098 119.748 94.404  1.00 26.81  ? 915  LEU A CA  1 
ATOM   7245  C  C   . LEU A 1 1344 ? 124.166 120.509 93.641  1.00 25.89  ? 915  LEU A C   1 
ATOM   7246  O  O   . LEU A 1 1344 ? 124.516 120.182 92.510  1.00 33.36  ? 915  LEU A O   1 
ATOM   7247  C  CB  . LEU A 1 1344 ? 123.080 118.282 94.002  1.00 31.69  ? 915  LEU A CB  1 
ATOM   7248  C  CG  . LEU A 1 1344 ? 122.136 117.394 94.803  1.00 42.89  ? 915  LEU A CG  1 
ATOM   7249  C  CD1 . LEU A 1 1344 ? 122.101 115.978 94.234  1.00 42.75  ? 915  LEU A CD1 1 
ATOM   7250  C  CD2 . LEU A 1 1344 ? 122.563 117.377 96.278  1.00 43.53  ? 915  LEU A CD2 1 
ATOM   7251  N  N   . ASN A 1 1345 ? 124.648 121.503 94.238  1.00 24.90  ? 916  ASN A N   1 
ATOM   7252  C  CA  . ASN A 1 1345 ? 125.641 122.280 93.516  1.00 24.84  ? 916  ASN A CA  1 
ATOM   7253  C  C   . ASN A 1 1345 ? 127.024 121.780 93.867  1.00 25.11  ? 916  ASN A C   1 
ATOM   7254  O  O   . ASN A 1 1345 ? 127.353 121.691 95.050  1.00 40.46  ? 916  ASN A O   1 
ATOM   7255  C  CB  . ASN A 1 1345 ? 125.523 123.738 93.872  1.00 33.35  ? 916  ASN A CB  1 
ATOM   7256  C  CG  . ASN A 1 1345 ? 126.360 124.622 92.988  1.00 50.08  ? 916  ASN A CG  1 
ATOM   7257  O  OD1 . ASN A 1 1345 ? 126.784 124.224 91.900  1.00 45.67  ? 916  ASN A OD1 1 
ATOM   7258  N  ND2 . ASN A 1 1345 ? 126.583 125.864 93.442  1.00 53.23  ? 916  ASN A ND2 1 
ATOM   7259  N  N   . PRO A 1 1346 ? 127.846 121.410 92.898  1.00 23.71  ? 917  PRO A N   1 
ATOM   7260  C  CA  . PRO A 1 1346 ? 129.177 120.911 93.240  1.00 28.10  ? 917  PRO A CA  1 
ATOM   7261  C  C   . PRO A 1 1346 ? 129.989 121.901 94.023  1.00 36.56  ? 917  PRO A C   1 
ATOM   7262  O  O   . PRO A 1 1346 ? 130.770 121.510 94.896  1.00 44.10  ? 917  PRO A O   1 
ATOM   7263  C  CB  . PRO A 1 1346 ? 129.816 120.637 91.878  1.00 30.39  ? 917  PRO A CB  1 
ATOM   7264  C  CG  . PRO A 1 1346 ? 128.709 120.451 90.986  1.00 37.07  ? 917  PRO A CG  1 
ATOM   7265  C  CD  . PRO A 1 1346 ? 127.621 121.377 91.457  1.00 37.38  ? 917  PRO A CD  1 
ATOM   7266  N  N   . GLU A 1 1347 ? 129.810 123.180 93.760  1.00 39.17  ? 918  GLU A N   1 
ATOM   7267  C  CA  . GLU A 1 1347 ? 130.591 124.186 94.453  1.00 36.34  ? 918  GLU A CA  1 
ATOM   7268  C  C   . GLU A 1 1347 ? 130.385 124.123 95.952  1.00 32.65  ? 918  GLU A C   1 
ATOM   7269  O  O   . GLU A 1 1347 ? 131.220 124.630 96.700  1.00 45.76  ? 918  GLU A O   1 
ATOM   7270  C  CB  . GLU A 1 1347 ? 130.202 125.547 93.886  1.00 48.25  ? 918  GLU A CB  1 
ATOM   7271  C  CG  . GLU A 1 1347 ? 131.019 126.746 94.269  1.00 59.87  ? 918  GLU A CG  1 
ATOM   7272  C  CD  . GLU A 1 1347 ? 130.706 127.925 93.324  1.00 69.46  ? 918  GLU A CD  1 
ATOM   7273  O  OE1 . GLU A 1 1347 ? 129.957 127.707 92.336  1.00 60.90  ? 918  GLU A OE1 1 
ATOM   7274  O  OE2 . GLU A 1 1347 ? 131.170 129.068 93.576  1.00 59.67  ? 918  GLU A OE2 1 
ATOM   7275  N  N   . LYS A 1 1348 ? 129.304 123.514 96.417  1.00 29.74  ? 919  LYS A N   1 
ATOM   7276  C  CA  . LYS A 1 1348 ? 129.117 123.504 97.854  1.00 29.45  ? 919  LYS A CA  1 
ATOM   7277  C  C   . LYS A 1 1348 ? 130.075 122.550 98.548  1.00 39.89  ? 919  LYS A C   1 
ATOM   7278  O  O   . LYS A 1 1348 ? 130.129 122.561 99.778  1.00 45.28  ? 919  LYS A O   1 
ATOM   7279  C  CB  . LYS A 1 1348 ? 127.688 123.133 98.210  1.00 45.49  ? 919  LYS A CB  1 
ATOM   7280  C  CG  . LYS A 1 1348 ? 126.637 123.845 97.368  1.00 53.94  ? 919  LYS A CG  1 
ATOM   7281  C  CD  . LYS A 1 1348 ? 126.817 125.357 97.367  1.00 56.42  ? 919  LYS A CD  1 
ATOM   7282  C  CE  . LYS A 1 1348 ? 126.391 125.969 98.693  1.00 62.99  ? 919  LYS A CE  1 
ATOM   7283  N  NZ  . LYS A 1 1348 ? 124.923 125.838 98.934  1.00 62.33  ? 919  LYS A NZ  1 
ATOM   7284  N  N   . CYS A 1 1349 ? 130.823 121.719 97.800  1.00 46.57  ? 920  CYS A N   1 
ATOM   7285  C  CA  . CYS A 1 1349 ? 131.907 120.900 98.372  1.00 39.92  ? 920  CYS A CA  1 
ATOM   7286  C  C   . CYS A 1 1349 ? 133.118 121.737 98.747  1.00 41.17  ? 920  CYS A C   1 
ATOM   7287  O  O   . CYS A 1 1349 ? 133.935 121.307 99.570  1.00 50.13  ? 920  CYS A O   1 
ATOM   7288  C  CB  . CYS A 1 1349 ? 132.390 119.843 97.377  1.00 34.26  ? 920  CYS A CB  1 
ATOM   7289  S  SG  . CYS A 1 1349 ? 131.139 118.709 96.763  1.00 62.96  ? 920  CYS A SG  1 
ATOM   7290  N  N   . PHE A 1 1350 ? 133.265 122.899 98.130  1.00 31.23  ? 921  PHE A N   1 
ATOM   7291  C  CA  . PHE A 1 1350 ? 134.350 123.797 98.433  1.00 25.84  ? 921  PHE A CA  1 
ATOM   7292  C  C   . PHE A 1 1350 ? 134.020 124.772 99.557  1.00 40.92  ? 921  PHE A C   1 
ATOM   7293  O  O   . PHE A 1 1350 ? 134.919 125.112 100.333 1.00 48.36  ? 921  PHE A O   1 
ATOM   7294  C  CB  . PHE A 1 1350 ? 134.723 124.548 97.176  1.00 23.23  ? 921  PHE A CB  1 
ATOM   7295  C  CG  . PHE A 1 1350 ? 135.204 123.674 96.151  1.00 18.94  ? 921  PHE A CG  1 
ATOM   7296  C  CD1 . PHE A 1 1350 ? 134.345 123.082 95.306  1.00 31.65  ? 921  PHE A CD1 1 
ATOM   7297  C  CD2 . PHE A 1 1350 ? 136.515 123.358 96.084  1.00 36.37  ? 921  PHE A CD2 1 
ATOM   7298  C  CE1 . PHE A 1 1350 ? 134.789 122.212 94.347  1.00 41.76  ? 921  PHE A CE1 1 
ATOM   7299  C  CE2 . PHE A 1 1350 ? 136.983 122.491 95.129  1.00 40.34  ? 921  PHE A CE2 1 
ATOM   7300  C  CZ  . PHE A 1 1350 ? 136.113 121.913 94.257  1.00 37.49  ? 921  PHE A CZ  1 
ATOM   7301  N  N   . TYR A 1 1351 ? 132.775 125.244 99.674  1.00 35.97  ? 922  TYR A N   1 
ATOM   7302  C  CA  . TYR A 1 1351 ? 132.429 126.112 100.791 1.00 28.97  ? 922  TYR A CA  1 
ATOM   7303  C  C   . TYR A 1 1351 ? 130.938 126.270 100.903 1.00 30.64  ? 922  TYR A C   1 
ATOM   7304  O  O   . TYR A 1 1351 ? 130.204 126.211 99.918  1.00 43.46  ? 922  TYR A O   1 
ATOM   7305  C  CB  . TYR A 1 1351 ? 133.016 127.486 100.648 1.00 35.59  ? 922  TYR A CB  1 
ATOM   7306  C  CG  . TYR A 1 1351 ? 132.934 127.987 99.249  1.00 40.18  ? 922  TYR A CG  1 
ATOM   7307  C  CD1 . TYR A 1 1351 ? 131.843 128.700 98.828  1.00 50.81  ? 922  TYR A CD1 1 
ATOM   7308  C  CD2 . TYR A 1 1351 ? 133.952 127.754 98.346  1.00 44.78  ? 922  TYR A CD2 1 
ATOM   7309  C  CE1 . TYR A 1 1351 ? 131.765 129.178 97.548  1.00 50.59  ? 922  TYR A CE1 1 
ATOM   7310  C  CE2 . TYR A 1 1351 ? 133.877 128.217 97.065  1.00 43.28  ? 922  TYR A CE2 1 
ATOM   7311  C  CZ  . TYR A 1 1351 ? 132.785 128.933 96.677  1.00 44.46  ? 922  TYR A CZ  1 
ATOM   7312  O  OH  . TYR A 1 1351 ? 132.709 129.407 95.399  1.00 53.36  ? 922  TYR A OH  1 
ATOM   7313  N  N   . ARG A 1 1352 ? 130.521 126.574 102.113 1.00 35.01  ? 923  ARG A N   1 
ATOM   7314  C  CA  . ARG A 1 1352 ? 129.112 126.470 102.452 1.00 40.59  ? 923  ARG A CA  1 
ATOM   7315  C  C   . ARG A 1 1352 ? 128.350 127.663 101.896 1.00 51.67  ? 923  ARG A C   1 
ATOM   7316  O  O   . ARG A 1 1352 ? 127.575 127.538 100.946 1.00 57.50  ? 923  ARG A O   1 
ATOM   7317  C  CB  . ARG A 1 1352 ? 128.977 126.437 103.971 1.00 59.61  ? 923  ARG A CB  1 
ATOM   7318  C  CG  . ARG A 1 1352 ? 127.571 126.489 104.476 1.00 68.19  ? 923  ARG A CG  1 
ATOM   7319  C  CD  . ARG A 1 1352 ? 126.899 125.130 104.365 1.00 76.52  ? 923  ARG A CD  1 
ATOM   7320  N  NE  . ARG A 1 1352 ? 127.606 124.151 105.200 1.00 75.48  ? 923  ARG A NE  1 
ATOM   7321  C  CZ  . ARG A 1 1352 ? 127.519 124.099 106.532 1.00 79.62  ? 923  ARG A CZ  1 
ATOM   7322  N  NH1 . ARG A 1 1352 ? 126.773 124.981 107.198 1.00 67.64  ? 923  ARG A NH1 1 
ATOM   7323  N  NH2 . ARG A 1 1352 ? 128.194 123.174 107.206 1.00 81.80  ? 923  ARG A NH2 1 
ATOM   7324  N  N   . ASN A 1 1353 ? 128.601 128.843 102.443 1.00 52.52  ? 924  ASN A N   1 
ATOM   7325  C  CA  . ASN A 1 1353 ? 127.830 130.004 102.048 1.00 41.22  ? 924  ASN A CA  1 
ATOM   7326  C  C   . ASN A 1 1353 ? 128.384 130.521 100.749 1.00 41.11  ? 924  ASN A C   1 
ATOM   7327  O  O   . ASN A 1 1353 ? 129.594 130.577 100.547 1.00 52.82  ? 924  ASN A O   1 
ATOM   7328  C  CB  . ASN A 1 1353 ? 127.896 131.087 103.103 1.00 59.52  ? 924  ASN A CB  1 
ATOM   7329  C  CG  . ASN A 1 1353 ? 127.113 130.724 104.329 1.00 81.49  ? 924  ASN A CG  1 
ATOM   7330  O  OD1 . ASN A 1 1353 ? 127.619 130.803 105.452 1.00 87.71  ? 924  ASN A OD1 1 
ATOM   7331  N  ND2 . ASN A 1 1353 ? 125.878 130.279 104.127 1.00 75.31  ? 924  ASN A ND2 1 
ATOM   7332  N  N   . LEU A 1 1354 ? 127.504 130.892 99.865  1.00 36.89  ? 925  LEU A N   1 
ATOM   7333  C  CA  . LEU A 1 1354 ? 127.895 131.121 98.498  1.00 38.86  ? 925  LEU A CA  1 
ATOM   7334  C  C   . LEU A 1 1354 ? 127.809 132.610 98.210  1.00 46.96  ? 925  LEU A C   1 
ATOM   7335  O  O   . LEU A 1 1354 ? 126.814 133.254 98.561  1.00 49.50  ? 925  LEU A O   1 
ATOM   7336  C  CB  . LEU A 1 1354 ? 126.990 130.277 97.607  1.00 55.60  ? 925  LEU A CB  1 
ATOM   7337  C  CG  . LEU A 1 1354 ? 127.263 129.950 96.150  1.00 55.86  ? 925  LEU A CG  1 
ATOM   7338  C  CD1 . LEU A 1 1354 ? 128.548 129.157 96.055  1.00 58.21  ? 925  LEU A CD1 1 
ATOM   7339  C  CD2 . LEU A 1 1354 ? 126.120 129.016 95.772  1.00 59.27  ? 925  LEU A CD2 1 
ATOM   7340  N  N   . GLY A 1 1355 ? 128.851 133.157 97.575  1.00 49.38  ? 926  GLY A N   1 
ATOM   7341  C  CA  . GLY A 1 1355 ? 128.907 134.601 97.380  1.00 53.78  ? 926  GLY A CA  1 
ATOM   7342  C  C   . GLY A 1 1355 ? 127.706 135.133 96.624  1.00 45.50  ? 926  GLY A C   1 
ATOM   7343  O  O   . GLY A 1 1355 ? 127.034 136.066 97.071  1.00 48.54  ? 926  GLY A O   1 
ATOM   7344  N  N   . ASP A 1 1356 ? 127.392 134.524 95.510  1.00 33.67  ? 927  ASP A N   1 
ATOM   7345  C  CA  . ASP A 1 1356 ? 126.176 134.922 94.827  1.00 27.71  ? 927  ASP A CA  1 
ATOM   7346  C  C   . ASP A 1 1356 ? 125.476 133.722 94.221  1.00 34.67  ? 927  ASP A C   1 
ATOM   7347  O  O   . ASP A 1 1356 ? 126.045 133.070 93.339  1.00 44.62  ? 927  ASP A O   1 
ATOM   7348  C  CB  . ASP A 1 1356 ? 126.493 135.921 93.734  1.00 35.29  ? 927  ASP A CB  1 
ATOM   7349  C  CG  . ASP A 1 1356 ? 125.234 136.567 93.160  1.00 53.68  ? 927  ASP A CG  1 
ATOM   7350  O  OD1 . ASP A 1 1356 ? 124.167 136.504 93.831  1.00 47.99  ? 927  ASP A OD1 1 
ATOM   7351  O  OD2 . ASP A 1 1356 ? 125.302 137.119 92.024  1.00 47.58  ? 927  ASP A OD2 1 
ATOM   7352  N  N   . PRO A 1 1357 ? 124.263 133.390 94.641  1.00 23.39  ? 928  PRO A N   1 
ATOM   7353  C  CA  . PRO A 1 1357 ? 123.640 132.186 94.101  1.00 20.35  ? 928  PRO A CA  1 
ATOM   7354  C  C   . PRO A 1 1357 ? 123.450 132.256 92.610  1.00 26.50  ? 928  PRO A C   1 
ATOM   7355  O  O   . PRO A 1 1357 ? 123.601 131.238 91.934  1.00 31.71  ? 928  PRO A O   1 
ATOM   7356  C  CB  . PRO A 1 1357 ? 122.295 132.133 94.805  1.00 26.66  ? 928  PRO A CB  1 
ATOM   7357  C  CG  . PRO A 1 1357 ? 122.046 133.522 95.172  1.00 38.64  ? 928  PRO A CG  1 
ATOM   7358  C  CD  . PRO A 1 1357 ? 123.357 134.124 95.511  1.00 31.96  ? 928  PRO A CD  1 
ATOM   7359  N  N   . VAL A 1 1358 ? 123.137 133.419 92.055  1.00 25.93  ? 929  VAL A N   1 
ATOM   7360  C  CA  . VAL A 1 1358 ? 122.937 133.452 90.620  1.00 16.92  ? 929  VAL A CA  1 
ATOM   7361  C  C   . VAL A 1 1358 ? 124.224 133.204 89.896  1.00 22.03  ? 929  VAL A C   1 
ATOM   7362  O  O   . VAL A 1 1358 ? 124.248 132.434 88.941  1.00 36.37  ? 929  VAL A O   1 
ATOM   7363  C  CB  . VAL A 1 1358 ? 122.318 134.759 90.171  1.00 19.91  ? 929  VAL A CB  1 
ATOM   7364  C  CG1 . VAL A 1 1358 ? 122.167 134.690 88.711  1.00 28.24  ? 929  VAL A CG1 1 
ATOM   7365  C  CG2 . VAL A 1 1358 ? 120.967 134.841 90.758  1.00 37.00  ? 929  VAL A CG2 1 
ATOM   7366  N  N   . THR A 1 1359 ? 125.312 133.826 90.312  1.00 18.11  ? 930  THR A N   1 
ATOM   7367  C  CA  . THR A 1 1359 ? 126.548 133.600 89.579  1.00 21.51  ? 930  THR A CA  1 
ATOM   7368  C  C   . THR A 1 1359 ? 127.050 132.167 89.720  1.00 31.58  ? 930  THR A C   1 
ATOM   7369  O  O   . THR A 1 1359 ? 127.524 131.570 88.744  1.00 39.41  ? 930  THR A O   1 
ATOM   7370  C  CB  . THR A 1 1359 ? 127.616 134.531 90.061  1.00 29.97  ? 930  THR A CB  1 
ATOM   7371  O  OG1 . THR A 1 1359 ? 127.788 134.317 91.458  1.00 36.00  ? 930  THR A OG1 1 
ATOM   7372  C  CG2 . THR A 1 1359 ? 127.178 135.932 89.844  1.00 37.72  ? 930  THR A CG2 1 
ATOM   7373  N  N   . SER A 1 1360 ? 126.972 131.594 90.920  1.00 32.27  ? 931  SER A N   1 
ATOM   7374  C  CA  . SER A 1 1360 ? 127.390 130.201 91.086  1.00 40.08  ? 931  SER A CA  1 
ATOM   7375  C  C   . SER A 1 1360 ? 126.504 129.264 90.286  1.00 37.83  ? 931  SER A C   1 
ATOM   7376  O  O   . SER A 1 1360 ? 126.996 128.351 89.616  1.00 44.81  ? 931  SER A O   1 
ATOM   7377  C  CB  . SER A 1 1360 ? 127.322 129.785 92.546  1.00 47.92  ? 931  SER A CB  1 
ATOM   7378  O  OG  . SER A 1 1360 ? 125.997 129.975 93.001  1.00 44.13  ? 931  SER A OG  1 
ATOM   7379  N  N   . GLY A 1 1361 ? 125.189 129.444 90.390  1.00 31.11  ? 932  GLY A N   1 
ATOM   7380  C  CA  . GLY A 1 1361 ? 124.288 128.623 89.613  1.00 32.26  ? 932  GLY A CA  1 
ATOM   7381  C  C   . GLY A 1 1361 ? 124.577 128.736 88.136  1.00 23.49  ? 932  GLY A C   1 
ATOM   7382  O  O   . GLY A 1 1361 ? 124.552 127.744 87.410  1.00 29.06  ? 932  GLY A O   1 
ATOM   7383  N  N   . LEU A 1 1362 ? 124.868 129.933 87.676  1.00 19.25  ? 933  LEU A N   1 
ATOM   7384  C  CA  . LEU A 1 1362 ? 125.126 130.062 86.274  1.00 20.98  ? 933  LEU A CA  1 
ATOM   7385  C  C   . LEU A 1 1362 ? 126.385 129.316 85.912  1.00 27.43  ? 933  LEU A C   1 
ATOM   7386  O  O   . LEU A 1 1362 ? 126.424 128.619 84.892  1.00 38.68  ? 933  LEU A O   1 
ATOM   7387  C  CB  . LEU A 1 1362 ? 125.212 131.523 85.887  1.00 27.32  ? 933  LEU A CB  1 
ATOM   7388  C  CG  . LEU A 1 1362 ? 123.858 132.232 85.895  1.00 29.40  ? 933  LEU A CG  1 
ATOM   7389  C  CD1 . LEU A 1 1362 ? 124.054 133.725 85.678  1.00 40.16  ? 933  LEU A CD1 1 
ATOM   7390  C  CD2 . LEU A 1 1362 ? 122.977 131.683 84.826  1.00 37.12  ? 933  LEU A CD2 1 
ATOM   7391  N  N   . PHE A 1 1363 ? 127.418 129.424 86.731  1.00 24.40  ? 934  PHE A N   1 
ATOM   7392  C  CA  . PHE A 1 1363 ? 128.644 128.710 86.396  1.00 30.34  ? 934  PHE A CA  1 
ATOM   7393  C  C   . PHE A 1 1363 ? 128.439 127.207 86.388  1.00 30.34  ? 934  PHE A C   1 
ATOM   7394  O  O   . PHE A 1 1363 ? 129.022 126.495 85.562  1.00 37.82  ? 934  PHE A O   1 
ATOM   7395  C  CB  . PHE A 1 1363 ? 129.742 129.051 87.369  1.00 36.12  ? 934  PHE A CB  1 
ATOM   7396  C  CG  . PHE A 1 1363 ? 130.942 128.254 87.164  1.00 25.99  ? 934  PHE A CG  1 
ATOM   7397  C  CD1 . PHE A 1 1363 ? 131.808 128.557 86.164  1.00 34.05  ? 934  PHE A CD1 1 
ATOM   7398  C  CD2 . PHE A 1 1363 ? 131.203 127.196 87.977  1.00 36.11  ? 934  PHE A CD2 1 
ATOM   7399  C  CE1 . PHE A 1 1363 ? 132.933 127.815 85.976  1.00 44.67  ? 934  PHE A CE1 1 
ATOM   7400  C  CE2 . PHE A 1 1363 ? 132.332 126.446 87.807  1.00 49.92  ? 934  PHE A CE2 1 
ATOM   7401  C  CZ  . PHE A 1 1363 ? 133.202 126.752 86.803  1.00 48.83  ? 934  PHE A CZ  1 
ATOM   7402  N  N   . GLN A 1 1364 ? 127.645 126.702 87.327  1.00 27.65  ? 935  GLN A N   1 
ATOM   7403  C  CA  . GLN A 1 1364 ? 127.357 125.278 87.352  1.00 23.51  ? 935  GLN A CA  1 
ATOM   7404  C  C   . GLN A 1 1364 ? 126.614 124.850 86.111  1.00 26.42  ? 935  GLN A C   1 
ATOM   7405  O  O   . GLN A 1 1364 ? 126.946 123.830 85.492  1.00 35.33  ? 935  GLN A O   1 
ATOM   7406  C  CB  . GLN A 1 1364 ? 126.518 124.934 88.548  1.00 21.29  ? 935  GLN A CB  1 
ATOM   7407  C  CG  . GLN A 1 1364 ? 125.927 123.602 88.409  1.00 22.16  ? 935  GLN A CG  1 
ATOM   7408  C  CD  . GLN A 1 1364 ? 124.800 123.429 89.366  1.00 35.12  ? 935  GLN A CD  1 
ATOM   7409  O  OE1 . GLN A 1 1364 ? 124.536 124.314 90.184  1.00 35.16  ? 935  GLN A OE1 1 
ATOM   7410  N  NE2 . GLN A 1 1364 ? 124.142 122.277 89.314  1.00 33.79  ? 935  GLN A NE2 1 
ATOM   7411  N  N   . LEU A 1 1365 ? 125.584 125.598 85.747  1.00 24.95  ? 936  LEU A N   1 
ATOM   7412  C  CA  . LEU A 1 1365 ? 124.831 125.239 84.560  1.00 22.85  ? 936  LEU A CA  1 
ATOM   7413  C  C   . LEU A 1 1365 ? 125.735 125.252 83.362  1.00 17.90  ? 936  LEU A C   1 
ATOM   7414  O  O   . LEU A 1 1365 ? 125.639 124.390 82.488  1.00 27.68  ? 936  LEU A O   1 
ATOM   7415  C  CB  . LEU A 1 1365 ? 123.669 126.193 84.360  1.00 18.84  ? 936  LEU A CB  1 
ATOM   7416  C  CG  . LEU A 1 1365 ? 122.775 125.767 83.232  1.00 22.13  ? 936  LEU A CG  1 
ATOM   7417  C  CD1 . LEU A 1 1365 ? 122.329 124.371 83.518  1.00 32.49  ? 936  LEU A CD1 1 
ATOM   7418  C  CD2 . LEU A 1 1365 ? 121.586 126.680 83.221  1.00 35.16  ? 936  LEU A CD2 1 
ATOM   7419  N  N   . LYS A 1 1366 ? 126.641 126.197 83.320  1.00 17.59  ? 937  LYS A N   1 
ATOM   7420  C  CA  . LYS A 1 1366 ? 127.490 126.267 82.162  1.00 20.57  ? 937  LYS A CA  1 
ATOM   7421  C  C   . LYS A 1 1366 ? 128.401 125.065 82.096  1.00 28.13  ? 937  LYS A C   1 
ATOM   7422  O  O   . LYS A 1 1366 ? 128.582 124.492 81.018  1.00 38.79  ? 937  LYS A O   1 
ATOM   7423  C  CB  . LYS A 1 1366 ? 128.296 127.550 82.174  1.00 43.26  ? 937  LYS A CB  1 
ATOM   7424  C  CG  . LYS A 1 1366 ? 129.368 127.584 81.094  1.00 57.65  ? 937  LYS A CG  1 
ATOM   7425  C  CD  . LYS A 1 1366 ? 130.109 128.934 81.026  1.00 71.20  ? 937  LYS A CD  1 
ATOM   7426  C  CE  . LYS A 1 1366 ? 129.208 130.077 80.513  1.00 68.69  ? 937  LYS A CE  1 
ATOM   7427  N  NZ  . LYS A 1 1366 ? 129.856 131.427 80.601  1.00 64.79  ? 937  LYS A NZ  1 
ATOM   7428  N  N   . THR A 1 1367 ? 128.977 124.651 83.230  1.00 28.96  ? 938  THR A N   1 
ATOM   7429  C  CA  . THR A 1 1367 ? 129.866 123.481 83.197  1.00 26.93  ? 938  THR A CA  1 
ATOM   7430  C  C   . THR A 1 1367 ? 129.115 122.198 82.858  1.00 32.03  ? 938  THR A C   1 
ATOM   7431  O  O   . THR A 1 1367 ? 129.617 121.365 82.092  1.00 40.01  ? 938  THR A O   1 
ATOM   7432  C  CB  . THR A 1 1367 ? 130.613 123.314 84.509  1.00 32.80  ? 938  THR A CB  1 
ATOM   7433  O  OG1 . THR A 1 1367 ? 131.441 124.462 84.747  1.00 44.08  ? 938  THR A OG1 1 
ATOM   7434  C  CG2 . THR A 1 1367 ? 131.449 122.064 84.490  1.00 39.94  ? 938  THR A CG2 1 
ATOM   7435  N  N   . TYR A 1 1368 ? 127.912 122.016 83.401  1.00 27.58  ? 939  TYR A N   1 
ATOM   7436  C  CA  . TYR A 1 1368 ? 127.113 120.858 83.009  1.00 25.39  ? 939  TYR A CA  1 
ATOM   7437  C  C   . TYR A 1 1368 ? 126.881 120.843 81.513  1.00 28.08  ? 939  TYR A C   1 
ATOM   7438  O  O   . TYR A 1 1368 ? 127.107 119.826 80.843  1.00 38.60  ? 939  TYR A O   1 
ATOM   7439  C  CB  . TYR A 1 1368 ? 125.774 120.901 83.696  1.00 28.30  ? 939  TYR A CB  1 
ATOM   7440  C  CG  . TYR A 1 1368 ? 124.977 119.648 83.596  1.00 27.71  ? 939  TYR A CG  1 
ATOM   7441  C  CD1 . TYR A 1 1368 ? 124.993 118.745 84.637  1.00 44.93  ? 939  TYR A CD1 1 
ATOM   7442  C  CD2 . TYR A 1 1368 ? 124.181 119.374 82.509  1.00 24.17  ? 939  TYR A CD2 1 
ATOM   7443  C  CE1 . TYR A 1 1368 ? 124.237 117.604 84.609  1.00 38.95  ? 939  TYR A CE1 1 
ATOM   7444  C  CE2 . TYR A 1 1368 ? 123.417 118.225 82.474  1.00 28.78  ? 939  TYR A CE2 1 
ATOM   7445  C  CZ  . TYR A 1 1368 ? 123.457 117.350 83.536  1.00 28.73  ? 939  TYR A CZ  1 
ATOM   7446  O  OH  . TYR A 1 1368 ? 122.738 116.191 83.563  1.00 39.56  ? 939  TYR A OH  1 
ATOM   7447  N  N   . LEU A 1 1369 ? 126.407 121.960 80.967  1.00 26.08  ? 940  LEU A N   1 
ATOM   7448  C  CA  . LEU A 1 1369 ? 126.123 121.946 79.550  1.00 20.62  ? 940  LEU A CA  1 
ATOM   7449  C  C   . LEU A 1 1369 ? 127.383 121.730 78.779  1.00 25.92  ? 940  LEU A C   1 
ATOM   7450  O  O   . LEU A 1 1369 ? 127.342 121.110 77.718  1.00 40.37  ? 940  LEU A O   1 
ATOM   7451  C  CB  . LEU A 1 1369 ? 125.440 123.221 79.105  1.00 19.55  ? 940  LEU A CB  1 
ATOM   7452  C  CG  . LEU A 1 1369 ? 124.104 123.253 79.835  1.00 28.40  ? 940  LEU A CG  1 
ATOM   7453  C  CD1 . LEU A 1 1369 ? 123.230 124.433 79.445  1.00 37.98  ? 940  LEU A CD1 1 
ATOM   7454  C  CD2 . LEU A 1 1369 ? 123.377 121.944 79.627  1.00 35.10  ? 940  LEU A CD2 1 
ATOM   7455  N  N   . ARG A 1 1370 ? 128.515 122.174 79.288  1.00 21.54  ? 941  ARG A N   1 
ATOM   7456  C  CA  . ARG A 1 1370 ? 129.698 121.872 78.510  1.00 31.00  ? 941  ARG A CA  1 
ATOM   7457  C  C   . ARG A 1 1370 ? 129.996 120.392 78.553  1.00 34.84  ? 941  ARG A C   1 
ATOM   7458  O  O   . ARG A 1 1370 ? 130.526 119.833 77.591  1.00 47.21  ? 941  ARG A O   1 
ATOM   7459  C  CB  . ARG A 1 1370 ? 130.896 122.694 78.970  1.00 45.79  ? 941  ARG A CB  1 
ATOM   7460  C  CG  . ARG A 1 1370 ? 132.147 122.496 78.095  1.00 50.21  ? 941  ARG A CG  1 
ATOM   7461  C  CD  . ARG A 1 1370 ? 133.041 123.743 78.096  1.00 52.81  ? 941  ARG A CD  1 
ATOM   7462  N  NE  . ARG A 1 1370 ? 133.739 123.927 79.363  1.00 62.47  ? 941  ARG A NE  1 
ATOM   7463  C  CZ  . ARG A 1 1370 ? 134.952 123.449 79.632  1.00 76.31  ? 941  ARG A CZ  1 
ATOM   7464  N  NH1 . ARG A 1 1370 ? 135.606 122.740 78.716  1.00 74.17  ? 941  ARG A NH1 1 
ATOM   7465  N  NH2 . ARG A 1 1370 ? 135.507 123.668 80.825  1.00 68.03  ? 941  ARG A NH2 1 
ATOM   7466  N  N   . MET A 1 1371 ? 129.649 119.737 79.642  1.00 34.22  ? 942  MET A N   1 
ATOM   7467  C  CA  . MET A 1 1371 ? 129.928 118.311 79.713  1.00 39.87  ? 942  MET A CA  1 
ATOM   7468  C  C   . MET A 1 1371 ? 129.085 117.559 78.697  1.00 32.28  ? 942  MET A C   1 
ATOM   7469  O  O   . MET A 1 1371 ? 129.615 116.854 77.832  1.00 36.90  ? 942  MET A O   1 
ATOM   7470  C  CB  . MET A 1 1371 ? 129.669 117.794 81.141  1.00 49.21  ? 942  MET A CB  1 
ATOM   7471  C  CG  . MET A 1 1371 ? 129.812 116.281 81.327  1.00 48.40  ? 942  MET A CG  1 
ATOM   7472  S  SD  . MET A 1 1371 ? 129.234 115.651 82.922  1.00 43.61  ? 942  MET A SD  1 
ATOM   7473  C  CE  . MET A 1 1371 ? 127.504 116.098 82.859  1.00 39.21  ? 942  MET A CE  1 
ATOM   7474  N  N   . ILE A 1 1372 ? 127.774 117.759 78.735  1.00 31.57  ? 943  ILE A N   1 
ATOM   7475  C  CA  . ILE A 1 1372 ? 126.901 116.908 77.934  1.00 36.24  ? 943  ILE A CA  1 
ATOM   7476  C  C   . ILE A 1 1372 ? 126.859 117.423 76.492  1.00 41.31  ? 943  ILE A C   1 
ATOM   7477  O  O   . ILE A 1 1372 ? 126.043 116.968 75.680  1.00 47.82  ? 943  ILE A O   1 
ATOM   7478  C  CB  . ILE A 1 1372 ? 125.480 116.788 78.552  1.00 34.28  ? 943  ILE A CB  1 
ATOM   7479  C  CG1 . ILE A 1 1372 ? 124.800 118.157 78.743  1.00 41.02  ? 943  ILE A CG1 1 
ATOM   7480  C  CG2 . ILE A 1 1372 ? 125.487 116.022 79.848  1.00 31.52  ? 943  ILE A CG2 1 
ATOM   7481  C  CD1 . ILE A 1 1372 ? 123.301 118.068 79.110  1.00 37.88  ? 943  ILE A CD1 1 
ATOM   7482  N  N   . GLU A 1 1373 ? 127.741 118.359 76.156  1.00 31.21  ? 944  GLU A N   1 
ATOM   7483  C  CA  . GLU A 1 1373 ? 127.818 118.887 74.801  1.00 27.38  ? 944  GLU A CA  1 
ATOM   7484  C  C   . GLU A 1 1373 ? 126.461 119.377 74.342  1.00 25.95  ? 944  GLU A C   1 
ATOM   7485  O  O   . GLU A 1 1373 ? 125.888 118.881 73.381  1.00 35.35  ? 944  GLU A O   1 
ATOM   7486  C  CB  . GLU A 1 1373 ? 128.352 117.846 73.831  1.00 40.90  ? 944  GLU A CB  1 
ATOM   7487  C  CG  . GLU A 1 1373 ? 129.808 117.489 74.093  1.00 62.58  ? 944  GLU A CG  1 
ATOM   7488  C  CD  . GLU A 1 1373 ? 130.738 118.711 74.073  1.00 75.52  ? 944  GLU A CD  1 
ATOM   7489  O  OE1 . GLU A 1 1373 ? 131.546 118.866 75.025  1.00 64.53  ? 944  GLU A OE1 1 
ATOM   7490  O  OE2 . GLU A 1 1373 ? 130.640 119.536 73.134  1.00 74.38  ? 944  GLU A OE2 1 
ATOM   7491  N  N   . MET A 1 1374 ? 125.922 120.317 75.084  1.00 31.80  ? 945  MET A N   1 
ATOM   7492  C  CA  . MET A 1 1374 ? 124.719 121.030 74.713  1.00 28.47  ? 945  MET A CA  1 
ATOM   7493  C  C   . MET A 1 1374 ? 124.889 122.500 75.038  1.00 39.83  ? 945  MET A C   1 
ATOM   7494  O  O   . MET A 1 1374 ? 123.995 123.153 75.583  1.00 45.16  ? 945  MET A O   1 
ATOM   7495  C  CB  . MET A 1 1374 ? 123.540 120.459 75.452  1.00 38.75  ? 945  MET A CB  1 
ATOM   7496  C  CG  . MET A 1 1374 ? 123.164 119.099 74.960  1.00 63.63  ? 945  MET A CG  1 
ATOM   7497  S  SD  . MET A 1 1374 ? 121.764 118.458 75.908  1.00 135.24 ? 945  MET A SD  1 
ATOM   7498  C  CE  . MET A 1 1374 ? 121.458 116.888 75.085  1.00 86.06  ? 945  MET A CE  1 
ATOM   7499  N  N   . ASP A 1 1375 ? 126.075 123.034 74.724  1.00 36.10  ? 946  ASP A N   1 
ATOM   7500  C  CA  . ASP A 1 1375 ? 126.359 124.437 75.002  1.00 32.74  ? 946  ASP A CA  1 
ATOM   7501  C  C   . ASP A 1 1375 ? 125.258 125.328 74.465  1.00 33.00  ? 946  ASP A C   1 
ATOM   7502  O  O   . ASP A 1 1375 ? 124.789 126.230 75.155  1.00 35.25  ? 946  ASP A O   1 
ATOM   7503  C  CB  . ASP A 1 1375 ? 127.695 124.817 74.378  1.00 36.35  ? 946  ASP A CB  1 
ATOM   7504  C  CG  . ASP A 1 1375 ? 128.865 124.172 75.092  1.00 53.70  ? 946  ASP A CG  1 
ATOM   7505  O  OD1 . ASP A 1 1375 ? 128.892 124.235 76.343  1.00 54.48  ? 946  ASP A OD1 1 
ATOM   7506  O  OD2 . ASP A 1 1375 ? 129.733 123.570 74.420  1.00 53.53  ? 946  ASP A OD2 1 
ATOM   7507  N  N   . ASP A 1 1376 ? 124.812 125.065 73.245  1.00 37.42  ? 947  ASP A N   1 
ATOM   7508  C  CA  . ASP A 1 1376 ? 123.838 125.932 72.617  1.00 36.81  ? 947  ASP A CA  1 
ATOM   7509  C  C   . ASP A 1 1376 ? 122.535 125.960 73.379  1.00 31.78  ? 947  ASP A C   1 
ATOM   7510  O  O   . ASP A 1 1376 ? 121.700 126.828 73.125  1.00 41.39  ? 947  ASP A O   1 
ATOM   7511  C  CB  . ASP A 1 1376 ? 123.634 125.481 71.172  1.00 42.54  ? 947  ASP A CB  1 
ATOM   7512  C  CG  . ASP A 1 1376 ? 123.353 123.993 71.068  1.00 51.73  ? 947  ASP A CG  1 
ATOM   7513  O  OD1 . ASP A 1 1376 ? 123.373 123.324 72.124  1.00 50.26  ? 947  ASP A OD1 1 
ATOM   7514  O  OD2 . ASP A 1 1376 ? 123.148 123.482 69.940  1.00 61.97  ? 947  ASP A OD2 1 
ATOM   7515  N  N   . LEU A 1 1377 ? 122.343 125.059 74.311  1.00 29.15  ? 948  LEU A N   1 
ATOM   7516  C  CA  . LEU A 1 1377 ? 121.116 125.055 75.069  1.00 32.23  ? 948  LEU A CA  1 
ATOM   7517  C  C   . LEU A 1 1377 ? 121.210 125.971 76.255  1.00 38.62  ? 948  LEU A C   1 
ATOM   7518  O  O   . LEU A 1 1377 ? 120.291 126.000 77.079  1.00 46.76  ? 948  LEU A O   1 
ATOM   7519  C  CB  . LEU A 1 1377 ? 120.803 123.640 75.530  1.00 42.54  ? 948  LEU A CB  1 
ATOM   7520  C  CG  . LEU A 1 1377 ? 119.375 123.299 75.902  1.00 54.24  ? 948  LEU A CG  1 
ATOM   7521  C  CD1 . LEU A 1 1377 ? 118.442 123.642 74.751  1.00 55.60  ? 948  LEU A CD1 1 
ATOM   7522  C  CD2 . LEU A 1 1377 ? 119.310 121.819 76.266  1.00 61.11  ? 948  LEU A CD2 1 
ATOM   7523  N  N   . PHE A 1 1378 ? 122.306 126.728 76.354  1.00 39.72  ? 949  PHE A N   1 
ATOM   7524  C  CA  . PHE A 1 1378 ? 122.593 127.526 77.548  1.00 45.79  ? 949  PHE A CA  1 
ATOM   7525  C  C   . PHE A 1 1378 ? 121.585 128.659 77.716  1.00 46.42  ? 949  PHE A C   1 
ATOM   7526  O  O   . PHE A 1 1378 ? 120.765 128.645 78.646  1.00 43.45  ? 949  PHE A O   1 
ATOM   7527  C  CB  . PHE A 1 1378 ? 124.032 128.071 77.482  1.00 39.01  ? 949  PHE A CB  1 
ATOM   7528  C  CG  . PHE A 1 1378 ? 124.487 128.710 78.740  1.00 29.85  ? 949  PHE A CG  1 
ATOM   7529  C  CD1 . PHE A 1 1378 ? 125.063 129.946 78.732  1.00 39.58  ? 949  PHE A CD1 1 
ATOM   7530  C  CD2 . PHE A 1 1378 ? 124.301 128.076 79.950  1.00 45.41  ? 949  PHE A CD2 1 
ATOM   7531  C  CE1 . PHE A 1 1378 ? 125.488 130.543 79.928  1.00 55.74  ? 949  PHE A CE1 1 
ATOM   7532  C  CE2 . PHE A 1 1378 ? 124.717 128.660 81.158  1.00 48.81  ? 949  PHE A CE2 1 
ATOM   7533  C  CZ  . PHE A 1 1378 ? 125.313 129.894 81.146  1.00 47.16  ? 949  PHE A CZ  1 
ATOM   7534  N  N   . LEU A 1 1379 ? 121.595 129.612 76.784  1.00 39.95  ? 950  LEU A N   1 
ATOM   7535  C  CA  . LEU A 1 1379 ? 120.898 130.864 76.965  1.00 24.03  ? 950  LEU A CA  1 
ATOM   7536  C  C   . LEU A 1 1379 ? 119.436 130.559 77.156  1.00 27.59  ? 950  LEU A C   1 
ATOM   7537  O  O   . LEU A 1 1379 ? 118.839 131.044 78.115  1.00 44.40  ? 950  LEU A O   1 
ATOM   7538  C  CB  . LEU A 1 1379 ? 121.065 131.790 75.790  1.00 25.10  ? 950  LEU A CB  1 
ATOM   7539  C  CG  . LEU A 1 1379 ? 122.415 132.472 75.918  1.00 37.20  ? 950  LEU A CG  1 
ATOM   7540  C  CD1 . LEU A 1 1379 ? 122.400 133.247 77.218  1.00 52.92  ? 950  LEU A CD1 1 
ATOM   7541  C  CD2 . LEU A 1 1379 ? 123.656 131.573 75.736  1.00 34.89  ? 950  LEU A CD2 1 
ATOM   7542  N  N   . PRO A 1 1380 ? 118.842 129.724 76.327  1.00 16.40  ? 951  PRO A N   1 
ATOM   7543  C  CA  . PRO A 1 1380 ? 117.431 129.414 76.532  1.00 20.83  ? 951  PRO A CA  1 
ATOM   7544  C  C   . PRO A 1 1380 ? 117.090 128.881 77.896  1.00 28.31  ? 951  PRO A C   1 
ATOM   7545  O  O   . PRO A 1 1380 ? 116.046 129.259 78.430  1.00 38.06  ? 951  PRO A O   1 
ATOM   7546  C  CB  . PRO A 1 1380 ? 117.154 128.385 75.448  1.00 34.82  ? 951  PRO A CB  1 
ATOM   7547  C  CG  . PRO A 1 1380 ? 118.071 128.770 74.395  1.00 41.22  ? 951  PRO A CG  1 
ATOM   7548  C  CD  . PRO A 1 1380 ? 119.315 129.216 75.044  1.00 24.90  ? 951  PRO A CD  1 
ATOM   7549  N  N   . LEU A 1 1381 ? 117.903 128.019 78.485  1.00 28.64  ? 952  LEU A N   1 
ATOM   7550  C  CA  . LEU A 1 1381 ? 117.578 127.566 79.833  1.00 33.48  ? 952  LEU A CA  1 
ATOM   7551  C  C   . LEU A 1 1381 ? 117.576 128.722 80.828  1.00 48.23  ? 952  LEU A C   1 
ATOM   7552  O  O   . LEU A 1 1381 ? 116.778 128.744 81.776  1.00 47.74  ? 952  LEU A O   1 
ATOM   7553  C  CB  . LEU A 1 1381 ? 118.579 126.523 80.291  1.00 41.47  ? 952  LEU A CB  1 
ATOM   7554  C  CG  . LEU A 1 1381 ? 118.398 125.173 79.652  1.00 52.81  ? 952  LEU A CG  1 
ATOM   7555  C  CD1 . LEU A 1 1381 ? 119.558 124.258 80.048  1.00 53.43  ? 952  LEU A CD1 1 
ATOM   7556  C  CD2 . LEU A 1 1381 ? 117.066 124.640 80.112  1.00 60.30  ? 952  LEU A CD2 1 
ATOM   7557  N  N   . ILE A 1 1382 ? 118.505 129.665 80.652  1.00 46.75  ? 953  ILE A N   1 
ATOM   7558  C  CA  . ILE A 1 1382 ? 118.628 130.814 81.547  1.00 38.31  ? 953  ILE A CA  1 
ATOM   7559  C  C   . ILE A 1 1382 ? 117.475 131.773 81.343  1.00 45.17  ? 953  ILE A C   1 
ATOM   7560  O  O   . ILE A 1 1382 ? 116.621 131.946 82.217  1.00 52.10  ? 953  ILE A O   1 
ATOM   7561  C  CB  . ILE A 1 1382 ? 119.955 131.540 81.294  1.00 40.41  ? 953  ILE A CB  1 
ATOM   7562  C  CG1 . ILE A 1 1382 ? 121.094 130.541 81.274  1.00 56.59  ? 953  ILE A CG1 1 
ATOM   7563  C  CG2 . ILE A 1 1382 ? 120.208 132.597 82.320  1.00 41.78  ? 953  ILE A CG2 1 
ATOM   7564  C  CD1 . ILE A 1 1382 ? 122.307 131.149 80.682  1.00 58.67  ? 953  ILE A CD1 1 
ATOM   7565  N  N   . ALA A 1 1383 ? 117.433 132.400 80.175  1.00 41.69  ? 954  ALA A N   1 
ATOM   7566  C  CA  . ALA A 1 1383 ? 116.452 133.434 79.919  1.00 43.67  ? 954  ALA A CA  1 
ATOM   7567  C  C   . ALA A 1 1383 ? 115.075 132.847 80.069  1.00 33.24  ? 954  ALA A C   1 
ATOM   7568  O  O   . ALA A 1 1383 ? 114.627 132.079 79.217  1.00 47.52  ? 954  ALA A O   1 
ATOM   7569  C  CB  . ALA A 1 1383 ? 116.607 134.006 78.507  1.00 57.77  ? 954  ALA A CB  1 
ATOM   7570  N  N   . LYS A 1 1384 ? 114.402 133.175 81.141  1.00 24.47  ? 955  LYS A N   1 
ATOM   7571  C  CA  . LYS A 1 1384 ? 113.015 132.791 81.217  1.00 40.65  ? 955  LYS A CA  1 
ATOM   7572  C  C   . LYS A 1 1384 ? 112.153 134.037 81.142  1.00 47.29  ? 955  LYS A C   1 
ATOM   7573  O  O   . LYS A 1 1384 ? 112.643 135.168 81.111  1.00 52.69  ? 955  LYS A O   1 
ATOM   7574  C  CB  . LYS A 1 1384 ? 112.744 131.992 82.492  1.00 51.14  ? 955  LYS A CB  1 
ATOM   7575  C  CG  . LYS A 1 1384 ? 113.350 130.604 82.432  1.00 54.42  ? 955  LYS A CG  1 
ATOM   7576  C  CD  . LYS A 1 1384 ? 113.214 129.855 83.754  1.00 54.23  ? 955  LYS A CD  1 
ATOM   7577  C  CE  . LYS A 1 1384 ? 113.859 128.463 83.673  1.00 57.29  ? 955  LYS A CE  1 
ATOM   7578  N  NZ  . LYS A 1 1384 ? 113.110 127.521 82.773  1.00 63.33  ? 955  LYS A NZ  1 
ATOM   7579  N  N   . ASN A 1 1385 ? 110.864 133.822 81.089  1.00 48.87  ? 956  ASN A N   1 
ATOM   7580  C  CA  . ASN A 1 1385 ? 109.949 134.940 81.185  1.00 49.01  ? 956  ASN A CA  1 
ATOM   7581  C  C   . ASN A 1 1385 ? 109.917 135.402 82.630  1.00 39.05  ? 956  ASN A C   1 
ATOM   7582  O  O   . ASN A 1 1385 ? 109.562 134.618 83.517  1.00 43.88  ? 956  ASN A O   1 
ATOM   7583  C  CB  . ASN A 1 1385 ? 108.558 134.536 80.718  1.00 62.07  ? 956  ASN A CB  1 
ATOM   7584  C  CG  . ASN A 1 1385 ? 108.508 134.250 79.221  1.00 75.38  ? 956  ASN A CG  1 
ATOM   7585  O  OD1 . ASN A 1 1385 ? 109.151 134.936 78.425  1.00 63.69  ? 956  ASN A OD1 1 
ATOM   7586  N  ND2 . ASN A 1 1385 ? 107.758 133.213 78.836  1.00 78.21  ? 956  ASN A ND2 1 
ATOM   7587  N  N   . PRO A 1 1386 ? 110.293 136.632 82.913  1.00 28.94  ? 957  PRO A N   1 
ATOM   7588  C  CA  . PRO A 1 1386 ? 110.231 137.113 84.281  1.00 25.96  ? 957  PRO A CA  1 
ATOM   7589  C  C   . PRO A 1 1386 ? 108.813 137.027 84.770  1.00 22.91  ? 957  PRO A C   1 
ATOM   7590  O  O   . PRO A 1 1386 ? 107.866 137.182 84.007  1.00 32.61  ? 957  PRO A O   1 
ATOM   7591  C  CB  . PRO A 1 1386 ? 110.689 138.562 84.172  1.00 40.15  ? 957  PRO A CB  1 
ATOM   7592  C  CG  . PRO A 1 1386 ? 110.393 138.916 82.757  1.00 45.92  ? 957  PRO A CG  1 
ATOM   7593  C  CD  . PRO A 1 1386 ? 110.636 137.690 81.965  1.00 44.56  ? 957  PRO A CD  1 
ATOM   7594  N  N   . GLY A 1 1387 ? 108.676 136.733 86.047  1.00 30.54  ? 958  GLY A N   1 
ATOM   7595  C  CA  . GLY A 1 1387 ? 107.374 136.607 86.655  1.00 39.20  ? 958  GLY A CA  1 
ATOM   7596  C  C   . GLY A 1 1387 ? 106.870 137.928 87.176  1.00 34.52  ? 958  GLY A C   1 
ATOM   7597  O  O   . GLY A 1 1387 ? 107.482 138.977 87.002  1.00 41.65  ? 958  GLY A O   1 
ATOM   7598  N  N   . ASN A 1 1388 ? 105.720 137.870 87.821  1.00 35.53  ? 959  ASN A N   1 
ATOM   7599  C  CA  . ASN A 1 1388 ? 105.104 139.056 88.395  1.00 40.67  ? 959  ASN A CA  1 
ATOM   7600  C  C   . ASN A 1 1388 ? 105.282 139.011 89.897  1.00 49.85  ? 959  ASN A C   1 
ATOM   7601  O  O   . ASN A 1 1388 ? 104.470 138.435 90.619  1.00 54.10  ? 959  ASN A O   1 
ATOM   7602  C  CB  . ASN A 1 1388 ? 103.642 139.147 88.016  1.00 50.18  ? 959  ASN A CB  1 
ATOM   7603  C  CG  . ASN A 1 1388 ? 103.461 139.450 86.555  1.00 65.95  ? 959  ASN A CG  1 
ATOM   7604  O  OD1 . ASN A 1 1388 ? 104.429 139.440 85.787  1.00 62.06  ? 959  ASN A OD1 1 
ATOM   7605  N  ND2 . ASN A 1 1388 ? 102.221 139.739 86.154  1.00 68.24  ? 959  ASN A ND2 1 
ATOM   7606  N  N   . CYS A 1 1389 ? 106.342 139.652 90.370  1.00 52.43  ? 960  CYS A N   1 
ATOM   7607  C  CA  . CYS A 1 1389 ? 106.663 139.685 91.788  1.00 52.41  ? 960  CYS A CA  1 
ATOM   7608  C  C   . CYS A 1 1389 ? 106.802 141.122 92.241  1.00 40.77  ? 960  CYS A C   1 
ATOM   7609  O  O   . CYS A 1 1389 ? 107.454 141.933 91.579  1.00 45.90  ? 960  CYS A O   1 
ATOM   7610  C  CB  . CYS A 1 1389 ? 107.946 138.899 92.089  1.00 67.96  ? 960  CYS A CB  1 
ATOM   7611  S  SG  . CYS A 1 1389 ? 107.848 137.082 91.738  1.00 86.03  ? 960  CYS A SG  1 
ATOM   7612  N  N   . THR A 1 1390 ? 106.200 141.424 93.372  1.00 43.92  ? 961  THR A N   1 
ATOM   7613  C  CA  . THR A 1 1390 ? 106.186 142.791 93.840  1.00 55.51  ? 961  THR A CA  1 
ATOM   7614  C  C   . THR A 1 1390 ? 107.520 143.142 94.482  1.00 40.37  ? 961  THR A C   1 
ATOM   7615  O  O   . THR A 1 1390 ? 108.429 142.325 94.602  1.00 44.17  ? 961  THR A O   1 
ATOM   7616  C  CB  . THR A 1 1390 ? 105.050 142.999 94.834  1.00 68.21  ? 961  THR A CB  1 
ATOM   7617  O  OG1 . THR A 1 1390 ? 105.310 142.225 96.014  1.00 66.56  ? 961  THR A OG1 1 
ATOM   7618  C  CG2 . THR A 1 1390 ? 103.711 142.560 94.215  1.00 63.82  ? 961  THR A CG2 1 
ATOM   7619  N  N   . ALA A 1 1391 ? 107.641 144.386 94.890  1.00 31.71  ? 962  ALA A N   1 
ATOM   7620  C  CA  . ALA A 1 1391 ? 108.858 144.739 95.557  1.00 30.86  ? 962  ALA A CA  1 
ATOM   7621  C  C   . ALA A 1 1391 ? 108.962 144.050 96.889  1.00 38.38  ? 962  ALA A C   1 
ATOM   7622  O  O   . ALA A 1 1391 ? 110.077 143.907 97.404  1.00 52.60  ? 962  ALA A O   1 
ATOM   7623  C  CB  . ALA A 1 1391 ? 108.954 146.250 95.722  1.00 52.08  ? 962  ALA A CB  1 
ATOM   7624  N  N   . ILE A 1 1392 ? 107.849 143.615 97.473  1.00 32.34  ? 963  ILE A N   1 
ATOM   7625  C  CA  . ILE A 1 1392 ? 107.989 142.935 98.752  1.00 35.38  ? 963  ILE A CA  1 
ATOM   7626  C  C   . ILE A 1 1392 ? 108.827 141.680 98.579  1.00 59.19  ? 963  ILE A C   1 
ATOM   7627  O  O   . ILE A 1 1392 ? 109.669 141.352 99.429  1.00 62.74  ? 963  ILE A O   1 
ATOM   7628  C  CB  . ILE A 1 1392 ? 106.631 142.594 99.366  1.00 44.46  ? 963  ILE A CB  1 
ATOM   7629  C  CG1 . ILE A 1 1392 ? 105.759 143.838 99.433  1.00 66.23  ? 963  ILE A CG1 1 
ATOM   7630  C  CG2 . ILE A 1 1392 ? 106.858 142.036 100.767 1.00 46.64  ? 963  ILE A CG2 1 
ATOM   7631  C  CD1 . ILE A 1 1392 ? 104.353 143.568 99.978  1.00 75.74  ? 963  ILE A CD1 1 
ATOM   7632  N  N   . ASP A 1 1393 ? 108.613 140.953 97.473  1.00 61.44  ? 964  ASP A N   1 
ATOM   7633  C  CA  . ASP A 1 1393 ? 109.371 139.725 97.219  1.00 56.53  ? 964  ASP A CA  1 
ATOM   7634  C  C   . ASP A 1 1393 ? 110.842 140.028 97.005  1.00 36.66  ? 964  ASP A C   1 
ATOM   7635  O  O   . ASP A 1 1393 ? 111.713 139.319 97.514  1.00 46.30  ? 964  ASP A O   1 
ATOM   7636  C  CB  . ASP A 1 1393 ? 108.783 138.987 96.010  1.00 68.46  ? 964  ASP A CB  1 
ATOM   7637  C  CG  . ASP A 1 1393 ? 107.313 138.542 96.238  1.00 83.24  ? 964  ASP A CG  1 
ATOM   7638  O  OD1 . ASP A 1 1393 ? 106.941 138.233 97.396  1.00 79.43  ? 964  ASP A OD1 1 
ATOM   7639  O  OD2 . ASP A 1 1393 ? 106.520 138.535 95.262  1.00 76.39  ? 964  ASP A OD2 1 
ATOM   7640  N  N   . PHE A 1 1394 ? 111.129 141.093 96.282  1.00 33.70  ? 965  PHE A N   1 
ATOM   7641  C  CA  . PHE A 1 1394 ? 112.509 141.458 96.074  1.00 29.96  ? 965  PHE A CA  1 
ATOM   7642  C  C   . PHE A 1 1394 ? 113.197 141.737 97.377  1.00 29.99  ? 965  PHE A C   1 
ATOM   7643  O  O   . PHE A 1 1394 ? 114.349 141.351 97.570  1.00 44.70  ? 965  PHE A O   1 
ATOM   7644  C  CB  . PHE A 1 1394 ? 112.594 142.683 95.201  1.00 39.72  ? 965  PHE A CB  1 
ATOM   7645  C  CG  . PHE A 1 1394 ? 113.969 143.021 94.845  1.00 46.00  ? 965  PHE A CG  1 
ATOM   7646  C  CD1 . PHE A 1 1394 ? 114.866 142.008 94.548  1.00 51.65  ? 965  PHE A CD1 1 
ATOM   7647  C  CD2 . PHE A 1 1394 ? 114.377 144.337 94.739  1.00 63.89  ? 965  PHE A CD2 1 
ATOM   7648  C  CE1 . PHE A 1 1394 ? 116.181 142.293 94.183  1.00 65.75  ? 965  PHE A CE1 1 
ATOM   7649  C  CE2 . PHE A 1 1394 ? 115.695 144.653 94.369  1.00 75.74  ? 965  PHE A CE2 1 
ATOM   7650  C  CZ  . PHE A 1 1394 ? 116.599 143.623 94.083  1.00 76.13  ? 965  PHE A CZ  1 
ATOM   7651  N  N   . VAL A 1 1395 ? 112.532 142.445 98.272  1.00 37.28  ? 966  VAL A N   1 
ATOM   7652  C  CA  . VAL A 1 1395 ? 113.183 142.772 99.530  1.00 40.20  ? 966  VAL A CA  1 
ATOM   7653  C  C   . VAL A 1 1395 ? 113.336 141.526 100.393 1.00 49.41  ? 966  VAL A C   1 
ATOM   7654  O  O   . VAL A 1 1395 ? 114.349 141.364 101.086 1.00 52.70  ? 966  VAL A O   1 
ATOM   7655  C  CB  . VAL A 1 1395 ? 112.414 143.889 100.252 1.00 55.09  ? 966  VAL A CB  1 
ATOM   7656  C  CG1 . VAL A 1 1395 ? 112.964 144.098 101.655 1.00 60.98  ? 966  VAL A CG1 1 
ATOM   7657  C  CG2 . VAL A 1 1395 ? 112.489 145.183 99.435  1.00 58.94  ? 966  VAL A CG2 1 
ATOM   7658  N  N   . LEU A 1 1396 ? 112.346 140.617 100.358 1.00 49.47  ? 967  LEU A N   1 
ATOM   7659  C  CA  . LEU A 1 1396 ? 112.439 139.375 101.136 1.00 47.57  ? 967  LEU A CA  1 
ATOM   7660  C  C   . LEU A 1 1396 ? 113.491 138.406 100.596 1.00 57.88  ? 967  LEU A C   1 
ATOM   7661  O  O   . LEU A 1 1396 ? 114.026 137.588 101.356 1.00 60.69  ? 967  LEU A O   1 
ATOM   7662  C  CB  . LEU A 1 1396 ? 111.095 138.668 101.179 1.00 38.29  ? 967  LEU A CB  1 
ATOM   7663  C  CG  . LEU A 1 1396 ? 110.120 139.436 102.037 1.00 58.05  ? 967  LEU A CG  1 
ATOM   7664  C  CD1 . LEU A 1 1396 ? 108.731 138.817 101.929 1.00 68.27  ? 967  LEU A CD1 1 
ATOM   7665  C  CD2 . LEU A 1 1396 ? 110.646 139.427 103.472 1.00 60.30  ? 967  LEU A CD2 1 
ATOM   7666  N  N   . ASN A 1 1397 ? 113.774 138.441 99.297  1.00 47.96  ? 968  ASN A N   1 
ATOM   7667  C  CA  . ASN A 1 1397 ? 114.745 137.548 98.679  1.00 28.15  ? 968  ASN A CA  1 
ATOM   7668  C  C   . ASN A 1 1397 ? 115.659 138.342 97.771  1.00 31.91  ? 968  ASN A C   1 
ATOM   7669  O  O   . ASN A 1 1397 ? 115.503 138.313 96.545  1.00 43.40  ? 968  ASN A O   1 
ATOM   7670  C  CB  . ASN A 1 1397 ? 114.048 136.467 97.877  1.00 41.48  ? 968  ASN A CB  1 
ATOM   7671  C  CG  . ASN A 1 1397 ? 114.784 135.153 97.943  1.00 70.36  ? 968  ASN A CG  1 
ATOM   7672  O  OD1 . ASN A 1 1397 ? 115.473 134.870 98.929  1.00 67.84  ? 968  ASN A OD1 1 
ATOM   7673  N  ND2 . ASN A 1 1397 ? 114.692 134.360 96.872  1.00 65.84  ? 968  ASN A ND2 1 
ATOM   7674  N  N   . PRO A 1 1398 ? 116.617 139.039 98.318  1.00 31.41  ? 969  PRO A N   1 
ATOM   7675  C  CA  . PRO A 1 1398 ? 117.380 139.992 97.511  1.00 27.90  ? 969  PRO A CA  1 
ATOM   7676  C  C   . PRO A 1 1398 ? 118.174 139.329 96.413  1.00 31.31  ? 969  PRO A C   1 
ATOM   7677  O  O   . PRO A 1 1398 ? 118.086 139.717 95.244  1.00 42.38  ? 969  PRO A O   1 
ATOM   7678  C  CB  . PRO A 1 1398 ? 118.306 140.656 98.529  1.00 40.31  ? 969  PRO A CB  1 
ATOM   7679  C  CG  . PRO A 1 1398 ? 117.652 140.432 99.854  1.00 49.87  ? 969  PRO A CG  1 
ATOM   7680  C  CD  . PRO A 1 1398 ? 117.003 139.080 99.732  1.00 50.33  ? 969  PRO A CD  1 
ATOM   7681  N  N   . SER A 1 1399 ? 118.937 138.313 96.761  1.00 25.48  ? 970  SER A N   1 
ATOM   7682  C  CA  . SER A 1 1399 ? 119.888 137.835 95.774  1.00 32.93  ? 970  SER A CA  1 
ATOM   7683  C  C   . SER A 1 1399 ? 119.231 137.190 94.570  1.00 27.42  ? 970  SER A C   1 
ATOM   7684  O  O   . SER A 1 1399 ? 119.899 137.021 93.548  1.00 32.69  ? 970  SER A O   1 
ATOM   7685  C  CB  . SER A 1 1399 ? 120.862 136.847 96.418  1.00 46.61  ? 970  SER A CB  1 
ATOM   7686  O  OG  . SER A 1 1399 ? 120.164 135.733 96.963  1.00 49.42  ? 970  SER A OG  1 
ATOM   7687  N  N   . GLY A 1 1400 ? 117.954 136.844 94.648  1.00 32.70  ? 971  GLY A N   1 
ATOM   7688  C  CA  . GLY A 1 1400 ? 117.343 135.988 93.647  1.00 45.20  ? 971  GLY A CA  1 
ATOM   7689  C  C   . GLY A 1 1400 ? 117.020 136.685 92.321  1.00 46.18  ? 971  GLY A C   1 
ATOM   7690  O  O   . GLY A 1 1400 ? 117.315 137.859 92.092  1.00 47.87  ? 971  GLY A O   1 
ATOM   7691  N  N   . LEU A 1 1401 ? 116.422 135.919 91.419  1.00 26.48  ? 972  LEU A N   1 
ATOM   7692  C  CA  . LEU A 1 1401 ? 115.889 136.488 90.207  1.00 16.64  ? 972  LEU A CA  1 
ATOM   7693  C  C   . LEU A 1 1401 ? 114.379 136.473 90.265  1.00 39.38  ? 972  LEU A C   1 
ATOM   7694  O  O   . LEU A 1 1401 ? 113.765 135.769 91.069  1.00 45.06  ? 972  LEU A O   1 
ATOM   7695  C  CB  . LEU A 1 1401 ? 116.320 135.703 89.002  1.00 17.25  ? 972  LEU A CB  1 
ATOM   7696  C  CG  . LEU A 1 1401 ? 117.769 135.659 89.223  1.00 18.14  ? 972  LEU A CG  1 
ATOM   7697  C  CD1 . LEU A 1 1401 ? 118.275 134.679 88.238  1.00 28.36  ? 972  LEU A CD1 1 
ATOM   7698  C  CD2 . LEU A 1 1401 ? 118.290 137.033 89.039  1.00 30.73  ? 972  LEU A CD2 1 
ATOM   7699  N  N   . ASN A 1 1402 ? 113.779 137.225 89.354  1.00 35.69  ? 973  ASN A N   1 
ATOM   7700  C  CA  . ASN A 1 1402 ? 112.329 137.284 89.232  1.00 27.97  ? 973  ASN A CA  1 
ATOM   7701  C  C   . ASN A 1 1402 ? 111.816 136.227 88.263  1.00 37.10  ? 973  ASN A C   1 
ATOM   7702  O  O   . ASN A 1 1402 ? 111.208 136.524 87.239  1.00 46.04  ? 973  ASN A O   1 
ATOM   7703  C  CB  . ASN A 1 1402 ? 111.909 138.675 88.795  1.00 38.84  ? 973  ASN A CB  1 
ATOM   7704  C  CG  . ASN A 1 1402 ? 110.424 138.850 88.802  1.00 46.56  ? 973  ASN A CG  1 
ATOM   7705  O  OD1 . ASN A 1 1402 ? 109.697 138.001 89.324  1.00 45.82  ? 973  ASN A OD1 1 
ATOM   7706  N  ND2 . ASN A 1 1402 ? 109.949 139.959 88.230  1.00 47.45  ? 973  ASN A ND2 1 
ATOM   7707  N  N   . VAL A 1 1403 ? 112.026 134.967 88.624  1.00 33.35  ? 974  VAL A N   1 
ATOM   7708  C  CA  . VAL A 1 1403 ? 111.626 133.836 87.801  1.00 26.25  ? 974  VAL A CA  1 
ATOM   7709  C  C   . VAL A 1 1403 ? 110.659 132.983 88.603  1.00 25.28  ? 974  VAL A C   1 
ATOM   7710  O  O   . VAL A 1 1403 ? 110.974 132.611 89.731  1.00 38.37  ? 974  VAL A O   1 
ATOM   7711  C  CB  . VAL A 1 1403 ? 112.829 132.998 87.352  1.00 34.46  ? 974  VAL A CB  1 
ATOM   7712  C  CG1 . VAL A 1 1403 ? 112.332 131.762 86.672  1.00 50.58  ? 974  VAL A CG1 1 
ATOM   7713  C  CG2 . VAL A 1 1403 ? 113.675 133.820 86.404  1.00 40.04  ? 974  VAL A CG2 1 
ATOM   7714  N  N   . PRO A 1 1404 ? 109.477 132.684 88.090  1.00 21.12  ? 975  PRO A N   1 
ATOM   7715  C  CA  . PRO A 1 1404 ? 108.493 131.969 88.903  1.00 25.44  ? 975  PRO A CA  1 
ATOM   7716  C  C   . PRO A 1 1404 ? 108.962 130.611 89.342  1.00 36.89  ? 975  PRO A C   1 
ATOM   7717  O  O   . PRO A 1 1404 ? 108.628 130.175 90.451  1.00 40.23  ? 975  PRO A O   1 
ATOM   7718  C  CB  . PRO A 1 1404 ? 107.277 131.867 87.983  1.00 28.58  ? 975  PRO A CB  1 
ATOM   7719  C  CG  . PRO A 1 1404 ? 107.452 132.949 87.032  1.00 36.10  ? 975  PRO A CG  1 
ATOM   7720  C  CD  . PRO A 1 1404 ? 108.932 133.068 86.798  1.00 35.18  ? 975  PRO A CD  1 
ATOM   7721  N  N   . GLY A 1 1405 ? 109.741 129.921 88.516  1.00 41.19  ? 976  GLY A N   1 
ATOM   7722  C  CA  . GLY A 1 1405 ? 110.316 128.665 88.969  1.00 43.79  ? 976  GLY A CA  1 
ATOM   7723  C  C   . GLY A 1 1405 ? 111.167 128.837 90.215  1.00 44.20  ? 976  GLY A C   1 
ATOM   7724  O  O   . GLY A 1 1405 ? 111.156 127.991 91.110  1.00 49.98  ? 976  GLY A O   1 
ATOM   7725  N  N   . SER A 1 1406 ? 111.887 129.947 90.307  1.00 37.28  ? 977  SER A N   1 
ATOM   7726  C  CA  . SER A 1 1406 ? 112.768 130.189 91.438  1.00 36.45  ? 977  SER A CA  1 
ATOM   7727  C  C   . SER A 1 1406 ? 111.993 130.673 92.656  1.00 41.63  ? 977  SER A C   1 
ATOM   7728  O  O   . SER A 1 1406 ? 112.317 131.713 93.239  1.00 51.47  ? 977  SER A O   1 
ATOM   7729  C  CB  . SER A 1 1406 ? 113.827 131.224 91.039  1.00 47.70  ? 977  SER A CB  1 
ATOM   7730  O  OG  . SER A 1 1406 ? 114.593 131.659 92.158  1.00 50.70  ? 977  SER A OG  1 
ATOM   7731  N  N   . GLN A 1 1407 ? 110.966 129.951 93.051  1.00 34.96  ? 978  GLN A N   1 
ATOM   7732  C  CA  . GLN A 1 1407 ? 110.093 130.435 94.100  1.00 36.82  ? 978  GLN A CA  1 
ATOM   7733  C  C   . GLN A 1 1407 ? 109.648 129.260 94.930  1.00 48.98  ? 978  GLN A C   1 
ATOM   7734  O  O   . GLN A 1 1407 ? 109.200 128.251 94.380  1.00 54.52  ? 978  GLN A O   1 
ATOM   7735  C  CB  . GLN A 1 1407 ? 108.867 131.125 93.519  1.00 54.15  ? 978  GLN A CB  1 
ATOM   7736  C  CG  . GLN A 1 1407 ? 109.109 132.496 92.937  1.00 63.66  ? 978  GLN A CG  1 
ATOM   7737  C  CD  . GLN A 1 1407 ? 108.953 133.580 93.981  1.00 69.95  ? 978  GLN A CD  1 
ATOM   7738  O  OE1 . GLN A 1 1407 ? 107.863 134.146 94.136  1.00 67.56  ? 978  GLN A OE1 1 
ATOM   7739  N  NE2 . GLN A 1 1407 ? 110.022 133.858 94.722  1.00 68.15  ? 978  GLN A NE2 1 
ATOM   7740  N  N   . ASP A 1 1408 ? 109.751 129.392 96.239  1.00 55.49  ? 979  ASP A N   1 
ATOM   7741  C  CA  . ASP A 1 1408 ? 109.287 128.331 97.117  1.00 54.44  ? 979  ASP A CA  1 
ATOM   7742  C  C   . ASP A 1 1408 ? 107.887 128.638 97.612  1.00 38.57  ? 979  ASP A C   1 
ATOM   7743  O  O   . ASP A 1 1408 ? 107.385 129.752 97.483  1.00 48.84  ? 979  ASP A O   1 
ATOM   7744  C  CB  . ASP A 1 1408 ? 110.257 128.139 98.282  1.00 66.57  ? 979  ASP A CB  1 
ATOM   7745  C  CG  . ASP A 1 1408 ? 110.631 129.455 98.950  1.00 70.22  ? 979  ASP A CG  1 
ATOM   7746  O  OD1 . ASP A 1 1408 ? 111.078 129.440 100.123 1.00 66.35  ? 979  ASP A OD1 1 
ATOM   7747  O  OD2 . ASP A 1 1408 ? 110.455 130.512 98.296  1.00 67.50  ? 979  ASP A OD2 1 
ATOM   7748  N  N   . LEU A 1 1409 ? 107.287 127.675 98.179  1.00 31.66  ? 980  LEU A N   1 
ATOM   7749  C  CA  . LEU A 1 1409 ? 105.928 127.977 98.466  1.00 29.08  ? 980  LEU A CA  1 
ATOM   7750  C  C   . LEU A 1 1409 ? 105.770 128.977 99.487  1.00 43.50  ? 980  LEU A C   1 
ATOM   7751  O  O   . LEU A 1 1409 ? 104.612 129.168 99.821  1.00 57.15  ? 980  LEU A O   1 
ATOM   7752  C  CB  . LEU A 1 1409 ? 105.215 126.701 98.890  1.00 41.51  ? 980  LEU A CB  1 
ATOM   7753  C  CG  . LEU A 1 1409 ? 105.164 125.727 97.732  1.00 49.18  ? 980  LEU A CG  1 
ATOM   7754  C  CD1 . LEU A 1 1409 ? 104.129 124.683 98.030  1.00 57.28  ? 980  LEU A CD1 1 
ATOM   7755  C  CD2 . LEU A 1 1409 ? 104.820 126.481 96.460  1.00 57.59  ? 980  LEU A CD2 1 
ATOM   7756  N  N   . THR A 1 1410 ? 106.798 129.657 100.004 1.00 52.72  ? 981  THR A N   1 
ATOM   7757  C  CA  . THR A 1 1410 ? 106.602 130.499 101.187 1.00 61.41  ? 981  THR A CA  1 
ATOM   7758  C  C   . THR A 1 1410 ? 105.641 131.646 100.910 1.00 55.97  ? 981  THR A C   1 
ATOM   7759  O  O   . THR A 1 1410 ? 104.857 132.024 101.787 1.00 59.72  ? 981  THR A O   1 
ATOM   7760  C  CB  . THR A 1 1410 ? 107.929 131.075 101.709 1.00 70.48  ? 981  THR A CB  1 
ATOM   7761  O  OG1 . THR A 1 1410 ? 108.644 131.723 100.646 1.00 67.75  ? 981  THR A OG1 1 
ATOM   7762  C  CG2 . THR A 1 1410 ? 108.804 129.976 102.356 1.00 76.11  ? 981  THR A CG2 1 
ATOM   7763  N  N   . SER A 1 1411 ? 105.706 132.242 99.720  1.00 51.61  ? 982  SER A N   1 
ATOM   7764  C  CA  . SER A 1 1411 ? 104.800 133.348 99.434  1.00 52.92  ? 982  SER A CA  1 
ATOM   7765  C  C   . SER A 1 1411 ? 103.356 132.898 99.552  1.00 46.47  ? 982  SER A C   1 
ATOM   7766  O  O   . SER A 1 1411 ? 102.530 133.569 100.181 1.00 52.30  ? 982  SER A O   1 
ATOM   7767  C  CB  . SER A 1 1411 ? 105.060 133.901 98.035  1.00 58.93  ? 982  SER A CB  1 
ATOM   7768  O  OG  . SER A 1 1411 ? 104.792 132.911 97.056  1.00 57.56  ? 982  SER A OG  1 
ATOM   7769  N  N   . PHE A 1 1412 ? 103.046 131.750 98.972  1.00 38.80  ? 983  PHE A N   1 
ATOM   7770  C  CA  . PHE A 1 1412 ? 101.691 131.255 99.035  1.00 34.24  ? 983  PHE A CA  1 
ATOM   7771  C  C   . PHE A 1 1412 ? 101.263 131.015 100.475 1.00 38.68  ? 983  PHE A C   1 
ATOM   7772  O  O   . PHE A 1 1412 ? 100.156 131.396 100.881 1.00 51.48  ? 983  PHE A O   1 
ATOM   7773  C  CB  . PHE A 1 1412 ? 101.593 129.993 98.205  1.00 30.85  ? 983  PHE A CB  1 
ATOM   7774  C  CG  . PHE A 1 1412 ? 100.391 129.223 98.479  1.00 35.53  ? 983  PHE A CG  1 
ATOM   7775  C  CD1 . PHE A 1 1412 ? 99.173  129.687 98.065  1.00 44.56  ? 983  PHE A CD1 1 
ATOM   7776  C  CD2 . PHE A 1 1412 ? 100.463 128.021 99.134  1.00 53.45  ? 983  PHE A CD2 1 
ATOM   7777  C  CE1 . PHE A 1 1412 ? 98.033  128.981 98.312  1.00 54.91  ? 983  PHE A CE1 1 
ATOM   7778  C  CE2 . PHE A 1 1412 ? 99.318  127.297 99.389  1.00 60.28  ? 983  PHE A CE2 1 
ATOM   7779  C  CZ  . PHE A 1 1412 ? 98.100  127.776 98.967  1.00 58.07  ? 983  PHE A CZ  1 
ATOM   7780  N  N   . LEU A 1 1413 ? 102.128 130.418 101.274 1.00 34.46  ? 984  LEU A N   1 
ATOM   7781  C  CA  . LEU A 1 1413 ? 101.745 130.167 102.649 1.00 34.28  ? 984  LEU A CA  1 
ATOM   7782  C  C   . LEU A 1 1413 ? 101.536 131.467 103.392 1.00 44.69  ? 984  LEU A C   1 
ATOM   7783  O  O   . LEU A 1 1413 ? 100.633 131.567 104.230 1.00 55.31  ? 984  LEU A O   1 
ATOM   7784  C  CB  . LEU A 1 1413 ? 102.809 129.336 103.353 1.00 61.27  ? 984  LEU A CB  1 
ATOM   7785  C  CG  . LEU A 1 1413 ? 103.181 127.974 102.762 1.00 74.81  ? 984  LEU A CG  1 
ATOM   7786  C  CD1 . LEU A 1 1413 ? 104.313 127.317 103.577 1.00 71.13  ? 984  LEU A CD1 1 
ATOM   7787  C  CD2 . LEU A 1 1413 ? 101.947 127.073 102.671 1.00 73.52  ? 984  LEU A CD2 1 
ATOM   7788  N  N   . ARG A 1 1414 ? 102.394 132.462 103.147 1.00 43.22  ? 985  ARG A N   1 
ATOM   7789  C  CA  . ARG A 1 1414 ? 102.257 133.711 103.887 1.00 46.30  ? 985  ARG A CA  1 
ATOM   7790  C  C   . ARG A 1 1414 ? 100.991 134.426 103.490 1.00 39.07  ? 985  ARG A C   1 
ATOM   7791  O  O   . ARG A 1 1414 ? 100.365 135.092 104.316 1.00 44.78  ? 985  ARG A O   1 
ATOM   7792  C  CB  . ARG A 1 1414 ? 103.459 134.631 103.688 1.00 40.44  ? 985  ARG A CB  1 
ATOM   7793  C  CG  . ARG A 1 1414 ? 104.720 134.099 104.286 1.00 39.24  ? 985  ARG A CG  1 
ATOM   7794  C  CD  . ARG A 1 1414 ? 105.726 135.198 104.348 1.00 49.67  ? 985  ARG A CD  1 
ATOM   7795  N  NE  . ARG A 1 1414 ? 105.728 135.977 103.121 1.00 48.46  ? 985  ARG A NE  1 
ATOM   7796  C  CZ  . ARG A 1 1414 ? 106.600 135.781 102.149 1.00 55.19  ? 985  ARG A CZ  1 
ATOM   7797  N  NH1 . ARG A 1 1414 ? 107.520 134.833 102.288 1.00 59.44  ? 985  ARG A NH1 1 
ATOM   7798  N  NH2 . ARG A 1 1414 ? 106.557 136.521 101.049 1.00 59.42  ? 985  ARG A NH2 1 
ATOM   7799  N  N   . GLN A 1 1415 ? 100.582 134.271 102.250 1.00 35.42  ? 986  GLN A N   1 
ATOM   7800  C  CA  . GLN A 1 1415 ? 99.302  134.824 101.875 1.00 34.07  ? 986  GLN A CA  1 
ATOM   7801  C  C   . GLN A 1 1415 ? 98.172  134.102 102.602 1.00 32.92  ? 986  GLN A C   1 
ATOM   7802  O  O   . GLN A 1 1415 ? 97.203  134.735 103.019 1.00 41.73  ? 986  GLN A O   1 
ATOM   7803  C  CB  . GLN A 1 1415 ? 99.142  134.754 100.367 1.00 44.43  ? 986  GLN A CB  1 
ATOM   7804  C  CG  . GLN A 1 1415 ? 98.011  135.578 99.848  1.00 48.14  ? 986  GLN A CG  1 
ATOM   7805  C  CD  . GLN A 1 1415 ? 96.715  134.804 99.878  1.00 58.77  ? 986  GLN A CD  1 
ATOM   7806  O  OE1 . GLN A 1 1415 ? 96.717  133.576 100.025 1.00 55.89  ? 986  GLN A OE1 1 
ATOM   7807  N  NE2 . GLN A 1 1415 ? 95.596  135.511 99.717  1.00 58.34  ? 986  GLN A NE2 1 
ATOM   7808  N  N   . ILE A 1 1416 ? 98.259  132.786 102.777 1.00 30.93  ? 987  ILE A N   1 
ATOM   7809  C  CA  . ILE A 1 1416 ? 97.184  132.134 103.530 1.00 29.08  ? 987  ILE A CA  1 
ATOM   7810  C  C   . ILE A 1 1416 ? 97.172  132.525 104.997 1.00 38.57  ? 987  ILE A C   1 
ATOM   7811  O  O   . ILE A 1 1416 ? 96.103  132.720 105.587 1.00 48.93  ? 987  ILE A O   1 
ATOM   7812  C  CB  . ILE A 1 1416 ? 97.192  130.616 103.389 1.00 36.26  ? 987  ILE A CB  1 
ATOM   7813  C  CG1 . ILE A 1 1416 ? 96.741  130.217 101.996 1.00 53.70  ? 987  ILE A CG1 1 
ATOM   7814  C  CG2 . ILE A 1 1416 ? 96.379  129.980 104.455 1.00 50.02  ? 987  ILE A CG2 1 
ATOM   7815  C  CD1 . ILE A 1 1416 ? 96.675  128.735 101.862 1.00 60.93  ? 987  ILE A CD1 1 
ATOM   7816  N  N   . VAL A 1 1417 ? 98.330  132.639 105.622 1.00 39.59  ? 988  VAL A N   1 
ATOM   7817  C  CA  . VAL A 1 1417 ? 98.313  133.096 107.004 1.00 33.95  ? 988  VAL A CA  1 
ATOM   7818  C  C   . VAL A 1 1417 ? 97.767  134.516 107.073 1.00 42.30  ? 988  VAL A C   1 
ATOM   7819  O  O   . VAL A 1 1417 ? 97.045  134.871 108.004 1.00 47.49  ? 988  VAL A O   1 
ATOM   7820  C  CB  . VAL A 1 1417 ? 99.715  133.019 107.613 1.00 43.49  ? 988  VAL A CB  1 
ATOM   7821  C  CG1 . VAL A 1 1417 ? 99.678  133.587 109.021 1.00 48.83  ? 988  VAL A CG1 1 
ATOM   7822  C  CG2 . VAL A 1 1417 ? 100.290 131.601 107.530 1.00 56.14  ? 988  VAL A CG2 1 
ATOM   7823  N  N   . ARG A 1 1418 ? 98.121  135.363 106.101 1.00 40.35  ? 989  ARG A N   1 
ATOM   7824  C  CA  . ARG A 1 1418 ? 97.616  136.726 106.107 1.00 33.07  ? 989  ARG A CA  1 
ATOM   7825  C  C   . ARG A 1 1418 ? 96.117  136.733 105.984 1.00 30.33  ? 989  ARG A C   1 
ATOM   7826  O  O   . ARG A 1 1418 ? 95.432  137.494 106.667 1.00 44.43  ? 989  ARG A O   1 
ATOM   7827  C  CB  . ARG A 1 1418 ? 98.254  137.530 104.980 1.00 39.55  ? 989  ARG A CB  1 
ATOM   7828  C  CG  . ARG A 1 1418 ? 97.779  138.980 104.887 1.00 48.59  ? 989  ARG A CG  1 
ATOM   7829  C  CD  . ARG A 1 1418 ? 98.254  139.842 106.053 1.00 53.01  ? 989  ARG A CD  1 
ATOM   7830  N  NE  . ARG A 1 1418 ? 97.582  141.152 106.079 1.00 62.29  ? 989  ARG A NE  1 
ATOM   7831  C  CZ  . ARG A 1 1418 ? 96.517  141.457 106.830 1.00 59.53  ? 989  ARG A CZ  1 
ATOM   7832  N  NH1 . ARG A 1 1418 ? 95.966  140.546 107.631 1.00 56.21  ? 989  ARG A NH1 1 
ATOM   7833  N  NH2 . ARG A 1 1418 ? 95.995  142.679 106.778 1.00 53.15  ? 989  ARG A NH2 1 
ATOM   7834  N  N   . ARG A 1 1419 ? 95.591  135.901 105.116 1.00 33.71  ? 990  ARG A N   1 
ATOM   7835  C  CA  . ARG A 1 1419 ? 94.151  135.835 104.988 1.00 42.39  ? 990  ARG A CA  1 
ATOM   7836  C  C   . ARG A 1 1419 ? 93.522  135.364 106.286 1.00 38.84  ? 990  ARG A C   1 
ATOM   7837  O  O   . ARG A 1 1419 ? 92.502  135.904 106.723 1.00 52.85  ? 990  ARG A O   1 
ATOM   7838  C  CB  . ARG A 1 1419 ? 93.784  134.917 103.823 1.00 55.54  ? 990  ARG A CB  1 
ATOM   7839  C  CG  . ARG A 1 1419 ? 92.314  134.819 103.545 1.00 69.58  ? 990  ARG A CG  1 
ATOM   7840  C  CD  . ARG A 1 1419 ? 91.732  136.164 103.173 1.00 84.07  ? 990  ARG A CD  1 
ATOM   7841  N  NE  . ARG A 1 1419 ? 90.314  136.044 102.839 1.00 108.93 ? 990  ARG A NE  1 
ATOM   7842  C  CZ  . ARG A 1 1419 ? 89.538  137.057 102.459 1.00 121.52 ? 990  ARG A CZ  1 
ATOM   7843  N  NH1 . ARG A 1 1419 ? 90.041  138.282 102.358 1.00 116.42 ? 990  ARG A NH1 1 
ATOM   7844  N  NH2 . ARG A 1 1419 ? 88.257  136.843 102.177 1.00 129.06 ? 990  ARG A NH2 1 
ATOM   7845  N  N   . THR A 1 1420 ? 94.120  134.376 106.935 1.00 34.60  ? 991  THR A N   1 
ATOM   7846  C  CA  . THR A 1 1420 ? 93.514  133.921 108.173 1.00 39.06  ? 991  THR A CA  1 
ATOM   7847  C  C   . THR A 1 1420 ? 93.691  134.920 109.297 1.00 43.74  ? 991  THR A C   1 
ATOM   7848  O  O   . THR A 1 1420 ? 92.963  134.855 110.292 1.00 50.40  ? 991  THR A O   1 
ATOM   7849  C  CB  . THR A 1 1420 ? 94.084  132.582 108.615 1.00 63.59  ? 991  THR A CB  1 
ATOM   7850  O  OG1 . THR A 1 1420 ? 93.174  131.990 109.547 1.00 80.22  ? 991  THR A OG1 1 
ATOM   7851  C  CG2 . THR A 1 1420 ? 95.428  132.749 109.312 1.00 60.12  ? 991  THR A CG2 1 
ATOM   7852  N  N   . ILE A 1 1421 ? 94.652  135.823 109.173 1.00 43.29  ? 992  ILE A N   1 
ATOM   7853  C  CA  . ILE A 1 1421 ? 94.832  136.838 110.194 1.00 38.39  ? 992  ILE A CA  1 
ATOM   7854  C  C   . ILE A 1 1421 ? 93.811  137.939 110.019 1.00 41.37  ? 992  ILE A C   1 
ATOM   7855  O  O   . ILE A 1 1421 ? 93.111  138.320 110.963 1.00 53.61  ? 992  ILE A O   1 
ATOM   7856  C  CB  . ILE A 1 1421 ? 96.267  137.382 110.165 1.00 43.75  ? 992  ILE A CB  1 
ATOM   7857  C  CG1 . ILE A 1 1421 ? 97.224  136.349 110.785 1.00 49.54  ? 992  ILE A CG1 1 
ATOM   7858  C  CG2 . ILE A 1 1421 ? 96.331  138.732 110.859 1.00 50.79  ? 992  ILE A CG2 1 
ATOM   7859  C  CD1 . ILE A 1 1421 ? 98.688  136.770 110.801 1.00 49.49  ? 992  ILE A CD1 1 
ATOM   7860  N  N   . THR A 1 1422 ? 93.669  138.428 108.801 1.00 38.53  ? 993  THR A N   1 
ATOM   7861  C  CA  . THR A 1 1422 ? 92.642  139.419 108.555 1.00 42.10  ? 993  THR A CA  1 
ATOM   7862  C  C   . THR A 1 1422 ? 91.248  138.852 108.754 1.00 37.25  ? 993  THR A C   1 
ATOM   7863  O  O   . THR A 1 1422 ? 90.303  139.615 108.949 1.00 47.28  ? 993  THR A O   1 
ATOM   7864  C  CB  . THR A 1 1422 ? 92.759  139.973 107.135 1.00 55.94  ? 993  THR A CB  1 
ATOM   7865  O  OG1 . THR A 1 1422 ? 91.925  141.132 106.995 1.00 56.57  ? 993  THR A OG1 1 
ATOM   7866  C  CG2 . THR A 1 1422 ? 92.313  138.920 106.103 1.00 58.29  ? 993  THR A CG2 1 
ATOM   7867  N  N   . LEU A 1 1423 ? 91.083  137.545 108.718 1.00 39.35  ? 994  LEU A N   1 
ATOM   7868  C  CA  . LEU A 1 1423 ? 89.721  137.054 108.755 1.00 40.90  ? 994  LEU A CA  1 
ATOM   7869  C  C   . LEU A 1 1423 ? 89.278  136.782 110.183 1.00 51.63  ? 994  LEU A C   1 
ATOM   7870  O  O   . LEU A 1 1423 ? 88.299  137.366 110.651 1.00 61.15  ? 994  LEU A O   1 
ATOM   7871  C  CB  . LEU A 1 1423 ? 89.595  135.797 107.901 1.00 59.09  ? 994  LEU A CB  1 
ATOM   7872  C  CG  . LEU A 1 1423 ? 88.184  135.225 107.734 1.00 80.77  ? 994  LEU A CG  1 
ATOM   7873  C  CD1 . LEU A 1 1423 ? 87.262  136.262 107.105 1.00 75.97  ? 994  LEU A CD1 1 
ATOM   7874  C  CD2 . LEU A 1 1423 ? 88.183  133.917 106.920 1.00 98.64  ? 994  LEU A CD2 1 
ATOM   7875  N  N   . SER A 1 1424 ? 89.987  135.906 110.889 1.00 56.81  ? 995  SER A N   1 
ATOM   7876  C  CA  . SER A 1 1424 ? 89.537  135.426 112.197 1.00 65.82  ? 995  SER A CA  1 
ATOM   7877  C  C   . SER A 1 1424 ? 90.683  135.440 113.213 1.00 66.70  ? 995  SER A C   1 
ATOM   7878  O  O   . SER A 1 1424 ? 90.929  134.464 113.925 1.00 71.22  ? 995  SER A O   1 
ATOM   7879  C  CB  . SER A 1 1424 ? 88.918  134.031 112.076 1.00 72.94  ? 995  SER A CB  1 
ATOM   7880  O  OG  . SER A 1 1424 ? 88.465  133.548 113.332 1.00 72.38  ? 995  SER A OG  1 
ATOM   7881  N  N   . ALA A 1 1425 ? 91.407  136.560 113.286 1.00 57.23  ? 996  ALA A N   1 
ATOM   7882  C  CA  . ALA A 1 1425 ? 92.375  136.804 114.351 1.00 50.44  ? 996  ALA A CA  1 
ATOM   7883  C  C   . ALA A 1 1425 ? 91.829  137.924 115.226 1.00 50.21  ? 996  ALA A C   1 
ATOM   7884  O  O   . ALA A 1 1425 ? 91.794  139.086 114.809 1.00 56.35  ? 996  ALA A O   1 
ATOM   7885  C  CB  . ALA A 1 1425 ? 93.751  137.165 113.795 1.00 53.62  ? 996  ALA A CB  1 
ATOM   7886  N  N   . LYS A 1 1426 ? 91.412  137.579 116.432 1.00 39.51  ? 997  LYS A N   1 
ATOM   7887  C  CA  . LYS A 1 1426 ? 90.845  138.547 117.344 1.00 32.11  ? 997  LYS A CA  1 
ATOM   7888  C  C   . LYS A 1 1426 ? 91.882  139.227 118.202 1.00 32.15  ? 997  LYS A C   1 
ATOM   7889  O  O   . LYS A 1 1426 ? 91.525  140.087 118.999 1.00 43.32  ? 997  LYS A O   1 
ATOM   7890  C  CB  . LYS A 1 1426 ? 89.851  137.856 118.235 1.00 45.59  ? 997  LYS A CB  1 
ATOM   7891  C  CG  . LYS A 1 1426 ? 88.830  137.098 117.442 1.00 64.18  ? 997  LYS A CG  1 
ATOM   7892  C  CD  . LYS A 1 1426 ? 88.016  136.187 118.354 1.00 94.17  ? 997  LYS A CD  1 
ATOM   7893  C  CE  . LYS A 1 1426 ? 87.170  136.956 119.373 1.00 95.67  ? 997  LYS A CE  1 
ATOM   7894  N  NZ  . LYS A 1 1426 ? 86.118  137.792 118.725 1.00 88.95  ? 997  LYS A NZ  1 
ATOM   7895  N  N   . ASN A 1 1427 ? 93.143  138.852 118.081 1.00 38.24  ? 998  ASN A N   1 
ATOM   7896  C  CA  . ASN A 1 1427 ? 94.196  139.474 118.869 1.00 36.61  ? 998  ASN A CA  1 
ATOM   7897  C  C   . ASN A 1 1427 ? 94.270  140.968 118.630 1.00 46.20  ? 998  ASN A C   1 
ATOM   7898  O  O   . ASN A 1 1427 ? 94.305  141.424 117.483 1.00 51.77  ? 998  ASN A O   1 
ATOM   7899  C  CB  . ASN A 1 1427 ? 95.540  138.871 118.513 1.00 41.12  ? 998  ASN A CB  1 
ATOM   7900  C  CG  . ASN A 1 1427 ? 96.610  139.306 119.462 1.00 53.11  ? 998  ASN A CG  1 
ATOM   7901  O  OD1 . ASN A 1 1427 ? 97.135  140.418 119.341 1.00 56.23  ? 998  ASN A OD1 1 
ATOM   7902  N  ND2 . ASN A 1 1427 ? 96.972  138.434 120.399 1.00 56.28  ? 998  ASN A ND2 1 
ATOM   7903  N  N   . LYS A 1 1428 ? 94.351  141.735 119.716 1.00 47.77  ? 999  LYS A N   1 
ATOM   7904  C  CA  . LYS A 1 1428 ? 94.330  143.186 119.570 1.00 36.40  ? 999  LYS A CA  1 
ATOM   7905  C  C   . LYS A 1 1428 ? 95.633  143.703 119.002 1.00 31.80  ? 999  LYS A C   1 
ATOM   7906  O  O   . LYS A 1 1428 ? 95.634  144.552 118.114 1.00 40.49  ? 999  LYS A O   1 
ATOM   7907  C  CB  . LYS A 1 1428 ? 94.051  143.852 120.898 1.00 35.42  ? 999  LYS A CB  1 
ATOM   7908  C  CG  . LYS A 1 1428 ? 93.746  145.288 120.717 1.00 46.69  ? 999  LYS A CG  1 
ATOM   7909  C  CD  . LYS A 1 1428 ? 92.271  145.472 120.377 1.00 67.19  ? 999  LYS A CD  1 
ATOM   7910  C  CE  . LYS A 1 1428 ? 91.364  144.994 121.517 1.00 85.46  ? 999  LYS A CE  1 
ATOM   7911  N  NZ  . LYS A 1 1428 ? 89.908  145.204 121.233 1.00 78.20  ? 999  LYS A NZ  1 
ATOM   7912  N  N   . LEU A 1 1429 ? 96.745  143.222 119.497 1.00 33.35  ? 1000 LEU A N   1 
ATOM   7913  C  CA  . LEU A 1 1429 ? 97.996  143.782 119.038 1.00 35.26  ? 1000 LEU A CA  1 
ATOM   7914  C  C   . LEU A 1 1429 ? 98.466  143.137 117.763 1.00 43.62  ? 1000 LEU A C   1 
ATOM   7915  O  O   . LEU A 1 1429 ? 99.598  143.402 117.351 1.00 52.68  ? 1000 LEU A O   1 
ATOM   7916  C  CB  . LEU A 1 1429 ? 99.077  143.642 120.102 1.00 44.73  ? 1000 LEU A CB  1 
ATOM   7917  C  CG  . LEU A 1 1429 ? 99.210  144.814 121.087 1.00 55.56  ? 1000 LEU A CG  1 
ATOM   7918  C  CD1 . LEU A 1 1429 ? 97.942  145.057 121.912 1.00 42.27  ? 1000 LEU A CD1 1 
ATOM   7919  C  CD2 . LEU A 1 1429 ? 100.387 144.582 122.021 1.00 59.37  ? 1000 LEU A CD2 1 
ATOM   7920  N  N   . ILE A 1 1430 ? 97.665  142.257 117.170 1.00 40.95  ? 1001 ILE A N   1 
ATOM   7921  C  CA  . ILE A 1 1430 ? 97.907  141.777 115.810 1.00 48.08  ? 1001 ILE A CA  1 
ATOM   7922  C  C   . ILE A 1 1430 ? 96.985  142.459 114.803 1.00 47.29  ? 1001 ILE A C   1 
ATOM   7923  O  O   . ILE A 1 1430 ? 97.401  142.776 113.688 1.00 48.71  ? 1001 ILE A O   1 
ATOM   7924  C  CB  . ILE A 1 1430 ? 97.785  140.238 115.724 1.00 54.29  ? 1001 ILE A CB  1 
ATOM   7925  C  CG1 . ILE A 1 1430 ? 98.953  139.547 116.438 1.00 56.76  ? 1001 ILE A CG1 1 
ATOM   7926  C  CG2 . ILE A 1 1430 ? 97.696  139.770 114.266 1.00 55.50  ? 1001 ILE A CG2 1 
ATOM   7927  C  CD1 . ILE A 1 1430 ? 100.315 139.826 115.796 1.00 61.73  ? 1001 ILE A CD1 1 
ATOM   7928  N  N   . ASN A 1 1431 ? 95.735  142.710 115.172 1.00 38.39  ? 1002 ASN A N   1 
ATOM   7929  C  CA  . ASN A 1 1431 ? 94.888  143.475 114.282 1.00 30.52  ? 1002 ASN A CA  1 
ATOM   7930  C  C   . ASN A 1 1431 ? 95.425  144.880 114.089 1.00 43.02  ? 1002 ASN A C   1 
ATOM   7931  O  O   . ASN A 1 1431 ? 95.403  145.412 112.975 1.00 50.61  ? 1002 ASN A O   1 
ATOM   7932  C  CB  . ASN A 1 1431 ? 93.481  143.503 114.816 1.00 31.35  ? 1002 ASN A CB  1 
ATOM   7933  C  CG  . ASN A 1 1431 ? 92.720  142.303 114.389 1.00 50.13  ? 1002 ASN A CG  1 
ATOM   7934  O  OD1 . ASN A 1 1431 ? 93.281  141.409 113.747 1.00 50.71  ? 1002 ASN A OD1 1 
ATOM   7935  N  ND2 . ASN A 1 1431 ? 91.435  142.254 114.728 1.00 54.74  ? 1002 ASN A ND2 1 
ATOM   7936  N  N   . THR A 1 1432 ? 95.914  145.505 115.153 1.00 39.60  ? 1003 THR A N   1 
ATOM   7937  C  CA  . THR A 1 1432 ? 96.565  146.795 114.980 1.00 34.85  ? 1003 THR A CA  1 
ATOM   7938  C  C   . THR A 1 1432 ? 97.818  146.655 114.142 1.00 30.93  ? 1003 THR A C   1 
ATOM   7939  O  O   . THR A 1 1432 ? 98.102  147.500 113.293 1.00 42.31  ? 1003 THR A O   1 
ATOM   7940  C  CB  . THR A 1 1432 ? 96.900  147.412 116.337 1.00 51.49  ? 1003 THR A CB  1 
ATOM   7941  O  OG1 . THR A 1 1432 ? 95.694  147.569 117.102 1.00 47.02  ? 1003 THR A OG1 1 
ATOM   7942  C  CG2 . THR A 1 1432 ? 97.593  148.778 116.165 1.00 55.98  ? 1003 THR A CG2 1 
ATOM   7943  N  N   . LEU A 1 1433 ? 98.585  145.611 114.363 1.00 29.41  ? 1004 LEU A N   1 
ATOM   7944  C  CA  . LEU A 1 1433 ? 99.738  145.421 113.509 1.00 32.71  ? 1004 LEU A CA  1 
ATOM   7945  C  C   . LEU A 1 1433 ? 99.325  145.081 112.081 1.00 52.97  ? 1004 LEU A C   1 
ATOM   7946  O  O   . LEU A 1 1433 ? 99.917  145.598 111.125 1.00 57.72  ? 1004 LEU A O   1 
ATOM   7947  C  CB  . LEU A 1 1433 ? 100.630 144.342 114.088 1.00 39.57  ? 1004 LEU A CB  1 
ATOM   7948  C  CG  . LEU A 1 1433 ? 101.898 144.110 113.289 1.00 53.44  ? 1004 LEU A CG  1 
ATOM   7949  C  CD1 . LEU A 1 1433 ? 102.667 145.404 113.180 1.00 61.75  ? 1004 LEU A CD1 1 
ATOM   7950  C  CD2 . LEU A 1 1433 ? 102.747 143.049 113.991 1.00 65.54  ? 1004 LEU A CD2 1 
ATOM   7951  N  N   . PHE A 1 1434 ? 98.333  144.195 111.908 1.00 54.23  ? 1005 PHE A N   1 
ATOM   7952  C  CA  . PHE A 1 1434 ? 97.809  143.819 110.580 1.00 44.53  ? 1005 PHE A CA  1 
ATOM   7953  C  C   . PHE A 1 1434 ? 96.481  144.539 110.333 1.00 47.21  ? 1005 PHE A C   1 
ATOM   7954  O  O   . PHE A 1 1434 ? 95.407  143.934 110.290 1.00 47.02  ? 1005 PHE A O   1 
ATOM   7955  C  CB  . PHE A 1 1434 ? 97.621  142.308 110.489 1.00 42.27  ? 1005 PHE A CB  1 
ATOM   7956  C  CG  . PHE A 1 1434 ? 98.894  141.526 110.279 1.00 45.90  ? 1005 PHE A CG  1 
ATOM   7957  C  CD1 . PHE A 1 1434 ? 99.426  141.357 109.027 1.00 52.93  ? 1005 PHE A CD1 1 
ATOM   7958  C  CD2 . PHE A 1 1434 ? 99.542  140.930 111.350 1.00 50.15  ? 1005 PHE A CD2 1 
ATOM   7959  C  CE1 . PHE A 1 1434 ? 100.594 140.616 108.849 1.00 52.48  ? 1005 PHE A CE1 1 
ATOM   7960  C  CE2 . PHE A 1 1434 ? 100.704 140.201 111.173 1.00 48.77  ? 1005 PHE A CE2 1 
ATOM   7961  C  CZ  . PHE A 1 1434 ? 101.228 140.045 109.926 1.00 42.43  ? 1005 PHE A CZ  1 
ATOM   7962  N  N   . HIS A 1 1435 ? 96.560  145.860 110.208 1.00 45.44  ? 1006 HIS A N   1 
ATOM   7963  C  CA  . HIS A 1 1435 ? 95.387  146.693 109.959 1.00 38.85  ? 1006 HIS A CA  1 
ATOM   7964  C  C   . HIS A 1 1435 ? 94.912  146.499 108.522 1.00 47.48  ? 1006 HIS A C   1 
ATOM   7965  O  O   . HIS A 1 1435 ? 95.388  145.631 107.787 1.00 57.22  ? 1006 HIS A O   1 
ATOM   7966  C  CB  . HIS A 1 1435 ? 95.733  148.140 110.223 1.00 39.76  ? 1006 HIS A CB  1 
ATOM   7967  C  CG  . HIS A 1 1435 ? 97.098  148.485 109.739 1.00 51.11  ? 1006 HIS A CG  1 
ATOM   7968  N  ND1 . HIS A 1 1435 ? 97.416  148.554 108.401 1.00 61.14  ? 1006 HIS A ND1 1 
ATOM   7969  C  CD2 . HIS A 1 1435 ? 98.245  148.739 110.413 1.00 59.59  ? 1006 HIS A CD2 1 
ATOM   7970  C  CE1 . HIS A 1 1435 ? 98.697  148.855 108.270 1.00 66.90  ? 1006 HIS A CE1 1 
ATOM   7971  N  NE2 . HIS A 1 1435 ? 99.223  148.976 109.476 1.00 62.18  ? 1006 HIS A NE2 1 
ATOM   7972  N  N   . ALA A 1 1436 ? 93.944  147.301 108.096 1.00 40.75  ? 1007 ALA A N   1 
ATOM   7973  C  CA  . ALA A 1 1436 ? 93.402  147.082 106.763 1.00 41.48  ? 1007 ALA A CA  1 
ATOM   7974  C  C   . ALA A 1 1436 ? 94.435  147.388 105.696 1.00 39.27  ? 1007 ALA A C   1 
ATOM   7975  O  O   . ALA A 1 1436 ? 94.635  146.591 104.776 1.00 47.66  ? 1007 ALA A O   1 
ATOM   7976  C  CB  . ALA A 1 1436 ? 92.149  147.928 106.550 1.00 62.03  ? 1007 ALA A CB  1 
ATOM   7977  N  N   . SER A 1 1437 ? 95.138  148.507 105.827 1.00 37.30  ? 1008 SER A N   1 
ATOM   7978  C  CA  . SER A 1 1437 ? 96.079  148.923 104.801 1.00 42.74  ? 1008 SER A CA  1 
ATOM   7979  C  C   . SER A 1 1437 ? 97.431  148.283 104.990 1.00 43.76  ? 1008 SER A C   1 
ATOM   7980  O  O   . SER A 1 1437 ? 98.453  148.881 104.646 1.00 53.66  ? 1008 SER A O   1 
ATOM   7981  C  CB  . SER A 1 1437 ? 96.235  150.440 104.795 1.00 52.12  ? 1008 SER A CB  1 
ATOM   7982  O  OG  . SER A 1 1437 ? 96.735  150.896 106.042 1.00 54.46  ? 1008 SER A OG  1 
ATOM   7983  N  N   . ALA A 1 1438 ? 97.471  147.102 105.583 1.00 41.80  ? 1009 ALA A N   1 
ATOM   7984  C  CA  . ALA A 1 1438 ? 98.750  146.445 105.756 1.00 49.48  ? 1009 ALA A CA  1 
ATOM   7985  C  C   . ALA A 1 1438 ? 99.423  146.261 104.419 1.00 49.03  ? 1009 ALA A C   1 
ATOM   7986  O  O   . ALA A 1 1438 ? 100.591 146.630 104.237 1.00 61.10  ? 1009 ALA A O   1 
ATOM   7987  C  CB  . ALA A 1 1438 ? 98.564  145.092 106.441 1.00 60.31  ? 1009 ALA A CB  1 
ATOM   7988  N  N   . ASP A 1 1439 ? 98.694  145.708 103.463 1.00 43.65  ? 1010 ASP A N   1 
ATOM   7989  C  CA  . ASP A 1 1439 ? 99.340  145.368 102.215 1.00 58.01  ? 1010 ASP A CA  1 
ATOM   7990  C  C   . ASP A 1 1439 ? 99.859  146.620 101.536 1.00 60.64  ? 1010 ASP A C   1 
ATOM   7991  O  O   . ASP A 1 1439 ? 100.989 146.641 101.019 1.00 70.50  ? 1010 ASP A O   1 
ATOM   7992  C  CB  . ASP A 1 1439 ? 98.372  144.617 101.306 1.00 81.23  ? 1010 ASP A CB  1 
ATOM   7993  C  CG  . ASP A 1 1439 ? 99.083  143.932 100.145 1.00 93.10  ? 1010 ASP A CG  1 
ATOM   7994  O  OD1 . ASP A 1 1439 ? 100.336 143.974 100.104 1.00 88.62  ? 1010 ASP A OD1 1 
ATOM   7995  O  OD2 . ASP A 1 1439 ? 98.395  143.351 99.278  1.00 90.60  ? 1010 ASP A OD2 1 
ATOM   7996  N  N   . PHE A 1 1440 ? 99.061  147.680 101.562 1.00 55.57  ? 1011 PHE A N   1 
ATOM   7997  C  CA  . PHE A 1 1440 ? 99.469  148.919 100.924 1.00 57.80  ? 1011 PHE A CA  1 
ATOM   7998  C  C   . PHE A 1 1440 ? 100.752 149.452 101.547 1.00 57.35  ? 1011 PHE A C   1 
ATOM   7999  O  O   . PHE A 1 1440 ? 101.659 149.902 100.838 1.00 62.11  ? 1011 PHE A O   1 
ATOM   8000  C  CB  . PHE A 1 1440 ? 98.338  149.930 101.037 1.00 60.77  ? 1011 PHE A CB  1 
ATOM   8001  C  CG  . PHE A 1 1440 ? 98.544  151.138 100.212 1.00 70.51  ? 1011 PHE A CG  1 
ATOM   8002  C  CD1 . PHE A 1 1440 ? 99.327  151.078 99.071  1.00 75.18  ? 1011 PHE A CD1 1 
ATOM   8003  C  CD2 . PHE A 1 1440 ? 97.967  152.345 100.578 1.00 79.31  ? 1011 PHE A CD2 1 
ATOM   8004  C  CE1 . PHE A 1 1440 ? 99.530  152.206 98.301  1.00 88.93  ? 1011 PHE A CE1 1 
ATOM   8005  C  CE2 . PHE A 1 1440 ? 98.161  153.479 99.817  1.00 90.00  ? 1011 PHE A CE2 1 
ATOM   8006  C  CZ  . PHE A 1 1440 ? 98.944  153.413 98.674  1.00 96.87  ? 1011 PHE A CZ  1 
ATOM   8007  N  N   . GLU A 1 1441 ? 100.847 149.396 102.875 1.00 59.98  ? 1012 GLU A N   1 
ATOM   8008  C  CA  . GLU A 1 1441 ? 102.026 149.905 103.564 1.00 53.83  ? 1012 GLU A CA  1 
ATOM   8009  C  C   . GLU A 1 1441 ? 103.264 149.107 103.192 1.00 50.06  ? 1012 GLU A C   1 
ATOM   8010  O  O   . GLU A 1 1441 ? 104.333 149.680 102.974 1.00 55.12  ? 1012 GLU A O   1 
ATOM   8011  C  CB  . GLU A 1 1441 ? 101.792 149.879 105.078 1.00 59.68  ? 1012 GLU A CB  1 
ATOM   8012  C  CG  . GLU A 1 1441 ? 102.915 150.487 105.939 1.00 77.13  ? 1012 GLU A CG  1 
ATOM   8013  C  CD  . GLU A 1 1441 ? 102.677 150.322 107.462 1.00 85.22  ? 1012 GLU A CD  1 
ATOM   8014  O  OE1 . GLU A 1 1441 ? 103.652 150.080 108.217 1.00 76.71  ? 1012 GLU A OE1 1 
ATOM   8015  O  OE2 . GLU A 1 1441 ? 101.509 150.440 107.914 1.00 77.11  ? 1012 GLU A OE2 1 
ATOM   8016  N  N   . ASP A 1 1442 ? 103.154 147.780 103.148 1.00 55.79  ? 1013 ASP A N   1 
ATOM   8017  C  CA  . ASP A 1 1442 ? 104.331 146.987 102.810 1.00 51.34  ? 1013 ASP A CA  1 
ATOM   8018  C  C   . ASP A 1 1442 ? 104.785 147.291 101.409 1.00 40.72  ? 1013 ASP A C   1 
ATOM   8019  O  O   . ASP A 1 1442 ? 105.982 147.422 101.158 1.00 55.33  ? 1013 ASP A O   1 
ATOM   8020  C  CB  . ASP A 1 1442 ? 104.063 145.487 102.953 1.00 65.16  ? 1013 ASP A CB  1 
ATOM   8021  C  CG  . ASP A 1 1442 ? 103.713 145.073 104.382 1.00 69.23  ? 1013 ASP A CG  1 
ATOM   8022  O  OD1 . ASP A 1 1442 ? 103.634 145.956 105.267 1.00 67.31  ? 1013 ASP A OD1 1 
ATOM   8023  O  OD2 . ASP A 1 1442 ? 103.508 143.862 104.622 1.00 68.28  ? 1013 ASP A OD2 1 
ATOM   8024  N  N   . GLU A 1 1443 ? 103.850 147.436 100.487 1.00 42.60  ? 1014 GLU A N   1 
ATOM   8025  C  CA  . GLU A 1 1443 ? 104.250 147.832 99.146  1.00 53.15  ? 1014 GLU A CA  1 
ATOM   8026  C  C   . GLU A 1 1443 ? 104.926 149.204 99.146  1.00 62.47  ? 1014 GLU A C   1 
ATOM   8027  O  O   . GLU A 1 1443 ? 105.946 149.386 98.475  1.00 63.69  ? 1014 GLU A O   1 
ATOM   8028  C  CB  . GLU A 1 1443 ? 103.043 147.825 98.222  1.00 71.68  ? 1014 GLU A CB  1 
ATOM   8029  C  CG  . GLU A 1 1443 ? 102.515 146.417 97.944  1.00 92.63  ? 1014 GLU A CG  1 
ATOM   8030  C  CD  . GLU A 1 1443 ? 101.248 146.411 97.084  1.00 106.12 ? 1014 GLU A CD  1 
ATOM   8031  O  OE1 . GLU A 1 1443 ? 100.734 147.510 96.760  1.00 97.53  ? 1014 GLU A OE1 1 
ATOM   8032  O  OE2 . GLU A 1 1443 ? 100.754 145.306 96.755  1.00 99.52  ? 1014 GLU A OE2 1 
ATOM   8033  N  N   . MET A 1 1444 ? 104.381 150.184 99.886  1.00 56.98  ? 1015 MET A N   1 
ATOM   8034  C  CA  . MET A 1 1444 ? 104.973 151.525 99.872  1.00 41.62  ? 1015 MET A CA  1 
ATOM   8035  C  C   . MET A 1 1444 ? 106.344 151.534 100.502 1.00 41.03  ? 1015 MET A C   1 
ATOM   8036  O  O   . MET A 1 1444 ? 107.290 152.109 99.951  1.00 55.01  ? 1015 MET A O   1 
ATOM   8037  C  CB  . MET A 1 1444 ? 104.096 152.523 100.598 1.00 50.82  ? 1015 MET A CB  1 
ATOM   8038  C  CG  . MET A 1 1444 ? 102.800 152.784 99.906  1.00 71.48  ? 1015 MET A CG  1 
ATOM   8039  S  SD  . MET A 1 1444 ? 103.127 153.421 98.254  1.00 94.48  ? 1015 MET A SD  1 
ATOM   8040  C  CE  . MET A 1 1444 ? 103.967 154.962 98.634  1.00 80.91  ? 1015 MET A CE  1 
ATOM   8041  N  N   . VAL A 1 1445 ? 106.467 150.901 101.652 1.00 35.61  ? 1016 VAL A N   1 
ATOM   8042  C  CA  . VAL A 1 1445 ? 107.757 150.778 102.290 1.00 33.33  ? 1016 VAL A CA  1 
ATOM   8043  C  C   . VAL A 1 1445 ? 108.745 150.131 101.342 1.00 37.71  ? 1016 VAL A C   1 
ATOM   8044  O  O   . VAL A 1 1445 ? 109.867 150.614 101.165 1.00 47.50  ? 1016 VAL A O   1 
ATOM   8045  C  CB  . VAL A 1 1445 ? 107.619 149.980 103.592 1.00 42.91  ? 1016 VAL A CB  1 
ATOM   8046  C  CG1 . VAL A 1 1445 ? 108.969 149.511 104.065 1.00 50.30  ? 1016 VAL A CG1 1 
ATOM   8047  C  CG2 . VAL A 1 1445 ? 106.957 150.846 104.647 1.00 57.73  ? 1016 VAL A CG2 1 
ATOM   8048  N  N   . CYS A 1 1446 ? 108.345 149.042 100.700 1.00 39.84  ? 1017 CYS A N   1 
ATOM   8049  C  CA  . CYS A 1 1446 ? 109.304 148.337 99.870  1.00 43.30  ? 1017 CYS A CA  1 
ATOM   8050  C  C   . CYS A 1 1446 ? 109.688 149.147 98.647  1.00 48.08  ? 1017 CYS A C   1 
ATOM   8051  O  O   . CYS A 1 1446 ? 110.867 149.201 98.287  1.00 59.88  ? 1017 CYS A O   1 
ATOM   8052  C  CB  . CYS A 1 1446 ? 108.770 146.966 99.461  1.00 54.69  ? 1017 CYS A CB  1 
ATOM   8053  S  SG  . CYS A 1 1446 ? 108.614 145.792 100.831 1.00 81.79  ? 1017 CYS A SG  1 
ATOM   8054  N  N   . LYS A 1 1447 ? 108.731 149.778 97.981  1.00 41.94  ? 1018 LYS A N   1 
ATOM   8055  C  CA  . LYS A 1 1447 ? 109.116 150.578 96.831  1.00 36.15  ? 1018 LYS A CA  1 
ATOM   8056  C  C   . LYS A 1 1447 ? 110.063 151.659 97.274  1.00 37.43  ? 1018 LYS A C   1 
ATOM   8057  O  O   . LYS A 1 1447 ? 111.029 151.981 96.572  1.00 45.18  ? 1018 LYS A O   1 
ATOM   8058  C  CB  . LYS A 1 1447 ? 107.891 151.179 96.164  1.00 48.99  ? 1018 LYS A CB  1 
ATOM   8059  C  CG  . LYS A 1 1447 ? 107.113 150.156 95.339  1.00 62.36  ? 1018 LYS A CG  1 
ATOM   8060  C  CD  . LYS A 1 1447 ? 106.021 150.816 94.469  1.00 71.11  ? 1018 LYS A CD  1 
ATOM   8061  C  CE  . LYS A 1 1447 ? 104.901 151.450 95.320  1.00 68.69  ? 1018 LYS A CE  1 
ATOM   8062  N  NZ  . LYS A 1 1447 ? 104.130 150.429 96.119  1.00 74.77  ? 1018 LYS A NZ  1 
ATOM   8063  N  N   . TRP A 1 1448 ? 109.834 152.197 98.468  1.00 42.13  ? 1019 TRP A N   1 
ATOM   8064  C  CA  . TRP A 1 1448 ? 110.703 153.261 98.927  1.00 45.52  ? 1019 TRP A CA  1 
ATOM   8065  C  C   . TRP A 1 1448 ? 112.118 152.758 99.151  1.00 46.31  ? 1019 TRP A C   1 
ATOM   8066  O  O   . TRP A 1 1448 ? 113.065 153.259 98.532  1.00 47.77  ? 1019 TRP A O   1 
ATOM   8067  C  CB  . TRP A 1 1448 ? 110.134 153.929 100.171 1.00 40.59  ? 1019 TRP A CB  1 
ATOM   8068  C  CG  . TRP A 1 1448 ? 110.974 155.080 100.429 1.00 43.18  ? 1019 TRP A CG  1 
ATOM   8069  C  CD1 . TRP A 1 1448 ? 110.993 156.233 99.717  1.00 51.71  ? 1019 TRP A CD1 1 
ATOM   8070  C  CD2 . TRP A 1 1448 ? 111.863 155.261 101.514 1.00 39.52  ? 1019 TRP A CD2 1 
ATOM   8071  N  NE1 . TRP A 1 1448 ? 111.904 157.097 100.243 1.00 51.80  ? 1019 TRP A NE1 1 
ATOM   8072  C  CE2 . TRP A 1 1448 ? 112.442 156.530 101.364 1.00 46.94  ? 1019 TRP A CE2 1 
ATOM   8073  C  CE3 . TRP A 1 1448 ? 112.244 154.466 102.593 1.00 54.14  ? 1019 TRP A CE3 1 
ATOM   8074  C  CZ2 . TRP A 1 1448 ? 113.375 157.038 102.260 1.00 63.01  ? 1019 TRP A CZ2 1 
ATOM   8075  C  CZ3 . TRP A 1 1448 ? 113.184 154.961 103.477 1.00 65.26  ? 1019 TRP A CZ3 1 
ATOM   8076  C  CH2 . TRP A 1 1448 ? 113.741 156.238 103.306 1.00 70.99  ? 1019 TRP A CH2 1 
ATOM   8077  N  N   . LEU A 1 1449 ? 112.269 151.700 99.943  1.00 43.92  ? 1020 LEU A N   1 
ATOM   8078  C  CA  . LEU A 1 1449 ? 113.607 151.213 100.234 1.00 36.28  ? 1020 LEU A CA  1 
ATOM   8079  C  C   . LEU A 1 1449 ? 114.342 150.914 98.946  1.00 34.46  ? 1020 LEU A C   1 
ATOM   8080  O  O   . LEU A 1 1449 ? 115.572 150.973 98.894  1.00 44.69  ? 1020 LEU A O   1 
ATOM   8081  C  CB  . LEU A 1 1449 ? 113.521 149.978 101.120 1.00 43.96  ? 1020 LEU A CB  1 
ATOM   8082  C  CG  . LEU A 1 1449 ? 113.201 150.232 102.592 1.00 44.86  ? 1020 LEU A CG  1 
ATOM   8083  C  CD1 . LEU A 1 1449 ? 113.039 148.922 103.336 1.00 46.43  ? 1020 LEU A CD1 1 
ATOM   8084  C  CD2 . LEU A 1 1449 ? 114.290 151.056 103.235 1.00 46.21  ? 1020 LEU A CD2 1 
ATOM   8085  N  N   . LEU A 1 1450 ? 113.605 150.643 97.889  1.00 34.45  ? 1021 LEU A N   1 
ATOM   8086  C  CA  . LEU A 1 1450 ? 114.192 150.453 96.583  1.00 43.71  ? 1021 LEU A CA  1 
ATOM   8087  C  C   . LEU A 1 1450 ? 114.025 151.673 95.704  1.00 47.80  ? 1021 LEU A C   1 
ATOM   8088  O  O   . LEU A 1 1450 ? 114.245 151.583 94.493  1.00 50.48  ? 1021 LEU A O   1 
ATOM   8089  C  CB  . LEU A 1 1450 ? 113.562 149.246 95.886  1.00 55.95  ? 1021 LEU A CB  1 
ATOM   8090  C  CG  . LEU A 1 1450 ? 113.557 147.915 96.652  1.00 67.48  ? 1021 LEU A CG  1 
ATOM   8091  C  CD1 . LEU A 1 1450 ? 112.610 146.916 95.954  1.00 64.61  ? 1021 LEU A CD1 1 
ATOM   8092  C  CD2 . LEU A 1 1450 ? 114.972 147.329 96.885  1.00 64.08  ? 1021 LEU A CD2 1 
ATOM   8093  N  N   . SER A 1 1451 ? 113.602 152.794 96.255  1.00 37.05  ? 1022 SER A N   1 
ATOM   8094  C  CA  . SER A 1 1451 ? 113.489 153.952 95.399  1.00 33.99  ? 1022 SER A CA  1 
ATOM   8095  C  C   . SER A 1 1451 ? 114.794 154.726 95.299  1.00 40.79  ? 1022 SER A C   1 
ATOM   8096  O  O   . SER A 1 1451 ? 114.851 155.718 94.567  1.00 49.65  ? 1022 SER A O   1 
ATOM   8097  C  CB  . SER A 1 1451 ? 112.379 154.871 95.891  1.00 43.54  ? 1022 SER A CB  1 
ATOM   8098  O  OG  . SER A 1 1451 ? 112.670 155.341 97.195  1.00 48.84  ? 1022 SER A OG  1 
ATOM   8099  N  N   . SER A 1 1452 ? 115.840 154.306 95.998  1.00 34.78  ? 1023 SER A N   1 
ATOM   8100  C  CA  . SER A 1 1452 ? 117.102 155.020 95.918  1.00 36.11  ? 1023 SER A CA  1 
ATOM   8101  C  C   . SER A 1 1452 ? 117.673 154.929 94.521  1.00 36.26  ? 1023 SER A C   1 
ATOM   8102  O  O   . SER A 1 1452 ? 117.451 153.955 93.807  1.00 44.03  ? 1023 SER A O   1 
ATOM   8103  C  CB  . SER A 1 1452 ? 118.111 154.424 96.866  1.00 49.05  ? 1023 SER A CB  1 
ATOM   8104  O  OG  . SER A 1 1452 ? 118.315 153.073 96.500  1.00 53.90  ? 1023 SER A OG  1 
ATOM   8105  N  N   . THR A 1 1453 ? 118.422 155.954 94.129  1.00 43.40  ? 1024 THR A N   1 
ATOM   8106  C  CA  . THR A 1 1453 ? 118.955 155.968 92.769  1.00 49.10  ? 1024 THR A CA  1 
ATOM   8107  C  C   . THR A 1 1453 ? 119.941 154.843 92.518  1.00 51.60  ? 1024 THR A C   1 
ATOM   8108  O  O   . THR A 1 1453 ? 119.838 154.190 91.465  1.00 56.38  ? 1024 THR A O   1 
ATOM   8109  C  CB  . THR A 1 1453 ? 119.580 157.322 92.435  1.00 61.00  ? 1024 THR A CB  1 
ATOM   8110  O  OG1 . THR A 1 1453 ? 118.593 158.358 92.574  1.00 61.06  ? 1024 THR A OG1 1 
ATOM   8111  C  CG2 . THR A 1 1453 ? 120.137 157.293 90.998  1.00 64.47  ? 1024 THR A CG2 1 
ATOM   8112  N  N   . PRO A 1 1454 ? 120.913 154.577 93.374  1.00 44.17  ? 1025 PRO A N   1 
ATOM   8113  C  CA  . PRO A 1 1454 ? 121.531 153.246 93.351  1.00 46.41  ? 1025 PRO A CA  1 
ATOM   8114  C  C   . PRO A 1 1454 ? 120.750 152.304 94.250  1.00 48.91  ? 1025 PRO A C   1 
ATOM   8115  O  O   . PRO A 1 1454 ? 120.684 152.539 95.460  1.00 56.11  ? 1025 PRO A O   1 
ATOM   8116  C  CB  . PRO A 1 1454 ? 122.953 153.502 93.857  1.00 46.92  ? 1025 PRO A CB  1 
ATOM   8117  C  CG  . PRO A 1 1454 ? 122.887 154.839 94.572  1.00 52.54  ? 1025 PRO A CG  1 
ATOM   8118  C  CD  . PRO A 1 1454 ? 121.515 155.432 94.402  1.00 49.03  ? 1025 PRO A CD  1 
ATOM   8119  N  N   . VAL A 1 1455 ? 120.149 151.255 93.702  1.00 39.07  ? 1026 VAL A N   1 
ATOM   8120  C  CA  . VAL A 1 1455 ? 119.282 150.389 94.483  1.00 31.94  ? 1026 VAL A CA  1 
ATOM   8121  C  C   . VAL A 1 1455 ? 120.127 149.303 95.110  1.00 42.93  ? 1026 VAL A C   1 
ATOM   8122  O  O   . VAL A 1 1455 ? 120.936 148.668 94.425  1.00 51.00  ? 1026 VAL A O   1 
ATOM   8123  C  CB  . VAL A 1 1455 ? 118.197 149.773 93.611  1.00 38.77  ? 1026 VAL A CB  1 
ATOM   8124  C  CG1 . VAL A 1 1455 ? 117.232 148.991 94.488  1.00 52.58  ? 1026 VAL A CG1 1 
ATOM   8125  C  CG2 . VAL A 1 1455 ? 117.523 150.843 92.791  1.00 46.93  ? 1026 VAL A CG2 1 
ATOM   8126  N  N   . MET A 1 1456 ? 119.955 149.086 96.411  1.00 42.65  ? 1027 MET A N   1 
ATOM   8127  C  CA  . MET A 1 1456 ? 120.721 148.065 97.127  1.00 48.36  ? 1027 MET A CA  1 
ATOM   8128  C  C   . MET A 1 1456 ? 119.744 147.148 97.842  1.00 51.17  ? 1027 MET A C   1 
ATOM   8129  O  O   . MET A 1 1456 ? 119.232 147.476 98.914  1.00 54.10  ? 1027 MET A O   1 
ATOM   8130  C  CB  . MET A 1 1456 ? 121.710 148.674 98.101  1.00 51.69  ? 1027 MET A CB  1 
ATOM   8131  C  CG  . MET A 1 1456 ? 122.409 147.628 98.938  1.00 57.24  ? 1027 MET A CG  1 
ATOM   8132  S  SD  . MET A 1 1456 ? 123.974 148.211 99.626  1.00 91.70  ? 1027 MET A SD  1 
ATOM   8133  C  CE  . MET A 1 1456 ? 124.882 148.570 98.119  1.00 80.29  ? 1027 MET A CE  1 
ATOM   8134  N  N   . SER A 1 1457 ? 119.507 145.991 97.239  1.00 53.10  ? 1028 SER A N   1 
ATOM   8135  C  CA  . SER A 1 1457 ? 118.494 145.098 97.762  1.00 47.65  ? 1028 SER A CA  1 
ATOM   8136  C  C   . SER A 1 1457 ? 118.841 144.661 99.166  1.00 44.58  ? 1028 SER A C   1 
ATOM   8137  O  O   . SER A 1 1457 ? 117.962 144.577 100.030 1.00 57.60  ? 1028 SER A O   1 
ATOM   8138  C  CB  . SER A 1 1457 ? 118.346 143.891 96.839  1.00 58.75  ? 1028 SER A CB  1 
ATOM   8139  O  OG  . SER A 1 1457 ? 119.584 143.210 96.678  1.00 59.42  ? 1028 SER A OG  1 
ATOM   8140  N  N   . ARG A 1 1458 ? 120.110 144.374 99.421  1.00 44.90  ? 1029 ARG A N   1 
ATOM   8141  C  CA  . ARG A 1 1458 ? 120.433 143.826 100.728 1.00 56.89  ? 1029 ARG A CA  1 
ATOM   8142  C  C   . ARG A 1 1458 ? 120.159 144.845 101.825 1.00 66.38  ? 1029 ARG A C   1 
ATOM   8143  O  O   . ARG A 1 1458 ? 119.623 144.495 102.885 1.00 71.79  ? 1029 ARG A O   1 
ATOM   8144  C  CB  . ARG A 1 1458 ? 121.878 143.330 100.762 1.00 72.12  ? 1029 ARG A CB  1 
ATOM   8145  C  CG  . ARG A 1 1458 ? 122.062 142.098 101.663 1.00 81.87  ? 1029 ARG A CG  1 
ATOM   8146  C  CD  . ARG A 1 1458 ? 123.502 141.543 101.666 1.00 97.78  ? 1029 ARG A CD  1 
ATOM   8147  N  NE  . ARG A 1 1458 ? 123.957 141.143 100.331 1.00 101.09 ? 1029 ARG A NE  1 
ATOM   8148  C  CZ  . ARG A 1 1458 ? 124.823 141.830 99.587  1.00 103.53 ? 1029 ARG A CZ  1 
ATOM   8149  N  NH1 . ARG A 1 1458 ? 125.334 142.972 100.036 1.00 102.67 ? 1029 ARG A NH1 1 
ATOM   8150  N  NH2 . ARG A 1 1458 ? 125.169 141.377 98.385  1.00 91.01  ? 1029 ARG A NH2 1 
ATOM   8151  N  N   . PHE A 1 1459 ? 120.487 146.116 101.581 1.00 68.60  ? 1030 PHE A N   1 
ATOM   8152  C  CA  . PHE A 1 1459 ? 120.196 147.167 102.560 1.00 68.38  ? 1030 PHE A CA  1 
ATOM   8153  C  C   . PHE A 1 1459 ? 118.696 147.308 102.771 1.00 52.73  ? 1030 PHE A C   1 
ATOM   8154  O  O   . PHE A 1 1459 ? 118.223 147.497 103.900 1.00 56.51  ? 1030 PHE A O   1 
ATOM   8155  C  CB  . PHE A 1 1459 ? 120.822 148.487 102.089 1.00 67.00  ? 1030 PHE A CB  1 
ATOM   8156  C  CG  . PHE A 1 1459 ? 120.231 149.709 102.710 1.00 56.31  ? 1030 PHE A CG  1 
ATOM   8157  C  CD1 . PHE A 1 1459 ? 120.598 150.099 103.981 1.00 60.75  ? 1030 PHE A CD1 1 
ATOM   8158  C  CD2 . PHE A 1 1459 ? 119.320 150.480 102.009 1.00 63.15  ? 1030 PHE A CD2 1 
ATOM   8159  C  CE1 . PHE A 1 1459 ? 120.065 151.237 104.551 1.00 67.16  ? 1030 PHE A CE1 1 
ATOM   8160  C  CE2 . PHE A 1 1459 ? 118.779 151.620 102.569 1.00 71.90  ? 1030 PHE A CE2 1 
ATOM   8161  C  CZ  . PHE A 1 1459 ? 119.150 152.002 103.843 1.00 73.27  ? 1030 PHE A CZ  1 
ATOM   8162  N  N   . ALA A 1 1460 ? 117.938 147.236 101.683 1.00 52.19  ? 1031 ALA A N   1 
ATOM   8163  C  CA  . ALA A 1 1460 ? 116.501 147.219 101.812 1.00 47.14  ? 1031 ALA A CA  1 
ATOM   8164  C  C   . ALA A 1 1460 ? 116.088 146.125 102.768 1.00 44.77  ? 1031 ALA A C   1 
ATOM   8165  O  O   . ALA A 1 1460 ? 115.268 146.347 103.665 1.00 54.06  ? 1031 ALA A O   1 
ATOM   8166  C  CB  . ALA A 1 1460 ? 115.856 147.016 100.442 1.00 49.90  ? 1031 ALA A CB  1 
ATOM   8167  N  N   . ALA A 1 1461 ? 116.660 144.942 102.609 1.00 45.06  ? 1032 ALA A N   1 
ATOM   8168  C  CA  . ALA A 1 1461 ? 116.231 143.835 103.446 1.00 50.01  ? 1032 ALA A CA  1 
ATOM   8169  C  C   . ALA A 1 1461 ? 116.598 144.100 104.890 1.00 49.12  ? 1032 ALA A C   1 
ATOM   8170  O  O   . ALA A 1 1461 ? 115.835 143.773 105.810 1.00 56.54  ? 1032 ALA A O   1 
ATOM   8171  C  CB  . ALA A 1 1461 ? 116.847 142.526 102.947 1.00 54.09  ? 1032 ALA A CB  1 
ATOM   8172  N  N   . ASP A 1 1462 ? 117.745 144.734 105.099 1.00 48.94  ? 1033 ASP A N   1 
ATOM   8173  C  CA  . ASP A 1 1462 ? 118.216 144.948 106.457 1.00 52.30  ? 1033 ASP A CA  1 
ATOM   8174  C  C   . ASP A 1 1462 ? 117.324 145.929 107.203 1.00 53.67  ? 1033 ASP A C   1 
ATOM   8175  O  O   . ASP A 1 1462 ? 116.912 145.662 108.337 1.00 58.79  ? 1033 ASP A O   1 
ATOM   8176  C  CB  . ASP A 1 1462 ? 119.659 145.436 106.432 1.00 66.58  ? 1033 ASP A CB  1 
ATOM   8177  C  CG  . ASP A 1 1462 ? 120.365 145.242 107.764 1.00 83.33  ? 1033 ASP A CG  1 
ATOM   8178  O  OD1 . ASP A 1 1462 ? 119.754 144.658 108.689 1.00 78.01  ? 1033 ASP A OD1 1 
ATOM   8179  O  OD2 . ASP A 1 1462 ? 121.541 145.656 107.884 1.00 89.22  ? 1033 ASP A OD2 1 
ATOM   8180  N  N   . ILE A 1 1463 ? 117.002 147.059 106.584 1.00 50.82  ? 1034 ILE A N   1 
ATOM   8181  C  CA  . ILE A 1 1463 ? 116.075 147.989 107.224 1.00 45.58  ? 1034 ILE A CA  1 
ATOM   8182  C  C   . ILE A 1 1463 ? 114.726 147.317 107.434 1.00 47.72  ? 1034 ILE A C   1 
ATOM   8183  O  O   . ILE A 1 1463 ? 114.175 147.314 108.540 1.00 51.26  ? 1034 ILE A O   1 
ATOM   8184  C  CB  . ILE A 1 1463 ? 115.945 149.275 106.388 1.00 58.14  ? 1034 ILE A CB  1 
ATOM   8185  C  CG1 . ILE A 1 1463 ? 117.299 149.978 106.344 1.00 76.51  ? 1034 ILE A CG1 1 
ATOM   8186  C  CG2 . ILE A 1 1463 ? 114.862 150.210 106.937 1.00 59.99  ? 1034 ILE A CG2 1 
ATOM   8187  C  CD1 . ILE A 1 1463 ? 117.891 150.251 107.725 1.00 75.26  ? 1034 ILE A CD1 1 
ATOM   8188  N  N   . PHE A 1 1464 ? 114.200 146.698 106.378 1.00 47.22  ? 1035 PHE A N   1 
ATOM   8189  C  CA  . PHE A 1 1464 ? 112.911 146.048 106.451 1.00 33.53  ? 1035 PHE A CA  1 
ATOM   8190  C  C   . PHE A 1 1464 ? 112.839 145.156 107.656 1.00 31.18  ? 1035 PHE A C   1 
ATOM   8191  O  O   . PHE A 1 1464 ? 111.798 145.065 108.290 1.00 39.89  ? 1035 PHE A O   1 
ATOM   8192  C  CB  . PHE A 1 1464 ? 112.707 145.238 105.184 1.00 39.93  ? 1035 PHE A CB  1 
ATOM   8193  C  CG  . PHE A 1 1464 ? 111.302 144.831 104.936 1.00 53.50  ? 1035 PHE A CG  1 
ATOM   8194  C  CD1 . PHE A 1 1464 ? 110.866 143.561 105.284 1.00 65.78  ? 1035 PHE A CD1 1 
ATOM   8195  C  CD2 . PHE A 1 1464 ? 110.422 145.680 104.295 1.00 57.51  ? 1035 PHE A CD2 1 
ATOM   8196  C  CE1 . PHE A 1 1464 ? 109.549 143.155 105.035 1.00 63.74  ? 1035 PHE A CE1 1 
ATOM   8197  C  CE2 . PHE A 1 1464 ? 109.107 145.280 104.041 1.00 62.11  ? 1035 PHE A CE2 1 
ATOM   8198  C  CZ  . PHE A 1 1464 ? 108.672 144.015 104.409 1.00 58.62  ? 1035 PHE A CZ  1 
ATOM   8199  N  N   . SER A 1 1465 ? 113.938 144.509 108.014 1.00 36.78  ? 1036 SER A N   1 
ATOM   8200  C  CA  . SER A 1 1465 ? 113.876 143.657 109.192 1.00 43.39  ? 1036 SER A CA  1 
ATOM   8201  C  C   . SER A 1 1465 ? 113.478 144.437 110.439 1.00 55.62  ? 1036 SER A C   1 
ATOM   8202  O  O   . SER A 1 1465 ? 112.949 143.839 111.383 1.00 63.94  ? 1036 SER A O   1 
ATOM   8203  C  CB  . SER A 1 1465 ? 115.216 142.947 109.442 1.00 53.88  ? 1036 SER A CB  1 
ATOM   8204  O  OG  . SER A 1 1465 ? 115.568 142.061 108.386 1.00 55.78  ? 1036 SER A OG  1 
ATOM   8205  N  N   . ARG A 1 1466 ? 113.715 145.751 110.465 1.00 48.38  ? 1037 ARG A N   1 
ATOM   8206  C  CA  . ARG A 1 1466 ? 113.403 146.594 111.615 1.00 41.77  ? 1037 ARG A CA  1 
ATOM   8207  C  C   . ARG A 1 1466 ? 112.090 147.330 111.471 1.00 40.46  ? 1037 ARG A C   1 
ATOM   8208  O  O   . ARG A 1 1466 ? 111.508 147.725 112.481 1.00 49.81  ? 1037 ARG A O   1 
ATOM   8209  C  CB  . ARG A 1 1466 ? 114.501 147.642 111.822 1.00 52.36  ? 1037 ARG A CB  1 
ATOM   8210  C  CG  . ARG A 1 1466 ? 115.778 147.143 112.490 1.00 67.43  ? 1037 ARG A CG  1 
ATOM   8211  C  CD  . ARG A 1 1466 ? 116.697 146.358 111.545 1.00 58.17  ? 1037 ARG A CD  1 
ATOM   8212  N  NE  . ARG A 1 1466 ? 117.955 145.997 112.189 1.00 57.95  ? 1037 ARG A NE  1 
ATOM   8213  C  CZ  . ARG A 1 1466 ? 118.790 145.077 111.724 1.00 61.42  ? 1037 ARG A CZ  1 
ATOM   8214  N  NH1 . ARG A 1 1466 ? 118.485 144.392 110.635 1.00 62.25  ? 1037 ARG A NH1 1 
ATOM   8215  N  NH2 . ARG A 1 1466 ? 119.910 144.807 112.375 1.00 71.52  ? 1037 ARG A NH2 1 
ATOM   8216  N  N   . THR A 1 1467 ? 111.639 147.546 110.245 1.00 40.80  ? 1038 THR A N   1 
ATOM   8217  C  CA  . THR A 1 1467 ? 110.416 148.266 110.009 1.00 36.17  ? 1038 THR A CA  1 
ATOM   8218  C  C   . THR A 1 1467 ? 109.258 147.378 110.439 1.00 32.08  ? 1038 THR A C   1 
ATOM   8219  O  O   . THR A 1 1467 ? 109.427 146.176 110.619 1.00 43.99  ? 1038 THR A O   1 
ATOM   8220  C  CB  . THR A 1 1467 ? 110.328 148.656 108.531 1.00 46.72  ? 1038 THR A CB  1 
ATOM   8221  O  OG1 . THR A 1 1467 ? 109.304 149.630 108.329 1.00 59.15  ? 1038 THR A OG1 1 
ATOM   8222  C  CG2 . THR A 1 1467 ? 109.975 147.467 107.676 1.00 50.14  ? 1038 THR A CG2 1 
ATOM   8223  N  N   . PRO A 1 1468 ? 108.101 147.951 110.696 1.00 30.11  ? 1039 PRO A N   1 
ATOM   8224  C  CA  . PRO A 1 1468 ? 106.965 147.123 111.077 1.00 33.58  ? 1039 PRO A CA  1 
ATOM   8225  C  C   . PRO A 1 1468 ? 106.587 146.117 110.030 1.00 48.32  ? 1039 PRO A C   1 
ATOM   8226  O  O   . PRO A 1 1468 ? 106.017 145.066 110.362 1.00 57.70  ? 1039 PRO A O   1 
ATOM   8227  C  CB  . PRO A 1 1468 ? 105.849 148.141 111.287 1.00 47.70  ? 1039 PRO A CB  1 
ATOM   8228  C  CG  . PRO A 1 1468 ? 106.555 149.346 111.680 1.00 62.62  ? 1039 PRO A CG  1 
ATOM   8229  C  CD  . PRO A 1 1468 ? 107.838 149.368 110.932 1.00 55.02  ? 1039 PRO A CD  1 
ATOM   8230  N  N   . SER A 1 1469 ? 106.864 146.396 108.767 1.00 40.83  ? 1040 SER A N   1 
ATOM   8231  C  CA  . SER A 1 1469 ? 106.540 145.406 107.755 1.00 38.02  ? 1040 SER A CA  1 
ATOM   8232  C  C   . SER A 1 1469 ? 107.365 144.139 107.940 1.00 43.74  ? 1040 SER A C   1 
ATOM   8233  O  O   . SER A 1 1469 ? 106.870 143.035 107.700 1.00 56.44  ? 1040 SER A O   1 
ATOM   8234  C  CB  . SER A 1 1469 ? 106.752 146.008 106.379 1.00 53.42  ? 1040 SER A CB  1 
ATOM   8235  O  OG  . SER A 1 1469 ? 105.952 147.172 106.227 1.00 61.44  ? 1040 SER A OG  1 
ATOM   8236  N  N   . GLY A 1 1470 ? 108.604 144.266 108.408 1.00 46.60  ? 1041 GLY A N   1 
ATOM   8237  C  CA  . GLY A 1 1470 ? 109.388 143.085 108.731 1.00 38.59  ? 1041 GLY A CA  1 
ATOM   8238  C  C   . GLY A 1 1470 ? 108.798 142.295 109.878 1.00 43.75  ? 1041 GLY A C   1 
ATOM   8239  O  O   . GLY A 1 1470 ? 108.845 141.064 109.877 1.00 54.82  ? 1041 GLY A O   1 
ATOM   8240  N  N   . LYS A 1 1471 ? 108.228 142.984 110.869 1.00 43.04  ? 1042 LYS A N   1 
ATOM   8241  C  CA  . LYS A 1 1471 ? 107.548 142.289 111.963 1.00 52.19  ? 1042 LYS A CA  1 
ATOM   8242  C  C   . LYS A 1 1471 ? 106.311 141.544 111.474 1.00 45.72  ? 1042 LYS A C   1 
ATOM   8243  O  O   . LYS A 1 1471 ? 106.023 140.430 111.933 1.00 52.37  ? 1042 LYS A O   1 
ATOM   8244  C  CB  . LYS A 1 1471 ? 107.176 143.275 113.072 1.00 62.13  ? 1042 LYS A CB  1 
ATOM   8245  C  CG  . LYS A 1 1471 ? 108.370 144.033 113.677 1.00 72.23  ? 1042 LYS A CG  1 
ATOM   8246  C  CD  . LYS A 1 1471 ? 109.300 143.106 114.484 1.00 84.74  ? 1042 LYS A CD  1 
ATOM   8247  C  CE  . LYS A 1 1471 ? 108.594 142.493 115.705 1.00 86.60  ? 1042 LYS A CE  1 
ATOM   8248  N  NZ  . LYS A 1 1471 ? 108.116 143.527 116.686 1.00 76.46  ? 1042 LYS A NZ  1 
ATOM   8249  N  N   . ARG A 1 1472 ? 105.567 142.135 110.551 1.00 38.41  ? 1043 ARG A N   1 
ATOM   8250  C  CA  . ARG A 1 1472 ? 104.456 141.398 109.971 1.00 36.57  ? 1043 ARG A CA  1 
ATOM   8251  C  C   . ARG A 1 1472 ? 104.956 140.176 109.199 1.00 42.83  ? 1043 ARG A C   1 
ATOM   8252  O  O   . ARG A 1 1472 ? 104.345 139.103 109.272 1.00 50.43  ? 1043 ARG A O   1 
ATOM   8253  C  CB  . ARG A 1 1472 ? 103.632 142.323 109.079 1.00 47.70  ? 1043 ARG A CB  1 
ATOM   8254  C  CG  . ARG A 1 1472 ? 102.800 143.339 109.869 1.00 54.72  ? 1043 ARG A CG  1 
ATOM   8255  C  CD  . ARG A 1 1472 ? 101.779 144.049 109.005 1.00 51.28  ? 1043 ARG A CD  1 
ATOM   8256  N  NE  . ARG A 1 1472 ? 102.455 145.029 108.166 1.00 57.99  ? 1043 ARG A NE  1 
ATOM   8257  C  CZ  . ARG A 1 1472 ? 102.583 146.316 108.472 1.00 67.29  ? 1043 ARG A CZ  1 
ATOM   8258  N  NH1 . ARG A 1 1472 ? 102.085 146.777 109.612 1.00 64.02  ? 1043 ARG A NH1 1 
ATOM   8259  N  NH2 . ARG A 1 1472 ? 103.225 147.138 107.645 1.00 68.24  ? 1043 ARG A NH2 1 
ATOM   8260  N  N   . LEU A 1 1473 ? 106.071 140.304 108.459 1.00 37.25  ? 1044 LEU A N   1 
ATOM   8261  C  CA  . LEU A 1 1473 ? 106.591 139.146 107.725 1.00 28.79  ? 1044 LEU A CA  1 
ATOM   8262  C  C   . LEU A 1 1473 ? 107.140 138.074 108.635 1.00 31.72  ? 1044 LEU A C   1 
ATOM   8263  O  O   . LEU A 1 1473 ? 107.203 136.912 108.237 1.00 39.51  ? 1044 LEU A O   1 
ATOM   8264  C  CB  . LEU A 1 1473 ? 107.677 139.525 106.739 1.00 31.91  ? 1044 LEU A CB  1 
ATOM   8265  C  CG  . LEU A 1 1473 ? 107.084 139.951 105.401 1.00 56.19  ? 1044 LEU A CG  1 
ATOM   8266  C  CD1 . LEU A 1 1473 ? 106.338 138.740 104.816 1.00 58.90  ? 1044 LEU A CD1 1 
ATOM   8267  C  CD2 . LEU A 1 1473 ? 106.176 141.173 105.427 1.00 57.86  ? 1044 LEU A CD2 1 
ATOM   8268  N  N   . GLN A 1 1474 ? 107.582 138.439 109.826 1.00 35.12  ? 1045 GLN A N   1 
ATOM   8269  C  CA  . GLN A 1 1474 ? 108.002 137.432 110.790 1.00 37.73  ? 1045 GLN A CA  1 
ATOM   8270  C  C   . GLN A 1 1474 ? 106.814 136.743 111.421 1.00 30.22  ? 1045 GLN A C   1 
ATOM   8271  O  O   . GLN A 1 1474 ? 106.814 135.524 111.577 1.00 45.73  ? 1045 GLN A O   1 
ATOM   8272  C  CB  . GLN A 1 1474 ? 108.863 138.062 111.883 1.00 56.92  ? 1045 GLN A CB  1 
ATOM   8273  C  CG  . GLN A 1 1474 ? 110.255 138.485 111.391 1.00 71.99  ? 1045 GLN A CG  1 
ATOM   8274  C  CD  . GLN A 1 1474 ? 111.134 139.092 112.481 1.00 82.02  ? 1045 GLN A CD  1 
ATOM   8275  O  OE1 . GLN A 1 1474 ? 110.778 139.090 113.665 1.00 83.11  ? 1045 GLN A OE1 1 
ATOM   8276  N  NE2 . GLN A 1 1474 ? 112.267 139.666 112.071 1.00 75.18  ? 1045 GLN A NE2 1 
ATOM   8277  N  N   . ILE A 1 1475 ? 105.801 137.490 111.801 1.00 25.96  ? 1046 ILE A N   1 
ATOM   8278  C  CA  . ILE A 1 1475 ? 104.638 136.837 112.359 1.00 25.96  ? 1046 ILE A CA  1 
ATOM   8279  C  C   . ILE A 1 1475 ? 104.018 135.890 111.348 1.00 36.45  ? 1046 ILE A C   1 
ATOM   8280  O  O   . ILE A 1 1475 ? 103.620 134.776 111.700 1.00 45.08  ? 1046 ILE A O   1 
ATOM   8281  C  CB  . ILE A 1 1475 ? 103.632 137.886 112.834 1.00 43.12  ? 1046 ILE A CB  1 
ATOM   8282  C  CG1 . ILE A 1 1475 ? 104.038 138.388 114.210 1.00 57.31  ? 1046 ILE A CG1 1 
ATOM   8283  C  CG2 . ILE A 1 1475 ? 102.235 137.300 112.854 1.00 53.94  ? 1046 ILE A CG2 1 
ATOM   8284  C  CD1 . ILE A 1 1475 ? 103.956 137.288 115.257 1.00 69.45  ? 1046 ILE A CD1 1 
ATOM   8285  N  N   . LEU A 1 1476 ? 103.916 136.313 110.075 1.00 41.32  ? 1047 LEU A N   1 
ATOM   8286  C  CA  . LEU A 1 1476 ? 103.296 135.470 109.044 1.00 32.41  ? 1047 LEU A CA  1 
ATOM   8287  C  C   . LEU A 1 1476 ? 104.076 134.191 108.811 1.00 43.81  ? 1047 LEU A C   1 
ATOM   8288  O  O   . LEU A 1 1476 ? 103.482 133.125 108.620 1.00 54.69  ? 1047 LEU A O   1 
ATOM   8289  C  CB  . LEU A 1 1476 ? 103.175 136.194 107.707 1.00 31.83  ? 1047 LEU A CB  1 
ATOM   8290  C  CG  . LEU A 1 1476 ? 102.228 137.365 107.515 1.00 39.92  ? 1047 LEU A CG  1 
ATOM   8291  C  CD1 . LEU A 1 1476 ? 102.255 137.858 106.074 1.00 42.15  ? 1047 LEU A CD1 1 
ATOM   8292  C  CD2 . LEU A 1 1476 ? 100.849 136.922 107.872 1.00 45.14  ? 1047 LEU A CD2 1 
ATOM   8293  N  N   . GLY A 1 1477 ? 105.400 134.276 108.764 1.00 42.24  ? 1048 GLY A N   1 
ATOM   8294  C  CA  . GLY A 1 1477 ? 106.190 133.096 108.481 1.00 44.36  ? 1048 GLY A CA  1 
ATOM   8295  C  C   . GLY A 1 1477 ? 106.243 132.142 109.655 1.00 54.78  ? 1048 GLY A C   1 
ATOM   8296  O  O   . GLY A 1 1477 ? 107.299 131.976 110.276 1.00 59.81  ? 1048 GLY A O   1 
ATOM   8297  N  N   . TYR A 1 1478 ? 105.105 131.525 109.993 1.00 56.62  ? 1049 TYR A N   1 
ATOM   8298  C  CA  . TYR A 1 1478 ? 105.069 130.500 111.029 1.00 60.69  ? 1049 TYR A CA  1 
ATOM   8299  C  C   . TYR A 1 1478 ? 104.545 129.155 110.545 1.00 70.84  ? 1049 TYR A C   1 
ATOM   8300  O  O   . TYR A 1 1478 ? 104.521 128.202 111.333 1.00 75.50  ? 1049 TYR A O   1 
ATOM   8301  C  CB  . TYR A 1 1478 ? 104.213 130.934 112.217 1.00 50.18  ? 1049 TYR A CB  1 
ATOM   8302  C  CG  . TYR A 1 1478 ? 102.767 130.619 112.013 1.00 49.19  ? 1049 TYR A CG  1 
ATOM   8303  C  CD1 . TYR A 1 1478 ? 102.219 129.447 112.507 1.00 64.93  ? 1049 TYR A CD1 1 
ATOM   8304  C  CD2 . TYR A 1 1478 ? 101.929 131.513 111.382 1.00 58.51  ? 1049 TYR A CD2 1 
ATOM   8305  C  CE1 . TYR A 1 1478 ? 100.882 129.139 112.316 1.00 74.99  ? 1049 TYR A CE1 1 
ATOM   8306  C  CE2 . TYR A 1 1478 ? 100.577 131.230 111.204 1.00 68.13  ? 1049 TYR A CE2 1 
ATOM   8307  C  CZ  . TYR A 1 1478 ? 100.056 130.041 111.672 1.00 70.66  ? 1049 TYR A CZ  1 
ATOM   8308  O  OH  . TYR A 1 1478 ? 98.716  129.756 111.493 1.00 62.87  ? 1049 TYR A OH  1 
ATOM   8309  N  N   . LEU A 1 1479 ? 104.114 129.045 109.293 1.00 69.52  ? 1050 LEU A N   1 
ATOM   8310  C  CA  . LEU A 1 1479 ? 103.514 127.822 108.767 1.00 70.36  ? 1050 LEU A CA  1 
ATOM   8311  C  C   . LEU A 1 1479 ? 104.559 127.057 107.959 1.00 72.36  ? 1050 LEU A C   1 
ATOM   8312  O  O   . LEU A 1 1479 ? 104.968 127.506 106.883 1.00 77.98  ? 1050 LEU A O   1 
ATOM   8313  C  CB  . LEU A 1 1479 ? 102.293 128.172 107.918 1.00 73.07  ? 1050 LEU A CB  1 
ATOM   8314  C  CG  . LEU A 1 1479 ? 101.193 127.131 107.740 1.00 77.75  ? 1050 LEU A CG  1 
ATOM   8315  C  CD1 . LEU A 1 1479 ? 100.574 126.804 109.087 1.00 82.43  ? 1050 LEU A CD1 1 
ATOM   8316  C  CD2 . LEU A 1 1479 ? 100.136 127.687 106.799 1.00 77.09  ? 1050 LEU A CD2 1 
ATOM   8317  N  N   . GLU A 1 1480 ? 104.999 125.902 108.472 1.00 72.37  ? 1051 GLU A N   1 
ATOM   8318  C  CA  . GLU A 1 1480 ? 105.964 125.083 107.745 1.00 77.39  ? 1051 GLU A CA  1 
ATOM   8319  C  C   . GLU A 1 1480 ? 105.599 123.601 107.696 1.00 78.66  ? 1051 GLU A C   1 
ATOM   8320  O  O   . GLU A 1 1480 ? 106.415 122.793 107.240 1.00 85.49  ? 1051 GLU A O   1 
ATOM   8321  C  CB  . GLU A 1 1480 ? 107.385 125.228 108.323 1.00 83.40  ? 1051 GLU A CB  1 
ATOM   8322  C  CG  . GLU A 1 1480 ? 108.057 126.602 108.146 1.00 91.51  ? 1051 GLU A CG  1 
ATOM   8323  C  CD  . GLU A 1 1480 ? 107.729 127.595 109.271 1.00 95.97  ? 1051 GLU A CD  1 
ATOM   8324  O  OE1 . GLU A 1 1480 ? 107.155 127.166 110.302 1.00 93.11  ? 1051 GLU A OE1 1 
ATOM   8325  O  OE2 . GLU A 1 1480 ? 108.065 128.799 109.136 1.00 85.17  ? 1051 GLU A OE2 1 
ATOM   8326  N  N   . GLY A 1 1481 ? 104.411 123.216 108.135 1.00 74.08  ? 1052 GLY A N   1 
ATOM   8327  C  CA  . GLY A 1 1481 ? 103.952 121.839 108.028 1.00 71.72  ? 1052 GLY A CA  1 
ATOM   8328  C  C   . GLY A 1 1481 ? 102.830 121.751 107.009 1.00 77.89  ? 1052 GLY A C   1 
ATOM   8329  O  O   . GLY A 1 1481 ? 102.084 122.712 106.816 1.00 85.59  ? 1052 GLY A O   1 
ATOM   8330  N  N   . THR A 1 1482 ? 102.737 120.606 106.334 1.00 76.38  ? 1053 THR A N   1 
ATOM   8331  C  CA  . THR A 1 1482 ? 101.636 120.395 105.396 1.00 77.81  ? 1053 THR A CA  1 
ATOM   8332  C  C   . THR A 1 1482 ? 100.326 120.096 106.115 1.00 74.70  ? 1053 THR A C   1 
ATOM   8333  O  O   . THR A 1 1482 ? 99.259  120.572 105.705 1.00 83.01  ? 1053 THR A O   1 
ATOM   8334  C  CB  . THR A 1 1482 ? 101.979 119.263 104.427 1.00 83.48  ? 1053 THR A CB  1 
ATOM   8335  O  OG1 . THR A 1 1482 ? 103.094 119.648 103.606 1.00 74.94  ? 1053 THR A OG1 1 
ATOM   8336  C  CG2 . THR A 1 1482 ? 100.753 118.882 103.559 1.00 77.02  ? 1053 THR A CG2 1 
ATOM   8337  N  N   . ARG A 1 1483 ? 100.383 119.298 107.177 1.00 77.10  ? 1054 ARG A N   1 
ATOM   8338  C  CA  . ARG A 1 1483 ? 99.173  118.980 107.924 1.00 79.53  ? 1054 ARG A CA  1 
ATOM   8339  C  C   . ARG A 1 1483 ? 98.593  120.221 108.592 1.00 84.06  ? 1054 ARG A C   1 
ATOM   8340  O  O   . ARG A 1 1483 ? 97.370  120.373 108.662 1.00 91.93  ? 1054 ARG A O   1 
ATOM   8341  C  CB  . ARG A 1 1483 ? 99.469  117.900 108.962 1.00 92.79  ? 1054 ARG A CB  1 
ATOM   8342  C  CG  . ARG A 1 1483 ? 98.272  117.476 109.801 1.00 98.11  ? 1054 ARG A CG  1 
ATOM   8343  C  CD  . ARG A 1 1483 ? 98.698  116.468 110.868 1.00 109.02 ? 1054 ARG A CD  1 
ATOM   8344  N  NE  . ARG A 1 1483 ? 99.691  117.036 111.794 1.00 117.31 ? 1054 ARG A NE  1 
ATOM   8345  C  CZ  . ARG A 1 1483 ? 99.397  117.731 112.895 1.00 118.61 ? 1054 ARG A CZ  1 
ATOM   8346  N  NH1 . ARG A 1 1483 ? 98.131  117.954 113.228 1.00 120.90 ? 1054 ARG A NH1 1 
ATOM   8347  N  NH2 . ARG A 1 1483 ? 100.369 118.204 113.667 1.00 106.43 ? 1054 ARG A NH2 1 
ATOM   8348  N  N   . THR A 1 1484 ? 99.446  121.118 109.102 1.00 82.30  ? 1055 THR A N   1 
ATOM   8349  C  CA  . THR A 1 1484 ? 98.924  122.336 109.721 1.00 81.93  ? 1055 THR A CA  1 
ATOM   8350  C  C   . THR A 1 1484 ? 98.201  123.203 108.696 1.00 79.27  ? 1055 THR A C   1 
ATOM   8351  O  O   . THR A 1 1484 ? 97.105  123.705 108.959 1.00 91.10  ? 1055 THR A O   1 
ATOM   8352  C  CB  . THR A 1 1484 ? 100.045 123.133 110.392 1.00 83.81  ? 1055 THR A CB  1 
ATOM   8353  O  OG1 . THR A 1 1484 ? 100.965 123.596 109.398 1.00 83.50  ? 1055 THR A OG1 1 
ATOM   8354  C  CG2 . THR A 1 1484 ? 100.798 122.252 111.394 1.00 92.02  ? 1055 THR A CG2 1 
ATOM   8355  N  N   . LEU A 1 1485 ? 98.792  123.374 107.516 1.00 74.71  ? 1056 LEU A N   1 
ATOM   8356  C  CA  . LEU A 1 1485 ? 98.129  124.142 106.473 1.00 74.67  ? 1056 LEU A CA  1 
ATOM   8357  C  C   . LEU A 1 1485 ? 96.802  123.505 106.085 1.00 83.01  ? 1056 LEU A C   1 
ATOM   8358  O  O   . LEU A 1 1485 ? 95.778  124.189 105.997 1.00 93.78  ? 1056 LEU A O   1 
ATOM   8359  C  CB  . LEU A 1 1485 ? 99.041  124.249 105.251 1.00 77.30  ? 1056 LEU A CB  1 
ATOM   8360  C  CG  . LEU A 1 1485 ? 98.405  124.791 103.966 1.00 85.32  ? 1056 LEU A CG  1 
ATOM   8361  C  CD1 . LEU A 1 1485 ? 98.055  126.265 104.142 1.00 84.06  ? 1056 LEU A CD1 1 
ATOM   8362  C  CD2 . LEU A 1 1485 ? 99.276  124.559 102.716 1.00 75.64  ? 1056 LEU A CD2 1 
ATOM   8363  N  N   . LEU A 1 1486 ? 96.795  122.192 105.877 1.00 90.02  ? 1057 LEU A N   1 
ATOM   8364  C  CA  . LEU A 1 1486 ? 95.664  121.506 105.262 1.00 88.98  ? 1057 LEU A CA  1 
ATOM   8365  C  C   . LEU A 1 1486 ? 94.618  121.046 106.265 1.00 85.67  ? 1057 LEU A C   1 
ATOM   8366  O  O   . LEU A 1 1486 ? 93.585  120.513 105.853 1.00 94.14  ? 1057 LEU A O   1 
ATOM   8367  C  CB  . LEU A 1 1486 ? 96.168  120.300 104.447 1.00 80.32  ? 1057 LEU A CB  1 
ATOM   8368  C  CG  . LEU A 1 1486 ? 95.301  119.772 103.302 1.00 81.98  ? 1057 LEU A CG  1 
ATOM   8369  C  CD1 . LEU A 1 1486 ? 94.944  120.896 102.325 1.00 77.43  ? 1057 LEU A CD1 1 
ATOM   8370  C  CD2 . LEU A 1 1486 ? 96.013  118.626 102.580 1.00 71.66  ? 1057 LEU A CD2 1 
ATOM   8371  N  N   . ALA A 1 1487 ? 94.850  121.228 107.563 1.00 89.46  ? 1058 ALA A N   1 
ATOM   8372  C  CA  . ALA A 1 1487 ? 93.913  120.704 108.548 1.00 103.94 ? 1058 ALA A CA  1 
ATOM   8373  C  C   . ALA A 1 1487 ? 93.717  121.629 109.742 1.00 117.66 ? 1058 ALA A C   1 
ATOM   8374  O  O   . ALA A 1 1487 ? 93.158  121.188 110.758 1.00 119.65 ? 1058 ALA A O   1 
ATOM   8375  C  CB  . ALA A 1 1487 ? 94.358  119.317 109.046 1.00 104.96 ? 1058 ALA A CB  1 
ATOM   8376  N  N   . SER A 1 1488 ? 94.170  122.881 109.669 1.00 115.99 ? 1059 SER A N   1 
ATOM   8377  C  CA  . SER A 1 1488 ? 93.984  123.810 110.780 1.00 126.94 ? 1059 SER A CA  1 
ATOM   8378  C  C   . SER A 1 1488 ? 92.524  124.273 110.854 1.00 135.12 ? 1059 SER A C   1 
ATOM   8379  O  O   . SER A 1 1488 ? 91.855  124.433 109.826 1.00 133.66 ? 1059 SER A O   1 
ATOM   8380  C  CB  . SER A 1 1488 ? 94.930  125.008 110.623 1.00 120.43 ? 1059 SER A CB  1 
ATOM   8381  O  OG  . SER A 1 1488 ? 94.805  125.941 111.684 1.00 123.18 ? 1059 SER A OG  1 
ATOM   8382  N  N   . LYS A 1 1489 ? 92.021  124.470 112.087 1.00 138.11 ? 1060 LYS A N   1 
ATOM   8383  C  CA  . LYS A 1 1489 ? 90.664  124.992 112.284 1.00 141.61 ? 1060 LYS A CA  1 
ATOM   8384  C  C   . LYS A 1 1489 ? 90.550  126.473 111.908 1.00 138.92 ? 1060 LYS A C   1 
ATOM   8385  O  O   . LYS A 1 1489 ? 89.438  126.943 111.628 1.00 139.33 ? 1060 LYS A O   1 
ATOM   8386  C  CB  . LYS A 1 1489 ? 90.204  124.771 113.744 1.00 139.47 ? 1060 LYS A CB  1 
ATOM   8387  C  CG  . LYS A 1 1489 ? 88.665  124.816 113.973 1.00 135.20 ? 1060 LYS A CG  1 
ATOM   8388  C  CD  . LYS A 1 1489 ? 88.278  124.573 115.448 1.00 122.92 ? 1060 LYS A CD  1 
ATOM   8389  C  CE  . LYS A 1 1489 ? 86.760  124.438 115.636 1.00 111.19 ? 1060 LYS A CE  1 
ATOM   8390  N  NZ  . LYS A 1 1489 ? 86.176  123.277 114.894 1.00 106.32 ? 1060 LYS A NZ  1 
ATOM   8391  N  N   . ILE A 1 1490 ? 91.674  127.205 111.870 1.00 139.19 ? 1061 ILE A N   1 
ATOM   8392  C  CA  . ILE A 1 1490 ? 91.676  128.630 111.517 1.00 139.88 ? 1061 ILE A CA  1 
ATOM   8393  C  C   . ILE A 1 1490 ? 92.148  128.896 110.066 1.00 135.13 ? 1061 ILE A C   1 
ATOM   8394  O  O   . ILE A 1 1490 ? 92.021  130.039 109.595 1.00 124.35 ? 1061 ILE A O   1 
ATOM   8395  C  CB  . ILE A 1 1490 ? 92.510  129.451 112.550 1.00 130.57 ? 1061 ILE A CB  1 
ATOM   8396  C  CG1 . ILE A 1 1490 ? 92.056  130.929 112.656 1.00 119.61 ? 1061 ILE A CG1 1 
ATOM   8397  C  CG2 . ILE A 1 1490 ? 94.036  129.349 112.307 1.00 114.55 ? 1061 ILE A CG2 1 
ATOM   8398  C  CD1 . ILE A 1 1490 ? 90.617  131.130 113.162 1.00 110.62 ? 1061 ILE A CD1 1 
ATOM   8399  N  N   . ILE A 1 1491 ? 92.659  127.883 109.344 1.00 137.25 ? 1062 ILE A N   1 
ATOM   8400  C  CA  . ILE A 1 1491 ? 93.144  128.045 107.951 1.00 134.84 ? 1062 ILE A CA  1 
ATOM   8401  C  C   . ILE A 1 1491 ? 92.083  127.644 106.916 1.00 136.98 ? 1062 ILE A C   1 
ATOM   8402  O  O   . ILE A 1 1491 ? 91.858  128.373 105.942 1.00 136.94 ? 1062 ILE A O   1 
ATOM   8403  C  CB  . ILE A 1 1491 ? 94.473  127.263 107.726 1.00 129.11 ? 1062 ILE A CB  1 
ATOM   8404  C  CG1 . ILE A 1 1491 ? 95.664  127.851 108.522 1.00 117.45 ? 1062 ILE A CG1 1 
ATOM   8405  C  CG2 . ILE A 1 1491 ? 94.815  127.163 106.226 1.00 118.56 ? 1062 ILE A CG2 1 
ATOM   8406  C  CD1 . ILE A 1 1491 ? 96.091  129.288 108.117 1.00 103.37 ? 1062 ILE A CD1 1 
ATOM   8407  N  N   . ASN A 1 1492 ? 91.422  126.488 107.104 1.00 139.73 ? 1063 ASN A N   1 
ATOM   8408  C  CA  . ASN A 1 1492 ? 90.425  125.970 106.162 1.00 144.56 ? 1063 ASN A CA  1 
ATOM   8409  C  C   . ASN A 1 1492 ? 89.047  126.634 106.291 1.00 148.45 ? 1063 ASN A C   1 
ATOM   8410  O  O   . ASN A 1 1492 ? 88.150  126.312 105.498 1.00 144.86 ? 1063 ASN A O   1 
ATOM   8411  C  CB  . ASN A 1 1492 ? 90.277  124.439 106.310 1.00 142.27 ? 1063 ASN A CB  1 
ATOM   8412  C  CG  . ASN A 1 1492 ? 91.586  123.682 106.034 1.00 128.17 ? 1063 ASN A CG  1 
ATOM   8413  O  OD1 . ASN A 1 1492 ? 92.540  124.255 105.500 1.00 122.12 ? 1063 ASN A OD1 1 
ATOM   8414  N  ND2 . ASN A 1 1492 ? 91.593  122.374 106.303 1.00 120.51 ? 1063 ASN A ND2 1 
ATOM   8415  N  N   . ASN A 1 1493 ? 88.853  127.564 107.242 1.00 147.12 ? 1064 ASN A N   1 
ATOM   8416  C  CA  . ASN A 1 1493 ? 87.554  128.224 107.407 1.00 152.50 ? 1064 ASN A CA  1 
ATOM   8417  C  C   . ASN A 1 1493 ? 87.273  129.294 106.344 1.00 157.12 ? 1064 ASN A C   1 
ATOM   8418  O  O   . ASN A 1 1493 ? 86.155  129.823 106.319 1.00 152.39 ? 1064 ASN A O   1 
ATOM   8419  C  CB  . ASN A 1 1493 ? 87.426  128.850 108.814 1.00 147.74 ? 1064 ASN A CB  1 
ATOM   8420  C  CG  . ASN A 1 1493 ? 88.555  129.838 109.147 1.00 142.96 ? 1064 ASN A CG  1 
ATOM   8421  O  OD1 . ASN A 1 1493 ? 89.336  130.230 108.277 1.00 142.00 ? 1064 ASN A OD1 1 
ATOM   8422  N  ND2 . ASN A 1 1493 ? 88.640  130.237 110.421 1.00 130.20 ? 1064 ASN A ND2 1 
ATOM   8423  N  N   . ASN A 1 1494 ? 88.242  129.623 105.475 1.00 156.79 ? 1065 ASN A N   1 
ATOM   8424  C  CA  . ASN A 1 1494 ? 88.053  130.676 104.473 1.00 154.25 ? 1065 ASN A CA  1 
ATOM   8425  C  C   . ASN A 1 1494 ? 86.907  130.328 103.518 1.00 157.25 ? 1065 ASN A C   1 
ATOM   8426  O  O   . ASN A 1 1494 ? 86.688  129.157 103.183 1.00 156.23 ? 1065 ASN A O   1 
ATOM   8427  C  CB  . ASN A 1 1494 ? 89.364  130.928 103.687 1.00 149.35 ? 1065 ASN A CB  1 
ATOM   8428  C  CG  . ASN A 1 1494 ? 90.056  129.628 103.184 1.00 145.67 ? 1065 ASN A CG  1 
ATOM   8429  O  OD1 . ASN A 1 1494 ? 89.491  128.535 103.230 1.00 143.87 ? 1065 ASN A OD1 1 
ATOM   8430  N  ND2 . ASN A 1 1494 ? 91.300  129.769 102.712 1.00 133.88 ? 1065 ASN A ND2 1 
ATOM   8431  N  N   . THR A 1 1495 ? 86.160  131.354 103.083 1.00 154.51 ? 1066 THR A N   1 
ATOM   8432  C  CA  . THR A 1 1495 ? 85.015  131.159 102.188 1.00 157.52 ? 1066 THR A CA  1 
ATOM   8433  C  C   . THR A 1 1495 ? 85.410  131.125 100.705 1.00 154.44 ? 1066 THR A C   1 
ATOM   8434  O  O   . THR A 1 1495 ? 84.531  130.976 99.846  1.00 147.85 ? 1066 THR A O   1 
ATOM   8435  C  CB  . THR A 1 1495 ? 83.936  132.247 102.434 1.00 148.51 ? 1066 THR A CB  1 
ATOM   8436  O  OG1 . THR A 1 1495 ? 82.799  132.021 101.585 1.00 138.89 ? 1066 THR A OG1 1 
ATOM   8437  C  CG2 . THR A 1 1495 ? 84.484  133.667 102.194 1.00 137.85 ? 1066 THR A CG2 1 
ATOM   8438  N  N   . GLU A 1 1496 ? 86.709  131.236 100.393 1.00 152.32 ? 1067 GLU A N   1 
ATOM   8439  C  CA  . GLU A 1 1496 ? 87.230  131.206 99.026  1.00 145.66 ? 1067 GLU A CA  1 
ATOM   8440  C  C   . GLU A 1 1496 ? 87.353  129.748 98.540  1.00 131.89 ? 1067 GLU A C   1 
ATOM   8441  O  O   . GLU A 1 1496 ? 86.795  128.820 99.135  1.00 123.95 ? 1067 GLU A O   1 
ATOM   8442  C  CB  . GLU A 1 1496 ? 88.566  131.962 98.958  1.00 140.31 ? 1067 GLU A CB  1 
ATOM   8443  C  CG  . GLU A 1 1496 ? 88.523  133.440 99.412  1.00 136.45 ? 1067 GLU A CG  1 
ATOM   8444  C  CD  . GLU A 1 1496 ? 89.893  134.119 99.374  1.00 127.42 ? 1067 GLU A CD  1 
ATOM   8445  O  OE1 . GLU A 1 1496 ? 90.019  135.240 99.916  1.00 123.18 ? 1067 GLU A OE1 1 
ATOM   8446  O  OE2 . GLU A 1 1496 ? 90.840  133.534 98.798  1.00 124.76 ? 1067 GLU A OE2 1 
ATOM   8447  N  N   . THR A 1 1497 ? 88.069  129.536 97.426  1.00 127.75 ? 1068 THR A N   1 
ATOM   8448  C  CA  . THR A 1 1497 ? 88.319  128.182 96.926  1.00 113.09 ? 1068 THR A CA  1 
ATOM   8449  C  C   . THR A 1 1497 ? 89.154  127.398 97.942  1.00 93.08  ? 1068 THR A C   1 
ATOM   8450  O  O   . THR A 1 1497 ? 90.049  127.967 98.580  1.00 99.74  ? 1068 THR A O   1 
ATOM   8451  C  CB  . THR A 1 1497 ? 89.033  128.222 95.562  1.00 111.66 ? 1068 THR A CB  1 
ATOM   8452  O  OG1 . THR A 1 1497 ? 90.290  128.908 95.677  1.00 103.84 ? 1068 THR A OG1 1 
ATOM   8453  C  CG2 . THR A 1 1497 ? 88.162  128.930 94.500  1.00 114.93 ? 1068 THR A CG2 1 
ATOM   8454  N  N   . PRO A 1 1498 ? 88.887  126.110 98.135  1.00 70.14  ? 1069 PRO A N   1 
ATOM   8455  C  CA  . PRO A 1 1498 ? 89.531  125.393 99.235  1.00 63.46  ? 1069 PRO A CA  1 
ATOM   8456  C  C   . PRO A 1 1498 ? 91.026  125.319 99.012  1.00 70.77  ? 1069 PRO A C   1 
ATOM   8457  O  O   . PRO A 1 1498 ? 91.521  125.400 97.886  1.00 76.17  ? 1069 PRO A O   1 
ATOM   8458  C  CB  . PRO A 1 1498 ? 88.909  124.000 99.184  1.00 59.29  ? 1069 PRO A CB  1 
ATOM   8459  C  CG  . PRO A 1 1498 ? 88.443  123.868 97.804  1.00 71.96  ? 1069 PRO A CG  1 
ATOM   8460  C  CD  . PRO A 1 1498 ? 88.020  125.229 97.348  1.00 76.14  ? 1069 PRO A CD  1 
ATOM   8461  N  N   . VAL A 1 1499 ? 91.746  125.158 100.119 1.00 66.59  ? 1070 VAL A N   1 
ATOM   8462  C  CA  . VAL A 1 1499 ? 93.200  125.151 100.057 1.00 61.95  ? 1070 VAL A CA  1 
ATOM   8463  C  C   . VAL A 1 1499 ? 93.683  124.046 99.138  1.00 54.45  ? 1070 VAL A C   1 
ATOM   8464  O  O   . VAL A 1 1499 ? 94.634  124.229 98.371  1.00 59.31  ? 1070 VAL A O   1 
ATOM   8465  C  CB  . VAL A 1 1499 ? 93.789  125.007 101.471 1.00 79.96  ? 1070 VAL A CB  1 
ATOM   8466  C  CG1 . VAL A 1 1499 ? 95.309  125.133 101.432 1.00 86.15  ? 1070 VAL A CG1 1 
ATOM   8467  C  CG2 . VAL A 1 1499 ? 93.180  126.056 102.405 1.00 96.37  ? 1070 VAL A CG2 1 
ATOM   8468  N  N   . LEU A 1 1500 ? 93.031  122.891 99.185  1.00 56.65  ? 1071 LEU A N   1 
ATOM   8469  C  CA  . LEU A 1 1500 ? 93.543  121.758 98.433  1.00 54.90  ? 1071 LEU A CA  1 
ATOM   8470  C  C   . LEU A 1 1500 ? 93.504  122.035 96.935  1.00 51.06  ? 1071 LEU A C   1 
ATOM   8471  O  O   . LEU A 1 1500 ? 94.436  121.671 96.207  1.00 57.42  ? 1071 LEU A O   1 
ATOM   8472  C  CB  . LEU A 1 1500 ? 92.758  120.496 98.772  1.00 48.59  ? 1071 LEU A CB  1 
ATOM   8473  C  CG  . LEU A 1 1500 ? 93.437  119.269 98.182  1.00 49.97  ? 1071 LEU A CG  1 
ATOM   8474  C  CD1 . LEU A 1 1500 ? 94.830  119.179 98.788  1.00 48.61  ? 1071 LEU A CD1 1 
ATOM   8475  C  CD2 . LEU A 1 1500 ? 92.637  117.998 98.440  1.00 58.23  ? 1071 LEU A CD2 1 
ATOM   8476  N  N   . ASP A 1 1501 ? 92.447  122.680 96.448  1.00 43.99  ? 1072 ASP A N   1 
ATOM   8477  C  CA  . ASP A 1 1501 ? 92.382  122.910 95.011  1.00 45.09  ? 1072 ASP A CA  1 
ATOM   8478  C  C   . ASP A 1 1501 ? 93.398  123.943 94.579  1.00 44.42  ? 1072 ASP A C   1 
ATOM   8479  O  O   . ASP A 1 1501 ? 94.018  123.816 93.514  1.00 53.51  ? 1072 ASP A O   1 
ATOM   8480  C  CB  . ASP A 1 1501 ? 90.972  123.310 94.596  1.00 58.02  ? 1072 ASP A CB  1 
ATOM   8481  C  CG  . ASP A 1 1501 ? 90.009  122.114 94.599  1.00 75.92  ? 1072 ASP A CG  1 
ATOM   8482  O  OD1 . ASP A 1 1501 ? 90.124  121.249 93.695  1.00 70.23  ? 1072 ASP A OD1 1 
ATOM   8483  O  OD2 . ASP A 1 1501 ? 89.145  122.020 95.501  1.00 68.58  ? 1072 ASP A OD2 1 
ATOM   8484  N  N   . ARG A 1 1502 ? 93.603  124.960 95.397  1.00 47.69  ? 1073 ARG A N   1 
ATOM   8485  C  CA  . ARG A 1 1502 ? 94.622  125.935 95.063  1.00 51.90  ? 1073 ARG A CA  1 
ATOM   8486  C  C   . ARG A 1 1502 ? 95.980  125.277 95.027  1.00 46.92  ? 1073 ARG A C   1 
ATOM   8487  O  O   . ARG A 1 1502 ? 96.809  125.575 94.160  1.00 54.83  ? 1073 ARG A O   1 
ATOM   8488  C  CB  . ARG A 1 1502 ? 94.604  127.067 96.077  1.00 63.73  ? 1073 ARG A CB  1 
ATOM   8489  C  CG  . ARG A 1 1502 ? 94.983  128.392 95.474  1.00 75.88  ? 1073 ARG A CG  1 
ATOM   8490  C  CD  . ARG A 1 1502 ? 95.169  129.424 96.561  1.00 80.20  ? 1073 ARG A CD  1 
ATOM   8491  N  NE  . ARG A 1 1502 ? 94.376  129.090 97.742  1.00 74.62  ? 1073 ARG A NE  1 
ATOM   8492  C  CZ  . ARG A 1 1502 ? 93.134  129.515 97.937  1.00 86.28  ? 1073 ARG A CZ  1 
ATOM   8493  N  NH1 . ARG A 1 1502 ? 92.543  130.279 97.023  1.00 90.44  ? 1073 ARG A NH1 1 
ATOM   8494  N  NH2 . ARG A 1 1502 ? 92.477  129.170 99.035  1.00 96.28  ? 1073 ARG A NH2 1 
ATOM   8495  N  N   . LEU A 1 1503 ? 96.219  124.377 95.969  1.00 46.84  ? 1074 LEU A N   1 
ATOM   8496  C  CA  . LEU A 1 1503 ? 97.491  123.682 96.011  1.00 46.64  ? 1074 LEU A CA  1 
ATOM   8497  C  C   . LEU A 1 1503 ? 97.670  122.836 94.762  1.00 39.22  ? 1074 LEU A C   1 
ATOM   8498  O  O   . LEU A 1 1503 ? 98.773  122.751 94.216  1.00 48.38  ? 1074 LEU A O   1 
ATOM   8499  C  CB  . LEU A 1 1503 ? 97.571  122.829 97.285  1.00 53.31  ? 1074 LEU A CB  1 
ATOM   8500  C  CG  . LEU A 1 1503 ? 97.866  123.567 98.598  1.00 48.69  ? 1074 LEU A CG  1 
ATOM   8501  C  CD1 . LEU A 1 1503 ? 97.453  122.728 99.792  1.00 54.85  ? 1074 LEU A CD1 1 
ATOM   8502  C  CD2 . LEU A 1 1503 ? 99.342  123.927 98.699  1.00 56.45  ? 1074 LEU A CD2 1 
ATOM   8503  N  N   . ARG A 1 1504 ? 96.608  122.194 94.296  1.00 33.61  ? 1075 ARG A N   1 
ATOM   8504  C  CA  . ARG A 1 1504 ? 96.775  121.382 93.103  1.00 32.43  ? 1075 ARG A CA  1 
ATOM   8505  C  C   . ARG A 1 1504 ? 97.120  122.256 91.914  1.00 38.54  ? 1075 ARG A C   1 
ATOM   8506  O  O   . ARG A 1 1504 ? 97.977  121.904 91.094  1.00 47.85  ? 1075 ARG A O   1 
ATOM   8507  C  CB  . ARG A 1 1504 ? 95.521  120.573 92.829  1.00 37.59  ? 1075 ARG A CB  1 
ATOM   8508  C  CG  . ARG A 1 1504 ? 95.279  119.566 93.898  1.00 44.11  ? 1075 ARG A CG  1 
ATOM   8509  C  CD  . ARG A 1 1504 ? 94.091  118.742 93.583  1.00 39.80  ? 1075 ARG A CD  1 
ATOM   8510  N  NE  . ARG A 1 1504 ? 93.840  117.823 94.668  1.00 35.42  ? 1075 ARG A NE  1 
ATOM   8511  C  CZ  . ARG A 1 1504 ? 92.902  116.896 94.625  1.00 41.84  ? 1075 ARG A CZ  1 
ATOM   8512  N  NH1 . ARG A 1 1504 ? 92.164  116.762 93.531  1.00 42.57  ? 1075 ARG A NH1 1 
ATOM   8513  N  NH2 . ARG A 1 1504 ? 92.722  116.087 95.660  1.00 49.26  ? 1075 ARG A NH2 1 
ATOM   8514  N  N   . LYS A 1 1505 ? 96.468  123.408 91.809  1.00 40.25  ? 1076 LYS A N   1 
ATOM   8515  C  CA  . LYS A 1 1505 ? 96.780  124.312 90.714  1.00 35.59  ? 1076 LYS A CA  1 
ATOM   8516  C  C   . LYS A 1 1505 ? 98.234  124.731 90.769  1.00 36.41  ? 1076 LYS A C   1 
ATOM   8517  O  O   . LYS A 1 1505 ? 98.934  124.725 89.753  1.00 45.19  ? 1076 LYS A O   1 
ATOM   8518  C  CB  . LYS A 1 1505 ? 95.877  125.532 90.785  1.00 46.31  ? 1076 LYS A CB  1 
ATOM   8519  C  CG  . LYS A 1 1505 ? 94.590  125.379 90.017  1.00 56.46  ? 1076 LYS A CG  1 
ATOM   8520  C  CD  . LYS A 1 1505 ? 93.733  126.613 90.217  1.00 66.15  ? 1076 LYS A CD  1 
ATOM   8521  C  CE  . LYS A 1 1505 ? 94.566  127.870 90.018  1.00 68.81  ? 1076 LYS A CE  1 
ATOM   8522  N  NZ  . LYS A 1 1505 ? 95.175  127.892 88.654  1.00 68.35  ? 1076 LYS A NZ  1 
ATOM   8523  N  N   . ILE A 1 1506 ? 98.702  125.107 91.956  1.00 39.24  ? 1077 ILE A N   1 
ATOM   8524  C  CA  . ILE A 1 1506 ? 100.074 125.577 92.098  1.00 32.93  ? 1077 ILE A CA  1 
ATOM   8525  C  C   . ILE A 1 1506 ? 101.041 124.464 91.740  1.00 39.31  ? 1077 ILE A C   1 
ATOM   8526  O  O   . ILE A 1 1506 ? 102.042 124.695 91.055  1.00 46.38  ? 1077 ILE A O   1 
ATOM   8527  C  CB  . ILE A 1 1506 ? 100.321 126.078 93.528  1.00 35.74  ? 1077 ILE A CB  1 
ATOM   8528  C  CG1 . ILE A 1 1506 ? 99.487  127.315 93.824  1.00 47.07  ? 1077 ILE A CG1 1 
ATOM   8529  C  CG2 . ILE A 1 1506 ? 101.776 126.442 93.705  1.00 43.64  ? 1077 ILE A CG2 1 
ATOM   8530  C  CD1 . ILE A 1 1506 ? 99.630  127.760 95.268  1.00 55.18  ? 1077 ILE A CD1 1 
ATOM   8531  N  N   . THR A 1 1507 ? 100.769 123.239 92.211  1.00 40.12  ? 1078 THR A N   1 
ATOM   8532  C  CA  . THR A 1 1507 ? 101.633 122.107 91.894  1.00 30.21  ? 1078 THR A CA  1 
ATOM   8533  C  C   . THR A 1 1507 ? 101.725 121.919 90.406  1.00 29.62  ? 1078 THR A C   1 
ATOM   8534  O  O   . THR A 1 1507 ? 102.812 121.749 89.854  1.00 38.62  ? 1078 THR A O   1 
ATOM   8535  C  CB  . THR A 1 1507 ? 101.101 120.820 92.516  1.00 32.54  ? 1078 THR A CB  1 
ATOM   8536  O  OG1 . THR A 1 1507 ? 100.970 120.971 93.937  1.00 43.09  ? 1078 THR A OG1 1 
ATOM   8537  C  CG2 . THR A 1 1507 ? 102.032 119.661 92.197  1.00 47.17  ? 1078 THR A CG2 1 
ATOM   8538  N  N   . LEU A 1 1508 ? 100.602 121.980 89.739  1.00 32.48  ? 1079 LEU A N   1 
ATOM   8539  C  CA  . LEU A 1 1508 ? 100.618 121.642 88.340  1.00 30.20  ? 1079 LEU A CA  1 
ATOM   8540  C  C   . LEU A 1 1508 ? 101.311 122.739 87.556  1.00 32.16  ? 1079 LEU A C   1 
ATOM   8541  O  O   . LEU A 1 1508 ? 102.066 122.455 86.624  1.00 42.00  ? 1079 LEU A O   1 
ATOM   8542  C  CB  . LEU A 1 1508 ? 99.187  121.436 87.901  1.00 38.90  ? 1079 LEU A CB  1 
ATOM   8543  C  CG  . LEU A 1 1508 ? 98.965  120.540 86.722  1.00 51.88  ? 1079 LEU A CG  1 
ATOM   8544  C  CD1 . LEU A 1 1508 ? 99.289  119.161 87.263  1.00 51.67  ? 1079 LEU A CD1 1 
ATOM   8545  C  CD2 . LEU A 1 1508 ? 97.496  120.632 86.345  1.00 64.20  ? 1079 LEU A CD2 1 
ATOM   8546  N  N   . GLN A 1 1509 ? 101.108 124.001 87.948  1.00 32.22  ? 1080 GLN A N   1 
ATOM   8547  C  CA  . GLN A 1 1509 ? 101.836 125.098 87.311  1.00 30.76  ? 1080 GLN A CA  1 
ATOM   8548  C  C   . GLN A 1 1509 ? 103.334 124.964 87.531  1.00 39.98  ? 1080 GLN A C   1 
ATOM   8549  O  O   . GLN A 1 1509 ? 104.126 125.159 86.605  1.00 48.35  ? 1080 GLN A O   1 
ATOM   8550  C  CB  . GLN A 1 1509 ? 101.379 126.453 87.847  1.00 41.97  ? 1080 GLN A CB  1 
ATOM   8551  C  CG  . GLN A 1 1509 ? 99.968  126.854 87.505  1.00 61.55  ? 1080 GLN A CG  1 
ATOM   8552  C  CD  . GLN A 1 1509 ? 99.589  128.208 88.119  1.00 72.66  ? 1080 GLN A CD  1 
ATOM   8553  O  OE1 . GLN A 1 1509 ? 100.381 128.819 88.845  1.00 67.62  ? 1080 GLN A OE1 1 
ATOM   8554  N  NE2 . GLN A 1 1509 ? 98.384  128.693 87.799  1.00 73.58  ? 1080 GLN A NE2 1 
ATOM   8555  N  N   . ARG A 1 1510 ? 103.746 124.688 88.765  1.00 30.45  ? 1081 ARG A N   1 
ATOM   8556  C  CA  . ARG A 1 1510 ? 105.158 124.534 89.050  1.00 20.48  ? 1081 ARG A CA  1 
ATOM   8557  C  C   . ARG A 1 1510 ? 105.748 123.410 88.230  1.00 26.12  ? 1081 ARG A C   1 
ATOM   8558  O  O   . ARG A 1 1510 ? 106.852 123.533 87.689  1.00 35.17  ? 1081 ARG A O   1 
ATOM   8559  C  CB  . ARG A 1 1510 ? 105.341 124.252 90.528  1.00 26.86  ? 1081 ARG A CB  1 
ATOM   8560  C  CG  . ARG A 1 1510 ? 105.130 125.475 91.356  1.00 40.26  ? 1081 ARG A CG  1 
ATOM   8561  C  CD  . ARG A 1 1510 ? 105.026 125.137 92.829  1.00 42.00  ? 1081 ARG A CD  1 
ATOM   8562  N  NE  . ARG A 1 1510 ? 106.314 124.749 93.353  1.00 36.84  ? 1081 ARG A NE  1 
ATOM   8563  C  CZ  . ARG A 1 1510 ? 107.211 125.631 93.750  1.00 43.69  ? 1081 ARG A CZ  1 
ATOM   8564  N  NH1 . ARG A 1 1510 ? 106.950 126.927 93.606  1.00 45.73  ? 1081 ARG A NH1 1 
ATOM   8565  N  NH2 . ARG A 1 1510 ? 108.385 125.225 94.226  1.00 48.69  ? 1081 ARG A NH2 1 
ATOM   8566  N  N   . TRP A 1 1511 ? 105.054 122.288 88.158  1.00 25.19  ? 1082 TRP A N   1 
ATOM   8567  C  CA  . TRP A 1 1511 ? 105.563 121.209 87.337  1.00 23.97  ? 1082 TRP A CA  1 
ATOM   8568  C  C   . TRP A 1 1511 ? 105.689 121.669 85.903  1.00 30.38  ? 1082 TRP A C   1 
ATOM   8569  O  O   . TRP A 1 1511 ? 106.676 121.353 85.224  1.00 42.71  ? 1082 TRP A O   1 
ATOM   8570  C  CB  . TRP A 1 1511 ? 104.670 119.977 87.458  1.00 30.86  ? 1082 TRP A CB  1 
ATOM   8571  C  CG  . TRP A 1 1511 ? 105.020 119.123 88.661  1.00 36.64  ? 1082 TRP A CG  1 
ATOM   8572  C  CD1 . TRP A 1 1511 ? 104.774 119.391 89.991  1.00 34.44  ? 1082 TRP A CD1 1 
ATOM   8573  C  CD2 . TRP A 1 1511 ? 105.700 117.872 88.628  1.00 31.18  ? 1082 TRP A CD2 1 
ATOM   8574  N  NE1 . TRP A 1 1511 ? 105.254 118.370 90.772  1.00 30.44  ? 1082 TRP A NE1 1 
ATOM   8575  C  CE2 . TRP A 1 1511 ? 105.831 117.430 89.956  1.00 29.16  ? 1082 TRP A CE2 1 
ATOM   8576  C  CE3 . TRP A 1 1511 ? 106.213 117.079 87.594  1.00 32.92  ? 1082 TRP A CE3 1 
ATOM   8577  C  CZ2 . TRP A 1 1511 ? 106.458 116.234 90.274  1.00 37.79  ? 1082 TRP A CZ2 1 
ATOM   8578  C  CZ3 . TRP A 1 1511 ? 106.830 115.895 87.906  1.00 32.70  ? 1082 TRP A CZ3 1 
ATOM   8579  C  CH2 . TRP A 1 1511 ? 106.950 115.478 89.232  1.00 36.45  ? 1082 TRP A CH2 1 
ATOM   8580  N  N   . SER A 1 1512 ? 104.731 122.464 85.441  1.00 26.73  ? 1083 SER A N   1 
ATOM   8581  C  CA  . SER A 1 1512 ? 104.822 122.995 84.094  1.00 25.57  ? 1083 SER A CA  1 
ATOM   8582  C  C   . SER A 1 1512 ? 106.074 123.828 83.919  1.00 30.09  ? 1083 SER A C   1 
ATOM   8583  O  O   . SER A 1 1512 ? 106.760 123.732 82.898  1.00 38.91  ? 1083 SER A O   1 
ATOM   8584  C  CB  . SER A 1 1512 ? 103.604 123.849 83.787  1.00 41.32  ? 1083 SER A CB  1 
ATOM   8585  O  OG  . SER A 1 1512 ? 103.753 124.459 82.518  1.00 52.20  ? 1083 SER A OG  1 
ATOM   8586  N  N   . LEU A 1 1513 ? 106.378 124.659 84.902  1.00 30.49  ? 1084 LEU A N   1 
ATOM   8587  C  CA  . LEU A 1 1513 ? 107.513 125.564 84.782  1.00 30.03  ? 1084 LEU A CA  1 
ATOM   8588  C  C   . LEU A 1 1513 ? 108.809 124.780 84.717  1.00 30.21  ? 1084 LEU A C   1 
ATOM   8589  O  O   . LEU A 1 1513 ? 109.636 124.987 83.821  1.00 35.20  ? 1084 LEU A O   1 
ATOM   8590  C  CB  . LEU A 1 1513 ? 107.538 126.520 85.973  1.00 33.33  ? 1084 LEU A CB  1 
ATOM   8591  C  CG  . LEU A 1 1513 ? 106.351 127.482 85.998  1.00 45.16  ? 1084 LEU A CG  1 
ATOM   8592  C  CD1 . LEU A 1 1513 ? 106.266 128.249 87.327  1.00 44.36  ? 1084 LEU A CD1 1 
ATOM   8593  C  CD2 . LEU A 1 1513 ? 106.397 128.426 84.788  1.00 57.52  ? 1084 LEU A CD2 1 
ATOM   8594  N  N   . TRP A 1 1514 ? 108.973 123.840 85.648  1.00 29.73  ? 1085 TRP A N   1 
ATOM   8595  C  CA  . TRP A 1 1514 ? 110.221 123.099 85.785  1.00 26.39  ? 1085 TRP A CA  1 
ATOM   8596  C  C   . TRP A 1 1514 ? 110.485 122.222 84.575  1.00 32.47  ? 1085 TRP A C   1 
ATOM   8597  O  O   . TRP A 1 1514 ? 111.614 122.145 84.078  1.00 32.67  ? 1085 TRP A O   1 
ATOM   8598  C  CB  . TRP A 1 1514 ? 110.151 122.207 87.000  1.00 25.89  ? 1085 TRP A CB  1 
ATOM   8599  C  CG  . TRP A 1 1514 ? 110.123 122.949 88.147  1.00 16.26  ? 1085 TRP A CG  1 
ATOM   8600  C  CD1 . TRP A 1 1514 ? 110.603 124.160 88.303  1.00 22.39  ? 1085 TRP A CD1 1 
ATOM   8601  C  CD2 . TRP A 1 1514 ? 109.590 122.546 89.353  1.00 8.57   ? 1085 TRP A CD2 1 
ATOM   8602  N  NE1 . TRP A 1 1514 ? 110.398 124.569 89.568  1.00 27.64  ? 1085 TRP A NE1 1 
ATOM   8603  C  CE2 . TRP A 1 1514 ? 109.767 123.566 90.232  1.00 13.73  ? 1085 TRP A CE2 1 
ATOM   8604  C  CE3 . TRP A 1 1514 ? 108.976 121.404 89.772  1.00 19.22  ? 1085 TRP A CE3 1 
ATOM   8605  C  CZ2 . TRP A 1 1514 ? 109.360 123.501 91.511  1.00 31.36  ? 1085 TRP A CZ2 1 
ATOM   8606  C  CZ3 . TRP A 1 1514 ? 108.559 121.323 91.037  1.00 26.99  ? 1085 TRP A CZ3 1 
ATOM   8607  C  CH2 . TRP A 1 1514 ? 108.748 122.363 91.905  1.00 34.24  ? 1085 TRP A CH2 1 
ATOM   8608  N  N   . PHE A 1 1515 ? 109.470 121.506 84.124  1.00 27.25  ? 1086 PHE A N   1 
ATOM   8609  C  CA  . PHE A 1 1515 ? 109.722 120.459 83.173  1.00 22.93  ? 1086 PHE A CA  1 
ATOM   8610  C  C   . PHE A 1 1515 ? 109.315 120.809 81.762  1.00 40.77  ? 1086 PHE A C   1 
ATOM   8611  O  O   . PHE A 1 1515 ? 109.342 119.929 80.901  1.00 55.29  ? 1086 PHE A O   1 
ATOM   8612  C  CB  . PHE A 1 1515 ? 109.036 119.189 83.626  1.00 34.38  ? 1086 PHE A CB  1 
ATOM   8613  C  CG  . PHE A 1 1515 ? 109.538 118.700 84.929  1.00 37.37  ? 1086 PHE A CG  1 
ATOM   8614  C  CD1 . PHE A 1 1515 ? 110.659 117.890 84.979  1.00 41.79  ? 1086 PHE A CD1 1 
ATOM   8615  C  CD2 . PHE A 1 1515 ? 108.897 119.013 86.096  1.00 36.33  ? 1086 PHE A CD2 1 
ATOM   8616  C  CE1 . PHE A 1 1515 ? 111.156 117.424 86.170  1.00 33.76  ? 1086 PHE A CE1 1 
ATOM   8617  C  CE2 . PHE A 1 1515 ? 109.384 118.541 87.300  1.00 38.98  ? 1086 PHE A CE2 1 
ATOM   8618  C  CZ  . PHE A 1 1515 ? 110.518 117.744 87.332  1.00 37.07  ? 1086 PHE A CZ  1 
ATOM   8619  N  N   . SER A 1 1516 ? 108.968 122.058 81.479  1.00 38.45  ? 1087 SER A N   1 
ATOM   8620  C  CA  . SER A 1 1516 ? 108.826 122.511 80.094  1.00 35.83  ? 1087 SER A CA  1 
ATOM   8621  C  C   . SER A 1 1516 ? 109.617 123.798 79.989  1.00 39.16  ? 1087 SER A C   1 
ATOM   8622  O  O   . SER A 1 1516 ? 109.145 124.854 80.409  1.00 48.01  ? 1087 SER A O   1 
ATOM   8623  C  CB  . SER A 1 1516 ? 107.379 122.735 79.710  1.00 45.29  ? 1087 SER A CB  1 
ATOM   8624  O  OG  . SER A 1 1516 ? 106.617 121.583 79.990  1.00 53.00  ? 1087 SER A OG  1 
ATOM   8625  N  N   . TYR A 1 1517 ? 110.822 123.720 79.458  1.00 42.44  ? 1088 TYR A N   1 
ATOM   8626  C  CA  . TYR A 1 1517 ? 111.617 124.930 79.393  1.00 54.83  ? 1088 TYR A CA  1 
ATOM   8627  C  C   . TYR A 1 1517 ? 111.471 125.668 78.063  1.00 63.23  ? 1088 TYR A C   1 
ATOM   8628  O  O   . TYR A 1 1517 ? 111.669 126.888 78.025  1.00 66.89  ? 1088 TYR A O   1 
ATOM   8629  C  CB  . TYR A 1 1517 ? 113.095 124.615 79.649  1.00 59.60  ? 1088 TYR A CB  1 
ATOM   8630  C  CG  . TYR A 1 1517 ? 113.760 123.927 78.483  1.00 68.17  ? 1088 TYR A CG  1 
ATOM   8631  C  CD1 . TYR A 1 1517 ? 113.597 122.564 78.276  1.00 76.32  ? 1088 TYR A CD1 1 
ATOM   8632  C  CD2 . TYR A 1 1517 ? 114.536 124.646 77.568  1.00 64.65  ? 1088 TYR A CD2 1 
ATOM   8633  C  CE1 . TYR A 1 1517 ? 114.196 121.923 77.191  1.00 83.14  ? 1088 TYR A CE1 1 
ATOM   8634  C  CE2 . TYR A 1 1517 ? 115.140 124.018 76.488  1.00 66.29  ? 1088 TYR A CE2 1 
ATOM   8635  C  CZ  . TYR A 1 1517 ? 114.966 122.656 76.302  1.00 72.71  ? 1088 TYR A CZ  1 
ATOM   8636  O  OH  . TYR A 1 1517 ? 115.561 122.023 75.231  1.00 68.88  ? 1088 TYR A OH  1 
ATOM   8637  N  N   . LEU A 1 1518 ? 111.138 124.979 76.968  1.00 57.89  ? 1089 LEU A N   1 
ATOM   8638  C  CA  . LEU A 1 1518 ? 110.949 125.684 75.702  1.00 54.33  ? 1089 LEU A CA  1 
ATOM   8639  C  C   . LEU A 1 1518 ? 109.752 126.606 75.775  1.00 51.99  ? 1089 LEU A C   1 
ATOM   8640  O  O   . LEU A 1 1518 ? 109.764 127.704 75.210  1.00 56.32  ? 1089 LEU A O   1 
ATOM   8641  C  CB  . LEU A 1 1518 ? 110.774 124.693 74.561  1.00 61.79  ? 1089 LEU A CB  1 
ATOM   8642  C  CG  . LEU A 1 1518 ? 112.080 123.973 74.217  1.00 77.29  ? 1089 LEU A CG  1 
ATOM   8643  C  CD1 . LEU A 1 1518 ? 111.859 122.912 73.134  1.00 83.97  ? 1089 LEU A CD1 1 
ATOM   8644  C  CD2 . LEU A 1 1518 ? 113.176 124.974 73.819  1.00 72.65  ? 1089 LEU A CD2 1 
ATOM   8645  N  N   . ASP A 1 1519 ? 108.706 126.168 76.463  1.00 56.27  ? 1090 ASP A N   1 
ATOM   8646  C  CA  . ASP A 1 1519 ? 107.516 126.988 76.566  1.00 56.13  ? 1090 ASP A CA  1 
ATOM   8647  C  C   . ASP A 1 1519 ? 107.839 128.282 77.265  1.00 49.92  ? 1090 ASP A C   1 
ATOM   8648  O  O   . ASP A 1 1519 ? 107.722 129.366 76.689  1.00 62.80  ? 1090 ASP A O   1 
ATOM   8649  C  CB  . ASP A 1 1519 ? 106.425 126.225 77.314  1.00 63.58  ? 1090 ASP A CB  1 
ATOM   8650  C  CG  . ASP A 1 1519 ? 105.665 125.253 76.400  1.00 85.94  ? 1090 ASP A CG  1 
ATOM   8651  O  OD1 . ASP A 1 1519 ? 105.926 125.259 75.170  1.00 83.81  ? 1090 ASP A OD1 1 
ATOM   8652  O  OD2 . ASP A 1 1519 ? 104.822 124.472 76.906  1.00 81.61  ? 1090 ASP A OD2 1 
ATOM   8653  N  N   . HIS A 1 1520 ? 108.306 128.188 78.489  1.00 50.43  ? 1091 HIS A N   1 
ATOM   8654  C  CA  . HIS A 1 1520 ? 108.519 129.387 79.277  1.00 62.25  ? 1091 HIS A CA  1 
ATOM   8655  C  C   . HIS A 1 1520 ? 109.903 129.907 78.936  1.00 64.12  ? 1091 HIS A C   1 
ATOM   8656  O  O   . HIS A 1 1520 ? 110.869 129.773 79.694  1.00 68.47  ? 1091 HIS A O   1 
ATOM   8657  C  CB  . HIS A 1 1520 ? 108.357 129.075 80.756  1.00 64.39  ? 1091 HIS A CB  1 
ATOM   8658  C  CG  . HIS A 1 1520 ? 107.082 128.366 81.054  1.00 55.40  ? 1091 HIS A CG  1 
ATOM   8659  N  ND1 . HIS A 1 1520 ? 106.987 126.991 81.075  1.00 55.61  ? 1091 HIS A ND1 1 
ATOM   8660  C  CD2 . HIS A 1 1520 ? 105.831 128.836 81.263  1.00 58.22  ? 1091 HIS A CD2 1 
ATOM   8661  C  CE1 . HIS A 1 1520 ? 105.737 126.645 81.325  1.00 60.04  ? 1091 HIS A CE1 1 
ATOM   8662  N  NE2 . HIS A 1 1520 ? 105.015 127.746 81.443  1.00 62.95  ? 1091 HIS A NE2 1 
ATOM   8663  N  N   . CYS A 1 1521 ? 110.013 130.497 77.764  1.00 48.70  ? 1092 CYS A N   1 
ATOM   8664  C  CA  . CYS A 1 1521 ? 111.270 131.139 77.472  1.00 46.31  ? 1092 CYS A CA  1 
ATOM   8665  C  C   . CYS A 1 1521 ? 110.963 132.508 76.917  1.00 52.15  ? 1092 CYS A C   1 
ATOM   8666  O  O   . CYS A 1 1521 ? 109.934 132.703 76.272  1.00 64.21  ? 1092 CYS A O   1 
ATOM   8667  C  CB  . CYS A 1 1521 ? 112.095 130.307 76.510  1.00 50.43  ? 1092 CYS A CB  1 
ATOM   8668  S  SG  . CYS A 1 1521 ? 113.614 131.094 76.023  1.00 65.51  ? 1092 CYS A SG  1 
ATOM   8669  N  N   . ASP A 1 1522 ? 111.839 133.463 77.196  1.00 55.71  ? 1093 ASP A N   1 
ATOM   8670  C  CA  . ASP A 1 1522 ? 111.717 134.805 76.643  1.00 55.50  ? 1093 ASP A CA  1 
ATOM   8671  C  C   . ASP A 1 1522 ? 112.809 135.001 75.606  1.00 54.32  ? 1093 ASP A C   1 
ATOM   8672  O  O   . ASP A 1 1522 ? 113.993 134.839 75.916  1.00 59.70  ? 1093 ASP A O   1 
ATOM   8673  C  CB  . ASP A 1 1522 ? 111.854 135.866 77.723  1.00 57.16  ? 1093 ASP A CB  1 
ATOM   8674  C  CG  . ASP A 1 1522 ? 111.843 137.262 77.146  1.00 69.71  ? 1093 ASP A CG  1 
ATOM   8675  O  OD1 . ASP A 1 1522 ? 112.815 137.655 76.463  1.00 63.36  ? 1093 ASP A OD1 1 
ATOM   8676  O  OD2 . ASP A 1 1522 ? 110.847 137.981 77.383  1.00 77.69  ? 1093 ASP A OD2 1 
ATOM   8677  N  N   . ASN A 1 1523 ? 112.422 135.374 74.394  1.00 50.62  ? 1094 ASN A N   1 
ATOM   8678  C  CA  . ASN A 1 1523 ? 113.431 135.587 73.366  1.00 55.59  ? 1094 ASN A CA  1 
ATOM   8679  C  C   . ASN A 1 1523 ? 114.155 136.925 73.489  1.00 63.84  ? 1094 ASN A C   1 
ATOM   8680  O  O   . ASN A 1 1523 ? 115.325 137.029 73.097  1.00 65.41  ? 1094 ASN A O   1 
ATOM   8681  C  CB  . ASN A 1 1523 ? 112.810 135.487 71.985  1.00 69.63  ? 1094 ASN A CB  1 
ATOM   8682  C  CG  . ASN A 1 1523 ? 113.853 135.276 70.914  1.00 83.14  ? 1094 ASN A CG  1 
ATOM   8683  O  OD1 . ASN A 1 1523 ? 114.980 134.859 71.205  1.00 75.64  ? 1094 ASN A OD1 1 
ATOM   8684  N  ND2 . ASN A 1 1523 ? 113.499 135.583 69.668  1.00 86.61  ? 1094 ASN A ND2 1 
ATOM   8685  N  N   . ILE A 1 1524 ? 113.489 137.961 73.986  1.00 60.74  ? 1095 ILE A N   1 
ATOM   8686  C  CA  . ILE A 1 1524 ? 114.155 139.250 74.121  1.00 58.22  ? 1095 ILE A CA  1 
ATOM   8687  C  C   . ILE A 1 1524 ? 115.388 139.099 74.999  1.00 59.31  ? 1095 ILE A C   1 
ATOM   8688  O  O   . ILE A 1 1524 ? 116.517 139.387 74.584  1.00 55.43  ? 1095 ILE A O   1 
ATOM   8689  C  CB  . ILE A 1 1524 ? 113.173 140.289 74.698  1.00 70.98  ? 1095 ILE A CB  1 
ATOM   8690  C  CG1 . ILE A 1 1524 ? 112.006 140.540 73.731  1.00 78.17  ? 1095 ILE A CG1 1 
ATOM   8691  C  CG2 . ILE A 1 1524 ? 113.878 141.600 75.041  1.00 74.56  ? 1095 ILE A CG2 1 
ATOM   8692  C  CD1 . ILE A 1 1524 ? 110.803 139.608 73.913  1.00 73.14  ? 1095 ILE A CD1 1 
ATOM   8693  N  N   . LEU A 1 1525 ? 115.182 138.572 76.209  1.00 66.00  ? 1096 LEU A N   1 
ATOM   8694  C  CA  . LEU A 1 1525 ? 116.271 138.361 77.151  1.00 53.72  ? 1096 LEU A CA  1 
ATOM   8695  C  C   . LEU A 1 1525 ? 117.312 137.452 76.553  1.00 42.93  ? 1096 LEU A C   1 
ATOM   8696  O  O   . LEU A 1 1525 ? 118.510 137.652 76.757  1.00 56.43  ? 1096 LEU A O   1 
ATOM   8697  C  CB  . LEU A 1 1525 ? 115.733 137.751 78.444  1.00 55.75  ? 1096 LEU A CB  1 
ATOM   8698  C  CG  . LEU A 1 1525 ? 116.779 137.538 79.533  1.00 64.67  ? 1096 LEU A CG  1 
ATOM   8699  C  CD1 . LEU A 1 1525 ? 117.487 138.867 79.826  1.00 68.41  ? 1096 LEU A CD1 1 
ATOM   8700  C  CD2 . LEU A 1 1525 ? 116.185 136.907 80.814  1.00 64.68  ? 1096 LEU A CD2 1 
ATOM   8701  N  N   . ALA A 1 1526 ? 116.871 136.446 75.814  1.00 46.94  ? 1097 ALA A N   1 
ATOM   8702  C  CA  . ALA A 1 1526 ? 117.819 135.556 75.172  1.00 51.14  ? 1097 ALA A CA  1 
ATOM   8703  C  C   . ALA A 1 1526 ? 118.693 136.323 74.205  1.00 54.35  ? 1097 ALA A C   1 
ATOM   8704  O  O   . ALA A 1 1526 ? 119.868 135.989 74.026  1.00 62.73  ? 1097 ALA A O   1 
ATOM   8705  C  CB  . ALA A 1 1526 ? 117.091 134.424 74.456  1.00 59.11  ? 1097 ALA A CB  1 
ATOM   8706  N  N   . GLU A 1 1527 ? 118.150 137.362 73.579  1.00 51.51  ? 1098 GLU A N   1 
ATOM   8707  C  CA  . GLU A 1 1527 ? 118.992 138.194 72.726  1.00 59.54  ? 1098 GLU A CA  1 
ATOM   8708  C  C   . GLU A 1 1527 ? 119.891 139.101 73.549  1.00 50.89  ? 1098 GLU A C   1 
ATOM   8709  O  O   . GLU A 1 1527 ? 121.063 139.298 73.214  1.00 54.52  ? 1098 GLU A O   1 
ATOM   8710  C  CB  . GLU A 1 1527 ? 118.127 139.011 71.770  1.00 77.61  ? 1098 GLU A CB  1 
ATOM   8711  C  CG  . GLU A 1 1527 ? 117.348 138.161 70.750  1.00 89.14  ? 1098 GLU A CG  1 
ATOM   8712  C  CD  . GLU A 1 1527 ? 118.258 137.484 69.709  1.00 94.55  ? 1098 GLU A CD  1 
ATOM   8713  O  OE1 . GLU A 1 1527 ? 119.341 138.039 69.403  1.00 90.91  ? 1098 GLU A OE1 1 
ATOM   8714  O  OE2 . GLU A 1 1527 ? 117.894 136.399 69.199  1.00 87.63  ? 1098 GLU A OE2 1 
ATOM   8715  N  N   . ALA A 1 1528 ? 119.362 139.651 74.633  1.00 47.20  ? 1099 ALA A N   1 
ATOM   8716  C  CA  . ALA A 1 1528 ? 120.174 140.478 75.507  1.00 44.74  ? 1099 ALA A CA  1 
ATOM   8717  C  C   . ALA A 1 1528 ? 121.375 139.706 76.032  1.00 50.19  ? 1099 ALA A C   1 
ATOM   8718  O  O   . ALA A 1 1528 ? 122.497 140.221 76.043  1.00 56.90  ? 1099 ALA A O   1 
ATOM   8719  C  CB  . ALA A 1 1528 ? 119.324 140.988 76.668  1.00 47.46  ? 1099 ALA A CB  1 
ATOM   8720  N  N   . LEU A 1 1529 ? 121.168 138.464 76.443  1.00 47.98  ? 1100 LEU A N   1 
ATOM   8721  C  CA  . LEU A 1 1529 ? 122.212 137.704 77.107  1.00 46.39  ? 1100 LEU A CA  1 
ATOM   8722  C  C   . LEU A 1 1529 ? 123.238 137.130 76.148  1.00 47.07  ? 1100 LEU A C   1 
ATOM   8723  O  O   . LEU A 1 1529 ? 124.214 136.522 76.598  1.00 55.51  ? 1100 LEU A O   1 
ATOM   8724  C  CB  . LEU A 1 1529 ? 121.613 136.542 77.895  1.00 56.90  ? 1100 LEU A CB  1 
ATOM   8725  C  CG  . LEU A 1 1529 ? 120.686 136.740 79.092  1.00 62.99  ? 1100 LEU A CG  1 
ATOM   8726  C  CD1 . LEU A 1 1529 ? 119.959 135.417 79.418  1.00 63.27  ? 1100 LEU A CD1 1 
ATOM   8727  C  CD2 . LEU A 1 1529 ? 121.455 137.238 80.297  1.00 55.61  ? 1100 LEU A CD2 1 
ATOM   8728  N  N   . THR A 1 1530 ? 123.043 137.271 74.855  1.00 44.70  ? 1101 THR A N   1 
ATOM   8729  C  CA  . THR A 1 1530 ? 123.968 136.651 73.928  1.00 52.34  ? 1101 THR A CA  1 
ATOM   8730  C  C   . THR A 1 1530 ? 125.377 137.231 74.086  1.00 49.60  ? 1101 THR A C   1 
ATOM   8731  O  O   . THR A 1 1530 ? 125.570 138.344 74.583  1.00 50.75  ? 1101 THR A O   1 
ATOM   8732  C  CB  . THR A 1 1530 ? 123.462 136.840 72.490  1.00 66.07  ? 1101 THR A CB  1 
ATOM   8733  O  OG1 . THR A 1 1530 ? 123.009 138.190 72.306  1.00 63.58  ? 1101 THR A OG1 1 
ATOM   8734  C  CG2 . THR A 1 1530 ? 122.302 135.900 72.188  1.00 58.96  ? 1101 THR A CG2 1 
ATOM   8735  N  N   . GLN A 1 1531 ? 126.361 136.432 73.692  1.00 51.99  ? 1102 GLN A N   1 
ATOM   8736  C  CA  . GLN A 1 1531 ? 127.757 136.843 73.541  1.00 55.67  ? 1102 GLN A CA  1 
ATOM   8737  C  C   . GLN A 1 1531 ? 128.223 137.697 74.713  1.00 54.56  ? 1102 GLN A C   1 
ATOM   8738  O  O   . GLN A 1 1531 ? 128.564 138.871 74.568  1.00 54.31  ? 1102 GLN A O   1 
ATOM   8739  C  CB  . GLN A 1 1531 ? 127.981 137.579 72.221  1.00 64.15  ? 1102 GLN A CB  1 
ATOM   8740  C  CG  . GLN A 1 1531 ? 127.908 136.641 71.015  1.00 80.77  ? 1102 GLN A CG  1 
ATOM   8741  C  CD  . GLN A 1 1531 ? 129.085 135.669 70.931  1.00 84.88  ? 1102 GLN A CD  1 
ATOM   8742  O  OE1 . GLN A 1 1531 ? 130.193 135.965 71.388  1.00 82.28  ? 1102 GLN A OE1 1 
ATOM   8743  N  NE2 . GLN A 1 1531 ? 128.841 134.496 70.342  1.00 77.21  ? 1102 GLN A NE2 1 
ATOM   8744  N  N   . ILE A 1 1532 ? 128.215 137.079 75.894  1.00 57.92  ? 1103 ILE A N   1 
ATOM   8745  C  CA  . ILE A 1 1532 ? 128.741 137.691 77.108  1.00 48.59  ? 1103 ILE A CA  1 
ATOM   8746  C  C   . ILE A 1 1532 ? 129.555 136.664 77.879  1.00 46.82  ? 1103 ILE A C   1 
ATOM   8747  O  O   . ILE A 1 1532 ? 129.018 135.650 78.337  1.00 49.80  ? 1103 ILE A O   1 
ATOM   8748  C  CB  . ILE A 1 1532 ? 127.631 138.256 77.986  1.00 40.58  ? 1103 ILE A CB  1 
ATOM   8749  C  CG1 . ILE A 1 1532 ? 127.034 139.465 77.270  1.00 54.90  ? 1103 ILE A CG1 1 
ATOM   8750  C  CG2 . ILE A 1 1532 ? 128.191 138.592 79.360  1.00 51.87  ? 1103 ILE A CG2 1 
ATOM   8751  C  CD1 . ILE A 1 1532 ? 125.922 140.155 78.010  1.00 65.99  ? 1103 ILE A CD1 1 
ATOM   8752  N  N   . THR A 1 1533 ? 130.833 136.948 78.068  1.00 47.92  ? 1104 THR A N   1 
ATOM   8753  C  CA  . THR A 1 1533 ? 131.745 135.912 78.515  1.00 46.79  ? 1104 THR A CA  1 
ATOM   8754  C  C   . THR A 1 1533 ? 131.482 135.543 79.965  1.00 42.19  ? 1104 THR A C   1 
ATOM   8755  O  O   . THR A 1 1533 ? 131.112 134.406 80.262  1.00 47.89  ? 1104 THR A O   1 
ATOM   8756  C  CB  . THR A 1 1533 ? 133.191 136.385 78.320  1.00 69.78  ? 1104 THR A CB  1 
ATOM   8757  O  OG1 . THR A 1 1533 ? 133.431 137.552 79.122  1.00 67.70  ? 1104 THR A OG1 1 
ATOM   8758  C  CG2 . THR A 1 1533 ? 133.451 136.752 76.844  1.00 72.84  ? 1104 THR A CG2 1 
ATOM   8759  N  N   . CYS A 1 1534 ? 131.628 136.503 80.876  1.00 53.60  ? 1105 CYS A N   1 
ATOM   8760  C  CA  . CYS A 1 1534 ? 131.814 136.184 82.288  1.00 58.72  ? 1105 CYS A CA  1 
ATOM   8761  C  C   . CYS A 1 1534 ? 130.487 136.067 83.021  1.00 40.60  ? 1105 CYS A C   1 
ATOM   8762  O  O   . CYS A 1 1534 ? 129.496 136.712 82.685  1.00 47.06  ? 1105 CYS A O   1 
ATOM   8763  C  CB  . CYS A 1 1534 ? 132.672 137.232 83.000  1.00 66.30  ? 1105 CYS A CB  1 
ATOM   8764  S  SG  . CYS A 1 1534 ? 132.958 136.815 84.764  1.00 71.44  ? 1105 CYS A SG  1 
ATOM   8765  N  N   . THR A 1 1535 ? 130.483 135.232 84.043  1.00 35.95  ? 1106 THR A N   1 
ATOM   8766  C  CA  . THR A 1 1535 ? 129.226 134.984 84.697  1.00 27.35  ? 1106 THR A CA  1 
ATOM   8767  C  C   . THR A 1 1535 ? 128.744 136.209 85.413  1.00 39.70  ? 1106 THR A C   1 
ATOM   8768  O  O   . THR A 1 1535 ? 127.537 136.398 85.538  1.00 47.95  ? 1106 THR A O   1 
ATOM   8769  C  CB  . THR A 1 1535 ? 129.335 133.844 85.687  1.00 35.59  ? 1106 THR A CB  1 
ATOM   8770  O  OG1 . THR A 1 1535 ? 129.828 132.674 85.024  1.00 45.86  ? 1106 THR A OG1 1 
ATOM   8771  C  CG2 . THR A 1 1535 ? 127.992 133.563 86.272  1.00 37.97  ? 1106 THR A CG2 1 
ATOM   8772  N  N   . VAL A 1 1536 ? 129.645 137.060 85.897  1.00 43.17  ? 1107 VAL A N   1 
ATOM   8773  C  CA  . VAL A 1 1536 ? 129.155 138.168 86.711  1.00 37.84  ? 1107 VAL A CA  1 
ATOM   8774  C  C   . VAL A 1 1536 ? 128.341 139.120 85.857  1.00 39.40  ? 1107 VAL A C   1 
ATOM   8775  O  O   . VAL A 1 1536 ? 127.284 139.601 86.278  1.00 46.56  ? 1107 VAL A O   1 
ATOM   8776  C  CB  . VAL A 1 1536 ? 130.304 138.890 87.416  1.00 45.41  ? 1107 VAL A CB  1 
ATOM   8777  C  CG1 . VAL A 1 1536 ? 131.330 139.320 86.413  1.00 57.42  ? 1107 VAL A CG1 1 
ATOM   8778  C  CG2 . VAL A 1 1536 ? 129.757 140.085 88.155  1.00 58.43  ? 1107 VAL A CG2 1 
ATOM   8779  N  N   . ASP A 1 1537 ? 128.789 139.373 84.632  1.00 36.99  ? 1108 ASP A N   1 
ATOM   8780  C  CA  . ASP A 1 1537 ? 127.997 140.188 83.729  1.00 31.56  ? 1108 ASP A CA  1 
ATOM   8781  C  C   . ASP A 1 1537 ? 126.656 139.547 83.450  1.00 38.10  ? 1108 ASP A C   1 
ATOM   8782  O  O   . ASP A 1 1537 ? 125.614 140.211 83.522  1.00 45.60  ? 1108 ASP A O   1 
ATOM   8783  C  CB  . ASP A 1 1537 ? 128.754 140.405 82.435  1.00 34.43  ? 1108 ASP A CB  1 
ATOM   8784  C  CG  . ASP A 1 1537 ? 130.160 140.851 82.687  1.00 63.32  ? 1108 ASP A CG  1 
ATOM   8785  O  OD1 . ASP A 1 1537 ? 130.370 141.557 83.701  1.00 64.25  ? 1108 ASP A OD1 1 
ATOM   8786  O  OD2 . ASP A 1 1537 ? 131.063 140.481 81.908  1.00 67.90  ? 1108 ASP A OD2 1 
ATOM   8787  N  N   . LEU A 1 1538 ? 126.660 138.273 83.061  1.00 37.24  ? 1109 LEU A N   1 
ATOM   8788  C  CA  . LEU A 1 1538 ? 125.390 137.620 82.802  1.00 30.72  ? 1109 LEU A CA  1 
ATOM   8789  C  C   . LEU A 1 1538 ? 124.496 137.794 83.988  1.00 29.45  ? 1109 LEU A C   1 
ATOM   8790  O  O   . LEU A 1 1538 ? 123.314 138.096 83.845  1.00 47.93  ? 1109 LEU A O   1 
ATOM   8791  C  CB  . LEU A 1 1538 ? 125.554 136.133 82.528  1.00 25.88  ? 1109 LEU A CB  1 
ATOM   8792  C  CG  . LEU A 1 1538 ? 126.210 135.849 81.201  1.00 34.68  ? 1109 LEU A CG  1 
ATOM   8793  C  CD1 . LEU A 1 1538 ? 126.571 134.361 81.021  1.00 37.53  ? 1109 LEU A CD1 1 
ATOM   8794  C  CD2 . LEU A 1 1538 ? 125.259 136.355 80.142  1.00 48.91  ? 1109 LEU A CD2 1 
ATOM   8795  N  N   . ALA A 1 1539 ? 125.042 137.634 85.166  1.00 24.46  ? 1110 ALA A N   1 
ATOM   8796  C  CA  . ALA A 1 1539 ? 124.171 137.630 86.311  1.00 31.42  ? 1110 ALA A CA  1 
ATOM   8797  C  C   . ALA A 1 1539 ? 123.615 139.012 86.544  1.00 45.80  ? 1110 ALA A C   1 
ATOM   8798  O  O   . ALA A 1 1539 ? 122.467 139.152 86.966  1.00 48.69  ? 1110 ALA A O   1 
ATOM   8799  C  CB  . ALA A 1 1539 ? 124.905 137.133 87.543  1.00 45.94  ? 1110 ALA A CB  1 
ATOM   8800  N  N   . GLN A 1 1540 ? 124.398 140.054 86.245  1.00 50.63  ? 1111 GLN A N   1 
ATOM   8801  C  CA  . GLN A 1 1540 ? 123.912 141.401 86.539  1.00 50.11  ? 1111 GLN A CA  1 
ATOM   8802  C  C   . GLN A 1 1540 ? 122.911 141.869 85.498  1.00 45.16  ? 1111 GLN A C   1 
ATOM   8803  O  O   . GLN A 1 1540 ? 121.917 142.514 85.840  1.00 50.71  ? 1111 GLN A O   1 
ATOM   8804  C  CB  . GLN A 1 1540 ? 125.052 142.394 86.654  1.00 40.11  ? 1111 GLN A CB  1 
ATOM   8805  C  CG  . GLN A 1 1540 ? 124.573 143.709 87.155  1.00 37.56  ? 1111 GLN A CG  1 
ATOM   8806  C  CD  . GLN A 1 1540 ? 125.690 144.452 87.811  1.00 57.62  ? 1111 GLN A CD  1 
ATOM   8807  O  OE1 . GLN A 1 1540 ? 126.858 144.232 87.489  1.00 67.67  ? 1111 GLN A OE1 1 
ATOM   8808  N  NE2 . GLN A 1 1540 ? 125.359 145.316 88.763  1.00 61.08  ? 1111 GLN A NE2 1 
ATOM   8809  N  N   . ILE A 1 1541 ? 123.118 141.523 84.231  1.00 31.94  ? 1112 ILE A N   1 
ATOM   8810  C  CA  . ILE A 1 1541 ? 122.110 141.934 83.262  1.00 31.37  ? 1112 ILE A CA  1 
ATOM   8811  C  C   . ILE A 1 1541 ? 120.877 141.061 83.363  1.00 31.34  ? 1112 ILE A C   1 
ATOM   8812  O  O   . ILE A 1 1541 ? 119.756 141.520 83.115  1.00 39.58  ? 1112 ILE A O   1 
ATOM   8813  C  CB  . ILE A 1 1541 ? 122.658 141.878 81.861  1.00 30.05  ? 1112 ILE A CB  1 
ATOM   8814  C  CG1 . ILE A 1 1541 ? 122.904 140.433 81.532  1.00 42.28  ? 1112 ILE A CG1 1 
ATOM   8815  C  CG2 . ILE A 1 1541 ? 123.981 142.599 81.863  1.00 43.46  ? 1112 ILE A CG2 1 
ATOM   8816  C  CD1 . ILE A 1 1541 ? 123.169 140.213 80.095  1.00 63.49  ? 1112 ILE A CD1 1 
ATOM   8817  N  N   . LEU A 1 1542 ? 121.032 139.825 83.792  1.00 29.46  ? 1113 LEU A N   1 
ATOM   8818  C  CA  . LEU A 1 1542 ? 119.851 139.038 84.001  1.00 24.15  ? 1113 LEU A CA  1 
ATOM   8819  C  C   . LEU A 1 1542 ? 119.161 139.462 85.255  1.00 23.40  ? 1113 LEU A C   1 
ATOM   8820  O  O   . LEU A 1 1542 ? 117.930 139.505 85.296  1.00 39.53  ? 1113 LEU A O   1 
ATOM   8821  C  CB  . LEU A 1 1542 ? 120.193 137.568 84.055  1.00 31.30  ? 1113 LEU A CB  1 
ATOM   8822  C  CG  . LEU A 1 1542 ? 118.860 136.837 84.056  1.00 55.54  ? 1113 LEU A CG  1 
ATOM   8823  C  CD1 . LEU A 1 1542 ? 119.017 135.593 83.273  1.00 64.42  ? 1113 LEU A CD1 1 
ATOM   8824  C  CD2 . LEU A 1 1542 ? 118.448 136.446 85.460  1.00 51.57  ? 1113 LEU A CD2 1 
ATOM   8825  N  N   . ARG A 1 1543 ? 119.907 139.824 86.263  1.00 22.07  ? 1114 ARG A N   1 
ATOM   8826  C  CA  . ARG A 1 1543 ? 119.245 140.254 87.466  1.00 32.69  ? 1114 ARG A CA  1 
ATOM   8827  C  C   . ARG A 1 1543 ? 118.533 141.589 87.261  1.00 37.47  ? 1114 ARG A C   1 
ATOM   8828  O  O   . ARG A 1 1543 ? 117.431 141.784 87.787  1.00 40.73  ? 1114 ARG A O   1 
ATOM   8829  C  CB  . ARG A 1 1543 ? 120.255 140.240 88.633  1.00 42.29  ? 1114 ARG A CB  1 
ATOM   8830  C  CG  . ARG A 1 1543 ? 119.609 140.785 89.878  1.00 48.43  ? 1114 ARG A CG  1 
ATOM   8831  C  CD  . ARG A 1 1543 ? 120.408 140.712 91.162  1.00 46.38  ? 1114 ARG A CD  1 
ATOM   8832  N  NE  . ARG A 1 1543 ? 120.561 139.368 91.694  1.00 36.44  ? 1114 ARG A NE  1 
ATOM   8833  C  CZ  . ARG A 1 1543 ? 121.691 138.690 91.705  1.00 36.31  ? 1114 ARG A CZ  1 
ATOM   8834  N  NH1 . ARG A 1 1543 ? 122.760 139.214 91.140  1.00 43.90  ? 1114 ARG A NH1 1 
ATOM   8835  N  NH2 . ARG A 1 1543 ? 121.722 137.474 92.244  1.00 37.98  ? 1114 ARG A NH2 1 
ATOM   8836  N  N   . GLU A 1 1544 ? 119.091 142.485 86.448  1.00 39.17  ? 1115 GLU A N   1 
ATOM   8837  C  CA  . GLU A 1 1544 ? 118.421 143.755 86.201  1.00 34.62  ? 1115 GLU A CA  1 
ATOM   8838  C  C   . GLU A 1 1544 ? 117.215 143.587 85.287  1.00 34.99  ? 1115 GLU A C   1 
ATOM   8839  O  O   . GLU A 1 1544 ? 116.219 144.307 85.435  1.00 41.21  ? 1115 GLU A O   1 
ATOM   8840  C  CB  . GLU A 1 1544 ? 119.401 144.751 85.592  1.00 41.48  ? 1115 GLU A CB  1 
ATOM   8841  C  CG  . GLU A 1 1544 ? 120.499 145.212 86.564  1.00 59.24  ? 1115 GLU A CG  1 
ATOM   8842  C  CD  . GLU A 1 1544 ? 120.972 146.650 86.298  1.00 76.29  ? 1115 GLU A CD  1 
ATOM   8843  O  OE1 . GLU A 1 1544 ? 120.585 147.231 85.250  1.00 74.50  ? 1115 GLU A OE1 1 
ATOM   8844  O  OE2 . GLU A 1 1544 ? 121.732 147.202 87.133  1.00 64.34  ? 1115 GLU A OE2 1 
ATOM   8845  N  N   . TYR A 1 1545 ? 117.273 142.649 84.340  1.00 30.75  ? 1116 TYR A N   1 
ATOM   8846  C  CA  . TYR A 1 1545 ? 116.119 142.429 83.480  1.00 34.37  ? 1116 TYR A CA  1 
ATOM   8847  C  C   . TYR A 1 1545 ? 114.978 141.744 84.205  1.00 26.85  ? 1116 TYR A C   1 
ATOM   8848  O  O   . TYR A 1 1545 ? 113.817 141.915 83.836  1.00 35.44  ? 1116 TYR A O   1 
ATOM   8849  C  CB  . TYR A 1 1545 ? 116.508 141.577 82.287  1.00 41.60  ? 1116 TYR A CB  1 
ATOM   8850  C  CG  . TYR A 1 1545 ? 115.345 141.342 81.379  1.00 39.05  ? 1116 TYR A CG  1 
ATOM   8851  C  CD1 . TYR A 1 1545 ? 114.974 142.288 80.455  1.00 43.70  ? 1116 TYR A CD1 1 
ATOM   8852  C  CD2 . TYR A 1 1545 ? 114.596 140.194 81.478  1.00 52.58  ? 1116 TYR A CD2 1 
ATOM   8853  C  CE1 . TYR A 1 1545 ? 113.910 142.092 79.630  1.00 54.56  ? 1116 TYR A CE1 1 
ATOM   8854  C  CE2 . TYR A 1 1545 ? 113.520 139.980 80.655  1.00 62.76  ? 1116 TYR A CE2 1 
ATOM   8855  C  CZ  . TYR A 1 1545 ? 113.179 140.937 79.731  1.00 63.58  ? 1116 TYR A CZ  1 
ATOM   8856  O  OH  . TYR A 1 1545 ? 112.100 140.735 78.898  1.00 70.23  ? 1116 TYR A OH  1 
ATOM   8857  N  N   . SER A 1 1546 ? 115.280 140.899 85.162  1.00 24.24  ? 1117 SER A N   1 
ATOM   8858  C  CA  . SER A 1 1546 ? 114.186 140.267 85.853  1.00 23.91  ? 1117 SER A CA  1 
ATOM   8859  C  C   . SER A 1 1546 ? 113.426 141.299 86.632  1.00 27.59  ? 1117 SER A C   1 
ATOM   8860  O  O   . SER A 1 1546 ? 112.228 141.493 86.418  1.00 41.75  ? 1117 SER A O   1 
ATOM   8861  C  CB  . SER A 1 1546 ? 114.705 139.199 86.790  1.00 38.58  ? 1117 SER A CB  1 
ATOM   8862  O  OG  . SER A 1 1546 ? 115.622 139.795 87.694  1.00 39.12  ? 1117 SER A OG  1 
ATOM   8863  N  N   . TRP A 1 1547 ? 114.115 142.018 87.503  1.00 27.77  ? 1118 TRP A N   1 
ATOM   8864  C  CA  . TRP A 1 1547 ? 113.441 143.033 88.296  1.00 35.32  ? 1118 TRP A CA  1 
ATOM   8865  C  C   . TRP A 1 1547 ? 113.297 144.343 87.550  1.00 39.66  ? 1118 TRP A C   1 
ATOM   8866  O  O   . TRP A 1 1547 ? 113.152 145.391 88.193  1.00 47.48  ? 1118 TRP A O   1 
ATOM   8867  C  CB  . TRP A 1 1547 ? 114.160 143.284 89.628  1.00 42.84  ? 1118 TRP A CB  1 
ATOM   8868  C  CG  . TRP A 1 1547 ? 114.300 142.101 90.533  1.00 37.85  ? 1118 TRP A CG  1 
ATOM   8869  C  CD1 . TRP A 1 1547 ? 115.432 141.413 90.806  1.00 39.47  ? 1118 TRP A CD1 1 
ATOM   8870  C  CD2 . TRP A 1 1547 ? 113.256 141.464 91.266  1.00 30.11  ? 1118 TRP A CD2 1 
ATOM   8871  N  NE1 . TRP A 1 1547 ? 115.164 140.393 91.673  1.00 39.99  ? 1118 TRP A NE1 1 
ATOM   8872  C  CE2 . TRP A 1 1547 ? 113.828 140.400 91.964  1.00 31.97  ? 1118 TRP A CE2 1 
ATOM   8873  C  CE3 . TRP A 1 1547 ? 111.890 141.696 91.396  1.00 39.60  ? 1118 TRP A CE3 1 
ATOM   8874  C  CZ2 . TRP A 1 1547 ? 113.089 139.567 92.789  1.00 41.00  ? 1118 TRP A CZ2 1 
ATOM   8875  C  CZ3 . TRP A 1 1547 ? 111.155 140.869 92.206  1.00 41.82  ? 1118 TRP A CZ3 1 
ATOM   8876  C  CH2 . TRP A 1 1547 ? 111.753 139.815 92.894  1.00 42.56  ? 1118 TRP A CH2 1 
ATOM   8877  N  N   . ALA A 1 1548 ? 113.312 144.319 86.216  1.00 36.08  ? 1119 ALA A N   1 
ATOM   8878  C  CA  . ALA A 1 1548 ? 113.213 145.571 85.480  1.00 34.30  ? 1119 ALA A CA  1 
ATOM   8879  C  C   . ALA A 1 1548 ? 112.070 146.411 86.014  1.00 33.08  ? 1119 ALA A C   1 
ATOM   8880  O  O   . ALA A 1 1548 ? 112.265 147.571 86.386  1.00 41.36  ? 1119 ALA A O   1 
ATOM   8881  C  CB  . ALA A 1 1548 ? 113.007 145.301 83.990  1.00 33.43  ? 1119 ALA A CB  1 
ATOM   8882  N  N   . HIS A 1 1549 ? 110.899 145.815 86.166  1.00 29.62  ? 1120 HIS A N   1 
ATOM   8883  C  CA  . HIS A 1 1549 ? 109.763 146.656 86.454  1.00 31.71  ? 1120 HIS A CA  1 
ATOM   8884  C  C   . HIS A 1 1549 ? 109.848 147.273 87.832  1.00 32.63  ? 1120 HIS A C   1 
ATOM   8885  O  O   . HIS A 1 1549 ? 109.214 148.299 88.075  1.00 46.77  ? 1120 HIS A O   1 
ATOM   8886  C  CB  . HIS A 1 1549 ? 108.464 145.883 86.334  1.00 33.35  ? 1120 HIS A CB  1 
ATOM   8887  C  CG  . HIS A 1 1549 ? 108.239 144.929 87.456  1.00 39.00  ? 1120 HIS A CG  1 
ATOM   8888  N  ND1 . HIS A 1 1549 ? 108.730 143.641 87.450  1.00 49.21  ? 1120 HIS A ND1 1 
ATOM   8889  C  CD2 . HIS A 1 1549 ? 107.623 145.093 88.651  1.00 42.94  ? 1120 HIS A CD2 1 
ATOM   8890  C  CE1 . HIS A 1 1549 ? 108.393 143.038 88.577  1.00 49.26  ? 1120 HIS A CE1 1 
ATOM   8891  N  NE2 . HIS A 1 1549 ? 107.724 143.898 89.325  1.00 47.99  ? 1120 HIS A NE2 1 
ATOM   8892  N  N   . ILE A 1 1550 ? 110.594 146.694 88.746  1.00 27.69  ? 1121 ILE A N   1 
ATOM   8893  C  CA  . ILE A 1 1550 ? 110.736 147.379 90.018  1.00 29.49  ? 1121 ILE A CA  1 
ATOM   8894  C  C   . ILE A 1 1550 ? 111.896 148.354 89.980  1.00 35.10  ? 1121 ILE A C   1 
ATOM   8895  O  O   . ILE A 1 1550 ? 111.833 149.423 90.584  1.00 48.59  ? 1121 ILE A O   1 
ATOM   8896  C  CB  . ILE A 1 1550 ? 110.880 146.365 91.163  1.00 34.35  ? 1121 ILE A CB  1 
ATOM   8897  C  CG1 . ILE A 1 1550 ? 109.565 145.652 91.379  1.00 43.63  ? 1121 ILE A CG1 1 
ATOM   8898  C  CG2 . ILE A 1 1550 ? 111.229 147.032 92.452  1.00 35.66  ? 1121 ILE A CG2 1 
ATOM   8899  C  CD1 . ILE A 1 1550 ? 109.687 144.527 92.349  1.00 49.23  ? 1121 ILE A CD1 1 
ATOM   8900  N  N   . LEU A 1 1551 ? 112.980 148.020 89.295  1.00 36.76  ? 1122 LEU A N   1 
ATOM   8901  C  CA  . LEU A 1 1551 ? 114.104 148.947 89.250  1.00 39.14  ? 1122 LEU A CA  1 
ATOM   8902  C  C   . LEU A 1 1551 ? 113.786 150.173 88.409  1.00 46.49  ? 1122 LEU A C   1 
ATOM   8903  O  O   . LEU A 1 1551 ? 114.205 151.287 88.748  1.00 53.70  ? 1122 LEU A O   1 
ATOM   8904  C  CB  . LEU A 1 1551 ? 115.354 148.263 88.709  1.00 47.82  ? 1122 LEU A CB  1 
ATOM   8905  C  CG  . LEU A 1 1551 ? 115.947 147.182 89.605  1.00 59.01  ? 1122 LEU A CG  1 
ATOM   8906  C  CD1 . LEU A 1 1551 ? 117.124 146.488 88.891  1.00 62.98  ? 1122 LEU A CD1 1 
ATOM   8907  C  CD2 . LEU A 1 1551 ? 116.373 147.808 90.934  1.00 51.17  ? 1122 LEU A CD2 1 
ATOM   8908  N  N   . GLU A 1 1552 ? 113.067 149.995 87.307  1.00 43.99  ? 1123 GLU A N   1 
ATOM   8909  C  CA  . GLU A 1 1552 ? 112.776 151.101 86.408  1.00 36.83  ? 1123 GLU A CA  1 
ATOM   8910  C  C   . GLU A 1 1552 ? 114.076 151.782 86.013  1.00 37.77  ? 1123 GLU A C   1 
ATOM   8911  O  O   . GLU A 1 1552 ? 114.279 152.975 86.232  1.00 43.46  ? 1123 GLU A O   1 
ATOM   8912  C  CB  . GLU A 1 1552 ? 111.817 152.087 87.069  1.00 51.75  ? 1123 GLU A CB  1 
ATOM   8913  C  CG  . GLU A 1 1552 ? 110.466 151.463 87.490  1.00 68.61  ? 1123 GLU A CG  1 
ATOM   8914  C  CD  . GLU A 1 1552 ? 109.441 152.496 88.002  1.00 89.72  ? 1123 GLU A CD  1 
ATOM   8915  O  OE1 . GLU A 1 1552 ? 109.777 153.703 88.061  1.00 90.48  ? 1123 GLU A OE1 1 
ATOM   8916  O  OE2 . GLU A 1 1552 ? 108.308 152.095 88.364  1.00 80.18  ? 1123 GLU A OE2 1 
ATOM   8917  N  N   . GLY A 1 1553 ? 115.010 150.981 85.519  1.00 41.81  ? 1124 GLY A N   1 
ATOM   8918  C  CA  . GLY A 1 1553 ? 116.228 151.508 84.948  1.00 46.37  ? 1124 GLY A CA  1 
ATOM   8919  C  C   . GLY A 1 1553 ? 117.276 151.972 85.934  1.00 37.13  ? 1124 GLY A C   1 
ATOM   8920  O  O   . GLY A 1 1553 ? 118.449 152.089 85.561  1.00 36.28  ? 1124 GLY A O   1 
ATOM   8921  N  N   . ARG A 1 1554 ? 116.908 152.254 87.165  1.00 31.70  ? 1125 ARG A N   1 
ATOM   8922  C  CA  . ARG A 1 1554 ? 117.919 152.631 88.134  1.00 34.51  ? 1125 ARG A CA  1 
ATOM   8923  C  C   . ARG A 1 1554 ? 118.879 151.460 88.333  1.00 36.87  ? 1125 ARG A C   1 
ATOM   8924  O  O   . ARG A 1 1554 ? 118.439 150.306 88.356  1.00 50.34  ? 1125 ARG A O   1 
ATOM   8925  C  CB  . ARG A 1 1554 ? 117.243 152.992 89.451  1.00 43.42  ? 1125 ARG A CB  1 
ATOM   8926  C  CG  . ARG A 1 1554 ? 116.186 154.061 89.278  1.00 41.87  ? 1125 ARG A CG  1 
ATOM   8927  C  CD  . ARG A 1 1554 ? 115.496 154.353 90.576  1.00 37.16  ? 1125 ARG A CD  1 
ATOM   8928  N  NE  . ARG A 1 1554 ? 114.892 153.176 91.173  1.00 39.43  ? 1125 ARG A NE  1 
ATOM   8929  C  CZ  . ARG A 1 1554 ? 113.863 153.232 92.012  1.00 48.44  ? 1125 ARG A CZ  1 
ATOM   8930  N  NH1 . ARG A 1 1554 ? 113.337 154.411 92.320  1.00 52.16  ? 1125 ARG A NH1 1 
ATOM   8931  N  NH2 . ARG A 1 1554 ? 113.355 152.122 92.540  1.00 46.21  ? 1125 ARG A NH2 1 
ATOM   8932  N  N   . PRO A 1 1555 ? 120.180 151.700 88.458  1.00 28.45  ? 1126 PRO A N   1 
ATOM   8933  C  CA  . PRO A 1 1555 ? 121.125 150.586 88.497  1.00 24.77  ? 1126 PRO A CA  1 
ATOM   8934  C  C   . PRO A 1 1555 ? 120.911 149.807 89.761  1.00 42.97  ? 1126 PRO A C   1 
ATOM   8935  O  O   . PRO A 1 1555 ? 120.515 150.367 90.785  1.00 48.68  ? 1126 PRO A O   1 
ATOM   8936  C  CB  . PRO A 1 1555 ? 122.482 151.262 88.556  1.00 28.97  ? 1126 PRO A CB  1 
ATOM   8937  C  CG  . PRO A 1 1555 ? 122.191 152.512 89.243  1.00 36.01  ? 1126 PRO A CG  1 
ATOM   8938  C  CD  . PRO A 1 1555 ? 120.845 152.961 88.770  1.00 40.05  ? 1126 PRO A CD  1 
ATOM   8939  N  N   . LEU A 1 1556 ? 121.204 148.509 89.699  1.00 49.84  ? 1127 LEU A N   1 
ATOM   8940  C  CA  . LEU A 1 1556 ? 121.183 147.645 90.875  1.00 42.46  ? 1127 LEU A CA  1 
ATOM   8941  C  C   . LEU A 1 1556 ? 122.609 147.275 91.226  1.00 42.94  ? 1127 LEU A C   1 
ATOM   8942  O  O   . LEU A 1 1556 ? 123.321 146.692 90.406  1.00 52.18  ? 1127 LEU A O   1 
ATOM   8943  C  CB  . LEU A 1 1556 ? 120.351 146.396 90.629  1.00 42.75  ? 1127 LEU A CB  1 
ATOM   8944  C  CG  . LEU A 1 1556 ? 120.334 145.390 91.776  1.00 54.42  ? 1127 LEU A CG  1 
ATOM   8945  C  CD1 . LEU A 1 1556 ? 119.853 146.000 93.079  1.00 53.54  ? 1127 LEU A CD1 1 
ATOM   8946  C  CD2 . LEU A 1 1556 ? 119.439 144.223 91.371  1.00 58.62  ? 1127 LEU A CD2 1 
ATOM   8947  N  N   . ILE A 1 1557 ? 123.034 147.633 92.426  1.00 40.50  ? 1128 ILE A N   1 
ATOM   8948  C  CA  . ILE A 1 1557 ? 124.380 147.314 92.854  1.00 35.97  ? 1128 ILE A CA  1 
ATOM   8949  C  C   . ILE A 1 1557 ? 124.297 146.641 94.203  1.00 48.35  ? 1128 ILE A C   1 
ATOM   8950  O  O   . ILE A 1 1557 ? 123.300 146.741 94.921  1.00 53.92  ? 1128 ILE A O   1 
ATOM   8951  C  CB  . ILE A 1 1557 ? 125.263 148.543 92.960  1.00 46.52  ? 1128 ILE A CB  1 
ATOM   8952  C  CG1 . ILE A 1 1557 ? 124.798 149.362 94.171  1.00 60.18  ? 1128 ILE A CG1 1 
ATOM   8953  C  CG2 . ILE A 1 1557 ? 125.187 149.320 91.656  1.00 57.07  ? 1128 ILE A CG2 1 
ATOM   8954  C  CD1 . ILE A 1 1557 ? 125.565 150.651 94.401  1.00 71.42  ? 1128 ILE A CD1 1 
ATOM   8955  N  N   . GLY A 1 1558 ? 125.384 145.974 94.562  1.00 60.88  ? 1129 GLY A N   1 
ATOM   8956  C  CA  . GLY A 1 1558 ? 125.388 145.213 95.794  1.00 69.11  ? 1129 GLY A CA  1 
ATOM   8957  C  C   . GLY A 1 1558 ? 124.613 143.916 95.705  1.00 76.49  ? 1129 GLY A C   1 
ATOM   8958  O  O   . GLY A 1 1558 ? 124.057 143.464 96.713  1.00 72.67  ? 1129 GLY A O   1 
ATOM   8959  N  N   . ALA A 1 1559 ? 124.547 143.306 94.517  1.00 65.61  ? 1130 ALA A N   1 
ATOM   8960  C  CA  . ALA A 1 1559 ? 123.826 142.049 94.374  1.00 59.31  ? 1130 ALA A CA  1 
ATOM   8961  C  C   . ALA A 1 1559 ? 124.518 141.011 93.508  1.00 50.33  ? 1130 ALA A C   1 
ATOM   8962  O  O   . ALA A 1 1559 ? 123.992 139.901 93.388  1.00 50.86  ? 1130 ALA A O   1 
ATOM   8963  C  CB  . ALA A 1 1559 ? 122.418 142.304 93.816  1.00 64.08  ? 1130 ALA A CB  1 
ATOM   8964  N  N   . THR A 1 1560 ? 125.649 141.311 92.886  1.00 39.06  ? 1131 THR A N   1 
ATOM   8965  C  CA  . THR A 1 1560 ? 126.337 140.324 92.069  1.00 37.54  ? 1131 THR A CA  1 
ATOM   8966  C  C   . THR A 1 1560 ? 127.810 140.219 92.462  1.00 39.11  ? 1131 THR A C   1 
ATOM   8967  O  O   . THR A 1 1560 ? 128.553 141.203 92.408  1.00 42.96  ? 1131 THR A O   1 
ATOM   8968  C  CB  . THR A 1 1560 ? 126.168 140.666 90.591  1.00 48.23  ? 1131 THR A CB  1 
ATOM   8969  O  OG1 . THR A 1 1560 ? 126.899 139.722 89.791  1.00 51.31  ? 1131 THR A OG1 1 
ATOM   8970  C  CG2 . THR A 1 1560 ? 126.589 142.108 90.306  1.00 50.81  ? 1131 THR A CG2 1 
ATOM   8971  N  N   . LEU A 1 1561 ? 128.226 139.029 92.856  1.00 27.18  ? 1132 LEU A N   1 
ATOM   8972  C  CA  . LEU A 1 1561 ? 129.583 138.747 93.249  1.00 17.95  ? 1132 LEU A CA  1 
ATOM   8973  C  C   . LEU A 1 1561 ? 130.072 137.557 92.474  1.00 20.91  ? 1132 LEU A C   1 
ATOM   8974  O  O   . LEU A 1 1561 ? 129.307 136.641 92.202  1.00 34.11  ? 1132 LEU A O   1 
ATOM   8975  C  CB  . LEU A 1 1561 ? 129.670 138.399 94.714  1.00 28.73  ? 1132 LEU A CB  1 
ATOM   8976  C  CG  . LEU A 1 1561 ? 129.254 139.566 95.556  1.00 44.61  ? 1132 LEU A CG  1 
ATOM   8977  C  CD1 . LEU A 1 1561 ? 129.302 139.140 97.022  1.00 55.52  ? 1132 LEU A CD1 1 
ATOM   8978  C  CD2 . LEU A 1 1561 ? 130.218 140.700 95.233  1.00 45.01  ? 1132 LEU A CD2 1 
ATOM   8979  N  N   . PRO A 1 1562 ? 131.336 137.518 92.159  1.00 20.64  ? 1133 PRO A N   1 
ATOM   8980  C  CA  . PRO A 1 1562 ? 131.822 136.525 91.211  1.00 25.47  ? 1133 PRO A CA  1 
ATOM   8981  C  C   . PRO A 1 1562 ? 131.750 135.127 91.788  1.00 39.49  ? 1133 PRO A C   1 
ATOM   8982  O  O   . PRO A 1 1562 ? 131.881 134.917 92.996  1.00 41.28  ? 1133 PRO A O   1 
ATOM   8983  C  CB  . PRO A 1 1562 ? 133.274 136.929 90.992  1.00 36.54  ? 1133 PRO A CB  1 
ATOM   8984  C  CG  . PRO A 1 1562 ? 133.629 137.599 92.262  1.00 44.44  ? 1133 PRO A CG  1 
ATOM   8985  C  CD  . PRO A 1 1562 ? 132.409 138.330 92.715  1.00 37.19  ? 1133 PRO A CD  1 
ATOM   8986  N  N   . CYS A 1 1563 ? 131.544 134.160 90.899  1.00 42.00  ? 1134 CYS A N   1 
ATOM   8987  C  CA  . CYS A 1 1563 ? 131.548 132.753 91.285  1.00 31.95  ? 1134 CYS A CA  1 
ATOM   8988  C  C   . CYS A 1 1563 ? 132.976 132.305 91.493  1.00 29.78  ? 1134 CYS A C   1 
ATOM   8989  O  O   . CYS A 1 1563 ? 133.698 132.037 90.529  1.00 34.19  ? 1134 CYS A O   1 
ATOM   8990  C  CB  . CYS A 1 1563 ? 130.874 131.910 90.212  1.00 48.58  ? 1134 CYS A CB  1 
ATOM   8991  S  SG  . CYS A 1 1563 ? 130.897 130.143 90.585  1.00 70.95  ? 1134 CYS A SG  1 
ATOM   8992  N  N   . MET A 1 1564 ? 133.369 132.177 92.748  1.00 32.36  ? 1135 MET A N   1 
ATOM   8993  C  CA  . MET A 1 1564 ? 134.784 132.088 93.045  1.00 28.74  ? 1135 MET A CA  1 
ATOM   8994  C  C   . MET A 1 1564 ? 135.461 131.005 92.256  1.00 27.78  ? 1135 MET A C   1 
ATOM   8995  O  O   . MET A 1 1564 ? 136.679 131.050 92.092  1.00 40.71  ? 1135 MET A O   1 
ATOM   8996  C  CB  . MET A 1 1564 ? 135.004 131.821 94.521  1.00 30.13  ? 1135 MET A CB  1 
ATOM   8997  C  CG  . MET A 1 1564 ? 136.419 132.032 94.967  1.00 35.46  ? 1135 MET A CG  1 
ATOM   8998  S  SD  . MET A 1 1564 ? 136.449 132.279 96.743  1.00 65.71  ? 1135 MET A SD  1 
ATOM   8999  C  CE  . MET A 1 1564 ? 135.552 133.829 96.878  1.00 45.65  ? 1135 MET A CE  1 
ATOM   9000  N  N   . ILE A 1 1565 ? 134.728 130.026 91.765  1.00 24.76  ? 1136 ILE A N   1 
ATOM   9001  C  CA  . ILE A 1 1565 ? 135.445 128.979 91.072  1.00 29.70  ? 1136 ILE A CA  1 
ATOM   9002  C  C   . ILE A 1 1565 ? 135.984 129.483 89.754  1.00 36.89  ? 1136 ILE A C   1 
ATOM   9003  O  O   . ILE A 1 1565 ? 137.073 129.082 89.324  1.00 45.91  ? 1136 ILE A O   1 
ATOM   9004  C  CB  . ILE A 1 1565 ? 134.596 127.717 90.911  1.00 43.42  ? 1136 ILE A CB  1 
ATOM   9005  C  CG1 . ILE A 1 1565 ? 134.304 127.149 92.299  1.00 54.45  ? 1136 ILE A CG1 1 
ATOM   9006  C  CG2 . ILE A 1 1565 ? 135.285 126.700 89.991  1.00 51.59  ? 1136 ILE A CG2 1 
ATOM   9007  C  CD1 . ILE A 1 1565 ? 133.484 125.888 92.268  1.00 58.72  ? 1136 ILE A CD1 1 
ATOM   9008  N  N   . GLU A 1 1566 ? 135.265 130.365 89.092  1.00 34.54  ? 1137 GLU A N   1 
ATOM   9009  C  CA  . GLU A 1 1566 ? 135.820 130.892 87.855  1.00 37.60  ? 1137 GLU A CA  1 
ATOM   9010  C  C   . GLU A 1 1566 ? 136.779 132.035 88.113  1.00 39.21  ? 1137 GLU A C   1 
ATOM   9011  O  O   . GLU A 1 1566 ? 137.652 132.312 87.285  1.00 43.98  ? 1137 GLU A O   1 
ATOM   9012  C  CB  . GLU A 1 1566 ? 134.687 131.333 86.941  1.00 47.26  ? 1137 GLU A CB  1 
ATOM   9013  C  CG  . GLU A 1 1566 ? 133.944 132.541 87.475  1.00 55.49  ? 1137 GLU A CG  1 
ATOM   9014  C  CD  . GLU A 1 1566 ? 132.840 132.998 86.540  1.00 65.96  ? 1137 GLU A CD  1 
ATOM   9015  O  OE1 . GLU A 1 1566 ? 132.521 132.240 85.586  1.00 60.10  ? 1137 GLU A OE1 1 
ATOM   9016  O  OE2 . GLU A 1 1566 ? 132.266 134.088 86.782  1.00 63.08  ? 1137 GLU A OE2 1 
ATOM   9017  N  N   . GLN A 1 1567 ? 136.640 132.696 89.253  1.00 42.74  ? 1138 GLN A N   1 
ATOM   9018  C  CA  . GLN A 1 1567 ? 137.479 133.843 89.541  1.00 36.52  ? 1138 GLN A CA  1 
ATOM   9019  C  C   . GLN A 1 1567 ? 138.910 133.411 89.746  1.00 28.90  ? 1138 GLN A C   1 
ATOM   9020  O  O   . GLN A 1 1567 ? 139.830 134.043 89.233  1.00 44.00  ? 1138 GLN A O   1 
ATOM   9021  C  CB  . GLN A 1 1567 ? 136.927 134.567 90.762  1.00 35.96  ? 1138 GLN A CB  1 
ATOM   9022  C  CG  . GLN A 1 1567 ? 137.600 135.830 91.123  1.00 39.65  ? 1138 GLN A CG  1 
ATOM   9023  C  CD  . GLN A 1 1567 ? 136.857 136.505 92.238  1.00 41.51  ? 1138 GLN A CD  1 
ATOM   9024  O  OE1 . GLN A 1 1567 ? 136.056 135.877 92.927  1.00 37.15  ? 1138 GLN A OE1 1 
ATOM   9025  N  NE2 . GLN A 1 1567 ? 137.118 137.784 92.434  1.00 52.55  ? 1138 GLN A NE2 1 
ATOM   9026  N  N   . PHE A 1 1568 ? 139.115 132.319 90.435  1.00 23.39  ? 1139 PHE A N   1 
ATOM   9027  C  CA  . PHE A 1 1568 ? 140.443 131.873 90.754  1.00 25.09  ? 1139 PHE A CA  1 
ATOM   9028  C  C   . PHE A 1 1568 ? 140.723 130.545 90.097  1.00 34.56  ? 1139 PHE A C   1 
ATOM   9029  O  O   . PHE A 1 1568 ? 139.963 129.588 90.273  1.00 40.57  ? 1139 PHE A O   1 
ATOM   9030  C  CB  . PHE A 1 1568 ? 140.589 131.716 92.238  1.00 34.54  ? 1139 PHE A CB  1 
ATOM   9031  C  CG  . PHE A 1 1568 ? 140.589 132.992 92.967  1.00 39.13  ? 1139 PHE A CG  1 
ATOM   9032  C  CD1 . PHE A 1 1568 ? 141.761 133.666 93.193  1.00 39.38  ? 1139 PHE A CD1 1 
ATOM   9033  C  CD2 . PHE A 1 1568 ? 139.417 133.522 93.433  1.00 47.33  ? 1139 PHE A CD2 1 
ATOM   9034  C  CE1 . PHE A 1 1568 ? 141.768 134.836 93.880  1.00 48.41  ? 1139 PHE A CE1 1 
ATOM   9035  C  CE2 . PHE A 1 1568 ? 139.413 134.706 94.122  1.00 50.72  ? 1139 PHE A CE2 1 
ATOM   9036  C  CZ  . PHE A 1 1568 ? 140.595 135.364 94.347  1.00 52.43  ? 1139 PHE A CZ  1 
ATOM   9037  N  N   . LYS A 1 1569 ? 141.839 130.471 89.401  1.00 29.83  ? 1140 LYS A N   1 
ATOM   9038  C  CA  . LYS A 1 1569 ? 142.302 129.235 88.806  1.00 26.68  ? 1140 LYS A CA  1 
ATOM   9039  C  C   . LYS A 1 1569 ? 143.501 128.708 89.577  1.00 38.12  ? 1140 LYS A C   1 
ATOM   9040  O  O   . LYS A 1 1569 ? 144.372 129.488 89.974  1.00 44.91  ? 1140 LYS A O   1 
ATOM   9041  C  CB  . LYS A 1 1569 ? 142.665 129.465 87.355  1.00 34.44  ? 1140 LYS A CB  1 
ATOM   9042  C  CG  . LYS A 1 1569 ? 143.073 128.212 86.671  1.00 49.08  ? 1140 LYS A CG  1 
ATOM   9043  C  CD  . LYS A 1 1569 ? 143.339 128.464 85.200  1.00 68.53  ? 1140 LYS A CD  1 
ATOM   9044  C  CE  . LYS A 1 1569 ? 143.838 127.188 84.519  1.00 79.71  ? 1140 LYS A CE  1 
ATOM   9045  N  NZ  . LYS A 1 1569 ? 142.940 126.007 84.678  1.00 76.07  ? 1140 LYS A NZ  1 
ATOM   9046  N  N   . VAL A 1 1570 ? 143.567 127.380 89.766  1.00 39.31  ? 1141 VAL A N   1 
ATOM   9047  C  CA  . VAL A 1 1570 ? 144.518 126.745 90.689  1.00 30.68  ? 1141 VAL A CA  1 
ATOM   9048  C  C   . VAL A 1 1570 ? 145.737 126.248 89.951  1.00 28.24  ? 1141 VAL A C   1 
ATOM   9049  O  O   . VAL A 1 1570 ? 145.619 125.432 89.033  1.00 42.40  ? 1141 VAL A O   1 
ATOM   9050  C  CB  . VAL A 1 1570 ? 143.883 125.568 91.437  1.00 39.46  ? 1141 VAL A CB  1 
ATOM   9051  C  CG1 . VAL A 1 1570 ? 144.907 124.987 92.390  1.00 44.01  ? 1141 VAL A CG1 1 
ATOM   9052  C  CG2 . VAL A 1 1570 ? 142.653 126.027 92.196  1.00 50.62  ? 1141 VAL A CG2 1 
ATOM   9053  N  N   . PHE A 1 1571 ? 146.906 126.651 90.409  1.00 29.70  ? 1142 PHE A N   1 
ATOM   9054  C  CA  . PHE A 1 1571 ? 148.164 126.162 89.867  1.00 36.22  ? 1142 PHE A CA  1 
ATOM   9055  C  C   . PHE A 1 1571 ? 148.976 125.480 90.953  1.00 44.87  ? 1142 PHE A C   1 
ATOM   9056  O  O   . PHE A 1 1571 ? 149.586 126.158 91.790  1.00 49.16  ? 1142 PHE A O   1 
ATOM   9057  C  CB  . PHE A 1 1571 ? 148.936 127.293 89.274  1.00 38.73  ? 1142 PHE A CB  1 
ATOM   9058  C  CG  . PHE A 1 1571 ? 148.376 127.748 88.018  1.00 38.03  ? 1142 PHE A CG  1 
ATOM   9059  C  CD1 . PHE A 1 1571 ? 147.358 128.655 88.013  1.00 41.97  ? 1142 PHE A CD1 1 
ATOM   9060  C  CD2 . PHE A 1 1571 ? 148.833 127.226 86.828  1.00 48.91  ? 1142 PHE A CD2 1 
ATOM   9061  C  CE1 . PHE A 1 1571 ? 146.818 129.076 86.829  1.00 54.53  ? 1142 PHE A CE1 1 
ATOM   9062  C  CE2 . PHE A 1 1571 ? 148.306 127.635 85.640  1.00 59.49  ? 1142 PHE A CE2 1 
ATOM   9063  C  CZ  . PHE A 1 1571 ? 147.290 128.563 85.634  1.00 62.12  ? 1142 PHE A CZ  1 
ATOM   9064  N  N   . TRP A 1 1572 ? 148.963 124.146 90.948  1.00 42.60  ? 1143 TRP A N   1 
ATOM   9065  C  CA  . TRP A 1 1572 ? 149.739 123.397 91.918  1.00 42.75  ? 1143 TRP A CA  1 
ATOM   9066  C  C   . TRP A 1 1572 ? 151.194 123.422 91.521  1.00 49.57  ? 1143 TRP A C   1 
ATOM   9067  O  O   . TRP A 1 1572 ? 151.535 123.619 90.353  1.00 53.14  ? 1143 TRP A O   1 
ATOM   9068  C  CB  . TRP A 1 1572 ? 149.314 121.949 91.996  1.00 39.35  ? 1143 TRP A CB  1 
ATOM   9069  C  CG  . TRP A 1 1572 ? 147.936 121.777 92.161  1.00 29.03  ? 1143 TRP A CG  1 
ATOM   9070  C  CD1 . TRP A 1 1572 ? 147.023 121.672 91.197  1.00 36.35  ? 1143 TRP A CD1 1 
ATOM   9071  C  CD2 . TRP A 1 1572 ? 147.266 121.689 93.373  1.00 22.49  ? 1143 TRP A CD2 1 
ATOM   9072  N  NE1 . TRP A 1 1572 ? 145.792 121.508 91.734  1.00 34.18  ? 1143 TRP A NE1 1 
ATOM   9073  C  CE2 . TRP A 1 1572 ? 145.924 121.521 93.088  1.00 24.45  ? 1143 TRP A CE2 1 
ATOM   9074  C  CE3 . TRP A 1 1572 ? 147.674 121.739 94.685  1.00 42.55  ? 1143 TRP A CE3 1 
ATOM   9075  C  CZ2 . TRP A 1 1572 ? 144.978 121.394 94.057  1.00 42.96  ? 1143 TRP A CZ2 1 
ATOM   9076  C  CZ3 . TRP A 1 1572 ? 146.743 121.616 95.657  1.00 56.16  ? 1143 TRP A CZ3 1 
ATOM   9077  C  CH2 . TRP A 1 1572 ? 145.402 121.437 95.344  1.00 54.73  ? 1143 TRP A CH2 1 
ATOM   9078  N  N   . LEU A 1 1573 ? 152.059 123.186 92.497  1.00 45.31  ? 1144 LEU A N   1 
ATOM   9079  C  CA  . LEU A 1 1573 ? 153.480 123.272 92.242  1.00 43.61  ? 1144 LEU A CA  1 
ATOM   9080  C  C   . LEU A 1 1573 ? 154.198 122.122 92.915  1.00 54.52  ? 1144 LEU A C   1 
ATOM   9081  O  O   . LEU A 1 1573 ? 153.939 121.827 94.084  1.00 61.88  ? 1144 LEU A O   1 
ATOM   9082  C  CB  . LEU A 1 1573 ? 154.019 124.592 92.761  1.00 50.91  ? 1144 LEU A CB  1 
ATOM   9083  C  CG  . LEU A 1 1573 ? 153.531 125.747 91.909  1.00 57.49  ? 1144 LEU A CG  1 
ATOM   9084  C  CD1 . LEU A 1 1573 ? 154.107 127.077 92.398  1.00 65.72  ? 1144 LEU A CD1 1 
ATOM   9085  C  CD2 . LEU A 1 1573 ? 153.937 125.439 90.487  1.00 68.14  ? 1144 LEU A CD2 1 
ATOM   9086  N  N   . LYS A 1 1574 ? 155.095 121.480 92.183  1.00 53.44  ? 1145 LYS A N   1 
ATOM   9087  C  CA  . LYS A 1 1574 ? 156.045 120.586 92.812  1.00 55.24  ? 1145 LYS A CA  1 
ATOM   9088  C  C   . LYS A 1 1574 ? 157.136 121.399 93.518  1.00 60.47  ? 1145 LYS A C   1 
ATOM   9089  O  O   . LYS A 1 1574 ? 157.444 122.521 93.103  1.00 66.06  ? 1145 LYS A O   1 
ATOM   9090  C  CB  . LYS A 1 1574 ? 156.638 119.665 91.759  1.00 60.96  ? 1145 LYS A CB  1 
ATOM   9091  C  CG  . LYS A 1 1574 ? 155.573 118.797 91.083  1.00 65.62  ? 1145 LYS A CG  1 
ATOM   9092  C  CD  . LYS A 1 1574 ? 156.168 117.867 90.018  1.00 75.67  ? 1145 LYS A CD  1 
ATOM   9093  C  CE  . LYS A 1 1574 ? 155.120 116.925 89.397  1.00 78.98  ? 1145 LYS A CE  1 
ATOM   9094  N  NZ  . LYS A 1 1574 ? 153.974 117.629 88.746  1.00 77.27  ? 1145 LYS A NZ  1 
ATOM   9095  N  N   . PRO A 1 1575 ? 157.726 120.869 94.594  1.00 53.81  ? 1146 PRO A N   1 
ATOM   9096  C  CA  . PRO A 1 1575 ? 158.726 121.646 95.331  1.00 53.64  ? 1146 PRO A CA  1 
ATOM   9097  C  C   . PRO A 1 1575 ? 159.854 122.057 94.416  1.00 57.77  ? 1146 PRO A C   1 
ATOM   9098  O  O   . PRO A 1 1575 ? 160.201 121.345 93.474  1.00 62.91  ? 1146 PRO A O   1 
ATOM   9099  C  CB  . PRO A 1 1575 ? 159.210 120.677 96.409  1.00 51.53  ? 1146 PRO A CB  1 
ATOM   9100  C  CG  . PRO A 1 1575 ? 158.071 119.765 96.604  1.00 51.42  ? 1146 PRO A CG  1 
ATOM   9101  C  CD  . PRO A 1 1575 ? 157.483 119.571 95.235  1.00 55.83  ? 1146 PRO A CD  1 
ATOM   9102  N  N   . TYR A 1 1576 ? 160.383 123.242 94.666  1.00 58.38  ? 1147 TYR A N   1 
ATOM   9103  C  CA  . TYR A 1 1576 ? 161.459 123.786 93.853  1.00 68.91  ? 1147 TYR A CA  1 
ATOM   9104  C  C   . TYR A 1 1576 ? 160.993 123.978 92.422  1.00 75.96  ? 1147 TYR A C   1 
ATOM   9105  O  O   . TYR A 1 1576 ? 161.679 123.596 91.472  1.00 81.43  ? 1147 TYR A O   1 
ATOM   9106  C  CB  . TYR A 1 1576 ? 162.691 122.889 93.866  1.00 67.50  ? 1147 TYR A CB  1 
ATOM   9107  C  CG  . TYR A 1 1576 ? 163.209 122.667 95.223  1.00 71.37  ? 1147 TYR A CG  1 
ATOM   9108  C  CD1 . TYR A 1 1576 ? 162.897 123.545 96.247  1.00 77.29  ? 1147 TYR A CD1 1 
ATOM   9109  C  CD2 . TYR A 1 1576 ? 164.008 121.579 95.495  1.00 81.51  ? 1147 TYR A CD2 1 
ATOM   9110  C  CE1 . TYR A 1 1576 ? 163.368 123.345 97.517  1.00 90.91  ? 1147 TYR A CE1 1 
ATOM   9111  C  CE2 . TYR A 1 1576 ? 164.493 121.361 96.761  1.00 92.36  ? 1147 TYR A CE2 1 
ATOM   9112  C  CZ  . TYR A 1 1576 ? 164.171 122.249 97.775  1.00 98.11  ? 1147 TYR A CZ  1 
ATOM   9113  O  OH  . TYR A 1 1576 ? 164.652 122.041 99.051  1.00 101.38 ? 1147 TYR A OH  1 
ATOM   9114  N  N   . GLU A 1 1577 ? 159.803 124.543 92.269  1.00 75.25  ? 1148 GLU A N   1 
ATOM   9115  C  CA  . GLU A 1 1577 ? 159.356 124.943 90.943  1.00 85.98  ? 1148 GLU A CA  1 
ATOM   9116  C  C   . GLU A 1 1577 ? 158.454 126.161 91.057  1.00 87.88  ? 1148 GLU A C   1 
ATOM   9117  O  O   . GLU A 1 1577 ? 157.769 126.351 92.066  1.00 85.75  ? 1148 GLU A O   1 
ATOM   9118  C  CB  . GLU A 1 1577 ? 158.624 123.806 90.214  1.00 90.41  ? 1148 GLU A CB  1 
ATOM   9119  C  CG  . GLU A 1 1577 ? 159.543 122.843 89.456  1.00 99.28  ? 1148 GLU A CG  1 
ATOM   9120  C  CD  . GLU A 1 1577 ? 160.168 123.473 88.202  1.00 105.25 ? 1148 GLU A CD  1 
ATOM   9121  O  OE1 . GLU A 1 1577 ? 161.006 122.805 87.557  1.00 102.14 ? 1148 GLU A OE1 1 
ATOM   9122  O  OE2 . GLU A 1 1577 ? 159.839 124.639 87.871  1.00 98.91  ? 1148 GLU A OE2 1 
ATOM   9123  N  N   . GLN A 1 1578 ? 158.458 126.986 90.015  1.00 82.22  ? 1149 GLN A N   1 
ATOM   9124  C  CA  . GLN A 1 1578 ? 157.620 128.175 89.970  1.00 82.28  ? 1149 GLN A CA  1 
ATOM   9125  C  C   . GLN A 1 1578 ? 156.446 127.961 89.017  1.00 86.61  ? 1149 GLN A C   1 
ATOM   9126  O  O   . GLN A 1 1578 ? 156.561 127.252 88.011  1.00 90.84  ? 1149 GLN A O   1 
ATOM   9127  C  CB  . GLN A 1 1578 ? 158.451 129.394 89.557  1.00 86.35  ? 1149 GLN A CB  1 
ATOM   9128  C  CG  . GLN A 1 1578 ? 159.068 129.318 88.156  1.00 95.63  ? 1149 GLN A CG  1 
ATOM   9129  C  CD  . GLN A 1 1578 ? 160.323 128.452 88.102  1.00 88.91  ? 1149 GLN A CD  1 
ATOM   9130  O  OE1 . GLN A 1 1578 ? 160.634 127.728 89.049  1.00 86.33  ? 1149 GLN A OE1 1 
ATOM   9131  N  NE2 . GLN A 1 1578 ? 161.050 128.533 86.993  1.00 87.54  ? 1149 GLN A NE2 1 
ATOM   9132  N  N   . CYS A 1 1579 ? 155.285 128.562 89.362  1.00 74.55  ? 1150 CYS A N   1 
ATOM   9133  C  CA  . CYS A 1 1579 ? 154.106 128.307 88.546  1.00 67.26  ? 1150 CYS A CA  1 
ATOM   9134  C  C   . CYS A 1 1579 ? 154.142 129.133 87.265  1.00 69.98  ? 1150 CYS A C   1 
ATOM   9135  O  O   . CYS A 1 1579 ? 154.691 130.235 87.245  1.00 83.52  ? 1150 CYS A O   1 
ATOM   9136  C  CB  . CYS A 1 1579 ? 152.835 128.583 89.348  1.00 62.11  ? 1150 CYS A CB  1 
ATOM   9137  S  SG  . CYS A 1 1579 ? 152.302 130.269 89.437  1.00 50.25  ? 1150 CYS A SG  1 
ATOM   9138  N  N   . PRO A 1 1580 ? 153.602 128.599 86.173  1.00 66.45  ? 1151 PRO A N   1 
ATOM   9139  C  CA  . PRO A 1 1580 ? 153.702 129.309 84.892  1.00 73.34  ? 1151 PRO A CA  1 
ATOM   9140  C  C   . PRO A 1 1580 ? 153.083 130.686 84.922  1.00 84.79  ? 1151 PRO A C   1 
ATOM   9141  O  O   . PRO A 1 1580 ? 153.571 131.578 84.218  1.00 96.44  ? 1151 PRO A O   1 
ATOM   9142  C  CB  . PRO A 1 1580 ? 152.964 128.387 83.912  1.00 81.38  ? 1151 PRO A CB  1 
ATOM   9143  C  CG  . PRO A 1 1580 ? 153.027 127.051 84.535  1.00 92.37  ? 1151 PRO A CG  1 
ATOM   9144  C  CD  . PRO A 1 1580 ? 152.984 127.277 86.026  1.00 82.72  ? 1151 PRO A CD  1 
ATOM   9145  N  N   . GLN A 1 1581 ? 152.023 130.899 85.703  1.00 78.61  ? 1152 GLN A N   1 
ATOM   9146  C  CA  . GLN A 1 1581 ? 151.438 132.234 85.758  1.00 79.43  ? 1152 GLN A CA  1 
ATOM   9147  C  C   . GLN A 1 1581 ? 152.434 133.234 86.307  1.00 81.88  ? 1152 GLN A C   1 
ATOM   9148  O  O   . GLN A 1 1581 ? 152.521 134.371 85.827  1.00 95.52  ? 1152 GLN A O   1 
ATOM   9149  C  CB  . GLN A 1 1581 ? 150.165 132.242 86.605  1.00 75.48  ? 1152 GLN A CB  1 
ATOM   9150  C  CG  . GLN A 1 1581 ? 149.063 131.404 86.019  1.00 71.57  ? 1152 GLN A CG  1 
ATOM   9151  C  CD  . GLN A 1 1581 ? 148.678 131.861 84.623  1.00 82.59  ? 1152 GLN A CD  1 
ATOM   9152  O  OE1 . GLN A 1 1581 ? 148.458 131.038 83.732  1.00 80.42  ? 1152 GLN A OE1 1 
ATOM   9153  N  NE2 . GLN A 1 1581 ? 148.588 133.180 84.425  1.00 89.88  ? 1152 GLN A NE2 1 
ATOM   9154  N  N   . CYS A 1 1582 ? 153.188 132.834 87.319  1.00 73.48  ? 1153 CYS A N   1 
ATOM   9155  C  CA  . CYS A 1 1582 ? 154.136 133.758 87.902  1.00 78.98  ? 1153 CYS A CA  1 
ATOM   9156  C  C   . CYS A 1 1582 ? 155.351 133.989 87.004  1.00 102.77 ? 1153 CYS A C   1 
ATOM   9157  O  O   . CYS A 1 1582 ? 156.029 135.013 87.161  1.00 108.87 ? 1153 CYS A O   1 
ATOM   9158  C  CB  . CYS A 1 1582 ? 154.533 133.254 89.280  1.00 75.46  ? 1153 CYS A CB  1 
ATOM   9159  S  SG  . CYS A 1 1582 ? 153.314 133.712 90.520  1.00 79.12  ? 1153 CYS A SG  1 
ATOM   9160  N  N   . SER A 1 1583 ? 155.629 133.085 86.049  1.00 100.87 ? 1154 SER A N   1 
ATOM   9161  C  CA  . SER A 1 1583 ? 156.764 133.222 85.130  1.00 108.07 ? 1154 SER A CA  1 
ATOM   9162  C  C   . SER A 1 1583 ? 156.426 134.010 83.855  1.00 115.02 ? 1154 SER A C   1 
ATOM   9163  O  O   . SER A 1 1583 ? 157.273 134.763 83.360  1.00 116.79 ? 1154 SER A O   1 
ATOM   9164  C  CB  . SER A 1 1583 ? 157.321 131.837 84.757  1.00 98.84  ? 1154 SER A CB  1 
ATOM   9165  O  OG  . SER A 1 1583 ? 156.375 131.056 84.046  1.00 100.51 ? 1154 SER A OG  1 
ATOM   9166  N  N   . ASN A 1 1584 ? 155.213 133.849 83.303  1.00 117.78 ? 1155 ASN A N   1 
ATOM   9167  C  CA  . ASN A 1 1584 ? 154.823 134.575 82.086  1.00 130.25 ? 1155 ASN A CA  1 
ATOM   9168  C  C   . ASN A 1 1584 ? 154.723 136.082 82.336  1.00 137.01 ? 1155 ASN A C   1 
ATOM   9169  O  O   . ASN A 1 1584 ? 155.115 136.888 81.479  1.00 136.64 ? 1155 ASN A O   1 
ATOM   9170  C  CB  . ASN A 1 1584 ? 153.492 134.015 81.546  1.00 126.30 ? 1155 ASN A CB  1 
ATOM   9171  C  CG  . ASN A 1 1584 ? 153.152 134.507 80.124  1.00 127.62 ? 1155 ASN A CG  1 
ATOM   9172  O  OD1 . ASN A 1 1584 ? 154.010 135.022 79.402  1.00 125.76 ? 1155 ASN A OD1 1 
ATOM   9173  N  ND2 . ASN A 1 1584 ? 151.888 134.339 79.727  1.00 119.31 ? 1155 ASN A ND2 1 
ATOM   9174  N  N   . ALA A 1 1585 ? 154.190 136.479 83.497  1.00 133.44 ? 1156 ALA A N   1 
ATOM   9175  C  CA  . ALA A 1 1585 ? 154.042 137.891 83.850  1.00 141.51 ? 1156 ALA A CA  1 
ATOM   9176  C  C   . ALA A 1 1585 ? 155.412 138.532 84.061  1.00 148.18 ? 1156 ALA A C   1 
ATOM   9177  O  O   . ALA A 1 1585 ? 156.175 138.097 84.935  1.00 139.81 ? 1156 ALA A O   1 
ATOM   9178  C  CB  . ALA A 1 1585 ? 153.193 138.024 85.115  1.00 131.99 ? 1156 ALA A CB  1 
ATOM   9179  N  N   . LYS A 1 1586 ? 155.740 139.555 83.254  1.00 152.83 ? 1157 LYS A N   1 
ATOM   9180  C  CA  . LYS A 1 1586 ? 157.026 140.221 83.441  1.00 154.13 ? 1157 LYS A CA  1 
ATOM   9181  C  C   . LYS A 1 1586 ? 157.050 140.944 84.792  1.00 156.42 ? 1157 LYS A C   1 
ATOM   9182  O  O   . LYS A 1 1586 ? 157.661 140.444 85.746  1.00 152.14 ? 1157 LYS A O   1 
ATOM   9183  C  CB  . LYS A 1 1586 ? 157.305 141.205 82.286  1.00 147.02 ? 1157 LYS A CB  1 
ATOM   9184  C  CG  . LYS A 1 1586 ? 157.188 140.614 80.865  1.00 137.50 ? 1157 LYS A CG  1 
ATOM   9185  C  CD  . LYS A 1 1586 ? 157.462 141.670 79.785  1.00 129.69 ? 1157 LYS A CD  1 
ATOM   9186  C  CE  . LYS A 1 1586 ? 157.266 141.105 78.379  1.00 120.31 ? 1157 LYS A CE  1 
ATOM   9187  N  NZ  . LYS A 1 1586 ? 155.871 140.610 78.177  1.00 111.01 ? 1157 LYS A NZ  1 
ATOM   9188  N  N   . GLN A 1 1587 ? 156.398 142.130 84.897  1.00 159.54 ? 1158 GLN A N   1 
ATOM   9189  C  CA  . GLN A 1 1587 ? 155.947 142.682 86.179  1.00 159.48 ? 1158 GLN A CA  1 
ATOM   9190  C  C   . GLN A 1 1587 ? 154.468 142.384 86.485  1.00 157.10 ? 1158 GLN A C   1 
ATOM   9191  O  O   . GLN A 1 1587 ? 154.177 141.695 87.476  1.00 147.43 ? 1158 GLN A O   1 
ATOM   9192  C  CB  . GLN A 1 1587 ? 156.221 144.198 86.253  1.00 155.02 ? 1158 GLN A CB  1 
ATOM   9193  C  CG  . GLN A 1 1587 ? 157.635 144.647 85.826  1.00 150.31 ? 1158 GLN A CG  1 
ATOM   9194  C  CD  . GLN A 1 1587 ? 157.762 144.874 84.311  1.00 146.40 ? 1158 GLN A CD  1 
ATOM   9195  O  OE1 . GLN A 1 1587 ? 156.782 144.755 83.565  1.00 146.88 ? 1158 GLN A OE1 1 
ATOM   9196  N  NE2 . GLN A 1 1587 ? 158.973 145.190 83.858  1.00 137.42 ? 1158 GLN A NE2 1 
ATOM   9197  N  N   . PRO A 1 1588 ? 153.472 142.888 85.633  1.00 160.00 ? 1159 PRO A N   1 
ATOM   9198  C  CA  . PRO A 1 1588 ? 152.063 142.917 86.080  1.00 156.14 ? 1159 PRO A CA  1 
ATOM   9199  C  C   . PRO A 1 1588 ? 151.103 141.836 85.558  1.00 147.32 ? 1159 PRO A C   1 
ATOM   9200  O  O   . PRO A 1 1588 ? 149.973 141.761 86.055  1.00 138.83 ? 1159 PRO A O   1 
ATOM   9201  C  CB  . PRO A 1 1588 ? 151.603 144.312 85.614  1.00 150.01 ? 1159 PRO A CB  1 
ATOM   9202  C  CG  . PRO A 1 1588 ? 152.493 144.633 84.379  1.00 145.21 ? 1159 PRO A CG  1 
ATOM   9203  C  CD  . PRO A 1 1588 ? 153.594 143.563 84.321  1.00 154.51 ? 1159 PRO A CD  1 
ATOM   9204  N  N   . GLY A 1 1589 ? 151.509 141.008 84.586  1.00 144.69 ? 1160 GLY A N   1 
ATOM   9205  C  CA  . GLY A 1 1589 ? 150.581 140.191 83.805  1.00 135.82 ? 1160 GLY A CA  1 
ATOM   9206  C  C   . GLY A 1 1589 ? 149.539 139.347 84.529  1.00 132.59 ? 1160 GLY A C   1 
ATOM   9207  O  O   . GLY A 1 1589 ? 148.342 139.649 84.458  1.00 125.83 ? 1160 GLY A O   1 
ATOM   9208  N  N   . GLY A 1 1590 ? 149.972 138.287 85.219  1.00 124.25 ? 1161 GLY A N   1 
ATOM   9209  C  CA  . GLY A 1 1590 ? 149.069 137.434 85.971  1.00 109.67 ? 1161 GLY A CA  1 
ATOM   9210  C  C   . GLY A 1 1590 ? 149.489 137.366 87.420  1.00 81.29  ? 1161 GLY A C   1 
ATOM   9211  O  O   . GLY A 1 1590 ? 149.233 136.383 88.120  1.00 74.16  ? 1161 GLY A O   1 
ATOM   9212  N  N   . LYS A 1 1591 ? 150.090 138.452 87.887  1.00 80.26  ? 1162 LYS A N   1 
ATOM   9213  C  CA  . LYS A 1 1591 ? 150.762 138.407 89.176  1.00 82.31  ? 1162 LYS A CA  1 
ATOM   9214  C  C   . LYS A 1 1591 ? 149.861 138.001 90.334  1.00 63.70  ? 1162 LYS A C   1 
ATOM   9215  O  O   . LYS A 1 1591 ? 150.310 137.196 91.167  1.00 73.37  ? 1162 LYS A O   1 
ATOM   9216  C  CB  . LYS A 1 1591 ? 151.463 139.752 89.444  1.00 104.17 ? 1162 LYS A CB  1 
ATOM   9217  C  CG  . LYS A 1 1591 ? 150.588 141.010 89.546  1.00 106.18 ? 1162 LYS A CG  1 
ATOM   9218  C  CD  . LYS A 1 1591 ? 151.416 142.200 90.105  1.00 120.91 ? 1162 LYS A CD  1 
ATOM   9219  C  CE  . LYS A 1 1591 ? 150.561 143.451 90.367  1.00 125.63 ? 1162 LYS A CE  1 
ATOM   9220  N  NZ  . LYS A 1 1591 ? 151.328 144.586 90.982  1.00 114.64 ? 1162 LYS A NZ  1 
ATOM   9221  N  N   . PRO A 1 1592 ? 148.644 138.479 90.468  1.00 35.67  ? 1163 PRO A N   1 
ATOM   9222  C  CA  . PRO A 1 1592 ? 148.007 138.409 91.774  1.00 39.88  ? 1163 PRO A CA  1 
ATOM   9223  C  C   . PRO A 1 1592 ? 147.478 137.016 92.023  1.00 42.09  ? 1163 PRO A C   1 
ATOM   9224  O  O   . PRO A 1 1592 ? 146.943 136.380 91.116  1.00 50.43  ? 1163 PRO A O   1 
ATOM   9225  C  CB  . PRO A 1 1592 ? 146.882 139.432 91.663  1.00 51.85  ? 1163 PRO A CB  1 
ATOM   9226  C  CG  . PRO A 1 1592 ? 146.658 139.579 90.204  1.00 66.29  ? 1163 PRO A CG  1 
ATOM   9227  C  CD  . PRO A 1 1592 ? 147.691 138.854 89.440  1.00 43.14  ? 1163 PRO A CD  1 
ATOM   9228  N  N   . PHE A 1 1593 ? 147.658 136.528 93.259  1.00 47.71  ? 1164 PHE A N   1 
ATOM   9229  C  CA  . PHE A 1 1593 ? 147.299 135.152 93.607  1.00 41.71  ? 1164 PHE A CA  1 
ATOM   9230  C  C   . PHE A 1 1593 ? 147.236 134.962 95.111  1.00 37.04  ? 1164 PHE A C   1 
ATOM   9231  O  O   . PHE A 1 1593 ? 147.771 135.757 95.880  1.00 55.13  ? 1164 PHE A O   1 
ATOM   9232  C  CB  . PHE A 1 1593 ? 148.311 134.159 93.073  1.00 47.50  ? 1164 PHE A CB  1 
ATOM   9233  C  CG  . PHE A 1 1593 ? 149.646 134.222 93.758  1.00 49.76  ? 1164 PHE A CG  1 
ATOM   9234  C  CD1 . PHE A 1 1593 ? 149.936 133.362 94.803  1.00 54.84  ? 1164 PHE A CD1 1 
ATOM   9235  C  CD2 . PHE A 1 1593 ? 150.622 135.117 93.346  1.00 56.67  ? 1164 PHE A CD2 1 
ATOM   9236  C  CE1 . PHE A 1 1593 ? 151.179 133.396 95.425  1.00 61.15  ? 1164 PHE A CE1 1 
ATOM   9237  C  CE2 . PHE A 1 1593 ? 151.867 135.159 93.968  1.00 59.79  ? 1164 PHE A CE2 1 
ATOM   9238  C  CZ  . PHE A 1 1593 ? 152.146 134.293 95.007  1.00 59.62  ? 1164 PHE A CZ  1 
ATOM   9239  N  N   . VAL A 1 1594 ? 146.644 133.850 95.513  1.00 25.84  ? 1165 VAL A N   1 
ATOM   9240  C  CA  . VAL A 1 1594 ? 146.612 133.434 96.906  1.00 28.73  ? 1165 VAL A CA  1 
ATOM   9241  C  C   . VAL A 1 1594 ? 147.537 132.248 97.086  1.00 40.11  ? 1165 VAL A C   1 
ATOM   9242  O  O   . VAL A 1 1594 ? 147.385 131.230 96.403  1.00 50.06  ? 1165 VAL A O   1 
ATOM   9243  C  CB  . VAL A 1 1594 ? 145.197 133.061 97.345  1.00 32.69  ? 1165 VAL A CB  1 
ATOM   9244  C  CG1 . VAL A 1 1594 ? 145.238 132.449 98.730  1.00 38.25  ? 1165 VAL A CG1 1 
ATOM   9245  C  CG2 . VAL A 1 1594 ? 144.343 134.291 97.324  1.00 49.62  ? 1165 VAL A CG2 1 
ATOM   9246  N  N   . SER A 1 1595 ? 148.481 132.356 98.009  1.00 41.39  ? 1166 SER A N   1 
ATOM   9247  C  CA  . SER A 1 1595 ? 149.496 131.326 98.163  1.00 33.12  ? 1166 SER A CA  1 
ATOM   9248  C  C   . SER A 1 1595 ? 149.102 130.382 99.281  1.00 40.12  ? 1166 SER A C   1 
ATOM   9249  O  O   . SER A 1 1595 ? 148.785 130.825 100.384 1.00 48.81  ? 1166 SER A O   1 
ATOM   9250  C  CB  . SER A 1 1595 ? 150.854 131.941 98.474  1.00 41.87  ? 1166 SER A CB  1 
ATOM   9251  O  OG  . SER A 1 1595 ? 151.782 130.919 98.782  1.00 50.95  ? 1166 SER A OG  1 
ATOM   9252  N  N   . VAL A 1 1596 ? 149.144 129.089 99.013  1.00 43.09  ? 1167 VAL A N   1 
ATOM   9253  C  CA  . VAL A 1 1596 ? 148.870 128.078 100.020 1.00 41.43  ? 1167 VAL A CA  1 
ATOM   9254  C  C   . VAL A 1 1596 ? 150.077 127.158 100.078 1.00 55.10  ? 1167 VAL A C   1 
ATOM   9255  O  O   . VAL A 1 1596 ? 150.662 126.823 99.043  1.00 53.30  ? 1167 VAL A O   1 
ATOM   9256  C  CB  . VAL A 1 1596 ? 147.590 127.287 99.702  1.00 40.96  ? 1167 VAL A CB  1 
ATOM   9257  C  CG1 . VAL A 1 1596 ? 147.228 126.397 100.875 1.00 49.11  ? 1167 VAL A CG1 1 
ATOM   9258  C  CG2 . VAL A 1 1596 ? 146.469 128.232 99.371  1.00 46.12  ? 1167 VAL A CG2 1 
ATOM   9259  N  N   . ALA A 1 1597 ? 150.474 126.776 101.284 1.00 51.97  ? 1168 ALA A N   1 
ATOM   9260  C  CA  . ALA A 1 1597 ? 151.598 125.865 101.428 1.00 49.38  ? 1168 ALA A CA  1 
ATOM   9261  C  C   . ALA A 1 1597 ? 151.327 124.924 102.590 1.00 52.40  ? 1168 ALA A C   1 
ATOM   9262  O  O   . ALA A 1 1597 ? 150.504 125.210 103.469 1.00 58.84  ? 1168 ALA A O   1 
ATOM   9263  C  CB  . ALA A 1 1597 ? 152.916 126.623 101.636 1.00 53.73  ? 1168 ALA A CB  1 
ATOM   9264  N  N   . VAL A 1 1598 ? 152.038 123.816 102.601 1.00 44.75  ? 1169 VAL A N   1 
ATOM   9265  C  CA  . VAL A 1 1598 ? 151.850 122.803 103.627 1.00 42.39  ? 1169 VAL A CA  1 
ATOM   9266  C  C   . VAL A 1 1598 ? 152.746 123.115 104.821 1.00 52.88  ? 1169 VAL A C   1 
ATOM   9267  O  O   . VAL A 1 1598 ? 153.795 123.748 104.687 1.00 63.09  ? 1169 VAL A O   1 
ATOM   9268  C  CB  . VAL A 1 1598 ? 152.149 121.416 103.045 1.00 49.03  ? 1169 VAL A CB  1 
ATOM   9269  C  CG1 . VAL A 1 1598 ? 151.291 121.189 101.814 1.00 51.98  ? 1169 VAL A CG1 1 
ATOM   9270  C  CG2 . VAL A 1 1598 ? 153.626 121.289 102.729 1.00 55.31  ? 1169 VAL A CG2 1 
ATOM   9271  N  N   . LYS A 1 1599 ? 152.313 122.694 106.005 1.00 49.84  ? 1170 LYS A N   1 
ATOM   9272  C  CA  . LYS A 1 1599 ? 153.102 122.766 107.230 1.00 50.05  ? 1170 LYS A CA  1 
ATOM   9273  C  C   . LYS A 1 1599 ? 153.664 121.390 107.551 1.00 64.48  ? 1170 LYS A C   1 
ATOM   9274  O  O   . LYS A 1 1599 ? 152.913 120.407 107.589 1.00 65.59  ? 1170 LYS A O   1 
ATOM   9275  C  CB  . LYS A 1 1599 ? 152.248 123.225 108.406 1.00 58.16  ? 1170 LYS A CB  1 
ATOM   9276  C  CG  . LYS A 1 1599 ? 151.957 124.684 108.468 1.00 64.79  ? 1170 LYS A CG  1 
ATOM   9277  C  CD  . LYS A 1 1599 ? 151.199 124.952 109.761 1.00 66.15  ? 1170 LYS A CD  1 
ATOM   9278  C  CE  . LYS A 1 1599 ? 151.167 126.435 110.093 1.00 77.27  ? 1170 LYS A CE  1 
ATOM   9279  N  NZ  . LYS A 1 1599 ? 152.557 126.967 110.303 1.00 78.61  ? 1170 LYS A NZ  1 
ATOM   9280  N  N   . LYS A 1 1600 ? 154.970 121.318 107.814 1.00 57.28  ? 1171 LYS A N   1 
ATOM   9281  C  CA  . LYS A 1 1600 ? 155.548 120.005 108.049 1.00 53.13  ? 1171 LYS A CA  1 
ATOM   9282  C  C   . LYS A 1 1600 ? 155.217 119.471 109.428 1.00 49.44  ? 1171 LYS A C   1 
ATOM   9283  O  O   . LYS A 1 1600 ? 155.155 118.252 109.620 1.00 54.41  ? 1171 LYS A O   1 
ATOM   9284  C  CB  . LYS A 1 1600 ? 157.053 120.042 107.835 1.00 61.20  ? 1171 LYS A CB  1 
ATOM   9285  C  CG  . LYS A 1 1600 ? 157.412 119.882 106.378 1.00 72.13  ? 1171 LYS A CG  1 
ATOM   9286  C  CD  . LYS A 1 1600 ? 156.908 118.541 105.858 1.00 80.54  ? 1171 LYS A CD  1 
ATOM   9287  C  CE  . LYS A 1 1600 ? 157.234 118.326 104.373 1.00 101.48 ? 1171 LYS A CE  1 
ATOM   9288  N  NZ  . LYS A 1 1600 ? 156.607 119.332 103.449 1.00 89.20  ? 1171 LYS A NZ  1 
ATOM   9289  N  N   . HIS A 1 1601 ? 154.982 120.345 110.381 1.00 48.07  ? 1172 HIS A N   1 
ATOM   9290  C  CA  . HIS A 1 1601 ? 154.721 119.882 111.726 1.00 51.01  ? 1172 HIS A CA  1 
ATOM   9291  C  C   . HIS A 1 1601 ? 153.375 119.175 111.771 1.00 52.35  ? 1172 HIS A C   1 
ATOM   9292  O  O   . HIS A 1 1601 ? 152.460 119.496 111.009 1.00 58.11  ? 1172 HIS A O   1 
ATOM   9293  C  CB  . HIS A 1 1601 ? 154.734 121.066 112.674 1.00 65.18  ? 1172 HIS A CB  1 
ATOM   9294  C  CG  . HIS A 1 1601 ? 155.242 120.736 114.029 1.00 66.55  ? 1172 HIS A CG  1 
ATOM   9295  N  ND1 . HIS A 1 1601 ? 156.500 120.213 114.234 1.00 70.23  ? 1172 HIS A ND1 1 
ATOM   9296  C  CD2 . HIS A 1 1601 ? 154.688 120.893 115.253 1.00 71.71  ? 1172 HIS A CD2 1 
ATOM   9297  C  CE1 . HIS A 1 1601 ? 156.691 120.040 115.529 1.00 81.73  ? 1172 HIS A CE1 1 
ATOM   9298  N  NE2 . HIS A 1 1601 ? 155.608 120.446 116.170 1.00 81.46  ? 1172 HIS A NE2 1 
ATOM   9299  N  N   . ILE A 1 1602 ? 153.263 118.182 112.646 1.00 45.68  ? 1173 ILE A N   1 
ATOM   9300  C  CA  . ILE A 1 1602 ? 152.020 117.450 112.850 1.00 31.96  ? 1173 ILE A CA  1 
ATOM   9301  C  C   . ILE A 1 1602 ? 151.770 117.400 114.343 1.00 34.85  ? 1173 ILE A C   1 
ATOM   9302  O  O   . ILE A 1 1602 ? 152.318 116.542 115.036 1.00 44.17  ? 1173 ILE A O   1 
ATOM   9303  C  CB  . ILE A 1 1602 ? 152.079 116.046 112.285 1.00 30.89  ? 1173 ILE A CB  1 
ATOM   9304  C  CG1 . ILE A 1 1602 ? 152.411 116.082 110.809 1.00 44.63  ? 1173 ILE A CG1 1 
ATOM   9305  C  CG2 . ILE A 1 1602 ? 150.759 115.374 112.497 1.00 40.34  ? 1173 ILE A CG2 1 
ATOM   9306  C  CD1 . ILE A 1 1602 ? 152.496 114.685 110.214 1.00 54.65  ? 1173 ILE A CD1 1 
ATOM   9307  N  N   . VAL A 1 1603 ? 150.932 118.294 114.844 1.00 34.88  ? 1174 VAL A N   1 
ATOM   9308  C  CA  . VAL A 1 1603 ? 150.666 118.307 116.272 1.00 29.88  ? 1174 VAL A CA  1 
ATOM   9309  C  C   . VAL A 1 1603 ? 150.058 116.992 116.705 1.00 40.36  ? 1174 VAL A C   1 
ATOM   9310  O  O   . VAL A 1 1603 ? 150.449 116.425 117.730 1.00 52.33  ? 1174 VAL A O   1 
ATOM   9311  C  CB  . VAL A 1 1603 ? 149.748 119.482 116.637 1.00 54.94  ? 1174 VAL A CB  1 
ATOM   9312  C  CG1 . VAL A 1 1603 ? 149.369 119.431 118.132 1.00 57.29  ? 1174 VAL A CG1 1 
ATOM   9313  C  CG2 . VAL A 1 1603 ? 150.421 120.809 116.263 1.00 67.58  ? 1174 VAL A CG2 1 
ATOM   9314  N  N   . SER A 1 1604 ? 149.103 116.476 115.940 1.00 37.07  ? 1175 SER A N   1 
ATOM   9315  C  CA  . SER A 1 1604 ? 148.380 115.287 116.364 1.00 32.34  ? 1175 SER A CA  1 
ATOM   9316  C  C   . SER A 1 1604 ? 147.951 114.479 115.156 1.00 36.81  ? 1175 SER A C   1 
ATOM   9317  O  O   . SER A 1 1604 ? 147.518 115.048 114.152 1.00 43.46  ? 1175 SER A O   1 
ATOM   9318  C  CB  . SER A 1 1604 ? 147.151 115.665 117.179 1.00 35.56  ? 1175 SER A CB  1 
ATOM   9319  O  OG  . SER A 1 1604 ? 146.437 114.495 117.520 1.00 44.95  ? 1175 SER A OG  1 
ATOM   9320  N  N   . ALA A 1 1605 ? 148.043 113.157 115.254 1.00 34.48  ? 1176 ALA A N   1 
ATOM   9321  C  CA  . ALA A 1 1605 ? 147.616 112.299 114.157 1.00 35.07  ? 1176 ALA A CA  1 
ATOM   9322  C  C   . ALA A 1 1605 ? 146.961 111.063 114.737 1.00 35.96  ? 1176 ALA A C   1 
ATOM   9323  O  O   . ALA A 1 1605 ? 147.578 110.362 115.542 1.00 42.89  ? 1176 ALA A O   1 
ATOM   9324  C  CB  . ALA A 1 1605 ? 148.794 111.907 113.261 1.00 36.81  ? 1176 ALA A CB  1 
ATOM   9325  N  N   . TRP A 1 1606 ? 145.719 110.797 114.340 1.00 30.72  ? 1177 TRP A N   1 
ATOM   9326  C  CA  . TRP A 1 1606 ? 145.085 109.544 114.680 1.00 30.80  ? 1177 TRP A CA  1 
ATOM   9327  C  C   . TRP A 1 1606 ? 144.307 109.068 113.471 1.00 34.57  ? 1177 TRP A C   1 
ATOM   9328  O  O   . TRP A 1 1606 ? 143.419 109.796 112.993 1.00 40.32  ? 1177 TRP A O   1 
ATOM   9329  C  CB  . TRP A 1 1606 ? 144.151 109.697 115.858 1.00 40.28  ? 1177 TRP A CB  1 
ATOM   9330  C  CG  . TRP A 1 1606 ? 144.860 110.250 117.001 1.00 44.27  ? 1177 TRP A CG  1 
ATOM   9331  C  CD1 . TRP A 1 1606 ? 144.779 111.516 117.459 1.00 50.41  ? 1177 TRP A CD1 1 
ATOM   9332  C  CD2 . TRP A 1 1606 ? 145.781 109.563 117.855 1.00 35.65  ? 1177 TRP A CD2 1 
ATOM   9333  N  NE1 . TRP A 1 1606 ? 145.603 111.674 118.544 1.00 52.38  ? 1177 TRP A NE1 1 
ATOM   9334  C  CE2 . TRP A 1 1606 ? 146.224 110.484 118.810 1.00 38.46  ? 1177 TRP A CE2 1 
ATOM   9335  C  CE3 . TRP A 1 1606 ? 146.270 108.262 117.898 1.00 48.66  ? 1177 TRP A CE3 1 
ATOM   9336  C  CZ2 . TRP A 1 1606 ? 147.134 110.158 119.802 1.00 46.16  ? 1177 TRP A CZ2 1 
ATOM   9337  C  CZ3 . TRP A 1 1606 ? 147.181 107.936 118.884 1.00 61.79  ? 1177 TRP A CZ3 1 
ATOM   9338  C  CH2 . TRP A 1 1606 ? 147.606 108.885 119.824 1.00 53.65  ? 1177 TRP A CH2 1 
ATOM   9339  N  N   . PRO A 1 1607 ? 144.545 107.842 112.999 1.00 31.41  ? 1178 PRO A N   1 
ATOM   9340  C  CA  . PRO A 1 1607 ? 145.403 106.835 113.602 1.00 28.31  ? 1178 PRO A CA  1 
ATOM   9341  C  C   . PRO A 1 1607 ? 146.818 107.004 113.207 1.00 26.84  ? 1178 PRO A C   1 
ATOM   9342  O  O   . PRO A 1 1607 ? 147.704 106.533 113.903 1.00 41.21  ? 1178 PRO A O   1 
ATOM   9343  C  CB  . PRO A 1 1607 ? 144.885 105.529 113.027 1.00 33.92  ? 1178 PRO A CB  1 
ATOM   9344  C  CG  . PRO A 1 1607 ? 144.384 105.911 111.710 1.00 46.19  ? 1178 PRO A CG  1 
ATOM   9345  C  CD  . PRO A 1 1607 ? 143.784 107.284 111.874 1.00 43.74  ? 1178 PRO A CD  1 
ATOM   9346  N  N   . ASN A 1 1608 ? 147.056 107.648 112.094 1.00 23.86  ? 1179 ASN A N   1 
ATOM   9347  C  CA  . ASN A 1 1608 ? 148.434 107.912 111.744 1.00 28.28  ? 1179 ASN A CA  1 
ATOM   9348  C  C   . ASN A 1 1608 ? 148.444 109.063 110.762 1.00 31.04  ? 1179 ASN A C   1 
ATOM   9349  O  O   . ASN A 1 1608 ? 147.403 109.626 110.424 1.00 38.40  ? 1179 ASN A O   1 
ATOM   9350  C  CB  . ASN A 1 1608 ? 149.104 106.648 111.211 1.00 35.50  ? 1179 ASN A CB  1 
ATOM   9351  C  CG  . ASN A 1 1608 ? 148.279 105.964 110.152 1.00 49.57  ? 1179 ASN A CG  1 
ATOM   9352  O  OD1 . ASN A 1 1608 ? 147.405 106.584 109.547 1.00 52.20  ? 1179 ASN A OD1 1 
ATOM   9353  N  ND2 . ASN A 1 1608 ? 148.531 104.671 109.932 1.00 44.83  ? 1179 ASN A ND2 1 
ATOM   9354  N  N   . ALA A 1 1609 ? 149.625 109.433 110.323 1.00 32.17  ? 1180 ALA A N   1 
ATOM   9355  C  CA  . ALA A 1 1609 ? 149.736 110.591 109.466 1.00 40.88  ? 1180 ALA A CA  1 
ATOM   9356  C  C   . ALA A 1 1609 ? 149.506 110.257 107.996 1.00 43.75  ? 1180 ALA A C   1 
ATOM   9357  O  O   . ALA A 1 1609 ? 149.941 111.021 107.130 1.00 46.95  ? 1180 ALA A O   1 
ATOM   9358  C  CB  . ALA A 1 1609 ? 151.101 111.256 109.667 1.00 50.59  ? 1180 ALA A CB  1 
ATOM   9359  N  N   . SER A 1 1610 ? 148.841 109.138 107.691 1.00 39.93  ? 1181 SER A N   1 
ATOM   9360  C  CA  . SER A 1 1610 ? 148.718 108.723 106.293 1.00 40.09  ? 1181 SER A CA  1 
ATOM   9361  C  C   . SER A 1 1610 ? 147.913 109.724 105.470 1.00 48.81  ? 1181 SER A C   1 
ATOM   9362  O  O   . SER A 1 1610 ? 148.277 110.030 104.330 1.00 54.15  ? 1181 SER A O   1 
ATOM   9363  C  CB  . SER A 1 1610 ? 148.076 107.339 106.196 1.00 47.27  ? 1181 SER A CB  1 
ATOM   9364  O  OG  . SER A 1 1610 ? 148.856 106.347 106.847 1.00 55.82  ? 1181 SER A OG  1 
ATOM   9365  N  N   . ARG A 1 1611 ? 146.822 110.241 106.020 1.00 43.21  ? 1182 ARG A N   1 
ATOM   9366  C  CA  . ARG A 1 1611 ? 145.904 111.104 105.295 1.00 31.05  ? 1182 ARG A CA  1 
ATOM   9367  C  C   . ARG A 1 1611 ? 145.959 112.510 105.847 1.00 32.01  ? 1182 ARG A C   1 
ATOM   9368  O  O   . ARG A 1 1611 ? 146.051 112.701 107.059 1.00 38.84  ? 1182 ARG A O   1 
ATOM   9369  C  CB  . ARG A 1 1611 ? 144.483 110.590 105.420 1.00 40.48  ? 1182 ARG A CB  1 
ATOM   9370  C  CG  . ARG A 1 1611 ? 144.063 109.728 104.273 1.00 44.82  ? 1182 ARG A CG  1 
ATOM   9371  C  CD  . ARG A 1 1611 ? 144.972 108.550 104.121 1.00 39.29  ? 1182 ARG A CD  1 
ATOM   9372  N  NE  . ARG A 1 1611 ? 144.475 107.690 103.073 1.00 37.22  ? 1182 ARG A NE  1 
ATOM   9373  C  CZ  . ARG A 1 1611 ? 145.124 106.626 102.644 1.00 43.33  ? 1182 ARG A CZ  1 
ATOM   9374  N  NH1 . ARG A 1 1611 ? 146.306 106.328 103.157 1.00 51.12  ? 1182 ARG A NH1 1 
ATOM   9375  N  NH2 . ARG A 1 1611 ? 144.607 105.877 101.684 1.00 51.36  ? 1182 ARG A NH2 1 
ATOM   9376  N  N   . ILE A 1 1612 ? 145.867 113.496 104.966 1.00 29.82  ? 1183 ILE A N   1 
ATOM   9377  C  CA  . ILE A 1 1612 ? 145.840 114.857 105.463 1.00 21.63  ? 1183 ILE A CA  1 
ATOM   9378  C  C   . ILE A 1 1612 ? 144.709 115.026 106.425 1.00 20.13  ? 1183 ILE A C   1 
ATOM   9379  O  O   . ILE A 1 1612 ? 144.829 115.725 107.431 1.00 31.42  ? 1183 ILE A O   1 
ATOM   9380  C  CB  . ILE A 1 1612 ? 145.723 115.855 104.319 1.00 32.69  ? 1183 ILE A CB  1 
ATOM   9381  C  CG1 . ILE A 1 1612 ? 146.966 115.710 103.458 1.00 56.23  ? 1183 ILE A CG1 1 
ATOM   9382  C  CG2 . ILE A 1 1612 ? 145.565 117.250 104.880 1.00 39.76  ? 1183 ILE A CG2 1 
ATOM   9383  C  CD1 . ILE A 1 1612 ? 148.247 116.022 104.252 1.00 58.47  ? 1183 ILE A CD1 1 
ATOM   9384  N  N   . SER A 1 1613 ? 143.610 114.368 106.162 1.00 23.13  ? 1184 SER A N   1 
ATOM   9385  C  CA  . SER A 1 1613 ? 142.475 114.597 107.021 1.00 31.29  ? 1184 SER A CA  1 
ATOM   9386  C  C   . SER A 1 1613 ? 142.686 114.049 108.419 1.00 38.49  ? 1184 SER A C   1 
ATOM   9387  O  O   . SER A 1 1613 ? 141.927 114.398 109.330 1.00 42.34  ? 1184 SER A O   1 
ATOM   9388  C  CB  . SER A 1 1613 ? 141.241 113.966 106.405 1.00 41.50  ? 1184 SER A CB  1 
ATOM   9389  O  OG  . SER A 1 1613 ? 140.170 114.014 107.327 1.00 47.55  ? 1184 SER A OG  1 
ATOM   9390  N  N   . TRP A 1 1614 ? 143.681 113.201 108.613 1.00 36.94  ? 1185 TRP A N   1 
ATOM   9391  C  CA  . TRP A 1 1614 ? 143.916 112.598 109.915 1.00 34.12  ? 1185 TRP A CA  1 
ATOM   9392  C  C   . TRP A 1 1614 ? 144.844 113.396 110.825 1.00 35.02  ? 1185 TRP A C   1 
ATOM   9393  O  O   . TRP A 1 1614 ? 144.921 113.081 112.013 1.00 39.96  ? 1185 TRP A O   1 
ATOM   9394  C  CB  . TRP A 1 1614 ? 144.471 111.185 109.713 1.00 34.54  ? 1185 TRP A CB  1 
ATOM   9395  C  CG  . TRP A 1 1614 ? 143.451 110.205 109.206 1.00 38.04  ? 1185 TRP A CG  1 
ATOM   9396  C  CD1 . TRP A 1 1614 ? 142.097 110.393 109.123 1.00 42.69  ? 1185 TRP A CD1 1 
ATOM   9397  C  CD2 . TRP A 1 1614 ? 143.696 108.877 108.751 1.00 29.78  ? 1185 TRP A CD2 1 
ATOM   9398  N  NE1 . TRP A 1 1614 ? 141.494 109.259 108.655 1.00 34.95  ? 1185 TRP A NE1 1 
ATOM   9399  C  CE2 . TRP A 1 1614 ? 142.459 108.317 108.416 1.00 34.85  ? 1185 TRP A CE2 1 
ATOM   9400  C  CE3 . TRP A 1 1614 ? 144.844 108.104 108.598 1.00 37.66  ? 1185 TRP A CE3 1 
ATOM   9401  C  CZ2 . TRP A 1 1614 ? 142.339 107.020 107.936 1.00 46.10  ? 1185 TRP A CZ2 1 
ATOM   9402  C  CZ3 . TRP A 1 1614 ? 144.720 106.808 108.125 1.00 39.23  ? 1185 TRP A CZ3 1 
ATOM   9403  C  CH2 . TRP A 1 1614 ? 143.483 106.282 107.802 1.00 40.13  ? 1185 TRP A CH2 1 
ATOM   9404  N  N   . THR A 1 1615 ? 145.542 114.404 110.317 1.00 26.88  ? 1186 THR A N   1 
ATOM   9405  C  CA  . THR A 1 1615 ? 146.571 115.104 111.062 1.00 19.92  ? 1186 THR A CA  1 
ATOM   9406  C  C   . THR A 1 1615 ? 146.206 116.569 111.202 1.00 29.90  ? 1186 THR A C   1 
ATOM   9407  O  O   . THR A 1 1615 ? 145.611 117.148 110.293 1.00 37.95  ? 1186 THR A O   1 
ATOM   9408  C  CB  . THR A 1 1615 ? 147.868 115.018 110.341 1.00 25.34  ? 1186 THR A CB  1 
ATOM   9409  O  OG1 . THR A 1 1615 ? 147.864 116.002 109.305 1.00 32.52  ? 1186 THR A OG1 1 
ATOM   9410  C  CG2 . THR A 1 1615 ? 147.999 113.663 109.698 1.00 35.51  ? 1186 THR A CG2 1 
ATOM   9411  N  N   . ILE A 1 1616 ? 146.572 117.191 112.323 1.00 24.92  ? 1187 ILE A N   1 
ATOM   9412  C  CA  . ILE A 1 1616 ? 146.397 118.630 112.465 1.00 24.26  ? 1187 ILE A CA  1 
ATOM   9413  C  C   . ILE A 1 1616 ? 147.758 119.263 112.722 1.00 46.17  ? 1187 ILE A C   1 
ATOM   9414  O  O   . ILE A 1 1616 ? 148.545 118.762 113.534 1.00 49.24  ? 1187 ILE A O   1 
ATOM   9415  C  CB  . ILE A 1 1616 ? 145.419 119.011 113.581 1.00 22.30  ? 1187 ILE A CB  1 
ATOM   9416  C  CG1 . ILE A 1 1616 ? 145.920 118.552 114.916 1.00 28.63  ? 1187 ILE A CG1 1 
ATOM   9417  C  CG2 . ILE A 1 1616 ? 144.143 118.282 113.376 1.00 38.34  ? 1187 ILE A CG2 1 
ATOM   9418  C  CD1 . ILE A 1 1616 ? 145.222 119.235 116.044 1.00 40.60  ? 1187 ILE A CD1 1 
ATOM   9419  N  N   . GLY A 1 1617 ? 148.053 120.349 112.004 1.00 49.02  ? 1188 GLY A N   1 
ATOM   9420  C  CA  . GLY A 1 1617 ? 149.238 121.141 112.254 1.00 38.72  ? 1188 GLY A CA  1 
ATOM   9421  C  C   . GLY A 1 1617 ? 148.952 122.185 113.309 1.00 48.54  ? 1188 GLY A C   1 
ATOM   9422  O  O   . GLY A 1 1617 ? 147.881 122.226 113.916 1.00 55.13  ? 1188 GLY A O   1 
ATOM   9423  N  N   . ASP A 1 1618 ? 149.923 123.051 113.524 1.00 54.72  ? 1189 ASP A N   1 
ATOM   9424  C  CA  . ASP A 1 1618 ? 149.783 124.057 114.562 1.00 55.13  ? 1189 ASP A CA  1 
ATOM   9425  C  C   . ASP A 1 1618 ? 149.112 125.322 114.071 1.00 49.07  ? 1189 ASP A C   1 
ATOM   9426  O  O   . ASP A 1 1618 ? 148.830 126.208 114.881 1.00 58.92  ? 1189 ASP A O   1 
ATOM   9427  C  CB  . ASP A 1 1618 ? 151.164 124.369 115.167 1.00 74.77  ? 1189 ASP A CB  1 
ATOM   9428  C  CG  . ASP A 1 1618 ? 152.188 124.795 114.116 1.00 85.64  ? 1189 ASP A CG  1 
ATOM   9429  O  OD1 . ASP A 1 1618 ? 152.122 124.272 112.976 1.00 80.31  ? 1189 ASP A OD1 1 
ATOM   9430  O  OD2 . ASP A 1 1618 ? 153.063 125.637 114.426 1.00 80.04  ? 1189 ASP A OD2 1 
ATOM   9431  N  N   . GLY A 1 1619 ? 148.813 125.410 112.786 1.00 56.24  ? 1190 GLY A N   1 
ATOM   9432  C  CA  . GLY A 1 1619 ? 148.368 126.666 112.227 1.00 73.28  ? 1190 GLY A CA  1 
ATOM   9433  C  C   . GLY A 1 1619 ? 147.073 127.152 112.843 1.00 86.08  ? 1190 GLY A C   1 
ATOM   9434  O  O   . GLY A 1 1619 ? 146.303 126.391 113.433 1.00 82.14  ? 1190 GLY A O   1 
ATOM   9435  N  N   . ILE A 1 1620 ? 146.856 128.460 112.723 1.00 99.97  ? 1191 ILE A N   1 
ATOM   9436  C  CA  . ILE A 1 1620 ? 145.596 129.083 113.124 1.00 110.48 ? 1191 ILE A CA  1 
ATOM   9437  C  C   . ILE A 1 1620 ? 144.514 128.555 112.186 1.00 122.72 ? 1191 ILE A C   1 
ATOM   9438  O  O   . ILE A 1 1620 ? 144.823 128.196 111.037 1.00 116.07 ? 1191 ILE A O   1 
ATOM   9439  C  CB  . ILE A 1 1620 ? 145.684 130.626 113.109 1.00 114.21 ? 1191 ILE A CB  1 
ATOM   9440  C  CG1 . ILE A 1 1620 ? 146.163 131.165 111.746 1.00 120.57 ? 1191 ILE A CG1 1 
ATOM   9441  C  CG2 . ILE A 1 1620 ? 146.551 131.141 114.265 1.00 104.63 ? 1191 ILE A CG2 1 
ATOM   9442  C  CD1 . ILE A 1 1620 ? 146.350 132.700 111.693 1.00 112.48 ? 1191 ILE A CD1 1 
ATOM   9443  N  N   . PRO A 1 1621 ? 143.231 128.452 112.636 1.00 133.78 ? 1192 PRO A N   1 
ATOM   9444  C  CA  . PRO A 1 1621 ? 142.184 127.890 111.758 1.00 143.42 ? 1192 PRO A CA  1 
ATOM   9445  C  C   . PRO A 1 1621 ? 141.901 128.714 110.497 1.00 140.97 ? 1192 PRO A C   1 
ATOM   9446  O  O   . PRO A 1 1621 ? 142.051 128.192 109.383 1.00 129.21 ? 1192 PRO A O   1 
ATOM   9447  C  CB  . PRO A 1 1621 ? 140.952 127.814 112.682 1.00 138.47 ? 1192 PRO A CB  1 
ATOM   9448  C  CG  . PRO A 1 1621 ? 141.226 128.802 113.797 1.00 132.04 ? 1192 PRO A CG  1 
ATOM   9449  C  CD  . PRO A 1 1621 ? 142.723 128.747 113.992 1.00 129.85 ? 1192 PRO A CD  1 
ATOM   9450  N  N   . TYR A 1 1622 ? 141.518 129.988 110.646 1.00 142.31 ? 1193 TYR A N   1 
ATOM   9451  C  CA  . TYR A 1 1622 ? 141.218 130.862 109.511 1.00 141.89 ? 1193 TYR A CA  1 
ATOM   9452  C  C   . TYR A 1 1622 ? 141.577 132.300 109.890 1.00 142.64 ? 1193 TYR A C   1 
ATOM   9453  O  O   . TYR A 1 1622 ? 141.710 132.634 111.074 1.00 134.66 ? 1193 TYR A O   1 
ATOM   9454  C  CB  . TYR A 1 1622 ? 139.736 130.734 109.064 1.00 138.82 ? 1193 TYR A CB  1 
ATOM   9455  C  CG  . TYR A 1 1622 ? 139.369 129.377 108.435 1.00 137.80 ? 1193 TYR A CG  1 
ATOM   9456  C  CD1 . TYR A 1 1622 ? 139.773 129.049 107.131 1.00 121.85 ? 1193 TYR A CD1 1 
ATOM   9457  C  CD2 . TYR A 1 1622 ? 138.645 128.415 109.153 1.00 132.97 ? 1193 TYR A CD2 1 
ATOM   9458  C  CE1 . TYR A 1 1622 ? 139.454 127.799 106.554 1.00 110.50 ? 1193 TYR A CE1 1 
ATOM   9459  C  CE2 . TYR A 1 1622 ? 138.324 127.164 108.587 1.00 126.85 ? 1193 TYR A CE2 1 
ATOM   9460  C  CZ  . TYR A 1 1622 ? 138.730 126.863 107.290 1.00 116.87 ? 1193 TYR A CZ  1 
ATOM   9461  O  OH  . TYR A 1 1622 ? 138.413 125.636 106.733 1.00 94.44  ? 1193 TYR A OH  1 
ATOM   9462  N  N   . ILE A 1 1623 ? 141.762 133.142 108.866 1.00 138.62 ? 1194 ILE A N   1 
ATOM   9463  C  CA  . ILE A 1 1623 ? 142.113 134.557 109.065 1.00 138.24 ? 1194 ILE A CA  1 
ATOM   9464  C  C   . ILE A 1 1623 ? 141.305 135.442 108.107 1.00 123.41 ? 1194 ILE A C   1 
ATOM   9465  O  O   . ILE A 1 1623 ? 140.189 135.099 107.707 1.00 115.82 ? 1194 ILE A O   1 
ATOM   9466  C  CB  . ILE A 1 1623 ? 143.662 134.798 108.903 1.00 140.04 ? 1194 ILE A CB  1 
ATOM   9467  C  CG1 . ILE A 1 1623 ? 144.041 136.259 109.219 1.00 132.80 ? 1194 ILE A CG1 1 
ATOM   9468  C  CG2 . ILE A 1 1623 ? 144.158 134.355 107.503 1.00 129.12 ? 1194 ILE A CG2 1 
ATOM   9469  C  CD1 . ILE A 1 1623 ? 145.543 136.570 109.097 1.00 116.73 ? 1194 ILE A CD1 1 
ATOM   9470  N  N   . GLN A 1 1633 ? 131.770 155.122 117.748 1.00 113.33 ? 1204 GLN A N   1 
ATOM   9471  C  CA  . GLN A 1 1633 ? 131.285 154.702 119.060 1.00 105.18 ? 1204 GLN A CA  1 
ATOM   9472  C  C   . GLN A 1 1633 ? 130.157 155.603 119.526 1.00 95.21  ? 1204 GLN A C   1 
ATOM   9473  O  O   . GLN A 1 1633 ? 130.076 156.767 119.133 1.00 97.54  ? 1204 GLN A O   1 
ATOM   9474  C  CB  . GLN A 1 1633 ? 132.417 154.701 120.088 1.00 103.57 ? 1204 GLN A CB  1 
ATOM   9475  C  CG  . GLN A 1 1633 ? 133.335 153.490 119.983 1.00 117.22 ? 1204 GLN A CG  1 
ATOM   9476  C  CD  . GLN A 1 1633 ? 134.274 153.356 121.175 1.00 123.10 ? 1204 GLN A CD  1 
ATOM   9477  O  OE1 . GLN A 1 1633 ? 134.656 154.352 121.794 1.00 121.07 ? 1204 GLN A OE1 1 
ATOM   9478  N  NE2 . GLN A 1 1633 ? 134.660 152.122 121.492 1.00 119.84 ? 1204 GLN A NE2 1 
ATOM   9479  N  N   . PRO A 1 1634 ? 129.276 155.058 120.356 1.00 94.46  ? 1205 PRO A N   1 
ATOM   9480  C  CA  . PRO A 1 1634 ? 128.117 155.832 120.810 1.00 95.49  ? 1205 PRO A CA  1 
ATOM   9481  C  C   . PRO A 1 1634 ? 128.493 156.823 121.896 1.00 87.89  ? 1205 PRO A C   1 
ATOM   9482  O  O   . PRO A 1 1634 ? 129.307 156.533 122.777 1.00 92.71  ? 1205 PRO A O   1 
ATOM   9483  C  CB  . PRO A 1 1634 ? 127.171 154.753 121.350 1.00 101.64 ? 1205 PRO A CB  1 
ATOM   9484  C  CG  . PRO A 1 1634 ? 128.105 153.671 121.822 1.00 103.18 ? 1205 PRO A CG  1 
ATOM   9485  C  CD  . PRO A 1 1634 ? 129.259 153.674 120.864 1.00 97.46  ? 1205 PRO A CD  1 
ATOM   9486  N  N   . ALA A 1 1635 ? 127.887 158.007 121.824 1.00 83.87  ? 1206 ALA A N   1 
ATOM   9487  C  CA  . ALA A 1 1635 ? 128.123 159.014 122.852 1.00 87.27  ? 1206 ALA A CA  1 
ATOM   9488  C  C   . ALA A 1 1635 ? 127.548 158.574 124.196 1.00 92.39  ? 1206 ALA A C   1 
ATOM   9489  O  O   . ALA A 1 1635 ? 128.241 158.614 125.220 1.00 98.92  ? 1206 ALA A O   1 
ATOM   9490  C  CB  . ALA A 1 1635 ? 127.533 160.357 122.415 1.00 87.80  ? 1206 ALA A CB  1 
ATOM   9491  N  N   . ILE A 1 1636 ? 126.281 158.148 124.211 1.00 91.31  ? 1207 ILE A N   1 
ATOM   9492  C  CA  . ILE A 1 1636 ? 125.596 157.672 125.414 1.00 88.48  ? 1207 ILE A CA  1 
ATOM   9493  C  C   . ILE A 1 1636 ? 124.940 156.330 125.108 1.00 87.97  ? 1207 ILE A C   1 
ATOM   9494  O  O   . ILE A 1 1636 ? 124.039 156.260 124.265 1.00 91.63  ? 1207 ILE A O   1 
ATOM   9495  C  CB  . ILE A 1 1636 ? 124.537 158.670 125.914 1.00 93.91  ? 1207 ILE A CB  1 
ATOM   9496  C  CG1 . ILE A 1 1636 ? 125.147 160.060 126.167 1.00 103.36 ? 1207 ILE A CG1 1 
ATOM   9497  C  CG2 . ILE A 1 1636 ? 123.861 158.128 127.155 1.00 97.64  ? 1207 ILE A CG2 1 
ATOM   9498  C  CD1 . ILE A 1 1636 ? 126.159 160.126 127.324 1.00 103.92 ? 1207 ILE A CD1 1 
ATOM   9499  N  N   . LYS A 1 1637 ? 125.361 155.275 125.815 1.00 87.16  ? 1208 LYS A N   1 
ATOM   9500  C  CA  . LYS A 1 1637 ? 124.840 153.930 125.586 1.00 86.95  ? 1208 LYS A CA  1 
ATOM   9501  C  C   . LYS A 1 1637 ? 123.794 153.585 126.633 1.00 83.79  ? 1208 LYS A C   1 
ATOM   9502  O  O   . LYS A 1 1637 ? 124.106 153.644 127.828 1.00 96.26  ? 1208 LYS A O   1 
ATOM   9503  C  CB  . LYS A 1 1637 ? 125.973 152.909 125.618 1.00 92.23  ? 1208 LYS A CB  1 
ATOM   9504  C  CG  . LYS A 1 1637 ? 125.502 151.456 125.520 1.00 103.51 ? 1208 LYS A CG  1 
ATOM   9505  C  CD  . LYS A 1 1637 ? 124.873 151.153 124.146 1.00 111.15 ? 1208 LYS A CD  1 
ATOM   9506  C  CE  . LYS A 1 1637 ? 125.894 151.208 123.001 1.00 112.72 ? 1208 LYS A CE  1 
ATOM   9507  N  NZ  . LYS A 1 1637 ? 125.293 150.938 121.654 1.00 101.29 ? 1208 LYS A NZ  1 
ATOM   9508  N  N   . PRO A 1 1638 ? 122.563 153.239 126.265 1.00 72.11  ? 1209 PRO A N   1 
ATOM   9509  C  CA  . PRO A 1 1638 ? 121.577 152.882 127.285 1.00 68.62  ? 1209 PRO A CA  1 
ATOM   9510  C  C   . PRO A 1 1638 ? 122.002 151.609 127.994 1.00 82.97  ? 1209 PRO A C   1 
ATOM   9511  O  O   . PRO A 1 1638 ? 122.568 150.705 127.377 1.00 85.85  ? 1209 PRO A O   1 
ATOM   9512  C  CB  . PRO A 1 1638 ? 120.296 152.668 126.483 1.00 72.69  ? 1209 PRO A CB  1 
ATOM   9513  C  CG  . PRO A 1 1638 ? 120.770 152.325 125.123 1.00 80.70  ? 1209 PRO A CG  1 
ATOM   9514  C  CD  . PRO A 1 1638 ? 122.012 153.120 124.909 1.00 85.40  ? 1209 PRO A CD  1 
ATOM   9515  N  N   . LYS A 1 1639 ? 121.732 151.545 129.309 1.00 93.94  ? 1210 LYS A N   1 
ATOM   9516  C  CA  . LYS A 1 1639 ? 122.158 150.399 130.123 1.00 97.69  ? 1210 LYS A CA  1 
ATOM   9517  C  C   . LYS A 1 1639 ? 121.297 149.150 129.899 1.00 96.68  ? 1210 LYS A C   1 
ATOM   9518  O  O   . LYS A 1 1639 ? 121.833 148.036 129.849 1.00 94.23  ? 1210 LYS A O   1 
ATOM   9519  C  CB  . LYS A 1 1639 ? 122.187 150.752 131.623 1.00 108.76 ? 1210 LYS A CB  1 
ATOM   9520  C  CG  . LYS A 1 1639 ? 123.179 151.864 132.051 1.00 113.32 ? 1210 LYS A CG  1 
ATOM   9521  C  CD  . LYS A 1 1639 ? 123.454 151.899 133.586 1.00 113.76 ? 1210 LYS A CD  1 
ATOM   9522  C  CE  . LYS A 1 1639 ? 122.167 152.080 134.410 1.00 115.96 ? 1210 LYS A CE  1 
ATOM   9523  N  NZ  . LYS A 1 1639 ? 122.388 152.090 135.890 1.00 104.49 ? 1210 LYS A NZ  1 
ATOM   9524  N  N   . CYS A 1 1640 ? 119.974 149.296 129.778 1.00 90.43  ? 1211 CYS A N   1 
ATOM   9525  C  CA  . CYS A 1 1640 ? 119.080 148.167 129.501 1.00 79.79  ? 1211 CYS A CA  1 
ATOM   9526  C  C   . CYS A 1 1640 ? 118.212 148.518 128.302 1.00 73.18  ? 1211 CYS A C   1 
ATOM   9527  O  O   . CYS A 1 1640 ? 117.030 148.854 128.452 1.00 73.51  ? 1211 CYS A O   1 
ATOM   9528  C  CB  . CYS A 1 1640 ? 118.230 147.814 130.721 1.00 78.45  ? 1211 CYS A CB  1 
ATOM   9529  S  SG  . CYS A 1 1640 ? 119.202 147.280 132.160 1.00 88.39  ? 1211 CYS A SG  1 
ATOM   9530  N  N   . PRO A 1 1641 ? 118.768 148.457 127.095 1.00 66.27  ? 1212 PRO A N   1 
ATOM   9531  C  CA  . PRO A 1 1641 ? 117.992 148.855 125.929 1.00 56.87  ? 1212 PRO A CA  1 
ATOM   9532  C  C   . PRO A 1 1641 ? 116.938 147.814 125.652 1.00 62.77  ? 1212 PRO A C   1 
ATOM   9533  O  O   . PRO A 1 1641 ? 117.174 146.612 125.785 1.00 72.24  ? 1212 PRO A O   1 
ATOM   9534  C  CB  . PRO A 1 1641 ? 119.031 148.910 124.809 1.00 66.53  ? 1212 PRO A CB  1 
ATOM   9535  C  CG  . PRO A 1 1641 ? 120.024 147.898 125.201 1.00 71.40  ? 1212 PRO A CG  1 
ATOM   9536  C  CD  . PRO A 1 1641 ? 120.080 147.915 126.711 1.00 74.63  ? 1212 PRO A CD  1 
ATOM   9537  N  N   . SER A 1 1642 ? 115.754 148.289 125.300 1.00 68.55  ? 1213 SER A N   1 
ATOM   9538  C  CA  . SER A 1 1642 ? 114.707 147.390 124.859 1.00 69.89  ? 1213 SER A CA  1 
ATOM   9539  C  C   . SER A 1 1642 ? 114.969 146.940 123.422 1.00 69.83  ? 1213 SER A C   1 
ATOM   9540  O  O   . SER A 1 1642 ? 115.746 147.549 122.682 1.00 71.81  ? 1213 SER A O   1 
ATOM   9541  C  CB  . SER A 1 1642 ? 113.344 148.073 124.969 1.00 77.85  ? 1213 SER A CB  1 
ATOM   9542  O  OG  . SER A 1 1642 ? 112.304 147.248 124.467 1.00 77.93  ? 1213 SER A OG  1 
ATOM   9543  N  N   . ALA A 1 1643 ? 114.310 145.847 123.033 1.00 72.69  ? 1214 ALA A N   1 
ATOM   9544  C  CA  . ALA A 1 1643 ? 114.461 145.365 121.667 1.00 68.99  ? 1214 ALA A CA  1 
ATOM   9545  C  C   . ALA A 1 1643 ? 114.100 146.456 120.688 1.00 59.68  ? 1214 ALA A C   1 
ATOM   9546  O  O   . ALA A 1 1643 ? 114.778 146.636 119.677 1.00 70.54  ? 1214 ALA A O   1 
ATOM   9547  C  CB  . ALA A 1 1643 ? 113.592 144.130 121.422 1.00 69.51  ? 1214 ALA A CB  1 
ATOM   9548  N  N   . ALA A 1 1644 ? 113.044 147.207 120.981 1.00 55.13  ? 1215 ALA A N   1 
ATOM   9549  C  CA  . ALA A 1 1644 ? 112.624 148.256 120.067 1.00 59.82  ? 1215 ALA A CA  1 
ATOM   9550  C  C   . ALA A 1 1644 ? 113.666 149.353 119.978 1.00 64.29  ? 1215 ALA A C   1 
ATOM   9551  O  O   . ALA A 1 1644 ? 113.992 149.817 118.882 1.00 68.25  ? 1215 ALA A O   1 
ATOM   9552  C  CB  . ALA A 1 1644 ? 111.288 148.834 120.505 1.00 70.70  ? 1215 ALA A CB  1 
ATOM   9553  N  N   . LEU A 1 1645 ? 114.203 149.780 121.121 1.00 68.75  ? 1216 LEU A N   1 
ATOM   9554  C  CA  . LEU A 1 1645 ? 115.244 150.806 121.118 1.00 69.75  ? 1216 LEU A CA  1 
ATOM   9555  C  C   . LEU A 1 1645 ? 116.504 150.321 120.419 1.00 67.13  ? 1216 LEU A C   1 
ATOM   9556  O  O   . LEU A 1 1645 ? 117.129 151.068 119.663 1.00 69.49  ? 1216 LEU A O   1 
ATOM   9557  C  CB  . LEU A 1 1645 ? 115.564 151.230 122.548 1.00 70.08  ? 1216 LEU A CB  1 
ATOM   9558  C  CG  . LEU A 1 1645 ? 116.706 152.232 122.668 1.00 75.11  ? 1216 LEU A CG  1 
ATOM   9559  C  CD1 . LEU A 1 1645 ? 116.354 153.500 121.910 1.00 78.53  ? 1216 LEU A CD1 1 
ATOM   9560  C  CD2 . LEU A 1 1645 ? 116.975 152.531 124.141 1.00 74.78  ? 1216 LEU A CD2 1 
ATOM   9561  N  N   . ARG A 1 1646 ? 116.897 149.079 120.673 1.00 68.79  ? 1217 ARG A N   1 
ATOM   9562  C  CA  . ARG A 1 1646 ? 118.075 148.530 120.024 1.00 67.44  ? 1217 ARG A CA  1 
ATOM   9563  C  C   . ARG A 1 1646 ? 117.888 148.461 118.513 1.00 65.30  ? 1217 ARG A C   1 
ATOM   9564  O  O   . ARG A 1 1646 ? 118.773 148.856 117.751 1.00 70.56  ? 1217 ARG A O   1 
ATOM   9565  C  CB  . ARG A 1 1646 ? 118.361 147.148 120.606 1.00 79.42  ? 1217 ARG A CB  1 
ATOM   9566  C  CG  . ARG A 1 1646 ? 119.734 146.583 120.278 1.00 94.66  ? 1217 ARG A CG  1 
ATOM   9567  C  CD  . ARG A 1 1646 ? 119.887 145.095 120.686 1.00 101.99 ? 1217 ARG A CD  1 
ATOM   9568  N  NE  . ARG A 1 1646 ? 119.689 144.837 122.121 1.00 107.71 ? 1217 ARG A NE  1 
ATOM   9569  C  CZ  . ARG A 1 1646 ? 118.601 144.276 122.656 1.00 106.78 ? 1217 ARG A CZ  1 
ATOM   9570  N  NH1 . ARG A 1 1646 ? 118.526 144.086 123.974 1.00 90.08  ? 1217 ARG A NH1 1 
ATOM   9571  N  NH2 . ARG A 1 1646 ? 117.595 143.883 121.877 1.00 98.96  ? 1217 ARG A NH2 1 
ATOM   9572  N  N   . GLU A 1 1647 ? 116.743 147.964 118.061 1.00 68.56  ? 1218 GLU A N   1 
ATOM   9573  C  CA  . GLU A 1 1647 ? 116.481 147.961 116.633 1.00 64.18  ? 1218 GLU A CA  1 
ATOM   9574  C  C   . GLU A 1 1647 ? 116.438 149.371 116.111 1.00 63.86  ? 1218 GLU A C   1 
ATOM   9575  O  O   . GLU A 1 1647 ? 116.866 149.630 114.987 1.00 68.17  ? 1218 GLU A O   1 
ATOM   9576  C  CB  . GLU A 1 1647 ? 115.169 147.248 116.320 1.00 65.10  ? 1218 GLU A CB  1 
ATOM   9577  C  CG  . GLU A 1 1647 ? 115.201 145.776 116.673 1.00 79.00  ? 1218 GLU A CG  1 
ATOM   9578  C  CD  . GLU A 1 1647 ? 113.948 145.028 116.254 1.00 88.66  ? 1218 GLU A CD  1 
ATOM   9579  O  OE1 . GLU A 1 1647 ? 113.300 145.436 115.258 1.00 79.32  ? 1218 GLU A OE1 1 
ATOM   9580  O  OE2 . GLU A 1 1647 ? 113.610 144.028 116.932 1.00 87.70  ? 1218 GLU A OE2 1 
ATOM   9581  N  N   . ALA A 1 1648 ? 115.918 150.301 116.909 1.00 56.28  ? 1219 ALA A N   1 
ATOM   9582  C  CA  . ALA A 1 1648 ? 115.863 151.684 116.466 1.00 63.74  ? 1219 ALA A CA  1 
ATOM   9583  C  C   . ALA A 1 1648 ? 117.268 152.219 116.212 1.00 74.12  ? 1219 ALA A C   1 
ATOM   9584  O  O   . ALA A 1 1648 ? 117.543 152.808 115.161 1.00 74.46  ? 1219 ALA A O   1 
ATOM   9585  C  CB  . ALA A 1 1648 ? 115.136 152.533 117.502 1.00 57.74  ? 1219 ALA A CB  1 
ATOM   9586  N  N   . ILE A 1 1649 ? 118.174 151.995 117.165 1.00 70.85  ? 1220 ILE A N   1 
ATOM   9587  C  CA  . ILE A 1 1649 ? 119.552 152.463 117.041 1.00 56.65  ? 1220 ILE A CA  1 
ATOM   9588  C  C   . ILE A 1 1649 ? 120.213 151.802 115.859 1.00 51.17  ? 1220 ILE A C   1 
ATOM   9589  O  O   . ILE A 1 1649 ? 120.941 152.439 115.102 1.00 65.62  ? 1220 ILE A O   1 
ATOM   9590  C  CB  . ILE A 1 1649 ? 120.337 152.170 118.331 1.00 68.32  ? 1220 ILE A CB  1 
ATOM   9591  C  CG1 . ILE A 1 1649 ? 119.796 152.988 119.513 1.00 84.22  ? 1220 ILE A CG1 1 
ATOM   9592  C  CG2 . ILE A 1 1649 ? 121.813 152.423 118.108 1.00 69.52  ? 1220 ILE A CG2 1 
ATOM   9593  C  CD1 . ILE A 1 1649 ? 120.506 152.706 120.846 1.00 85.96  ? 1220 ILE A CD1 1 
ATOM   9594  N  N   . GLU A 1 1650 ? 119.995 150.505 115.700 1.00 61.11  ? 1221 GLU A N   1 
ATOM   9595  C  CA  . GLU A 1 1650 ? 120.572 149.809 114.562 1.00 71.16  ? 1221 GLU A CA  1 
ATOM   9596  C  C   . GLU A 1 1650 ? 120.040 150.386 113.265 1.00 65.23  ? 1221 GLU A C   1 
ATOM   9597  O  O   . GLU A 1 1650 ? 120.793 150.598 112.305 1.00 63.65  ? 1221 GLU A O   1 
ATOM   9598  C  CB  . GLU A 1 1650 ? 120.247 148.316 114.643 1.00 87.10  ? 1221 GLU A CB  1 
ATOM   9599  C  CG  . GLU A 1 1650 ? 120.763 147.601 115.906 1.00 93.89  ? 1221 GLU A CG  1 
ATOM   9600  C  CD  . GLU A 1 1650 ? 120.173 146.196 116.085 1.00 96.90  ? 1221 GLU A CD  1 
ATOM   9601  O  OE1 . GLU A 1 1650 ? 120.100 145.438 115.090 1.00 100.29 ? 1221 GLU A OE1 1 
ATOM   9602  O  OE2 . GLU A 1 1650 ? 119.775 145.852 117.218 1.00 85.65  ? 1221 GLU A OE2 1 
ATOM   9603  N  N   . LEU A 1 1651 ? 118.740 150.636 113.220 1.00 56.63  ? 1222 LEU A N   1 
ATOM   9604  C  CA  . LEU A 1 1651 ? 118.148 151.147 112.013 1.00 49.40  ? 1222 LEU A CA  1 
ATOM   9605  C  C   . LEU A 1 1651 ? 118.733 152.496 111.695 1.00 58.63  ? 1222 LEU A C   1 
ATOM   9606  O  O   . LEU A 1 1651 ? 119.078 152.783 110.542 1.00 67.20  ? 1222 LEU A O   1 
ATOM   9607  C  CB  . LEU A 1 1651 ? 116.643 151.211 112.180 1.00 45.86  ? 1222 LEU A CB  1 
ATOM   9608  C  CG  . LEU A 1 1651 ? 116.000 151.687 110.885 1.00 70.45  ? 1222 LEU A CG  1 
ATOM   9609  C  CD1 . LEU A 1 1651 ? 114.639 151.048 110.720 1.00 74.63  ? 1222 LEU A CD1 1 
ATOM   9610  C  CD2 . LEU A 1 1651 ? 115.830 153.213 110.891 1.00 72.59  ? 1222 LEU A CD2 1 
ATOM   9611  N  N   . ALA A 1 1652 ? 118.873 153.330 112.713 1.00 54.15  ? 1223 ALA A N   1 
ATOM   9612  C  CA  . ALA A 1 1652 ? 119.447 154.646 112.507 1.00 58.16  ? 1223 ALA A CA  1 
ATOM   9613  C  C   . ALA A 1 1652 ? 120.893 154.544 112.061 1.00 48.42  ? 1223 ALA A C   1 
ATOM   9614  O  O   . ALA A 1 1652 ? 121.335 155.302 111.194 1.00 58.93  ? 1223 ALA A O   1 
ATOM   9615  C  CB  . ALA A 1 1652 ? 119.334 155.469 113.785 1.00 70.20  ? 1223 ALA A CB  1 
ATOM   9616  N  N   . SER A 1 1653 ? 121.646 153.623 112.647 1.00 46.85  ? 1224 SER A N   1 
ATOM   9617  C  CA  . SER A 1 1653 ? 123.049 153.487 112.293 1.00 54.02  ? 1224 SER A CA  1 
ATOM   9618  C  C   . SER A 1 1653 ? 123.193 153.097 110.836 1.00 57.49  ? 1224 SER A C   1 
ATOM   9619  O  O   . SER A 1 1653 ? 124.012 153.662 110.100 1.00 65.25  ? 1224 SER A O   1 
ATOM   9620  C  CB  . SER A 1 1653 ? 123.715 152.448 113.191 1.00 61.96  ? 1224 SER A CB  1 
ATOM   9621  O  OG  . SER A 1 1653 ? 125.028 152.157 112.748 1.00 70.03  ? 1224 SER A OG  1 
ATOM   9622  N  N   . ARG A 1 1654 ? 122.379 152.156 110.396 1.00 58.12  ? 1225 ARG A N   1 
ATOM   9623  C  CA  . ARG A 1 1654 ? 122.429 151.749 109.004 1.00 56.55  ? 1225 ARG A CA  1 
ATOM   9624  C  C   . ARG A 1 1654 ? 122.036 152.891 108.098 1.00 46.48  ? 1225 ARG A C   1 
ATOM   9625  O  O   . ARG A 1 1654 ? 122.730 153.181 107.124 1.00 57.56  ? 1225 ARG A O   1 
ATOM   9626  C  CB  . ARG A 1 1654 ? 121.508 150.549 108.812 1.00 79.79  ? 1225 ARG A CB  1 
ATOM   9627  C  CG  . ARG A 1 1654 ? 122.164 149.269 109.289 1.00 90.07  ? 1225 ARG A CG  1 
ATOM   9628  C  CD  . ARG A 1 1654 ? 121.180 148.229 109.758 1.00 74.65  ? 1225 ARG A CD  1 
ATOM   9629  N  NE  . ARG A 1 1654 ? 121.891 147.007 110.123 1.00 86.81  ? 1225 ARG A NE  1 
ATOM   9630  C  CZ  . ARG A 1 1654 ? 122.539 146.836 111.275 1.00 93.17  ? 1225 ARG A CZ  1 
ATOM   9631  N  NH1 . ARG A 1 1654 ? 122.574 147.817 112.169 1.00 88.02  ? 1225 ARG A NH1 1 
ATOM   9632  N  NH2 . ARG A 1 1654 ? 123.161 145.687 111.529 1.00 96.13  ? 1225 ARG A NH2 1 
ATOM   9633  N  N   . LEU A 1 1655 ? 120.948 153.570 108.421 1.00 42.16  ? 1226 LEU A N   1 
ATOM   9634  C  CA  . LEU A 1 1655 ? 120.511 154.634 107.550 1.00 42.16  ? 1226 LEU A CA  1 
ATOM   9635  C  C   . LEU A 1 1655 ? 121.554 155.719 107.449 1.00 45.85  ? 1226 LEU A C   1 
ATOM   9636  O  O   . LEU A 1 1655 ? 121.823 156.224 106.357 1.00 59.11  ? 1226 LEU A O   1 
ATOM   9637  C  CB  . LEU A 1 1655 ? 119.203 155.204 108.043 1.00 49.11  ? 1226 LEU A CB  1 
ATOM   9638  C  CG  . LEU A 1 1655 ? 118.039 154.459 107.413 1.00 59.24  ? 1226 LEU A CG  1 
ATOM   9639  C  CD1 . LEU A 1 1655 ? 116.730 155.050 107.889 1.00 62.19  ? 1226 LEU A CD1 1 
ATOM   9640  C  CD2 . LEU A 1 1655 ? 118.160 154.579 105.910 1.00 64.84  ? 1226 LEU A CD2 1 
ATOM   9641  N  N   . THR A 1 1656 ? 122.157 156.096 108.561 1.00 46.16  ? 1227 THR A N   1 
ATOM   9642  C  CA  . THR A 1 1656 ? 123.158 157.138 108.468 1.00 46.16  ? 1227 THR A CA  1 
ATOM   9643  C  C   . THR A 1 1656 ? 124.324 156.666 107.634 1.00 47.71  ? 1227 THR A C   1 
ATOM   9644  O  O   . THR A 1 1656 ? 124.785 157.380 106.741 1.00 63.14  ? 1227 THR A O   1 
ATOM   9645  C  CB  . THR A 1 1656 ? 123.650 157.561 109.846 1.00 65.36  ? 1227 THR A CB  1 
ATOM   9646  O  OG1 . THR A 1 1656 ? 123.924 156.400 110.633 1.00 70.71  ? 1227 THR A OG1 1 
ATOM   9647  C  CG2 . THR A 1 1656 ? 122.605 158.427 110.557 1.00 72.38  ? 1227 THR A CG2 1 
ATOM   9648  N  N   . TRP A 1 1657 ? 124.797 155.451 107.883 1.00 51.48  ? 1228 TRP A N   1 
ATOM   9649  C  CA  . TRP A 1 1657 ? 126.001 155.006 107.199 1.00 59.90  ? 1228 TRP A CA  1 
ATOM   9650  C  C   . TRP A 1 1657 ? 125.780 154.908 105.698 1.00 64.34  ? 1228 TRP A C   1 
ATOM   9651  O  O   . TRP A 1 1657 ? 126.652 155.287 104.908 1.00 74.34  ? 1228 TRP A O   1 
ATOM   9652  C  CB  . TRP A 1 1657 ? 126.454 153.665 107.771 1.00 77.36  ? 1228 TRP A CB  1 
ATOM   9653  C  CG  . TRP A 1 1657 ? 127.560 152.981 107.000 1.00 95.15  ? 1228 TRP A CG  1 
ATOM   9654  C  CD1 . TRP A 1 1657 ? 128.749 153.526 106.586 1.00 104.33 ? 1228 TRP A CD1 1 
ATOM   9655  C  CD2 . TRP A 1 1657 ? 127.578 151.615 106.571 1.00 105.87 ? 1228 TRP A CD2 1 
ATOM   9656  N  NE1 . TRP A 1 1657 ? 129.498 152.582 105.918 1.00 105.31 ? 1228 TRP A NE1 1 
ATOM   9657  C  CE2 . TRP A 1 1657 ? 128.802 151.401 105.896 1.00 109.43 ? 1228 TRP A CE2 1 
ATOM   9658  C  CE3 . TRP A 1 1657 ? 126.674 150.551 106.689 1.00 112.02 ? 1228 TRP A CE3 1 
ATOM   9659  C  CZ2 . TRP A 1 1657 ? 129.144 150.162 105.341 1.00 116.27 ? 1228 TRP A CZ2 1 
ATOM   9660  C  CZ3 . TRP A 1 1657 ? 127.015 149.322 106.137 1.00 124.80 ? 1228 TRP A CZ3 1 
ATOM   9661  C  CH2 . TRP A 1 1657 ? 128.241 149.138 105.473 1.00 120.84 ? 1228 TRP A CH2 1 
ATOM   9662  N  N   . VAL A 1 1658 ? 124.624 154.397 105.286 1.00 63.93  ? 1229 VAL A N   1 
ATOM   9663  C  CA  . VAL A 1 1658 ? 124.362 154.207 103.864 1.00 64.60  ? 1229 VAL A CA  1 
ATOM   9664  C  C   . VAL A 1 1658 ? 124.135 155.539 103.177 1.00 55.01  ? 1229 VAL A C   1 
ATOM   9665  O  O   . VAL A 1 1658 ? 124.606 155.769 102.057 1.00 66.07  ? 1229 VAL A O   1 
ATOM   9666  C  CB  . VAL A 1 1658 ? 123.165 153.261 103.672 1.00 77.40  ? 1229 VAL A CB  1 
ATOM   9667  C  CG1 . VAL A 1 1658 ? 122.709 153.279 102.234 1.00 72.26  ? 1229 VAL A CG1 1 
ATOM   9668  C  CG2 . VAL A 1 1658 ? 123.536 151.825 104.124 1.00 86.78  ? 1229 VAL A CG2 1 
ATOM   9669  N  N   . THR A 1 1659 ? 123.414 156.434 103.831 1.00 49.45  ? 1230 THR A N   1 
ATOM   9670  C  CA  . THR A 1 1659 ? 123.057 157.705 103.231 1.00 51.98  ? 1230 THR A CA  1 
ATOM   9671  C  C   . THR A 1 1659 ? 124.006 158.779 103.687 1.00 59.38  ? 1230 THR A C   1 
ATOM   9672  O  O   . THR A 1 1659 ? 123.594 159.909 103.942 1.00 71.09  ? 1230 THR A O   1 
ATOM   9673  C  CB  . THR A 1 1659 ? 121.624 158.077 103.583 1.00 60.89  ? 1230 THR A CB  1 
ATOM   9674  O  OG1 . THR A 1 1659 ? 121.540 158.341 104.985 1.00 62.32  ? 1230 THR A OG1 1 
ATOM   9675  C  CG2 . THR A 1 1659 ? 120.673 156.926 103.249 1.00 63.41  ? 1230 THR A CG2 1 
ATOM   9676  N  N   . GLN A 1 1660 ? 125.282 158.434 103.852 1.00 65.36  ? 1231 GLN A N   1 
ATOM   9677  C  CA  . GLN A 1 1660 ? 126.238 159.401 104.387 1.00 76.81  ? 1231 GLN A CA  1 
ATOM   9678  C  C   . GLN A 1 1660 ? 126.464 160.559 103.420 1.00 88.65  ? 1231 GLN A C   1 
ATOM   9679  O  O   . GLN A 1 1660 ? 126.670 161.699 103.854 1.00 90.32  ? 1231 GLN A O   1 
ATOM   9680  C  CB  . GLN A 1 1660 ? 127.563 158.715 104.717 1.00 82.38  ? 1231 GLN A CB  1 
ATOM   9681  C  CG  . GLN A 1 1660 ? 128.401 159.436 105.782 1.00 94.78  ? 1231 GLN A CG  1 
ATOM   9682  C  CD  . GLN A 1 1660 ? 129.556 158.580 106.306 1.00 108.70 ? 1231 GLN A CD  1 
ATOM   9683  O  OE1 . GLN A 1 1660 ? 130.054 157.691 105.605 1.00 109.79 ? 1231 GLN A OE1 1 
ATOM   9684  N  NE2 . GLN A 1 1660 ? 129.984 158.844 107.542 1.00 104.90 ? 1231 GLN A NE2 1 
ATOM   9685  N  N   . GLY A 1 1661 ? 126.432 160.288 102.107 1.00 88.69  ? 1232 GLY A N   1 
ATOM   9686  C  CA  . GLY A 1 1661 ? 126.690 161.339 101.127 1.00 83.57  ? 1232 GLY A CA  1 
ATOM   9687  C  C   . GLY A 1 1661 ? 125.646 162.444 101.141 1.00 83.41  ? 1232 GLY A C   1 
ATOM   9688  O  O   . GLY A 1 1661 ? 125.982 163.630 101.077 1.00 84.54  ? 1232 GLY A O   1 
ATOM   9689  N  N   . SER A 1 1662 ? 124.371 162.073 101.228 1.00 84.53  ? 1233 SER A N   1 
ATOM   9690  C  CA  . SER A 1 1662 ? 123.291 163.053 101.242 1.00 86.55  ? 1233 SER A CA  1 
ATOM   9691  C  C   . SER A 1 1662 ? 123.235 163.803 102.572 1.00 77.89  ? 1233 SER A C   1 
ATOM   9692  O  O   . SER A 1 1662 ? 123.577 163.273 103.633 1.00 75.74  ? 1233 SER A O   1 
ATOM   9693  C  CB  . SER A 1 1662 ? 121.945 162.365 100.966 1.00 90.53  ? 1233 SER A CB  1 
ATOM   9694  O  OG  . SER A 1 1662 ? 121.644 161.358 101.927 1.00 81.11  ? 1233 SER A OG  1 
ATOM   9695  N  N   . SER A 1 1663 ? 122.791 165.055 102.505 1.00 81.88  ? 1234 SER A N   1 
ATOM   9696  C  CA  . SER A 1 1663 ? 122.684 165.897 103.692 1.00 95.02  ? 1234 SER A CA  1 
ATOM   9697  C  C   . SER A 1 1663 ? 121.323 165.803 104.371 1.00 85.18  ? 1234 SER A C   1 
ATOM   9698  O  O   . SER A 1 1663 ? 121.136 166.383 105.449 1.00 84.22  ? 1234 SER A O   1 
ATOM   9699  C  CB  . SER A 1 1663 ? 122.972 167.366 103.338 1.00 95.29  ? 1234 SER A CB  1 
ATOM   9700  O  OG  . SER A 1 1663 ? 121.976 167.896 102.475 1.00 89.93  ? 1234 SER A OG  1 
ATOM   9701  N  N   . ASN A 1 1664 ? 120.369 165.102 103.773 1.00 67.33  ? 1235 ASN A N   1 
ATOM   9702  C  CA  . ASN A 1 1664 ? 119.050 164.974 104.356 1.00 57.99  ? 1235 ASN A CA  1 
ATOM   9703  C  C   . ASN A 1 1664 ? 118.906 163.683 105.133 1.00 65.36  ? 1235 ASN A C   1 
ATOM   9704  O  O   . ASN A 1 1664 ? 117.790 163.179 105.285 1.00 70.41  ? 1235 ASN A O   1 
ATOM   9705  C  CB  . ASN A 1 1664 ? 118.003 165.044 103.261 1.00 61.21  ? 1235 ASN A CB  1 
ATOM   9706  C  CG  . ASN A 1 1664 ? 118.067 163.846 102.360 1.00 68.23  ? 1235 ASN A CG  1 
ATOM   9707  O  OD1 . ASN A 1 1664 ? 119.139 163.276 102.164 1.00 70.39  ? 1235 ASN A OD1 1 
ATOM   9708  N  ND2 . ASN A 1 1664 ? 116.922 163.431 101.827 1.00 72.64  ? 1235 ASN A ND2 1 
ATOM   9709  N  N   . SER A 1 1665 ? 120.017 163.125 105.612 1.00 68.38  ? 1236 SER A N   1 
ATOM   9710  C  CA  . SER A 1 1665 ? 119.956 161.805 106.228 1.00 67.75  ? 1236 SER A CA  1 
ATOM   9711  C  C   . SER A 1 1665 ? 118.897 161.774 107.311 1.00 59.01  ? 1236 SER A C   1 
ATOM   9712  O  O   . SER A 1 1665 ? 118.090 160.843 107.381 1.00 65.73  ? 1236 SER A O   1 
ATOM   9713  C  CB  . SER A 1 1665 ? 121.310 161.409 106.815 1.00 65.89  ? 1236 SER A CB  1 
ATOM   9714  O  OG  . SER A 1 1665 ? 121.676 162.287 107.860 1.00 74.93  ? 1236 SER A OG  1 
ATOM   9715  N  N   . ASP A 1 1666 ? 118.867 162.801 108.150 1.00 59.95  ? 1237 ASP A N   1 
ATOM   9716  C  CA  . ASP A 1 1666 ? 117.908 162.789 109.240 1.00 68.14  ? 1237 ASP A CA  1 
ATOM   9717  C  C   . ASP A 1 1666 ? 116.495 162.742 108.704 1.00 57.02  ? 1237 ASP A C   1 
ATOM   9718  O  O   . ASP A 1 1666 ? 115.669 161.958 109.183 1.00 69.20  ? 1237 ASP A O   1 
ATOM   9719  C  CB  . ASP A 1 1666 ? 118.115 163.998 110.153 1.00 89.03  ? 1237 ASP A CB  1 
ATOM   9720  C  CG  . ASP A 1 1666 ? 119.500 164.010 110.803 1.00 100.56 ? 1237 ASP A CG  1 
ATOM   9721  O  OD1 . ASP A 1 1666 ? 120.314 163.104 110.501 1.00 92.38  ? 1237 ASP A OD1 1 
ATOM   9722  O  OD2 . ASP A 1 1666 ? 119.767 164.916 111.628 1.00 96.77  ? 1237 ASP A OD2 1 
ATOM   9723  N  N   . LEU A 1 1667 ? 116.216 163.513 107.669 1.00 51.63  ? 1238 LEU A N   1 
ATOM   9724  C  CA  . LEU A 1 1667 ? 114.874 163.490 107.122 1.00 62.00  ? 1238 LEU A CA  1 
ATOM   9725  C  C   . LEU A 1 1667 ? 114.487 162.096 106.609 1.00 71.58  ? 1238 LEU A C   1 
ATOM   9726  O  O   . LEU A 1 1667 ? 113.291 161.786 106.538 1.00 72.49  ? 1238 LEU A O   1 
ATOM   9727  C  CB  . LEU A 1 1667 ? 114.764 164.548 106.020 1.00 74.32  ? 1238 LEU A CB  1 
ATOM   9728  C  CG  . LEU A 1 1667 ? 114.843 166.017 106.472 1.00 78.49  ? 1238 LEU A CG  1 
ATOM   9729  C  CD1 . LEU A 1 1667 ? 114.732 166.974 105.277 1.00 73.68  ? 1238 LEU A CD1 1 
ATOM   9730  C  CD2 . LEU A 1 1667 ? 113.787 166.341 107.536 1.00 71.17  ? 1238 LEU A CD2 1 
ATOM   9731  N  N   . LEU A 1 1668 ? 115.463 161.243 106.256 1.00 64.61  ? 1239 LEU A N   1 
ATOM   9732  C  CA  . LEU A 1 1668 ? 115.145 159.874 105.845 1.00 53.52  ? 1239 LEU A CA  1 
ATOM   9733  C  C   . LEU A 1 1668 ? 114.843 158.984 107.034 1.00 47.80  ? 1239 LEU A C   1 
ATOM   9734  O  O   . LEU A 1 1668 ? 113.993 158.097 106.946 1.00 52.45  ? 1239 LEU A O   1 
ATOM   9735  C  CB  . LEU A 1 1668 ? 116.299 159.271 105.058 1.00 59.94  ? 1239 LEU A CB  1 
ATOM   9736  C  CG  . LEU A 1 1668 ? 116.703 160.005 103.785 1.00 67.50  ? 1239 LEU A CG  1 
ATOM   9737  C  CD1 . LEU A 1 1668 ? 117.850 159.277 103.071 1.00 66.33  ? 1239 LEU A CD1 1 
ATOM   9738  C  CD2 . LEU A 1 1668 ? 115.486 160.188 102.873 1.00 64.99  ? 1239 LEU A CD2 1 
ATOM   9739  N  N   . ILE A 1 1669 ? 115.563 159.188 108.132 1.00 51.72  ? 1240 ILE A N   1 
ATOM   9740  C  CA  . ILE A 1 1669 ? 115.426 158.314 109.281 1.00 46.83  ? 1240 ILE A CA  1 
ATOM   9741  C  C   . ILE A 1 1669 ? 114.122 158.558 109.969 1.00 49.19  ? 1240 ILE A C   1 
ATOM   9742  O  O   . ILE A 1 1669 ? 113.539 157.637 110.546 1.00 58.93  ? 1240 ILE A O   1 
ATOM   9743  C  CB  . ILE A 1 1669 ? 116.573 158.528 110.269 1.00 50.19  ? 1240 ILE A CB  1 
ATOM   9744  C  CG1 . ILE A 1 1669 ? 117.909 158.466 109.551 1.00 58.85  ? 1240 ILE A CG1 1 
ATOM   9745  C  CG2 . ILE A 1 1669 ? 116.541 157.466 111.321 1.00 57.45  ? 1240 ILE A CG2 1 
ATOM   9746  C  CD1 . ILE A 1 1669 ? 119.078 158.782 110.454 1.00 62.43  ? 1240 ILE A CD1 1 
ATOM   9747  N  N   . LYS A 1 1670 ? 113.639 159.782 109.915 1.00 51.12  ? 1241 LYS A N   1 
ATOM   9748  C  CA  . LYS A 1 1670 ? 112.587 160.171 110.835 1.00 61.66  ? 1241 LYS A CA  1 
ATOM   9749  C  C   . LYS A 1 1670 ? 111.404 159.218 110.839 1.00 58.81  ? 1241 LYS A C   1 
ATOM   9750  O  O   . LYS A 1 1670 ? 110.959 158.858 111.938 1.00 70.18  ? 1241 LYS A O   1 
ATOM   9751  C  CB  . LYS A 1 1670 ? 112.123 161.608 110.551 1.00 70.77  ? 1241 LYS A CB  1 
ATOM   9752  C  CG  . LYS A 1 1670 ? 111.686 161.906 109.141 1.00 67.99  ? 1241 LYS A CG  1 
ATOM   9753  C  CD  . LYS A 1 1670 ? 111.145 163.319 109.063 1.00 80.41  ? 1241 LYS A CD  1 
ATOM   9754  C  CE  . LYS A 1 1670 ? 110.505 163.592 107.714 1.00 86.98  ? 1241 LYS A CE  1 
ATOM   9755  N  NZ  . LYS A 1 1670 ? 111.464 163.386 106.592 1.00 82.12  ? 1241 LYS A NZ  1 
ATOM   9756  N  N   . PRO A 1 1671 ? 110.867 158.749 109.715 1.00 47.67  ? 1242 PRO A N   1 
ATOM   9757  C  CA  . PRO A 1 1671 ? 109.606 158.011 109.829 1.00 51.53  ? 1242 PRO A CA  1 
ATOM   9758  C  C   . PRO A 1 1671 ? 109.780 156.713 110.563 1.00 53.82  ? 1242 PRO A C   1 
ATOM   9759  O  O   . PRO A 1 1671 ? 108.951 156.376 111.418 1.00 62.38  ? 1242 PRO A O   1 
ATOM   9760  C  CB  . PRO A 1 1671 ? 109.178 157.792 108.374 1.00 66.00  ? 1242 PRO A CB  1 
ATOM   9761  C  CG  . PRO A 1 1671 ? 110.078 158.684 107.559 1.00 71.03  ? 1242 PRO A CG  1 
ATOM   9762  C  CD  . PRO A 1 1671 ? 111.347 158.756 108.332 1.00 58.89  ? 1242 PRO A CD  1 
ATOM   9763  N  N   . PHE A 1 1672 ? 110.877 156.003 110.303 1.00 52.76  ? 1243 PHE A N   1 
ATOM   9764  C  CA  . PHE A 1 1672 ? 111.055 154.692 110.915 1.00 59.40  ? 1243 PHE A CA  1 
ATOM   9765  C  C   . PHE A 1 1672 ? 111.163 154.793 112.433 1.00 68.68  ? 1243 PHE A C   1 
ATOM   9766  O  O   . PHE A 1 1672 ? 110.428 154.115 113.163 1.00 71.97  ? 1243 PHE A O   1 
ATOM   9767  C  CB  . PHE A 1 1672 ? 112.273 153.988 110.333 1.00 55.50  ? 1243 PHE A CB  1 
ATOM   9768  C  CG  . PHE A 1 1672 ? 112.191 153.777 108.867 1.00 52.22  ? 1243 PHE A CG  1 
ATOM   9769  C  CD1 . PHE A 1 1672 ? 111.314 152.848 108.341 1.00 61.67  ? 1243 PHE A CD1 1 
ATOM   9770  C  CD2 . PHE A 1 1672 ? 113.022 154.463 108.013 1.00 53.10  ? 1243 PHE A CD2 1 
ATOM   9771  C  CE1 . PHE A 1 1672 ? 111.242 152.636 106.972 1.00 66.77  ? 1243 PHE A CE1 1 
ATOM   9772  C  CE2 . PHE A 1 1672 ? 112.963 154.256 106.649 1.00 52.75  ? 1243 PHE A CE2 1 
ATOM   9773  C  CZ  . PHE A 1 1672 ? 112.075 153.343 106.123 1.00 55.18  ? 1243 PHE A CZ  1 
ATOM   9774  N  N   . LEU A 1 1673 ? 112.055 155.648 112.936 1.00 60.48  ? 1244 LEU A N   1 
ATOM   9775  C  CA  . LEU A 1 1673 ? 112.135 155.808 114.380 1.00 51.35  ? 1244 LEU A CA  1 
ATOM   9776  C  C   . LEU A 1 1673 ? 110.829 156.284 114.972 1.00 50.95  ? 1244 LEU A C   1 
ATOM   9777  O  O   . LEU A 1 1673 ? 110.613 156.119 116.172 1.00 64.97  ? 1244 LEU A O   1 
ATOM   9778  C  CB  . LEU A 1 1673 ? 113.228 156.787 114.761 1.00 64.53  ? 1244 LEU A CB  1 
ATOM   9779  C  CG  . LEU A 1 1673 ? 114.584 156.392 114.196 1.00 82.18  ? 1244 LEU A CG  1 
ATOM   9780  C  CD1 . LEU A 1 1673 ? 115.667 157.288 114.791 1.00 88.01  ? 1244 LEU A CD1 1 
ATOM   9781  C  CD2 . LEU A 1 1673 ? 114.861 154.904 114.461 1.00 74.97  ? 1244 LEU A CD2 1 
ATOM   9782  N  N   . GLU A 1 1674 ? 109.961 156.885 114.179 1.00 54.71  ? 1245 GLU A N   1 
ATOM   9783  C  CA  . GLU A 1 1674 ? 108.724 157.352 114.769 1.00 64.63  ? 1245 GLU A CA  1 
ATOM   9784  C  C   . GLU A 1 1674 ? 107.756 156.210 115.028 1.00 64.68  ? 1245 GLU A C   1 
ATOM   9785  O  O   . GLU A 1 1674 ? 106.815 156.377 115.813 1.00 73.61  ? 1245 GLU A O   1 
ATOM   9786  C  CB  . GLU A 1 1674 ? 108.086 158.438 113.886 1.00 76.18  ? 1245 GLU A CB  1 
ATOM   9787  C  CG  . GLU A 1 1674 ? 108.710 159.853 114.093 1.00 84.57  ? 1245 GLU A CG  1 
ATOM   9788  C  CD  . GLU A 1 1674 ? 108.401 160.848 112.962 1.00 87.36  ? 1245 GLU A CD  1 
ATOM   9789  O  OE1 . GLU A 1 1674 ? 107.486 160.576 112.147 1.00 88.11  ? 1245 GLU A OE1 1 
ATOM   9790  O  OE2 . GLU A 1 1674 ? 109.078 161.903 112.894 1.00 74.72  ? 1245 GLU A OE2 1 
ATOM   9791  N  N   . ALA A 1 1675 ? 107.966 155.054 114.414 1.00 58.17  ? 1246 ALA A N   1 
ATOM   9792  C  CA  . ALA A 1 1675 ? 107.148 153.888 114.713 1.00 64.99  ? 1246 ALA A CA  1 
ATOM   9793  C  C   . ALA A 1 1675 ? 107.777 152.996 115.767 1.00 65.67  ? 1246 ALA A C   1 
ATOM   9794  O  O   . ALA A 1 1675 ? 107.196 151.962 116.109 1.00 66.98  ? 1246 ALA A O   1 
ATOM   9795  C  CB  . ALA A 1 1675 ? 106.888 153.064 113.444 1.00 69.80  ? 1246 ALA A CB  1 
ATOM   9796  N  N   . ARG A 1 1676 ? 108.945 153.356 116.276 1.00 60.82  ? 1247 ARG A N   1 
ATOM   9797  C  CA  . ARG A 1 1676 ? 109.689 152.439 117.122 1.00 55.99  ? 1247 ARG A CA  1 
ATOM   9798  C  C   . ARG A 1 1676 ? 110.036 153.009 118.485 1.00 57.23  ? 1247 ARG A C   1 
ATOM   9799  O  O   . ARG A 1 1676 ? 109.954 152.293 119.479 1.00 66.18  ? 1247 ARG A O   1 
ATOM   9800  C  CB  . ARG A 1 1676 ? 110.967 151.993 116.401 1.00 61.43  ? 1247 ARG A CB  1 
ATOM   9801  C  CG  . ARG A 1 1676 ? 110.689 151.395 115.032 1.00 62.17  ? 1247 ARG A CG  1 
ATOM   9802  C  CD  . ARG A 1 1676 ? 109.944 150.075 115.163 1.00 62.76  ? 1247 ARG A CD  1 
ATOM   9803  N  NE  . ARG A 1 1676 ? 110.829 149.011 115.608 1.00 62.79  ? 1247 ARG A NE  1 
ATOM   9804  C  CZ  . ARG A 1 1676 ? 110.426 147.790 115.933 1.00 66.68  ? 1247 ARG A CZ  1 
ATOM   9805  N  NH1 . ARG A 1 1676 ? 109.149 147.463 115.864 1.00 67.20  ? 1247 ARG A NH1 1 
ATOM   9806  N  NH2 . ARG A 1 1676 ? 111.309 146.887 116.330 1.00 74.47  ? 1247 ARG A NH2 1 
ATOM   9807  N  N   . VAL A 1 1677 ? 110.429 154.272 118.573 1.00 52.60  ? 1248 VAL A N   1 
ATOM   9808  C  CA  . VAL A 1 1677 ? 110.851 154.844 119.840 1.00 51.64  ? 1248 VAL A CA  1 
ATOM   9809  C  C   . VAL A 1 1677 ? 110.236 156.220 120.033 1.00 55.97  ? 1248 VAL A C   1 
ATOM   9810  O  O   . VAL A 1 1677 ? 109.835 156.901 119.089 1.00 62.12  ? 1248 VAL A O   1 
ATOM   9811  C  CB  . VAL A 1 1677 ? 112.386 154.940 119.962 1.00 62.31  ? 1248 VAL A CB  1 
ATOM   9812  C  CG1 . VAL A 1 1677 ? 112.993 153.569 120.087 1.00 71.91  ? 1248 VAL A CG1 1 
ATOM   9813  C  CG2 . VAL A 1 1677 ? 112.980 155.671 118.762 1.00 65.96  ? 1248 VAL A CG2 1 
ATOM   9814  N  N   . ASN A 1 1678 ? 110.170 156.624 121.281 1.00 55.47  ? 1249 ASN A N   1 
ATOM   9815  C  CA  . ASN A 1 1678 ? 109.779 157.973 121.589 1.00 52.51  ? 1249 ASN A CA  1 
ATOM   9816  C  C   . ASN A 1 1678 ? 111.050 158.770 121.808 1.00 42.82  ? 1249 ASN A C   1 
ATOM   9817  O  O   . ASN A 1 1678 ? 111.397 159.188 122.900 1.00 54.09  ? 1249 ASN A O   1 
ATOM   9818  C  CB  . ASN A 1 1678 ? 108.867 158.000 122.797 1.00 66.47  ? 1249 ASN A CB  1 
ATOM   9819  C  CG  . ASN A 1 1678 ? 107.418 157.850 122.407 1.00 80.50  ? 1249 ASN A CG  1 
ATOM   9820  O  OD1 . ASN A 1 1678 ? 107.032 158.180 121.282 1.00 78.35  ? 1249 ASN A OD1 1 
ATOM   9821  N  ND2 . ASN A 1 1678 ? 106.597 157.366 123.339 1.00 83.10  ? 1249 ASN A ND2 1 
ATOM   9822  N  N   . LEU A 1 1679 ? 111.768 158.916 120.744 1.00 42.53  ? 1250 LEU A N   1 
ATOM   9823  C  CA  . LEU A 1 1679 ? 112.938 159.733 120.807 1.00 42.53  ? 1250 LEU A CA  1 
ATOM   9824  C  C   . LEU A 1 1679 ? 112.920 160.648 119.615 1.00 49.26  ? 1250 LEU A C   1 
ATOM   9825  O  O   . LEU A 1 1679 ? 112.410 160.297 118.555 1.00 60.50  ? 1250 LEU A O   1 
ATOM   9826  C  CB  . LEU A 1 1679 ? 114.188 158.913 120.789 1.00 62.45  ? 1250 LEU A CB  1 
ATOM   9827  C  CG  . LEU A 1 1679 ? 114.708 158.281 122.079 1.00 76.42  ? 1250 LEU A CG  1 
ATOM   9828  C  CD1 . LEU A 1 1679 ? 115.079 159.310 123.145 1.00 78.60  ? 1250 LEU A CD1 1 
ATOM   9829  C  CD2 . LEU A 1 1679 ? 113.744 157.277 122.621 1.00 73.64  ? 1250 LEU A CD2 1 
ATOM   9830  N  N   . SER A 1 1680 ? 113.462 161.831 119.797 1.00 52.42  ? 1251 SER A N   1 
ATOM   9831  C  CA  . SER A 1 1680 ? 113.790 162.628 118.640 1.00 52.42  ? 1251 SER A CA  1 
ATOM   9832  C  C   . SER A 1 1680 ? 114.990 162.029 117.935 1.00 56.25  ? 1251 SER A C   1 
ATOM   9833  O  O   . SER A 1 1680 ? 115.882 161.445 118.558 1.00 57.52  ? 1251 SER A O   1 
ATOM   9834  C  CB  . SER A 1 1680 ? 114.136 164.048 119.039 1.00 75.97  ? 1251 SER A CB  1 
ATOM   9835  O  OG  . SER A 1 1680 ? 115.327 164.036 119.810 1.00 80.85  ? 1251 SER A OG  1 
ATOM   9836  N  N   . VAL A 1 1681 ? 115.032 162.257 116.625 1.00 65.94  ? 1252 VAL A N   1 
ATOM   9837  C  CA  . VAL A 1 1681 ? 116.114 161.739 115.801 1.00 69.54  ? 1252 VAL A CA  1 
ATOM   9838  C  C   . VAL A 1 1681 ? 117.457 162.145 116.375 1.00 78.69  ? 1252 VAL A C   1 
ATOM   9839  O  O   . VAL A 1 1681 ? 118.406 161.358 116.362 1.00 81.06  ? 1252 VAL A O   1 
ATOM   9840  C  CB  . VAL A 1 1681 ? 115.967 162.226 114.349 1.00 71.64  ? 1252 VAL A CB  1 
ATOM   9841  C  CG1 . VAL A 1 1681 ? 117.094 161.669 113.490 1.00 76.26  ? 1252 VAL A CG1 1 
ATOM   9842  C  CG2 . VAL A 1 1681 ? 114.607 161.831 113.784 1.00 78.84  ? 1252 VAL A CG2 1 
ATOM   9843  N  N   . GLN A 1 1682 ? 117.574 163.384 116.864 1.00 82.06  ? 1253 GLN A N   1 
ATOM   9844  C  CA  . GLN A 1 1682 ? 118.851 163.811 117.426 1.00 81.32  ? 1253 GLN A CA  1 
ATOM   9845  C  C   . GLN A 1 1682 ? 119.215 162.976 118.637 1.00 77.83  ? 1253 GLN A C   1 
ATOM   9846  O  O   . GLN A 1 1682 ? 120.391 162.641 118.835 1.00 87.57  ? 1253 GLN A O   1 
ATOM   9847  C  CB  . GLN A 1 1682 ? 118.844 165.303 117.773 1.00 83.18  ? 1253 GLN A CB  1 
ATOM   9848  C  CG  . GLN A 1 1682 ? 118.339 166.215 116.648 1.00 99.47  ? 1253 GLN A CG  1 
ATOM   9849  C  CD  . GLN A 1 1682 ? 119.087 166.010 115.316 1.00 107.04 ? 1253 GLN A CD  1 
ATOM   9850  O  OE1 . GLN A 1 1682 ? 118.465 165.810 114.267 1.00 97.68  ? 1253 GLN A OE1 1 
ATOM   9851  N  NE2 . GLN A 1 1682 ? 120.420 166.060 115.361 1.00 103.49 ? 1253 GLN A NE2 1 
ATOM   9852  N  N   . GLU A 1 1683 ? 118.228 162.587 119.438 1.00 61.52  ? 1254 GLU A N   1 
ATOM   9853  C  CA  . GLU A 1 1683 ? 118.572 161.761 120.583 1.00 64.99  ? 1254 GLU A CA  1 
ATOM   9854  C  C   . GLU A 1 1683 ? 119.110 160.410 120.151 1.00 77.55  ? 1254 GLU A C   1 
ATOM   9855  O  O   . GLU A 1 1683 ? 120.153 159.951 120.646 1.00 80.28  ? 1254 GLU A O   1 
ATOM   9856  C  CB  . GLU A 1 1683 ? 117.376 161.623 121.489 1.00 61.45  ? 1254 GLU A CB  1 
ATOM   9857  C  CG  . GLU A 1 1683 ? 117.190 162.926 122.202 1.00 82.06  ? 1254 GLU A CG  1 
ATOM   9858  C  CD  . GLU A 1 1683 ? 115.820 163.088 122.788 1.00 92.65  ? 1254 GLU A CD  1 
ATOM   9859  O  OE1 . GLU A 1 1683 ? 114.905 162.348 122.360 1.00 87.93  ? 1254 GLU A OE1 1 
ATOM   9860  O  OE2 . GLU A 1 1683 ? 115.654 163.960 123.672 1.00 93.91  ? 1254 GLU A OE2 1 
ATOM   9861  N  N   . ILE A 1 1684 ? 118.448 159.777 119.191 1.00 80.08  ? 1255 ILE A N   1 
ATOM   9862  C  CA  . ILE A 1 1684 ? 118.937 158.488 118.725 1.00 79.72  ? 1255 ILE A CA  1 
ATOM   9863  C  C   . ILE A 1 1684 ? 120.317 158.645 118.100 1.00 72.65  ? 1255 ILE A C   1 
ATOM   9864  O  O   . ILE A 1 1684 ? 121.236 157.883 118.407 1.00 81.81  ? 1255 ILE A O   1 
ATOM   9865  C  CB  . ILE A 1 1684 ? 117.922 157.849 117.761 1.00 87.07  ? 1255 ILE A CB  1 
ATOM   9866  C  CG1 . ILE A 1 1684 ? 116.672 157.398 118.538 1.00 86.62  ? 1255 ILE A CG1 1 
ATOM   9867  C  CG2 . ILE A 1 1684 ? 118.550 156.673 117.032 1.00 86.67  ? 1255 ILE A CG2 1 
ATOM   9868  C  CD1 . ILE A 1 1684 ? 116.938 156.329 119.616 1.00 82.53  ? 1255 ILE A CD1 1 
ATOM   9869  N  N   . LEU A 1 1685 ? 120.500 159.668 117.264 1.00 73.74  ? 1256 LEU A N   1 
ATOM   9870  C  CA  . LEU A 1 1685 ? 121.804 159.905 116.660 1.00 71.38  ? 1256 LEU A CA  1 
ATOM   9871  C  C   . LEU A 1 1685 ? 122.884 160.051 117.713 1.00 75.92  ? 1256 LEU A C   1 
ATOM   9872  O  O   . LEU A 1 1685 ? 124.034 159.672 117.475 1.00 81.71  ? 1256 LEU A O   1 
ATOM   9873  C  CB  . LEU A 1 1685 ? 121.770 161.148 115.784 1.00 64.71  ? 1256 LEU A CB  1 
ATOM   9874  C  CG  . LEU A 1 1685 ? 120.861 160.995 114.572 1.00 73.03  ? 1256 LEU A CG  1 
ATOM   9875  C  CD1 . LEU A 1 1685 ? 120.925 162.242 113.717 1.00 86.27  ? 1256 LEU A CD1 1 
ATOM   9876  C  CD2 . LEU A 1 1685 ? 121.203 159.741 113.774 1.00 81.33  ? 1256 LEU A CD2 1 
ATOM   9877  N  N   . GLN A 1 1686 ? 122.544 160.605 118.876 1.00 76.84  ? 1257 GLN A N   1 
ATOM   9878  C  CA  . GLN A 1 1686 ? 123.517 160.608 119.962 1.00 82.00  ? 1257 GLN A CA  1 
ATOM   9879  C  C   . GLN A 1 1686 ? 123.745 159.203 120.494 1.00 86.36  ? 1257 GLN A C   1 
ATOM   9880  O  O   . GLN A 1 1686 ? 124.866 158.864 120.890 1.00 92.73  ? 1257 GLN A O   1 
ATOM   9881  C  CB  . GLN A 1 1686 ? 123.083 161.543 121.092 1.00 86.69  ? 1257 GLN A CB  1 
ATOM   9882  C  CG  . GLN A 1 1686 ? 123.103 163.014 120.709 1.00 89.75  ? 1257 GLN A CG  1 
ATOM   9883  C  CD  . GLN A 1 1686 ? 124.473 163.460 120.229 1.00 98.04  ? 1257 GLN A CD  1 
ATOM   9884  O  OE1 . GLN A 1 1686 ? 124.625 163.931 119.099 1.00 98.11  ? 1257 GLN A OE1 1 
ATOM   9885  N  NE2 . GLN A 1 1686 ? 125.481 163.306 121.084 1.00 100.78 ? 1257 GLN A NE2 1 
ATOM   9886  N  N   . MET A 1 1687 ? 122.697 158.369 120.517 1.00 84.42  ? 1258 MET A N   1 
ATOM   9887  C  CA  . MET A 1 1687 ? 122.863 156.988 120.987 1.00 87.65  ? 1258 MET A CA  1 
ATOM   9888  C  C   . MET A 1 1687 ? 123.461 156.045 119.943 1.00 87.82  ? 1258 MET A C   1 
ATOM   9889  O  O   . MET A 1 1687 ? 123.815 154.914 120.300 1.00 88.04  ? 1258 MET A O   1 
ATOM   9890  C  CB  . MET A 1 1687 ? 121.525 156.402 121.458 1.00 89.98  ? 1258 MET A CB  1 
ATOM   9891  C  CG  . MET A 1 1687 ? 121.013 156.954 122.788 1.00 101.43 ? 1258 MET A CG  1 
ATOM   9892  S  SD  . MET A 1 1687 ? 119.546 156.097 123.418 1.00 108.23 ? 1258 MET A SD  1 
ATOM   9893  C  CE  . MET A 1 1687 ? 119.443 156.792 125.066 1.00 90.59  ? 1258 MET A CE  1 
ATOM   9894  N  N   . THR A 1 1688 ? 123.564 156.476 118.636 1.00 89.62  ? 1259 THR A N   1 
ATOM   9895  C  CA  . THR A 1 1688 ? 124.087 155.627 117.563 1.00 80.88  ? 1259 THR A CA  1 
ATOM   9896  C  C   . THR A 1 1688 ? 125.597 155.515 117.676 1.00 86.11  ? 1259 THR A C   1 
ATOM   9897  O  O   . THR A 1 1688 ? 126.271 156.494 118.001 1.00 93.91  ? 1259 THR A O   1 
ATOM   9898  C  CB  . THR A 1 1688 ? 123.755 156.178 116.168 1.00 85.52  ? 1259 THR A CB  1 
ATOM   9899  O  OG1 . THR A 1 1688 ? 124.170 157.547 116.071 1.00 91.24  ? 1259 THR A OG1 1 
ATOM   9900  C  CG2 . THR A 1 1688 ? 122.255 156.073 115.868 1.00 86.46  ? 1259 THR A CG2 1 
ATOM   9901  N  N   . PRO A 1 1689 ? 126.146 154.367 117.375 1.00 93.50  ? 1260 PRO A N   1 
ATOM   9902  C  CA  . PRO A 1 1689 ? 127.604 154.251 117.318 1.00 101.04 ? 1260 PRO A CA  1 
ATOM   9903  C  C   . PRO A 1 1689 ? 128.120 154.673 115.952 1.00 99.66  ? 1260 PRO A C   1 
ATOM   9904  O  O   . PRO A 1 1689 ? 129.271 154.403 115.591 1.00 106.15 ? 1260 PRO A O   1 
ATOM   9905  C  CB  . PRO A 1 1689 ? 127.847 152.763 117.620 1.00 103.48 ? 1260 PRO A CB  1 
ATOM   9906  C  CG  . PRO A 1 1689 ? 126.522 152.052 117.263 1.00 96.31  ? 1260 PRO A CG  1 
ATOM   9907  C  CD  . PRO A 1 1689 ? 125.469 153.113 117.000 1.00 94.30  ? 1260 PRO A CD  1 
ATOM   9908  N  N   . SER A 1 1690 ? 127.271 155.367 115.198 1.00 92.47  ? 1261 SER A N   1 
ATOM   9909  C  CA  . SER A 1 1690 ? 127.565 155.665 113.805 1.00 103.59 ? 1261 SER A CA  1 
ATOM   9910  C  C   . SER A 1 1690 ? 128.682 156.692 113.688 1.00 115.78 ? 1261 SER A C   1 
ATOM   9911  O  O   . SER A 1 1690 ? 128.432 157.857 113.359 1.00 117.66 ? 1261 SER A O   1 
ATOM   9912  C  CB  . SER A 1 1690 ? 126.307 156.172 113.088 1.00 98.81  ? 1261 SER A CB  1 
ATOM   9913  O  OG  . SER A 1 1690 ? 126.571 156.498 111.727 1.00 87.64  ? 1261 SER A OG  1 
ATOM   9914  N  N   . HIS A 1 1691 ? 129.922 156.269 113.956 1.00 124.24 ? 1262 HIS A N   1 
ATOM   9915  C  CA  . HIS A 1 1691 ? 131.089 157.112 113.733 1.00 140.34 ? 1262 HIS A CA  1 
ATOM   9916  C  C   . HIS A 1 1691 ? 132.047 156.563 112.674 1.00 146.15 ? 1262 HIS A C   1 
ATOM   9917  O  O   . HIS A 1 1691 ? 132.909 157.315 112.198 1.00 143.66 ? 1262 HIS A O   1 
ATOM   9918  C  CB  . HIS A 1 1691 ? 131.853 157.338 115.056 1.00 141.22 ? 1262 HIS A CB  1 
ATOM   9919  C  CG  . HIS A 1 1691 ? 132.891 158.428 114.989 1.00 153.65 ? 1262 HIS A CG  1 
ATOM   9920  N  ND1 . HIS A 1 1691 ? 132.566 159.759 114.811 1.00 152.74 ? 1262 HIS A ND1 1 
ATOM   9921  C  CD2 . HIS A 1 1691 ? 134.243 158.385 115.093 1.00 150.84 ? 1262 HIS A CD2 1 
ATOM   9922  C  CE1 . HIS A 1 1691 ? 133.671 160.485 114.799 1.00 149.59 ? 1262 HIS A CE1 1 
ATOM   9923  N  NE2 . HIS A 1 1691 ? 134.703 159.676 114.968 1.00 150.28 ? 1262 HIS A NE2 1 
ATOM   9924  N  N   . TYR A 1 1692 ? 131.915 155.295 112.279 1.00 142.15 ? 1263 TYR A N   1 
ATOM   9925  C  CA  . TYR A 1 1692 ? 132.823 154.670 111.324 1.00 144.12 ? 1263 TYR A CA  1 
ATOM   9926  C  C   . TYR A 1 1692 ? 132.341 154.889 109.885 1.00 140.44 ? 1263 TYR A C   1 
ATOM   9927  O  O   . TYR A 1 1692 ? 131.158 155.131 109.625 1.00 132.57 ? 1263 TYR A O   1 
ATOM   9928  C  CB  . TYR A 1 1692 ? 132.973 153.166 111.623 1.00 141.95 ? 1263 TYR A CB  1 
ATOM   9929  C  CG  . TYR A 1 1692 ? 133.450 152.831 113.038 1.00 145.66 ? 1263 TYR A CG  1 
ATOM   9930  C  CD1 . TYR A 1 1692 ? 134.811 152.669 113.326 1.00 141.41 ? 1263 TYR A CD1 1 
ATOM   9931  C  CD2 . TYR A 1 1692 ? 132.540 152.707 114.093 1.00 141.21 ? 1263 TYR A CD2 1 
ATOM   9932  C  CE1 . TYR A 1 1692 ? 135.245 152.367 114.623 1.00 138.11 ? 1263 TYR A CE1 1 
ATOM   9933  C  CE2 . TYR A 1 1692 ? 132.964 152.414 115.390 1.00 135.45 ? 1263 TYR A CE2 1 
ATOM   9934  C  CZ  . TYR A 1 1692 ? 134.315 152.244 115.650 1.00 136.68 ? 1263 TYR A CZ  1 
ATOM   9935  O  OH  . TYR A 1 1692 ? 134.728 151.953 116.936 1.00 124.93 ? 1263 TYR A OH  1 
ATOM   9936  N  N   . SER A 1 1693 ? 133.291 154.813 108.948 1.00 142.85 ? 1264 SER A N   1 
ATOM   9937  C  CA  . SER A 1 1693 ? 133.016 154.993 107.525 1.00 139.13 ? 1264 SER A CA  1 
ATOM   9938  C  C   . SER A 1 1693 ? 133.961 154.104 106.716 1.00 142.99 ? 1264 SER A C   1 
ATOM   9939  O  O   . SER A 1 1693 ? 135.001 153.653 107.209 1.00 139.75 ? 1264 SER A O   1 
ATOM   9940  C  CB  . SER A 1 1693 ? 133.146 156.472 107.106 1.00 130.22 ? 1264 SER A CB  1 
ATOM   9941  O  OG  . SER A 1 1693 ? 132.892 156.645 105.720 1.00 127.18 ? 1264 SER A OG  1 
ATOM   9942  N  N   . GLY A 1 1694 ? 133.575 153.843 105.470 1.00 139.53 ? 1265 GLY A N   1 
ATOM   9943  C  CA  . GLY A 1 1694 ? 134.334 152.966 104.598 1.00 134.59 ? 1265 GLY A CA  1 
ATOM   9944  C  C   . GLY A 1 1694 ? 133.531 152.645 103.351 1.00 129.44 ? 1265 GLY A C   1 
ATOM   9945  O  O   . GLY A 1 1694 ? 132.509 153.280 103.072 1.00 125.89 ? 1265 GLY A O   1 
ATOM   9946  N  N   . ASN A 1 1695 ? 134.010 151.648 102.599 1.00 122.26 ? 1266 ASN A N   1 
ATOM   9947  C  CA  . ASN A 1 1695 ? 133.289 151.200 101.409 1.00 116.83 ? 1266 ASN A CA  1 
ATOM   9948  C  C   . ASN A 1 1695 ? 132.010 150.475 101.835 1.00 111.38 ? 1266 ASN A C   1 
ATOM   9949  O  O   . ASN A 1 1695 ? 132.075 149.471 102.553 1.00 108.53 ? 1266 ASN A O   1 
ATOM   9950  C  CB  . ASN A 1 1695 ? 134.182 150.294 100.552 1.00 113.99 ? 1266 ASN A CB  1 
ATOM   9951  C  CG  . ASN A 1 1695 ? 133.528 149.905 99.217  1.00 110.72 ? 1266 ASN A CG  1 
ATOM   9952  O  OD1 . ASN A 1 1695 ? 132.698 150.645 98.679  1.00 101.57 ? 1266 ASN A OD1 1 
ATOM   9953  N  ND2 . ASN A 1 1695 ? 133.910 148.743 98.680  1.00 106.97 ? 1266 ASN A ND2 1 
ATOM   9954  N  N   . ILE A 1 1696 ? 130.846 150.994 101.410 1.00 106.08 ? 1267 ILE A N   1 
ATOM   9955  C  CA  . ILE A 1 1696 ? 129.567 150.425 101.847 1.00 95.59  ? 1267 ILE A CA  1 
ATOM   9956  C  C   . ILE A 1 1696 ? 129.435 148.969 101.422 1.00 96.23  ? 1267 ILE A C   1 
ATOM   9957  O  O   . ILE A 1 1696 ? 129.086 148.101 102.228 1.00 102.94 ? 1267 ILE A O   1 
ATOM   9958  C  CB  . ILE A 1 1696 ? 128.382 151.257 101.329 1.00 86.29  ? 1267 ILE A CB  1 
ATOM   9959  C  CG1 . ILE A 1 1696 ? 127.078 150.654 101.833 1.00 84.57  ? 1267 ILE A CG1 1 
ATOM   9960  C  CG2 . ILE A 1 1696 ? 128.378 151.395 99.813  1.00 87.82  ? 1267 ILE A CG2 1 
ATOM   9961  C  CD1 . ILE A 1 1696 ? 125.891 151.474 101.478 1.00 83.16  ? 1267 ILE A CD1 1 
ATOM   9962  N  N   . VAL A 1 1697 ? 129.702 148.678 100.154 1.00 93.66  ? 1268 VAL A N   1 
ATOM   9963  C  CA  . VAL A 1 1697 ? 129.399 147.351 99.645  1.00 89.92  ? 1268 VAL A CA  1 
ATOM   9964  C  C   . VAL A 1 1697 ? 130.285 146.304 100.311 1.00 95.80  ? 1268 VAL A C   1 
ATOM   9965  O  O   . VAL A 1 1697 ? 129.785 145.336 100.893 1.00 102.62 ? 1268 VAL A O   1 
ATOM   9966  C  CB  . VAL A 1 1697 ? 129.504 147.337 98.110  1.00 92.79  ? 1268 VAL A CB  1 
ATOM   9967  C  CG1 . VAL A 1 1697 ? 128.519 148.341 97.521  1.00 92.64  ? 1268 VAL A CG1 1 
ATOM   9968  C  CG2 . VAL A 1 1697 ? 130.899 147.701 97.653  1.00 99.97  ? 1268 VAL A CG2 1 
ATOM   9969  N  N   . HIS A 1 1698 ? 131.607 146.513 100.301 1.00 102.34 ? 1269 HIS A N   1 
ATOM   9970  C  CA  . HIS A 1 1698 ? 132.521 145.474 100.771 1.00 113.53 ? 1269 HIS A CA  1 
ATOM   9971  C  C   . HIS A 1 1698 ? 132.284 145.201 102.253 1.00 116.64 ? 1269 HIS A C   1 
ATOM   9972  O  O   . HIS A 1 1698 ? 132.091 144.050 102.665 1.00 120.13 ? 1269 HIS A O   1 
ATOM   9973  C  CB  . HIS A 1 1698 ? 133.986 145.881 100.502 1.00 112.14 ? 1269 HIS A CB  1 
ATOM   9974  C  CG  . HIS A 1 1698 ? 134.996 144.780 100.716 1.00 121.26 ? 1269 HIS A CG  1 
ATOM   9975  N  ND1 . HIS A 1 1698 ? 134.670 143.438 100.673 1.00 123.06 ? 1269 HIS A ND1 1 
ATOM   9976  C  CD2 . HIS A 1 1698 ? 136.326 144.829 100.983 1.00 119.08 ? 1269 HIS A CD2 1 
ATOM   9977  C  CE1 . HIS A 1 1698 ? 135.753 142.709 100.892 1.00 115.61 ? 1269 HIS A CE1 1 
ATOM   9978  N  NE2 . HIS A 1 1698 ? 136.771 143.529 101.089 1.00 117.18 ? 1269 HIS A NE2 1 
ATOM   9979  N  N   . ARG A 1 1699 ? 132.228 146.261 103.063 1.00 116.69 ? 1270 ARG A N   1 
ATOM   9980  C  CA  . ARG A 1 1699 ? 132.013 146.112 104.498 1.00 119.12 ? 1270 ARG A CA  1 
ATOM   9981  C  C   . ARG A 1 1699 ? 130.593 145.666 104.784 1.00 104.91 ? 1270 ARG A C   1 
ATOM   9982  O  O   . ARG A 1 1699 ? 130.270 145.337 105.929 1.00 112.09 ? 1270 ARG A O   1 
ATOM   9983  C  CB  . ARG A 1 1699 ? 132.373 147.448 105.174 1.00 126.40 ? 1270 ARG A CB  1 
ATOM   9984  C  CG  . ARG A 1 1699 ? 132.448 147.578 106.717 1.00 124.32 ? 1270 ARG A CG  1 
ATOM   9985  C  CD  . ARG A 1 1699 ? 131.165 148.072 107.390 1.00 126.97 ? 1270 ARG A CD  1 
ATOM   9986  N  NE  . ARG A 1 1699 ? 131.391 148.354 108.814 1.00 128.98 ? 1270 ARG A NE  1 
ATOM   9987  C  CZ  . ARG A 1 1699 ? 131.297 147.473 109.809 1.00 131.68 ? 1270 ARG A CZ  1 
ATOM   9988  N  NH1 . ARG A 1 1699 ? 130.975 146.213 109.562 1.00 135.32 ? 1270 ARG A NH1 1 
ATOM   9989  N  NH2 . ARG A 1 1699 ? 131.529 147.866 111.060 1.00 125.89 ? 1270 ARG A NH2 1 
ATOM   9990  N  N   . TYR A 1 1700 ? 129.747 145.650 103.761 1.00 96.67  ? 1271 TYR A N   1 
ATOM   9991  C  CA  . TYR A 1 1700 ? 128.432 145.067 103.907 1.00 101.47 ? 1271 TYR A CA  1 
ATOM   9992  C  C   . TYR A 1 1700 ? 128.469 143.549 103.814 1.00 116.74 ? 1271 TYR A C   1 
ATOM   9993  O  O   . TYR A 1 1700 ? 127.626 142.881 104.423 1.00 119.71 ? 1271 TYR A O   1 
ATOM   9994  C  CB  . TYR A 1 1700 ? 127.498 145.601 102.838 1.00 103.50 ? 1271 TYR A CB  1 
ATOM   9995  C  CG  . TYR A 1 1700 ? 126.091 145.651 103.329 1.00 103.99 ? 1271 TYR A CG  1 
ATOM   9996  C  CD1 . TYR A 1 1700 ? 125.552 146.833 103.831 1.00 105.43 ? 1271 TYR A CD1 1 
ATOM   9997  C  CD2 . TYR A 1 1700 ? 125.326 144.497 103.392 1.00 110.12 ? 1271 TYR A CD2 1 
ATOM   9998  C  CE1 . TYR A 1 1700 ? 124.259 146.885 104.314 1.00 102.66 ? 1271 TYR A CE1 1 
ATOM   9999  C  CE2 . TYR A 1 1700 ? 124.035 144.525 103.883 1.00 111.18 ? 1271 TYR A CE2 1 
ATOM   10000 C  CZ  . TYR A 1 1700 ? 123.505 145.724 104.344 1.00 107.26 ? 1271 TYR A CZ  1 
ATOM   10001 O  OH  . TYR A 1 1700 ? 122.219 145.752 104.830 1.00 88.91  ? 1271 TYR A OH  1 
ATOM   10002 N  N   . ASN A 1 1701 ? 129.418 142.988 103.045 1.00 124.71 ? 1272 ASN A N   1 
ATOM   10003 C  CA  . ASN A 1 1701 ? 129.514 141.541 102.805 1.00 132.14 ? 1272 ASN A CA  1 
ATOM   10004 C  C   . ASN A 1 1701 ? 130.311 140.788 103.885 1.00 135.39 ? 1272 ASN A C   1 
ATOM   10005 O  O   . ASN A 1 1701 ? 129.955 139.654 104.234 1.00 129.66 ? 1272 ASN A O   1 
ATOM   10006 C  CB  . ASN A 1 1701 ? 130.141 141.252 101.421 1.00 114.27 ? 1272 ASN A CB  1 
ATOM   10007 C  CG  . ASN A 1 1701 ? 129.399 141.927 100.262 1.00 99.76  ? 1272 ASN A CG  1 
ATOM   10008 O  OD1 . ASN A 1 1701 ? 128.188 142.156 100.322 1.00 100.25 ? 1272 ASN A OD1 1 
ATOM   10009 N  ND2 . ASN A 1 1701 ? 130.131 142.221 99.188  1.00 88.45  ? 1272 ASN A ND2 1 
ATOM   10010 N  N   . ASP A 1 1702 ? 131.393 141.384 104.411 1.00 136.56 ? 1273 ASP A N   1 
ATOM   10011 C  CA  . ASP A 1 1702 ? 132.246 140.693 105.384 1.00 142.41 ? 1273 ASP A CA  1 
ATOM   10012 C  C   . ASP A 1 1702 ? 131.591 140.608 106.767 1.00 145.49 ? 1273 ASP A C   1 
ATOM   10013 O  O   . ASP A 1 1702 ? 131.606 139.545 107.405 1.00 137.39 ? 1273 ASP A O   1 
ATOM   10014 C  CB  . ASP A 1 1702 ? 133.614 141.391 105.477 1.00 143.98 ? 1273 ASP A CB  1 
ATOM   10015 C  CG  . ASP A 1 1702 ? 134.350 141.446 104.138 1.00 140.54 ? 1273 ASP A CG  1 
ATOM   10016 O  OD1 . ASP A 1 1702 ? 133.758 141.068 103.098 1.00 135.29 ? 1273 ASP A OD1 1 
ATOM   10017 O  OD2 . ASP A 1 1702 ? 135.519 141.896 104.126 1.00 136.47 ? 1273 ASP A OD2 1 
ATOM   10018 N  N   . GLN A 1 1703 ? 131.013 141.726 107.254 1.00 145.99 ? 1274 GLN A N   1 
ATOM   10019 C  CA  . GLN A 1 1703 ? 130.502 141.838 108.625 1.00 149.32 ? 1274 GLN A CA  1 
ATOM   10020 C  C   . GLN A 1 1703 ? 128.993 142.095 108.727 1.00 146.89 ? 1274 GLN A C   1 
ATOM   10021 O  O   . GLN A 1 1703 ? 128.396 141.736 109.749 1.00 142.85 ? 1274 GLN A O   1 
ATOM   10022 C  CB  . GLN A 1 1703 ? 131.248 142.957 109.399 1.00 141.68 ? 1274 GLN A CB  1 
ATOM   10023 C  CG  . GLN A 1 1703 ? 132.787 142.800 109.507 1.00 134.75 ? 1274 GLN A CG  1 
ATOM   10024 C  CD  . GLN A 1 1703 ? 133.445 143.849 110.416 1.00 129.71 ? 1274 GLN A CD  1 
ATOM   10025 O  OE1 . GLN A 1 1703 ? 132.789 144.453 111.268 1.00 127.36 ? 1274 GLN A OE1 1 
ATOM   10026 N  NE2 . GLN A 1 1703 ? 134.747 144.065 110.229 1.00 124.46 ? 1274 GLN A NE2 1 
ATOM   10027 N  N   . TYR A 1 1704 ? 128.358 142.705 107.711 1.00 143.58 ? 1275 TYR A N   1 
ATOM   10028 C  CA  . TYR A 1 1704 ? 126.920 142.999 107.735 1.00 143.39 ? 1275 TYR A CA  1 
ATOM   10029 C  C   . TYR A 1 1704 ? 126.062 141.954 107.022 1.00 136.55 ? 1275 TYR A C   1 
ATOM   10030 O  O   . TYR A 1 1704 ? 124.850 141.903 107.271 1.00 134.08 ? 1275 TYR A O   1 
ATOM   10031 C  CB  . TYR A 1 1704 ? 126.631 144.386 107.120 1.00 135.31 ? 1275 TYR A CB  1 
ATOM   10032 C  CG  . TYR A 1 1704 ? 126.690 145.559 108.104 1.00 137.39 ? 1275 TYR A CG  1 
ATOM   10033 C  CD1 . TYR A 1 1704 ? 125.630 145.819 108.986 1.00 130.98 ? 1275 TYR A CD1 1 
ATOM   10034 C  CD2 . TYR A 1 1704 ? 127.797 146.414 108.143 1.00 132.63 ? 1275 TYR A CD2 1 
ATOM   10035 C  CE1 . TYR A 1 1704 ? 125.678 146.892 109.887 1.00 126.35 ? 1275 TYR A CE1 1 
ATOM   10036 C  CE2 . TYR A 1 1704 ? 127.853 147.490 109.040 1.00 133.42 ? 1275 TYR A CE2 1 
ATOM   10037 C  CZ  . TYR A 1 1704 ? 126.791 147.724 109.910 1.00 130.58 ? 1275 TYR A CZ  1 
ATOM   10038 O  OH  . TYR A 1 1704 ? 126.843 148.784 110.796 1.00 121.87 ? 1275 TYR A OH  1 
ATOM   10039 N  N   . SER A 1 1705 ? 126.647 141.133 106.150 1.00 131.53 ? 1276 SER A N   1 
ATOM   10040 C  CA  . SER A 1 1705 ? 125.890 140.062 105.515 1.00 133.84 ? 1276 SER A CA  1 
ATOM   10041 C  C   . SER A 1 1705 ? 125.460 139.034 106.567 1.00 142.57 ? 1276 SER A C   1 
ATOM   10042 O  O   . SER A 1 1705 ? 126.221 138.749 107.503 1.00 137.82 ? 1276 SER A O   1 
ATOM   10043 C  CB  . SER A 1 1705 ? 126.730 139.392 104.423 1.00 128.26 ? 1276 SER A CB  1 
ATOM   10044 O  OG  . SER A 1 1705 ? 127.957 138.902 104.942 1.00 126.87 ? 1276 SER A OG  1 
ATOM   10045 N  N   . PRO A 1 1706 ? 124.243 138.474 106.456 1.00 147.04 ? 1277 PRO A N   1 
ATOM   10046 C  CA  . PRO A 1 1706 ? 123.807 137.467 107.453 1.00 147.16 ? 1277 PRO A CA  1 
ATOM   10047 C  C   . PRO A 1 1706 ? 124.682 136.205 107.512 1.00 141.13 ? 1277 PRO A C   1 
ATOM   10048 O  O   . PRO A 1 1706 ? 124.877 135.653 108.606 1.00 131.69 ? 1277 PRO A O   1 
ATOM   10049 C  CB  . PRO A 1 1706 ? 122.358 137.158 107.023 1.00 141.06 ? 1277 PRO A CB  1 
ATOM   10050 C  CG  . PRO A 1 1706 ? 122.300 137.514 105.550 1.00 133.71 ? 1277 PRO A CG  1 
ATOM   10051 C  CD  . PRO A 1 1706 ? 123.222 138.710 105.410 1.00 137.98 ? 1277 PRO A CD  1 
ATOM   10052 N  N   . HIS A 1 1707 ? 125.227 135.752 106.373 1.00 140.73 ? 1278 HIS A N   1 
ATOM   10053 C  CA  . HIS A 1 1707 ? 126.017 134.521 106.297 1.00 130.63 ? 1278 HIS A CA  1 
ATOM   10054 C  C   . HIS A 1 1707 ? 127.436 134.755 106.836 1.00 119.78 ? 1278 HIS A C   1 
ATOM   10055 O  O   . HIS A 1 1707 ? 128.096 135.737 106.474 1.00 118.37 ? 1278 HIS A O   1 
ATOM   10056 C  CB  . HIS A 1 1707 ? 126.089 134.009 104.843 1.00 124.84 ? 1278 HIS A CB  1 
ATOM   10057 C  CG  . HIS A 1 1707 ? 124.798 134.112 104.069 1.00 125.22 ? 1278 HIS A CG  1 
ATOM   10058 N  ND1 . HIS A 1 1707 ? 123.633 133.482 104.455 1.00 126.78 ? 1278 HIS A ND1 1 
ATOM   10059 C  CD2 . HIS A 1 1707 ? 124.504 134.761 102.913 1.00 125.84 ? 1278 HIS A CD2 1 
ATOM   10060 C  CE1 . HIS A 1 1707 ? 122.676 133.748 103.582 1.00 126.03 ? 1278 HIS A CE1 1 
ATOM   10061 N  NE2 . HIS A 1 1707 ? 123.178 134.522 102.637 1.00 126.13 ? 1278 HIS A NE2 1 
ATOM   10062 N  N   . SER A 1 1708 ? 127.913 133.847 107.689 1.00 109.38 ? 1279 SER A N   1 
ATOM   10063 C  CA  . SER A 1 1708 ? 129.240 133.975 108.282 1.00 103.67 ? 1279 SER A CA  1 
ATOM   10064 C  C   . SER A 1 1708 ? 130.344 133.367 107.409 1.00 91.46  ? 1279 SER A C   1 
ATOM   10065 O  O   . SER A 1 1708 ? 131.524 133.477 107.758 1.00 95.38  ? 1279 SER A O   1 
ATOM   10066 C  CB  . SER A 1 1708 ? 129.239 133.343 109.689 1.00 107.16 ? 1279 SER A CB  1 
ATOM   10067 O  OG  . SER A 1 1708 ? 130.447 133.587 110.399 1.00 104.10 ? 1279 SER A OG  1 
ATOM   10068 N  N   . PHE A 1 1709 ? 129.988 132.735 106.290 1.00 83.41  ? 1280 PHE A N   1 
ATOM   10069 C  CA  . PHE A 1 1709 ? 130.945 132.203 105.306 1.00 75.88  ? 1280 PHE A CA  1 
ATOM   10070 C  C   . PHE A 1 1709 ? 131.849 131.108 105.883 1.00 60.47  ? 1280 PHE A C   1 
ATOM   10071 O  O   . PHE A 1 1709 ? 133.068 131.140 105.736 1.00 57.41  ? 1280 PHE A O   1 
ATOM   10072 C  CB  . PHE A 1 1709 ? 131.774 133.333 104.677 1.00 74.86  ? 1280 PHE A CB  1 
ATOM   10073 C  CG  . PHE A 1 1709 ? 131.015 134.173 103.639 1.00 84.31  ? 1280 PHE A CG  1 
ATOM   10074 C  CD1 . PHE A 1 1709 ? 129.662 134.451 103.781 1.00 99.14  ? 1280 PHE A CD1 1 
ATOM   10075 C  CD2 . PHE A 1 1709 ? 131.657 134.671 102.514 1.00 70.53  ? 1280 PHE A CD2 1 
ATOM   10076 C  CE1 . PHE A 1 1709 ? 128.973 135.210 102.818 1.00 99.89  ? 1280 PHE A CE1 1 
ATOM   10077 C  CE2 . PHE A 1 1709 ? 130.962 135.416 101.552 1.00 68.73  ? 1280 PHE A CE2 1 
ATOM   10078 C  CZ  . PHE A 1 1709 ? 129.634 135.687 101.705 1.00 81.07  ? 1280 PHE A CZ  1 
ATOM   10079 N  N   . MET A 1 1710 ? 131.220 130.107 106.493 1.00 63.41  ? 1281 MET A N   1 
ATOM   10080 C  CA  . MET A 1 1710 ? 131.904 128.941 107.009 1.00 61.01  ? 1281 MET A CA  1 
ATOM   10081 C  C   . MET A 1 1710 ? 132.361 128.034 105.863 1.00 58.96  ? 1281 MET A C   1 
ATOM   10082 O  O   . MET A 1 1710 ? 131.796 128.048 104.752 1.00 62.12  ? 1281 MET A O   1 
ATOM   10083 C  CB  . MET A 1 1710 ? 130.991 128.188 107.972 1.00 69.97  ? 1281 MET A CB  1 
ATOM   10084 C  CG  . MET A 1 1710 ? 130.355 129.071 109.101 1.00 90.84  ? 1281 MET A CG  1 
ATOM   10085 S  SD  . MET A 1 1710 ? 131.340 129.413 110.600 1.00 126.53 ? 1281 MET A SD  1 
ATOM   10086 C  CE  . MET A 1 1710 ? 132.226 130.917 110.182 1.00 91.92  ? 1281 MET A CE  1 
ATOM   10087 N  N   . ALA A 1 1711 ? 133.353 127.191 106.138 1.00 60.58  ? 1282 ALA A N   1 
ATOM   10088 C  CA  . ALA A 1 1711 ? 133.856 126.247 105.144 1.00 59.32  ? 1282 ALA A CA  1 
ATOM   10089 C  C   . ALA A 1 1711 ? 133.035 124.971 105.223 1.00 51.05  ? 1282 ALA A C   1 
ATOM   10090 O  O   . ALA A 1 1711 ? 132.472 124.662 106.269 1.00 51.29  ? 1282 ALA A O   1 
ATOM   10091 C  CB  . ALA A 1 1711 ? 135.323 125.948 105.385 1.00 71.86  ? 1282 ALA A CB  1 
ATOM   10092 N  N   . ASN A 1 1712 ? 132.946 124.235 104.120 1.00 53.30  ? 1283 ASN A N   1 
ATOM   10093 C  CA  . ASN A 1 1712 ? 132.160 123.007 104.103 1.00 57.94  ? 1283 ASN A CA  1 
ATOM   10094 C  C   . ASN A 1 1712 ? 133.025 121.771 104.238 1.00 57.41  ? 1283 ASN A C   1 
ATOM   10095 O  O   . ASN A 1 1712 ? 132.542 120.646 104.124 1.00 57.93  ? 1283 ASN A O   1 
ATOM   10096 C  CB  . ASN A 1 1712 ? 131.306 122.916 102.841 1.00 61.70  ? 1283 ASN A CB  1 
ATOM   10097 C  CG  . ASN A 1 1712 ? 130.011 122.169 103.071 1.00 59.33  ? 1283 ASN A CG  1 
ATOM   10098 O  OD1 . ASN A 1 1712 ? 129.311 122.409 104.052 1.00 54.87  ? 1283 ASN A OD1 1 
ATOM   10099 N  ND2 . ASN A 1 1712 ? 129.677 121.270 102.156 1.00 65.14  ? 1283 ASN A ND2 1 
ATOM   10100 N  N   . ARG A 1 1713 ? 134.307 121.987 104.476 1.00 46.27  ? 1284 ARG A N   1 
ATOM   10101 C  CA  . ARG A 1 1713 ? 135.250 120.899 104.618 1.00 31.07  ? 1284 ARG A CA  1 
ATOM   10102 C  C   . ARG A 1 1713 ? 135.866 120.891 106.009 1.00 36.80  ? 1284 ARG A C   1 
ATOM   10103 O  O   . ARG A 1 1713 ? 136.200 121.940 106.549 1.00 52.62  ? 1284 ARG A O   1 
ATOM   10104 C  CB  . ARG A 1 1713 ? 136.332 121.018 103.554 1.00 36.88  ? 1284 ARG A CB  1 
ATOM   10105 C  CG  . ARG A 1 1713 ? 137.289 119.852 103.534 1.00 42.42  ? 1284 ARG A CG  1 
ATOM   10106 C  CD  . ARG A 1 1713 ? 136.506 118.563 103.468 1.00 45.81  ? 1284 ARG A CD  1 
ATOM   10107 N  NE  . ARG A 1 1713 ? 135.641 118.555 102.302 1.00 35.28  ? 1284 ARG A NE  1 
ATOM   10108 C  CZ  . ARG A 1 1713 ? 135.902 117.878 101.196 1.00 43.28  ? 1284 ARG A CZ  1 
ATOM   10109 N  NH1 . ARG A 1 1713 ? 137.002 117.149 101.118 1.00 46.73  ? 1284 ARG A NH1 1 
ATOM   10110 N  NH2 . ARG A 1 1713 ? 135.063 117.922 100.172 1.00 55.66  ? 1284 ARG A NH2 1 
ATOM   10111 N  N   . MET A 1 1714 ? 135.985 119.700 106.586 1.00 36.43  ? 1285 MET A N   1 
ATOM   10112 C  CA  . MET A 1 1714 ? 136.563 119.468 107.916 1.00 37.84  ? 1285 MET A CA  1 
ATOM   10113 C  C   . MET A 1 1714 ? 137.775 120.323 108.268 1.00 47.72  ? 1285 MET A C   1 
ATOM   10114 O  O   . MET A 1 1714 ? 138.698 120.479 107.473 1.00 51.80  ? 1285 MET A O   1 
ATOM   10115 C  CB  . MET A 1 1714 ? 136.962 118.003 108.054 1.00 35.32  ? 1285 MET A CB  1 
ATOM   10116 C  CG  . MET A 1 1714 ? 135.879 117.078 108.562 1.00 36.70  ? 1285 MET A CG  1 
ATOM   10117 S  SD  . MET A 1 1714 ? 136.584 115.448 108.828 1.00 41.45  ? 1285 MET A SD  1 
ATOM   10118 C  CE  . MET A 1 1714 ? 137.476 115.208 107.299 1.00 41.29  ? 1285 MET A CE  1 
ATOM   10119 N  N   . SER A 1 1715 ? 137.799 120.826 109.494 1.00 40.52  ? 1286 SER A N   1 
ATOM   10120 C  CA  . SER A 1 1715 ? 138.878 121.693 109.935 1.00 34.64  ? 1286 SER A CA  1 
ATOM   10121 C  C   . SER A 1 1715 ? 140.222 120.999 110.047 1.00 36.99  ? 1286 SER A C   1 
ATOM   10122 O  O   . SER A 1 1715 ? 141.206 121.664 110.382 1.00 43.57  ? 1286 SER A O   1 
ATOM   10123 C  CB  . SER A 1 1715 ? 138.551 122.310 111.288 1.00 43.37  ? 1286 SER A CB  1 
ATOM   10124 O  OG  . SER A 1 1715 ? 137.340 123.034 111.215 1.00 60.09  ? 1286 SER A OG  1 
ATOM   10125 N  N   . ASN A 1 1716 ? 140.315 119.697 109.823 1.00 33.95  ? 1287 ASN A N   1 
ATOM   10126 C  CA  . ASN A 1 1716 ? 141.589 119.053 110.067 1.00 23.45  ? 1287 ASN A CA  1 
ATOM   10127 C  C   . ASN A 1 1716 ? 142.595 119.503 109.063 1.00 25.96  ? 1287 ASN A C   1 
ATOM   10128 O  O   . ASN A 1 1716 ? 143.772 119.640 109.387 1.00 40.23  ? 1287 ASN A O   1 
ATOM   10129 C  CB  . ASN A 1 1716 ? 141.450 117.550 110.029 1.00 30.70  ? 1287 ASN A CB  1 
ATOM   10130 C  CG  . ASN A 1 1716 ? 140.697 117.017 111.237 1.00 40.73  ? 1287 ASN A CG  1 
ATOM   10131 O  OD1 . ASN A 1 1716 ? 140.847 117.533 112.344 1.00 40.33  ? 1287 ASN A OD1 1 
ATOM   10132 N  ND2 . ASN A 1 1716 ? 139.858 116.004 111.028 1.00 37.87  ? 1287 ASN A ND2 1 
ATOM   10133 N  N   . SER A 1 1717 ? 142.166 119.748 107.842 1.00 27.07  ? 1288 SER A N   1 
ATOM   10134 C  CA  . SER A 1 1717 ? 143.154 120.125 106.848 1.00 36.30  ? 1288 SER A CA  1 
ATOM   10135 C  C   . SER A 1 1717 ? 143.481 121.613 106.868 1.00 43.81  ? 1288 SER A C   1 
ATOM   10136 O  O   . SER A 1 1717 ? 144.539 122.003 106.356 1.00 44.83  ? 1288 SER A O   1 
ATOM   10137 C  CB  . SER A 1 1717 ? 142.686 119.724 105.452 1.00 51.58  ? 1288 SER A CB  1 
ATOM   10138 O  OG  . SER A 1 1717 ? 143.655 120.090 104.475 1.00 55.16  ? 1288 SER A OG  1 
ATOM   10139 N  N   . ALA A 1 1718 ? 142.608 122.452 107.432 1.00 42.23  ? 1289 ALA A N   1 
ATOM   10140 C  CA  . ALA A 1 1718 ? 142.912 123.880 107.486 1.00 44.73  ? 1289 ALA A CA  1 
ATOM   10141 C  C   . ALA A 1 1718 ? 144.120 124.159 108.380 1.00 45.85  ? 1289 ALA A C   1 
ATOM   10142 O  O   . ALA A 1 1718 ? 144.942 125.025 108.064 1.00 50.70  ? 1289 ALA A O   1 
ATOM   10143 C  CB  . ALA A 1 1718 ? 141.688 124.667 107.958 1.00 59.82  ? 1289 ALA A CB  1 
ATOM   10144 N  N   . THR A 1 1719 ? 144.253 123.433 109.491 1.00 36.98  ? 1290 THR A N   1 
ATOM   10145 C  CA  . THR A 1 1719 ? 145.407 123.624 110.354 1.00 38.97  ? 1290 THR A CA  1 
ATOM   10146 C  C   . THR A 1 1719 ? 146.684 123.154 109.700 1.00 33.17  ? 1290 THR A C   1 
ATOM   10147 O  O   . THR A 1 1719 ? 147.770 123.580 110.094 1.00 46.53  ? 1290 THR A O   1 
ATOM   10148 C  CB  . THR A 1 1719 ? 145.239 122.863 111.656 1.00 47.36  ? 1290 THR A CB  1 
ATOM   10149 O  OG1 . THR A 1 1719 ? 145.067 121.471 111.366 1.00 44.00  ? 1290 THR A OG1 1 
ATOM   10150 C  CG2 . THR A 1 1719 ? 144.014 123.362 112.402 1.00 54.64  ? 1290 THR A CG2 1 
ATOM   10151 N  N   . ARG A 1 1720 ? 146.592 122.292 108.730 1.00 25.25  ? 1291 ARG A N   1 
ATOM   10152 C  CA  . ARG A 1 1720 ? 147.819 121.897 108.093 1.00 26.04  ? 1291 ARG A CA  1 
ATOM   10153 C  C   . ARG A 1 1720 ? 148.275 122.858 107.020 1.00 37.47  ? 1291 ARG A C   1 
ATOM   10154 O  O   . ARG A 1 1720 ? 149.244 122.542 106.333 1.00 51.88  ? 1291 ARG A O   1 
ATOM   10155 C  CB  . ARG A 1 1720 ? 147.646 120.517 107.506 1.00 37.35  ? 1291 ARG A CB  1 
ATOM   10156 C  CG  . ARG A 1 1720 ? 147.887 119.471 108.539 1.00 44.22  ? 1291 ARG A CG  1 
ATOM   10157 C  CD  . ARG A 1 1720 ? 149.328 119.014 108.582 1.00 40.03  ? 1291 ARG A CD  1 
ATOM   10158 N  NE  . ARG A 1 1720 ? 149.521 117.994 107.555 1.00 39.86  ? 1291 ARG A NE  1 
ATOM   10159 C  CZ  . ARG A 1 1720 ? 150.695 117.488 107.217 1.00 44.81  ? 1291 ARG A CZ  1 
ATOM   10160 N  NH1 . ARG A 1 1720 ? 151.779 117.922 107.834 1.00 52.35  ? 1291 ARG A NH1 1 
ATOM   10161 N  NH2 . ARG A 1 1720 ? 150.780 116.543 106.283 1.00 41.91  ? 1291 ARG A NH2 1 
ATOM   10162 N  N   . LEU A 1 1721 ? 147.631 123.999 106.820 1.00 35.99  ? 1292 LEU A N   1 
ATOM   10163 C  CA  . LEU A 1 1721 ? 148.016 124.847 105.701 1.00 36.94  ? 1292 LEU A CA  1 
ATOM   10164 C  C   . LEU A 1 1721 ? 148.210 126.287 106.126 1.00 42.47  ? 1292 LEU A C   1 
ATOM   10165 O  O   . LEU A 1 1721 ? 147.559 126.764 107.054 1.00 47.77  ? 1292 LEU A O   1 
ATOM   10166 C  CB  . LEU A 1 1721 ? 146.991 124.823 104.567 1.00 41.96  ? 1292 LEU A CB  1 
ATOM   10167 C  CG  . LEU A 1 1721 ? 146.748 123.477 103.884 1.00 45.34  ? 1292 LEU A CG  1 
ATOM   10168 C  CD1 . LEU A 1 1721 ? 145.659 123.621 102.829 1.00 48.73  ? 1292 LEU A CD1 1 
ATOM   10169 C  CD2 . LEU A 1 1721 ? 148.033 122.905 103.283 1.00 51.38  ? 1292 LEU A CD2 1 
ATOM   10170 N  N   . ILE A 1 1722 ? 149.106 126.981 105.421 1.00 46.47  ? 1293 ILE A N   1 
ATOM   10171 C  CA  . ILE A 1 1722 ? 149.238 128.432 105.528 1.00 43.47  ? 1293 ILE A CA  1 
ATOM   10172 C  C   . ILE A 1 1722 ? 148.715 129.051 104.245 1.00 44.79  ? 1293 ILE A C   1 
ATOM   10173 O  O   . ILE A 1 1722 ? 149.111 128.644 103.144 1.00 50.06  ? 1293 ILE A O   1 
ATOM   10174 C  CB  . ILE A 1 1722 ? 150.683 128.884 105.790 1.00 50.94  ? 1293 ILE A CB  1 
ATOM   10175 C  CG1 . ILE A 1 1722 ? 151.665 128.231 104.814 1.00 57.02  ? 1293 ILE A CG1 1 
ATOM   10176 C  CG2 . ILE A 1 1722 ? 151.074 128.580 107.233 1.00 60.94  ? 1293 ILE A CG2 1 
ATOM   10177 C  CD1 . ILE A 1 1722 ? 153.084 128.789 104.946 1.00 60.71  ? 1293 ILE A CD1 1 
ATOM   10178 N  N   . VAL A 1 1723 ? 147.818 130.021 104.391 1.00 42.75  ? 1294 VAL A N   1 
ATOM   10179 C  CA  . VAL A 1 1723 ? 147.119 130.648 103.275 1.00 40.96  ? 1294 VAL A CA  1 
ATOM   10180 C  C   . VAL A 1 1723 ? 147.385 132.141 103.353 1.00 36.49  ? 1294 VAL A C   1 
ATOM   10181 O  O   . VAL A 1 1723 ? 146.775 132.859 104.150 1.00 46.04  ? 1294 VAL A O   1 
ATOM   10182 C  CB  . VAL A 1 1723 ? 145.620 130.337 103.280 1.00 46.34  ? 1294 VAL A CB  1 
ATOM   10183 C  CG1 . VAL A 1 1723 ? 145.388 128.891 102.907 1.00 53.11  ? 1294 VAL A CG1 1 
ATOM   10184 C  CG2 . VAL A 1 1723 ? 145.062 130.533 104.668 1.00 49.80  ? 1294 VAL A CG2 1 
ATOM   10185 N  N   . SER A 1 1724 ? 148.293 132.614 102.522 1.00 36.78  ? 1295 SER A N   1 
ATOM   10186 C  CA  . SER A 1 1724 ? 148.715 134.000 102.543 1.00 42.56  ? 1295 SER A CA  1 
ATOM   10187 C  C   . SER A 1 1724 ? 148.025 134.736 101.410 1.00 43.12  ? 1295 SER A C   1 
ATOM   10188 O  O   . SER A 1 1724 ? 148.136 134.337 100.241 1.00 48.03  ? 1295 SER A O   1 
ATOM   10189 C  CB  . SER A 1 1724 ? 150.229 134.105 102.405 1.00 49.78  ? 1295 SER A CB  1 
ATOM   10190 O  OG  . SER A 1 1724 ? 150.622 133.631 101.129 1.00 52.20  ? 1295 SER A OG  1 
ATOM   10191 N  N   . THR A 1 1725 ? 147.305 135.794 101.759 1.00 43.21  ? 1296 THR A N   1 
ATOM   10192 C  CA  . THR A 1 1725 ? 146.682 136.647 100.769 1.00 49.33  ? 1296 THR A CA  1 
ATOM   10193 C  C   . THR A 1 1725 ? 147.487 137.901 100.495 1.00 56.35  ? 1296 THR A C   1 
ATOM   10194 O  O   . THR A 1 1725 ? 147.051 138.735 99.699  1.00 65.46  ? 1296 THR A O   1 
ATOM   10195 C  CB  . THR A 1 1725 ? 145.264 137.036 101.200 1.00 50.73  ? 1296 THR A CB  1 
ATOM   10196 O  OG1 . THR A 1 1725 ? 145.303 137.689 102.474 1.00 46.03  ? 1296 THR A OG1 1 
ATOM   10197 C  CG2 . THR A 1 1725 ? 144.384 135.796 101.283 1.00 56.84  ? 1296 THR A CG2 1 
ATOM   10198 N  N   . ASN A 1 1726 ? 148.645 138.063 101.125 1.00 50.89  ? 1297 ASN A N   1 
ATOM   10199 C  CA  . ASN A 1 1726 ? 149.433 139.248 100.837 1.00 52.15  ? 1297 ASN A CA  1 
ATOM   10200 C  C   . ASN A 1 1726 ? 149.955 139.252 99.409  1.00 55.70  ? 1297 ASN A C   1 
ATOM   10201 O  O   . ASN A 1 1726 ? 150.274 140.324 98.890  1.00 67.60  ? 1297 ASN A O   1 
ATOM   10202 C  CB  . ASN A 1 1726 ? 150.601 139.373 101.817 1.00 64.35  ? 1297 ASN A CB  1 
ATOM   10203 C  CG  . ASN A 1 1726 ? 151.495 138.134 101.828 1.00 75.96  ? 1297 ASN A CG  1 
ATOM   10204 O  OD1 . ASN A 1 1726 ? 151.284 137.195 101.054 1.00 71.63  ? 1297 ASN A OD1 1 
ATOM   10205 N  ND2 . ASN A 1 1726 ? 152.496 138.127 102.713 1.00 72.23  ? 1297 ASN A ND2 1 
ATOM   10206 N  N   . THR A 1 1727 ? 150.040 138.098 98.753  1.00 48.64  ? 1298 THR A N   1 
ATOM   10207 C  CA  . THR A 1 1727 ? 150.605 138.105 97.411  1.00 49.83  ? 1298 THR A CA  1 
ATOM   10208 C  C   . THR A 1 1727 ? 149.600 138.540 96.370  1.00 51.93  ? 1298 THR A C   1 
ATOM   10209 O  O   . THR A 1 1727 ? 149.933 138.545 95.180  1.00 55.18  ? 1298 THR A O   1 
ATOM   10210 C  CB  . THR A 1 1727 ? 151.137 136.734 97.009  1.00 60.11  ? 1298 THR A CB  1 
ATOM   10211 O  OG1 . THR A 1 1727 ? 150.078 135.773 97.073  1.00 61.19  ? 1298 THR A OG1 1 
ATOM   10212 C  CG2 . THR A 1 1727 ? 152.277 136.289 97.932  1.00 66.20  ? 1298 THR A CG2 1 
ATOM   10213 N  N   . LEU A 1 1728 ? 148.380 138.877 96.783  1.00 57.63  ? 1299 LEU A N   1 
ATOM   10214 C  CA  . LEU A 1 1728 ? 147.401 139.407 95.846  1.00 62.13  ? 1299 LEU A CA  1 
ATOM   10215 C  C   . LEU A 1 1728 ? 147.783 140.789 95.317  1.00 81.02  ? 1299 LEU A C   1 
ATOM   10216 O  O   . LEU A 1 1728 ? 147.068 141.313 94.449  1.00 85.44  ? 1299 LEU A O   1 
ATOM   10217 C  CB  . LEU A 1 1728 ? 146.012 139.457 96.497  1.00 62.89  ? 1299 LEU A CB  1 
ATOM   10218 C  CG  . LEU A 1 1728 ? 145.195 138.165 96.527  1.00 58.43  ? 1299 LEU A CG  1 
ATOM   10219 C  CD1 . LEU A 1 1728 ? 143.880 138.359 97.268  1.00 65.47  ? 1299 LEU A CD1 1 
ATOM   10220 C  CD2 . LEU A 1 1728 ? 144.922 137.683 95.109  1.00 61.20  ? 1299 LEU A CD2 1 
ATOM   10221 N  N   . GLY A 1 1729 ? 148.880 141.383 95.798  1.00 78.65  ? 1300 GLY A N   1 
ATOM   10222 C  CA  . GLY A 1 1729 ? 149.257 142.712 95.334  1.00 79.24  ? 1300 GLY A CA  1 
ATOM   10223 C  C   . GLY A 1 1729 ? 148.245 143.747 95.793  1.00 84.69  ? 1300 GLY A C   1 
ATOM   10224 O  O   . GLY A 1 1729 ? 147.850 143.792 96.967  1.00 80.04  ? 1300 GLY A O   1 
ATOM   10225 N  N   . GLU A 1 1730 ? 147.803 144.585 94.854  1.00 84.89  ? 1301 GLU A N   1 
ATOM   10226 C  CA  . GLU A 1 1730 ? 146.900 145.663 95.225  1.00 85.93  ? 1301 GLU A CA  1 
ATOM   10227 C  C   . GLU A 1 1730 ? 145.634 145.109 95.854  1.00 80.40  ? 1301 GLU A C   1 
ATOM   10228 O  O   . GLU A 1 1730 ? 145.123 145.666 96.831  1.00 86.81  ? 1301 GLU A O   1 
ATOM   10229 C  CB  . GLU A 1 1730 ? 146.573 146.537 94.008  1.00 94.96  ? 1301 GLU A CB  1 
ATOM   10230 C  CG  . GLU A 1 1730 ? 146.009 145.802 92.786  1.00 99.20  ? 1301 GLU A CG  1 
ATOM   10231 C  CD  . GLU A 1 1730 ? 147.092 145.239 91.861  1.00 103.27 ? 1301 GLU A CD  1 
ATOM   10232 O  OE1 . GLU A 1 1730 ? 148.162 144.831 92.363  1.00 101.49 ? 1301 GLU A OE1 1 
ATOM   10233 O  OE2 . GLU A 1 1730 ? 146.870 145.201 90.627  1.00 103.40 ? 1301 GLU A OE2 1 
ATOM   10234 N  N   . PHE A 1 1731 ? 145.132 143.993 95.337  1.00 74.26  ? 1302 PHE A N   1 
ATOM   10235 C  CA  . PHE A 1 1731 ? 143.859 143.504 95.832  1.00 74.21  ? 1302 PHE A CA  1 
ATOM   10236 C  C   . PHE A 1 1731 ? 143.965 143.041 97.265  1.00 64.12  ? 1302 PHE A C   1 
ATOM   10237 O  O   . PHE A 1 1731 ? 142.938 142.868 97.922  1.00 72.29  ? 1302 PHE A O   1 
ATOM   10238 C  CB  . PHE A 1 1731 ? 143.336 142.372 94.951  1.00 85.11  ? 1302 PHE A CB  1 
ATOM   10239 C  CG  . PHE A 1 1731 ? 143.222 142.737 93.480  1.00 97.16  ? 1302 PHE A CG  1 
ATOM   10240 C  CD1 . PHE A 1 1731 ? 142.114 143.427 92.993  1.00 96.67  ? 1302 PHE A CD1 1 
ATOM   10241 C  CD2 . PHE A 1 1731 ? 144.221 142.371 92.577  1.00 100.70 ? 1302 PHE A CD2 1 
ATOM   10242 C  CE1 . PHE A 1 1731 ? 142.010 143.755 91.631  1.00 97.31  ? 1302 PHE A CE1 1 
ATOM   10243 C  CE2 . PHE A 1 1731 ? 144.122 142.693 91.218  1.00 96.90  ? 1302 PHE A CE2 1 
ATOM   10244 C  CZ  . PHE A 1 1731 ? 143.014 143.385 90.748  1.00 94.45  ? 1302 PHE A CZ  1 
ATOM   10245 N  N   . SER A 1 1732 ? 145.174 142.844 97.764  1.00 61.52  ? 1303 SER A N   1 
ATOM   10246 C  CA  . SER A 1 1732 ? 145.334 142.483 99.162  1.00 68.44  ? 1303 SER A CA  1 
ATOM   10247 C  C   . SER A 1 1732 ? 144.915 143.632 100.066 1.00 67.27  ? 1303 SER A C   1 
ATOM   10248 O  O   . SER A 1 1732 ? 145.106 144.805 99.736  1.00 76.81  ? 1303 SER A O   1 
ATOM   10249 C  CB  . SER A 1 1732 ? 146.783 142.104 99.456  1.00 74.77  ? 1303 SER A CB  1 
ATOM   10250 O  OG  . SER A 1 1732 ? 146.949 141.810 100.835 1.00 72.05  ? 1303 SER A OG  1 
ATOM   10251 N  N   . GLY A 1 1733 ? 144.342 143.288 101.212 1.00 57.51  ? 1304 GLY A N   1 
ATOM   10252 C  CA  . GLY A 1 1733 ? 143.947 144.289 102.180 1.00 53.69  ? 1304 GLY A CA  1 
ATOM   10253 C  C   . GLY A 1 1733 ? 145.150 145.014 102.740 1.00 61.00  ? 1304 GLY A C   1 
ATOM   10254 O  O   . GLY A 1 1733 ? 145.514 146.087 102.256 1.00 71.30  ? 1304 GLY A O   1 
ATOM   10255 N  N   . ALA A 1 1738 ? 144.961 149.297 101.467 1.00 110.25 ? 1309 ALA A N   1 
ATOM   10256 C  CA  . ALA A 1 1738 ? 143.709 150.050 101.387 1.00 119.64 ? 1309 ALA A CA  1 
ATOM   10257 C  C   . ALA A 1 1738 ? 143.061 149.905 99.997  1.00 127.12 ? 1309 ALA A C   1 
ATOM   10258 O  O   . ALA A 1 1738 ? 143.207 150.787 99.143  1.00 121.71 ? 1309 ALA A O   1 
ATOM   10259 C  CB  . ALA A 1 1738 ? 143.951 151.535 101.726 1.00 105.10 ? 1309 ALA A CB  1 
ATOM   10260 N  N   . ARG A 1 1739 ? 142.346 148.791 99.782  1.00 125.32 ? 1310 ARG A N   1 
ATOM   10261 C  CA  . ARG A 1 1739 ? 141.728 148.473 98.496  1.00 120.93 ? 1310 ARG A CA  1 
ATOM   10262 C  C   . ARG A 1 1739 ? 140.376 147.797 98.717  1.00 107.69 ? 1310 ARG A C   1 
ATOM   10263 O  O   . ARG A 1 1739 ? 140.165 147.102 99.715  1.00 107.90 ? 1310 ARG A O   1 
ATOM   10264 C  CB  . ARG A 1 1739 ? 142.646 147.563 97.641  1.00 114.27 ? 1310 ARG A CB  1 
ATOM   10265 C  CG  . ARG A 1 1739 ? 142.178 147.308 96.187  1.00 114.05 ? 1310 ARG A CG  1 
ATOM   10266 C  CD  . ARG A 1 1739 ? 142.045 148.627 95.389  1.00 122.23 ? 1310 ARG A CD  1 
ATOM   10267 N  NE  . ARG A 1 1739 ? 141.671 148.436 93.981  1.00 120.40 ? 1310 ARG A NE  1 
ATOM   10268 C  CZ  . ARG A 1 1739 ? 142.538 148.326 92.973  1.00 121.21 ? 1310 ARG A CZ  1 
ATOM   10269 N  NH1 . ARG A 1 1739 ? 143.845 148.405 93.202  1.00 113.87 ? 1310 ARG A NH1 1 
ATOM   10270 N  NH2 . ARG A 1 1739 ? 142.095 148.150 91.731  1.00 116.26 ? 1310 ARG A NH2 1 
ATOM   10271 N  N   . ASP A 1 1740 ? 139.466 148.000 97.765  1.00 94.08  ? 1311 ASP A N   1 
ATOM   10272 C  CA  . ASP A 1 1740 ? 138.143 147.396 97.792  1.00 86.39  ? 1311 ASP A CA  1 
ATOM   10273 C  C   . ASP A 1 1740 ? 137.928 146.580 96.527  1.00 82.50  ? 1311 ASP A C   1 
ATOM   10274 O  O   . ASP A 1 1740 ? 138.274 147.022 95.427  1.00 83.91  ? 1311 ASP A O   1 
ATOM   10275 C  CB  . ASP A 1 1740 ? 137.073 148.461 97.899  1.00 94.93  ? 1311 ASP A CB  1 
ATOM   10276 C  CG  . ASP A 1 1740 ? 137.279 149.579 96.897  1.00 101.25 ? 1311 ASP A CG  1 
ATOM   10277 O  OD1 . ASP A 1 1740 ? 138.362 149.619 96.272  1.00 95.44  ? 1311 ASP A OD1 1 
ATOM   10278 O  OD2 . ASP A 1 1740 ? 136.357 150.408 96.720  1.00 98.75  ? 1311 ASP A OD2 1 
ATOM   10279 N  N   . SER A 1 1741 ? 137.347 145.392 96.682  1.00 79.58  ? 1312 SER A N   1 
ATOM   10280 C  CA  . SER A 1 1741 ? 137.142 144.515 95.537  1.00 70.23  ? 1312 SER A CA  1 
ATOM   10281 C  C   . SER A 1 1741 ? 135.990 143.561 95.802  1.00 54.97  ? 1312 SER A C   1 
ATOM   10282 O  O   . SER A 1 1741 ? 135.578 143.340 96.941  1.00 62.61  ? 1312 SER A O   1 
ATOM   10283 C  CB  . SER A 1 1741 ? 138.412 143.724 95.200  1.00 77.75  ? 1312 SER A CB  1 
ATOM   10284 O  OG  . SER A 1 1741 ? 139.489 144.597 94.881  1.00 86.84  ? 1312 SER A OG  1 
ATOM   10285 N  N   . ASN A 1 1742 ? 135.492 142.984 94.726  1.00 52.18  ? 1313 ASN A N   1 
ATOM   10286 C  CA  . ASN A 1 1742 ? 134.476 141.970 94.893  1.00 46.76  ? 1313 ASN A CA  1 
ATOM   10287 C  C   . ASN A 1 1742 ? 135.034 140.677 95.441  1.00 50.40  ? 1313 ASN A C   1 
ATOM   10288 O  O   . ASN A 1 1742 ? 134.246 139.771 95.716  1.00 55.14  ? 1313 ASN A O   1 
ATOM   10289 C  CB  . ASN A 1 1742 ? 133.769 141.733 93.561  1.00 49.92  ? 1313 ASN A CB  1 
ATOM   10290 C  CG  . ASN A 1 1742 ? 134.733 141.578 92.411  1.00 53.46  ? 1313 ASN A CG  1 
ATOM   10291 O  OD1 . ASN A 1 1742 ? 135.920 141.328 92.607  1.00 58.89  ? 1313 ASN A OD1 1 
ATOM   10292 N  ND2 . ASN A 1 1742 ? 134.236 141.775 91.200  1.00 53.74  ? 1313 ASN A ND2 1 
ATOM   10293 N  N   . ILE A 1 1743 ? 136.353 140.556 95.613  1.00 53.53  ? 1314 ILE A N   1 
ATOM   10294 C  CA  . ILE A 1 1743 ? 136.928 139.321 96.143  1.00 48.98  ? 1314 ILE A CA  1 
ATOM   10295 C  C   . ILE A 1 1743 ? 136.431 139.103 97.559  1.00 41.22  ? 1314 ILE A C   1 
ATOM   10296 O  O   . ILE A 1 1743 ? 136.498 140.007 98.400  1.00 53.10  ? 1314 ILE A O   1 
ATOM   10297 C  CB  . ILE A 1 1743 ? 138.461 139.371 96.096  1.00 47.96  ? 1314 ILE A CB  1 
ATOM   10298 C  CG1 . ILE A 1 1743 ? 138.921 139.701 94.678  1.00 58.00  ? 1314 ILE A CG1 1 
ATOM   10299 C  CG2 . ILE A 1 1743 ? 139.046 138.064 96.566  1.00 44.78  ? 1314 ILE A CG2 1 
ATOM   10300 C  CD1 . ILE A 1 1743 ? 140.407 139.798 94.536  1.00 74.97  ? 1314 ILE A CD1 1 
ATOM   10301 N  N   . ILE A 1 1744 ? 135.914 137.918 97.829  1.00 31.05  ? 1315 ILE A N   1 
ATOM   10302 C  CA  . ILE A 1 1744 ? 135.420 137.594 99.153  1.00 31.96  ? 1315 ILE A CA  1 
ATOM   10303 C  C   . ILE A 1 1744 ? 136.506 136.828 99.888  1.00 39.77  ? 1315 ILE A C   1 
ATOM   10304 O  O   . ILE A 1 1744 ? 136.605 135.609 99.765  1.00 48.11  ? 1315 ILE A O   1 
ATOM   10305 C  CB  . ILE A 1 1744 ? 134.134 136.794 99.094  1.00 34.62  ? 1315 ILE A CB  1 
ATOM   10306 C  CG1 . ILE A 1 1744 ? 133.187 137.489 98.161  1.00 43.75  ? 1315 ILE A CG1 1 
ATOM   10307 C  CG2 . ILE A 1 1744 ? 133.571 136.776 100.443 1.00 53.88  ? 1315 ILE A CG2 1 
ATOM   10308 C  CD1 . ILE A 1 1744 ? 132.895 138.881 98.643  1.00 59.19  ? 1315 ILE A CD1 1 
ATOM   10309 N  N   . PHE A 1 1745 ? 137.298 137.531 100.689 1.00 35.74  ? 1316 PHE A N   1 
ATOM   10310 C  CA  . PHE A 1 1745 ? 138.520 136.927 101.185 1.00 33.61  ? 1316 PHE A CA  1 
ATOM   10311 C  C   . PHE A 1 1745 ? 138.233 135.719 102.036 1.00 34.96  ? 1316 PHE A C   1 
ATOM   10312 O  O   . PHE A 1 1745 ? 138.966 134.721 101.980 1.00 46.68  ? 1316 PHE A O   1 
ATOM   10313 C  CB  . PHE A 1 1745 ? 139.331 137.926 101.979 1.00 39.92  ? 1316 PHE A CB  1 
ATOM   10314 C  CG  . PHE A 1 1745 ? 140.124 138.821 101.138 1.00 36.19  ? 1316 PHE A CG  1 
ATOM   10315 C  CD1 . PHE A 1 1745 ? 139.547 139.918 100.548 1.00 43.10  ? 1316 PHE A CD1 1 
ATOM   10316 C  CD2 . PHE A 1 1745 ? 141.451 138.561 100.932 1.00 43.63  ? 1316 PHE A CD2 1 
ATOM   10317 C  CE1 . PHE A 1 1745 ? 140.282 140.747 99.762  1.00 54.91  ? 1316 PHE A CE1 1 
ATOM   10318 C  CE2 . PHE A 1 1745 ? 142.203 139.388 100.156 1.00 60.67  ? 1316 PHE A CE2 1 
ATOM   10319 C  CZ  . PHE A 1 1745 ? 141.616 140.487 99.560  1.00 64.29  ? 1316 PHE A CZ  1 
ATOM   10320 N  N   . GLN A 1 1746 ? 137.205 135.780 102.848 1.00 30.24  ? 1317 GLN A N   1 
ATOM   10321 C  CA  . GLN A 1 1746 ? 137.022 134.639 103.712 1.00 31.93  ? 1317 GLN A CA  1 
ATOM   10322 C  C   . GLN A 1 1746 ? 136.686 133.403 102.905 1.00 38.64  ? 1317 GLN A C   1 
ATOM   10323 O  O   . GLN A 1 1746 ? 137.171 132.311 103.217 1.00 47.39  ? 1317 GLN A O   1 
ATOM   10324 C  CB  . GLN A 1 1746 ? 135.976 134.961 104.744 1.00 54.48  ? 1317 GLN A CB  1 
ATOM   10325 C  CG  . GLN A 1 1746 ? 134.729 135.537 104.145 1.00 71.53  ? 1317 GLN A CG  1 
ATOM   10326 C  CD  . GLN A 1 1746 ? 133.746 135.961 105.228 1.00 96.93  ? 1317 GLN A CD  1 
ATOM   10327 O  OE1 . GLN A 1 1746 ? 133.995 135.748 106.420 1.00 90.18  ? 1317 GLN A OE1 1 
ATOM   10328 N  NE2 . GLN A 1 1746 ? 132.649 136.608 104.824 1.00 99.99  ? 1317 GLN A NE2 1 
ATOM   10329 N  N   . ASN A 1 1747 ? 135.902 133.539 101.833 1.00 42.38  ? 1318 ASN A N   1 
ATOM   10330 C  CA  . ASN A 1 1747 ? 135.707 132.350 101.003 1.00 36.93  ? 1318 ASN A CA  1 
ATOM   10331 C  C   . ASN A 1 1747 ? 136.890 132.023 100.125 1.00 29.83  ? 1318 ASN A C   1 
ATOM   10332 O  O   . ASN A 1 1747 ? 136.974 130.890 99.670  1.00 39.46  ? 1318 ASN A O   1 
ATOM   10333 C  CB  . ASN A 1 1747 ? 134.478 132.414 100.084 1.00 43.35  ? 1318 ASN A CB  1 
ATOM   10334 C  CG  . ASN A 1 1747 ? 133.164 132.036 100.785 1.00 52.61  ? 1318 ASN A CG  1 
ATOM   10335 O  OD1 . ASN A 1 1747 ? 132.118 132.650 100.554 1.00 63.96  ? 1318 ASN A OD1 1 
ATOM   10336 N  ND2 . ASN A 1 1747 ? 133.201 130.975 101.576 1.00 56.56  ? 1318 ASN A ND2 1 
ATOM   10337 N  N   . VAL A 1 1748 ? 137.778 132.958 99.821  1.00 26.79  ? 1319 VAL A N   1 
ATOM   10338 C  CA  . VAL A 1 1748 ? 138.991 132.528 99.140  1.00 27.39  ? 1319 VAL A CA  1 
ATOM   10339 C  C   . VAL A 1 1748 ? 139.784 131.614 100.042 1.00 30.99  ? 1319 VAL A C   1 
ATOM   10340 O  O   . VAL A 1 1748 ? 140.357 130.624 99.591  1.00 40.61  ? 1319 VAL A O   1 
ATOM   10341 C  CB  . VAL A 1 1748 ? 139.850 133.713 98.681  1.00 37.00  ? 1319 VAL A CB  1 
ATOM   10342 C  CG1 . VAL A 1 1748 ? 141.204 133.223 98.226  1.00 38.18  ? 1319 VAL A CG1 1 
ATOM   10343 C  CG2 . VAL A 1 1748 ? 139.185 134.453 97.558  1.00 46.01  ? 1319 VAL A CG2 1 
ATOM   10344 N  N   . ILE A 1 1749 ? 139.843 131.926 101.330 1.00 34.57  ? 1320 ILE A N   1 
ATOM   10345 C  CA  . ILE A 1 1749 ? 140.556 131.034 102.239 1.00 36.15  ? 1320 ILE A CA  1 
ATOM   10346 C  C   . ILE A 1 1749 ? 139.820 129.703 102.383 1.00 40.95  ? 1320 ILE A C   1 
ATOM   10347 O  O   . ILE A 1 1749 ? 140.443 128.633 102.346 1.00 49.89  ? 1320 ILE A O   1 
ATOM   10348 C  CB  . ILE A 1 1749 ? 140.767 131.709 103.602 1.00 50.97  ? 1320 ILE A CB  1 
ATOM   10349 C  CG1 . ILE A 1 1749 ? 141.495 133.054 103.438 1.00 51.33  ? 1320 ILE A CG1 1 
ATOM   10350 C  CG2 . ILE A 1 1749 ? 141.491 130.757 104.548 1.00 70.14  ? 1320 ILE A CG2 1 
ATOM   10351 C  CD1 . ILE A 1 1749 ? 142.874 132.967 102.819 1.00 58.40  ? 1320 ILE A CD1 1 
ATOM   10352 N  N   . ASN A 1 1750 ? 138.493 129.737 102.548 1.00 34.11  ? 1321 ASN A N   1 
ATOM   10353 C  CA  . ASN A 1 1750 ? 137.756 128.482 102.605 1.00 31.41  ? 1321 ASN A CA  1 
ATOM   10354 C  C   . ASN A 1 1750 ? 137.946 127.679 101.328 1.00 37.29  ? 1321 ASN A C   1 
ATOM   10355 O  O   . ASN A 1 1750 ? 138.079 126.453 101.376 1.00 46.50  ? 1321 ASN A O   1 
ATOM   10356 C  CB  . ASN A 1 1750 ? 136.280 128.722 102.833 1.00 33.86  ? 1321 ASN A CB  1 
ATOM   10357 C  CG  . ASN A 1 1750 ? 136.009 129.377 104.139 1.00 48.45  ? 1321 ASN A CG  1 
ATOM   10358 O  OD1 . ASN A 1 1750 ? 136.606 129.027 105.151 1.00 62.14  ? 1321 ASN A OD1 1 
ATOM   10359 N  ND2 . ASN A 1 1750 ? 135.059 130.302 104.152 1.00 52.67  ? 1321 ASN A ND2 1 
ATOM   10360 N  N   . TYR A 1 1751 ? 137.996 128.348 100.178 1.00 31.64  ? 1322 TYR A N   1 
ATOM   10361 C  CA  . TYR A 1 1751 ? 138.155 127.650 98.911  1.00 30.89  ? 1322 TYR A CA  1 
ATOM   10362 C  C   . TYR A 1 1751 ? 139.551 127.083 98.746  1.00 31.93  ? 1322 TYR A C   1 
ATOM   10363 O  O   . TYR A 1 1751 ? 139.698 125.959 98.271  1.00 44.87  ? 1322 TYR A O   1 
ATOM   10364 C  CB  . TYR A 1 1751 ? 137.810 128.581 97.750  1.00 35.50  ? 1322 TYR A CB  1 
ATOM   10365 C  CG  . TYR A 1 1751 ? 138.169 128.070 96.376  1.00 27.00  ? 1322 TYR A CG  1 
ATOM   10366 C  CD1 . TYR A 1 1751 ? 137.649 126.889 95.898  1.00 34.50  ? 1322 TYR A CD1 1 
ATOM   10367 C  CD2 . TYR A 1 1751 ? 138.912 128.838 95.518  1.00 32.20  ? 1322 TYR A CD2 1 
ATOM   10368 C  CE1 . TYR A 1 1751 ? 137.937 126.446 94.635  1.00 37.60  ? 1322 TYR A CE1 1 
ATOM   10369 C  CE2 . TYR A 1 1751 ? 139.201 128.418 94.254  1.00 38.00  ? 1322 TYR A CE2 1 
ATOM   10370 C  CZ  . TYR A 1 1751 ? 138.713 127.223 93.811  1.00 39.76  ? 1322 TYR A CZ  1 
ATOM   10371 O  OH  . TYR A 1 1751 ? 139.015 126.809 92.534  1.00 40.98  ? 1322 TYR A OH  1 
ATOM   10372 N  N   . ALA A 1 1752 ? 140.585 127.831 99.118  1.00 26.51  ? 1323 ALA A N   1 
ATOM   10373 C  CA  . ALA A 1 1752 ? 141.941 127.314 98.998  1.00 24.44  ? 1323 ALA A CA  1 
ATOM   10374 C  C   . ALA A 1 1752 ? 142.137 126.108 99.895  1.00 31.54  ? 1323 ALA A C   1 
ATOM   10375 O  O   . ALA A 1 1752 ? 142.608 125.052 99.448  1.00 43.91  ? 1323 ALA A O   1 
ATOM   10376 C  CB  . ALA A 1 1752 ? 142.951 128.396 99.346  1.00 34.77  ? 1323 ALA A CB  1 
ATOM   10377 N  N   . VAL A 1 1753 ? 141.747 126.227 101.163 1.00 30.13  ? 1324 VAL A N   1 
ATOM   10378 C  CA  . VAL A 1 1753 ? 141.894 125.093 102.064 1.00 28.83  ? 1324 VAL A CA  1 
ATOM   10379 C  C   . VAL A 1 1753 ? 141.090 123.912 101.554 1.00 33.86  ? 1324 VAL A C   1 
ATOM   10380 O  O   . VAL A 1 1753 ? 141.595 122.788 101.475 1.00 44.23  ? 1324 VAL A O   1 
ATOM   10381 C  CB  . VAL A 1 1753 ? 141.472 125.466 103.493 1.00 41.51  ? 1324 VAL A CB  1 
ATOM   10382 C  CG1 . VAL A 1 1753 ? 141.333 124.200 104.330 1.00 49.91  ? 1324 VAL A CG1 1 
ATOM   10383 C  CG2 . VAL A 1 1753 ? 142.487 126.414 104.130 1.00 57.92  ? 1324 VAL A CG2 1 
ATOM   10384 N  N   . ALA A 1 1754 ? 139.822 124.140 101.213 1.00 33.19  ? 1325 ALA A N   1 
ATOM   10385 C  CA  . ALA A 1 1754 ? 138.964 123.027 100.847 1.00 34.32  ? 1325 ALA A CA  1 
ATOM   10386 C  C   . ALA A 1 1754 ? 139.447 122.367 99.572  1.00 33.33  ? 1325 ALA A C   1 
ATOM   10387 O  O   . ALA A 1 1754 ? 139.355 121.146 99.431  1.00 46.45  ? 1325 ALA A O   1 
ATOM   10388 C  CB  . ALA A 1 1754 ? 137.519 123.496 100.692 1.00 40.41  ? 1325 ALA A CB  1 
ATOM   10389 N  N   . LEU A 1 1755 ? 139.946 123.146 98.626  1.00 30.23  ? 1326 LEU A N   1 
ATOM   10390 C  CA  . LEU A 1 1755 ? 140.478 122.557 97.410  1.00 36.35  ? 1326 LEU A CA  1 
ATOM   10391 C  C   . LEU A 1 1755 ? 141.698 121.712 97.670  1.00 42.09  ? 1326 LEU A C   1 
ATOM   10392 O  O   . LEU A 1 1755 ? 141.832 120.608 97.118  1.00 47.84  ? 1326 LEU A O   1 
ATOM   10393 C  CB  . LEU A 1 1755 ? 140.760 123.641 96.390  1.00 38.71  ? 1326 LEU A CB  1 
ATOM   10394 C  CG  . LEU A 1 1755 ? 141.447 123.017 95.207  1.00 43.84  ? 1326 LEU A CG  1 
ATOM   10395 C  CD1 . LEU A 1 1755 ? 140.935 123.587 93.947  1.00 52.20  ? 1326 LEU A CD1 1 
ATOM   10396 C  CD2 . LEU A 1 1755 ? 142.813 123.637 95.387  1.00 41.97  ? 1326 LEU A CD2 1 
ATOM   10397 N  N   . PHE A 1 1756 ? 142.594 122.194 98.515  1.00 46.61  ? 1327 PHE A N   1 
ATOM   10398 C  CA  . PHE A 1 1756 ? 143.744 121.368 98.842  1.00 45.84  ? 1327 PHE A CA  1 
ATOM   10399 C  C   . PHE A 1 1756 ? 143.317 120.086 99.539  1.00 41.64  ? 1327 PHE A C   1 
ATOM   10400 O  O   . PHE A 1 1756 ? 143.907 119.028 99.310  1.00 48.30  ? 1327 PHE A O   1 
ATOM   10401 C  CB  . PHE A 1 1756 ? 144.703 122.134 99.722  1.00 46.93  ? 1327 PHE A CB  1 
ATOM   10402 C  CG  . PHE A 1 1756 ? 145.975 121.453 99.882  1.00 42.60  ? 1327 PHE A CG  1 
ATOM   10403 C  CD1 . PHE A 1 1756 ? 146.124 120.461 100.828 1.00 44.21  ? 1327 PHE A CD1 1 
ATOM   10404 C  CD2 . PHE A 1 1756 ? 147.039 121.817 99.086  1.00 46.60  ? 1327 PHE A CD2 1 
ATOM   10405 C  CE1 . PHE A 1 1756 ? 147.319 119.824 100.977 1.00 56.10  ? 1327 PHE A CE1 1 
ATOM   10406 C  CE2 . PHE A 1 1756 ? 148.239 121.200 99.215  1.00 57.65  ? 1327 PHE A CE2 1 
ATOM   10407 C  CZ  . PHE A 1 1756 ? 148.393 120.193 100.165 1.00 66.54  ? 1327 PHE A CZ  1 
ATOM   10408 N  N   . ASP A 1 1757 ? 142.310 120.170 100.418 1.00 43.36  ? 1328 ASP A N   1 
ATOM   10409 C  CA  . ASP A 1 1757 ? 141.797 118.971 101.074 1.00 37.42  ? 1328 ASP A CA  1 
ATOM   10410 C  C   . ASP A 1 1757 ? 141.205 118.011 100.061 1.00 40.48  ? 1328 ASP A C   1 
ATOM   10411 O  O   . ASP A 1 1757 ? 141.419 116.797 100.144 1.00 49.32  ? 1328 ASP A O   1 
ATOM   10412 C  CB  . ASP A 1 1757 ? 140.741 119.318 102.122 1.00 40.13  ? 1328 ASP A CB  1 
ATOM   10413 C  CG  . ASP A 1 1757 ? 140.505 118.169 103.111 1.00 59.68  ? 1328 ASP A CG  1 
ATOM   10414 O  OD1 . ASP A 1 1757 ? 141.107 117.086 102.920 1.00 58.64  ? 1328 ASP A OD1 1 
ATOM   10415 O  OD2 . ASP A 1 1757 ? 139.750 118.341 104.098 1.00 58.05  ? 1328 ASP A OD2 1 
ATOM   10416 N  N   . ILE A 1 1758 ? 140.462 118.531 99.096  1.00 38.29  ? 1329 ILE A N   1 
ATOM   10417 C  CA  . ILE A 1 1758 ? 139.787 117.652 98.158  1.00 31.86  ? 1329 ILE A CA  1 
ATOM   10418 C  C   . ILE A 1 1758 ? 140.802 116.935 97.297  1.00 24.77  ? 1329 ILE A C   1 
ATOM   10419 O  O   . ILE A 1 1758 ? 140.640 115.760 96.971  1.00 34.76  ? 1329 ILE A O   1 
ATOM   10420 C  CB  . ILE A 1 1758 ? 138.788 118.454 97.314  1.00 32.26  ? 1329 ILE A CB  1 
ATOM   10421 C  CG1 . ILE A 1 1758 ? 137.569 118.796 98.144  1.00 36.90  ? 1329 ILE A CG1 1 
ATOM   10422 C  CG2 . ILE A 1 1758 ? 138.336 117.654 96.126  1.00 42.57  ? 1329 ILE A CG2 1 
ATOM   10423 C  CD1 . ILE A 1 1758 ? 136.570 119.651 97.410  1.00 47.90  ? 1329 ILE A CD1 1 
ATOM   10424 N  N   . LYS A 1 1759 ? 141.850 117.614 96.897  1.00 24.31  ? 1330 LYS A N   1 
ATOM   10425 C  CA  . LYS A 1 1759 ? 142.670 116.933 95.933  1.00 24.04  ? 1330 LYS A CA  1 
ATOM   10426 C  C   . LYS A 1 1759 ? 143.406 115.787 96.583  1.00 30.00  ? 1330 LYS A C   1 
ATOM   10427 O  O   . LYS A 1 1759 ? 143.701 114.787 95.928  1.00 41.70  ? 1330 LYS A O   1 
ATOM   10428 C  CB  . LYS A 1 1759 ? 143.619 117.906 95.261  1.00 36.42  ? 1330 LYS A CB  1 
ATOM   10429 C  CG  . LYS A 1 1759 ? 144.126 117.340 93.943  1.00 46.09  ? 1330 LYS A CG  1 
ATOM   10430 C  CD  . LYS A 1 1759 ? 145.228 118.181 93.315  1.00 53.52  ? 1330 LYS A CD  1 
ATOM   10431 C  CE  . LYS A 1 1759 ? 145.579 117.747 91.885  1.00 47.92  ? 1330 LYS A CE  1 
ATOM   10432 N  NZ  . LYS A 1 1759 ? 145.993 116.325 91.825  1.00 53.18  ? 1330 LYS A NZ  1 
ATOM   10433 N  N   . PHE A 1 1760 ? 143.644 115.867 97.867  1.00 31.22  ? 1331 PHE A N   1 
ATOM   10434 C  CA  . PHE A 1 1760 ? 144.463 114.869 98.526  1.00 28.71  ? 1331 PHE A CA  1 
ATOM   10435 C  C   . PHE A 1 1760 ? 143.708 114.148 99.625  1.00 30.66  ? 1331 PHE A C   1 
ATOM   10436 O  O   . PHE A 1 1760 ? 144.287 113.731 100.629 1.00 38.11  ? 1331 PHE A O   1 
ATOM   10437 C  CB  . PHE A 1 1760 ? 145.718 115.527 99.068  1.00 29.03  ? 1331 PHE A CB  1 
ATOM   10438 C  CG  . PHE A 1 1760 ? 146.454 116.265 98.036  1.00 32.35  ? 1331 PHE A CG  1 
ATOM   10439 C  CD1 . PHE A 1 1760 ? 147.118 115.581 97.050  1.00 46.28  ? 1331 PHE A CD1 1 
ATOM   10440 C  CD2 . PHE A 1 1760 ? 146.490 117.635 98.035  1.00 44.75  ? 1331 PHE A CD2 1 
ATOM   10441 C  CE1 . PHE A 1 1760 ? 147.810 116.247 96.069  1.00 54.24  ? 1331 PHE A CE1 1 
ATOM   10442 C  CE2 . PHE A 1 1760 ? 147.183 118.317 97.060  1.00 49.45  ? 1331 PHE A CE2 1 
ATOM   10443 C  CZ  . PHE A 1 1760 ? 147.847 117.619 96.074  1.00 52.28  ? 1331 PHE A CZ  1 
ATOM   10444 N  N   . ARG A 1 1761 ? 142.411 113.994 99.457  1.00 29.02  ? 1332 ARG A N   1 
ATOM   10445 C  CA  . ARG A 1 1761 ? 141.662 113.446 100.571 1.00 33.29  ? 1332 ARG A CA  1 
ATOM   10446 C  C   . ARG A 1 1761 ? 141.931 111.975 100.728 1.00 38.62  ? 1332 ARG A C   1 
ATOM   10447 O  O   . ARG A 1 1761 ? 141.782 111.444 101.831 1.00 51.29  ? 1332 ARG A O   1 
ATOM   10448 C  CB  . ARG A 1 1761 ? 140.162 113.684 100.402 1.00 39.67  ? 1332 ARG A CB  1 
ATOM   10449 C  CG  . ARG A 1 1761 ? 139.605 113.050 99.162  1.00 44.80  ? 1332 ARG A CG  1 
ATOM   10450 C  CD  . ARG A 1 1761 ? 138.183 113.488 98.911  1.00 41.49  ? 1332 ARG A CD  1 
ATOM   10451 N  NE  . ARG A 1 1761 ? 137.621 112.721 97.808  1.00 42.66  ? 1332 ARG A NE  1 
ATOM   10452 C  CZ  . ARG A 1 1761 ? 137.848 112.979 96.528  1.00 39.50  ? 1332 ARG A CZ  1 
ATOM   10453 N  NH1 . ARG A 1 1761 ? 138.616 113.995 96.170  1.00 37.80  ? 1332 ARG A NH1 1 
ATOM   10454 N  NH2 . ARG A 1 1761 ? 137.293 112.218 95.601  1.00 50.68  ? 1332 ARG A NH2 1 
ATOM   10455 N  N   . ASN A 1 1762 ? 142.328 111.296 99.663  1.00 34.48  ? 1333 ASN A N   1 
ATOM   10456 C  CA  . ASN A 1 1762 ? 142.605 109.881 99.790  1.00 29.13  ? 1333 ASN A CA  1 
ATOM   10457 C  C   . ASN A 1 1762 ? 144.054 109.543 99.610  1.00 31.84  ? 1333 ASN A C   1 
ATOM   10458 O  O   . ASN A 1 1762 ? 144.459 108.439 99.975  1.00 44.82  ? 1333 ASN A O   1 
ATOM   10459 C  CB  . ASN A 1 1762 ? 141.805 109.083 98.778  1.00 33.50  ? 1333 ASN A CB  1 
ATOM   10460 C  CG  . ASN A 1 1762 ? 140.340 109.154 99.058  1.00 49.86  ? 1333 ASN A CG  1 
ATOM   10461 O  OD1 . ASN A 1 1762 ? 139.934 109.364 100.206 1.00 46.87  ? 1333 ASN A OD1 1 
ATOM   10462 N  ND2 . ASN A 1 1762 ? 139.519 108.987 98.017  1.00 53.89  ? 1333 ASN A ND2 1 
ATOM   10463 N  N   . THR A 1 1763 ? 144.841 110.441 99.056  1.00 30.85  ? 1334 THR A N   1 
ATOM   10464 C  CA  . THR A 1 1763 ? 146.212 110.062 98.823  1.00 39.06  ? 1334 THR A CA  1 
ATOM   10465 C  C   . THR A 1 1763 ? 146.967 110.064 100.138 1.00 47.00  ? 1334 THR A C   1 
ATOM   10466 O  O   . THR A 1 1763 ? 146.631 110.791 101.075 1.00 46.75  ? 1334 THR A O   1 
ATOM   10467 C  CB  . THR A 1 1763 ? 146.891 110.988 97.826  1.00 48.83  ? 1334 THR A CB  1 
ATOM   10468 O  OG1 . THR A 1 1763 ? 148.171 110.442 97.479  1.00 59.13  ? 1334 THR A OG1 1 
ATOM   10469 C  CG2 . THR A 1 1763 ? 147.104 112.350 98.442  1.00 54.45  ? 1334 THR A CG2 1 
ATOM   10470 N  N   . GLU A 1 1764 ? 147.971 109.196 100.207 1.00 55.21  ? 1335 GLU A N   1 
ATOM   10471 C  CA  . GLU A 1 1764 ? 148.829 109.122 101.376 1.00 54.42  ? 1335 GLU A CA  1 
ATOM   10472 C  C   . GLU A 1 1764 ? 149.610 110.418 101.520 1.00 60.21  ? 1335 GLU A C   1 
ATOM   10473 O  O   . GLU A 1 1764 ? 150.033 111.015 100.527 1.00 67.34  ? 1335 GLU A O   1 
ATOM   10474 C  CB  . GLU A 1 1764 ? 149.784 107.942 101.253 1.00 61.09  ? 1335 GLU A CB  1 
ATOM   10475 C  CG  . GLU A 1 1764 ? 150.533 107.652 102.534 1.00 73.58  ? 1335 GLU A CG  1 
ATOM   10476 C  CD  . GLU A 1 1764 ? 151.291 106.337 102.493 1.00 86.70  ? 1335 GLU A CD  1 
ATOM   10477 O  OE1 . GLU A 1 1764 ? 151.213 105.624 101.467 1.00 82.84  ? 1335 GLU A OE1 1 
ATOM   10478 O  OE2 . GLU A 1 1764 ? 151.994 106.032 103.481 1.00 86.87  ? 1335 GLU A OE2 1 
ATOM   10479 N  N   . ALA A 1 1765 ? 149.788 110.864 102.762 1.00 56.53  ? 1336 ALA A N   1 
ATOM   10480 C  CA  . ALA A 1 1765 ? 150.409 112.164 102.978 1.00 59.44  ? 1336 ALA A CA  1 
ATOM   10481 C  C   . ALA A 1 1765 ? 151.832 112.189 102.447 1.00 58.00  ? 1336 ALA A C   1 
ATOM   10482 O  O   . ALA A 1 1765 ? 152.236 113.147 101.779 1.00 67.37  ? 1336 ALA A O   1 
ATOM   10483 C  CB  . ALA A 1 1765 ? 150.386 112.526 104.461 1.00 60.05  ? 1336 ALA A CB  1 
ATOM   10484 N  N   . THR A 1 1766 ? 152.602 111.147 102.712 1.00 53.86  ? 1337 THR A N   1 
ATOM   10485 C  CA  . THR A 1 1766 ? 153.977 111.203 102.260 1.00 60.26  ? 1337 THR A CA  1 
ATOM   10486 C  C   . THR A 1 1766 ? 154.096 111.144 100.747 1.00 71.29  ? 1337 THR A C   1 
ATOM   10487 O  O   . THR A 1 1766 ? 155.175 111.431 100.218 1.00 82.05  ? 1337 THR A O   1 
ATOM   10488 C  CB  . THR A 1 1766 ? 154.776 110.078 102.902 1.00 69.69  ? 1337 THR A CB  1 
ATOM   10489 O  OG1 . THR A 1 1766 ? 154.231 108.813 102.498 1.00 75.47  ? 1337 THR A OG1 1 
ATOM   10490 C  CG2 . THR A 1 1766 ? 154.713 110.208 104.417 1.00 71.31  ? 1337 THR A CG2 1 
ATOM   10491 N  N   . ASP A 1 1767 ? 153.025 110.804 100.036 1.00 71.79  ? 1338 ASP A N   1 
ATOM   10492 C  CA  . ASP A 1 1767 ? 153.065 110.661 98.583  1.00 84.50  ? 1338 ASP A CA  1 
ATOM   10493 C  C   . ASP A 1 1767 ? 152.564 111.911 97.845  1.00 82.10  ? 1338 ASP A C   1 
ATOM   10494 O  O   . ASP A 1 1767 ? 152.607 111.942 96.608  1.00 82.33  ? 1338 ASP A O   1 
ATOM   10495 C  CB  . ASP A 1 1767 ? 152.242 109.418 98.167  1.00 96.02  ? 1338 ASP A CB  1 
ATOM   10496 C  CG  . ASP A 1 1767 ? 152.650 108.839 96.796  1.00 102.88 ? 1338 ASP A CG  1 
ATOM   10497 O  OD1 . ASP A 1 1767 ? 153.659 109.297 96.214  1.00 99.90  ? 1338 ASP A OD1 1 
ATOM   10498 O  OD2 . ASP A 1 1767 ? 151.954 107.914 96.308  1.00 97.98  ? 1338 ASP A OD2 1 
ATOM   10499 N  N   . ILE A 1 1768 ? 152.091 112.936 98.570  1.00 73.71  ? 1339 ILE A N   1 
ATOM   10500 C  CA  . ILE A 1 1768 ? 151.663 114.193 97.950  1.00 56.34  ? 1339 ILE A CA  1 
ATOM   10501 C  C   . ILE A 1 1768 ? 152.851 114.841 97.262  1.00 62.60  ? 1339 ILE A C   1 
ATOM   10502 O  O   . ILE A 1 1768 ? 153.794 115.293 97.925  1.00 67.77  ? 1339 ILE A O   1 
ATOM   10503 C  CB  . ILE A 1 1768 ? 151.090 115.143 98.995  1.00 49.28  ? 1339 ILE A CB  1 
ATOM   10504 C  CG1 . ILE A 1 1768 ? 149.893 114.531 99.691  1.00 52.17  ? 1339 ILE A CG1 1 
ATOM   10505 C  CG2 . ILE A 1 1768 ? 150.695 116.447 98.357  1.00 57.36  ? 1339 ILE A CG2 1 
ATOM   10506 C  CD1 . ILE A 1 1768 ? 149.298 115.474 100.690 1.00 51.69  ? 1339 ILE A CD1 1 
ATOM   10507 N  N   . GLN A 1 1769 ? 152.802 114.929 95.937  1.00 56.52  ? 1340 GLN A N   1 
ATOM   10508 C  CA  . GLN A 1 1769 ? 153.943 115.432 95.190  1.00 52.34  ? 1340 GLN A CA  1 
ATOM   10509 C  C   . GLN A 1 1769 ? 153.929 116.950 95.053  1.00 57.28  ? 1340 GLN A C   1 
ATOM   10510 O  O   . GLN A 1 1769 ? 154.810 117.506 94.390  1.00 58.86  ? 1340 GLN A O   1 
ATOM   10511 C  CB  . GLN A 1 1769 ? 153.988 114.773 93.818  1.00 52.20  ? 1340 GLN A CB  1 
ATOM   10512 C  CG  . GLN A 1 1769 ? 152.737 115.027 93.015  1.00 72.13  ? 1340 GLN A CG  1 
ATOM   10513 C  CD  . GLN A 1 1769 ? 152.743 114.310 91.676  1.00 89.42  ? 1340 GLN A CD  1 
ATOM   10514 O  OE1 . GLN A 1 1769 ? 153.630 113.497 91.401  1.00 86.90  ? 1340 GLN A OE1 1 
ATOM   10515 N  NE2 . GLN A 1 1769 ? 151.756 114.616 90.827  1.00 86.52  ? 1340 GLN A NE2 1 
ATOM   10516 N  N   . TYR A 1 1770 ? 152.963 117.624 95.678  1.00 59.62  ? 1341 TYR A N   1 
ATOM   10517 C  CA  . TYR A 1 1770 ? 152.834 119.076 95.668  1.00 55.14  ? 1341 TYR A CA  1 
ATOM   10518 C  C   . TYR A 1 1770 ? 152.952 119.637 97.080  1.00 59.19  ? 1341 TYR A C   1 
ATOM   10519 O  O   . TYR A 1 1770 ? 152.380 119.090 98.029  1.00 62.85  ? 1341 TYR A O   1 
ATOM   10520 C  CB  . TYR A 1 1770 ? 151.488 119.499 95.080  1.00 54.92  ? 1341 TYR A CB  1 
ATOM   10521 C  CG  . TYR A 1 1770 ? 151.220 119.007 93.680  1.00 53.31  ? 1341 TYR A CG  1 
ATOM   10522 C  CD1 . TYR A 1 1770 ? 151.967 119.479 92.612  1.00 62.14  ? 1341 TYR A CD1 1 
ATOM   10523 C  CD2 . TYR A 1 1770 ? 150.214 118.083 93.420  1.00 58.88  ? 1341 TYR A CD2 1 
ATOM   10524 C  CE1 . TYR A 1 1770 ? 151.723 119.047 91.313  1.00 66.05  ? 1341 TYR A CE1 1 
ATOM   10525 C  CE2 . TYR A 1 1770 ? 149.963 117.639 92.121  1.00 66.96  ? 1341 TYR A CE2 1 
ATOM   10526 C  CZ  . TYR A 1 1770 ? 150.726 118.128 91.072  1.00 65.72  ? 1341 TYR A CZ  1 
ATOM   10527 O  OH  . TYR A 1 1770 ? 150.505 117.709 89.780  1.00 65.73  ? 1341 TYR A OH  1 
ATOM   10528 N  N   . ASN A 1 1771 ? 153.674 120.750 97.213  1.00 59.73  ? 1342 ASN A N   1 
ATOM   10529 C  CA  . ASN A 1 1771 ? 153.789 121.447 98.488  1.00 62.09  ? 1342 ASN A CA  1 
ATOM   10530 C  C   . ASN A 1 1771 ? 153.232 122.860 98.472  1.00 54.50  ? 1342 ASN A C   1 
ATOM   10531 O  O   . ASN A 1 1771 ? 152.979 123.416 99.547  1.00 56.08  ? 1342 ASN A O   1 
ATOM   10532 C  CB  . ASN A 1 1771 ? 155.258 121.505 98.932  1.00 63.86  ? 1342 ASN A CB  1 
ATOM   10533 C  CG  . ASN A 1 1771 ? 156.139 122.225 97.928  1.00 64.75  ? 1342 ASN A CG  1 
ATOM   10534 O  OD1 . ASN A 1 1771 ? 155.723 122.492 96.800  1.00 62.85  ? 1342 ASN A OD1 1 
ATOM   10535 N  ND2 . ASN A 1 1771 ? 157.373 122.520 98.326  1.00 67.95  ? 1342 ASN A ND2 1 
ATOM   10536 N  N   . ARG A 1 1772 ? 153.042 123.456 97.302  1.00 52.89  ? 1343 ARG A N   1 
ATOM   10537 C  CA  . ARG A 1 1772 ? 152.581 124.828 97.222  1.00 54.33  ? 1343 ARG A CA  1 
ATOM   10538 C  C   . ARG A 1 1772 ? 151.505 124.962 96.150  1.00 55.78  ? 1343 ARG A C   1 
ATOM   10539 O  O   . ARG A 1 1772 ? 151.511 124.249 95.138  1.00 55.48  ? 1343 ARG A O   1 
ATOM   10540 C  CB  . ARG A 1 1772 ? 153.754 125.755 96.941  1.00 58.03  ? 1343 ARG A CB  1 
ATOM   10541 C  CG  . ARG A 1 1772 ? 154.820 125.651 98.005  1.00 60.15  ? 1343 ARG A CG  1 
ATOM   10542 C  CD  . ARG A 1 1772 ? 156.065 126.341 97.569  1.00 53.14  ? 1343 ARG A CD  1 
ATOM   10543 N  NE  . ARG A 1 1772 ? 156.576 125.758 96.356  1.00 52.86  ? 1343 ARG A NE  1 
ATOM   10544 C  CZ  . ARG A 1 1772 ? 156.564 126.387 95.194  1.00 59.83  ? 1343 ARG A CZ  1 
ATOM   10545 N  NH1 . ARG A 1 1772 ? 156.045 127.606 95.111  1.00 56.82  ? 1343 ARG A NH1 1 
ATOM   10546 N  NH2 . ARG A 1 1772 ? 157.062 125.794 94.117  1.00 70.07  ? 1343 ARG A NH2 1 
ATOM   10547 N  N   . ALA A 1 1773 ? 150.572 125.881 96.390  1.00 45.34  ? 1344 ALA A N   1 
ATOM   10548 C  CA  . ALA A 1 1773 ? 149.470 126.139 95.478  1.00 50.30  ? 1344 ALA A CA  1 
ATOM   10549 C  C   . ALA A 1 1773 ? 149.315 127.636 95.293  1.00 44.28  ? 1344 ALA A C   1 
ATOM   10550 O  O   . ALA A 1 1773 ? 149.418 128.407 96.248  1.00 51.24  ? 1344 ALA A O   1 
ATOM   10551 C  CB  . ALA A 1 1773 ? 148.148 125.543 95.988  1.00 51.68  ? 1344 ALA A CB  1 
ATOM   10552 N  N   . HIS A 1 1774 ? 149.065 128.047 94.071  1.00 32.98  ? 1345 HIS A N   1 
ATOM   10553 C  CA  . HIS A 1 1774 ? 148.725 129.423 93.804  1.00 30.38  ? 1345 HIS A CA  1 
ATOM   10554 C  C   . HIS A 1 1774 ? 147.300 129.451 93.292  1.00 37.17  ? 1345 HIS A C   1 
ATOM   10555 O  O   . HIS A 1 1774 ? 146.982 128.749 92.329  1.00 48.15  ? 1345 HIS A O   1 
ATOM   10556 C  CB  . HIS A 1 1774 ? 149.628 129.982 92.727  1.00 47.52  ? 1345 HIS A CB  1 
ATOM   10557 C  CG  . HIS A 1 1774 ? 150.993 130.315 93.198  1.00 48.09  ? 1345 HIS A CG  1 
ATOM   10558 N  ND1 . HIS A 1 1774 ? 151.883 131.009 92.414  1.00 44.93  ? 1345 HIS A ND1 1 
ATOM   10559 C  CD2 . HIS A 1 1774 ? 151.642 130.014 94.344  1.00 44.70  ? 1345 HIS A CD2 1 
ATOM   10560 C  CE1 . HIS A 1 1774 ? 153.016 131.160 93.072  1.00 52.71  ? 1345 HIS A CE1 1 
ATOM   10561 N  NE2 . HIS A 1 1774 ? 152.899 130.558 94.244  1.00 51.94  ? 1345 HIS A NE2 1 
ATOM   10562 N  N   . LEU A 1 1775 ? 146.448 130.247 93.897  1.00 28.39  ? 1346 LEU A N   1 
ATOM   10563 C  CA  . LEU A 1 1775 ? 145.129 130.497 93.325  1.00 29.49  ? 1346 LEU A CA  1 
ATOM   10564 C  C   . LEU A 1 1775 ? 145.237 131.839 92.599  1.00 39.81  ? 1346 LEU A C   1 
ATOM   10565 O  O   . LEU A 1 1775 ? 145.118 132.897 93.222  1.00 48.72  ? 1346 LEU A O   1 
ATOM   10566 C  CB  . LEU A 1 1775 ? 144.045 130.495 94.403  1.00 30.78  ? 1346 LEU A CB  1 
ATOM   10567 C  CG  . LEU A 1 1775 ? 143.377 129.193 94.856  1.00 29.67  ? 1346 LEU A CG  1 
ATOM   10568 C  CD1 . LEU A 1 1775 ? 144.378 128.273 95.536  1.00 38.25  ? 1346 LEU A CD1 1 
ATOM   10569 C  CD2 . LEU A 1 1775 ? 142.237 129.490 95.803  1.00 26.77  ? 1346 LEU A CD2 1 
ATOM   10570 N  N   . HIS A 1 1776 ? 145.514 131.807 91.299  1.00 29.80  ? 1347 HIS A N   1 
ATOM   10571 C  CA  . HIS A 1 1776 ? 145.701 133.037 90.558  1.00 29.57  ? 1347 HIS A CA  1 
ATOM   10572 C  C   . HIS A 1 1776 ? 144.370 133.638 90.135  1.00 42.85  ? 1347 HIS A C   1 
ATOM   10573 O  O   . HIS A 1 1776 ? 143.386 132.920 89.920  1.00 48.61  ? 1347 HIS A O   1 
ATOM   10574 C  CB  . HIS A 1 1776 ? 146.521 132.774 89.328  1.00 31.13  ? 1347 HIS A CB  1 
ATOM   10575 C  CG  . HIS A 1 1776 ? 147.979 132.714 89.591  1.00 40.17  ? 1347 HIS A CG  1 
ATOM   10576 N  ND1 . HIS A 1 1776 ? 148.758 133.840 89.735  1.00 42.53  ? 1347 HIS A ND1 1 
ATOM   10577 C  CD2 . HIS A 1 1776 ? 148.809 131.658 89.751  1.00 51.81  ? 1347 HIS A CD2 1 
ATOM   10578 C  CE1 . HIS A 1 1776 ? 150.010 133.478 89.955  1.00 49.99  ? 1347 HIS A CE1 1 
ATOM   10579 N  NE2 . HIS A 1 1776 ? 150.067 132.159 89.975  1.00 50.15  ? 1347 HIS A NE2 1 
ATOM   10580 N  N   . LEU A 1 1777 ? 144.357 134.973 89.987  1.00 46.15  ? 1348 LEU A N   1 
ATOM   10581 C  CA  . LEU A 1 1777 ? 143.170 135.723 89.567  1.00 38.56  ? 1348 LEU A CA  1 
ATOM   10582 C  C   . LEU A 1 1777 ? 142.957 135.626 88.071  1.00 45.68  ? 1348 LEU A C   1 
ATOM   10583 O  O   . LEU A 1 1777 ? 143.831 135.992 87.279  1.00 54.10  ? 1348 LEU A O   1 
ATOM   10584 C  CB  . LEU A 1 1777 ? 143.264 137.190 89.963  1.00 41.94  ? 1348 LEU A CB  1 
ATOM   10585 C  CG  . LEU A 1 1777 ? 142.726 137.459 91.363  1.00 60.17  ? 1348 LEU A CG  1 
ATOM   10586 C  CD1 . LEU A 1 1777 ? 143.005 138.884 91.789  1.00 72.00  ? 1348 LEU A CD1 1 
ATOM   10587 C  CD2 . LEU A 1 1777 ? 141.225 137.193 91.348  1.00 61.91  ? 1348 LEU A CD2 1 
ATOM   10588 N  N   . THR A 1 1778 ? 141.783 135.153 87.690  1.00 49.39  ? 1349 THR A N   1 
ATOM   10589 C  CA  . THR A 1 1778 ? 141.360 135.198 86.302  1.00 59.51  ? 1349 THR A CA  1 
ATOM   10590 C  C   . THR A 1 1778 ? 140.910 136.625 86.002  1.00 79.18  ? 1349 THR A C   1 
ATOM   10591 O  O   . THR A 1 1778 ? 140.022 137.160 86.682  1.00 76.35  ? 1349 THR A O   1 
ATOM   10592 C  CB  . THR A 1 1778 ? 140.237 134.190 86.059  1.00 61.79  ? 1349 THR A CB  1 
ATOM   10593 O  OG1 . THR A 1 1778 ? 139.165 134.428 86.987  1.00 52.02  ? 1349 THR A OG1 1 
ATOM   10594 C  CG2 . THR A 1 1778 ? 140.756 132.750 86.261  1.00 59.57  ? 1349 THR A CG2 1 
ATOM   10595 N  N   . LYS A 1 1779 ? 141.526 137.244 84.991  1.00 79.47  ? 1350 LYS A N   1 
ATOM   10596 C  CA  . LYS A 1 1779 ? 141.312 138.669 84.756  1.00 79.25  ? 1350 LYS A CA  1 
ATOM   10597 C  C   . LYS A 1 1779 ? 139.849 138.968 84.485  1.00 68.18  ? 1350 LYS A C   1 
ATOM   10598 O  O   . LYS A 1 1779 ? 139.262 139.871 85.094  1.00 64.93  ? 1350 LYS A O   1 
ATOM   10599 C  CB  . LYS A 1 1779 ? 142.191 139.139 83.593  1.00 88.65  ? 1350 LYS A CB  1 
ATOM   10600 C  CG  . LYS A 1 1779 ? 143.685 139.093 83.909  1.00 95.25  ? 1350 LYS A CG  1 
ATOM   10601 C  CD  . LYS A 1 1779 ? 144.322 137.770 83.500  1.00 102.49 ? 1350 LYS A CD  1 
ATOM   10602 C  CE  . LYS A 1 1779 ? 145.820 137.767 83.797  1.00 109.95 ? 1350 LYS A CE  1 
ATOM   10603 N  NZ  . LYS A 1 1779 ? 146.511 136.521 83.339  1.00 109.46 ? 1350 LYS A NZ  1 
ATOM   10604 N  N   . CYS A 1 1780 ? 139.234 138.179 83.619  1.00 67.14  ? 1351 CYS A N   1 
ATOM   10605 C  CA  . CYS A 1 1780 ? 137.925 138.546 83.114  1.00 81.97  ? 1351 CYS A CA  1 
ATOM   10606 C  C   . CYS A 1 1780 ? 136.898 138.643 84.222  1.00 61.88  ? 1351 CYS A C   1 
ATOM   10607 O  O   . CYS A 1 1780 ? 135.953 139.430 84.125  1.00 70.40  ? 1351 CYS A O   1 
ATOM   10608 C  CB  . CYS A 1 1780 ? 137.470 137.530 82.069  1.00 95.64  ? 1351 CYS A CB  1 
ATOM   10609 S  SG  . CYS A 1 1780 ? 137.214 135.880 82.764  1.00 101.44 ? 1351 CYS A SG  1 
ATOM   10610 N  N   . CYS A 1 1781 ? 137.042 137.868 85.270  1.00 43.55  ? 1352 CYS A N   1 
ATOM   10611 C  CA  . CYS A 1 1781 ? 135.863 137.690 86.076  1.00 49.38  ? 1352 CYS A CA  1 
ATOM   10612 C  C   . CYS A 1 1781 ? 135.960 138.365 87.426  1.00 62.30  ? 1352 CYS A C   1 
ATOM   10613 O  O   . CYS A 1 1781 ? 135.229 138.001 88.349  1.00 64.33  ? 1352 CYS A O   1 
ATOM   10614 C  CB  . CYS A 1 1781 ? 135.566 136.214 86.205  1.00 56.23  ? 1352 CYS A CB  1 
ATOM   10615 S  SG  . CYS A 1 1781 ? 134.689 135.724 84.745  1.00 50.08  ? 1352 CYS A SG  1 
ATOM   10616 N  N   . THR A 1 1782 ? 136.820 139.363 87.561  1.00 65.15  ? 1353 THR A N   1 
ATOM   10617 C  CA  . THR A 1 1782 ? 136.809 140.155 88.783  1.00 63.68  ? 1353 THR A CA  1 
ATOM   10618 C  C   . THR A 1 1782 ? 137.125 141.601 88.458  1.00 72.05  ? 1353 THR A C   1 
ATOM   10619 O  O   . THR A 1 1782 ? 137.856 141.902 87.506  1.00 72.62  ? 1353 THR A O   1 
ATOM   10620 C  CB  . THR A 1 1782 ? 137.800 139.660 89.821  1.00 59.74  ? 1353 THR A CB  1 
ATOM   10621 O  OG1 . THR A 1 1782 ? 137.736 140.524 90.963  1.00 57.19  ? 1353 THR A OG1 1 
ATOM   10622 C  CG2 . THR A 1 1782 ? 139.205 139.671 89.236  1.00 71.03  ? 1353 THR A CG2 1 
ATOM   10623 N  N   . ARG A 1 1783 ? 136.557 142.496 89.259  1.00 67.40  ? 1354 ARG A N   1 
ATOM   10624 C  CA  . ARG A 1 1783 ? 136.777 143.906 89.007  1.00 63.87  ? 1354 ARG A CA  1 
ATOM   10625 C  C   . ARG A 1 1783 ? 136.451 144.711 90.250  1.00 62.81  ? 1354 ARG A C   1 
ATOM   10626 O  O   . ARG A 1 1783 ? 135.561 144.358 91.025  1.00 58.77  ? 1354 ARG A O   1 
ATOM   10627 C  CB  . ARG A 1 1783 ? 135.934 144.413 87.850  1.00 59.10  ? 1354 ARG A CB  1 
ATOM   10628 C  CG  . ARG A 1 1783 ? 134.488 144.311 88.117  1.00 59.87  ? 1354 ARG A CG  1 
ATOM   10629 C  CD  . ARG A 1 1783 ? 133.773 144.564 86.829  1.00 71.92  ? 1354 ARG A CD  1 
ATOM   10630 N  NE  . ARG A 1 1783 ? 133.978 143.503 85.859  1.00 66.63  ? 1354 ARG A NE  1 
ATOM   10631 C  CZ  . ARG A 1 1783 ? 133.139 142.490 85.703  1.00 67.46  ? 1354 ARG A CZ  1 
ATOM   10632 N  NH1 . ARG A 1 1783 ? 132.058 142.422 86.468  1.00 61.90  ? 1354 ARG A NH1 1 
ATOM   10633 N  NH2 . ARG A 1 1783 ? 133.370 141.554 84.788  1.00 67.51  ? 1354 ARG A NH2 1 
ATOM   10634 N  N   . GLU A 1 1784 ? 137.173 145.818 90.391  1.00 68.11  ? 1355 GLU A N   1 
ATOM   10635 C  CA  . GLU A 1 1784 ? 137.067 146.673 91.553  1.00 62.97  ? 1355 GLU A CA  1 
ATOM   10636 C  C   . GLU A 1 1784 ? 135.694 147.306 91.606  1.00 62.36  ? 1355 GLU A C   1 
ATOM   10637 O  O   . GLU A 1 1784 ? 135.188 147.816 90.609  1.00 68.15  ? 1355 GLU A O   1 
ATOM   10638 C  CB  . GLU A 1 1784 ? 138.148 147.735 91.500  1.00 77.38  ? 1355 GLU A CB  1 
ATOM   10639 C  CG  . GLU A 1 1784 ? 138.176 148.636 92.715  1.00 91.30  ? 1355 GLU A CG  1 
ATOM   10640 C  CD  . GLU A 1 1784 ? 137.303 149.881 92.539  1.00 97.38  ? 1355 GLU A CD  1 
ATOM   10641 O  OE1 . GLU A 1 1784 ? 136.820 150.115 91.404  1.00 90.91  ? 1355 GLU A OE1 1 
ATOM   10642 O  OE2 . GLU A 1 1784 ? 137.101 150.623 93.531  1.00 94.39  ? 1355 GLU A OE2 1 
ATOM   10643 N  N   . VAL A 1 1785 ? 135.078 147.263 92.780  1.00 68.86  ? 1356 VAL A N   1 
ATOM   10644 C  CA  . VAL A 1 1785 ? 133.741 147.792 92.985  1.00 80.20  ? 1356 VAL A CA  1 
ATOM   10645 C  C   . VAL A 1 1785 ? 133.860 149.242 93.487  1.00 81.54  ? 1356 VAL A C   1 
ATOM   10646 O  O   . VAL A 1 1785 ? 134.464 149.457 94.533  1.00 86.04  ? 1356 VAL A O   1 
ATOM   10647 C  CB  . VAL A 1 1785 ? 132.907 146.924 93.937  1.00 84.90  ? 1356 VAL A CB  1 
ATOM   10648 C  CG1 . VAL A 1 1785 ? 133.506 146.887 95.387  1.00 81.62  ? 1356 VAL A CG1 1 
ATOM   10649 C  CG2 . VAL A 1 1785 ? 131.457 147.388 93.944  1.00 88.57  ? 1356 VAL A CG2 1 
ATOM   10650 N  N   . PRO A 1 1786 ? 133.395 150.215 92.734  1.00 78.42  ? 1357 PRO A N   1 
ATOM   10651 C  CA  . PRO A 1 1786 ? 133.543 151.591 93.205  1.00 72.89  ? 1357 PRO A CA  1 
ATOM   10652 C  C   . PRO A 1 1786 ? 132.759 151.788 94.478  1.00 69.97  ? 1357 PRO A C   1 
ATOM   10653 O  O   . PRO A 1 1786 ? 131.660 151.256 94.638  1.00 76.30  ? 1357 PRO A O   1 
ATOM   10654 C  CB  . PRO A 1 1786 ? 132.954 152.439 92.075  1.00 81.69  ? 1357 PRO A CB  1 
ATOM   10655 C  CG  . PRO A 1 1786 ? 132.931 151.530 90.886  1.00 91.96  ? 1357 PRO A CG  1 
ATOM   10656 C  CD  . PRO A 1 1786 ? 132.731 150.147 91.426  1.00 85.65  ? 1357 PRO A CD  1 
ATOM   10657 N  N   . ALA A 1 1787 ? 133.309 152.591 95.386  1.00 69.84  ? 1358 ALA A N   1 
ATOM   10658 C  CA  . ALA A 1 1787 ? 132.546 152.963 96.571  1.00 69.97  ? 1358 ALA A CA  1 
ATOM   10659 C  C   . ALA A 1 1787 ? 131.467 153.958 96.174  1.00 67.01  ? 1358 ALA A C   1 
ATOM   10660 O  O   . ALA A 1 1787 ? 131.741 154.950 95.494  1.00 71.73  ? 1358 ALA A O   1 
ATOM   10661 C  CB  . ALA A 1 1787 ? 133.462 153.554 97.635  1.00 74.58  ? 1358 ALA A CB  1 
ATOM   10662 N  N   . GLN A 1 1788 ? 130.236 153.684 96.574  1.00 63.07  ? 1359 GLN A N   1 
ATOM   10663 C  CA  . GLN A 1 1788 ? 129.130 154.567 96.262  1.00 59.40  ? 1359 GLN A CA  1 
ATOM   10664 C  C   . GLN A 1 1788 ? 128.342 154.816 97.533  1.00 59.55  ? 1359 GLN A C   1 
ATOM   10665 O  O   . GLN A 1 1788 ? 128.679 154.313 98.606  1.00 68.26  ? 1359 GLN A O   1 
ATOM   10666 C  CB  . GLN A 1 1788 ? 128.242 153.963 95.180  1.00 64.60  ? 1359 GLN A CB  1 
ATOM   10667 C  CG  . GLN A 1 1788 ? 128.971 153.675 93.883  1.00 78.14  ? 1359 GLN A CG  1 
ATOM   10668 C  CD  . GLN A 1 1788 ? 128.025 153.185 92.794  1.00 91.55  ? 1359 GLN A CD  1 
ATOM   10669 O  OE1 . GLN A 1 1788 ? 126.858 153.587 92.745  1.00 87.97  ? 1359 GLN A OE1 1 
ATOM   10670 N  NE2 . GLN A 1 1788 ? 128.516 152.295 91.931  1.00 79.91  ? 1359 GLN A NE2 1 
ATOM   10671 N  N   . TYR A 1 1789 ? 127.282 155.599 97.411  1.00 55.50  ? 1360 TYR A N   1 
ATOM   10672 C  CA  . TYR A 1 1789 ? 126.385 155.790 98.534  1.00 58.51  ? 1360 TYR A CA  1 
ATOM   10673 C  C   . TYR A 1 1789 ? 124.964 155.949 98.037  1.00 61.63  ? 1360 TYR A C   1 
ATOM   10674 O  O   . TYR A 1 1789 ? 124.733 156.427 96.923  1.00 63.06  ? 1360 TYR A O   1 
ATOM   10675 C  CB  . TYR A 1 1789 ? 126.750 157.014 99.348  1.00 71.39  ? 1360 TYR A CB  1 
ATOM   10676 C  CG  . TYR A 1 1789 ? 128.046 156.902 100.086 1.00 78.17  ? 1360 TYR A CG  1 
ATOM   10677 C  CD1 . TYR A 1 1789 ? 129.236 157.336 99.520  1.00 80.61  ? 1360 TYR A CD1 1 
ATOM   10678 C  CD2 . TYR A 1 1789 ? 128.078 156.363 101.367 1.00 85.16  ? 1360 TYR A CD2 1 
ATOM   10679 C  CE1 . TYR A 1 1789 ? 130.429 157.244 100.219 1.00 88.91  ? 1360 TYR A CE1 1 
ATOM   10680 C  CE2 . TYR A 1 1789 ? 129.260 156.261 102.075 1.00 95.19  ? 1360 TYR A CE2 1 
ATOM   10681 C  CZ  . TYR A 1 1789 ? 130.435 156.702 101.499 1.00 102.03 ? 1360 TYR A CZ  1 
ATOM   10682 O  OH  . TYR A 1 1789 ? 131.613 156.594 102.209 1.00 106.66 ? 1360 TYR A OH  1 
ATOM   10683 N  N   . LEU A 1 1790 ? 124.010 155.586 98.886  1.00 52.72  ? 1361 LEU A N   1 
ATOM   10684 C  CA  . LEU A 1 1790 ? 122.616 155.681 98.491  1.00 52.99  ? 1361 LEU A CA  1 
ATOM   10685 C  C   . LEU A 1 1790 ? 122.116 157.109 98.620  1.00 56.83  ? 1361 LEU A C   1 
ATOM   10686 O  O   . LEU A 1 1790 ? 122.429 157.805 99.592  1.00 61.72  ? 1361 LEU A O   1 
ATOM   10687 C  CB  . LEU A 1 1790 ? 121.751 154.755 99.330  1.00 53.15  ? 1361 LEU A CB  1 
ATOM   10688 C  CG  . LEU A 1 1790 ? 121.668 153.351 98.754  1.00 56.27  ? 1361 LEU A CG  1 
ATOM   10689 C  CD1 . LEU A 1 1790 ? 123.012 152.631 98.829  1.00 64.70  ? 1361 LEU A CD1 1 
ATOM   10690 C  CD2 . LEU A 1 1790 ? 120.567 152.573 99.449  1.00 61.77  ? 1361 LEU A CD2 1 
ATOM   10691 N  N   . THR A 1 1791 ? 121.338 157.549 97.628  1.00 50.38  ? 1362 THR A N   1 
ATOM   10692 C  CA  . THR A 1 1791 ? 120.809 158.914 97.602  1.00 53.28  ? 1362 THR A CA  1 
ATOM   10693 C  C   . THR A 1 1791 ? 119.314 158.868 97.344  1.00 43.89  ? 1362 THR A C   1 
ATOM   10694 O  O   . THR A 1 1791 ? 118.856 158.907 96.202  1.00 53.06  ? 1362 THR A O   1 
ATOM   10695 C  CB  . THR A 1 1791 ? 121.520 159.768 96.564  1.00 63.47  ? 1362 THR A CB  1 
ATOM   10696 O  OG1 . THR A 1 1791 ? 121.343 159.186 95.267  1.00 62.50  ? 1362 THR A OG1 1 
ATOM   10697 C  CG2 . THR A 1 1791 ? 123.020 159.887 96.892  1.00 69.09  ? 1362 THR A CG2 1 
ATOM   10698 N  N   . TYR A 1 1792 ? 118.555 158.810 98.419  1.00 46.22  ? 1363 TYR A N   1 
ATOM   10699 C  CA  . TYR A 1 1792 ? 117.110 158.886 98.317  1.00 49.67  ? 1363 TYR A CA  1 
ATOM   10700 C  C   . TYR A 1 1792 ? 116.702 160.307 97.957  1.00 55.11  ? 1363 TYR A C   1 
ATOM   10701 O  O   . TYR A 1 1792 ? 117.102 161.267 98.623  1.00 59.01  ? 1363 TYR A O   1 
ATOM   10702 C  CB  . TYR A 1 1792 ? 116.486 158.492 99.651  1.00 63.02  ? 1363 TYR A CB  1 
ATOM   10703 C  CG  . TYR A 1 1792 ? 116.514 157.012 99.926  1.00 58.24  ? 1363 TYR A CG  1 
ATOM   10704 C  CD1 . TYR A 1 1792 ? 117.712 156.360 100.186 1.00 56.70  ? 1363 TYR A CD1 1 
ATOM   10705 C  CD2 . TYR A 1 1792 ? 115.351 156.277 99.946  1.00 49.22  ? 1363 TYR A CD2 1 
ATOM   10706 C  CE1 . TYR A 1 1792 ? 117.745 155.028 100.439 1.00 52.30  ? 1363 TYR A CE1 1 
ATOM   10707 C  CE2 . TYR A 1 1792 ? 115.369 154.950 100.211 1.00 48.45  ? 1363 TYR A CE2 1 
ATOM   10708 C  CZ  . TYR A 1 1792 ? 116.567 154.323 100.450 1.00 55.17  ? 1363 TYR A CZ  1 
ATOM   10709 O  OH  . TYR A 1 1792 ? 116.580 152.969 100.706 1.00 63.86  ? 1363 TYR A OH  1 
ATOM   10710 N  N   . THR A 1 1793 ? 115.887 160.445 96.926  1.00 52.36  ? 1364 THR A N   1 
ATOM   10711 C  CA  . THR A 1 1793 ? 115.416 161.751 96.503  1.00 46.49  ? 1364 THR A CA  1 
ATOM   10712 C  C   . THR A 1 1793 ? 114.047 162.096 97.062  1.00 44.89  ? 1364 THR A C   1 
ATOM   10713 O  O   . THR A 1 1793 ? 113.465 163.101 96.651  1.00 54.43  ? 1364 THR A O   1 
ATOM   10714 C  CB  . THR A 1 1793 ? 115.379 161.823 94.975  1.00 55.01  ? 1364 THR A CB  1 
ATOM   10715 O  OG1 . THR A 1 1793 ? 114.434 160.864 94.469  1.00 48.11  ? 1364 THR A OG1 1 
ATOM   10716 C  CG2 . THR A 1 1793 ? 116.768 161.536 94.404  1.00 58.08  ? 1364 THR A CG2 1 
ATOM   10717 N  N   . SER A 1 1794 ? 113.506 161.289 97.958  1.00 37.50  ? 1365 SER A N   1 
ATOM   10718 C  CA  . SER A 1 1794 ? 112.188 161.563 98.505  1.00 37.89  ? 1365 SER A CA  1 
ATOM   10719 C  C   . SER A 1 1794 ? 112.070 160.814 99.820  1.00 48.27  ? 1365 SER A C   1 
ATOM   10720 O  O   . SER A 1 1794 ? 112.926 159.995 100.161 1.00 55.23  ? 1365 SER A O   1 
ATOM   10721 C  CB  . SER A 1 1794 ? 111.103 161.142 97.533  1.00 37.88  ? 1365 SER A CB  1 
ATOM   10722 O  OG  . SER A 1 1794 ? 111.254 159.762 97.262  1.00 46.38  ? 1365 SER A OG  1 
ATOM   10723 N  N   . THR A 1 1795 ? 111.012 161.104 100.567 1.00 41.92  ? 1366 THR A N   1 
ATOM   10724 C  CA  . THR A 1 1795 ? 110.849 160.485 101.870 1.00 38.56  ? 1366 THR A CA  1 
ATOM   10725 C  C   . THR A 1 1795 ? 109.566 159.681 101.923 1.00 44.50  ? 1366 THR A C   1 
ATOM   10726 O  O   . THR A 1 1795 ? 108.591 159.989 101.236 1.00 50.84  ? 1366 THR A O   1 
ATOM   10727 C  CB  . THR A 1 1795 ? 110.846 161.509 102.978 1.00 52.05  ? 1366 THR A CB  1 
ATOM   10728 O  OG1 . THR A 1 1795 ? 111.935 162.414 102.770 1.00 61.21  ? 1366 THR A OG1 1 
ATOM   10729 C  CG2 . THR A 1 1795 ? 111.038 160.818 104.326 1.00 59.61  ? 1366 THR A CG2 1 
ATOM   10730 N  N   . LEU A 1 1796 ? 109.600 158.623 102.728 1.00 50.44  ? 1367 LEU A N   1 
ATOM   10731 C  CA  . LEU A 1 1796 ? 108.420 157.815 102.964 1.00 48.66  ? 1367 LEU A CA  1 
ATOM   10732 C  C   . LEU A 1 1796 ? 107.326 158.710 103.505 1.00 61.93  ? 1367 LEU A C   1 
ATOM   10733 O  O   . LEU A 1 1796 ? 107.496 159.334 104.556 1.00 66.17  ? 1367 LEU A O   1 
ATOM   10734 C  CB  . LEU A 1 1796 ? 108.729 156.700 103.961 1.00 54.23  ? 1367 LEU A CB  1 
ATOM   10735 C  CG  . LEU A 1 1796 ? 107.558 155.744 104.243 1.00 69.25  ? 1367 LEU A CG  1 
ATOM   10736 C  CD1 . LEU A 1 1796 ? 107.214 154.927 102.985 1.00 67.30  ? 1367 LEU A CD1 1 
ATOM   10737 C  CD2 . LEU A 1 1796 ? 107.777 154.829 105.462 1.00 66.51  ? 1367 LEU A CD2 1 
ATOM   10738 N  N   . ASP A 1 1797 ? 106.214 158.793 102.779 1.00 62.58  ? 1368 ASP A N   1 
ATOM   10739 C  CA  . ASP A 1 1797 ? 105.122 159.693 103.129 1.00 61.48  ? 1368 ASP A CA  1 
ATOM   10740 C  C   . ASP A 1 1797 ? 104.099 159.068 104.070 1.00 68.34  ? 1368 ASP A C   1 
ATOM   10741 O  O   . ASP A 1 1797 ? 103.228 159.786 104.574 1.00 76.65  ? 1368 ASP A O   1 
ATOM   10742 C  CB  . ASP A 1 1797 ? 104.410 160.157 101.861 1.00 70.35  ? 1368 ASP A CB  1 
ATOM   10743 C  CG  . ASP A 1 1797 ? 103.972 158.985 100.986 1.00 84.67  ? 1368 ASP A CG  1 
ATOM   10744 O  OD1 . ASP A 1 1797 ? 104.279 157.821 101.349 1.00 75.88  ? 1368 ASP A OD1 1 
ATOM   10745 O  OD2 . ASP A 1 1797 ? 103.320 159.224 99.943  1.00 88.16  ? 1368 ASP A OD2 1 
ATOM   10746 N  N   . LEU A 1 1798 ? 104.175 157.765 104.311 1.00 59.56  ? 1369 LEU A N   1 
ATOM   10747 C  CA  . LEU A 1 1798 ? 103.266 157.109 105.236 1.00 56.83  ? 1369 LEU A CA  1 
ATOM   10748 C  C   . LEU A 1 1798 ? 103.489 157.595 106.664 1.00 70.02  ? 1369 LEU A C   1 
ATOM   10749 O  O   . LEU A 1 1798 ? 104.612 157.892 107.080 1.00 71.30  ? 1369 LEU A O   1 
ATOM   10750 C  CB  . LEU A 1 1798 ? 103.498 155.617 105.198 1.00 70.27  ? 1369 LEU A CB  1 
ATOM   10751 C  CG  . LEU A 1 1798 ? 103.233 155.023 103.832 1.00 78.69  ? 1369 LEU A CG  1 
ATOM   10752 C  CD1 . LEU A 1 1798 ? 103.559 153.532 103.881 1.00 74.25  ? 1369 LEU A CD1 1 
ATOM   10753 C  CD2 . LEU A 1 1798 ? 101.790 155.295 103.417 1.00 77.24  ? 1369 LEU A CD2 1 
ATOM   10754 N  N   . ASP A 1 1799 ? 102.409 157.632 107.436 1.00 80.01  ? 1370 ASP A N   1 
ATOM   10755 C  CA  . ASP A 1 1799 ? 102.451 158.069 108.836 1.00 78.07  ? 1370 ASP A CA  1 
ATOM   10756 C  C   . ASP A 1 1799 ? 102.546 156.825 109.708 1.00 69.95  ? 1370 ASP A C   1 
ATOM   10757 O  O   . ASP A 1 1799 ? 101.544 156.320 110.222 1.00 72.28  ? 1370 ASP A O   1 
ATOM   10758 C  CB  . ASP A 1 1799 ? 101.220 158.906 109.186 1.00 92.54  ? 1370 ASP A CB  1 
ATOM   10759 C  CG  . ASP A 1 1799 ? 99.908  158.275 108.686 1.00 103.86 ? 1370 ASP A CG  1 
ATOM   10760 O  OD1 . ASP A 1 1799 ? 99.954  157.247 107.967 1.00 98.26  ? 1370 ASP A OD1 1 
ATOM   10761 O  OD2 . ASP A 1 1799 ? 98.828  158.823 108.997 1.00 100.28 ? 1370 ASP A OD2 1 
ATOM   10762 N  N   . LEU A 1 1800 ? 103.771 156.337 109.892 1.00 70.15  ? 1371 LEU A N   1 
ATOM   10763 C  CA  . LEU A 1 1800 ? 103.967 155.136 110.699 1.00 69.70  ? 1371 LEU A CA  1 
ATOM   10764 C  C   . LEU A 1 1800 ? 103.614 155.341 112.170 1.00 69.10  ? 1371 LEU A C   1 
ATOM   10765 O  O   . LEU A 1 1800 ? 103.729 154.395 112.958 1.00 70.88  ? 1371 LEU A O   1 
ATOM   10766 C  CB  . LEU A 1 1800 ? 105.412 154.651 110.581 1.00 57.75  ? 1371 LEU A CB  1 
ATOM   10767 C  CG  . LEU A 1 1800 ? 105.819 154.215 109.185 1.00 68.67  ? 1371 LEU A CG  1 
ATOM   10768 C  CD1 . LEU A 1 1800 ? 107.210 153.584 109.205 1.00 73.94  ? 1371 LEU A CD1 1 
ATOM   10769 C  CD2 . LEU A 1 1800 ? 104.772 153.259 108.640 1.00 72.23  ? 1371 LEU A CD2 1 
ATOM   10770 N  N   . THR A 1 1801 ? 103.160 156.529 112.561 1.00 63.03  ? 1372 THR A N   1 
ATOM   10771 C  CA  . THR A 1 1801 ? 102.831 156.763 113.953 1.00 59.61  ? 1372 THR A CA  1 
ATOM   10772 C  C   . THR A 1 1801 ? 101.671 155.906 114.429 1.00 60.95  ? 1372 THR A C   1 
ATOM   10773 O  O   . THR A 1 1801 ? 101.401 155.885 115.634 1.00 67.32  ? 1372 THR A O   1 
ATOM   10774 C  CB  . THR A 1 1801 ? 102.499 158.239 114.159 1.00 70.22  ? 1372 THR A CB  1 
ATOM   10775 O  OG1 . THR A 1 1801 ? 102.175 158.476 115.535 1.00 69.78  ? 1372 THR A OG1 1 
ATOM   10776 C  CG2 . THR A 1 1801 ? 101.318 158.647 113.268 1.00 71.85  ? 1372 THR A CG2 1 
ATOM   10777 N  N   . ARG A 1 1802 ? 100.982 155.203 113.528 1.00 55.36  ? 1373 ARG A N   1 
ATOM   10778 C  CA  . ARG A 1 1802 ? 99.872  154.368 113.966 1.00 53.58  ? 1373 ARG A CA  1 
ATOM   10779 C  C   . ARG A 1 1802 ? 100.306 153.372 115.013 1.00 48.51  ? 1373 ARG A C   1 
ATOM   10780 O  O   . ARG A 1 1802 ? 99.510  152.983 115.871 1.00 56.90  ? 1373 ARG A O   1 
ATOM   10781 C  CB  . ARG A 1 1802 ? 99.276  153.603 112.800 1.00 57.41  ? 1373 ARG A CB  1 
ATOM   10782 C  CG  . ARG A 1 1802 ? 98.099  152.710 113.208 1.00 59.49  ? 1373 ARG A CG  1 
ATOM   10783 C  CD  . ARG A 1 1802 ? 97.713  151.791 112.079 1.00 54.82  ? 1373 ARG A CD  1 
ATOM   10784 N  NE  . ARG A 1 1802 ? 97.232  152.585 110.966 1.00 53.69  ? 1373 ARG A NE  1 
ATOM   10785 C  CZ  . ARG A 1 1802 ? 97.994  152.938 109.938 1.00 62.94  ? 1373 ARG A CZ  1 
ATOM   10786 N  NH1 . ARG A 1 1802 ? 99.273  152.579 109.904 1.00 62.45  ? 1373 ARG A NH1 1 
ATOM   10787 N  NH2 . ARG A 1 1802 ? 97.487  153.676 108.959 1.00 73.80  ? 1373 ARG A NH2 1 
ATOM   10788 N  N   . TYR A 1 1803 ? 101.547 152.946 114.963 1.00 45.22  ? 1374 TYR A N   1 
ATOM   10789 C  CA  . TYR A 1 1803 ? 101.965 151.902 115.863 1.00 48.63  ? 1374 TYR A CA  1 
ATOM   10790 C  C   . TYR A 1 1803 ? 102.268 152.422 117.247 1.00 62.28  ? 1374 TYR A C   1 
ATOM   10791 O  O   . TYR A 1 1803 ? 103.049 151.792 117.967 1.00 68.38  ? 1374 TYR A O   1 
ATOM   10792 C  CB  . TYR A 1 1803 ? 103.166 151.161 115.280 1.00 54.67  ? 1374 TYR A CB  1 
ATOM   10793 C  CG  . TYR A 1 1803 ? 102.901 150.658 113.883 1.00 53.24  ? 1374 TYR A CG  1 
ATOM   10794 C  CD1 . TYR A 1 1803 ? 102.066 149.576 113.671 1.00 57.86  ? 1374 TYR A CD1 1 
ATOM   10795 C  CD2 . TYR A 1 1803 ? 103.502 151.240 112.780 1.00 56.27  ? 1374 TYR A CD2 1 
ATOM   10796 C  CE1 . TYR A 1 1803 ? 101.815 149.106 112.397 1.00 56.44  ? 1374 TYR A CE1 1 
ATOM   10797 C  CE2 . TYR A 1 1803 ? 103.255 150.769 111.500 1.00 54.65  ? 1374 TYR A CE2 1 
ATOM   10798 C  CZ  . TYR A 1 1803 ? 102.420 149.708 111.321 1.00 49.22  ? 1374 TYR A CZ  1 
ATOM   10799 O  OH  . TYR A 1 1803 ? 102.181 149.243 110.060 1.00 53.54  ? 1374 TYR A OH  1 
ATOM   10800 N  N   . ARG A 1 1804 ? 101.697 153.558 117.650 1.00 60.87  ? 1375 ARG A N   1 
ATOM   10801 C  CA  . ARG A 1 1804 ? 102.049 154.088 118.960 1.00 57.61  ? 1375 ARG A CA  1 
ATOM   10802 C  C   . ARG A 1 1804 ? 101.524 153.206 120.065 1.00 50.96  ? 1375 ARG A C   1 
ATOM   10803 O  O   . ARG A 1 1804 ? 102.223 152.943 121.044 1.00 60.33  ? 1375 ARG A O   1 
ATOM   10804 C  CB  . ARG A 1 1804 ? 101.579 155.531 119.129 1.00 72.71  ? 1375 ARG A CB  1 
ATOM   10805 C  CG  . ARG A 1 1804 ? 101.864 156.075 120.539 1.00 78.93  ? 1375 ARG A CG  1 
ATOM   10806 C  CD  . ARG A 1 1804 ? 101.715 157.604 120.631 1.00 82.40  ? 1375 ARG A CD  1 
ATOM   10807 N  NE  . ARG A 1 1804 ? 102.822 158.286 119.956 1.00 82.49  ? 1375 ARG A NE  1 
ATOM   10808 C  CZ  . ARG A 1 1804 ? 102.757 158.784 118.725 1.00 85.81  ? 1375 ARG A CZ  1 
ATOM   10809 N  NH1 . ARG A 1 1804 ? 101.645 158.645 118.016 1.00 81.57  ? 1375 ARG A NH1 1 
ATOM   10810 N  NH2 . ARG A 1 1804 ? 103.814 159.383 118.188 1.00 84.40  ? 1375 ARG A NH2 1 
ATOM   10811 N  N   . GLU A 1 1805 ? 100.317 152.709 119.907 1.00 53.26  ? 1376 GLU A N   1 
ATOM   10812 C  CA  . GLU A 1 1805 ? 99.724  151.881 120.933 1.00 59.90  ? 1376 GLU A CA  1 
ATOM   10813 C  C   . GLU A 1 1805 ? 100.297 150.470 120.920 1.00 58.18  ? 1376 GLU A C   1 
ATOM   10814 O  O   . GLU A 1 1805 ? 100.333 149.811 121.964 1.00 60.40  ? 1376 GLU A O   1 
ATOM   10815 C  CB  . GLU A 1 1805 ? 98.213  151.868 120.724 1.00 76.16  ? 1376 GLU A CB  1 
ATOM   10816 C  CG  . GLU A 1 1805 ? 97.615  153.284 120.578 1.00 83.59  ? 1376 GLU A CG  1 
ATOM   10817 C  CD  . GLU A 1 1805 ? 97.562  153.776 119.116 1.00 87.33  ? 1376 GLU A CD  1 
ATOM   10818 O  OE1 . GLU A 1 1805 ? 97.647  152.930 118.194 1.00 84.95  ? 1376 GLU A OE1 1 
ATOM   10819 O  OE2 . GLU A 1 1805 ? 97.429  155.003 118.887 1.00 80.00  ? 1376 GLU A OE2 1 
ATOM   10820 N  N   . ASN A 1 1806 ? 100.757 150.003 119.764 1.00 61.35  ? 1377 ASN A N   1 
ATOM   10821 C  CA  . ASN A 1 1806 ? 101.206 148.620 119.574 1.00 65.42  ? 1377 ASN A CA  1 
ATOM   10822 C  C   . ASN A 1 1806 ? 102.534 148.400 120.288 1.00 65.05  ? 1377 ASN A C   1 
ATOM   10823 O  O   . ASN A 1 1806 ? 103.597 148.705 119.742 1.00 68.13  ? 1377 ASN A O   1 
ATOM   10824 C  CB  . ASN A 1 1806 ? 101.338 148.327 118.081 1.00 69.14  ? 1377 ASN A CB  1 
ATOM   10825 C  CG  . ASN A 1 1806 ? 101.524 146.844 117.779 1.00 68.71  ? 1377 ASN A CG  1 
ATOM   10826 O  OD1 . ASN A 1 1806 ? 102.284 146.147 118.456 1.00 70.41  ? 1377 ASN A OD1 1 
ATOM   10827 N  ND2 . ASN A 1 1806 ? 100.826 146.357 116.746 1.00 64.80  ? 1377 ASN A ND2 1 
ATOM   10828 N  N   . GLU A 1 1807 ? 102.496 147.826 121.496 1.00 61.80  ? 1378 GLU A N   1 
ATOM   10829 C  CA  . GLU A 1 1807 ? 103.723 147.757 122.278 1.00 58.51  ? 1378 GLU A CA  1 
ATOM   10830 C  C   . GLU A 1 1807 ? 104.672 146.693 121.750 1.00 59.47  ? 1378 GLU A C   1 
ATOM   10831 O  O   . GLU A 1 1807 ? 105.863 146.719 122.085 1.00 63.41  ? 1378 GLU A O   1 
ATOM   10832 C  CB  . GLU A 1 1807 ? 103.417 147.491 123.752 1.00 66.05  ? 1378 GLU A CB  1 
ATOM   10833 C  CG  . GLU A 1 1807 ? 102.832 146.110 124.063 1.00 73.99  ? 1378 GLU A CG  1 
ATOM   10834 C  CD  . GLU A 1 1807 ? 103.928 145.074 124.409 1.00 75.93  ? 1378 GLU A CD  1 
ATOM   10835 O  OE1 . GLU A 1 1807 ? 105.051 145.512 124.788 1.00 68.63  ? 1378 GLU A OE1 1 
ATOM   10836 O  OE2 . GLU A 1 1807 ? 103.665 143.843 124.334 1.00 66.11  ? 1378 GLU A OE2 1 
ATOM   10837 N  N   . LEU A 1 1808 ? 104.173 145.754 120.943 1.00 54.96  ? 1379 LEU A N   1 
ATOM   10838 C  CA  . LEU A 1 1808 ? 105.080 144.861 120.243 1.00 51.73  ? 1379 LEU A CA  1 
ATOM   10839 C  C   . LEU A 1 1808 ? 105.991 145.661 119.349 1.00 52.36  ? 1379 LEU A C   1 
ATOM   10840 O  O   . LEU A 1 1808 ? 107.151 145.304 119.170 1.00 64.89  ? 1379 LEU A O   1 
ATOM   10841 C  CB  . LEU A 1 1808 ? 104.313 143.850 119.393 1.00 61.90  ? 1379 LEU A CB  1 
ATOM   10842 C  CG  . LEU A 1 1808 ? 103.199 143.078 120.105 1.00 73.42  ? 1379 LEU A CG  1 
ATOM   10843 C  CD1 . LEU A 1 1808 ? 102.446 142.142 119.142 1.00 66.40  ? 1379 LEU A CD1 1 
ATOM   10844 C  CD2 . LEU A 1 1808 ? 103.748 142.315 121.346 1.00 75.07  ? 1379 LEU A CD2 1 
ATOM   10845 N  N   . ILE A 1 1809 ? 105.492 146.746 118.780 1.00 52.47  ? 1380 ILE A N   1 
ATOM   10846 C  CA  . ILE A 1 1809 ? 106.290 147.508 117.849 1.00 52.55  ? 1380 ILE A CA  1 
ATOM   10847 C  C   . ILE A 1 1809 ? 106.884 148.734 118.506 1.00 63.08  ? 1380 ILE A C   1 
ATOM   10848 O  O   . ILE A 1 1809 ? 107.951 149.173 118.093 1.00 67.13  ? 1380 ILE A O   1 
ATOM   10849 C  CB  . ILE A 1 1809 ? 105.475 147.876 116.599 1.00 66.99  ? 1380 ILE A CB  1 
ATOM   10850 C  CG1 . ILE A 1 1809 ? 104.782 146.641 116.024 1.00 75.37  ? 1380 ILE A CG1 1 
ATOM   10851 C  CG2 . ILE A 1 1809 ? 106.392 148.543 115.525 1.00 67.74  ? 1380 ILE A CG2 1 
ATOM   10852 C  CD1 . ILE A 1 1809 ? 105.696 145.507 115.671 1.00 79.78  ? 1380 ILE A CD1 1 
ATOM   10853 N  N   . TYR A 1 1810 ? 106.247 149.293 119.525 1.00 64.63  ? 1381 TYR A N   1 
ATOM   10854 C  CA  . TYR A 1 1810 ? 106.619 150.669 119.745 1.00 57.98  ? 1381 TYR A CA  1 
ATOM   10855 C  C   . TYR A 1 1810 ? 107.784 150.498 120.752 1.00 65.80  ? 1381 TYR A C   1 
ATOM   10856 O  O   . TYR A 1 1810 ? 108.266 149.374 120.978 1.00 69.88  ? 1381 TYR A O   1 
ATOM   10857 C  CB  . TYR A 1 1810 ? 105.604 151.530 120.476 1.00 57.45  ? 1381 TYR A CB  1 
ATOM   10858 C  CG  . TYR A 1 1810 ? 105.791 153.026 120.246 1.00 58.57  ? 1381 TYR A CG  1 
ATOM   10859 C  CD1 . TYR A 1 1810 ? 105.111 153.581 119.160 1.00 61.12  ? 1381 TYR A CD1 1 
ATOM   10860 C  CD2 . TYR A 1 1810 ? 106.831 153.871 120.914 1.00 76.72  ? 1381 TYR A CD2 1 
ATOM   10861 C  CE1 . TYR A 1 1810 ? 105.284 154.891 118.762 1.00 75.78  ? 1381 TYR A CE1 1 
ATOM   10862 C  CE2 . TYR A 1 1810 ? 107.043 155.178 120.506 1.00 79.76  ? 1381 TYR A CE2 1 
ATOM   10863 C  CZ  . TYR A 1 1810 ? 106.244 155.694 119.523 1.00 82.98  ? 1381 TYR A CZ  1 
ATOM   10864 O  OH  . TYR A 1 1810 ? 106.543 157.023 119.345 1.00 81.11  ? 1381 TYR A OH  1 
ATOM   10865 N  N   . ASP A 1 1811 ? 108.142 151.580 121.457 1.00 71.36  ? 1382 ASP A N   1 
ATOM   10866 C  CA  . ASP A 1 1811 ? 108.811 151.572 122.757 1.00 70.90  ? 1382 ASP A CA  1 
ATOM   10867 C  C   . ASP A 1 1811 ? 108.519 152.912 123.426 1.00 65.59  ? 1382 ASP A C   1 
ATOM   10868 O  O   . ASP A 1 1811 ? 109.149 153.930 123.104 1.00 65.81  ? 1382 ASP A O   1 
ATOM   10869 C  CB  . ASP A 1 1811 ? 110.318 151.362 122.645 1.00 75.12  ? 1382 ASP A CB  1 
ATOM   10870 C  CG  . ASP A 1 1811 ? 110.948 151.043 123.997 1.00 86.66  ? 1382 ASP A CG  1 
ATOM   10871 O  OD1 . ASP A 1 1811 ? 110.177 150.980 124.985 1.00 85.26  ? 1382 ASP A OD1 1 
ATOM   10872 O  OD2 . ASP A 1 1811 ? 112.179 150.898 124.115 1.00 82.18  ? 1382 ASP A OD2 1 
ATOM   10873 N  N   . SER A 1 1812 ? 107.553 152.928 124.342 1.00 63.38  ? 1383 SER A N   1 
ATOM   10874 C  CA  . SER A 1 1812 ? 107.047 154.204 124.818 1.00 56.52  ? 1383 SER A CA  1 
ATOM   10875 C  C   . SER A 1 1812 ? 108.123 154.963 125.564 1.00 64.51  ? 1383 SER A C   1 
ATOM   10876 O  O   . SER A 1 1812 ? 108.389 156.131 125.266 1.00 70.72  ? 1383 SER A O   1 
ATOM   10877 C  CB  . SER A 1 1812 ? 105.825 153.983 125.692 1.00 59.34  ? 1383 SER A CB  1 
ATOM   10878 O  OG  . SER A 1 1812 ? 104.793 153.347 124.964 1.00 62.67  ? 1383 SER A OG  1 
ATOM   10879 N  N   . ASN A 1 1813 ? 108.780 154.310 126.516 1.00 65.01  ? 1384 ASN A N   1 
ATOM   10880 C  CA  . ASN A 1 1813 ? 109.723 154.969 127.417 1.00 61.87  ? 1384 ASN A CA  1 
ATOM   10881 C  C   . ASN A 1 1813 ? 111.071 154.289 127.312 1.00 61.12  ? 1384 ASN A C   1 
ATOM   10882 O  O   . ASN A 1 1813 ? 111.474 153.527 128.198 1.00 75.11  ? 1384 ASN A O   1 
ATOM   10883 C  CB  . ASN A 1 1813 ? 109.225 154.950 128.860 1.00 73.29  ? 1384 ASN A CB  1 
ATOM   10884 C  CG  . ASN A 1 1813 ? 109.790 156.091 129.671 1.00 85.85  ? 1384 ASN A CG  1 
ATOM   10885 O  OD1 . ASN A 1 1813 ? 110.851 156.626 129.338 1.00 81.27  ? 1384 ASN A OD1 1 
ATOM   10886 N  ND2 . ASN A 1 1813 ? 109.096 156.467 130.746 1.00 82.08  ? 1384 ASN A ND2 1 
ATOM   10887 N  N   . PRO A 1 1814 ? 111.796 154.546 126.234 1.00 58.68  ? 1385 PRO A N   1 
ATOM   10888 C  CA  . PRO A 1 1814 ? 113.030 153.792 125.981 1.00 71.78  ? 1385 PRO A CA  1 
ATOM   10889 C  C   . PRO A 1 1814 ? 114.116 154.025 127.007 1.00 80.81  ? 1385 PRO A C   1 
ATOM   10890 O  O   . PRO A 1 1814 ? 114.970 153.149 127.196 1.00 84.52  ? 1385 PRO A O   1 
ATOM   10891 C  CB  . PRO A 1 1814 ? 113.446 154.274 124.588 1.00 68.52  ? 1385 PRO A CB  1 
ATOM   10892 C  CG  . PRO A 1 1814 ? 112.181 154.770 123.995 1.00 70.24  ? 1385 PRO A CG  1 
ATOM   10893 C  CD  . PRO A 1 1814 ? 111.440 155.405 125.108 1.00 62.86  ? 1385 PRO A CD  1 
ATOM   10894 N  N   . LEU A 1 1815 ? 114.109 155.169 127.685 1.00 75.93  ? 1386 LEU A N   1 
ATOM   10895 C  CA  . LEU A 1 1815 ? 115.110 155.470 128.701 1.00 66.52  ? 1386 LEU A CA  1 
ATOM   10896 C  C   . LEU A 1 1815 ? 114.447 155.276 130.059 1.00 81.91  ? 1386 LEU A C   1 
ATOM   10897 O  O   . LEU A 1 1815 ? 113.963 156.216 130.690 1.00 87.71  ? 1386 LEU A O   1 
ATOM   10898 C  CB  . LEU A 1 1815 ? 115.630 156.875 128.525 1.00 65.92  ? 1386 LEU A CB  1 
ATOM   10899 C  CG  . LEU A 1 1815 ? 116.630 157.055 127.404 1.00 82.18  ? 1386 LEU A CG  1 
ATOM   10900 C  CD1 . LEU A 1 1815 ? 115.947 156.920 126.047 1.00 82.12  ? 1386 LEU A CD1 1 
ATOM   10901 C  CD2 . LEU A 1 1815 ? 117.207 158.452 127.556 1.00 97.22  ? 1386 LEU A CD2 1 
ATOM   10902 N  N   . LYS A 1 1816 ? 114.393 154.023 130.491 1.00 83.82  ? 1387 LYS A N   1 
ATOM   10903 C  CA  . LYS A 1 1816 ? 113.852 153.665 131.796 1.00 94.77  ? 1387 LYS A CA  1 
ATOM   10904 C  C   . LYS A 1 1816 ? 114.878 152.963 132.663 1.00 102.04 ? 1387 LYS A C   1 
ATOM   10905 O  O   . LYS A 1 1816 ? 114.937 153.207 133.874 1.00 104.95 ? 1387 LYS A O   1 
ATOM   10906 C  CB  . LYS A 1 1816 ? 112.604 152.758 131.640 1.00 103.13 ? 1387 LYS A CB  1 
ATOM   10907 C  CG  . LYS A 1 1816 ? 111.748 152.585 132.922 1.00 107.94 ? 1387 LYS A CG  1 
ATOM   10908 C  CD  . LYS A 1 1816 ? 110.553 151.626 132.733 1.00 104.32 ? 1387 LYS A CD  1 
ATOM   10909 C  CE  . LYS A 1 1816 ? 111.023 150.194 132.418 1.00 96.62  ? 1387 LYS A CE  1 
ATOM   10910 N  NZ  . LYS A 1 1816 ? 109.920 149.188 132.285 1.00 85.94  ? 1387 LYS A NZ  1 
ATOM   10911 N  N   . GLY A 1 1817 ? 115.709 152.113 132.064 1.00 103.44 ? 1388 GLY A N   1 
ATOM   10912 C  CA  . GLY A 1 1817 ? 116.718 151.361 132.776 1.00 110.87 ? 1388 GLY A CA  1 
ATOM   10913 C  C   . GLY A 1 1817 ? 117.972 152.130 133.105 1.00 110.81 ? 1388 GLY A C   1 
ATOM   10914 O  O   . GLY A 1 1817 ? 118.897 151.564 133.697 1.00 112.11 ? 1388 GLY A O   1 
ATOM   10915 N  N   . GLY A 1 1818 ? 118.025 153.410 132.740 1.00 100.92 ? 1389 GLY A N   1 
ATOM   10916 C  CA  . GLY A 1 1818 ? 119.180 154.237 133.002 1.00 108.13 ? 1389 GLY A CA  1 
ATOM   10917 C  C   . GLY A 1 1818 ? 120.137 154.297 131.824 1.00 109.96 ? 1389 GLY A C   1 
ATOM   10918 O  O   . GLY A 1 1818 ? 120.008 153.582 130.827 1.00 106.63 ? 1389 GLY A O   1 
ATOM   10919 N  N   . LEU A 1 1819 ? 121.129 155.181 131.955 1.00 113.37 ? 1390 LEU A N   1 
ATOM   10920 C  CA  . LEU A 1 1819 ? 122.131 155.423 130.924 1.00 111.43 ? 1390 LEU A CA  1 
ATOM   10921 C  C   . LEU A 1 1819 ? 123.518 155.483 131.571 1.00 118.88 ? 1390 LEU A C   1 
ATOM   10922 O  O   . LEU A 1 1819 ? 123.652 155.739 132.771 1.00 118.25 ? 1390 LEU A O   1 
ATOM   10923 C  CB  . LEU A 1 1819 ? 121.831 156.728 130.145 1.00 113.20 ? 1390 LEU A CB  1 
ATOM   10924 C  CG  . LEU A 1 1819 ? 120.492 156.886 129.395 1.00 112.92 ? 1390 LEU A CG  1 
ATOM   10925 C  CD1 . LEU A 1 1819 ? 119.331 157.310 130.315 1.00 110.35 ? 1390 LEU A CD1 1 
ATOM   10926 C  CD2 . LEU A 1 1819 ? 120.622 157.866 128.235 1.00 111.68 ? 1390 LEU A CD2 1 
ATOM   10927 N  N   . ASN A 1 1820 ? 124.557 155.225 130.764 1.00 121.51 ? 1391 ASN A N   1 
ATOM   10928 C  CA  . ASN A 1 1820 ? 125.953 155.269 131.205 1.00 122.57 ? 1391 ASN A CA  1 
ATOM   10929 C  C   . ASN A 1 1820 ? 126.746 156.216 130.302 1.00 131.45 ? 1391 ASN A C   1 
ATOM   10930 O  O   . ASN A 1 1820 ? 126.284 156.611 129.226 1.00 125.38 ? 1391 ASN A O   1 
ATOM   10931 C  CB  . ASN A 1 1820 ? 126.613 153.852 131.238 1.00 116.86 ? 1391 ASN A CB  1 
ATOM   10932 C  CG  . ASN A 1 1820 ? 126.570 153.116 129.877 1.00 121.47 ? 1391 ASN A CG  1 
ATOM   10933 O  OD1 . ASN A 1 1820 ? 126.988 153.650 128.844 1.00 124.96 ? 1391 ASN A OD1 1 
ATOM   10934 N  ND2 . ASN A 1 1820 ? 126.073 151.876 129.889 1.00 113.34 ? 1391 ASN A ND2 1 
ATOM   10935 N  N   . CYS A 1 1821 ? 127.940 156.607 130.765 1.00 140.10 ? 1392 CYS A N   1 
ATOM   10936 C  CA  . CYS A 1 1821 ? 128.840 157.445 129.972 1.00 144.74 ? 1392 CYS A CA  1 
ATOM   10937 C  C   . CYS A 1 1821 ? 129.683 156.582 129.018 1.00 149.67 ? 1392 CYS A C   1 
ATOM   10938 O  O   . CYS A 1 1821 ? 129.610 155.347 129.029 1.00 145.94 ? 1392 CYS A O   1 
ATOM   10939 C  CB  . CYS A 1 1821 ? 129.725 158.317 130.885 1.00 142.51 ? 1392 CYS A CB  1 
ATOM   10940 S  SG  . CYS A 1 1821 ? 130.903 157.480 132.020 1.00 138.60 ? 1392 CYS A SG  1 
ATOM   10941 N  N   . ASN A 1 1822 ? 130.474 157.261 128.172 1.00 150.21 ? 1393 ASN A N   1 
ATOM   10942 C  CA  . ASN A 1 1822 ? 131.353 156.669 127.128 1.00 148.68 ? 1393 ASN A CA  1 
ATOM   10943 C  C   . ASN A 1 1822 ? 131.013 155.237 126.662 1.00 139.27 ? 1393 ASN A C   1 
ATOM   10944 O  O   . ASN A 1 1822 ? 130.016 155.007 125.968 1.00 124.93 ? 1393 ASN A O   1 
ATOM   10945 C  CB  . ASN A 1 1822 ? 132.832 156.719 127.594 1.00 148.83 ? 1393 ASN A CB  1 
ATOM   10946 C  CG  . ASN A 1 1822 ? 133.066 156.063 128.966 1.00 147.76 ? 1393 ASN A CG  1 
ATOM   10947 O  OD1 . ASN A 1 1822 ? 132.384 155.109 129.348 1.00 146.75 ? 1393 ASN A OD1 1 
ATOM   10948 N  ND2 . ASN A 1 1822 ? 134.033 156.595 129.716 1.00 141.64 ? 1393 ASN A ND2 1 
ATOM   10949 N  N   . ASP B 2 440  ? 138.646 152.025 172.278 1.00 88.39  ? 123  ASP B N   1 
ATOM   10950 C  CA  . ASP B 2 440  ? 139.310 151.443 171.108 1.00 98.49  ? 123  ASP B CA  1 
ATOM   10951 C  C   . ASP B 2 440  ? 138.836 150.011 170.814 1.00 104.82 ? 123  ASP B C   1 
ATOM   10952 O  O   . ASP B 2 440  ? 139.457 149.036 171.248 1.00 102.28 ? 123  ASP B O   1 
ATOM   10953 C  CB  . ASP B 2 440  ? 140.834 151.450 171.294 1.00 101.64 ? 123  ASP B CB  1 
ATOM   10954 C  CG  . ASP B 2 440  ? 141.589 151.028 170.031 1.00 101.27 ? 123  ASP B CG  1 
ATOM   10955 O  OD1 . ASP B 2 440  ? 140.969 150.960 168.946 1.00 100.75 ? 123  ASP B OD1 1 
ATOM   10956 O  OD2 . ASP B 2 440  ? 142.806 150.750 170.129 1.00 99.21  ? 123  ASP B OD2 1 
ATOM   10957 N  N   . MET B 2 441  ? 137.744 149.895 170.051 1.00 105.24 ? 124  MET B N   1 
ATOM   10958 C  CA  . MET B 2 441  ? 137.171 148.609 169.664 1.00 94.40  ? 124  MET B CA  1 
ATOM   10959 C  C   . MET B 2 441  ? 137.109 148.441 168.152 1.00 91.68  ? 124  MET B C   1 
ATOM   10960 O  O   . MET B 2 441  ? 136.353 147.601 167.661 1.00 94.96  ? 124  MET B O   1 
ATOM   10961 C  CB  . MET B 2 441  ? 135.778 148.459 170.270 1.00 88.36  ? 124  MET B CB  1 
ATOM   10962 C  CG  . MET B 2 441  ? 135.780 148.482 171.782 1.00 97.41  ? 124  MET B CG  1 
ATOM   10963 S  SD  . MET B 2 441  ? 134.117 148.469 172.461 1.00 122.56 ? 124  MET B SD  1 
ATOM   10964 C  CE  . MET B 2 441  ? 133.486 150.012 171.788 1.00 101.50 ? 124  MET B CE  1 
ATOM   10965 N  N   . ALA B 2 442  ? 137.896 149.223 167.406 1.00 96.79  ? 125  ALA B N   1 
ATOM   10966 C  CA  . ALA B 2 442  ? 137.791 149.231 165.949 1.00 100.16 ? 125  ALA B CA  1 
ATOM   10967 C  C   . ALA B 2 442  ? 138.128 147.866 165.358 1.00 99.24  ? 125  ALA B C   1 
ATOM   10968 O  O   . ALA B 2 442  ? 137.387 147.337 164.519 1.00 99.47  ? 125  ALA B O   1 
ATOM   10969 C  CB  . ALA B 2 442  ? 138.703 150.312 165.363 1.00 101.47 ? 125  ALA B CB  1 
ATOM   10970 N  N   . LYS B 2 443  ? 139.242 147.273 165.792 1.00 97.92  ? 126  LYS B N   1 
ATOM   10971 C  CA  . LYS B 2 443  ? 139.617 145.956 165.283 1.00 105.73 ? 126  LYS B CA  1 
ATOM   10972 C  C   . LYS B 2 443  ? 138.628 144.880 165.731 1.00 102.81 ? 126  LYS B C   1 
ATOM   10973 O  O   . LYS B 2 443  ? 138.237 144.008 164.936 1.00 100.23 ? 126  LYS B O   1 
ATOM   10974 C  CB  . LYS B 2 443  ? 141.035 145.611 165.741 1.00 111.87 ? 126  LYS B CB  1 
ATOM   10975 C  CG  . LYS B 2 443  ? 142.057 146.711 165.483 1.00 113.88 ? 126  LYS B CG  1 
ATOM   10976 C  CD  . LYS B 2 443  ? 143.235 146.602 166.446 1.00 117.70 ? 126  LYS B CD  1 
ATOM   10977 C  CE  . LYS B 2 443  ? 142.775 146.740 167.899 1.00 112.74 ? 126  LYS B CE  1 
ATOM   10978 N  NZ  . LYS B 2 443  ? 142.051 148.024 168.157 1.00 105.36 ? 126  LYS B NZ  1 
ATOM   10979 N  N   . THR B 2 444  ? 138.221 144.923 167.005 1.00 97.95  ? 127  THR B N   1 
ATOM   10980 C  CA  . THR B 2 444  ? 137.302 143.918 167.532 1.00 93.85  ? 127  THR B CA  1 
ATOM   10981 C  C   . THR B 2 444  ? 135.938 144.012 166.861 1.00 90.07  ? 127  THR B C   1 
ATOM   10982 O  O   . THR B 2 444  ? 135.320 142.989 166.532 1.00 92.16  ? 127  THR B O   1 
ATOM   10983 C  CB  . THR B 2 444  ? 137.168 144.079 169.046 1.00 97.83  ? 127  THR B CB  1 
ATOM   10984 O  OG1 . THR B 2 444  ? 136.625 145.372 169.342 1.00 98.22  ? 127  THR B OG1 1 
ATOM   10985 C  CG2 . THR B 2 444  ? 138.540 143.931 169.723 1.00 98.57  ? 127  THR B CG2 1 
ATOM   10986 N  N   . ILE B 2 445  ? 135.462 145.232 166.620 1.00 87.59  ? 128  ILE B N   1 
ATOM   10987 C  CA  . ILE B 2 445  ? 134.180 145.359 165.949 1.00 80.83  ? 128  ILE B CA  1 
ATOM   10988 C  C   . ILE B 2 445  ? 134.298 145.006 164.469 1.00 88.03  ? 128  ILE B C   1 
ATOM   10989 O  O   . ILE B 2 445  ? 133.331 144.523 163.875 1.00 90.22  ? 128  ILE B O   1 
ATOM   10990 C  CB  . ILE B 2 445  ? 133.580 146.759 166.166 1.00 92.30  ? 128  ILE B CB  1 
ATOM   10991 C  CG1 . ILE B 2 445  ? 132.075 146.708 165.904 1.00 99.76  ? 128  ILE B CG1 1 
ATOM   10992 C  CG2 . ILE B 2 445  ? 134.237 147.796 165.262 1.00 97.01  ? 128  ILE B CG2 1 
ATOM   10993 C  CD1 . ILE B 2 445  ? 131.363 145.671 166.759 1.00 100.46 ? 128  ILE B CD1 1 
ATOM   10994 N  N   . SER B 2 446  ? 135.467 145.204 163.843 1.00 89.84  ? 129  SER B N   1 
ATOM   10995 C  CA  . SER B 2 446  ? 135.617 144.770 162.452 1.00 84.00  ? 129  SER B CA  1 
ATOM   10996 C  C   . SER B 2 446  ? 135.568 143.251 162.330 1.00 79.59  ? 129  SER B C   1 
ATOM   10997 O  O   . SER B 2 446  ? 134.918 142.716 161.421 1.00 83.58  ? 129  SER B O   1 
ATOM   10998 C  CB  . SER B 2 446  ? 136.919 145.297 161.854 1.00 90.03  ? 129  SER B CB  1 
ATOM   10999 O  OG  . SER B 2 446  ? 137.059 144.857 160.513 1.00 90.00  ? 129  SER B OG  1 
ATOM   11000 N  N   . SER B 2 447  ? 136.258 142.539 163.225 1.00 84.42  ? 130  SER B N   1 
ATOM   11001 C  CA  . SER B 2 447  ? 136.171 141.078 163.206 1.00 87.95  ? 130  SER B CA  1 
ATOM   11002 C  C   . SER B 2 447  ? 134.746 140.617 163.487 1.00 81.94  ? 130  SER B C   1 
ATOM   11003 O  O   . SER B 2 447  ? 134.247 139.673 162.849 1.00 82.10  ? 130  SER B O   1 
ATOM   11004 C  CB  . SER B 2 447  ? 137.128 140.454 164.227 1.00 95.52  ? 130  SER B CB  1 
ATOM   11005 O  OG  . SER B 2 447  ? 136.826 140.859 165.553 1.00 90.08  ? 130  SER B OG  1 
ATOM   11006 N  N   . LEU B 2 448  ? 134.082 141.260 164.453 1.00 76.35  ? 131  LEU B N   1 
ATOM   11007 C  CA  . LEU B 2 448  ? 132.698 140.917 164.737 1.00 73.77  ? 131  LEU B CA  1 
ATOM   11008 C  C   . LEU B 2 448  ? 131.823 141.157 163.520 1.00 64.86  ? 131  LEU B C   1 
ATOM   11009 O  O   . LEU B 2 448  ? 130.912 140.377 163.241 1.00 68.88  ? 131  LEU B O   1 
ATOM   11010 C  CB  . LEU B 2 448  ? 132.201 141.719 165.935 1.00 86.63  ? 131  LEU B CB  1 
ATOM   11011 C  CG  . LEU B 2 448  ? 130.818 141.386 166.493 1.00 94.01  ? 131  LEU B CG  1 
ATOM   11012 C  CD1 . LEU B 2 448  ? 130.826 141.587 167.998 1.00 95.64  ? 131  LEU B CD1 1 
ATOM   11013 C  CD2 . LEU B 2 448  ? 129.738 142.262 165.856 1.00 93.68  ? 131  LEU B CD2 1 
ATOM   11014 N  N   . ASN B 2 449  ? 132.096 142.220 162.774 1.00 68.01  ? 132  ASN B N   1 
ATOM   11015 C  CA  . ASN B 2 449  ? 131.317 142.501 161.580 1.00 68.44  ? 132  ASN B CA  1 
ATOM   11016 C  C   . ASN B 2 449  ? 131.531 141.430 160.522 1.00 66.24  ? 132  ASN B C   1 
ATOM   11017 O  O   . ASN B 2 449  ? 130.573 140.992 159.883 1.00 71.02  ? 132  ASN B O   1 
ATOM   11018 C  CB  . ASN B 2 449  ? 131.685 143.878 161.034 1.00 85.38  ? 132  ASN B CB  1 
ATOM   11019 C  CG  . ASN B 2 449  ? 130.968 144.204 159.736 1.00 90.54  ? 132  ASN B CG  1 
ATOM   11020 O  OD1 . ASN B 2 449  ? 129.854 143.730 159.487 1.00 84.74  ? 132  ASN B OD1 1 
ATOM   11021 N  ND2 . ASN B 2 449  ? 131.607 145.022 158.897 1.00 84.59  ? 132  ASN B ND2 1 
ATOM   11022 N  N   . ARG B 2 450  ? 132.775 140.984 160.331 1.00 68.02  ? 133  ARG B N   1 
ATOM   11023 C  CA  . ARG B 2 450  ? 133.044 139.946 159.334 1.00 59.87  ? 133  ARG B CA  1 
ATOM   11024 C  C   . ARG B 2 450  ? 132.345 138.638 159.678 1.00 59.36  ? 133  ARG B C   1 
ATOM   11025 O  O   . ARG B 2 450  ? 131.617 138.071 158.849 1.00 63.68  ? 133  ARG B O   1 
ATOM   11026 C  CB  . ARG B 2 450  ? 134.536 139.720 159.195 1.00 66.43  ? 133  ARG B CB  1 
ATOM   11027 C  CG  . ARG B 2 450  ? 135.234 140.923 158.608 1.00 87.38  ? 133  ARG B CG  1 
ATOM   11028 C  CD  . ARG B 2 450  ? 136.717 140.664 158.406 1.00 102.34 ? 133  ARG B CD  1 
ATOM   11029 N  NE  . ARG B 2 450  ? 136.937 139.520 157.512 1.00 120.98 ? 133  ARG B NE  1 
ATOM   11030 C  CZ  . ARG B 2 450  ? 137.003 139.584 156.178 1.00 121.87 ? 133  ARG B CZ  1 
ATOM   11031 N  NH1 . ARG B 2 450  ? 136.832 140.743 155.544 1.00 108.72 ? 133  ARG B NH1 1 
ATOM   11032 N  NH2 . ARG B 2 450  ? 137.214 138.476 155.469 1.00 106.83 ? 133  ARG B NH2 1 
ATOM   11033 N  N   . VAL B 2 451  ? 132.508 138.165 160.914 1.00 56.28  ? 134  VAL B N   1 
ATOM   11034 C  CA  . VAL B 2 451  ? 131.879 136.897 161.276 1.00 50.07  ? 134  VAL B CA  1 
ATOM   11035 C  C   . VAL B 2 451  ? 130.362 137.020 161.297 1.00 49.10  ? 134  VAL B C   1 
ATOM   11036 O  O   . VAL B 2 451  ? 129.655 136.124 160.830 1.00 62.39  ? 134  VAL B O   1 
ATOM   11037 C  CB  . VAL B 2 451  ? 132.387 136.380 162.627 1.00 68.24  ? 134  VAL B CB  1 
ATOM   11038 C  CG1 . VAL B 2 451  ? 132.029 137.347 163.740 1.00 73.59  ? 134  VAL B CG1 1 
ATOM   11039 C  CG2 . VAL B 2 451  ? 131.808 134.998 162.893 1.00 73.13  ? 134  VAL B CG2 1 
ATOM   11040 N  N   . CYS B 2 452  ? 129.831 138.111 161.843 1.00 55.03  ? 135  CYS B N   1 
ATOM   11041 C  CA  . CYS B 2 452  ? 128.388 138.270 161.928 1.00 55.82  ? 135  CYS B CA  1 
ATOM   11042 C  C   . CYS B 2 452  ? 127.760 138.428 160.556 1.00 46.89  ? 135  CYS B C   1 
ATOM   11043 O  O   . CYS B 2 452  ? 126.682 137.888 160.303 1.00 59.46  ? 135  CYS B O   1 
ATOM   11044 C  CB  . CYS B 2 452  ? 128.052 139.475 162.804 1.00 75.92  ? 135  CYS B CB  1 
ATOM   11045 S  SG  . CYS B 2 452  ? 126.289 139.793 163.034 1.00 120.83 ? 135  CYS B SG  1 
ATOM   11046 N  N   . ALA B 2 453  ? 128.390 139.179 159.667 1.00 42.43  ? 136  ALA B N   1 
ATOM   11047 C  CA  . ALA B 2 453  ? 127.837 139.298 158.334 1.00 49.63  ? 136  ALA B CA  1 
ATOM   11048 C  C   . ALA B 2 453  ? 127.849 137.954 157.634 1.00 52.65  ? 136  ALA B C   1 
ATOM   11049 O  O   . ALA B 2 453  ? 126.886 137.605 156.943 1.00 57.06  ? 136  ALA B O   1 
ATOM   11050 C  CB  . ALA B 2 453  ? 128.608 140.342 157.530 1.00 61.69  ? 136  ALA B CB  1 
ATOM   11051 N  N   . GLU B 2 454  ? 128.917 137.173 157.809 1.00 52.62  ? 137  GLU B N   1 
ATOM   11052 C  CA  . GLU B 2 454  ? 128.915 135.838 157.228 1.00 48.92  ? 137  GLU B CA  1 
ATOM   11053 C  C   . GLU B 2 454  ? 127.791 135.000 157.797 1.00 45.12  ? 137  GLU B C   1 
ATOM   11054 O  O   . GLU B 2 454  ? 127.130 134.254 157.065 1.00 57.23  ? 137  GLU B O   1 
ATOM   11055 C  CB  . GLU B 2 454  ? 130.244 135.147 157.475 1.00 59.07  ? 137  GLU B CB  1 
ATOM   11056 C  CG  . GLU B 2 454  ? 130.398 133.851 156.715 1.00 66.97  ? 137  GLU B CG  1 
ATOM   11057 C  CD  . GLU B 2 454  ? 131.669 133.118 157.103 1.00 75.68  ? 137  GLU B CD  1 
ATOM   11058 O  OE1 . GLU B 2 454  ? 132.137 133.324 158.248 1.00 71.91  ? 137  GLU B OE1 1 
ATOM   11059 O  OE2 . GLU B 2 454  ? 132.202 132.351 156.268 1.00 77.05  ? 137  GLU B OE2 1 
ATOM   11060 N  N   . MET B 2 455  ? 127.569 135.096 159.103 1.00 44.28  ? 138  MET B N   1 
ATOM   11061 C  CA  . MET B 2 455  ? 126.558 134.259 159.722 1.00 40.75  ? 138  MET B CA  1 
ATOM   11062 C  C   . MET B 2 455  ? 125.179 134.659 159.254 1.00 47.90  ? 138  MET B C   1 
ATOM   11063 O  O   . MET B 2 455  ? 124.326 133.796 159.011 1.00 61.33  ? 138  MET B O   1 
ATOM   11064 C  CB  . MET B 2 455  ? 126.638 134.350 161.230 1.00 51.11  ? 138  MET B CB  1 
ATOM   11065 C  CG  . MET B 2 455  ? 125.459 133.715 161.909 1.00 64.53  ? 138  MET B CG  1 
ATOM   11066 S  SD  . MET B 2 455  ? 124.188 134.921 162.279 1.00 112.52 ? 138  MET B SD  1 
ATOM   11067 C  CE  . MET B 2 455  ? 125.081 136.023 163.370 1.00 83.66  ? 138  MET B CE  1 
ATOM   11068 N  N   . VAL B 2 456  ? 124.941 135.965 159.110 1.00 51.13  ? 139  VAL B N   1 
ATOM   11069 C  CA  . VAL B 2 456  ? 123.647 136.440 158.617 1.00 53.80  ? 139  VAL B CA  1 
ATOM   11070 C  C   . VAL B 2 456  ? 123.429 136.008 157.177 1.00 57.67  ? 139  VAL B C   1 
ATOM   11071 O  O   . VAL B 2 456  ? 122.344 135.546 156.821 1.00 64.42  ? 139  VAL B O   1 
ATOM   11072 C  CB  . VAL B 2 456  ? 123.516 137.964 158.759 1.00 51.47  ? 139  VAL B CB  1 
ATOM   11073 C  CG1 . VAL B 2 456  ? 122.312 138.446 157.985 1.00 57.75  ? 139  VAL B CG1 1 
ATOM   11074 C  CG2 . VAL B 2 456  ? 123.337 138.314 160.197 1.00 60.91  ? 139  VAL B CG2 1 
ATOM   11075 N  N   . ALA B 2 457  ? 124.446 136.151 156.324 1.00 53.16  ? 140  ALA B N   1 
ATOM   11076 C  CA  . ALA B 2 457  ? 124.290 135.711 154.942 1.00 54.99  ? 140  ALA B CA  1 
ATOM   11077 C  C   . ALA B 2 457  ? 123.925 134.235 154.889 1.00 49.18  ? 140  ALA B C   1 
ATOM   11078 O  O   . ALA B 2 457  ? 122.926 133.848 154.263 1.00 56.37  ? 140  ALA B O   1 
ATOM   11079 C  CB  . ALA B 2 457  ? 125.571 135.981 154.147 1.00 57.92  ? 140  ALA B CB  1 
ATOM   11080 N  N   . LYS B 2 458  ? 124.713 133.397 155.558 1.00 47.98  ? 141  LYS B N   1 
ATOM   11081 C  CA  . LYS B 2 458  ? 124.457 131.969 155.486 1.00 53.07  ? 141  LYS B CA  1 
ATOM   11082 C  C   . LYS B 2 458  ? 123.075 131.644 156.033 1.00 48.27  ? 141  LYS B C   1 
ATOM   11083 O  O   . LYS B 2 458  ? 122.296 130.929 155.387 1.00 58.20  ? 141  LYS B O   1 
ATOM   11084 C  CB  . LYS B 2 458  ? 125.547 131.188 156.225 1.00 56.37  ? 141  LYS B CB  1 
ATOM   11085 C  CG  . LYS B 2 458  ? 126.888 131.110 155.474 1.00 52.48  ? 141  LYS B CG  1 
ATOM   11086 C  CD  . LYS B 2 458  ? 127.917 130.333 156.288 1.00 58.57  ? 141  LYS B CD  1 
ATOM   11087 C  CE  . LYS B 2 458  ? 129.118 129.918 155.458 1.00 59.69  ? 141  LYS B CE  1 
ATOM   11088 N  NZ  . LYS B 2 458  ? 129.752 131.099 154.799 1.00 67.11  ? 141  LYS B NZ  1 
ATOM   11089 N  N   . TYR B 2 459  ? 122.725 132.181 157.195 1.00 40.00  ? 142  TYR B N   1 
ATOM   11090 C  CA  . TYR B 2 459  ? 121.439 131.772 157.738 1.00 58.32  ? 142  TYR B CA  1 
ATOM   11091 C  C   . TYR B 2 459  ? 120.253 132.407 157.021 1.00 62.98  ? 142  TYR B C   1 
ATOM   11092 O  O   . TYR B 2 459  ? 119.145 131.843 157.049 1.00 61.09  ? 142  TYR B O   1 
ATOM   11093 C  CB  . TYR B 2 459  ? 121.392 132.027 159.243 1.00 63.76  ? 142  TYR B CB  1 
ATOM   11094 C  CG  . TYR B 2 459  ? 121.967 130.879 160.008 1.00 55.04  ? 142  TYR B CG  1 
ATOM   11095 C  CD1 . TYR B 2 459  ? 123.334 130.692 160.075 1.00 58.73  ? 142  TYR B CD1 1 
ATOM   11096 C  CD2 . TYR B 2 459  ? 121.138 129.965 160.645 1.00 50.94  ? 142  TYR B CD2 1 
ATOM   11097 C  CE1 . TYR B 2 459  ? 123.875 129.627 160.763 1.00 59.32  ? 142  TYR B CE1 1 
ATOM   11098 C  CE2 . TYR B 2 459  ? 121.662 128.898 161.336 1.00 57.64  ? 142  TYR B CE2 1 
ATOM   11099 C  CZ  . TYR B 2 459  ? 123.039 128.732 161.393 1.00 59.18  ? 142  TYR B CZ  1 
ATOM   11100 O  OH  . TYR B 2 459  ? 123.595 127.674 162.079 1.00 57.16  ? 142  TYR B OH  1 
ATOM   11101 N  N   . ASP B 2 460  ? 120.464 133.515 156.314 1.00 56.93  ? 143  ASP B N   1 
ATOM   11102 C  CA  . ASP B 2 460  ? 119.377 134.073 155.525 1.00 57.34  ? 143  ASP B CA  1 
ATOM   11103 C  C   . ASP B 2 460  ? 119.138 133.225 154.280 1.00 60.35  ? 143  ASP B C   1 
ATOM   11104 O  O   . ASP B 2 460  ? 117.985 133.021 153.871 1.00 66.08  ? 143  ASP B O   1 
ATOM   11105 C  CB  . ASP B 2 460  ? 119.685 135.527 155.158 1.00 66.86  ? 143  ASP B CB  1 
ATOM   11106 C  CG  . ASP B 2 460  ? 118.486 136.251 154.533 1.00 82.40  ? 143  ASP B CG  1 
ATOM   11107 O  OD1 . ASP B 2 460  ? 117.350 135.722 154.600 1.00 76.82  ? 143  ASP B OD1 1 
ATOM   11108 O  OD2 . ASP B 2 460  ? 118.686 137.352 153.964 1.00 79.11  ? 143  ASP B OD2 1 
ATOM   11109 N  N   . LEU B 2 461  ? 120.210 132.704 153.666 1.00 55.19  ? 144  LEU B N   1 
ATOM   11110 C  CA  . LEU B 2 461  ? 119.997 131.756 152.574 1.00 45.65  ? 144  LEU B CA  1 
ATOM   11111 C  C   . LEU B 2 461  ? 119.319 130.495 153.061 1.00 39.29  ? 144  LEU B C   1 
ATOM   11112 O  O   . LEU B 2 461  ? 118.463 129.940 152.368 1.00 48.98  ? 144  LEU B O   1 
ATOM   11113 C  CB  . LEU B 2 461  ? 121.295 131.434 151.856 1.00 39.09  ? 144  LEU B CB  1 
ATOM   11114 C  CG  . LEU B 2 461  ? 121.027 130.542 150.657 1.00 41.53  ? 144  LEU B CG  1 
ATOM   11115 C  CD1 . LEU B 2 461  ? 122.056 130.854 149.635 1.00 49.18  ? 144  LEU B CD1 1 
ATOM   11116 C  CD2 . LEU B 2 461  ? 121.266 129.072 151.047 1.00 50.53  ? 144  LEU B CD2 1 
ATOM   11117 N  N   . LEU B 2 462  ? 119.678 130.031 154.247 1.00 40.67  ? 145  LEU B N   1 
ATOM   11118 C  CA  . LEU B 2 462  ? 118.987 128.869 154.779 1.00 37.21  ? 145  LEU B CA  1 
ATOM   11119 C  C   . LEU B 2 462  ? 117.504 129.154 154.959 1.00 36.33  ? 145  LEU B C   1 
ATOM   11120 O  O   . LEU B 2 462  ? 116.669 128.286 154.696 1.00 47.44  ? 145  LEU B O   1 
ATOM   11121 C  CB  . LEU B 2 462  ? 119.639 128.431 156.086 1.00 41.84  ? 145  LEU B CB  1 
ATOM   11122 C  CG  . LEU B 2 462  ? 119.080 127.194 156.770 1.00 45.97  ? 145  LEU B CG  1 
ATOM   11123 C  CD1 . LEU B 2 462  ? 119.101 126.030 155.820 1.00 57.97  ? 145  LEU B CD1 1 
ATOM   11124 C  CD2 . LEU B 2 462  ? 119.954 126.883 157.949 1.00 49.86  ? 145  LEU B CD2 1 
ATOM   11125 N  N   . VAL B 2 463  ? 117.150 130.358 155.401 1.00 39.31  ? 146  VAL B N   1 
ATOM   11126 C  CA  . VAL B 2 463  ? 115.732 130.686 155.539 1.00 37.40  ? 146  VAL B CA  1 
ATOM   11127 C  C   . VAL B 2 463  ? 115.048 130.707 154.189 1.00 42.91  ? 146  VAL B C   1 
ATOM   11128 O  O   . VAL B 2 463  ? 113.922 130.224 154.038 1.00 48.29  ? 146  VAL B O   1 
ATOM   11129 C  CB  . VAL B 2 463  ? 115.554 132.047 156.217 1.00 57.81  ? 146  VAL B CB  1 
ATOM   11130 C  CG1 . VAL B 2 463  ? 114.086 132.440 156.164 1.00 63.11  ? 146  VAL B CG1 1 
ATOM   11131 C  CG2 . VAL B 2 463  ? 116.093 132.033 157.616 1.00 62.42  ? 146  VAL B CG2 1 
ATOM   11132 N  N   . MET B 2 464  ? 115.692 131.325 153.200 1.00 49.68  ? 147  MET B N   1 
ATOM   11133 C  CA  . MET B 2 464  ? 115.105 131.432 151.868 1.00 44.74  ? 147  MET B CA  1 
ATOM   11134 C  C   . MET B 2 464  ? 114.875 130.059 151.237 1.00 53.11  ? 147  MET B C   1 
ATOM   11135 O  O   . MET B 2 464  ? 113.851 129.841 150.576 1.00 55.23  ? 147  MET B O   1 
ATOM   11136 C  CB  . MET B 2 464  ? 116.013 132.266 150.974 1.00 48.11  ? 147  MET B CB  1 
ATOM   11137 C  CG  . MET B 2 464  ? 115.423 132.553 149.605 1.00 59.83  ? 147  MET B CG  1 
ATOM   11138 S  SD  . MET B 2 464  ? 116.431 133.720 148.666 1.00 91.37  ? 147  MET B SD  1 
ATOM   11139 C  CE  . MET B 2 464  ? 116.330 135.200 149.695 1.00 91.16  ? 147  MET B CE  1 
ATOM   11140 N  N   . THR B 2 465  ? 115.826 129.126 151.406 1.00 44.32  ? 148  THR B N   1 
ATOM   11141 C  CA  . THR B 2 465  ? 115.684 127.803 150.799 1.00 32.94  ? 148  THR B CA  1 
ATOM   11142 C  C   . THR B 2 465  ? 114.565 127.014 151.459 1.00 39.60  ? 148  THR B C   1 
ATOM   11143 O  O   . THR B 2 465  ? 113.649 126.535 150.781 1.00 49.18  ? 148  THR B O   1 
ATOM   11144 C  CB  . THR B 2 465  ? 116.977 127.002 150.896 1.00 38.66  ? 148  THR B CB  1 
ATOM   11145 O  OG1 . THR B 2 465  ? 117.415 126.952 152.256 1.00 52.00  ? 148  THR B OG1 1 
ATOM   11146 C  CG2 . THR B 2 465  ? 118.064 127.610 150.031 1.00 42.56  ? 148  THR B CG2 1 
ATOM   11147 N  N   . THR B 2 466  ? 114.634 126.839 152.777 1.00 33.72  ? 149  THR B N   1 
ATOM   11148 C  CA  . THR B 2 466  ? 113.604 126.097 153.494 1.00 32.20  ? 149  THR B CA  1 
ATOM   11149 C  C   . THR B 2 466  ? 112.441 127.046 153.716 1.00 38.37  ? 149  THR B C   1 
ATOM   11150 O  O   . THR B 2 466  ? 112.535 127.959 154.540 1.00 47.19  ? 149  THR B O   1 
ATOM   11151 C  CB  . THR B 2 466  ? 114.118 125.601 154.837 1.00 46.85  ? 149  THR B CB  1 
ATOM   11152 O  OG1 . THR B 2 466  ? 114.339 126.726 155.698 1.00 50.25  ? 149  THR B OG1 1 
ATOM   11153 C  CG2 . THR B 2 466  ? 115.452 124.870 154.669 1.00 55.37  ? 149  THR B CG2 1 
ATOM   11154 N  N   . GLY B 2 467  ? 111.345 126.845 153.000 1.00 45.77  ? 150  GLY B N   1 
ATOM   11155 C  CA  . GLY B 2 467  ? 110.263 127.807 153.027 1.00 44.78  ? 150  GLY B CA  1 
ATOM   11156 C  C   . GLY B 2 467  ? 109.556 127.895 154.357 1.00 42.54  ? 150  GLY B C   1 
ATOM   11157 O  O   . GLY B 2 467  ? 110.080 127.468 155.386 1.00 46.83  ? 150  GLY B O   1 
ATOM   11158 N  N   . ARG B 2 468  ? 108.350 128.441 154.347 1.00 47.94  ? 151  ARG B N   1 
ATOM   11159 C  CA  . ARG B 2 468  ? 107.648 128.673 155.596 1.00 48.95  ? 151  ARG B CA  1 
ATOM   11160 C  C   . ARG B 2 468  ? 107.209 127.391 156.274 1.00 49.55  ? 151  ARG B C   1 
ATOM   11161 O  O   . ARG B 2 468  ? 106.782 127.439 157.432 1.00 62.32  ? 151  ARG B O   1 
ATOM   11162 C  CB  . ARG B 2 468  ? 106.446 129.582 155.354 1.00 59.31  ? 151  ARG B CB  1 
ATOM   11163 C  CG  . ARG B 2 468  ? 105.957 130.319 156.593 1.00 63.12  ? 151  ARG B CG  1 
ATOM   11164 C  CD  . ARG B 2 468  ? 104.925 131.364 156.223 1.00 69.24  ? 151  ARG B CD  1 
ATOM   11165 N  NE  . ARG B 2 468  ? 105.433 132.257 155.183 1.00 82.97  ? 151  ARG B NE  1 
ATOM   11166 C  CZ  . ARG B 2 468  ? 106.172 133.339 155.429 1.00 92.00  ? 151  ARG B CZ  1 
ATOM   11167 N  NH1 . ARG B 2 468  ? 106.489 133.659 156.678 1.00 93.98  ? 151  ARG B NH1 1 
ATOM   11168 N  NH2 . ARG B 2 468  ? 106.601 134.107 154.432 1.00 89.14  ? 151  ARG B NH2 1 
ATOM   11169 N  N   . ALA B 2 469  ? 107.302 126.249 155.608 1.00 42.08  ? 152  ALA B N   1 
ATOM   11170 C  CA  . ALA B 2 469  ? 106.823 125.013 156.200 1.00 43.72  ? 152  ALA B CA  1 
ATOM   11171 C  C   . ALA B 2 469  ? 107.962 124.118 156.669 1.00 42.48  ? 152  ALA B C   1 
ATOM   11172 O  O   . ALA B 2 469  ? 107.826 122.890 156.646 1.00 52.86  ? 152  ALA B O   1 
ATOM   11173 C  CB  . ALA B 2 469  ? 105.917 124.275 155.210 1.00 54.89  ? 152  ALA B CB  1 
ATOM   11174 N  N   . THR B 2 470  ? 109.083 124.697 157.095 1.00 39.95  ? 153  THR B N   1 
ATOM   11175 C  CA  . THR B 2 470  ? 110.176 123.889 157.636 1.00 36.68  ? 153  THR B CA  1 
ATOM   11176 C  C   . THR B 2 470  ? 109.752 123.185 158.903 1.00 40.21  ? 153  THR B C   1 
ATOM   11177 O  O   . THR B 2 470  ? 109.195 123.806 159.807 1.00 57.72  ? 153  THR B O   1 
ATOM   11178 C  CB  . THR B 2 470  ? 111.386 124.738 157.972 1.00 43.69  ? 153  THR B CB  1 
ATOM   11179 O  OG1 . THR B 2 470  ? 111.827 125.445 156.807 1.00 53.44  ? 153  THR B OG1 1 
ATOM   11180 C  CG2 . THR B 2 470  ? 112.484 123.861 158.546 1.00 43.16  ? 153  THR B CG2 1 
ATOM   11181 N  N   . ALA B 2 471  ? 110.047 121.905 158.995 1.00 42.97  ? 154  ALA B N   1 
ATOM   11182 C  CA  . ALA B 2 471  ? 109.706 121.146 160.185 1.00 54.95  ? 154  ALA B CA  1 
ATOM   11183 C  C   . ALA B 2 471  ? 110.829 121.301 161.202 1.00 58.12  ? 154  ALA B C   1 
ATOM   11184 O  O   . ALA B 2 471  ? 112.013 121.233 160.846 1.00 60.24  ? 154  ALA B O   1 
ATOM   11185 C  CB  . ALA B 2 471  ? 109.474 119.670 159.843 1.00 59.76  ? 154  ALA B CB  1 
ATOM   11186 N  N   . THR B 2 472  ? 110.454 121.524 162.459 1.00 51.18  ? 155  THR B N   1 
ATOM   11187 C  CA  . THR B 2 472  ? 111.434 121.665 163.521 1.00 51.92  ? 155  THR B CA  1 
ATOM   11188 C  C   . THR B 2 472  ? 112.029 120.309 163.865 1.00 52.28  ? 155  THR B C   1 
ATOM   11189 O  O   . THR B 2 472  ? 111.499 119.261 163.493 1.00 61.89  ? 155  THR B O   1 
ATOM   11190 C  CB  . THR B 2 472  ? 110.783 122.241 164.769 1.00 63.22  ? 155  THR B CB  1 
ATOM   11191 O  OG1 . THR B 2 472  ? 110.002 121.217 165.395 1.00 58.84  ? 155  THR B OG1 1 
ATOM   11192 C  CG2 . THR B 2 472  ? 109.865 123.409 164.392 1.00 69.19  ? 155  THR B CG2 1 
ATOM   11193 N  N   . ALA B 2 473  ? 113.127 120.328 164.618 1.00 46.13  ? 156  ALA B N   1 
ATOM   11194 C  CA  . ALA B 2 473  ? 113.706 119.067 165.059 1.00 44.68  ? 156  ALA B CA  1 
ATOM   11195 C  C   . ALA B 2 473  ? 112.660 118.217 165.771 1.00 47.23  ? 156  ALA B C   1 
ATOM   11196 O  O   . ALA B 2 473  ? 112.464 117.037 165.440 1.00 56.59  ? 156  ALA B O   1 
ATOM   11197 C  CB  . ALA B 2 473  ? 114.906 119.330 165.964 1.00 49.94  ? 156  ALA B CB  1 
ATOM   11198 N  N   . ALA B 2 474  ? 111.954 118.808 166.731 1.00 46.77  ? 157  ALA B N   1 
ATOM   11199 C  CA  . ALA B 2 474  ? 110.938 118.054 167.451 1.00 52.58  ? 157  ALA B CA  1 
ATOM   11200 C  C   . ALA B 2 474  ? 109.843 117.607 166.509 1.00 45.89  ? 157  ALA B C   1 
ATOM   11201 O  O   . ALA B 2 474  ? 109.391 116.457 166.561 1.00 53.66  ? 157  ALA B O   1 
ATOM   11202 C  CB  . ALA B 2 474  ? 110.346 118.898 168.582 1.00 61.91  ? 157  ALA B CB  1 
ATOM   11203 N  N   . ALA B 2 475  ? 109.400 118.501 165.640 1.00 45.94  ? 158  ALA B N   1 
ATOM   11204 C  CA  . ALA B 2 475  ? 108.324 118.123 164.739 1.00 54.97  ? 158  ALA B CA  1 
ATOM   11205 C  C   . ALA B 2 475  ? 108.773 117.002 163.805 1.00 54.87  ? 158  ALA B C   1 
ATOM   11206 O  O   . ALA B 2 475  ? 108.011 116.062 163.539 1.00 59.19  ? 158  ALA B O   1 
ATOM   11207 C  CB  . ALA B 2 475  ? 107.839 119.343 163.950 1.00 63.39  ? 158  ALA B CB  1 
ATOM   11208 N  N   . THR B 2 476  ? 109.999 117.097 163.273 1.00 49.59  ? 159  THR B N   1 
ATOM   11209 C  CA  . THR B 2 476  ? 110.510 116.032 162.409 1.00 39.27  ? 159  THR B CA  1 
ATOM   11210 C  C   . THR B 2 476  ? 110.461 114.698 163.090 1.00 46.45  ? 159  THR B C   1 
ATOM   11211 O  O   . THR B 2 476  ? 109.989 113.709 162.513 1.00 59.59  ? 159  THR B O   1 
ATOM   11212 C  CB  . THR B 2 476  ? 111.947 116.313 161.969 1.00 49.77  ? 159  THR B CB  1 
ATOM   11213 O  OG1 . THR B 2 476  ? 111.972 117.550 161.241 1.00 55.67  ? 159  THR B OG1 1 
ATOM   11214 C  CG2 . THR B 2 476  ? 112.569 115.141 161.174 1.00 56.92  ? 159  THR B CG2 1 
ATOM   11215 N  N   . GLU B 2 477  ? 110.970 114.630 164.308 1.00 48.63  ? 160  GLU B N   1 
ATOM   11216 C  CA  . GLU B 2 477  ? 111.076 113.286 164.838 1.00 51.66  ? 160  GLU B CA  1 
ATOM   11217 C  C   . GLU B 2 477  ? 109.697 112.787 165.356 1.00 51.35  ? 160  GLU B C   1 
ATOM   11218 O  O   . GLU B 2 477  ? 109.389 111.589 165.281 1.00 57.79  ? 160  GLU B O   1 
ATOM   11219 C  CB  . GLU B 2 477  ? 112.226 113.232 165.857 1.00 57.44  ? 160  GLU B CB  1 
ATOM   11220 C  CG  . GLU B 2 477  ? 112.461 111.816 166.194 1.00 86.04  ? 160  GLU B CG  1 
ATOM   11221 C  CD  . GLU B 2 477  ? 113.604 111.518 167.143 1.00 99.03  ? 160  GLU B CD  1 
ATOM   11222 O  OE1 . GLU B 2 477  ? 114.364 112.342 167.615 1.00 96.82  ? 160  GLU B OE1 1 
ATOM   11223 O  OE2 . GLU B 2 477  ? 113.795 110.303 167.358 1.00 98.30  ? 160  GLU B OE2 1 
ATOM   11224 N  N   . ALA B 2 478  ? 108.810 113.671 165.783 1.00 47.39  ? 161  ALA B N   1 
ATOM   11225 C  CA  . ALA B 2 478  ? 107.443 113.243 165.987 1.00 50.75  ? 161  ALA B CA  1 
ATOM   11226 C  C   . ALA B 2 478  ? 106.896 112.601 164.712 1.00 46.34  ? 161  ALA B C   1 
ATOM   11227 O  O   . ALA B 2 478  ? 106.392 111.469 164.729 1.00 55.34  ? 161  ALA B O   1 
ATOM   11228 C  CB  . ALA B 2 478  ? 106.626 114.458 166.426 1.00 57.63  ? 161  ALA B CB  1 
ATOM   11229 N  N   . TYR B 2 479  ? 107.034 113.298 163.585 1.00 48.70  ? 162  TYR B N   1 
ATOM   11230 C  CA  . TYR B 2 479  ? 106.473 112.782 162.341 1.00 62.81  ? 162  TYR B CA  1 
ATOM   11231 C  C   . TYR B 2 479  ? 107.124 111.471 161.934 1.00 54.00  ? 162  TYR B C   1 
ATOM   11232 O  O   . TYR B 2 479  ? 106.453 110.594 161.390 1.00 63.97  ? 162  TYR B O   1 
ATOM   11233 C  CB  . TYR B 2 479  ? 106.589 113.811 161.200 1.00 75.62  ? 162  TYR B CB  1 
ATOM   11234 C  CG  . TYR B 2 479  ? 105.545 113.590 160.083 1.00 76.38  ? 162  TYR B CG  1 
ATOM   11235 C  CD1 . TYR B 2 479  ? 105.779 112.690 159.035 1.00 63.80  ? 162  TYR B CD1 1 
ATOM   11236 C  CD2 . TYR B 2 479  ? 104.304 114.237 160.119 1.00 77.42  ? 162  TYR B CD2 1 
ATOM   11237 C  CE1 . TYR B 2 479  ? 104.829 112.477 158.048 1.00 66.02  ? 162  TYR B CE1 1 
ATOM   11238 C  CE2 . TYR B 2 479  ? 103.346 114.018 159.138 1.00 72.82  ? 162  TYR B CE2 1 
ATOM   11239 C  CZ  . TYR B 2 479  ? 103.615 113.140 158.106 1.00 76.93  ? 162  TYR B CZ  1 
ATOM   11240 O  OH  . TYR B 2 479  ? 102.665 112.929 157.124 1.00 81.69  ? 162  TYR B OH  1 
ATOM   11241 N  N   . TRP B 2 480  ? 108.412 111.314 162.176 1.00 44.97  ? 163  TRP B N   1 
ATOM   11242 C  CA  . TRP B 2 480  ? 109.009 110.007 162.005 1.00 43.37  ? 163  TRP B CA  1 
ATOM   11243 C  C   . TRP B 2 480  ? 108.283 108.970 162.836 1.00 45.36  ? 163  TRP B C   1 
ATOM   11244 O  O   . TRP B 2 480  ? 108.034 107.846 162.390 1.00 51.09  ? 163  TRP B O   1 
ATOM   11245 C  CB  . TRP B 2 480  ? 110.458 110.065 162.427 1.00 55.11  ? 163  TRP B CB  1 
ATOM   11246 C  CG  . TRP B 2 480  ? 111.215 110.757 161.491 1.00 43.76  ? 163  TRP B CG  1 
ATOM   11247 C  CD1 . TRP B 2 480  ? 110.754 111.346 160.378 1.00 48.37  ? 163  TRP B CD1 1 
ATOM   11248 C  CD2 . TRP B 2 480  ? 112.607 110.992 161.546 1.00 49.54  ? 163  TRP B CD2 1 
ATOM   11249 N  NE1 . TRP B 2 480  ? 111.790 111.929 159.698 1.00 59.43  ? 163  TRP B NE1 1 
ATOM   11250 C  CE2 . TRP B 2 480  ? 112.945 111.723 160.403 1.00 55.87  ? 163  TRP B CE2 1 
ATOM   11251 C  CE3 . TRP B 2 480  ? 113.612 110.642 162.446 1.00 67.98  ? 163  TRP B CE3 1 
ATOM   11252 C  CZ2 . TRP B 2 480  ? 114.253 112.118 160.125 1.00 62.96  ? 163  TRP B CZ2 1 
ATOM   11253 C  CZ3 . TRP B 2 480  ? 114.917 111.035 162.172 1.00 75.45  ? 163  TRP B CZ3 1 
ATOM   11254 C  CH2 . TRP B 2 480  ? 115.224 111.767 161.019 1.00 66.48  ? 163  TRP B CH2 1 
ATOM   11255 N  N   . ALA B 2 481  ? 107.970 109.331 164.069 1.00 50.25  ? 164  ALA B N   1 
ATOM   11256 C  CA  . ALA B 2 481  ? 107.434 108.358 165.000 1.00 58.39  ? 164  ALA B CA  1 
ATOM   11257 C  C   . ALA B 2 481  ? 106.049 107.903 164.567 1.00 56.70  ? 164  ALA B C   1 
ATOM   11258 O  O   . ALA B 2 481  ? 105.813 106.711 164.362 1.00 61.61  ? 164  ALA B O   1 
ATOM   11259 C  CB  . ALA B 2 481  ? 107.407 108.954 166.413 1.00 63.64  ? 164  ALA B CB  1 
ATOM   11260 N  N   . GLU B 2 482  ? 105.127 108.835 164.409 1.00 55.34  ? 165  GLU B N   1 
ATOM   11261 C  CA  . GLU B 2 482  ? 103.735 108.469 164.227 1.00 52.45  ? 165  GLU B CA  1 
ATOM   11262 C  C   . GLU B 2 482  ? 103.386 108.193 162.779 1.00 52.03  ? 165  GLU B C   1 
ATOM   11263 O  O   . GLU B 2 482  ? 102.251 107.821 162.486 1.00 58.69  ? 165  GLU B O   1 
ATOM   11264 C  CB  . GLU B 2 482  ? 102.846 109.571 164.804 1.00 69.18  ? 165  GLU B CB  1 
ATOM   11265 C  CG  . GLU B 2 482  ? 103.046 110.966 164.183 1.00 82.22  ? 165  GLU B CG  1 
ATOM   11266 C  CD  . GLU B 2 482  ? 102.018 111.327 163.111 1.00 91.32  ? 165  GLU B CD  1 
ATOM   11267 O  OE1 . GLU B 2 482  ? 101.000 110.611 162.994 1.00 86.39  ? 165  GLU B OE1 1 
ATOM   11268 O  OE2 . GLU B 2 482  ? 102.221 112.338 162.394 1.00 88.79  ? 165  GLU B OE2 1 
ATOM   11269 N  N   . HIS B 2 483  ? 104.321 108.388 161.871 1.00 55.91  ? 166  HIS B N   1 
ATOM   11270 C  CA  . HIS B 2 483  ? 104.112 108.073 160.474 1.00 56.24  ? 166  HIS B CA  1 
ATOM   11271 C  C   . HIS B 2 483  ? 105.431 107.582 159.913 1.00 54.69  ? 166  HIS B C   1 
ATOM   11272 O  O   . HIS B 2 483  ? 106.500 108.008 160.350 1.00 58.54  ? 166  HIS B O   1 
ATOM   11273 C  CB  . HIS B 2 483  ? 103.661 109.287 159.674 1.00 68.89  ? 166  HIS B CB  1 
ATOM   11274 C  CG  . HIS B 2 483  ? 102.184 109.503 159.682 1.00 80.43  ? 166  HIS B CG  1 
ATOM   11275 N  ND1 . HIS B 2 483  ? 101.594 110.592 160.289 1.00 78.92  ? 166  HIS B ND1 1 
ATOM   11276 C  CD2 . HIS B 2 483  ? 101.172 108.745 159.198 1.00 88.73  ? 166  HIS B CD2 1 
ATOM   11277 C  CE1 . HIS B 2 483  ? 100.283 110.515 160.144 1.00 85.83  ? 166  HIS B CE1 1 
ATOM   11278 N  NE2 . HIS B 2 483  ? 100.000 109.400 159.491 1.00 93.35  ? 166  HIS B NE2 1 
ATOM   11279 N  N   . GLY B 2 484  ? 105.361 106.708 158.924 1.00 54.57  ? 167  GLY B N   1 
ATOM   11280 C  CA  . GLY B 2 484  ? 106.594 106.207 158.356 1.00 60.40  ? 167  GLY B CA  1 
ATOM   11281 C  C   . GLY B 2 484  ? 107.452 107.304 157.752 1.00 54.48  ? 167  GLY B C   1 
ATOM   11282 O  O   . GLY B 2 484  ? 108.648 107.378 158.021 1.00 57.53  ? 167  GLY B O   1 
ATOM   11283 N  N   . GLN B 2 485  ? 106.844 108.201 156.992 1.00 49.04  ? 168  GLN B N   1 
ATOM   11284 C  CA  . GLN B 2 485  ? 107.550 109.059 156.048 1.00 54.58  ? 168  GLN B CA  1 
ATOM   11285 C  C   . GLN B 2 485  ? 108.095 110.309 156.735 1.00 50.27  ? 168  GLN B C   1 
ATOM   11286 O  O   . GLN B 2 485  ? 107.788 110.577 157.895 1.00 59.41  ? 168  GLN B O   1 
ATOM   11287 C  CB  . GLN B 2 485  ? 106.602 109.419 154.896 1.00 72.80  ? 168  GLN B CB  1 
ATOM   11288 C  CG  . GLN B 2 485  ? 106.128 108.237 153.997 1.00 77.27  ? 168  GLN B CG  1 
ATOM   11289 C  CD  . GLN B 2 485  ? 107.266 107.373 153.433 1.00 74.34  ? 168  GLN B CD  1 
ATOM   11290 O  OE1 . GLN B 2 485  ? 108.259 107.892 152.914 1.00 64.91  ? 168  GLN B OE1 1 
ATOM   11291 N  NE2 . GLN B 2 485  ? 107.109 106.048 153.520 1.00 73.56  ? 168  GLN B NE2 1 
ATOM   11292 N  N   . PRO B 2 486  ? 108.922 111.099 156.043 1.00 39.12  ? 169  PRO B N   1 
ATOM   11293 C  CA  . PRO B 2 486  ? 109.349 112.395 156.568 1.00 41.02  ? 169  PRO B CA  1 
ATOM   11294 C  C   . PRO B 2 486  ? 108.189 113.371 156.640 1.00 55.81  ? 169  PRO B C   1 
ATOM   11295 O  O   . PRO B 2 486  ? 107.191 113.209 155.925 1.00 64.10  ? 169  PRO B O   1 
ATOM   11296 C  CB  . PRO B 2 486  ? 110.360 112.872 155.526 1.00 36.68  ? 169  PRO B CB  1 
ATOM   11297 C  CG  . PRO B 2 486  ? 110.001 112.177 154.348 1.00 35.69  ? 169  PRO B CG  1 
ATOM   11298 C  CD  . PRO B 2 486  ? 109.568 110.840 154.760 1.00 44.41  ? 169  PRO B CD  1 
ATOM   11299 N  N   . PRO B 2 487  ? 108.289 114.409 157.465 1.00 44.37  ? 170  PRO B N   1 
ATOM   11300 C  CA  . PRO B 2 487  ? 107.212 115.398 157.573 1.00 38.31  ? 170  PRO B CA  1 
ATOM   11301 C  C   . PRO B 2 487  ? 107.148 116.261 156.332 1.00 41.75  ? 170  PRO B C   1 
ATOM   11302 O  O   . PRO B 2 487  ? 108.154 116.411 155.626 1.00 49.38  ? 170  PRO B O   1 
ATOM   11303 C  CB  . PRO B 2 487  ? 107.625 116.238 158.780 1.00 53.46  ? 170  PRO B CB  1 
ATOM   11304 C  CG  . PRO B 2 487  ? 109.110 116.107 158.803 1.00 62.95  ? 170  PRO B CG  1 
ATOM   11305 C  CD  . PRO B 2 487  ? 109.407 114.709 158.365 1.00 52.49  ? 170  PRO B CD  1 
ATOM   11306 N  N   . PRO B 2 488  ? 106.007 116.859 156.049 1.00 40.89  ? 171  PRO B N   1 
ATOM   11307 C  CA  . PRO B 2 488  ? 105.786 117.538 154.769 1.00 32.07  ? 171  PRO B CA  1 
ATOM   11308 C  C   . PRO B 2 488  ? 106.427 118.910 154.769 1.00 31.22  ? 171  PRO B C   1 
ATOM   11309 O  O   . PRO B 2 488  ? 105.802 119.945 154.891 1.00 45.45  ? 171  PRO B O   1 
ATOM   11310 C  CB  . PRO B 2 488  ? 104.263 117.641 154.693 1.00 50.21  ? 171  PRO B CB  1 
ATOM   11311 C  CG  . PRO B 2 488  ? 103.826 117.690 156.111 1.00 59.50  ? 171  PRO B CG  1 
ATOM   11312 C  CD  . PRO B 2 488  ? 104.793 116.818 156.868 1.00 60.62  ? 171  PRO B CD  1 
ATOM   11313 N  N   . GLY B 2 489  ? 107.727 118.919 154.633 1.00 32.84  ? 172  GLY B N   1 
ATOM   11314 C  CA  . GLY B 2 489  ? 108.432 120.163 154.605 1.00 31.01  ? 172  GLY B CA  1 
ATOM   11315 C  C   . GLY B 2 489  ? 109.852 119.903 154.983 1.00 29.43  ? 172  GLY B C   1 
ATOM   11316 O  O   . GLY B 2 489  ? 110.168 118.945 155.695 1.00 37.70  ? 172  GLY B O   1 
ATOM   11317 N  N   . PRO B 2 490  ? 110.739 120.758 154.514 1.00 29.56  ? 173  PRO B N   1 
ATOM   11318 C  CA  . PRO B 2 490  ? 112.160 120.527 154.740 1.00 31.61  ? 173  PRO B CA  1 
ATOM   11319 C  C   . PRO B 2 490  ? 112.400 120.407 156.231 1.00 47.30  ? 173  PRO B C   1 
ATOM   11320 O  O   . PRO B 2 490  ? 111.749 121.075 157.036 1.00 55.01  ? 173  PRO B O   1 
ATOM   11321 C  CB  . PRO B 2 490  ? 112.824 121.783 154.174 1.00 34.64  ? 173  PRO B CB  1 
ATOM   11322 C  CG  . PRO B 2 490  ? 111.837 122.350 153.252 1.00 42.57  ? 173  PRO B CG  1 
ATOM   11323 C  CD  . PRO B 2 490  ? 110.485 122.035 153.843 1.00 37.38  ? 173  PRO B CD  1 
ATOM   11324 N  N   . SER B 2 491  ? 113.309 119.523 156.598 1.00 45.91  ? 174  SER B N   1 
ATOM   11325 C  CA  . SER B 2 491  ? 113.753 119.405 157.975 1.00 45.02  ? 174  SER B CA  1 
ATOM   11326 C  C   . SER B 2 491  ? 115.258 119.566 157.990 1.00 43.80  ? 174  SER B C   1 
ATOM   11327 O  O   . SER B 2 491  ? 115.931 119.182 157.031 1.00 51.16  ? 174  SER B O   1 
ATOM   11328 C  CB  . SER B 2 491  ? 113.360 118.072 158.571 1.00 54.46  ? 174  SER B CB  1 
ATOM   11329 O  OG  . SER B 2 491  ? 113.729 118.034 159.939 1.00 58.45  ? 174  SER B OG  1 
ATOM   11330 N  N   . LEU B 2 492  ? 115.790 120.146 159.051 1.00 39.85  ? 175  LEU B N   1 
ATOM   11331 C  CA  . LEU B 2 492  ? 117.223 120.391 159.138 1.00 49.30  ? 175  LEU B CA  1 
ATOM   11332 C  C   . LEU B 2 492  ? 117.853 119.415 160.135 1.00 60.93  ? 175  LEU B C   1 
ATOM   11333 O  O   . LEU B 2 492  ? 117.327 119.235 161.240 1.00 61.41  ? 175  LEU B O   1 
ATOM   11334 C  CB  . LEU B 2 492  ? 117.478 121.836 159.558 1.00 54.13  ? 175  LEU B CB  1 
ATOM   11335 C  CG  . LEU B 2 492  ? 117.318 122.942 158.515 1.00 62.78  ? 175  LEU B CG  1 
ATOM   11336 C  CD1 . LEU B 2 492  ? 117.385 124.313 159.188 1.00 69.38  ? 175  LEU B CD1 1 
ATOM   11337 C  CD2 . LEU B 2 492  ? 118.406 122.816 157.469 1.00 57.43  ? 175  LEU B CD2 1 
ATOM   11338 N  N   . TYR B 2 493  ? 118.969 118.778 159.751 1.00 42.30  ? 176  TYR B N   1 
ATOM   11339 C  CA  . TYR B 2 493  ? 119.701 117.902 160.650 1.00 26.15  ? 176  TYR B CA  1 
ATOM   11340 C  C   . TYR B 2 493  ? 121.157 118.258 160.667 1.00 32.58  ? 176  TYR B C   1 
ATOM   11341 O  O   . TYR B 2 493  ? 121.693 118.735 159.672 1.00 48.02  ? 176  TYR B O   1 
ATOM   11342 C  CB  . TYR B 2 493  ? 119.639 116.501 160.254 1.00 35.18  ? 176  TYR B CB  1 
ATOM   11343 C  CG  . TYR B 2 493  ? 118.317 116.051 159.732 1.00 50.46  ? 176  TYR B CG  1 
ATOM   11344 C  CD1 . TYR B 2 493  ? 117.277 115.791 160.612 1.00 59.37  ? 176  TYR B CD1 1 
ATOM   11345 C  CD2 . TYR B 2 493  ? 118.122 115.783 158.385 1.00 52.65  ? 176  TYR B CD2 1 
ATOM   11346 C  CE1 . TYR B 2 493  ? 116.058 115.338 160.171 1.00 59.75  ? 176  TYR B CE1 1 
ATOM   11347 C  CE2 . TYR B 2 493  ? 116.903 115.319 157.924 1.00 54.46  ? 176  TYR B CE2 1 
ATOM   11348 C  CZ  . TYR B 2 493  ? 115.870 115.100 158.823 1.00 63.42  ? 176  TYR B CZ  1 
ATOM   11349 O  OH  . TYR B 2 493  ? 114.640 114.648 158.376 1.00 69.01  ? 176  TYR B OH  1 
ATOM   11350 N  N   . GLU B 2 494  ? 121.815 117.999 161.785 1.00 35.27  ? 177  GLU B N   1 
ATOM   11351 C  CA  . GLU B 2 494  ? 123.264 118.008 161.718 1.00 41.96  ? 177  GLU B CA  1 
ATOM   11352 C  C   . GLU B 2 494  ? 123.741 116.750 161.012 1.00 51.04  ? 177  GLU B C   1 
ATOM   11353 O  O   . GLU B 2 494  ? 123.059 115.722 160.989 1.00 53.55  ? 177  GLU B O   1 
ATOM   11354 C  CB  . GLU B 2 494  ? 123.911 118.114 163.096 1.00 47.83  ? 177  GLU B CB  1 
ATOM   11355 C  CG  . GLU B 2 494  ? 123.624 119.428 163.800 1.00 61.44  ? 177  GLU B CG  1 
ATOM   11356 C  CD  . GLU B 2 494  ? 124.653 119.776 164.876 1.00 74.23  ? 177  GLU B CD  1 
ATOM   11357 O  OE1 . GLU B 2 494  ? 125.841 119.407 164.715 1.00 75.52  ? 177  GLU B OE1 1 
ATOM   11358 O  OE2 . GLU B 2 494  ? 124.274 120.422 165.881 1.00 68.06  ? 177  GLU B OE2 1 
ATOM   11359 N  N   . GLU B 2 495  ? 124.910 116.855 160.392 1.00 51.28  ? 178  GLU B N   1 
ATOM   11360 C  CA  . GLU B 2 495  ? 125.476 115.700 159.726 1.00 41.40  ? 178  GLU B CA  1 
ATOM   11361 C  C   . GLU B 2 495  ? 125.537 114.539 160.682 1.00 41.04  ? 178  GLU B C   1 
ATOM   11362 O  O   . GLU B 2 495  ? 125.007 113.467 160.405 1.00 55.39  ? 178  GLU B O   1 
ATOM   11363 C  CB  . GLU B 2 495  ? 126.869 116.040 159.222 1.00 57.55  ? 178  GLU B CB  1 
ATOM   11364 C  CG  . GLU B 2 495  ? 127.564 114.900 158.561 1.00 66.07  ? 178  GLU B CG  1 
ATOM   11365 C  CD  . GLU B 2 495  ? 127.020 114.667 157.176 1.00 74.50  ? 178  GLU B CD  1 
ATOM   11366 O  OE1 . GLU B 2 495  ? 126.540 115.646 156.567 1.00 69.11  ? 178  GLU B OE1 1 
ATOM   11367 O  OE2 . GLU B 2 495  ? 127.093 113.521 156.682 1.00 77.88  ? 178  GLU B OE2 1 
ATOM   11368 N  N   . SER B 2 496  ? 126.129 114.760 161.848 1.00 46.65  ? 179  SER B N   1 
ATOM   11369 C  CA  . SER B 2 496  ? 126.297 113.680 162.800 1.00 48.69  ? 179  SER B CA  1 
ATOM   11370 C  C   . SER B 2 496  ? 124.990 113.280 163.438 1.00 38.32  ? 179  SER B C   1 
ATOM   11371 O  O   . SER B 2 496  ? 124.855 112.141 163.883 1.00 49.10  ? 179  SER B O   1 
ATOM   11372 C  CB  . SER B 2 496  ? 127.287 114.085 163.890 1.00 55.70  ? 179  SER B CB  1 
ATOM   11373 O  OG  . SER B 2 496  ? 126.864 115.273 164.541 1.00 56.53  ? 179  SER B OG  1 
ATOM   11374 N  N   . ALA B 2 497  ? 124.040 114.192 163.531 1.00 40.97  ? 180  ALA B N   1 
ATOM   11375 C  CA  . ALA B 2 497  ? 122.795 113.836 164.183 1.00 49.51  ? 180  ALA B CA  1 
ATOM   11376 C  C   . ALA B 2 497  ? 122.132 112.694 163.447 1.00 48.99  ? 180  ALA B C   1 
ATOM   11377 O  O   . ALA B 2 497  ? 121.707 111.710 164.056 1.00 60.45  ? 180  ALA B O   1 
ATOM   11378 C  CB  . ALA B 2 497  ? 121.864 115.046 164.253 1.00 63.01  ? 180  ALA B CB  1 
ATOM   11379 N  N   . ILE B 2 498  ? 122.071 112.787 162.126 1.00 49.95  ? 181  ILE B N   1 
ATOM   11380 C  CA  . ILE B 2 498  ? 121.467 111.723 161.346 1.00 52.32  ? 181  ILE B CA  1 
ATOM   11381 C  C   . ILE B 2 498  ? 122.466 110.670 160.911 1.00 52.49  ? 181  ILE B C   1 
ATOM   11382 O  O   . ILE B 2 498  ? 122.056 109.567 160.538 1.00 65.81  ? 181  ILE B O   1 
ATOM   11383 C  CB  . ILE B 2 498  ? 120.729 112.293 160.125 1.00 66.54  ? 181  ILE B CB  1 
ATOM   11384 C  CG1 . ILE B 2 498  ? 121.671 113.186 159.286 1.00 69.78  ? 181  ILE B CG1 1 
ATOM   11385 C  CG2 . ILE B 2 498  ? 119.414 112.945 160.557 1.00 65.51  ? 181  ILE B CG2 1 
ATOM   11386 C  CD1 . ILE B 2 498  ? 121.067 113.680 157.958 1.00 69.59  ? 181  ILE B CD1 1 
ATOM   11387 N  N   . ARG B 2 499  ? 123.756 110.970 160.933 1.00 53.52  ? 182  ARG B N   1 
ATOM   11388 C  CA  . ARG B 2 499  ? 124.727 109.895 160.900 1.00 50.52  ? 182  ARG B CA  1 
ATOM   11389 C  C   . ARG B 2 499  ? 124.370 108.885 161.971 1.00 59.35  ? 182  ARG B C   1 
ATOM   11390 O  O   . ARG B 2 499  ? 124.213 107.691 161.699 1.00 70.38  ? 182  ARG B O   1 
ATOM   11391 C  CB  . ARG B 2 499  ? 126.119 110.462 161.149 1.00 66.79  ? 182  ARG B CB  1 
ATOM   11392 C  CG  . ARG B 2 499  ? 127.222 109.447 161.040 1.00 78.31  ? 182  ARG B CG  1 
ATOM   11393 C  CD  . ARG B 2 499  ? 127.364 108.896 159.648 1.00 78.17  ? 182  ARG B CD  1 
ATOM   11394 N  NE  . ARG B 2 499  ? 127.468 109.979 158.682 1.00 83.72  ? 182  ARG B NE  1 
ATOM   11395 C  CZ  . ARG B 2 499  ? 128.594 110.656 158.454 1.00 92.23  ? 182  ARG B CZ  1 
ATOM   11396 N  NH1 . ARG B 2 499  ? 129.698 110.376 159.145 1.00 85.71  ? 182  ARG B NH1 1 
ATOM   11397 N  NH2 . ARG B 2 499  ? 128.618 111.629 157.548 1.00 89.58  ? 182  ARG B NH2 1 
ATOM   11398 N  N   . GLY B 2 500  ? 124.184 109.367 163.192 1.00 61.59  ? 183  GLY B N   1 
ATOM   11399 C  CA  . GLY B 2 500  ? 123.583 108.555 164.215 1.00 58.15  ? 183  GLY B CA  1 
ATOM   11400 C  C   . GLY B 2 500  ? 122.137 108.279 163.891 1.00 52.85  ? 183  GLY B C   1 
ATOM   11401 O  O   . GLY B 2 500  ? 121.535 108.896 163.026 1.00 59.35  ? 183  GLY B O   1 
ATOM   11402 N  N   . LYS B 2 501  ? 121.600 107.278 164.550 1.00 55.34  ? 184  LYS B N   1 
ATOM   11403 C  CA  . LYS B 2 501  ? 120.254 106.795 164.300 1.00 63.73  ? 184  LYS B CA  1 
ATOM   11404 C  C   . LYS B 2 501  ? 120.048 106.420 162.845 1.00 67.06  ? 184  LYS B C   1 
ATOM   11405 O  O   . LYS B 2 501  ? 118.933 106.056 162.449 1.00 75.31  ? 184  LYS B O   1 
ATOM   11406 C  CB  . LYS B 2 501  ? 119.187 107.796 164.759 1.00 70.39  ? 184  LYS B CB  1 
ATOM   11407 C  CG  . LYS B 2 501  ? 118.704 108.789 163.729 1.00 69.37  ? 184  LYS B CG  1 
ATOM   11408 C  CD  . LYS B 2 501  ? 117.566 109.594 164.318 1.00 76.06  ? 184  LYS B CD  1 
ATOM   11409 C  CE  . LYS B 2 501  ? 117.991 110.297 165.593 1.00 77.41  ? 184  LYS B CE  1 
ATOM   11410 N  NZ  . LYS B 2 501  ? 119.215 111.119 165.394 1.00 78.19  ? 184  LYS B NZ  1 
ATOM   11411 N  N   . ILE B 2 502  ? 121.102 106.468 162.039 1.00 66.71  ? 185  ILE B N   1 
ATOM   11412 C  CA  . ILE B 2 502  ? 121.170 105.716 160.799 1.00 77.00  ? 185  ILE B CA  1 
ATOM   11413 C  C   . ILE B 2 502  ? 122.201 104.598 160.882 1.00 75.06  ? 185  ILE B C   1 
ATOM   11414 O  O   . ILE B 2 502  ? 121.931 103.470 160.466 1.00 84.50  ? 185  ILE B O   1 
ATOM   11415 C  CB  . ILE B 2 502  ? 121.421 106.622 159.569 1.00 83.77  ? 185  ILE B CB  1 
ATOM   11416 C  CG1 . ILE B 2 502  ? 120.163 107.458 159.268 1.00 88.92  ? 185  ILE B CG1 1 
ATOM   11417 C  CG2 . ILE B 2 502  ? 121.859 105.814 158.353 1.00 84.32  ? 185  ILE B CG2 1 
ATOM   11418 C  CD1 . ILE B 2 502  ? 120.351 108.508 158.157 1.00 84.82  ? 185  ILE B CD1 1 
ATOM   11419 N  N   . GLU B 2 503  ? 123.354 104.867 161.472 1.00 62.78  ? 186  GLU B N   1 
ATOM   11420 C  CA  . GLU B 2 503  ? 124.277 103.799 161.789 1.00 68.23  ? 186  GLU B CA  1 
ATOM   11421 C  C   . GLU B 2 503  ? 123.750 102.895 162.904 1.00 72.45  ? 186  GLU B C   1 
ATOM   11422 O  O   . GLU B 2 503  ? 124.192 101.745 163.018 1.00 81.30  ? 186  GLU B O   1 
ATOM   11423 C  CB  . GLU B 2 503  ? 125.589 104.456 162.159 1.00 75.83  ? 186  GLU B CB  1 
ATOM   11424 C  CG  . GLU B 2 503  ? 125.549 105.031 163.569 1.00 88.84  ? 186  GLU B CG  1 
ATOM   11425 C  CD  . GLU B 2 503  ? 126.604 106.110 163.800 1.00 91.35  ? 186  GLU B CD  1 
ATOM   11426 O  OE1 . GLU B 2 503  ? 127.391 106.380 162.858 1.00 87.79  ? 186  GLU B OE1 1 
ATOM   11427 O  OE2 . GLU B 2 503  ? 126.647 106.686 164.911 1.00 81.89  ? 186  GLU B OE2 1 
ATOM   11428 N  N   . SER B 2 504  ? 122.823 103.377 163.732 1.00 64.26  ? 187  SER B N   1 
ATOM   11429 C  CA  . SER B 2 504  ? 122.252 102.558 164.793 1.00 71.78  ? 187  SER B CA  1 
ATOM   11430 C  C   . SER B 2 504  ? 120.888 102.034 164.364 1.00 79.87  ? 187  SER B C   1 
ATOM   11431 O  O   . SER B 2 504  ? 120.060 102.789 163.849 1.00 79.96  ? 187  SER B O   1 
ATOM   11432 C  CB  . SER B 2 504  ? 122.098 103.341 166.093 1.00 75.68  ? 187  SER B CB  1 
ATOM   11433 O  OG  . SER B 2 504  ? 120.922 104.129 166.061 1.00 78.61  ? 187  SER B OG  1 
ATOM   11434 N  N   . ARG B 2 505  ? 120.655 100.743 164.593 1.00 88.53  ? 188  ARG B N   1 
ATOM   11435 C  CA  . ARG B 2 505  ? 119.410 100.109 164.171 1.00 91.24  ? 188  ARG B CA  1 
ATOM   11436 C  C   . ARG B 2 505  ? 118.250 100.753 164.913 1.00 100.17 ? 188  ARG B C   1 
ATOM   11437 O  O   . ARG B 2 505  ? 118.063 100.527 166.114 1.00 101.38 ? 188  ARG B O   1 
ATOM   11438 C  CB  . ARG B 2 505  ? 119.449 98.598  164.418 1.00 101.63 ? 188  ARG B CB  1 
ATOM   11439 C  CG  . ARG B 2 505  ? 120.674 97.852  163.856 1.00 107.34 ? 188  ARG B CG  1 
ATOM   11440 C  CD  . ARG B 2 505  ? 120.578 97.606  162.334 1.00 113.18 ? 188  ARG B CD  1 
ATOM   11441 N  NE  . ARG B 2 505  ? 120.784 98.829  161.551 1.00 112.10 ? 188  ARG B NE  1 
ATOM   11442 C  CZ  . ARG B 2 505  ? 121.959 99.243  161.075 1.00 104.17 ? 188  ARG B CZ  1 
ATOM   11443 N  NH1 . ARG B 2 505  ? 123.064 98.540  161.303 1.00 103.08 ? 188  ARG B NH1 1 
ATOM   11444 N  NH2 . ARG B 2 505  ? 122.032 100.375 160.380 1.00 90.11  ? 188  ARG B NH2 1 
ATOM   11445 N  N   . ASP B 2 506  ? 117.465 101.558 164.196 1.00 108.58 ? 189  ASP B N   1 
ATOM   11446 C  CA  . ASP B 2 506  ? 116.352 102.262 164.813 1.00 116.20 ? 189  ASP B CA  1 
ATOM   11447 C  C   . ASP B 2 506  ? 115.285 102.544 163.757 1.00 103.78 ? 189  ASP B C   1 
ATOM   11448 O  O   . ASP B 2 506  ? 115.586 102.761 162.579 1.00 93.44  ? 189  ASP B O   1 
ATOM   11449 C  CB  . ASP B 2 506  ? 116.845 103.553 165.499 1.00 114.57 ? 189  ASP B CB  1 
ATOM   11450 C  CG  . ASP B 2 506  ? 115.772 104.218 166.361 1.00 118.07 ? 189  ASP B CG  1 
ATOM   11451 O  OD1 . ASP B 2 506  ? 115.217 103.541 167.259 1.00 111.40 ? 189  ASP B OD1 1 
ATOM   11452 O  OD2 . ASP B 2 506  ? 115.500 105.423 166.153 1.00 116.44 ? 189  ASP B OD2 1 
ATOM   11453 N  N   . GLU B 2 507  ? 114.033 102.543 164.205 1.00 107.85 ? 190  GLU B N   1 
ATOM   11454 C  CA  . GLU B 2 507  ? 112.870 102.626 163.333 1.00 108.92 ? 190  GLU B CA  1 
ATOM   11455 C  C   . GLU B 2 507  ? 112.410 104.055 163.080 1.00 99.20  ? 190  GLU B C   1 
ATOM   11456 O  O   . GLU B 2 507  ? 111.433 104.251 162.348 1.00 95.29  ? 190  GLU B O   1 
ATOM   11457 C  CB  . GLU B 2 507  ? 111.702 101.814 163.927 1.00 116.78 ? 190  GLU B CB  1 
ATOM   11458 C  CG  . GLU B 2 507  ? 112.028 100.348 164.294 1.00 124.07 ? 190  GLU B CG  1 
ATOM   11459 C  CD  . GLU B 2 507  ? 112.609 100.163 165.705 1.00 124.75 ? 190  GLU B CD  1 
ATOM   11460 O  OE1 . GLU B 2 507  ? 112.852 101.174 166.407 1.00 120.14 ? 190  GLU B OE1 1 
ATOM   11461 O  OE2 . GLU B 2 507  ? 112.831 98.996  166.104 1.00 116.41 ? 190  GLU B OE2 1 
ATOM   11462 N  N   . THR B 2 508  ? 113.070 105.055 163.666 1.00 98.88  ? 191  THR B N   1 
ATOM   11463 C  CA  . THR B 2 508  ? 112.599 106.427 163.492 1.00 98.50  ? 191  THR B CA  1 
ATOM   11464 C  C   . THR B 2 508  ? 112.855 106.928 162.070 1.00 82.81  ? 191  THR B C   1 
ATOM   11465 O  O   . THR B 2 508  ? 111.959 107.504 161.442 1.00 75.93  ? 191  THR B O   1 
ATOM   11466 C  CB  . THR B 2 508  ? 113.226 107.369 164.539 1.00 101.29 ? 191  THR B CB  1 
ATOM   11467 O  OG1 . THR B 2 508  ? 114.647 107.172 164.611 1.00 98.19  ? 191  THR B OG1 1 
ATOM   11468 C  CG2 . THR B 2 508  ? 112.586 107.169 165.933 1.00 101.64 ? 191  THR B CG2 1 
ATOM   11469 N  N   . VAL B 2 509  ? 114.058 106.726 161.540 1.00 74.70  ? 192  VAL B N   1 
ATOM   11470 C  CA  . VAL B 2 509  ? 114.308 107.264 160.196 1.00 60.57  ? 192  VAL B CA  1 
ATOM   11471 C  C   . VAL B 2 509  ? 113.423 106.540 159.190 1.00 64.34  ? 192  VAL B C   1 
ATOM   11472 O  O   . VAL B 2 509  ? 113.349 105.300 159.205 1.00 73.03  ? 192  VAL B O   1 
ATOM   11473 C  CB  . VAL B 2 509  ? 115.785 107.160 159.822 1.00 56.48  ? 192  VAL B CB  1 
ATOM   11474 C  CG1 . VAL B 2 509  ? 116.610 108.085 160.680 1.00 61.35  ? 192  VAL B CG1 1 
ATOM   11475 C  CG2 . VAL B 2 509  ? 116.269 105.747 160.028 1.00 69.90  ? 192  VAL B CG2 1 
ATOM   11476 N  N   . PRO B 2 510  ? 112.685 107.271 158.361 1.00 61.65  ? 193  PRO B N   1 
ATOM   11477 C  CA  . PRO B 2 510  ? 111.965 106.649 157.244 1.00 54.57  ? 193  PRO B CA  1 
ATOM   11478 C  C   . PRO B 2 510  ? 112.949 106.064 156.253 1.00 53.56  ? 193  PRO B C   1 
ATOM   11479 O  O   . PRO B 2 510  ? 114.108 106.473 156.170 1.00 62.66  ? 193  PRO B O   1 
ATOM   11480 C  CB  . PRO B 2 510  ? 111.204 107.817 156.606 1.00 67.00  ? 193  PRO B CB  1 
ATOM   11481 C  CG  . PRO B 2 510  ? 111.221 108.934 157.641 1.00 68.97  ? 193  PRO B CG  1 
ATOM   11482 C  CD  . PRO B 2 510  ? 112.479 108.727 158.436 1.00 69.74  ? 193  PRO B CD  1 
ATOM   11483 N  N   . GLN B 2 511  ? 112.471 105.110 155.471 1.00 50.58  ? 194  GLN B N   1 
ATOM   11484 C  CA  . GLN B 2 511  ? 113.351 104.528 154.475 1.00 54.09  ? 194  GLN B CA  1 
ATOM   11485 C  C   . GLN B 2 511  ? 113.826 105.589 153.491 1.00 51.38  ? 194  GLN B C   1 
ATOM   11486 O  O   . GLN B 2 511  ? 114.989 105.582 153.077 1.00 59.78  ? 194  GLN B O   1 
ATOM   11487 C  CB  . GLN B 2 511  ? 112.638 103.372 153.771 1.00 65.60  ? 194  GLN B CB  1 
ATOM   11488 C  CG  . GLN B 2 511  ? 113.549 102.206 153.397 1.00 70.42  ? 194  GLN B CG  1 
ATOM   11489 C  CD  . GLN B 2 511  ? 114.604 102.576 152.358 1.00 77.11  ? 194  GLN B CD  1 
ATOM   11490 O  OE1 . GLN B 2 511  ? 114.313 103.264 151.375 1.00 73.59  ? 194  GLN B OE1 1 
ATOM   11491 N  NE2 . GLN B 2 511  ? 115.843 102.143 152.589 1.00 74.55  ? 194  GLN B NE2 1 
ATOM   11492 N  N   . SER B 2 512  ? 112.957 106.530 153.130 1.00 49.72  ? 195  SER B N   1 
ATOM   11493 C  CA  . SER B 2 512  ? 113.357 107.545 152.163 1.00 50.19  ? 195  SER B CA  1 
ATOM   11494 C  C   . SER B 2 512  ? 114.471 108.418 152.712 1.00 47.61  ? 195  SER B C   1 
ATOM   11495 O  O   . SER B 2 512  ? 115.387 108.787 151.975 1.00 52.56  ? 195  SER B O   1 
ATOM   11496 C  CB  . SER B 2 512  ? 112.163 108.411 151.764 1.00 59.11  ? 195  SER B CB  1 
ATOM   11497 O  OG  . SER B 2 512  ? 111.621 109.082 152.889 1.00 55.72  ? 195  SER B OG  1 
ATOM   11498 N  N   . VAL B 2 513  ? 114.400 108.773 153.995 1.00 46.69  ? 196  VAL B N   1 
ATOM   11499 C  CA  . VAL B 2 513  ? 115.441 109.599 154.595 1.00 41.38  ? 196  VAL B CA  1 
ATOM   11500 C  C   . VAL B 2 513  ? 116.763 108.850 154.666 1.00 52.61  ? 196  VAL B C   1 
ATOM   11501 O  O   . VAL B 2 513  ? 117.823 109.424 154.388 1.00 62.23  ? 196  VAL B O   1 
ATOM   11502 C  CB  . VAL B 2 513  ? 114.993 110.102 155.972 1.00 51.36  ? 196  VAL B CB  1 
ATOM   11503 C  CG1 . VAL B 2 513  ? 116.131 110.811 156.673 1.00 59.81  ? 196  VAL B CG1 1 
ATOM   11504 C  CG2 . VAL B 2 513  ? 113.827 111.071 155.788 1.00 60.42  ? 196  VAL B CG2 1 
ATOM   11505 N  N   . ARG B 2 514  ? 116.735 107.563 155.027 1.00 57.35  ? 197  ARG B N   1 
ATOM   11506 C  CA  . ARG B 2 514  ? 117.965 106.767 155.026 1.00 55.51  ? 197  ARG B CA  1 
ATOM   11507 C  C   . ARG B 2 514  ? 118.554 106.664 153.629 1.00 42.10  ? 197  ARG B C   1 
ATOM   11508 O  O   . ARG B 2 514  ? 119.764 106.815 153.447 1.00 54.66  ? 197  ARG B O   1 
ATOM   11509 C  CB  . ARG B 2 514  ? 117.697 105.364 155.575 1.00 72.96  ? 197  ARG B CB  1 
ATOM   11510 C  CG  . ARG B 2 514  ? 118.804 104.320 155.287 1.00 79.62  ? 197  ARG B CG  1 
ATOM   11511 C  CD  . ARG B 2 514  ? 118.374 102.890 155.674 1.00 72.05  ? 197  ARG B CD  1 
ATOM   11512 N  NE  . ARG B 2 514  ? 118.347 102.696 157.122 1.00 77.98  ? 197  ARG B NE  1 
ATOM   11513 C  CZ  . ARG B 2 514  ? 117.244 102.771 157.864 1.00 87.10  ? 197  ARG B CZ  1 
ATOM   11514 N  NH1 . ARG B 2 514  ? 116.073 103.048 157.294 1.00 77.29  ? 197  ARG B NH1 1 
ATOM   11515 N  NH2 . ARG B 2 514  ? 117.306 102.584 159.179 1.00 88.98  ? 197  ARG B NH2 1 
ATOM   11516 N  N   . GLU B 2 515  ? 117.716 106.415 152.633 1.00 42.26  ? 198  GLU B N   1 
ATOM   11517 C  CA  . GLU B 2 515  ? 118.210 106.333 151.268 1.00 50.38  ? 198  GLU B CA  1 
ATOM   11518 C  C   . GLU B 2 515  ? 118.794 107.668 150.810 1.00 56.25  ? 198  GLU B C   1 
ATOM   11519 O  O   . GLU B 2 515  ? 119.858 107.705 150.175 1.00 59.84  ? 198  GLU B O   1 
ATOM   11520 C  CB  . GLU B 2 515  ? 117.082 105.903 150.332 1.00 62.51  ? 198  GLU B CB  1 
ATOM   11521 C  CG  . GLU B 2 515  ? 117.550 105.515 148.930 1.00 71.46  ? 198  GLU B CG  1 
ATOM   11522 C  CD  . GLU B 2 515  ? 118.281 104.173 148.913 1.00 85.92  ? 198  GLU B CD  1 
ATOM   11523 O  OE1 . GLU B 2 515  ? 118.088 103.376 149.861 1.00 81.17  ? 198  GLU B OE1 1 
ATOM   11524 O  OE2 . GLU B 2 515  ? 119.063 103.924 147.967 1.00 84.39  ? 198  GLU B OE2 1 
ATOM   11525 N  N   . ALA B 2 516  ? 118.108 108.776 151.121 1.00 49.13  ? 199  ALA B N   1 
ATOM   11526 C  CA  . ALA B 2 516  ? 118.594 110.100 150.748 1.00 43.44  ? 199  ALA B CA  1 
ATOM   11527 C  C   . ALA B 2 516  ? 119.953 110.355 151.357 1.00 40.71  ? 199  ALA B C   1 
ATOM   11528 O  O   . ALA B 2 516  ? 120.900 110.759 150.669 1.00 50.31  ? 199  ALA B O   1 
ATOM   11529 C  CB  . ALA B 2 516  ? 117.615 111.181 151.209 1.00 44.48  ? 199  ALA B CB  1 
ATOM   11530 N  N   . PHE B 2 517  ? 120.067 110.116 152.649 1.00 35.25  ? 200  PHE B N   1 
ATOM   11531 C  CA  . PHE B 2 517  ? 121.322 110.398 153.302 1.00 39.63  ? 200  PHE B CA  1 
ATOM   11532 C  C   . PHE B 2 517  ? 122.433 109.507 152.782 1.00 45.87  ? 200  PHE B C   1 
ATOM   11533 O  O   . PHE B 2 517  ? 123.565 109.972 152.615 1.00 56.82  ? 200  PHE B O   1 
ATOM   11534 C  CB  . PHE B 2 517  ? 121.168 110.267 154.805 1.00 58.89  ? 200  PHE B CB  1 
ATOM   11535 C  CG  . PHE B 2 517  ? 122.407 110.591 155.537 1.00 64.20  ? 200  PHE B CG  1 
ATOM   11536 C  CD1 . PHE B 2 517  ? 122.901 111.888 155.534 1.00 69.07  ? 200  PHE B CD1 1 
ATOM   11537 C  CD2 . PHE B 2 517  ? 123.081 109.606 156.245 1.00 73.64  ? 200  PHE B CD2 1 
ATOM   11538 C  CE1 . PHE B 2 517  ? 124.068 112.204 156.215 1.00 79.68  ? 200  PHE B CE1 1 
ATOM   11539 C  CE2 . PHE B 2 517  ? 124.247 109.905 156.943 1.00 85.64  ? 200  PHE B CE2 1 
ATOM   11540 C  CZ  . PHE B 2 517  ? 124.744 111.207 156.929 1.00 85.60  ? 200  PHE B CZ  1 
ATOM   11541 N  N   . ASN B 2 518  ? 122.152 108.227 152.535 1.00 45.42  ? 201  ASN B N   1 
ATOM   11542 C  CA  . ASN B 2 518  ? 123.192 107.366 151.980 1.00 44.61  ? 201  ASN B CA  1 
ATOM   11543 C  C   . ASN B 2 518  ? 123.651 107.865 150.624 1.00 47.89  ? 201  ASN B C   1 
ATOM   11544 O  O   . ASN B 2 518  ? 124.848 107.852 150.331 1.00 51.81  ? 201  ASN B O   1 
ATOM   11545 C  CB  . ASN B 2 518  ? 122.725 105.915 151.878 1.00 47.58  ? 201  ASN B CB  1 
ATOM   11546 C  CG  . ASN B 2 518  ? 122.784 105.193 153.208 1.00 64.05  ? 201  ASN B CG  1 
ATOM   11547 O  OD1 . ASN B 2 518  ? 123.833 104.656 153.577 1.00 65.74  ? 201  ASN B OD1 1 
ATOM   11548 N  ND2 . ASN B 2 518  ? 121.670 105.174 153.937 1.00 70.07  ? 201  ASN B ND2 1 
ATOM   11549 N  N   . ASN B 2 519  ? 122.724 108.301 149.777 1.00 45.09  ? 202  ASN B N   1 
ATOM   11550 C  CA  . ASN B 2 519  ? 123.145 108.822 148.486 1.00 41.91  ? 202  ASN B CA  1 
ATOM   11551 C  C   . ASN B 2 519  ? 124.064 110.021 148.675 1.00 45.01  ? 202  ASN B C   1 
ATOM   11552 O  O   . ASN B 2 519  ? 125.138 110.100 148.068 1.00 47.57  ? 202  ASN B O   1 
ATOM   11553 C  CB  . ASN B 2 519  ? 121.917 109.200 147.664 1.00 44.62  ? 202  ASN B CB  1 
ATOM   11554 C  CG  . ASN B 2 519  ? 121.131 107.997 147.232 1.00 50.39  ? 202  ASN B CG  1 
ATOM   11555 O  OD1 . ASN B 2 519  ? 119.916 107.935 147.411 1.00 50.29  ? 202  ASN B OD1 1 
ATOM   11556 N  ND2 . ASN B 2 519  ? 121.829 107.001 146.704 1.00 57.32  ? 202  ASN B ND2 1 
ATOM   11557 N  N   . LEU B 2 520  ? 123.668 110.945 149.554 1.00 49.64  ? 203  LEU B N   1 
ATOM   11558 C  CA  . LEU B 2 520  ? 124.424 112.176 149.758 1.00 36.16  ? 203  LEU B CA  1 
ATOM   11559 C  C   . LEU B 2 520  ? 125.811 111.897 150.298 1.00 46.57  ? 203  LEU B C   1 
ATOM   11560 O  O   . LEU B 2 520  ? 126.775 112.570 149.926 1.00 54.68  ? 203  LEU B O   1 
ATOM   11561 C  CB  . LEU B 2 520  ? 123.677 113.074 150.725 1.00 41.81  ? 203  LEU B CB  1 
ATOM   11562 C  CG  . LEU B 2 520  ? 124.425 114.354 151.025 1.00 54.78  ? 203  LEU B CG  1 
ATOM   11563 C  CD1 . LEU B 2 520  ? 124.624 115.109 149.719 1.00 54.42  ? 203  LEU B CD1 1 
ATOM   11564 C  CD2 . LEU B 2 520  ? 123.667 115.192 152.065 1.00 59.49  ? 203  LEU B CD2 1 
ATOM   11565 N  N   . ASN B 2 521  ? 125.930 110.930 151.204 1.00 49.28  ? 204  ASN B N   1 
ATOM   11566 C  CA  . ASN B 2 521  ? 127.223 110.570 151.766 1.00 40.62  ? 204  ASN B CA  1 
ATOM   11567 C  C   . ASN B 2 521  ? 127.998 109.604 150.898 1.00 38.73  ? 204  ASN B C   1 
ATOM   11568 O  O   . ASN B 2 521  ? 129.179 109.370 151.160 1.00 48.64  ? 204  ASN B O   1 
ATOM   11569 C  CB  . ASN B 2 521  ? 127.051 109.939 153.135 1.00 56.45  ? 204  ASN B CB  1 
ATOM   11570 C  CG  . ASN B 2 521  ? 128.316 109.993 153.954 1.00 71.23  ? 204  ASN B CG  1 
ATOM   11571 O  OD1 . ASN B 2 521  ? 129.201 110.815 153.697 1.00 64.86  ? 204  ASN B OD1 1 
ATOM   11572 N  ND2 . ASN B 2 521  ? 128.421 109.107 154.944 1.00 76.68  ? 204  ASN B ND2 1 
ATOM   11573 N  N   . SER B 2 522  ? 127.366 109.013 149.899 1.00 38.72  ? 205  SER B N   1 
ATOM   11574 C  CA  . SER B 2 522  ? 128.118 108.181 148.986 1.00 37.75  ? 205  SER B CA  1 
ATOM   11575 C  C   . SER B 2 522  ? 129.141 108.992 148.229 1.00 49.77  ? 205  SER B C   1 
ATOM   11576 O  O   . SER B 2 522  ? 130.217 108.478 147.906 1.00 56.25  ? 205  SER B O   1 
ATOM   11577 C  CB  . SER B 2 522  ? 127.191 107.492 147.998 1.00 51.20  ? 205  SER B CB  1 
ATOM   11578 O  OG  . SER B 2 522  ? 127.960 106.803 147.027 1.00 54.18  ? 205  SER B OG  1 
ATOM   11579 N  N   . THR B 2 523  ? 128.830 110.255 147.926 1.00 45.13  ? 206  THR B N   1 
ATOM   11580 C  CA  . THR B 2 523  ? 129.777 111.070 147.179 1.00 45.33  ? 206  THR B CA  1 
ATOM   11581 C  C   . THR B 2 523  ? 130.951 111.562 148.025 1.00 52.10  ? 206  THR B C   1 
ATOM   11582 O  O   . THR B 2 523  ? 131.936 112.043 147.450 1.00 56.32  ? 206  THR B O   1 
ATOM   11583 C  CB  . THR B 2 523  ? 129.092 112.287 146.569 1.00 54.44  ? 206  THR B CB  1 
ATOM   11584 O  OG1 . THR B 2 523  ? 129.968 112.880 145.595 1.00 53.53  ? 206  THR B OG1 1 
ATOM   11585 C  CG2 . THR B 2 523  ? 128.816 113.328 147.673 1.00 53.77  ? 206  THR B CG2 1 
ATOM   11586 N  N   . THR B 2 524  ? 130.880 111.475 149.361 1.00 46.65  ? 207  THR B N   1 
ATOM   11587 C  CA  . THR B 2 524  ? 132.017 111.893 150.179 1.00 38.75  ? 207  THR B CA  1 
ATOM   11588 C  C   . THR B 2 524  ? 133.236 111.001 149.945 1.00 42.09  ? 207  THR B C   1 
ATOM   11589 O  O   . THR B 2 524  ? 134.372 111.487 149.932 1.00 49.93  ? 207  THR B O   1 
ATOM   11590 C  CB  . THR B 2 524  ? 131.623 111.923 151.655 1.00 42.08  ? 207  THR B CB  1 
ATOM   11591 O  OG1 . THR B 2 524  ? 130.528 112.834 151.831 1.00 44.94  ? 207  THR B OG1 1 
ATOM   11592 C  CG2 . THR B 2 524  ? 132.784 112.396 152.513 1.00 51.35  ? 207  THR B CG2 1 
ATOM   11593 N  N   . SER B 2 525  ? 133.024 109.702 149.724 1.00 41.50  ? 208  SER B N   1 
ATOM   11594 C  CA  . SER B 2 525  ? 134.138 108.779 149.510 1.00 39.65  ? 208  SER B CA  1 
ATOM   11595 C  C   . SER B 2 525  ? 134.893 109.028 148.208 1.00 36.73  ? 208  SER B C   1 
ATOM   11596 O  O   . SER B 2 525  ? 136.049 108.613 148.086 1.00 42.52  ? 208  SER B O   1 
ATOM   11597 C  CB  . SER B 2 525  ? 133.620 107.343 149.514 1.00 46.28  ? 208  SER B CB  1 
ATOM   11598 O  OG  . SER B 2 525  ? 132.859 107.075 150.676 1.00 49.52  ? 208  SER B OG  1 
ATOM   11599 N  N   . LEU B 2 526  ? 134.269 109.680 147.237 1.00 39.03  ? 209  LEU B N   1 
ATOM   11600 C  CA  . LEU B 2 526  ? 134.868 109.841 145.917 1.00 42.47  ? 209  LEU B CA  1 
ATOM   11601 C  C   . LEU B 2 526  ? 136.131 110.690 146.004 1.00 40.23  ? 209  LEU B C   1 
ATOM   11602 O  O   . LEU B 2 526  ? 136.113 111.799 146.543 1.00 49.76  ? 209  LEU B O   1 
ATOM   11603 C  CB  . LEU B 2 526  ? 133.862 110.515 144.985 1.00 44.82  ? 209  LEU B CB  1 
ATOM   11604 C  CG  . LEU B 2 526  ? 132.522 109.777 144.862 1.00 53.50  ? 209  LEU B CG  1 
ATOM   11605 C  CD1 . LEU B 2 526  ? 131.528 110.521 143.963 1.00 57.41  ? 209  LEU B CD1 1 
ATOM   11606 C  CD2 . LEU B 2 526  ? 132.732 108.337 144.372 1.00 64.15  ? 209  LEU B CD2 1 
ATOM   11607 N  N   . THR B 2 527  ? 137.223 110.191 145.459 1.00 34.52  ? 210  THR B N   1 
ATOM   11608 C  CA  . THR B 2 527  ? 138.415 111.015 145.342 1.00 33.72  ? 210  THR B CA  1 
ATOM   11609 C  C   . THR B 2 527  ? 138.853 110.996 143.897 1.00 45.30  ? 210  THR B C   1 
ATOM   11610 O  O   . THR B 2 527  ? 138.066 110.625 143.026 1.00 55.00  ? 210  THR B O   1 
ATOM   11611 C  CB  . THR B 2 527  ? 139.528 110.509 146.236 1.00 50.81  ? 210  THR B CB  1 
ATOM   11612 O  OG1 . THR B 2 527  ? 139.813 109.141 145.919 1.00 53.59  ? 210  THR B OG1 1 
ATOM   11613 C  CG2 . THR B 2 527  ? 139.083 110.599 147.683 1.00 62.35  ? 210  THR B CG2 1 
ATOM   11614 N  N   . GLU B 2 528  ? 140.077 111.418 143.601 1.00 49.85  ? 211  GLU B N   1 
ATOM   11615 C  CA  . GLU B 2 528  ? 140.518 111.289 142.217 1.00 54.04  ? 211  GLU B CA  1 
ATOM   11616 C  C   . GLU B 2 528  ? 140.834 109.847 141.868 1.00 59.56  ? 211  GLU B C   1 
ATOM   11617 O  O   . GLU B 2 528  ? 140.626 109.431 140.722 1.00 65.43  ? 211  GLU B O   1 
ATOM   11618 C  CB  . GLU B 2 528  ? 141.738 112.154 141.949 1.00 59.00  ? 211  GLU B CB  1 
ATOM   11619 C  CG  . GLU B 2 528  ? 142.934 111.781 142.786 1.00 72.43  ? 211  GLU B CG  1 
ATOM   11620 C  CD  . GLU B 2 528  ? 144.174 112.514 142.342 1.00 83.45  ? 211  GLU B CD  1 
ATOM   11621 O  OE1 . GLU B 2 528  ? 144.057 113.366 141.431 1.00 75.84  ? 211  GLU B OE1 1 
ATOM   11622 O  OE2 . GLU B 2 528  ? 145.261 112.246 142.899 1.00 83.67  ? 211  GLU B OE2 1 
ATOM   11623 N  N   . GLU B 2 529  ? 141.335 109.068 142.824 1.00 56.19  ? 212  GLU B N   1 
ATOM   11624 C  CA  . GLU B 2 529  ? 141.610 107.671 142.521 1.00 59.62  ? 212  GLU B CA  1 
ATOM   11625 C  C   . GLU B 2 529  ? 140.325 106.876 142.446 1.00 53.11  ? 212  GLU B C   1 
ATOM   11626 O  O   . GLU B 2 529  ? 140.177 105.993 141.599 1.00 58.87  ? 212  GLU B O   1 
ATOM   11627 C  CB  . GLU B 2 529  ? 142.536 107.063 143.574 1.00 71.30  ? 212  GLU B CB  1 
ATOM   11628 C  CG  . GLU B 2 529  ? 143.725 107.948 143.926 1.00 85.18  ? 212  GLU B CG  1 
ATOM   11629 C  CD  . GLU B 2 529  ? 144.713 108.098 142.773 1.00 90.65  ? 212  GLU B CD  1 
ATOM   11630 O  OE1 . GLU B 2 529  ? 144.741 107.217 141.881 1.00 85.38  ? 212  GLU B OE1 1 
ATOM   11631 O  OE2 . GLU B 2 529  ? 145.447 109.112 142.747 1.00 85.78  ? 212  GLU B OE2 1 
ATOM   11632 N  N   . ASN B 2 530  ? 139.389 107.174 143.319 1.00 40.27  ? 213  ASN B N   1 
ATOM   11633 C  CA  . ASN B 2 530  ? 138.235 106.326 143.364 1.00 31.50  ? 213  ASN B CA  1 
ATOM   11634 C  C   . ASN B 2 530  ? 137.277 106.599 142.229 1.00 39.32  ? 213  ASN B C   1 
ATOM   11635 O  O   . ASN B 2 530  ? 136.484 105.725 141.884 1.00 53.53  ? 213  ASN B O   1 
ATOM   11636 C  CB  . ASN B 2 530  ? 137.536 106.493 144.684 1.00 42.56  ? 213  ASN B CB  1 
ATOM   11637 C  CG  . ASN B 2 530  ? 136.466 105.462 144.872 1.00 65.24  ? 213  ASN B CG  1 
ATOM   11638 O  OD1 . ASN B 2 530  ? 135.336 105.632 144.403 1.00 66.49  ? 213  ASN B OD1 1 
ATOM   11639 N  ND2 . ASN B 2 530  ? 136.823 104.343 145.505 1.00 59.01  ? 213  ASN B ND2 1 
ATOM   11640 N  N   . PHE B 2 531  ? 137.328 107.779 141.628 1.00 48.82  ? 214  PHE B N   1 
ATOM   11641 C  CA  . PHE B 2 531  ? 136.305 108.185 140.662 1.00 55.89  ? 214  PHE B CA  1 
ATOM   11642 C  C   . PHE B 2 531  ? 136.516 107.505 139.313 1.00 60.75  ? 214  PHE B C   1 
ATOM   11643 O  O   . PHE B 2 531  ? 137.567 107.674 138.682 1.00 56.94  ? 214  PHE B O   1 
ATOM   11644 C  CB  . PHE B 2 531  ? 136.326 109.701 140.492 1.00 56.66  ? 214  PHE B CB  1 
ATOM   11645 C  CG  . PHE B 2 531  ? 135.000 110.298 140.133 1.00 53.03  ? 214  PHE B CG  1 
ATOM   11646 C  CD1 . PHE B 2 531  ? 134.073 110.604 141.116 1.00 54.34  ? 214  PHE B CD1 1 
ATOM   11647 C  CD2 . PHE B 2 531  ? 134.703 110.605 138.813 1.00 57.68  ? 214  PHE B CD2 1 
ATOM   11648 C  CE1 . PHE B 2 531  ? 132.856 111.189 140.783 1.00 59.74  ? 214  PHE B CE1 1 
ATOM   11649 C  CE2 . PHE B 2 531  ? 133.491 111.186 138.469 1.00 58.88  ? 214  PHE B CE2 1 
ATOM   11650 C  CZ  . PHE B 2 531  ? 132.563 111.480 139.453 1.00 60.01  ? 214  PHE B CZ  1 
ATOM   11651 N  N   . GLY B 2 532  ? 135.497 106.762 138.856 1.00 63.57  ? 215  GLY B N   1 
ATOM   11652 C  CA  . GLY B 2 532  ? 135.523 106.064 137.583 1.00 58.76  ? 215  GLY B CA  1 
ATOM   11653 C  C   . GLY B 2 532  ? 136.048 104.636 137.604 1.00 66.52  ? 215  GLY B C   1 
ATOM   11654 O  O   . GLY B 2 532  ? 136.042 103.982 136.553 1.00 70.20  ? 215  GLY B O   1 
ATOM   11655 N  N   . LYS B 2 533  ? 136.507 104.130 138.753 1.00 65.66  ? 216  LYS B N   1 
ATOM   11656 C  CA  . LYS B 2 533  ? 137.053 102.776 138.825 1.00 57.30  ? 216  LYS B CA  1 
ATOM   11657 C  C   . LYS B 2 533  ? 135.912 101.782 138.935 1.00 62.63  ? 216  LYS B C   1 
ATOM   11658 O  O   . LYS B 2 533  ? 135.137 101.850 139.896 1.00 64.97  ? 216  LYS B O   1 
ATOM   11659 C  CB  . LYS B 2 533  ? 137.964 102.614 140.024 1.00 61.63  ? 216  LYS B CB  1 
ATOM   11660 C  CG  . LYS B 2 533  ? 138.572 101.228 140.151 1.00 66.49  ? 216  LYS B CG  1 
ATOM   11661 C  CD  . LYS B 2 533  ? 139.437 101.139 141.402 1.00 71.27  ? 216  LYS B CD  1 
ATOM   11662 C  CE  . LYS B 2 533  ? 140.576 102.159 141.399 1.00 80.57  ? 216  LYS B CE  1 
ATOM   11663 N  NZ  . LYS B 2 533  ? 141.446 102.032 142.619 1.00 79.83  ? 216  LYS B NZ  1 
ATOM   11664 N  N   . PRO B 2 534  ? 135.775 100.855 137.998 1.00 61.00  ? 217  PRO B N   1 
ATOM   11665 C  CA  . PRO B 2 534  ? 134.672 99.891  138.069 1.00 65.64  ? 217  PRO B CA  1 
ATOM   11666 C  C   . PRO B 2 534  ? 134.896 98.858  139.165 1.00 71.37  ? 217  PRO B C   1 
ATOM   11667 O  O   . PRO B 2 534  ? 136.030 98.558  139.546 1.00 74.16  ? 217  PRO B O   1 
ATOM   11668 C  CB  . PRO B 2 534  ? 134.688 99.244  136.681 1.00 70.52  ? 217  PRO B CB  1 
ATOM   11669 C  CG  . PRO B 2 534  ? 136.146 99.336  136.271 1.00 65.39  ? 217  PRO B CG  1 
ATOM   11670 C  CD  . PRO B 2 534  ? 136.654 100.634 136.840 1.00 55.49  ? 217  PRO B CD  1 
ATOM   11671 N  N   . ASP B 2 535  ? 133.791 98.310  139.675 1.00 71.84  ? 218  ASP B N   1 
ATOM   11672 C  CA  . ASP B 2 535  ? 133.834 97.203  140.635 1.00 74.57  ? 218  ASP B CA  1 
ATOM   11673 C  C   . ASP B 2 535  ? 133.690 95.904  139.844 1.00 79.15  ? 218  ASP B C   1 
ATOM   11674 O  O   . ASP B 2 535  ? 132.587 95.538  139.422 1.00 79.63  ? 218  ASP B O   1 
ATOM   11675 C  CB  . ASP B 2 535  ? 132.740 97.367  141.690 1.00 84.41  ? 218  ASP B CB  1 
ATOM   11676 C  CG  . ASP B 2 535  ? 132.937 96.454  142.908 1.00 92.64  ? 218  ASP B CG  1 
ATOM   11677 O  OD1 . ASP B 2 535  ? 133.919 95.675  142.932 1.00 80.37  ? 218  ASP B OD1 1 
ATOM   11678 O  OD2 . ASP B 2 535  ? 132.110 96.530  143.849 1.00 89.95  ? 218  ASP B OD2 1 
ATOM   11679 N  N   . ILE B 2 536  ? 134.805 95.200  139.641 1.00 71.36  ? 219  ILE B N   1 
ATOM   11680 C  CA  . ILE B 2 536  ? 134.862 94.048  138.746 1.00 63.76  ? 219  ILE B CA  1 
ATOM   11681 C  C   . ILE B 2 536  ? 134.899 92.784  139.585 1.00 53.66  ? 219  ILE B C   1 
ATOM   11682 O  O   . ILE B 2 536  ? 135.912 92.484  140.225 1.00 57.45  ? 219  ILE B O   1 
ATOM   11683 C  CB  . ILE B 2 536  ? 136.065 94.124  137.801 1.00 69.38  ? 219  ILE B CB  1 
ATOM   11684 C  CG1 . ILE B 2 536  ? 135.990 95.402  136.961 1.00 69.42  ? 219  ILE B CG1 1 
ATOM   11685 C  CG2 . ILE B 2 536  ? 136.107 92.906  136.893 1.00 73.32  ? 219  ILE B CG2 1 
ATOM   11686 C  CD1 . ILE B 2 536  ? 137.310 95.831  136.396 1.00 67.13  ? 219  ILE B CD1 1 
ATOM   11687 N  N   . SER B 2 537  ? 133.801 92.031  139.558 1.00 56.31  ? 220  SER B N   1 
ATOM   11688 C  CA  . SER B 2 537  ? 133.674 90.792  140.309 1.00 60.95  ? 220  SER B CA  1 
ATOM   11689 C  C   . SER B 2 537  ? 134.199 89.626  139.474 1.00 58.18  ? 220  SER B C   1 
ATOM   11690 O  O   . SER B 2 537  ? 134.617 89.793  138.328 1.00 64.51  ? 220  SER B O   1 
ATOM   11691 C  CB  . SER B 2 537  ? 132.221 90.574  140.735 1.00 62.53  ? 220  SER B CB  1 
ATOM   11692 O  OG  . SER B 2 537  ? 131.342 90.582  139.623 1.00 60.67  ? 220  SER B OG  1 
ATOM   11693 N  N   . ALA B 2 538  ? 134.201 88.425  140.055 1.00 54.71  ? 221  ALA B N   1 
ATOM   11694 C  CA  . ALA B 2 538  ? 134.700 87.275  139.311 1.00 58.66  ? 221  ALA B CA  1 
ATOM   11695 C  C   . ALA B 2 538  ? 133.785 86.943  138.142 1.00 62.46  ? 221  ALA B C   1 
ATOM   11696 O  O   . ALA B 2 538  ? 134.260 86.680  137.030 1.00 67.20  ? 221  ALA B O   1 
ATOM   11697 C  CB  . ALA B 2 538  ? 134.858 86.065  140.234 1.00 68.45  ? 221  ALA B CB  1 
ATOM   11698 N  N   . LYS B 2 539  ? 132.468 86.964  138.368 1.00 60.56  ? 222  LYS B N   1 
ATOM   11699 C  CA  . LYS B 2 539  ? 131.534 86.644  137.293 1.00 65.65  ? 222  LYS B CA  1 
ATOM   11700 C  C   . LYS B 2 539  ? 131.621 87.663  136.158 1.00 62.79  ? 222  LYS B C   1 
ATOM   11701 O  O   . LYS B 2 539  ? 131.655 87.297  134.972 1.00 62.32  ? 222  LYS B O   1 
ATOM   11702 C  CB  . LYS B 2 539  ? 130.113 86.563  137.850 1.00 67.38  ? 222  LYS B CB  1 
ATOM   11703 C  CG  . LYS B 2 539  ? 129.048 86.359  136.784 1.00 73.64  ? 222  LYS B CG  1 
ATOM   11704 C  CD  . LYS B 2 539  ? 127.681 86.841  137.253 1.00 82.12  ? 222  LYS B CD  1 
ATOM   11705 C  CE  . LYS B 2 539  ? 127.255 86.125  138.538 1.00 92.02  ? 222  LYS B CE  1 
ATOM   11706 N  NZ  . LYS B 2 539  ? 125.929 86.583  139.060 1.00 88.09  ? 222  LYS B NZ  1 
ATOM   11707 N  N   . ASP B 2 540  ? 131.661 88.947  136.503 1.00 59.50  ? 223  ASP B N   1 
ATOM   11708 C  CA  . ASP B 2 540  ? 131.766 89.961  135.470 1.00 51.10  ? 223  ASP B CA  1 
ATOM   11709 C  C   . ASP B 2 540  ? 133.089 89.855  134.758 1.00 41.58  ? 223  ASP B C   1 
ATOM   11710 O  O   . ASP B 2 540  ? 133.173 90.115  133.556 1.00 56.91  ? 223  ASP B O   1 
ATOM   11711 C  CB  . ASP B 2 540  ? 131.601 91.349  136.068 1.00 59.34  ? 223  ASP B CB  1 
ATOM   11712 C  CG  . ASP B 2 540  ? 130.215 91.564  136.634 1.00 70.20  ? 223  ASP B CG  1 
ATOM   11713 O  OD1 . ASP B 2 540  ? 129.251 90.990  136.075 1.00 63.37  ? 223  ASP B OD1 1 
ATOM   11714 O  OD2 . ASP B 2 540  ? 130.089 92.300  137.639 1.00 73.15  ? 223  ASP B OD2 1 
ATOM   11715 N  N   . LEU B 2 541  ? 134.131 89.487  135.469 1.00 38.24  ? 224  LEU B N   1 
ATOM   11716 C  CA  . LEU B 2 541  ? 135.394 89.357  134.784 1.00 38.95  ? 224  LEU B CA  1 
ATOM   11717 C  C   . LEU B 2 541  ? 135.328 88.216  133.783 1.00 55.70  ? 224  LEU B C   1 
ATOM   11718 O  O   . LEU B 2 541  ? 135.836 88.343  132.663 1.00 62.66  ? 224  LEU B O   1 
ATOM   11719 C  CB  . LEU B 2 541  ? 136.515 89.150  135.784 1.00 47.69  ? 224  LEU B CB  1 
ATOM   11720 C  CG  . LEU B 2 541  ? 137.877 89.371  135.156 1.00 53.65  ? 224  LEU B CG  1 
ATOM   11721 C  CD1 . LEU B 2 541  ? 137.856 90.747  134.527 1.00 55.43  ? 224  LEU B CD1 1 
ATOM   11722 C  CD2 . LEU B 2 541  ? 138.985 89.261  136.192 1.00 64.04  ? 224  LEU B CD2 1 
ATOM   11723 N  N   . ARG B 2 542  ? 134.680 87.103  134.153 1.00 57.61  ? 225  ARG B N   1 
ATOM   11724 C  CA  . ARG B 2 542  ? 134.524 85.991  133.211 1.00 50.35  ? 225  ARG B CA  1 
ATOM   11725 C  C   . ARG B 2 542  ? 133.743 86.410  131.973 1.00 60.67  ? 225  ARG B C   1 
ATOM   11726 O  O   . ARG B 2 542  ? 134.136 86.076  130.853 1.00 62.15  ? 225  ARG B O   1 
ATOM   11727 C  CB  . ARG B 2 542  ? 133.831 84.805  133.880 1.00 55.96  ? 225  ARG B CB  1 
ATOM   11728 C  CG  . ARG B 2 542  ? 134.711 83.995  134.806 1.00 72.78  ? 225  ARG B CG  1 
ATOM   11729 C  CD  . ARG B 2 542  ? 134.013 82.706  135.254 1.00 86.96  ? 225  ARG B CD  1 
ATOM   11730 N  NE  . ARG B 2 542  ? 132.805 82.976  136.044 1.00 89.85  ? 225  ARG B NE  1 
ATOM   11731 C  CZ  . ARG B 2 542  ? 131.556 82.906  135.581 1.00 90.63  ? 225  ARG B CZ  1 
ATOM   11732 N  NH1 . ARG B 2 542  ? 131.325 82.580  134.314 1.00 86.69  ? 225  ARG B NH1 1 
ATOM   11733 N  NH2 . ARG B 2 542  ? 130.534 83.172  136.390 1.00 86.92  ? 225  ARG B NH2 1 
ATOM   11734 N  N   . ASN B 2 543  ? 132.622 87.127  132.153 1.00 56.79  ? 226  ASN B N   1 
ATOM   11735 C  CA  . ASN B 2 543  ? 131.823 87.556  131.002 1.00 35.94  ? 226  ASN B CA  1 
ATOM   11736 C  C   . ASN B 2 543  ? 132.601 88.512  130.118 1.00 35.54  ? 226  ASN B C   1 
ATOM   11737 O  O   . ASN B 2 543  ? 132.491 88.462  128.894 1.00 45.45  ? 226  ASN B O   1 
ATOM   11738 C  CB  . ASN B 2 543  ? 130.544 88.223  131.467 1.00 37.72  ? 226  ASN B CB  1 
ATOM   11739 C  CG  . ASN B 2 543  ? 129.546 87.245  131.985 1.00 48.05  ? 226  ASN B CG  1 
ATOM   11740 O  OD1 . ASN B 2 543  ? 129.878 86.091  132.258 1.00 51.95  ? 226  ASN B OD1 1 
ATOM   11741 N  ND2 . ASN B 2 543  ? 128.308 87.701  132.165 1.00 52.96  ? 226  ASN B ND2 1 
ATOM   11742 N  N   . ILE B 2 544  ? 133.365 89.413  130.720 1.00 37.45  ? 227  ILE B N   1 
ATOM   11743 C  CA  . ILE B 2 544  ? 134.159 90.339  129.934 1.00 38.93  ? 227  ILE B CA  1 
ATOM   11744 C  C   . ILE B 2 544  ? 135.211 89.592  129.145 1.00 43.56  ? 227  ILE B C   1 
ATOM   11745 O  O   . ILE B 2 544  ? 135.480 89.921  127.986 1.00 53.80  ? 227  ILE B O   1 
ATOM   11746 C  CB  . ILE B 2 544  ? 134.809 91.399  130.837 1.00 49.50  ? 227  ILE B CB  1 
ATOM   11747 C  CG1 . ILE B 2 544  ? 133.779 92.406  131.324 1.00 48.17  ? 227  ILE B CG1 1 
ATOM   11748 C  CG2 . ILE B 2 544  ? 135.928 92.134  130.095 1.00 57.02  ? 227  ILE B CG2 1 
ATOM   11749 C  CD1 . ILE B 2 544  ? 134.416 93.529  132.115 1.00 54.30  ? 227  ILE B CD1 1 
ATOM   11750 N  N   . MET B 2 545  ? 135.856 88.600  129.757 1.00 45.59  ? 228  MET B N   1 
ATOM   11751 C  CA  . MET B 2 545  ? 136.914 87.915  129.021 1.00 56.67  ? 228  MET B CA  1 
ATOM   11752 C  C   . MET B 2 545  ? 136.368 86.922  127.999 1.00 55.54  ? 228  MET B C   1 
ATOM   11753 O  O   . MET B 2 545  ? 136.996 86.716  126.954 1.00 58.63  ? 228  MET B O   1 
ATOM   11754 C  CB  . MET B 2 545  ? 137.905 87.234  129.975 1.00 65.42  ? 228  MET B CB  1 
ATOM   11755 C  CG  . MET B 2 545  ? 138.634 88.216  130.906 1.00 69.39  ? 228  MET B CG  1 
ATOM   11756 S  SD  . MET B 2 545  ? 139.695 87.467  132.168 1.00 103.27 ? 228  MET B SD  1 
ATOM   11757 C  CE  . MET B 2 545  ? 141.063 86.916  131.169 1.00 81.60  ? 228  MET B CE  1 
ATOM   11758 N  N   . TYR B 2 546  ? 135.209 86.320  128.256 1.00 48.04  ? 229  TYR B N   1 
ATOM   11759 C  CA  . TYR B 2 546  ? 134.623 85.450  127.252 1.00 42.07  ? 229  TYR B CA  1 
ATOM   11760 C  C   . TYR B 2 546  ? 134.441 86.224  125.960 1.00 44.19  ? 229  TYR B C   1 
ATOM   11761 O  O   . TYR B 2 546  ? 134.986 85.855  124.915 1.00 52.66  ? 229  TYR B O   1 
ATOM   11762 C  CB  . TYR B 2 546  ? 133.273 84.920  127.729 1.00 43.30  ? 229  TYR B CB  1 
ATOM   11763 C  CG  . TYR B 2 546  ? 133.367 83.762  128.682 1.00 52.69  ? 229  TYR B CG  1 
ATOM   11764 C  CD1 . TYR B 2 546  ? 134.578 83.141  128.926 1.00 62.55  ? 229  TYR B CD1 1 
ATOM   11765 C  CD2 . TYR B 2 546  ? 132.241 83.292  129.350 1.00 57.81  ? 229  TYR B CD2 1 
ATOM   11766 C  CE1 . TYR B 2 546  ? 134.668 82.086  129.818 1.00 68.56  ? 229  TYR B CE1 1 
ATOM   11767 C  CE2 . TYR B 2 546  ? 132.320 82.233  130.237 1.00 60.64  ? 229  TYR B CE2 1 
ATOM   11768 C  CZ  . TYR B 2 546  ? 133.536 81.637  130.468 1.00 68.56  ? 229  TYR B CZ  1 
ATOM   11769 O  OH  . TYR B 2 546  ? 133.627 80.588  131.351 1.00 77.41  ? 229  TYR B OH  1 
ATOM   11770 N  N   . ASP B 2 547  ? 133.771 87.368  126.045 1.00 43.70  ? 230  ASP B N   1 
ATOM   11771 C  CA  . ASP B 2 547  ? 133.340 88.049  124.839 1.00 43.97  ? 230  ASP B CA  1 
ATOM   11772 C  C   . ASP B 2 547  ? 134.494 88.296  123.917 1.00 39.41  ? 230  ASP B C   1 
ATOM   11773 O  O   . ASP B 2 547  ? 134.312 88.304  122.702 1.00 53.53  ? 230  ASP B O   1 
ATOM   11774 C  CB  . ASP B 2 547  ? 132.638 89.371  125.158 1.00 50.12  ? 230  ASP B CB  1 
ATOM   11775 C  CG  . ASP B 2 547  ? 131.286 89.170  125.842 1.00 55.41  ? 230  ASP B CG  1 
ATOM   11776 O  OD1 . ASP B 2 547  ? 130.859 88.000  126.002 1.00 54.46  ? 230  ASP B OD1 1 
ATOM   11777 O  OD2 . ASP B 2 547  ? 130.645 90.182  126.213 1.00 50.77  ? 230  ASP B OD2 1 
ATOM   11778 N  N   . HIS B 2 548  ? 135.684 88.453  124.444 1.00 36.60  ? 231  HIS B N   1 
ATOM   11779 C  CA  . HIS B 2 548  ? 136.755 88.615  123.486 1.00 52.21  ? 231  HIS B CA  1 
ATOM   11780 C  C   . HIS B 2 548  ? 137.145 87.299  122.805 1.00 63.47  ? 231  HIS B C   1 
ATOM   11781 O  O   . HIS B 2 548  ? 137.592 87.319  121.649 1.00 62.49  ? 231  HIS B O   1 
ATOM   11782 C  CB  . HIS B 2 548  ? 137.939 89.294  124.152 1.00 47.93  ? 231  HIS B CB  1 
ATOM   11783 C  CG  . HIS B 2 548  ? 137.705 90.739  124.420 1.00 43.50  ? 231  HIS B CG  1 
ATOM   11784 N  ND1 . HIS B 2 548  ? 137.007 91.191  125.517 1.00 50.75  ? 231  HIS B ND1 1 
ATOM   11785 C  CD2 . HIS B 2 548  ? 138.070 91.839  123.723 1.00 48.19  ? 231  HIS B CD2 1 
ATOM   11786 C  CE1 . HIS B 2 548  ? 136.961 92.511  125.493 1.00 53.31  ? 231  HIS B CE1 1 
ATOM   11787 N  NE2 . HIS B 2 548  ? 137.600 92.930  124.414 1.00 50.77  ? 231  HIS B NE2 1 
ATOM   11788 N  N   . LEU B 2 549  ? 136.955 86.156  123.458 1.00 57.95  ? 232  LEU B N   1 
ATOM   11789 C  CA  . LEU B 2 549  ? 137.459 84.894  122.897 1.00 61.31  ? 232  LEU B CA  1 
ATOM   11790 C  C   . LEU B 2 549  ? 136.574 84.393  121.755 1.00 69.80  ? 232  LEU B C   1 
ATOM   11791 O  O   . LEU B 2 549  ? 135.347 84.333  121.908 1.00 70.07  ? 232  LEU B O   1 
ATOM   11792 C  CB  . LEU B 2 549  ? 137.535 83.829  123.975 1.00 61.51  ? 232  LEU B CB  1 
ATOM   11793 C  CG  . LEU B 2 549  ? 138.560 84.147  125.051 1.00 71.85  ? 232  LEU B CG  1 
ATOM   11794 C  CD1 . LEU B 2 549  ? 138.490 83.101  126.166 1.00 80.10  ? 232  LEU B CD1 1 
ATOM   11795 C  CD2 . LEU B 2 549  ? 139.956 84.242  124.430 1.00 74.10  ? 232  LEU B CD2 1 
ATOM   11796 N  N   . PRO B 2 550  ? 137.149 83.996  120.620 1.00 63.15  ? 233  PRO B N   1 
ATOM   11797 C  CA  . PRO B 2 550  ? 136.338 83.449  119.530 1.00 55.07  ? 233  PRO B CA  1 
ATOM   11798 C  C   . PRO B 2 550  ? 135.894 82.029  119.810 1.00 50.67  ? 233  PRO B C   1 
ATOM   11799 O  O   . PRO B 2 550  ? 136.575 81.257  120.485 1.00 59.37  ? 233  PRO B O   1 
ATOM   11800 C  CB  . PRO B 2 550  ? 137.283 83.487  118.326 1.00 61.99  ? 233  PRO B CB  1 
ATOM   11801 C  CG  . PRO B 2 550  ? 138.660 83.544  118.898 1.00 64.32  ? 233  PRO B CG  1 
ATOM   11802 C  CD  . PRO B 2 550  ? 138.587 83.825  120.376 1.00 64.84  ? 233  PRO B CD  1 
ATOM   11803 N  N   . GLY B 2 551  ? 134.735 81.692  119.263 1.00 60.03  ? 234  GLY B N   1 
ATOM   11804 C  CA  . GLY B 2 551  ? 134.164 80.375  119.445 1.00 64.11  ? 234  GLY B CA  1 
ATOM   11805 C  C   . GLY B 2 551  ? 133.490 80.219  120.791 1.00 61.09  ? 234  GLY B C   1 
ATOM   11806 O  O   . GLY B 2 551  ? 133.385 81.145  121.596 1.00 68.66  ? 234  GLY B O   1 
ATOM   11807 N  N   . PHE B 2 552  ? 133.015 79.008  121.028 1.00 56.57  ? 235  PHE B N   1 
ATOM   11808 C  CA  . PHE B 2 552  ? 132.429 78.654  122.304 1.00 72.17  ? 235  PHE B CA  1 
ATOM   11809 C  C   . PHE B 2 552  ? 133.098 77.400  122.849 1.00 81.58  ? 235  PHE B C   1 
ATOM   11810 O  O   . PHE B 2 552  ? 133.372 76.456  122.101 1.00 83.08  ? 235  PHE B O   1 
ATOM   11811 C  CB  . PHE B 2 552  ? 130.916 78.442  122.187 1.00 90.86  ? 235  PHE B CB  1 
ATOM   11812 C  CG  . PHE B 2 552  ? 130.284 77.872  123.444 1.00 111.48 ? 235  PHE B CG  1 
ATOM   11813 C  CD1 . PHE B 2 552  ? 130.056 78.676  124.566 1.00 105.13 ? 235  PHE B CD1 1 
ATOM   11814 C  CD2 . PHE B 2 552  ? 129.930 76.521  123.510 1.00 115.19 ? 235  PHE B CD2 1 
ATOM   11815 C  CE1 . PHE B 2 552  ? 129.478 78.139  125.729 1.00 110.14 ? 235  PHE B CE1 1 
ATOM   11816 C  CE2 . PHE B 2 552  ? 129.354 75.978  124.665 1.00 115.54 ? 235  PHE B CE2 1 
ATOM   11817 C  CZ  . PHE B 2 552  ? 129.127 76.788  125.774 1.00 114.67 ? 235  PHE B CZ  1 
ATOM   11818 N  N   . GLY B 2 553  ? 133.360 77.403  124.157 1.00 84.36  ? 236  GLY B N   1 
ATOM   11819 C  CA  . GLY B 2 553  ? 133.887 76.239  124.845 1.00 79.63  ? 236  GLY B CA  1 
ATOM   11820 C  C   . GLY B 2 553  ? 135.332 75.906  124.553 1.00 82.30  ? 236  GLY B C   1 
ATOM   11821 O  O   . GLY B 2 553  ? 135.754 74.777  124.815 1.00 91.83  ? 236  GLY B O   1 
ATOM   11822 N  N   . THR B 2 554  ? 136.114 76.850  124.023 1.00 77.53  ? 237  THR B N   1 
ATOM   11823 C  CA  . THR B 2 554  ? 137.506 76.567  123.688 1.00 75.80  ? 237  THR B CA  1 
ATOM   11824 C  C   . THR B 2 554  ? 138.323 76.342  124.962 1.00 70.32  ? 237  THR B C   1 
ATOM   11825 O  O   . THR B 2 554  ? 137.848 76.551  126.081 1.00 76.98  ? 237  THR B O   1 
ATOM   11826 C  CB  . THR B 2 554  ? 138.109 77.706  122.857 1.00 72.83  ? 237  THR B CB  1 
ATOM   11827 O  OG1 . THR B 2 554  ? 138.014 78.938  123.581 1.00 72.97  ? 237  THR B OG1 1 
ATOM   11828 C  CG2 . THR B 2 554  ? 137.386 77.854  121.520 1.00 71.59  ? 237  THR B CG2 1 
ATOM   11829 N  N   . ALA B 2 555  ? 139.566 75.895  124.792 1.00 64.12  ? 238  ALA B N   1 
ATOM   11830 C  CA  . ALA B 2 555  ? 140.423 75.773  125.961 1.00 67.28  ? 238  ALA B CA  1 
ATOM   11831 C  C   . ALA B 2 555  ? 140.571 77.111  126.651 1.00 64.94  ? 238  ALA B C   1 
ATOM   11832 O  O   . ALA B 2 555  ? 140.629 77.176  127.883 1.00 72.95  ? 238  ALA B O   1 
ATOM   11833 C  CB  . ALA B 2 555  ? 141.795 75.227  125.577 1.00 79.30  ? 238  ALA B CB  1 
ATOM   11834 N  N   . PHE B 2 556  ? 140.594 78.187  125.879 1.00 55.65  ? 239  PHE B N   1 
ATOM   11835 C  CA  . PHE B 2 556  ? 140.731 79.492  126.492 1.00 62.85  ? 239  PHE B CA  1 
ATOM   11836 C  C   . PHE B 2 556  ? 139.585 79.805  127.428 1.00 63.78  ? 239  PHE B C   1 
ATOM   11837 O  O   . PHE B 2 556  ? 139.796 80.474  128.442 1.00 73.12  ? 239  PHE B O   1 
ATOM   11838 C  CB  . PHE B 2 556  ? 140.843 80.550  125.421 1.00 66.71  ? 239  PHE B CB  1 
ATOM   11839 C  CG  . PHE B 2 556  ? 142.076 80.436  124.650 1.00 71.12  ? 239  PHE B CG  1 
ATOM   11840 C  CD1 . PHE B 2 556  ? 143.223 81.066  125.083 1.00 76.40  ? 239  PHE B CD1 1 
ATOM   11841 C  CD2 . PHE B 2 556  ? 142.120 79.629  123.534 1.00 71.10  ? 239  PHE B CD2 1 
ATOM   11842 C  CE1 . PHE B 2 556  ? 144.386 80.942  124.381 1.00 87.68  ? 239  PHE B CE1 1 
ATOM   11843 C  CE2 . PHE B 2 556  ? 143.275 79.495  122.822 1.00 81.53  ? 239  PHE B CE2 1 
ATOM   11844 C  CZ  . PHE B 2 556  ? 144.419 80.150  123.245 1.00 94.71  ? 239  PHE B CZ  1 
ATOM   11845 N  N   . HIS B 2 557  ? 138.369 79.362  127.115 1.00 64.15  ? 240  HIS B N   1 
ATOM   11846 C  CA  . HIS B 2 557  ? 137.278 79.605  128.051 1.00 65.72  ? 240  HIS B CA  1 
ATOM   11847 C  C   . HIS B 2 557  ? 137.565 78.944  129.392 1.00 74.33  ? 240  HIS B C   1 
ATOM   11848 O  O   . HIS B 2 557  ? 137.332 79.544  130.456 1.00 80.28  ? 240  HIS B O   1 
ATOM   11849 C  CB  . HIS B 2 557  ? 135.930 79.137  127.484 1.00 67.23  ? 240  HIS B CB  1 
ATOM   11850 C  CG  . HIS B 2 557  ? 135.400 79.988  126.364 1.00 72.81  ? 240  HIS B CG  1 
ATOM   11851 N  ND1 . HIS B 2 557  ? 136.068 80.167  125.170 1.00 76.43  ? 240  HIS B ND1 1 
ATOM   11852 C  CD2 . HIS B 2 557  ? 134.263 80.723  126.268 1.00 70.41  ? 240  HIS B CD2 1 
ATOM   11853 C  CE1 . HIS B 2 557  ? 135.364 80.968  124.386 1.00 73.08  ? 240  HIS B CE1 1 
ATOM   11854 N  NE2 . HIS B 2 557  ? 134.265 81.321  125.029 1.00 68.60  ? 240  HIS B NE2 1 
ATOM   11855 N  N   . GLN B 2 558  ? 138.090 77.720  129.375 1.00 69.90  ? 241  GLN B N   1 
ATOM   11856 C  CA  . GLN B 2 558  ? 138.401 77.081  130.648 1.00 72.02  ? 241  GLN B CA  1 
ATOM   11857 C  C   . GLN B 2 558  ? 139.535 77.803  131.350 1.00 68.08  ? 241  GLN B C   1 
ATOM   11858 O  O   . GLN B 2 558  ? 139.517 77.968  132.576 1.00 74.67  ? 241  GLN B O   1 
ATOM   11859 C  CB  . GLN B 2 558  ? 138.742 75.614  130.446 1.00 80.54  ? 241  GLN B CB  1 
ATOM   11860 C  CG  . GLN B 2 558  ? 138.937 74.877  131.752 1.00 89.59  ? 241  GLN B CG  1 
ATOM   11861 C  CD  . GLN B 2 558  ? 137.651 74.666  132.541 1.00 97.47  ? 241  GLN B CD  1 
ATOM   11862 O  OE1 . GLN B 2 558  ? 137.489 75.206  133.639 1.00 95.06  ? 241  GLN B OE1 1 
ATOM   11863 N  NE2 . GLN B 2 558  ? 136.730 73.881  131.984 1.00 98.28  ? 241  GLN B NE2 1 
ATOM   11864 N  N   . LEU B 2 559  ? 140.519 78.250  130.584 1.00 63.05  ? 242  LEU B N   1 
ATOM   11865 C  CA  . LEU B 2 559  ? 141.585 79.040  131.166 1.00 55.16  ? 242  LEU B CA  1 
ATOM   11866 C  C   . LEU B 2 559  ? 141.020 80.240  131.883 1.00 51.87  ? 242  LEU B C   1 
ATOM   11867 O  O   . LEU B 2 559  ? 141.460 80.582  132.980 1.00 62.83  ? 242  LEU B O   1 
ATOM   11868 C  CB  . LEU B 2 559  ? 142.539 79.482  130.072 1.00 63.31  ? 242  LEU B CB  1 
ATOM   11869 C  CG  . LEU B 2 559  ? 143.635 80.434  130.507 1.00 74.08  ? 242  LEU B CG  1 
ATOM   11870 C  CD1 . LEU B 2 559  ? 144.522 79.757  131.542 1.00 78.24  ? 242  LEU B CD1 1 
ATOM   11871 C  CD2 . LEU B 2 559  ? 144.434 80.865  129.286 1.00 80.10  ? 242  LEU B CD2 1 
ATOM   11872 N  N   . VAL B 2 560  ? 140.036 80.887  131.275 1.00 59.02  ? 243  VAL B N   1 
ATOM   11873 C  CA  . VAL B 2 560  ? 139.484 82.107  131.845 1.00 65.20  ? 243  VAL B CA  1 
ATOM   11874 C  C   . VAL B 2 560  ? 138.759 81.801  133.144 1.00 67.60  ? 243  VAL B C   1 
ATOM   11875 O  O   . VAL B 2 560  ? 138.948 82.488  134.154 1.00 76.91  ? 243  VAL B O   1 
ATOM   11876 C  CB  . VAL B 2 560  ? 138.559 82.814  130.833 1.00 68.71  ? 243  VAL B CB  1 
ATOM   11877 C  CG1 . VAL B 2 560  ? 137.627 83.796  131.546 1.00 68.80  ? 243  VAL B CG1 1 
ATOM   11878 C  CG2 . VAL B 2 560  ? 139.385 83.543  129.761 1.00 70.88  ? 243  VAL B CG2 1 
ATOM   11879 N  N   . GLN B 2 561  ? 137.924 80.768  133.150 1.00 65.46  ? 244  GLN B N   1 
ATOM   11880 C  CA  . GLN B 2 561  ? 137.188 80.518  134.385 1.00 65.87  ? 244  GLN B CA  1 
ATOM   11881 C  C   . GLN B 2 561  ? 138.081 79.944  135.476 1.00 63.39  ? 244  GLN B C   1 
ATOM   11882 O  O   . GLN B 2 561  ? 137.692 79.959  136.647 1.00 68.56  ? 244  GLN B O   1 
ATOM   11883 C  CB  . GLN B 2 561  ? 135.993 79.616  134.120 1.00 66.65  ? 244  GLN B CB  1 
ATOM   11884 C  CG  . GLN B 2 561  ? 136.363 78.311  133.488 1.00 75.60  ? 244  GLN B CG  1 
ATOM   11885 C  CD  . GLN B 2 561  ? 135.229 77.735  132.661 1.00 85.92  ? 244  GLN B CD  1 
ATOM   11886 O  OE1 . GLN B 2 561  ? 134.511 78.468  131.978 1.00 82.22  ? 244  GLN B OE1 1 
ATOM   11887 N  NE2 . GLN B 2 561  ? 135.073 76.416  132.703 1.00 93.17  ? 244  GLN B NE2 1 
ATOM   11888 N  N   . VAL B 2 562  ? 139.268 79.447  135.123 1.00 65.59  ? 245  VAL B N   1 
ATOM   11889 C  CA  . VAL B 2 562  ? 140.268 79.123  136.137 1.00 62.35  ? 245  VAL B CA  1 
ATOM   11890 C  C   . VAL B 2 562  ? 140.916 80.396  136.665 1.00 69.43  ? 245  VAL B C   1 
ATOM   11891 O  O   . VAL B 2 562  ? 141.076 80.572  137.878 1.00 76.25  ? 245  VAL B O   1 
ATOM   11892 C  CB  . VAL B 2 562  ? 141.325 78.158  135.568 1.00 73.18  ? 245  VAL B CB  1 
ATOM   11893 C  CG1 . VAL B 2 562  ? 142.587 78.168  136.431 1.00 73.38  ? 245  VAL B CG1 1 
ATOM   11894 C  CG2 . VAL B 2 562  ? 140.756 76.738  135.441 1.00 84.68  ? 245  VAL B CG2 1 
ATOM   11895 N  N   . ILE B 2 563  ? 141.304 81.302  135.758 1.00 72.32  ? 246  ILE B N   1 
ATOM   11896 C  CA  . ILE B 2 563  ? 141.997 82.533  136.148 1.00 64.99  ? 246  ILE B CA  1 
ATOM   11897 C  C   . ILE B 2 563  ? 141.129 83.360  137.075 1.00 63.76  ? 246  ILE B C   1 
ATOM   11898 O  O   . ILE B 2 563  ? 141.591 83.878  138.097 1.00 73.60  ? 246  ILE B O   1 
ATOM   11899 C  CB  . ILE B 2 563  ? 142.407 83.344  134.907 1.00 54.45  ? 246  ILE B CB  1 
ATOM   11900 C  CG1 . ILE B 2 563  ? 143.599 82.691  134.236 1.00 60.53  ? 246  ILE B CG1 1 
ATOM   11901 C  CG2 . ILE B 2 563  ? 142.707 84.784  135.269 1.00 65.71  ? 246  ILE B CG2 1 
ATOM   11902 C  CD1 . ILE B 2 563  ? 143.894 83.260  132.921 1.00 63.08  ? 246  ILE B CD1 1 
ATOM   11903 N  N   . CYS B 2 564  ? 139.857 83.493  136.733 1.00 61.34  ? 247  CYS B N   1 
ATOM   11904 C  CA  . CYS B 2 564  ? 138.959 84.215  137.610 1.00 65.50  ? 247  CYS B CA  1 
ATOM   11905 C  C   . CYS B 2 564  ? 138.756 83.496  138.929 1.00 71.94  ? 247  CYS B C   1 
ATOM   11906 O  O   . CYS B 2 564  ? 138.314 84.124  139.895 1.00 79.46  ? 247  CYS B O   1 
ATOM   11907 C  CB  . CYS B 2 564  ? 137.629 84.445  136.910 1.00 69.55  ? 247  CYS B CB  1 
ATOM   11908 S  SG  . CYS B 2 564  ? 137.847 85.523  135.485 1.00 88.16  ? 247  CYS B SG  1 
ATOM   11909 N  N   . LYS B 2 565  ? 139.076 82.205  139.005 1.00 68.05  ? 248  LYS B N   1 
ATOM   11910 C  CA  . LYS B 2 565  ? 138.951 81.524  140.286 1.00 70.15  ? 248  LYS B CA  1 
ATOM   11911 C  C   . LYS B 2 565  ? 140.171 81.788  141.164 1.00 73.11  ? 248  LYS B C   1 
ATOM   11912 O  O   . LYS B 2 565  ? 140.024 82.080  142.355 1.00 81.60  ? 248  LYS B O   1 
ATOM   11913 C  CB  . LYS B 2 565  ? 138.736 80.023  140.068 1.00 84.20  ? 248  LYS B CB  1 
ATOM   11914 C  CG  . LYS B 2 565  ? 138.632 79.164  141.343 1.00 92.46  ? 248  LYS B CG  1 
ATOM   11915 C  CD  . LYS B 2 565  ? 137.444 79.579  142.225 1.00 94.41  ? 248  LYS B CD  1 
ATOM   11916 C  CE  . LYS B 2 565  ? 137.188 78.574  143.360 1.00 94.53  ? 248  LYS B CE  1 
ATOM   11917 N  NZ  . LYS B 2 565  ? 138.374 78.362  144.240 1.00 92.61  ? 248  LYS B NZ  1 
ATOM   11918 N  N   . LEU B 2 566  ? 141.379 81.706  140.595 1.00 72.10  ? 249  LEU B N   1 
ATOM   11919 C  CA  . LEU B 2 566  ? 142.580 82.038  141.361 1.00 75.38  ? 249  LEU B CA  1 
ATOM   11920 C  C   . LEU B 2 566  ? 142.605 83.512  141.729 1.00 72.95  ? 249  LEU B C   1 
ATOM   11921 O  O   . LEU B 2 566  ? 143.038 83.879  142.829 1.00 75.24  ? 249  LEU B O   1 
ATOM   11922 C  CB  . LEU B 2 566  ? 143.837 81.667  140.576 1.00 80.75  ? 249  LEU B CB  1 
ATOM   11923 C  CG  . LEU B 2 566  ? 144.090 80.165  140.381 1.00 97.62  ? 249  LEU B CG  1 
ATOM   11924 C  CD1 . LEU B 2 566  ? 145.357 79.882  139.565 1.00 99.80  ? 249  LEU B CD1 1 
ATOM   11925 C  CD2 . LEU B 2 566  ? 144.142 79.436  141.727 1.00 95.97  ? 249  LEU B CD2 1 
ATOM   11926 N  N   . GLY B 2 567  ? 142.153 84.369  140.818 1.00 72.16  ? 250  GLY B N   1 
ATOM   11927 C  CA  . GLY B 2 567  ? 142.113 85.786  141.115 1.00 71.17  ? 250  GLY B CA  1 
ATOM   11928 C  C   . GLY B 2 567  ? 141.193 86.120  142.274 1.00 74.12  ? 250  GLY B C   1 
ATOM   11929 O  O   . GLY B 2 567  ? 141.574 86.867  143.179 1.00 81.68  ? 250  GLY B O   1 
ATOM   11930 N  N   . LYS B 2 568  ? 139.979 85.562  142.275 1.00 66.48  ? 251  LYS B N   1 
ATOM   11931 C  CA  . LYS B 2 568  ? 139.017 85.909  143.318 1.00 67.06  ? 251  LYS B CA  1 
ATOM   11932 C  C   . LYS B 2 568  ? 139.530 85.520  144.695 1.00 71.41  ? 251  LYS B C   1 
ATOM   11933 O  O   . LYS B 2 568  ? 139.349 86.260  145.669 1.00 75.65  ? 251  LYS B O   1 
ATOM   11934 C  CB  . LYS B 2 568  ? 137.678 85.234  143.049 1.00 72.15  ? 251  LYS B CB  1 
ATOM   11935 C  CG  . LYS B 2 568  ? 136.512 85.828  143.814 1.00 75.90  ? 251  LYS B CG  1 
ATOM   11936 C  CD  . LYS B 2 568  ? 135.285 84.932  143.677 1.00 79.56  ? 251  LYS B CD  1 
ATOM   11937 C  CE  . LYS B 2 568  ? 134.039 85.568  144.274 1.00 81.54  ? 251  LYS B CE  1 
ATOM   11938 N  NZ  . LYS B 2 568  ? 134.187 85.780  145.744 1.00 81.29  ? 251  LYS B NZ  1 
ATOM   11939 N  N   . ASP B 2 569  ? 140.165 84.356  144.797 1.00 71.12  ? 252  ASP B N   1 
ATOM   11940 C  CA  . ASP B 2 569  ? 140.714 83.935  146.077 1.00 75.13  ? 252  ASP B CA  1 
ATOM   11941 C  C   . ASP B 2 569  ? 141.853 84.849  146.517 1.00 71.50  ? 252  ASP B C   1 
ATOM   11942 O  O   . ASP B 2 569  ? 141.910 85.260  147.682 1.00 72.49  ? 252  ASP B O   1 
ATOM   11943 C  CB  . ASP B 2 569  ? 141.181 82.479  145.982 1.00 89.00  ? 252  ASP B CB  1 
ATOM   11944 C  CG  . ASP B 2 569  ? 140.018 81.495  145.819 1.00 94.69  ? 252  ASP B CG  1 
ATOM   11945 O  OD1 . ASP B 2 569  ? 138.847 81.938  145.876 1.00 88.90  ? 252  ASP B OD1 1 
ATOM   11946 O  OD2 . ASP B 2 569  ? 140.278 80.281  145.632 1.00 90.81  ? 252  ASP B OD2 1 
ATOM   11947 N  N   . SER B 2 570  ? 142.751 85.203  145.599 1.00 68.24  ? 253  SER B N   1 
ATOM   11948 C  CA  . SER B 2 570  ? 143.910 86.024  145.919 1.00 65.80  ? 253  SER B CA  1 
ATOM   11949 C  C   . SER B 2 570  ? 143.598 87.513  145.900 1.00 70.81  ? 253  SER B C   1 
ATOM   11950 O  O   . SER B 2 570  ? 144.513 88.328  146.068 1.00 72.68  ? 253  SER B O   1 
ATOM   11951 C  CB  . SER B 2 570  ? 145.046 85.733  144.947 1.00 58.86  ? 253  SER B CB  1 
ATOM   11952 O  OG  . SER B 2 570  ? 144.665 86.094  143.639 1.00 65.58  ? 253  SER B OG  1 
ATOM   11953 N  N   . ASN B 2 571  ? 142.336 87.876  145.684 1.00 73.48  ? 254  ASN B N   1 
ATOM   11954 C  CA  . ASN B 2 571  ? 141.897 89.267  145.643 1.00 75.74  ? 254  ASN B CA  1 
ATOM   11955 C  C   . ASN B 2 571  ? 142.789 90.081  144.703 1.00 71.38  ? 254  ASN B C   1 
ATOM   11956 O  O   . ASN B 2 571  ? 143.247 91.178  145.028 1.00 76.44  ? 254  ASN B O   1 
ATOM   11957 C  CB  . ASN B 2 571  ? 141.844 89.868  147.052 1.00 80.21  ? 254  ASN B CB  1 
ATOM   11958 C  CG  . ASN B 2 571  ? 141.023 91.157  147.112 1.00 90.79  ? 254  ASN B CG  1 
ATOM   11959 O  OD1 . ASN B 2 571  ? 140.256 91.466  146.192 1.00 83.94  ? 254  ASN B OD1 1 
ATOM   11960 N  ND2 . ASN B 2 571  ? 141.184 91.915  148.197 1.00 91.54  ? 254  ASN B ND2 1 
ATOM   11961 N  N   . SER B 2 572  ? 143.051 89.520  143.526 1.00 62.76  ? 255  SER B N   1 
ATOM   11962 C  CA  . SER B 2 572  ? 143.889 90.153  142.521 1.00 61.45  ? 255  SER B CA  1 
ATOM   11963 C  C   . SER B 2 572  ? 143.171 90.319  141.177 1.00 70.37  ? 255  SER B C   1 
ATOM   11964 O  O   . SER B 2 572  ? 143.819 90.359  140.127 1.00 68.81  ? 255  SER B O   1 
ATOM   11965 C  CB  . SER B 2 572  ? 145.177 89.357  142.362 1.00 64.54  ? 255  SER B CB  1 
ATOM   11966 O  OG  . SER B 2 572  ? 144.877 88.018  142.037 1.00 70.46  ? 255  SER B OG  1 
ATOM   11967 N  N   . LEU B 2 573  ? 141.829 90.449  141.199 1.00 75.03  ? 256  LEU B N   1 
ATOM   11968 C  CA  . LEU B 2 573  ? 141.047 90.638  139.968 1.00 66.55  ? 256  LEU B CA  1 
ATOM   11969 C  C   . LEU B 2 573  ? 141.423 91.918  139.242 1.00 62.28  ? 256  LEU B C   1 
ATOM   11970 O  O   . LEU B 2 573  ? 141.530 91.933  138.012 1.00 65.54  ? 256  LEU B O   1 
ATOM   11971 C  CB  . LEU B 2 573  ? 139.549 90.670  140.267 1.00 45.85  ? 256  LEU B CB  1 
ATOM   11972 C  CG  . LEU B 2 573  ? 138.959 89.366  140.747 1.00 54.59  ? 256  LEU B CG  1 
ATOM   11973 C  CD1 . LEU B 2 573  ? 137.483 89.538  140.967 1.00 60.33  ? 256  LEU B CD1 1 
ATOM   11974 C  CD2 . LEU B 2 573  ? 139.223 88.324  139.676 1.00 67.66  ? 256  LEU B CD2 1 
ATOM   11975 N  N   . ASP B 2 574  ? 141.580 93.011  139.980 1.00 62.79  ? 257  ASP B N   1 
ATOM   11976 C  CA  . ASP B 2 574  ? 141.870 94.279  139.336 1.00 63.52  ? 257  ASP B CA  1 
ATOM   11977 C  C   . ASP B 2 574  ? 143.184 94.205  138.587 1.00 65.64  ? 257  ASP B C   1 
ATOM   11978 O  O   . ASP B 2 574  ? 143.298 94.724  137.473 1.00 70.72  ? 257  ASP B O   1 
ATOM   11979 C  CB  . ASP B 2 574  ? 141.902 95.399  140.369 1.00 66.52  ? 257  ASP B CB  1 
ATOM   11980 C  CG  . ASP B 2 574  ? 140.547 95.632  141.006 1.00 79.11  ? 257  ASP B CG  1 
ATOM   11981 O  OD1 . ASP B 2 574  ? 139.519 95.367  140.339 1.00 76.32  ? 257  ASP B OD1 1 
ATOM   11982 O  OD2 . ASP B 2 574  ? 140.508 96.068  142.179 1.00 84.90  ? 257  ASP B OD2 1 
ATOM   11983 N  N   . ILE B 2 575  ? 144.188 93.564  139.178 1.00 58.71  ? 258  ILE B N   1 
ATOM   11984 C  CA  . ILE B 2 575  ? 145.473 93.459  138.503 1.00 58.76  ? 258  ILE B CA  1 
ATOM   11985 C  C   . ILE B 2 575  ? 145.340 92.616  137.251 1.00 58.56  ? 258  ILE B C   1 
ATOM   11986 O  O   . ILE B 2 575  ? 145.888 92.948  136.193 1.00 62.72  ? 258  ILE B O   1 
ATOM   11987 C  CB  . ILE B 2 575  ? 146.531 92.895  139.464 1.00 68.74  ? 258  ILE B CB  1 
ATOM   11988 C  CG1 . ILE B 2 575  ? 146.769 93.875  140.622 1.00 77.11  ? 258  ILE B CG1 1 
ATOM   11989 C  CG2 . ILE B 2 575  ? 147.822 92.591  138.713 1.00 71.44  ? 258  ILE B CG2 1 
ATOM   11990 C  CD1 . ILE B 2 575  ? 145.970 93.570  141.881 1.00 74.77  ? 258  ILE B CD1 1 
ATOM   11991 N  N   . ILE B 2 576  ? 144.595 91.524  137.346 1.00 60.26  ? 259  ILE B N   1 
ATOM   11992 C  CA  . ILE B 2 576  ? 144.374 90.670  136.191 1.00 57.82  ? 259  ILE B CA  1 
ATOM   11993 C  C   . ILE B 2 576  ? 143.736 91.468  135.064 1.00 60.78  ? 259  ILE B C   1 
ATOM   11994 O  O   . ILE B 2 576  ? 144.263 91.520  133.950 1.00 63.77  ? 259  ILE B O   1 
ATOM   11995 C  CB  . ILE B 2 576  ? 143.517 89.460  136.615 1.00 66.94  ? 259  ILE B CB  1 
ATOM   11996 C  CG1 . ILE B 2 576  ? 144.369 88.429  137.357 1.00 72.28  ? 259  ILE B CG1 1 
ATOM   11997 C  CG2 . ILE B 2 576  ? 142.733 88.850  135.474 1.00 73.89  ? 259  ILE B CG2 1 
ATOM   11998 C  CD1 . ILE B 2 576  ? 143.594 87.194  137.744 1.00 74.23  ? 259  ILE B CD1 1 
ATOM   11999 N  N   . HIS B 2 577  ? 142.628 92.153  135.354 1.00 63.96  ? 260  HIS B N   1 
ATOM   12000 C  CA  . HIS B 2 577  ? 141.931 92.885  134.303 1.00 56.65  ? 260  HIS B CA  1 
ATOM   12001 C  C   . HIS B 2 577  ? 142.770 94.010  133.753 1.00 56.48  ? 260  HIS B C   1 
ATOM   12002 O  O   . HIS B 2 577  ? 142.715 94.300  132.557 1.00 67.49  ? 260  HIS B O   1 
ATOM   12003 C  CB  . HIS B 2 577  ? 140.620 93.471  134.782 1.00 59.01  ? 260  HIS B CB  1 
ATOM   12004 C  CG  . HIS B 2 577  ? 139.762 93.933  133.655 1.00 62.73  ? 260  HIS B CG  1 
ATOM   12005 N  ND1 . HIS B 2 577  ? 138.675 94.759  133.828 1.00 74.96  ? 260  HIS B ND1 1 
ATOM   12006 C  CD2 . HIS B 2 577  ? 139.851 93.701  132.324 1.00 66.72  ? 260  HIS B CD2 1 
ATOM   12007 C  CE1 . HIS B 2 577  ? 138.117 95.001  132.654 1.00 81.12  ? 260  HIS B CE1 1 
ATOM   12008 N  NE2 . HIS B 2 577  ? 138.812 94.370  131.724 1.00 76.18  ? 260  HIS B NE2 1 
ATOM   12009 N  N   . ALA B 2 578  ? 143.489 94.711  134.614 1.00 58.90  ? 261  ALA B N   1 
ATOM   12010 C  CA  . ALA B 2 578  ? 144.383 95.722  134.098 1.00 57.25  ? 261  ALA B CA  1 
ATOM   12011 C  C   . ALA B 2 578  ? 145.351 95.083  133.131 1.00 56.52  ? 261  ALA B C   1 
ATOM   12012 O  O   . ALA B 2 578  ? 145.612 95.625  132.051 1.00 66.12  ? 261  ALA B O   1 
ATOM   12013 C  CB  . ALA B 2 578  ? 145.119 96.413  135.243 1.00 62.71  ? 261  ALA B CB  1 
ATOM   12014 N  N   . GLU B 2 579  ? 145.848 93.898  133.474 1.00 53.31  ? 262  GLU B N   1 
ATOM   12015 C  CA  . GLU B 2 579  ? 146.799 93.240  132.595 1.00 65.16  ? 262  GLU B CA  1 
ATOM   12016 C  C   . GLU B 2 579  ? 146.153 92.865  131.270 1.00 71.70  ? 262  GLU B C   1 
ATOM   12017 O  O   . GLU B 2 579  ? 146.741 93.063  130.198 1.00 76.35  ? 262  GLU B O   1 
ATOM   12018 C  CB  . GLU B 2 579  ? 147.388 92.016  133.289 1.00 75.85  ? 262  GLU B CB  1 
ATOM   12019 C  CG  . GLU B 2 579  ? 148.482 91.337  132.458 1.00 92.61  ? 262  GLU B CG  1 
ATOM   12020 C  CD  . GLU B 2 579  ? 149.699 92.236  132.195 1.00 104.73 ? 262  GLU B CD  1 
ATOM   12021 O  OE1 . GLU B 2 579  ? 150.127 92.325  131.018 1.00 106.38 ? 262  GLU B OE1 1 
ATOM   12022 O  OE2 . GLU B 2 579  ? 150.231 92.842  133.155 1.00 97.65  ? 262  GLU B OE2 1 
ATOM   12023 N  N   . PHE B 2 580  ? 144.932 92.353  131.330 1.00 68.73  ? 263  PHE B N   1 
ATOM   12024 C  CA  . PHE B 2 580  ? 144.216 91.936  130.132 1.00 65.83  ? 263  PHE B CA  1 
ATOM   12025 C  C   . PHE B 2 580  ? 143.972 93.120  129.200 1.00 60.59  ? 263  PHE B C   1 
ATOM   12026 O  O   . PHE B 2 580  ? 144.304 93.071  128.012 1.00 65.16  ? 263  PHE B O   1 
ATOM   12027 C  CB  . PHE B 2 580  ? 142.911 91.272  130.571 1.00 66.87  ? 263  PHE B CB  1 
ATOM   12028 C  CG  . PHE B 2 580  ? 142.048 90.811  129.458 1.00 69.36  ? 263  PHE B CG  1 
ATOM   12029 C  CD1 . PHE B 2 580  ? 142.485 89.852  128.571 1.00 73.29  ? 263  PHE B CD1 1 
ATOM   12030 C  CD2 . PHE B 2 580  ? 140.780 91.355  129.295 1.00 77.51  ? 263  PHE B CD2 1 
ATOM   12031 C  CE1 . PHE B 2 580  ? 141.667 89.424  127.528 1.00 77.73  ? 263  PHE B CE1 1 
ATOM   12032 C  CE2 . PHE B 2 580  ? 139.954 90.944  128.264 1.00 80.39  ? 263  PHE B CE2 1 
ATOM   12033 C  CZ  . PHE B 2 580  ? 140.399 89.969  127.373 1.00 79.89  ? 263  PHE B CZ  1 
ATOM   12034 N  N   . GLN B 2 581  ? 143.406 94.202  129.735 1.00 66.52  ? 264  GLN B N   1 
ATOM   12035 C  CA  . GLN B 2 581  ? 143.143 95.387  128.929 1.00 68.29  ? 264  GLN B CA  1 
ATOM   12036 C  C   . GLN B 2 581  ? 144.423 95.926  128.327 1.00 67.16  ? 264  GLN B C   1 
ATOM   12037 O  O   . GLN B 2 581  ? 144.448 96.318  127.155 1.00 75.19  ? 264  GLN B O   1 
ATOM   12038 C  CB  . GLN B 2 581  ? 142.478 96.478  129.778 1.00 69.70  ? 264  GLN B CB  1 
ATOM   12039 C  CG  . GLN B 2 581  ? 141.073 96.182  130.253 1.00 72.00  ? 264  GLN B CG  1 
ATOM   12040 C  CD  . GLN B 2 581  ? 140.029 96.381  129.166 1.00 82.87  ? 264  GLN B CD  1 
ATOM   12041 O  OE1 . GLN B 2 581  ? 138.905 95.876  129.269 1.00 77.63  ? 264  GLN B OE1 1 
ATOM   12042 N  NE2 . GLN B 2 581  ? 140.379 97.162  128.139 1.00 79.74  ? 264  GLN B NE2 1 
ATOM   12043 N  N   . ALA B 2 582  ? 145.488 96.002  129.122 1.00 64.30  ? 265  ALA B N   1 
ATOM   12044 C  CA  . ALA B 2 582  ? 146.729 96.513  128.575 1.00 65.68  ? 265  ALA B CA  1 
ATOM   12045 C  C   . ALA B 2 582  ? 147.201 95.618  127.445 1.00 71.43  ? 265  ALA B C   1 
ATOM   12046 O  O   . ALA B 2 582  ? 147.697 96.104  126.419 1.00 78.22  ? 265  ALA B O   1 
ATOM   12047 C  CB  . ALA B 2 582  ? 147.788 96.631  129.670 1.00 65.42  ? 265  ALA B CB  1 
ATOM   12048 N  N   . SER B 2 583  ? 147.023 94.306  127.593 1.00 60.37  ? 266  SER B N   1 
ATOM   12049 C  CA  . SER B 2 583  ? 147.461 93.426  126.522 1.00 70.18  ? 266  SER B CA  1 
ATOM   12050 C  C   . SER B 2 583  ? 146.624 93.644  125.267 1.00 76.12  ? 266  SER B C   1 
ATOM   12051 O  O   . SER B 2 583  ? 147.161 93.673  124.153 1.00 80.65  ? 266  SER B O   1 
ATOM   12052 C  CB  . SER B 2 583  ? 147.416 91.968  126.970 1.00 78.96  ? 266  SER B CB  1 
ATOM   12053 O  OG  . SER B 2 583  ? 147.980 91.124  125.974 1.00 79.63  ? 266  SER B OG  1 
ATOM   12054 N  N   . LEU B 2 584  ? 145.309 93.822  125.430 1.00 71.64  ? 267  LEU B N   1 
ATOM   12055 C  CA  . LEU B 2 584  ? 144.453 94.079  124.274 1.00 62.32  ? 267  LEU B CA  1 
ATOM   12056 C  C   . LEU B 2 584  ? 144.894 95.335  123.556 1.00 63.49  ? 267  LEU B C   1 
ATOM   12057 O  O   . LEU B 2 584  ? 145.030 95.352  122.328 1.00 67.39  ? 267  LEU B O   1 
ATOM   12058 C  CB  . LEU B 2 584  ? 143.007 94.243  124.708 1.00 47.41  ? 267  LEU B CB  1 
ATOM   12059 C  CG  . LEU B 2 584  ? 142.420 92.953  125.211 1.00 61.75  ? 267  LEU B CG  1 
ATOM   12060 C  CD1 . LEU B 2 584  ? 140.935 93.149  125.458 1.00 71.62  ? 267  LEU B CD1 1 
ATOM   12061 C  CD2 . LEU B 2 584  ? 142.700 91.847  124.215 1.00 68.17  ? 267  LEU B CD2 1 
ATOM   12062 N  N   . ALA B 2 585  ? 145.135 96.392  124.320 1.00 63.51  ? 268  ALA B N   1 
ATOM   12063 C  CA  . ALA B 2 585  ? 145.521 97.655  123.725 1.00 67.81  ? 268  ALA B CA  1 
ATOM   12064 C  C   . ALA B 2 585  ? 146.827 97.509  122.968 1.00 76.06  ? 268  ALA B C   1 
ATOM   12065 O  O   . ALA B 2 585  ? 146.970 98.036  121.859 1.00 83.98  ? 268  ALA B O   1 
ATOM   12066 C  CB  . ALA B 2 585  ? 145.634 98.731  124.806 1.00 69.85  ? 268  ALA B CB  1 
ATOM   12067 N  N   . GLU B 2 586  ? 147.783 96.773  123.531 1.00 78.14  ? 269  GLU B N   1 
ATOM   12068 C  CA  . GLU B 2 586  ? 149.093 96.706  122.889 1.00 90.90  ? 269  GLU B CA  1 
ATOM   12069 C  C   . GLU B 2 586  ? 149.107 95.714  121.727 1.00 92.47  ? 269  GLU B C   1 
ATOM   12070 O  O   . GLU B 2 586  ? 149.998 94.861  121.650 1.00 95.45  ? 269  GLU B O   1 
ATOM   12071 C  CB  . GLU B 2 586  ? 150.186 96.345  123.913 1.00 96.10  ? 269  GLU B CB  1 
ATOM   12072 C  CG  . GLU B 2 586  ? 150.673 97.503  124.821 1.00 105.71 ? 269  GLU B CG  1 
ATOM   12073 C  CD  . GLU B 2 586  ? 151.318 98.667  124.054 1.00 110.87 ? 269  GLU B CD  1 
ATOM   12074 O  OE1 . GLU B 2 586  ? 150.798 99.805  124.136 1.00 108.21 ? 269  GLU B OE1 1 
ATOM   12075 O  OE2 . GLU B 2 586  ? 152.359 98.446  123.394 1.00 104.95 ? 269  GLU B OE2 1 
ATOM   12076 N  N   . GLY B 2 587  ? 148.138 95.827  120.813 1.00 89.68  ? 270  GLY B N   1 
ATOM   12077 C  CA  . GLY B 2 587  ? 148.141 95.083  119.564 1.00 85.27  ? 270  GLY B CA  1 
ATOM   12078 C  C   . GLY B 2 587  ? 148.217 93.576  119.697 1.00 77.23  ? 270  GLY B C   1 
ATOM   12079 O  O   . GLY B 2 587  ? 148.958 92.925  118.955 1.00 82.06  ? 270  GLY B O   1 
ATOM   12080 N  N   . ASP B 2 588  ? 147.463 93.005  120.631 1.00 69.60  ? 271  ASP B N   1 
ATOM   12081 C  CA  . ASP B 2 588  ? 147.500 91.575  120.876 1.00 68.46  ? 271  ASP B CA  1 
ATOM   12082 C  C   . ASP B 2 588  ? 146.096 91.008  120.796 1.00 67.76  ? 271  ASP B C   1 
ATOM   12083 O  O   . ASP B 2 588  ? 145.120 91.675  121.141 1.00 74.78  ? 271  ASP B O   1 
ATOM   12084 C  CB  . ASP B 2 588  ? 148.100 91.232  122.252 1.00 84.23  ? 271  ASP B CB  1 
ATOM   12085 C  CG  . ASP B 2 588  ? 149.562 91.648  122.381 1.00 96.80  ? 271  ASP B CG  1 
ATOM   12086 O  OD1 . ASP B 2 588  ? 150.293 91.592  121.365 1.00 95.03  ? 271  ASP B OD1 1 
ATOM   12087 O  OD2 . ASP B 2 588  ? 149.985 92.015  123.502 1.00 94.02  ? 271  ASP B OD2 1 
ATOM   12088 N  N   . SER B 2 589  ? 146.007 89.775  120.340 1.00 64.34  ? 272  SER B N   1 
ATOM   12089 C  CA  . SER B 2 589  ? 144.746 89.063  120.333 1.00 61.08  ? 272  SER B CA  1 
ATOM   12090 C  C   . SER B 2 589  ? 144.409 88.575  121.738 1.00 61.61  ? 272  SER B C   1 
ATOM   12091 O  O   . SER B 2 589  ? 145.281 88.514  122.607 1.00 69.20  ? 272  SER B O   1 
ATOM   12092 C  CB  . SER B 2 589  ? 144.821 87.891  119.361 1.00 73.54  ? 272  SER B CB  1 
ATOM   12093 O  OG  . SER B 2 589  ? 145.839 86.976  119.742 1.00 79.31  ? 272  SER B OG  1 
ATOM   12094 N  N   . PRO B 2 590  ? 143.141 88.242  121.990 1.00 56.87  ? 273  PRO B N   1 
ATOM   12095 C  CA  . PRO B 2 590  ? 142.759 87.733  123.319 1.00 55.33  ? 273  PRO B CA  1 
ATOM   12096 C  C   . PRO B 2 590  ? 143.471 86.458  123.742 1.00 69.56  ? 273  PRO B C   1 
ATOM   12097 O  O   . PRO B 2 590  ? 143.653 86.251  124.950 1.00 75.58  ? 273  PRO B O   1 
ATOM   12098 C  CB  . PRO B 2 590  ? 141.255 87.510  123.183 1.00 55.34  ? 273  PRO B CB  1 
ATOM   12099 C  CG  . PRO B 2 590  ? 140.849 88.495  122.161 1.00 64.50  ? 273  PRO B CG  1 
ATOM   12100 C  CD  . PRO B 2 590  ? 141.967 88.569  121.174 1.00 63.89  ? 273  PRO B CD  1 
ATOM   12101 N  N   . GLN B 2 591  ? 143.878 85.591  122.813 1.00 68.19  ? 274  GLN B N   1 
ATOM   12102 C  CA  . GLN B 2 591  ? 144.704 84.451  123.207 1.00 72.91  ? 274  GLN B CA  1 
ATOM   12103 C  C   . GLN B 2 591  ? 146.038 84.911  123.787 1.00 76.01  ? 274  GLN B C   1 
ATOM   12104 O  O   . GLN B 2 591  ? 146.477 84.423  124.842 1.00 80.39  ? 274  GLN B O   1 
ATOM   12105 C  CB  . GLN B 2 591  ? 144.933 83.514  122.023 1.00 74.59  ? 274  GLN B CB  1 
ATOM   12106 C  CG  . GLN B 2 591  ? 143.663 83.003  121.402 1.00 77.11  ? 274  GLN B CG  1 
ATOM   12107 C  CD  . GLN B 2 591  ? 143.106 83.974  120.404 1.00 82.26  ? 274  GLN B CD  1 
ATOM   12108 O  OE1 . GLN B 2 591  ? 143.770 84.945  120.041 1.00 83.99  ? 274  GLN B OE1 1 
ATOM   12109 N  NE2 . GLN B 2 591  ? 141.876 83.737  119.962 1.00 82.92  ? 274  GLN B NE2 1 
ATOM   12110 N  N   . CYS B 2 592  ? 146.704 85.848  123.110 1.00 68.63  ? 275  CYS B N   1 
ATOM   12111 C  CA  . CYS B 2 592  ? 147.947 86.377  123.654 1.00 68.90  ? 275  CYS B CA  1 
ATOM   12112 C  C   . CYS B 2 592  ? 147.701 87.040  124.998 1.00 71.69  ? 275  CYS B C   1 
ATOM   12113 O  O   . CYS B 2 592  ? 148.539 86.957  125.905 1.00 80.19  ? 275  CYS B O   1 
ATOM   12114 C  CB  . CYS B 2 592  ? 148.577 87.371  122.679 1.00 80.79  ? 275  CYS B CB  1 
ATOM   12115 S  SG  . CYS B 2 592  ? 148.880 86.720  121.017 1.00 103.04 ? 275  CYS B SG  1 
ATOM   12116 N  N   . ALA B 2 593  ? 146.548 87.694  125.148 1.00 72.26  ? 276  ALA B N   1 
ATOM   12117 C  CA  . ALA B 2 593  ? 146.229 88.376  126.397 1.00 76.18  ? 276  ALA B CA  1 
ATOM   12118 C  C   . ALA B 2 593  ? 146.081 87.391  127.546 1.00 66.97  ? 276  ALA B C   1 
ATOM   12119 O  O   . ALA B 2 593  ? 146.587 87.635  128.644 1.00 75.50  ? 276  ALA B O   1 
ATOM   12120 C  CB  . ALA B 2 593  ? 144.959 89.210  126.232 1.00 77.16  ? 276  ALA B CB  1 
ATOM   12121 N  N   . LEU B 2 594  ? 145.412 86.268  127.314 1.00 61.77  ? 277  LEU B N   1 
ATOM   12122 C  CA  . LEU B 2 594  ? 145.318 85.254  128.358 1.00 62.95  ? 277  LEU B CA  1 
ATOM   12123 C  C   . LEU B 2 594  ? 146.677 84.641  128.698 1.00 76.46  ? 277  LEU B C   1 
ATOM   12124 O  O   . LEU B 2 594  ? 147.006 84.464  129.877 1.00 82.12  ? 277  LEU B O   1 
ATOM   12125 C  CB  . LEU B 2 594  ? 144.327 84.170  127.955 1.00 77.88  ? 277  LEU B CB  1 
ATOM   12126 C  CG  . LEU B 2 594  ? 142.893 84.405  128.413 1.00 79.36  ? 277  LEU B CG  1 
ATOM   12127 C  CD1 . LEU B 2 594  ? 142.954 84.431  129.899 1.00 73.51  ? 277  LEU B CD1 1 
ATOM   12128 C  CD2 . LEU B 2 594  ? 142.303 85.700  127.907 1.00 75.25  ? 277  LEU B CD2 1 
ATOM   12129 N  N   . ILE B 2 595  ? 147.486 84.280  127.695 1.00 78.73  ? 278  ILE B N   1 
ATOM   12130 C  CA  . ILE B 2 595  ? 148.745 83.628  128.070 1.00 73.13  ? 278  ILE B CA  1 
ATOM   12131 C  C   . ILE B 2 595  ? 149.649 84.605  128.822 1.00 75.19  ? 278  ILE B C   1 
ATOM   12132 O  O   . ILE B 2 595  ? 150.313 84.232  129.800 1.00 82.98  ? 278  ILE B O   1 
ATOM   12133 C  CB  . ILE B 2 595  ? 149.457 82.987  126.861 1.00 75.56  ? 278  ILE B CB  1 
ATOM   12134 C  CG1 . ILE B 2 595  ? 149.874 84.021  125.807 1.00 82.06  ? 278  ILE B CG1 1 
ATOM   12135 C  CG2 . ILE B 2 595  ? 148.583 81.897  126.255 1.00 85.75  ? 278  ILE B CG2 1 
ATOM   12136 C  CD1 . ILE B 2 595  ? 150.596 83.422  124.591 1.00 74.69  ? 278  ILE B CD1 1 
ATOM   12137 N  N   . GLN B 2 596  ? 149.670 85.876  128.415 1.00 76.31  ? 279  GLN B N   1 
ATOM   12138 C  CA  . GLN B 2 596  ? 150.481 86.829  129.163 1.00 79.71  ? 279  GLN B CA  1 
ATOM   12139 C  C   . GLN B 2 596  ? 149.868 87.140  130.524 1.00 80.40  ? 279  GLN B C   1 
ATOM   12140 O  O   . GLN B 2 596  ? 150.594 87.500  131.457 1.00 88.54  ? 279  GLN B O   1 
ATOM   12141 C  CB  . GLN B 2 596  ? 150.697 88.117  128.355 1.00 84.94  ? 279  GLN B CB  1 
ATOM   12142 C  CG  . GLN B 2 596  ? 151.565 87.968  127.093 1.00 88.71  ? 279  GLN B CG  1 
ATOM   12143 C  CD  . GLN B 2 596  ? 151.714 89.289  126.330 1.00 99.56  ? 279  GLN B CD  1 
ATOM   12144 O  OE1 . GLN B 2 596  ? 151.129 90.305  126.713 1.00 93.26  ? 279  GLN B OE1 1 
ATOM   12145 N  NE2 . GLN B 2 596  ? 152.493 89.275  125.244 1.00 103.69 ? 279  GLN B NE2 1 
ATOM   12146 N  N   . ILE B 2 597  ? 148.548 87.010  130.665 1.00 75.26  ? 280  ILE B N   1 
ATOM   12147 C  CA  . ILE B 2 597  ? 147.927 87.306  131.949 1.00 75.87  ? 280  ILE B CA  1 
ATOM   12148 C  C   . ILE B 2 597  ? 148.216 86.175  132.908 1.00 71.76  ? 280  ILE B C   1 
ATOM   12149 O  O   . ILE B 2 597  ? 148.105 86.353  134.125 1.00 78.19  ? 280  ILE B O   1 
ATOM   12150 C  CB  . ILE B 2 597  ? 146.408 87.517  131.794 1.00 82.31  ? 280  ILE B CB  1 
ATOM   12151 C  CG1 . ILE B 2 597  ? 145.773 88.161  133.004 1.00 74.07  ? 280  ILE B CG1 1 
ATOM   12152 C  CG2 . ILE B 2 597  ? 145.649 86.202  131.795 1.00 79.64  ? 280  ILE B CG2 1 
ATOM   12153 C  CD1 . ILE B 2 597  ? 144.395 88.615  132.643 1.00 70.88  ? 280  ILE B CD1 1 
ATOM   12154 N  N   . THR B 2 598  ? 148.570 85.010  132.372 1.00 72.82  ? 281  THR B N   1 
ATOM   12155 C  CA  . THR B 2 598  ? 148.971 83.905  133.224 1.00 73.03  ? 281  THR B CA  1 
ATOM   12156 C  C   . THR B 2 598  ? 150.454 84.004  133.573 1.00 79.17  ? 281  THR B C   1 
ATOM   12157 O  O   . THR B 2 598  ? 150.844 83.708  134.704 1.00 86.58  ? 281  THR B O   1 
ATOM   12158 C  CB  . THR B 2 598  ? 148.656 82.576  132.540 1.00 81.43  ? 281  THR B CB  1 
ATOM   12159 O  OG1 . THR B 2 598  ? 147.275 82.555  132.159 1.00 84.18  ? 281  THR B OG1 1 
ATOM   12160 C  CG2 . THR B 2 598  ? 148.858 81.452  133.531 1.00 93.97  ? 281  THR B CG2 1 
ATOM   12161 N  N   . LYS B 2 599  ? 151.302 84.399  132.613 1.00 85.63  ? 282  LYS B N   1 
ATOM   12162 C  CA  . LYS B 2 599  ? 152.709 84.697  132.922 1.00 84.75  ? 282  LYS B CA  1 
ATOM   12163 C  C   . LYS B 2 599  ? 152.856 85.797  133.969 1.00 80.29  ? 282  LYS B C   1 
ATOM   12164 O  O   . LYS B 2 599  ? 153.361 85.559  135.071 1.00 81.76  ? 282  LYS B O   1 
ATOM   12165 C  CB  . LYS B 2 599  ? 153.490 85.066  131.648 1.00 84.34  ? 282  LYS B CB  1 
ATOM   12166 C  CG  . LYS B 2 599  ? 153.602 84.017  130.522 1.00 86.03  ? 282  LYS B CG  1 
ATOM   12167 C  CD  . LYS B 2 599  ? 154.553 82.865  130.948 1.00 99.84  ? 282  LYS B CD  1 
ATOM   12168 C  CE  . LYS B 2 599  ? 153.894 81.648  131.584 1.00 111.49 ? 282  LYS B CE  1 
ATOM   12169 N  NZ  . LYS B 2 599  ? 154.883 80.549  131.861 1.00 113.81 ? 282  LYS B NZ  1 
ATOM   12170 N  N   . ARG B 2 600  ? 152.415 87.010  133.642 1.00 81.30  ? 283  ARG B N   1 
ATOM   12171 C  CA  . ARG B 2 600  ? 152.878 88.184  134.375 1.00 84.24  ? 283  ARG B CA  1 
ATOM   12172 C  C   . ARG B 2 600  ? 152.227 88.348  135.739 1.00 77.30  ? 283  ARG B C   1 
ATOM   12173 O  O   . ARG B 2 600  ? 152.871 88.856  136.659 1.00 81.72  ? 283  ARG B O   1 
ATOM   12174 C  CB  . ARG B 2 600  ? 152.657 89.449  133.546 1.00 90.04  ? 283  ARG B CB  1 
ATOM   12175 C  CG  . ARG B 2 600  ? 153.632 89.589  132.396 1.00 90.13  ? 283  ARG B CG  1 
ATOM   12176 C  CD  . ARG B 2 600  ? 153.514 90.950  131.748 1.00 102.54 ? 283  ARG B CD  1 
ATOM   12177 N  NE  . ARG B 2 600  ? 154.583 91.165  130.773 1.00 121.14 ? 283  ARG B NE  1 
ATOM   12178 C  CZ  . ARG B 2 600  ? 154.723 92.259  130.025 1.00 122.19 ? 283  ARG B CZ  1 
ATOM   12179 N  NH1 . ARG B 2 600  ? 153.862 93.264  130.139 1.00 114.79 ? 283  ARG B NH1 1 
ATOM   12180 N  NH2 . ARG B 2 600  ? 155.739 92.351  129.172 1.00 116.06 ? 283  ARG B NH2 1 
ATOM   12181 N  N   . VAL B 2 601  ? 150.974 87.959  135.897 1.00 75.63  ? 284  VAL B N   1 
ATOM   12182 C  CA  . VAL B 2 601  ? 150.325 88.155  137.198 1.00 79.40  ? 284  VAL B CA  1 
ATOM   12183 C  C   . VAL B 2 601  ? 151.016 87.280  138.241 1.00 85.09  ? 284  VAL B C   1 
ATOM   12184 O  O   . VAL B 2 601  ? 151.199 86.069  138.016 1.00 89.41  ? 284  VAL B O   1 
ATOM   12185 C  CB  . VAL B 2 601  ? 148.834 87.840  137.103 1.00 92.27  ? 284  VAL B CB  1 
ATOM   12186 C  CG1 . VAL B 2 601  ? 148.200 87.810  138.492 1.00 91.59  ? 284  VAL B CG1 1 
ATOM   12187 C  CG2 . VAL B 2 601  ? 148.132 88.867  136.208 1.00 91.96  ? 284  VAL B CG2 1 
ATOM   12188 N  N   . PRO B 2 602  ? 151.434 87.841  139.378 1.00 82.03  ? 285  PRO B N   1 
ATOM   12189 C  CA  . PRO B 2 602  ? 152.244 87.065  140.331 1.00 76.98  ? 285  PRO B CA  1 
ATOM   12190 C  C   . PRO B 2 602  ? 151.505 85.925  141.016 1.00 85.64  ? 285  PRO B C   1 
ATOM   12191 O  O   . PRO B 2 602  ? 152.164 84.972  141.442 1.00 94.78  ? 285  PRO B O   1 
ATOM   12192 C  CB  . PRO B 2 602  ? 152.697 88.121  141.346 1.00 85.47  ? 285  PRO B CB  1 
ATOM   12193 C  CG  . PRO B 2 602  ? 151.658 89.195  141.262 1.00 96.27  ? 285  PRO B CG  1 
ATOM   12194 C  CD  . PRO B 2 602  ? 151.199 89.223  139.826 1.00 91.06  ? 285  PRO B CD  1 
ATOM   12195 N  N   . ILE B 2 603  ? 150.175 85.978  141.149 1.00 88.09  ? 286  ILE B N   1 
ATOM   12196 C  CA  . ILE B 2 603  ? 149.442 84.886  141.796 1.00 83.49  ? 286  ILE B CA  1 
ATOM   12197 C  C   . ILE B 2 603  ? 149.629 83.599  141.024 1.00 72.83  ? 286  ILE B C   1 
ATOM   12198 O  O   . ILE B 2 603  ? 149.488 82.504  141.574 1.00 79.56  ? 286  ILE B O   1 
ATOM   12199 C  CB  . ILE B 2 603  ? 147.937 85.224  141.925 1.00 86.94  ? 286  ILE B CB  1 
ATOM   12200 C  CG1 . ILE B 2 603  ? 147.725 86.586  142.632 1.00 93.86  ? 286  ILE B CG1 1 
ATOM   12201 C  CG2 . ILE B 2 603  ? 147.163 84.078  142.601 1.00 77.76  ? 286  ILE B CG2 1 
ATOM   12202 C  CD1 . ILE B 2 603  ? 148.352 86.713  144.030 1.00 88.38  ? 286  ILE B CD1 1 
ATOM   12203 N  N   . PHE B 2 604  ? 149.950 83.709  139.748 1.00 75.09  ? 287  PHE B N   1 
ATOM   12204 C  CA  . PHE B 2 604  ? 150.193 82.559  138.899 1.00 88.49  ? 287  PHE B CA  1 
ATOM   12205 C  C   . PHE B 2 604  ? 151.667 82.209  138.804 1.00 105.44 ? 287  PHE B C   1 
ATOM   12206 O  O   . PHE B 2 604  ? 152.103 81.666  137.779 1.00 108.87 ? 287  PHE B O   1 
ATOM   12207 C  CB  . PHE B 2 604  ? 149.628 82.821  137.507 1.00 97.02  ? 287  PHE B CB  1 
ATOM   12208 C  CG  . PHE B 2 604  ? 148.192 83.257  137.501 1.00 95.11  ? 287  PHE B CG  1 
ATOM   12209 C  CD1 . PHE B 2 604  ? 147.287 82.732  138.408 1.00 98.54  ? 287  PHE B CD1 1 
ATOM   12210 C  CD2 . PHE B 2 604  ? 147.746 84.193  136.578 1.00 94.51  ? 287  PHE B CD2 1 
ATOM   12211 C  CE1 . PHE B 2 604  ? 145.962 83.136  138.397 1.00 93.81  ? 287  PHE B CE1 1 
ATOM   12212 C  CE2 . PHE B 2 604  ? 146.421 84.604  136.563 1.00 95.64  ? 287  PHE B CE2 1 
ATOM   12213 C  CZ  . PHE B 2 604  ? 145.528 84.072  137.475 1.00 95.34  ? 287  PHE B CZ  1 
ATOM   12214 N  N   . GLN B 2 605  ? 152.452 82.517  139.840 1.00 108.27 ? 288  GLN B N   1 
ATOM   12215 C  CA  . GLN B 2 605  ? 153.893 82.267  139.794 1.00 117.36 ? 288  GLN B CA  1 
ATOM   12216 C  C   . GLN B 2 605  ? 154.191 80.786  139.569 1.00 116.92 ? 288  GLN B C   1 
ATOM   12217 O  O   . GLN B 2 605  ? 154.880 80.413  138.613 1.00 115.94 ? 288  GLN B O   1 
ATOM   12218 C  CB  . GLN B 2 605  ? 154.547 82.766  141.092 1.00 122.05 ? 288  GLN B CB  1 
ATOM   12219 C  CG  . GLN B 2 605  ? 156.049 82.473  141.232 1.00 129.30 ? 288  GLN B CG  1 
ATOM   12220 C  CD  . GLN B 2 605  ? 156.888 83.083  140.114 1.00 130.01 ? 288  GLN B CD  1 
ATOM   12221 O  OE1 . GLN B 2 605  ? 157.496 82.365  139.315 1.00 128.18 ? 288  GLN B OE1 1 
ATOM   12222 N  NE2 . GLN B 2 605  ? 156.940 84.414  140.069 1.00 125.70 ? 288  GLN B NE2 1 
ATOM   12223 N  N   . ASP B 2 606  ? 153.679 79.922  140.452 1.00 113.55 ? 289  ASP B N   1 
ATOM   12224 C  CA  . ASP B 2 606  ? 153.946 78.494  140.356 1.00 114.77 ? 289  ASP B CA  1 
ATOM   12225 C  C   . ASP B 2 606  ? 152.728 77.652  140.726 1.00 110.13 ? 289  ASP B C   1 
ATOM   12226 O  O   . ASP B 2 606  ? 152.867 76.433  140.889 1.00 113.62 ? 289  ASP B O   1 
ATOM   12227 C  CB  . ASP B 2 606  ? 155.151 78.123  141.251 1.00 125.22 ? 289  ASP B CB  1 
ATOM   12228 C  CG  . ASP B 2 606  ? 155.846 76.832  140.816 1.00 126.10 ? 289  ASP B CG  1 
ATOM   12229 O  OD1 . ASP B 2 606  ? 156.441 76.820  139.715 1.00 125.43 ? 289  ASP B OD1 1 
ATOM   12230 O  OD2 . ASP B 2 606  ? 155.816 75.842  141.583 1.00 121.29 ? 289  ASP B OD2 1 
ATOM   12231 N  N   . ALA B 2 607  ? 151.550 78.257  140.868 1.00 105.68 ? 290  ALA B N   1 
ATOM   12232 C  CA  . ALA B 2 607  ? 150.374 77.514  141.302 1.00 98.77  ? 290  ALA B CA  1 
ATOM   12233 C  C   . ALA B 2 607  ? 150.084 76.369  140.344 1.00 94.79  ? 290  ALA B C   1 
ATOM   12234 O  O   . ALA B 2 607  ? 150.200 76.510  139.125 1.00 102.82 ? 290  ALA B O   1 
ATOM   12235 C  CB  . ALA B 2 607  ? 149.160 78.443  141.397 1.00 103.36 ? 290  ALA B CB  1 
ATOM   12236 N  N   . ALA B 2 608  ? 149.735 75.231  140.900 1.00 95.40  ? 291  ALA B N   1 
ATOM   12237 C  CA  . ALA B 2 608  ? 149.397 74.082  140.080 1.00 98.22  ? 291  ALA B CA  1 
ATOM   12238 C  C   . ALA B 2 608  ? 147.990 74.238  139.502 1.00 89.96  ? 291  ALA B C   1 
ATOM   12239 O  O   . ALA B 2 608  ? 147.165 74.973  140.050 1.00 94.37  ? 291  ALA B O   1 
ATOM   12240 C  CB  . ALA B 2 608  ? 149.488 72.797  140.903 1.00 101.92 ? 291  ALA B CB  1 
ATOM   12241 N  N   . PRO B 2 609  ? 147.702 73.584  138.383 1.00 91.17  ? 292  PRO B N   1 
ATOM   12242 C  CA  . PRO B 2 609  ? 146.352 73.635  137.821 1.00 82.94  ? 292  PRO B CA  1 
ATOM   12243 C  C   . PRO B 2 609  ? 145.349 73.056  138.794 1.00 82.94  ? 292  PRO B C   1 
ATOM   12244 O  O   . PRO B 2 609  ? 145.624 72.047  139.456 1.00 95.50  ? 292  PRO B O   1 
ATOM   12245 C  CB  . PRO B 2 609  ? 146.452 72.758  136.566 1.00 98.13  ? 292  PRO B CB  1 
ATOM   12246 C  CG  . PRO B 2 609  ? 147.895 72.724  136.235 1.00 110.64 ? 292  PRO B CG  1 
ATOM   12247 C  CD  . PRO B 2 609  ? 148.618 72.795  137.545 1.00 108.50 ? 292  PRO B CD  1 
ATOM   12248 N  N   . PRO B 2 610  ? 144.179 73.653  138.906 1.00 84.30  ? 293  PRO B N   1 
ATOM   12249 C  CA  . PRO B 2 610  ? 143.127 73.041  139.714 1.00 85.50  ? 293  PRO B CA  1 
ATOM   12250 C  C   . PRO B 2 610  ? 142.588 71.795  139.032 1.00 104.26 ? 293  PRO B C   1 
ATOM   12251 O  O   . PRO B 2 610  ? 142.654 71.644  137.809 1.00 107.93 ? 293  PRO B O   1 
ATOM   12252 C  CB  . PRO B 2 610  ? 142.067 74.138  139.805 1.00 93.74  ? 293  PRO B CB  1 
ATOM   12253 C  CG  . PRO B 2 610  ? 142.269 74.932  138.553 1.00 99.46  ? 293  PRO B CG  1 
ATOM   12254 C  CD  . PRO B 2 610  ? 143.741 74.895  138.256 1.00 92.75  ? 293  PRO B CD  1 
ATOM   12255 N  N   . VAL B 2 611  ? 142.074 70.884  139.847 1.00 105.97 ? 294  VAL B N   1 
ATOM   12256 C  CA  . VAL B 2 611  ? 141.451 69.657  139.369 1.00 108.82 ? 294  VAL B CA  1 
ATOM   12257 C  C   . VAL B 2 611  ? 139.950 69.880  139.293 1.00 112.57 ? 294  VAL B C   1 
ATOM   12258 O  O   . VAL B 2 611  ? 139.350 70.494  140.186 1.00 111.46 ? 294  VAL B O   1 
ATOM   12259 C  CB  . VAL B 2 611  ? 141.789 68.458  140.279 1.00 122.74 ? 294  VAL B CB  1 
ATOM   12260 C  CG1 . VAL B 2 611  ? 143.260 68.087  140.158 1.00 122.37 ? 294  VAL B CG1 1 
ATOM   12261 C  CG2 . VAL B 2 611  ? 141.427 68.749  141.736 1.00 119.79 ? 294  VAL B CG2 1 
ATOM   12262 N  N   . ILE B 2 612  ? 139.337 69.391  138.222 1.00 124.23 ? 295  ILE B N   1 
ATOM   12263 C  CA  . ILE B 2 612  ? 137.895 69.494  138.029 1.00 137.00 ? 295  ILE B CA  1 
ATOM   12264 C  C   . ILE B 2 612  ? 137.350 68.081  137.860 1.00 140.22 ? 295  ILE B C   1 
ATOM   12265 O  O   . ILE B 2 612  ? 137.717 67.377  136.910 1.00 137.24 ? 295  ILE B O   1 
ATOM   12266 C  CB  . ILE B 2 612  ? 137.533 70.389  136.826 1.00 139.56 ? 295  ILE B CB  1 
ATOM   12267 C  CG1 . ILE B 2 612  ? 138.030 71.833  137.027 1.00 129.61 ? 295  ILE B CG1 1 
ATOM   12268 C  CG2 . ILE B 2 612  ? 136.023 70.381  136.567 1.00 136.24 ? 295  ILE B CG2 1 
ATOM   12269 C  CD1 . ILE B 2 612  ? 139.416 72.134  136.465 1.00 119.56 ? 295  ILE B CD1 1 
ATOM   12270 N  N   . HIS B 2 613  ? 136.483 67.663  138.783 1.00 141.44 ? 296  HIS B N   1 
ATOM   12271 C  CA  . HIS B 2 613  ? 135.879 66.340  138.705 1.00 141.21 ? 296  HIS B CA  1 
ATOM   12272 C  C   . HIS B 2 613  ? 134.782 66.334  137.643 1.00 142.63 ? 296  HIS B C   1 
ATOM   12273 O  O   . HIS B 2 613  ? 133.918 67.218  137.622 1.00 140.66 ? 296  HIS B O   1 
ATOM   12274 C  CB  . HIS B 2 613  ? 135.306 65.915  140.063 1.00 143.86 ? 296  HIS B CB  1 
ATOM   12275 C  CG  . HIS B 2 613  ? 134.159 66.761  140.540 1.00 149.14 ? 296  HIS B CG  1 
ATOM   12276 N  ND1 . HIS B 2 613  ? 134.336 67.968  141.184 1.00 149.53 ? 296  HIS B ND1 1 
ATOM   12277 C  CD2 . HIS B 2 613  ? 132.819 66.569  140.465 1.00 147.43 ? 296  HIS B CD2 1 
ATOM   12278 C  CE1 . HIS B 2 613  ? 133.156 68.482  141.486 1.00 146.26 ? 296  HIS B CE1 1 
ATOM   12279 N  NE2 . HIS B 2 613  ? 132.219 67.653  141.059 1.00 147.61 ? 296  HIS B NE2 1 
ATOM   12280 N  N   . ILE B 2 614  ? 134.827 65.341  136.756 1.00 147.11 ? 297  ILE B N   1 
ATOM   12281 C  CA  . ILE B 2 614  ? 133.802 65.139  135.737 1.00 149.20 ? 297  ILE B CA  1 
ATOM   12282 C  C   . ILE B 2 614  ? 133.428 63.659  135.710 1.00 143.14 ? 297  ILE B C   1 
ATOM   12283 O  O   . ILE B 2 614  ? 134.294 62.782  135.814 1.00 139.57 ? 297  ILE B O   1 
ATOM   12284 C  CB  . ILE B 2 614  ? 134.259 65.625  134.337 1.00 148.03 ? 297  ILE B CB  1 
ATOM   12285 C  CG1 . ILE B 2 614  ? 135.648 65.071  133.981 1.00 148.89 ? 297  ILE B CG1 1 
ATOM   12286 C  CG2 . ILE B 2 614  ? 134.224 67.163  134.252 1.00 136.71 ? 297  ILE B CG2 1 
ATOM   12287 C  CD1 . ILE B 2 614  ? 136.115 65.413  132.567 1.00 140.28 ? 297  ILE B CD1 1 
ATOM   12288 N  N   . ARG B 2 615  ? 132.127 63.387  135.586 1.00 136.34 ? 298  ARG B N   1 
ATOM   12289 C  CA  . ARG B 2 615  ? 131.658 62.008  135.595 1.00 131.89 ? 298  ARG B CA  1 
ATOM   12290 C  C   . ARG B 2 615  ? 132.183 61.224  134.393 1.00 137.71 ? 298  ARG B C   1 
ATOM   12291 O  O   . ARG B 2 615  ? 132.375 60.006  134.489 1.00 137.51 ? 298  ARG B O   1 
ATOM   12292 C  CB  . ARG B 2 615  ? 130.126 61.990  135.656 1.00 131.55 ? 298  ARG B CB  1 
ATOM   12293 C  CG  . ARG B 2 615  ? 129.439 62.772  134.534 1.00 136.61 ? 298  ARG B CG  1 
ATOM   12294 C  CD  . ARG B 2 615  ? 127.987 63.128  134.869 1.00 135.28 ? 298  ARG B CD  1 
ATOM   12295 N  NE  . ARG B 2 615  ? 127.852 63.838  136.146 1.00 135.72 ? 298  ARG B NE  1 
ATOM   12296 C  CZ  . ARG B 2 615  ? 128.066 65.143  136.316 1.00 135.23 ? 298  ARG B CZ  1 
ATOM   12297 N  NH1 . ARG B 2 615  ? 128.429 65.905  135.290 1.00 135.40 ? 298  ARG B NH1 1 
ATOM   12298 N  NH2 . ARG B 2 615  ? 127.914 65.691  137.516 1.00 126.26 ? 298  ARG B NH2 1 
ATOM   12299 N  N   . SER B 2 616  ? 132.451 61.896  133.271 1.00 132.45 ? 299  SER B N   1 
ATOM   12300 C  CA  . SER B 2 616  ? 132.915 61.216  132.069 1.00 124.90 ? 299  SER B CA  1 
ATOM   12301 C  C   . SER B 2 616  ? 133.770 62.166  131.248 1.00 121.46 ? 299  SER B C   1 
ATOM   12302 O  O   . SER B 2 616  ? 133.772 63.378  131.468 1.00 126.07 ? 299  SER B O   1 
ATOM   12303 C  CB  . SER B 2 616  ? 131.748 60.698  131.214 1.00 124.34 ? 299  SER B CB  1 
ATOM   12304 O  OG  . SER B 2 616  ? 130.898 61.756  130.806 1.00 123.64 ? 299  SER B OG  1 
ATOM   12305 N  N   . ARG B 2 617  ? 134.501 61.592  130.290 1.00 119.07 ? 300  ARG B N   1 
ATOM   12306 C  CA  . ARG B 2 617  ? 135.348 62.381  129.406 1.00 114.07 ? 300  ARG B CA  1 
ATOM   12307 C  C   . ARG B 2 617  ? 134.554 63.181  128.380 1.00 113.31 ? 300  ARG B C   1 
ATOM   12308 O  O   . ARG B 2 617  ? 135.129 64.056  127.725 1.00 114.71 ? 300  ARG B O   1 
ATOM   12309 C  CB  . ARG B 2 617  ? 136.336 61.482  128.677 1.00 104.63 ? 300  ARG B CB  1 
ATOM   12310 C  CG  . ARG B 2 617  ? 137.541 62.230  128.168 1.00 109.10 ? 300  ARG B CG  1 
ATOM   12311 C  CD  . ARG B 2 617  ? 138.118 61.534  126.970 1.00 110.26 ? 300  ARG B CD  1 
ATOM   12312 N  NE  . ARG B 2 617  ? 137.082 61.371  125.957 1.00 103.07 ? 300  ARG B NE  1 
ATOM   12313 C  CZ  . ARG B 2 617  ? 136.669 62.343  125.154 1.00 102.91 ? 300  ARG B CZ  1 
ATOM   12314 N  NH1 . ARG B 2 617  ? 137.207 63.546  125.251 1.00 110.67 ? 300  ARG B NH1 1 
ATOM   12315 N  NH2 . ARG B 2 617  ? 135.721 62.114  124.257 1.00 99.86  ? 300  ARG B NH2 1 
ATOM   12316 N  N   . GLY B 2 618  ? 133.262 62.902  128.215 1.00 117.18 ? 301  GLY B N   1 
ATOM   12317 C  CA  . GLY B 2 618  ? 132.407 63.654  127.315 1.00 123.45 ? 301  GLY B CA  1 
ATOM   12318 C  C   . GLY B 2 618  ? 131.835 64.950  127.859 1.00 131.55 ? 301  GLY B C   1 
ATOM   12319 O  O   . GLY B 2 618  ? 131.127 65.650  127.128 1.00 130.57 ? 301  GLY B O   1 
ATOM   12320 N  N   . ASP B 2 619  ? 132.116 65.289  129.127 1.00 133.77 ? 302  ASP B N   1 
ATOM   12321 C  CA  . ASP B 2 619  ? 131.604 66.528  129.722 1.00 138.58 ? 302  ASP B CA  1 
ATOM   12322 C  C   . ASP B 2 619  ? 132.276 67.770  129.140 1.00 132.44 ? 302  ASP B C   1 
ATOM   12323 O  O   . ASP B 2 619  ? 131.646 68.834  129.062 1.00 126.04 ? 302  ASP B O   1 
ATOM   12324 C  CB  . ASP B 2 619  ? 131.789 66.506  131.246 1.00 146.36 ? 302  ASP B CB  1 
ATOM   12325 C  CG  . ASP B 2 619  ? 130.938 65.440  131.939 1.00 144.87 ? 302  ASP B CG  1 
ATOM   12326 O  OD1 . ASP B 2 619  ? 129.789 65.196  131.506 1.00 139.68 ? 302  ASP B OD1 1 
ATOM   12327 O  OD2 . ASP B 2 619  ? 131.427 64.843  132.924 1.00 141.51 ? 302  ASP B OD2 1 
ATOM   12328 N  N   . ILE B 2 620  ? 133.548 67.667  128.760 1.00 130.16 ? 303  ILE B N   1 
ATOM   12329 C  CA  . ILE B 2 620  ? 134.275 68.772  128.139 1.00 125.27 ? 303  ILE B CA  1 
ATOM   12330 C  C   . ILE B 2 620  ? 133.644 69.056  126.784 1.00 120.19 ? 303  ILE B C   1 
ATOM   12331 O  O   . ILE B 2 620  ? 133.205 68.123  126.095 1.00 124.14 ? 303  ILE B O   1 
ATOM   12332 C  CB  . ILE B 2 620  ? 135.771 68.453  127.989 1.00 125.31 ? 303  ILE B CB  1 
ATOM   12333 C  CG1 . ILE B 2 620  ? 135.964 67.212  127.113 1.00 126.11 ? 303  ILE B CG1 1 
ATOM   12334 C  CG2 . ILE B 2 620  ? 136.416 68.259  129.362 1.00 131.19 ? 303  ILE B CG2 1 
ATOM   12335 C  CD1 . ILE B 2 620  ? 137.411 66.828  126.884 1.00 127.32 ? 303  ILE B CD1 1 
ATOM   12336 N  N   . PRO B 2 621  ? 133.575 70.309  126.359 1.00 117.35 ? 304  PRO B N   1 
ATOM   12337 C  CA  . PRO B 2 621  ? 132.928 70.610  125.082 1.00 118.84 ? 304  PRO B CA  1 
ATOM   12338 C  C   . PRO B 2 621  ? 133.749 70.086  123.922 1.00 115.46 ? 304  PRO B C   1 
ATOM   12339 O  O   . PRO B 2 621  ? 134.925 69.743  124.055 1.00 116.39 ? 304  PRO B O   1 
ATOM   12340 C  CB  . PRO B 2 621  ? 132.855 72.139  125.066 1.00 120.73 ? 304  PRO B CB  1 
ATOM   12341 C  CG  . PRO B 2 621  ? 133.978 72.561  125.950 1.00 123.46 ? 304  PRO B CG  1 
ATOM   12342 C  CD  . PRO B 2 621  ? 134.100 71.514  127.019 1.00 120.72 ? 304  PRO B CD  1 
ATOM   12343 N  N   . ARG B 2 622  ? 133.088 70.015  122.766 1.00 119.42 ? 305  ARG B N   1 
ATOM   12344 C  CA  . ARG B 2 622  ? 133.740 69.500  121.567 1.00 125.26 ? 305  ARG B CA  1 
ATOM   12345 C  C   . ARG B 2 622  ? 134.953 70.347  121.184 1.00 122.35 ? 305  ARG B C   1 
ATOM   12346 O  O   . ARG B 2 622  ? 135.973 69.810  120.738 1.00 121.40 ? 305  ARG B O   1 
ATOM   12347 C  CB  . ARG B 2 622  ? 132.734 69.426  120.413 1.00 130.72 ? 305  ARG B CB  1 
ATOM   12348 C  CG  . ARG B 2 622  ? 131.625 68.379  120.590 1.00 131.93 ? 305  ARG B CG  1 
ATOM   12349 C  CD  . ARG B 2 622  ? 130.688 68.324  119.375 1.00 136.90 ? 305  ARG B CD  1 
ATOM   12350 N  NE  . ARG B 2 622  ? 129.909 69.557  119.218 1.00 138.76 ? 305  ARG B NE  1 
ATOM   12351 C  CZ  . ARG B 2 622  ? 128.696 69.761  119.733 1.00 134.29 ? 305  ARG B CZ  1 
ATOM   12352 N  NH1 . ARG B 2 622  ? 128.098 68.811  120.442 1.00 130.74 ? 305  ARG B NH1 1 
ATOM   12353 N  NH2 . ARG B 2 622  ? 128.077 70.920  119.536 1.00 126.42 ? 305  ARG B NH2 1 
ATOM   12354 N  N   . ALA B 2 623  ? 134.866 71.672  121.346 1.00 118.05 ? 306  ALA B N   1 
ATOM   12355 C  CA  . ALA B 2 623  ? 136.015 72.518  121.038 1.00 105.17 ? 306  ALA B CA  1 
ATOM   12356 C  C   . ALA B 2 623  ? 137.177 72.254  121.984 1.00 100.63 ? 306  ALA B C   1 
ATOM   12357 O  O   . ALA B 2 623  ? 138.313 72.614  121.668 1.00 100.81 ? 306  ALA B O   1 
ATOM   12358 C  CB  . ALA B 2 623  ? 135.622 73.998  121.078 1.00 95.72  ? 306  ALA B CB  1 
ATOM   12359 N  N   . CYS B 2 624  ? 136.914 71.636  123.133 1.00 105.41 ? 307  CYS B N   1 
ATOM   12360 C  CA  . CYS B 2 624  ? 137.944 71.304  124.109 1.00 117.87 ? 307  CYS B CA  1 
ATOM   12361 C  C   . CYS B 2 624  ? 138.617 69.956  123.834 1.00 127.37 ? 307  CYS B C   1 
ATOM   12362 O  O   . CYS B 2 624  ? 139.634 69.639  124.466 1.00 123.10 ? 307  CYS B O   1 
ATOM   12363 C  CB  . CYS B 2 624  ? 137.329 71.311  125.519 1.00 124.38 ? 307  CYS B CB  1 
ATOM   12364 S  SG  . CYS B 2 624  ? 138.500 71.318  126.909 1.00 142.29 ? 307  CYS B SG  1 
ATOM   12365 N  N   . GLN B 2 625  ? 138.094 69.169  122.894 1.00 122.84 ? 308  GLN B N   1 
ATOM   12366 C  CA  . GLN B 2 625  ? 138.620 67.833  122.646 1.00 114.05 ? 308  GLN B CA  1 
ATOM   12367 C  C   . GLN B 2 625  ? 139.960 67.859  121.921 1.00 108.60 ? 308  GLN B C   1 
ATOM   12368 O  O   . GLN B 2 625  ? 140.633 66.828  121.860 1.00 111.58 ? 308  GLN B O   1 
ATOM   12369 C  CB  . GLN B 2 625  ? 137.623 67.033  121.804 1.00 121.67 ? 308  GLN B CB  1 
ATOM   12370 C  CG  . GLN B 2 625  ? 136.215 66.924  122.382 1.00 121.70 ? 308  GLN B CG  1 
ATOM   12371 C  CD  . GLN B 2 625  ? 136.130 66.005  123.570 1.00 121.62 ? 308  GLN B CD  1 
ATOM   12372 O  OE1 . GLN B 2 625  ? 137.085 65.300  123.888 1.00 122.10 ? 308  GLN B OE1 1 
ATOM   12373 N  NE2 . GLN B 2 625  ? 134.974 65.990  124.226 1.00 121.38 ? 308  GLN B NE2 1 
ATOM   12374 N  N   . LYS B 2 626  ? 140.340 68.992  121.329 1.00 105.88 ? 309  LYS B N   1 
ATOM   12375 C  CA  . LYS B 2 626  ? 141.479 68.995  120.418 1.00 105.39 ? 309  LYS B CA  1 
ATOM   12376 C  C   . LYS B 2 626  ? 142.788 68.807  121.170 1.00 104.23 ? 309  LYS B C   1 
ATOM   12377 O  O   . LYS B 2 626  ? 143.532 67.854  120.917 1.00 111.47 ? 309  LYS B O   1 
ATOM   12378 C  CB  . LYS B 2 626  ? 141.511 70.285  119.590 1.00 109.08 ? 309  LYS B CB  1 
ATOM   12379 C  CG  . LYS B 2 626  ? 141.137 71.568  120.334 1.00 117.46 ? 309  LYS B CG  1 
ATOM   12380 C  CD  . LYS B 2 626  ? 141.310 72.808  119.438 1.00 122.21 ? 309  LYS B CD  1 
ATOM   12381 C  CE  . LYS B 2 626  ? 140.661 74.069  120.033 1.00 117.51 ? 309  LYS B CE  1 
ATOM   12382 N  NZ  . LYS B 2 626  ? 139.167 73.997  120.094 1.00 106.00 ? 309  LYS B NZ  1 
ATOM   12383 N  N   . SER B 2 627  ? 143.087 69.697  122.092 1.00 97.84  ? 310  SER B N   1 
ATOM   12384 C  CA  . SER B 2 627  ? 144.394 69.719  122.726 1.00 97.34  ? 310  SER B CA  1 
ATOM   12385 C  C   . SER B 2 627  ? 144.213 69.311  124.183 1.00 107.80 ? 310  SER B C   1 
ATOM   12386 O  O   . SER B 2 627  ? 143.749 70.104  125.007 1.00 112.30 ? 310  SER B O   1 
ATOM   12387 C  CB  . SER B 2 627  ? 145.026 71.096  122.581 1.00 103.15 ? 310  SER B CB  1 
ATOM   12388 O  OG  . SER B 2 627  ? 146.322 71.131  123.145 1.00 110.54 ? 310  SER B OG  1 
ATOM   12389 N  N   . LEU B 2 628  ? 144.557 68.061  124.487 1.00 112.73 ? 311  LEU B N   1 
ATOM   12390 C  CA  . LEU B 2 628  ? 144.576 67.552  125.854 1.00 114.62 ? 311  LEU B CA  1 
ATOM   12391 C  C   . LEU B 2 628  ? 145.434 66.295  125.896 1.00 115.33 ? 311  LEU B C   1 
ATOM   12392 O  O   . LEU B 2 628  ? 145.382 65.470  124.981 1.00 118.31 ? 311  LEU B O   1 
ATOM   12393 C  CB  . LEU B 2 628  ? 143.156 67.279  126.390 1.00 118.14 ? 311  LEU B CB  1 
ATOM   12394 C  CG  . LEU B 2 628  ? 142.272 66.122  125.915 1.00 121.83 ? 311  LEU B CG  1 
ATOM   12395 C  CD1 . LEU B 2 628  ? 141.067 65.952  126.824 1.00 122.52 ? 311  LEU B CD1 1 
ATOM   12396 C  CD2 . LEU B 2 628  ? 141.782 66.407  124.525 1.00 112.45 ? 311  LEU B CD2 1 
ATOM   12397 N  N   . ARG B 2 629  ? 146.232 66.169  126.948 1.00 121.04 ? 312  ARG B N   1 
ATOM   12398 C  CA  . ARG B 2 629  ? 147.194 65.083  127.085 1.00 130.50 ? 312  ARG B CA  1 
ATOM   12399 C  C   . ARG B 2 629  ? 147.230 64.616  128.534 1.00 136.85 ? 312  ARG B C   1 
ATOM   12400 O  O   . ARG B 2 629  ? 146.796 65.343  129.434 1.00 136.25 ? 312  ARG B O   1 
ATOM   12401 C  CB  . ARG B 2 629  ? 148.594 65.519  126.620 1.00 124.46 ? 312  ARG B CB  1 
ATOM   12402 C  CG  . ARG B 2 629  ? 148.815 65.371  125.124 1.00 123.37 ? 312  ARG B CG  1 
ATOM   12403 C  CD  . ARG B 2 629  ? 149.946 66.254  124.637 1.00 126.86 ? 312  ARG B CD  1 
ATOM   12404 N  NE  . ARG B 2 629  ? 149.603 67.671  124.766 1.00 131.25 ? 312  ARG B NE  1 
ATOM   12405 C  CZ  . ARG B 2 629  ? 148.887 68.356  123.876 1.00 129.52 ? 312  ARG B CZ  1 
ATOM   12406 N  NH1 . ARG B 2 629  ? 148.422 67.757  122.786 1.00 124.88 ? 312  ARG B NH1 1 
ATOM   12407 N  NH2 . ARG B 2 629  ? 148.624 69.642  124.076 1.00 127.85 ? 312  ARG B NH2 1 
ATOM   12408 N  N   . PRO B 2 630  ? 147.712 63.396  128.791 1.00 132.68 ? 313  PRO B N   1 
ATOM   12409 C  CA  . PRO B 2 630  ? 147.762 62.908  130.180 1.00 128.45 ? 313  PRO B CA  1 
ATOM   12410 C  C   . PRO B 2 630  ? 148.625 63.805  131.055 1.00 123.97 ? 313  PRO B C   1 
ATOM   12411 O  O   . PRO B 2 630  ? 149.641 64.341  130.612 1.00 127.36 ? 313  PRO B O   1 
ATOM   12412 C  CB  . PRO B 2 630  ? 148.360 61.501  130.043 1.00 133.28 ? 313  PRO B CB  1 
ATOM   12413 C  CG  . PRO B 2 630  ? 148.994 61.470  128.669 1.00 132.87 ? 313  PRO B CG  1 
ATOM   12414 C  CD  . PRO B 2 630  ? 148.141 62.363  127.829 1.00 130.91 ? 313  PRO B CD  1 
ATOM   12415 N  N   . VAL B 2 631  ? 148.210 63.969  132.307 1.00 124.12 ? 314  VAL B N   1 
ATOM   12416 C  CA  . VAL B 2 631  ? 148.831 64.943  133.208 1.00 131.84 ? 314  VAL B CA  1 
ATOM   12417 C  C   . VAL B 2 631  ? 150.216 64.497  133.680 1.00 134.58 ? 314  VAL B C   1 
ATOM   12418 O  O   . VAL B 2 631  ? 150.363 63.386  134.210 1.00 134.84 ? 314  VAL B O   1 
ATOM   12419 C  CB  . VAL B 2 631  ? 147.888 65.252  134.387 1.00 138.08 ? 314  VAL B CB  1 
ATOM   12420 C  CG1 . VAL B 2 631  ? 147.537 63.990  135.169 1.00 137.29 ? 314  VAL B CG1 1 
ATOM   12421 C  CG2 . VAL B 2 631  ? 148.525 66.281  135.318 1.00 138.61 ? 314  VAL B CG2 1 
ATOM   12422 N  N   . PRO B 2 632  ? 151.262 65.300  133.466 1.00 138.03 ? 315  PRO B N   1 
ATOM   12423 C  CA  . PRO B 2 632  ? 152.585 64.988  134.048 1.00 143.35 ? 315  PRO B CA  1 
ATOM   12424 C  C   . PRO B 2 632  ? 152.659 65.433  135.498 1.00 147.07 ? 315  PRO B C   1 
ATOM   12425 O  O   . PRO B 2 632  ? 151.894 66.316  135.919 1.00 144.40 ? 315  PRO B O   1 
ATOM   12426 C  CB  . PRO B 2 632  ? 153.564 65.791  133.172 1.00 138.77 ? 315  PRO B CB  1 
ATOM   12427 C  CG  . PRO B 2 632  ? 152.787 66.168  131.950 1.00 138.81 ? 315  PRO B CG  1 
ATOM   12428 C  CD  . PRO B 2 632  ? 151.368 66.333  132.426 1.00 138.53 ? 315  PRO B CD  1 
ATOM   12429 N  N   . PRO B 2 633  ? 153.565 64.853  136.292 1.00 152.41 ? 316  PRO B N   1 
ATOM   12430 C  CA  . PRO B 2 633  ? 153.666 65.245  137.705 1.00 153.30 ? 316  PRO B CA  1 
ATOM   12431 C  C   . PRO B 2 633  ? 154.152 66.680  137.874 1.00 151.86 ? 316  PRO B C   1 
ATOM   12432 O  O   . PRO B 2 633  ? 154.920 67.204  137.061 1.00 148.56 ? 316  PRO B O   1 
ATOM   12433 C  CB  . PRO B 2 633  ? 154.672 64.239  138.285 1.00 150.30 ? 316  PRO B CB  1 
ATOM   12434 C  CG  . PRO B 2 633  ? 155.484 63.795  137.106 1.00 148.36 ? 316  PRO B CG  1 
ATOM   12435 C  CD  . PRO B 2 633  ? 154.521 63.782  135.946 1.00 149.94 ? 316  PRO B CD  1 
ATOM   12436 N  N   . SER B 2 634  ? 153.680 67.314  138.962 1.00 152.12 ? 317  SER B N   1 
ATOM   12437 C  CA  . SER B 2 634  ? 153.969 68.694  139.357 1.00 151.41 ? 317  SER B CA  1 
ATOM   12438 C  C   . SER B 2 634  ? 153.825 69.667  138.186 1.00 149.06 ? 317  SER B C   1 
ATOM   12439 O  O   . SER B 2 634  ? 154.834 70.207  137.708 1.00 145.48 ? 317  SER B O   1 
ATOM   12440 C  CB  . SER B 2 634  ? 155.374 68.802  139.970 1.00 144.43 ? 317  SER B CB  1 
ATOM   12441 O  OG  . SER B 2 634  ? 156.394 68.539  139.018 1.00 141.56 ? 317  SER B OG  1 
ATOM   12442 N  N   . PRO B 2 635  ? 152.610 69.927  137.700 1.00 141.95 ? 318  PRO B N   1 
ATOM   12443 C  CA  . PRO B 2 635  ? 152.443 70.906  136.624 1.00 133.46 ? 318  PRO B CA  1 
ATOM   12444 C  C   . PRO B 2 635  ? 152.213 72.314  137.160 1.00 123.02 ? 318  PRO B C   1 
ATOM   12445 O  O   . PRO B 2 635  ? 151.798 72.524  138.300 1.00 120.76 ? 318  PRO B O   1 
ATOM   12446 C  CB  . PRO B 2 635  ? 151.202 70.389  135.872 1.00 130.32 ? 318  PRO B CB  1 
ATOM   12447 C  CG  . PRO B 2 635  ? 150.525 69.367  136.814 1.00 129.90 ? 318  PRO B CG  1 
ATOM   12448 C  CD  . PRO B 2 635  ? 151.308 69.369  138.109 1.00 136.64 ? 318  PRO B CD  1 
ATOM   12449 N  N   . LYS B 2 636  ? 152.518 73.282  136.307 1.00 121.36 ? 319  LYS B N   1 
ATOM   12450 C  CA  . LYS B 2 636  ? 152.176 74.689  136.478 1.00 123.95 ? 319  LYS B CA  1 
ATOM   12451 C  C   . LYS B 2 636  ? 151.024 75.059  135.535 1.00 125.93 ? 319  LYS B C   1 
ATOM   12452 O  O   . LYS B 2 636  ? 150.671 74.306  134.624 1.00 127.39 ? 319  LYS B O   1 
ATOM   12453 C  CB  . LYS B 2 636  ? 153.420 75.568  136.250 1.00 128.00 ? 319  LYS B CB  1 
ATOM   12454 C  CG  . LYS B 2 636  ? 153.150 77.067  136.290 1.00 131.52 ? 319  LYS B CG  1 
ATOM   12455 C  CD  . LYS B 2 636  ? 154.384 77.886  136.017 1.00 132.65 ? 319  LYS B CD  1 
ATOM   12456 C  CE  . LYS B 2 636  ? 154.006 79.350  135.926 1.00 127.08 ? 319  LYS B CE  1 
ATOM   12457 N  NZ  . LYS B 2 636  ? 153.124 79.516  134.707 1.00 116.32 ? 319  LYS B NZ  1 
ATOM   12458 N  N   . ILE B 2 637  ? 150.402 76.217  135.774 1.00 114.99 ? 320  ILE B N   1 
ATOM   12459 C  CA  . ILE B 2 637  ? 149.238 76.589  134.978 1.00 108.75 ? 320  ILE B CA  1 
ATOM   12460 C  C   . ILE B 2 637  ? 149.604 77.088  133.586 1.00 112.24 ? 320  ILE B C   1 
ATOM   12461 O  O   . ILE B 2 637  ? 148.817 76.917  132.647 1.00 114.36 ? 320  ILE B O   1 
ATOM   12462 C  CB  . ILE B 2 637  ? 148.390 77.601  135.752 1.00 107.43 ? 320  ILE B CB  1 
ATOM   12463 C  CG1 . ILE B 2 637  ? 149.231 78.796  136.158 1.00 112.07 ? 320  ILE B CG1 1 
ATOM   12464 C  CG2 . ILE B 2 637  ? 147.706 76.957  136.938 1.00 110.75 ? 320  ILE B CG2 1 
ATOM   12465 C  CD1 . ILE B 2 637  ? 148.378 79.812  136.792 1.00 116.02 ? 320  ILE B CD1 1 
ATOM   12466 N  N   . ASP B 2 638  ? 150.765 77.702  133.395 1.00 110.12 ? 321  ASP B N   1 
ATOM   12467 C  CA  . ASP B 2 638  ? 151.105 78.011  132.013 1.00 115.85 ? 321  ASP B CA  1 
ATOM   12468 C  C   . ASP B 2 638  ? 152.430 77.427  131.572 1.00 112.65 ? 321  ASP B C   1 
ATOM   12469 O  O   . ASP B 2 638  ? 152.514 76.862  130.476 1.00 113.70 ? 321  ASP B O   1 
ATOM   12470 C  CB  . ASP B 2 638  ? 151.116 79.524  131.774 1.00 119.39 ? 321  ASP B CB  1 
ATOM   12471 C  CG  . ASP B 2 638  ? 151.041 79.878  130.284 1.00 118.36 ? 321  ASP B CG  1 
ATOM   12472 O  OD1 . ASP B 2 638  ? 150.818 78.949  129.471 1.00 118.24 ? 321  ASP B OD1 1 
ATOM   12473 O  OD2 . ASP B 2 638  ? 151.176 81.073  129.925 1.00 105.63 ? 321  ASP B OD2 1 
ATOM   12474 N  N   . ARG B 2 639  ? 153.469 77.532  132.395 1.00 111.36 ? 322  ARG B N   1 
ATOM   12475 C  CA  . ARG B 2 639  ? 154.687 76.798  132.086 1.00 125.95 ? 322  ARG B CA  1 
ATOM   12476 C  C   . ARG B 2 639  ? 154.413 75.302  132.012 1.00 133.04 ? 322  ARG B C   1 
ATOM   12477 O  O   . ARG B 2 639  ? 155.136 74.567  131.328 1.00 132.39 ? 322  ARG B O   1 
ATOM   12478 C  CB  . ARG B 2 639  ? 155.765 77.106  133.124 1.00 134.39 ? 322  ARG B CB  1 
ATOM   12479 C  CG  . ARG B 2 639  ? 157.128 76.479  132.859 1.00 140.38 ? 322  ARG B CG  1 
ATOM   12480 C  CD  . ARG B 2 639  ? 157.794 77.033  131.608 1.00 140.65 ? 322  ARG B CD  1 
ATOM   12481 N  NE  . ARG B 2 639  ? 159.150 76.509  131.443 1.00 134.59 ? 322  ARG B NE  1 
ATOM   12482 C  CZ  . ARG B 2 639  ? 159.981 76.873  130.471 1.00 127.90 ? 322  ARG B CZ  1 
ATOM   12483 N  NH1 . ARG B 2 639  ? 161.195 76.342  130.403 1.00 121.69 ? 322  ARG B NH1 1 
ATOM   12484 N  NH2 . ARG B 2 639  ? 159.594 77.757  129.559 1.00 124.39 ? 322  ARG B NH2 1 
ATOM   12485 N  N   . GLY B 2 640  ? 153.365 74.839  132.694 1.00 134.60 ? 323  GLY B N   1 
ATOM   12486 C  CA  . GLY B 2 640  ? 152.915 73.463  132.608 1.00 137.90 ? 323  GLY B CA  1 
ATOM   12487 C  C   . GLY B 2 640  ? 151.679 73.312  131.737 1.00 139.07 ? 323  GLY B C   1 
ATOM   12488 O  O   . GLY B 2 640  ? 151.786 73.287  130.505 1.00 137.48 ? 323  GLY B O   1 
ATOM   12489 N  N   . TRP B 2 641  ? 150.496 73.210  132.356 1.00 134.80 ? 324  TRP B N   1 
ATOM   12490 C  CA  . TRP B 2 641  ? 149.264 72.965  131.617 1.00 133.22 ? 324  TRP B CA  1 
ATOM   12491 C  C   . TRP B 2 641  ? 148.123 73.789  132.211 1.00 114.56 ? 324  TRP B C   1 
ATOM   12492 O  O   . TRP B 2 641  ? 148.092 74.063  133.411 1.00 111.56 ? 324  TRP B O   1 
ATOM   12493 C  CB  . TRP B 2 641  ? 148.928 71.451  131.599 1.00 136.57 ? 324  TRP B CB  1 
ATOM   12494 C  CG  . TRP B 2 641  ? 150.149 70.572  131.302 1.00 143.10 ? 324  TRP B CG  1 
ATOM   12495 C  CD1 . TRP B 2 641  ? 150.995 70.000  132.219 1.00 144.24 ? 324  TRP B CD1 1 
ATOM   12496 C  CD2 . TRP B 2 641  ? 150.696 70.254  130.006 1.00 141.54 ? 324  TRP B CD2 1 
ATOM   12497 N  NE1 . TRP B 2 641  ? 152.002 69.316  131.574 1.00 146.26 ? 324  TRP B NE1 1 
ATOM   12498 C  CE2 . TRP B 2 641  ? 151.844 69.455  130.219 1.00 147.00 ? 324  TRP B CE2 1 
ATOM   12499 C  CE3 . TRP B 2 641  ? 150.315 70.549  128.691 1.00 135.54 ? 324  TRP B CE3 1 
ATOM   12500 C  CZ2 . TRP B 2 641  ? 152.612 68.949  129.164 1.00 147.39 ? 324  TRP B CZ2 1 
ATOM   12501 C  CZ3 . TRP B 2 641  ? 151.080 70.044  127.644 1.00 139.32 ? 324  TRP B CZ3 1 
ATOM   12502 C  CH2 . TRP B 2 641  ? 152.214 69.254  127.888 1.00 145.48 ? 324  TRP B CH2 1 
ATOM   12503 N  N   . VAL B 2 642  ? 147.183 74.170  131.343 1.00 108.87 ? 325  VAL B N   1 
ATOM   12504 C  CA  . VAL B 2 642  ? 146.098 75.074  131.722 1.00 97.87  ? 325  VAL B CA  1 
ATOM   12505 C  C   . VAL B 2 642  ? 145.350 74.542  132.926 1.00 85.78  ? 325  VAL B C   1 
ATOM   12506 O  O   . VAL B 2 642  ? 145.250 75.205  133.963 1.00 98.56  ? 325  VAL B O   1 
ATOM   12507 C  CB  . VAL B 2 642  ? 145.137 75.283  130.543 1.00 110.71 ? 325  VAL B CB  1 
ATOM   12508 C  CG1 . VAL B 2 642  ? 143.927 76.090  130.996 1.00 103.56 ? 325  VAL B CG1 1 
ATOM   12509 C  CG2 . VAL B 2 642  ? 145.857 75.971  129.387 1.00 115.36 ? 325  VAL B CG2 1 
ATOM   12510 N  N   . CYS B 2 643  ? 144.801 73.347  132.801 1.00 90.96  ? 326  CYS B N   1 
ATOM   12511 C  CA  . CYS B 2 643  ? 144.006 72.791  133.880 1.00 111.21 ? 326  CYS B CA  1 
ATOM   12512 C  C   . CYS B 2 643  ? 143.830 71.297  133.645 1.00 128.51 ? 326  CYS B C   1 
ATOM   12513 O  O   . CYS B 2 643  ? 143.932 70.818  132.511 1.00 124.78 ? 326  CYS B O   1 
ATOM   12514 C  CB  . CYS B 2 643  ? 142.669 73.521  133.979 1.00 108.69 ? 326  CYS B CB  1 
ATOM   12515 S  SG  . CYS B 2 643  ? 141.649 73.175  132.571 1.00 125.00 ? 326  CYS B SG  1 
ATOM   12516 N  N   . VAL B 2 644  ? 143.573 70.565  134.734 1.00 128.45 ? 327  VAL B N   1 
ATOM   12517 C  CA  . VAL B 2 644  ? 143.462 69.106  134.711 1.00 131.18 ? 327  VAL B CA  1 
ATOM   12518 C  C   . VAL B 2 644  ? 142.083 68.691  135.220 1.00 134.17 ? 327  VAL B C   1 
ATOM   12519 O  O   . VAL B 2 644  ? 141.675 69.078  136.322 1.00 126.22 ? 327  VAL B O   1 
ATOM   12520 C  CB  . VAL B 2 644  ? 144.584 68.433  135.529 1.00 131.52 ? 327  VAL B CB  1 
ATOM   12521 C  CG1 . VAL B 2 644  ? 145.938 68.671  134.870 1.00 128.24 ? 327  VAL B CG1 1 
ATOM   12522 C  CG2 . VAL B 2 644  ? 144.613 68.966  136.959 1.00 123.52 ? 327  VAL B CG2 1 
ATOM   12523 N  N   . PHE B 2 645  ? 141.365 67.905  134.406 1.00 138.56 ? 328  PHE B N   1 
ATOM   12524 C  CA  . PHE B 2 645  ? 140.058 67.350  134.772 1.00 139.57 ? 328  PHE B CA  1 
ATOM   12525 C  C   . PHE B 2 645  ? 140.277 65.907  135.218 1.00 145.43 ? 328  PHE B C   1 
ATOM   12526 O  O   . PHE B 2 645  ? 140.472 65.018  134.384 1.00 145.25 ? 328  PHE B O   1 
ATOM   12527 C  CB  . PHE B 2 645  ? 139.065 67.381  133.609 1.00 141.94 ? 328  PHE B CB  1 
ATOM   12528 C  CG  . PHE B 2 645  ? 139.000 68.690  132.853 1.00 147.89 ? 328  PHE B CG  1 
ATOM   12529 C  CD1 . PHE B 2 645  ? 138.513 69.847  133.457 1.00 144.20 ? 328  PHE B CD1 1 
ATOM   12530 C  CD2 . PHE B 2 645  ? 139.373 68.742  131.512 1.00 143.54 ? 328  PHE B CD2 1 
ATOM   12531 C  CE1 . PHE B 2 645  ? 138.438 71.046  132.746 1.00 138.47 ? 328  PHE B CE1 1 
ATOM   12532 C  CE2 . PHE B 2 645  ? 139.300 69.931  130.795 1.00 142.73 ? 328  PHE B CE2 1 
ATOM   12533 C  CZ  . PHE B 2 645  ? 138.831 71.086  131.412 1.00 137.32 ? 328  PHE B CZ  1 
ATOM   12534 N  N   . GLN B 2 646  ? 140.216 65.658  136.527 1.00 148.44 ? 329  GLN B N   1 
ATOM   12535 C  CA  . GLN B 2 646  ? 140.341 64.299  137.051 1.00 150.78 ? 329  GLN B CA  1 
ATOM   12536 C  C   . GLN B 2 646  ? 138.970 63.623  137.033 1.00 148.02 ? 329  GLN B C   1 
ATOM   12537 O  O   . GLN B 2 646  ? 138.038 64.064  137.718 1.00 143.66 ? 329  GLN B O   1 
ATOM   12538 C  CB  . GLN B 2 646  ? 140.956 64.299  138.456 1.00 149.96 ? 329  GLN B CB  1 
ATOM   12539 C  CG  . GLN B 2 646  ? 140.171 65.047  139.538 1.00 147.64 ? 329  GLN B CG  1 
ATOM   12540 C  CD  . GLN B 2 646  ? 139.285 64.130  140.364 1.00 146.63 ? 329  GLN B CD  1 
ATOM   12541 O  OE1 . GLN B 2 646  ? 139.383 62.905  140.271 1.00 142.92 ? 329  GLN B OE1 1 
ATOM   12542 N  NE2 . GLN B 2 646  ? 138.402 64.722  141.164 1.00 143.21 ? 329  GLN B NE2 1 
ATOM   12543 N  N   . LEU B 2 647  ? 138.834 62.579  136.218 1.00 143.55 ? 330  LEU B N   1 
ATOM   12544 C  CA  . LEU B 2 647  ? 137.564 61.874  136.174 1.00 143.69 ? 330  LEU B CA  1 
ATOM   12545 C  C   . LEU B 2 647  ? 137.402 61.020  137.428 1.00 145.77 ? 330  LEU B C   1 
ATOM   12546 O  O   . LEU B 2 647  ? 138.375 60.678  138.111 1.00 142.00 ? 330  LEU B O   1 
ATOM   12547 C  CB  . LEU B 2 647  ? 137.448 61.007  134.915 1.00 138.99 ? 330  LEU B CB  1 
ATOM   12548 C  CG  . LEU B 2 647  ? 137.172 61.685  133.567 1.00 135.49 ? 330  LEU B CG  1 
ATOM   12549 C  CD1 . LEU B 2 647  ? 138.418 62.385  133.028 1.00 135.75 ? 330  LEU B CD1 1 
ATOM   12550 C  CD2 . LEU B 2 647  ? 136.619 60.691  132.551 1.00 131.23 ? 330  LEU B CD2 1 
ATOM   12551 N  N   . GLN B 2 648  ? 136.144 60.692  137.741 1.00 143.01 ? 331  GLN B N   1 
ATOM   12552 C  CA  . GLN B 2 648  ? 135.869 59.879  138.922 1.00 140.06 ? 331  GLN B CA  1 
ATOM   12553 C  C   . GLN B 2 648  ? 136.464 58.479  138.803 1.00 138.80 ? 331  GLN B C   1 
ATOM   12554 O  O   . GLN B 2 648  ? 136.775 57.850  139.822 1.00 136.18 ? 331  GLN B O   1 
ATOM   12555 C  CB  . GLN B 2 648  ? 134.361 59.822  139.177 1.00 136.26 ? 331  GLN B CB  1 
ATOM   12556 C  CG  . GLN B 2 648  ? 133.524 59.383  137.990 1.00 135.30 ? 331  GLN B CG  1 
ATOM   12557 C  CD  . GLN B 2 648  ? 132.050 59.320  138.332 1.00 130.93 ? 331  GLN B CD  1 
ATOM   12558 O  OE1 . GLN B 2 648  ? 131.318 60.295  138.157 1.00 124.62 ? 331  GLN B OE1 1 
ATOM   12559 N  NE2 . GLN B 2 648  ? 131.604 58.166  138.821 1.00 127.37 ? 331  GLN B NE2 1 
ATOM   12560 N  N   . ASP B 2 649  ? 136.636 57.978  137.581 1.00 137.32 ? 332  ASP B N   1 
ATOM   12561 C  CA  . ASP B 2 649  ? 137.341 56.714  137.349 1.00 135.97 ? 332  ASP B CA  1 
ATOM   12562 C  C   . ASP B 2 649  ? 138.829 56.924  137.047 1.00 131.58 ? 332  ASP B C   1 
ATOM   12563 O  O   . ASP B 2 649  ? 139.376 56.406  136.072 1.00 128.21 ? 332  ASP B O   1 
ATOM   12564 C  CB  . ASP B 2 649  ? 136.647 55.931  136.237 1.00 137.21 ? 332  ASP B CB  1 
ATOM   12565 C  CG  . ASP B 2 649  ? 136.532 56.718  134.941 1.00 139.29 ? 332  ASP B CG  1 
ATOM   12566 O  OD1 . ASP B 2 649  ? 136.844 57.927  134.939 1.00 139.36 ? 332  ASP B OD1 1 
ATOM   12567 O  OD2 . ASP B 2 649  ? 136.126 56.124  133.920 1.00 135.35 ? 332  ASP B OD2 1 
ATOM   12568 N  N   . GLY B 2 650  ? 139.495 57.696  137.905 1.00 132.10 ? 333  GLY B N   1 
ATOM   12569 C  CA  . GLY B 2 650  ? 140.942 57.789  137.899 1.00 126.53 ? 333  GLY B CA  1 
ATOM   12570 C  C   . GLY B 2 650  ? 141.512 58.691  136.829 1.00 125.06 ? 333  GLY B C   1 
ATOM   12571 O  O   . GLY B 2 650  ? 142.511 59.381  137.053 1.00 125.63 ? 333  GLY B O   1 
ATOM   12572 N  N   . LYS B 2 651  ? 140.877 58.696  135.662 1.00 128.69 ? 334  LYS B N   1 
ATOM   12573 C  CA  . LYS B 2 651  ? 141.458 59.364  134.509 1.00 139.09 ? 334  LYS B CA  1 
ATOM   12574 C  C   . LYS B 2 651  ? 141.598 60.861  134.756 1.00 138.19 ? 334  LYS B C   1 
ATOM   12575 O  O   . LYS B 2 651  ? 140.767 61.485  135.422 1.00 135.37 ? 334  LYS B O   1 
ATOM   12576 C  CB  . LYS B 2 651  ? 140.617 59.102  133.250 1.00 147.08 ? 334  LYS B CB  1 
ATOM   12577 C  CG  . LYS B 2 651  ? 140.677 57.656  132.713 1.00 144.75 ? 334  LYS B CG  1 
ATOM   12578 C  CD  . LYS B 2 651  ? 139.836 57.470  131.432 1.00 140.48 ? 334  LYS B CD  1 
ATOM   12579 C  CE  . LYS B 2 651  ? 140.265 58.406  130.296 1.00 135.68 ? 334  LYS B CE  1 
ATOM   12580 N  NZ  . LYS B 2 651  ? 141.705 58.249  129.934 1.00 131.57 ? 334  LYS B NZ  1 
ATOM   12581 N  N   A THR B 2 652  ? 142.673 61.433  134.218 0.42 137.27 ? 335  THR B N   1 
ATOM   12582 N  N   B THR B 2 652  ? 142.681 61.430  134.228 0.58 138.29 ? 335  THR B N   1 
ATOM   12583 C  CA  A THR B 2 652  ? 142.949 62.857  134.339 0.42 135.52 ? 335  THR B CA  1 
ATOM   12584 C  CA  B THR B 2 652  ? 142.953 62.856  134.337 0.58 131.50 ? 335  THR B CA  1 
ATOM   12585 C  C   A THR B 2 652  ? 143.675 63.316  133.084 0.42 134.11 ? 335  THR B C   1 
ATOM   12586 C  C   B THR B 2 652  ? 143.679 63.317  133.081 0.58 129.67 ? 335  THR B C   1 
ATOM   12587 O  O   A THR B 2 652  ? 144.681 62.718  132.692 0.42 134.59 ? 335  THR B O   1 
ATOM   12588 O  O   B THR B 2 652  ? 144.682 62.717  132.681 0.58 132.13 ? 335  THR B O   1 
ATOM   12589 C  CB  A THR B 2 652  ? 143.795 63.157  135.580 0.42 134.18 ? 335  THR B CB  1 
ATOM   12590 C  CB  B THR B 2 652  ? 143.786 63.165  135.585 0.58 137.66 ? 335  THR B CB  1 
ATOM   12591 O  OG1 A THR B 2 652  ? 143.204 62.538  136.729 0.42 136.83 ? 335  THR B OG1 1 
ATOM   12592 O  OG1 B THR B 2 652  ? 143.177 62.555  136.729 0.58 136.33 ? 335  THR B OG1 1 
ATOM   12593 C  CG2 A THR B 2 652  ? 143.893 64.657  135.812 0.42 142.55 ? 335  THR B CG2 1 
ATOM   12594 C  CG2 B THR B 2 652  ? 143.876 64.664  135.809 0.58 138.01 ? 335  THR B CG2 1 
ATOM   12595 N  N   . LEU B 2 653  ? 143.157 64.370  132.458 1.00 136.49 ? 336  LEU B N   1 
ATOM   12596 C  CA  . LEU B 2 653  ? 143.720 64.910  131.229 1.00 139.30 ? 336  LEU B CA  1 
ATOM   12597 C  C   . LEU B 2 653  ? 143.869 66.421  131.403 1.00 142.92 ? 336  LEU B C   1 
ATOM   12598 O  O   . LEU B 2 653  ? 142.954 67.081  131.911 1.00 139.46 ? 336  LEU B O   1 
ATOM   12599 C  CB  . LEU B 2 653  ? 142.816 64.598  130.027 1.00 139.26 ? 336  LEU B CB  1 
ATOM   12600 C  CG  . LEU B 2 653  ? 142.870 63.237  129.312 1.00 137.84 ? 336  LEU B CG  1 
ATOM   12601 C  CD1 . LEU B 2 653  ? 144.227 63.008  128.677 1.00 134.59 ? 336  LEU B CD1 1 
ATOM   12602 C  CD2 . LEU B 2 653  ? 142.471 62.049  130.199 1.00 134.28 ? 336  LEU B CD2 1 
ATOM   12603 N  N   . GLY B 2 654  ? 145.020 66.968  131.008 1.00 139.87 ? 337  GLY B N   1 
ATOM   12604 C  CA  . GLY B 2 654  ? 145.298 68.390  131.137 1.00 131.69 ? 337  GLY B CA  1 
ATOM   12605 C  C   . GLY B 2 654  ? 145.323 69.093  129.791 1.00 123.37 ? 337  GLY B C   1 
ATOM   12606 O  O   . GLY B 2 654  ? 145.656 68.486  128.763 1.00 128.27 ? 337  GLY B O   1 
ATOM   12607 N  N   . LEU B 2 655  ? 144.976 70.378  129.802 1.00 111.45 ? 338  LEU B N   1 
ATOM   12608 C  CA  . LEU B 2 655  ? 144.862 71.169  128.587 1.00 107.97 ? 338  LEU B CA  1 
ATOM   12609 C  C   . LEU B 2 655  ? 146.126 71.970  128.336 1.00 106.25 ? 338  LEU B C   1 
ATOM   12610 O  O   . LEU B 2 655  ? 146.902 72.248  129.246 1.00 112.69 ? 338  LEU B O   1 
ATOM   12611 C  CB  . LEU B 2 655  ? 143.673 72.125  128.661 1.00 113.97 ? 338  LEU B CB  1 
ATOM   12612 C  CG  . LEU B 2 655  ? 142.306 71.502  128.919 1.00 121.52 ? 338  LEU B CG  1 
ATOM   12613 C  CD1 . LEU B 2 655  ? 141.247 72.592  128.947 1.00 122.40 ? 338  LEU B CD1 1 
ATOM   12614 C  CD2 . LEU B 2 655  ? 141.984 70.454  127.863 1.00 122.12 ? 338  LEU B CD2 1 
ATOM   12615 N  N   . LYS B 2 656  ? 146.306 72.367  127.084 1.00 107.64 ? 339  LYS B N   1 
ATOM   12616 C  CA  . LYS B 2 656  ? 147.443 73.184  126.700 1.00 116.35 ? 339  LYS B CA  1 
ATOM   12617 C  C   . LYS B 2 656  ? 146.994 74.181  125.646 1.00 125.49 ? 339  LYS B C   1 
ATOM   12618 O  O   . LYS B 2 656  ? 146.103 73.894  124.842 1.00 123.79 ? 339  LYS B O   1 
ATOM   12619 C  CB  . LYS B 2 656  ? 148.601 72.332  126.161 1.00 124.28 ? 339  LYS B CB  1 
ATOM   12620 C  CG  . LYS B 2 656  ? 149.899 73.100  125.911 1.00 128.47 ? 339  LYS B CG  1 
ATOM   12621 C  CD  . LYS B 2 656  ? 150.433 73.700  127.207 1.00 130.68 ? 339  LYS B CD  1 
ATOM   12622 C  CE  . LYS B 2 656  ? 151.713 74.487  126.986 1.00 129.15 ? 339  LYS B CE  1 
ATOM   12623 N  NZ  . LYS B 2 656  ? 152.215 75.068  128.267 1.00 125.79 ? 339  LYS B NZ  1 
ATOM   12624 N  N   . ILE B 2 657  ? 147.622 75.355  125.659 1.00 134.65 ? 340  ILE B N   1 
ATOM   12625 C  CA  . ILE B 2 657  ? 147.316 76.426  124.705 1.00 145.98 ? 340  ILE B CA  1 
ATOM   12626 C  C   . ILE B 2 657  ? 147.765 76.015  123.291 1.00 142.95 ? 340  ILE B C   1 
ATOM   12627 O  O   . ILE B 2 657  ? 148.811 75.384  123.111 1.00 137.68 ? 340  ILE B O   1 
ATOM   12628 C  CB  . ILE B 2 657  ? 147.976 77.776  125.148 1.00 139.85 ? 340  ILE B CB  1 
ATOM   12629 C  CG1 . ILE B 2 657  ? 147.480 78.210  126.541 1.00 132.78 ? 340  ILE B CG1 1 
ATOM   12630 C  CG2 . ILE B 2 657  ? 147.739 78.886  124.107 1.00 125.86 ? 340  ILE B CG2 1 
ATOM   12631 C  CD1 . ILE B 2 657  ? 145.967 78.418  126.650 1.00 122.57 ? 340  ILE B CD1 1 
ATOM   12632 O  OXT . ILE B 2 657  ? 147.091 76.294  122.292 1.00 134.93 ? 340  ILE B OXT 1 
ATOM   12633 N  N   . MET C 2 441  ? 132.527 147.846 175.618 1.00 112.40 ? 124  MET C N   1 
ATOM   12634 C  CA  . MET C 2 441  ? 132.415 146.532 176.239 1.00 106.94 ? 124  MET C CA  1 
ATOM   12635 C  C   . MET C 2 441  ? 133.087 145.476 175.379 1.00 98.14  ? 124  MET C C   1 
ATOM   12636 O  O   . MET C 2 441  ? 132.433 144.788 174.601 1.00 100.72 ? 124  MET C O   1 
ATOM   12637 C  CB  . MET C 2 441  ? 130.948 146.188 176.489 1.00 103.41 ? 124  MET C CB  1 
ATOM   12638 C  CG  . MET C 2 441  ? 130.303 147.177 177.467 1.00 117.33 ? 124  MET C CG  1 
ATOM   12639 S  SD  . MET C 2 441  ? 131.053 147.269 179.134 1.00 104.27 ? 124  MET C SD  1 
ATOM   12640 C  CE  . MET C 2 441  ? 132.146 148.679 179.004 1.00 64.19  ? 124  MET C CE  1 
ATOM   12641 N  N   . ALA C 2 442  ? 134.412 145.372 175.531 1.00 103.68 ? 125  ALA C N   1 
ATOM   12642 C  CA  . ALA C 2 442  ? 135.195 144.416 174.751 1.00 107.24 ? 125  ALA C CA  1 
ATOM   12643 C  C   . ALA C 2 442  ? 134.836 142.970 175.096 1.00 112.38 ? 125  ALA C C   1 
ATOM   12644 O  O   . ALA C 2 442  ? 134.992 142.074 174.250 1.00 112.72 ? 125  ALA C O   1 
ATOM   12645 C  CB  . ALA C 2 442  ? 136.694 144.665 174.958 1.00 100.66 ? 125  ALA C CB  1 
ATOM   12646 N  N   . LYS C 2 443  ? 134.351 142.720 176.321 1.00 106.37 ? 126  LYS C N   1 
ATOM   12647 C  CA  . LYS C 2 443  ? 133.943 141.367 176.699 1.00 106.10 ? 126  LYS C CA  1 
ATOM   12648 C  C   . LYS C 2 443  ? 132.695 140.924 175.941 1.00 103.92 ? 126  LYS C C   1 
ATOM   12649 O  O   . LYS C 2 443  ? 132.612 139.777 175.474 1.00 105.30 ? 126  LYS C O   1 
ATOM   12650 C  CB  . LYS C 2 443  ? 133.717 141.299 178.203 1.00 104.99 ? 126  LYS C CB  1 
ATOM   12651 C  CG  . LYS C 2 443  ? 132.861 142.423 178.724 1.00 107.95 ? 126  LYS C CG  1 
ATOM   12652 C  CD  . LYS C 2 443  ? 132.684 142.299 180.228 1.00 122.78 ? 126  LYS C CD  1 
ATOM   12653 C  CE  . LYS C 2 443  ? 131.720 143.355 180.753 1.00 118.24 ? 126  LYS C CE  1 
ATOM   12654 N  NZ  . LYS C 2 443  ? 130.377 143.255 180.110 1.00 110.43 ? 126  LYS C NZ  1 
ATOM   12655 N  N   . THR C 2 444  ? 131.729 141.830 175.779 1.00 99.73  ? 127  THR C N   1 
ATOM   12656 C  CA  . THR C 2 444  ? 130.548 141.523 174.979 1.00 99.39  ? 127  THR C CA  1 
ATOM   12657 C  C   . THR C 2 444  ? 130.904 141.305 173.506 1.00 92.03  ? 127  THR C C   1 
ATOM   12658 O  O   . THR C 2 444  ? 130.339 140.420 172.854 1.00 91.61  ? 127  THR C O   1 
ATOM   12659 C  CB  . THR C 2 444  ? 129.527 142.647 175.136 1.00 108.10 ? 127  THR C CB  1 
ATOM   12660 O  OG1 . THR C 2 444  ? 129.424 142.996 176.525 1.00 109.18 ? 127  THR C OG1 1 
ATOM   12661 C  CG2 . THR C 2 444  ? 128.163 142.197 174.639 1.00 104.83 ? 127  THR C CG2 1 
ATOM   12662 N  N   . ILE C 2 445  ? 131.840 142.100 172.967 1.00 96.90  ? 128  ILE C N   1 
ATOM   12663 C  CA  . ILE C 2 445  ? 132.270 141.942 171.572 1.00 93.40  ? 128  ILE C CA  1 
ATOM   12664 C  C   . ILE C 2 445  ? 132.929 140.585 171.362 1.00 86.80  ? 128  ILE C C   1 
ATOM   12665 O  O   . ILE C 2 445  ? 132.666 139.902 170.367 1.00 91.63  ? 128  ILE C O   1 
ATOM   12666 C  CB  . ILE C 2 445  ? 133.218 143.081 171.142 1.00 95.96  ? 128  ILE C CB  1 
ATOM   12667 C  CG1 . ILE C 2 445  ? 132.509 144.447 171.131 1.00 107.77 ? 128  ILE C CG1 1 
ATOM   12668 C  CG2 . ILE C 2 445  ? 133.848 142.778 169.770 1.00 83.19  ? 128  ILE C CG2 1 
ATOM   12669 C  CD1 . ILE C 2 445  ? 131.338 144.561 170.166 1.00 103.66 ? 128  ILE C CD1 1 
ATOM   12670 N  N   . SER C 2 446  ? 133.818 140.182 172.271 1.00 86.30  ? 129  SER C N   1 
ATOM   12671 C  CA  . SER C 2 446  ? 134.422 138.863 172.107 1.00 84.69  ? 129  SER C CA  1 
ATOM   12672 C  C   . SER C 2 446  ? 133.390 137.753 172.263 1.00 90.81  ? 129  SER C C   1 
ATOM   12673 O  O   . SER C 2 446  ? 133.453 136.746 171.546 1.00 95.05  ? 129  SER C O   1 
ATOM   12674 C  CB  . SER C 2 446  ? 135.583 138.660 173.078 1.00 91.25  ? 129  SER C CB  1 
ATOM   12675 O  OG  . SER C 2 446  ? 136.626 139.581 172.822 1.00 90.70  ? 129  SER C OG  1 
ATOM   12676 N  N   . SER C 2 447  ? 132.435 137.904 173.192 1.00 90.47  ? 130  SER C N   1 
ATOM   12677 C  CA  . SER C 2 447  ? 131.418 136.864 173.364 1.00 97.76  ? 130  SER C CA  1 
ATOM   12678 C  C   . SER C 2 447  ? 130.562 136.712 172.108 1.00 94.80  ? 130  SER C C   1 
ATOM   12679 O  O   . SER C 2 447  ? 130.253 135.587 171.679 1.00 93.64  ? 130  SER C O   1 
ATOM   12680 C  CB  . SER C 2 447  ? 130.541 137.174 174.579 1.00 97.20  ? 130  SER C CB  1 
ATOM   12681 O  OG  . SER C 2 447  ? 129.459 136.260 174.675 1.00 96.78  ? 130  SER C OG  1 
ATOM   12682 N  N   . LEU C 2 448  ? 130.176 137.835 171.500 1.00 91.08  ? 131  LEU C N   1 
ATOM   12683 C  CA  . LEU C 2 448  ? 129.382 137.780 170.280 1.00 83.66  ? 131  LEU C CA  1 
ATOM   12684 C  C   . LEU C 2 448  ? 130.196 137.223 169.110 1.00 78.35  ? 131  LEU C C   1 
ATOM   12685 O  O   . LEU C 2 448  ? 129.685 136.417 168.326 1.00 84.24  ? 131  LEU C O   1 
ATOM   12686 C  CB  . LEU C 2 448  ? 128.829 139.168 169.966 1.00 90.35  ? 131  LEU C CB  1 
ATOM   12687 C  CG  . LEU C 2 448  ? 127.859 139.269 168.791 1.00 105.30 ? 131  LEU C CG  1 
ATOM   12688 C  CD1 . LEU C 2 448  ? 126.728 138.256 168.991 1.00 102.91 ? 131  LEU C CD1 1 
ATOM   12689 C  CD2 . LEU C 2 448  ? 127.302 140.685 168.632 1.00 103.47 ? 131  LEU C CD2 1 
ATOM   12690 N  N   . ASN C 2 449  ? 131.457 137.643 168.963 1.00 75.21  ? 132  ASN C N   1 
ATOM   12691 C  CA  . ASN C 2 449  ? 132.362 136.993 168.012 1.00 67.35  ? 132  ASN C CA  1 
ATOM   12692 C  C   . ASN C 2 449  ? 132.410 135.478 168.189 1.00 67.65  ? 132  ASN C C   1 
ATOM   12693 O  O   . ASN C 2 449  ? 132.345 134.728 167.211 1.00 72.26  ? 132  ASN C O   1 
ATOM   12694 C  CB  . ASN C 2 449  ? 133.762 137.554 168.164 1.00 72.76  ? 132  ASN C CB  1 
ATOM   12695 C  CG  . ASN C 2 449  ? 134.609 137.433 166.910 1.00 72.09  ? 132  ASN C CG  1 
ATOM   12696 O  OD1 . ASN C 2 449  ? 134.146 137.057 165.849 1.00 73.69  ? 132  ASN C OD1 1 
ATOM   12697 N  ND2 . ASN C 2 449  ? 135.908 137.555 167.107 1.00 78.97  ? 132  ASN C ND2 1 
ATOM   12698 N  N   . ARG C 2 450  ? 132.547 134.997 169.422 1.00 71.77  ? 133  ARG C N   1 
ATOM   12699 C  CA  . ARG C 2 450  ? 132.625 133.545 169.598 1.00 83.40  ? 133  ARG C CA  1 
ATOM   12700 C  C   . ARG C 2 450  ? 131.301 132.850 169.244 1.00 82.23  ? 133  ARG C C   1 
ATOM   12701 O  O   . ARG C 2 450  ? 131.308 131.809 168.567 1.00 81.00  ? 133  ARG C O   1 
ATOM   12702 C  CB  . ARG C 2 450  ? 133.052 133.202 171.020 1.00 103.88 ? 133  ARG C CB  1 
ATOM   12703 C  CG  . ARG C 2 450  ? 132.851 131.754 171.438 1.00 108.45 ? 133  ARG C CG  1 
ATOM   12704 C  CD  . ARG C 2 450  ? 133.597 131.518 172.747 1.00 115.46 ? 133  ARG C CD  1 
ATOM   12705 N  NE  . ARG C 2 450  ? 133.583 132.710 173.612 1.00 115.01 ? 133  ARG C NE  1 
ATOM   12706 C  CZ  . ARG C 2 450  ? 132.616 132.987 174.486 1.00 112.43 ? 133  ARG C CZ  1 
ATOM   12707 N  NH1 . ARG C 2 450  ? 131.568 132.177 174.578 1.00 111.33 ? 133  ARG C NH1 1 
ATOM   12708 N  NH2 . ARG C 2 450  ? 132.674 134.079 175.240 1.00 104.42 ? 133  ARG C NH2 1 
ATOM   12709 N  N   . VAL C 2 451  ? 130.155 133.410 169.658 1.00 69.44  ? 134  VAL C N   1 
ATOM   12710 C  CA  . VAL C 2 451  ? 128.874 132.775 169.330 1.00 55.81  ? 134  VAL C CA  1 
ATOM   12711 C  C   . VAL C 2 451  ? 128.648 132.735 167.827 1.00 61.10  ? 134  VAL C C   1 
ATOM   12712 O  O   . VAL C 2 451  ? 128.180 131.726 167.281 1.00 67.12  ? 134  VAL C O   1 
ATOM   12713 C  CB  . VAL C 2 451  ? 127.713 133.478 170.034 1.00 61.03  ? 134  VAL C CB  1 
ATOM   12714 C  CG1 . VAL C 2 451  ? 126.398 132.973 169.460 1.00 61.95  ? 134  VAL C CG1 1 
ATOM   12715 C  CG2 . VAL C 2 451  ? 127.789 133.194 171.521 1.00 73.59  ? 134  VAL C CG2 1 
ATOM   12716 N  N   . CYS C 2 452  ? 128.959 133.829 167.130 1.00 65.10  ? 135  CYS C N   1 
ATOM   12717 C  CA  . CYS C 2 452  ? 128.834 133.829 165.674 1.00 67.62  ? 135  CYS C CA  1 
ATOM   12718 C  C   . CYS C 2 452  ? 129.790 132.837 165.017 1.00 61.41  ? 135  CYS C C   1 
ATOM   12719 O  O   . CYS C 2 452  ? 129.424 132.177 164.035 1.00 66.06  ? 135  CYS C O   1 
ATOM   12720 C  CB  . CYS C 2 452  ? 129.070 135.233 165.118 1.00 78.08  ? 135  CYS C CB  1 
ATOM   12721 S  SG  . CYS C 2 452  ? 127.859 136.475 165.631 1.00 112.00 ? 135  CYS C SG  1 
ATOM   12722 N  N   . ALA C 2 453  ? 131.027 132.741 165.507 1.00 51.81  ? 136  ALA C N   1 
ATOM   12723 C  CA  . ALA C 2 453  ? 131.951 131.796 164.897 1.00 47.29  ? 136  ALA C CA  1 
ATOM   12724 C  C   . ALA C 2 453  ? 131.452 130.375 165.078 1.00 48.36  ? 136  ALA C C   1 
ATOM   12725 O  O   . ALA C 2 453  ? 131.569 129.545 164.170 1.00 58.43  ? 136  ALA C O   1 
ATOM   12726 C  CB  . ALA C 2 453  ? 133.349 131.962 165.483 1.00 57.71  ? 136  ALA C CB  1 
ATOM   12727 N  N   . GLU C 2 454  ? 130.856 130.084 166.226 1.00 45.66  ? 137  GLU C N   1 
ATOM   12728 C  CA  . GLU C 2 454  ? 130.305 128.752 166.434 1.00 49.49  ? 137  GLU C CA  1 
ATOM   12729 C  C   . GLU C 2 454  ? 129.112 128.482 165.521 1.00 54.66  ? 137  GLU C C   1 
ATOM   12730 O  O   . GLU C 2 454  ? 128.978 127.379 164.984 1.00 58.43  ? 137  GLU C O   1 
ATOM   12731 C  CB  . GLU C 2 454  ? 129.906 128.583 167.891 1.00 67.44  ? 137  GLU C CB  1 
ATOM   12732 C  CG  . GLU C 2 454  ? 131.092 128.537 168.841 1.00 80.17  ? 137  GLU C CG  1 
ATOM   12733 C  CD  . GLU C 2 454  ? 130.673 128.297 170.286 1.00 93.28  ? 137  GLU C CD  1 
ATOM   12734 O  OE1 . GLU C 2 454  ? 129.489 127.963 170.521 1.00 87.04  ? 137  GLU C OE1 1 
ATOM   12735 O  OE2 . GLU C 2 454  ? 131.523 128.476 171.189 1.00 97.22  ? 137  GLU C OE2 1 
ATOM   12736 N  N   . MET C 2 455  ? 128.227 129.465 165.337 1.00 54.16  ? 138  MET C N   1 
ATOM   12737 C  CA  . MET C 2 455  ? 127.106 129.266 164.419 1.00 43.63  ? 138  MET C CA  1 
ATOM   12738 C  C   . MET C 2 455  ? 127.593 129.019 162.998 1.00 45.70  ? 138  MET C C   1 
ATOM   12739 O  O   . MET C 2 455  ? 127.109 128.101 162.324 1.00 58.78  ? 138  MET C O   1 
ATOM   12740 C  CB  . MET C 2 455  ? 126.174 130.469 164.445 1.00 46.33  ? 138  MET C CB  1 
ATOM   12741 C  CG  . MET C 2 455  ? 125.409 130.607 165.737 1.00 56.47  ? 138  MET C CG  1 
ATOM   12742 S  SD  . MET C 2 455  ? 124.084 129.406 165.890 1.00 73.08  ? 138  MET C SD  1 
ATOM   12743 C  CE  . MET C 2 455  ? 122.929 130.058 164.682 1.00 66.73  ? 138  MET C CE  1 
ATOM   12744 N  N   . VAL C 2 456  ? 128.558 129.812 162.525 1.00 40.96  ? 139  VAL C N   1 
ATOM   12745 C  CA  . VAL C 2 456  ? 129.073 129.601 161.173 1.00 39.45  ? 139  VAL C CA  1 
ATOM   12746 C  C   . VAL C 2 456  ? 129.710 128.237 161.061 1.00 39.63  ? 139  VAL C C   1 
ATOM   12747 O  O   . VAL C 2 456  ? 129.597 127.567 160.030 1.00 51.88  ? 139  VAL C O   1 
ATOM   12748 C  CB  . VAL C 2 456  ? 130.072 130.691 160.761 1.00 52.09  ? 139  VAL C CB  1 
ATOM   12749 C  CG1 . VAL C 2 456  ? 130.684 130.335 159.408 1.00 54.39  ? 139  VAL C CG1 1 
ATOM   12750 C  CG2 . VAL C 2 456  ? 129.384 132.041 160.677 1.00 59.61  ? 139  VAL C CG2 1 
ATOM   12751 N  N   . ALA C 2 457  ? 130.400 127.801 162.099 1.00 38.49  ? 140  ALA C N   1 
ATOM   12752 C  CA  . ALA C 2 457  ? 130.961 126.467 162.019 1.00 45.03  ? 140  ALA C CA  1 
ATOM   12753 C  C   . ALA C 2 457  ? 129.854 125.428 161.923 1.00 39.32  ? 140  ALA C C   1 
ATOM   12754 O  O   . ALA C 2 457  ? 129.901 124.535 161.072 1.00 50.28  ? 140  ALA C O   1 
ATOM   12755 C  CB  . ALA C 2 457  ? 131.866 126.203 163.224 1.00 56.97  ? 140  ALA C CB  1 
ATOM   12756 N  N   . LYS C 2 458  ? 128.829 125.548 162.757 1.00 37.86  ? 141  LYS C N   1 
ATOM   12757 C  CA  . LYS C 2 458  ? 127.793 124.526 162.773 1.00 44.22  ? 141  LYS C CA  1 
ATOM   12758 C  C   . LYS C 2 458  ? 126.985 124.531 161.495 1.00 41.61  ? 141  LYS C C   1 
ATOM   12759 O  O   . LYS C 2 458  ? 126.283 123.557 161.209 1.00 49.03  ? 141  LYS C O   1 
ATOM   12760 C  CB  . LYS C 2 458  ? 126.872 124.724 163.975 1.00 56.45  ? 141  LYS C CB  1 
ATOM   12761 C  CG  . LYS C 2 458  ? 127.559 124.468 165.325 1.00 68.74  ? 141  LYS C CG  1 
ATOM   12762 C  CD  . LYS C 2 458  ? 126.980 125.338 166.461 1.00 76.98  ? 141  LYS C CD  1 
ATOM   12763 C  CE  . LYS C 2 458  ? 125.456 125.207 166.602 1.00 76.63  ? 141  LYS C CE  1 
ATOM   12764 N  NZ  . LYS C 2 458  ? 124.907 126.111 167.665 1.00 70.56  ? 141  LYS C NZ  1 
ATOM   12765 N  N   . TYR C 2 459  ? 127.070 125.607 160.728 1.00 41.93  ? 142  TYR C N   1 
ATOM   12766 C  CA  . TYR C 2 459  ? 126.377 125.655 159.446 1.00 43.21  ? 142  TYR C CA  1 
ATOM   12767 C  C   . TYR C 2 459  ? 126.975 124.686 158.435 1.00 45.60  ? 142  TYR C C   1 
ATOM   12768 O  O   . TYR C 2 459  ? 126.243 124.103 157.629 1.00 56.38  ? 142  TYR C O   1 
ATOM   12769 C  CB  . TYR C 2 459  ? 126.415 127.072 158.898 1.00 55.73  ? 142  TYR C CB  1 
ATOM   12770 C  CG  . TYR C 2 459  ? 125.528 127.326 157.703 1.00 55.53  ? 142  TYR C CG  1 
ATOM   12771 C  CD1 . TYR C 2 459  ? 124.164 127.520 157.854 1.00 54.66  ? 142  TYR C CD1 1 
ATOM   12772 C  CD2 . TYR C 2 459  ? 126.068 127.421 156.432 1.00 50.78  ? 142  TYR C CD2 1 
ATOM   12773 C  CE1 . TYR C 2 459  ? 123.361 127.774 156.768 1.00 53.58  ? 142  TYR C CE1 1 
ATOM   12774 C  CE2 . TYR C 2 459  ? 125.283 127.683 155.348 1.00 45.07  ? 142  TYR C CE2 1 
ATOM   12775 C  CZ  . TYR C 2 459  ? 123.929 127.859 155.515 1.00 48.41  ? 142  TYR C CZ  1 
ATOM   12776 O  OH  . TYR C 2 459  ? 123.142 128.109 154.411 1.00 48.23  ? 142  TYR C OH  1 
ATOM   12777 N  N   . ASP C 2 460  ? 128.295 124.521 158.431 1.00 41.72  ? 143  ASP C N   1 
ATOM   12778 C  CA  . ASP C 2 460  ? 128.935 123.662 157.443 1.00 32.65  ? 143  ASP C CA  1 
ATOM   12779 C  C   . ASP C 2 460  ? 128.625 122.203 157.663 1.00 37.18  ? 143  ASP C C   1 
ATOM   12780 O  O   . ASP C 2 460  ? 128.875 121.391 156.771 1.00 43.41  ? 143  ASP C O   1 
ATOM   12781 C  CB  . ASP C 2 460  ? 130.429 123.860 157.507 1.00 43.95  ? 143  ASP C CB  1 
ATOM   12782 C  CG  . ASP C 2 460  ? 130.832 125.261 157.096 1.00 69.82  ? 143  ASP C CG  1 
ATOM   12783 O  OD1 . ASP C 2 460  ? 129.923 126.073 156.778 1.00 62.25  ? 143  ASP C OD1 1 
ATOM   12784 O  OD2 . ASP C 2 460  ? 132.046 125.574 157.140 1.00 68.11  ? 143  ASP C OD2 1 
ATOM   12785 N  N   . LEU C 2 461  ? 128.107 121.862 158.838 1.00 42.62  ? 144  LEU C N   1 
ATOM   12786 C  CA  . LEU C 2 461  ? 127.692 120.514 159.188 1.00 41.17  ? 144  LEU C CA  1 
ATOM   12787 C  C   . LEU C 2 461  ? 126.175 120.382 159.171 1.00 44.61  ? 144  LEU C C   1 
ATOM   12788 O  O   . LEU C 2 461  ? 125.603 119.665 159.993 1.00 51.02  ? 144  LEU C O   1 
ATOM   12789 C  CB  . LEU C 2 461  ? 128.218 120.142 160.571 1.00 56.86  ? 144  LEU C CB  1 
ATOM   12790 C  CG  . LEU C 2 461  ? 129.729 119.993 160.768 1.00 71.39  ? 144  LEU C CG  1 
ATOM   12791 C  CD1 . LEU C 2 461  ? 130.076 119.727 162.247 1.00 69.02  ? 144  LEU C CD1 1 
ATOM   12792 C  CD2 . LEU C 2 461  ? 130.277 118.891 159.864 1.00 64.86  ? 144  LEU C CD2 1 
ATOM   12793 N  N   . LEU C 2 462  ? 125.502 121.098 158.285 1.00 37.78  ? 145  LEU C N   1 
ATOM   12794 C  CA  . LEU C 2 462  ? 124.064 120.953 158.178 1.00 33.00  ? 145  LEU C CA  1 
ATOM   12795 C  C   . LEU C 2 462  ? 123.722 120.113 156.965 1.00 41.42  ? 145  LEU C C   1 
ATOM   12796 O  O   . LEU C 2 462  ? 124.444 120.100 155.967 1.00 46.94  ? 145  LEU C O   1 
ATOM   12797 C  CB  . LEU C 2 462  ? 123.353 122.293 158.070 1.00 38.06  ? 145  LEU C CB  1 
ATOM   12798 C  CG  . LEU C 2 462  ? 123.049 123.012 159.381 1.00 44.97  ? 145  LEU C CG  1 
ATOM   12799 C  CD1 . LEU C 2 462  ? 122.404 124.354 159.091 1.00 55.31  ? 145  LEU C CD1 1 
ATOM   12800 C  CD2 . LEU C 2 462  ? 122.140 122.190 160.233 1.00 43.01  ? 145  LEU C CD2 1 
ATOM   12801 N  N   . VAL C 2 463  ? 122.618 119.386 157.079 1.00 43.01  ? 146  VAL C N   1 
ATOM   12802 C  CA  . VAL C 2 463  ? 122.023 118.642 155.979 1.00 36.46  ? 146  VAL C CA  1 
ATOM   12803 C  C   . VAL C 2 463  ? 120.507 118.779 156.085 1.00 42.15  ? 146  VAL C C   1 
ATOM   12804 O  O   . VAL C 2 463  ? 119.940 118.625 157.172 1.00 47.16  ? 146  VAL C O   1 
ATOM   12805 C  CB  . VAL C 2 463  ? 122.460 117.170 156.012 1.00 37.69  ? 146  VAL C CB  1 
ATOM   12806 C  CG1 . VAL C 2 463  ? 121.580 116.337 155.104 1.00 56.41  ? 146  VAL C CG1 1 
ATOM   12807 C  CG2 . VAL C 2 463  ? 123.889 117.061 155.575 1.00 48.58  ? 146  VAL C CG2 1 
ATOM   12808 N  N   . MET C 2 464  ? 119.848 119.082 154.972 1.00 37.26  ? 147  MET C N   1 
ATOM   12809 C  CA  . MET C 2 464  ? 118.404 119.207 154.972 1.00 37.90  ? 147  MET C CA  1 
ATOM   12810 C  C   . MET C 2 464  ? 117.778 118.248 153.976 1.00 41.17  ? 147  MET C C   1 
ATOM   12811 O  O   . MET C 2 464  ? 118.363 117.923 152.938 1.00 44.67  ? 147  MET C O   1 
ATOM   12812 C  CB  . MET C 2 464  ? 117.945 120.608 154.629 1.00 48.56  ? 147  MET C CB  1 
ATOM   12813 C  CG  . MET C 2 464  ? 118.333 121.099 153.253 1.00 46.78  ? 147  MET C CG  1 
ATOM   12814 S  SD  . MET C 2 464  ? 117.567 122.717 152.996 1.00 48.59  ? 147  MET C SD  1 
ATOM   12815 C  CE  . MET C 2 464  ? 118.232 123.166 151.398 1.00 44.64  ? 147  MET C CE  1 
ATOM   12816 N  N   . THR C 2 465  ? 116.557 117.828 154.292 1.00 36.91  ? 148  THR C N   1 
ATOM   12817 C  CA  . THR C 2 465  ? 115.777 116.952 153.432 1.00 36.79  ? 148  THR C CA  1 
ATOM   12818 C  C   . THR C 2 465  ? 114.642 117.739 152.785 1.00 39.17  ? 148  THR C C   1 
ATOM   12819 O  O   . THR C 2 465  ? 113.756 118.245 153.482 1.00 42.25  ? 148  THR C O   1 
ATOM   12820 C  CB  . THR C 2 465  ? 115.234 115.756 154.216 1.00 44.62  ? 148  THR C CB  1 
ATOM   12821 O  OG1 . THR C 2 465  ? 114.492 116.217 155.352 1.00 47.75  ? 148  THR C OG1 1 
ATOM   12822 C  CG2 . THR C 2 465  ? 116.372 114.812 154.657 1.00 52.02  ? 148  THR C CG2 1 
ATOM   12823 N  N   . THR C 2 466  ? 114.661 117.812 151.454 1.00 34.50  ? 149  THR C N   1 
ATOM   12824 C  CA  . THR C 2 466  ? 113.629 118.528 150.727 1.00 26.58  ? 149  THR C CA  1 
ATOM   12825 C  C   . THR C 2 466  ? 112.284 117.910 151.007 1.00 28.29  ? 149  THR C C   1 
ATOM   12826 O  O   . THR C 2 466  ? 112.138 116.691 151.044 1.00 34.15  ? 149  THR C O   1 
ATOM   12827 C  CB  . THR C 2 466  ? 113.871 118.464 149.243 1.00 37.15  ? 149  THR C CB  1 
ATOM   12828 O  OG1 . THR C 2 466  ? 113.614 117.123 148.811 1.00 42.82  ? 149  THR C OG1 1 
ATOM   12829 C  CG2 . THR C 2 466  ? 115.301 118.841 148.932 1.00 43.75  ? 149  THR C CG2 1 
ATOM   12830 N  N   . GLY C 2 467  ? 111.294 118.766 151.203 1.00 35.55  ? 150  GLY C N   1 
ATOM   12831 C  CA  . GLY C 2 467  ? 109.990 118.333 151.628 1.00 37.52  ? 150  GLY C CA  1 
ATOM   12832 C  C   . GLY C 2 467  ? 109.015 118.249 150.476 1.00 35.04  ? 150  GLY C C   1 
ATOM   12833 O  O   . GLY C 2 467  ? 109.284 118.616 149.338 1.00 40.39  ? 150  GLY C O   1 
ATOM   12834 N  N   . ARG C 2 468  ? 107.842 117.777 150.812 1.00 35.88  ? 151  ARG C N   1 
ATOM   12835 C  CA  . ARG C 2 468  ? 106.778 117.712 149.849 1.00 34.52  ? 151  ARG C CA  1 
ATOM   12836 C  C   . ARG C 2 468  ? 105.947 118.961 149.829 1.00 38.83  ? 151  ARG C C   1 
ATOM   12837 O  O   . ARG C 2 468  ? 104.992 119.028 149.057 1.00 56.88  ? 151  ARG C O   1 
ATOM   12838 C  CB  . ARG C 2 468  ? 105.875 116.543 150.167 1.00 51.34  ? 151  ARG C CB  1 
ATOM   12839 C  CG  . ARG C 2 468  ? 106.633 115.289 150.349 1.00 56.37  ? 151  ARG C CG  1 
ATOM   12840 C  CD  . ARG C 2 468  ? 105.662 114.171 150.543 1.00 58.72  ? 151  ARG C CD  1 
ATOM   12841 N  NE  . ARG C 2 468  ? 104.739 114.473 151.618 1.00 56.74  ? 151  ARG C NE  1 
ATOM   12842 C  CZ  . ARG C 2 468  ? 105.022 114.236 152.894 1.00 69.04  ? 151  ARG C CZ  1 
ATOM   12843 N  NH1 . ARG C 2 468  ? 106.210 113.727 153.220 1.00 63.09  ? 151  ARG C NH1 1 
ATOM   12844 N  NH2 . ARG C 2 468  ? 104.136 114.511 153.848 1.00 72.56  ? 151  ARG C NH2 1 
ATOM   12845 N  N   . ALA C 2 469  ? 106.237 119.934 150.671 1.00 36.35  ? 152  ALA C N   1 
ATOM   12846 C  CA  . ALA C 2 469  ? 105.365 121.091 150.721 1.00 39.07  ? 152  ALA C CA  1 
ATOM   12847 C  C   . ALA C 2 469  ? 106.103 122.380 150.441 1.00 35.84  ? 152  ALA C C   1 
ATOM   12848 O  O   . ALA C 2 469  ? 105.538 123.451 150.662 1.00 48.62  ? 152  ALA C O   1 
ATOM   12849 C  CB  . ALA C 2 469  ? 104.657 121.192 152.076 1.00 47.16  ? 152  ALA C CB  1 
ATOM   12850 N  N   . THR C 2 470  ? 107.345 122.324 149.988 1.00 27.23  ? 153  THR C N   1 
ATOM   12851 C  CA  . THR C 2 470  ? 108.072 123.570 149.855 1.00 26.22  ? 153  THR C CA  1 
ATOM   12852 C  C   . THR C 2 470  ? 107.487 124.419 148.751 1.00 43.35  ? 153  THR C C   1 
ATOM   12853 O  O   . THR C 2 470  ? 107.247 125.620 148.939 1.00 54.34  ? 153  THR C O   1 
ATOM   12854 C  CB  . THR C 2 470  ? 109.533 123.309 149.590 1.00 40.45  ? 153  THR C CB  1 
ATOM   12855 O  OG1 . THR C 2 470  ? 109.995 122.374 150.566 1.00 51.04  ? 153  THR C OG1 1 
ATOM   12856 C  CG2 . THR C 2 470  ? 110.327 124.609 149.744 1.00 42.57  ? 153  THR C CG2 1 
ATOM   12857 N  N   . ALA C 2 471  ? 107.232 123.819 147.593 1.00 39.85  ? 154  ALA C N   1 
ATOM   12858 C  CA  . ALA C 2 471  ? 106.650 124.595 146.507 1.00 35.41  ? 154  ALA C CA  1 
ATOM   12859 C  C   . ALA C 2 471  ? 105.300 125.172 146.911 1.00 32.18  ? 154  ALA C C   1 
ATOM   12860 O  O   . ALA C 2 471  ? 105.041 126.359 146.710 1.00 40.70  ? 154  ALA C O   1 
ATOM   12861 C  CB  . ALA C 2 471  ? 106.508 123.716 145.276 1.00 45.66  ? 154  ALA C CB  1 
ATOM   12862 N  N   . THR C 2 472  ? 104.445 124.361 147.520 1.00 33.11  ? 155  THR C N   1 
ATOM   12863 C  CA  . THR C 2 472  ? 103.149 124.869 147.931 1.00 33.92  ? 155  THR C CA  1 
ATOM   12864 C  C   . THR C 2 472  ? 103.277 125.914 149.038 1.00 39.67  ? 155  THR C C   1 
ATOM   12865 O  O   . THR C 2 472  ? 102.449 126.829 149.119 1.00 48.36  ? 155  THR C O   1 
ATOM   12866 C  CB  . THR C 2 472  ? 102.265 123.714 148.398 1.00 48.53  ? 155  THR C CB  1 
ATOM   12867 O  OG1 . THR C 2 472  ? 102.101 122.758 147.338 1.00 45.64  ? 155  THR C OG1 1 
ATOM   12868 C  CG2 . THR C 2 472  ? 100.890 124.235 148.846 1.00 50.12  ? 155  THR C CG2 1 
ATOM   12869 N  N   . ALA C 2 473  ? 104.276 125.804 149.911 1.00 32.01  ? 156  ALA C N   1 
ATOM   12870 C  CA  . ALA C 2 473  ? 104.390 126.801 150.966 1.00 29.03  ? 156  ALA C CA  1 
ATOM   12871 C  C   . ALA C 2 473  ? 104.849 128.123 150.399 1.00 26.47  ? 156  ALA C C   1 
ATOM   12872 O  O   . ALA C 2 473  ? 104.337 129.176 150.784 1.00 40.00  ? 156  ALA C O   1 
ATOM   12873 C  CB  . ALA C 2 473  ? 105.339 126.332 152.065 1.00 46.68  ? 156  ALA C CB  1 
ATOM   12874 N  N   . ALA C 2 474  ? 105.774 128.096 149.451 1.00 26.94  ? 157  ALA C N   1 
ATOM   12875 C  CA  . ALA C 2 474  ? 106.127 129.342 148.782 1.00 33.47  ? 157  ALA C CA  1 
ATOM   12876 C  C   . ALA C 2 474  ? 104.978 129.886 147.929 1.00 45.08  ? 157  ALA C C   1 
ATOM   12877 O  O   . ALA C 2 474  ? 104.889 131.101 147.736 1.00 50.30  ? 157  ALA C O   1 
ATOM   12878 C  CB  . ALA C 2 474  ? 107.377 129.153 147.931 1.00 38.01  ? 157  ALA C CB  1 
ATOM   12879 N  N   . ALA C 2 475  ? 104.093 129.026 147.403 1.00 40.83  ? 158  ALA C N   1 
ATOM   12880 C  CA  . ALA C 2 475  ? 102.942 129.527 146.644 1.00 35.39  ? 158  ALA C CA  1 
ATOM   12881 C  C   . ALA C 2 475  ? 101.907 130.190 147.548 1.00 33.82  ? 158  ALA C C   1 
ATOM   12882 O  O   . ALA C 2 475  ? 101.420 131.278 147.244 1.00 46.41  ? 158  ALA C O   1 
ATOM   12883 C  CB  . ALA C 2 475  ? 102.286 128.406 145.837 1.00 49.37  ? 158  ALA C CB  1 
ATOM   12884 N  N   . THR C 2 476  ? 101.527 129.544 148.638 1.00 25.77  ? 159  THR C N   1 
ATOM   12885 C  CA  . THR C 2 476  ? 100.672 130.240 149.574 1.00 29.97  ? 159  THR C CA  1 
ATOM   12886 C  C   . THR C 2 476  ? 101.303 131.557 149.984 1.00 32.39  ? 159  THR C C   1 
ATOM   12887 O  O   . THR C 2 476  ? 100.617 132.578 150.079 1.00 42.08  ? 159  THR C O   1 
ATOM   12888 C  CB  . THR C 2 476  ? 100.407 129.374 150.798 1.00 46.31  ? 159  THR C CB  1 
ATOM   12889 O  OG1 . THR C 2 476  ? 99.889  128.110 150.373 1.00 48.02  ? 159  THR C OG1 1 
ATOM   12890 C  CG2 . THR C 2 476  ? 99.402  130.046 151.735 1.00 53.14  ? 159  THR C CG2 1 
ATOM   12891 N  N   . GLU C 2 477  ? 102.609 131.564 150.217 1.00 33.18  ? 160  GLU C N   1 
ATOM   12892 C  CA  . GLU C 2 477  ? 103.256 132.796 150.640 1.00 35.05  ? 160  GLU C CA  1 
ATOM   12893 C  C   . GLU C 2 477  ? 103.214 133.862 149.553 1.00 37.68  ? 160  GLU C C   1 
ATOM   12894 O  O   . GLU C 2 477  ? 102.999 135.041 149.851 1.00 44.18  ? 160  GLU C O   1 
ATOM   12895 C  CB  . GLU C 2 477  ? 104.700 132.509 151.048 1.00 57.01  ? 160  GLU C CB  1 
ATOM   12896 C  CG  . GLU C 2 477  ? 105.593 133.756 151.217 1.00 74.21  ? 160  GLU C CG  1 
ATOM   12897 C  CD  . GLU C 2 477  ? 107.096 133.420 151.362 1.00 82.82  ? 160  GLU C CD  1 
ATOM   12898 O  OE1 . GLU C 2 477  ? 107.449 132.219 151.422 1.00 73.51  ? 160  GLU C OE1 1 
ATOM   12899 O  OE2 . GLU C 2 477  ? 107.925 134.362 151.391 1.00 78.48  ? 160  GLU C OE2 1 
ATOM   12900 N  N   . ALA C 2 478  ? 103.443 133.488 148.297 1.00 33.36  ? 161  ALA C N   1 
ATOM   12901 C  CA  . ALA C 2 478  ? 103.487 134.505 147.253 1.00 29.83  ? 161  ALA C CA  1 
ATOM   12902 C  C   . ALA C 2 478  ? 102.097 134.961 146.863 1.00 36.48  ? 161  ALA C C   1 
ATOM   12903 O  O   . ALA C 2 478  ? 101.936 136.079 146.369 1.00 44.95  ? 161  ALA C O   1 
ATOM   12904 C  CB  . ALA C 2 478  ? 104.230 133.994 146.025 1.00 33.54  ? 161  ALA C CB  1 
ATOM   12905 N  N   . TYR C 2 479  ? 101.088 134.116 147.066 1.00 37.63  ? 162  TYR C N   1 
ATOM   12906 C  CA  . TYR C 2 479  ? 99.714  134.498 146.766 1.00 40.06  ? 162  TYR C CA  1 
ATOM   12907 C  C   . TYR C 2 479  ? 99.099  135.340 147.886 1.00 42.35  ? 162  TYR C C   1 
ATOM   12908 O  O   . TYR C 2 479  ? 98.310  136.245 147.604 1.00 52.00  ? 162  TYR C O   1 
ATOM   12909 C  CB  . TYR C 2 479  ? 98.872  133.245 146.507 1.00 53.36  ? 162  TYR C CB  1 
ATOM   12910 C  CG  . TYR C 2 479  ? 97.748  133.434 145.503 1.00 57.92  ? 162  TYR C CG  1 
ATOM   12911 C  CD1 . TYR C 2 479  ? 96.530  133.985 145.871 1.00 57.88  ? 162  TYR C CD1 1 
ATOM   12912 C  CD2 . TYR C 2 479  ? 97.916  133.045 144.179 1.00 60.88  ? 162  TYR C CD2 1 
ATOM   12913 C  CE1 . TYR C 2 479  ? 95.514  134.166 144.935 1.00 63.17  ? 162  TYR C CE1 1 
ATOM   12914 C  CE2 . TYR C 2 479  ? 96.915  133.211 143.240 1.00 65.35  ? 162  TYR C CE2 1 
ATOM   12915 C  CZ  . TYR C 2 479  ? 95.713  133.775 143.617 1.00 69.18  ? 162  TYR C CZ  1 
ATOM   12916 O  OH  . TYR C 2 479  ? 94.717  133.936 142.668 1.00 68.78  ? 162  TYR C OH  1 
ATOM   12917 N  N   . TRP C 2 480  ? 99.437  135.078 149.150 1.00 35.66  ? 163  TRP C N   1 
ATOM   12918 C  CA  . TRP C 2 480  ? 98.934  135.935 150.213 1.00 28.01  ? 163  TRP C CA  1 
ATOM   12919 C  C   . TRP C 2 480  ? 99.552  137.302 150.145 1.00 31.72  ? 163  TRP C C   1 
ATOM   12920 O  O   . TRP C 2 480  ? 98.892  138.302 150.434 1.00 46.76  ? 163  TRP C O   1 
ATOM   12921 C  CB  . TRP C 2 480  ? 99.199  135.325 151.564 1.00 31.98  ? 163  TRP C CB  1 
ATOM   12922 C  CG  . TRP C 2 480  ? 97.992  134.649 152.019 1.00 50.39  ? 163  TRP C CG  1 
ATOM   12923 C  CD1 . TRP C 2 480  ? 97.676  133.341 151.821 1.00 59.00  ? 163  TRP C CD1 1 
ATOM   12924 C  CD2 . TRP C 2 480  ? 96.910  135.217 152.764 1.00 59.80  ? 163  TRP C CD2 1 
ATOM   12925 N  NE1 . TRP C 2 480  ? 96.449  133.061 152.372 1.00 63.16  ? 163  TRP C NE1 1 
ATOM   12926 C  CE2 . TRP C 2 480  ? 95.960  134.193 152.965 1.00 58.42  ? 163  TRP C CE2 1 
ATOM   12927 C  CE3 . TRP C 2 480  ? 96.648  136.494 153.282 1.00 72.22  ? 163  TRP C CE3 1 
ATOM   12928 C  CZ2 . TRP C 2 480  ? 94.770  134.398 153.663 1.00 62.58  ? 163  TRP C CZ2 1 
ATOM   12929 C  CZ3 . TRP C 2 480  ? 95.452  136.701 153.980 1.00 77.41  ? 163  TRP C CZ3 1 
ATOM   12930 C  CH2 . TRP C 2 480  ? 94.532  135.654 154.160 1.00 79.91  ? 163  TRP C CH2 1 
ATOM   12931 N  N   . ALA C 2 481  ? 100.813 137.379 149.773 1.00 32.14  ? 164  ALA C N   1 
ATOM   12932 C  CA  . ALA C 2 481  ? 101.424 138.693 149.697 1.00 41.62  ? 164  ALA C CA  1 
ATOM   12933 C  C   . ALA C 2 481  ? 100.820 139.503 148.570 1.00 36.26  ? 164  ALA C C   1 
ATOM   12934 O  O   . ALA C 2 481  ? 100.557 140.698 148.727 1.00 45.33  ? 164  ALA C O   1 
ATOM   12935 C  CB  . ALA C 2 481  ? 102.936 138.567 149.518 1.00 47.85  ? 164  ALA C CB  1 
ATOM   12936 N  N   . GLU C 2 482  ? 100.577 138.872 147.436 1.00 38.41  ? 165  GLU C N   1 
ATOM   12937 C  CA  . GLU C 2 482  ? 100.228 139.647 146.257 1.00 47.82  ? 165  GLU C CA  1 
ATOM   12938 C  C   . GLU C 2 482  ? 98.747  140.013 146.226 1.00 51.74  ? 165  GLU C C   1 
ATOM   12939 O  O   . GLU C 2 482  ? 98.391  141.151 145.911 1.00 57.81  ? 165  GLU C O   1 
ATOM   12940 C  CB  . GLU C 2 482  ? 100.621 138.877 145.001 1.00 53.72  ? 165  GLU C CB  1 
ATOM   12941 C  CG  . GLU C 2 482  ? 100.611 139.745 143.769 1.00 61.82  ? 165  GLU C CG  1 
ATOM   12942 C  CD  . GLU C 2 482  ? 101.760 140.740 143.765 1.00 68.03  ? 165  GLU C CD  1 
ATOM   12943 O  OE1 . GLU C 2 482  ? 102.732 140.535 144.532 1.00 65.41  ? 165  GLU C OE1 1 
ATOM   12944 O  OE2 . GLU C 2 482  ? 101.686 141.728 142.996 1.00 68.65  ? 165  GLU C OE2 1 
ATOM   12945 N  N   . HIS C 2 483  ? 97.872  139.072 146.550 1.00 43.76  ? 166  HIS C N   1 
ATOM   12946 C  CA  . HIS C 2 483  ? 96.445  139.297 146.443 1.00 38.57  ? 166  HIS C CA  1 
ATOM   12947 C  C   . HIS C 2 483  ? 95.746  139.342 147.774 1.00 38.67  ? 166  HIS C C   1 
ATOM   12948 O  O   . HIS C 2 483  ? 94.605  139.790 147.840 1.00 52.10  ? 166  HIS C O   1 
ATOM   12949 C  CB  . HIS C 2 483  ? 95.821  138.186 145.623 1.00 48.09  ? 166  HIS C CB  1 
ATOM   12950 C  CG  . HIS C 2 483  ? 96.326  138.163 144.233 1.00 49.92  ? 166  HIS C CG  1 
ATOM   12951 N  ND1 . HIS C 2 483  ? 95.567  138.561 143.157 1.00 59.32  ? 166  HIS C ND1 1 
ATOM   12952 C  CD2 . HIS C 2 483  ? 97.563  137.903 143.753 1.00 53.70  ? 166  HIS C CD2 1 
ATOM   12953 C  CE1 . HIS C 2 483  ? 96.294  138.470 142.058 1.00 67.87  ? 166  HIS C CE1 1 
ATOM   12954 N  NE2 . HIS C 2 483  ? 97.512  138.080 142.394 1.00 62.95  ? 166  HIS C NE2 1 
ATOM   12955 N  N   . GLY C 2 484  ? 96.371  138.866 148.812 1.00 38.19  ? 167  GLY C N   1 
ATOM   12956 C  CA  . GLY C 2 484  ? 95.730  138.945 150.080 1.00 43.53  ? 167  GLY C CA  1 
ATOM   12957 C  C   . GLY C 2 484  ? 94.693  137.881 150.315 1.00 55.02  ? 167  GLY C C   1 
ATOM   12958 O  O   . GLY C 2 484  ? 94.033  137.916 151.359 1.00 71.36  ? 167  GLY C O   1 
ATOM   12959 N  N   . GLN C 2 485  ? 94.517  136.939 149.404 1.00 49.42  ? 168  GLN C N   1 
ATOM   12960 C  CA  . GLN C 2 485  ? 93.643  135.805 149.664 1.00 58.72  ? 168  GLN C CA  1 
ATOM   12961 C  C   . GLN C 2 485  ? 94.452  134.536 149.463 1.00 61.34  ? 168  GLN C C   1 
ATOM   12962 O  O   . GLN C 2 485  ? 95.538  134.578 148.876 1.00 65.80  ? 168  GLN C O   1 
ATOM   12963 C  CB  . GLN C 2 485  ? 92.417  135.814 148.739 1.00 61.31  ? 168  GLN C CB  1 
ATOM   12964 C  CG  . GLN C 2 485  ? 91.593  137.086 148.837 1.00 67.94  ? 168  GLN C CG  1 
ATOM   12965 C  CD  . GLN C 2 485  ? 91.641  137.909 147.552 1.00 80.51  ? 168  GLN C CD  1 
ATOM   12966 O  OE1 . GLN C 2 485  ? 92.550  137.739 146.728 1.00 75.94  ? 168  GLN C OE1 1 
ATOM   12967 N  NE2 . GLN C 2 485  ? 90.672  138.811 147.379 1.00 75.56  ? 168  GLN C NE2 1 
ATOM   12968 N  N   . PRO C 2 486  ? 93.981  133.399 149.968 1.00 49.95  ? 169  PRO C N   1 
ATOM   12969 C  CA  . PRO C 2 486  ? 94.654  132.137 149.639 1.00 48.60  ? 169  PRO C CA  1 
ATOM   12970 C  C   . PRO C 2 486  ? 94.508  131.827 148.209 1.00 44.30  ? 169  PRO C C   1 
ATOM   12971 O  O   . PRO C 2 486  ? 93.567  132.302 147.517 1.00 59.37  ? 169  PRO C O   1 
ATOM   12972 C  CB  . PRO C 2 486  ? 93.912  131.118 150.526 1.00 62.12  ? 169  PRO C CB  1 
ATOM   12973 C  CG  . PRO C 2 486  ? 93.255  131.933 151.601 1.00 65.60  ? 169  PRO C CG  1 
ATOM   12974 C  CD  . PRO C 2 486  ? 92.901  133.234 150.947 1.00 56.33  ? 169  PRO C CD  1 
ATOM   12975 N  N   . PRO C 2 487  ? 95.415  131.047 147.609 1.00 40.05  ? 170  PRO C N   1 
ATOM   12976 C  CA  . PRO C 2 487  ? 95.264  130.614 146.231 1.00 48.10  ? 170  PRO C CA  1 
ATOM   12977 C  C   . PRO C 2 487  ? 93.916  129.949 146.052 1.00 53.04  ? 170  PRO C C   1 
ATOM   12978 O  O   . PRO C 2 487  ? 93.472  129.177 146.914 1.00 60.08  ? 170  PRO C O   1 
ATOM   12979 C  CB  . PRO C 2 487  ? 96.399  129.606 146.038 1.00 58.35  ? 170  PRO C CB  1 
ATOM   12980 C  CG  . PRO C 2 487  ? 97.416  130.021 147.022 1.00 67.08  ? 170  PRO C CG  1 
ATOM   12981 C  CD  . PRO C 2 487  ? 96.651  130.536 148.224 1.00 57.24  ? 170  PRO C CD  1 
ATOM   12982 N  N   . PRO C 2 488  ? 93.233  130.232 144.972 1.00 42.15  ? 171  PRO C N   1 
ATOM   12983 C  CA  . PRO C 2 488  ? 91.830  129.868 144.858 1.00 39.68  ? 171  PRO C CA  1 
ATOM   12984 C  C   . PRO C 2 488  ? 91.726  128.421 144.410 1.00 56.18  ? 171  PRO C C   1 
ATOM   12985 O  O   . PRO C 2 488  ? 92.726  127.738 144.198 1.00 56.80  ? 171  PRO C O   1 
ATOM   12986 C  CB  . PRO C 2 488  ? 91.330  130.804 143.773 1.00 53.03  ? 171  PRO C CB  1 
ATOM   12987 C  CG  . PRO C 2 488  ? 92.519  130.931 142.883 1.00 55.94  ? 171  PRO C CG  1 
ATOM   12988 C  CD  . PRO C 2 488  ? 93.730  130.889 143.763 1.00 51.27  ? 171  PRO C CD  1 
ATOM   12989 N  N   . GLY C 2 489  ? 90.483  127.977 144.224 1.00 65.51  ? 172  GLY C N   1 
ATOM   12990 C  CA  . GLY C 2 489  ? 90.191  126.690 143.628 1.00 66.93  ? 172  GLY C CA  1 
ATOM   12991 C  C   . GLY C 2 489  ? 90.467  125.494 144.518 1.00 52.70  ? 172  GLY C C   1 
ATOM   12992 O  O   . GLY C 2 489  ? 90.429  125.578 145.751 1.00 51.05  ? 172  GLY C O   1 
ATOM   12993 N  N   . PRO C 2 490  ? 90.728  124.346 143.901 1.00 50.06  ? 173  PRO C N   1 
ATOM   12994 C  CA  . PRO C 2 490  ? 90.961  123.135 144.687 1.00 53.29  ? 173  PRO C CA  1 
ATOM   12995 C  C   . PRO C 2 490  ? 92.211  123.335 145.514 1.00 54.35  ? 173  PRO C C   1 
ATOM   12996 O  O   . PRO C 2 490  ? 93.052  124.184 145.213 1.00 59.75  ? 173  PRO C O   1 
ATOM   12997 C  CB  . PRO C 2 490  ? 91.170  122.042 143.631 1.00 58.08  ? 173  PRO C CB  1 
ATOM   12998 C  CG  . PRO C 2 490  ? 90.634  122.626 142.334 1.00 56.78  ? 173  PRO C CG  1 
ATOM   12999 C  CD  . PRO C 2 490  ? 90.884  124.108 142.454 1.00 54.26  ? 173  PRO C CD  1 
ATOM   13000 N  N   . SER C 2 491  ? 92.323  122.562 146.579 1.00 43.17  ? 174  SER C N   1 
ATOM   13001 C  CA  . SER C 2 491  ? 93.487  122.704 147.429 1.00 40.82  ? 174  SER C CA  1 
ATOM   13002 C  C   . SER C 2 491  ? 94.758  122.500 146.621 1.00 31.16  ? 174  SER C C   1 
ATOM   13003 O  O   . SER C 2 491  ? 94.772  121.773 145.630 1.00 41.74  ? 174  SER C O   1 
ATOM   13004 C  CB  . SER C 2 491  ? 93.419  121.696 148.566 1.00 66.03  ? 174  SER C CB  1 
ATOM   13005 O  OG  . SER C 2 491  ? 94.673  121.600 149.211 1.00 72.80  ? 174  SER C OG  1 
ATOM   13006 N  N   . LEU C 2 492  ? 95.830  123.149 147.042 1.00 28.21  ? 175  LEU C N   1 
ATOM   13007 C  CA  . LEU C 2 492  ? 97.111  122.910 146.401 1.00 32.51  ? 175  LEU C CA  1 
ATOM   13008 C  C   . LEU C 2 492  ? 97.631  121.528 146.831 1.00 42.33  ? 175  LEU C C   1 
ATOM   13009 O  O   . LEU C 2 492  ? 96.916  120.735 147.448 1.00 46.88  ? 175  LEU C O   1 
ATOM   13010 C  CB  . LEU C 2 492  ? 98.088  124.018 146.731 1.00 36.32  ? 175  LEU C CB  1 
ATOM   13011 C  CG  . LEU C 2 492  ? 97.738  125.372 146.124 1.00 45.49  ? 175  LEU C CG  1 
ATOM   13012 C  CD1 . LEU C 2 492  ? 98.788  126.446 146.459 1.00 49.27  ? 175  LEU C CD1 1 
ATOM   13013 C  CD2 . LEU C 2 492  ? 97.492  125.264 144.673 1.00 44.22  ? 175  LEU C CD2 1 
ATOM   13014 N  N   . TYR C 2 493  ? 98.882  121.205 146.472 1.00 40.08  ? 176  TYR C N   1 
ATOM   13015 C  CA  . TYR C 2 493  ? 99.380  119.835 146.602 1.00 34.61  ? 176  TYR C CA  1 
ATOM   13016 C  C   . TYR C 2 493  ? 99.547  119.397 148.050 1.00 44.56  ? 176  TYR C C   1 
ATOM   13017 O  O   . TYR C 2 493  ? 99.105  118.309 148.428 1.00 55.72  ? 176  TYR C O   1 
ATOM   13018 C  CB  . TYR C 2 493  ? 100.697 119.677 145.853 1.00 47.12  ? 176  TYR C CB  1 
ATOM   13019 C  CG  . TYR C 2 493  ? 101.318 118.304 146.043 1.00 55.99  ? 176  TYR C CG  1 
ATOM   13020 C  CD1 . TYR C 2 493  ? 100.588 117.147 145.795 1.00 49.72  ? 176  TYR C CD1 1 
ATOM   13021 C  CD2 . TYR C 2 493  ? 102.650 118.166 146.442 1.00 57.33  ? 176  TYR C CD2 1 
ATOM   13022 C  CE1 . TYR C 2 493  ? 101.154 115.891 145.984 1.00 48.75  ? 176  TYR C CE1 1 
ATOM   13023 C  CE2 . TYR C 2 493  ? 103.228 116.915 146.619 1.00 52.66  ? 176  TYR C CE2 1 
ATOM   13024 C  CZ  . TYR C 2 493  ? 102.471 115.780 146.387 1.00 54.39  ? 176  TYR C CZ  1 
ATOM   13025 O  OH  . TYR C 2 493  ? 103.028 114.528 146.552 1.00 59.98  ? 176  TYR C OH  1 
ATOM   13026 N  N   . GLU C 2 494  ? 100.211 120.191 148.869 1.00 42.53  ? 177  GLU C N   1 
ATOM   13027 C  CA  . GLU C 2 494  ? 100.391 119.844 150.273 1.00 46.47  ? 177  GLU C CA  1 
ATOM   13028 C  C   . GLU C 2 494  ? 100.111 121.078 151.102 1.00 58.01  ? 177  GLU C C   1 
ATOM   13029 O  O   . GLU C 2 494  ? 101.032 121.822 151.447 1.00 65.73  ? 177  GLU C O   1 
ATOM   13030 C  CB  . GLU C 2 494  ? 101.779 119.318 150.532 1.00 54.91  ? 177  GLU C CB  1 
ATOM   13031 C  CG  . GLU C 2 494  ? 101.988 117.898 150.124 1.00 61.43  ? 177  GLU C CG  1 
ATOM   13032 C  CD  . GLU C 2 494  ? 101.402 116.937 151.139 1.00 74.32  ? 177  GLU C CD  1 
ATOM   13033 O  OE1 . GLU C 2 494  ? 101.394 115.712 150.881 1.00 72.52  ? 177  GLU C OE1 1 
ATOM   13034 O  OE2 . GLU C 2 494  ? 100.984 117.409 152.220 1.00 71.73  ? 177  GLU C OE2 1 
ATOM   13035 N  N   . GLU C 2 495  ? 98.850  121.292 151.437 1.00 64.07  ? 178  GLU C N   1 
ATOM   13036 C  CA  . GLU C 2 495  ? 98.498  122.435 152.260 1.00 85.44  ? 178  GLU C CA  1 
ATOM   13037 C  C   . GLU C 2 495  ? 98.625  122.074 153.740 1.00 99.60  ? 178  GLU C C   1 
ATOM   13038 O  O   . GLU C 2 495  ? 98.522  120.904 154.126 1.00 93.67  ? 178  GLU C O   1 
ATOM   13039 C  CB  . GLU C 2 495  ? 97.080  122.930 151.939 1.00 94.69  ? 178  GLU C CB  1 
ATOM   13040 C  CG  . GLU C 2 495  ? 95.949  121.954 152.273 1.00 102.88 ? 178  GLU C CG  1 
ATOM   13041 C  CD  . GLU C 2 495  ? 94.547  122.570 152.121 1.00 103.59 ? 178  GLU C CD  1 
ATOM   13042 O  OE1 . GLU C 2 495  ? 94.427  123.704 151.598 1.00 88.75  ? 178  GLU C OE1 1 
ATOM   13043 O  OE2 . GLU C 2 495  ? 93.563  121.915 152.536 1.00 107.48 ? 178  GLU C OE2 1 
ATOM   13044 N  N   . SER C 2 496  ? 98.883  123.095 154.564 1.00 107.29 ? 179  SER C N   1 
ATOM   13045 C  CA  . SER C 2 496  ? 99.017  122.924 156.017 1.00 107.27 ? 179  SER C CA  1 
ATOM   13046 C  C   . SER C 2 496  ? 97.651  122.699 156.676 1.00 108.96 ? 179  SER C C   1 
ATOM   13047 O  O   . SER C 2 496  ? 96.609  123.083 156.132 1.00 105.04 ? 179  SER C O   1 
ATOM   13048 C  CB  . SER C 2 496  ? 99.705  124.141 156.653 1.00 99.21  ? 179  SER C CB  1 
ATOM   13049 O  OG  . SER C 2 496  ? 98.932  125.321 156.492 1.00 95.91  ? 179  SER C OG  1 
ATOM   13050 N  N   . PRO D 2 437  ? 127.984 159.646 171.694 1.00 90.00  ? 120  PRO D N   1 
ATOM   13051 C  CA  . PRO D 2 437  ? 126.930 158.622 171.597 1.00 104.99 ? 120  PRO D CA  1 
ATOM   13052 C  C   . PRO D 2 437  ? 127.384 157.177 171.907 1.00 107.87 ? 120  PRO D C   1 
ATOM   13053 O  O   . PRO D 2 437  ? 126.891 156.238 171.290 1.00 105.91 ? 120  PRO D O   1 
ATOM   13054 C  CB  . PRO D 2 437  ? 126.459 158.766 170.147 1.00 92.26  ? 120  PRO D CB  1 
ATOM   13055 C  CG  . PRO D 2 437  ? 126.659 160.227 169.859 1.00 73.28  ? 120  PRO D CG  1 
ATOM   13056 C  CD  . PRO D 2 437  ? 127.911 160.627 170.596 1.00 73.28  ? 120  PRO D CD  1 
ATOM   13057 N  N   . VAL D 2 438  ? 128.285 157.031 172.890 1.00 121.63 ? 121  VAL D N   1 
ATOM   13058 C  CA  . VAL D 2 438  ? 128.763 155.717 173.348 1.00 135.69 ? 121  VAL D CA  1 
ATOM   13059 C  C   . VAL D 2 438  ? 127.644 154.911 174.019 1.00 137.33 ? 121  VAL D C   1 
ATOM   13060 O  O   . VAL D 2 438  ? 127.629 153.669 173.948 1.00 135.59 ? 121  VAL D O   1 
ATOM   13061 C  CB  . VAL D 2 438  ? 129.984 155.886 174.295 1.00 137.69 ? 121  VAL D CB  1 
ATOM   13062 C  CG1 . VAL D 2 438  ? 130.587 154.522 174.704 1.00 132.62 ? 121  VAL D CG1 1 
ATOM   13063 C  CG2 . VAL D 2 438  ? 131.056 156.779 173.662 1.00 124.31 ? 121  VAL D CG2 1 
ATOM   13064 N  N   . TYR D 2 439  ? 126.716 155.587 174.711 1.00 137.34 ? 122  TYR D N   1 
ATOM   13065 C  CA  . TYR D 2 439  ? 125.562 154.888 175.281 1.00 140.78 ? 122  TYR D CA  1 
ATOM   13066 C  C   . TYR D 2 439  ? 124.698 154.267 174.186 1.00 133.52 ? 122  TYR D C   1 
ATOM   13067 O  O   . TYR D 2 439  ? 124.115 153.187 174.381 1.00 129.79 ? 122  TYR D O   1 
ATOM   13068 C  CB  . TYR D 2 439  ? 124.742 155.846 176.159 1.00 144.61 ? 122  TYR D CB  1 
ATOM   13069 C  CG  . TYR D 2 439  ? 125.548 156.576 177.230 1.00 147.34 ? 122  TYR D CG  1 
ATOM   13070 C  CD1 . TYR D 2 439  ? 126.625 155.956 177.875 1.00 146.37 ? 122  TYR D CD1 1 
ATOM   13071 C  CD2 . TYR D 2 439  ? 125.246 157.893 177.577 1.00 144.51 ? 122  TYR D CD2 1 
ATOM   13072 C  CE1 . TYR D 2 439  ? 127.365 156.622 178.852 1.00 144.97 ? 122  TYR D CE1 1 
ATOM   13073 C  CE2 . TYR D 2 439  ? 125.982 158.569 178.547 1.00 145.97 ? 122  TYR D CE2 1 
ATOM   13074 C  CZ  . TYR D 2 439  ? 127.040 157.930 179.180 1.00 145.70 ? 122  TYR D CZ  1 
ATOM   13075 O  OH  . TYR D 2 439  ? 127.769 158.600 180.142 1.00 133.77 ? 122  TYR D OH  1 
ATOM   13076 N  N   . ASP D 2 440  ? 124.635 154.916 173.018 1.00 126.66 ? 123  ASP D N   1 
ATOM   13077 C  CA  . ASP D 2 440  ? 123.968 154.316 171.867 1.00 127.88 ? 123  ASP D CA  1 
ATOM   13078 C  C   . ASP D 2 440  ? 124.664 153.024 171.430 1.00 125.14 ? 123  ASP D C   1 
ATOM   13079 O  O   . ASP D 2 440  ? 123.997 152.040 171.081 1.00 118.03 ? 123  ASP D O   1 
ATOM   13080 C  CB  . ASP D 2 440  ? 123.903 155.337 170.725 1.00 126.98 ? 123  ASP D CB  1 
ATOM   13081 C  CG  . ASP D 2 440  ? 123.032 156.547 171.068 1.00 131.05 ? 123  ASP D CG  1 
ATOM   13082 O  OD1 . ASP D 2 440  ? 122.072 156.389 171.859 1.00 130.52 ? 123  ASP D OD1 1 
ATOM   13083 O  OD2 . ASP D 2 440  ? 123.316 157.656 170.561 1.00 126.58 ? 123  ASP D OD2 1 
ATOM   13084 N  N   . MET D 2 441  ? 126.004 153.003 171.455 1.00 128.40 ? 124  MET D N   1 
ATOM   13085 C  CA  . MET D 2 441  ? 126.740 151.784 171.117 1.00 120.38 ? 124  MET D CA  1 
ATOM   13086 C  C   . MET D 2 441  ? 126.446 150.669 172.117 1.00 109.07 ? 124  MET D C   1 
ATOM   13087 O  O   . MET D 2 441  ? 126.278 149.511 171.725 1.00 106.90 ? 124  MET D O   1 
ATOM   13088 C  CB  . MET D 2 441  ? 128.252 152.049 171.059 1.00 126.37 ? 124  MET D CB  1 
ATOM   13089 C  CG  . MET D 2 441  ? 128.697 153.276 170.248 1.00 133.05 ? 124  MET D CG  1 
ATOM   13090 S  SD  . MET D 2 441  ? 128.186 153.326 168.515 1.00 133.43 ? 124  MET D SD  1 
ATOM   13091 C  CE  . MET D 2 441  ? 126.870 154.553 168.609 1.00 128.43 ? 124  MET D CE  1 
ATOM   13092 N  N   . ALA D 2 442  ? 126.394 150.993 173.415 1.00 113.07 ? 125  ALA D N   1 
ATOM   13093 C  CA  . ALA D 2 442  ? 126.079 149.967 174.410 1.00 105.66 ? 125  ALA D CA  1 
ATOM   13094 C  C   . ALA D 2 442  ? 124.673 149.420 174.210 1.00 97.97  ? 125  ALA D C   1 
ATOM   13095 O  O   . ALA D 2 442  ? 124.456 148.204 174.295 1.00 98.31  ? 125  ALA D O   1 
ATOM   13096 C  CB  . ALA D 2 442  ? 126.237 150.516 175.827 1.00 109.00 ? 125  ALA D CB  1 
ATOM   13097 N  N   . LYS D 2 443  ? 123.707 150.298 173.920 1.00 100.40 ? 126  LYS D N   1 
ATOM   13098 C  CA  . LYS D 2 443  ? 122.336 149.838 173.701 1.00 103.70 ? 126  LYS D CA  1 
ATOM   13099 C  C   . LYS D 2 443  ? 122.224 148.950 172.461 1.00 103.36 ? 126  LYS D C   1 
ATOM   13100 O  O   . LYS D 2 443  ? 121.582 147.890 172.496 1.00 98.35  ? 126  LYS D O   1 
ATOM   13101 C  CB  . LYS D 2 443  ? 121.383 151.032 173.603 1.00 102.86 ? 126  LYS D CB  1 
ATOM   13102 C  CG  . LYS D 2 443  ? 119.942 150.649 173.267 1.00 98.36  ? 126  LYS D CG  1 
ATOM   13103 C  CD  . LYS D 2 443  ? 119.378 149.636 174.263 1.00 105.42 ? 126  LYS D CD  1 
ATOM   13104 C  CE  . LYS D 2 443  ? 119.301 150.194 175.678 1.00 107.62 ? 126  LYS D CE  1 
ATOM   13105 N  NZ  . LYS D 2 443  ? 118.755 149.186 176.634 1.00 95.48  ? 126  LYS D NZ  1 
ATOM   13106 N  N   . THR D 2 444  ? 122.843 149.361 171.351 1.00 107.04 ? 127  THR D N   1 
ATOM   13107 C  CA  . THR D 2 444  ? 122.742 148.560 170.131 1.00 106.09 ? 127  THR D CA  1 
ATOM   13108 C  C   . THR D 2 444  ? 123.542 147.259 170.227 1.00 91.30  ? 127  THR D C   1 
ATOM   13109 O  O   . THR D 2 444  ? 123.122 146.243 169.673 1.00 92.61  ? 127  THR D O   1 
ATOM   13110 C  CB  . THR D 2 444  ? 123.154 149.395 168.899 1.00 112.96 ? 127  THR D CB  1 
ATOM   13111 O  OG1 . THR D 2 444  ? 122.900 148.659 167.689 1.00 99.38  ? 127  THR D OG1 1 
ATOM   13112 C  CG2 . THR D 2 444  ? 124.609 149.823 168.959 1.00 112.75 ? 127  THR D CG2 1 
ATOM   13113 N  N   . ILE D 2 445  ? 124.669 147.249 170.931 1.00 85.98  ? 128  ILE D N   1 
ATOM   13114 C  CA  . ILE D 2 445  ? 125.362 145.991 171.137 1.00 72.86  ? 128  ILE D CA  1 
ATOM   13115 C  C   . ILE D 2 445  ? 124.518 145.076 172.004 1.00 76.47  ? 128  ILE D C   1 
ATOM   13116 O  O   . ILE D 2 445  ? 124.477 143.864 171.780 1.00 89.33  ? 128  ILE D O   1 
ATOM   13117 C  CB  . ILE D 2 445  ? 126.755 146.239 171.743 1.00 95.44  ? 128  ILE D CB  1 
ATOM   13118 C  CG1 . ILE D 2 445  ? 127.705 146.844 170.697 1.00 104.60 ? 128  ILE D CG1 1 
ATOM   13119 C  CG2 . ILE D 2 445  ? 127.341 144.947 172.317 1.00 94.35  ? 128  ILE D CG2 1 
ATOM   13120 C  CD1 . ILE D 2 445  ? 129.090 147.238 171.250 1.00 105.17 ? 128  ILE D CD1 1 
ATOM   13121 N  N   . SER D 2 446  ? 123.826 145.627 173.001 1.00 80.35  ? 129  SER D N   1 
ATOM   13122 C  CA  . SER D 2 446  ? 122.938 144.789 173.797 1.00 82.33  ? 129  SER D CA  1 
ATOM   13123 C  C   . SER D 2 446  ? 121.825 144.222 172.943 1.00 80.26  ? 129  SER D C   1 
ATOM   13124 O  O   . SER D 2 446  ? 121.469 143.044 173.068 1.00 87.92  ? 129  SER D O   1 
ATOM   13125 C  CB  . SER D 2 446  ? 122.343 145.575 174.960 1.00 94.60  ? 129  SER D CB  1 
ATOM   13126 O  OG  . SER D 2 446  ? 121.407 144.774 175.663 1.00 96.30  ? 129  SER D OG  1 
ATOM   13127 N  N   . SER D 2 447  ? 121.276 145.042 172.055 1.00 78.76  ? 130  SER D N   1 
ATOM   13128 C  CA  . SER D 2 447  ? 120.234 144.561 171.157 1.00 90.13  ? 130  SER D CA  1 
ATOM   13129 C  C   . SER D 2 447  ? 120.762 143.471 170.220 1.00 94.27  ? 130  SER D C   1 
ATOM   13130 O  O   . SER D 2 447  ? 120.089 142.457 169.985 1.00 94.02  ? 130  SER D O   1 
ATOM   13131 C  CB  . SER D 2 447  ? 119.661 145.734 170.361 1.00 94.11  ? 130  SER D CB  1 
ATOM   13132 O  OG  . SER D 2 447  ? 119.126 146.717 171.232 1.00 98.64  ? 130  SER D OG  1 
ATOM   13133 N  N   . LEU D 2 448  ? 121.968 143.666 169.677 1.00 93.30  ? 131  LEU D N   1 
ATOM   13134 C  CA  . LEU D 2 448  ? 122.543 142.723 168.721 1.00 87.74  ? 131  LEU D CA  1 
ATOM   13135 C  C   . LEU D 2 448  ? 122.864 141.394 169.388 1.00 82.20  ? 131  LEU D C   1 
ATOM   13136 O  O   . LEU D 2 448  ? 122.596 140.324 168.828 1.00 91.99  ? 131  LEU D O   1 
ATOM   13137 C  CB  . LEU D 2 448  ? 123.797 143.330 168.088 1.00 88.89  ? 131  LEU D CB  1 
ATOM   13138 C  CG  . LEU D 2 448  ? 124.489 142.594 166.943 1.00 97.77  ? 131  LEU D CG  1 
ATOM   13139 C  CD1 . LEU D 2 448  ? 123.504 142.340 165.800 1.00 87.56  ? 131  LEU D CD1 1 
ATOM   13140 C  CD2 . LEU D 2 448  ? 125.695 143.396 166.456 1.00 92.66  ? 131  LEU D CD2 1 
ATOM   13141 N  N   . ASN D 2 449  ? 123.429 141.439 170.585 1.00 72.94  ? 132  ASN D N   1 
ATOM   13142 C  CA  . ASN D 2 449  ? 123.629 140.205 171.315 1.00 75.34  ? 132  ASN D CA  1 
ATOM   13143 C  C   . ASN D 2 449  ? 122.300 139.548 171.642 1.00 82.04  ? 132  ASN D C   1 
ATOM   13144 O  O   . ASN D 2 449  ? 122.187 138.318 171.600 1.00 89.43  ? 132  ASN D O   1 
ATOM   13145 C  CB  . ASN D 2 449  ? 124.434 140.469 172.576 1.00 85.94  ? 132  ASN D CB  1 
ATOM   13146 C  CG  . ASN D 2 449  ? 125.914 140.564 172.297 1.00 92.68  ? 132  ASN D CG  1 
ATOM   13147 O  OD1 . ASN D 2 449  ? 126.652 139.590 172.449 1.00 94.88  ? 132  ASN D OD1 1 
ATOM   13148 N  ND2 . ASN D 2 449  ? 126.358 141.739 171.869 1.00 95.86  ? 132  ASN D ND2 1 
ATOM   13149 N  N   . ARG D 2 450  ? 121.275 140.340 171.960 1.00 75.99  ? 133  ARG D N   1 
ATOM   13150 C  CA  . ARG D 2 450  ? 119.983 139.738 172.257 1.00 78.31  ? 133  ARG D CA  1 
ATOM   13151 C  C   . ARG D 2 450  ? 119.448 138.971 171.052 1.00 91.89  ? 133  ARG D C   1 
ATOM   13152 O  O   . ARG D 2 450  ? 118.973 137.834 171.186 1.00 94.75  ? 133  ARG D O   1 
ATOM   13153 C  CB  . ARG D 2 450  ? 118.992 140.810 172.701 1.00 88.91  ? 133  ARG D CB  1 
ATOM   13154 C  CG  . ARG D 2 450  ? 117.829 140.267 173.522 1.00 97.99  ? 133  ARG D CG  1 
ATOM   13155 C  CD  . ARG D 2 450  ? 118.324 139.707 174.850 1.00 110.19 ? 133  ARG D CD  1 
ATOM   13156 N  NE  . ARG D 2 450  ? 119.314 140.591 175.468 1.00 117.74 ? 133  ARG D NE  1 
ATOM   13157 C  CZ  . ARG D 2 450  ? 119.015 141.646 176.225 1.00 120.48 ? 133  ARG D CZ  1 
ATOM   13158 N  NH1 . ARG D 2 450  ? 119.988 142.393 176.740 1.00 108.17 ? 133  ARG D NH1 1 
ATOM   13159 N  NH2 . ARG D 2 450  ? 117.744 141.958 176.464 1.00 119.02 ? 133  ARG D NH2 1 
ATOM   13160 N  N   . VAL D 2 451  ? 119.535 139.570 169.854 1.00 96.84  ? 134  VAL D N   1 
ATOM   13161 C  CA  . VAL D 2 451  ? 118.971 138.914 168.663 1.00 95.43  ? 134  VAL D CA  1 
ATOM   13162 C  C   . VAL D 2 451  ? 119.826 137.715 168.222 1.00 90.96  ? 134  VAL D C   1 
ATOM   13163 O  O   . VAL D 2 451  ? 119.284 136.711 167.736 1.00 91.69  ? 134  VAL D O   1 
ATOM   13164 C  CB  . VAL D 2 451  ? 118.732 139.911 167.499 1.00 91.97  ? 134  VAL D CB  1 
ATOM   13165 C  CG1 . VAL D 2 451  ? 117.793 141.068 167.925 1.00 90.22  ? 134  VAL D CG1 1 
ATOM   13166 C  CG2 . VAL D 2 451  ? 120.044 140.439 166.910 1.00 89.32  ? 134  VAL D CG2 1 
ATOM   13167 N  N   . CYS D 2 452  ? 121.156 137.768 168.397 1.00 82.53  ? 135  CYS D N   1 
ATOM   13168 C  CA  . CYS D 2 452  ? 121.966 136.583 168.104 1.00 75.51  ? 135  CYS D CA  1 
ATOM   13169 C  C   . CYS D 2 452  ? 121.682 135.442 169.075 1.00 76.09  ? 135  CYS D C   1 
ATOM   13170 O  O   . CYS D 2 452  ? 121.652 134.272 168.672 1.00 79.78  ? 135  CYS D O   1 
ATOM   13171 C  CB  . CYS D 2 452  ? 123.447 136.926 168.114 1.00 75.19  ? 135  CYS D CB  1 
ATOM   13172 S  SG  . CYS D 2 452  ? 123.909 137.957 166.727 1.00 98.79  ? 135  CYS D SG  1 
ATOM   13173 N  N   . ALA D 2 453  ? 121.482 135.751 170.356 1.00 81.18  ? 136  ALA D N   1 
ATOM   13174 C  CA  . ALA D 2 453  ? 121.079 134.706 171.293 1.00 87.73  ? 136  ALA D CA  1 
ATOM   13175 C  C   . ALA D 2 453  ? 119.719 134.125 170.913 1.00 78.86  ? 136  ALA D C   1 
ATOM   13176 O  O   . ALA D 2 453  ? 119.497 132.909 171.018 1.00 81.65  ? 136  ALA D O   1 
ATOM   13177 C  CB  . ALA D 2 453  ? 121.056 135.255 172.724 1.00 90.94  ? 136  ALA D CB  1 
ATOM   13178 N  N   . GLU D 2 454  ? 118.798 134.972 170.461 1.00 71.51  ? 137  GLU D N   1 
ATOM   13179 C  CA  . GLU D 2 454  ? 117.510 134.449 170.034 1.00 78.86  ? 137  GLU D CA  1 
ATOM   13180 C  C   . GLU D 2 454  ? 117.675 133.527 168.829 1.00 80.20  ? 137  GLU D C   1 
ATOM   13181 O  O   . GLU D 2 454  ? 117.013 132.485 168.746 1.00 83.94  ? 137  GLU D O   1 
ATOM   13182 C  CB  . GLU D 2 454  ? 116.542 135.601 169.741 1.00 95.60  ? 137  GLU D CB  1 
ATOM   13183 C  CG  . GLU D 2 454  ? 115.081 135.175 169.459 1.00 106.51 ? 137  GLU D CG  1 
ATOM   13184 C  CD  . GLU D 2 454  ? 114.125 136.366 169.273 1.00 117.06 ? 137  GLU D CD  1 
ATOM   13185 O  OE1 . GLU D 2 454  ? 114.591 137.531 169.316 1.00 109.82 ? 137  GLU D OE1 1 
ATOM   13186 O  OE2 . GLU D 2 454  ? 112.907 136.132 169.089 1.00 113.05 ? 137  GLU D OE2 1 
ATOM   13187 N  N   . MET D 2 455  ? 118.573 133.874 167.894 1.00 79.24  ? 138  MET D N   1 
ATOM   13188 C  CA  . MET D 2 455  ? 118.767 133.021 166.714 1.00 81.89  ? 138  MET D CA  1 
ATOM   13189 C  C   . MET D 2 455  ? 119.412 131.691 167.075 1.00 69.41  ? 138  MET D C   1 
ATOM   13190 O  O   . MET D 2 455  ? 119.099 130.658 166.474 1.00 69.50  ? 138  MET D O   1 
ATOM   13191 C  CB  . MET D 2 455  ? 119.624 133.702 165.650 1.00 83.45  ? 138  MET D CB  1 
ATOM   13192 C  CG  . MET D 2 455  ? 119.714 132.879 164.356 1.00 74.63  ? 138  MET D CG  1 
ATOM   13193 S  SD  . MET D 2 455  ? 120.897 133.543 163.191 1.00 106.71 ? 138  MET D SD  1 
ATOM   13194 C  CE  . MET D 2 455  ? 120.290 135.225 163.072 1.00 84.78  ? 138  MET D CE  1 
ATOM   13195 N  N   . VAL D 2 456  ? 120.348 131.702 168.015 1.00 65.31  ? 139  VAL D N   1 
ATOM   13196 C  CA  . VAL D 2 456  ? 120.906 130.441 168.472 1.00 58.15  ? 139  VAL D CA  1 
ATOM   13197 C  C   . VAL D 2 456  ? 119.815 129.591 169.099 1.00 49.89  ? 139  VAL D C   1 
ATOM   13198 O  O   . VAL D 2 456  ? 119.739 128.384 168.866 1.00 57.57  ? 139  VAL D O   1 
ATOM   13199 C  CB  . VAL D 2 456  ? 122.064 130.697 169.450 1.00 73.05  ? 139  VAL D CB  1 
ATOM   13200 C  CG1 . VAL D 2 456  ? 122.494 129.388 170.111 1.00 78.34  ? 139  VAL D CG1 1 
ATOM   13201 C  CG2 . VAL D 2 456  ? 123.231 131.391 168.734 1.00 74.04  ? 139  VAL D CG2 1 
ATOM   13202 N  N   . ALA D 2 457  ? 118.952 130.207 169.899 1.00 56.71  ? 140  ALA D N   1 
ATOM   13203 C  CA  . ALA D 2 457  ? 117.878 129.450 170.523 1.00 58.15  ? 140  ALA D CA  1 
ATOM   13204 C  C   . ALA D 2 457  ? 116.942 128.861 169.478 1.00 56.67  ? 140  ALA D C   1 
ATOM   13205 O  O   . ALA D 2 457  ? 116.431 127.749 169.651 1.00 63.02  ? 140  ALA D O   1 
ATOM   13206 C  CB  . ALA D 2 457  ? 117.107 130.340 171.497 1.00 71.46  ? 140  ALA D CB  1 
ATOM   13207 N  N   . LYS D 2 458  ? 116.685 129.598 168.396 1.00 60.53  ? 141  LYS D N   1 
ATOM   13208 C  CA  . LYS D 2 458  ? 115.801 129.082 167.349 1.00 65.97  ? 141  LYS D CA  1 
ATOM   13209 C  C   . LYS D 2 458  ? 116.483 128.003 166.499 1.00 59.88  ? 141  LYS D C   1 
ATOM   13210 O  O   . LYS D 2 458  ? 115.815 127.072 166.034 1.00 64.05  ? 141  LYS D O   1 
ATOM   13211 C  CB  . LYS D 2 458  ? 115.295 130.229 166.457 1.00 74.00  ? 141  LYS D CB  1 
ATOM   13212 C  CG  . LYS D 2 458  ? 114.560 131.375 167.188 1.00 81.34  ? 141  LYS D CG  1 
ATOM   13213 C  CD  . LYS D 2 458  ? 113.274 130.929 167.891 1.00 87.59  ? 141  LYS D CD  1 
ATOM   13214 C  CE  . LYS D 2 458  ? 112.079 130.930 166.935 1.00 88.59  ? 141  LYS D CE  1 
ATOM   13215 N  NZ  . LYS D 2 458  ? 111.829 132.307 166.414 1.00 81.49  ? 141  LYS D NZ  1 
ATOM   13216 N  N   . TYR D 2 459  ? 117.797 128.111 166.289 1.00 48.73  ? 142  TYR D N   1 
ATOM   13217 C  CA  . TYR D 2 459  ? 118.543 127.088 165.565 1.00 35.31  ? 142  TYR D CA  1 
ATOM   13218 C  C   . TYR D 2 459  ? 118.375 125.719 166.191 1.00 43.10  ? 142  TYR D C   1 
ATOM   13219 O  O   . TYR D 2 459  ? 118.015 124.754 165.513 1.00 56.55  ? 142  TYR D O   1 
ATOM   13220 C  CB  . TYR D 2 459  ? 120.014 127.440 165.573 1.00 47.37  ? 142  TYR D CB  1 
ATOM   13221 C  CG  . TYR D 2 459  ? 120.927 126.290 165.222 1.00 50.67  ? 142  TYR D CG  1 
ATOM   13222 C  CD1 . TYR D 2 459  ? 121.406 125.427 166.199 1.00 46.77  ? 142  TYR D CD1 1 
ATOM   13223 C  CD2 . TYR D 2 459  ? 121.399 126.134 163.942 1.00 55.87  ? 142  TYR D CD2 1 
ATOM   13224 C  CE1 . TYR D 2 459  ? 122.247 124.410 165.892 1.00 42.27  ? 142  TYR D CE1 1 
ATOM   13225 C  CE2 . TYR D 2 459  ? 122.262 125.121 163.633 1.00 51.52  ? 142  TYR D CE2 1 
ATOM   13226 C  CZ  . TYR D 2 459  ? 122.682 124.269 164.611 1.00 46.01  ? 142  TYR D CZ  1 
ATOM   13227 O  OH  . TYR D 2 459  ? 123.540 123.255 164.277 1.00 59.19  ? 142  TYR D OH  1 
ATOM   13228 N  N   . ASP D 2 460  ? 118.673 125.604 167.480 1.00 41.75  ? 143  ASP D N   1 
ATOM   13229 C  CA  . ASP D 2 460  ? 118.596 124.304 168.114 1.00 42.90  ? 143  ASP D CA  1 
ATOM   13230 C  C   . ASP D 2 460  ? 117.176 123.791 168.147 1.00 48.60  ? 143  ASP D C   1 
ATOM   13231 O  O   . ASP D 2 460  ? 116.969 122.594 168.371 1.00 58.99  ? 143  ASP D O   1 
ATOM   13232 C  CB  . ASP D 2 460  ? 119.104 124.344 169.549 1.00 59.65  ? 143  ASP D CB  1 
ATOM   13233 C  CG  . ASP D 2 460  ? 118.339 125.350 170.410 1.00 74.37  ? 143  ASP D CG  1 
ATOM   13234 O  OD1 . ASP D 2 460  ? 117.141 125.106 170.695 1.00 72.25  ? 143  ASP D OD1 1 
ATOM   13235 O  OD2 . ASP D 2 460  ? 118.928 126.383 170.811 1.00 71.67  ? 143  ASP D OD2 1 
ATOM   13236 N  N   . LEU D 2 461  ? 116.191 124.662 167.976 1.00 43.14  ? 144  LEU D N   1 
ATOM   13237 C  CA  . LEU D 2 461  ? 114.850 124.129 167.837 1.00 52.97  ? 144  LEU D CA  1 
ATOM   13238 C  C   . LEU D 2 461  ? 114.588 123.615 166.416 1.00 60.14  ? 144  LEU D C   1 
ATOM   13239 O  O   . LEU D 2 461  ? 113.868 122.620 166.256 1.00 62.80  ? 144  LEU D O   1 
ATOM   13240 C  CB  . LEU D 2 461  ? 113.819 125.173 168.263 1.00 63.74  ? 144  LEU D CB  1 
ATOM   13241 C  CG  . LEU D 2 461  ? 112.370 124.672 168.409 1.00 82.56  ? 144  LEU D CG  1 
ATOM   13242 C  CD1 . LEU D 2 461  ? 112.277 123.380 169.255 1.00 72.46  ? 144  LEU D CD1 1 
ATOM   13243 C  CD2 . LEU D 2 461  ? 111.446 125.781 168.951 1.00 82.60  ? 144  LEU D CD2 1 
ATOM   13244 N  N   . LEU D 2 462  ? 115.176 124.230 165.379 1.00 49.48  ? 145  LEU D N   1 
ATOM   13245 C  CA  . LEU D 2 462  ? 115.046 123.660 164.040 1.00 41.05  ? 145  LEU D CA  1 
ATOM   13246 C  C   . LEU D 2 462  ? 115.912 122.435 163.869 1.00 43.89  ? 145  LEU D C   1 
ATOM   13247 O  O   . LEU D 2 462  ? 115.413 121.343 163.585 1.00 56.97  ? 145  LEU D O   1 
ATOM   13248 C  CB  . LEU D 2 462  ? 115.408 124.659 162.952 1.00 46.53  ? 145  LEU D CB  1 
ATOM   13249 C  CG  . LEU D 2 462  ? 114.387 125.777 162.859 1.00 70.64  ? 145  LEU D CG  1 
ATOM   13250 C  CD1 . LEU D 2 462  ? 114.793 126.795 161.784 1.00 62.63  ? 145  LEU D CD1 1 
ATOM   13251 C  CD2 . LEU D 2 462  ? 112.989 125.177 162.625 1.00 69.12  ? 145  LEU D CD2 1 
ATOM   13252 N  N   . VAL D 2 463  ? 117.195 122.600 164.010 1.00 35.33  ? 146  VAL D N   1 
ATOM   13253 C  CA  . VAL D 2 463  ? 118.139 121.531 163.731 1.00 35.85  ? 146  VAL D CA  1 
ATOM   13254 C  C   . VAL D 2 463  ? 118.132 120.478 164.819 1.00 46.68  ? 146  VAL D C   1 
ATOM   13255 O  O   . VAL D 2 463  ? 118.173 120.801 166.009 1.00 55.34  ? 146  VAL D O   1 
ATOM   13256 C  CB  . VAL D 2 463  ? 119.532 122.120 163.579 1.00 48.73  ? 146  VAL D CB  1 
ATOM   13257 C  CG1 . VAL D 2 463  ? 120.488 121.025 163.228 1.00 51.45  ? 146  VAL D CG1 1 
ATOM   13258 C  CG2 . VAL D 2 463  ? 119.471 123.205 162.499 1.00 62.38  ? 146  VAL D CG2 1 
ATOM   13259 N  N   . MET D 2 464  ? 118.113 119.206 164.413 1.00 45.01  ? 147  MET D N   1 
ATOM   13260 C  CA  . MET D 2 464  ? 118.273 118.129 165.380 1.00 46.03  ? 147  MET D CA  1 
ATOM   13261 C  C   . MET D 2 464  ? 119.651 118.209 166.017 1.00 63.10  ? 147  MET D C   1 
ATOM   13262 O  O   . MET D 2 464  ? 120.645 118.512 165.352 1.00 65.20  ? 147  MET D O   1 
ATOM   13263 C  CB  . MET D 2 464  ? 118.107 116.771 164.732 1.00 44.81  ? 147  MET D CB  1 
ATOM   13264 C  CG  . MET D 2 464  ? 116.729 116.486 164.228 1.00 63.29  ? 147  MET D CG  1 
ATOM   13265 S  SD  . MET D 2 464  ? 116.384 114.718 164.413 1.00 84.03  ? 147  MET D SD  1 
ATOM   13266 C  CE  . MET D 2 464  ? 117.845 114.006 163.643 1.00 62.62  ? 147  MET D CE  1 
ATOM   13267 N  N   . THR D 2 465  ? 119.711 117.935 167.317 1.00 65.62  ? 148  THR D N   1 
ATOM   13268 C  CA  . THR D 2 465  ? 120.949 118.158 168.051 1.00 68.88  ? 148  THR D CA  1 
ATOM   13269 C  C   . THR D 2 465  ? 121.926 117.006 167.848 1.00 71.55  ? 148  THR D C   1 
ATOM   13270 O  O   . THR D 2 465  ? 123.018 117.191 167.300 1.00 70.46  ? 148  THR D O   1 
ATOM   13271 C  CB  . THR D 2 465  ? 120.637 118.369 169.538 1.00 83.76  ? 148  THR D CB  1 
ATOM   13272 O  OG1 . THR D 2 465  ? 119.990 117.201 170.066 1.00 82.83  ? 148  THR D OG1 1 
ATOM   13273 C  CG2 . THR D 2 465  ? 119.742 119.613 169.744 1.00 74.47  ? 148  THR D CG2 1 
ATOM   13274 N  N   . THR D 2 466  ? 121.545 115.808 168.284 1.00 81.82  ? 149  THR D N   1 
ATOM   13275 C  CA  . THR D 2 466  ? 122.393 114.621 168.138 1.00 92.47  ? 149  THR D CA  1 
ATOM   13276 C  C   . THR D 2 466  ? 121.557 113.397 167.718 1.00 91.66  ? 149  THR D C   1 
ATOM   13277 O  O   . THR D 2 466  ? 121.510 112.375 168.412 1.00 87.63  ? 149  THR D O   1 
ATOM   13278 C  CB  . THR D 2 466  ? 123.171 114.304 169.449 1.00 85.64  ? 149  THR D CB  1 
ATOM   13279 O  OG1 . THR D 2 466  ? 122.305 114.474 170.582 1.00 83.78  ? 149  THR D OG1 1 
ATOM   13280 C  CG2 . THR D 2 466  ? 124.405 115.210 169.585 1.00 78.04  ? 149  THR D CG2 1 
ATOM   13281 N  N   . ASP E 2 440  ? 133.317 155.544 163.975 1.00 67.11  ? 123  ASP E N   1 
ATOM   13282 C  CA  . ASP E 2 440  ? 132.356 155.214 162.906 1.00 96.63  ? 123  ASP E CA  1 
ATOM   13283 C  C   . ASP E 2 440  ? 131.727 153.813 162.989 1.00 97.30  ? 123  ASP E C   1 
ATOM   13284 O  O   . ASP E 2 440  ? 131.293 153.238 161.987 1.00 88.65  ? 123  ASP E O   1 
ATOM   13285 C  CB  . ASP E 2 440  ? 133.014 155.353 161.537 1.00 110.15 ? 123  ASP E CB  1 
ATOM   13286 C  CG  . ASP E 2 440  ? 133.372 156.780 161.206 1.00 112.70 ? 123  ASP E CG  1 
ATOM   13287 O  OD1 . ASP E 2 440  ? 132.642 157.691 161.652 1.00 108.90 ? 123  ASP E OD1 1 
ATOM   13288 O  OD2 . ASP E 2 440  ? 134.362 156.990 160.473 1.00 113.51 ? 123  ASP E OD2 1 
ATOM   13289 N  N   . MET E 2 441  ? 131.678 153.283 164.201 1.00 100.09 ? 124  MET E N   1 
ATOM   13290 C  CA  . MET E 2 441  ? 131.203 151.929 164.432 1.00 84.09  ? 124  MET E CA  1 
ATOM   13291 C  C   . MET E 2 441  ? 129.684 151.856 164.396 1.00 78.80  ? 124  MET E C   1 
ATOM   13292 O  O   . MET E 2 441  ? 129.126 150.828 164.004 1.00 85.70  ? 124  MET E O   1 
ATOM   13293 C  CB  . MET E 2 441  ? 131.730 151.466 165.788 1.00 97.35  ? 124  MET E CB  1 
ATOM   13294 C  CG  . MET E 2 441  ? 133.268 151.359 165.833 1.00 111.42 ? 124  MET E CG  1 
ATOM   13295 S  SD  . MET E 2 441  ? 134.144 152.976 165.639 1.00 147.10 ? 124  MET E SD  1 
ATOM   13296 C  CE  . MET E 2 441  ? 133.769 153.903 167.131 1.00 94.07  ? 124  MET E CE  1 
ATOM   13297 N  N   . ALA E 2 442  ? 129.015 152.942 164.794 1.00 83.18  ? 125  ALA E N   1 
ATOM   13298 C  CA  . ALA E 2 442  ? 127.569 152.951 164.998 1.00 82.64  ? 125  ALA E CA  1 
ATOM   13299 C  C   . ALA E 2 442  ? 126.834 152.326 163.832 1.00 78.43  ? 125  ALA E C   1 
ATOM   13300 O  O   . ALA E 2 442  ? 126.178 151.285 163.974 1.00 82.07  ? 125  ALA E O   1 
ATOM   13301 C  CB  . ALA E 2 442  ? 127.086 154.387 165.195 1.00 92.49  ? 125  ALA E CB  1 
ATOM   13302 N  N   . LYS E 2 443  ? 126.959 152.947 162.656 1.00 85.76  ? 126  LYS E N   1 
ATOM   13303 C  CA  . LYS E 2 443  ? 126.373 152.412 161.435 1.00 92.79  ? 126  LYS E CA  1 
ATOM   13304 C  C   . LYS E 2 443  ? 126.576 150.898 161.351 1.00 90.37  ? 126  LYS E C   1 
ATOM   13305 O  O   . LYS E 2 443  ? 125.603 150.130 161.304 1.00 82.67  ? 126  LYS E O   1 
ATOM   13306 C  CB  . LYS E 2 443  ? 126.968 153.120 160.206 1.00 97.37  ? 126  LYS E CB  1 
ATOM   13307 C  CG  . LYS E 2 443  ? 126.557 154.593 160.050 1.00 107.17 ? 126  LYS E CG  1 
ATOM   13308 C  CD  . LYS E 2 443  ? 127.231 155.251 158.835 1.00 115.40 ? 126  LYS E CD  1 
ATOM   13309 C  CE  . LYS E 2 443  ? 128.745 155.404 158.999 1.00 113.46 ? 126  LYS E CE  1 
ATOM   13310 N  NZ  . LYS E 2 443  ? 129.116 156.260 160.163 1.00 106.32 ? 126  LYS E NZ  1 
ATOM   13311 N  N   . THR E 2 444  ? 127.839 150.456 161.401 1.00 86.47  ? 127  THR E N   1 
ATOM   13312 C  CA  . THR E 2 444  ? 128.136 149.032 161.313 1.00 71.88  ? 127  THR E CA  1 
ATOM   13313 C  C   . THR E 2 444  ? 127.263 148.248 162.271 1.00 68.39  ? 127  THR E C   1 
ATOM   13314 O  O   . THR E 2 444  ? 126.457 147.412 161.857 1.00 78.22  ? 127  THR E O   1 
ATOM   13315 C  CB  . THR E 2 444  ? 129.605 148.754 161.619 1.00 76.70  ? 127  THR E CB  1 
ATOM   13316 O  OG1 . THR E 2 444  ? 129.820 148.856 163.034 1.00 85.10  ? 127  THR E OG1 1 
ATOM   13317 C  CG2 . THR E 2 444  ? 130.515 149.733 160.865 1.00 85.05  ? 127  THR E CG2 1 
ATOM   13318 N  N   . ILE E 2 445  ? 127.381 148.531 163.557 1.00 61.99  ? 128  ILE E N   1 
ATOM   13319 C  CA  . ILE E 2 445  ? 126.605 147.752 164.502 1.00 63.84  ? 128  ILE E CA  1 
ATOM   13320 C  C   . ILE E 2 445  ? 125.127 147.996 164.299 1.00 63.81  ? 128  ILE E C   1 
ATOM   13321 O  O   . ILE E 2 445  ? 124.331 147.052 164.318 1.00 76.59  ? 128  ILE E O   1 
ATOM   13322 C  CB  . ILE E 2 445  ? 127.098 148.021 165.927 1.00 76.14  ? 128  ILE E CB  1 
ATOM   13323 C  CG1 . ILE E 2 445  ? 127.161 149.517 166.200 1.00 95.09  ? 128  ILE E CG1 1 
ATOM   13324 C  CG2 . ILE E 2 445  ? 128.428 147.373 166.154 1.00 78.89  ? 128  ILE E CG2 1 
ATOM   13325 C  CD1 . ILE E 2 445  ? 127.683 149.837 167.573 1.00 104.76 ? 128  ILE E CD1 1 
ATOM   13326 N  N   . SER E 2 446  ? 124.739 149.228 163.985 1.00 65.06  ? 129  SER E N   1 
ATOM   13327 C  CA  . SER E 2 446  ? 123.332 149.428 163.672 1.00 69.62  ? 129  SER E CA  1 
ATOM   13328 C  C   . SER E 2 446  ? 122.959 148.599 162.461 1.00 71.61  ? 129  SER E C   1 
ATOM   13329 O  O   . SER E 2 446  ? 121.913 147.939 162.444 1.00 75.71  ? 129  SER E O   1 
ATOM   13330 C  CB  . SER E 2 446  ? 123.013 150.904 163.431 1.00 80.98  ? 129  SER E CB  1 
ATOM   13331 O  OG  . SER E 2 446  ? 123.487 151.346 162.172 1.00 84.88  ? 129  SER E OG  1 
ATOM   13332 N  N   . SER E 2 447  ? 123.835 148.570 161.462 1.00 67.78  ? 130  SER E N   1 
ATOM   13333 C  CA  . SER E 2 447  ? 123.535 147.790 160.276 1.00 73.38  ? 130  SER E CA  1 
ATOM   13334 C  C   . SER E 2 447  ? 123.331 146.324 160.631 1.00 66.66  ? 130  SER E C   1 
ATOM   13335 O  O   . SER E 2 447  ? 122.467 145.659 160.053 1.00 74.56  ? 130  SER E O   1 
ATOM   13336 C  CB  . SER E 2 447  ? 124.645 147.960 159.238 1.00 85.67  ? 130  SER E CB  1 
ATOM   13337 O  OG  . SER E 2 447  ? 124.348 147.251 158.042 1.00 85.66  ? 130  SER E OG  1 
ATOM   13338 N  N   . LEU E 2 448  ? 124.088 145.806 161.597 1.00 61.03  ? 131  LEU E N   1 
ATOM   13339 C  CA  . LEU E 2 448  ? 123.865 144.420 161.977 1.00 53.78  ? 131  LEU E CA  1 
ATOM   13340 C  C   . LEU E 2 448  ? 122.479 144.241 162.552 1.00 62.33  ? 131  LEU E C   1 
ATOM   13341 O  O   . LEU E 2 448  ? 121.786 143.274 162.226 1.00 73.63  ? 131  LEU E O   1 
ATOM   13342 C  CB  . LEU E 2 448  ? 124.920 143.955 162.963 1.00 63.61  ? 131  LEU E CB  1 
ATOM   13343 C  CG  . LEU E 2 448  ? 126.293 144.012 162.304 1.00 78.91  ? 131  LEU E CG  1 
ATOM   13344 C  CD1 . LEU E 2 448  ? 127.391 143.533 163.251 1.00 84.21  ? 131  LEU E CD1 1 
ATOM   13345 C  CD2 . LEU E 2 448  ? 126.274 143.210 160.996 1.00 78.03  ? 131  LEU E CD2 1 
ATOM   13346 N  N   . ASN E 2 449  ? 122.037 145.175 163.384 1.00 62.78  ? 132  ASN E N   1 
ATOM   13347 C  CA  . ASN E 2 449  ? 120.679 145.097 163.892 1.00 59.88  ? 132  ASN E CA  1 
ATOM   13348 C  C   . ASN E 2 449  ? 119.664 145.243 162.780 1.00 61.92  ? 132  ASN E C   1 
ATOM   13349 O  O   . ASN E 2 449  ? 118.545 144.735 162.893 1.00 60.81  ? 132  ASN E O   1 
ATOM   13350 C  CB  . ASN E 2 449  ? 120.475 146.178 164.930 1.00 69.24  ? 132  ASN E CB  1 
ATOM   13351 C  CG  . ASN E 2 449  ? 121.384 145.999 166.114 1.00 85.16  ? 132  ASN E CG  1 
ATOM   13352 O  OD1 . ASN E 2 449  ? 122.452 146.610 166.190 1.00 82.99  ? 132  ASN E OD1 1 
ATOM   13353 N  ND2 . ASN E 2 449  ? 120.985 145.136 167.038 1.00 87.81  ? 132  ASN E ND2 1 
ATOM   13354 N  N   . ARG E 2 450  ? 120.041 145.918 161.702 1.00 72.00  ? 133  ARG E N   1 
ATOM   13355 C  CA  . ARG E 2 450  ? 119.172 146.047 160.546 1.00 80.91  ? 133  ARG E CA  1 
ATOM   13356 C  C   . ARG E 2 450  ? 119.075 144.748 159.750 1.00 83.13  ? 133  ARG E C   1 
ATOM   13357 O  O   . ARG E 2 450  ? 118.250 144.676 158.831 1.00 88.26  ? 133  ARG E O   1 
ATOM   13358 C  CB  . ARG E 2 450  ? 119.673 147.189 159.634 1.00 89.98  ? 133  ARG E CB  1 
ATOM   13359 C  CG  . ARG E 2 450  ? 118.609 147.862 158.734 1.00 94.73  ? 133  ARG E CG  1 
ATOM   13360 C  CD  . ARG E 2 450  ? 119.210 148.823 157.664 1.00 104.47 ? 133  ARG E CD  1 
ATOM   13361 N  NE  . ARG E 2 450  ? 119.850 150.028 158.215 1.00 114.12 ? 133  ARG E NE  1 
ATOM   13362 C  CZ  . ARG E 2 450  ? 121.162 150.282 158.184 1.00 113.43 ? 133  ARG E CZ  1 
ATOM   13363 N  NH1 . ARG E 2 450  ? 121.998 149.425 157.605 1.00 107.99 ? 133  ARG E NH1 1 
ATOM   13364 N  NH2 . ARG E 2 450  ? 121.642 151.407 158.716 1.00 105.70 ? 133  ARG E NH2 1 
ATOM   13365 N  N   . VAL E 2 451  ? 119.898 143.729 160.042 1.00 71.25  ? 134  VAL E N   1 
ATOM   13366 C  CA  . VAL E 2 451  ? 119.751 142.465 159.320 1.00 66.92  ? 134  VAL E CA  1 
ATOM   13367 C  C   . VAL E 2 451  ? 119.370 141.335 160.263 1.00 66.04  ? 134  VAL E C   1 
ATOM   13368 O  O   . VAL E 2 451  ? 118.340 140.681 160.063 1.00 71.36  ? 134  VAL E O   1 
ATOM   13369 C  CB  . VAL E 2 451  ? 121.000 142.100 158.487 1.00 66.47  ? 134  VAL E CB  1 
ATOM   13370 C  CG1 . VAL E 2 451  ? 121.158 143.049 157.320 1.00 72.84  ? 134  VAL E CG1 1 
ATOM   13371 C  CG2 . VAL E 2 451  ? 122.259 142.147 159.323 1.00 70.65  ? 134  VAL E CG2 1 
ATOM   13372 N  N   . CYS E 2 452  ? 120.178 141.100 161.293 1.00 56.49  ? 135  CYS E N   1 
ATOM   13373 C  CA  . CYS E 2 452  ? 119.935 139.956 162.151 1.00 48.13  ? 135  CYS E CA  1 
ATOM   13374 C  C   . CYS E 2 452  ? 118.500 139.947 162.620 1.00 52.42  ? 135  CYS E C   1 
ATOM   13375 O  O   . CYS E 2 452  ? 117.782 138.964 162.427 1.00 65.63  ? 135  CYS E O   1 
ATOM   13376 C  CB  . CYS E 2 452  ? 120.871 139.985 163.344 1.00 60.74  ? 135  CYS E CB  1 
ATOM   13377 S  SG  . CYS E 2 452  ? 122.584 140.238 162.921 1.00 100.75 ? 135  CYS E SG  1 
ATOM   13378 N  N   . ALA E 2 453  ? 118.040 141.065 163.173 1.00 59.87  ? 136  ALA E N   1 
ATOM   13379 C  CA  . ALA E 2 453  ? 116.677 141.110 163.680 1.00 67.96  ? 136  ALA E CA  1 
ATOM   13380 C  C   . ALA E 2 453  ? 115.709 140.626 162.618 1.00 60.82  ? 136  ALA E C   1 
ATOM   13381 O  O   . ALA E 2 453  ? 114.931 139.693 162.846 1.00 72.56  ? 136  ALA E O   1 
ATOM   13382 C  CB  . ALA E 2 453  ? 116.317 142.528 164.133 1.00 75.38  ? 136  ALA E CB  1 
ATOM   13383 N  N   . GLU E 2 454  ? 115.826 141.178 161.417 1.00 58.03  ? 137  GLU E N   1 
ATOM   13384 C  CA  . GLU E 2 454  ? 114.914 140.823 160.341 1.00 60.99  ? 137  GLU E CA  1 
ATOM   13385 C  C   . GLU E 2 454  ? 114.916 139.325 160.095 1.00 69.42  ? 137  GLU E C   1 
ATOM   13386 O  O   . GLU E 2 454  ? 113.853 138.693 160.042 1.00 72.64  ? 137  GLU E O   1 
ATOM   13387 C  CB  . GLU E 2 454  ? 115.296 141.597 159.083 1.00 70.15  ? 137  GLU E CB  1 
ATOM   13388 C  CG  . GLU E 2 454  ? 114.811 143.070 159.091 1.00 88.94  ? 137  GLU E CG  1 
ATOM   13389 C  CD  . GLU E 2 454  ? 115.629 144.011 160.003 1.00 93.73  ? 137  GLU E CD  1 
ATOM   13390 O  OE1 . GLU E 2 454  ? 116.548 143.536 160.713 1.00 87.57  ? 137  GLU E OE1 1 
ATOM   13391 O  OE2 . GLU E 2 454  ? 115.365 145.239 159.988 1.00 91.36  ? 137  GLU E OE2 1 
ATOM   13392 N  N   . MET E 2 455  ? 116.108 138.721 160.007 1.00 70.86  ? 138  MET E N   1 
ATOM   13393 C  CA  . MET E 2 455  ? 116.142 137.291 159.715 1.00 67.21  ? 138  MET E CA  1 
ATOM   13394 C  C   . MET E 2 455  ? 115.700 136.472 160.910 1.00 57.41  ? 138  MET E C   1 
ATOM   13395 O  O   . MET E 2 455  ? 115.091 135.412 160.734 1.00 69.57  ? 138  MET E O   1 
ATOM   13396 C  CB  . MET E 2 455  ? 117.522 136.843 159.251 1.00 62.39  ? 138  MET E CB  1 
ATOM   13397 C  CG  . MET E 2 455  ? 118.602 136.947 160.272 1.00 67.00  ? 138  MET E CG  1 
ATOM   13398 S  SD  . MET E 2 455  ? 119.963 135.913 159.731 1.00 79.98  ? 138  MET E SD  1 
ATOM   13399 C  CE  . MET E 2 455  ? 119.004 134.455 159.346 1.00 72.39  ? 138  MET E CE  1 
ATOM   13400 N  N   . VAL E 2 456  ? 115.943 136.959 162.123 1.00 53.33  ? 139  VAL E N   1 
ATOM   13401 C  CA  . VAL E 2 456  ? 115.328 136.309 163.268 1.00 56.15  ? 139  VAL E CA  1 
ATOM   13402 C  C   . VAL E 2 456  ? 113.819 136.332 163.119 1.00 66.42  ? 139  VAL E C   1 
ATOM   13403 O  O   . VAL E 2 456  ? 113.149 135.308 163.313 1.00 78.51  ? 139  VAL E O   1 
ATOM   13404 C  CB  . VAL E 2 456  ? 115.776 136.970 164.579 1.00 73.12  ? 139  VAL E CB  1 
ATOM   13405 C  CG1 . VAL E 2 456  ? 114.900 136.487 165.729 1.00 81.54  ? 139  VAL E CG1 1 
ATOM   13406 C  CG2 . VAL E 2 456  ? 117.247 136.657 164.839 1.00 79.18  ? 139  VAL E CG2 1 
ATOM   13407 N  N   . ALA E 2 457  ? 113.263 137.477 162.701 1.00 69.36  ? 140  ALA E N   1 
ATOM   13408 C  CA  . ALA E 2 457  ? 111.827 137.549 162.435 1.00 69.99  ? 140  ALA E CA  1 
ATOM   13409 C  C   . ALA E 2 457  ? 111.409 136.489 161.427 1.00 71.67  ? 140  ALA E C   1 
ATOM   13410 O  O   . ALA E 2 457  ? 110.345 135.876 161.569 1.00 74.70  ? 140  ALA E O   1 
ATOM   13411 C  CB  . ALA E 2 457  ? 111.441 138.943 161.937 1.00 69.72  ? 140  ALA E CB  1 
ATOM   13412 N  N   . LYS E 2 458  ? 112.258 136.228 160.425 1.00 70.28  ? 141  LYS E N   1 
ATOM   13413 C  CA  . LYS E 2 458  ? 111.974 135.154 159.480 1.00 65.49  ? 141  LYS E CA  1 
ATOM   13414 C  C   . LYS E 2 458  ? 111.855 133.817 160.197 1.00 68.03  ? 141  LYS E C   1 
ATOM   13415 O  O   . LYS E 2 458  ? 110.822 133.143 160.112 1.00 76.46  ? 141  LYS E O   1 
ATOM   13416 C  CB  . LYS E 2 458  ? 113.057 135.096 158.410 1.00 58.42  ? 141  LYS E CB  1 
ATOM   13417 C  CG  . LYS E 2 458  ? 113.204 136.382 157.623 1.00 65.33  ? 141  LYS E CG  1 
ATOM   13418 C  CD  . LYS E 2 458  ? 113.622 136.077 156.183 1.00 69.84  ? 141  LYS E CD  1 
ATOM   13419 C  CE  . LYS E 2 458  ? 114.021 137.328 155.416 1.00 61.28  ? 141  LYS E CE  1 
ATOM   13420 N  NZ  . LYS E 2 458  ? 115.350 137.834 155.840 1.00 61.79  ? 141  LYS E NZ  1 
ATOM   13421 N  N   . TYR E 2 459  ? 112.876 133.448 160.966 1.00 64.97  ? 142  TYR E N   1 
ATOM   13422 C  CA  . TYR E 2 459  ? 112.779 132.204 161.707 1.00 64.02  ? 142  TYR E CA  1 
ATOM   13423 C  C   . TYR E 2 459  ? 111.597 132.252 162.663 1.00 72.10  ? 142  TYR E C   1 
ATOM   13424 O  O   . TYR E 2 459  ? 111.088 131.200 163.064 1.00 81.32  ? 142  TYR E O   1 
ATOM   13425 C  CB  . TYR E 2 459  ? 114.083 131.941 162.474 1.00 66.88  ? 142  TYR E CB  1 
ATOM   13426 C  CG  . TYR E 2 459  ? 115.242 131.454 161.619 1.00 64.43  ? 142  TYR E CG  1 
ATOM   13427 C  CD1 . TYR E 2 459  ? 115.186 130.252 160.929 1.00 69.45  ? 142  TYR E CD1 1 
ATOM   13428 C  CD2 . TYR E 2 459  ? 116.393 132.214 161.497 1.00 69.25  ? 142  TYR E CD2 1 
ATOM   13429 C  CE1 . TYR E 2 459  ? 116.257 129.826 160.146 1.00 61.95  ? 142  TYR E CE1 1 
ATOM   13430 C  CE2 . TYR E 2 459  ? 117.455 131.797 160.723 1.00 66.08  ? 142  TYR E CE2 1 
ATOM   13431 C  CZ  . TYR E 2 459  ? 117.390 130.612 160.055 1.00 54.41  ? 142  TYR E CZ  1 
ATOM   13432 O  OH  . TYR E 2 459  ? 118.462 130.244 159.284 1.00 50.46  ? 142  TYR E OH  1 
ATOM   13433 N  N   . ASP E 2 460  ? 111.141 133.458 163.021 1.00 69.27  ? 143  ASP E N   1 
ATOM   13434 C  CA  . ASP E 2 460  ? 110.016 133.572 163.935 1.00 76.88  ? 143  ASP E CA  1 
ATOM   13435 C  C   . ASP E 2 460  ? 108.752 133.019 163.295 1.00 87.17  ? 143  ASP E C   1 
ATOM   13436 O  O   . ASP E 2 460  ? 107.942 132.367 163.967 1.00 90.57  ? 143  ASP E O   1 
ATOM   13437 C  CB  . ASP E 2 460  ? 109.816 135.033 164.359 1.00 87.80  ? 143  ASP E CB  1 
ATOM   13438 C  CG  . ASP E 2 460  ? 108.956 135.174 165.634 1.00 104.55 ? 143  ASP E CG  1 
ATOM   13439 O  OD1 . ASP E 2 460  ? 108.586 134.133 166.228 1.00 101.97 ? 143  ASP E OD1 1 
ATOM   13440 O  OD2 . ASP E 2 460  ? 108.642 136.322 166.038 1.00 100.26 ? 143  ASP E OD2 1 
ATOM   13441 N  N   . LEU E 2 461  ? 108.568 133.260 161.994 1.00 83.03  ? 144  LEU E N   1 
ATOM   13442 C  CA  . LEU E 2 461  ? 107.364 132.765 161.334 1.00 78.78  ? 144  LEU E CA  1 
ATOM   13443 C  C   . LEU E 2 461  ? 107.322 131.245 161.345 1.00 76.56  ? 144  LEU E C   1 
ATOM   13444 O  O   . LEU E 2 461  ? 106.252 130.646 161.504 1.00 73.81  ? 144  LEU E O   1 
ATOM   13445 C  CB  . LEU E 2 461  ? 107.280 133.306 159.909 1.00 79.03  ? 144  LEU E CB  1 
ATOM   13446 C  CG  . LEU E 2 461  ? 106.665 134.708 159.795 1.00 91.14  ? 144  LEU E CG  1 
ATOM   13447 C  CD1 . LEU E 2 461  ? 105.227 134.671 160.331 1.00 92.59  ? 144  LEU E CD1 1 
ATOM   13448 C  CD2 . LEU E 2 461  ? 107.472 135.824 160.470 1.00 83.49  ? 144  LEU E CD2 1 
ATOM   13449 N  N   . LEU E 2 462  ? 108.485 130.606 161.202 1.00 77.94  ? 145  LEU E N   1 
ATOM   13450 C  CA  . LEU E 2 462  ? 108.531 129.152 161.162 1.00 76.29  ? 145  LEU E CA  1 
ATOM   13451 C  C   . LEU E 2 462  ? 108.024 128.551 162.465 1.00 78.92  ? 145  LEU E C   1 
ATOM   13452 O  O   . LEU E 2 462  ? 107.254 127.584 162.447 1.00 87.72  ? 145  LEU E O   1 
ATOM   13453 C  CB  . LEU E 2 462  ? 109.959 128.674 160.872 1.00 83.78  ? 145  LEU E CB  1 
ATOM   13454 C  CG  . LEU E 2 462  ? 110.764 129.310 159.716 1.00 88.10  ? 145  LEU E CG  1 
ATOM   13455 C  CD1 . LEU E 2 462  ? 112.153 128.638 159.515 1.00 78.80  ? 145  LEU E CD1 1 
ATOM   13456 C  CD2 . LEU E 2 462  ? 109.969 129.353 158.390 1.00 76.54  ? 145  LEU E CD2 1 
ATOM   13457 N  N   . VAL E 2 463  ? 108.426 129.113 163.602 1.00 79.10  ? 146  VAL E N   1 
ATOM   13458 C  CA  . VAL E 2 463  ? 108.080 128.518 164.893 1.00 88.05  ? 146  VAL E CA  1 
ATOM   13459 C  C   . VAL E 2 463  ? 106.906 129.283 165.537 1.00 91.97  ? 146  VAL E C   1 
ATOM   13460 O  O   . VAL E 2 463  ? 107.072 130.056 166.487 1.00 88.64  ? 146  VAL E O   1 
ATOM   13461 C  CB  . VAL E 2 463  ? 109.318 128.457 165.827 1.00 84.54  ? 146  VAL E CB  1 
ATOM   13462 C  CG1 . VAL E 2 463  ? 108.992 127.730 167.135 1.00 82.79  ? 146  VAL E CG1 1 
ATOM   13463 C  CG2 . VAL E 2 463  ? 110.478 127.769 165.115 1.00 84.53  ? 146  VAL E CG2 1 
HETATM 13464 ZN ZN  . ZN  F 3 .    ? 151.861 131.982 90.790  1.00 44.75  ? 1501 ZN  A ZN  1 
# 
